CNRS Nantes University US2B US2B
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***  HYDROLASE/HYDROLASE INHIBITOR 20-FEB-18 6CGP  ***

elNémo ID: 2401041138063808977

Job options:

ID        	=	 2401041138063808977
JOBID     	=	 HYDROLASE/HYDROLASE INHIBITOR 20-FEB-18 6CGP
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    HYDROLASE/HYDROLASE INHIBITOR           20-FEB-18   6CGP              
TITLE     CRYSTAL STRUCTURE OF DANIO RERIO HISTONE DEACETYLASE 6 CATALYTIC      
TITLE    2 DOMAIN 2 COMPLEXED WITH MAIP-032                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HDAC6 PROTEIN;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN 2 (UNP RESIDUES 288-646);                 
COMPND   5 SYNONYM: HISTONE DEACETYLASE 6;                                      
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DANIO RERIO;                                    
SOURCE   3 ORGANISM_COMMON: ZEBRAFISH;                                          
SOURCE   4 ORGANISM_TAXID: 7955;                                                
SOURCE   5 GENE: HDAC6;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HISTONE DEACETYLASE, METALLOHYDROLASE, HYDROLASE-HYDROLASE INHIBITOR  
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.D.OSKO,D.W.CHRISTIANSON                                             
REVDAT   3   18-DEC-19 6CGP    1       REMARK                                   
REVDAT   2   26-DEC-18 6CGP    1       JRNL                                     
REVDAT   1   13-JUN-18 6CGP    0                                                
JRNL        AUTH   M.K.W.MACKWITZ,A.HAMACHER,J.D.OSKO,J.HELD,A.SCHOLER,         
JRNL        AUTH 2 D.W.CHRISTIANSON,M.U.KASSACK,F.K.HANSEN                      
JRNL        TITL   MULTICOMPONENT SYNTHESIS AND BINDING MODE OF IMIDAZO[1,2-    
JRNL        TITL 2 A]PYRIDINE-CAPPED SELECTIVE HDAC6 INHIBITORS.                
JRNL        REF    ORG. LETT.                    V.  20  3255 2018              
JRNL        REFN                   ISSN 1523-7052                               
JRNL        PMID   29790770                                                     
JRNL        DOI    10.1021/ACS.ORGLETT.8B01118                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.08                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 14821                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.460                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 661                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.0810 -  4.2734    0.99     2975   144  0.1546 0.1877        
REMARK   3     2  4.2734 -  3.3926    0.99     2876   107  0.1944 0.2718        
REMARK   3     3  3.3926 -  2.9639    0.99     2770   152  0.2645 0.3400        
REMARK   3     4  2.9639 -  2.6930    1.00     2777   136  0.2985 0.3420        
REMARK   3     5  2.6930 -  2.5000    0.98     2762   122  0.3175 0.3524        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.970           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           2837                                  
REMARK   3   ANGLE     :  0.700           3856                                  
REMARK   3   CHIRALITY :  0.043            422                                  
REMARK   3   PLANARITY :  0.005            503                                  
REMARK   3   DIHEDRAL  :  9.368           1668                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6CGP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000232681.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : LIQUID NITROGEN-COOLED DOUBLE      
REMARK 200                                   CRYSTAL SI(111)                    
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14843                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.250                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.22000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 5.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 5EEM                                       
REMARK 200                                                                      
REMARK 200 REMARK: THIN NEEDLE-LIKE CRYSTALS                                    
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MG/ML ZCD2, MES, PH 6.0, 14% W/V      
REMARK 280  PEG4000, CRYSTALS APPEARED WITHIN 2 DAYS, VAPOR DIFFUSION,          
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.47500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.24950            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.47500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       70.24950            
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 TOTAL BURIED SURFACE AREA: 390 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 12790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL                          
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     SER A   435                                                      
REMARK 465     ASN A   436                                                      
REMARK 465     ALA A   437                                                      
REMARK 465     GLY A   438                                                      
REMARK 465     GLY A   439                                                      
REMARK 465     SER A   440                                                      
REMARK 465     SER A   441                                                      
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     GLU A 478    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 497    CD   OE1  OE2                                       
REMARK 470     LYS A 506    CG   CD   CE   NZ                                   
REMARK 470     ILE A 510    CD1                                                 
REMARK 470     LYS A 518    CG   CD   CE   NZ                                   
REMARK 470     ARG A 520    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 524    CZ   NH1  NH2                                       
REMARK 470     GLN A 560    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 577    CE   NZ                                             
REMARK 470     ASP A 639    OD1  OD2                                            
REMARK 470     LYS A 658    CG   CD   CE   NZ                                   
REMARK 470     LYS A 672    CE   NZ                                             
REMARK 470     ASP A 770    CG   OD1  OD2                                       
REMARK 470     HIS A 771    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR A 773    OG1  CG2                                            
REMARK 470     LYS A 776    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    PRO A 571     -178.23    -65.58                                   
REMARK 500    THR A 600     -106.50   -117.77                                   
REMARK 500    LEU A 685      -61.63   -130.83                                   
REMARK 500    GLU A 742     -101.53   -126.96                                   
REMARK 500    ASP A 770     -148.28     29.16                                   
REMARK 500    LEU A 772      -59.01     55.25                                   
REMARK 500    THR A 773     -129.23     83.29                                   
REMARK 500    PRO A 774     -160.76   -105.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 801   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 610   O                                                      
REMARK 620 2 ASP A 610   OD1  75.1                                              
REMARK 620 3 ASP A 612   O   103.3  97.4                                        
REMARK 620 4 HIS A 614   O   169.4  96.4  71.2                                  
REMARK 620 5 SER A 633   OG   83.6 117.9 144.5 106.2                            
REMARK 620 6 LEU A 634   O    77.8 139.1  60.1 106.0  88.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 803  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 612   OD1                                                    
REMARK 620 2 ASP A 612   OD2  55.3                                              
REMARK 620 3 HIS A 614   ND1  97.0 145.7                                        
REMARK 620 4 ASP A 705   OD2 104.4  76.9  93.6                                  
REMARK 620 5 F1Y A 804   O16 153.8 106.1 106.1  86.7                            
REMARK 620 6 HOH A 903   O    84.1  97.0  99.8 163.2  79.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 802   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE A 623   O                                                      
REMARK 620 2 ASP A 626   O    76.5                                              
REMARK 620 3 VAL A 629   O   121.1  86.0                                        
REMARK 620 4 TYR A 662   O   147.6 118.3  89.8                                  
REMARK 620 5 HOH A 914   O    64.8 139.1 124.9  90.6                            
REMARK 620 6 HOH A 902   O    75.8  84.6 157.9  77.2  73.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 801                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 802                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue F1Y A 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 805                 
DBREF  6CGP A  440   798  UNP    A7YT55   A7YT55_DANRE   288    646             
SEQADV 6CGP SER A  435  UNP  A7YT55              EXPRESSION TAG                 
SEQADV 6CGP ASN A  436  UNP  A7YT55              EXPRESSION TAG                 
SEQADV 6CGP ALA A  437  UNP  A7YT55              EXPRESSION TAG                 
SEQADV 6CGP GLY A  438  UNP  A7YT55              EXPRESSION TAG                 
SEQADV 6CGP GLY A  439  UNP  A7YT55              EXPRESSION TAG                 
SEQRES   1 A  364  SER ASN ALA GLY GLY SER SER PRO ILE THR GLY LEU VAL          
SEQRES   2 A  364  TYR ASP GLN ARG MET MET LEU HIS HIS ASN MET TRP ASP          
SEQRES   3 A  364  SER HIS HIS PRO GLU LEU PRO GLN ARG ILE SER ARG ILE          
SEQRES   4 A  364  PHE SER ARG HIS GLU GLU LEU ARG LEU LEU SER ARG CYS          
SEQRES   5 A  364  HIS ARG ILE PRO ALA ARG LEU ALA THR GLU GLU GLU LEU          
SEQRES   6 A  364  ALA LEU CYS HIS SER SER LYS HIS ILE SER ILE ILE LYS          
SEQRES   7 A  364  SER SER GLU HIS MET LYS PRO ARG ASP LEU ASN ARG LEU          
SEQRES   8 A  364  GLY ASP GLU TYR ASN SER ILE PHE ILE SER ASN GLU SER          
SEQRES   9 A  364  TYR THR CYS ALA LEU LEU ALA ALA GLY SER CYS PHE ASN          
SEQRES  10 A  364  SER ALA GLN ALA ILE LEU THR GLY GLN VAL ARG ASN ALA          
SEQRES  11 A  364  VAL ALA ILE VAL ARG PRO PRO GLY HIS HIS ALA GLU LYS          
SEQRES  12 A  364  ASP THR ALA CYS GLY PHE CYS PHE PHE ASN THR ALA ALA          
SEQRES  13 A  364  LEU THR ALA ARG TYR ALA GLN SER ILE THR ARG GLU SER          
SEQRES  14 A  364  LEU ARG VAL LEU ILE VAL ASP TRP ASP VAL HIS HIS GLY          
SEQRES  15 A  364  ASN GLY THR GLN HIS ILE PHE GLU GLU ASP ASP SER VAL          
SEQRES  16 A  364  LEU TYR ILE SER LEU HIS ARG TYR GLU ASP GLY ALA PHE          
SEQRES  17 A  364  PHE PRO ASN SER GLU ASP ALA ASN TYR ASP LYS VAL GLY          
SEQRES  18 A  364  LEU GLY LYS GLY ARG GLY TYR ASN VAL ASN ILE PRO TRP          
SEQRES  19 A  364  ASN GLY GLY LYS MET GLY ASP PRO GLU TYR MET ALA ALA          
SEQRES  20 A  364  PHE HIS HIS LEU VAL MET PRO ILE ALA ARG GLU PHE ALA          
SEQRES  21 A  364  PRO GLU LEU VAL LEU VAL SER ALA GLY PHE ASP ALA ALA          
SEQRES  22 A  364  ARG GLY ASP PRO LEU GLY GLY PHE GLN VAL THR PRO GLU          
SEQRES  23 A  364  GLY TYR ALA HIS LEU THR HIS GLN LEU MET SER LEU ALA          
SEQRES  24 A  364  ALA GLY ARG VAL LEU ILE ILE LEU GLU GLY GLY TYR ASN          
SEQRES  25 A  364  LEU THR SER ILE SER GLU SER MET SER MET CYS THR SER          
SEQRES  26 A  364  MET LEU LEU GLY ASP SER PRO PRO SER LEU ASP HIS LEU          
SEQRES  27 A  364  THR PRO LEU LYS THR SER ALA THR VAL SER ILE ASN ASN          
SEQRES  28 A  364  VAL LEU ARG ALA HIS ALA PRO PHE TRP SER SER LEU ARG          
HET      K  A 801       1                                                       
HET      K  A 802       1                                                       
HET     ZN  A 803       1                                                       
HET    F1Y  A 804      23                                                       
HET    EDO  A 805       4                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM      ZN ZINC ION                                                         
HETNAM     F1Y N-HYDROXY-4-[(2-PROPYLIMIDAZO[1,2-A]PYRIDIN-3-YL)                
HETNAM   2 F1Y  AMINO]BENZAMIDE                                                 
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2    K    2(K 1+)                                                      
FORMUL   4   ZN    ZN 2+                                                        
FORMUL   5  F1Y    C17 H18 N4 O2                                                
FORMUL   6  EDO    C2 H6 O2                                                     
FORMUL   7  HOH   *14(H2 O)                                                     
HELIX    1 AA1 ASP A  449  LEU A  454  5                                   6    
HELIX    2 AA2 PRO A  467  LEU A  480  1                                  14    
HELIX    3 AA3 LEU A  482  CYS A  486  5                                   5    
HELIX    4 AA4 THR A  495  ALA A  500  1                                   6    
HELIX    5 AA5 SER A  504  SER A  514  1                                  11    
HELIX    6 AA6 LYS A  518  ASP A  527  1                                  10    
HELIX    7 AA7 GLU A  537  GLY A  559  1                                  23    
HELIX    8 AA8 ASN A  587  THR A  600  1                                  14    
HELIX    9 AA9 GLY A  616  PHE A  623  1                                   8    
HELIX   10 AB1 SER A  646  ASN A  650  5                                   5    
HELIX   11 AB2 LEU A  656  ARG A  660  5                                   5    
HELIX   12 AB3 GLY A  674  LEU A  685  1                                  12    
HELIX   13 AB4 LEU A  685  ALA A  694  1                                  10    
HELIX   14 AB5 THR A  718  MET A  730  1                                  13    
HELIX   15 AB6 SER A  731  GLY A  735  5                                   5    
HELIX   16 AB7 ASN A  746  GLY A  763  1                                  18    
HELIX   17 AB8 LYS A  776  ALA A  791  1                                  16    
HELIX   18 AB9 TRP A  794  ARG A  798  5                                   5    
SHEET    1 AA1 8 HIS A 487  ILE A 489  0                                        
SHEET    2 AA1 8 THR A 444  VAL A 447  1  N  THR A 444   O  HIS A 487           
SHEET    3 AA1 8 ASN A 563  ALA A 566  1  O  ASN A 563   N  GLY A 445           
SHEET    4 AA1 8 VAL A 737  LEU A 741  1  O  ILE A 739   N  ALA A 566           
SHEET    5 AA1 8 LEU A 697  ALA A 702  1  N  VAL A 698   O  LEU A 738           
SHEET    6 AA1 8 VAL A 606  ASP A 610  1  N  LEU A 607   O  LEU A 697           
SHEET    7 AA1 8 VAL A 629  ARG A 636  1  O  ILE A 632   N  ASP A 610           
SHEET    8 AA1 8 ASN A 663  TRP A 668  1  O  VAL A 664   N  TYR A 631           
LINK         O   ASP A 610                 K     K A 801     1555   1555  2.82  
LINK         OD1 ASP A 610                 K     K A 801     1555   1555  2.83  
LINK         O   ASP A 612                 K     K A 801     1555   1555  2.64  
LINK         OD1 ASP A 612                ZN    ZN A 803     1555   1555  2.15  
LINK         OD2 ASP A 612                ZN    ZN A 803     1555   1555  2.52  
LINK         O   HIS A 614                 K     K A 801     1555   1555  2.86  
LINK         ND1 HIS A 614                ZN    ZN A 803     1555   1555  2.43  
LINK         O   PHE A 623                 K     K A 802     1555   1555  2.69  
LINK         O   ASP A 626                 K     K A 802     1555   1555  2.91  
LINK         O   VAL A 629                 K     K A 802     1555   1555  2.70  
LINK         OG  SER A 633                 K     K A 801     1555   1555  2.79  
LINK         O   LEU A 634                 K     K A 801     1555   1555  2.89  
LINK         O   TYR A 662                 K     K A 802     1555   1555  2.89  
LINK         OD2 ASP A 705                ZN    ZN A 803     1555   1555  1.99  
LINK         K     K A 802                 O   HOH A 914     1555   1555  2.94  
LINK         K     K A 802                 O   HOH A 902     1555   1555  2.98  
LINK        ZN    ZN A 803                 O16 F1Y A 804     1555   1555  2.01  
LINK        ZN    ZN A 803                 O   HOH A 903     1555   1555  2.23  
CISPEP   1 ARG A  569    PRO A  570          0         1.74                     
CISPEP   2 PHE A  643    PRO A  644          0         4.88                     
SITE     1 AC1  5 ASP A 610  ASP A 612  HIS A 614  SER A 633                    
SITE     2 AC1  5 LEU A 634                                                     
SITE     1 AC2  6 PHE A 623  ASP A 626  VAL A 629  TYR A 662                    
SITE     2 AC2  6 HOH A 902  HOH A 914                                          
SITE     1 AC3  5 ASP A 612  HIS A 614  ASP A 705  F1Y A 804                    
SITE     2 AC3  5 HOH A 903                                                     
SITE     1 AC4 16 SER A 531  HIS A 574  GLY A 582  PHE A 583                    
SITE     2 AC4 16 ASP A 612  HIS A 614  PHE A 643  ASP A 705                    
SITE     3 AC4 16 LEU A 712  GLY A 743  TYR A 745  SER A 796                    
SITE     4 AC4 16 ARG A 798   ZN A 803  EDO A 805  HOH A 903                    
SITE     1 AC5  5 ASN A 530  SER A 531  LEU A 787  LEU A 797                    
SITE     2 AC5  5 F1Y A 804                                                     
CRYST1   45.310   64.950  140.499  90.00  90.00  90.00 P 2 21 21     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022070  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015397  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007117        0.00000                         
ATOM      1  N   PRO A 442     -38.672  -9.993  13.262  1.00 65.62           N  
ATOM      2  CA  PRO A 442     -37.453 -10.605  12.726  1.00 67.17           C  
ATOM      3  C   PRO A 442     -36.710  -9.675  11.774  1.00 61.57           C  
ATOM      4  O   PRO A 442     -35.588  -9.979  11.377  1.00 65.65           O  
ATOM      5  CB  PRO A 442     -37.976 -11.837  11.978  1.00 67.05           C  
ATOM      6  CG  PRO A 442     -39.276 -12.151  12.626  1.00 71.70           C  
ATOM      7  CD  PRO A 442     -39.861 -10.826  13.017  1.00 70.30           C  
ATOM      8  N   ILE A 443     -37.328  -8.559  11.403  1.00 53.34           N  
ATOM      9  CA  ILE A 443     -36.714  -7.614  10.480  1.00 54.09           C  
ATOM     10  C   ILE A 443     -36.415  -6.325  11.232  1.00 45.86           C  
ATOM     11  O   ILE A 443     -37.045  -6.007  12.249  1.00 38.46           O  
ATOM     12  CB  ILE A 443     -37.602  -7.367   9.239  1.00 57.19           C  
ATOM     13  CG1 ILE A 443     -38.822  -6.505   9.584  1.00 50.99           C  
ATOM     14  CG2 ILE A 443     -38.058  -8.700   8.665  1.00 51.91           C  
ATOM     15  CD1 ILE A 443     -39.598  -5.973   8.357  1.00 54.51           C  
ATOM     16  N   THR A 444     -35.416  -5.597  10.743  1.00 44.84           N  
ATOM     17  CA  THR A 444     -34.924  -4.376  11.370  1.00 43.96           C  
ATOM     18  C   THR A 444     -35.307  -3.186  10.502  1.00 42.20           C  
ATOM     19  O   THR A 444     -34.895  -3.107   9.340  1.00 44.90           O  
ATOM     20  CB  THR A 444     -33.406  -4.432  11.554  1.00 41.22           C  
ATOM     21  OG1 THR A 444     -33.066  -5.468  12.484  1.00 41.86           O  
ATOM     22  CG2 THR A 444     -32.869  -3.097  12.060  1.00 39.37           C  
ATOM     23  N   GLY A 445     -36.087  -2.267  11.062  1.00 37.60           N  
ATOM     24  CA  GLY A 445     -36.395  -1.041  10.357  1.00 34.67           C  
ATOM     25  C   GLY A 445     -35.250  -0.047  10.430  1.00 37.87           C  
ATOM     26  O   GLY A 445     -34.461  -0.034  11.373  1.00 38.10           O  
ATOM     27  N   LEU A 446     -35.150   0.787   9.398  1.00 37.61           N  
ATOM     28  CA  LEU A 446     -34.170   1.868   9.366  1.00 33.99           C  
ATOM     29  C   LEU A 446     -34.840   3.094   8.772  1.00 39.70           C  
ATOM     30  O   LEU A 446     -35.371   3.030   7.659  1.00 41.54           O  
ATOM     31  CB  LEU A 446     -32.928   1.487   8.551  1.00 30.51           C  
ATOM     32  CG  LEU A 446     -31.787   2.511   8.523  1.00 37.08           C  
ATOM     33  CD1 LEU A 446     -30.437   1.811   8.577  1.00 37.32           C  
ATOM     34  CD2 LEU A 446     -31.867   3.419   7.298  1.00 36.23           C  
ATOM     35  N   VAL A 447     -34.816   4.203   9.502  1.00 38.12           N  
ATOM     36  CA  VAL A 447     -35.385   5.453   9.022  1.00 37.90           C  
ATOM     37  C   VAL A 447     -34.267   6.474   8.871  1.00 35.62           C  
ATOM     38  O   VAL A 447     -33.391   6.593   9.735  1.00 36.83           O  
ATOM     39  CB  VAL A 447     -36.509   5.971   9.947  1.00 38.15           C  
ATOM     40  CG1 VAL A 447     -35.987   6.291  11.339  1.00 32.31           C  
ATOM     41  CG2 VAL A 447     -37.184   7.181   9.325  1.00 39.07           C  
ATOM     42  N   TYR A 448     -34.281   7.182   7.746  1.00 41.95           N  
ATOM     43  CA  TYR A 448     -33.313   8.229   7.461  1.00 45.62           C  
ATOM     44  C   TYR A 448     -33.897   9.124   6.379  1.00 47.92           C  
ATOM     45  O   TYR A 448     -34.531   8.633   5.441  1.00 50.29           O  
ATOM     46  CB  TYR A 448     -31.966   7.650   7.008  1.00 42.34           C  
ATOM     47  CG  TYR A 448     -31.058   8.663   6.342  1.00 49.35           C  
ATOM     48  CD1 TYR A 448     -30.267   9.517   7.098  1.00 43.47           C  
ATOM     49  CD2 TYR A 448     -30.997   8.767   4.957  1.00 45.05           C  
ATOM     50  CE1 TYR A 448     -29.439  10.445   6.496  1.00 46.81           C  
ATOM     51  CE2 TYR A 448     -30.174   9.692   4.347  1.00 46.32           C  
ATOM     52  CZ  TYR A 448     -29.397  10.528   5.120  1.00 50.83           C  
ATOM     53  OH  TYR A 448     -28.575  11.451   4.515  1.00 54.07           O  
ATOM     54  N   ASP A 449     -33.685  10.431   6.515  1.00 47.63           N  
ATOM     55  CA  ASP A 449     -34.168  11.388   5.528  1.00 45.59           C  
ATOM     56  C   ASP A 449     -33.083  12.418   5.268  1.00 46.10           C  
ATOM     57  O   ASP A 449     -32.599  13.063   6.204  1.00 48.16           O  
ATOM     58  CB  ASP A 449     -35.460  12.066   5.992  1.00 45.31           C  
ATOM     59  CG  ASP A 449     -36.243  12.672   4.842  1.00 51.14           C  
ATOM     60  OD1 ASP A 449     -35.617  13.260   3.935  1.00 47.54           O  
ATOM     61  OD2 ASP A 449     -37.486  12.549   4.839  1.00 51.97           O  
ATOM     62  N   GLN A 450     -32.709  12.565   3.995  1.00 46.99           N  
ATOM     63  CA  GLN A 450     -31.722  13.565   3.598  1.00 52.24           C  
ATOM     64  C   GLN A 450     -32.129  14.962   4.053  1.00 47.59           C  
ATOM     65  O   GLN A 450     -31.280  15.771   4.449  1.00 44.80           O  
ATOM     66  CB  GLN A 450     -31.545  13.521   2.079  1.00 56.36           C  
