CNRS Nantes University UFIP UFIP
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elNémo ID: 19110503162176669

Job options:

ID        	=	 19110503162176669
JOBID     	=	 dot
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER dot

HEADER    TRANSFERASE                             11-FEB-11   3QOW              
TITLE     DOT1L STRUCTURE IN COMPLEX WITH SAM                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-416;                                        
COMPND   5 SYNONYM: DOT1-LIKE PROTEIN, HISTONE H3-K79 METHYLTRANSFERASE, H3-K79-
COMPND   6 HMTASE, LYSINE N-METHYLTRANSFERASE 4;                                
COMPND   7 EC: 2.1.1.43;                                                        
COMPND   8 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: DOT1L, KIAA1814, KMT4;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    H3K79 METHYLATION, TRANSFERASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.JIN                                                                 
REVDAT   2   10-AUG-11 3QOW    1       JRNL   VERSN                             
REVDAT   1   25-MAY-11 3QOW    0                                                
JRNL        AUTH   V.M.RICHON,D.JOHNSTON,C.J.SNEERINGER,L.JIN,C.R.MAJER,        
JRNL        AUTH 2 K.ELLISTON,L.F.JERVA,M.P.SCOTT,R.A.COPELAND                  
JRNL        TITL   CHEMOGENETIC ANALYSIS OF HUMAN PROTEIN METHYLTRANSFERASES.   
JRNL        REF    CHEM.BIOL.DRUG DES.           V.  78   199 2011              
JRNL        REFN                   ISSN 1747-0277                               
JRNL        PMID   21564555                                                     
JRNL        DOI    10.1111/J.1747-0285.2011.01135.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.87                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 38415                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.162                           
REMARK   3   R VALUE            (WORKING SET) : 0.160                           
REMARK   3   FREE R VALUE                     : 0.192                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1956                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2777                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.80                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 118                          
REMARK   3   BIN FREE R VALUE                    : 0.1760                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2597                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 37                                      
REMARK   3   SOLVENT ATOMS            : 144                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.99000                                             
REMARK   3    B22 (A**2) : -0.99000                                             
REMARK   3    B33 (A**2) : 1.98000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.023         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.064         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.426         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2722 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3699 ; 1.242 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   325 ; 5.170 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   131 ;33.008 ;23.817       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   460 ;16.202 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;17.521 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   399 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2070 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1623 ; 0.734 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2628 ; 1.338 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1099 ; 1.701 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1068 ; 2.746 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3QOW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063917.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40579                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 10.500                             
REMARK 200  R MERGE                    (I) : 0.12100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M AMMONIUM SULFATE, 0.1 M SODIUM       
REMARK 280  ACETATE, PH 5.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       34.20933            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       17.10467            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       25.65700            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        8.55233            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       42.76167            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     VAL A    59                                                      
REMARK 465     GLY A   301                                                      
REMARK 465     SER A   302                                                      
REMARK 465     VAL A   303                                                      
REMARK 465     SER A   304                                                      
REMARK 465     ASN A   331                                                      
REMARK 465     PRO A   332                                                      
REMARK 465     LYS A   333                                                      
REMARK 465     LEU A   334                                                      
REMARK 465     ARG A   335                                                      
REMARK 465     GLU A   336                                                      
REMARK 465     GLU A   337                                                      
REMARK 465     GLN A   338                                                      
REMARK 465     GLU A   339                                                      
REMARK 465     ALA A   340                                                      
REMARK 465     ALA A   341                                                      
REMARK 465     ARG A   342                                                      
REMARK 465     ARG A   343                                                      
REMARK 465     ARG A   344                                                      
REMARK 465     GLN A   345                                                      
REMARK 465     GLN A   346                                                      
REMARK 465     ARG A   347                                                      
REMARK 465     GLU A   348                                                      
REMARK 465     SER A   349                                                      
REMARK 465     LYS A   350                                                      
REMARK 465     SER A   351                                                      
REMARK 465     ASN A   352                                                      
REMARK 465     ALA A   353                                                      
REMARK 465     ALA A   354                                                      
REMARK 465     THR A   355                                                      
REMARK 465     PRO A   356                                                      
REMARK 465     THR A   357                                                      
REMARK 465     LYS A   358                                                      
REMARK 465     GLY A   359                                                      
REMARK 465     PRO A   360                                                      
REMARK 465     GLU A   361                                                      
REMARK 465     GLY A   362                                                      
REMARK 465     LYS A   363                                                      
REMARK 465     VAL A   364                                                      
REMARK 465     ALA A   365                                                      
REMARK 465     GLY A   366                                                      
REMARK 465     PRO A   367                                                      
REMARK 465     ALA A   368                                                      
REMARK 465     ASP A   369                                                      
REMARK 465     ALA A   370                                                      
REMARK 465     PRO A   371                                                      
REMARK 465     MET A   372                                                      
REMARK 465     ASP A   373                                                      
REMARK 465     SER A   374                                                      
REMARK 465     GLY A   375                                                      
REMARK 465     ALA A   376                                                      
REMARK 465     GLU A   377                                                      
REMARK 465     GLU A   378                                                      
REMARK 465     GLU A   379                                                      
REMARK 465     LYS A   380                                                      
REMARK 465     ALA A   381                                                      
REMARK 465     GLY A   382                                                      
REMARK 465     ALA A   383                                                      
REMARK 465     ALA A   384                                                      
REMARK 465     THR A   385                                                      
REMARK 465     VAL A   386                                                      
REMARK 465     LYS A   387                                                      
REMARK 465     LYS A   388                                                      
REMARK 465     PRO A   389                                                      
REMARK 465     SER A   390                                                      
REMARK 465     PRO A   391                                                      
REMARK 465     SER A   392                                                      
REMARK 465     LYS A   393                                                      
REMARK 465     ALA A   394                                                      
REMARK 465     ARG A   395                                                      
REMARK 465     LYS A   396                                                      
REMARK 465     LYS A   397                                                      
REMARK 465     LYS A   398                                                      
REMARK 465     LEU A   399                                                      
REMARK 465     ASN A   400                                                      
REMARK 465     LYS A   401                                                      
REMARK 465     LYS A   402                                                      
REMARK 465     GLY A   403                                                      
REMARK 465     ARG A   404                                                      
REMARK 465     LYS A   405                                                      
REMARK 465     MET A   406                                                      
REMARK 465     ALA A   407                                                      
REMARK 465     GLY A   408                                                      
REMARK 465     ARG A   409                                                      
REMARK 465     LYS A   410                                                      
REMARK 465     ARG A   411                                                      
REMARK 465     GLY A   412                                                      
REMARK 465     ARG A   413                                                      
REMARK 465     PRO A   414                                                      
REMARK 465     LYS A   415                                                      
REMARK 465     LYS A   416                                                      
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     LYS A   4    CG   CD   CE   NZ                                   
REMARK 470     ASN A  57    CG   OD1                                            
REMARK 470     TYR A  58    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A  60    CG   CD1  CD2                                       
REMARK 470     ILE A  61    CG1  CG2  CD1                                       
REMARK 470     ASP A  62    CG   OD1  OD2                                       
REMARK 470     TYR A  63    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 300    CG   CD   CE   NZ                                   
REMARK 470     LYS A 308    CG   CD   CE   NZ                                   
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 A  62       94.14    -68.42                                   
REMARK 500    ASN A  99       45.21     36.77                                   
REMARK 500    ASN A 276       36.24    -98.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 417                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 418                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 419                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3QOX   RELATED DB: PDB                                   
REMARK 900 DOT1L STRUCTURE IN COMPLEX WITH SAH                                  
DBREF  3QOW A    1   416  UNP    Q8TEK3   DOT1L_HUMAN      1    416             
SEQADV 3QOW MET A   -9  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3QOW HIS A   -8  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3QOW HIS A   -7  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3QOW HIS A   -6  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3QOW HIS A   -5  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3QOW HIS A   -4  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3QOW HIS A   -3  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3QOW SER A   -2  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3QOW SER A   -1  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3QOW GLY A    0  UNP  Q8TEK3              EXPRESSION TAG                 
SEQRES   1 A  426  MET HIS HIS HIS HIS HIS HIS SER SER GLY MET GLY GLU          
SEQRES   2 A  426  LYS LEU GLU LEU ARG LEU LYS SER PRO VAL GLY ALA GLU          
SEQRES   3 A  426  PRO ALA VAL TYR PRO TRP PRO LEU PRO VAL TYR ASP LYS          
SEQRES   4 A  426  HIS HIS ASP ALA ALA HIS GLU ILE ILE GLU THR ILE ARG          
SEQRES   5 A  426  TRP VAL CYS GLU GLU ILE PRO ASP LEU LYS LEU ALA MET          
SEQRES   6 A  426  GLU ASN TYR VAL LEU ILE ASP TYR ASP THR LYS SER PHE          
SEQRES   7 A  426  GLU SER MET GLN ARG LEU CYS ASP LYS TYR ASN ARG ALA          
SEQRES   8 A  426  ILE ASP SER ILE HIS GLN LEU TRP LYS GLY THR THR GLN          
SEQRES   9 A  426  PRO MET LYS LEU ASN THR ARG PRO SER THR GLY LEU LEU          
SEQRES  10 A  426  ARG HIS ILE LEU GLN GLN VAL TYR ASN HIS SER VAL THR          
SEQRES  11 A  426  ASP PRO GLU LYS LEU ASN ASN TYR GLU PRO PHE SER PRO          
SEQRES  12 A  426  GLU VAL TYR GLY GLU THR SER PHE ASP LEU VAL ALA GLN          
SEQRES  13 A  426  MET ILE ASP GLU ILE LYS MET THR ASP ASP ASP LEU PHE          
SEQRES  14 A  426  VAL ASP LEU GLY SER GLY VAL GLY GLN VAL VAL LEU GLN          
SEQRES  15 A  426  VAL ALA ALA ALA THR ASN CYS LYS HIS HIS TYR GLY VAL          
SEQRES  16 A  426  GLU LYS ALA ASP ILE PRO ALA LYS TYR ALA GLU THR MET          
SEQRES  17 A  426  ASP ARG GLU PHE ARG LYS TRP MET LYS TRP TYR GLY LYS          
SEQRES  18 A  426  LYS HIS ALA GLU TYR THR LEU GLU ARG GLY ASP PHE LEU          
SEQRES  19 A  426  SER GLU GLU TRP ARG GLU ARG ILE ALA ASN THR SER VAL          
SEQRES  20 A  426  ILE PHE VAL ASN ASN PHE ALA PHE GLY PRO GLU VAL ASP          
SEQRES  21 A  426  HIS GLN LEU LYS GLU ARG PHE ALA ASN MET LYS GLU GLY          
SEQRES  22 A  426  GLY ARG ILE VAL SER SER LYS PRO PHE ALA PRO LEU ASN          
SEQRES  23 A  426  PHE ARG ILE ASN SER ARG ASN LEU SER ASP ILE GLY THR          
SEQRES  24 A  426  ILE MET ARG VAL VAL GLU LEU SER PRO LEU LYS GLY SER          
SEQRES  25 A  426  VAL SER TRP THR GLY LYS PRO VAL SER TYR TYR LEU HIS          
SEQRES  26 A  426  THR ILE ASP ARG THR ILE LEU GLU ASN TYR PHE SER SER          
SEQRES  27 A  426  LEU LYS ASN PRO LYS LEU ARG GLU GLU GLN GLU ALA ALA          
SEQRES  28 A  426  ARG ARG ARG GLN GLN ARG GLU SER LYS SER ASN ALA ALA          
SEQRES  29 A  426  THR PRO THR LYS GLY PRO GLU GLY LYS VAL ALA GLY PRO          
SEQRES  30 A  426  ALA ASP ALA PRO MET ASP SER GLY ALA GLU GLU GLU LYS          
SEQRES  31 A  426  ALA GLY ALA ALA THR VAL LYS LYS PRO SER PRO SER LYS          
SEQRES  32 A  426  ALA ARG LYS LYS LYS LEU ASN LYS LYS GLY ARG LYS MET          
SEQRES  33 A  426  ALA GLY ARG LYS ARG GLY ARG PRO LYS LYS                      
HET    SAM  A 417      27                                                       
HET    SO4  A 418       5                                                       
HET    SO4  A 419       5                                                       
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  SAM    C15 H22 N6 O5 S                                              
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  HOH   *144(H2 O)                                                    
HELIX    1   1 ALA A   33  ILE A   48  1                                  16    
HELIX    2   2 ILE A   48  ASN A   57  1                                  10    
HELIX    3   3 SER A   67  TRP A   89  1                                  23    
HELIX    4   4 SER A  103  VAL A  119  1                                  17    
HELIX    5   5 ASP A  121  ASN A  127  5                                   7    
HELIX    6   6 SER A  140  ILE A  151  1                                  12    
HELIX    7   7 GLY A  167  THR A  177  1                                  11    
HELIX    8   8 ALA A  188  GLY A  210  1                                  23    
HELIX    9   9 SER A  225  ASN A  234  1                                  10    
HELIX   10  10 GLY A  246  ALA A  258  1                                  13    
HELIX   11  11 ASP A  286  THR A  289  5                                   4    
HELIX   12  12 ARG A  319  LEU A  329  1                                  11    
SHEET    1   A 2 GLU A   6  LEU A   9  0                                        
SHEET    2   A 2 ALA A  18  PRO A  21 -1  O  TYR A  20   N  LEU A   7           
SHEET    1   B 2 VAL A  26  ASP A  28  0                                        
SHEET    2   B 2 HIS A  31  ASP A  32 -1  O  HIS A  31   N  TYR A  27           
SHEET    1   C 7 TYR A 216  ARG A 220  0                                        
SHEET    2   C 7 HIS A 181  GLU A 186  1  N  GLY A 184   O  GLU A 219           
SHEET    3   C 7 LEU A 158  LEU A 162  1  N  ASP A 161   O  TYR A 183           
SHEET    4   C 7 VAL A 237  VAL A 240  1  O  PHE A 239   N  VAL A 160           
SHEET    5   C 7 ARG A 265  SER A 268  1  O  VAL A 267   N  ILE A 238           
SHEET    6   C 7 TYR A 313  ILE A 317 -1  O  HIS A 315   N  ILE A 266           
SHEET    7   C 7 MET A 291  GLU A 295 -1  N  VAL A 294   O  LEU A 314           
CISPEP   1 TRP A   22    PRO A   23          0        -1.95                     
SITE     1 AC1 21 PRO A 133  VAL A 135  GLY A 137  GLU A 138                    
SITE     2 AC1 21 THR A 139  ASP A 161  GLY A 163  SER A 164                    
SITE     3 AC1 21 GLN A 168  VAL A 169  GLU A 186  LYS A 187                    
SITE     4 AC1 21 GLY A 221  ASP A 222  PHE A 223  PHE A 239                    
SITE     5 AC1 21 ASN A 241  PHE A 245  HOH A 441  HOH A 464                    
SITE     6 AC1 21 HOH A 524                                                     
SITE     1 AC2  4 ARG A 203  HIS A 213  HOH A 448  HOH A 553                    
SITE     1 AC3  4 ARG A 229  GLN A 252  GLU A 255  ARG A 256                    
CRYST1  153.204  153.204   51.314  90.00  90.00 120.00 P 65          6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006527  0.003769  0.000000        0.00000                         
SCALE2      0.000000  0.007537  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019488        0.00000                         
ATOM      1  N   LYS A   4      55.455  43.720 -14.128  1.00 59.24           N  
ATOM      2  CA  LYS A   4      56.570  44.706 -13.963  1.00 59.02           C  
ATOM      3  C   LYS A   4      56.802  45.056 -12.490  1.00 58.73           C  
ATOM      4  O   LYS A   4      56.489  44.256 -11.600  1.00 58.94           O  
ATOM      5  CB  LYS A   4      56.290  45.969 -14.785  1.00 59.21           C  
ATOM      6  N   LEU A   5      57.359  46.241 -12.238  1.00 57.98           N  
ATOM      7  CA  LEU A   5      57.560  46.726 -10.875  1.00 57.17           C  
ATOM      8  C   LEU A   5      56.220  46.823 -10.139  1.00 56.58           C  
ATOM      9  O   LEU A   5      55.221  47.303 -10.696  1.00 56.30           O  
ATOM     10  CB  LEU A   5      58.259  48.088 -10.871  1.00 57.39           C  
ATOM     11  CG  LEU A   5      59.475  48.332 -11.770  1.00 57.69           C  
ATOM     12  CD1 LEU A   5      59.028  48.710 -13.191  1.00 58.35           C  
ATOM     13  CD2 LEU A   5      60.352  49.429 -11.180  1.00 57.66           C  
ATOM     14  N   GLU A   6      56.212  46.361  -8.891  1.00 55.44           N  
ATOM     15  CA  GLU A   6      54.997  46.283  -8.090  1.00 54.19           C  
ATOM     16  C   GLU A   6      55.258  46.675  -6.649  1.00 52.79           C  
ATOM     17  O   GLU A   6      56.348  46.429  -6.112  1.00 52.56           O  
ATOM     18  CB  GLU A   6      54.437  44.861  -8.111  1.00 54.91           C  
ATOM     19  CG  GLU A   6      53.245  44.651  -9.027  1.00 56.20           C  
ATOM     20  CD  GLU A   6      52.704  43.231  -8.949  1.00 58.69           C  
ATOM     21  OE1 GLU A   6      51.933  42.836  -9.848  1.00 59.85           O  
ATOM     22  OE2 GLU A   6      53.044  42.505  -7.990  1.00 59.60           O  
ATOM     23  N   LEU A   7      54.259  47.306  -6.037  1.00 50.47           N  
ATOM     24  CA  LEU A   7      54.231  47.507  -4.600  1.00 48.51           C  
ATOM     25  C   LEU A   7      53.063  46.716  -4.021  1.00 47.15           C  
ATOM     26  O   LEU A   7      51.972  46.715  -4.595  1.00 47.09           O  
ATOM     27  CB  LEU A   7      54.102  48.986  -4.257  1.00 48.28           C  
ATOM     28  CG  LEU A   7      55.351  49.860  -4.368  1.00 48.97           C  
ATOM     29  CD1 LEU A   7      55.076  51.248  -3.840  1.00 47.54           C  
ATOM     30  CD2 LEU A   7      56.534  49.235  -3.613  1.00 50.61           C  
ATOM     31  N   ARG A   8      53.298  46.046  -2.891  1.00 45.20           N  
ATOM     32  CA  ARG A   8      52.317  45.143  -2.292  1.00 43.52           C  
ATOM     33  C   ARG A   8      52.165  45.448  -0.808  1.00 41.51           C  
ATOM     34  O   ARG A   8      53.160  45.557  -0.097  1.00 41.53           O  
ATOM     35  CB  ARG A   8      52.739  43.669  -2.457  1.00 43.98           C  
ATOM     36  CG  ARG A   8      53.010  43.197  -3.887  1.00 46.12           C  
ATOM     37  CD  ARG A   8      53.492  41.737  -3.928  1.00 49.25           C  
ATOM     38  NE  ARG A   8      52.372  40.799  -3.841  1.00 51.99           N  
ATOM     39  CZ  ARG A   8      51.648  40.386  -4.881  1.00 53.26           C  
ATOM     40  NH1 ARG A   8      51.929  40.814  -6.111  1.00 54.72           N  
ATOM     41  NH2 ARG A   8      50.638  39.545  -4.691  1.00 53.89           N  
ATOM     42  N   LEU A   9      50.920  45.576  -0.349  1.00 39.52           N  
ATOM     43  CA  LEU A   9      50.614  45.661   1.080  1.00 37.23           C  
ATOM     44  C   LEU A   9      49.770  44.456   1.499  1.00 36.23           C  
ATOM     45  O   LEU A   9      48.684  44.241   0.960  1.00 35.90           O  
ATOM     46  CB  LEU A   9      49.853  46.968   1.425  1.00 36.97           C  
ATOM     47  CG  LEU A   9      50.475  48.362   1.232  1.00 35.03           C  
ATOM     48  CD1 LEU A   9      49.470  49.473   1.621  1.00 33.43           C  
ATOM     49  CD2 LEU A   9      51.776  48.540   2.004  1.00 30.94           C  
ATOM     50  N   LYS A  10      50.264  43.691   2.477  1.00 35.10           N  
ATOM     51  CA  LYS A  10      49.515  42.586   3.058  1.00 34.51           C  
ATOM     52  C   LYS A  10      48.350  43.084   3.921  1.00 33.89           C  
ATOM     53  O   LYS A  10      48.474  44.083   4.625  1.00 34.17           O  
ATOM     54  CB  LYS A  10      50.437  41.688   3.906  1.00 34.36           C  
ATOM     55  CG  LYS A  10      51.488  40.897   3.105  1.00 34.41           C  
ATOM     56  CD  LYS A  10      52.250  39.935   4.029  1.00 37.83           C  
ATOM     57  CE  LYS A  10      53.208  39.023   3.248  1.00 37.36           C  
ATOM     58  NZ  LYS A  10      53.351  37.694   3.952  1.00 38.52           N  
ATOM     59  N   SER A  11      47.241  42.362   3.864  1.00 33.69           N  
ATOM     60  CA  SER A  11      46.056  42.629   4.672  1.00 33.37           C  
ATOM     61  C   SER A  11      46.286  42.232   6.134  1.00 33.62           C  
ATOM     62  O   SER A  11      46.904  41.188   6.410  1.00 33.72           O  
ATOM     63  CB  SER A  11      44.858  41.877   4.081  1.00 33.38           C  
ATOM     64  OG  SER A  11      43.724  41.893   4.936  1.00 31.28           O  
ATOM     65  N   PRO A  12      45.807  43.062   7.084  1.00 33.37           N  
ATOM     66  CA  PRO A  12      45.941  42.703   8.494  1.00 33.83           C  
ATOM     67  C   PRO A  12      45.108  41.478   8.881  1.00 34.15           C  
ATOM     68  O   PRO A  12      45.397  40.833   9.896  1.00 34.44           O  
ATOM     69  CB  PRO A  12      45.406  43.935   9.220  1.00 33.95           C  
ATOM     70  CG  PRO A  12      44.547  44.648   8.207  1.00 33.27           C  
ATOM     71  CD  PRO A  12      45.241  44.416   6.918  1.00 33.25           C  
ATOM     72  N   VAL A  13      44.082  41.173   8.095  1.00 34.09           N  
ATOM     73  CA  VAL A  13      43.244  40.006   8.365  1.00 34.88           C  
ATOM     74  C   VAL A  13      43.455  38.871   7.359  1.00 35.21           C  
ATOM     75  O   VAL A  13      42.674  37.928   7.312  1.00 34.98           O  
ATOM     76  CB  VAL A  13      41.736  40.368   8.457  1.00 35.03           C  
ATOM     77  CG1 VAL A  13      41.472  41.322   9.655  1.00 34.52           C  
ATOM     78  CG2 VAL A  13      41.222  40.954   7.121  1.00 34.33           C  
ATOM     79  N   GLY A  14      44.509  38.970   6.560  1.00 35.78           N  
ATOM     80  CA  GLY A  14      44.844  37.914   5.600  1.00 36.93           C  
ATOM     81  C   GLY A  14      43.986  37.857   4.344  1.00 37.56           C  
ATOM     82  O   GLY A  14      43.809  36.784   3.759  1.00 36.67           O  
ATOM     83  N   ALA A  15      43.444  39.000   3.918  1.00 37.71           N  
ATOM     84  CA  ALA A  15      42.762  39.047   2.621  1.00 38.67           C  
ATOM     85  C   ALA A  15      43.822  39.150   1.528  1.00 39.32           C  
ATOM     86  O   ALA A  15      45.016  39.247   1.819  1.00 39.21           O  
ATOM     87  CB  ALA A  15      41.795  40.225   2.549  1.00 38.68           C  
ATOM     88  N   GLU A  16      43.399  39.131   0.270  1.00 40.55           N  
ATOM     89  CA  GLU A  16      44.342  39.319  -0.821  1.00 42.01           C  
ATOM     90  C   GLU A  16      45.101  40.628  -0.621  1.00 41.42           C  
ATOM     91  O   GLU A  16      44.510  41.620  -0.212  1.00 41.71           O  
ATOM     92  CB  GLU A  16      43.641  39.267  -2.184  1.00 42.47           C  
ATOM     93  CG  GLU A  16      43.208  37.849  -2.598  1.00 46.50           C  
ATOM     94  CD  GLU A  16      44.378  36.944  -2.936  1.00 49.83           C  
ATOM     95  OE1 GLU A  16      44.854  36.976  -4.093  1.00 53.92           O  
ATOM     96  OE2 GLU A  16      44.822  36.199  -2.043  1.00 51.23           O  
ATOM     97  N   PRO A  17      46.424  40.614  -0.849  1.00 40.99           N  
ATOM     98  CA  PRO A  17      47.223  41.824  -0.749  1.00 40.95           C  
ATOM     99  C   PRO A  17      46.760  42.892  -1.742  1.00 40.82           C  
ATOM    100  O   PRO A  17      46.282  42.557  -2.818  1.00 40.56           O  
ATOM    101  CB  PRO A  17      48.643  41.339  -1.102  1.00 40.83           C  
ATOM    102  CG  PRO A  17      48.440  40.036  -1.806  1.00 40.45           C  
ATOM    103  CD  PRO A  17      47.264  39.436  -1.136  1.00 41.33           C  
ATOM    104  N   ALA A  18      46.879  44.163  -1.356  1.00 40.47           N  
ATOM    105  CA  ALA A  18      46.642  45.273  -2.263  1.00 40.55           C  
ATOM    106  C   ALA A  18      47.890  45.444  -3.152  1.00 41.23           C  
ATOM    107  O   ALA A  18      49.012  45.428  -2.640  1.00 40.83           O  
ATOM    108  CB  ALA A  18      46.362  46.534  -1.467  1.00 39.56           C  
ATOM    109  N   VAL A  19      47.683  45.587  -4.466  1.00 42.19           N  
ATOM    110  CA  VAL A  19      48.771  45.692  -5.468  1.00 43.77           C  
ATOM    111  C   VAL A  19      48.783  47.054  -6.137  1.00 43.54           C  
ATOM    112  O   VAL A  19      47.744  47.496  -6.622  1.00 43.99           O  
ATOM    113  CB  VAL A  19      48.561  44.732  -6.668  1.00 43.86           C  
ATOM    114  CG1 VAL A  19      49.879  44.134  -7.114  1.00 45.59           C  
ATOM    115  CG2 VAL A  19      47.532  43.691  -6.369  1.00 46.79           C  
ATOM    116  N   TYR A  20      49.947  47.702  -6.193  1.00 43.48           N  
ATOM    117  CA  TYR A  20      50.089  49.015  -6.832  1.00 43.12           C  
ATOM    118  C   TYR A  20      51.197  49.034  -7.905  1.00 44.14           C  
ATOM    119  O   TYR A  20      52.337  48.640  -7.631  1.00 43.91           O  
ATOM    120  CB  TYR A  20      50.435  50.091  -5.803  1.00 42.79           C  
ATOM    121  CG  TYR A  20      49.416  50.368  -4.721  1.00 40.07           C  
ATOM    122  CD1 TYR A  20      49.386  49.594  -3.559  1.00 36.63           C  
ATOM    123  CD2 TYR A  20      48.520  51.437  -4.831  1.00 37.33           C  
ATOM    124  CE1 TYR A  20      48.474  49.848  -2.542  1.00 34.90           C  
ATOM    125  CE2 TYR A  20      47.589  51.707  -3.798  1.00 35.79           C  
ATOM    126  CZ  TYR A  20      47.583  50.902  -2.663  1.00 33.63           C  
ATOM    127  OH  TYR A  20      46.707  51.125  -1.637  1.00 32.57           O  
ATOM    128  N   PRO A  21      50.883  49.546  -9.110  1.00 44.99           N  
ATOM    129  CA  PRO A  21      51.888  49.559 -10.177  1.00 45.29           C  
ATOM    130  C   PRO A  21      52.942  50.651  -9.992  1.00 45.75           C  
ATOM    131  O   PRO A  21      52.678  51.673  -9.349  1.00 45.87           O  
ATOM    132  CB  PRO A  21      51.056  49.825 -11.436  1.00 45.81           C  
ATOM    133  CG  PRO A  21      49.838  50.584 -10.956  1.00 45.69           C  
ATOM    134  CD  PRO A  21      49.606  50.180  -9.515  1.00 44.71           C  