ATOM     67  CG  GLN A 450     -30.559  14.520   1.512  1.00 62.68           C  
ATOM     68  CD  GLN A 450     -29.667  13.903   0.451  1.00 73.24           C  
ATOM     69  OE1 GLN A 450     -28.444  14.044   0.490  1.00 76.12           O  
ATOM     70  NE2 GLN A 450     -30.277  13.206  -0.501  1.00 70.45           N  
ATOM     71  N   ARG A 451     -33.434  15.250   4.029  1.00 43.72           N  
ATOM     72  CA  ARG A 451     -33.943  16.575   4.366  1.00 44.62           C  
ATOM     73  C   ARG A 451     -33.537  17.034   5.760  1.00 47.00           C  
ATOM     74  O   ARG A 451     -33.605  18.233   6.047  1.00 43.91           O  
ATOM     75  CB  ARG A 451     -35.468  16.593   4.261  1.00 45.09           C  
ATOM     76  CG  ARG A 451     -36.010  16.494   2.852  1.00 37.64           C  
ATOM     77  CD  ARG A 451     -37.522  16.585   2.872  1.00 43.15           C  
ATOM     78  NE  ARG A 451     -38.125  15.371   3.412  1.00 46.63           N  
ATOM     79  CZ  ARG A 451     -39.316  15.329   3.999  1.00 50.21           C  
ATOM     80  NH1 ARG A 451     -40.032  16.438   4.127  1.00 42.38           N  
ATOM     81  NH2 ARG A 451     -39.790  14.179   4.459  1.00 46.56           N  
ATOM     82  N   MET A 452     -33.127  16.119   6.636  1.00 50.96           N  
ATOM     83  CA  MET A 452     -32.718  16.511   7.978  1.00 46.88           C  
ATOM     84  C   MET A 452     -31.333  17.143   8.017  1.00 44.15           C  
ATOM     85  O   MET A 452     -30.852  17.469   9.108  1.00 40.07           O  
ATOM     86  CB  MET A 452     -32.776  15.304   8.918  1.00 45.87           C  
ATOM     87  CG  MET A 452     -34.136  15.120   9.572  1.00 45.41           C  
ATOM     88  SD  MET A 452     -34.232  13.701  10.676  1.00 42.21           S  
ATOM     89  CE  MET A 452     -33.620  12.401   9.607  1.00 43.01           C  
ATOM     90  N   MET A 453     -30.685  17.332   6.868  1.00 42.54           N  
ATOM     91  CA  MET A 453     -29.414  18.042   6.827  1.00 43.74           C  
ATOM     92  C   MET A 453     -29.574  19.544   6.623  1.00 45.15           C  
ATOM     93  O   MET A 453     -28.579  20.272   6.703  1.00 44.49           O  
ATOM     94  CB  MET A 453     -28.523  17.475   5.718  1.00 43.42           C  
ATOM     95  CG  MET A 453     -28.053  16.055   5.969  1.00 43.52           C  
ATOM     96  SD  MET A 453     -26.745  15.558   4.834  1.00 49.15           S  
ATOM     97  CE  MET A 453     -27.660  15.430   3.306  1.00 43.76           C  
ATOM     98  N   LEU A 454     -30.793  20.024   6.369  1.00 45.08           N  
ATOM     99  CA  LEU A 454     -31.015  21.442   6.108  1.00 43.67           C  
ATOM    100  C   LEU A 454     -30.866  22.306   7.354  1.00 49.00           C  
ATOM    101  O   LEU A 454     -30.860  23.536   7.236  1.00 49.93           O  
ATOM    102  CB  LEU A 454     -32.402  21.645   5.498  1.00 39.43           C  
ATOM    103  CG  LEU A 454     -32.683  20.817   4.243  1.00 40.43           C  
ATOM    104  CD1 LEU A 454     -34.113  21.018   3.772  1.00 36.88           C  
ATOM    105  CD2 LEU A 454     -31.695  21.168   3.140  1.00 40.71           C  
ATOM    106  N   HIS A 455     -30.754  21.699   8.531  1.00 43.74           N  
ATOM    107  CA  HIS A 455     -30.517  22.423   9.772  1.00 43.44           C  
ATOM    108  C   HIS A 455     -29.015  22.634   9.928  1.00 46.39           C  
ATOM    109  O   HIS A 455     -28.247  21.666   9.928  1.00 44.14           O  
ATOM    110  CB  HIS A 455     -31.098  21.642  10.950  1.00 39.24           C  
ATOM    111  CG  HIS A 455     -30.515  22.012  12.278  1.00 42.16           C  
ATOM    112  ND1 HIS A 455     -30.868  23.161  12.951  1.00 40.47           N  
ATOM    113  CD2 HIS A 455     -29.618  21.374  13.066  1.00 44.20           C  
ATOM    114  CE1 HIS A 455     -30.207  23.220  14.093  1.00 41.17           C  
ATOM    115  NE2 HIS A 455     -29.442  22.147  14.188  1.00 42.07           N  
ATOM    116  N   HIS A 456     -28.593  23.893  10.046  1.00 44.34           N  
ATOM    117  CA  HIS A 456     -27.171  24.205  10.018  1.00 45.41           C  
ATOM    118  C   HIS A 456     -26.888  25.466  10.822  1.00 44.65           C  
ATOM    119  O   HIS A 456     -27.793  26.225  11.182  1.00 39.68           O  
ATOM    120  CB  HIS A 456     -26.667  24.367   8.579  1.00 49.05           C  
ATOM    121  CG  HIS A 456     -27.276  25.523   7.847  1.00 55.74           C  
ATOM    122  ND1 HIS A 456     -28.616  25.580   7.526  1.00 56.36           N  
ATOM    123  CD2 HIS A 456     -26.728  26.668   7.375  1.00 50.60           C  
ATOM    124  CE1 HIS A 456     -28.865  26.707   6.883  1.00 53.97           C  
ATOM    125  NE2 HIS A 456     -27.737  27.387   6.782  1.00 50.39           N  
ATOM    126  N   ASN A 457     -25.601  25.674  11.102  1.00 45.33           N  
ATOM    127  CA  ASN A 457     -25.111  26.844  11.823  1.00 50.37           C  
ATOM    128  C   ASN A 457     -24.504  27.805  10.806  1.00 55.94           C  
ATOM    129  O   ASN A 457     -23.441  27.531  10.239  1.00 54.88           O  
ATOM    130  CB  ASN A 457     -24.086  26.432  12.879  1.00 46.56           C  
ATOM    131  CG  ASN A 457     -23.766  27.548  13.857  1.00 50.48           C  
ATOM    132  OD1 ASN A 457     -23.841  28.729  13.520  1.00 60.26           O  
ATOM    133  ND2 ASN A 457     -23.401  27.175  15.079  1.00 45.38           N  
ATOM    134  N   MET A 458     -25.177  28.935  10.581  1.00 53.95           N  
ATOM    135  CA  MET A 458     -24.721  29.886   9.575  1.00 54.77           C  
ATOM    136  C   MET A 458     -23.544  30.723  10.058  1.00 55.57           C  
ATOM    137  O   MET A 458     -22.748  31.194   9.238  1.00 55.01           O  
ATOM    138  CB  MET A 458     -25.874  30.797   9.160  1.00 46.79           C  
ATOM    139  CG  MET A 458     -27.227  30.114   9.180  1.00 52.38           C  
ATOM    140  SD  MET A 458     -28.551  31.239   8.706  1.00 80.47           S  
ATOM    141  CE  MET A 458     -29.040  31.875  10.304  1.00 54.12           C  
ATOM    142  N   TRP A 459     -23.415  30.915  11.371  1.00 54.30           N  
ATOM    143  CA  TRP A 459     -22.341  31.725  11.928  1.00 50.66           C  
ATOM    144  C   TRP A 459     -21.062  30.937  12.172  1.00 60.61           C  
ATOM    145  O   TRP A 459     -19.982  31.538  12.222  1.00 60.11           O  
ATOM    146  CB  TRP A 459     -22.811  32.370  13.232  1.00 51.57           C  
ATOM    147  CG  TRP A 459     -24.097  33.108  13.057  1.00 62.05           C  
ATOM    148  CD1 TRP A 459     -24.259  34.372  12.565  1.00 61.08           C  
ATOM    149  CD2 TRP A 459     -25.412  32.616  13.339  1.00 62.11           C  
ATOM    150  NE1 TRP A 459     -25.592  34.702  12.539  1.00 62.00           N  
ATOM    151  CE2 TRP A 459     -26.321  33.641  13.009  1.00 64.89           C  
ATOM    152  CE3 TRP A 459     -25.908  31.411  13.847  1.00 55.28           C  
ATOM    153  CZ2 TRP A 459     -27.696  33.497  13.167  1.00 59.21           C  
ATOM    154  CZ3 TRP A 459     -27.274  31.271  14.006  1.00 55.54           C  
ATOM    155  CH2 TRP A 459     -28.152  32.309  13.670  1.00 58.07           C  
ATOM    156  N   ASP A 460     -21.154  29.617  12.325  1.00 60.49           N  
ATOM    157  CA  ASP A 460     -19.990  28.743  12.449  1.00 55.76           C  
ATOM    158  C   ASP A 460     -20.211  27.551  11.529  1.00 57.56           C  
ATOM    159  O   ASP A 460     -21.083  26.715  11.790  1.00 53.27           O  
ATOM    160  CB  ASP A 460     -19.780  28.293  13.897  1.00 52.86           C  
ATOM    161  CG  ASP A 460     -18.496  27.495  14.091  1.00 56.17           C  
ATOM    162  OD1 ASP A 460     -17.845  27.124  13.090  1.00 56.45           O  
ATOM    163  OD2 ASP A 460     -18.131  27.237  15.257  1.00 58.22           O  
ATOM    164  N   SER A 461     -19.422  27.471  10.458  1.00 59.66           N  
ATOM    165  CA  SER A 461     -19.557  26.375   9.508  1.00 56.73           C  
ATOM    166  C   SER A 461     -18.959  25.074  10.022  1.00 57.15           C  
ATOM    167  O   SER A 461     -19.307  24.005   9.511  1.00 58.10           O  
ATOM    168  CB  SER A 461     -18.902  26.746   8.177  1.00 58.62           C  
ATOM    169  OG  SER A 461     -19.534  26.085   7.095  1.00 67.16           O  
ATOM    170  N   HIS A 462     -18.076  25.140  11.017  1.00 61.94           N  
ATOM    171  CA  HIS A 462     -17.388  23.964  11.533  1.00 63.38           C  
ATOM    172  C   HIS A 462     -17.882  23.551  12.913  1.00 61.79           C  
ATOM    173  O   HIS A 462     -17.252  22.705  13.557  1.00 59.46           O  
ATOM    174  CB  HIS A 462     -15.879  24.213  11.562  1.00 69.62           C  
ATOM    175  CG  HIS A 462     -15.302  24.568  10.227  1.00 73.45           C  
ATOM    176  ND1 HIS A 462     -14.748  23.629   9.383  1.00 76.52           N  
ATOM    177  CD2 HIS A 462     -15.200  25.757   9.587  1.00 66.26           C  
ATOM    178  CE1 HIS A 462     -14.325  24.226   8.283  1.00 72.34           C  
ATOM    179  NE2 HIS A 462     -14.588  25.517   8.381  1.00 71.05           N  
ATOM    180  N   HIS A 463     -18.983  24.133  13.382  1.00 57.23           N  
ATOM    181  CA  HIS A 463     -19.595  23.716  14.633  1.00 51.77           C  
ATOM    182  C   HIS A 463     -19.850  22.211  14.600  1.00 53.25           C  
ATOM    183  O   HIS A 463     -20.444  21.711  13.633  1.00 52.81           O  
ATOM    184  CB  HIS A 463     -20.901  24.484  14.852  1.00 52.30           C  
ATOM    185  CG  HIS A 463     -21.621  24.120  16.113  1.00 52.82           C  
ATOM    186  ND1 HIS A 463     -22.316  22.940  16.261  1.00 50.87           N  
ATOM    187  CD2 HIS A 463     -21.762  24.788  17.283  1.00 54.46           C  
ATOM    188  CE1 HIS A 463     -22.850  22.894  17.468  1.00 51.07           C  
ATOM    189  NE2 HIS A 463     -22.529  24.003  18.108  1.00 51.97           N  
ATOM    190  N   PRO A 464     -19.438  21.460  15.627  1.00 55.24           N  
ATOM    191  CA  PRO A 464     -19.331  19.996  15.484  1.00 49.87           C  
ATOM    192  C   PRO A 464     -20.635  19.291  15.141  1.00 43.59           C  
ATOM    193  O   PRO A 464     -20.589  18.191  14.576  1.00 40.94           O  
ATOM    194  CB  PRO A 464     -18.797  19.547  16.852  1.00 48.39           C  
ATOM    195  CG  PRO A 464     -19.176  20.645  17.791  1.00 50.28           C  
ATOM    196  CD  PRO A 464     -19.095  21.910  16.988  1.00 53.03           C  
ATOM    197  N   GLU A 465     -21.791  19.878  15.452  1.00 44.10           N  
ATOM    198  CA  GLU A 465     -23.079  19.273  15.110  1.00 41.53           C  
ATOM    199  C   GLU A 465     -23.356  19.485  13.620  1.00 40.05           C  
ATOM    200  O   GLU A 465     -24.267  20.207  13.209  1.00 42.27           O  
ATOM    201  CB  GLU A 465     -24.186  19.851  15.980  1.00 40.17           C  
ATOM    202  CG  GLU A 465     -25.291  18.863  16.314  1.00 44.82           C  
ATOM    203  CD  GLU A 465     -26.276  18.684  15.177  1.00 44.90           C  
ATOM    204  OE1 GLU A 465     -26.111  17.731  14.386  1.00 49.05           O  
ATOM    205  OE2 GLU A 465     -27.217  19.501  15.074  1.00 48.97           O  
ATOM    206  N   LEU A 466     -22.537  18.821  12.797  1.00 38.90           N  
ATOM    207  CA  LEU A 466     -22.589  18.990  11.353  1.00 44.35           C  
ATOM    208  C   LEU A 466     -23.766  18.227  10.749  1.00 46.43           C  
ATOM    209  O   LEU A 466     -24.198  17.204  11.288  1.00 44.22           O  
ATOM    210  CB  LEU A 466     -21.294  18.504  10.708  1.00 44.32           C  
ATOM    211  CG  LEU A 466     -19.960  19.022  11.244  1.00 44.85           C  
ATOM    212  CD1 LEU A 466     -18.820  18.140  10.756  1.00 39.82           C  
ATOM    213  CD2 LEU A 466     -19.736  20.466  10.823  1.00 49.00           C  
ATOM    214  N   PRO A 467     -24.301  18.709   9.625  1.00 48.89           N  
ATOM    215  CA  PRO A 467     -25.352  17.945   8.936  1.00 48.56           C  
ATOM    216  C   PRO A 467     -24.864  16.625   8.367  1.00 44.11           C  
ATOM    217  O   PRO A 467     -25.666  15.695   8.217  1.00 39.23           O  
ATOM    218  CB  PRO A 467     -25.809  18.902   7.824  1.00 50.39           C  
ATOM    219  CG  PRO A 467     -25.405  20.261   8.294  1.00 45.18           C  
ATOM    220  CD  PRO A 467     -24.130  20.057   9.056  1.00 47.74           C  
ATOM    221  N   GLN A 468     -23.573  16.511   8.045  1.00 46.28           N  
ATOM    222  CA  GLN A 468     -23.059  15.281   7.453  1.00 44.43           C  
ATOM    223  C   GLN A 468     -23.143  14.096   8.405  1.00 45.70           C  
ATOM    224  O   GLN A 468     -23.076  12.947   7.950  1.00 43.73           O  
ATOM    225  CB  GLN A 468     -21.611  15.472   7.003  1.00 43.14           C  
ATOM    226  CG  GLN A 468     -21.428  16.501   5.908  1.00 51.59           C  
ATOM    227  CD  GLN A 468     -20.506  17.623   6.326  1.00 49.51           C  
ATOM    228  OE1 GLN A 468     -20.842  18.427   7.194  1.00 50.94           O  
ATOM    229  NE2 GLN A 468     -19.329  17.679   5.714  1.00 56.17           N  
ATOM    230  N   ARG A 469     -23.293  14.354   9.708  1.00 42.37           N  
ATOM    231  CA  ARG A 469     -23.323  13.283  10.700  1.00 40.80           C  
ATOM    232  C   ARG A 469     -24.319  12.195  10.322  1.00 41.51           C  
ATOM    233  O   ARG A 469     -23.990  11.005  10.332  1.00 45.72           O  
ATOM    234  CB  ARG A 469     -23.656  13.859  12.077  1.00 39.60           C  
ATOM    235  CG  ARG A 469     -22.504  14.603  12.722  1.00 40.94           C  
ATOM    236  CD  ARG A 469     -22.933  15.285  14.008  1.00 40.24           C  
ATOM    237  NE  ARG A 469     -23.583  14.363  14.933  1.00 39.72           N  
ATOM    238  CZ  ARG A 469     -24.847  14.470  15.329  1.00 35.95           C  
ATOM    239  NH1 ARG A 469     -25.602  15.462  14.880  1.00 45.17           N  
ATOM    240  NH2 ARG A 469     -25.356  13.585  16.176  1.00 36.82           N  
ATOM    241  N   ILE A 470     -25.544  12.587   9.970  1.00 35.55           N  
ATOM    242  CA  ILE A 470     -26.545  11.585   9.629  1.00 42.37           C  
ATOM    243  C   ILE A 470     -26.284  10.998   8.248  1.00 45.46           C  
ATOM    244  O   ILE A 470     -26.601   9.829   7.996  1.00 47.37           O  
ATOM    245  CB  ILE A 470     -27.958  12.181   9.734  1.00 41.98           C  
ATOM    246  CG1 ILE A 470     -28.106  13.375   8.790  1.00 36.97           C  
ATOM    247  CG2 ILE A 470     -28.255  12.578  11.172  1.00 38.52           C  
ATOM    248  CD1 ILE A 470     -29.536  13.780   8.554  1.00 38.36           C  
ATOM    249  N   SER A 471     -25.700  11.779   7.335  1.00 46.00           N  
ATOM    250  CA  SER A 471     -25.432  11.258   5.998  1.00 42.06           C  
ATOM    251  C   SER A 471     -24.287  10.256   6.030  1.00 42.03           C  
ATOM    252  O   SER A 471     -24.414   9.135   5.519  1.00 52.51           O  
ATOM    253  CB  SER A 471     -25.122  12.404   5.032  1.00 43.31           C  
ATOM    254  OG  SER A 471     -23.762  12.798   5.113  1.00 42.92           O  
ATOM    255  N   ARG A 472     -23.165  10.642   6.644  1.00 39.91           N  
ATOM    256  CA  ARG A 472     -22.004   9.766   6.753  1.00 42.02           C  
ATOM    257  C   ARG A 472     -22.394   8.401   7.305  1.00 47.04           C  
ATOM    258  O   ARG A 472     -22.165   7.368   6.663  1.00 44.25           O  
ATOM    259  CB  ARG A 472     -20.945  10.428   7.636  1.00 42.15           C  
ATOM    260  CG  ARG A 472     -20.159  11.517   6.931  1.00 46.61           C  
ATOM    261  CD  ARG A 472     -19.141  10.913   5.981  1.00 42.45           C  
ATOM    262  NE  ARG A 472     -18.234  10.005   6.676  1.00 40.40           N  
ATOM    263  CZ  ARG A 472     -17.108  10.385   7.269  1.00 45.03           C  
ATOM    264  NH1 ARG A 472     -16.741  11.659   7.246  1.00 51.24           N  
ATOM    265  NH2 ARG A 472     -16.344   9.491   7.882  1.00 47.22           N  
ATOM    266  N   ILE A 473     -22.999   8.388   8.499  1.00 44.44           N  
ATOM    267  CA  ILE A 473     -23.522   7.150   9.076  1.00 44.98           C  
ATOM    268  C   ILE A 473     -24.320   6.382   8.034  1.00 46.88           C  
ATOM    269  O   ILE A 473     -24.053   5.204   7.763  1.00 51.81           O  
ATOM    270  CB  ILE A 473     -24.381   7.454  10.318  1.00 46.26           C  
ATOM    271  CG1 ILE A 473     -23.536   8.069  11.435  1.00 40.07           C  
ATOM    272  CG2 ILE A 473     -25.081   6.190  10.805  1.00 36.68           C  
ATOM    273  CD1 ILE A 473     -24.366   8.655  12.560  1.00 30.09           C  
ATOM    274  N   PHE A 474     -25.291   7.056   7.409  1.00 43.88           N  
ATOM    275  CA  PHE A 474     -26.130   6.407   6.408  1.00 45.35           C  
ATOM    276  C   PHE A 474     -25.282   5.754   5.326  1.00 48.95           C  
ATOM    277  O   PHE A 474     -25.488   4.585   4.978  1.00 49.97           O  
ATOM    278  CB  PHE A 474     -27.094   7.426   5.798  1.00 47.06           C  
ATOM    279  CG  PHE A 474     -28.041   6.841   4.789  1.00 48.45           C  
ATOM    280  CD1 PHE A 474     -29.053   5.982   5.184  1.00 51.32           C  
ATOM    281  CD2 PHE A 474     -27.924   7.158   3.446  1.00 47.54           C  
ATOM    282  CE1 PHE A 474     -29.929   5.447   4.257  1.00 50.34           C  
ATOM    283  CE2 PHE A 474     -28.797   6.626   2.515  1.00 47.55           C  
ATOM    284  CZ  PHE A 474     -29.800   5.771   2.921  1.00 51.45           C  
ATOM    285  N   SER A 475     -24.290   6.487   4.810  1.00 50.54           N  
ATOM    286  CA  SER A 475     -23.440   5.933   3.761  1.00 52.69           C  
ATOM    287  C   SER A 475     -22.765   4.652   4.226  1.00 52.84           C  
ATOM    288  O   SER A 475     -22.703   3.669   3.478  1.00 58.16           O  
ATOM    289  CB  SER A 475     -22.399   6.963   3.321  1.00 56.31           C  
ATOM    290  OG  SER A 475     -23.009   8.051   2.653  1.00 61.12           O  
ATOM    291  N   ARG A 476     -22.280   4.636   5.472  1.00 49.78           N  
ATOM    292  CA  ARG A 476     -21.675   3.424   6.012  1.00 50.24           C  
ATOM    293  C   ARG A 476     -22.659   2.264   5.952  1.00 48.40           C  
ATOM    294  O   ARG A 476     -22.320   1.168   5.488  1.00 53.96           O  
ATOM    295  CB  ARG A 476     -21.202   3.667   7.446  1.00 46.93           C  
ATOM    296  CG  ARG A 476     -20.047   2.781   7.883  1.00 47.56           C  
ATOM    297  CD  ARG A 476     -18.727   3.246   7.287  1.00 51.85           C  
ATOM    298  NE  ARG A 476     -17.612   2.397   7.698  1.00 64.43           N  
ATOM    299  CZ  ARG A 476     -17.147   1.370   6.991  1.00 65.55           C  
ATOM    300  NH1 ARG A 476     -17.698   1.055   5.827  1.00 60.76           N  
ATOM    301  NH2 ARG A 476     -16.128   0.656   7.449  1.00 68.44           N  
ATOM    302  N   HIS A 477     -23.907   2.509   6.367  1.00 45.68           N  
ATOM    303  CA  HIS A 477     -24.915   1.454   6.343  1.00 50.45           C  
ATOM    304  C   HIS A 477     -25.130   0.921   4.935  1.00 53.77           C  
ATOM    305  O   HIS A 477     -25.502  -0.246   4.763  1.00 44.73           O  
ATOM    306  CB  HIS A 477     -26.232   1.969   6.925  1.00 43.12           C  
ATOM    307  CG  HIS A 477     -26.239   2.054   8.419  1.00 48.15           C  
ATOM    308  ND1 HIS A 477     -25.368   2.857   9.124  1.00 48.52           N  
ATOM    309  CD2 HIS A 477     -27.012   1.435   9.343  1.00 44.05           C  
ATOM    310  CE1 HIS A 477     -25.605   2.730  10.418  1.00 44.32           C  
ATOM    311  NE2 HIS A 477     -26.597   1.873  10.577  1.00 48.52           N  
ATOM    312  N   GLU A 478     -24.890   1.750   3.916  1.00 55.54           N  
ATOM    313  CA  GLU A 478     -25.016   1.267   2.548  1.00 53.45           C  
ATOM    314  C   GLU A 478     -23.784   0.479   2.124  1.00 56.08           C  
ATOM    315  O   GLU A 478     -23.904  -0.531   1.422  1.00 56.60           O  
ATOM    316  CB  GLU A 478     -25.259   2.435   1.592  1.00 47.64           C  
ATOM    317  N   GLU A 479     -22.594   0.904   2.559  1.00 58.86           N  
ATOM    318  CA  GLU A 479     -21.370   0.298   2.050  1.00 58.16           C  
ATOM    319  C   GLU A 479     -20.951  -0.944   2.826  1.00 54.13           C  
ATOM    320  O   GLU A 479     -20.271  -1.810   2.264  1.00 51.02           O  
ATOM    321  CB  GLU A 479     -20.236   1.328   2.028  1.00 56.10           C  
ATOM    322  CG  GLU A 479     -19.726   1.760   3.382  1.00 55.11           C  
ATOM    323  CD  GLU A 479     -18.750   2.917   3.281  1.00 66.37           C  
ATOM    324  OE1 GLU A 479     -18.958   3.798   2.418  1.00 67.90           O  
ATOM    325  OE2 GLU A 479     -17.771   2.942   4.056  1.00 69.39           O  
ATOM    326  N   LEU A 480     -21.342  -1.061   4.095  1.00 54.72           N  
ATOM    327  CA  LEU A 480     -21.269  -2.348   4.777  1.00 53.15           C  
ATOM    328  C   LEU A 480     -22.431  -3.259   4.407  1.00 51.23           C  
ATOM    329  O   LEU A 480     -22.540  -4.357   4.964  1.00 50.81           O  
ATOM    330  CB  LEU A 480     -21.231  -2.155   6.296  1.00 50.36           C  
ATOM    331  CG  LEU A 480     -20.008  -1.450   6.881  1.00 51.12           C  
ATOM    332  CD1 LEU A 480     -20.343  -0.871   8.243  1.00 49.08           C  
ATOM    333  CD2 LEU A 480     -18.834  -2.407   6.981  1.00 43.10           C  
ATOM    334  N   ARG A 481     -23.292  -2.818   3.488  1.00 52.98           N  
ATOM    335  CA  ARG A 481     -24.446  -3.580   3.013  1.00 50.63           C  
ATOM    336  C   ARG A 481     -25.389  -3.958   4.153  1.00 48.57           C  
ATOM    337  O   ARG A 481     -26.032  -5.010   4.120  1.00 49.74           O  
ATOM    338  CB  ARG A 481     -24.008  -4.819   2.224  1.00 51.58           C  
ATOM    339  CG  ARG A 481     -23.544  -4.484   0.810  1.00 55.83           C  
ATOM    340  CD  ARG A 481     -22.969  -5.685   0.075  1.00 57.81           C  
ATOM    341  NE  ARG A 481     -22.035  -6.445   0.898  1.00 64.61           N  
ATOM    342  CZ  ARG A 481     -22.244  -7.693   1.304  1.00 65.52           C  
ATOM    343  NH1 ARG A 481     -23.358  -8.325   0.962  1.00 61.72           N  
ATOM    344  NH2 ARG A 481     -21.340  -8.310   2.053  1.00 62.66           N  
ATOM    345  N   LEU A 482     -25.478  -3.095   5.168  1.00 50.13           N  
ATOM    346  CA  LEU A 482     -26.485  -3.260   6.211  1.00 42.04           C  
ATOM    347  C   LEU A 482     -27.839  -2.719   5.773  1.00 42.50           C  
ATOM    348  O   LEU A 482     -28.877  -3.258   6.173  1.00 43.82           O  
ATOM    349  CB  LEU A 482     -26.037  -2.558   7.495  1.00 38.95           C  
ATOM    350  CG  LEU A 482     -24.684  -2.960   8.087  1.00 41.83           C  
ATOM    351  CD1 LEU A 482     -24.164  -1.882   9.028  1.00 42.88           C  
ATOM    352  CD2 LEU A 482     -24.793  -4.291   8.808  1.00 43.84           C  
ATOM    353  N   LEU A 483     -27.841  -1.663   4.956  1.00 46.21           N  
ATOM    354  CA  LEU A 483     -29.091  -1.077   4.484  1.00 46.00           C  
ATOM    355  C   LEU A 483     -29.876  -2.052   3.618  1.00 49.39           C  
ATOM    356  O   LEU A 483     -31.113  -2.035   3.629  1.00 47.27           O  
ATOM    357  CB  LEU A 483     -28.797   0.207   3.706  1.00 49.99           C  
ATOM    358  CG  LEU A 483     -29.988   0.979   3.139  1.00 47.94           C  
ATOM    359  CD1 LEU A 483     -31.058   1.189   4.200  1.00 44.42           C  
ATOM    360  CD2 LEU A 483     -29.530   2.306   2.559  1.00 52.14           C  
ATOM    361  N   SER A 484     -29.179  -2.905   2.860  1.00 54.89           N  
ATOM    362  CA  SER A 484     -29.860  -3.898   2.038  1.00 47.93           C  
ATOM    363  C   SER A 484     -30.695  -4.846   2.887  1.00 51.21           C  
ATOM    364  O   SER A 484     -31.743  -5.324   2.438  1.00 53.37           O  
ATOM    365  CB  SER A 484     -28.840  -4.693   1.219  1.00 47.63           C  
ATOM    366  OG  SER A 484     -27.752  -3.879   0.816  1.00 54.37           O  
ATOM    367  N   ARG A 485     -30.257  -5.117   4.115  1.00 49.58           N  
ATOM    368  CA  ARG A 485     -30.898  -6.091   4.987  1.00 43.82           C  
ATOM    369  C   ARG A 485     -31.965  -5.480   5.886  1.00 44.97           C  
ATOM    370  O   ARG A 485     -32.501  -6.183   6.748  1.00 42.38           O  
ATOM    371  CB  ARG A 485     -29.841  -6.789   5.848  1.00 38.44           C  
ATOM    372  CG  ARG A 485     -28.558  -7.133   5.102  1.00 37.61           C  
ATOM    373  CD  ARG A 485     -27.428  -7.484   6.059  1.00 39.10           C  
ATOM    374  NE  ARG A 485     -27.856  -8.427   7.089  1.00 46.04           N  
ATOM    375  CZ  ARG A 485     -27.090  -8.834   8.096  1.00 45.27           C  
ATOM    376  NH1 ARG A 485     -25.848  -8.384   8.214  1.00 44.47           N  
ATOM    377  NH2 ARG A 485     -27.566  -9.695   8.987  1.00 39.44           N  
ATOM    378  N   CYS A 486     -32.289  -4.201   5.708  1.00 47.46           N  
ATOM    379  CA  CYS A 486     -33.238  -3.499   6.557  1.00 43.46           C  
ATOM    380  C   CYS A 486     -34.497  -3.134   5.782  1.00 42.32           C  
ATOM    381  O   CYS A 486     -34.508  -3.083   4.549  1.00 44.75           O  
ATOM    382  CB  CYS A 486     -32.613  -2.228   7.145  1.00 40.02           C  
ATOM    383  SG  CYS A 486     -31.388  -2.513   8.441  1.00 46.35           S  
ATOM    384  N   HIS A 487     -35.566  -2.879   6.531  1.00 38.79           N  
ATOM    385  CA  HIS A 487     -36.816  -2.370   5.983  1.00 40.80           C  
ATOM    386  C   HIS A 487     -36.845  -0.858   6.171  1.00 44.89           C  
ATOM    387  O   HIS A 487     -36.821  -0.370   7.307  1.00 43.97           O  
ATOM    388  CB  HIS A 487     -38.019  -3.021   6.663  1.00 42.91           C  
ATOM    389  CG  HIS A 487     -39.336  -2.460   6.227  1.00 47.44           C  
ATOM    390  ND1 HIS A 487     -39.938  -2.812   5.038  1.00 50.64           N  
ATOM    391  CD2 HIS A 487     -40.167  -1.571   6.821  1.00 48.51           C  
ATOM    392  CE1 HIS A 487     -41.083  -2.165   4.918  1.00 52.66           C  
ATOM    393  NE2 HIS A 487     -41.247  -1.405   5.987  1.00 50.45           N  
ATOM    394  N   ARG A 488     -36.893  -0.123   5.063  1.00 46.98           N  
ATOM    395  CA  ARG A 488     -36.828   1.332   5.120  1.00 44.49           C  
ATOM    396  C   ARG A 488     -38.146   1.900   5.634  1.00 44.21           C  
ATOM    397  O   ARG A 488     -39.202   1.689   5.027  1.00 42.82           O  
ATOM    398  CB  ARG A 488     -36.496   1.901   3.743  1.00 40.41           C  
ATOM    399  CG  ARG A 488     -36.249   3.398   3.740  1.00 53.18           C  
ATOM    400  CD  ARG A 488     -35.027   3.759   4.566  1.00 47.83           C  
ATOM    401  NE  ARG A 488     -34.563   5.113   4.286  1.00 49.55           N  
ATOM    402  CZ  ARG A 488     -33.725   5.424   3.303  1.00 50.04           C  
ATOM    403  NH1 ARG A 488     -33.353   6.683   3.118  1.00 54.37           N  
ATOM    404  NH2 ARG A 488     -33.258   4.474   2.505  1.00 50.40           N  
ATOM    405  N   ILE A 489     -38.083   2.615   6.746  1.00 42.17           N  
ATOM    406  CA  ILE A 489     -39.246   3.257   7.352  1.00 40.90           C  
ATOM    407  C   ILE A 489     -39.294   4.698   6.870  1.00 43.80           C  
ATOM    408  O   ILE A 489     -38.255   5.379   6.887  1.00 44.58           O  
ATOM    409  CB  ILE A 489     -39.187   3.189   8.890  1.00 41.59           C  
ATOM    410  CG1 ILE A 489     -39.232   1.734   9.357  1.00 39.94           C  
ATOM    411  CG2 ILE A 489     -40.318   3.996   9.514  1.00 34.14           C  
ATOM    412  CD1 ILE A 489     -39.339   1.572  10.855  1.00 39.07           C  
ATOM    413  N   PRO A 490     -40.443   5.202   6.424  1.00 44.39           N  
ATOM    414  CA  PRO A 490     -40.499   6.574   5.912  1.00 41.47           C  
ATOM    415  C   PRO A 490     -40.480   7.602   7.031  1.00 42.40           C  
ATOM    416  O   PRO A 490     -41.109   7.428   8.078  1.00 37.31           O  
ATOM    417  CB  PRO A 490     -41.831   6.611   5.154  1.00 38.75           C  
ATOM    418  CG  PRO A 490     -42.679   5.611   5.867  1.00 42.45           C  
ATOM    419  CD  PRO A 490     -41.744   4.515   6.311  1.00 40.04           C  
ATOM    420  N   ALA A 491     -39.740   8.682   6.799  1.00 45.44           N  
ATOM    421  CA  ALA A 491     -39.788   9.821   7.697  1.00 37.20           C  
ATOM    422  C   ALA A 491     -41.101  10.576   7.513  1.00 36.41           C  
ATOM    423  O   ALA A 491     -41.791  10.439   6.500  1.00 44.06           O  
ATOM    424  CB  ALA A 491     -38.603  10.754   7.448  1.00 37.05           C  
ATOM    425  N   ARG A 492     -41.447  11.377   8.516  1.00 36.36           N  
ATOM    426  CA  ARG A 492     -42.635  12.214   8.438  1.00 38.98           C  
ATOM    427  C   ARG A 492     -42.503  13.339   9.453  1.00 41.32           C  
ATOM    428  O   ARG A 492     -41.606  13.341  10.298  1.00 39.82           O  
ATOM    429  CB  ARG A 492     -43.915  11.404   8.671  1.00 34.24           C  
ATOM    430  CG  ARG A 492     -44.142  10.958  10.106  1.00 36.86           C  
ATOM    431  CD  ARG A 492     -45.628  10.796  10.373  1.00 36.14           C  
ATOM    432  NE  ARG A 492     -45.906  10.142  11.646  1.00 37.45           N  
ATOM    433  CZ  ARG A 492     -46.263  10.783  12.755  1.00 42.35           C  
ATOM    434  NH1 ARG A 492     -46.382  12.104  12.755  1.00 34.76           N  
ATOM    435  NH2 ARG A 492     -46.502  10.100  13.866  1.00 44.04           N  
ATOM    436  N   LEU A 493     -43.413  14.303   9.351  1.00 36.18           N  
ATOM    437  CA  LEU A 493     -43.419  15.458  10.236  1.00 34.58           C  
ATOM    438  C   LEU A 493     -44.272  15.167  11.462  1.00 38.83           C  
ATOM    439  O   LEU A 493     -45.404  14.688  11.340  1.00 38.96           O  
ATOM    440  CB  LEU A 493     -43.952  16.693   9.512  1.00 35.09           C  
ATOM    441  CG  LEU A 493     -43.058  17.338   8.454  1.00 38.62           C  
ATOM    442  CD1 LEU A 493     -43.462  18.786   8.240  1.00 32.13           C  
ATOM    443  CD2 LEU A 493     -41.602  17.244   8.862  1.00 38.52           C  
ATOM    444  N   ALA A 494     -43.727  15.457  12.638  1.00 36.99           N  
ATOM    445  CA  ALA A 494     -44.517  15.373  13.855  1.00 36.77           C  
ATOM    446  C   ALA A 494     -45.510  16.527  13.909  1.00 43.17           C  
ATOM    447  O   ALA A 494     -45.173  17.673  13.600  1.00 41.23           O  
ATOM    448  CB  ALA A 494     -43.612  15.399  15.085  1.00 36.52           C  
ATOM    449  N   THR A 495     -46.744  16.217  14.289  1.00 43.91           N  
ATOM    450  CA  THR A 495     -47.749  17.256  14.430  1.00 43.40           C  
ATOM    451  C   THR A 495     -47.528  18.031  15.725  1.00 43.83           C  
ATOM    452  O   THR A 495     -46.840  17.580  16.643  1.00 47.17           O  
ATOM    453  CB  THR A 495     -49.155  16.657  14.404  1.00 43.03           C  
ATOM    454  OG1 THR A 495     -49.502  16.191  15.713  1.00 47.27           O  
ATOM    455  CG2 THR A 495     -49.218  15.496  13.424  1.00 39.57           C  
ATOM    456  N   GLU A 496     -48.121  19.225  15.786  1.00 47.79           N  
ATOM    457  CA  GLU A 496     -47.965  20.057  16.973  1.00 41.15           C  
ATOM    458  C   GLU A 496     -48.726  19.482  18.161  1.00 46.44           C  
ATOM    459  O   GLU A 496     -48.301  19.654  19.311  1.00 48.31           O  
ATOM    460  CB  GLU A 496     -48.415  21.485  16.670  1.00 46.34           C  
ATOM    461  CG  GLU A 496     -47.637  22.125  15.528  1.00 53.81           C  
ATOM    462  CD  GLU A 496     -48.095  23.535  15.216  1.00 57.32           C  
ATOM    463  OE1 GLU A 496     -48.424  24.280  16.164  1.00 52.42           O  
ATOM    464  OE2 GLU A 496     -48.123  23.898  14.021  1.00 58.11           O  
ATOM    465  N   GLU A 497     -49.843  18.796  17.908  1.00 46.12           N  
ATOM    466  CA  GLU A 497     -50.501  18.049  18.973  1.00 50.82           C  
ATOM    467  C   GLU A 497     -49.602  16.935  19.495  1.00 52.07           C  
ATOM    468  O   GLU A 497     -49.670  16.583  20.678  1.00 54.95           O  
ATOM    469  CB  GLU A 497     -51.830  17.479  18.472  1.00 50.01           C  
ATOM    470  CG  GLU A 497     -52.665  16.791  19.543  1.00 49.04           C  
ATOM    471  N   GLU A 498     -48.749  16.379  18.629  1.00 48.36           N  
ATOM    472  CA  GLU A 498     -47.789  15.371  19.067  1.00 40.96           C  
ATOM    473  C   GLU A 498     -46.655  16.000  19.869  1.00 42.36           C  
ATOM    474  O   GLU A 498     -46.191  15.418  20.856  1.00 43.16           O  
ATOM    475  CB  GLU A 498     -47.242  14.611  17.859  1.00 39.65           C  
ATOM    476  CG  GLU A 498     -48.238  13.645  17.234  1.00 43.09           C  
ATOM    477  CD  GLU A 498     -47.693  12.950  15.999  1.00 44.13           C  
ATOM    478  OE1 GLU A 498     -46.878  13.561  15.276  1.00 44.90           O  
ATOM    479  OE2 GLU A 498     -48.084  11.791  15.749  1.00 47.20           O  
ATOM    480  N   LEU A 499     -46.191  17.185  19.461  1.00 44.38           N  
ATOM    481  CA  LEU A 499     -45.207  17.899  20.268  1.00 40.98           C  
ATOM    482  C   LEU A 499     -45.784  18.297  21.620  1.00 45.72           C  
ATOM    483  O   LEU A 499     -45.036  18.462  22.591  1.00 46.28           O  
ATOM    484  CB  LEU A 499     -44.706  19.141  19.531  1.00 33.11           C  
ATOM    485  CG  LEU A 499     -43.948  18.985  18.214  1.00 35.99           C  
ATOM    486  CD1 LEU A 499     -43.523  20.355  17.716  1.00 40.67           C  
ATOM    487  CD2 LEU A 499     -42.743  18.079  18.381  1.00 35.24           C  
ATOM    488  N   ALA A 500     -47.107  18.456  21.702  1.00 47.56           N  
ATOM    489  CA  ALA A 500     -47.754  18.791  22.964  1.00 44.89           C  
ATOM    490  C   ALA A 500     -47.698  17.659  23.982  1.00 49.42           C  
ATOM    491  O   ALA A 500     -48.056  17.882  25.143  1.00 48.35           O  
ATOM    492  CB  ALA A 500     -49.211  19.184  22.716  1.00 49.62           C  
ATOM    493  N   LEU A 501     -47.266  16.458  23.582  1.00 50.25           N  
ATOM    494  CA  LEU A 501     -47.171  15.351  24.531  1.00 40.56           C  
ATOM    495  C   LEU A 501     -46.128  15.620  25.608  1.00 36.94           C  
ATOM    496  O   LEU A 501     -46.224  15.074  26.713  1.00 42.15           O  
ATOM    497  CB  LEU A 501     -46.843  14.050  23.797  1.00 40.55           C  
ATOM    498  CG  LEU A 501     -47.878  13.502  22.814  1.00 40.35           C  
ATOM    499  CD1 LEU A 501     -47.287  12.365  21.998  1.00 36.42           C  
ATOM    500  CD2 LEU A 501     -49.128  13.042  23.546  1.00 43.92           C  
ATOM    501  N   CYS A 502     -45.130  16.452  25.310  1.00 41.93           N  
ATOM    502  CA  CYS A 502     -44.067  16.763  26.258  1.00 40.52           C  
ATOM    503  C   CYS A 502     -43.747  18.244  26.381  1.00 45.64           C  
ATOM    504  O   CYS A 502     -43.118  18.631  27.372  1.00 49.64           O  
ATOM    505  CB  CYS A 502     -42.773  16.026  25.881  1.00 44.98           C  
ATOM    506  SG  CYS A 502     -42.896  14.225  25.871  1.00 43.96           S  
ATOM    507  N   HIS A 503     -44.148  19.080  25.428  1.00 44.13           N  
ATOM    508  CA  HIS A 503     -43.717  20.468  25.385  1.00 45.45           C  
ATOM    509  C   HIS A 503     -44.906  21.410  25.506  1.00 51.72           C  
ATOM    510  O   HIS A 503     -46.009  21.112  25.037  1.00 46.68           O  
ATOM    511  CB  HIS A 503     -42.952  20.760  24.094  1.00 49.37           C  
ATOM    512  CG  HIS A 503     -41.722  19.925  23.926  1.00 45.52           C  
ATOM    513  ND1 HIS A 503     -40.480  20.338  24.355  1.00 43.73           N  
ATOM    514  CD2 HIS A 503     -41.546  18.696  23.387  1.00 48.15           C  
ATOM    515  CE1 HIS A 503     -39.589  19.402  24.080  1.00 44.52           C  
ATOM    516  NE2 HIS A 503     -40.210  18.395  23.493  1.00 44.83           N  
ATOM    517  N   SER A 504     -44.663  22.553  26.141  1.00 50.01           N  
ATOM    518  CA  SER A 504     -45.698  23.564  26.300  1.00 51.92           C  
ATOM    519  C   SER A 504     -45.921  24.310  24.990  1.00 51.49           C  
ATOM    520  O   SER A 504     -45.038  24.383  24.131  1.00 44.91           O  
ATOM    521  CB  SER A 504     -45.318  24.549  27.406  1.00 50.30           C  
ATOM    522  OG  SER A 504     -44.182  25.313  27.043  1.00 48.97           O  
ATOM    523  N   SER A 505     -47.124  24.875  24.849  1.00 58.36           N  
ATOM    524  CA  SER A 505     -47.487  25.555  23.610  1.00 54.30           C  
ATOM    525  C   SER A 505     -46.588  26.754  23.332  1.00 50.73           C  
ATOM    526  O   SER A 505     -46.368  27.104  22.166  1.00 50.78           O  
ATOM    527  CB  SER A 505     -48.952  25.989  23.664  1.00 55.41           C  
ATOM    528  OG  SER A 505     -49.259  26.581  24.915  1.00 56.02           O  
ATOM    529  N   LYS A 506     -46.058  27.390  24.380  1.00 48.08           N  
ATOM    530  CA  LYS A 506     -45.192  28.549  24.186  1.00 44.40           C  
ATOM    531  C   LYS A 506     -43.903  28.160  23.470  1.00 48.16           C  
ATOM    532  O   LYS A 506     -43.546  28.752  22.445  1.00 50.09           O  
ATOM    533  CB  LYS A 506     -44.885  29.203  25.534  1.00 46.46           C  
ATOM    534  N   HIS A 507     -43.195  27.158  24.000  1.00 56.28           N  
ATOM    535  CA  HIS A 507     -41.948  26.693  23.393  1.00 47.27           C  
ATOM    536  C   HIS A 507     -42.160  26.285  21.937  1.00 44.79           C  
ATOM    537  O   HIS A 507     -41.411  26.704  21.039  1.00 48.83           O  
ATOM    538  CB  HIS A 507     -41.397  25.528  24.220  1.00 45.00           C  
ATOM    539  CG  HIS A 507     -40.186  24.873  23.634  1.00 45.00           C  
ATOM    540  ND1 HIS A 507     -39.073  25.581  23.235  1.00 45.01           N  
ATOM    541  CD2 HIS A 507     -39.909  23.569  23.395  1.00 43.06           C  
ATOM    542  CE1 HIS A 507     -38.165  24.742  22.768  1.00 41.74           C  
ATOM    543  NE2 HIS A 507     -38.648  23.515  22.853  1.00 43.25           N  
ATOM    544  N   ILE A 508     -43.195  25.474  21.688  1.00 41.77           N  
ATOM    545  CA  ILE A 508     -43.538  25.072  20.324  1.00 43.51           C  
ATOM    546  C   ILE A 508     -43.752  26.298  19.446  1.00 47.60           C  
ATOM    547  O   ILE A 508     -43.262  26.366  18.315  1.00 47.48           O  
ATOM    548  CB  ILE A 508     -44.785  24.169  20.326  1.00 44.76           C  
ATOM    549  CG1 ILE A 508     -44.633  23.023  21.325  1.00 45.25           C  
ATOM    550  CG2 ILE A 508     -45.047  23.629  18.930  1.00 46.06           C  
ATOM    551  CD1 ILE A 508     -45.802  22.063  21.325  1.00 37.23           C  
ATOM    552  N   SER A 509     -44.490  27.286  19.957  1.00 47.25           N  
ATOM    553  CA  SER A 509     -44.823  28.453  19.146  1.00 46.11           C  
ATOM    554  C   SER A 509     -43.582  29.274  18.814  1.00 50.19           C  
ATOM    555  O   SER A 509     -43.475  29.832  17.716  1.00 49.74           O  
ATOM    556  CB  SER A 509     -45.861  29.313  19.865  1.00 44.36           C  
ATOM    557  OG  SER A 509     -46.640  30.043  18.934  1.00 62.78           O  
ATOM    558  N   ILE A 510     -42.633  29.358  19.748  1.00 47.85           N  
ATOM    559  CA  ILE A 510     -41.398  30.096  19.491  1.00 42.20           C  
ATOM    560  C   ILE A 510     -40.576  29.397  18.412  1.00 45.30           C  
ATOM    561  O   ILE A 510     -40.221  29.997  17.384  1.00 42.97           O  
ATOM    562  CB  ILE A 510     -40.592  30.267  20.791  1.00 43.47           C  
ATOM    563  CG1 ILE A 510     -41.441  30.954  21.860  1.00 44.74           C  
ATOM    564  CG2 ILE A 510     -39.324  31.065  20.534  1.00 46.79           C  
ATOM    565  N   ILE A 511     -40.265  28.113  18.628  1.00 46.86           N  
ATOM    566  CA  ILE A 511     -39.436  27.400  17.657  1.00 43.09           C  
ATOM    567  C   ILE A 511     -40.124  27.348  16.299  1.00 37.25           C  
ATOM    568  O   ILE A 511     -39.464  27.396  15.254  1.00 33.80           O  
ATOM    569  CB  ILE A 511     -39.089  25.990  18.175  1.00 45.78           C  
ATOM    570  CG1 ILE A 511     -38.564  26.069  19.610  1.00 40.70           C  
ATOM    571  CG2 ILE A 511     -38.060  25.323  17.272  1.00 38.54           C  
ATOM    572  CD1 ILE A 511     -37.225  26.768  19.735  1.00 41.74           C  
ATOM    573  N   LYS A 512     -41.456  27.269  16.291  1.00 40.99           N  
ATOM    574  CA  LYS A 512     -42.205  27.329  15.040  1.00 45.35           C  
ATOM    575  C   LYS A 512     -42.053  28.692  14.379  1.00 49.29           C  
ATOM    576  O   LYS A 512     -41.923  28.786  13.153  1.00 50.36           O  
ATOM    577  CB  LYS A 512     -43.678  27.016  15.305  1.00 44.34           C  
ATOM    578  CG  LYS A 512     -44.606  27.233  14.118  1.00 48.27           C  
ATOM    579  CD  LYS A 512     -46.033  26.815  14.460  1.00 49.45           C  
ATOM    580  CE  LYS A 512     -46.974  26.996  13.277  1.00 49.07           C  
ATOM    581  NZ  LYS A 512     -46.457  26.325  12.051  1.00 47.37           N  
ATOM    582  N   SER A 513     -42.061  29.763  15.180  1.00 47.70           N  
ATOM    583  CA  SER A 513     -41.861  31.105  14.646  1.00 49.83           C  
ATOM    584  C   SER A 513     -40.462  31.297  14.081  1.00 49.12           C  
ATOM    585  O   SER A 513     -40.259  32.197  13.258  1.00 48.02           O  
ATOM    586  CB  SER A 513     -42.126  32.154  15.726  1.00 37.94           C  
ATOM    587  OG  SER A 513     -40.995  32.320  16.563  1.00 42.01           O  
ATOM    588  N   SER A 514     -39.493  30.479  14.505  1.00 49.51           N  
ATOM    589  CA  SER A 514     -38.167  30.534  13.894  1.00 47.14           C  
ATOM    590  C   SER A 514     -38.195  30.232  12.398  1.00 45.65           C  
ATOM    591  O   SER A 514     -37.232  30.558  11.695  1.00 46.17           O  
ATOM    592  CB  SER A 514     -37.224  29.551  14.587  1.00 48.57           C  
ATOM    593  OG  SER A 514     -37.345  28.256  14.024  1.00 41.75           O  
ATOM    594  N   GLU A 515     -39.274  29.620  11.901  1.00 44.94           N  
ATOM    595  CA  GLU A 515     -39.322  29.189  10.506  1.00 51.90           C  
ATOM    596  C   GLU A 515     -39.142  30.359   9.546  1.00 56.13           C  
ATOM    597  O   GLU A 515     -38.467  30.229   8.518  1.00 51.62           O  
ATOM    598  CB  GLU A 515     -40.646  28.476  10.230  1.00 50.39           C  
ATOM    599  CG  GLU A 515     -40.686  27.698   8.927  1.00 59.65           C  
ATOM    600  CD  GLU A 515     -41.694  26.566   8.962  1.00 63.77           C  
ATOM    601  OE1 GLU A 515     -42.635  26.631   9.782  1.00 61.22           O  
ATOM    602  OE2 GLU A 515     -41.547  25.613   8.167  1.00 70.52           O  
ATOM    603  N   HIS A 516     -39.740  31.505   9.859  1.00 59.00           N  
ATOM    604  CA  HIS A 516     -39.704  32.689   9.003  1.00 56.55           C  
ATOM    605  C   HIS A 516     -39.086  33.828   9.809  1.00 56.13           C  
ATOM    606  O   HIS A 516     -39.798  34.627  10.422  1.00 57.52           O  
ATOM    607  CB  HIS A 516     -41.104  33.042   8.502  1.00 59.24           C  
ATOM    608  CG  HIS A 516     -41.839  31.885   7.901  1.00 58.63           C  
ATOM    609  ND1 HIS A 516     -41.352  31.172   6.826  1.00 60.61           N  
ATOM    610  CD2 HIS A 516     -43.022  31.313   8.227  1.00 55.50           C  
ATOM    611  CE1 HIS A 516     -42.205  30.212   6.515  1.00 56.95           C  
ATOM    612  NE2 HIS A 516     -43.227  30.275   7.349  1.00 56.34           N  
ATOM    613  N   MET A 517     -37.756  33.900   9.801  1.00 55.84           N  
ATOM    614  CA  MET A 517     -37.028  34.904  10.561  1.00 49.09           C  
ATOM    615  C   MET A 517     -35.826  35.386   9.763  1.00 51.78           C  
ATOM    616  O   MET A 517     -35.237  34.635   8.981  1.00 50.37           O  
ATOM    617  CB  MET A 517     -36.547  34.358  11.912  1.00 48.90           C  
ATOM    618  CG  MET A 517     -37.590  34.354  13.013  1.00 47.61           C  
ATOM    619  SD  MET A 517     -36.825  34.148  14.634  1.00 50.61           S  
ATOM    620  CE  MET A 517     -38.265  33.876  15.662  1.00 43.20           C  
ATOM    621  N   LYS A 518     -35.468  36.651   9.975  1.00 49.33           N  
ATOM    622  CA  LYS A 518     -34.238  37.184   9.417  1.00 49.76           C  
ATOM    623  C   LYS A 518     -33.041  36.654  10.205  1.00 48.56           C  
ATOM    624  O   LYS A 518     -33.171  36.318  11.385  1.00 52.26           O  
ATOM    625  CB  LYS A 518     -34.255  38.709   9.450  1.00 52.40           C  
ATOM    626  N   PRO A 519     -31.867  36.557   9.570  1.00 40.77           N  
ATOM    627  CA  PRO A 519     -30.696  35.997  10.272  1.00 45.55           C  
ATOM    628  C   PRO A 519     -30.367  36.690  11.587  1.00 50.84           C  
ATOM    629  O   PRO A 519     -29.936  36.026  12.541  1.00 57.66           O  
ATOM    630  CB  PRO A 519     -29.571  36.163   9.243  1.00 46.73           C  
ATOM    631  CG  PRO A 519     -30.265  36.153   7.927  1.00 41.56           C  
ATOM    632  CD  PRO A 519     -31.585  36.828   8.150  1.00 37.89           C  
ATOM    633  N   ARG A 520     -30.562  38.009  11.666  1.00 49.35           N  
ATOM    634  CA  ARG A 520     -30.345  38.712  12.926  1.00 52.09           C  
ATOM    635  C   ARG A 520     -31.289  38.201  14.007  1.00 58.65           C  
ATOM    636  O   ARG A 520     -30.881  38.001  15.158  1.00 62.76           O  
ATOM    637  CB  ARG A 520     -30.520  40.217  12.725  1.00 46.74           C  
ATOM    638  N   ASP A 521     -32.557  37.973  13.653  1.00 54.92           N  
ATOM    639  CA  ASP A 521     -33.503  37.421  14.616  1.00 57.65           C  
ATOM    640  C   ASP A 521     -33.172  35.977  14.967  1.00 57.71           C  
ATOM    641  O   ASP A 521     -33.422  35.542  16.096  1.00 56.20           O  
ATOM    642  CB  ASP A 521     -34.927  37.518  14.070  1.00 57.57           C  
ATOM    643  CG  ASP A 521     -35.597  38.830  14.422  1.00 68.06           C  
ATOM    644  OD1 ASP A 521     -34.957  39.889  14.256  1.00 71.00           O  
ATOM    645  OD2 ASP A 521     -36.764  38.799  14.866  1.00 68.62           O  
ATOM    646  N   LEU A 522     -32.619  35.219  14.017  1.00 56.23           N  
ATOM    647  CA  LEU A 522     -32.223  33.846  14.313  1.00 52.93           C  