ATOM    135  N   TRP A  22      54.137  50.441 -10.535  1.00 45.88           N  
ATOM    136  CA  TRP A  22      55.120  51.530 -10.599  1.00 45.79           C  
ATOM    137  C   TRP A  22      55.314  51.965 -12.048  1.00 45.39           C  
ATOM    138  O   TRP A  22      55.414  51.107 -12.937  1.00 46.01           O  
ATOM    139  CB  TRP A  22      56.455  51.163  -9.928  1.00 46.12           C  
ATOM    140  CG  TRP A  22      57.336  52.368  -9.691  1.00 46.13           C  
ATOM    141  CD1 TRP A  22      58.200  52.936 -10.581  1.00 46.04           C  
ATOM    142  CD2 TRP A  22      57.417  53.156  -8.495  1.00 46.13           C  
ATOM    143  NE1 TRP A  22      58.809  54.034 -10.017  1.00 47.41           N  
ATOM    144  CE2 TRP A  22      58.351  54.183  -8.734  1.00 46.83           C  
ATOM    145  CE3 TRP A  22      56.789  53.093  -7.246  1.00 47.93           C  
ATOM    146  CZ2 TRP A  22      58.678  55.141  -7.769  1.00 48.02           C  
ATOM    147  CZ3 TRP A  22      57.118  54.044  -6.281  1.00 48.04           C  
ATOM    148  CH2 TRP A  22      58.051  55.059  -6.554  1.00 48.68           C  
ATOM    149  N   PRO A  23      55.342  53.294 -12.301  1.00 44.36           N  
ATOM    150  CA  PRO A  23      55.163  54.363 -11.315  1.00 43.58           C  
ATOM    151  C   PRO A  23      53.762  54.404 -10.706  1.00 42.90           C  
ATOM    152  O   PRO A  23      52.789  53.943 -11.325  1.00 42.27           O  
ATOM    153  CB  PRO A  23      55.454  55.649 -12.113  1.00 43.88           C  
ATOM    154  CG  PRO A  23      55.398  55.248 -13.558  1.00 43.92           C  
ATOM    155  CD  PRO A  23      55.823  53.817 -13.592  1.00 44.41           C  
ATOM    156  N   LEU A  24      53.684  54.914  -9.477  1.00 42.37           N  
ATOM    157  CA  LEU A  24      52.421  55.016  -8.748  1.00 41.74           C  
ATOM    158  C   LEU A  24      51.533  56.114  -9.356  1.00 41.11           C  
ATOM    159  O   LEU A  24      52.007  57.207  -9.625  1.00 41.08           O  
ATOM    160  CB  LEU A  24      52.687  55.275  -7.265  1.00 41.72           C  
ATOM    161  CG  LEU A  24      53.392  54.144  -6.486  1.00 42.27           C  
ATOM    162  CD1 LEU A  24      53.931  54.648  -5.160  1.00 42.15           C  
ATOM    163  CD2 LEU A  24      52.481  52.931  -6.271  1.00 41.35           C  
ATOM    164  N   PRO A  25      50.245  55.818  -9.586  1.00 40.89           N  
ATOM    165  CA  PRO A  25      49.398  56.830 -10.224  1.00 40.39           C  
ATOM    166  C   PRO A  25      49.051  58.040  -9.334  1.00 39.66           C  
ATOM    167  O   PRO A  25      49.185  57.978  -8.105  1.00 38.91           O  
ATOM    168  CB  PRO A  25      48.138  56.042 -10.613  1.00 40.65           C  
ATOM    169  CG  PRO A  25      48.117  54.877  -9.675  1.00 41.31           C  
ATOM    170  CD  PRO A  25      49.554  54.523  -9.451  1.00 40.87           C  
ATOM    171  N   VAL A  26      48.679  59.138  -9.995  1.00 39.07           N  
ATOM    172  CA AVAL A  26      48.175  60.354  -9.350  0.50 39.19           C  
ATOM    173  CA BVAL A  26      48.161  60.327  -9.323  0.50 39.14           C  
ATOM    174  C   VAL A  26      46.655  60.424  -9.546  1.00 39.32           C  
ATOM    175  O   VAL A  26      46.142  60.058 -10.606  1.00 38.72           O  
ATOM    176  CB AVAL A  26      48.861  61.637  -9.920  0.50 39.15           C  
ATOM    177  CB BVAL A  26      48.848  61.645  -9.779  0.50 39.12           C  
ATOM    178  CG1AVAL A  26      48.124  62.914  -9.505  0.50 39.14           C  
ATOM    179  CG1BVAL A  26      50.119  61.892  -8.986  0.50 39.05           C  
ATOM    180  CG2AVAL A  26      50.292  61.717  -9.455  0.50 39.18           C  
ATOM    181  CG2BVAL A  26      49.118  61.648 -11.273  0.50 38.82           C  
ATOM    182  N   TYR A  27      45.947  60.894  -8.528  1.00 39.96           N  
ATOM    183  CA  TYR A  27      44.495  60.933  -8.573  1.00 41.30           C  
ATOM    184  C   TYR A  27      44.009  62.322  -8.910  1.00 42.76           C  
ATOM    185  O   TYR A  27      43.143  62.484  -9.762  1.00 42.83           O  
ATOM    186  CB  TYR A  27      43.895  60.472  -7.244  1.00 41.21           C  
ATOM    187  CG  TYR A  27      44.286  59.062  -6.843  1.00 39.49           C  
ATOM    188  CD1 TYR A  27      44.131  57.996  -7.729  1.00 38.74           C  
ATOM    189  CD2 TYR A  27      44.806  58.800  -5.579  1.00 38.61           C  
ATOM    190  CE1 TYR A  27      44.477  56.707  -7.362  1.00 39.84           C  
ATOM    191  CE2 TYR A  27      45.145  57.505  -5.200  1.00 38.93           C  
ATOM    192  CZ  TYR A  27      44.992  56.474  -6.096  1.00 39.01           C  
ATOM    193  OH  TYR A  27      45.334  55.197  -5.727  1.00 38.57           O  
ATOM    194  N   ASP A  28      44.571  63.316  -8.227  1.00 44.50           N  
ATOM    195  CA  ASP A  28      44.281  64.706  -8.506  1.00 46.60           C  
ATOM    196  C   ASP A  28      45.441  65.546  -8.029  1.00 47.75           C  
ATOM    197  O   ASP A  28      46.510  65.019  -7.705  1.00 47.77           O  
ATOM    198  CB  ASP A  28      42.979  65.140  -7.822  1.00 47.23           C  
ATOM    199  CG  ASP A  28      42.923  64.722  -6.377  1.00 47.80           C  
ATOM    200  OD1 ASP A  28      43.661  65.315  -5.564  1.00 49.14           O  
ATOM    201  OD2 ASP A  28      42.148  63.794  -6.066  1.00 50.69           O  
ATOM    202  N   LYS A  29      45.218  66.854  -7.980  1.00 48.92           N  
ATOM    203  CA  LYS A  29      46.235  67.818  -7.575  1.00 49.80           C  
ATOM    204  C   LYS A  29      46.738  67.532  -6.146  1.00 50.00           C  
ATOM    205  O   LYS A  29      47.906  67.786  -5.827  1.00 50.32           O  
ATOM    206  CB  LYS A  29      45.649  69.230  -7.718  1.00 50.10           C  
ATOM    207  CG  LYS A  29      46.576  70.391  -7.411  1.00 51.81           C  
ATOM    208  CD  LYS A  29      45.776  71.699  -7.339  1.00 53.71           C  
ATOM    209  CE  LYS A  29      46.509  72.753  -6.507  1.00 55.04           C  
ATOM    210  NZ  LYS A  29      45.574  73.650  -5.739  1.00 55.82           N  
ATOM    211  N   HIS A  30      45.867  66.979  -5.298  1.00 50.25           N  
ATOM    212  CA  HIS A  30      46.219  66.743  -3.890  1.00 50.40           C  
ATOM    213  C   HIS A  30      46.147  65.277  -3.429  1.00 49.52           C  
ATOM    214  O   HIS A  30      46.208  65.006  -2.229  1.00 49.81           O  
ATOM    215  CB  HIS A  30      45.356  67.620  -2.965  1.00 50.93           C  
ATOM    216  CG  HIS A  30      45.571  69.093  -3.143  1.00 52.56           C  
ATOM    217  ND1 HIS A  30      46.767  69.716  -2.850  1.00 54.53           N  
ATOM    218  CD2 HIS A  30      44.731  70.071  -3.561  1.00 53.80           C  
ATOM    219  CE1 HIS A  30      46.658  71.011  -3.093  1.00 54.38           C  
ATOM    220  NE2 HIS A  30      45.433  71.252  -3.525  1.00 54.69           N  
ATOM    221  N   HIS A  31      46.019  64.340  -4.367  1.00 48.36           N  
ATOM    222  CA  HIS A  31      45.937  62.911  -4.024  1.00 47.18           C  
ATOM    223  C   HIS A  31      46.780  62.033  -4.954  1.00 45.57           C  
ATOM    224  O   HIS A  31      46.666  62.126  -6.177  1.00 45.28           O  
ATOM    225  CB  HIS A  31      44.481  62.416  -4.052  1.00 47.56           C  
ATOM    226  CG  HIS A  31      43.621  62.980  -2.964  1.00 48.93           C  
ATOM    227  ND1 HIS A  31      43.507  62.389  -1.724  1.00 49.99           N  
ATOM    228  CD2 HIS A  31      42.821  64.073  -2.936  1.00 49.69           C  
ATOM    229  CE1 HIS A  31      42.690  63.103  -0.973  1.00 49.81           C  
ATOM    230  NE2 HIS A  31      42.255  64.127  -1.686  1.00 50.76           N  
ATOM    231  N   ASP A  32      47.614  61.174  -4.373  1.00 43.64           N  
ATOM    232  CA  ASP A  32      48.302  60.149  -5.157  1.00 42.32           C  
ATOM    233  C   ASP A  32      48.351  58.781  -4.470  1.00 40.98           C  
ATOM    234  O   ASP A  32      48.017  58.647  -3.291  1.00 40.38           O  
ATOM    235  CB  ASP A  32      49.695  60.613  -5.619  1.00 42.51           C  
ATOM    236  CG  ASP A  32      50.636  60.940  -4.468  1.00 44.47           C  
ATOM    237  OD1 ASP A  32      50.700  60.172  -3.481  1.00 46.48           O  
ATOM    238  OD2 ASP A  32      51.346  61.964  -4.568  1.00 45.86           O  
ATOM    239  N   ALA A  33      48.758  57.775  -5.234  1.00 39.36           N  
ATOM    240  CA  ALA A  33      48.851  56.412  -4.738  1.00 38.46           C  
ATOM    241  C   ALA A  33      49.972  56.257  -3.688  1.00 37.66           C  
ATOM    242  O   ALA A  33      49.839  55.473  -2.746  1.00 37.43           O  
ATOM    243  CB  ALA A  33      49.023  55.451  -5.890  1.00 37.95           C  
ATOM    244  N   ALA A  34      51.038  57.048  -3.827  1.00 36.40           N  
ATOM    245  CA  ALA A  34      52.141  57.039  -2.867  1.00 35.61           C  
ATOM    246  C   ALA A  34      51.637  57.345  -1.468  1.00 35.05           C  
ATOM    247  O   ALA A  34      51.893  56.584  -0.534  1.00 34.82           O  
ATOM    248  CB  ALA A  34      53.245  58.027  -3.280  1.00 35.64           C  
ATOM    249  N   HIS A  35      50.894  58.445  -1.354  1.00 34.48           N  
ATOM    250  CA AHIS A  35      50.320  58.930  -0.090  0.50 34.14           C  
ATOM    251  CA BHIS A  35      50.364  58.886  -0.075  0.50 33.88           C  
ATOM    252  C   HIS A  35      49.220  58.007   0.425  1.00 33.44           C  
ATOM    253  O   HIS A  35      49.075  57.817   1.622  1.00 33.99           O  
ATOM    254  CB AHIS A  35      49.760  60.354  -0.271  0.50 34.25           C  
ATOM    255  CB BHIS A  35      49.974  60.368  -0.148  0.50 33.88           C  
ATOM    256  CG AHIS A  35      49.318  61.008   1.006  0.50 35.36           C  
ATOM    257  CG BHIS A  35      51.157  61.281  -0.240  0.50 33.76           C  
ATOM    258  ND1AHIS A  35      50.206  61.548   1.913  0.50 36.25           N  
ATOM    259  ND1BHIS A  35      51.752  61.839   0.870  0.50 33.36           N  
ATOM    260  CD2AHIS A  35      48.081  61.227   1.515  0.50 36.39           C  
ATOM    261  CD2BHIS A  35      51.886  61.693  -1.305  0.50 33.52           C  
ATOM    262  CE1AHIS A  35      49.536  62.060   2.931  0.50 36.31           C  
ATOM    263  CE1BHIS A  35      52.787  62.570   0.493  0.50 34.18           C  
ATOM    264  NE2AHIS A  35      48.245  61.882   2.713  0.50 36.66           N  
ATOM    265  NE2BHIS A  35      52.891  62.497  -0.823  0.50 33.83           N  
ATOM    266  N   GLU A  36      48.426  57.455  -0.487  1.00 32.68           N  
ATOM    267  CA  GLU A  36      47.422  56.450  -0.110  1.00 32.10           C  
ATOM    268  C   GLU A  36      48.079  55.270   0.639  1.00 31.59           C  
ATOM    269  O   GLU A  36      47.564  54.809   1.664  1.00 31.75           O  
ATOM    270  CB  GLU A  36      46.693  55.915  -1.336  1.00 32.00           C  
ATOM    271  CG  GLU A  36      45.573  54.940  -0.992  1.00 31.02           C  
ATOM    272  CD  GLU A  36      44.941  54.351  -2.219  1.00 33.44           C  
ATOM    273  OE1 GLU A  36      44.470  55.133  -3.070  1.00 33.20           O  
ATOM    274  OE2 GLU A  36      44.893  53.105  -2.335  1.00 32.78           O  
ATOM    275  N   ILE A  37      49.207  54.801   0.107  1.00 31.03           N  
ATOM    276  CA  ILE A  37      49.980  53.692   0.676  1.00 31.08           C  
ATOM    277  C   ILE A  37      50.424  54.031   2.096  1.00 30.97           C  
ATOM    278  O   ILE A  37      50.216  53.257   3.036  1.00 31.35           O  
ATOM    279  CB  ILE A  37      51.193  53.327  -0.250  1.00 30.70           C  
ATOM    280  CG1 ILE A  37      50.708  52.486  -1.420  1.00 31.22           C  
ATOM    281  CG2 ILE A  37      52.328  52.592   0.511  1.00 31.89           C  
ATOM    282  CD1 ILE A  37      51.577  52.529  -2.681  1.00 29.64           C  
ATOM    283  N   ILE A  38      51.017  55.207   2.256  1.00 31.01           N  
ATOM    284  CA  ILE A  38      51.547  55.621   3.547  1.00 30.46           C  
ATOM    285  C   ILE A  38      50.431  55.778   4.587  1.00 29.97           C  
ATOM    286  O   ILE A  38      50.560  55.319   5.740  1.00 28.41           O  
ATOM    287  CB  ILE A  38      52.417  56.894   3.400  1.00 30.66           C  
ATOM    288  CG1 ILE A  38      53.718  56.540   2.644  1.00 32.88           C  
ATOM    289  CG2 ILE A  38      52.730  57.478   4.757  1.00 31.86           C  
ATOM    290  CD1 ILE A  38      54.337  57.697   1.817  1.00 37.04           C  
ATOM    291  N   GLU A  39      49.318  56.376   4.164  1.00 29.06           N  
ATOM    292  CA  GLU A  39      48.131  56.488   5.026  1.00 29.78           C  
ATOM    293  C   GLU A  39      47.463  55.169   5.330  1.00 29.05           C  
ATOM    294  O   GLU A  39      46.903  54.989   6.419  1.00 29.91           O  
ATOM    295  CB  GLU A  39      47.101  57.446   4.429  1.00 29.81           C  
ATOM    296  CG  GLU A  39      47.656  58.854   4.264  1.00 32.69           C  
ATOM    297  CD  GLU A  39      47.873  59.550   5.594  1.00 35.89           C  
ATOM    298  OE1 GLU A  39      47.106  59.310   6.549  1.00 38.16           O  
ATOM    299  OE2 GLU A  39      48.813  60.343   5.683  1.00 40.66           O  
ATOM    300  N   THR A  40      47.496  54.250   4.373  1.00 28.38           N  
ATOM    301  CA  THR A  40      46.961  52.923   4.614  1.00 28.10           C  
ATOM    302  C   THR A  40      47.778  52.232   5.724  1.00 28.49           C  
ATOM    303  O   THR A  40      47.215  51.707   6.672  1.00 28.88           O  
ATOM    304  CB  THR A  40      46.881  52.123   3.298  1.00 27.76           C  
ATOM    305  OG1 THR A  40      45.859  52.709   2.474  1.00 27.01           O  
ATOM    306  CG2 THR A  40      46.574  50.627   3.550  1.00 27.39           C  
ATOM    307  N   ILE A  41      49.099  52.272   5.622  1.00 29.24           N  
ATOM    308  CA  ILE A  41      49.953  51.727   6.694  1.00 30.33           C  
ATOM    309  C   ILE A  41      49.651  52.397   8.040  1.00 30.63           C  
ATOM    310  O   ILE A  41      49.525  51.724   9.060  1.00 30.47           O  
ATOM    311  CB  ILE A  41      51.458  51.816   6.361  1.00 30.31           C  
ATOM    312  CG1 ILE A  41      51.797  50.894   5.183  1.00 31.09           C  
ATOM    313  CG2 ILE A  41      52.324  51.432   7.618  1.00 29.67           C  
ATOM    314  CD1 ILE A  41      52.904  51.397   4.272  1.00 35.08           C  
ATOM    315  N   ARG A  42      49.516  53.721   8.037  1.00 31.67           N  
ATOM    316  CA  ARG A  42      49.201  54.462   9.266  1.00 31.91           C  
ATOM    317  C   ARG A  42      47.899  54.003   9.923  1.00 31.79           C  
ATOM    318  O   ARG A  42      47.850  53.810  11.140  1.00 31.98           O  
ATOM    319  CB  ARG A  42      49.200  55.978   8.999  1.00 32.23           C  
ATOM    320  CG  ARG A  42      48.191  56.757   9.799  1.00 36.01           C  
ATOM    321  CD  ARG A  42      48.725  58.085  10.261  1.00 41.09           C  
ATOM    322  NE  ARG A  42      47.817  59.182   9.953  1.00 42.85           N  
ATOM    323  CZ  ARG A  42      46.630  59.394  10.525  1.00 44.50           C  
ATOM    324  NH1 ARG A  42      46.145  58.569  11.449  1.00 43.92           N  
ATOM    325  NH2 ARG A  42      45.915  60.446  10.151  1.00 44.86           N  
ATOM    326  N   TRP A  43      46.851  53.809   9.117  1.00 31.55           N  
ATOM    327  CA  TRP A  43      45.566  53.376   9.641  1.00 31.41           C  
ATOM    328  C   TRP A  43      45.575  51.943  10.136  1.00 31.70           C  
ATOM    329  O   TRP A  43      44.930  51.620  11.138  1.00 31.34           O  
ATOM    330  CB  TRP A  43      44.434  53.643   8.636  1.00 31.14           C  
ATOM    331  CG  TRP A  43      44.077  55.080   8.715  1.00 30.85           C  
ATOM    332  CD1 TRP A  43      44.382  56.071   7.822  1.00 30.27           C  
ATOM    333  CD2 TRP A  43      43.433  55.709   9.819  1.00 30.32           C  
ATOM    334  NE1 TRP A  43      43.940  57.286   8.303  1.00 30.38           N  
ATOM    335  CE2 TRP A  43      43.346  57.083   9.526  1.00 30.93           C  
ATOM    336  CE3 TRP A  43      42.889  55.232  11.022  1.00 31.29           C  
ATOM    337  CZ2 TRP A  43      42.738  57.995  10.396  1.00 31.68           C  
ATOM    338  CZ3 TRP A  43      42.302  56.139  11.895  1.00 32.05           C  
ATOM    339  CH2 TRP A  43      42.238  57.503  11.577  1.00 31.48           C  
ATOM    340  N   VAL A  44      46.315  51.081   9.447  1.00 31.51           N  
ATOM    341  CA  VAL A  44      46.456  49.714   9.954  1.00 31.25           C  
ATOM    342  C   VAL A  44      47.124  49.722  11.320  1.00 31.68           C  
ATOM    343  O   VAL A  44      46.661  49.039  12.225  1.00 31.95           O  
ATOM    344  CB  VAL A  44      47.125  48.751   8.944  1.00 30.77           C  
ATOM    345  CG1 VAL A  44      47.234  47.356   9.524  1.00 30.26           C  
ATOM    346  CG2 VAL A  44      46.301  48.697   7.659  1.00 28.51           C  
ATOM    347  N   CYS A  45      48.173  50.522  11.468  1.00 32.96           N  
ATOM    348  CA  CYS A  45      48.853  50.698  12.747  1.00 34.67           C  
ATOM    349  C   CYS A  45      47.895  51.185  13.828  1.00 35.58           C  
ATOM    350  O   CYS A  45      48.059  50.856  15.007  1.00 34.77           O  
ATOM    351  CB  CYS A  45      50.031  51.671  12.612  1.00 34.82           C  
ATOM    352  SG  CYS A  45      51.462  50.983  11.724  1.00 38.08           S  
ATOM    353  N   GLU A  46      46.894  51.965  13.425  1.00 36.86           N  
ATOM    354  CA  GLU A  46      45.855  52.375  14.363  1.00 38.82           C  
ATOM    355  C   GLU A  46      45.010  51.186  14.807  1.00 39.62           C  
ATOM    356  O   GLU A  46      44.745  51.032  15.997  1.00 39.92           O  
ATOM    357  CB  GLU A  46      44.995  53.512  13.785  1.00 39.11           C  
ATOM    358  CG  GLU A  46      45.746  54.831  13.660  1.00 40.54           C  
ATOM    359  CD  GLU A  46      46.333  55.335  14.987  1.00 44.86           C  
ATOM    360  OE1 GLU A  46      45.648  55.249  16.043  1.00 44.94           O  
ATOM    361  OE2 GLU A  46      47.485  55.835  14.969  1.00 45.70           O  
ATOM    362  N   GLU A  47      44.629  50.334  13.854  1.00 40.58           N  
ATOM    363  CA  GLU A  47      43.834  49.132  14.122  1.00 41.88           C  
ATOM    364  C   GLU A  47      44.505  48.127  15.049  1.00 42.62           C  
ATOM    365  O   GLU A  47      43.833  47.413  15.785  1.00 43.51           O  
ATOM    366  CB  GLU A  47      43.550  48.386  12.817  1.00 42.11           C  
ATOM    367  CG  GLU A  47      42.596  49.042  11.862  1.00 41.55           C  
ATOM    368  CD  GLU A  47      42.230  48.092  10.736  1.00 44.25           C  
ATOM    369  OE1 GLU A  47      43.108  47.768   9.898  1.00 42.36           O  
ATOM    370  OE2 GLU A  47      41.067  47.652  10.699  1.00 44.21           O  
ATOM    371  N   ILE A  48      45.824  48.020  14.955  1.00 43.44           N  
ATOM    372  CA  ILE A  48      46.562  47.009  15.700  1.00 44.06           C  
ATOM    373  C   ILE A  48      47.733  47.677  16.419  1.00 44.42           C  
ATOM    374  O   ILE A  48      48.745  47.999  15.797  1.00 44.41           O  
ATOM    375  CB  ILE A  48      47.061  45.847  14.766  1.00 44.07           C  
ATOM    376  CG1 ILE A  48      45.894  45.221  13.987  1.00 43.60           C  
ATOM    377  CG2 ILE A  48      47.763  44.773  15.581  1.00 44.56           C  
ATOM    378  CD1 ILE A  48      46.306  44.367  12.782  1.00 45.23           C  
ATOM    379  N   PRO A  49      47.591  47.905  17.736  1.00 45.10           N  
ATOM    380  CA  PRO A  49      48.644  48.517  18.560  1.00 45.56           C  
ATOM    381  C   PRO A  49      50.015  47.827  18.432  1.00 45.40           C  
ATOM    382  O   PRO A  49      51.039  48.501  18.325  1.00 45.52           O  
ATOM    383  CB  PRO A  49      48.089  48.367  19.981  1.00 45.85           C  
ATOM    384  CG  PRO A  49      46.606  48.436  19.790  1.00 46.02           C  
ATOM    385  CD  PRO A  49      46.364  47.663  18.515  1.00 45.56           C  
ATOM    386  N   ASP A  50      50.022  46.495  18.427  1.00 45.71           N  
ATOM    387  CA  ASP A  50      51.249  45.723  18.225  1.00 45.54           C  
ATOM    388  C   ASP A  50      51.987  46.149  16.965  1.00 45.16           C  
ATOM    389  O   ASP A  50      53.198  46.363  16.995  1.00 44.63           O  
ATOM    390  CB  ASP A  50      50.941  44.225  18.195  1.00 46.13           C  
ATOM    391  CG  ASP A  50      50.573  43.678  19.564  1.00 46.94           C  
ATOM    392  OD1 ASP A  50      51.247  44.041  20.553  1.00 49.51           O  
ATOM    393  OD2 ASP A  50      49.621  42.880  19.658  1.00 48.70           O  
ATOM    394  N   LEU A  51      51.242  46.306  15.873  1.00 45.23           N  
ATOM    395  CA  LEU A  51      51.816  46.751  14.611  1.00 45.76           C  
ATOM    396  C   LEU A  51      52.415  48.150  14.734  1.00 46.22           C  
ATOM    397  O   LEU A  51      53.520  48.401  14.242  1.00 46.07           O  
ATOM    398  CB  LEU A  51      50.788  46.662  13.473  1.00 45.47           C  
ATOM    399  CG  LEU A  51      51.205  47.163  12.086  1.00 45.97           C  
ATOM    400  CD1 LEU A  51      52.360  46.364  11.470  1.00 44.19           C  
ATOM    401  CD2 LEU A  51      50.015  47.160  11.164  1.00 45.25           C  
ATOM    402  N   LYS A  52      51.700  49.044  15.421  1.00 46.78           N  
ATOM    403  CA  LYS A  52      52.184  50.400  15.641  1.00 47.52           C  
ATOM    404  C   LYS A  52      53.509  50.346  16.387  1.00 47.74           C  
ATOM    405  O   LYS A  52      54.450  51.046  16.024  1.00 48.07           O  
ATOM    406  CB  LYS A  52      51.156  51.226  16.421  1.00 47.66           C  
ATOM    407  CG  LYS A  52      51.385  52.725  16.361  1.00 47.80           C  
ATOM    408  CD  LYS A  52      50.162  53.484  16.883  1.00 47.53           C  
ATOM    409  CE  LYS A  52      50.350  54.986  16.755  1.00 47.31           C  
ATOM    410  NZ  LYS A  52      49.349  55.733  17.579  1.00 49.50           N  
ATOM    411  N   LEU A  53      53.573  49.498  17.413  1.00 48.40           N  
ATOM    412  CA  LEU A  53      54.819  49.244  18.138  1.00 49.09           C  
ATOM    413  C   LEU A  53      55.938  48.905  17.182  1.00 49.16           C  
ATOM    414  O   LEU A  53      56.929  49.621  17.110  1.00 49.48           O  
ATOM    415  CB  LEU A  53      54.665  48.104  19.148  1.00 49.28           C  
ATOM    416  CG  LEU A  53      54.193  48.420  20.564  1.00 49.60           C  
ATOM    417  CD1 LEU A  53      54.069  47.137  21.355  1.00 48.89           C  
ATOM    418  CD2 LEU A  53      55.141  49.387  21.271  1.00 49.76           C  
ATOM    419  N   ALA A  54      55.773  47.817  16.437  1.00 49.46           N  
ATOM    420  CA  ALA A  54      56.783  47.399  15.478  1.00 49.64           C  
ATOM    421  C   ALA A  54      57.144  48.533  14.508  1.00 49.95           C  
ATOM    422  O   ALA A  54      58.309  48.718  14.171  1.00 49.29           O  
ATOM    423  CB  ALA A  54      56.316  46.151  14.724  1.00 49.72           C  
ATOM    424  N   MET A  55      56.147  49.308  14.078  1.00 50.57           N  
ATOM    425  CA  MET A  55      56.413  50.405  13.149  1.00 51.58           C  
ATOM    426  C   MET A  55      57.037  51.601  13.868  1.00 52.96           C  
ATOM    427  O   MET A  55      57.743  52.391  13.240  1.00 53.27           O  
ATOM    428  CB  MET A  55      55.160  50.808  12.357  1.00 50.99           C  
ATOM    429  CG  MET A  55      54.609  49.728  11.390  1.00 49.61           C  
ATOM    430  SD  MET A  55      55.696  49.149  10.058  1.00 46.39           S  
ATOM    431  CE  MET A  55      56.110  50.661   9.182  1.00 45.62           C  
ATOM    432  N   GLU A  56      56.766  51.723  15.174  1.00 54.65           N  
ATOM    433  CA  GLU A  56      57.416  52.708  16.050  1.00 56.23           C  
ATOM    434  C   GLU A  56      58.914  52.415  15.951  1.00 57.26           C  
ATOM    435  O   GLU A  56      59.711  53.273  15.540  1.00 57.14           O  
ATOM    436  CB  GLU A  56      56.946  52.525  17.506  1.00 56.42           C  
ATOM    437  CG  GLU A  56      56.399  53.765  18.231  1.00 57.51           C  
ATOM    438  CD  GLU A  56      54.896  53.666  18.559  1.00 59.22           C  
ATOM    439  OE1 GLU A  56      54.467  52.636  19.136  1.00 59.18           O  
ATOM    440  OE2 GLU A  56      54.146  54.629  18.262  1.00 58.39           O  
ATOM    441  N   ASN A  57      59.265  51.168  16.285  1.00 58.38           N  
ATOM    442  CA  ASN A  57      60.626  50.646  16.188  1.00 59.15           C  
ATOM    443  C   ASN A  57      61.093  50.497  14.741  1.00 59.74           C  
ATOM    444  O   ASN A  57      60.433  49.829  13.941  1.00 60.01           O  
ATOM    445  CB  ASN A  57      60.719  49.295  16.905  1.00 59.13           C  
ATOM    446  N   TYR A  58      62.231  51.124  14.430  1.00 60.03           N  
ATOM    447  CA  TYR A  58      62.853  51.129  13.094  1.00 60.19           C  
ATOM    448  C   TYR A  58      61.882  51.029  11.905  1.00 60.19           C  
ATOM    449  O   TYR A  58      61.459  49.935  11.504  1.00 60.44           O  
ATOM    450  CB  TYR A  58      63.972  50.084  13.001  1.00 60.21           C  
ATOM    451  N   LEU A  60      60.344  54.021  11.592  1.00 64.01           N  
ATOM    452  CA  LEU A  60      60.312  55.356  11.000  1.00 64.19           C  
ATOM    453  C   LEU A  60      61.503  55.567  10.074  1.00 64.24           C  
ATOM    454  O   LEU A  60      62.615  55.126  10.379  1.00 64.08           O  
ATOM    455  CB  LEU A  60      60.298  56.427  12.092  1.00 63.98           C  
ATOM    456  N   ILE A  61      61.257  56.237   8.947  1.00 64.54           N  
ATOM    457  CA  ILE A  61      62.288  56.514   7.932  1.00 64.98           C  
ATOM    458  C   ILE A  61      61.848  57.592   6.933  1.00 65.11           C  
ATOM    459  O   ILE A  61      60.651  57.784   6.695  1.00 65.42           O  
ATOM    460  CB  ILE A  61      62.689  55.238   7.146  1.00 64.88           C  
ATOM    461  N   ASP A  62      62.826  58.291   6.357  1.00 65.30           N  
ATOM    462  CA  ASP A  62      62.568  59.309   5.341  1.00 65.36           C  
ATOM    463  C   ASP A  62      62.060  58.644   4.067  1.00 65.37           C  
ATOM    464  O   ASP A  62      62.845  58.172   3.232  1.00 65.48           O  
ATOM    465  CB  ASP A  62      63.831  60.129   5.055  1.00 65.29           C  
ATOM    466  N   TYR A  63      60.739  58.577   3.940  1.00 65.18           N  
ATOM    467  CA  TYR A  63      60.121  58.007   2.748  1.00 65.14           C  
ATOM    468  C   TYR A  63      60.268  58.987   1.589  1.00 64.97           C  
ATOM    469  O   TYR A  63      59.846  60.143   1.683  1.00 64.94           O  
ATOM    470  CB  TYR A  63      58.643  57.677   2.994  1.00 65.04           C  
ATOM    471  N   ASP A  64      60.902  58.528   0.517  1.00 64.71           N  
ATOM    472  CA  ASP A  64      60.919  59.284  -0.723  1.00 64.54           C  
ATOM    473  C   ASP A  64      59.839  58.722  -1.640  1.00 64.30           C  
ATOM    474  O   ASP A  64      60.043  57.690  -2.292  1.00 64.02           O  
ATOM    475  CB  ASP A  64      62.293  59.220  -1.402  1.00 64.68           C  
ATOM    476  CG  ASP A  64      62.423  60.213  -2.544  1.00 65.02           C  
ATOM    477  OD1 ASP A  64      61.722  61.252  -2.521  1.00 65.67           O  
ATOM    478  OD2 ASP A  64      63.228  59.963  -3.463  1.00 64.80           O  
ATOM    479  N   THR A  65      58.691  59.402  -1.674  1.00 64.02           N  
ATOM    480  CA  THR A  65      57.535  58.968  -2.471  1.00 63.85           C  
ATOM    481  C   THR A  65      57.874  59.009  -3.953  1.00 63.80           C  
ATOM    482  O   THR A  65      57.078  58.601  -4.800  1.00 64.01           O  
ATOM    483  CB  THR A  65      56.285  59.855  -2.221  1.00 63.91           C  
ATOM    484  OG1 THR A  65      56.449  61.121  -2.877  1.00 63.64           O  
ATOM    485  CG2 THR A  65      56.036  60.064  -0.719  1.00 63.55           C  
ATOM    486  N   LYS A  66      59.067  59.519  -4.241  1.00 63.62           N  
ATOM    487  CA  LYS A  66      59.599  59.609  -5.586  1.00 63.56           C  
ATOM    488  C   LYS A  66      60.320  58.314  -5.936  1.00 63.24           C  
ATOM    489  O   LYS A  66      60.289  57.875  -7.085  1.00 63.42           O  
ATOM    490  CB  LYS A  66      60.577  60.789  -5.694  1.00 63.71           C  
ATOM    491  CG  LYS A  66      60.099  62.106  -5.058  1.00 64.26           C  
ATOM    492  CD  LYS A  66      59.241  62.937  -6.007  1.00 65.33           C  
ATOM    493  CE  LYS A  66      58.980  64.335  -5.447  1.00 65.71           C  
ATOM    494  NZ  LYS A  66      58.690  65.307  -6.546  1.00 65.90           N  
ATOM    495  N   SER A  67      60.947  57.698  -4.933  1.00 62.68           N  
ATOM    496  CA  SER A  67      61.846  56.559  -5.140  1.00 62.30           C  
ATOM    497  C   SER A  67      61.189  55.195  -4.926  1.00 61.76           C  
ATOM    498  O   SER A  67      60.616  54.932  -3.860  1.00 61.51           O  
ATOM    499  CB  SER A  67      63.082  56.695  -4.239  1.00 62.29           C  
ATOM    500  OG  SER A  67      63.925  55.557  -4.346  1.00 63.02           O  
ATOM    501  N   PHE A  68      61.304  54.327  -5.936  1.00 61.09           N  
ATOM    502  CA  PHE A  68      60.760  52.970  -5.869  1.00 60.56           C  
ATOM    503  C   PHE A  68      61.403  52.176  -4.745  1.00 60.10           C  
ATOM    504  O   PHE A  68      60.697  51.609  -3.908  1.00 59.64           O  
ATOM    505  CB  PHE A  68      60.921  52.218  -7.197  1.00 60.63           C  
ATOM    506  CG  PHE A  68      60.443  50.786  -7.141  1.00 61.48           C  
ATOM    507  CD1 PHE A  68      59.105  50.471  -7.374  1.00 62.21           C  
ATOM    508  CD2 PHE A  68      61.328  49.752  -6.843  1.00 62.33           C  
ATOM    509  CE1 PHE A  68      58.649  49.147  -7.318  1.00 62.42           C  
ATOM    510  CE2 PHE A  68      60.889  48.429  -6.786  1.00 62.89           C  
ATOM    511  CZ  PHE A  68      59.540  48.127  -7.021  1.00 63.32           C  
ATOM    512  N   GLU A  69      62.739  52.141  -4.740  1.00 59.46           N  
ATOM    513  CA  GLU A  69      63.505  51.470  -3.689  1.00 59.01           C  
ATOM    514  C   GLU A  69      62.983  51.880  -2.325  1.00 58.00           C  
ATOM    515  O   GLU A  69      62.723  51.025  -1.474  1.00 58.02           O  
ATOM    516  CB  GLU A  69      65.001  51.808  -3.790  1.00 59.46           C  
ATOM    517  CG  GLU A  69      65.812  50.870  -4.685  1.00 61.22           C  
ATOM    518  CD  GLU A  69      67.310  51.153  -4.626  1.00 63.82           C  
ATOM    519  OE1 GLU A  69      67.911  51.390  -5.697  1.00 64.96           O  
ATOM    520  OE2 GLU A  69      67.887  51.154  -3.512  1.00 65.17           O  