ATOM    648  C   LEU A 522     -31.073  33.812  15.313  1.00 58.40           C  
ATOM    649  O   LEU A 522     -31.069  32.985  16.233  1.00 58.67           O  
ATOM    650  CB  LEU A 522     -31.856  33.115  13.020  1.00 51.96           C  
ATOM    651  CG  LEU A 522     -33.035  32.834  12.080  1.00 48.84           C  
ATOM    652  CD1 LEU A 522     -32.576  32.263  10.744  1.00 37.86           C  
ATOM    653  CD2 LEU A 522     -34.037  31.901  12.743  1.00 45.46           C  
ATOM    654  N   ASN A 523     -30.093  34.709  15.158  1.00 52.53           N  
ATOM    655  CA  ASN A 523     -29.041  34.826  16.164  1.00 54.65           C  
ATOM    656  C   ASN A 523     -29.612  35.277  17.503  1.00 56.38           C  
ATOM    657  O   ASN A 523     -29.252  34.737  18.558  1.00 56.79           O  
ATOM    658  CB  ASN A 523     -27.963  35.800  15.684  1.00 55.22           C  
ATOM    659  CG  ASN A 523     -26.795  35.903  16.648  1.00 61.05           C  
ATOM    660  OD1 ASN A 523     -26.247  34.893  17.091  1.00 65.62           O  
ATOM    661  ND2 ASN A 523     -26.405  37.130  16.975  1.00 67.78           N  
ATOM    662  N   ARG A 524     -30.517  36.261  17.475  1.00 57.71           N  
ATOM    663  CA  ARG A 524     -31.112  36.772  18.706  1.00 57.31           C  
ATOM    664  C   ARG A 524     -31.828  35.670  19.479  1.00 56.32           C  
ATOM    665  O   ARG A 524     -31.683  35.567  20.702  1.00 55.07           O  
ATOM    666  CB  ARG A 524     -32.077  37.914  18.384  1.00 58.50           C  
ATOM    667  CG  ARG A 524     -32.860  38.431  19.580  1.00 56.00           C  
ATOM    668  CD  ARG A 524     -34.267  38.854  19.180  1.00 57.59           C  
ATOM    669  NE  ARG A 524     -35.107  37.710  18.837  1.00 62.92           N  
ATOM    670  N   LEU A 525     -32.603  34.833  18.783  1.00 59.35           N  
ATOM    671  CA  LEU A 525     -33.312  33.748  19.453  1.00 55.76           C  
ATOM    672  C   LEU A 525     -32.375  32.615  19.850  1.00 48.52           C  
ATOM    673  O   LEU A 525     -32.595  31.968  20.881  1.00 40.98           O  
ATOM    674  CB  LEU A 525     -34.432  33.216  18.557  1.00 49.54           C  
ATOM    675  CG  LEU A 525     -35.273  32.079  19.143  1.00 42.88           C  
ATOM    676  CD1 LEU A 525     -35.954  32.535  20.421  1.00 40.82           C  
ATOM    677  CD2 LEU A 525     -36.297  31.579  18.137  1.00 42.99           C  
ATOM    678  N   GLY A 526     -31.332  32.364  19.057  1.00 46.41           N  
ATOM    679  CA  GLY A 526     -30.366  31.344  19.428  1.00 46.02           C  
ATOM    680  C   GLY A 526     -29.627  31.682  20.709  1.00 50.45           C  
ATOM    681  O   GLY A 526     -29.327  30.797  21.516  1.00 48.92           O  
ATOM    682  N   ASP A 527     -29.331  32.967  20.919  1.00 48.62           N  
ATOM    683  CA  ASP A 527     -28.618  33.381  22.123  1.00 46.12           C  
ATOM    684  C   ASP A 527     -29.479  33.323  23.381  1.00 45.11           C  
ATOM    685  O   ASP A 527     -28.936  33.443  24.484  1.00 40.88           O  
ATOM    686  CB  ASP A 527     -28.059  34.793  21.941  1.00 47.32           C  
ATOM    687  CG  ASP A 527     -26.672  34.795  21.324  1.00 56.16           C  
ATOM    688  OD1 ASP A 527     -26.130  33.700  21.065  1.00 66.63           O  
ATOM    689  OD2 ASP A 527     -26.121  35.893  21.101  1.00 63.63           O  
ATOM    690  N   GLU A 528     -30.794  33.145  23.251  1.00 44.63           N  
ATOM    691  CA  GLU A 528     -31.668  33.007  24.411  1.00 43.30           C  
ATOM    692  C   GLU A 528     -31.634  31.609  25.014  1.00 44.29           C  
ATOM    693  O   GLU A 528     -32.285  31.375  26.039  1.00 38.69           O  
ATOM    694  CB  GLU A 528     -33.108  33.363  24.033  1.00 44.98           C  
ATOM    695  CG  GLU A 528     -33.250  34.680  23.289  1.00 50.16           C  
ATOM    696  CD  GLU A 528     -34.676  35.199  23.284  1.00 63.52           C  
ATOM    697  OE1 GLU A 528     -35.611  34.372  23.339  1.00 57.91           O  
ATOM    698  OE2 GLU A 528     -34.860  36.434  23.219  1.00 72.55           O  
ATOM    699  N   TYR A 529     -30.904  30.682  24.405  1.00 40.28           N  
ATOM    700  CA  TYR A 529     -30.812  29.310  24.871  1.00 42.13           C  
ATOM    701  C   TYR A 529     -29.354  28.954  25.117  1.00 42.59           C  
ATOM    702  O   TYR A 529     -28.439  29.567  24.557  1.00 36.28           O  
ATOM    703  CB  TYR A 529     -31.421  28.336  23.853  1.00 39.30           C  
ATOM    704  CG  TYR A 529     -32.888  28.569  23.572  1.00 34.58           C  
ATOM    705  CD1 TYR A 529     -33.309  29.076  22.347  1.00 34.79           C  
ATOM    706  CD2 TYR A 529     -33.852  28.275  24.526  1.00 35.46           C  
ATOM    707  CE1 TYR A 529     -34.652  29.290  22.085  1.00 34.35           C  
ATOM    708  CE2 TYR A 529     -35.196  28.484  24.274  1.00 39.23           C  
ATOM    709  CZ  TYR A 529     -35.591  28.991  23.054  1.00 41.69           C  
ATOM    710  OH  TYR A 529     -36.929  29.197  22.805  1.00 46.71           O  
ATOM    711  N   ASN A 530     -29.146  27.947  25.961  1.00 44.52           N  
ATOM    712  CA  ASN A 530     -27.803  27.453  26.231  1.00 40.58           C  
ATOM    713  C   ASN A 530     -27.396  26.469  25.141  1.00 40.99           C  
ATOM    714  O   ASN A 530     -28.030  25.421  24.976  1.00 46.38           O  
ATOM    715  CB  ASN A 530     -27.748  26.795  27.607  1.00 46.10           C  
ATOM    716  CG  ASN A 530     -26.351  26.353  27.987  1.00 50.39           C  
ATOM    717  OD1 ASN A 530     -26.083  25.160  28.115  1.00 55.35           O  
ATOM    718  ND2 ASN A 530     -25.449  27.314  28.162  1.00 55.32           N  
ATOM    719  N   SER A 531     -26.345  26.814  24.396  1.00 42.50           N  
ATOM    720  CA  SER A 531     -25.779  25.961  23.350  1.00 42.52           C  
ATOM    721  C   SER A 531     -26.837  25.594  22.306  1.00 42.29           C  
ATOM    722  O   SER A 531     -27.247  24.441  22.163  1.00 38.56           O  
ATOM    723  CB  SER A 531     -25.155  24.699  23.955  1.00 48.26           C  
ATOM    724  OG  SER A 531     -24.302  25.021  25.037  1.00 51.11           O  
ATOM    725  N   ILE A 532     -27.269  26.617  21.574  1.00 43.32           N  
ATOM    726  CA  ILE A 532     -28.291  26.460  20.546  1.00 37.37           C  
ATOM    727  C   ILE A 532     -27.994  27.420  19.404  1.00 37.58           C  
ATOM    728  O   ILE A 532     -27.847  28.627  19.620  1.00 43.22           O  
ATOM    729  CB  ILE A 532     -29.708  26.709  21.103  1.00 37.07           C  
ATOM    730  CG1 ILE A 532     -30.262  25.439  21.753  1.00 40.51           C  
ATOM    731  CG2 ILE A 532     -30.647  27.188  20.001  1.00 37.21           C  
ATOM    732  CD1 ILE A 532     -30.512  24.314  20.768  1.00 33.20           C  
ATOM    733  N   PHE A 533     -27.891  26.882  18.193  1.00 36.19           N  
ATOM    734  CA  PHE A 533     -27.934  27.677  16.978  1.00 39.76           C  
ATOM    735  C   PHE A 533     -29.195  27.314  16.204  1.00 41.91           C  
ATOM    736  O   PHE A 533     -29.648  26.167  16.229  1.00 42.14           O  
ATOM    737  CB  PHE A 533     -26.684  27.468  16.110  1.00 37.69           C  
ATOM    738  CG  PHE A 533     -26.529  26.070  15.575  1.00 42.59           C  
ATOM    739  CD1 PHE A 533     -27.170  25.676  14.410  1.00 44.52           C  
ATOM    740  CD2 PHE A 533     -25.721  25.154  16.226  1.00 43.62           C  
ATOM    741  CE1 PHE A 533     -27.021  24.392  13.919  1.00 44.30           C  
ATOM    742  CE2 PHE A 533     -25.566  23.870  15.736  1.00 45.30           C  
ATOM    743  CZ  PHE A 533     -26.216  23.489  14.581  1.00 43.40           C  
ATOM    744  N   ILE A 534     -29.772  28.304  15.530  1.00 47.09           N  
ATOM    745  CA  ILE A 534     -31.052  28.140  14.855  1.00 39.34           C  
ATOM    746  C   ILE A 534     -30.905  28.536  13.395  1.00 46.01           C  
ATOM    747  O   ILE A 534     -30.225  29.515  13.069  1.00 43.73           O  
ATOM    748  CB  ILE A 534     -32.162  28.971  15.531  1.00 41.77           C  
ATOM    749  CG1 ILE A 534     -32.243  28.636  17.022  1.00 36.49           C  
ATOM    750  CG2 ILE A 534     -33.501  28.730  14.849  1.00 38.99           C  
ATOM    751  CD1 ILE A 534     -33.547  29.033  17.669  1.00 40.83           C  
ATOM    752  N   SER A 535     -31.539  27.766  12.520  1.00 48.92           N  
ATOM    753  CA  SER A 535     -31.663  28.088  11.110  1.00 41.23           C  
ATOM    754  C   SER A 535     -33.138  28.202  10.751  1.00 41.82           C  
ATOM    755  O   SER A 535     -34.025  27.883  11.547  1.00 42.68           O  
ATOM    756  CB  SER A 535     -30.980  27.030  10.236  1.00 43.21           C  
ATOM    757  OG  SER A 535     -30.871  27.477   8.898  1.00 56.53           O  
ATOM    758  N   ASN A 536     -33.395  28.673   9.531  1.00 46.15           N  
ATOM    759  CA  ASN A 536     -34.770  28.731   9.052  1.00 48.05           C  
ATOM    760  C   ASN A 536     -35.367  27.337   8.914  1.00 47.28           C  
ATOM    761  O   ASN A 536     -36.589  27.172   9.013  1.00 48.81           O  
ATOM    762  CB  ASN A 536     -34.831  29.473   7.717  1.00 52.27           C  
ATOM    763  CG  ASN A 536     -35.068  30.960   7.887  1.00 54.20           C  
ATOM    764  OD1 ASN A 536     -35.849  31.381   8.739  1.00 57.53           O  
ATOM    765  ND2 ASN A 536     -34.398  31.764   7.069  1.00 60.58           N  
ATOM    766  N   GLU A 537     -34.524  26.327   8.702  1.00 49.72           N  
ATOM    767  CA  GLU A 537     -34.951  24.952   8.480  1.00 45.01           C  
ATOM    768  C   GLU A 537     -34.950  24.106   9.747  1.00 42.40           C  
ATOM    769  O   GLU A 537     -35.294  22.921   9.680  1.00 45.25           O  
ATOM    770  CB  GLU A 537     -34.046  24.284   7.436  1.00 44.47           C  
ATOM    771  CG  GLU A 537     -33.919  25.033   6.113  1.00 51.19           C  
ATOM    772  CD  GLU A 537     -32.844  26.108   6.131  1.00 54.88           C  
ATOM    773  OE1 GLU A 537     -32.909  27.010   6.992  1.00 57.68           O  
ATOM    774  OE2 GLU A 537     -31.929  26.048   5.280  1.00 52.22           O  
ATOM    775  N   SER A 538     -34.569  24.678  10.892  1.00 41.30           N  
ATOM    776  CA  SER A 538     -34.374  23.877  12.098  1.00 38.79           C  
ATOM    777  C   SER A 538     -35.680  23.261  12.586  1.00 34.27           C  
ATOM    778  O   SER A 538     -35.715  22.080  12.955  1.00 39.26           O  
ATOM    779  CB  SER A 538     -33.745  24.735  13.192  1.00 36.13           C  
ATOM    780  OG  SER A 538     -32.459  25.182  12.799  1.00 38.74           O  
ATOM    781  N   TYR A 539     -36.758  24.047  12.601  1.00 38.63           N  
ATOM    782  CA  TYR A 539     -38.049  23.551  13.072  1.00 38.08           C  
ATOM    783  C   TYR A 539     -38.506  22.341  12.263  1.00 39.55           C  
ATOM    784  O   TYR A 539     -38.944  21.328  12.828  1.00 38.70           O  
ATOM    785  CB  TYR A 539     -39.071  24.687  13.002  1.00 29.90           C  
ATOM    786  CG  TYR A 539     -40.495  24.317  13.337  1.00 36.14           C  
ATOM    787  CD1 TYR A 539     -40.882  24.066  14.646  1.00 41.51           C  
ATOM    788  CD2 TYR A 539     -41.464  24.255  12.345  1.00 39.13           C  
ATOM    789  CE1 TYR A 539     -42.192  23.742  14.954  1.00 41.83           C  
ATOM    790  CE2 TYR A 539     -42.772  23.934  12.642  1.00 38.88           C  
ATOM    791  CZ  TYR A 539     -43.132  23.679  13.946  1.00 36.29           C  
ATOM    792  OH  TYR A 539     -44.437  23.359  14.240  1.00 43.65           O  
ATOM    793  N   THR A 540     -38.381  22.420  10.936  1.00 44.56           N  
ATOM    794  CA  THR A 540     -38.769  21.307  10.077  1.00 35.06           C  
ATOM    795  C   THR A 540     -37.933  20.066  10.367  1.00 39.76           C  
ATOM    796  O   THR A 540     -38.470  18.955  10.448  1.00 38.71           O  
ATOM    797  CB  THR A 540     -38.644  21.722   8.608  1.00 41.68           C  
ATOM    798  OG1 THR A 540     -39.776  22.521   8.239  1.00 46.24           O  
ATOM    799  CG2 THR A 540     -38.564  20.504   7.693  1.00 31.32           C  
ATOM    800  N   CYS A 541     -36.620  20.234  10.545  1.00 37.34           N  
ATOM    801  CA  CYS A 541     -35.757  19.084  10.804  1.00 40.06           C  
ATOM    802  C   CYS A 541     -36.083  18.430  12.143  1.00 39.17           C  
ATOM    803  O   CYS A 541     -36.072  17.197  12.257  1.00 42.50           O  
ATOM    804  CB  CYS A 541     -34.290  19.506  10.753  1.00 39.47           C  
ATOM    805  SG  CYS A 541     -33.688  19.841   9.086  1.00 57.32           S  
ATOM    806  N   ALA A 542     -36.372  19.236  13.167  1.00 40.10           N  
ATOM    807  CA  ALA A 542     -36.815  18.676  14.440  1.00 40.01           C  
ATOM    808  C   ALA A 542     -38.099  17.872  14.261  1.00 37.74           C  
ATOM    809  O   ALA A 542     -38.225  16.749  14.773  1.00 44.32           O  
ATOM    810  CB  ALA A 542     -37.011  19.796  15.463  1.00 30.55           C  
ATOM    811  N   LEU A 543     -39.061  18.430  13.517  1.00 38.49           N  
ATOM    812  CA  LEU A 543     -40.293  17.697  13.237  1.00 38.27           C  
ATOM    813  C   LEU A 543     -40.010  16.393  12.500  1.00 35.59           C  
ATOM    814  O   LEU A 543     -40.697  15.386  12.715  1.00 32.92           O  
ATOM    815  CB  LEU A 543     -41.254  18.569  12.429  1.00 39.07           C  
ATOM    816  CG  LEU A 543     -41.856  19.777  13.148  1.00 42.38           C  
ATOM    817  CD1 LEU A 543     -42.996  20.377  12.338  1.00 36.38           C  
ATOM    818  CD2 LEU A 543     -42.331  19.381  14.531  1.00 38.35           C  
ATOM    819  N   LEU A 544     -38.997  16.393  11.628  1.00 35.75           N  
ATOM    820  CA  LEU A 544     -38.656  15.188  10.878  1.00 32.54           C  
ATOM    821  C   LEU A 544     -38.063  14.121  11.785  1.00 39.04           C  
ATOM    822  O   LEU A 544     -38.362  12.931  11.629  1.00 34.85           O  
ATOM    823  CB  LEU A 544     -37.679  15.524   9.753  1.00 36.90           C  
ATOM    824  CG  LEU A 544     -38.271  15.939   8.408  1.00 44.06           C  
ATOM    825  CD1 LEU A 544     -37.176  16.423   7.474  1.00 44.74           C  
ATOM    826  CD2 LEU A 544     -39.037  14.784   7.792  1.00 42.74           C  
ATOM    827  N   ALA A 545     -37.206  14.522  12.726  1.00 34.55           N  
ATOM    828  CA  ALA A 545     -36.656  13.560  13.675  1.00 36.67           C  
ATOM    829  C   ALA A 545     -37.760  12.944  14.527  1.00 37.52           C  
ATOM    830  O   ALA A 545     -37.875  11.711  14.632  1.00 33.25           O  
ATOM    831  CB  ALA A 545     -35.606  14.238  14.555  1.00 34.64           C  
ATOM    832  N   ALA A 546     -38.600  13.794  15.129  1.00 34.77           N  
ATOM    833  CA  ALA A 546     -39.669  13.283  15.981  1.00 36.16           C  
ATOM    834  C   ALA A 546     -40.612  12.369  15.204  1.00 34.48           C  
ATOM    835  O   ALA A 546     -40.965  11.281  15.679  1.00 36.20           O  
ATOM    836  CB  ALA A 546     -40.438  14.443  16.612  1.00 35.66           C  
ATOM    837  N   GLY A 547     -41.017  12.784  14.002  1.00 35.09           N  
ATOM    838  CA  GLY A 547     -41.931  11.967  13.219  1.00 34.62           C  
ATOM    839  C   GLY A 547     -41.312  10.661  12.755  1.00 37.55           C  
ATOM    840  O   GLY A 547     -41.983   9.625  12.722  1.00 36.06           O  
ATOM    841  N   SER A 548     -40.031  10.695  12.378  1.00 36.86           N  
ATOM    842  CA  SER A 548     -39.332   9.467  12.014  1.00 32.27           C  
ATOM    843  C   SER A 548     -39.340   8.473  13.166  1.00 38.89           C  
ATOM    844  O   SER A 548     -39.603   7.278  12.970  1.00 31.03           O  
ATOM    845  CB  SER A 548     -37.895   9.781  11.597  1.00 33.57           C  
ATOM    846  OG  SER A 548     -37.852  10.737  10.553  1.00 38.15           O  
ATOM    847  N   CYS A 549     -39.062   8.951  14.382  1.00 39.02           N  
ATOM    848  CA  CYS A 549     -39.074   8.039  15.520  1.00 34.95           C  
ATOM    849  C   CYS A 549     -40.486   7.581  15.865  1.00 33.30           C  
ATOM    850  O   CYS A 549     -40.666   6.470  16.377  1.00 35.56           O  
ATOM    851  CB  CYS A 549     -38.399   8.697  16.717  1.00 25.70           C  
ATOM    852  SG  CYS A 549     -36.621   8.851  16.475  1.00 31.81           S  
ATOM    853  N   PHE A 550     -41.496   8.411  15.591  1.00 38.76           N  
ATOM    854  CA  PHE A 550     -42.875   7.966  15.776  1.00 37.24           C  
ATOM    855  C   PHE A 550     -43.216   6.833  14.816  1.00 39.68           C  
ATOM    856  O   PHE A 550     -43.836   5.838  15.214  1.00 37.07           O  
ATOM    857  CB  PHE A 550     -43.842   9.133  15.583  1.00 33.72           C  
ATOM    858  CG  PHE A 550     -43.668  10.240  16.583  1.00 40.32           C  
ATOM    859  CD1 PHE A 550     -43.057  10.005  17.803  1.00 34.49           C  
ATOM    860  CD2 PHE A 550     -44.121  11.519  16.302  1.00 42.39           C  
ATOM    861  CE1 PHE A 550     -42.899  11.024  18.721  1.00 37.34           C  
ATOM    862  CE2 PHE A 550     -43.967  12.541  17.217  1.00 39.91           C  
ATOM    863  CZ  PHE A 550     -43.355  12.294  18.428  1.00 41.88           C  
ATOM    864  N   ASN A 551     -42.819   6.967  13.549  1.00 39.55           N  
ATOM    865  CA  ASN A 551     -43.070   5.908  12.578  1.00 34.54           C  
ATOM    866  C   ASN A 551     -42.306   4.642  12.938  1.00 38.03           C  
ATOM    867  O   ASN A 551     -42.810   3.529  12.742  1.00 39.96           O  
ATOM    868  CB  ASN A 551     -42.696   6.385  11.174  1.00 28.58           C  
ATOM    869  CG  ASN A 551     -43.817   7.147  10.500  1.00 30.87           C  
ATOM    870  OD1 ASN A 551     -44.892   7.326  11.073  1.00 36.73           O  
ATOM    871  ND2 ASN A 551     -43.572   7.604   9.278  1.00 34.99           N  
ATOM    872  N   SER A 552     -41.090   4.790  13.469  1.00 36.89           N  
ATOM    873  CA  SER A 552     -40.326   3.622  13.897  1.00 34.38           C  
ATOM    874  C   SER A 552     -41.018   2.908  15.053  1.00 36.86           C  
ATOM    875  O   SER A 552     -41.225   1.686  15.010  1.00 37.01           O  
ATOM    876  CB  SER A 552     -38.908   4.041  14.285  1.00 32.91           C  
ATOM    877  OG  SER A 552     -38.232   4.621  13.182  1.00 33.43           O  
ATOM    878  N   ALA A 553     -41.393   3.659  16.093  1.00 29.37           N  
ATOM    879  CA  ALA A 553     -42.110   3.065  17.217  1.00 33.02           C  
ATOM    880  C   ALA A 553     -43.412   2.415  16.771  1.00 40.40           C  
ATOM    881  O   ALA A 553     -43.816   1.387  17.328  1.00 37.19           O  
ATOM    882  CB  ALA A 553     -42.383   4.124  18.285  1.00 31.46           C  
ATOM    883  N   GLN A 554     -44.078   2.994  15.769  1.00 41.32           N  
ATOM    884  CA  GLN A 554     -45.294   2.388  15.236  1.00 38.15           C  
ATOM    885  C   GLN A 554     -44.990   1.057  14.559  1.00 42.99           C  
ATOM    886  O   GLN A 554     -45.648   0.045  14.832  1.00 45.90           O  
ATOM    887  CB  GLN A 554     -45.968   3.348  14.258  1.00 40.45           C  
ATOM    888  CG  GLN A 554     -47.476   3.216  14.201  1.00 48.39           C  
ATOM    889  CD  GLN A 554     -48.088   4.063  13.105  1.00 50.66           C  
ATOM    890  OE1 GLN A 554     -47.416   4.440  12.144  1.00 50.22           O  
ATOM    891  NE2 GLN A 554     -49.372   4.370  13.245  1.00 53.25           N  
ATOM    892  N   ALA A 555     -43.989   1.040  13.674  1.00 38.59           N  
ATOM    893  CA  ALA A 555     -43.627  -0.194  12.985  1.00 38.63           C  
ATOM    894  C   ALA A 555     -43.208  -1.284  13.962  1.00 43.97           C  
ATOM    895  O   ALA A 555     -43.399  -2.473  13.681  1.00 43.71           O  
ATOM    896  CB  ALA A 555     -42.510   0.074  11.976  1.00 33.12           C  
ATOM    897  N   ILE A 556     -42.638  -0.906  15.108  1.00 43.70           N  
ATOM    898  CA  ILE A 556     -42.271  -1.901  16.112  1.00 41.02           C  
ATOM    899  C   ILE A 556     -43.502  -2.399  16.856  1.00 41.67           C  
ATOM    900  O   ILE A 556     -43.721  -3.609  16.986  1.00 46.02           O  
ATOM    901  CB  ILE A 556     -41.228  -1.325  17.087  1.00 40.82           C  
ATOM    902  CG1 ILE A 556     -39.922  -1.008  16.360  1.00 39.87           C  
ATOM    903  CG2 ILE A 556     -40.977  -2.299  18.224  1.00 38.47           C  
ATOM    904  CD1 ILE A 556     -38.862  -0.398  17.248  1.00 35.69           C  
ATOM    905  N   LEU A 557     -44.325  -1.474  17.358  1.00 40.19           N  
ATOM    906  CA  LEU A 557     -45.444  -1.849  18.214  1.00 44.31           C  
ATOM    907  C   LEU A 557     -46.564  -2.554  17.457  1.00 50.33           C  
ATOM    908  O   LEU A 557     -47.353  -3.274  18.079  1.00 50.24           O  
ATOM    909  CB  LEU A 557     -45.996  -0.615  18.927  1.00 35.85           C  
ATOM    910  CG  LEU A 557     -45.084   0.002  19.989  1.00 44.98           C  
ATOM    911  CD1 LEU A 557     -45.631   1.341  20.458  1.00 45.56           C  
ATOM    912  CD2 LEU A 557     -44.899  -0.949  21.163  1.00 39.48           C  
ATOM    913  N   THR A 558     -46.664  -2.363  16.140  1.00 47.15           N  
ATOM    914  CA  THR A 558     -47.680  -3.090  15.387  1.00 46.34           C  
ATOM    915  C   THR A 558     -47.226  -4.510  15.077  1.00 52.97           C  
ATOM    916  O   THR A 558     -48.019  -5.454  15.167  1.00 58.00           O  
ATOM    917  CB  THR A 558     -48.020  -2.351  14.092  1.00 47.39           C  
ATOM    918  OG1 THR A 558     -46.828  -2.155  13.318  1.00 44.31           O  
ATOM    919  CG2 THR A 558     -48.661  -1.007  14.401  1.00 42.90           C  
ATOM    920  N   GLY A 559     -45.958  -4.681  14.721  1.00 49.57           N  
ATOM    921  CA  GLY A 559     -45.450  -5.985  14.352  1.00 38.09           C  
ATOM    922  C   GLY A 559     -44.799  -5.988  12.986  1.00 40.47           C  
ATOM    923  O   GLY A 559     -44.311  -7.025  12.521  1.00 50.04           O  
ATOM    924  N   GLN A 560     -44.801  -4.821  12.332  1.00 45.63           N  
ATOM    925  CA  GLN A 560     -44.117  -4.686  11.050  1.00 36.88           C  
ATOM    926  C   GLN A 560     -42.645  -5.057  11.172  1.00 44.02           C  
ATOM    927  O   GLN A 560     -42.149  -5.905  10.422  1.00 46.51           O  
ATOM    928  CB  GLN A 560     -44.268  -3.261  10.512  1.00 43.99           C  
ATOM    929  N   VAL A 561     -41.933  -4.445  12.122  1.00 47.53           N  
ATOM    930  CA  VAL A 561     -40.526  -4.739  12.357  1.00 41.52           C  
ATOM    931  C   VAL A 561     -40.357  -5.246  13.781  1.00 37.56           C  
ATOM    932  O   VAL A 561     -41.216  -5.048  14.643  1.00 38.65           O  
ATOM    933  CB  VAL A 561     -39.621  -3.513  12.124  1.00 40.13           C  
ATOM    934  CG1 VAL A 561     -39.728  -3.042  10.682  1.00 39.08           C  
ATOM    935  CG2 VAL A 561     -39.962  -2.399  13.119  1.00 34.91           C  
ATOM    936  N   ARG A 562     -39.223  -5.908  14.021  1.00 34.59           N  
ATOM    937  CA  ARG A 562     -38.866  -6.320  15.375  1.00 35.72           C  