ATOM    521  N   SER A  70      62.811  53.189  -2.144  1.00 56.68           N  
ATOM    522  CA  SER A  70      62.357  53.765  -0.884  1.00 55.81           C  
ATOM    523  C   SER A  70      60.941  53.296  -0.534  1.00 55.06           C  
ATOM    524  O   SER A  70      60.650  52.988   0.627  1.00 54.74           O  
ATOM    525  CB  SER A  70      62.419  55.291  -0.954  1.00 55.88           C  
ATOM    526  OG  SER A  70      62.310  55.891   0.329  1.00 56.94           O  
ATOM    527  N   MET A  71      60.071  53.234  -1.543  1.00 54.01           N  
ATOM    528  CA  MET A  71      58.679  52.828  -1.325  1.00 52.86           C  
ATOM    529  C   MET A  71      58.570  51.313  -1.090  1.00 52.31           C  
ATOM    530  O   MET A  71      57.843  50.874  -0.190  1.00 51.99           O  
ATOM    531  CB  MET A  71      57.767  53.309  -2.462  1.00 52.55           C  
ATOM    532  CG  MET A  71      57.546  54.829  -2.495  1.00 50.77           C  
ATOM    533  SD  MET A  71      56.857  55.516  -0.970  1.00 49.53           S  
ATOM    534  CE  MET A  71      55.158  54.940  -1.104  1.00 48.15           C  
ATOM    535  N   GLN A  72      59.314  50.535  -1.879  1.00 51.73           N  
ATOM    536  CA  GLN A  72      59.447  49.094  -1.666  1.00 51.39           C  
ATOM    537  C   GLN A  72      59.989  48.777  -0.274  1.00 50.98           C  
ATOM    538  O   GLN A  72      59.512  47.856   0.389  1.00 50.97           O  
ATOM    539  CB  GLN A  72      60.341  48.472  -2.731  1.00 51.47           C  
ATOM    540  CG  GLN A  72      60.659  47.004  -2.489  1.00 51.70           C  
ATOM    541  CD  GLN A  72      61.260  46.337  -3.706  1.00 51.62           C  
ATOM    542  OE1 GLN A  72      62.287  46.774  -4.222  1.00 51.58           O  
ATOM    543  NE2 GLN A  72      60.625  45.266  -4.169  1.00 50.74           N  
ATOM    544  N   ARG A  73      60.984  49.551   0.155  1.00 50.47           N  
ATOM    545  CA  ARG A  73      61.555  49.435   1.491  1.00 49.30           C  
ATOM    546  C   ARG A  73      60.497  49.618   2.591  1.00 48.03           C  
ATOM    547  O   ARG A  73      60.413  48.791   3.500  1.00 48.11           O  
ATOM    548  CB  ARG A  73      62.705  50.438   1.657  1.00 50.19           C  
ATOM    549  CG  ARG A  73      63.580  50.230   2.880  1.00 51.24           C  
ATOM    550  CD  ARG A  73      64.720  51.254   2.955  1.00 54.90           C  
ATOM    551  NE  ARG A  73      65.288  51.270   4.301  1.00 56.98           N  
ATOM    552  CZ  ARG A  73      66.453  51.808   4.654  1.00 58.74           C  
ATOM    553  NH1 ARG A  73      67.245  52.412   3.768  1.00 58.95           N  
ATOM    554  NH2 ARG A  73      66.824  51.734   5.927  1.00 59.91           N  
ATOM    555  N   LEU A  74      59.700  50.690   2.509  1.00 46.00           N  
ATOM    556  CA  LEU A  74      58.658  50.971   3.511  1.00 44.17           C  
ATOM    557  C   LEU A  74      57.556  49.895   3.527  1.00 42.81           C  
ATOM    558  O   LEU A  74      57.083  49.508   4.593  1.00 43.06           O  
ATOM    559  CB  LEU A  74      58.050  52.374   3.315  1.00 44.07           C  
ATOM    560  CG  LEU A  74      56.720  52.677   4.035  1.00 43.74           C  
ATOM    561  CD1 LEU A  74      56.928  53.058   5.499  1.00 41.03           C  
ATOM    562  CD2 LEU A  74      55.933  53.768   3.305  1.00 44.27           C  
ATOM    563  N   CYS A  75      57.180  49.420   2.345  1.00 41.10           N  
ATOM    564  CA  CYS A  75      56.167  48.382   2.177  1.00 40.15           C  
ATOM    565  C   CYS A  75      56.640  47.071   2.823  1.00 39.90           C  
ATOM    566  O   CYS A  75      55.849  46.355   3.444  1.00 38.88           O  
ATOM    567  CB  CYS A  75      55.878  48.156   0.688  1.00 39.98           C  
ATOM    568  SG  CYS A  75      54.818  49.412  -0.141  1.00 40.63           S  
ATOM    569  N   ASP A  76      57.939  46.787   2.660  1.00 39.02           N  
ATOM    570  CA  ASP A  76      58.599  45.625   3.250  1.00 38.63           C  
ATOM    571  C   ASP A  76      58.548  45.660   4.756  1.00 37.56           C  
ATOM    572  O   ASP A  76      58.192  44.670   5.375  1.00 37.38           O  
ATOM    573  CB  ASP A  76      60.055  45.545   2.784  1.00 39.49           C  
ATOM    574  CG  ASP A  76      60.178  45.106   1.359  1.00 41.19           C  
ATOM    575  OD1 ASP A  76      59.238  44.465   0.860  1.00 46.07           O  
ATOM    576  OD2 ASP A  76      61.210  45.404   0.721  1.00 46.04           O  
ATOM    577  N   LYS A  77      58.879  46.814   5.340  1.00 37.06           N  
ATOM    578  CA  LYS A  77      58.853  46.982   6.795  1.00 36.38           C  
ATOM    579  C   LYS A  77      57.469  46.690   7.368  1.00 35.53           C  
ATOM    580  O   LYS A  77      57.346  46.049   8.429  1.00 35.63           O  
ATOM    581  CB  LYS A  77      59.355  48.375   7.234  1.00 36.75           C  
ATOM    582  CG  LYS A  77      60.763  48.734   6.729  1.00 39.84           C  
ATOM    583  CD  LYS A  77      61.465  49.802   7.577  1.00 43.49           C  
ATOM    584  CE  LYS A  77      62.866  50.161   6.997  1.00 45.10           C  
ATOM    585  NZ  LYS A  77      63.799  48.978   6.933  1.00 48.32           N  
ATOM    586  N   TYR A  78      56.437  47.159   6.663  1.00 33.81           N  
ATOM    587  CA  TYR A  78      55.044  46.901   7.025  1.00 31.64           C  
ATOM    588  C   TYR A  78      54.673  45.428   6.869  1.00 31.31           C  
ATOM    589  O   TYR A  78      54.095  44.819   7.775  1.00 29.94           O  
ATOM    590  CB  TYR A  78      54.089  47.773   6.195  1.00 30.46           C  
ATOM    591  CG  TYR A  78      52.642  47.314   6.255  1.00 29.47           C  
ATOM    592  CD1 TYR A  78      51.823  47.669   7.325  1.00 26.77           C  
ATOM    593  CD2 TYR A  78      52.091  46.542   5.233  1.00 27.71           C  
ATOM    594  CE1 TYR A  78      50.493  47.235   7.395  1.00 27.18           C  
ATOM    595  CE2 TYR A  78      50.770  46.110   5.287  1.00 28.46           C  
ATOM    596  CZ  TYR A  78      49.976  46.458   6.375  1.00 26.97           C  
ATOM    597  OH  TYR A  78      48.665  46.032   6.444  1.00 28.62           O  
ATOM    598  N   ASN A  79      54.994  44.870   5.708  1.00 31.26           N  
ATOM    599  CA  ASN A  79      54.691  43.468   5.428  1.00 31.76           C  
ATOM    600  C   ASN A  79      55.365  42.477   6.382  1.00 31.91           C  
ATOM    601  O   ASN A  79      54.750  41.491   6.776  1.00 31.84           O  
ATOM    602  CB  ASN A  79      55.022  43.136   3.976  1.00 32.01           C  
ATOM    603  CG  ASN A  79      54.046  43.750   3.017  1.00 32.57           C  
ATOM    604  OD1 ASN A  79      52.883  44.001   3.367  1.00 37.27           O  
ATOM    605  ND2 ASN A  79      54.497  44.003   1.799  1.00 32.96           N  
ATOM    606  N   ARG A  80      56.616  42.755   6.748  1.00 32.11           N  
ATOM    607  CA  ARG A  80      57.347  41.968   7.761  1.00 32.34           C  
ATOM    608  C   ARG A  80      56.704  42.093   9.132  1.00 32.02           C  
ATOM    609  O   ARG A  80      56.543  41.099   9.853  1.00 31.76           O  
ATOM    610  CB  ARG A  80      58.833  42.396   7.829  1.00 32.43           C  
ATOM    611  CG  ARG A  80      59.584  42.179   6.522  1.00 34.64           C  
ATOM    612  CD  ARG A  80      61.087  42.191   6.669  1.00 39.08           C  
ATOM    613  NE  ARG A  80      61.539  43.256   7.567  1.00 42.99           N  
ATOM    614  CZ  ARG A  80      62.062  44.412   7.175  1.00 43.98           C  
ATOM    615  NH1 ARG A  80      62.423  45.313   8.090  1.00 44.68           N  
ATOM    616  NH2 ARG A  80      62.221  44.675   5.885  1.00 46.10           N  
ATOM    617  N   ALA A  81      56.331  43.320   9.501  1.00 32.11           N  
ATOM    618  CA  ALA A  81      55.606  43.527  10.749  1.00 31.56           C  
ATOM    619  C   ALA A  81      54.253  42.818  10.782  1.00 30.91           C  
ATOM    620  O   ALA A  81      53.895  42.233  11.794  1.00 30.97           O  
ATOM    621  CB  ALA A  81      55.457  45.005  11.056  1.00 32.35           C  
ATOM    622  N   ILE A  82      53.509  42.857   9.682  1.00 30.72           N  
ATOM    623  CA  ILE A  82      52.279  42.058   9.551  1.00 31.01           C  
ATOM    624  C   ILE A  82      52.532  40.527   9.723  1.00 31.23           C  
ATOM    625  O   ILE A  82      51.717  39.808  10.297  1.00 30.44           O  
ATOM    626  CB  ILE A  82      51.604  42.306   8.177  1.00 31.06           C  
ATOM    627  CG1 ILE A  82      51.000  43.718   8.083  1.00 31.51           C  
ATOM    628  CG2 ILE A  82      50.511  41.304   7.917  1.00 30.65           C  
ATOM    629  CD1 ILE A  82      49.792  43.957   8.982  1.00 30.76           C  
ATOM    630  N   ASP A  83      53.653  40.036   9.213  1.00 32.07           N  
ATOM    631  CA  ASP A  83      53.959  38.608   9.344  1.00 32.88           C  
ATOM    632  C   ASP A  83      54.129  38.268  10.811  1.00 32.80           C  
ATOM    633  O   ASP A  83      53.484  37.359  11.319  1.00 32.74           O  
ATOM    634  CB  ASP A  83      55.223  38.239   8.560  1.00 33.08           C  
ATOM    635  CG  ASP A  83      54.982  38.163   7.068  1.00 34.20           C  
ATOM    636  OD1 ASP A  83      53.826  37.944   6.647  1.00 37.45           O  
ATOM    637  OD2 ASP A  83      55.957  38.338   6.311  1.00 37.04           O  
ATOM    638  N   SER A  84      54.965  39.036  11.499  1.00 33.68           N  
ATOM    639  CA  SER A  84      55.182  38.811  12.916  1.00 35.00           C  
ATOM    640  C   SER A  84      53.907  38.923  13.754  1.00 35.27           C  
ATOM    641  O   SER A  84      53.713  38.133  14.673  1.00 35.65           O  
ATOM    642  CB  SER A  84      56.316  39.689  13.463  1.00 35.40           C  
ATOM    643  OG  SER A  84      55.944  41.046  13.597  1.00 38.66           O  
ATOM    644  N   ILE A  85      53.026  39.874  13.426  1.00 35.20           N  
ATOM    645  CA  ILE A  85      51.738  39.977  14.144  1.00 35.41           C  
ATOM    646  C   ILE A  85      50.886  38.738  13.960  1.00 34.80           C  
ATOM    647  O   ILE A  85      50.272  38.263  14.922  1.00 34.96           O  
ATOM    648  CB  ILE A  85      50.919  41.277  13.802  1.00 35.21           C  
ATOM    649  CG1 ILE A  85      51.163  42.349  14.853  1.00 37.09           C  
ATOM    650  CG2 ILE A  85      49.440  41.004  13.816  1.00 34.59           C  
ATOM    651  CD1 ILE A  85      52.363  43.225  14.582  1.00 38.76           C  
ATOM    652  N   HIS A  86      50.857  38.203  12.741  1.00 35.00           N  
ATOM    653  CA  HIS A  86      50.103  36.975  12.475  1.00 35.46           C  
ATOM    654  C   HIS A  86      50.653  35.753  13.237  1.00 35.78           C  
ATOM    655  O   HIS A  86      49.897  34.858  13.595  1.00 35.63           O  
ATOM    656  CB  HIS A  86      50.013  36.691  10.972  1.00 35.63           C  
ATOM    657  CG  HIS A  86      49.119  37.646  10.234  1.00 37.16           C  
ATOM    658  ND1 HIS A  86      49.223  37.873   8.877  1.00 36.81           N  
ATOM    659  CD2 HIS A  86      48.121  38.450  10.676  1.00 37.66           C  
ATOM    660  CE1 HIS A  86      48.311  38.757   8.511  1.00 39.17           C  
ATOM    661  NE2 HIS A  86      47.627  39.121   9.584  1.00 38.61           N  
ATOM    662  N   GLN A  87      51.960  35.736  13.473  1.00 36.70           N  
ATOM    663  CA  GLN A  87      52.601  34.697  14.293  1.00 37.86           C  
ATOM    664  C   GLN A  87      52.218  34.886  15.761  1.00 39.04           C  
ATOM    665  O   GLN A  87      51.881  33.921  16.458  1.00 39.48           O  
ATOM    666  CB  GLN A  87      54.128  34.742  14.134  1.00 37.22           C  
ATOM    667  CG  GLN A  87      54.685  34.007  12.893  1.00 36.00           C  
ATOM    668  CD  GLN A  87      54.239  32.549  12.792  1.00 34.45           C  
ATOM    669  OE1 GLN A  87      54.017  31.884  13.792  1.00 35.27           O  
ATOM    670  NE2 GLN A  87      54.134  32.046  11.569  1.00 35.36           N  
ATOM    671  N   LEU A  88      52.264  36.141  16.213  1.00 40.19           N  
ATOM    672  CA  LEU A  88      51.817  36.526  17.553  1.00 41.33           C  
ATOM    673  C   LEU A  88      50.414  36.000  17.840  1.00 41.78           C  
ATOM    674  O   LEU A  88      50.152  35.438  18.907  1.00 42.39           O  
ATOM    675  CB  LEU A  88      51.854  38.056  17.687  1.00 41.62           C  
ATOM    676  CG  LEU A  88      52.258  38.685  19.011  1.00 42.41           C  
ATOM    677  CD1 LEU A  88      53.514  38.012  19.550  1.00 42.51           C  
ATOM    678  CD2 LEU A  88      52.508  40.202  18.809  1.00 43.05           C  
ATOM    679  N   TRP A  89      49.515  36.172  16.876  1.00 42.69           N  
ATOM    680  CA  TRP A  89      48.149  35.666  16.999  1.00 43.16           C  
ATOM    681  C   TRP A  89      48.061  34.129  17.008  1.00 44.19           C  
ATOM    682  O   TRP A  89      47.057  33.572  17.446  1.00 44.60           O  
ATOM    683  CB  TRP A  89      47.238  36.252  15.917  1.00 42.85           C  
ATOM    684  CG  TRP A  89      47.100  37.781  15.901  1.00 42.03           C  
ATOM    685  CD1 TRP A  89      47.517  38.676  16.858  1.00 41.53           C  
ATOM    686  CD2 TRP A  89      46.458  38.556  14.888  1.00 40.95           C  
ATOM    687  NE1 TRP A  89      47.190  39.961  16.485  1.00 40.04           N  
ATOM    688  CE2 TRP A  89      46.536  39.913  15.281  1.00 41.66           C  
ATOM    689  CE3 TRP A  89      45.834  38.237  13.675  1.00 41.76           C  
ATOM    690  CZ2 TRP A  89      46.015  40.947  14.497  1.00 40.27           C  
ATOM    691  CZ3 TRP A  89      45.314  39.264  12.904  1.00 40.77           C  
ATOM    692  CH2 TRP A  89      45.410  40.598  13.318  1.00 41.27           C  
ATOM    693  N   LYS A  90      49.104  33.442  16.541  1.00 45.49           N  
ATOM    694  CA  LYS A  90      49.156  31.973  16.669  1.00 46.22           C  
ATOM    695  C   LYS A  90      49.476  31.527  18.104  1.00 46.86           C  
ATOM    696  O   LYS A  90      49.063  30.454  18.541  1.00 47.52           O  
ATOM    697  CB  LYS A  90      50.151  31.363  15.674  1.00 46.47           C  
ATOM    698  CG  LYS A  90      49.677  31.361  14.225  1.00 45.12           C  
ATOM    699  CD  LYS A  90      50.793  30.939  13.283  1.00 44.16           C  
ATOM    700  CE  LYS A  90      50.412  31.172  11.829  1.00 43.41           C  
ATOM    701  NZ  LYS A  90      49.302  30.289  11.404  1.00 43.85           N  
ATOM    702  N   GLY A  91      50.209  32.360  18.830  1.00 48.08           N  
ATOM    703  CA  GLY A  91      50.484  32.131  20.237  1.00 49.62           C  
ATOM    704  C   GLY A  91      49.290  32.466  21.116  1.00 50.77           C  
ATOM    705  O   GLY A  91      48.151  32.094  20.820  1.00 50.75           O  
ATOM    706  N   THR A  92      49.553  33.182  22.201  1.00 52.14           N  
ATOM    707  CA  THR A  92      48.520  33.479  23.193  1.00 53.52           C  
ATOM    708  C   THR A  92      47.778  34.786  22.906  1.00 54.15           C  
ATOM    709  O   THR A  92      46.599  34.912  23.244  1.00 54.52           O  
ATOM    710  CB  THR A  92      49.101  33.501  24.621  1.00 53.36           C  
ATOM    711  OG1 THR A  92      50.268  34.329  24.648  1.00 54.52           O  
ATOM    712  CG2 THR A  92      49.485  32.087  25.067  1.00 54.47           C  
ATOM    713  N   THR A  93      48.484  35.741  22.286  1.00 55.01           N  
ATOM    714  CA  THR A  93      47.957  37.071  21.927  1.00 55.44           C  
ATOM    715  C   THR A  93      46.588  37.017  21.236  1.00 55.51           C  
ATOM    716  O   THR A  93      46.374  36.231  20.310  1.00 55.61           O  
ATOM    717  CB  THR A  93      48.965  37.843  21.029  1.00 55.55           C  
ATOM    718  OG1 THR A  93      50.178  38.077  21.758  1.00 56.01           O  
ATOM    719  CG2 THR A  93      48.397  39.188  20.557  1.00 55.63           C  
ATOM    720  N   GLN A  94      45.666  37.854  21.707  1.00 55.72           N  
ATOM    721  CA  GLN A  94      44.355  37.994  21.080  1.00 55.80           C  
ATOM    722  C   GLN A  94      44.510  38.603  19.691  1.00 55.06           C  
ATOM    723  O   GLN A  94      45.191  39.620  19.537  1.00 55.02           O  
ATOM    724  CB  GLN A  94      43.422  38.861  21.946  1.00 56.36           C  
ATOM    725  CG  GLN A  94      43.193  38.340  23.375  1.00 57.53           C  
ATOM    726  CD  GLN A  94      42.241  37.151  23.442  1.00 59.71           C  
ATOM    727  OE1 GLN A  94      42.395  36.160  22.715  1.00 60.25           O  
ATOM    728  NE2 GLN A  94      41.252  37.241  24.330  1.00 59.53           N  
ATOM    729  N   PRO A  95      43.903  37.969  18.669  1.00 54.68           N  
ATOM    730  CA  PRO A  95      43.898  38.566  17.329  1.00 54.16           C  
ATOM    731  C   PRO A  95      42.963  39.766  17.276  1.00 53.88           C  
ATOM    732  O   PRO A  95      42.181  39.974  18.214  1.00 53.76           O  
ATOM    733  CB  PRO A  95      43.367  37.440  16.430  1.00 54.10           C  
ATOM    734  CG  PRO A  95      42.588  36.555  17.347  1.00 54.93           C  
ATOM    735  CD  PRO A  95      43.285  36.630  18.683  1.00 54.62           C  
ATOM    736  N   MET A  96      43.057  40.548  16.198  1.00 53.04           N  
ATOM    737  CA  MET A  96      42.173  41.692  15.977  1.00 52.37           C  
ATOM    738  C   MET A  96      40.728  41.221  16.009  1.00 51.74           C  
ATOM    739  O   MET A  96      40.373  40.219  15.380  1.00 51.97           O  
ATOM    740  CB  MET A  96      42.479  42.383  14.635  1.00 52.30           C  
ATOM    741  CG  MET A  96      41.888  43.791  14.481  1.00 52.63           C  
ATOM    742  SD  MET A  96      42.068  44.491  12.815  1.00 52.11           S  
ATOM    743  CE  MET A  96      40.483  44.107  12.075  1.00 50.23           C  
ATOM    744  N   LYS A  97      39.908  41.938  16.770  1.00 50.96           N  
ATOM    745  CA  LYS A  97      38.479  41.681  16.825  1.00 49.82           C  
ATOM    746  C   LYS A  97      37.929  41.822  15.408  1.00 49.41           C  
ATOM    747  O   LYS A  97      38.223  42.793  14.702  1.00 49.20           O  
ATOM    748  CB  LYS A  97      37.810  42.661  17.792  1.00 49.70           C  
ATOM    749  CG  LYS A  97      36.379  42.318  18.185  1.00 49.22           C  
ATOM    750  CD  LYS A  97      35.737  43.488  18.940  1.00 47.17           C  
ATOM    751  CE  LYS A  97      34.205  43.372  18.967  1.00 45.81           C  
ATOM    752  NZ  LYS A  97      33.711  42.335  19.897  1.00 46.69           N  
ATOM    753  N   LEU A  98      37.170  40.824  14.976  1.00 48.68           N  
ATOM    754  CA  LEU A  98      36.641  40.827  13.627  1.00 48.09           C  
ATOM    755  C   LEU A  98      35.256  41.466  13.573  1.00 47.76           C  
ATOM    756  O   LEU A  98      34.626  41.695  14.609  1.00 47.24           O  
ATOM    757  CB  LEU A  98      36.648  39.414  13.044  1.00 48.47           C  
ATOM    758  CG  LEU A  98      38.039  38.758  12.994  1.00 48.54           C  
ATOM    759  CD1 LEU A  98      37.997  37.439  12.246  1.00 48.45           C  
ATOM    760  CD2 LEU A  98      39.079  39.707  12.363  1.00 48.26           C  
ATOM    761  N   ASN A  99      34.816  41.761  12.352  1.00 47.18           N  
ATOM    762  CA  ASN A  99      33.538  42.421  12.070  1.00 46.52           C  
ATOM    763  C   ASN A  99      33.060  43.517  13.044  1.00 44.96           C  
ATOM    764  O   ASN A  99      31.899  43.550  13.452  1.00 44.81           O  
ATOM    765  CB  ASN A  99      32.430  41.401  11.693  1.00 47.35           C  
ATOM    766  CG  ASN A  99      31.919  40.571  12.884  1.00 49.15           C  
ATOM    767  OD1 ASN A  99      32.206  40.855  14.048  1.00 50.69           O  
ATOM    768  ND2 ASN A  99      31.130  39.545  12.576  1.00 50.25           N  
ATOM    769  N   THR A 100      33.973  44.406  13.418  1.00 42.61           N  
ATOM    770  CA  THR A 100      33.564  45.676  13.986  1.00 40.82           C  
ATOM    771  C   THR A 100      33.479  46.716  12.861  1.00 39.15           C  
ATOM    772  O   THR A 100      34.109  46.574  11.810  1.00 37.83           O  
ATOM    773  CB  THR A 100      34.511  46.174  15.091  1.00 40.98           C  
ATOM    774  OG1 THR A 100      35.777  46.509  14.522  1.00 42.96           O  
ATOM    775  CG2 THR A 100      34.713  45.103  16.157  1.00 41.15           C  
ATOM    776  N   ARG A 101      32.666  47.739  13.096  1.00 37.47           N  
ATOM    777  CA  ARG A 101      32.551  48.882  12.212  1.00 36.04           C  
ATOM    778  C   ARG A 101      33.798  49.741  12.320  1.00 34.91           C  
ATOM    779  O   ARG A 101      34.398  49.820  13.384  1.00 34.12           O  
ATOM    780  CB  ARG A 101      31.316  49.712  12.591  1.00 36.71           C  
ATOM    781  CG  ARG A 101      30.017  48.905  12.543  1.00 37.41           C  
ATOM    782  CD  ARG A 101      29.481  48.840  11.136  1.00 42.66           C  
ATOM    783  NE  ARG A 101      28.265  48.035  11.005  1.00 46.04           N  
ATOM    784  CZ  ARG A 101      27.137  48.235  11.689  1.00 46.49           C  
ATOM    785  NH1 ARG A 101      27.058  49.209  12.586  1.00 46.54           N  
ATOM    786  NH2 ARG A 101      26.093  47.439  11.483  1.00 44.01           N  
ATOM    787  N   PRO A 102      34.188  50.390  11.218  1.00 34.17           N  
ATOM    788  CA  PRO A 102      35.419  51.173  11.240  1.00 34.15           C  
ATOM    789  C   PRO A 102      35.225  52.439  12.061  1.00 34.30           C  
ATOM    790  O   PRO A 102      34.106  52.946  12.167  1.00 34.52           O  
ATOM    791  CB  PRO A 102      35.641  51.515   9.760  1.00 33.71           C  
ATOM    792  CG  PRO A 102      34.246  51.534   9.162  1.00 34.56           C  
ATOM    793  CD  PRO A 102      33.459  50.506   9.934  1.00 33.85           C  
ATOM    794  N   SER A 103      36.301  52.944  12.644  1.00 34.34           N  
ATOM    795  CA  SER A 103      36.260  54.235  13.297  1.00 33.89           C  
ATOM    796  C   SER A 103      35.970  55.289  12.233  1.00 33.90           C  
ATOM    797  O   SER A 103      36.202  55.051  11.040  1.00 33.76           O  
ATOM    798  CB  SER A 103      37.617  54.535  13.916  1.00 34.22           C  
ATOM    799  OG  SER A 103      38.534  54.937  12.906  1.00 34.83           O  
ATOM    800  N   THR A 104      35.512  56.458  12.668  1.00 33.12           N  
ATOM    801  CA  THR A 104      35.232  57.571  11.764  1.00 33.32           C  
ATOM    802  C   THR A 104      36.447  57.935  10.924  1.00 32.62           C  
ATOM    803  O   THR A 104      36.347  58.086   9.702  1.00 33.22           O  
ATOM    804  CB  THR A 104      34.773  58.808  12.573  1.00 32.95           C  
ATOM    805  OG1 THR A 104      33.562  58.477  13.228  1.00 33.24           O  
ATOM    806  CG2 THR A 104      34.553  60.022  11.678  1.00 31.81           C  
ATOM    807  N   GLY A 105      37.591  58.082  11.584  1.00 32.27           N  
ATOM    808  CA  GLY A 105      38.844  58.372  10.897  1.00 30.54           C  
ATOM    809  C   GLY A 105      39.270  57.289   9.902  1.00 29.92           C  
ATOM    810  O   GLY A 105      39.759  57.601   8.812  1.00 29.96           O  
ATOM    811  N   LEU A 106      39.100  56.017  10.264  1.00 29.26           N  
ATOM    812  CA  LEU A 106      39.373  54.959   9.311  1.00 27.75           C  
ATOM    813  C   LEU A 106      38.388  55.009   8.136  1.00 27.52           C  
ATOM    814  O   LEU A 106      38.783  54.890   6.973  1.00 28.19           O  
ATOM    815  CB  LEU A 106      39.380  53.578   9.967  1.00 27.47           C  
ATOM    816  CG  LEU A 106      39.554  52.433   8.967  1.00 26.61           C  
ATOM    817  CD1 LEU A 106      40.947  52.511   8.329  1.00 24.89           C  
ATOM    818  CD2 LEU A 106      39.281  51.064   9.618  1.00 28.08           C  
ATOM    819  N   LEU A 107      37.107  55.191   8.435  1.00 26.62           N  
ATOM    820  CA  LEU A 107      36.091  55.267   7.390  1.00 25.05           C  
ATOM    821  C   LEU A 107      36.400  56.365   6.358  1.00 24.88           C  
ATOM    822  O   LEU A 107      36.262  56.131   5.142  1.00 25.12           O  
ATOM    823  CB  LEU A 107      34.685  55.427   7.988  1.00 24.37           C  
ATOM    824  CG  LEU A 107      33.477  55.411   7.039  1.00 24.42           C  
ATOM    825  CD1 LEU A 107      33.516  54.259   6.044  1.00 19.46           C  
ATOM    826  CD2 LEU A 107      32.142  55.377   7.858  1.00 23.86           C  
ATOM    827  N   ARG A 108      36.817  57.545   6.831  1.00 24.58           N  
ATOM    828  CA AARG A 108      37.164  58.646   5.927  0.50 24.65           C  
ATOM    829  CA BARG A 108      37.182  58.655   5.955  0.50 24.68           C  
ATOM    830  C   ARG A 108      38.234  58.204   4.934  1.00 24.50           C  
ATOM    831  O   ARG A 108      38.145  58.505   3.730  1.00 23.72           O  
ATOM    832  CB AARG A 108      37.657  59.891   6.686  0.50 24.34           C  
ATOM    833  CB BARG A 108      37.723  59.823   6.797  0.50 24.35           C  
ATOM    834  CG AARG A 108      37.809  61.134   5.786  0.50 25.17           C  
ATOM    835  CG BARG A 108      37.911  61.138   6.047  0.50 25.44           C  
ATOM    836  CD AARG A 108      38.656  62.242   6.422  0.50 25.10           C  
ATOM    837  CD BARG A 108      38.410  62.265   6.965  0.50 25.35           C  
ATOM    838  NE AARG A 108      38.039  62.767   7.630  0.50 25.45           N  
ATOM    839  NE BARG A 108      37.318  62.922   7.691  0.50 25.86           N  
ATOM    840  CZ AARG A 108      37.058  63.667   7.649  0.50 22.57           C  
ATOM    841  CZ BARG A 108      37.171  62.884   9.012  0.50 24.95           C  
ATOM    842  NH1AARG A 108      36.572  64.176   6.511  0.50 23.07           N  
ATOM    843  NH1BARG A 108      38.046  62.218   9.760  0.50 24.47           N  
ATOM    844  NH2AARG A 108      36.572  64.066   8.812  0.50 19.27           N  
ATOM    845  NH2BARG A 108      36.151  63.507   9.582  0.50 23.29           N  
ATOM    846  N   HIS A 109      39.246  57.515   5.446  1.00 24.56           N  
ATOM    847  CA  HIS A 109      40.360  57.077   4.633  1.00 24.51           C  
ATOM    848  C   HIS A 109      39.903  56.033   3.629  1.00 24.07           C  
ATOM    849  O   HIS A 109      40.276  56.101   2.465  1.00 24.59           O  
ATOM    850  CB  HIS A 109      41.504  56.533   5.503  1.00 25.08           C  
ATOM    851  CG  HIS A 109      42.551  55.807   4.709  1.00 26.04           C  
ATOM    852  ND1 HIS A 109      43.445  56.455   3.885  1.00 26.69           N  
ATOM    853  CD2 HIS A 109      42.797  54.484   4.568  1.00 25.68           C  
ATOM    854  CE1 HIS A 109      44.222  55.560   3.293  1.00 26.95           C  
ATOM    855  NE2 HIS A 109      43.845  54.358   3.690  1.00 26.74           N  
ATOM    856  N   ILE A 110      39.091  55.074   4.088  1.00 24.02           N  
ATOM    857  CA  ILE A 110      38.594  54.003   3.237  1.00 23.34           C  
ATOM    858  C   ILE A 110      37.788  54.577   2.078  1.00 23.59           C  
ATOM    859  O   ILE A 110      38.016  54.203   0.910  1.00 22.33           O  
ATOM    860  CB  ILE A 110      37.740  52.970   4.031  1.00 22.62           C  
ATOM    861  CG1 ILE A 110      38.645  52.114   4.948  1.00 24.11           C  
ATOM    862  CG2 ILE A 110      37.018  52.058   3.087  1.00 21.32           C  
ATOM    863  CD1 ILE A 110      37.870  51.224   5.946  1.00 23.78           C  
ATOM    864  N   LEU A 111      36.857  55.487   2.393  1.00 23.22           N  
ATOM    865  CA  LEU A 111      36.047  56.121   1.339  1.00 24.17           C  
ATOM    866  C   LEU A 111      36.866  56.942   0.352  1.00 24.65           C  
ATOM    867  O   LEU A 111      36.532  56.995  -0.815  1.00 23.67           O  
ATOM    868  CB  LEU A 111      34.897  56.972   1.905  1.00 24.27           C  
ATOM    869  CG  LEU A 111      33.896  56.169   2.754  1.00 24.31           C  
ATOM    870  CD1 LEU A 111      32.913  57.072   3.510  1.00 21.96           C  
ATOM    871  CD2 LEU A 111      33.147  55.111   1.913  1.00 25.28           C  
ATOM    872  N   GLN A 112      37.917  57.614   0.817  1.00 25.55           N  
ATOM    873  CA  GLN A 112      38.766  58.337  -0.115  1.00 27.09           C  
ATOM    874  C   GLN A 112      39.501  57.353  -1.050  1.00 27.17           C  
ATOM    875  O   GLN A 112      39.634  57.583  -2.265  1.00 27.54           O  
ATOM    876  CB  GLN A 112      39.741  59.252   0.644  1.00 28.08           C  
ATOM    877  CG  GLN A 112      40.740  59.978  -0.253  1.00 32.54           C  
ATOM    878  CD  GLN A 112      40.079  61.065  -1.128  1.00 38.31           C  
ATOM    879  OE1 GLN A 112      39.863  60.882  -2.330  1.00 42.99           O  
ATOM    880  NE2 GLN A 112      39.732  62.176  -0.509  1.00 41.69           N  
ATOM    881  N   GLN A 113      39.963  56.263  -0.460  1.00 27.11           N  
ATOM    882  CA  GLN A 113      40.683  55.205  -1.165  1.00 27.30           C  
ATOM    883  C   GLN A 113      39.780  54.592  -2.222  1.00 26.82           C  
ATOM    884  O   GLN A 113      40.153  54.494  -3.377  1.00 26.28           O  
ATOM    885  CB  GLN A 113      41.168  54.180  -0.132  1.00 27.42           C  
ATOM    886  CG  GLN A 113      41.978  53.023  -0.637  1.00 28.48           C  
ATOM    887  CD  GLN A 113      42.711  52.358   0.505  1.00 31.12           C  
ATOM    888  OE1 GLN A 113      42.140  52.138   1.584  1.00 30.28           O  
ATOM    889  NE2 GLN A 113      43.989  52.047   0.287  1.00 31.84           N  
ATOM    890  N   VAL A 114      38.551  54.269  -1.835  1.00 26.56           N  
ATOM    891  CA  VAL A 114      37.566  53.728  -2.751  1.00 26.86           C  
ATOM    892  C   VAL A 114      37.215  54.721  -3.870  1.00 27.05           C  
ATOM    893  O   VAL A 114      37.100  54.350  -5.038  1.00 26.02           O  
ATOM    894  CB  VAL A 114      36.301  53.324  -1.956  1.00 26.40           C  
ATOM    895  CG1 VAL A 114      35.137  53.057  -2.859  1.00 26.97           C  
ATOM    896  CG2 VAL A 114      36.628  52.092  -1.073  1.00 26.70           C  
ATOM    897  N   TYR A 115      37.014  55.981  -3.504  1.00 27.87           N  
ATOM    898  CA  TYR A 115      36.721  56.993  -4.504  1.00 28.51           C  
ATOM    899  C   TYR A 115      37.877  57.105  -5.532  1.00 29.16           C  
ATOM    900  O   TYR A 115      37.659  57.007  -6.736  1.00 27.95           O  
ATOM    901  CB  TYR A 115      36.444  58.329  -3.821  1.00 29.06           C  
ATOM    902  CG  TYR A 115      35.898  59.415  -4.727  1.00 29.89           C  
ATOM    903  CD1 TYR A 115      34.530  59.711  -4.744  1.00 30.35           C  
ATOM    904  CD2 TYR A 115      36.750  60.163  -5.547  1.00 32.32           C  
ATOM    905  CE1 TYR A 115      34.032  60.715  -5.549  1.00 32.44           C  
ATOM    906  CE2 TYR A 115      36.253  61.172  -6.366  1.00 33.10           C  
ATOM    907  CZ  TYR A 115      34.892  61.435  -6.364  1.00 33.00           C  
ATOM    908  OH  TYR A 115      34.394  62.436  -7.160  1.00 33.84           O  
ATOM    909  N   ASN A 116      39.096  57.323  -5.050  1.00 29.73           N  
ATOM    910  CA  ASN A 116      40.263  57.443  -5.935  1.00 30.78           C  
ATOM    911  C   ASN A 116      40.490  56.226  -6.833  1.00 30.40           C  
ATOM    912  O   ASN A 116      40.931  56.379  -7.959  1.00 30.72           O  
ATOM    913  CB  ASN A 116      41.532  57.727  -5.128  1.00 30.66           C  
ATOM    914  CG  ASN A 116      41.576  59.130  -4.591  1.00 32.38           C  
ATOM    915  OD1 ASN A 116      42.029  59.356  -3.475  1.00 35.19           O  
ATOM    916  ND2 ASN A 116      41.109  60.094  -5.385  1.00 33.34           N  
ATOM    917  N   HIS A 117      40.197  55.028  -6.337  1.00 30.53           N  
ATOM    918  CA  HIS A 117      40.293  53.828  -7.157  1.00 31.60           C  
ATOM    919  C   HIS A 117      39.125  53.673  -8.127  1.00 31.93           C  
ATOM    920  O   HIS A 117      39.269  52.975  -9.105  1.00 32.28           O  
ATOM    921  CB  HIS A 117      40.383  52.556  -6.299  1.00 31.62           C  
ATOM    922  CG  HIS A 117      41.738  52.309  -5.719  1.00 33.10           C  
ATOM    923  ND1 HIS A 117      42.677  51.501  -6.330  1.00 35.08           N  
ATOM    924  CD2 HIS A 117      42.318  52.770  -4.587  1.00 32.58           C  
ATOM    925  CE1 HIS A 117      43.780  51.487  -5.603  1.00 32.96           C  
ATOM    926  NE2 HIS A 117      43.581  52.233  -4.531  1.00 34.25           N  
ATOM    927  N   SER A 118      37.970  54.292  -7.864  1.00 31.39           N  
ATOM    928  CA  SER A 118      36.778  54.006  -8.694  1.00 30.78           C  
ATOM    929  C   SER A 118      36.452  55.125  -9.668  1.00 31.22           C  
ATOM    930  O   SER A 118      36.006  54.875 -10.790  1.00 30.57           O  
ATOM    931  CB  SER A 118      35.531  53.734  -7.839  1.00 31.06           C  
ATOM    932  OG  SER A 118      35.791  52.841  -6.770  1.00 28.93           O  
ATOM    933  N   VAL A 119      36.659  56.365  -9.234  1.00 32.09           N  
ATOM    934  CA  VAL A 119      36.301  57.522 -10.043  1.00 33.43           C  
ATOM    935  C   VAL A 119      37.533  57.889 -10.871  1.00 35.06           C  
ATOM    936  O   VAL A 119      38.311  58.766 -10.497  1.00 35.58           O  
ATOM    937  CB  VAL A 119      35.787  58.691  -9.148  1.00 33.14           C  
ATOM    938  CG1 VAL A 119      35.378  59.892  -9.986  1.00 32.65           C  
ATOM    939  CG2 VAL A 119      34.593  58.203  -8.284  1.00 31.77           C  
ATOM    940  N   THR A 120      37.720  57.184 -11.983  1.00 36.95           N  
ATOM    941  CA  THR A 120      38.985  57.266 -12.733  1.00 39.03           C  
ATOM    942  C   THR A 120      39.208  58.620 -13.381  1.00 39.91           C  
ATOM    943  O   THR A 120      40.323  59.151 -13.330  1.00 40.44           O  
ATOM    944  CB  THR A 120      39.150  56.134 -13.765  1.00 39.02           C  
ATOM    945  OG1 THR A 120      37.967  56.033 -14.560  1.00 41.32           O  
ATOM    946  CG2 THR A 120      39.417  54.796 -13.064  1.00 38.99           C  
ATOM    947  N   ASP A 121      38.151  59.180 -13.975  1.00 40.39           N  
ATOM    948  CA  ASP A 121      38.204  60.557 -14.457  1.00 40.93           C  
ATOM    949  C   ASP A 121      37.105  61.434 -13.830  1.00 40.65           C  
ATOM    950  O   ASP A 121      36.000  61.513 -14.374  1.00 40.35           O  
ATOM    951  CB  ASP A 121      38.138  60.609 -15.987  1.00 40.84           C  
ATOM    952  CG  ASP A 121      38.422  61.991 -16.528  1.00 42.41           C  
ATOM    953  OD1 ASP A 121      38.775  62.882 -15.729  1.00 42.18           O  
ATOM    954  OD2 ASP A 121      38.304  62.186 -17.758  1.00 45.90           O  
ATOM    955  N   PRO A 122      37.420  62.085 -12.685  1.00 40.75           N  
ATOM    956  CA  PRO A 122      36.522  62.943 -11.914  1.00 40.87           C  
ATOM    957  C   PRO A 122      35.853  64.027 -12.768  1.00 41.51           C  
ATOM    958  O   PRO A 122      34.659  64.300 -12.590  1.00 41.01           O  
ATOM    959  CB  PRO A 122      37.447  63.569 -10.872  1.00 41.07           C  
ATOM    960  CG  PRO A 122      38.521  62.564 -10.669  1.00 40.87           C  
ATOM    961  CD  PRO A 122      38.726  61.917 -12.009  1.00 41.37           C  
ATOM    962  N   GLU A 123      36.612  64.613 -13.701  1.00 41.49           N  
ATOM    963  CA  GLU A 123      36.086  65.645 -14.601  1.00 41.72           C  
ATOM    964  C   GLU A 123      34.803  65.223 -15.313  1.00 41.23           C  
ATOM    965  O   GLU A 123      33.957  66.064 -15.609  1.00 41.84           O  
ATOM    966  CB  GLU A 123      37.149  66.063 -15.630  1.00 41.69           C  
ATOM    967  CG  GLU A 123      36.658  67.019 -16.704  1.00 42.89           C  
ATOM    968  CD  GLU A 123      35.961  68.261 -16.142  1.00 43.99           C  
ATOM    969  OE1 GLU A 123      34.958  68.707 -16.753  1.00 44.62           O  
ATOM    970  OE2 GLU A 123      36.409  68.775 -15.093  1.00 44.16           O  
ATOM    971  N   LYS A 124      34.663  63.929 -15.586  1.00 41.01           N  
ATOM    972  CA  LYS A 124      33.495  63.397 -16.296  1.00 41.23           C  
ATOM    973  C   LYS A 124      32.153  63.578 -15.558  1.00 41.20           C  
ATOM    974  O   LYS A 124      31.086  63.527 -16.180  1.00 40.96           O  
ATOM    975  CB  LYS A 124      33.707  61.922 -16.654  1.00 41.73           C  
ATOM    976  CG  LYS A 124      34.569  61.675 -17.909  1.00 43.03           C  
ATOM    977  CD  LYS A 124      34.566  60.197 -18.271  1.00 46.60           C  
ATOM    978  CE  LYS A 124      34.895  59.966 -19.754  1.00 48.86           C  
ATOM    979  NZ  LYS A 124      36.329  59.619 -19.969  1.00 49.78           N  
ATOM    980  N   LEU A 125      32.218  63.765 -14.240  1.00 40.96           N  
ATOM    981  CA  LEU A 125      31.031  64.003 -13.410  1.00 41.05           C  
ATOM    982  C   LEU A 125      30.492  65.423 -13.582  1.00 41.53           C  
ATOM    983  O   LEU A 125      29.374  65.728 -13.143  1.00 41.69           O  
ATOM    984  CB  LEU A 125      31.344  63.746 -11.932  1.00 40.36           C  
ATOM    985  CG  LEU A 125      31.553  62.285 -11.509  1.00 38.25           C  
ATOM    986  CD1 LEU A 125      32.295  62.200 -10.167  1.00 35.33           C  
ATOM    987  CD2 LEU A 125      30.220  61.526 -11.474  1.00 35.04           C  
ATOM    988  N   ASN A 126      31.301  66.290 -14.190  1.00 41.81           N  
ATOM    989  CA  ASN A 126      30.870  67.655 -14.504  1.00 42.74           C  
ATOM    990  C   ASN A 126      30.200  67.743 -15.872  1.00 42.49           C  
ATOM    991  O   ASN A 126      29.784  68.823 -16.284  1.00 42.72           O  
ATOM    992  CB  ASN A 126      32.030  68.661 -14.403  1.00 42.81           C  
ATOM    993  CG  ASN A 126      32.524  68.864 -12.962  1.00 44.85           C  
ATOM    994  OD1 ASN A 126      33.731  68.912 -12.710  1.00 46.28           O  
ATOM    995  ND2 ASN A 126      31.593  68.994 -12.021  1.00 45.60           N  
ATOM    996  N   ASN A 127      30.098  66.610 -16.568  1.00 42.68           N  
ATOM    997  CA  ASN A 127      29.440  66.566 -17.876  1.00 42.84           C  
ATOM    998  C   ASN A 127      27.942  66.373 -17.696  1.00 42.37           C  
ATOM    999  O   ASN A 127      27.382  65.360 -18.092  1.00 42.92           O  
ATOM   1000  CB  ASN A 127      29.986  65.432 -18.752  1.00 43.07           C  
ATOM   1001  CG  ASN A 127      31.434  65.626 -19.139  1.00 43.95           C  
ATOM   1002  OD1 ASN A 127      32.008  66.704 -18.961  1.00 45.85           O  
ATOM   1003  ND2 ASN A 127      32.042  64.566 -19.675  1.00 45.97           N  
ATOM   1004  N   TYR A 128      27.293  67.340 -17.071  1.00 41.56           N  
ATOM   1005  CA  TYR A 128      25.862  67.264 -16.909  1.00 40.83           C  
ATOM   1006  C   TYR A 128      25.221  68.435 -17.650  1.00 41.41           C  
ATOM   1007  O   TYR A 128      25.892  69.405 -17.981  1.00 41.01           O  
ATOM   1008  CB  TYR A 128      25.492  67.275 -15.423  1.00 39.86           C  
ATOM   1009  CG  TYR A 128      26.114  68.410 -14.646  1.00 36.91           C  
ATOM   1010  CD1 TYR A 128      25.595  69.702 -14.727  1.00 34.25           C  
ATOM   1011  CD2 TYR A 128      27.223  68.193 -13.824  1.00 31.69           C  
ATOM   1012  CE1 TYR A 128      26.163  70.749 -14.009  1.00 32.60           C  
ATOM   1013  CE2 TYR A 128      27.790  69.227 -13.104  1.00 31.46           C  
ATOM   1014  CZ  TYR A 128      27.253  70.497 -13.195  1.00 31.84           C  
ATOM   1015  OH  TYR A 128      27.821  71.528 -12.499  1.00 31.71           O  
ATOM   1016  N   GLU A 129      23.920  68.340 -17.902  1.00 41.79           N  
ATOM   1017  CA  GLU A 129      23.177  69.482 -18.409  1.00 42.21           C  
ATOM   1018  C   GLU A 129      23.053  70.531 -17.294  1.00 41.65           C  
ATOM   1019  O   GLU A 129      22.463  70.269 -16.251  1.00 41.41           O  
ATOM   1020  CB  GLU A 129      21.810  69.035 -18.947  1.00 42.86           C  
ATOM   1021  CG  GLU A 129      21.027  70.127 -19.691  1.00 45.39           C  
ATOM   1022  CD  GLU A 129      19.681  69.629 -20.182  1.00 49.88           C  
ATOM   1023  OE1 GLU A 129      18.643  70.195 -19.765  1.00 52.91           O  
ATOM   1024  OE2 GLU A 129      19.657  68.657 -20.972  1.00 52.00           O  
ATOM   1025  N   PRO A 130      23.656  71.713 -17.495  1.00 41.75           N  
ATOM   1026  CA  PRO A 130      23.569  72.757 -16.487  1.00 41.51           C  
ATOM   1027  C   PRO A 130      22.141  73.240 -16.417  1.00 41.70           C  
ATOM   1028  O   PRO A 130      21.384  73.052 -17.387  1.00 41.31           O  
ATOM   1029  CB  PRO A 130      24.474  73.867 -17.039  1.00 41.47           C  
ATOM   1030  CG  PRO A 130      25.345  73.203 -18.055  1.00 41.86           C  
ATOM   1031  CD  PRO A 130      24.470  72.139 -18.652  1.00 41.78           C  
ATOM   1032  N   PHE A 131      21.776  73.818 -15.273  1.00 41.47           N  
ATOM   1033  CA  PHE A 131      20.435  74.365 -15.050  1.00 42.19           C  
ATOM   1034  C   PHE A 131      19.337  73.296 -15.188  1.00 42.21           C  
ATOM   1035  O   PHE A 131      18.243  73.554 -15.719  1.00 42.82           O  
ATOM   1036  CB  PHE A 131      20.208  75.613 -15.935  1.00 42.23           C  
ATOM   1037  CG  PHE A 131      21.253  76.690 -15.717  1.00 42.62           C  
ATOM   1038  CD1 PHE A 131      21.303  77.399 -14.511  1.00 42.83           C  
ATOM   1039  CD2 PHE A 131      22.212  76.960 -16.687  1.00 43.64           C  
ATOM   1040  CE1 PHE A 131      22.280  78.373 -14.287  1.00 43.35           C  
ATOM   1041  CE2 PHE A 131      23.191  77.934 -16.472  1.00 42.13           C  
ATOM   1042  CZ  PHE A 131      23.223  78.639 -15.267  1.00 42.77           C  
ATOM   1043  N   SER A 132      19.649  72.097 -14.689  1.00 41.78           N  
ATOM   1044  CA  SER A 132      18.752  70.947 -14.725  1.00 40.97           C  
ATOM   1045  C   SER A 132      18.919  70.137 -13.429  1.00 40.77           C  
ATOM   1046  O   SER A 132      19.877  70.355 -12.689  1.00 40.39           O  
ATOM   1047  CB  SER A 132      19.059  70.072 -15.956  1.00 41.27           C  
ATOM   1048  OG  SER A 132      19.997  69.037 -15.665  1.00 40.67           O  
ATOM   1049  N   PRO A 133      17.986  69.205 -13.146  1.00 40.55           N  
ATOM   1050  CA  PRO A 133      18.109  68.280 -12.001  1.00 39.93           C  
ATOM   1051  C   PRO A 133      19.346  67.391 -12.039  1.00 39.31           C  
ATOM   1052  O   PRO A 133      19.703  66.785 -11.030  1.00 38.73           O  
ATOM   1053  CB  PRO A 133      16.845  67.420 -12.119  1.00 40.10           C  
ATOM   1054  CG  PRO A 133      15.832  68.389 -12.663  1.00 40.80           C  
ATOM   1055  CD  PRO A 133      16.620  69.180 -13.709  1.00 40.54           C  
ATOM   1056  N   GLU A 134      20.002  67.331 -13.187  1.00 39.00           N  
ATOM   1057  CA  GLU A 134      21.188  66.508 -13.347  1.00 39.30           C  
ATOM   1058  C   GLU A 134      22.437  67.096 -12.673  1.00 38.24           C  
ATOM   1059  O   GLU A 134      23.448  66.410 -12.539  1.00 38.10           O  
ATOM   1060  CB  GLU A 134      21.458  66.242 -14.827  1.00 40.06           C  
ATOM   1061  CG  GLU A 134      22.468  65.131 -15.048  1.00 43.60           C  
ATOM   1062  CD  GLU A 134      22.574  64.705 -16.494  1.00 47.97           C  
ATOM   1063  OE1 GLU A 134      22.338  65.547 -17.403  1.00 49.83           O  
ATOM   1064  OE2 GLU A 134      22.906  63.522 -16.711  1.00 48.28           O  
ATOM   1065  N   VAL A 135      22.368  68.359 -12.256  1.00 37.14           N  
ATOM   1066  CA  VAL A 135      23.527  69.018 -11.640  1.00 36.00           C  
ATOM   1067  C   VAL A 135      24.145  68.141 -10.529  1.00 35.55           C  
ATOM   1068  O   VAL A 135      23.451  67.760  -9.567  1.00 33.84           O  
ATOM   1069  CB  VAL A 135      23.156  70.413 -11.100  1.00 35.89           C  
ATOM   1070  CG1 VAL A 135      24.242  70.947 -10.160  1.00 36.28           C  
ATOM   1071  CG2 VAL A 135      22.901  71.411 -12.275  1.00 35.92           C  
ATOM   1072  N   TYR A 136      25.433  67.810 -10.704  1.00 34.33           N  
ATOM   1073  CA  TYR A 136      26.187  66.983  -9.756  1.00 34.06           C  
ATOM   1074  C   TYR A 136      26.883  67.843  -8.708  1.00 33.55           C  
ATOM   1075  O   TYR A 136      27.432  68.884  -9.018  1.00 34.48           O  
ATOM   1076  CB  TYR A 136      27.235  66.133 -10.489  1.00 33.39           C  
ATOM   1077  CG  TYR A 136      27.934  65.114  -9.614  1.00 32.96           C  
ATOM   1078  CD1 TYR A 136      27.350  63.867  -9.362  1.00 33.99           C  
ATOM   1079  CD2 TYR A 136      29.177  65.386  -9.041  1.00 31.75           C  
ATOM   1080  CE1 TYR A 136      27.988  62.921  -8.564  1.00 33.77           C  
ATOM   1081  CE2 TYR A 136      29.828  64.436  -8.238  1.00 30.71           C  
ATOM   1082  CZ  TYR A 136      29.224  63.212  -8.006  1.00 32.53           C  
ATOM   1083  OH  TYR A 136      29.841  62.268  -7.231  1.00 32.51           O  
ATOM   1084  N   GLY A 137      26.839  67.386  -7.468  1.00 33.85           N  
ATOM   1085  CA  GLY A 137      27.635  67.933  -6.361  1.00 33.08           C  
ATOM   1086  C   GLY A 137      27.665  66.867  -5.279  1.00 32.63           C  
ATOM   1087  O   GLY A 137      26.742  66.051  -5.211  1.00 32.60           O  
ATOM   1088  N   GLU A 138      28.707  66.858  -4.436  1.00 30.94           N  
ATOM   1089  CA  GLU A 138      28.831  65.832  -3.401  1.00 30.49           C  
ATOM   1090  C   GLU A 138      28.721  66.470  -2.035  1.00 30.13           C  
ATOM   1091  O   GLU A 138      29.320  67.509  -1.774  1.00 30.94           O  
ATOM   1092  CB  GLU A 138      30.149  65.023  -3.516  1.00 30.45           C  
ATOM   1093  CG  GLU A 138      30.542  64.693  -4.964  1.00 31.07           C  
ATOM   1094  CD  GLU A 138      31.839  63.887  -5.119  1.00 32.06           C  
ATOM   1095  OE1 GLU A 138      32.725  63.918  -4.230  1.00 32.45           O  
ATOM   1096  OE2 GLU A 138      31.975  63.233  -6.161  1.00 31.25           O  
ATOM   1097  N   THR A 139      27.903  65.857  -1.197  1.00 29.47           N  
ATOM   1098  CA  THR A 139      27.798  66.187   0.200  1.00 29.54           C  
ATOM   1099  C   THR A 139      29.111  65.698   0.814  1.00 29.24           C  
ATOM   1100  O   THR A 139      29.546  64.601   0.507  1.00 28.78           O  
ATOM   1101  CB  THR A 139      26.621  65.433   0.808  1.00 29.35           C  
ATOM   1102  OG1 THR A 139      25.415  65.829   0.133  1.00 30.79           O  
ATOM   1103  CG2 THR A 139      26.488  65.726   2.310  1.00 29.50           C  
ATOM   1104  N   SER A 140      29.742  66.532   1.632  1.00 28.79           N  
ATOM   1105  CA  SER A 140      31.016  66.184   2.271  1.00 29.20           C  
ATOM   1106  C   SER A 140      30.844  65.083   3.325  1.00 28.32           C  
ATOM   1107  O   SER A 140      29.764  64.927   3.905  1.00 27.71           O  
ATOM   1108  CB  SER A 140      31.626  67.414   2.937  1.00 29.37           C  
ATOM   1109  OG  SER A 140      30.821  67.801   4.052  1.00 32.07           O  
ATOM   1110  N   PHE A 141      31.920  64.333   3.565  1.00 27.32           N  
ATOM   1111  CA  PHE A 141      31.960  63.337   4.644  1.00 26.97           C  
ATOM   1112  C   PHE A 141      31.508  63.937   5.970  1.00 26.37           C  
ATOM   1113  O   PHE A 141      30.720  63.325   6.696  1.00 26.07           O  
ATOM   1114  CB  PHE A 141      33.393  62.782   4.803  1.00 27.12           C  
ATOM   1115  CG  PHE A 141      33.536  61.741   5.896  1.00 26.82           C  
ATOM   1116  CD1 PHE A 141      33.569  60.393   5.582  1.00 26.58           C  
ATOM   1117  CD2 PHE A 141      33.671  62.121   7.235  1.00 28.22           C  
ATOM   1118  CE1 PHE A 141      33.714  59.429   6.572  1.00 26.09           C  
ATOM   1119  CE2 PHE A 141      33.801  61.169   8.252  1.00 24.92           C  
ATOM   1120  CZ  PHE A 141      33.830  59.815   7.915  1.00 29.27           C  
ATOM   1121  N   ASP A 142      32.012  65.126   6.291  1.00 26.32           N  
ATOM   1122  CA  ASP A 142      31.662  65.808   7.539  1.00 27.34           C  
ATOM   1123  C   ASP A 142      30.153  66.046   7.732  1.00 27.40           C  
ATOM   1124  O   ASP A 142      29.619  65.820   8.827  1.00 26.37           O  
ATOM   1125  CB  ASP A 142      32.460  67.124   7.666  1.00 28.90           C  
ATOM   1126  CG  ASP A 142      33.938  66.878   7.928  1.00 30.35           C  
ATOM   1127  OD1 ASP A 142      34.280  65.778   8.407  1.00 33.06           O  
ATOM   1128  OD2 ASP A 142      34.762  67.775   7.663  1.00 33.89           O  
ATOM   1129  N   LEU A 143      29.462  66.488   6.681  1.00 27.50           N  
ATOM   1130  CA  LEU A 143      28.005  66.648   6.790  1.00 28.32           C  
ATOM   1131  C   LEU A 143      27.245  65.320   6.948  1.00 27.57           C  
ATOM   1132  O   LEU A 143      26.363  65.205   7.811  1.00 27.37           O  
ATOM   1133  CB  LEU A 143      27.402  67.463   5.648  1.00 28.84           C  
ATOM   1134  CG  LEU A 143      25.935  67.678   6.048  1.00 31.88           C  
ATOM   1135  CD1 LEU A 143      25.649  69.105   6.436  1.00 34.05           C  
ATOM   1136  CD2 LEU A 143      24.996  67.183   4.973  1.00 34.85           C  
ATOM   1137  N   VAL A 144      27.579  64.328   6.127  1.00 27.19           N  
ATOM   1138  CA  VAL A 144      27.046  62.976   6.297  1.00 26.52           C  
ATOM   1139  C   VAL A 144      27.255  62.498   7.748  1.00 27.53           C  
ATOM   1140  O   VAL A 144      26.305  61.991   8.387  1.00 26.59           O  
ATOM   1141  CB  VAL A 144      27.658  61.966   5.274  1.00 26.70           C  
ATOM   1142  CG1 VAL A 144      27.036  60.587   5.411  1.00 26.17           C  
ATOM   1143  CG2 VAL A 144      27.463  62.443   3.830  1.00 26.38           C  
ATOM   1144  N   ALA A 145      28.476  62.669   8.284  1.00 27.51           N  
ATOM   1145  CA  ALA A 145      28.757  62.214   9.659  1.00 29.73           C  
ATOM   1146  C   ALA A 145      27.864  62.944  10.672  1.00 30.86           C  
ATOM   1147  O   ALA A 145      27.371  62.332  11.625  1.00 31.35           O  
ATOM   1148  CB  ALA A 145      30.240  62.381  10.038  1.00 28.72           C  
ATOM   1149  N   GLN A 146      27.661  64.242  10.461  1.00 32.20           N  
ATOM   1150  CA  GLN A 146      26.706  64.993  11.278  1.00 34.08           C  
ATOM   1151  C   GLN A 146      25.296  64.397  11.200  1.00 35.34           C  
ATOM   1152  O   GLN A 146      24.596  64.279  12.205  1.00 35.71           O  
ATOM   1153  CB  GLN A 146      26.646  66.460  10.855  1.00 33.60           C  
ATOM   1154  CG  GLN A 146      25.801  67.277  11.831  1.00 34.81           C  
ATOM   1155  CD  GLN A 146      25.533  68.686  11.376  1.00 35.36           C  
ATOM   1156  OE1 GLN A 146      25.696  69.025  10.202  1.00 36.94           O  
ATOM   1157  NE2 GLN A 146      25.102  69.521  12.305  1.00 35.80           N  
ATOM   1158  N   MET A 147      24.867  64.048  10.000  1.00 36.46           N  
ATOM   1159  CA  MET A 147      23.551  63.482   9.852  1.00 38.71           C  
ATOM   1160  C   MET A 147      23.416  62.160  10.609  1.00 40.33           C  
ATOM   1161  O   MET A 147      22.401  61.925  11.280  1.00 40.99           O  
ATOM   1162  CB  MET A 147      23.203  63.305   8.389  1.00 38.04           C  
ATOM   1163  CG  MET A 147      22.170  62.235   8.226  1.00 39.07           C  
ATOM   1164  SD  MET A 147      21.634  62.094   6.559  1.00 38.60           S  
ATOM   1165  CE  MET A 147      22.922  61.062   5.868  1.00 40.28           C  
ATOM   1166  N   ILE A 148      24.431  61.306  10.490  1.00 41.43           N  
ATOM   1167  CA  ILE A 148      24.493  60.056  11.242  1.00 43.58           C  
ATOM   1168  C   ILE A 148      24.458  60.331  12.761  1.00 45.32           C  
ATOM   1169  O   ILE A 148      23.613  59.785  13.465  1.00 46.27           O  
ATOM   1170  CB  ILE A 148      25.737  59.197  10.851  1.00 42.64           C  
ATOM   1171  CG1 ILE A 148      25.679  58.794   9.364  1.00 41.40           C  
ATOM   1172  CG2 ILE A 148      25.829  57.950  11.732  1.00 42.90           C  
ATOM   1173  CD1 ILE A 148      27.026  58.282   8.786  1.00 37.97           C  
ATOM   1174  N   ASP A 149      25.348  61.200  13.241  1.00 47.38           N  
ATOM   1175  CA  ASP A 149      25.430  61.556  14.666  1.00 48.89           C  
ATOM   1176  C   ASP A 149      24.094  61.992  15.280  1.00 49.92           C  
ATOM   1177  O   ASP A 149      23.778  61.620  16.418  1.00 49.85           O  
ATOM   1178  CB  ASP A 149      26.457  62.669  14.884  1.00 49.11           C  
ATOM   1179  CG  ASP A 149      27.890  62.159  14.938  1.00 50.49           C  
ATOM   1180  OD1 ASP A 149      28.107  60.966  15.247  1.00 50.90           O  
ATOM   1181  OD2 ASP A 149      28.812  62.968  14.674  1.00 52.23           O  
ATOM   1182  N   GLU A 150      23.315  62.764  14.520  1.00 51.11           N  
ATOM   1183  CA  GLU A 150      22.114  63.427  15.040  1.00 51.95           C  
ATOM   1184  C   GLU A 150      20.790  62.700  14.776  1.00 52.71           C  
ATOM   1185  O   GLU A 150      19.953  62.587  15.678  1.00 52.65           O  
ATOM   1186  CB  GLU A 150      22.056  64.884  14.560  1.00 52.23           C  
ATOM   1187  CG  GLU A 150      23.050  65.802  15.296  1.00 52.13           C  
ATOM   1188  CD  GLU A 150      23.101  67.223  14.745  1.00 52.60           C  
ATOM   1189  OE1 GLU A 150      22.093  67.680  14.156  1.00 52.33           O  
ATOM   1190  OE2 GLU A 150      24.156  67.886  14.907  1.00 52.40           O  
ATOM   1191  N   ILE A 151      20.583  62.216  13.552  1.00 53.12           N  
ATOM   1192  CA  ILE A 151      19.423  61.366  13.294  1.00 53.32           C  
ATOM   1193  C   ILE A 151      19.855  59.958  13.665  1.00 53.64           C  
ATOM   1194  O   ILE A 151      20.685  59.350  12.979  1.00 54.11           O  
ATOM   1195  CB  ILE A 151      18.919  61.441  11.824  1.00 53.57           C  
ATOM   1196  CG1 ILE A 151      19.401  60.228  11.014  1.00 53.40           C  
ATOM   1197  CG2 ILE A 151      19.280  62.783  11.178  1.00 52.89           C  
ATOM   1198  CD1 ILE A 151      19.594  60.485   9.543  1.00 55.23           C  
ATOM   1199  N   LYS A 152      19.336  59.432  14.764  1.00 53.55           N  
ATOM   1200  CA  LYS A 152      19.858  58.159  15.218  1.00 53.62           C  
ATOM   1201  C   LYS A 152      19.034  57.034  14.639  1.00 53.11           C  
ATOM   1202  O   LYS A 152      17.834  56.931  14.882  1.00 53.49           O  
ATOM   1203  CB  LYS A 152      20.034  58.104  16.745  1.00 53.92           C  
ATOM   1204  CG  LYS A 152      21.289  58.890  17.184  1.00 55.43           C  
ATOM   1205  CD  LYS A 152      21.667  58.706  18.650  1.00 56.95           C  
ATOM   1206  CE  LYS A 152      21.186  59.867  19.513  1.00 57.65           C  
ATOM   1207  NZ  LYS A 152      21.735  61.190  19.071  1.00 57.09           N  
ATOM   1208  N   MET A 153      19.693  56.239  13.807  1.00 51.98           N  
ATOM   1209  CA  MET A 153      19.059  55.124  13.138  1.00 51.29           C  
ATOM   1210  C   MET A 153      19.271  53.870  13.969  1.00 50.69           C  
ATOM   1211  O   MET A 153      20.284  53.723  14.643  1.00 50.32           O  
ATOM   1212  CB  MET A 153      19.645  54.934  11.737  1.00 51.11           C  
ATOM   1213  CG  MET A 153      19.069  55.862  10.657  1.00 51.28           C  
ATOM   1214  SD  MET A 153      20.076  55.847   9.149  1.00 50.23           S  
ATOM   1215  CE  MET A 153      21.097  57.287   9.414  1.00 50.06           C  
ATOM   1216  N   THR A 154      18.295  52.977  13.921  1.00 50.54           N  
ATOM   1217  CA  THR A 154      18.405  51.680  14.568  1.00 50.42           C  
ATOM   1218  C   THR A 154      18.235  50.617  13.507  1.00 50.01           C  
ATOM   1219  O   THR A 154      18.043  50.926  12.325  1.00 49.76           O  
ATOM   1220  CB  THR A 154      17.309  51.460  15.630  1.00 50.50           C  
ATOM   1221  OG1 THR A 154      16.137  50.945  14.988  1.00 50.94           O  
ATOM   1222  CG2 THR A 154      16.981  52.762  16.382  1.00 50.86           C  
ATOM   1223  N   ASP A 155      18.283  49.359  13.938  1.00 49.42           N  
ATOM   1224  CA  ASP A 155      18.140  48.223  13.035  1.00 48.88           C  
ATOM   1225  C   ASP A 155      16.747  48.113  12.433  1.00 48.05           C  
ATOM   1226  O   ASP A 155      16.513  47.264  11.586  1.00 48.16           O  
ATOM   1227  CB  ASP A 155      18.516  46.933  13.756  1.00 49.50           C  
ATOM   1228  CG  ASP A 155      18.132  46.966  15.214  1.00 51.07           C  
ATOM   1229  OD1 ASP A 155      18.888  47.581  16.011  1.00 53.07           O  
ATOM   1230  OD2 ASP A 155      17.073  46.395  15.552  1.00 52.12           O  
ATOM   1231  N   ASP A 156      15.824  48.964  12.869  1.00 46.85           N  
ATOM   1232  CA  ASP A 156      14.503  49.023  12.248  1.00 46.52           C  
ATOM   1233  C   ASP A 156      14.503  49.908  10.996  1.00 45.24           C  
ATOM   1234  O   ASP A 156      13.664  49.744  10.110  1.00 45.45           O  
ATOM   1235  CB  ASP A 156      13.458  49.524  13.257  1.00 47.23           C  
ATOM   1236  CG  ASP A 156      13.402  48.664  14.513  1.00 49.11           C  
ATOM   1237  OD1 ASP A 156      13.308  47.424  14.386  1.00 51.08           O  
ATOM   1238  OD2 ASP A 156      13.457  49.229  15.627  1.00 52.70           O  
ATOM   1239  N   ASP A 157      15.462  50.828  10.923  1.00 43.60           N  
ATOM   1240  CA  ASP A 157      15.447  51.876   9.906  1.00 41.85           C  
ATOM   1241  C   ASP A 157      15.912  51.456   8.519  1.00 40.30           C  
ATOM   1242  O   ASP A 157      16.752  50.562   8.364  1.00 40.42           O  
ATOM   1243  CB  ASP A 157      16.184  53.114  10.402  1.00 42.42           C  
ATOM   1244  CG  ASP A 157      15.313  53.972  11.282  1.00 42.87           C  
ATOM   1245  OD1 ASP A 157      14.085  53.930  11.084  1.00 45.48           O  
ATOM   1246  OD2 ASP A 157      15.828  54.675  12.169  1.00 44.54           O  
ATOM   1247  N   LEU A 158      15.309  52.097   7.522  1.00 37.70           N  
ATOM   1248  CA  LEU A 158      15.629  51.898   6.124  1.00 35.58           C  
ATOM   1249  C   LEU A 158      16.031  53.261   5.572  1.00 34.32           C  
ATOM   1250  O   LEU A 158      15.303  54.254   5.734  1.00 33.58           O  
ATOM   1251  CB  LEU A 158      14.424  51.335   5.360  1.00 35.71           C  
ATOM   1252  CG  LEU A 158      14.004  49.881   5.606  1.00 37.76           C  
ATOM   1253  CD1 LEU A 158      12.674  49.575   4.902  1.00 38.41           C  
ATOM   1254  CD2 LEU A 158      15.063  48.906   5.138  1.00 38.44           C  
ATOM   1255  N   PHE A 159      17.204  53.303   4.946  1.00 32.58           N  
ATOM   1256  CA  PHE A 159      17.801  54.548   4.508  1.00 31.38           C  
ATOM   1257  C   PHE A 159      17.919  54.553   3.003  1.00 30.64           C  
ATOM   1258  O   PHE A 159      18.281  53.530   2.395  1.00 30.38           O  
ATOM   1259  CB  PHE A 159      19.184  54.744   5.150  1.00 31.07           C  
ATOM   1260  CG  PHE A 159      19.943  55.929   4.609  1.00 31.50           C  
ATOM   1261  CD1 PHE A 159      19.917  57.151   5.266  1.00 31.37           C  
ATOM   1262  CD2 PHE A 159      20.684  55.821   3.432  1.00 31.36           C  
ATOM   1263  CE1 PHE A 159      20.607  58.252   4.752  1.00 32.26           C  
ATOM   1264  CE2 PHE A 159      21.375  56.909   2.925  1.00 31.13           C  
ATOM   1265  CZ  PHE A 159      21.342  58.121   3.580  1.00 29.20           C  
ATOM   1266  N   VAL A 160      17.633  55.712   2.409  1.00 29.50           N  
ATOM   1267  CA  VAL A 160      17.690  55.888   0.957  1.00 28.98           C  
ATOM   1268  C   VAL A 160      18.274  57.268   0.597  1.00 28.22           C  
ATOM   1269  O   VAL A 160      17.813  58.293   1.098  1.00 29.04           O  
ATOM   1270  CB  VAL A 160      16.291  55.750   0.291  1.00 29.01           C  
ATOM   1271  CG1 VAL A 160      16.398  55.968  -1.231  1.00 29.47           C  
ATOM   1272  CG2 VAL A 160      15.648  54.352   0.581  1.00 30.11           C  
ATOM   1273  N   ASP A 161      19.291  57.270  -0.254  1.00 27.64           N  
ATOM   1274  CA  ASP A 161      19.804  58.480  -0.868  1.00 27.67           C  
ATOM   1275  C   ASP A 161      19.153  58.560  -2.238  1.00 27.11           C  
ATOM   1276  O   ASP A 161      19.466  57.768  -3.132  1.00 27.02           O  
ATOM   1277  CB  ASP A 161      21.343  58.439  -0.993  1.00 27.24           C  
ATOM   1278  CG  ASP A 161      21.921  59.734  -1.539  1.00 27.15           C  
ATOM   1279  OD1 ASP A 161      21.140  60.662  -1.865  1.00 27.90           O  
ATOM   1280  OD2 ASP A 161      23.161  59.834  -1.653  1.00 26.31           O  
ATOM   1281  N   LEU A 162      18.225  59.504  -2.372  1.00 27.15           N  
ATOM   1282  CA  LEU A 162      17.567  59.796  -3.644  1.00 26.39           C  
ATOM   1283  C   LEU A 162      18.457  60.682  -4.492  1.00 25.64           C  
ATOM   1284  O   LEU A 162      18.687  61.839  -4.146  1.00 25.76           O  
ATOM   1285  CB  LEU A 162      16.230  60.506  -3.397  1.00 25.98           C  
ATOM   1286  CG  LEU A 162      15.194  59.739  -2.566  1.00 27.61           C  
ATOM   1287  CD1 LEU A 162      14.011  60.646  -2.246  1.00 25.47           C  
ATOM   1288  CD2 LEU A 162      14.776  58.468  -3.323  1.00 26.34           C  
ATOM   1289  N   GLY A 163      18.911  60.148  -5.622  1.00 25.18           N  
ATOM   1290  CA  GLY A 163      19.954  60.780  -6.419  1.00 25.54           C  
ATOM   1291  C   GLY A 163      21.326  60.596  -5.800  1.00 25.10           C  
ATOM   1292  O   GLY A 163      21.980  61.558  -5.427  1.00 24.81           O  