ATOM    938  C   ARG A 562     -38.187  -5.182  16.129  1.00 42.44           C  
ATOM    939  O   ARG A 562     -38.663  -4.745  17.182  1.00 41.31           O  
ATOM    940  CB  ARG A 562     -37.953  -7.549  15.337  1.00 44.23           C  
ATOM    941  CG  ARG A 562     -37.296  -7.873  16.677  1.00 45.62           C  
ATOM    942  CD  ARG A 562     -38.102  -8.890  17.480  1.00 50.15           C  
ATOM    943  NE  ARG A 562     -38.098 -10.206  16.846  1.00 60.18           N  
ATOM    944  CZ  ARG A 562     -37.048 -11.021  16.808  1.00 66.94           C  
ATOM    945  NH1 ARG A 562     -35.903 -10.671  17.383  1.00 61.43           N  
ATOM    946  NH2 ARG A 562     -37.144 -12.194  16.198  1.00 70.35           N  
ATOM    947  N   ASN A 563     -37.066  -4.696  15.602  1.00 38.09           N  
ATOM    948  CA  ASN A 563     -36.339  -3.565  16.157  1.00 31.59           C  
ATOM    949  C   ASN A 563     -36.077  -2.563  15.041  1.00 39.05           C  
ATOM    950  O   ASN A 563     -36.329  -2.837  13.865  1.00 42.16           O  
ATOM    951  CB  ASN A 563     -35.029  -4.016  16.818  1.00 32.33           C  
ATOM    952  CG  ASN A 563     -34.260  -5.010  15.972  1.00 32.86           C  
ATOM    953  OD1 ASN A 563     -34.188  -4.880  14.751  1.00 36.06           O  
ATOM    954  ND2 ASN A 563     -33.684  -6.017  16.620  1.00 33.63           N  
ATOM    955  N   ALA A 564     -35.567  -1.389  15.410  1.00 35.30           N  
ATOM    956  CA  ALA A 564     -35.365  -0.337  14.423  1.00 33.22           C  
ATOM    957  C   ALA A 564     -34.275   0.618  14.887  1.00 33.51           C  
ATOM    958  O   ALA A 564     -33.940   0.689  16.074  1.00 30.71           O  
ATOM    959  CB  ALA A 564     -36.663   0.430  14.148  1.00 29.42           C  
ATOM    960  N   VAL A 565     -33.735   1.364  13.924  1.00 32.54           N  
ATOM    961  CA  VAL A 565     -32.688   2.351  14.157  1.00 32.51           C  
ATOM    962  C   VAL A 565     -33.088   3.650  13.466  1.00 31.42           C  
ATOM    963  O   VAL A 565     -33.646   3.630  12.362  1.00 33.77           O  
ATOM    964  CB  VAL A 565     -31.316   1.841  13.658  1.00 33.61           C  
ATOM    965  CG1 VAL A 565     -31.423   1.298  12.240  1.00 36.20           C  
ATOM    966  CG2 VAL A 565     -30.262   2.932  13.742  1.00 33.85           C  
ATOM    967  N   ALA A 566     -32.822   4.778  14.124  1.00 34.08           N  
ATOM    968  CA  ALA A 566     -33.222   6.100  13.645  1.00 27.48           C  
ATOM    969  C   ALA A 566     -31.989   6.986  13.515  1.00 28.39           C  
ATOM    970  O   ALA A 566     -31.379   7.367  14.523  1.00 27.62           O  
ATOM    971  CB  ALA A 566     -34.251   6.735  14.580  1.00 23.64           C  
ATOM    972  N   ILE A 567     -31.637   7.318  12.276  1.00 29.50           N  
ATOM    973  CA  ILE A 567     -30.497   8.181  11.973  1.00 33.14           C  
ATOM    974  C   ILE A 567     -31.068   9.581  11.769  1.00 38.33           C  
ATOM    975  O   ILE A 567     -31.388   9.989  10.652  1.00 43.44           O  
ATOM    976  CB  ILE A 567     -29.724   7.690  10.751  1.00 33.73           C  
ATOM    977  CG1 ILE A 567     -29.528   6.173  10.825  1.00 31.59           C  
ATOM    978  CG2 ILE A 567     -28.390   8.415  10.637  1.00 31.46           C  
ATOM    979  CD1 ILE A 567     -28.709   5.602   9.688  1.00 35.98           C  
ATOM    980  N   VAL A 568     -31.190  10.334  12.864  1.00 31.60           N  
ATOM    981  CA  VAL A 568     -31.891  11.609  12.852  1.00 27.27           C  
ATOM    982  C   VAL A 568     -31.019  12.698  13.463  1.00 36.43           C  
ATOM    983  O   VAL A 568     -30.045  12.431  14.171  1.00 38.93           O  
ATOM    984  CB  VAL A 568     -33.239  11.532  13.601  1.00 32.63           C  
ATOM    985  CG1 VAL A 568     -34.177  10.552  12.914  1.00 33.54           C  
ATOM    986  CG2 VAL A 568     -33.016  11.144  15.054  1.00 30.81           C  
ATOM    987  N   ARG A 569     -31.391  13.943  13.167  1.00 34.46           N  
ATOM    988  CA  ARG A 569     -30.801  15.136  13.760  1.00 37.03           C  
ATOM    989  C   ARG A 569     -31.781  16.281  13.558  1.00 36.27           C  
ATOM    990  O   ARG A 569     -32.547  16.264  12.588  1.00 33.74           O  
ATOM    991  CB  ARG A 569     -29.439  15.470  13.130  1.00 34.62           C  
ATOM    992  CG  ARG A 569     -29.508  15.996  11.704  1.00 29.97           C  
ATOM    993  CD  ARG A 569     -28.116  16.269  11.151  1.00 35.48           C  
ATOM    994  NE  ARG A 569     -27.494  17.436  11.773  1.00 42.90           N  
ATOM    995  CZ  ARG A 569     -27.698  18.690  11.380  1.00 41.31           C  
ATOM    996  NH1 ARG A 569     -28.509  18.944  10.363  1.00 42.01           N  
ATOM    997  NH2 ARG A 569     -27.091  19.692  12.001  1.00 43.10           N  
ATOM    998  N   PRO A 570     -31.798  17.283  14.454  1.00 38.16           N  
ATOM    999  CA  PRO A 570     -30.955  17.475  15.641  1.00 33.74           C  
ATOM   1000  C   PRO A 570     -31.299  16.524  16.789  1.00 33.16           C  
ATOM   1001  O   PRO A 570     -32.390  15.953  16.793  1.00 31.96           O  
ATOM   1002  CB  PRO A 570     -31.246  18.926  16.035  1.00 31.79           C  
ATOM   1003  CG  PRO A 570     -32.630  19.162  15.566  1.00 31.80           C  
ATOM   1004  CD  PRO A 570     -32.771  18.380  14.292  1.00 32.20           C  
ATOM   1005  N   PRO A 571     -30.376  16.356  17.750  1.00 34.21           N  
ATOM   1006  CA  PRO A 571     -30.656  15.481  18.899  1.00 31.90           C  
ATOM   1007  C   PRO A 571     -31.779  16.020  19.772  1.00 29.00           C  
ATOM   1008  O   PRO A 571     -32.352  17.071  19.466  1.00 28.80           O  
ATOM   1009  CB  PRO A 571     -29.319  15.445  19.655  1.00 31.46           C  
ATOM   1010  CG  PRO A 571     -28.298  15.974  18.690  1.00 37.45           C  
ATOM   1011  CD  PRO A 571     -29.022  16.930  17.807  1.00 30.15           C  
ATOM   1012  N   GLY A 572     -32.100  15.330  20.867  1.00 25.87           N  
ATOM   1013  CA  GLY A 572     -33.274  15.713  21.626  1.00 26.51           C  
ATOM   1014  C   GLY A 572     -33.229  15.645  23.141  1.00 28.58           C  
ATOM   1015  O   GLY A 572     -34.050  16.293  23.796  1.00 35.98           O  
ATOM   1016  N   HIS A 573     -32.301  14.888  23.727  1.00 27.78           N  
ATOM   1017  CA  HIS A 573     -32.428  14.583  25.150  1.00 32.04           C  
ATOM   1018  C   HIS A 573     -32.101  15.760  26.068  1.00 27.29           C  
ATOM   1019  O   HIS A 573     -32.388  15.678  27.267  1.00 30.78           O  
ATOM   1020  CB  HIS A 573     -31.566  13.369  25.524  1.00 28.76           C  
ATOM   1021  CG  HIS A 573     -30.093  13.583  25.367  1.00 27.25           C  
ATOM   1022  ND1 HIS A 573     -29.169  13.014  26.216  1.00 24.74           N  
ATOM   1023  CD2 HIS A 573     -29.382  14.285  24.453  1.00 27.05           C  
ATOM   1024  CE1 HIS A 573     -27.952  13.362  25.838  1.00 27.40           C  
ATOM   1025  NE2 HIS A 573     -28.054  14.135  24.772  1.00 30.54           N  
ATOM   1026  N   HIS A 574     -31.531  16.849  25.550  1.00 28.03           N  
ATOM   1027  CA  HIS A 574     -31.356  18.055  26.352  1.00 34.48           C  
ATOM   1028  C   HIS A 574     -32.576  18.961  26.332  1.00 33.88           C  
ATOM   1029  O   HIS A 574     -32.700  19.830  27.203  1.00 34.00           O  
ATOM   1030  CB  HIS A 574     -30.143  18.852  25.870  1.00 33.90           C  
ATOM   1031  CG  HIS A 574     -28.834  18.196  26.170  1.00 32.86           C  
ATOM   1032  ND1 HIS A 574     -28.468  17.815  27.443  1.00 29.40           N  
ATOM   1033  CD2 HIS A 574     -27.803  17.854  25.363  1.00 32.80           C  
ATOM   1034  CE1 HIS A 574     -27.268  17.264  27.406  1.00 38.05           C  
ATOM   1035  NE2 HIS A 574     -26.842  17.276  26.156  1.00 37.65           N  
ATOM   1036  N   ALA A 575     -33.468  18.782  25.362  1.00 33.07           N  
ATOM   1037  CA  ALA A 575     -34.663  19.605  25.274  1.00 32.54           C  
ATOM   1038  C   ALA A 575     -35.608  19.301  26.427  1.00 35.74           C  
ATOM   1039  O   ALA A 575     -35.830  18.140  26.781  1.00 38.33           O  
ATOM   1040  CB  ALA A 575     -35.371  19.372  23.942  1.00 32.01           C  
ATOM   1041  N   GLU A 576     -36.168  20.354  27.008  1.00 41.47           N  
ATOM   1042  CA  GLU A 576     -37.089  20.254  28.126  1.00 41.81           C  
ATOM   1043  C   GLU A 576     -38.488  20.658  27.675  1.00 39.98           C  
ATOM   1044  O   GLU A 576     -38.707  21.052  26.526  1.00 46.07           O  
ATOM   1045  CB  GLU A 576     -36.607  21.115  29.293  1.00 45.10           C  
ATOM   1046  CG  GLU A 576     -35.232  20.735  29.803  1.00 45.11           C  
ATOM   1047  CD  GLU A 576     -35.259  20.346  31.263  1.00 45.60           C  
ATOM   1048  OE1 GLU A 576     -36.307  19.842  31.719  1.00 49.80           O  
ATOM   1049  OE2 GLU A 576     -34.237  20.539  31.954  1.00 58.48           O  
ATOM   1050  N   LYS A 577     -39.443  20.551  28.603  1.00 38.55           N  
ATOM   1051  CA  LYS A 577     -40.830  20.879  28.287  1.00 43.27           C  
ATOM   1052  C   LYS A 577     -40.966  22.314  27.790  1.00 45.92           C  
ATOM   1053  O   LYS A 577     -41.758  22.591  26.882  1.00 49.27           O  
ATOM   1054  CB  LYS A 577     -41.712  20.649  29.518  1.00 44.49           C  
ATOM   1055  CG  LYS A 577     -42.882  21.617  29.663  1.00 46.71           C  
ATOM   1056  CD  LYS A 577     -44.157  20.900  30.081  1.00 44.91           C  
ATOM   1057  N   ASP A 578     -40.186  23.237  28.352  1.00 51.95           N  
ATOM   1058  CA  ASP A 578     -40.367  24.658  28.095  1.00 49.67           C  
ATOM   1059  C   ASP A 578     -39.194  25.327  27.391  1.00 46.08           C  
ATOM   1060  O   ASP A 578     -39.278  26.527  27.104  1.00 46.92           O  
ATOM   1061  CB  ASP A 578     -40.640  25.400  29.413  1.00 48.74           C  
ATOM   1062  CG  ASP A 578     -42.121  25.562  29.695  1.00 63.70           C  
ATOM   1063  OD1 ASP A 578     -42.743  26.467  29.099  1.00 63.69           O  
ATOM   1064  OD2 ASP A 578     -42.660  24.787  30.515  1.00 68.03           O  
ATOM   1065  N   THR A 579     -38.113  24.608  27.097  1.00 43.03           N  
ATOM   1066  CA  THR A 579     -36.926  25.282  26.588  1.00 44.18           C  
ATOM   1067  C   THR A 579     -36.105  24.336  25.723  1.00 42.62           C  
ATOM   1068  O   THR A 579     -36.255  23.113  25.782  1.00 46.32           O  
ATOM   1069  CB  THR A 579     -36.073  25.834  27.735  1.00 47.02           C  
ATOM   1070  OG1 THR A 579     -34.925  26.506  27.203  1.00 51.35           O  
ATOM   1071  CG2 THR A 579     -35.623  24.708  28.659  1.00 40.83           C  
ATOM   1072  N   ALA A 580     -35.231  24.933  24.914  1.00 40.14           N  
ATOM   1073  CA  ALA A 580     -34.288  24.216  24.070  1.00 35.04           C  
ATOM   1074  C   ALA A 580     -32.891  24.331  24.663  1.00 37.89           C  
ATOM   1075  O   ALA A 580     -32.497  25.398  25.143  1.00 40.22           O  
ATOM   1076  CB  ALA A 580     -34.297  24.768  22.641  1.00 36.04           C  
ATOM   1077  N   CYS A 581     -32.142  23.231  24.628  1.00 37.34           N  
ATOM   1078  CA  CYS A 581     -30.822  23.183  25.238  1.00 30.68           C  
ATOM   1079  C   CYS A 581     -29.906  22.304  24.401  1.00 32.15           C  
ATOM   1080  O   CYS A 581     -30.363  21.449  23.639  1.00 36.04           O  
ATOM   1081  CB  CYS A 581     -30.889  22.655  26.680  1.00 26.91           C  
ATOM   1082  SG  CYS A 581     -29.386  22.902  27.656  1.00 48.66           S  
ATOM   1083  N   GLY A 582     -28.602  22.542  24.553  1.00 34.70           N  
ATOM   1084  CA  GLY A 582     -27.544  21.719  23.989  1.00 38.50           C  
ATOM   1085  C   GLY A 582     -27.823  21.029  22.669  1.00 34.98           C  
ATOM   1086  O   GLY A 582     -27.886  19.798  22.611  1.00 39.52           O  
ATOM   1087  N   PHE A 583     -28.006  21.817  21.608  1.00 34.81           N  
ATOM   1088  CA  PHE A 583     -28.224  21.390  20.227  1.00 28.82           C  
ATOM   1089  C   PHE A 583     -29.594  20.759  20.002  1.00 30.58           C  
ATOM   1090  O   PHE A 583     -29.870  20.306  18.883  1.00 31.08           O  
ATOM   1091  CB  PHE A 583     -27.157  20.401  19.728  1.00 34.05           C  
ATOM   1092  CG  PHE A 583     -25.738  20.825  20.007  1.00 43.62           C  
ATOM   1093  CD1 PHE A 583     -25.414  22.156  20.215  1.00 43.42           C  
ATOM   1094  CD2 PHE A 583     -24.725  19.880  20.056  1.00 43.74           C  
ATOM   1095  CE1 PHE A 583     -24.113  22.534  20.474  1.00 47.44           C  
ATOM   1096  CE2 PHE A 583     -23.420  20.253  20.310  1.00 42.31           C  
ATOM   1097  CZ  PHE A 583     -23.113  21.581  20.520  1.00 47.77           C  
ATOM   1098  N   CYS A 584     -30.460  20.716  21.011  1.00 24.91           N  
ATOM   1099  CA  CYS A 584     -31.752  20.049  20.920  1.00 30.43           C  
ATOM   1100  C   CYS A 584     -32.881  21.068  20.978  1.00 29.40           C  
ATOM   1101  O   CYS A 584     -32.806  22.049  21.724  1.00 35.99           O  
ATOM   1102  CB  CYS A 584     -31.934  19.033  22.054  1.00 34.67           C  
ATOM   1103  SG  CYS A 584     -30.521  17.957  22.389  1.00 31.03           S  
ATOM   1104  N   PHE A 585     -33.934  20.818  20.200  1.00 34.86           N  
ATOM   1105  CA  PHE A 585     -35.139  21.641  20.198  1.00 30.74           C  
ATOM   1106  C   PHE A 585     -36.326  20.942  20.843  1.00 31.32           C  
ATOM   1107  O   PHE A 585     -36.994  21.522  21.705  1.00 33.61           O  
ATOM   1108  CB  PHE A 585     -35.498  22.051  18.763  1.00 28.16           C  
ATOM   1109  CG  PHE A 585     -34.451  22.886  18.091  1.00 29.45           C  
ATOM   1110  CD1 PHE A 585     -34.446  24.263  18.238  1.00 33.03           C  
ATOM   1111  CD2 PHE A 585     -33.470  22.297  17.312  1.00 32.54           C  
ATOM   1112  CE1 PHE A 585     -33.482  25.035  17.621  1.00 37.94           C  
ATOM   1113  CE2 PHE A 585     -32.503  23.064  16.693  1.00 35.49           C  
ATOM   1114  CZ  PHE A 585     -32.509  24.436  16.847  1.00 39.50           C  
ATOM   1115  N   PHE A 586     -36.613  19.707  20.436  1.00 32.46           N  
ATOM   1116  CA  PHE A 586     -37.657  18.895  21.041  1.00 37.84           C  
ATOM   1117  C   PHE A 586     -37.065  17.556  21.454  1.00 31.06           C  
ATOM   1118  O   PHE A 586     -36.130  17.056  20.824  1.00 32.84           O  
ATOM   1119  CB  PHE A 586     -38.836  18.678  20.081  1.00 36.48           C  
ATOM   1120  CG  PHE A 586     -39.376  19.948  19.491  1.00 37.93           C  
ATOM   1121  CD1 PHE A 586     -40.047  20.866  20.282  1.00 41.41           C  
ATOM   1122  CD2 PHE A 586     -39.210  20.228  18.145  1.00 38.93           C  
ATOM   1123  CE1 PHE A 586     -40.544  22.037  19.742  1.00 39.89           C  
ATOM   1124  CE2 PHE A 586     -39.705  21.398  17.599  1.00 40.68           C  
ATOM   1125  CZ  PHE A 586     -40.373  22.303  18.398  1.00 38.81           C  
ATOM   1126  N   ASN A 587     -37.614  16.978  22.521  1.00 34.72           N  
ATOM   1127  CA  ASN A 587     -37.086  15.732  23.076  1.00 32.96           C  
ATOM   1128  C   ASN A 587     -37.644  14.560  22.279  1.00 32.10           C  
ATOM   1129  O   ASN A 587     -38.757  14.094  22.530  1.00 30.72           O  
ATOM   1130  CB  ASN A 587     -37.429  15.607  24.555  1.00 34.16           C  
ATOM   1131  CG  ASN A 587     -36.552  14.596  25.270  1.00 38.37           C  
ATOM   1132  OD1 ASN A 587     -36.438  13.445  24.847  1.00 32.09           O  
ATOM   1133  ND2 ASN A 587     -35.915  15.027  26.353  1.00 36.60           N  
ATOM   1134  N   THR A 588     -36.849  14.066  21.328  1.00 27.65           N  
ATOM   1135  CA  THR A 588     -37.310  12.999  20.446  1.00 28.29           C  
ATOM   1136  C   THR A 588     -37.619  11.721  21.219  1.00 35.52           C  
ATOM   1137  O   THR A 588     -38.641  11.071  20.971  1.00 33.10           O  
ATOM   1138  CB  THR A 588     -36.265  12.733  19.363  1.00 32.04           C  
ATOM   1139  OG1 THR A 588     -35.966  13.957  18.678  1.00 28.07           O  
ATOM   1140  CG2 THR A 588     -36.787  11.718  18.367  1.00 22.77           C  
ATOM   1141  N   ALA A 589     -36.754  11.347  22.165  1.00 33.61           N  
ATOM   1142  CA  ALA A 589     -36.954  10.099  22.898  1.00 33.94           C  
ATOM   1143  C   ALA A 589     -38.195  10.166  23.780  1.00 32.76           C  
ATOM   1144  O   ALA A 589     -39.037   9.258  23.755  1.00 30.78           O  
ATOM   1145  CB  ALA A 589     -35.715   9.775  23.734  1.00 32.24           C  
ATOM   1146  N   ALA A 590     -38.323  11.235  24.570  1.00 30.31           N  
ATOM   1147  CA  ALA A 590     -39.491  11.395  25.431  1.00 33.39           C  
ATOM   1148  C   ALA A 590     -40.775  11.424  24.612  1.00 32.57           C  
ATOM   1149  O   ALA A 590     -41.770  10.778  24.966  1.00 38.73           O  
ATOM   1150  CB  ALA A 590     -39.354  12.670  26.265  1.00 33.21           C  
ATOM   1151  N   LEU A 591     -40.765  12.169  23.504  1.00 33.54           N  
ATOM   1152  CA  LEU A 591     -41.942  12.231  22.645  1.00 34.86           C  
ATOM   1153  C   LEU A 591     -42.264  10.867  22.052  1.00 33.35           C  
ATOM   1154  O   LEU A 591     -43.437  10.529  21.859  1.00 40.06           O  
ATOM   1155  CB  LEU A 591     -41.730  13.260  21.535  1.00 34.05           C  
ATOM   1156  CG  LEU A 591     -41.806  14.733  21.938  1.00 31.34           C  
ATOM   1157  CD1 LEU A 591     -41.316  15.611  20.801  1.00 35.44           C  
ATOM   1158  CD2 LEU A 591     -43.220  15.114  22.341  1.00 39.14           C  
ATOM   1159  N   THR A 592     -41.237  10.067  21.752  1.00 33.04           N  
ATOM   1160  CA  THR A 592     -41.482   8.734  21.214  1.00 31.48           C  
ATOM   1161  C   THR A 592     -42.066   7.805  22.270  1.00 36.23           C  
ATOM   1162  O   THR A 592     -42.897   6.948  21.948  1.00 37.39           O  
ATOM   1163  CB  THR A 592     -40.192   8.146  20.639  1.00 34.51           C  
ATOM   1164  OG1 THR A 592     -39.634   9.056  19.685  1.00 29.75           O  
ATOM   1165  CG2 THR A 592     -40.472   6.818  19.948  1.00 29.00           C  
ATOM   1166  N   ALA A 593     -41.656   7.961  23.531  1.00 33.70           N  
ATOM   1167  CA  ALA A 593     -42.276   7.186  24.601  1.00 35.25           C  
ATOM   1168  C   ALA A 593     -43.739   7.575  24.780  1.00 40.13           C  
ATOM   1169  O   ALA A 593     -44.625   6.710  24.818  1.00 41.74           O  
ATOM   1170  CB  ALA A 593     -41.500   7.374  25.905  1.00 34.44           C  
ATOM   1171  N   ARG A 594     -44.012   8.881  24.879  1.00 40.03           N  
ATOM   1172  CA  ARG A 594     -45.386   9.342  25.057  1.00 37.82           C  
ATOM   1173  C   ARG A 594     -46.270   8.927  23.887  1.00 37.73           C  
ATOM   1174  O   ARG A 594     -47.427   8.536  24.081  1.00 43.69           O  
ATOM   1175  CB  ARG A 594     -45.410  10.859  25.229  1.00 39.26           C  
ATOM   1176  CG  ARG A 594     -44.815  11.333  26.536  1.00 41.32           C  
ATOM   1177  CD  ARG A 594     -45.521  10.699  27.717  1.00 40.84           C  
ATOM   1178  NE  ARG A 594     -45.105  11.298  28.980  1.00 41.59           N  
ATOM   1179  CZ  ARG A 594     -45.306  10.741  30.169  1.00 43.00           C  
ATOM   1180  NH1 ARG A 594     -45.919   9.569  30.257  1.00 39.46           N  
ATOM   1181  NH2 ARG A 594     -44.892  11.356  31.269  1.00 46.10           N  
ATOM   1182  N   TYR A 595     -45.744   9.013  22.663  1.00 35.76           N  
ATOM   1183  CA  TYR A 595     -46.507   8.592  21.493  1.00 34.67           C  
ATOM   1184  C   TYR A 595     -46.751   7.090  21.510  1.00 39.97           C  
ATOM   1185  O   TYR A 595     -47.858   6.630  21.201  1.00 47.00           O  
ATOM   1186  CB  TYR A 595     -45.772   9.007  20.218  1.00 35.79           C  
ATOM   1187  CG  TYR A 595     -46.286   8.350  18.953  1.00 41.31           C  
ATOM   1188  CD1 TYR A 595     -47.333   8.911  18.235  1.00 40.90           C  
ATOM   1189  CD2 TYR A 595     -45.713   7.178  18.468  1.00 36.18           C  
ATOM   1190  CE1 TYR A 595     -47.804   8.321  17.077  1.00 39.54           C  
ATOM   1191  CE2 TYR A 595     -46.179   6.580  17.313  1.00 39.25           C  
ATOM   1192  CZ  TYR A 595     -47.224   7.156  16.622  1.00 36.54           C  
ATOM   1193  OH  TYR A 595     -47.691   6.569  15.470  1.00 44.97           O  
ATOM   1194  N   ALA A 596     -45.724   6.311  21.859  1.00 41.61           N  
ATOM   1195  CA  ALA A 596     -45.882   4.865  21.969  1.00 41.69           C  
ATOM   1196  C   ALA A 596     -46.983   4.509  22.957  1.00 39.73           C  
ATOM   1197  O   ALA A 596     -47.757   3.572  22.728  1.00 37.25           O  
ATOM   1198  CB  ALA A 596     -44.559   4.226  22.389  1.00 39.92           C  
ATOM   1199  N   GLN A 597     -47.069   5.251  24.063  1.00 43.93           N  
ATOM   1200  CA  GLN A 597     -48.170   5.048  24.998  1.00 45.81           C  
ATOM   1201  C   GLN A 597     -49.497   5.493  24.396  1.00 50.30           C  
ATOM   1202  O   GLN A 597     -50.540   4.883  24.658  1.00 52.91           O  
ATOM   1203  CB  GLN A 597     -47.900   5.800  26.301  1.00 45.76           C  
ATOM   1204  CG  GLN A 597     -46.712   5.278  27.087  1.00 42.84           C  
ATOM   1205  CD  GLN A 597     -46.397   6.134  28.296  1.00 46.89           C  
ATOM   1206  OE1 GLN A 597     -46.625   7.344  28.291  1.00 47.98           O  
ATOM   1207  NE2 GLN A 597     -45.868   5.509  29.341  1.00 49.31           N  
ATOM   1208  N   SER A 598     -49.479   6.551  23.580  1.00 46.25           N  
ATOM   1209  CA  SER A 598     -50.726   7.103  23.059  1.00 47.32           C  
ATOM   1210  C   SER A 598     -51.341   6.214  21.986  1.00 48.46           C  
ATOM   1211  O   SER A 598     -52.563   6.236  21.797  1.00 58.09           O  
ATOM   1212  CB  SER A 598     -50.494   8.514  22.516  1.00 45.47           C  
ATOM   1213  OG  SER A 598     -49.952   8.481  21.208  1.00 44.44           O  
ATOM   1214  N   ILE A 599     -50.527   5.429  21.275  1.00 43.88           N  
ATOM   1215  CA  ILE A 599     -51.052   4.495  20.284  1.00 44.30           C  
ATOM   1216  C   ILE A 599     -51.239   3.095  20.847  1.00 51.96           C  
ATOM   1217  O   ILE A 599     -51.755   2.215  20.143  1.00 51.87           O  
ATOM   1218  CB  ILE A 599     -50.163   4.457  19.025  1.00 45.44           C  
ATOM   1219  CG1 ILE A 599     -48.924   3.589  19.256  1.00 44.28           C  
ATOM   1220  CG2 ILE A 599     -49.775   5.865  18.619  1.00 45.75           C  
ATOM   1221  CD1 ILE A 599     -48.135   3.315  17.992  1.00 38.43           C  
ATOM   1222  N   THR A 600     -50.831   2.858  22.093  1.00 54.99           N  
ATOM   1223  CA  THR A 600     -51.168   1.628  22.799  1.00 49.67           C  
ATOM   1224  C   THR A 600     -52.001   1.972  24.028  1.00 58.49           C  
ATOM   1225  O   THR A 600     -53.175   2.337  23.905  1.00 61.51           O  
ATOM   1226  CB  THR A 600     -49.909   0.855  23.198  1.00 46.02           C  
ATOM   1227  OG1 THR A 600     -49.058   1.696  23.985  1.00 51.96           O  
ATOM   1228  CG2 THR A 600     -49.155   0.392  21.963  1.00 43.18           C  