ATOM   1293  N   SER A 164      21.771  59.347  -5.735  1.00 25.00           N  
ATOM   1294  CA  SER A 164      22.916  58.959  -4.919  1.00 24.68           C  
ATOM   1295  C   SER A 164      24.317  59.216  -5.515  1.00 25.25           C  
ATOM   1296  O   SER A 164      25.315  59.029  -4.828  1.00 25.09           O  
ATOM   1297  CB  SER A 164      22.765  57.493  -4.512  1.00 24.76           C  
ATOM   1298  OG  SER A 164      22.366  56.700  -5.625  1.00 23.67           O  
ATOM   1299  N   GLY A 165      24.373  59.667  -6.771  1.00 25.47           N  
ATOM   1300  CA  GLY A 165      25.620  60.000  -7.444  1.00 25.94           C  
ATOM   1301  C   GLY A 165      26.487  58.784  -7.642  1.00 26.64           C  
ATOM   1302  O   GLY A 165      26.046  57.803  -8.216  1.00 27.29           O  
ATOM   1303  N   VAL A 166      27.719  58.844  -7.134  1.00 27.27           N  
ATOM   1304  CA  VAL A 166      28.623  57.693  -7.166  1.00 27.06           C  
ATOM   1305  C   VAL A 166      28.460  56.813  -5.929  1.00 27.30           C  
ATOM   1306  O   VAL A 166      29.115  55.768  -5.800  1.00 28.00           O  
ATOM   1307  CB  VAL A 166      30.107  58.118  -7.419  1.00 27.21           C  
ATOM   1308  CG1 VAL A 166      30.171  58.933  -8.711  1.00 26.63           C  
ATOM   1309  CG2 VAL A 166      30.674  58.905  -6.234  1.00 26.80           C  
ATOM   1310  N   GLY A 167      27.558  57.206  -5.026  1.00 27.36           N  
ATOM   1311  CA  GLY A 167      27.133  56.296  -3.968  1.00 26.58           C  
ATOM   1312  C   GLY A 167      27.843  56.438  -2.637  1.00 26.81           C  
ATOM   1313  O   GLY A 167      27.614  55.643  -1.732  1.00 26.90           O  
ATOM   1314  N   GLN A 168      28.652  57.479  -2.483  1.00 26.76           N  
ATOM   1315  CA  GLN A 168      29.504  57.588  -1.297  1.00 26.69           C  
ATOM   1316  C   GLN A 168      28.758  57.959  -0.013  1.00 26.16           C  
ATOM   1317  O   GLN A 168      29.259  57.681   1.073  1.00 26.15           O  
ATOM   1318  CB  GLN A 168      30.725  58.498  -1.548  1.00 26.65           C  
ATOM   1319  CG  GLN A 168      30.572  60.002  -1.261  1.00 27.20           C  
ATOM   1320  CD  GLN A 168      29.613  60.719  -2.191  1.00 27.99           C  
ATOM   1321  OE1 GLN A 168      29.277  60.236  -3.293  1.00 27.35           O  
ATOM   1322  NE2 GLN A 168      29.157  61.885  -1.750  1.00 25.01           N  
ATOM   1323  N   VAL A 169      27.578  58.566  -0.139  1.00 25.42           N  
ATOM   1324  CA  VAL A 169      26.720  58.791   1.023  1.00 25.79           C  
ATOM   1325  C   VAL A 169      26.224  57.469   1.596  1.00 26.46           C  
ATOM   1326  O   VAL A 169      26.349  57.235   2.809  1.00 26.33           O  
ATOM   1327  CB  VAL A 169      25.511  59.751   0.752  1.00 26.21           C  
ATOM   1328  CG1 VAL A 169      24.680  59.979   2.044  1.00 25.38           C  
ATOM   1329  CG2 VAL A 169      25.993  61.103   0.212  1.00 23.75           C  
ATOM   1330  N   VAL A 170      25.668  56.622   0.721  1.00 26.21           N  
ATOM   1331  CA  VAL A 170      25.174  55.300   1.084  1.00 26.48           C  
ATOM   1332  C   VAL A 170      26.261  54.392   1.712  1.00 26.86           C  
ATOM   1333  O   VAL A 170      25.980  53.662   2.680  1.00 26.95           O  
ATOM   1334  CB  VAL A 170      24.560  54.606  -0.139  1.00 26.68           C  
ATOM   1335  CG1 VAL A 170      24.040  53.216   0.215  1.00 28.37           C  
ATOM   1336  CG2 VAL A 170      23.453  55.469  -0.757  1.00 27.19           C  
ATOM   1337  N   LEU A 171      27.486  54.437   1.176  1.00 25.96           N  
ATOM   1338  CA  LEU A 171      28.573  53.598   1.718  1.00 26.20           C  
ATOM   1339  C   LEU A 171      28.920  54.062   3.108  1.00 25.64           C  
ATOM   1340  O   LEU A 171      29.161  53.246   3.994  1.00 26.16           O  
ATOM   1341  CB  LEU A 171      29.853  53.641   0.857  1.00 25.47           C  
ATOM   1342  CG  LEU A 171      29.749  53.259  -0.616  1.00 27.06           C  
ATOM   1343  CD1 LEU A 171      31.105  53.406  -1.299  1.00 24.42           C  
ATOM   1344  CD2 LEU A 171      29.183  51.857  -0.841  1.00 25.88           C  
ATOM   1345  N   GLN A 172      28.969  55.379   3.303  1.00 25.15           N  
ATOM   1346  CA  GLN A 172      29.320  55.911   4.609  1.00 25.28           C  
ATOM   1347  C   GLN A 172      28.269  55.507   5.659  1.00 26.42           C  
ATOM   1348  O   GLN A 172      28.619  55.057   6.758  1.00 26.82           O  
ATOM   1349  CB  GLN A 172      29.526  57.426   4.574  1.00 24.59           C  
ATOM   1350  CG  GLN A 172      29.904  58.028   5.932  1.00 24.30           C  
ATOM   1351  CD  GLN A 172      30.227  59.503   5.893  1.00 25.11           C  
ATOM   1352  OE1 GLN A 172      30.345  60.105   4.827  1.00 24.00           O  
ATOM   1353  NE2 GLN A 172      30.357  60.104   7.073  1.00 26.18           N  
ATOM   1354  N   VAL A 173      26.992  55.678   5.315  1.00 26.97           N  
ATOM   1355  CA  VAL A 173      25.897  55.257   6.191  1.00 27.16           C  
ATOM   1356  C   VAL A 173      25.869  53.743   6.457  1.00 28.13           C  
ATOM   1357  O   VAL A 173      25.645  53.339   7.596  1.00 27.37           O  
ATOM   1358  CB  VAL A 173      24.515  55.784   5.706  1.00 27.77           C  
ATOM   1359  CG1 VAL A 173      23.427  55.499   6.744  1.00 25.88           C  
ATOM   1360  CG2 VAL A 173      24.580  57.294   5.514  1.00 26.16           C  
ATOM   1361  N   ALA A 174      26.125  52.920   5.433  1.00 28.65           N  
ATOM   1362  CA  ALA A 174      26.169  51.475   5.630  1.00 30.24           C  
ATOM   1363  C   ALA A 174      27.277  51.016   6.596  1.00 31.51           C  
ATOM   1364  O   ALA A 174      27.142  49.982   7.244  1.00 31.25           O  
ATOM   1365  CB  ALA A 174      26.270  50.729   4.275  1.00 29.97           C  
ATOM   1366  N   ALA A 175      28.364  51.783   6.666  1.00 33.65           N  
ATOM   1367  CA  ALA A 175      29.518  51.472   7.514  1.00 35.92           C  
ATOM   1368  C   ALA A 175      29.401  52.041   8.928  1.00 37.40           C  
ATOM   1369  O   ALA A 175      30.152  51.655   9.808  1.00 38.59           O  
ATOM   1370  CB  ALA A 175      30.796  51.975   6.866  1.00 35.41           C  
ATOM   1371  N   ALA A 176      28.476  52.970   9.134  1.00 38.82           N  
ATOM   1372  CA  ALA A 176      28.372  53.663  10.401  1.00 40.54           C  
ATOM   1373  C   ALA A 176      27.114  53.316  11.183  1.00 41.99           C  
ATOM   1374  O   ALA A 176      27.059  53.573  12.379  1.00 42.75           O  
ATOM   1375  CB  ALA A 176      28.477  55.171  10.198  1.00 40.16           C  
ATOM   1376  N   THR A 177      26.113  52.741  10.519  1.00 43.51           N  
ATOM   1377  CA  THR A 177      24.836  52.443  11.172  1.00 45.22           C  
ATOM   1378  C   THR A 177      24.429  50.984  10.995  1.00 46.94           C  
ATOM   1379  O   THR A 177      24.997  50.257  10.174  1.00 47.69           O  
ATOM   1380  CB  THR A 177      23.676  53.333  10.648  1.00 44.70           C  
ATOM   1381  OG1 THR A 177      23.196  52.816   9.405  1.00 43.62           O  
ATOM   1382  CG2 THR A 177      24.101  54.784  10.481  1.00 44.43           C  
ATOM   1383  N   ASN A 178      23.428  50.561  11.754  1.00 48.76           N  
ATOM   1384  CA  ASN A 178      22.940  49.195  11.627  1.00 50.35           C  
ATOM   1385  C   ASN A 178      21.515  49.092  11.080  1.00 51.03           C  
ATOM   1386  O   ASN A 178      20.714  48.293  11.564  1.00 51.57           O  
ATOM   1387  CB  ASN A 178      23.174  48.372  12.922  1.00 50.75           C  
ATOM   1388  CG  ASN A 178      22.404  48.903  14.148  1.00 52.55           C  
ATOM   1389  OD1 ASN A 178      22.422  50.097  14.463  1.00 55.30           O  
ATOM   1390  ND2 ASN A 178      21.759  47.988  14.868  1.00 53.99           N  
ATOM   1391  N   CYS A 179      21.214  49.894  10.054  1.00 51.50           N  
ATOM   1392  CA  CYS A 179      19.975  49.748   9.290  1.00 52.18           C  
ATOM   1393  C   CYS A 179      19.889  48.362   8.646  1.00 51.87           C  
ATOM   1394  O   CYS A 179      20.914  47.696   8.451  1.00 52.16           O  
ATOM   1395  CB  CYS A 179      19.869  50.811   8.188  1.00 52.54           C  
ATOM   1396  SG  CYS A 179      19.792  52.518   8.745  1.00 55.57           S  
ATOM   1397  N   LYS A 180      18.667  47.936   8.308  1.00 51.38           N  
ATOM   1398  CA  LYS A 180      18.454  46.635   7.660  1.00 50.52           C  
ATOM   1399  C   LYS A 180      19.017  46.646   6.259  1.00 49.36           C  
ATOM   1400  O   LYS A 180      19.561  45.653   5.789  1.00 49.88           O  
ATOM   1401  CB  LYS A 180      16.970  46.279   7.536  1.00 51.05           C  
ATOM   1402  CG  LYS A 180      16.046  46.754   8.638  1.00 52.09           C  
ATOM   1403  CD  LYS A 180      14.585  46.720   8.163  1.00 54.04           C  
ATOM   1404  CE  LYS A 180      14.234  45.387   7.510  1.00 54.42           C  
ATOM   1405  NZ  LYS A 180      13.283  45.556   6.380  1.00 55.79           N  
ATOM   1406  N   HIS A 181      18.831  47.768   5.578  1.00 47.77           N  
ATOM   1407  CA  HIS A 181      19.302  47.925   4.221  1.00 46.40           C  
ATOM   1408  C   HIS A 181      19.393  49.409   3.893  1.00 44.89           C  
ATOM   1409  O   HIS A 181      18.625  50.240   4.401  1.00 44.87           O  
ATOM   1410  CB  HIS A 181      18.365  47.219   3.238  1.00 46.77           C  
ATOM   1411  CG  HIS A 181      19.063  46.648   2.041  1.00 47.80           C  
ATOM   1412  ND1 HIS A 181      19.300  45.299   1.889  1.00 48.00           N  
ATOM   1413  CD2 HIS A 181      19.562  47.245   0.933  1.00 48.56           C  
ATOM   1414  CE1 HIS A 181      19.922  45.090   0.741  1.00 49.20           C  
ATOM   1415  NE2 HIS A 181      20.093  46.256   0.141  1.00 47.15           N  
ATOM   1416  N   HIS A 182      20.367  49.736   3.062  1.00 42.54           N  
ATOM   1417  CA  HIS A 182      20.539  51.091   2.576  1.00 39.85           C  
ATOM   1418  C   HIS A 182      20.405  50.995   1.066  1.00 38.03           C  
ATOM   1419  O   HIS A 182      20.781  49.984   0.487  1.00 37.03           O  
ATOM   1420  CB  HIS A 182      21.919  51.622   2.968  1.00 40.19           C  
ATOM   1421  CG  HIS A 182      22.220  51.530   4.434  1.00 39.78           C  
ATOM   1422  ND1 HIS A 182      22.461  52.639   5.216  1.00 40.46           N  
ATOM   1423  CD2 HIS A 182      22.340  50.462   5.257  1.00 39.54           C  
ATOM   1424  CE1 HIS A 182      22.708  52.260   6.457  1.00 39.31           C  
ATOM   1425  NE2 HIS A 182      22.639  50.943   6.508  1.00 39.91           N  
ATOM   1426  N   TYR A 183      19.821  52.018   0.441  1.00 36.66           N  
ATOM   1427  CA  TYR A 183      19.751  52.101  -1.016  1.00 34.89           C  
ATOM   1428  C   TYR A 183      20.168  53.464  -1.545  1.00 33.53           C  
ATOM   1429  O   TYR A 183      19.930  54.502  -0.918  1.00 31.86           O  
ATOM   1430  CB  TYR A 183      18.335  51.828  -1.534  1.00 35.98           C  
ATOM   1431  CG  TYR A 183      17.722  50.525  -1.091  1.00 37.38           C  
ATOM   1432  CD1 TYR A 183      17.007  50.453   0.102  1.00 40.53           C  
ATOM   1433  CD2 TYR A 183      17.832  49.373  -1.871  1.00 40.22           C  
ATOM   1434  CE1 TYR A 183      16.423  49.276   0.518  1.00 41.90           C  
ATOM   1435  CE2 TYR A 183      17.240  48.163  -1.452  1.00 41.83           C  
ATOM   1436  CZ  TYR A 183      16.535  48.142  -0.253  1.00 43.06           C  
ATOM   1437  OH  TYR A 183      15.940  46.994   0.212  1.00 46.15           O  
ATOM   1438  N   GLY A 184      20.774  53.443  -2.726  1.00 32.12           N  
ATOM   1439  CA  GLY A 184      20.975  54.644  -3.483  1.00 30.98           C  
ATOM   1440  C   GLY A 184      20.400  54.440  -4.861  1.00 30.29           C  
ATOM   1441  O   GLY A 184      20.514  53.362  -5.447  1.00 30.09           O  
ATOM   1442  N   VAL A 185      19.765  55.476  -5.375  1.00 30.23           N  
ATOM   1443  CA  VAL A 185      19.232  55.423  -6.706  1.00 30.62           C  
ATOM   1444  C   VAL A 185      19.700  56.642  -7.462  1.00 31.55           C  
ATOM   1445  O   VAL A 185      19.542  57.778  -6.997  1.00 31.01           O  
ATOM   1446  CB  VAL A 185      17.696  55.247  -6.735  1.00 30.48           C  
ATOM   1447  CG1 VAL A 185      16.978  56.290  -5.860  1.00 30.14           C  
ATOM   1448  CG2 VAL A 185      17.199  55.266  -8.160  1.00 29.66           C  
ATOM   1449  N   GLU A 186      20.320  56.378  -8.609  1.00 32.09           N  
ATOM   1450  CA  GLU A 186      20.904  57.413  -9.446  1.00 33.44           C  
ATOM   1451  C   GLU A 186      20.437  57.188 -10.874  1.00 34.14           C  
ATOM   1452  O   GLU A 186      20.494  56.064 -11.385  1.00 34.95           O  
ATOM   1453  CB  GLU A 186      22.440  57.388  -9.375  1.00 32.69           C  
ATOM   1454  CG  GLU A 186      23.136  58.343 -10.371  1.00 32.99           C  
ATOM   1455  CD  GLU A 186      22.675  59.796 -10.218  1.00 34.22           C  
ATOM   1456  OE1 GLU A 186      22.792  60.355  -9.101  1.00 33.37           O  
ATOM   1457  OE2 GLU A 186      22.213  60.384 -11.226  1.00 35.91           O  
ATOM   1458  N   LYS A 187      19.993  58.269 -11.504  1.00 35.37           N  
ATOM   1459  CA  LYS A 187      19.514  58.250 -12.884  1.00 36.60           C  
ATOM   1460  C   LYS A 187      20.609  58.420 -13.941  1.00 36.35           C  
ATOM   1461  O   LYS A 187      20.550  57.781 -14.988  1.00 36.69           O  
ATOM   1462  CB  LYS A 187      18.491  59.361 -13.063  1.00 37.07           C  
ATOM   1463  CG  LYS A 187      17.436  59.095 -14.124  1.00 39.34           C  
ATOM   1464  CD  LYS A 187      16.324  60.134 -14.012  1.00 41.68           C  
ATOM   1465  CE  LYS A 187      16.529  61.287 -14.991  1.00 44.47           C  
ATOM   1466  NZ  LYS A 187      15.973  60.899 -16.329  1.00 45.51           N  
ATOM   1467  N   ALA A 188      21.580  59.302 -13.696  1.00 36.44           N  
ATOM   1468  CA  ALA A 188      22.524  59.698 -14.757  1.00 36.48           C  
ATOM   1469  C   ALA A 188      23.598  58.644 -14.967  1.00 36.98           C  
ATOM   1470  O   ALA A 188      24.128  58.076 -14.002  1.00 36.79           O  
ATOM   1471  CB  ALA A 188      23.141  61.044 -14.476  1.00 36.81           C  
ATOM   1472  N   ASP A 189      23.895  58.392 -16.240  1.00 36.98           N  
ATOM   1473  CA  ASP A 189      24.707  57.270 -16.676  1.00 37.59           C  
ATOM   1474  C   ASP A 189      26.117  57.308 -16.106  1.00 36.91           C  
ATOM   1475  O   ASP A 189      26.613  56.308 -15.591  1.00 36.72           O  
ATOM   1476  CB  ASP A 189      24.748  57.223 -18.214  1.00 38.78           C  
ATOM   1477  CG  ASP A 189      23.421  56.756 -18.835  1.00 41.42           C  
ATOM   1478  OD1 ASP A 189      22.459  56.418 -18.097  1.00 45.90           O  
ATOM   1479  OD2 ASP A 189      23.335  56.725 -20.081  1.00 46.31           O  
ATOM   1480  N   ILE A 190      26.756  58.466 -16.195  1.00 36.12           N  
ATOM   1481  CA  ILE A 190      28.123  58.614 -15.712  1.00 35.79           C  
ATOM   1482  C   ILE A 190      28.303  58.282 -14.200  1.00 35.10           C  
ATOM   1483  O   ILE A 190      29.110  57.407 -13.857  1.00 35.29           O  
ATOM   1484  CB  ILE A 190      28.740  59.981 -16.131  1.00 35.26           C  
ATOM   1485  CG1 ILE A 190      28.937  60.004 -17.665  1.00 36.26           C  
ATOM   1486  CG2 ILE A 190      30.055  60.213 -15.399  1.00 36.27           C  
ATOM   1487  CD1 ILE A 190      29.431  61.351 -18.267  1.00 33.50           C  
ATOM   1488  N   PRO A 191      27.548  58.946 -13.302  1.00 34.91           N  
ATOM   1489  CA  PRO A 191      27.743  58.561 -11.879  1.00 34.47           C  
ATOM   1490  C   PRO A 191      27.268  57.139 -11.555  1.00 34.35           C  
ATOM   1491  O   PRO A 191      27.940  56.421 -10.788  1.00 33.31           O  
ATOM   1492  CB  PRO A 191      26.954  59.615 -11.095  1.00 34.50           C  
ATOM   1493  CG  PRO A 191      25.989  60.230 -12.108  1.00 34.99           C  
ATOM   1494  CD  PRO A 191      26.629  60.091 -13.466  1.00 33.76           C  
ATOM   1495  N   ALA A 192      26.159  56.706 -12.157  1.00 34.12           N  
ATOM   1496  CA  ALA A 192      25.692  55.335 -11.951  1.00 34.23           C  
ATOM   1497  C   ALA A 192      26.730  54.299 -12.360  1.00 35.10           C  
ATOM   1498  O   ALA A 192      26.893  53.284 -11.672  1.00 35.38           O  
ATOM   1499  CB  ALA A 192      24.397  55.077 -12.654  1.00 34.77           C  
ATOM   1500  N   LYS A 193      27.428  54.555 -13.468  1.00 35.01           N  
ATOM   1501  CA  LYS A 193      28.518  53.690 -13.913  1.00 35.69           C  
ATOM   1502  C   LYS A 193      29.645  53.607 -12.858  1.00 35.10           C  
ATOM   1503  O   LYS A 193      30.049  52.514 -12.455  1.00 35.45           O  
ATOM   1504  CB  LYS A 193      29.046  54.160 -15.283  1.00 36.01           C  
ATOM   1505  CG  LYS A 193      30.207  53.338 -15.846  1.00 39.66           C  
ATOM   1506  CD  LYS A 193      29.800  51.888 -16.125  1.00 43.03           C  
ATOM   1507  CE  LYS A 193      31.024  51.014 -16.327  1.00 45.69           C  
ATOM   1508  NZ  LYS A 193      30.656  49.566 -16.414  1.00 47.75           N  
ATOM   1509  N   TYR A 194      30.120  54.760 -12.395  1.00 34.11           N  
ATOM   1510  CA  TYR A 194      31.160  54.812 -11.363  1.00 33.35           C  
ATOM   1511  C   TYR A 194      30.742  54.150 -10.049  1.00 32.35           C  
ATOM   1512  O   TYR A 194      31.573  53.535  -9.358  1.00 31.18           O  
ATOM   1513  CB  TYR A 194      31.568  56.251 -11.087  1.00 33.00           C  
ATOM   1514  CG  TYR A 194      32.500  56.867 -12.098  1.00 34.98           C  
ATOM   1515  CD1 TYR A 194      33.517  56.118 -12.704  1.00 37.30           C  
ATOM   1516  CD2 TYR A 194      32.399  58.210 -12.423  1.00 35.58           C  
ATOM   1517  CE1 TYR A 194      34.390  56.691 -13.617  1.00 36.38           C  
ATOM   1518  CE2 TYR A 194      33.278  58.797 -13.342  1.00 38.07           C  
ATOM   1519  CZ  TYR A 194      34.265  58.025 -13.931  1.00 39.62           C  
ATOM   1520  OH  TYR A 194      35.128  58.596 -14.835  1.00 41.28           O  
ATOM   1521  N   ALA A 195      29.460  54.278  -9.712  1.00 31.16           N  
ATOM   1522  CA  ALA A 195      28.917  53.687  -8.488  1.00 31.52           C  
ATOM   1523  C   ALA A 195      29.055  52.166  -8.475  1.00 31.67           C  
ATOM   1524  O   ALA A 195      29.092  51.570  -7.415  1.00 31.72           O  
ATOM   1525  CB  ALA A 195      27.435  54.101  -8.283  1.00 30.78           C  
ATOM   1526  N   GLU A 196      29.097  51.546  -9.658  1.00 32.55           N  
ATOM   1527  CA  GLU A 196      29.226  50.086  -9.782  1.00 32.33           C  
ATOM   1528  C   GLU A 196      30.592  49.651  -9.309  1.00 31.57           C  
ATOM   1529  O   GLU A 196      30.713  48.644  -8.590  1.00 31.40           O  
ATOM   1530  CB  GLU A 196      29.013  49.623 -11.233  1.00 32.67           C  
ATOM   1531  CG  GLU A 196      27.644  49.972 -11.806  1.00 35.26           C  
ATOM   1532  CD  GLU A 196      27.386  49.389 -13.196  1.00 40.24           C  
ATOM   1533  OE1 GLU A 196      28.315  49.328 -14.035  1.00 43.56           O  
ATOM   1534  OE2 GLU A 196      26.229  49.015 -13.461  1.00 43.08           O  
ATOM   1535  N   THR A 197      31.611  50.396  -9.744  1.00 31.07           N  
ATOM   1536  CA  THR A 197      32.990  50.221  -9.281  1.00 30.91           C  
ATOM   1537  C   THR A 197      33.141  50.622  -7.820  1.00 30.38           C  
ATOM   1538  O   THR A 197      33.833  49.925  -7.074  1.00 29.41           O  
ATOM   1539  CB  THR A 197      34.028  51.036 -10.124  1.00 31.44           C  
ATOM   1540  OG1 THR A 197      33.803  50.820 -11.517  1.00 32.59           O  
ATOM   1541  CG2 THR A 197      35.462  50.606  -9.805  1.00 30.27           C  
ATOM   1542  N   MET A 198      32.512  51.739  -7.411  1.00 30.10           N  
ATOM   1543  CA  MET A 198      32.549  52.155  -5.995  1.00 29.71           C  
ATOM   1544  C   MET A 198      32.059  51.012  -5.125  1.00 29.51           C  
ATOM   1545  O   MET A 198      32.653  50.701  -4.113  1.00 29.61           O  
ATOM   1546  CB  MET A 198      31.687  53.405  -5.729  1.00 29.22           C  
ATOM   1547  CG  MET A 198      32.216  54.696  -6.321  1.00 28.30           C  
ATOM   1548  SD  MET A 198      33.484  55.545  -5.399  1.00 27.93           S  
ATOM   1549  CE  MET A 198      32.620  56.049  -3.895  1.00 26.14           C  
ATOM   1550  N   ASP A 199      30.968  50.374  -5.541  1.00 30.52           N  
ATOM   1551  CA  ASP A 199      30.388  49.279  -4.777  1.00 31.14           C  
ATOM   1552  C   ASP A 199      31.422  48.161  -4.569  1.00 31.55           C  
ATOM   1553  O   ASP A 199      31.662  47.733  -3.431  1.00 30.72           O  
ATOM   1554  CB  ASP A 199      29.127  48.762  -5.495  1.00 32.36           C  
ATOM   1555  CG  ASP A 199      28.549  47.500  -4.867  1.00 33.47           C  
ATOM   1556  OD1 ASP A 199      28.567  47.329  -3.629  1.00 33.51           O  
ATOM   1557  OD2 ASP A 199      28.060  46.664  -5.640  1.00 39.69           O  
ATOM   1558  N   ARG A 200      32.044  47.728  -5.668  1.00 31.93           N  
ATOM   1559  CA  ARG A 200      33.043  46.657  -5.648  1.00 32.27           C  
ATOM   1560  C   ARG A 200      34.282  47.014  -4.842  1.00 31.48           C  
ATOM   1561  O   ARG A 200      34.767  46.185  -4.066  1.00 32.05           O  
ATOM   1562  CB  ARG A 200      33.477  46.265  -7.075  1.00 33.29           C  
ATOM   1563  CG  ARG A 200      32.331  45.765  -7.974  1.00 35.68           C  
ATOM   1564  CD  ARG A 200      32.837  45.359  -9.366  1.00 41.07           C  
ATOM   1565  NE  ARG A 200      32.053  46.030 -10.410  1.00 45.51           N  
ATOM   1566  CZ  ARG A 200      32.546  46.892 -11.298  1.00 47.79           C  
ATOM   1567  NH1 ARG A 200      33.847  47.186 -11.324  1.00 48.47           N  
ATOM   1568  NH2 ARG A 200      31.731  47.454 -12.176  1.00 49.49           N  
ATOM   1569  N   GLU A 201      34.812  48.221  -5.046  1.00 30.13           N  
ATOM   1570  CA  GLU A 201      36.018  48.656  -4.329  1.00 29.14           C  
ATOM   1571  C   GLU A 201      35.777  48.770  -2.826  1.00 28.01           C  
ATOM   1572  O   GLU A 201      36.653  48.446  -2.029  1.00 27.30           O  
ATOM   1573  CB  GLU A 201      36.552  49.984  -4.879  1.00 28.74           C  
ATOM   1574  CG  GLU A 201      37.132  49.916  -6.302  1.00 30.47           C  
ATOM   1575  CD  GLU A 201      38.569  49.388  -6.349  1.00 31.74           C  
ATOM   1576  OE1 GLU A 201      39.249  49.355  -5.304  1.00 29.17           O  
ATOM   1577  OE2 GLU A 201      39.017  49.015  -7.452  1.00 31.80           O  
ATOM   1578  N   PHE A 202      34.594  49.258  -2.448  1.00 27.76           N  
ATOM   1579  CA  PHE A 202      34.227  49.349  -1.044  1.00 27.78           C  
ATOM   1580  C   PHE A 202      34.141  47.965  -0.389  1.00 28.46           C  
ATOM   1581  O   PHE A 202      34.729  47.744   0.672  1.00 28.14           O  
ATOM   1582  CB  PHE A 202      32.913  50.113  -0.884  1.00 27.92           C  
ATOM   1583  CG  PHE A 202      32.475  50.283   0.551  1.00 26.87           C  
ATOM   1584  CD1 PHE A 202      33.111  51.209   1.381  1.00 27.20           C  
ATOM   1585  CD2 PHE A 202      31.434  49.517   1.060  1.00 26.58           C  
ATOM   1586  CE1 PHE A 202      32.703  51.388   2.684  1.00 25.37           C  
ATOM   1587  CE2 PHE A 202      30.999  49.681   2.364  1.00 28.14           C  
ATOM   1588  CZ  PHE A 202      31.633  50.612   3.185  1.00 28.64           C  
ATOM   1589  N   ARG A 203      33.406  47.037  -1.002  1.00 28.49           N  
ATOM   1590  CA  ARG A 203      33.315  45.683  -0.433  1.00 29.46           C  
ATOM   1591  C   ARG A 203      34.725  45.049  -0.333  1.00 29.39           C  
ATOM   1592  O   ARG A 203      35.044  44.396   0.660  1.00 28.19           O  
ATOM   1593  CB  ARG A 203      32.355  44.782  -1.239  1.00 29.62           C  
ATOM   1594  CG  ARG A 203      30.871  45.183  -1.117  1.00 30.66           C  
ATOM   1595  CD  ARG A 203      29.932  44.329  -2.016  1.00 34.74           C  
ATOM   1596  NE  ARG A 203      28.645  45.010  -2.194  1.00 36.08           N  
ATOM   1597  CZ  ARG A 203      27.593  44.900  -1.376  1.00 38.54           C  
ATOM   1598  NH1 ARG A 203      27.634  44.086  -0.322  1.00 37.20           N  
ATOM   1599  NH2 ARG A 203      26.479  45.593  -1.625  1.00 38.61           N  
ATOM   1600  N   LYS A 204      35.573  45.282  -1.343  1.00 29.85           N  
ATOM   1601  CA  LYS A 204      36.945  44.749  -1.293  1.00 30.18           C  
ATOM   1602  C   LYS A 204      37.818  45.378  -0.193  1.00 29.79           C  
ATOM   1603  O   LYS A 204      38.463  44.651   0.574  1.00 29.42           O  
ATOM   1604  CB  LYS A 204      37.630  44.810  -2.674  1.00 31.01           C  
ATOM   1605  CG  LYS A 204      39.154  44.551  -2.639  1.00 32.49           C  
ATOM   1606  CD  LYS A 204      39.858  44.996  -3.923  1.00 35.69           C  
ATOM   1607  CE  LYS A 204      39.860  46.502  -4.027  1.00 36.59           C  
ATOM   1608  NZ  LYS A 204      40.790  47.034  -5.042  1.00 36.48           N  
ATOM   1609  N   TRP A 205      37.864  46.709  -0.124  1.00 28.94           N  
ATOM   1610  CA  TRP A 205      38.689  47.372   0.902  1.00 29.09           C  
ATOM   1611  C   TRP A 205      38.197  47.093   2.313  1.00 29.49           C  
ATOM   1612  O   TRP A 205      39.015  46.903   3.203  1.00 28.51           O  
ATOM   1613  CB  TRP A 205      38.847  48.901   0.672  1.00 28.58           C  
ATOM   1614  CG  TRP A 205      39.785  49.198  -0.431  1.00 27.52           C  
ATOM   1615  CD1 TRP A 205      39.467  49.603  -1.699  1.00 29.02           C  
ATOM   1616  CD2 TRP A 205      41.214  49.054  -0.403  1.00 28.41           C  
ATOM   1617  NE1 TRP A 205      40.617  49.740  -2.456  1.00 30.67           N  
ATOM   1618  CE2 TRP A 205      41.699  49.418  -1.683  1.00 27.57           C  
ATOM   1619  CE3 TRP A 205      42.133  48.662   0.581  1.00 27.80           C  
ATOM   1620  CZ2 TRP A 205      43.060  49.395  -2.004  1.00 29.28           C  
ATOM   1621  CZ3 TRP A 205      43.504  48.666   0.260  1.00 27.78           C  
ATOM   1622  CH2 TRP A 205      43.941  49.010  -1.022  1.00 26.19           C  
ATOM   1623  N   MET A 206      36.871  47.048   2.510  1.00 30.05           N  
ATOM   1624  CA  MET A 206      36.327  46.753   3.827  1.00 30.13           C  
ATOM   1625  C   MET A 206      36.753  45.351   4.292  1.00 31.10           C  
ATOM   1626  O   MET A 206      37.062  45.160   5.460  1.00 30.95           O  
ATOM   1627  CB  MET A 206      34.807  46.916   3.860  1.00 30.47           C  
ATOM   1628  CG  MET A 206      34.340  48.398   3.803  1.00 29.91           C  
ATOM   1629  SD  MET A 206      34.611  49.350   5.312  1.00 30.39           S  
ATOM   1630  CE  MET A 206      33.262  48.666   6.305  1.00 30.28           C  
ATOM   1631  N   LYS A 207      36.797  44.398   3.359  1.00 31.46           N  
ATOM   1632  CA  LYS A 207      37.290  43.049   3.646  1.00 32.54           C  
ATOM   1633  C   LYS A 207      38.793  43.086   3.917  1.00 31.62           C  
ATOM   1634  O   LYS A 207      39.262  42.452   4.846  1.00 32.16           O  
ATOM   1635  CB  LYS A 207      36.958  42.088   2.506  1.00 32.50           C  
ATOM   1636  CG  LYS A 207      35.504  41.620   2.527  1.00 36.77           C  
ATOM   1637  CD  LYS A 207      35.174  40.670   1.366  1.00 40.89           C  
ATOM   1638  CE  LYS A 207      35.414  39.216   1.747  1.00 44.55           C  
ATOM   1639  NZ  LYS A 207      35.068  38.258   0.635  1.00 47.28           N  
ATOM   1640  N   TRP A 208      39.529  43.883   3.149  1.00 31.28           N  
ATOM   1641  CA  TRP A 208      40.974  44.063   3.369  1.00 30.53           C  
ATOM   1642  C   TRP A 208      41.309  44.551   4.786  1.00 30.54           C  
ATOM   1643  O   TRP A 208      42.265  44.076   5.406  1.00 30.28           O  
ATOM   1644  CB  TRP A 208      41.555  45.034   2.345  1.00 30.07           C  
ATOM   1645  CG  TRP A 208      43.067  44.988   2.221  1.00 30.06           C  
ATOM   1646  CD1 TRP A 208      43.784  44.188   1.383  1.00 28.13           C  
ATOM   1647  CD2 TRP A 208      44.032  45.786   2.938  1.00 30.17           C  
ATOM   1648  NE1 TRP A 208      45.132  44.435   1.527  1.00 30.51           N  
ATOM   1649  CE2 TRP A 208      45.311  45.405   2.478  1.00 30.74           C  
ATOM   1650  CE3 TRP A 208      43.938  46.781   3.918  1.00 30.56           C  
ATOM   1651  CZ2 TRP A 208      46.488  45.989   2.959  1.00 32.77           C  
ATOM   1652  CZ3 TRP A 208      45.107  47.349   4.412  1.00 30.84           C  
ATOM   1653  CH2 TRP A 208      46.372  46.955   3.924  1.00 32.01           C  
ATOM   1654  N   TYR A 209      40.539  45.518   5.280  1.00 30.18           N  
ATOM   1655  CA  TYR A 209      40.780  46.085   6.614  1.00 30.19           C  
ATOM   1656  C   TYR A 209      40.157  45.229   7.714  1.00 30.35           C  
ATOM   1657  O   TYR A 209      40.456  45.435   8.886  1.00 31.58           O  
ATOM   1658  CB  TYR A 209      40.232  47.515   6.725  1.00 29.11           C  
ATOM   1659  CG  TYR A 209      41.046  48.560   5.992  1.00 28.34           C  
ATOM   1660  CD1 TYR A 209      42.202  49.082   6.559  1.00 24.88           C  
ATOM   1661  CD2 TYR A 209      40.647  49.030   4.739  1.00 25.76           C  
ATOM   1662  CE1 TYR A 209      42.953  50.041   5.907  1.00 28.08           C  
ATOM   1663  CE2 TYR A 209      41.397  49.978   4.067  1.00 28.00           C  
ATOM   1664  CZ  TYR A 209      42.536  50.493   4.665  1.00 26.71           C  
ATOM   1665  OH  TYR A 209      43.281  51.435   4.027  1.00 29.62           O  
ATOM   1666  N   GLY A 210      39.304  44.288   7.316  1.00 30.81           N  
ATOM   1667  CA  GLY A 210      38.568  43.406   8.211  1.00 31.53           C  
ATOM   1668  C   GLY A 210      37.475  44.128   8.983  1.00 32.60           C  
ATOM   1669  O   GLY A 210      37.291  43.887  10.186  1.00 32.53           O  
ATOM   1670  N   LYS A 211      36.757  45.020   8.298  1.00 32.24           N  
ATOM   1671  CA  LYS A 211      35.726  45.827   8.954  1.00 33.27           C  
ATOM   1672  C   LYS A 211      34.357  45.503   8.407  1.00 33.71           C  
ATOM   1673  O   LYS A 211      34.240  45.080   7.257  1.00 33.10           O  
ATOM   1674  CB  LYS A 211      36.016  47.319   8.779  1.00 33.15           C  
ATOM   1675  CG  LYS A 211      37.282  47.792   9.440  1.00 33.20           C  
ATOM   1676  CD  LYS A 211      37.170  47.610  10.938  1.00 33.81           C  
ATOM   1677  CE  LYS A 211      38.403  48.076  11.667  1.00 34.99           C  
ATOM   1678  NZ  LYS A 211      38.187  47.831  13.121  1.00 37.46           N  
ATOM   1679  N   LYS A 212      33.319  45.702   9.226  1.00 34.85           N  
ATOM   1680  CA  LYS A 212      31.954  45.363   8.829  1.00 36.07           C  
ATOM   1681  C   LYS A 212      31.149  46.560   8.293  1.00 36.06           C  
ATOM   1682  O   LYS A 212      31.380  47.694   8.689  1.00 36.07           O  
ATOM   1683  CB  LYS A 212      31.210  44.771  10.032  1.00 37.02           C  
ATOM   1684  CG  LYS A 212      29.802  44.307   9.745  1.00 38.85           C  
ATOM   1685  CD  LYS A 212      28.834  44.773  10.841  1.00 42.72           C  
ATOM   1686  CE  LYS A 212      28.985  43.964  12.112  1.00 44.07           C  
ATOM   1687  NZ  LYS A 212      28.371  44.676  13.262  1.00 46.08           N  
ATOM   1688  N   HIS A 213      30.196  46.281   7.407  1.00 36.68           N  
ATOM   1689  CA  HIS A 213      29.178  47.247   6.980  1.00 37.25           C  
ATOM   1690  C   HIS A 213      27.823  46.549   6.878  1.00 37.97           C  
ATOM   1691  O   HIS A 213      27.764  45.335   6.714  1.00 38.26           O  
ATOM   1692  CB  HIS A 213      29.534  47.848   5.621  1.00 36.95           C  
ATOM   1693  CG  HIS A 213      29.649  46.832   4.527  1.00 37.57           C  
ATOM   1694  ND1 HIS A 213      28.557  46.350   3.840  1.00 36.00           N  
ATOM   1695  CD2 HIS A 213      30.729  46.196   4.009  1.00 37.75           C  
ATOM   1696  CE1 HIS A 213      28.954  45.462   2.945  1.00 36.52           C  
ATOM   1697  NE2 HIS A 213      30.269  45.360   3.018  1.00 37.50           N  
ATOM   1698  N   ALA A 214      26.743  47.321   6.954  1.00 39.06           N  
ATOM   1699  CA  ALA A 214      25.394  46.816   6.687  1.00 39.71           C  
ATOM   1700  C   ALA A 214      25.162  46.556   5.196  1.00 40.11           C  
ATOM   1701  O   ALA A 214      25.923  47.018   4.344  1.00 40.50           O  
ATOM   1702  CB  ALA A 214      24.354  47.801   7.207  1.00 40.26           C  
ATOM   1703  N   GLU A 215      24.090  45.827   4.893  1.00 39.78           N  
ATOM   1704  CA  GLU A 215      23.679  45.571   3.518  1.00 39.41           C  
ATOM   1705  C   GLU A 215      23.311  46.887   2.840  1.00 38.28           C  
ATOM   1706  O   GLU A 215      22.747  47.788   3.472  1.00 37.88           O  
ATOM   1707  CB  GLU A 215      22.471  44.625   3.494  1.00 39.95           C  
ATOM   1708  CG  GLU A 215      22.404  43.656   4.705  1.00 43.38           C  
ATOM   1709  CD  GLU A 215      21.400  42.505   4.530  1.00 47.83           C  
ATOM   1710  OE1 GLU A 215      20.373  42.673   3.825  1.00 49.09           O  
ATOM   1711  OE2 GLU A 215      21.638  41.429   5.120  1.00 49.62           O  
ATOM   1712  N   TYR A 216      23.647  47.005   1.561  1.00 37.18           N  
ATOM   1713  CA  TYR A 216      23.281  48.193   0.787  1.00 36.83           C  
ATOM   1714  C   TYR A 216      23.208  47.842  -0.683  1.00 36.77           C  
ATOM   1715  O   TYR A 216      23.837  46.896  -1.132  1.00 37.21           O  
ATOM   1716  CB  TYR A 216      24.284  49.334   1.001  1.00 36.23           C  
ATOM   1717  CG  TYR A 216      25.632  49.076   0.365  1.00 35.13           C  
ATOM   1718  CD1 TYR A 216      25.878  49.402  -0.975  1.00 35.35           C  
ATOM   1719  CD2 TYR A 216      26.655  48.485   1.097  1.00 34.65           C  
ATOM   1720  CE1 TYR A 216      27.140  49.146  -1.557  1.00 35.19           C  
ATOM   1721  CE2 TYR A 216      27.898  48.220   0.531  1.00 32.31           C  
ATOM   1722  CZ  TYR A 216      28.135  48.546  -0.785  1.00 32.95           C  
ATOM   1723  OH  TYR A 216      29.382  48.269  -1.314  1.00 33.05           O  
ATOM   1724  N   THR A 217      22.462  48.623  -1.445  1.00 36.93           N  
ATOM   1725  CA  THR A 217      22.444  48.431  -2.881  1.00 37.54           C  
ATOM   1726  C   THR A 217      22.494  49.782  -3.555  1.00 37.66           C  
ATOM   1727  O   THR A 217      21.743  50.699  -3.185  1.00 37.34           O  
ATOM   1728  CB  THR A 217      21.166  47.691  -3.325  1.00 37.54           C  
ATOM   1729  OG1 THR A 217      21.007  46.514  -2.522  1.00 38.34           O  
ATOM   1730  CG2 THR A 217      21.258  47.302  -4.804  1.00 38.82           C  
ATOM   1731  N   LEU A 218      23.374  49.895  -4.542  1.00 37.10           N  
ATOM   1732  CA  LEU A 218      23.421  51.064  -5.390  1.00 37.51           C  
ATOM   1733  C   LEU A 218      22.802  50.721  -6.740  1.00 38.00           C  
ATOM   1734  O   LEU A 218      23.334  49.898  -7.481  1.00 38.23           O  
ATOM   1735  CB  LEU A 218      24.865  51.581  -5.534  1.00 36.94           C  
ATOM   1736  CG  LEU A 218      25.607  51.969  -4.246  1.00 36.15           C  
ATOM   1737  CD1 LEU A 218      27.069  52.331  -4.576  1.00 35.10           C  
ATOM   1738  CD2 LEU A 218      24.926  53.151  -3.544  1.00 32.43           C  
ATOM   1739  N   GLU A 219      21.668  51.357  -7.038  1.00 38.85           N  
ATOM   1740  CA  GLU A 219      20.867  51.075  -8.240  1.00 39.82           C  
ATOM   1741  C   GLU A 219      20.872  52.234  -9.224  1.00 40.62           C  
ATOM   1742  O   GLU A 219      20.926  53.410  -8.833  1.00 40.59           O  
ATOM   1743  CB  GLU A 219      19.401  50.807  -7.841  1.00 39.41           C  
ATOM   1744  CG  GLU A 219      19.204  49.606  -6.935  1.00 40.29           C  
ATOM   1745  CD  GLU A 219      17.798  49.498  -6.370  1.00 41.52           C  
ATOM   1746  OE1 GLU A 219      16.830  49.905  -7.047  1.00 42.17           O  
ATOM   1747  OE2 GLU A 219      17.666  48.994  -5.238  1.00 42.60           O  
ATOM   1748  N   ARG A 220      20.809  51.898 -10.505  1.00 41.24           N  
ATOM   1749  CA  ARG A 220      20.473  52.871 -11.525  1.00 42.31           C  
ATOM   1750  C   ARG A 220      18.933  52.996 -11.557  1.00 42.29           C  
ATOM   1751  O   ARG A 220      18.227  51.994 -11.405  1.00 42.81           O  
ATOM   1752  CB  ARG A 220      21.042  52.421 -12.869  1.00 43.05           C  
ATOM   1753  CG  ARG A 220      20.479  53.139 -14.099  1.00 45.56           C  
ATOM   1754  CD  ARG A 220      20.867  52.399 -15.377  1.00 48.89           C  
ATOM   1755  NE  ARG A 220      22.307  52.478 -15.623  1.00 51.42           N  
ATOM   1756  CZ  ARG A 220      22.923  53.539 -16.134  1.00 52.53           C  
ATOM   1757  NH1 ARG A 220      22.225  54.621 -16.456  1.00 53.48           N  
ATOM   1758  NH2 ARG A 220      24.239  53.523 -16.318  1.00 53.88           N  
ATOM   1759  N   GLY A 221      18.410  54.213 -11.703  1.00 41.82           N  
ATOM   1760  CA  GLY A 221      16.950  54.407 -11.808  1.00 41.23           C  
ATOM   1761  C   GLY A 221      16.434  55.834 -11.649  1.00 40.84           C  
ATOM   1762  O   GLY A 221      17.205  56.757 -11.380  1.00 40.76           O  
ATOM   1763  N   ASP A 222      15.118  56.001 -11.811  1.00 40.11           N  
ATOM   1764  CA  ASP A 222      14.434  57.290 -11.652  1.00 39.46           C  
ATOM   1765  C   ASP A 222      13.603  57.294 -10.355  1.00 38.73           C  
ATOM   1766  O   ASP A 222      12.604  56.578 -10.243  1.00 38.10           O  
ATOM   1767  CB  ASP A 222      13.523  57.516 -12.869  1.00 40.12           C  
ATOM   1768  CG  ASP A 222      12.961  58.931 -12.964  1.00 40.32           C  
ATOM   1769  OD1 ASP A 222      12.852  59.652 -11.953  1.00 39.26           O  
ATOM   1770  OD2 ASP A 222      12.598  59.324 -14.095  1.00 43.94           O  
ATOM   1771  N   PHE A 223      13.986  58.100  -9.369  1.00 37.44           N  
ATOM   1772  CA  PHE A 223      13.243  58.050  -8.096  1.00 36.56           C  
ATOM   1773  C   PHE A 223      11.809  58.615  -8.193  1.00 35.72           C  
ATOM   1774  O   PHE A 223      11.058  58.636  -7.211  1.00 34.93           O  
ATOM   1775  CB  PHE A 223      14.020  58.715  -6.956  1.00 36.01           C  
ATOM   1776  CG  PHE A 223      14.337  60.164  -7.190  1.00 37.78           C  
ATOM   1777  CD1 PHE A 223      13.328  61.095  -7.441  1.00 37.04           C  
ATOM   1778  CD2 PHE A 223      15.658  60.614  -7.115  1.00 37.01           C  
ATOM   1779  CE1 PHE A 223      13.632  62.449  -7.653  1.00 37.33           C  
ATOM   1780  CE2 PHE A 223      15.969  61.958  -7.320  1.00 36.48           C  
ATOM   1781  CZ  PHE A 223      14.948  62.878  -7.591  1.00 37.13           C  
ATOM   1782  N   LEU A 224      11.443  59.093  -9.367  1.00 35.95           N  
ATOM   1783  CA  LEU A 224      10.077  59.567  -9.579  1.00 37.28           C  
ATOM   1784  C   LEU A 224       9.151  58.500 -10.185  1.00 37.91           C  
ATOM   1785  O   LEU A 224       7.927  58.703 -10.255  1.00 38.39           O  
ATOM   1786  CB  LEU A 224      10.068  60.844 -10.420  1.00 36.82           C  
ATOM   1787  CG  LEU A 224      10.718  62.084  -9.801  1.00 37.27           C  
ATOM   1788  CD1 LEU A 224      10.609  63.238 -10.749  1.00 36.33           C  
ATOM   1789  CD2 LEU A 224      10.070  62.451  -8.476  1.00 38.49           C  
ATOM   1790  N   SER A 225       9.730  57.370 -10.595  1.00 38.92           N  
ATOM   1791  CA  SER A 225       8.985  56.244 -11.199  1.00 39.46           C  
ATOM   1792  C   SER A 225       7.874  55.686 -10.303  1.00 40.62           C  
ATOM   1793  O   SER A 225       7.839  55.945  -9.086  1.00 39.97           O  
ATOM   1794  CB  SER A 225       9.944  55.103 -11.545  1.00 39.67           C  
ATOM   1795  OG  SER A 225      10.366  54.421 -10.370  1.00 38.25           O  
ATOM   1796  N   GLU A 226       6.986  54.893 -10.911  1.00 41.65           N  
ATOM   1797  CA  GLU A 226       5.903  54.231 -10.185  1.00 42.66           C  
ATOM   1798  C   GLU A 226       6.439  53.304  -9.103  1.00 42.26           C  
ATOM   1799  O   GLU A 226       5.987  53.357  -7.961  1.00 42.55           O  
ATOM   1800  CB  GLU A 226       4.991  53.454 -11.152  1.00 43.42           C  
ATOM   1801  CG  GLU A 226       3.561  53.304 -10.653  1.00 47.15           C  
ATOM   1802  CD  GLU A 226       2.811  54.632 -10.627  1.00 51.67           C  
ATOM   1803  OE1 GLU A 226       2.265  54.994  -9.563  1.00 52.47           O  
ATOM   1804  OE2 GLU A 226       2.777  55.315 -11.676  1.00 54.31           O  
ATOM   1805  N   GLU A 227       7.403  52.459  -9.460  1.00 41.97           N  
ATOM   1806  CA  GLU A 227       8.057  51.576  -8.491  1.00 41.93           C  
ATOM   1807  C   GLU A 227       8.515  52.361  -7.250  1.00 41.03           C  
ATOM   1808  O   GLU A 227       8.296  51.929  -6.121  1.00 41.19           O  
ATOM   1809  CB  GLU A 227       9.245  50.841  -9.147  1.00 42.54           C  
ATOM   1810  CG  GLU A 227      10.348  50.324  -8.180  1.00 44.92           C  
ATOM   1811  CD  GLU A 227      11.742  50.160  -8.839  1.00 48.43           C  
ATOM   1812  OE1 GLU A 227      11.847  50.003 -10.077  1.00 50.03           O  
ATOM   1813  OE2 GLU A 227      12.752  50.184  -8.103  1.00 49.50           O  
ATOM   1814  N   TRP A 228       9.138  53.516  -7.469  1.00 40.06           N  
ATOM   1815  CA  TRP A 228       9.751  54.267  -6.379  1.00 38.77           C  
ATOM   1816  C   TRP A 228       8.784  54.938  -5.404  1.00 38.74           C  
ATOM   1817  O   TRP A 228       9.167  55.227  -4.251  1.00 38.26           O  
ATOM   1818  CB  TRP A 228      10.833  55.219  -6.909  1.00 38.39           C  
ATOM   1819  CG  TRP A 228      12.154  54.527  -6.971  1.00 38.00           C  
ATOM   1820  CD1 TRP A 228      12.747  53.977  -8.073  1.00 37.61           C  
ATOM   1821  CD2 TRP A 228      13.032  54.264  -5.866  1.00 36.94           C  
ATOM   1822  NE1 TRP A 228      13.955  53.402  -7.719  1.00 38.65           N  
ATOM   1823  CE2 TRP A 228      14.150  53.565  -6.373  1.00 37.04           C  
ATOM   1824  CE3 TRP A 228      12.986  54.566  -4.493  1.00 37.33           C  
ATOM   1825  CZ2 TRP A 228      15.215  53.152  -5.554  1.00 37.27           C  
ATOM   1826  CZ3 TRP A 228      14.043  54.159  -3.678  1.00 36.40           C  
ATOM   1827  CH2 TRP A 228      15.144  53.460  -4.213  1.00 36.41           C  
ATOM   1828  N   ARG A 229       7.524  55.126  -5.837  1.00 38.55           N  
ATOM   1829  CA  ARG A 229       6.476  55.727  -4.994  1.00 38.54           C  
ATOM   1830  C   ARG A 229       6.287  54.965  -3.705  1.00 38.34           C  
ATOM   1831  O   ARG A 229       6.322  55.551  -2.629  1.00 37.75           O  
ATOM   1832  CB  ARG A 229       5.119  55.791  -5.712  1.00 38.40           C  
ATOM   1833  CG  ARG A 229       5.011  56.870  -6.758  1.00 39.68           C  
ATOM   1834  CD  ARG A 229       3.590  56.943  -7.327  1.00 41.26           C  
ATOM   1835  NE  ARG A 229       3.502  57.894  -8.436  1.00 41.03           N  
ATOM   1836  CZ  ARG A 229       3.092  59.152  -8.323  1.00 42.21           C  
ATOM   1837  NH1 ARG A 229       3.052  59.928  -9.394  1.00 42.08           N  
ATOM   1838  NH2 ARG A 229       2.711  59.637  -7.149  1.00 42.58           N  
ATOM   1839  N   GLU A 230       6.089  53.652  -3.829  1.00 38.30           N  
ATOM   1840  CA  GLU A 230       5.911  52.782  -2.671  1.00 38.40           C  
ATOM   1841  C   GLU A 230       7.215  52.612  -1.880  1.00 36.98           C  
ATOM   1842  O   GLU A 230       7.190  52.461  -0.659  1.00 36.25           O  
ATOM   1843  CB  GLU A 230       5.368  51.411  -3.107  1.00 39.27           C  
ATOM   1844  CG  GLU A 230       4.717  50.603  -1.964  1.00 43.32           C  
ATOM   1845  CD  GLU A 230       3.353  51.147  -1.542  1.00 49.07           C  
ATOM   1846  OE1 GLU A 230       2.386  51.059  -2.338  1.00 52.17           O  
ATOM   1847  OE2 GLU A 230       3.235  51.650  -0.403  1.00 51.50           O  
ATOM   1848  N   ARG A 231       8.354  52.631  -2.566  1.00 36.03           N  
ATOM   1849  CA  ARG A 231       9.628  52.471  -1.854  1.00 35.43           C  
ATOM   1850  C   ARG A 231       9.840  53.667  -0.930  1.00 34.37           C  
ATOM   1851  O   ARG A 231      10.171  53.491   0.241  1.00 35.20           O  
ATOM   1852  CB  ARG A 231      10.800  52.283  -2.810  1.00 35.35           C  
ATOM   1853  CG  ARG A 231      10.770  50.948  -3.581  1.00 36.07           C  
ATOM   1854  CD  ARG A 231      11.910  50.866  -4.595  1.00 35.87           C  
ATOM   1855  NE  ARG A 231      13.170  50.540  -3.937  1.00 36.94           N  
ATOM   1856  CZ  ARG A 231      14.266  50.105  -4.549  1.00 36.85           C  
ATOM   1857  NH1 ARG A 231      15.354  49.847  -3.824  1.00 37.03           N  
ATOM   1858  NH2 ARG A 231      14.290  49.929  -5.870  1.00 34.99           N  
ATOM   1859  N   ILE A 232       9.603  54.868  -1.454  1.00 33.86           N  
ATOM   1860  CA  ILE A 232       9.711  56.108  -0.681  1.00 33.50           C  
ATOM   1861  C   ILE A 232       8.752  56.109   0.518  1.00 33.83           C  
ATOM   1862  O   ILE A 232       9.147  56.472   1.636  1.00 32.94           O  
ATOM   1863  CB  ILE A 232       9.524  57.356  -1.584  1.00 33.21           C  
ATOM   1864  CG1 ILE A 232      10.740  57.499  -2.508  1.00 33.87           C  
ATOM   1865  CG2 ILE A 232       9.329  58.614  -0.749  1.00 34.12           C  
ATOM   1866  CD1 ILE A 232      10.548  58.438  -3.655  1.00 35.63           C  
ATOM   1867  N   ALA A 233       7.510  55.657   0.285  1.00 34.14           N  
ATOM   1868  CA  ALA A 233       6.498  55.534   1.344  1.00 35.23           C  
ATOM   1869  C   ALA A 233       6.965  54.679   2.528  1.00 35.92           C  
ATOM   1870  O   ALA A 233       6.668  54.992   3.669  1.00 36.42           O  
ATOM   1871  CB  ALA A 233       5.169  54.979   0.763  1.00 35.67           C  
ATOM   1872  N   ASN A 234       7.737  53.633   2.249  1.00 36.82           N  
ATOM   1873  CA  ASN A 234       8.175  52.675   3.275  1.00 37.67           C  
ATOM   1874  C   ASN A 234       9.602  52.928   3.819  1.00 37.53           C  
ATOM   1875  O   ASN A 234      10.121  52.166   4.630  1.00 38.09           O  
ATOM   1876  CB  ASN A 234       8.019  51.246   2.728  1.00 38.03           C  
ATOM   1877  CG  ASN A 234       6.543  50.859   2.494  1.00 40.39           C  
ATOM   1878  OD1 ASN A 234       5.688  51.032   3.380  1.00 42.72           O  
ATOM   1879  ND2 ASN A 234       6.246  50.330   1.307  1.00 40.71           N  
ATOM   1880  N   THR A 235      10.229  54.008   3.365  1.00 36.91           N  
ATOM   1881  CA  THR A 235      11.555  54.384   3.838  1.00 36.08           C  
ATOM   1882  C   THR A 235      11.423  55.220   5.093  1.00 35.29           C  
ATOM   1883  O   THR A 235      10.618  56.144   5.140  1.00 35.82           O  
ATOM   1884  CB  THR A 235      12.330  55.191   2.757  1.00 36.06           C  
ATOM   1885  OG1 THR A 235      12.436  54.407   1.568  1.00 35.86           O  
ATOM   1886  CG2 THR A 235      13.723  55.555   3.241  1.00 34.64           C  
ATOM   1887  N   SER A 236      12.219  54.921   6.111  1.00 34.22           N  
ATOM   1888  CA  SER A 236      12.127  55.708   7.329  1.00 34.30           C  
ATOM   1889  C   SER A 236      13.088  56.894   7.348  1.00 33.25           C  
ATOM   1890  O   SER A 236      12.869  57.854   8.093  1.00 33.24           O  
ATOM   1891  CB  SER A 236      12.266  54.832   8.583  1.00 35.32           C  
ATOM   1892  OG  SER A 236      13.486  54.111   8.587  1.00 37.33           O  
ATOM   1893  N   VAL A 237      14.147  56.840   6.542  1.00 31.69           N  
ATOM   1894  CA  VAL A 237      15.075  57.959   6.457  1.00 31.21           C  
ATOM   1895  C   VAL A 237      15.481  58.211   5.015  1.00 30.45           C  
ATOM   1896  O   VAL A 237      16.095  57.363   4.369  1.00 29.76           O  
ATOM   1897  CB  VAL A 237      16.367  57.777   7.311  1.00 30.86           C  
ATOM   1898  CG1 VAL A 237      17.231  59.030   7.207  1.00 30.95           C  
ATOM   1899  CG2 VAL A 237      16.042  57.495   8.770  1.00 31.22           C  
ATOM   1900  N   ILE A 238      15.117  59.391   4.534  1.00 30.42           N  
ATOM   1901  CA  ILE A 238      15.406  59.823   3.179  1.00 29.47           C  
ATOM   1902  C   ILE A 238      16.538  60.852   3.269  1.00 28.80           C  
ATOM   1903  O   ILE A 238      16.475  61.762   4.085  1.00 28.60           O  
ATOM   1904  CB  ILE A 238      14.154  60.489   2.549  1.00 29.55           C  
ATOM   1905  CG1 ILE A 238      13.054  59.460   2.208  1.00 30.28           C  
ATOM   1906  CG2 ILE A 238      14.545  61.376   1.341  1.00 29.63           C  
ATOM   1907  CD1 ILE A 238      13.233  58.709   0.886  1.00 31.94           C  
ATOM   1908  N   PHE A 239      17.588  60.670   2.471  1.00 27.93           N  
ATOM   1909  CA  PHE A 239      18.557  61.733   2.242  1.00 27.67           C  
ATOM   1910  C   PHE A 239      18.405  62.150   0.795  1.00 26.79           C  
ATOM   1911  O   PHE A 239      18.375  61.301  -0.082  1.00 27.66           O  
ATOM   1912  CB  PHE A 239      20.007  61.266   2.490  1.00 26.70           C  
ATOM   1913  CG  PHE A 239      21.035  62.343   2.198  1.00 26.89           C  
ATOM   1914  CD1 PHE A 239      21.310  63.320   3.143  1.00 25.40           C  
ATOM   1915  CD2 PHE A 239      21.674  62.415   0.956  1.00 26.63           C  
ATOM   1916  CE1 PHE A 239      22.203  64.325   2.878  1.00 26.76           C  
ATOM   1917  CE2 PHE A 239      22.577  63.430   0.678  1.00 27.41           C  
ATOM   1918  CZ  PHE A 239      22.850  64.386   1.640  1.00 26.65           C  
ATOM   1919  N   VAL A 240      18.317  63.454   0.545  1.00 27.52           N  
ATOM   1920  CA  VAL A 240      18.164  63.970  -0.817  1.00 26.31           C  
ATOM   1921  C   VAL A 240      18.838  65.347  -1.011  1.00 26.45           C  
ATOM   1922  O   VAL A 240      18.502  66.336  -0.343  1.00 25.36           O  
ATOM   1923  CB  VAL A 240      16.669  63.959  -1.236  1.00 26.81           C  
ATOM   1924  CG1 VAL A 240      15.849  64.982  -0.439  1.00 25.49           C  
ATOM   1925  CG2 VAL A 240      16.516  64.135  -2.723  1.00 26.69           C  
ATOM   1926  N   ASN A 241      19.814  65.399  -1.911  1.00 25.54           N  
ATOM   1927  CA  ASN A 241      20.579  66.632  -2.114  1.00 26.89           C  
ATOM   1928  C   ASN A 241      19.874  67.370  -3.232  1.00 27.73           C  
ATOM   1929  O   ASN A 241      20.292  67.287  -4.377  1.00 27.91           O  
ATOM   1930  CB  ASN A 241      22.049  66.330  -2.492  1.00 26.25           C  
ATOM   1931  CG  ASN A 241      22.929  67.608  -2.554  1.00 28.04           C  
ATOM   1932  OD1 ASN A 241      22.434  68.750  -2.537  1.00 29.41           O  
ATOM   1933  ND2 ASN A 241      24.220  67.408  -2.657  1.00 27.42           N  
ATOM   1934  N   ASN A 242      18.791  68.074  -2.898  1.00 28.80           N  
ATOM   1935  CA  ASN A 242      17.863  68.559  -3.922  1.00 30.51           C  
ATOM   1936  C   ASN A 242      18.105  70.003  -4.337  1.00 32.00           C  
ATOM   1937  O   ASN A 242      17.339  70.551  -5.119  1.00 32.85           O  
ATOM   1938  CB  ASN A 242      16.429  68.410  -3.430  1.00 29.60           C  
ATOM   1939  CG  ASN A 242      16.189  69.170  -2.148  1.00 29.21           C  
ATOM   1940  OD1 ASN A 242      17.053  69.195  -1.260  1.00 26.58           O  
ATOM   1941  ND2 ASN A 242      15.031  69.819  -2.047  1.00 27.18           N  
ATOM   1942  N   PHE A 243      19.182  70.609  -3.835  1.00 33.69           N  
ATOM   1943  CA  PHE A 243      19.422  72.027  -4.050  1.00 35.04           C  
ATOM   1944  C   PHE A 243      19.158  72.509  -5.475  1.00 35.27           C  
ATOM   1945  O   PHE A 243      18.605  73.610  -5.680  1.00 35.84           O  
ATOM   1946  CB  PHE A 243      20.849  72.397  -3.664  1.00 35.65           C  
ATOM   1947  CG  PHE A 243      21.085  73.873  -3.601  1.00 38.07           C  
ATOM   1948  CD1 PHE A 243      20.704  74.600  -2.483  1.00 38.24           C  
ATOM   1949  CD2 PHE A 243      21.706  74.538  -4.664  1.00 40.94           C  
ATOM   1950  CE1 PHE A 243      20.927  75.977  -2.420  1.00 40.67           C  
ATOM   1951  CE2 PHE A 243      21.933  75.904  -4.612  1.00 41.03           C  
ATOM   1952  CZ  PHE A 243      21.545  76.627  -3.486  1.00 42.58           C  
ATOM   1953  N   ALA A 244      19.579  71.717  -6.453  1.00 34.83           N  
ATOM   1954  CA  ALA A 244      19.417  72.106  -7.855  1.00 35.22           C  
ATOM   1955  C   ALA A 244      18.282  71.352  -8.576  1.00 35.10           C  
ATOM   1956  O   ALA A 244      18.190  71.413  -9.802  1.00 36.03           O  
ATOM   1957  CB  ALA A 244      20.732  71.924  -8.601  1.00 35.12           C  
ATOM   1958  N   PHE A 245      17.425  70.644  -7.842  1.00 34.72           N  
ATOM   1959  CA  PHE A 245      16.329  69.897  -8.498  1.00 34.50           C  
ATOM   1960  C   PHE A 245      15.294  70.814  -9.172  1.00 34.77           C  
ATOM   1961  O   PHE A 245      14.807  70.507 -10.254  1.00 34.53           O  
ATOM   1962  CB  PHE A 245      15.620  68.930  -7.523  1.00 34.07           C  
ATOM   1963  CG  PHE A 245      16.407  67.695  -7.177  1.00 33.07           C  
ATOM   1964  CD1 PHE A 245      17.643  67.421  -7.777  1.00 31.72           C  
ATOM   1965  CD2 PHE A 245      15.881  66.767  -6.278  1.00 30.83           C  
ATOM   1966  CE1 PHE A 245      18.355  66.251  -7.459  1.00 29.91           C  
ATOM   1967  CE2 PHE A 245      16.586  65.618  -5.942  1.00 30.78           C  
ATOM   1968  CZ  PHE A 245      17.822  65.351  -6.532  1.00 31.80           C  
ATOM   1969  N   GLY A 246      14.969  71.938  -8.533  1.00 35.50           N  
ATOM   1970  CA  GLY A 246      13.918  72.851  -9.026  1.00 36.46           C  
ATOM   1971  C   GLY A 246      12.546  72.601  -8.405  1.00 37.13           C  
ATOM   1972  O   GLY A 246      12.320  71.551  -7.795  1.00 36.79           O  
ATOM   1973  N   PRO A 247      11.600  73.551  -8.597  1.00 37.81           N  
ATOM   1974  CA  PRO A 247      10.273  73.442  -7.988  1.00 37.79           C  
ATOM   1975  C   PRO A 247       9.443  72.256  -8.478  1.00 37.76           C  
ATOM   1976  O   PRO A 247       8.692  71.698  -7.695  1.00 38.11           O  
ATOM   1977  CB  PRO A 247       9.595  74.773  -8.357  1.00 37.63           C  
ATOM   1978  CG  PRO A 247      10.302  75.228  -9.589  1.00 38.33           C  
ATOM   1979  CD  PRO A 247      11.733  74.778  -9.406  1.00 37.85           C  
ATOM   1980  N   GLU A 248       9.603  71.867  -9.740  1.00 37.90           N  
ATOM   1981  CA  GLU A 248       8.845  70.765 -10.332  1.00 37.56           C  
ATOM   1982  C   GLU A 248       9.190  69.421  -9.720  1.00 36.93           C  
ATOM   1983  O   GLU A 248       8.290  68.647  -9.353  1.00 36.61           O  
ATOM   1984  CB  GLU A 248       9.069  70.711 -11.845  1.00 38.41           C  
ATOM   1985  CG  GLU A 248       8.281  69.611 -12.556  1.00 42.07           C  
ATOM   1986  CD  GLU A 248       6.786  69.881 -12.577  1.00 46.81           C  
ATOM   1987  OE1 GLU A 248       6.385  70.982 -13.036  1.00 49.66           O  
ATOM   1988  OE2 GLU A 248       6.017  68.996 -12.130  1.00 48.06           O  
ATOM   1989  N   VAL A 249      10.488  69.137  -9.610  1.00 35.07           N  
ATOM   1990  CA  VAL A 249      10.933  67.893  -8.990  1.00 34.17           C  
ATOM   1991  C   VAL A 249      10.592  67.901  -7.497  1.00 33.73           C  
ATOM   1992  O   VAL A 249      10.029  66.937  -7.002  1.00 33.40           O  
ATOM   1993  CB  VAL A 249      12.435  67.573  -9.311  1.00 33.69           C  
ATOM   1994  CG1 VAL A 249      12.952  66.339  -8.552  1.00 33.32           C  
ATOM   1995  CG2 VAL A 249      12.624  67.378 -10.821  1.00 34.50           C  
ATOM   1996  N   ASP A 250      10.884  68.995  -6.790  1.00 34.47           N  
ATOM   1997  CA  ASP A 250      10.546  69.066  -5.366  1.00 34.41           C  
ATOM   1998  C   ASP A 250       9.047  68.831  -5.136  1.00 35.03           C  
ATOM   1999  O   ASP A 250       8.672  68.094  -4.218  1.00 34.16           O  
ATOM   2000  CB  ASP A 250      10.984  70.385  -4.710  1.00 34.65           C  
ATOM   2001  CG  ASP A 250      12.511  70.495  -4.511  1.00 34.08           C  
ATOM   2002  OD1 ASP A 250      13.239  69.482  -4.588  1.00 33.29           O  
ATOM   2003  OD2 ASP A 250      12.987  71.623  -4.296  1.00 34.20           O  
ATOM   2004  N   HIS A 251       8.202  69.464  -5.961  1.00 35.56           N  
ATOM   2005  CA  HIS A 251       6.760  69.293  -5.841  1.00 36.05           C  
ATOM   2006  C   HIS A 251       6.411  67.813  -5.953  1.00 35.90           C  
ATOM   2007  O   HIS A 251       5.654  67.299  -5.138  1.00 35.77           O  
ATOM   2008  CB  HIS A 251       6.021  70.114  -6.896  1.00 36.52           C  
ATOM   2009  CG  HIS A 251       4.545  69.863  -6.933  1.00 39.10           C  
ATOM   2010  ND1 HIS A 251       3.651  70.557  -6.147  1.00 40.72           N  
ATOM   2011  CD2 HIS A 251       3.808  68.995  -7.666  1.00 40.94           C  
ATOM   2012  CE1 HIS A 251       2.426  70.131  -6.394  1.00 42.11           C  
ATOM   2013  NE2 HIS A 251       2.495  69.182  -7.314  1.00 43.02           N  
ATOM   2014  N   GLN A 252       6.978  67.120  -6.946  1.00 35.58           N  
ATOM   2015  CA  GLN A 252       6.699  65.695  -7.099  1.00 35.60           C  
ATOM   2016  C   GLN A 252       7.199  64.880  -5.903  1.00 35.05           C  
ATOM   2017  O   GLN A 252       6.537  63.923  -5.484  1.00 34.76           O  
ATOM   2018  CB  GLN A 252       7.269  65.151  -8.411  1.00 36.68           C  
ATOM   2019  CG  GLN A 252       6.723  65.870  -9.657  1.00 38.37           C  
ATOM   2020  CD  GLN A 252       7.515  65.558 -10.903  1.00 40.60           C  
ATOM   2021  OE1 GLN A 252       8.306  66.379 -11.368  1.00 44.42           O  
ATOM   2022  NE2 GLN A 252       7.306  64.373 -11.460  1.00 41.79           N  
ATOM   2023  N   LEU A 253       8.344  65.266  -5.333  1.00 33.61           N  
ATOM   2024  CA  LEU A 253       8.827  64.592  -4.117  1.00 32.84           C  
ATOM   2025  C   LEU A 253       7.897  64.793  -2.912  1.00 32.24           C  
ATOM   2026  O   LEU A 253       7.636  63.835  -2.193  1.00 31.22           O  
ATOM   2027  CB  LEU A 253      10.281  64.974  -3.771  1.00 32.22           C  
ATOM   2028  CG  LEU A 253      11.357  64.313  -4.645  1.00 31.10           C  
ATOM   2029  CD1 LEU A 253      12.645  65.075  -4.568  1.00 29.95           C  
ATOM   2030  CD2 LEU A 253      11.582  62.848  -4.251  1.00 30.34           C  
ATOM   2031  N   LYS A 254       7.408  66.023  -2.713  1.00 32.09           N  
ATOM   2032  CA  LYS A 254       6.432  66.337  -1.649  1.00 33.57           C  
ATOM   2033  C   LYS A 254       5.281  65.325  -1.669  1.00 33.50           C  
ATOM   2034  O   LYS A 254       4.862  64.801  -0.633  1.00 33.33           O  
ATOM   2035  CB  LYS A 254       5.847  67.744  -1.839  1.00 33.62           C  
ATOM   2036  CG  LYS A 254       6.771  68.891  -1.448  1.00 34.41           C  
ATOM   2037  CD  LYS A 254       6.158  70.230  -1.821  1.00 34.70           C  
ATOM   2038  CE  LYS A 254       7.246  71.252  -2.051  1.00 36.38           C  
ATOM   2039  NZ  LYS A 254       6.849  72.617  -1.593  1.00 39.64           N  
ATOM   2040  N   GLU A 255       4.803  65.054  -2.878  1.00 34.03           N  
ATOM   2041  CA  GLU A 255       3.686  64.144  -3.108  1.00 34.62           C  
ATOM   2042  C   GLU A 255       4.033  62.747  -2.637  1.00 34.33           C  
ATOM   2043  O   GLU A 255       3.186  62.038  -2.068  1.00 34.65           O  
ATOM   2044  CB  GLU A 255       3.356  64.151  -4.594  1.00 34.87           C  
ATOM   2045  CG  GLU A 255       2.587  62.959  -5.100  1.00 39.21           C  
ATOM   2046  CD  GLU A 255       1.860  63.279  -6.383  1.00 42.17           C  
ATOM   2047  OE1 GLU A 255       1.772  62.386  -7.246  1.00 45.64           O  
ATOM   2048  OE2 GLU A 255       1.394  64.430  -6.531  1.00 44.33           O  
ATOM   2049  N   ARG A 256       5.275  62.336  -2.884  1.00 33.36           N  
ATOM   2050  CA  ARG A 256       5.707  61.025  -2.449  1.00 33.13           C  
ATOM   2051  C   ARG A 256       6.002  60.976  -0.964  1.00 32.66           C  
ATOM   2052  O   ARG A 256       5.774  59.947  -0.336  1.00 32.52           O  
ATOM   2053  CB  ARG A 256       6.878  60.508  -3.292  1.00 33.53           C  
ATOM   2054  CG  ARG A 256       6.403  60.059  -4.679  1.00 34.84           C  
ATOM   2055  CD  ARG A 256       7.346  60.616  -5.683  1.00 37.12           C  
ATOM   2056  NE  ARG A 256       7.046  60.214  -7.055  1.00 38.85           N  
ATOM   2057  CZ  ARG A 256       6.392  60.973  -7.931  1.00 36.10           C  
ATOM   2058  NH1 ARG A 256       5.921  62.162  -7.574  1.00 35.92           N  
ATOM   2059  NH2 ARG A 256       6.204  60.535  -9.157  1.00 35.67           N  
ATOM   2060  N   PHE A 257       6.476  62.083  -0.394  1.00 32.41           N  
ATOM   2061  CA  PHE A 257       6.678  62.145   1.058  1.00 32.90           C  
ATOM   2062  C   PHE A 257       5.361  62.060   1.849  1.00 33.56           C  
ATOM   2063  O   PHE A 257       5.314  61.500   2.945  1.00 32.92           O  
ATOM   2064  CB  PHE A 257       7.467  63.385   1.459  1.00 32.35           C  