ATOM   1229  N   ARG A 601     -51.404   1.877  25.214  1.00 53.06           N  
ATOM   1230  CA  ARG A 601     -52.071   2.256  26.449  1.00 51.17           C  
ATOM   1231  C   ARG A 601     -51.171   3.190  27.246  1.00 52.11           C  
ATOM   1232  O   ARG A 601     -49.954   3.234  27.048  1.00 52.74           O  
ATOM   1233  CB  ARG A 601     -52.449   1.027  27.289  1.00 57.16           C  
ATOM   1234  CG  ARG A 601     -51.454   0.687  28.379  1.00 55.81           C  
ATOM   1235  CD  ARG A 601     -51.224  -0.807  28.476  1.00 58.39           C  
ATOM   1236  NE  ARG A 601     -50.154  -1.121  29.417  1.00 58.77           N  
ATOM   1237  CZ  ARG A 601     -49.312  -2.138  29.275  1.00 58.47           C  
ATOM   1238  NH1 ARG A 601     -48.366  -2.348  30.180  1.00 57.83           N  
ATOM   1239  NH2 ARG A 601     -49.417  -2.945  28.228  1.00 52.07           N  
ATOM   1240  N   GLU A 602     -51.792   3.943  28.158  1.00 56.36           N  
ATOM   1241  CA  GLU A 602     -51.062   4.955  28.916  1.00 54.25           C  
ATOM   1242  C   GLU A 602     -50.024   4.335  29.846  1.00 54.95           C  
ATOM   1243  O   GLU A 602     -48.977   4.944  30.098  1.00 54.21           O  
ATOM   1244  CB  GLU A 602     -52.050   5.818  29.708  1.00 49.68           C  
ATOM   1245  CG  GLU A 602     -51.421   6.728  30.753  1.00 46.82           C  
ATOM   1246  CD  GLU A 602     -52.433   7.649  31.414  1.00 59.55           C  
ATOM   1247  OE1 GLU A 602     -52.598   8.794  30.941  1.00 58.93           O  
ATOM   1248  OE2 GLU A 602     -53.063   7.228  32.406  1.00 59.43           O  
ATOM   1249  N   SER A 603     -50.280   3.129  30.348  1.00 54.87           N  
ATOM   1250  CA  SER A 603     -49.408   2.493  31.328  1.00 53.27           C  
ATOM   1251  C   SER A 603     -48.274   1.691  30.700  1.00 58.41           C  
ATOM   1252  O   SER A 603     -47.520   1.045  31.437  1.00 61.02           O  
ATOM   1253  CB  SER A 603     -50.228   1.578  32.244  1.00 55.80           C  
ATOM   1254  OG  SER A 603     -50.825   0.522  31.511  1.00 63.48           O  
ATOM   1255  N   LEU A 604     -48.133   1.718  29.373  1.00 56.99           N  
ATOM   1256  CA  LEU A 604     -47.116   0.928  28.684  1.00 50.33           C  
ATOM   1257  C   LEU A 604     -45.728   1.219  29.237  1.00 49.56           C  
ATOM   1258  O   LEU A 604     -45.286   2.372  29.264  1.00 49.09           O  
ATOM   1259  CB  LEU A 604     -47.163   1.219  27.181  1.00 49.63           C  
ATOM   1260  CG  LEU A 604     -46.036   0.638  26.320  1.00 46.97           C  
ATOM   1261  CD1 LEU A 604     -46.435  -0.717  25.766  1.00 45.61           C  
ATOM   1262  CD2 LEU A 604     -45.660   1.586  25.189  1.00 43.65           C  
ATOM   1263  N   ARG A 605     -45.043   0.166  29.680  1.00 47.42           N  
ATOM   1264  CA  ARG A 605     -43.743   0.306  30.328  1.00 45.50           C  
ATOM   1265  C   ARG A 605     -42.673   0.549  29.270  1.00 42.58           C  
ATOM   1266  O   ARG A 605     -42.349  -0.348  28.484  1.00 43.44           O  
ATOM   1267  CB  ARG A 605     -43.436  -0.935  31.159  1.00 42.74           C  
ATOM   1268  CG  ARG A 605     -44.296  -1.061  32.408  1.00 43.42           C  
ATOM   1269  CD  ARG A 605     -43.893  -2.260  33.251  1.00 41.17           C  
ATOM   1270  NE  ARG A 605     -43.844  -3.494  32.470  1.00 43.27           N  
ATOM   1271  CZ  ARG A 605     -44.912  -4.214  32.138  1.00 42.45           C  
ATOM   1272  NH1 ARG A 605     -44.770  -5.322  31.423  1.00 45.81           N  
ATOM   1273  NH2 ARG A 605     -46.121  -3.827  32.520  1.00 41.94           N  
ATOM   1274  N   VAL A 606     -42.117   1.760  29.253  1.00 41.37           N  
ATOM   1275  CA  VAL A 606     -41.097   2.161  28.290  1.00 40.79           C  
ATOM   1276  C   VAL A 606     -39.785   2.373  29.029  1.00 39.70           C  
ATOM   1277  O   VAL A 606     -39.735   3.109  30.023  1.00 33.23           O  
ATOM   1278  CB  VAL A 606     -41.502   3.435  27.530  1.00 34.15           C  
ATOM   1279  CG1 VAL A 606     -40.460   3.768  26.469  1.00 30.82           C  
ATOM   1280  CG2 VAL A 606     -42.875   3.268  26.904  1.00 41.24           C  
ATOM   1281  N   LEU A 607     -38.725   1.738  28.538  1.00 39.34           N  
ATOM   1282  CA  LEU A 607     -37.389   1.869  29.104  1.00 34.09           C  
ATOM   1283  C   LEU A 607     -36.543   2.740  28.185  1.00 28.03           C  
ATOM   1284  O   LEU A 607     -36.315   2.382  27.026  1.00 32.44           O  
ATOM   1285  CB  LEU A 607     -36.738   0.498  29.287  1.00 32.52           C  
ATOM   1286  CG  LEU A 607     -35.226   0.483  29.530  1.00 27.28           C  
ATOM   1287  CD1 LEU A 607     -34.852   1.259  30.789  1.00 23.38           C  
ATOM   1288  CD2 LEU A 607     -34.706  -0.942  29.595  1.00 26.41           C  
ATOM   1289  N   ILE A 608     -36.077   3.871  28.700  1.00 26.88           N  
ATOM   1290  CA  ILE A 608     -35.175   4.754  27.971  1.00 25.36           C  
ATOM   1291  C   ILE A 608     -33.776   4.569  28.539  1.00 25.73           C  
ATOM   1292  O   ILE A 608     -33.542   4.816  29.728  1.00 27.48           O  
ATOM   1293  CB  ILE A 608     -35.621   6.221  28.065  1.00 29.27           C  
ATOM   1294  CG1 ILE A 608     -36.961   6.422  27.355  1.00 28.19           C  
ATOM   1295  CG2 ILE A 608     -34.561   7.139  27.474  1.00 29.97           C  
ATOM   1296  CD1 ILE A 608     -37.458   7.852  27.389  1.00 25.97           C  
ATOM   1297  N   VAL A 609     -32.848   4.126  27.696  1.00 25.76           N  
ATOM   1298  CA  VAL A 609     -31.451   3.950  28.078  1.00 24.89           C  
ATOM   1299  C   VAL A 609     -30.637   4.982  27.312  1.00 25.46           C  
ATOM   1300  O   VAL A 609     -30.513   4.909  26.084  1.00 28.05           O  
ATOM   1301  CB  VAL A 609     -30.952   2.526  27.805  1.00 22.57           C  
ATOM   1302  CG1 VAL A 609     -29.450   2.443  28.038  1.00 22.58           C  
ATOM   1303  CG2 VAL A 609     -31.683   1.540  28.694  1.00 19.18           C  
ATOM   1304  N   ASP A 610     -30.082   5.940  28.044  1.00 26.61           N  
ATOM   1305  CA  ASP A 610     -29.353   7.076  27.489  1.00 24.16           C  
ATOM   1306  C   ASP A 610     -27.869   6.820  27.721  1.00 25.02           C  
ATOM   1307  O   ASP A 610     -27.365   7.008  28.830  1.00 23.89           O  
ATOM   1308  CB  ASP A 610     -29.820   8.366  28.159  1.00 31.44           C  
ATOM   1309  CG  ASP A 610     -29.310   9.618  27.468  1.00 30.06           C  
ATOM   1310  OD1 ASP A 610     -28.321   9.539  26.709  1.00 33.10           O  
ATOM   1311  OD2 ASP A 610     -29.905  10.692  27.696  1.00 24.82           O  
ATOM   1312  N   TRP A 611     -27.165   6.378  26.679  1.00 26.48           N  
ATOM   1313  CA  TRP A 611     -25.734   6.126  26.794  1.00 24.14           C  
ATOM   1314  C   TRP A 611     -24.899   7.204  26.120  1.00 24.85           C  
ATOM   1315  O   TRP A 611     -23.684   7.035  25.974  1.00 25.61           O  
ATOM   1316  CB  TRP A 611     -25.380   4.729  26.262  1.00 27.74           C  
ATOM   1317  CG  TRP A 611     -25.429   4.498  24.763  1.00 25.65           C  
ATOM   1318  CD1 TRP A 611     -25.022   5.344  23.772  1.00 25.32           C  
ATOM   1319  CD2 TRP A 611     -25.879   3.305  24.106  1.00 27.54           C  
ATOM   1320  NE1 TRP A 611     -25.208   4.762  22.542  1.00 31.11           N  
ATOM   1321  CE2 TRP A 611     -25.733   3.510  22.720  1.00 28.11           C  
ATOM   1322  CE3 TRP A 611     -26.401   2.089  24.556  1.00 26.63           C  
ATOM   1323  CZ2 TRP A 611     -26.090   2.544  21.781  1.00 29.57           C  
ATOM   1324  CZ3 TRP A 611     -26.754   1.131  23.622  1.00 27.04           C  
ATOM   1325  CH2 TRP A 611     -26.597   1.364  22.252  1.00 25.26           C  
ATOM   1326  N   ASP A 612     -25.526   8.297  25.689  1.00 31.75           N  
ATOM   1327  CA  ASP A 612     -24.788   9.499  25.330  1.00 29.08           C  
ATOM   1328  C   ASP A 612     -23.934   9.940  26.512  1.00 31.02           C  
ATOM   1329  O   ASP A 612     -24.336   9.802  27.669  1.00 27.90           O  
ATOM   1330  CB  ASP A 612     -25.767  10.605  24.927  1.00 28.44           C  
ATOM   1331  CG  ASP A 612     -25.071  11.881  24.500  1.00 32.81           C  
ATOM   1332  OD1 ASP A 612     -24.663  12.663  25.384  1.00 36.91           O  
ATOM   1333  OD2 ASP A 612     -24.945  12.108  23.279  1.00 30.38           O  
ATOM   1334  N   VAL A 613     -22.740  10.464  26.222  1.00 30.78           N  
ATOM   1335  CA  VAL A 613     -21.815  10.806  27.298  1.00 30.76           C  
ATOM   1336  C   VAL A 613     -22.348  11.937  28.171  1.00 31.27           C  
ATOM   1337  O   VAL A 613     -21.907  12.088  29.317  1.00 32.76           O  
ATOM   1338  CB  VAL A 613     -20.426  11.157  26.727  1.00 33.38           C  
ATOM   1339  CG1 VAL A 613     -20.383  12.598  26.251  1.00 33.44           C  
ATOM   1340  CG2 VAL A 613     -19.340  10.895  27.763  1.00 36.21           C  
ATOM   1341  N   HIS A 614     -23.298  12.723  27.673  1.00 26.26           N  
ATOM   1342  CA  HIS A 614     -23.897  13.808  28.434  1.00 29.91           C  
ATOM   1343  C   HIS A 614     -25.194  13.345  29.086  1.00 27.87           C  
ATOM   1344  O   HIS A 614     -25.884  12.459  28.580  1.00 25.41           O  
ATOM   1345  CB  HIS A 614     -24.173  15.019  27.537  1.00 31.65           C  
ATOM   1346  CG  HIS A 614     -22.939  15.633  26.955  1.00 36.84           C  
ATOM   1347  ND1 HIS A 614     -22.378  15.201  25.773  1.00 33.26           N  
ATOM   1348  CD2 HIS A 614     -22.153  16.643  27.397  1.00 36.36           C  
ATOM   1349  CE1 HIS A 614     -21.301  15.920  25.510  1.00 33.69           C  
ATOM   1350  NE2 HIS A 614     -21.142  16.802  26.480  1.00 40.44           N  
ATOM   1351  N   HIS A 615     -25.519  13.958  30.220  1.00 25.71           N  
ATOM   1352  CA  HIS A 615     -26.764  13.644  30.903  1.00 26.13           C  
ATOM   1353  C   HIS A 615     -27.954  14.186  30.121  1.00 29.92           C  
ATOM   1354  O   HIS A 615     -27.928  15.312  29.617  1.00 29.88           O  
ATOM   1355  CB  HIS A 615     -26.757  14.231  32.314  1.00 27.75           C  
ATOM   1356  CG  HIS A 615     -27.993  13.929  33.103  1.00 31.12           C  
ATOM   1357  ND1 HIS A 615     -28.710  14.903  33.762  1.00 34.74           N  
ATOM   1358  CD2 HIS A 615     -28.634  12.761  33.346  1.00 32.43           C  
ATOM   1359  CE1 HIS A 615     -29.742  14.350  34.374  1.00 34.51           C  
ATOM   1360  NE2 HIS A 615     -29.719  13.051  34.137  1.00 31.64           N  
ATOM   1361  N   GLY A 616     -29.004  13.376  30.021  1.00 26.45           N  
ATOM   1362  CA  GLY A 616     -30.231  13.817  29.388  1.00 28.96           C  
ATOM   1363  C   GLY A 616     -31.161  14.501  30.369  1.00 32.36           C  
ATOM   1364  O   GLY A 616     -32.137  13.902  30.832  1.00 27.70           O  
ATOM   1365  N   ASN A 617     -30.857  15.763  30.691  1.00 33.57           N  
ATOM   1366  CA  ASN A 617     -31.640  16.500  31.681  1.00 33.36           C  
ATOM   1367  C   ASN A 617     -33.102  16.610  31.267  1.00 37.08           C  
ATOM   1368  O   ASN A 617     -34.004  16.519  32.111  1.00 38.38           O  
ATOM   1369  CB  ASN A 617     -31.037  17.890  31.884  1.00 31.14           C  
ATOM   1370  CG  ASN A 617     -30.757  18.600  30.571  1.00 38.28           C  
ATOM   1371  OD1 ASN A 617     -29.808  18.264  29.859  1.00 34.39           O  
ATOM   1372  ND2 ASN A 617     -31.587  19.584  30.241  1.00 40.37           N  
ATOM   1373  N   GLY A 618     -33.355  16.799  29.971  1.00 33.52           N  
ATOM   1374  CA  GLY A 618     -34.725  16.958  29.513  1.00 33.21           C  
ATOM   1375  C   GLY A 618     -35.565  15.718  29.738  1.00 35.72           C  
ATOM   1376  O   GLY A 618     -36.701  15.804  30.210  1.00 38.84           O  
ATOM   1377  N   THR A 619     -35.018  14.546  29.409  1.00 37.12           N  
ATOM   1378  CA  THR A 619     -35.758  13.304  29.608  1.00 30.89           C  
ATOM   1379  C   THR A 619     -35.981  13.025  31.089  1.00 30.54           C  
ATOM   1380  O   THR A 619     -37.079  12.616  31.494  1.00 35.31           O  
ATOM   1381  CB  THR A 619     -35.014  12.143  28.953  1.00 34.56           C  
ATOM   1382  OG1 THR A 619     -34.425  12.585  27.722  1.00 28.18           O  
ATOM   1383  CG2 THR A 619     -35.967  10.996  28.676  1.00 29.19           C  
ATOM   1384  N   GLN A 620     -34.948  13.240  31.908  1.00 29.55           N  
ATOM   1385  CA  GLN A 620     -35.089  13.061  33.349  1.00 32.12           C  
ATOM   1386  C   GLN A 620     -36.211  13.928  33.900  1.00 36.66           C  
ATOM   1387  O   GLN A 620     -37.122  13.430  34.570  1.00 42.16           O  
ATOM   1388  CB  GLN A 620     -33.774  13.384  34.055  1.00 33.04           C  
ATOM   1389  CG  GLN A 620     -33.942  13.653  35.542  1.00 33.12           C  
ATOM   1390  CD  GLN A 620     -32.654  13.481  36.317  1.00 39.86           C  
ATOM   1391  OE1 GLN A 620     -31.780  12.710  35.924  1.00 41.13           O  
ATOM   1392  NE2 GLN A 620     -32.530  14.200  37.428  1.00 40.75           N  
ATOM   1393  N   HIS A 621     -36.170  15.234  33.615  1.00 34.42           N  
ATOM   1394  CA  HIS A 621     -37.193  16.132  34.143  1.00 38.10           C  
ATOM   1395  C   HIS A 621     -38.566  15.845  33.548  1.00 33.49           C  
ATOM   1396  O   HIS A 621     -39.585  16.104  34.197  1.00 34.07           O  
ATOM   1397  CB  HIS A 621     -36.803  17.585  33.886  1.00 34.55           C  
ATOM   1398  CG  HIS A 621     -35.554  18.007  34.592  1.00 37.42           C  
ATOM   1399  ND1 HIS A 621     -34.595  18.799  33.999  1.00 43.19           N  
ATOM   1400  CD2 HIS A 621     -35.106  17.747  35.843  1.00 43.98           C  
ATOM   1401  CE1 HIS A 621     -33.611  19.010  34.854  1.00 47.78           C  
ATOM   1402  NE2 HIS A 621     -33.896  18.382  35.980  1.00 56.29           N  
ATOM   1403  N   ILE A 622     -38.617  15.317  32.324  1.00 31.95           N  
ATOM   1404  CA  ILE A 622     -39.903  15.025  31.701  1.00 32.21           C  
ATOM   1405  C   ILE A 622     -40.558  13.818  32.363  1.00 39.82           C  
ATOM   1406  O   ILE A 622     -41.778  13.797  32.570  1.00 37.40           O  
ATOM   1407  CB  ILE A 622     -39.727  14.828  30.182  1.00 32.77           C  
ATOM   1408  CG1 ILE A 622     -39.691  16.184  29.471  1.00 31.45           C  
ATOM   1409  CG2 ILE A 622     -40.840  13.962  29.610  1.00 33.36           C  
ATOM   1410  CD1 ILE A 622     -39.274  16.105  28.018  1.00 31.05           C  
ATOM   1411  N   PHE A 623     -39.768  12.804  32.727  1.00 39.52           N  
ATOM   1412  CA  PHE A 623     -40.311  11.599  33.346  1.00 38.85           C  
ATOM   1413  C   PHE A 623     -39.980  11.490  34.832  1.00 43.44           C  
ATOM   1414  O   PHE A 623     -40.095  10.403  35.405  1.00 44.29           O  
ATOM   1415  CB  PHE A 623     -39.814  10.354  32.612  1.00 38.41           C  
ATOM   1416  CG  PHE A 623     -40.242  10.286  31.179  1.00 42.11           C  
ATOM   1417  CD1 PHE A 623     -41.559  10.018  30.847  1.00 40.18           C  
ATOM   1418  CD2 PHE A 623     -39.326  10.487  30.162  1.00 41.88           C  
ATOM   1419  CE1 PHE A 623     -41.955   9.954  29.526  1.00 40.87           C  
ATOM   1420  CE2 PHE A 623     -39.714  10.422  28.842  1.00 39.32           C  
ATOM   1421  CZ  PHE A 623     -41.031  10.157  28.522  1.00 40.10           C  
ATOM   1422  N   GLU A 624     -39.597  12.597  35.474  1.00 42.91           N  
ATOM   1423  CA  GLU A 624     -39.103  12.532  36.848  1.00 45.63           C  
ATOM   1424  C   GLU A 624     -40.144  11.952  37.801  1.00 50.29           C  
ATOM   1425  O   GLU A 624     -39.809  11.157  38.686  1.00 52.74           O  
ATOM   1426  CB  GLU A 624     -38.669  13.922  37.312  1.00 49.36           C  
ATOM   1427  CG  GLU A 624     -37.548  13.916  38.336  1.00 51.86           C  
ATOM   1428  CD  GLU A 624     -36.895  15.275  38.488  1.00 57.68           C  
ATOM   1429  OE1 GLU A 624     -37.489  16.276  38.034  1.00 60.62           O  
ATOM   1430  OE2 GLU A 624     -35.787  15.342  39.060  1.00 61.88           O  
ATOM   1431  N   GLU A 625     -41.410  12.332  37.636  1.00 54.27           N  
ATOM   1432  CA  GLU A 625     -42.482  11.889  38.518  1.00 52.83           C  
ATOM   1433  C   GLU A 625     -43.310  10.762  37.910  1.00 49.56           C  
ATOM   1434  O   GLU A 625     -44.457  10.554  38.319  1.00 47.81           O  
ATOM   1435  CB  GLU A 625     -43.385  13.070  38.879  1.00 56.07           C  
ATOM   1436  CG  GLU A 625     -42.642  14.268  39.453  1.00 58.75           C  
ATOM   1437  CD  GLU A 625     -43.392  15.572  39.251  1.00 70.71           C  
ATOM   1438  OE1 GLU A 625     -44.302  15.609  38.396  1.00 74.94           O  
ATOM   1439  OE2 GLU A 625     -43.070  16.560  39.945  1.00 69.16           O  
ATOM   1440  N   ASP A 626     -42.749  10.025  36.955  1.00 51.21           N  
ATOM   1441  CA  ASP A 626     -43.483   9.030  36.186  1.00 47.49           C  
ATOM   1442  C   ASP A 626     -42.894   7.649  36.440  1.00 50.63           C  
ATOM   1443  O   ASP A 626     -41.671   7.477  36.411  1.00 47.96           O  
ATOM   1444  CB  ASP A 626     -43.438   9.367  34.691  1.00 45.71           C  
ATOM   1445  CG  ASP A 626     -44.397   8.527  33.868  1.00 50.47           C  
ATOM   1446  OD1 ASP A 626     -45.081   7.651  34.440  1.00 54.33           O  
ATOM   1447  OD2 ASP A 626     -44.472   8.751  32.641  1.00 50.73           O  
ATOM   1448  N   ASP A 627     -43.766   6.668  36.679  1.00 49.97           N  
ATOM   1449  CA  ASP A 627     -43.343   5.292  36.898  1.00 48.42           C  
ATOM   1450  C   ASP A 627     -43.568   4.392  35.689  1.00 49.16           C  
ATOM   1451  O   ASP A 627     -43.124   3.239  35.706  1.00 49.65           O  
ATOM   1452  CB  ASP A 627     -44.063   4.698  38.119  1.00 51.22           C  
ATOM   1453  CG  ASP A 627     -45.574   4.856  38.052  1.00 53.59           C  
ATOM   1454  OD1 ASP A 627     -46.157   4.673  36.963  1.00 52.86           O  
ATOM   1455  OD2 ASP A 627     -46.182   5.156  39.101  1.00 62.04           O  
ATOM   1456  N   SER A 628     -44.248   4.881  34.651  1.00 46.63           N  
ATOM   1457  CA  SER A 628     -44.469   4.092  33.447  1.00 43.39           C  
ATOM   1458  C   SER A 628     -43.285   4.130  32.490  1.00 39.59           C  
ATOM   1459  O   SER A 628     -43.219   3.297  31.580  1.00 39.05           O  
ATOM   1460  CB  SER A 628     -45.729   4.575  32.722  1.00 48.01           C  
ATOM   1461  OG  SER A 628     -45.612   5.936  32.342  1.00 47.17           O  
ATOM   1462  N   VAL A 629     -42.357   5.066  32.671  1.00 39.37           N  
ATOM   1463  CA  VAL A 629     -41.184   5.205  31.815  1.00 40.91           C  
ATOM   1464  C   VAL A 629     -39.955   5.189  32.712  1.00 46.50           C  
ATOM   1465  O   VAL A 629     -39.685   6.169  33.417  1.00 42.55           O  
ATOM   1466  CB  VAL A 629     -41.226   6.489  30.975  1.00 41.23           C  
ATOM   1467  CG1 VAL A 629     -39.910   6.683  30.234  1.00 37.23           C  
ATOM   1468  CG2 VAL A 629     -42.394   6.450  30.003  1.00 42.45           C  
ATOM   1469  N   LEU A 630     -39.212   4.084  32.690  1.00 42.07           N  
ATOM   1470  CA  LEU A 630     -37.969   3.987  33.445  1.00 33.79           C  
ATOM   1471  C   LEU A 630     -36.841   4.634  32.649  1.00 33.43           C  
ATOM   1472  O   LEU A 630     -36.553   4.221  31.522  1.00 32.18           O  
ATOM   1473  CB  LEU A 630     -37.644   2.528  33.755  1.00 31.82           C  
ATOM   1474  CG  LEU A 630     -36.212   2.241  34.213  1.00 32.81           C  
ATOM   1475  CD1 LEU A 630     -35.937   2.868  35.571  1.00 32.92           C  
ATOM   1476  CD2 LEU A 630     -35.949   0.745  34.247  1.00 31.68           C  
ATOM   1477  N   TYR A 631     -36.208   5.647  33.231  1.00 29.21           N  
ATOM   1478  CA  TYR A 631     -35.113   6.366  32.594  1.00 28.56           C  
ATOM   1479  C   TYR A 631     -33.805   5.969  33.265  1.00 26.38           C  
ATOM   1480  O   TYR A 631     -33.666   6.102  34.484  1.00 28.42           O  
ATOM   1481  CB  TYR A 631     -35.327   7.878  32.683  1.00 30.49           C  
ATOM   1482  CG  TYR A 631     -34.209   8.688  32.068  1.00 26.16           C  
ATOM   1483  CD1 TYR A 631     -33.978   8.659  30.699  1.00 30.81           C  
ATOM   1484  CD2 TYR A 631     -33.380   9.477  32.856  1.00 26.10           C  
ATOM   1485  CE1 TYR A 631     -32.956   9.395  30.131  1.00 31.01           C  
ATOM   1486  CE2 TYR A 631     -32.354  10.216  32.297  1.00 25.86           C  
ATOM   1487  CZ  TYR A 631     -32.147  10.170  30.934  1.00 27.55           C  
ATOM   1488  OH  TYR A 631     -31.128  10.900  30.369  1.00 25.15           O  
ATOM   1489  N   ILE A 632     -32.856   5.478  32.473  1.00 25.16           N  
ATOM   1490  CA  ILE A 632     -31.524   5.127  32.954  1.00 26.25           C  
ATOM   1491  C   ILE A 632     -30.512   5.845  32.077  1.00 24.60           C  
ATOM   1492  O   ILE A 632     -30.596   5.771  30.848  1.00 28.90           O  
ATOM   1493  CB  ILE A 632     -31.278   3.606  32.922  1.00 24.29           C  
ATOM   1494  CG1 ILE A 632     -32.356   2.863  33.713  1.00 27.27           C  
ATOM   1495  CG2 ILE A 632     -29.890   3.283  33.460  1.00 22.51           C  
ATOM   1496  CD1 ILE A 632     -32.232   1.353  33.643  1.00 25.21           C  
ATOM   1497  N   SER A 633     -29.560   6.535  32.699  1.00 25.92           N  
ATOM   1498  CA  SER A 633     -28.574   7.315  31.965  1.00 25.92           C  
ATOM   1499  C   SER A 633     -27.170   6.968  32.436  1.00 22.34           C  
ATOM   1500  O   SER A 633     -26.943   6.745  33.625  1.00 25.63           O  
ATOM   1501  CB  SER A 633     -28.822   8.824  32.135  1.00 28.35           C  
ATOM   1502  OG  SER A 633     -27.814   9.590  31.496  1.00 23.77           O  
ATOM   1503  N   LEU A 634     -26.237   6.910  31.490  1.00 25.51           N  
ATOM   1504  CA  LEU A 634     -24.810   6.809  31.767  1.00 26.38           C  
ATOM   1505  C   LEU A 634     -24.165   8.084  31.250  1.00 27.63           C  
ATOM   1506  O   LEU A 634     -24.313   8.411  30.069  1.00 31.93           O  
ATOM   1507  CB  LEU A 634     -24.162   5.594  31.079  1.00 23.02           C  
ATOM   1508  CG  LEU A 634     -24.587   4.115  31.131  1.00 25.66           C  
ATOM   1509  CD1 LEU A 634     -23.816   3.377  32.219  1.00 25.84           C  
ATOM   1510  CD2 LEU A 634     -26.091   3.865  31.264  1.00 27.91           C  
ATOM   1511  N   HIS A 635     -23.456   8.811  32.114  1.00 24.71           N  
ATOM   1512  CA  HIS A 635     -22.969  10.105  31.652  1.00 28.10           C  
ATOM   1513  C   HIS A 635     -21.716  10.527  32.403  1.00 32.27           C  
ATOM   1514  O   HIS A 635     -21.603  10.304  33.610  1.00 32.48           O  
ATOM   1515  CB  HIS A 635     -24.046  11.181  31.811  1.00 26.68           C  
ATOM   1516  CG  HIS A 635     -24.761  11.119  33.123  1.00 29.40           C  
ATOM   1517  ND1 HIS A 635     -25.946  10.436  33.292  1.00 28.15           N  
ATOM   1518  CD2 HIS A 635     -24.451  11.641  34.333  1.00 30.62           C  