ATOM   2065  CG  PHE A 257       8.848  63.462   0.836  1.00 31.54           C  
ATOM   2066  CD1 PHE A 257       9.518  62.313   0.429  1.00 32.13           C  
ATOM   2067  CD2 PHE A 257       9.467  64.688   0.665  1.00 31.66           C  
ATOM   2068  CE1 PHE A 257      10.807  62.385  -0.147  1.00 32.21           C  
ATOM   2069  CE2 PHE A 257      10.744  64.781   0.109  1.00 30.58           C  
ATOM   2070  CZ  PHE A 257      11.414  63.635  -0.313  1.00 29.79           C  
ATOM   2071  N   ALA A 258       4.291  62.589   1.260  1.00 34.25           N  
ATOM   2072  CA  ALA A 258       2.997  62.663   1.934  1.00 35.11           C  
ATOM   2073  C   ALA A 258       2.428  61.279   2.249  1.00 35.65           C  
ATOM   2074  O   ALA A 258       1.411  61.169   2.936  1.00 36.69           O  
ATOM   2075  CB  ALA A 258       2.002  63.517   1.094  1.00 35.29           C  
ATOM   2076  N   ASN A 259       3.100  60.229   1.767  1.00 35.70           N  
ATOM   2077  CA  ASN A 259       2.720  58.840   2.014  1.00 36.03           C  
ATOM   2078  C   ASN A 259       3.614  58.108   3.019  1.00 36.29           C  
ATOM   2079  O   ASN A 259       3.447  56.895   3.256  1.00 35.95           O  
ATOM   2080  CB  ASN A 259       2.669  58.060   0.694  1.00 36.15           C  
ATOM   2081  CG  ASN A 259       1.362  58.279  -0.064  1.00 37.78           C  
ATOM   2082  OD1 ASN A 259       0.314  58.506   0.535  1.00 39.25           O  
ATOM   2083  ND2 ASN A 259       1.425  58.205  -1.387  1.00 38.73           N  
ATOM   2084  N   MET A 260       4.566  58.851   3.586  1.00 35.86           N  
ATOM   2085  CA  MET A 260       5.522  58.316   4.543  1.00 36.79           C  
ATOM   2086  C   MET A 260       4.888  58.167   5.909  1.00 37.14           C  
ATOM   2087  O   MET A 260       3.942  58.893   6.259  1.00 36.70           O  
ATOM   2088  CB  MET A 260       6.765  59.226   4.656  1.00 36.13           C  
ATOM   2089  CG  MET A 260       7.716  59.128   3.465  1.00 36.85           C  
ATOM   2090  SD  MET A 260       9.112  60.271   3.603  1.00 35.82           S  
ATOM   2091  CE  MET A 260      10.046  59.505   4.931  1.00 35.15           C  
ATOM   2092  N   LYS A 261       5.440  57.224   6.666  1.00 37.77           N  
ATOM   2093  CA  LYS A 261       4.990  56.886   8.005  1.00 38.55           C  
ATOM   2094  C   LYS A 261       5.341  57.961   9.006  1.00 38.74           C  
ATOM   2095  O   LYS A 261       6.270  58.759   8.784  1.00 38.81           O  
ATOM   2096  CB  LYS A 261       5.588  55.540   8.428  1.00 38.87           C  
ATOM   2097  CG  LYS A 261       5.105  54.382   7.580  1.00 41.31           C  
ATOM   2098  CD  LYS A 261       6.085  53.214   7.635  1.00 44.17           C  
ATOM   2099  CE  LYS A 261       5.788  52.184   6.559  1.00 46.17           C  
ATOM   2100  NZ  LYS A 261       6.624  50.952   6.739  1.00 46.43           N  
ATOM   2101  N   GLU A 262       4.552  58.006  10.079  1.00 38.34           N  
ATOM   2102  CA  GLU A 262       4.820  58.831  11.251  1.00 38.74           C  
ATOM   2103  C   GLU A 262       6.256  58.656  11.734  1.00 37.98           C  
ATOM   2104  O   GLU A 262       6.740  57.547  11.841  1.00 37.96           O  
ATOM   2105  CB  GLU A 262       3.878  58.417  12.384  1.00 38.99           C  
ATOM   2106  CG  GLU A 262       3.504  59.552  13.303  1.00 40.55           C  
ATOM   2107  CD  GLU A 262       2.504  60.525  12.665  1.00 41.84           C  
ATOM   2108  OE1 GLU A 262       2.369  61.648  13.181  1.00 41.33           O  
ATOM   2109  OE2 GLU A 262       1.859  60.163  11.650  1.00 42.58           O  
ATOM   2110  N   GLY A 263       6.930  59.762  12.031  1.00 38.21           N  
ATOM   2111  CA  GLY A 263       8.304  59.706  12.518  1.00 37.61           C  
ATOM   2112  C   GLY A 263       9.363  59.504  11.438  1.00 37.25           C  
ATOM   2113  O   GLY A 263      10.574  59.500  11.743  1.00 37.23           O  
ATOM   2114  N   GLY A 264       8.931  59.333  10.186  1.00 35.51           N  
ATOM   2115  CA  GLY A 264       9.864  59.258   9.071  1.00 34.16           C  
ATOM   2116  C   GLY A 264      10.656  60.553   8.991  1.00 34.03           C  
ATOM   2117  O   GLY A 264      10.181  61.614   9.434  1.00 32.69           O  
ATOM   2118  N   ARG A 265      11.873  60.474   8.449  1.00 33.12           N  
ATOM   2119  CA  ARG A 265      12.727  61.656   8.393  1.00 32.42           C  
ATOM   2120  C   ARG A 265      13.264  61.871   7.005  1.00 31.36           C  
ATOM   2121  O   ARG A 265      13.494  60.911   6.284  1.00 31.26           O  
ATOM   2122  CB  ARG A 265      13.859  61.572   9.424  1.00 33.34           C  
ATOM   2123  CG  ARG A 265      13.359  61.710  10.867  1.00 34.96           C  
ATOM   2124  CD  ARG A 265      14.349  61.137  11.878  1.00 36.87           C  
ATOM   2125  NE  ARG A 265      14.514  59.687  11.755  1.00 37.07           N  
ATOM   2126  CZ  ARG A 265      15.342  58.965  12.519  1.00 37.98           C  
ATOM   2127  NH1 ARG A 265      15.430  57.650  12.351  1.00 36.41           N  
ATOM   2128  NH2 ARG A 265      16.077  59.557  13.462  1.00 37.18           N  
ATOM   2129  N   ILE A 266      13.412  63.146   6.638  1.00 30.55           N  
ATOM   2130  CA  ILE A 266      13.982  63.562   5.372  1.00 29.47           C  
ATOM   2131  C   ILE A 266      15.082  64.609   5.659  1.00 29.41           C  
ATOM   2132  O   ILE A 266      14.824  65.653   6.294  1.00 28.72           O  
ATOM   2133  CB  ILE A 266      12.903  64.176   4.446  1.00 29.64           C  
ATOM   2134  CG1 ILE A 266      11.767  63.173   4.162  1.00 30.78           C  
ATOM   2135  CG2 ILE A 266      13.520  64.672   3.136  1.00 28.50           C  
ATOM   2136  CD1 ILE A 266      10.403  63.790   4.125  1.00 32.02           C  
ATOM   2137  N   VAL A 267      16.298  64.323   5.194  1.00 28.57           N  
ATOM   2138  CA  VAL A 267      17.407  65.280   5.258  1.00 28.49           C  
ATOM   2139  C   VAL A 267      17.652  65.827   3.871  1.00 28.09           C  
ATOM   2140  O   VAL A 267      17.893  65.063   2.950  1.00 29.56           O  
ATOM   2141  CB  VAL A 267      18.725  64.615   5.822  1.00 28.94           C  
ATOM   2142  CG1 VAL A 267      19.903  65.593   5.751  1.00 27.26           C  
ATOM   2143  CG2 VAL A 267      18.499  64.180   7.264  1.00 29.63           C  
ATOM   2144  N   SER A 268      17.604  67.143   3.697  1.00 28.69           N  
ATOM   2145  CA  SER A 268      17.790  67.722   2.358  1.00 28.07           C  
ATOM   2146  C   SER A 268      18.576  69.030   2.372  1.00 28.79           C  
ATOM   2147  O   SER A 268      18.774  69.623   3.432  1.00 30.17           O  
ATOM   2148  CB  SER A 268      16.428  67.930   1.680  1.00 28.18           C  
ATOM   2149  OG  SER A 268      15.782  69.072   2.194  1.00 24.63           O  
ATOM   2150  N   SER A 269      19.030  69.481   1.204  1.00 29.51           N  
ATOM   2151  CA  SER A 269      19.780  70.754   1.099  1.00 30.71           C  
ATOM   2152  C   SER A 269      18.908  71.970   0.759  1.00 30.71           C  
ATOM   2153  O   SER A 269      19.423  73.082   0.606  1.00 30.74           O  
ATOM   2154  CB  SER A 269      20.937  70.651   0.094  1.00 30.20           C  
ATOM   2155  OG  SER A 269      20.528  70.003  -1.093  1.00 32.32           O  
ATOM   2156  N   LYS A 270      17.603  71.736   0.613  1.00 31.59           N  
ATOM   2157  CA  LYS A 270      16.596  72.798   0.417  1.00 32.21           C  
ATOM   2158  C   LYS A 270      15.308  72.310   1.078  1.00 31.88           C  
ATOM   2159  O   LYS A 270      14.834  71.217   0.755  1.00 31.48           O  
ATOM   2160  CB  LYS A 270      16.348  73.096  -1.068  1.00 32.42           C  
ATOM   2161  CG  LYS A 270      15.353  74.269  -1.324  1.00 35.76           C  
ATOM   2162  CD  LYS A 270      14.967  74.461  -2.804  1.00 38.75           C  
ATOM   2163  CE  LYS A 270      16.162  74.918  -3.645  1.00 42.30           C  
ATOM   2164  NZ  LYS A 270      15.871  74.955  -5.123  1.00 43.69           N  
ATOM   2165  N   PRO A 271      14.745  73.106   2.014  1.00 31.80           N  
ATOM   2166  CA  PRO A 271      13.578  72.646   2.764  1.00 32.46           C  
ATOM   2167  C   PRO A 271      12.401  72.325   1.846  1.00 32.77           C  
ATOM   2168  O   PRO A 271      12.233  72.978   0.810  1.00 33.30           O  
ATOM   2169  CB  PRO A 271      13.210  73.856   3.636  1.00 32.31           C  
ATOM   2170  CG  PRO A 271      14.394  74.736   3.613  1.00 32.08           C  
ATOM   2171  CD  PRO A 271      15.087  74.504   2.331  1.00 31.61           C  
ATOM   2172  N   PHE A 272      11.600  71.336   2.224  1.00 33.01           N  
ATOM   2173  CA  PHE A 272      10.390  71.009   1.476  1.00 33.74           C  
ATOM   2174  C   PHE A 272       9.158  71.747   2.028  1.00 34.84           C  
ATOM   2175  O   PHE A 272       8.099  71.730   1.410  1.00 34.97           O  
ATOM   2176  CB  PHE A 272      10.155  69.495   1.439  1.00 32.66           C  
ATOM   2177  CG  PHE A 272      11.094  68.764   0.522  1.00 32.18           C  
ATOM   2178  CD1 PHE A 272      10.920  68.828  -0.862  1.00 29.63           C  
ATOM   2179  CD2 PHE A 272      12.153  68.018   1.039  1.00 30.66           C  
ATOM   2180  CE1 PHE A 272      11.788  68.156  -1.724  1.00 31.18           C  
ATOM   2181  CE2 PHE A 272      13.042  67.329   0.182  1.00 31.73           C  
ATOM   2182  CZ  PHE A 272      12.859  67.411  -1.207  1.00 31.82           C  
ATOM   2183  N   ALA A 273       9.317  72.377   3.189  1.00 36.01           N  
ATOM   2184  CA  ALA A 273       8.295  73.223   3.797  1.00 37.07           C  
ATOM   2185  C   ALA A 273       8.994  74.401   4.488  1.00 37.98           C  
ATOM   2186  O   ALA A 273      10.086  74.227   5.038  1.00 37.69           O  
ATOM   2187  CB  ALA A 273       7.493  72.411   4.802  1.00 37.21           C  
ATOM   2188  N   PRO A 274       8.366  75.601   4.487  1.00 38.96           N  
ATOM   2189  CA  PRO A 274       9.070  76.729   5.100  1.00 39.65           C  
ATOM   2190  C   PRO A 274       9.268  76.499   6.597  1.00 40.60           C  
ATOM   2191  O   PRO A 274       8.427  75.869   7.243  1.00 39.87           O  
ATOM   2192  CB  PRO A 274       8.155  77.934   4.812  1.00 39.59           C  
ATOM   2193  CG  PRO A 274       6.804  77.355   4.614  1.00 39.52           C  
ATOM   2194  CD  PRO A 274       6.987  75.952   4.089  1.00 38.52           C  
ATOM   2195  N   LEU A 275      10.401  76.968   7.121  1.00 41.41           N  
ATOM   2196  CA  LEU A 275      10.753  76.754   8.520  1.00 43.11           C  
ATOM   2197  C   LEU A 275       9.713  77.333   9.486  1.00 44.12           C  
ATOM   2198  O   LEU A 275       9.459  76.771  10.566  1.00 44.08           O  
ATOM   2199  CB  LEU A 275      12.159  77.303   8.809  1.00 43.17           C  
ATOM   2200  CG  LEU A 275      13.327  76.387   8.402  1.00 44.23           C  
ATOM   2201  CD1 LEU A 275      14.652  77.147   8.339  1.00 43.51           C  
ATOM   2202  CD2 LEU A 275      13.436  75.225   9.352  1.00 42.77           C  
ATOM   2203  N   ASN A 276       9.104  78.440   9.070  1.00 45.36           N  
ATOM   2204  CA  ASN A 276       8.086  79.135   9.859  1.00 47.34           C  
ATOM   2205  C   ASN A 276       6.640  78.799   9.452  1.00 47.85           C  
ATOM   2206  O   ASN A 276       5.765  79.667   9.477  1.00 47.90           O  
ATOM   2207  CB  ASN A 276       8.301  80.648   9.742  1.00 47.51           C  
ATOM   2208  CG  ASN A 276       7.984  81.179   8.351  1.00 49.14           C  
ATOM   2209  OD1 ASN A 276       7.858  80.417   7.387  1.00 51.71           O  
ATOM   2210  ND2 ASN A 276       7.848  82.490   8.245  1.00 50.16           N  
ATOM   2211  N   PHE A 277       6.392  77.549   9.074  1.00 48.59           N  
ATOM   2212  CA  PHE A 277       5.058  77.149   8.637  1.00 49.38           C  
ATOM   2213  C   PHE A 277       4.025  77.252   9.759  1.00 50.23           C  
ATOM   2214  O   PHE A 277       4.282  76.826  10.879  1.00 50.34           O  
ATOM   2215  CB  PHE A 277       5.076  75.735   8.061  1.00 49.14           C  
ATOM   2216  CG  PHE A 277       3.788  75.339   7.408  1.00 48.12           C  
ATOM   2217  CD1 PHE A 277       3.578  75.586   6.056  1.00 47.47           C  
ATOM   2218  CD2 PHE A 277       2.777  74.728   8.146  1.00 47.12           C  
ATOM   2219  CE1 PHE A 277       2.377  75.229   5.441  1.00 47.66           C  
ATOM   2220  CE2 PHE A 277       1.575  74.369   7.537  1.00 46.39           C  
ATOM   2221  CZ  PHE A 277       1.380  74.621   6.183  1.00 46.72           C  
ATOM   2222  N   ARG A 278       2.862  77.824   9.435  1.00 51.54           N  
ATOM   2223  CA  ARG A 278       1.711  77.890  10.344  1.00 52.45           C  
ATOM   2224  C   ARG A 278       0.441  77.472   9.587  1.00 52.84           C  
ATOM   2225  O   ARG A 278       0.117  78.057   8.544  1.00 52.64           O  
ATOM   2226  CB  ARG A 278       1.561  79.306  10.902  1.00 52.87           C  
ATOM   2227  CG  ARG A 278       0.862  79.382  12.247  1.00 54.87           C  
ATOM   2228  CD  ARG A 278       1.297  80.618  13.032  1.00 58.90           C  
ATOM   2229  NE  ARG A 278       0.975  80.484  14.457  1.00 61.02           N  
ATOM   2230  CZ  ARG A 278       0.805  81.499  15.301  1.00 62.08           C  
ATOM   2231  NH1 ARG A 278       0.919  82.756  14.886  1.00 62.89           N  
ATOM   2232  NH2 ARG A 278       0.510  81.255  16.570  1.00 63.09           N  
ATOM   2233  N   ILE A 279      -0.260  76.453  10.087  1.00 53.21           N  
ATOM   2234  CA  ILE A 279      -1.475  75.976   9.410  1.00 54.17           C  
ATOM   2235  C   ILE A 279      -2.585  77.027   9.473  1.00 53.99           C  
ATOM   2236  O   ILE A 279      -2.868  77.587  10.530  1.00 54.39           O  
ATOM   2237  CB  ILE A 279      -2.027  74.619   9.958  1.00 54.12           C  
ATOM   2238  CG1 ILE A 279      -0.980  73.512   9.895  1.00 55.09           C  
ATOM   2239  CG2 ILE A 279      -3.258  74.175   9.150  1.00 54.64           C  
ATOM   2240  CD1 ILE A 279      -1.535  72.132  10.198  1.00 56.49           C  
ATOM   2241  N   ASN A 280      -3.174  77.306   8.318  1.00 54.32           N  
ATOM   2242  CA  ASN A 280      -4.407  78.087   8.223  1.00 54.31           C  
ATOM   2243  C   ASN A 280      -5.333  77.457   7.177  1.00 54.23           C  
ATOM   2244  O   ASN A 280      -5.043  76.373   6.677  1.00 54.28           O  
ATOM   2245  CB  ASN A 280      -4.109  79.557   7.920  1.00 54.56           C  
ATOM   2246  CG  ASN A 280      -3.193  79.741   6.729  1.00 55.20           C  
ATOM   2247  OD1 ASN A 280      -3.478  79.280   5.621  1.00 57.38           O  
ATOM   2248  ND2 ASN A 280      -2.089  80.442   6.946  1.00 56.71           N  
ATOM   2249  N   SER A 281      -6.430  78.132   6.844  1.00 53.80           N  
ATOM   2250  CA  SER A 281      -7.468  77.542   5.999  1.00 53.38           C  
ATOM   2251  C   SER A 281      -7.158  77.577   4.500  1.00 53.14           C  
ATOM   2252  O   SER A 281      -7.911  77.019   3.702  1.00 53.26           O  
ATOM   2253  CB  SER A 281      -8.825  78.196   6.282  1.00 53.34           C  
ATOM   2254  OG  SER A 281      -8.720  79.608   6.198  1.00 53.51           O  
ATOM   2255  N   ARG A 282      -6.058  78.226   4.117  1.00 52.82           N  
ATOM   2256  CA  ARG A 282      -5.623  78.233   2.713  1.00 52.49           C  
ATOM   2257  C   ARG A 282      -4.495  77.238   2.430  1.00 51.62           C  
ATOM   2258  O   ARG A 282      -4.343  76.790   1.295  1.00 51.42           O  
ATOM   2259  CB  ARG A 282      -5.178  79.636   2.278  1.00 52.99           C  
ATOM   2260  CG  ARG A 282      -5.753  80.108   0.930  1.00 54.95           C  
ATOM   2261  CD  ARG A 282      -5.175  79.400  -0.316  1.00 57.64           C  
ATOM   2262  NE  ARG A 282      -5.942  79.756  -1.516  1.00 60.54           N  
ATOM   2263  CZ  ARG A 282      -5.687  79.339  -2.754  1.00 60.76           C  
ATOM   2264  NH1 ARG A 282      -6.463  79.746  -3.750  1.00 61.73           N  
ATOM   2265  NH2 ARG A 282      -4.669  78.523  -3.005  1.00 61.87           N  
ATOM   2266  N   ASN A 283      -3.699  76.905   3.450  1.00 50.64           N  
ATOM   2267  CA  ASN A 283      -2.541  76.019   3.260  1.00 49.16           C  
ATOM   2268  C   ASN A 283      -2.788  74.590   3.751  1.00 48.69           C  
ATOM   2269  O   ASN A 283      -1.859  73.774   3.856  1.00 47.82           O  
ATOM   2270  CB  ASN A 283      -1.262  76.633   3.863  1.00 49.47           C  
ATOM   2271  CG  ASN A 283      -1.316  76.779   5.378  1.00 48.89           C  
ATOM   2272  OD1 ASN A 283      -2.122  76.148   6.059  1.00 49.06           O  
ATOM   2273  ND2 ASN A 283      -0.435  77.609   5.912  1.00 49.53           N  
ATOM   2274  N   LEU A 284      -4.068  74.291   3.994  1.00 47.55           N  
ATOM   2275  CA  LEU A 284      -4.509  73.026   4.577  1.00 46.56           C  
ATOM   2276  C   LEU A 284      -3.986  71.763   3.895  1.00 45.56           C  
ATOM   2277  O   LEU A 284      -3.889  70.723   4.535  1.00 45.38           O  
ATOM   2278  CB  LEU A 284      -6.043  72.986   4.630  1.00 46.88           C  
ATOM   2279  CG  LEU A 284      -6.674  72.240   5.806  1.00 47.30           C  
ATOM   2280  CD1 LEU A 284      -5.941  72.536   7.127  1.00 48.51           C  
ATOM   2281  CD2 LEU A 284      -8.139  72.604   5.915  1.00 47.20           C  
ATOM   2282  N   SER A 285      -3.649  71.856   2.610  1.00 44.69           N  
ATOM   2283  CA  SER A 285      -3.141  70.707   1.857  1.00 43.86           C  
ATOM   2284  C   SER A 285      -1.615  70.700   1.640  1.00 43.24           C  
ATOM   2285  O   SER A 285      -1.072  69.738   1.088  1.00 43.00           O  
ATOM   2286  CB  SER A 285      -3.849  70.611   0.505  1.00 43.73           C  
ATOM   2287  OG  SER A 285      -3.528  71.728  -0.301  1.00 45.13           O  
ATOM   2288  N   ASP A 286      -0.944  71.771   2.060  1.00 42.53           N  
ATOM   2289  CA  ASP A 286       0.508  71.895   1.930  1.00 42.33           C  
ATOM   2290  C   ASP A 286       1.223  70.857   2.792  1.00 41.20           C  
ATOM   2291  O   ASP A 286       0.839  70.634   3.942  1.00 41.11           O  
ATOM   2292  CB  ASP A 286       0.964  73.299   2.344  1.00 42.40           C  
ATOM   2293  CG  ASP A 286       0.609  74.370   1.313  1.00 44.65           C  
ATOM   2294  OD1 ASP A 286       0.090  74.034   0.227  1.00 46.59           O  
ATOM   2295  OD2 ASP A 286       0.854  75.561   1.591  1.00 46.48           O  
ATOM   2296  N   ILE A 287       2.274  70.251   2.242  1.00 40.52           N  
ATOM   2297  CA  ILE A 287       3.097  69.265   2.970  1.00 38.71           C  
ATOM   2298  C   ILE A 287       3.540  69.755   4.363  1.00 38.01           C  
ATOM   2299  O   ILE A 287       3.747  68.946   5.274  1.00 37.40           O  
ATOM   2300  CB  ILE A 287       4.311  68.769   2.117  1.00 39.11           C  
ATOM   2301  CG1 ILE A 287       4.986  67.556   2.765  1.00 37.91           C  
ATOM   2302  CG2 ILE A 287       5.330  69.892   1.879  1.00 39.20           C  
ATOM   2303  CD1 ILE A 287       4.409  66.235   2.337  1.00 40.79           C  
ATOM   2304  N   GLY A 288       3.654  71.074   4.521  1.00 37.32           N  
ATOM   2305  CA  GLY A 288       3.981  71.704   5.809  1.00 37.77           C  
ATOM   2306  C   GLY A 288       3.082  71.314   6.975  1.00 37.74           C  
ATOM   2307  O   GLY A 288       3.487  71.397   8.141  1.00 37.35           O  
ATOM   2308  N   THR A 289       1.864  70.869   6.654  1.00 37.41           N  
ATOM   2309  CA  THR A 289       0.870  70.457   7.651  1.00 37.09           C  
ATOM   2310  C   THR A 289       1.206  69.128   8.330  1.00 36.93           C  
ATOM   2311  O   THR A 289       0.676  68.832   9.409  1.00 37.01           O  
ATOM   2312  CB  THR A 289      -0.541  70.281   7.006  1.00 37.37           C  
ATOM   2313  OG1 THR A 289      -0.458  69.329   5.941  1.00 36.31           O  
ATOM   2314  CG2 THR A 289      -1.084  71.608   6.458  1.00 36.85           C  
ATOM   2315  N   ILE A 290       2.043  68.308   7.693  1.00 36.39           N  
ATOM   2316  CA  ILE A 290       2.361  66.987   8.254  1.00 36.48           C  
ATOM   2317  C   ILE A 290       3.810  66.754   8.691  1.00 36.57           C  
ATOM   2318  O   ILE A 290       4.201  65.614   8.940  1.00 36.85           O  
ATOM   2319  CB  ILE A 290       1.926  65.826   7.331  1.00 36.29           C  
ATOM   2320  CG1 ILE A 290       2.636  65.899   5.971  1.00 34.71           C  
ATOM   2321  CG2 ILE A 290       0.392  65.805   7.209  1.00 36.53           C  
ATOM   2322  CD1 ILE A 290       2.800  64.531   5.292  1.00 32.94           C  
ATOM   2323  N   MET A 291       4.596  67.818   8.800  1.00 36.86           N  
ATOM   2324  CA  MET A 291       6.003  67.661   9.202  1.00 37.42           C  
ATOM   2325  C   MET A 291       6.583  68.838   9.954  1.00 37.86           C  
ATOM   2326  O   MET A 291       6.222  69.991   9.699  1.00 37.98           O  
ATOM   2327  CB  MET A 291       6.895  67.309   8.001  1.00 37.22           C  
ATOM   2328  CG  MET A 291       6.741  68.232   6.798  1.00 36.89           C  
ATOM   2329  SD  MET A 291       7.912  67.942   5.442  1.00 39.14           S  
ATOM   2330  CE  MET A 291       7.602  66.252   4.980  1.00 37.20           C  
ATOM   2331  N   ARG A 292       7.470  68.533  10.898  1.00 38.22           N  
ATOM   2332  CA  ARG A 292       8.345  69.549  11.473  1.00 39.27           C  
ATOM   2333  C   ARG A 292       9.563  69.717  10.572  1.00 38.72           C  
ATOM   2334  O   ARG A 292       9.963  68.791   9.873  1.00 38.39           O  
ATOM   2335  CB  ARG A 292       8.781  69.178  12.892  1.00 39.74           C  
ATOM   2336  CG  ARG A 292       7.679  69.345  13.940  1.00 42.81           C  
ATOM   2337  CD  ARG A 292       8.161  68.927  15.323  1.00 45.31           C  
ATOM   2338  NE  ARG A 292       7.923  67.500  15.520  1.00 49.06           N  
ATOM   2339  CZ  ARG A 292       8.870  66.571  15.632  1.00 48.48           C  
ATOM   2340  NH1 ARG A 292      10.156  66.901  15.592  1.00 49.58           N  
ATOM   2341  NH2 ARG A 292       8.521  65.305  15.800  1.00 48.34           N  
ATOM   2342  N   VAL A 293      10.131  70.912  10.575  1.00 38.49           N  
ATOM   2343  CA  VAL A 293      11.315  71.185   9.784  1.00 38.42           C  
ATOM   2344  C   VAL A 293      12.271  71.979  10.660  1.00 39.11           C  
ATOM   2345  O   VAL A 293      11.881  72.970  11.300  1.00 38.48           O  
ATOM   2346  CB  VAL A 293      10.986  71.989   8.502  1.00 38.88           C  
ATOM   2347  CG1 VAL A 293      12.189  72.036   7.568  1.00 36.92           C  
ATOM   2348  CG2 VAL A 293       9.771  71.393   7.768  1.00 39.16           C  
ATOM   2349  N   VAL A 294      13.519  71.521  10.708  1.00 39.14           N  
ATOM   2350  CA  VAL A 294      14.563  72.191  11.464  1.00 39.61           C  
ATOM   2351  C   VAL A 294      15.845  72.248  10.619  1.00 40.21           C  
ATOM   2352  O   VAL A 294      16.120  71.343   9.817  1.00 39.52           O  
ATOM   2353  CB  VAL A 294      14.816  71.505  12.847  1.00 39.69           C  
ATOM   2354  CG1 VAL A 294      13.577  71.603  13.752  1.00 40.45           C  
ATOM   2355  CG2 VAL A 294      15.207  70.050  12.690  1.00 39.78           C  
ATOM   2356  N   GLU A 295      16.601  73.328  10.774  1.00 40.21           N  
ATOM   2357  CA  GLU A 295      17.860  73.479  10.073  1.00 40.87           C  
ATOM   2358  C   GLU A 295      18.931  72.826  10.948  1.00 40.33           C  
ATOM   2359  O   GLU A 295      19.024  73.124  12.125  1.00 40.31           O  
ATOM   2360  CB  GLU A 295      18.127  74.967   9.815  1.00 41.00           C  
ATOM   2361  CG  GLU A 295      19.316  75.298   8.934  1.00 44.29           C  
ATOM   2362  CD  GLU A 295      19.419  76.791   8.633  1.00 46.73           C  
ATOM   2363  OE1 GLU A 295      18.456  77.543   8.900  1.00 49.06           O  
ATOM   2364  OE2 GLU A 295      20.474  77.216   8.132  1.00 50.31           O  
ATOM   2365  N   LEU A 296      19.701  71.893  10.387  1.00 40.54           N  
ATOM   2366  CA  LEU A 296      20.815  71.277  11.123  1.00 39.98           C  
ATOM   2367  C   LEU A 296      21.846  72.337  11.506  1.00 40.01           C  
ATOM   2368  O   LEU A 296      22.092  73.259  10.725  1.00 39.28           O  
ATOM   2369  CB  LEU A 296      21.484  70.175  10.295  1.00 40.19           C  
ATOM   2370  CG  LEU A 296      20.732  68.849  10.094  1.00 40.74           C  
ATOM   2371  CD1 LEU A 296      21.669  67.844   9.435  1.00 40.57           C  
ATOM   2372  CD2 LEU A 296      20.154  68.280  11.405  1.00 39.64           C  
ATOM   2373  N   SER A 297      22.427  72.208  12.704  1.00 39.89           N  
ATOM   2374  CA  SER A 297      23.434  73.163  13.182  1.00 40.73           C  
ATOM   2375  C   SER A 297      24.566  73.254  12.176  1.00 40.36           C  
ATOM   2376  O   SER A 297      24.977  72.240  11.620  1.00 40.17           O  
ATOM   2377  CB  SER A 297      23.997  72.749  14.543  1.00 40.95           C  
ATOM   2378  OG  SER A 297      22.979  72.604  15.510  1.00 42.02           O  
ATOM   2379  N   PRO A 298      25.039  74.472  11.899  1.00 40.41           N  
ATOM   2380  CA  PRO A 298      26.145  74.540  10.953  1.00 40.79           C  
ATOM   2381  C   PRO A 298      27.425  73.937  11.521  1.00 40.99           C  
ATOM   2382  O   PRO A 298      27.639  73.945  12.732  1.00 40.71           O  
ATOM   2383  CB  PRO A 298      26.328  76.035  10.711  1.00 40.43           C  
ATOM   2384  CG  PRO A 298      25.602  76.715  11.827  1.00 40.83           C  
ATOM   2385  CD  PRO A 298      24.506  75.799  12.240  1.00 40.24           C  
ATOM   2386  N   LEU A 299      28.247  73.398  10.635  1.00 41.63           N  
ATOM   2387  CA  LEU A 299      29.571  72.920  11.004  1.00 42.74           C  
ATOM   2388  C   LEU A 299      30.530  74.099  10.959  1.00 43.25           C  
ATOM   2389  O   LEU A 299      30.612  74.805   9.945  1.00 43.16           O  
ATOM   2390  CB  LEU A 299      30.005  71.792  10.065  1.00 42.77           C  
ATOM   2391  CG  LEU A 299      29.116  70.537  10.122  1.00 43.20           C  
ATOM   2392  CD1 LEU A 299      29.479  69.537   9.028  1.00 44.24           C  
ATOM   2393  CD2 LEU A 299      29.178  69.862  11.489  1.00 45.11           C  
ATOM   2394  N   LYS A 300      31.229  74.333  12.069  1.00 44.10           N  
ATOM   2395  CA  LYS A 300      32.171  75.461  12.166  1.00 44.90           C  
ATOM   2396  C   LYS A 300      33.349  75.257  11.222  1.00 44.96           C  
ATOM   2397  O   LYS A 300      33.407  75.862  10.152  1.00 45.73           O  
ATOM   2398  CB  LYS A 300      32.673  75.640  13.611  1.00 45.30           C  
ATOM   2399  N   TRP A 305      27.530  82.332   3.285  1.00 66.92           N  
ATOM   2400  CA  TRP A 305      26.883  82.000   2.018  1.00 66.70           C  
ATOM   2401  C   TRP A 305      27.879  82.002   0.857  1.00 66.48           C  
ATOM   2402  O   TRP A 305      28.658  82.947   0.698  1.00 66.58           O  
ATOM   2403  CB  TRP A 305      25.724  82.960   1.728  1.00 66.80           C  
ATOM   2404  CG  TRP A 305      24.920  82.536   0.539  1.00 67.25           C  
ATOM   2405  CD1 TRP A 305      23.787  81.774   0.543  1.00 68.04           C  
ATOM   2406  CD2 TRP A 305      25.207  82.824  -0.835  1.00 67.50           C  
ATOM   2407  NE1 TRP A 305      23.345  81.576  -0.746  1.00 67.78           N  
ATOM   2408  CE2 TRP A 305      24.200  82.210  -1.609  1.00 67.85           C  
ATOM   2409  CE3 TRP A 305      26.217  83.549  -1.488  1.00 67.87           C  
ATOM   2410  CZ2 TRP A 305      24.172  82.296  -3.004  1.00 68.49           C  
ATOM   2411  CZ3 TRP A 305      26.186  83.636  -2.877  1.00 67.66           C  
ATOM   2412  CH2 TRP A 305      25.170  83.014  -3.618  1.00 68.29           C  
ATOM   2413  N   THR A 306      27.823  80.953   0.036  1.00 66.19           N  
ATOM   2414  CA  THR A 306      28.803  80.743  -1.042  1.00 65.57           C  
ATOM   2415  C   THR A 306      28.207  80.643  -2.452  1.00 64.90           C  
ATOM   2416  O   THR A 306      28.824  81.102  -3.423  1.00 65.02           O  
ATOM   2417  CB  THR A 306      29.684  79.494  -0.784  1.00 65.78           C  
ATOM   2418  OG1 THR A 306      28.861  78.390  -0.375  1.00 66.14           O  
ATOM   2419  CG2 THR A 306      30.734  79.783   0.288  1.00 65.63           C  
ATOM   2420  N   GLY A 307      27.021  80.048  -2.560  1.00 63.88           N  
ATOM   2421  CA  GLY A 307      26.422  79.728  -3.860  1.00 62.68           C  
ATOM   2422  C   GLY A 307      26.126  78.244  -4.005  1.00 61.76           C  
ATOM   2423  O   GLY A 307      25.190  77.856  -4.711  1.00 61.56           O  
ATOM   2424  N   LYS A 308      26.940  77.424  -3.333  1.00 60.80           N  
ATOM   2425  CA  LYS A 308      26.779  75.961  -3.277  1.00 59.63           C  
ATOM   2426  C   LYS A 308      25.940  75.523  -2.060  1.00 58.65           C  
ATOM   2427  O   LYS A 308      25.881  76.253  -1.062  1.00 58.52           O  
ATOM   2428  CB  LYS A 308      28.149  75.288  -3.246  1.00 59.69           C  
ATOM   2429  N   PRO A 309      25.286  74.335  -2.136  1.00 57.54           N  
ATOM   2430  CA  PRO A 309      24.567  73.817  -0.958  1.00 56.48           C  
ATOM   2431  C   PRO A 309      25.473  73.646   0.275  1.00 55.24           C  
ATOM   2432  O   PRO A 309      26.444  72.883   0.239  1.00 55.44           O  
ATOM   2433  CB  PRO A 309      24.013  72.460  -1.436  1.00 56.55           C  
ATOM   2434  CG  PRO A 309      24.722  72.152  -2.717  1.00 57.02           C  
ATOM   2435  CD  PRO A 309      25.095  73.470  -3.316  1.00 57.66           C  
ATOM   2436  N   VAL A 310      25.165  74.384   1.341  1.00 53.62           N  
ATOM   2437  CA  VAL A 310      25.912  74.289   2.596  1.00 51.83           C  
ATOM   2438  C   VAL A 310      25.018  73.743   3.702  1.00 50.59           C  
ATOM   2439  O   VAL A 310      25.339  72.721   4.318  1.00 50.53           O  
ATOM   2440  CB  VAL A 310      26.516  75.649   3.053  1.00 52.24           C  
ATOM   2441  CG1 VAL A 310      27.761  75.412   3.909  1.00 51.67           C  
ATOM   2442  CG2 VAL A 310      26.879  76.530   1.857  1.00 52.39           C  
ATOM   2443  N   SER A 311      23.896  74.425   3.936  1.00 48.17           N  
ATOM   2444  CA  SER A 311      22.956  74.074   4.999  1.00 46.00           C  
ATOM   2445  C   SER A 311      22.063  72.891   4.648  1.00 44.12           C  
ATOM   2446  O   SER A 311      21.628  72.745   3.508  1.00 43.91           O  
ATOM   2447  CB  SER A 311      22.077  75.284   5.327  1.00 46.34           C  
ATOM   2448  OG  SER A 311      22.884  76.413   5.612  1.00 46.18           O  
ATOM   2449  N   TYR A 312      21.798  72.044   5.636  1.00 41.85           N  
ATOM   2450  CA  TYR A 312      20.887  70.919   5.456  1.00 39.89           C  
ATOM   2451  C   TYR A 312      19.754  70.986   6.478  1.00 38.45           C  