ATOM   1519  CE1 HIS A 635     -26.339  10.546  34.548  1.00 31.41           C  
ATOM   1520  NE2 HIS A 635     -25.450  11.273  35.200  1.00 33.11           N  
ATOM   1521  N   ARG A 636     -20.791  11.153  31.676  1.00 31.28           N  
ATOM   1522  CA  ARG A 636     -19.649  11.803  32.304  1.00 31.79           C  
ATOM   1523  C   ARG A 636     -20.131  12.956  33.175  1.00 34.24           C  
ATOM   1524  O   ARG A 636     -20.849  13.844  32.706  1.00 36.78           O  
ATOM   1525  CB  ARG A 636     -18.672  12.309  31.245  1.00 29.49           C  
ATOM   1526  CG  ARG A 636     -17.425  12.968  31.814  1.00 33.72           C  
ATOM   1527  CD  ARG A 636     -16.365  13.168  30.740  1.00 37.17           C  
ATOM   1528  NE  ARG A 636     -15.099  13.640  31.295  1.00 39.87           N  
ATOM   1529  CZ  ARG A 636     -14.042  13.978  30.563  1.00 44.82           C  
ATOM   1530  NH1 ARG A 636     -14.096  13.901  29.240  1.00 42.12           N  
ATOM   1531  NH2 ARG A 636     -12.931  14.397  31.152  1.00 51.03           N  
ATOM   1532  N   TYR A 637     -19.735  12.937  34.445  1.00 36.70           N  
ATOM   1533  CA  TYR A 637     -20.215  13.886  35.441  1.00 37.56           C  
ATOM   1534  C   TYR A 637     -19.104  14.760  35.997  1.00 44.68           C  
ATOM   1535  O   TYR A 637     -19.209  15.992  35.949  1.00 44.48           O  
ATOM   1536  CB  TYR A 637     -20.905  13.120  36.578  1.00 35.50           C  
ATOM   1537  CG  TYR A 637     -21.535  13.978  37.651  1.00 41.44           C  
ATOM   1538  CD1 TYR A 637     -22.347  15.055  37.326  1.00 40.67           C  
ATOM   1539  CD2 TYR A 637     -21.334  13.692  38.994  1.00 46.26           C  
ATOM   1540  CE1 TYR A 637     -22.931  15.830  38.311  1.00 47.97           C  
ATOM   1541  CE2 TYR A 637     -21.912  14.461  39.984  1.00 46.07           C  
ATOM   1542  CZ  TYR A 637     -22.709  15.528  39.639  1.00 45.97           C  
ATOM   1543  OH  TYR A 637     -23.286  16.295  40.625  1.00 44.42           O  
ATOM   1544  N   GLU A 638     -18.038  14.150  36.525  1.00 45.27           N  
ATOM   1545  CA  GLU A 638     -16.893  14.874  37.084  1.00 43.10           C  
ATOM   1546  C   GLU A 638     -17.327  15.869  38.157  1.00 45.14           C  
ATOM   1547  O   GLU A 638     -16.732  16.938  38.310  1.00 42.52           O  
ATOM   1548  CB  GLU A 638     -16.090  15.576  35.984  1.00 44.73           C  
ATOM   1549  CG  GLU A 638     -15.864  14.731  34.733  1.00 42.03           C  
ATOM   1550  CD  GLU A 638     -14.626  13.847  34.818  1.00 53.32           C  
ATOM   1551  OE1 GLU A 638     -14.379  13.252  35.889  1.00 50.08           O  
ATOM   1552  OE2 GLU A 638     -13.901  13.742  33.805  1.00 48.16           O  
ATOM   1553  N   ASP A 639     -18.373  15.512  38.907  1.00 46.31           N  
ATOM   1554  CA  ASP A 639     -18.924  16.343  39.978  1.00 43.86           C  
ATOM   1555  C   ASP A 639     -19.338  17.720  39.451  1.00 46.61           C  
ATOM   1556  O   ASP A 639     -18.912  18.765  39.946  1.00 50.16           O  
ATOM   1557  CB  ASP A 639     -17.934  16.467  41.142  1.00 45.76           C  
ATOM   1558  CG  ASP A 639     -18.554  16.093  42.475  1.00 54.85           C  
ATOM   1559  N   GLY A 640     -20.191  17.698  38.426  1.00 46.38           N  
ATOM   1560  CA  GLY A 640     -20.733  18.908  37.844  1.00 40.95           C  
ATOM   1561  C   GLY A 640     -19.833  19.622  36.861  1.00 41.35           C  
ATOM   1562  O   GLY A 640     -20.287  20.572  36.211  1.00 43.58           O  
ATOM   1563  N   ALA A 641     -18.574  19.202  36.721  1.00 44.25           N  
ATOM   1564  CA  ALA A 641     -17.644  19.891  35.835  1.00 43.99           C  
ATOM   1565  C   ALA A 641     -17.920  19.630  34.361  1.00 46.09           C  
ATOM   1566  O   ALA A 641     -17.346  20.323  33.513  1.00 51.13           O  
ATOM   1567  CB  ALA A 641     -16.206  19.488  36.167  1.00 46.22           C  
ATOM   1568  N   PHE A 642     -18.772  18.663  34.034  1.00 43.43           N  
ATOM   1569  CA  PHE A 642     -19.078  18.319  32.653  1.00 40.59           C  
ATOM   1570  C   PHE A 642     -20.486  18.778  32.298  1.00 39.29           C  
ATOM   1571  O   PHE A 642     -21.394  18.731  33.135  1.00 35.56           O  
ATOM   1572  CB  PHE A 642     -18.945  16.812  32.420  1.00 38.59           C  
ATOM   1573  CG  PHE A 642     -18.582  16.451  31.009  1.00 33.64           C  
ATOM   1574  CD1 PHE A 642     -17.291  16.639  30.545  1.00 30.79           C  
ATOM   1575  CD2 PHE A 642     -19.529  15.926  30.147  1.00 33.74           C  
ATOM   1576  CE1 PHE A 642     -16.951  16.311  29.247  1.00 38.16           C  
ATOM   1577  CE2 PHE A 642     -19.194  15.594  28.847  1.00 36.21           C  
ATOM   1578  CZ  PHE A 642     -17.904  15.787  28.397  1.00 37.19           C  
ATOM   1579  N   PHE A 643     -20.653  19.220  31.054  1.00 34.89           N  
ATOM   1580  CA  PHE A 643     -21.958  19.649  30.571  1.00 40.08           C  
ATOM   1581  C   PHE A 643     -22.971  18.514  30.732  1.00 41.72           C  
ATOM   1582  O   PHE A 643     -22.631  17.346  30.507  1.00 41.47           O  
ATOM   1583  CB  PHE A 643     -21.856  20.075  29.103  1.00 40.72           C  
ATOM   1584  CG  PHE A 643     -23.124  20.652  28.545  1.00 42.96           C  
ATOM   1585  CD1 PHE A 643     -24.049  19.842  27.905  1.00 38.78           C  
ATOM   1586  CD2 PHE A 643     -23.395  22.003  28.667  1.00 43.56           C  
ATOM   1587  CE1 PHE A 643     -25.219  20.370  27.400  1.00 40.23           C  
ATOM   1588  CE2 PHE A 643     -24.562  22.535  28.161  1.00 41.69           C  
ATOM   1589  CZ  PHE A 643     -25.475  21.719  27.526  1.00 44.48           C  
ATOM   1590  N   PRO A 644     -24.230  18.813  31.107  1.00 38.01           N  
ATOM   1591  CA  PRO A 644     -24.859  20.127  31.313  1.00 36.04           C  
ATOM   1592  C   PRO A 644     -24.577  20.801  32.658  1.00 43.96           C  
ATOM   1593  O   PRO A 644     -25.385  21.626  33.089  1.00 48.82           O  
ATOM   1594  CB  PRO A 644     -26.350  19.811  31.183  1.00 33.10           C  
ATOM   1595  CG  PRO A 644     -26.469  18.420  31.679  1.00 35.79           C  
ATOM   1596  CD  PRO A 644     -25.198  17.715  31.275  1.00 29.92           C  
ATOM   1597  N   ASN A 645     -23.466  20.444  33.303  1.00 43.15           N  
ATOM   1598  CA  ASN A 645     -22.919  21.199  34.432  1.00 39.75           C  
ATOM   1599  C   ASN A 645     -23.957  21.418  35.532  1.00 37.56           C  
ATOM   1600  O   ASN A 645     -24.170  22.535  36.004  1.00 45.11           O  
ATOM   1601  CB  ASN A 645     -22.347  22.538  33.956  1.00 37.80           C  
ATOM   1602  CG  ASN A 645     -21.040  22.382  33.196  1.00 43.24           C  
ATOM   1603  OD1 ASN A 645     -20.995  22.544  31.976  1.00 43.08           O  
ATOM   1604  ND2 ASN A 645     -19.969  22.075  33.918  1.00 43.13           N  
ATOM   1605  N   SER A 646     -24.610  20.336  35.946  1.00 35.45           N  
ATOM   1606  CA  SER A 646     -25.620  20.423  36.988  1.00 33.53           C  
ATOM   1607  C   SER A 646     -25.555  19.189  37.874  1.00 46.17           C  
ATOM   1608  O   SER A 646     -25.256  18.085  37.410  1.00 48.12           O  
ATOM   1609  CB  SER A 646     -27.029  20.567  36.400  1.00 31.91           C  
ATOM   1610  OG  SER A 646     -28.010  20.126  37.323  1.00 33.42           O  
ATOM   1611  N   GLU A 647     -25.848  19.387  39.160  1.00 50.34           N  
ATOM   1612  CA  GLU A 647     -25.902  18.281  40.110  1.00 45.09           C  
ATOM   1613  C   GLU A 647     -27.146  17.419  39.948  1.00 42.67           C  
ATOM   1614  O   GLU A 647     -27.357  16.514  40.764  1.00 45.03           O  
ATOM   1615  CB  GLU A 647     -25.826  18.814  41.543  1.00 47.59           C  
ATOM   1616  CG  GLU A 647     -24.485  19.425  41.909  1.00 50.31           C  
ATOM   1617  CD  GLU A 647     -24.213  19.377  43.400  1.00 60.53           C  
ATOM   1618  OE1 GLU A 647     -23.696  18.344  43.879  1.00 61.94           O  
ATOM   1619  OE2 GLU A 647     -24.516  20.372  44.092  1.00 55.21           O  
ATOM   1620  N   ASP A 648     -27.975  17.681  38.933  1.00 42.33           N  
ATOM   1621  CA  ASP A 648     -29.120  16.825  38.653  1.00 44.34           C  
ATOM   1622  C   ASP A 648     -28.709  15.496  38.034  1.00 43.36           C  
ATOM   1623  O   ASP A 648     -29.499  14.547  38.051  1.00 34.68           O  
ATOM   1624  CB  ASP A 648     -30.102  17.542  37.726  1.00 42.26           C  
ATOM   1625  CG  ASP A 648     -30.910  18.603  38.441  1.00 52.34           C  
ATOM   1626  OD1 ASP A 648     -30.877  19.772  38.003  1.00 45.84           O  
ATOM   1627  OD2 ASP A 648     -31.578  18.266  39.443  1.00 62.76           O  
ATOM   1628  N   ALA A 649     -27.500  15.413  37.482  1.00 40.69           N  
ATOM   1629  CA  ALA A 649     -26.991  14.183  36.892  1.00 39.16           C  
ATOM   1630  C   ALA A 649     -26.432  13.216  37.928  1.00 45.51           C  
ATOM   1631  O   ALA A 649     -25.948  12.142  37.552  1.00 45.45           O  
ATOM   1632  CB  ALA A 649     -25.911  14.510  35.858  1.00 39.06           C  
ATOM   1633  N   ASN A 650     -26.493  13.560  39.210  1.00 47.43           N  
ATOM   1634  CA  ASN A 650     -25.868  12.755  40.244  1.00 44.20           C  
ATOM   1635  C   ASN A 650     -26.733  11.545  40.593  1.00 40.27           C  
ATOM   1636  O   ASN A 650     -27.935  11.502  40.316  1.00 36.30           O  
ATOM   1637  CB  ASN A 650     -25.600  13.606  41.486  1.00 44.28           C  
ATOM   1638  CG  ASN A 650     -24.630  12.949  42.444  1.00 44.92           C  
ATOM   1639  OD1 ASN A 650     -24.938  12.756  43.619  1.00 46.81           O  
ATOM   1640  ND2 ASN A 650     -23.455  12.588  41.943  1.00 44.00           N  
ATOM   1641  N   TYR A 651     -26.095  10.553  41.220  1.00 38.84           N  
ATOM   1642  CA  TYR A 651     -26.739   9.268  41.474  1.00 38.84           C  
ATOM   1643  C   TYR A 651     -27.901   9.362  42.456  1.00 41.51           C  
ATOM   1644  O   TYR A 651     -28.741   8.455  42.487  1.00 37.10           O  
ATOM   1645  CB  TYR A 651     -25.704   8.262  41.988  1.00 36.37           C  
ATOM   1646  CG  TYR A 651     -24.962   8.699  43.236  1.00 36.81           C  
ATOM   1647  CD1 TYR A 651     -23.672   9.209  43.156  1.00 38.84           C  
ATOM   1648  CD2 TYR A 651     -25.544   8.586  44.494  1.00 37.76           C  
ATOM   1649  CE1 TYR A 651     -22.987   9.606  44.292  1.00 33.79           C  
ATOM   1650  CE2 TYR A 651     -24.868   8.981  45.635  1.00 35.90           C  
ATOM   1651  CZ  TYR A 651     -23.589   9.488  45.528  1.00 34.99           C  
ATOM   1652  OH  TYR A 651     -22.910   9.880  46.659  1.00 40.40           O  
ATOM   1653  N   ASP A 652     -27.970  10.422  43.262  1.00 40.77           N  
ATOM   1654  CA  ASP A 652     -29.020  10.511  44.269  1.00 43.13           C  
ATOM   1655  C   ASP A 652     -30.368  10.927  43.693  1.00 44.59           C  
ATOM   1656  O   ASP A 652     -31.378  10.830  44.399  1.00 50.31           O  
ATOM   1657  CB  ASP A 652     -28.612  11.482  45.383  1.00 44.55           C  
ATOM   1658  CG  ASP A 652     -28.089  12.802  44.851  1.00 48.16           C  
ATOM   1659  OD1 ASP A 652     -27.791  12.885  43.643  1.00 46.04           O  
ATOM   1660  OD2 ASP A 652     -27.975  13.759  45.647  1.00 52.99           O  
ATOM   1661  N   LYS A 653     -30.415  11.377  42.441  1.00 36.85           N  
ATOM   1662  CA  LYS A 653     -31.678  11.739  41.797  1.00 40.92           C  
ATOM   1663  C   LYS A 653     -32.346  10.459  41.315  1.00 36.16           C  
ATOM   1664  O   LYS A 653     -32.091   9.972  40.213  1.00 40.32           O  
ATOM   1665  CB  LYS A 653     -31.442  12.720  40.655  1.00 43.84           C  
ATOM   1666  CG  LYS A 653     -30.501  13.866  40.996  1.00 42.30           C  
ATOM   1667  CD  LYS A 653     -31.128  14.820  41.998  1.00 38.22           C  
ATOM   1668  CE  LYS A 653     -30.267  16.058  42.184  1.00 45.88           C  
ATOM   1669  NZ  LYS A 653     -29.392  15.953  43.385  1.00 42.98           N  
ATOM   1670  N   VAL A 654     -33.215   9.904  42.158  1.00 30.77           N  
ATOM   1671  CA  VAL A 654     -33.865   8.629  41.887  1.00 38.60           C  
ATOM   1672  C   VAL A 654     -35.314   8.813  41.461  1.00 36.75           C  
ATOM   1673  O   VAL A 654     -36.079   7.843  41.437  1.00 39.13           O  
ATOM   1674  CB  VAL A 654     -33.765   7.688  43.098  1.00 43.31           C  
ATOM   1675  CG1 VAL A 654     -32.306   7.424  43.440  1.00 38.20           C  
ATOM   1676  CG2 VAL A 654     -34.500   8.279  44.292  1.00 40.13           C  
ATOM   1677  N   GLY A 655     -35.710  10.031  41.114  1.00 41.50           N  
ATOM   1678  CA  GLY A 655     -37.089  10.329  40.783  1.00 42.76           C  
ATOM   1679  C   GLY A 655     -37.792  11.051  41.915  1.00 45.91           C  
ATOM   1680  O   GLY A 655     -37.225  11.330  42.977  1.00 48.86           O  
ATOM   1681  N   LEU A 656     -39.063  11.355  41.672  1.00 51.12           N  
ATOM   1682  CA  LEU A 656     -39.880  12.100  42.619  1.00 53.18           C  
ATOM   1683  C   LEU A 656     -41.214  11.399  42.816  1.00 52.73           C  
ATOM   1684  O   LEU A 656     -41.835  10.946  41.850  1.00 54.13           O  
ATOM   1685  CB  LEU A 656     -40.117  13.542  42.141  1.00 44.90           C  
ATOM   1686  CG  LEU A 656     -38.884  14.413  41.888  1.00 54.50           C  
ATOM   1687  CD1 LEU A 656     -39.284  15.739  41.261  1.00 53.77           C  
ATOM   1688  CD2 LEU A 656     -38.105  14.645  43.173  1.00 50.86           C  
ATOM   1689  N   GLY A 657     -41.645  11.317  44.074  1.00 53.47           N  
ATOM   1690  CA  GLY A 657     -42.942  10.772  44.429  1.00 52.48           C  
ATOM   1691  C   GLY A 657     -43.274   9.432  43.805  1.00 52.26           C  
ATOM   1692  O   GLY A 657     -42.642   8.417  44.113  1.00 58.87           O  
ATOM   1693  N   LYS A 658     -44.273   9.423  42.918  1.00 49.35           N  
ATOM   1694  CA  LYS A 658     -44.702   8.183  42.283  1.00 46.66           C  
ATOM   1695  C   LYS A 658     -43.630   7.598  41.374  1.00 52.30           C  
ATOM   1696  O   LYS A 658     -43.646   6.391  41.113  1.00 49.08           O  
ATOM   1697  CB  LYS A 658     -45.988   8.418  41.488  1.00 48.27           C  
ATOM   1698  N   GLY A 659     -42.701   8.419  40.893  1.00 50.23           N  
ATOM   1699  CA  GLY A 659     -41.659   7.937  40.009  1.00 49.49           C  
ATOM   1700  C   GLY A 659     -40.322   7.738  40.690  1.00 47.26           C  
ATOM   1701  O   GLY A 659     -39.276   7.766  40.034  1.00 45.60           O  
ATOM   1702  N   ARG A 660     -40.338   7.534  42.005  1.00 46.67           N  
ATOM   1703  CA  ARG A 660     -39.099   7.312  42.735  1.00 46.98           C  
ATOM   1704  C   ARG A 660     -38.542   5.929  42.426  1.00 50.73           C  
ATOM   1705  O   ARG A 660     -39.279   4.940  42.370  1.00 48.54           O  
ATOM   1706  CB  ARG A 660     -39.329   7.468  44.237  1.00 50.27           C  
ATOM   1707  CG  ARG A 660     -39.294   8.911  44.711  1.00 55.38           C  
ATOM   1708  CD  ARG A 660     -38.552   9.042  46.029  1.00 54.41           C  
ATOM   1709  NE  ARG A 660     -39.074   8.131  47.043  1.00 56.67           N  
ATOM   1710  CZ  ARG A 660     -38.406   7.768  48.133  1.00 59.17           C  
ATOM   1711  NH1 ARG A 660     -37.187   8.240  48.353  1.00 58.40           N  
ATOM   1712  NH2 ARG A 660     -38.958   6.933  49.003  1.00 61.31           N  
ATOM   1713  N   GLY A 661     -37.225   5.864  42.224  1.00 50.18           N  
ATOM   1714  CA  GLY A 661     -36.571   4.650  41.792  1.00 42.75           C  
ATOM   1715  C   GLY A 661     -36.610   4.404  40.302  1.00 42.18           C  
ATOM   1716  O   GLY A 661     -35.848   3.565  39.807  1.00 40.54           O  
ATOM   1717  N   TYR A 662     -37.469   5.109  39.566  1.00 46.51           N  
ATOM   1718  CA  TYR A 662     -37.571   4.975  38.121  1.00 45.26           C  
ATOM   1719  C   TYR A 662     -36.665   5.950  37.379  1.00 35.56           C  
ATOM   1720  O   TYR A 662     -36.870   6.190  36.183  1.00 35.77           O  
ATOM   1721  CB  TYR A 662     -39.025   5.156  37.679  1.00 43.13           C  
ATOM   1722  CG  TYR A 662     -39.923   4.008  38.082  1.00 44.65           C  
ATOM   1723  CD1 TYR A 662     -40.555   3.995  39.319  1.00 45.90           C  
ATOM   1724  CD2 TYR A 662     -40.132   2.932  37.229  1.00 41.68           C  
ATOM   1725  CE1 TYR A 662     -41.373   2.944  39.693  1.00 47.14           C  
ATOM   1726  CE2 TYR A 662     -40.947   1.879  37.594  1.00 44.25           C  
ATOM   1727  CZ  TYR A 662     -41.565   1.889  38.826  1.00 42.35           C  
ATOM   1728  OH  TYR A 662     -42.378   0.840  39.189  1.00 48.77           O  
ATOM   1729  N   ASN A 663     -35.670   6.515  38.061  1.00 34.19           N  
ATOM   1730  CA  ASN A 663     -34.695   7.410  37.439  1.00 36.37           C  
ATOM   1731  C   ASN A 663     -33.318   7.000  37.953  1.00 35.45           C  
ATOM   1732  O   ASN A 663     -32.953   7.316  39.089  1.00 34.82           O  
ATOM   1733  CB  ASN A 663     -35.001   8.870  37.752  1.00 31.57           C  
ATOM   1734  CG  ASN A 663     -34.131   9.830  36.965  1.00 34.59           C  
ATOM   1735  OD1 ASN A 663     -34.507  10.284  35.884  1.00 36.43           O  
ATOM   1736  ND2 ASN A 663     -32.961  10.148  37.507  1.00 31.99           N  
ATOM   1737  N   VAL A 664     -32.563   6.296  37.118  1.00 31.42           N  
ATOM   1738  CA  VAL A 664     -31.249   5.776  37.472  1.00 30.49           C  
ATOM   1739  C   VAL A 664     -30.203   6.636  36.779  1.00 31.53           C  
ATOM   1740  O   VAL A 664     -30.121   6.662  35.545  1.00 29.00           O  
ATOM   1741  CB  VAL A 664     -31.096   4.300  37.081  1.00 25.50           C  
ATOM   1742  CG1 VAL A 664     -29.685   3.823  37.379  1.00 25.72           C  
ATOM   1743  CG2 VAL A 664     -32.122   3.451  37.807  1.00 21.19           C  
ATOM   1744  N   ASN A 665     -29.397   7.338  37.570  1.00 31.96           N  
ATOM   1745  CA  ASN A 665     -28.275   8.114  37.060  1.00 30.34           C  
ATOM   1746  C   ASN A 665     -26.981   7.379  37.381  1.00 29.79           C  
ATOM   1747  O   ASN A 665     -26.711   7.069  38.546  1.00 32.08           O  
ATOM   1748  CB  ASN A 665     -28.255   9.520  37.658  1.00 32.07           C  
ATOM   1749  CG  ASN A 665     -29.203  10.468  36.953  1.00 39.54           C  
ATOM   1750  OD1 ASN A 665     -29.818  10.115  35.947  1.00 42.55           O  
ATOM   1751  ND2 ASN A 665     -29.316  11.684  37.472  1.00 37.95           N  
ATOM   1752  N   ILE A 666     -26.192   7.099  36.350  1.00 29.45           N  
ATOM   1753  CA  ILE A 666     -24.884   6.470  36.501  1.00 30.00           C  
ATOM   1754  C   ILE A 666     -23.831   7.489  36.078  1.00 26.88           C  
ATOM   1755  O   ILE A 666     -23.557   7.655  34.875  1.00 26.82           O  
ATOM   1756  CB  ILE A 666     -24.789   5.165  35.695  1.00 25.37           C  
ATOM   1757  CG1 ILE A 666     -25.929   4.221  36.088  1.00 24.59           C  
ATOM   1758  CG2 ILE A 666     -23.448   4.490  35.934  1.00 25.80           C  
ATOM   1759  CD1 ILE A 666     -25.980   2.936  35.282  1.00 24.73           C  
ATOM   1760  N   PRO A 667     -23.238   8.212  37.039  1.00 29.62           N  
ATOM   1761  CA  PRO A 667     -22.311   9.299  36.703  1.00 27.42           C  
ATOM   1762  C   PRO A 667     -20.846   8.904  36.816  1.00 29.19           C  
ATOM   1763  O   PRO A 667     -20.425   8.328  37.824  1.00 34.90           O  
ATOM   1764  CB  PRO A 667     -22.678  10.380  37.727  1.00 30.81           C  
ATOM   1765  CG  PRO A 667     -23.289   9.623  38.900  1.00 32.03           C  
ATOM   1766  CD  PRO A 667     -23.569   8.202  38.473  1.00 27.75           C  
ATOM   1767  N   TRP A 668     -20.060   9.229  35.794  1.00 33.46           N  
ATOM   1768  CA  TRP A 668     -18.655   8.855  35.716  1.00 34.47           C  
ATOM   1769  C   TRP A 668     -17.763   9.994  36.195  1.00 43.62           C  
ATOM   1770  O   TRP A 668     -17.981  11.158  35.845  1.00 39.55           O  
ATOM   1771  CB  TRP A 668     -18.270   8.480  34.283  1.00 32.02           C  
ATOM   1772  CG  TRP A 668     -19.003   7.293  33.720  1.00 36.99           C  
ATOM   1773  CD1 TRP A 668     -19.648   7.231  32.519  1.00 35.61           C  
ATOM   1774  CD2 TRP A 668     -19.145   5.994  34.318  1.00 35.75           C  
ATOM   1775  NE1 TRP A 668     -20.191   5.983  32.336  1.00 36.91           N  
ATOM   1776  CE2 TRP A 668     -19.897   5.204  33.424  1.00 37.86           C  
ATOM   1777  CE3 TRP A 668     -18.715   5.424  35.522  1.00 37.63           C  
ATOM   1778  CZ2 TRP A 668     -20.229   3.877  33.695  1.00 31.17           C  
ATOM   1779  CZ3 TRP A 668     -19.047   4.105  35.789  1.00 37.63           C  
ATOM   1780  CH2 TRP A 668     -19.796   3.347  34.880  1.00 31.63           C  
ATOM   1781  N   ASN A 669     -16.747   9.647  36.983  1.00 49.21           N  
ATOM   1782  CA  ASN A 669     -15.770  10.602  37.482  1.00 42.70           C  
ATOM   1783  C   ASN A 669     -14.370  10.028  37.325  1.00 46.29           C  
ATOM   1784  O   ASN A 669     -14.162   8.818  37.442  1.00 52.95           O  
ATOM   1785  CB  ASN A 669     -16.012  10.946  38.960  1.00 30.62           C  
ATOM   1786  CG  ASN A 669     -17.449  11.316  39.247  1.00 31.85           C  
ATOM   1787  OD1 ASN A 669     -18.065  12.083  38.509  1.00 40.77           O  
ATOM   1788  ND2 ASN A 669     -17.995  10.772  40.328  1.00 28.70           N  
ATOM   1789  N   GLY A 670     -13.409  10.907  37.053  1.00 40.47           N  
ATOM   1790  CA  GLY A 670     -12.016  10.505  37.034  1.00 40.16           C  
ATOM   1791  C   GLY A 670     -11.460  10.110  35.680  1.00 48.11           C  
ATOM   1792  O   GLY A 670     -10.847   9.047  35.544  1.00 59.29           O  
ATOM   1793  N   GLY A 671     -11.663  10.951  34.671  1.00 49.93           N  
ATOM   1794  CA  GLY A 671     -11.010  10.740  33.394  1.00 51.97           C  
ATOM   1795  C   GLY A 671     -11.740   9.774  32.475  1.00 51.93           C  
ATOM   1796  O   GLY A 671     -12.934   9.488  32.621  1.00 41.75           O  
ATOM   1797  N   LYS A 672     -10.980   9.258  31.508  1.00 54.23           N  
ATOM   1798  CA  LYS A 672     -11.558   8.473  30.426  1.00 48.24           C  
ATOM   1799  C   LYS A 672     -12.148   7.168  30.943  1.00 51.28           C  
ATOM   1800  O   LYS A 672     -11.571   6.500  31.806  1.00 59.86           O  
ATOM   1801  CB  LYS A 672     -10.500   8.172  29.360  1.00 47.18           C  
ATOM   1802  CG  LYS A 672      -9.865   9.401  28.729  1.00 45.43           C  
ATOM   1803  CD  LYS A 672      -9.169   9.056  27.421  1.00 47.13           C  
ATOM   1804  N   MET A 673     -13.311   6.813  30.410  1.00 46.37           N  
ATOM   1805  CA  MET A 673     -13.920   5.512  30.619  1.00 34.26           C  
ATOM   1806  C   MET A 673     -14.022   4.801  29.278  1.00 39.55           C  
ATOM   1807  O   MET A 673     -14.058   5.432  28.219  1.00 44.85           O  
ATOM   1808  CB  MET A 673     -15.311   5.628  31.258  1.00 38.61           C  
ATOM   1809  CG  MET A 673     -15.352   6.424  32.554  1.00 36.25           C  