ATOM   2452  O   TYR A 312      19.884  71.620   7.532  1.00 37.98           O  
ATOM   2453  CB  TYR A 312      21.621  69.567   5.490  1.00 39.73           C  
ATOM   2454  CG  TYR A 312      22.331  69.204   4.186  1.00 39.48           C  
ATOM   2455  CD1 TYR A 312      21.824  68.220   3.335  1.00 40.33           C  
ATOM   2456  CD2 TYR A 312      23.505  69.851   3.806  1.00 39.40           C  
ATOM   2457  CE1 TYR A 312      22.494  67.891   2.121  1.00 40.73           C  
ATOM   2458  CE2 TYR A 312      24.173  69.528   2.618  1.00 40.02           C  
ATOM   2459  CZ  TYR A 312      23.668  68.552   1.783  1.00 40.11           C  
ATOM   2460  OH  TYR A 312      24.356  68.251   0.615  1.00 39.65           O  
ATOM   2461  N   TYR A 313      18.642  70.335   6.149  1.00 36.90           N  
ATOM   2462  CA  TYR A 313      17.399  70.497   6.904  1.00 35.13           C  
ATOM   2463  C   TYR A 313      16.766  69.150   7.194  1.00 34.94           C  
ATOM   2464  O   TYR A 313      16.642  68.308   6.305  1.00 34.26           O  
ATOM   2465  CB  TYR A 313      16.415  71.380   6.135  1.00 34.25           C  
ATOM   2466  CG  TYR A 313      16.950  72.744   5.752  1.00 34.67           C  
ATOM   2467  CD1 TYR A 313      16.603  73.888   6.477  1.00 33.68           C  
ATOM   2468  CD2 TYR A 313      17.798  72.898   4.651  1.00 34.32           C  
ATOM   2469  CE1 TYR A 313      17.109  75.144   6.120  1.00 34.03           C  
ATOM   2470  CE2 TYR A 313      18.311  74.139   4.302  1.00 34.81           C  
ATOM   2471  CZ  TYR A 313      17.949  75.257   5.024  1.00 33.75           C  
ATOM   2472  OH  TYR A 313      18.458  76.478   4.651  1.00 34.29           O  
ATOM   2473  N   LEU A 314      16.365  68.960   8.447  1.00 34.19           N  
ATOM   2474  CA  LEU A 314      15.732  67.738   8.880  1.00 34.00           C  
ATOM   2475  C   LEU A 314      14.231  67.931   8.923  1.00 34.05           C  
ATOM   2476  O   LEU A 314      13.736  68.864   9.561  1.00 34.16           O  
ATOM   2477  CB  LEU A 314      16.248  67.322  10.265  1.00 34.01           C  
ATOM   2478  CG  LEU A 314      15.523  66.222  11.041  1.00 34.19           C  
ATOM   2479  CD1 LEU A 314      15.719  64.845  10.408  1.00 32.58           C  
ATOM   2480  CD2 LEU A 314      15.971  66.208  12.522  1.00 36.47           C  
ATOM   2481  N   HIS A 315      13.521  67.038   8.245  1.00 33.61           N  
ATOM   2482  CA  HIS A 315      12.057  67.023   8.239  1.00 33.65           C  
ATOM   2483  C   HIS A 315      11.625  65.774   8.978  1.00 33.69           C  
ATOM   2484  O   HIS A 315      12.120  64.700   8.671  1.00 33.99           O  
ATOM   2485  CB  HIS A 315      11.530  66.951   6.804  1.00 32.86           C  
ATOM   2486  CG  HIS A 315      12.101  67.997   5.898  1.00 33.38           C  
ATOM   2487  ND1 HIS A 315      13.357  67.890   5.336  1.00 32.78           N  
ATOM   2488  CD2 HIS A 315      11.586  69.166   5.448  1.00 32.31           C  
ATOM   2489  CE1 HIS A 315      13.592  68.951   4.583  1.00 32.65           C  
ATOM   2490  NE2 HIS A 315      12.533  69.740   4.633  1.00 31.07           N  
ATOM   2491  N   THR A 316      10.716  65.905   9.947  1.00 33.69           N  
ATOM   2492  CA  THR A 316      10.168  64.729  10.633  1.00 34.45           C  
ATOM   2493  C   THR A 316       8.648  64.644  10.421  1.00 35.23           C  
ATOM   2494  O   THR A 316       7.927  65.607  10.689  1.00 34.60           O  
ATOM   2495  CB  THR A 316      10.519  64.746  12.141  1.00 35.02           C  
ATOM   2496  OG1 THR A 316      11.942  64.905  12.290  1.00 34.41           O  
ATOM   2497  CG2 THR A 316      10.084  63.443  12.840  1.00 34.44           C  
ATOM   2498  N   ILE A 317       8.174  63.494   9.937  1.00 36.56           N  
ATOM   2499  CA  ILE A 317       6.746  63.299   9.655  1.00 37.86           C  
ATOM   2500  C   ILE A 317       5.976  63.329  10.976  1.00 38.25           C  
ATOM   2501  O   ILE A 317       6.129  62.431  11.795  1.00 38.82           O  
ATOM   2502  CB  ILE A 317       6.451  61.952   8.904  1.00 37.26           C  
ATOM   2503  CG1 ILE A 317       7.229  61.825   7.578  1.00 39.09           C  
ATOM   2504  CG2 ILE A 317       4.940  61.769   8.693  1.00 37.95           C  
ATOM   2505  CD1 ILE A 317       6.715  62.675   6.397  1.00 40.49           C  
ATOM   2506  N   ASP A 318       5.165  64.369  11.173  1.00 39.24           N  
ATOM   2507  CA  ASP A 318       4.437  64.596  12.437  1.00 39.81           C  
ATOM   2508  C   ASP A 318       3.022  65.070  12.131  1.00 39.78           C  
ATOM   2509  O   ASP A 318       2.802  66.247  11.888  1.00 39.23           O  
ATOM   2510  CB  ASP A 318       5.151  65.633  13.331  1.00 39.56           C  
ATOM   2511  CG  ASP A 318       4.391  65.923  14.642  1.00 40.11           C  
ATOM   2512  OD1 ASP A 318       3.181  65.673  14.709  1.00 40.22           O  
ATOM   2513  OD2 ASP A 318       4.990  66.428  15.617  1.00 41.61           O  
ATOM   2514  N   ARG A 319       2.078  64.143  12.161  1.00 40.99           N  
ATOM   2515  CA  ARG A 319       0.690  64.451  11.812  1.00 42.47           C  
ATOM   2516  C   ARG A 319      -0.093  65.084  12.959  1.00 43.66           C  
ATOM   2517  O   ARG A 319      -1.173  65.651  12.731  1.00 44.27           O  
ATOM   2518  CB  ARG A 319      -0.016  63.224  11.236  1.00 41.67           C  
ATOM   2519  CG  ARG A 319       0.165  63.130   9.731  1.00 42.36           C  
ATOM   2520  CD  ARG A 319      -0.161  61.758   9.155  1.00 41.72           C  
ATOM   2521  NE  ARG A 319       0.323  61.663   7.779  1.00 41.26           N  
ATOM   2522  CZ  ARG A 319       1.316  60.879   7.369  1.00 40.35           C  
ATOM   2523  NH1 ARG A 319       1.948  60.084   8.228  1.00 39.50           N  
ATOM   2524  NH2 ARG A 319       1.677  60.888   6.087  1.00 39.38           N  
ATOM   2525  N   THR A 320       0.470  65.044  14.172  1.00 44.66           N  
ATOM   2526  CA  THR A 320      -0.175  65.682  15.324  1.00 45.90           C  
ATOM   2527  C   THR A 320      -0.446  67.174  15.075  1.00 46.37           C  
ATOM   2528  O   THR A 320      -1.373  67.742  15.661  1.00 46.71           O  
ATOM   2529  CB  THR A 320       0.567  65.422  16.691  1.00 46.11           C  
ATOM   2530  OG1 THR A 320       1.760  66.209  16.778  1.00 46.87           O  
ATOM   2531  CG2 THR A 320       0.918  63.950  16.863  1.00 46.59           C  
ATOM   2532  N   ILE A 321       0.333  67.783  14.176  1.00 46.46           N  
ATOM   2533  CA  ILE A 321       0.184  69.204  13.807  1.00 46.70           C  
ATOM   2534  C   ILE A 321      -1.162  69.459  13.093  1.00 46.99           C  
ATOM   2535  O   ILE A 321      -1.866  70.427  13.400  1.00 47.22           O  
ATOM   2536  CB  ILE A 321       1.364  69.702  12.910  1.00 46.58           C  
ATOM   2537  CG1 ILE A 321       2.727  69.459  13.586  1.00 46.97           C  
ATOM   2538  CG2 ILE A 321       1.218  71.190  12.575  1.00 46.22           C  
ATOM   2539  CD1 ILE A 321       3.949  69.774  12.666  1.00 44.76           C  
ATOM   2540  N   LEU A 322      -1.502  68.588  12.144  1.00 47.04           N  
ATOM   2541  CA  LEU A 322      -2.774  68.666  11.431  1.00 47.36           C  
ATOM   2542  C   LEU A 322      -3.945  68.327  12.361  1.00 48.07           C  
ATOM   2543  O   LEU A 322      -4.977  69.009  12.338  1.00 48.10           O  
ATOM   2544  CB  LEU A 322      -2.775  67.732  10.224  1.00 46.74           C  
ATOM   2545  CG  LEU A 322      -3.931  67.796   9.218  1.00 45.76           C  
ATOM   2546  CD1 LEU A 322      -4.020  69.156   8.538  1.00 43.06           C  
ATOM   2547  CD2 LEU A 322      -3.763  66.688   8.181  1.00 43.94           C  
ATOM   2548  N   GLU A 323      -3.761  67.279  13.162  1.00 48.80           N  
ATOM   2549  CA  GLU A 323      -4.742  66.825  14.147  1.00 50.20           C  
ATOM   2550  C   GLU A 323      -5.073  67.952  15.121  1.00 50.61           C  
ATOM   2551  O   GLU A 323      -6.250  68.224  15.376  1.00 50.46           O  
ATOM   2552  CB  GLU A 323      -4.225  65.606  14.903  1.00 50.12           C  
ATOM   2553  CG  GLU A 323      -3.928  64.382  14.021  1.00 52.07           C  
ATOM   2554  CD  GLU A 323      -2.983  63.369  14.676  1.00 54.16           C  
ATOM   2555  OE1 GLU A 323      -2.261  63.736  15.637  1.00 54.96           O  
ATOM   2556  OE2 GLU A 323      -2.958  62.196  14.227  1.00 53.98           O  
ATOM   2557  N   ASN A 324      -4.029  68.607  15.635  1.00 51.07           N  
ATOM   2558  CA  ASN A 324      -4.160  69.733  16.557  1.00 51.99           C  
ATOM   2559  C   ASN A 324      -5.010  70.856  15.984  1.00 52.57           C  
ATOM   2560  O   ASN A 324      -5.896  71.385  16.670  1.00 52.34           O  
ATOM   2561  CB  ASN A 324      -2.785  70.305  16.936  1.00 52.01           C  
ATOM   2562  CG  ASN A 324      -2.016  69.422  17.908  1.00 52.57           C  
ATOM   2563  OD1 ASN A 324      -2.494  68.371  18.342  1.00 52.36           O  
ATOM   2564  ND2 ASN A 324      -0.799  69.850  18.247  1.00 53.32           N  
ATOM   2565  N   TYR A 325      -4.738  71.217  14.730  1.00 52.99           N  
ATOM   2566  CA  TYR A 325      -5.460  72.308  14.077  1.00 53.96           C  
ATOM   2567  C   TYR A 325      -6.968  72.042  14.026  1.00 54.53           C  
ATOM   2568  O   TYR A 325      -7.766  72.973  14.160  1.00 54.72           O  
ATOM   2569  CB  TYR A 325      -4.918  72.581  12.665  1.00 53.53           C  
ATOM   2570  CG  TYR A 325      -5.731  73.605  11.885  1.00 54.06           C  
ATOM   2571  CD1 TYR A 325      -5.592  74.971  12.132  1.00 53.70           C  
ATOM   2572  CD2 TYR A 325      -6.641  73.202  10.903  1.00 53.93           C  
ATOM   2573  CE1 TYR A 325      -6.334  75.913  11.422  1.00 55.03           C  
ATOM   2574  CE2 TYR A 325      -7.386  74.132  10.186  1.00 54.80           C  
ATOM   2575  CZ  TYR A 325      -7.232  75.486  10.452  1.00 55.30           C  
ATOM   2576  OH  TYR A 325      -7.974  76.406   9.750  1.00 56.02           O  
ATOM   2577  N   PHE A 326      -7.337  70.777  13.825  1.00 55.31           N  
ATOM   2578  CA  PHE A 326      -8.739  70.369  13.757  1.00 56.24           C  
ATOM   2579  C   PHE A 326      -9.400  70.393  15.138  1.00 57.13           C  
ATOM   2580  O   PHE A 326     -10.527  70.874  15.272  1.00 57.49           O  
ATOM   2581  CB  PHE A 326      -8.886  68.995  13.085  1.00 55.83           C  
ATOM   2582  CG  PHE A 326      -8.921  69.053  11.576  1.00 55.12           C  
ATOM   2583  CD1 PHE A 326      -7.738  69.065  10.834  1.00 54.05           C  
ATOM   2584  CD2 PHE A 326     -10.135  69.090  10.898  1.00 54.04           C  
ATOM   2585  CE1 PHE A 326      -7.763  69.120   9.439  1.00 53.69           C  
ATOM   2586  CE2 PHE A 326     -10.178  69.146   9.504  1.00 54.22           C  
ATOM   2587  CZ  PHE A 326      -8.988  69.159   8.769  1.00 54.41           C  
ATOM   2588  N   SER A 327      -8.698  69.890  16.156  1.00 58.01           N  
ATOM   2589  CA  SER A 327      -9.160  69.996  17.549  1.00 59.12           C  
ATOM   2590  C   SER A 327      -9.414  71.441  17.974  1.00 59.72           C  
ATOM   2591  O   SER A 327     -10.306  71.707  18.780  1.00 59.89           O  
ATOM   2592  CB  SER A 327      -8.171  69.347  18.517  1.00 58.90           C  
ATOM   2593  OG  SER A 327      -8.270  67.937  18.469  1.00 59.51           O  
ATOM   2594  N   SER A 328      -8.630  72.367  17.424  1.00 60.43           N  
ATOM   2595  CA  SER A 328      -8.799  73.785  17.714  1.00 61.09           C  
ATOM   2596  C   SER A 328     -10.000  74.390  16.973  1.00 61.47           C  
ATOM   2597  O   SER A 328     -10.538  75.422  17.392  1.00 61.62           O  
ATOM   2598  CB  SER A 328      -7.511  74.567  17.418  1.00 61.13           C  
ATOM   2599  OG  SER A 328      -7.404  74.898  16.042  1.00 61.45           O  
ATOM   2600  N   LEU A 329     -10.426  73.745  15.885  1.00 61.93           N  
ATOM   2601  CA  LEU A 329     -11.609  74.194  15.141  1.00 62.15           C  
ATOM   2602  C   LEU A 329     -12.914  73.792  15.838  1.00 62.39           C  
ATOM   2603  O   LEU A 329     -14.004  74.141  15.372  1.00 62.47           O  
ATOM   2604  CB  LEU A 329     -11.598  73.679  13.694  1.00 61.96           C  
ATOM   2605  CG  LEU A 329     -10.535  74.160  12.697  1.00 61.79           C  
ATOM   2606  CD1 LEU A 329     -10.675  73.392  11.390  1.00 61.34           C  
ATOM   2607  CD2 LEU A 329     -10.576  75.674  12.440  1.00 61.43           C  
ATOM   2608  N   LYS A 330     -12.789  73.079  16.958  1.00 62.62           N  
ATOM   2609  CA  LYS A 330     -13.932  72.579  17.718  1.00 62.72           C  
ATOM   2610  C   LYS A 330     -14.119  73.327  19.036  1.00 62.81           C  
ATOM   2611  O   LYS A 330     -13.186  73.454  19.830  1.00 62.96           O  
ATOM   2612  CB  LYS A 330     -13.773  71.082  17.978  1.00 62.79           C  
ATOM   2613  CG  LYS A 330     -13.739  70.256  16.710  1.00 62.72           C  
ATOM   2614  CD  LYS A 330     -13.512  68.791  16.995  1.00 63.70           C  
ATOM   2615  CE  LYS A 330     -13.385  68.014  15.687  1.00 64.52           C  
ATOM   2616  NZ  LYS A 330     -13.391  66.541  15.906  1.00 65.40           N  
TER    2617      LYS A 330                                                      
HETATM 2618  N   SAM A 417      23.564  62.164  -3.272  1.00 28.40           N  
HETATM 2619  CA  SAM A 417      24.946  62.582  -3.671  1.00 28.57           C  
HETATM 2620  C   SAM A 417      25.540  63.513  -2.605  1.00 28.92           C  
HETATM 2621  O   SAM A 417      24.794  64.234  -1.917  1.00 28.53           O  
HETATM 2622  OXT SAM A 417      26.765  63.570  -2.414  1.00 27.74           O  
HETATM 2623  CB  SAM A 417      24.913  63.262  -5.047  1.00 29.13           C  
HETATM 2624  CG  SAM A 417      23.919  64.439  -5.154  1.00 29.84           C  
HETATM 2625  SD  SAM A 417      23.905  65.262  -6.767  1.00 32.12           S  
HETATM 2626  CE  SAM A 417      23.872  67.034  -6.380  1.00 33.57           C  
HETATM 2627  C5' SAM A 417      22.191  65.028  -7.293  1.00 32.35           C  
HETATM 2628  C4' SAM A 417      21.995  63.741  -8.077  1.00 31.74           C  
HETATM 2629  O4' SAM A 417      20.595  63.533  -8.208  1.00 34.46           O  
HETATM 2630  C3' SAM A 417      22.550  63.896  -9.486  1.00 31.87           C  
HETATM 2631  O3' SAM A 417      23.625  63.012  -9.745  1.00 30.00           O  
HETATM 2632  C2' SAM A 417      21.357  63.672 -10.408  1.00 30.57           C  
HETATM 2633  O2' SAM A 417      21.665  62.824 -11.485  1.00 27.61           O  
HETATM 2634  C1' SAM A 417      20.398  62.952  -9.480  1.00 32.92           C  
HETATM 2635  N9  SAM A 417      18.997  62.959  -9.950  1.00 31.87           N  
HETATM 2636  C8  SAM A 417      18.276  64.027 -10.427  1.00 33.23           C  
HETATM 2637  N7  SAM A 417      17.036  63.589 -10.756  1.00 32.52           N  
HETATM 2638  C5  SAM A 417      16.952  62.269 -10.497  1.00 32.90           C  
HETATM 2639  C6  SAM A 417      15.929  61.333 -10.634  1.00 32.05           C  
HETATM 2640  N6  SAM A 417      14.731  61.664 -11.123  1.00 34.22           N  
HETATM 2641  N1  SAM A 417      16.169  60.027 -10.272  1.00 32.52           N  
HETATM 2642  C2  SAM A 417      17.394  59.624  -9.765  1.00 31.76           C  
HETATM 2643  N3  SAM A 417      18.394  60.567  -9.636  1.00 31.61           N  
HETATM 2644  C4  SAM A 417      18.186  61.860  -9.987  1.00 30.78           C  
HETATM 2645  S   SO4 A 418      30.459  41.786   1.098  1.00 67.14           S  
HETATM 2646  O1  SO4 A 418      29.165  42.124   0.516  1.00 67.20           O  
HETATM 2647  O2  SO4 A 418      31.314  41.184   0.076  1.00 65.66           O  
HETATM 2648  O3  SO4 A 418      31.102  42.992   1.622  1.00 66.62           O  
HETATM 2649  O4  SO4 A 418      30.235  40.854   2.200  1.00 67.55           O  
HETATM 2650  S   SO4 A 419       3.518  63.008 -10.494  1.00 95.11           S  
HETATM 2651  O1  SO4 A 419       3.052  64.047 -11.410  1.00 95.28           O  
HETATM 2652  O2  SO4 A 419       4.498  62.161 -11.171  1.00 94.66           O  
HETATM 2653  O3  SO4 A 419       4.127  63.630  -9.321  1.00 95.18           O  
HETATM 2654  O4  SO4 A 419       2.377  62.202 -10.078  1.00 94.92           O  
HETATM 2655  O   HOH A 420      20.902  67.821  -8.772  1.00 35.09           O  
HETATM 2656  O   HOH A 421       4.347  73.601   2.991  1.00 55.97           O  
HETATM 2657  O   HOH A 422      43.438  59.261   3.970  1.00 45.21           O  
HETATM 2658  O   HOH A 423      21.853  70.125  14.269  1.00 43.57           O  
HETATM 2659  O   HOH A 424      16.508  77.008  11.529  1.00 61.32           O  
HETATM 2660  O   HOH A 425      61.592  43.722  -1.952  1.00 58.20           O  
HETATM 2661  O   HOH A 426       8.285  57.882  -7.168  1.00 27.29           O  
HETATM 2662  O   HOH A 427      25.626  60.984 -16.988  1.00 37.78           O  
HETATM 2663  O   HOH A 428       8.755  56.025  10.583  1.00 50.32           O  
HETATM 2664  O   HOH A 429      28.285  61.358  -5.453  1.00 23.93           O  
HETATM 2665  O   HOH A 430      30.536  59.688   2.363  1.00 25.15           O  
HETATM 2666  O   HOH A 431      40.532  44.449  17.657  1.00 67.08           O  
HETATM 2667  O   HOH A 432      15.439  72.291  -5.523  1.00 35.01           O  
HETATM 2668  O   HOH A 433      53.398  35.152  10.159  1.00 46.51           O  
HETATM 2669  O   HOH A 434      35.007  56.898  15.661  1.00 46.85           O  
HETATM 2670  O   HOH A 435      23.069  72.587   8.071  1.00 41.15           O  
HETATM 2671  O   HOH A 436      38.957  57.931  14.197  1.00 46.80           O  
HETATM 2672  O   HOH A 437      12.317  70.753 -11.393  1.00 37.22           O  
HETATM 2673  O   HOH A 438      30.407  58.735   9.709  1.00 25.63           O  
HETATM 2674  O   HOH A 439       8.014  56.042   5.730  1.00 36.82           O  
HETATM 2675  O   HOH A 440      22.288  57.180  12.522  1.00 44.72           O  
HETATM 2676  O   HOH A 441      20.846  63.198  -2.840  1.00 27.25           O  
HETATM 2677  O   HOH A 442      47.733  34.259  12.476  1.00 36.72           O  
HETATM 2678  O   HOH A 443      12.251  67.443  12.078  1.00 29.40           O  
HETATM 2679  O   HOH A 444      23.771  53.885  -8.518  1.00 35.68           O  
HETATM 2680  O   HOH A 445      37.989  40.610   5.878  1.00 36.57           O  
HETATM 2681  O   HOH A 446      36.082  60.296   2.866  1.00 34.90           O  
HETATM 2682  O   HOH A 447      -0.864  60.897   0.121  1.00 58.26           O  
HETATM 2683  O   HOH A 448      33.179  44.037   2.718  1.00 39.78           O  
HETATM 2684  O   HOH A 449      10.046  66.260 -13.227  1.00 51.69           O  
HETATM 2685  O   HOH A 450      43.401  57.523  -2.160  1.00 32.76           O  
HETATM 2686  O   HOH A 451      33.479  70.632   6.751  1.00 57.11           O  
HETATM 2687  O   HOH A 452      28.710  69.151   1.703  1.00 48.39           O  
HETATM 2688  O   HOH A 453      51.756  58.446  -6.461  1.00 45.12           O  
HETATM 2689  O   HOH A 454      25.082  52.017 -10.237  1.00 35.06           O  
HETATM 2690  O   HOH A 455       4.900  57.907  -1.820  1.00 47.99           O  
HETATM 2691  O   HOH A 456       2.736  78.874   6.901  1.00 56.48           O  
HETATM 2692  O   HOH A 457      42.408  43.057  -1.231  1.00 48.19           O  
HETATM 2693  O   HOH A 458      47.588  39.816   2.441  1.00 41.16           O  
HETATM 2694  O   HOH A 459      55.919  37.374   2.304  1.00 47.00           O  
HETATM 2695  O   HOH A 460      29.977  62.141   1.034  1.00 42.96           O  
HETATM 2696  O   HOH A 461      29.238  60.169  12.236  1.00 39.60           O  
HETATM 2697  O   HOH A 462      27.430  63.777 -13.140  1.00 34.25           O  
HETATM 2698  O   HOH A 463      13.674  53.762 -12.727  1.00 45.71           O  
HETATM 2699  O   HOH A 464      24.820  63.974 -12.300  1.00 30.76           O  
HETATM 2700  O   HOH A 465      11.686  72.656  -1.970  1.00 40.89           O  
HETATM 2701  O   HOH A 466      39.615  42.328  -0.044  1.00 35.93           O  
HETATM 2702  O   HOH A 467      25.984  63.697 -15.952  1.00 74.08           O  
HETATM 2703  O   HOH A 468       3.499  76.106   2.628  1.00 47.18           O  
HETATM 2704  O   HOH A 469      31.691  70.055   5.015  1.00 36.57           O  
HETATM 2705  O   HOH A 470      58.144  45.522  -4.065  1.00 53.96           O  
HETATM 2706  O   HOH A 471      35.517  52.779 -13.261  1.00 54.27           O  
HETATM 2707  O   HOH A 472      25.262  71.260   8.909  1.00 43.30           O  
HETATM 2708  O   HOH A 473      21.964  45.463   7.409  1.00 70.87           O  
HETATM 2709  O   HOH A 474      30.229  43.466   6.263  1.00 44.52           O  
HETATM 2710  O   HOH A 475      25.630  49.766  -8.974  1.00 39.11           O  
HETATM 2711  O   HOH A 476      23.082  70.640  -5.347  1.00 50.95           O  
HETATM 2712  O   HOH A 477      13.197  47.775  -1.349  1.00 46.14           O  
HETATM 2713  O   HOH A 478      43.535  46.800  -4.068  1.00 39.41           O  
HETATM 2714  O   HOH A 479      20.538  68.777  -6.459  1.00 29.78           O  
HETATM 2715  O   HOH A 480      44.198  59.440   6.501  1.00 41.22           O  
HETATM 2716  O   HOH A 481      16.790  73.626 -12.129  1.00 55.87           O  
HETATM 2717  O   HOH A 482       5.784  73.119   0.812  1.00 36.99           O  
HETATM 2718  O   HOH A 483       3.435  71.920   0.001  1.00 41.10           O  
HETATM 2719  O   HOH A 484       0.424  61.954  -2.039  1.00 39.04           O  
HETATM 2720  O   HOH A 485       7.395  54.660 -14.013  1.00 56.76           O  
HETATM 2721  O   HOH A 486      25.548  58.441  -2.156  1.00 29.16           O  
HETATM 2722  O   HOH A 487      42.562  49.233  -8.583  1.00 53.24           O  
HETATM 2723  O   HOH A 488      24.683  55.698  -6.690  1.00 31.39           O  
HETATM 2724  O   HOH A 489      40.746  59.696   8.181  1.00 40.45           O  
HETATM 2725  O   HOH A 490      19.550  73.177 -11.419  1.00 49.90           O  
HETATM 2726  O   HOH A 491      42.591  45.850  -1.570  1.00 39.56           O  
HETATM 2727  O   HOH A 492      35.543  63.600  -3.660  1.00 43.17           O  
HETATM 2728  O   HOH A 493      31.774  54.140  11.640  1.00 37.24           O  
HETATM 2729  O   HOH A 494      31.478  56.715  11.192  1.00 34.86           O  
HETATM 2730  O   HOH A 495      29.377  57.606  13.178  1.00 39.35           O  
HETATM 2731  O   HOH A 496      13.346  50.319  -1.345  1.00 54.57           O  
HETATM 2732  O   HOH A 497      -7.682  80.655   8.251  1.00 50.67           O  
HETATM 2733  O   HOH A 498      57.677  36.592  13.073  1.00 45.75           O  
HETATM 2734  O   HOH A 499      28.598  66.169  14.308  1.00 54.24           O  
HETATM 2735  O   HOH A 500      20.496  49.735  16.765  1.00 67.17           O  
HETATM 2736  O   HOH A 501      36.811  63.272   3.451  1.00 45.08           O  
HETATM 2737  O   HOH A 502      41.430  60.645   4.827  1.00 36.87           O  
HETATM 2738  O   HOH A 503      11.561  59.960  14.164  1.00 38.13           O  
HETATM 2739  O   HOH A 504      13.345  64.124  14.178  1.00 28.52           O  
HETATM 2740  O   HOH A 505      40.800  38.459  -0.333  1.00 45.19           O  
HETATM 2741  O   HOH A 506      39.223  64.929 -17.874  1.00 57.82           O  
HETATM 2742  O   HOH A 507      22.102  74.118   1.443  1.00 50.91           O  
HETATM 2743  O   HOH A 508      57.128  43.712   0.157  1.00 49.42           O  
HETATM 2744  O   HOH A 509      30.605  68.918  -5.373  1.00 40.75           O  
HETATM 2745  O   HOH A 510      34.958  65.967  -9.912  1.00 50.44           O  
HETATM 2746  O   HOH A 511      13.050  57.829  11.037  1.00 34.84           O  
HETATM 2747  O   HOH A 512      12.174  74.078  -5.324  1.00 49.34           O  
HETATM 2748  O   HOH A 513      40.995  58.764  -9.459  1.00 40.52           O  
HETATM 2749  O   HOH A 514      34.438  43.469  -4.409  1.00 42.53           O  
HETATM 2750  O   HOH A 515      26.285  69.117  -2.577  1.00 44.05           O  
HETATM 2751  O   HOH A 516      51.465  36.969   7.373  1.00 46.09           O  
HETATM 2752  O   HOH A 517       5.462  72.396   9.520  1.00 38.91           O  
HETATM 2753  O   HOH A 518      20.502  49.000 -10.981  1.00 47.68           O  
HETATM 2754  O   HOH A 519       8.857  72.868  12.205  1.00 43.71           O  
HETATM 2755  O   HOH A 520       2.273  56.142  10.191  1.00 45.99           O  
HETATM 2756  O   HOH A 521      41.152  47.151  16.706  1.00 62.47           O  
HETATM 2757  O   HOH A 522      56.470  45.854  -1.987  1.00 49.72           O  
HETATM 2758  O   HOH A 523      35.711  56.533 -16.978  1.00 54.92           O  
HETATM 2759  O   HOH A 524      14.695  64.299 -12.133  1.00 48.92           O  
HETATM 2760  O   HOH A 525      35.703  64.530  -7.675  1.00 51.62           O  
HETATM 2761  O   HOH A 526      18.372  76.041   0.462  1.00 43.41           O  
HETATM 2762  O   HOH A 527       8.088  72.889  -5.373  1.00 53.41           O  
HETATM 2763  O   HOH A 528      31.251  61.542  13.622  1.00 57.04           O  
HETATM 2764  O   HOH A 529      26.834  47.372  -8.545  1.00 54.42           O  
HETATM 2765  O   HOH A 530      47.357  42.064  18.964  1.00 57.23           O  
HETATM 2766  O   HOH A 531      27.078  44.332  -5.494  1.00 42.91           O  
HETATM 2767  O   HOH A 532      20.438  76.805   1.939  1.00 51.56           O  
HETATM 2768  O   HOH A 533      14.362  46.473  -3.712  1.00 54.20           O  
HETATM 2769  O   HOH A 534      51.035  36.351   3.175  1.00 48.19           O  
HETATM 2770  O   HOH A 535       8.855  54.566   8.443  1.00 56.53           O  
HETATM 2771  O   HOH A 536      56.759  40.176   4.174  1.00 44.70           O  
HETATM 2772  O   HOH A 537      56.745  35.302  10.282  1.00 54.99           O  
HETATM 2773  O   HOH A 538      37.194  44.690  13.181  1.00 56.36           O  
HETATM 2774  O   HOH A 539      40.639  52.356  13.724  1.00 53.35           O  
HETATM 2775  O   HOH A 540      33.463  60.274   1.182  1.00 35.08           O  
HETATM 2776  O   HOH A 541      45.951  59.742  -2.062  1.00 42.11           O  
HETATM 2777  O   HOH A 542      45.451  48.634  -4.638  1.00 43.56           O  
HETATM 2778  O   HOH A 543       3.786  72.667  -4.243  1.00 69.00           O  
HETATM 2779  O   HOH A 544      12.439  75.464   0.105  1.00 44.04           O  
HETATM 2780  O   HOH A 545      16.024  62.754  14.293  1.00 46.68           O  
HETATM 2781  O   HOH A 546      51.162  52.256 -13.706  1.00 60.44           O  
HETATM 2782  O   HOH A 547       8.306  51.721 -12.188  1.00 52.83           O  
HETATM 2783  O   HOH A 548      26.185  43.010   3.748  1.00 51.06           O  
HETATM 2784  O   HOH A 549      24.751  43.333   1.368  1.00 57.20           O  
HETATM 2785  O   HOH A 550      33.477  52.955 -14.691  1.00 61.37           O  
HETATM 2786  O   HOH A 551      17.548  60.373  16.435  1.00 58.90           O  
HETATM 2787  O   HOH A 552      14.399  52.594  14.232  1.00 64.76           O  
HETATM 2788  O   HOH A 553      28.127  40.844  -1.954  1.00 70.55           O  
HETATM 2789  O   HOH A 554      26.948  58.697  16.486  1.00 47.60           O  
HETATM 2790  O   HOH A 555      18.248  65.077  14.773  1.00 59.94           O  
HETATM 2791  O   HOH A 556       7.868  84.220  10.766  1.00 59.33           O  
HETATM 2792  O   HOH A 557      23.452  76.668   1.854  1.00 63.50           O  
HETATM 2793  O   HOH A 558      29.931  52.631  13.433  1.00 72.45           O  
HETATM 2794  O   HOH A 559      31.189  65.847  11.095  1.00 37.70           O  
HETATM 2795  O   HOH A 560      41.440  64.547 -10.765  1.00 58.30           O  
HETATM 2796  O   HOH A 561      36.558  46.912  -9.484  1.00 64.61           O  
HETATM 2797  O   HOH A 562      34.970  71.578 -13.662  1.00 42.97           O  
HETATM 2798  O   HOH A 563      36.048  66.813  11.041  1.00 46.99           O  
CONECT 2618 2619                                                                
CONECT 2619 2618 2620 2623                                                      
CONECT 2620 2619 2621 2622                                                      
CONECT 2621 2620                                                                
CONECT 2622 2620                                                                
CONECT 2623 2619 2624                                                           
CONECT 2624 2623 2625                                                           
CONECT 2625 2624 2626 2627                                                      
CONECT 2626 2625                                                                
CONECT 2627 2625 2628                                                           
CONECT 2628 2627 2629 2630                                                      
CONECT 2629 2628 2634                                                           
CONECT 2630 2628 2631 2632                                                      
CONECT 2631 2630                                                                
CONECT 2632 2630 2633 2634                                                      
CONECT 2633 2632                                                                
CONECT 2634 2629 2632 2635                                                      
CONECT 2635 2634 2636 2644                                                      
CONECT 2636 2635 2637                                                           
CONECT 2637 2636 2638                                                           
CONECT 2638 2637 2639 2644                                                      
CONECT 2639 2638 2640 2641                                                      
CONECT 2640 2639                                                                
CONECT 2641 2639 2642                                                           
CONECT 2642 2641 2643                                                           
CONECT 2643 2642 2644                                                           
CONECT 2644 2635 2638 2643                                                      
CONECT 2645 2646 2647 2648 2649                                                 
CONECT 2646 2645                                                                
CONECT 2647 2645                                                                
CONECT 2648 2645                                                                
CONECT 2649 2645                                                                
CONECT 2650 2651 2652 2653 2654                                                 
CONECT 2651 2650                                                                
CONECT 2652 2650                                                                
CONECT 2653 2650                                                                
CONECT 2654 2650                                                                
MASTER      401    0    3   12   11    0    8    6 2778    1   37   33          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.