ATOM   1810  SD  MET A 673     -14.202   5.822  33.806  1.00 41.32           S  
ATOM   1811  CE  MET A 673     -14.952   6.472  35.296  1.00 29.48           C  
ATOM   1812  N   GLY A 674     -14.062   3.476  29.330  1.00 40.46           N  
ATOM   1813  CA  GLY A 674     -14.139   2.702  28.111  1.00 42.11           C  
ATOM   1814  C   GLY A 674     -15.120   1.555  28.193  1.00 36.72           C  
ATOM   1815  O   GLY A 674     -16.111   1.619  28.926  1.00 35.94           O  
ATOM   1816  N   ASP A 675     -14.845   0.497  27.437  1.00 40.42           N  
ATOM   1817  CA  ASP A 675     -15.720  -0.671  27.453  1.00 37.45           C  
ATOM   1818  C   ASP A 675     -15.829  -1.340  28.820  1.00 41.14           C  
ATOM   1819  O   ASP A 675     -16.955  -1.706  29.199  1.00 42.50           O  
ATOM   1820  CB  ASP A 675     -15.248  -1.672  26.392  1.00 41.90           C  
ATOM   1821  CG  ASP A 675     -15.216  -1.071  25.000  1.00 48.91           C  
ATOM   1822  OD1 ASP A 675     -15.681   0.076  24.836  1.00 44.53           O  
ATOM   1823  OD2 ASP A 675     -14.720  -1.741  24.070  1.00 49.37           O  
ATOM   1824  N   PRO A 676     -14.750  -1.543  29.591  1.00 43.16           N  
ATOM   1825  CA  PRO A 676     -14.913  -2.210  30.898  1.00 42.67           C  
ATOM   1826  C   PRO A 676     -15.934  -1.551  31.814  1.00 31.52           C  
ATOM   1827  O   PRO A 676     -16.740  -2.248  32.445  1.00 36.35           O  
ATOM   1828  CB  PRO A 676     -13.496  -2.154  31.497  1.00 46.08           C  
ATOM   1829  CG  PRO A 676     -12.713  -1.216  30.626  1.00 48.85           C  
ATOM   1830  CD  PRO A 676     -13.326  -1.332  29.278  1.00 46.04           C  
ATOM   1831  N   GLU A 677     -15.937  -0.220  31.888  1.00 35.44           N  
ATOM   1832  CA  GLU A 677     -16.799   0.465  32.846  1.00 35.20           C  
ATOM   1833  C   GLU A 677     -18.262   0.413  32.421  1.00 27.42           C  
ATOM   1834  O   GLU A 677     -19.148   0.185  33.254  1.00 24.97           O  
ATOM   1835  CB  GLU A 677     -16.331   1.909  33.022  1.00 37.67           C  
ATOM   1836  CG  GLU A 677     -14.966   2.037  33.690  1.00 36.01           C  
ATOM   1837  CD  GLU A 677     -13.815   1.772  32.740  1.00 41.21           C  
ATOM   1838  OE1 GLU A 677     -13.992   1.974  31.521  1.00 42.70           O  
ATOM   1839  OE2 GLU A 677     -12.736   1.355  33.212  1.00 43.13           O  
ATOM   1840  N   TYR A 678     -18.537   0.618  31.131  1.00 25.71           N  
ATOM   1841  CA  TYR A 678     -19.915   0.541  30.656  1.00 27.95           C  
ATOM   1842  C   TYR A 678     -20.436  -0.889  30.715  1.00 30.84           C  
ATOM   1843  O   TYR A 678     -21.614  -1.116  31.021  1.00 29.27           O  
ATOM   1844  CB  TYR A 678     -20.012   1.099  29.237  1.00 25.31           C  
ATOM   1845  CG  TYR A 678     -20.045   2.609  29.187  1.00 29.65           C  
ATOM   1846  CD1 TYR A 678     -18.936   3.359  29.558  1.00 33.95           C  
ATOM   1847  CD2 TYR A 678     -21.187   3.287  28.778  1.00 27.55           C  
ATOM   1848  CE1 TYR A 678     -18.960   4.738  29.521  1.00 37.42           C  
ATOM   1849  CE2 TYR A 678     -21.220   4.668  28.739  1.00 29.33           C  
ATOM   1850  CZ  TYR A 678     -20.103   5.388  29.111  1.00 31.77           C  
ATOM   1851  OH  TYR A 678     -20.126   6.761  29.073  1.00 35.80           O  
ATOM   1852  N   MET A 679     -19.568  -1.865  30.433  1.00 27.83           N  
ATOM   1853  CA  MET A 679     -19.956  -3.265  30.557  1.00 26.28           C  
ATOM   1854  C   MET A 679     -20.286  -3.618  32.000  1.00 27.66           C  
ATOM   1855  O   MET A 679     -21.250  -4.345  32.263  1.00 29.10           O  
ATOM   1856  CB  MET A 679     -18.844  -4.170  30.027  1.00 29.09           C  
ATOM   1857  CG  MET A 679     -18.714  -4.180  28.512  1.00 34.70           C  
ATOM   1858  SD  MET A 679     -20.185  -4.811  27.683  1.00 48.99           S  
ATOM   1859  CE  MET A 679     -20.080  -6.557  28.085  1.00 39.38           C  
ATOM   1860  N   ALA A 680     -19.498  -3.114  32.952  1.00 26.18           N  
ATOM   1861  CA  ALA A 680     -19.788  -3.384  34.357  1.00 25.71           C  
ATOM   1862  C   ALA A 680     -21.072  -2.694  34.802  1.00 29.15           C  
ATOM   1863  O   ALA A 680     -21.865  -3.272  35.557  1.00 32.92           O  
ATOM   1864  CB  ALA A 680     -18.617  -2.943  35.229  1.00 21.12           C  
ATOM   1865  N   ALA A 681     -21.292  -1.458  34.345  1.00 29.37           N  
ATOM   1866  CA  ALA A 681     -22.513  -0.743  34.703  1.00 28.03           C  
ATOM   1867  C   ALA A 681     -23.744  -1.439  34.139  1.00 27.15           C  
ATOM   1868  O   ALA A 681     -24.805  -1.451  34.772  1.00 25.40           O  
ATOM   1869  CB  ALA A 681     -22.438   0.701  34.211  1.00 28.22           C  
ATOM   1870  N   PHE A 682     -23.620  -2.028  32.946  1.00 29.27           N  
ATOM   1871  CA  PHE A 682     -24.727  -2.800  32.390  1.00 23.74           C  
ATOM   1872  C   PHE A 682     -24.915  -4.116  33.137  1.00 28.88           C  
ATOM   1873  O   PHE A 682     -26.049  -4.556  33.354  1.00 25.76           O  
ATOM   1874  CB  PHE A 682     -24.489  -3.057  30.903  1.00 26.77           C  
ATOM   1875  CG  PHE A 682     -25.138  -2.046  30.002  1.00 28.13           C  
ATOM   1876  CD1 PHE A 682     -24.718  -0.726  30.003  1.00 22.62           C  
ATOM   1877  CD2 PHE A 682     -26.171  -2.416  29.156  1.00 26.15           C  
ATOM   1878  CE1 PHE A 682     -25.315   0.206  29.176  1.00 23.11           C  
ATOM   1879  CE2 PHE A 682     -26.772  -1.489  28.326  1.00 23.98           C  
ATOM   1880  CZ  PHE A 682     -26.343  -0.177  28.336  1.00 28.25           C  
ATOM   1881  N   HIS A 683     -23.814  -4.755  33.541  1.00 29.92           N  
ATOM   1882  CA  HIS A 683     -23.907  -6.043  34.222  1.00 27.09           C  
ATOM   1883  C   HIS A 683     -24.561  -5.905  35.591  1.00 31.57           C  
ATOM   1884  O   HIS A 683     -25.388  -6.741  35.975  1.00 33.40           O  
ATOM   1885  CB  HIS A 683     -22.518  -6.667  34.370  1.00 32.82           C  
ATOM   1886  CG  HIS A 683     -21.930  -7.160  33.084  1.00 30.42           C  
ATOM   1887  ND1 HIS A 683     -22.692  -7.423  31.966  1.00 32.88           N  
ATOM   1888  CD2 HIS A 683     -20.649  -7.426  32.738  1.00 26.85           C  
ATOM   1889  CE1 HIS A 683     -21.906  -7.837  30.989  1.00 38.30           C  
ATOM   1890  NE2 HIS A 683     -20.661  -7.848  31.431  1.00 40.06           N  
ATOM   1891  N   HIS A 684     -24.202  -4.862  36.343  1.00 30.79           N  
ATOM   1892  CA  HIS A 684     -24.620  -4.754  37.735  1.00 30.18           C  
ATOM   1893  C   HIS A 684     -25.815  -3.837  37.955  1.00 32.36           C  
ATOM   1894  O   HIS A 684     -26.427  -3.899  39.027  1.00 39.49           O  
ATOM   1895  CB  HIS A 684     -23.451  -4.267  38.601  1.00 27.77           C  
ATOM   1896  CG  HIS A 684     -22.231  -5.129  38.505  1.00 36.50           C  
ATOM   1897  ND1 HIS A 684     -22.236  -6.467  38.836  1.00 45.57           N  
ATOM   1898  CD2 HIS A 684     -20.968  -4.845  38.106  1.00 36.46           C  
ATOM   1899  CE1 HIS A 684     -21.029  -6.970  38.649  1.00 43.60           C  
ATOM   1900  NE2 HIS A 684     -20.241  -6.007  38.205  1.00 44.80           N  
ATOM   1901  N   LEU A 685     -26.171  -3.002  36.979  1.00 33.76           N  
ATOM   1902  CA  LEU A 685     -27.224  -2.017  37.194  1.00 24.84           C  
ATOM   1903  C   LEU A 685     -28.269  -2.016  36.086  1.00 26.01           C  
ATOM   1904  O   LEU A 685     -29.448  -2.280  36.342  1.00 28.85           O  
ATOM   1905  CB  LEU A 685     -26.615  -0.620  37.326  1.00 27.37           C  
ATOM   1906  CG  LEU A 685     -25.952  -0.312  38.666  1.00 33.56           C  
ATOM   1907  CD1 LEU A 685     -25.044   0.899  38.538  1.00 32.81           C  
ATOM   1908  CD2 LEU A 685     -27.011  -0.090  39.734  1.00 31.28           C  
ATOM   1909  N   VAL A 686     -27.847  -1.718  34.855  1.00 24.43           N  
ATOM   1910  CA  VAL A 686     -28.800  -1.458  33.777  1.00 22.32           C  
ATOM   1911  C   VAL A 686     -29.663  -2.685  33.508  1.00 25.33           C  
ATOM   1912  O   VAL A 686     -30.894  -2.594  33.433  1.00 29.36           O  
ATOM   1913  CB  VAL A 686     -28.061  -1.000  32.508  1.00 24.17           C  
ATOM   1914  CG1 VAL A 686     -29.046  -0.809  31.366  1.00 18.09           C  
ATOM   1915  CG2 VAL A 686     -27.298   0.285  32.779  1.00 22.94           C  
ATOM   1916  N   MET A 687     -29.035  -3.851  33.362  1.00 29.67           N  
ATOM   1917  CA  MET A 687     -29.760  -5.063  32.990  1.00 23.60           C  
ATOM   1918  C   MET A 687     -30.560  -5.669  34.145  1.00 25.68           C  
ATOM   1919  O   MET A 687     -31.681  -6.137  33.916  1.00 27.25           O  
ATOM   1920  CB  MET A 687     -28.797  -6.101  32.409  1.00 22.56           C  
ATOM   1921  CG  MET A 687     -28.161  -5.675  31.101  1.00 22.34           C  
ATOM   1922  SD  MET A 687     -29.384  -5.143  29.888  1.00 27.79           S  
ATOM   1923  CE  MET A 687     -30.399  -6.615  29.752  1.00 28.93           C  
ATOM   1924  N   PRO A 688     -30.040  -5.716  35.381  1.00 27.83           N  
ATOM   1925  CA  PRO A 688     -30.903  -6.168  36.492  1.00 25.20           C  
ATOM   1926  C   PRO A 688     -32.140  -5.304  36.684  1.00 29.81           C  
ATOM   1927  O   PRO A 688     -33.265  -5.827  36.724  1.00 32.27           O  
ATOM   1928  CB  PRO A 688     -29.964  -6.104  37.703  1.00 26.43           C  
ATOM   1929  CG  PRO A 688     -28.613  -6.289  37.136  1.00 23.81           C  
ATOM   1930  CD  PRO A 688     -28.629  -5.614  35.800  1.00 23.61           C  
ATOM   1931  N   ILE A 689     -31.958  -3.984  36.804  1.00 27.75           N  
ATOM   1932  CA  ILE A 689     -33.090  -3.076  36.972  1.00 26.22           C  
ATOM   1933  C   ILE A 689     -34.033  -3.171  35.780  1.00 29.83           C  
ATOM   1934  O   ILE A 689     -35.259  -3.182  35.939  1.00 33.15           O  
ATOM   1935  CB  ILE A 689     -32.592  -1.632  37.179  1.00 31.41           C  
ATOM   1936  CG1 ILE A 689     -31.820  -1.509  38.492  1.00 26.53           C  
ATOM   1937  CG2 ILE A 689     -33.755  -0.650  37.152  1.00 30.05           C  
ATOM   1938  CD1 ILE A 689     -31.126  -0.178  38.658  1.00 28.54           C  
ATOM   1939  N   ALA A 690     -33.477  -3.237  34.568  1.00 28.38           N  
ATOM   1940  CA  ALA A 690     -34.313  -3.330  33.376  1.00 25.32           C  
ATOM   1941  C   ALA A 690     -35.131  -4.614  33.375  1.00 31.34           C  
ATOM   1942  O   ALA A 690     -36.310  -4.608  33.004  1.00 32.45           O  
ATOM   1943  CB  ALA A 690     -33.447  -3.243  32.121  1.00 20.88           C  
ATOM   1944  N   ARG A 691     -34.527  -5.726  33.797  1.00 31.30           N  
ATOM   1945  CA  ARG A 691     -35.245  -6.995  33.809  1.00 30.36           C  
ATOM   1946  C   ARG A 691     -36.334  -7.005  34.875  1.00 33.17           C  
ATOM   1947  O   ARG A 691     -37.416  -7.561  34.656  1.00 34.49           O  
ATOM   1948  CB  ARG A 691     -34.267  -8.150  34.014  1.00 24.02           C  
ATOM   1949  CG  ARG A 691     -33.659  -8.659  32.717  1.00 26.63           C  
ATOM   1950  CD  ARG A 691     -32.773  -9.870  32.944  1.00 25.47           C  
ATOM   1951  NE  ARG A 691     -31.613  -9.558  33.772  1.00 31.06           N  
ATOM   1952  CZ  ARG A 691     -30.386  -9.380  33.294  1.00 33.59           C  
ATOM   1953  NH1 ARG A 691     -29.384  -9.101  34.119  1.00 33.67           N  
ATOM   1954  NH2 ARG A 691     -30.161  -9.478  31.991  1.00 26.75           N  
ATOM   1955  N   GLU A 692     -36.074  -6.392  36.033  1.00 29.24           N  
ATOM   1956  CA  GLU A 692     -37.127  -6.284  37.039  1.00 33.63           C  
ATOM   1957  C   GLU A 692     -38.256  -5.382  36.557  1.00 40.83           C  
ATOM   1958  O   GLU A 692     -39.433  -5.652  36.822  1.00 48.54           O  
ATOM   1959  CB  GLU A 692     -36.554  -5.765  38.356  1.00 34.67           C  
ATOM   1960  CG  GLU A 692     -37.452  -6.022  39.556  1.00 45.62           C  
ATOM   1961  CD  GLU A 692     -36.770  -5.713  40.874  1.00 51.84           C  
ATOM   1962  OE1 GLU A 692     -35.647  -5.166  40.850  1.00 50.08           O  
ATOM   1963  OE2 GLU A 692     -37.356  -6.019  41.934  1.00 55.35           O  
ATOM   1964  N   PHE A 693     -37.912  -4.305  35.846  1.00 40.53           N  
ATOM   1965  CA  PHE A 693     -38.916  -3.389  35.317  1.00 37.47           C  
ATOM   1966  C   PHE A 693     -39.781  -4.056  34.256  1.00 36.89           C  
ATOM   1967  O   PHE A 693     -40.957  -3.704  34.107  1.00 42.50           O  
ATOM   1968  CB  PHE A 693     -38.219  -2.149  34.753  1.00 37.31           C  
ATOM   1969  CG  PHE A 693     -39.149  -1.144  34.131  1.00 39.46           C  
ATOM   1970  CD1 PHE A 693     -39.841  -0.240  34.918  1.00 43.11           C  
ATOM   1971  CD2 PHE A 693     -39.303  -1.083  32.756  1.00 38.03           C  
ATOM   1972  CE1 PHE A 693     -40.686   0.695  34.345  1.00 42.36           C  
ATOM   1973  CE2 PHE A 693     -40.146  -0.153  32.178  1.00 39.36           C  
ATOM   1974  CZ  PHE A 693     -40.838   0.738  32.974  1.00 40.70           C  
ATOM   1975  N   ALA A 694     -39.220  -5.022  33.523  1.00 33.46           N  
ATOM   1976  CA  ALA A 694     -39.902  -5.761  32.467  1.00 35.94           C  
ATOM   1977  C   ALA A 694     -40.512  -4.812  31.443  1.00 37.27           C  
ATOM   1978  O   ALA A 694     -41.741  -4.741  31.320  1.00 41.44           O  
ATOM   1979  CB  ALA A 694     -40.982  -6.671  33.054  1.00 35.07           C  
ATOM   1980  N   PRO A 695     -39.700  -4.078  30.687  1.00 36.67           N  
ATOM   1981  CA  PRO A 695     -40.260  -3.120  29.732  1.00 39.53           C  
ATOM   1982  C   PRO A 695     -40.860  -3.827  28.530  1.00 38.93           C  
ATOM   1983  O   PRO A 695     -40.537  -4.974  28.216  1.00 38.84           O  
ATOM   1984  CB  PRO A 695     -39.049  -2.276  29.331  1.00 37.45           C  
ATOM   1985  CG  PRO A 695     -37.909  -3.228  29.436  1.00 32.66           C  
ATOM   1986  CD  PRO A 695     -38.232  -4.152  30.588  1.00 34.77           C  
ATOM   1987  N   GLU A 696     -41.766  -3.117  27.859  1.00 42.70           N  
ATOM   1988  CA  GLU A 696     -42.357  -3.596  26.620  1.00 43.36           C  
ATOM   1989  C   GLU A 696     -41.850  -2.857  25.393  1.00 39.78           C  
ATOM   1990  O   GLU A 696     -42.033  -3.352  24.276  1.00 42.08           O  
ATOM   1991  CB  GLU A 696     -43.887  -3.491  26.685  1.00 44.95           C  
ATOM   1992  CG  GLU A 696     -44.461  -3.979  28.005  1.00 51.75           C  
ATOM   1993  CD  GLU A 696     -45.842  -3.429  28.287  1.00 51.93           C  
ATOM   1994  OE1 GLU A 696     -45.940  -2.256  28.708  1.00 49.17           O  
ATOM   1995  OE2 GLU A 696     -46.827  -4.172  28.094  1.00 47.35           O  
ATOM   1996  N   LEU A 697     -41.215  -1.700  25.574  1.00 37.44           N  
ATOM   1997  CA  LEU A 697     -40.543  -0.988  24.497  1.00 34.66           C  
ATOM   1998  C   LEU A 697     -39.253  -0.398  25.042  1.00 34.29           C  
ATOM   1999  O   LEU A 697     -39.255   0.211  26.117  1.00 31.60           O  
ATOM   2000  CB  LEU A 697     -41.425   0.120  23.914  1.00 33.15           C  
ATOM   2001  CG  LEU A 697     -40.789   0.903  22.765  1.00 29.61           C  
ATOM   2002  CD1 LEU A 697     -40.656   0.029  21.526  1.00 31.13           C  
ATOM   2003  CD2 LEU A 697     -41.583   2.159  22.461  1.00 30.24           C  
ATOM   2004  N   VAL A 698     -38.159  -0.579  24.306  1.00 32.28           N  
ATOM   2005  CA  VAL A 698     -36.851  -0.065  24.695  1.00 34.31           C  
ATOM   2006  C   VAL A 698     -36.429   1.000  23.691  1.00 29.99           C  
ATOM   2007  O   VAL A 698     -36.230   0.708  22.505  1.00 24.51           O  
ATOM   2008  CB  VAL A 698     -35.800  -1.182  24.781  1.00 30.43           C  
ATOM   2009  CG1 VAL A 698     -34.416  -0.579  24.965  1.00 30.57           C  
ATOM   2010  CG2 VAL A 698     -36.122  -2.131  25.923  1.00 26.11           C  
ATOM   2011  N   LEU A 699     -36.295   2.234  24.169  1.00 27.04           N  
ATOM   2012  CA  LEU A 699     -35.737   3.339  23.403  1.00 26.42           C  
ATOM   2013  C   LEU A 699     -34.328   3.618  23.907  1.00 25.54           C  
ATOM   2014  O   LEU A 699     -34.100   3.680  25.120  1.00 24.86           O  
ATOM   2015  CB  LEU A 699     -36.602   4.593  23.534  1.00 26.79           C  
ATOM   2016  CG  LEU A 699     -38.083   4.459  23.178  1.00 27.66           C  
ATOM   2017  CD1 LEU A 699     -38.782   5.793  23.361  1.00 22.55           C  
ATOM   2018  CD2 LEU A 699     -38.255   3.948  21.754  1.00 22.32           C  
ATOM   2019  N   VAL A 700     -33.390   3.784  22.982  1.00 26.12           N  
ATOM   2020  CA  VAL A 700     -31.991   4.020  23.315  1.00 23.22           C  
ATOM   2021  C   VAL A 700     -31.620   5.402  22.801  1.00 25.69           C  
ATOM   2022  O   VAL A 700     -31.565   5.624  21.584  1.00 30.12           O  
ATOM   2023  CB  VAL A 700     -31.070   2.948  22.721  1.00 24.30           C  
ATOM   2024  CG1 VAL A 700     -29.634   3.174  23.172  1.00 25.70           C  
ATOM   2025  CG2 VAL A 700     -31.552   1.563  23.113  1.00 26.63           C  
ATOM   2026  N   SER A 701     -31.381   6.336  23.725  1.00 29.13           N  
ATOM   2027  CA  SER A 701     -30.807   7.634  23.378  1.00 26.32           C  
ATOM   2028  C   SER A 701     -29.342   7.398  23.028  1.00 27.40           C  
ATOM   2029  O   SER A 701     -28.433   7.561  23.847  1.00 30.02           O  
ATOM   2030  CB  SER A 701     -30.962   8.629  24.519  1.00 29.28           C  
ATOM   2031  OG  SER A 701     -32.143   9.391  24.375  1.00 33.18           O  
ATOM   2032  N   ALA A 702     -29.122   7.003  21.774  1.00 27.04           N  
ATOM   2033  CA  ALA A 702     -27.827   6.497  21.330  1.00 26.75           C  
ATOM   2034  C   ALA A 702     -26.959   7.642  20.814  1.00 31.15           C  
ATOM   2035  O   ALA A 702     -26.731   7.816  19.615  1.00 35.97           O  
ATOM   2036  CB  ALA A 702     -28.017   5.420  20.273  1.00 29.69           C  
ATOM   2037  N   GLY A 703     -26.478   8.441  21.762  1.00 30.91           N  
ATOM   2038  CA  GLY A 703     -25.389   9.350  21.472  1.00 30.87           C  
ATOM   2039  C   GLY A 703     -24.076   8.585  21.481  1.00 33.40           C  
ATOM   2040  O   GLY A 703     -23.838   7.725  22.328  1.00 32.07           O  
ATOM   2041  N   PHE A 704     -23.226   8.890  20.504  1.00 34.26           N  
ATOM   2042  CA  PHE A 704     -21.956   8.193  20.349  1.00 31.74           C  
ATOM   2043  C   PHE A 704     -20.771   9.121  20.596  1.00 38.83           C  
ATOM   2044  O   PHE A 704     -19.695   8.934  20.025  1.00 38.80           O  
ATOM   2045  CB  PHE A 704     -21.867   7.543  18.969  1.00 31.65           C  
ATOM   2046  CG  PHE A 704     -22.907   6.482  18.737  1.00 35.16           C  
ATOM   2047  CD1 PHE A 704     -22.758   5.214  19.279  1.00 31.60           C  
ATOM   2048  CD2 PHE A 704     -24.042   6.757  17.992  1.00 30.62           C  
ATOM   2049  CE1 PHE A 704     -23.715   4.240  19.075  1.00 27.52           C  
ATOM   2050  CE2 PHE A 704     -25.004   5.786  17.785  1.00 33.21           C  
ATOM   2051  CZ  PHE A 704     -24.839   4.525  18.327  1.00 29.40           C  
ATOM   2052  N   ASP A 705     -20.956  10.123  21.454  1.00 37.33           N  
ATOM   2053  CA  ASP A 705     -19.881  11.030  21.828  1.00 38.11           C  
ATOM   2054  C   ASP A 705     -19.038  10.505  22.982  1.00 40.68           C  
ATOM   2055  O   ASP A 705     -18.084  11.176  23.390  1.00 42.54           O  
ATOM   2056  CB  ASP A 705     -20.446  12.413  22.176  1.00 38.52           C  
ATOM   2057  CG  ASP A 705     -21.692  12.341  23.036  1.00 36.65           C  
ATOM   2058  OD1 ASP A 705     -21.962  11.273  23.628  1.00 36.50           O  
ATOM   2059  OD2 ASP A 705     -22.406  13.360  23.117  1.00 30.63           O  
ATOM   2060  N   ALA A 706     -19.369   9.335  23.523  1.00 35.58           N  
ATOM   2061  CA  ALA A 706     -18.486   8.629  24.438  1.00 36.13           C  
ATOM   2062  C   ALA A 706     -17.546   7.684  23.706  1.00 34.25           C  
ATOM   2063  O   ALA A 706     -16.851   6.893  24.351  1.00 33.53           O  
ATOM   2064  CB  ALA A 706     -19.299   7.848  25.472  1.00 35.95           C  
ATOM   2065  N   ALA A 707     -17.509   7.757  22.379  1.00 37.56           N  
ATOM   2066  CA  ALA A 707     -16.750   6.822  21.570  1.00 40.06           C  
ATOM   2067  C   ALA A 707     -15.291   7.253  21.455  1.00 43.13           C  
ATOM   2068  O   ALA A 707     -14.905   8.373  21.798  1.00 42.41           O  
ATOM   2069  CB  ALA A 707     -17.376   6.688  20.183  1.00 35.37           C  
ATOM   2070  N   ARG A 708     -14.472   6.328  20.973  1.00 46.57           N  
ATOM   2071  CA  ARG A 708     -13.086   6.641  20.670  1.00 48.10           C  
ATOM   2072  C   ARG A 708     -13.021   7.722  19.595  1.00 51.11           C  
ATOM   2073  O   ARG A 708     -13.769   7.693  18.616  1.00 52.53           O  
ATOM   2074  CB  ARG A 708     -12.369   5.375  20.199  1.00 50.87           C  
ATOM   2075  CG  ARG A 708     -11.375   5.597  19.075  1.00 62.81           C  
ATOM   2076  CD  ARG A 708     -10.617   4.325  18.747  1.00 59.08           C  
ATOM   2077  NE  ARG A 708     -10.068   3.693  19.938  1.00 59.70           N  
ATOM   2078  CZ  ARG A 708     -10.204   2.404  20.227  1.00 63.23           C  
ATOM   2079  NH1 ARG A 708     -10.875   1.601  19.411  1.00 62.47           N  
ATOM   2080  NH2 ARG A 708      -9.667   1.919  21.336  1.00 64.06           N  
ATOM   2081  N   GLY A 709     -12.137   8.693  19.791  1.00 50.44           N  
ATOM   2082  CA  GLY A 709     -11.960   9.760  18.825  1.00 53.93           C  
ATOM   2083  C   GLY A 709     -12.983  10.874  18.878  1.00 52.65           C  
ATOM   2084  O   GLY A 709     -13.077  11.651  17.921  1.00 49.64           O  
ATOM   2085  N   ASP A 710     -13.749  10.987  19.958  1.00 49.77           N  
ATOM   2086  CA  ASP A 710     -14.689  12.099  20.028  1.00 46.91           C  
ATOM   2087  C   ASP A 710     -14.010  13.309  20.653  1.00 51.53           C  
ATOM   2088  O   ASP A 710     -13.371  13.178  21.704  1.00 50.53           O  
ATOM   2089  CB  ASP A 710     -15.923  11.728  20.835  1.00 44.16           C  
ATOM   2090  CG  ASP A 710     -17.056  12.718  20.644  1.00 46.21           C  
ATOM   2091  OD1 ASP A 710     -17.131  13.699  21.415  1.00 44.59           O  
ATOM   2092  OD2 ASP A 710     -17.865  12.522  19.711  1.00 48.66           O  
ATOM   2093  N   PRO A 711     -14.119  14.489  20.039  1.00 49.19           N  
ATOM   2094  CA  PRO A 711     -13.441  15.672  20.584  1.00 50.95           C  
ATOM   2095  C   PRO A 711     -14.136  16.286  21.785  1.00 54.96           C  
ATOM   2096  O   PRO A 711     -13.532  17.134  22.455  1.00 56.12           O  
ATOM   2097  CB  PRO A 711     -13.446  16.644  19.400  1.00 56.05           C  
ATOM   2098  CG  PRO A 711     -14.682  16.278  18.641  1.00 54.68           C  
ATOM   2099  CD  PRO A 711     -14.839  14.786  18.788  1.00 45.81           C  
ATOM   2100  N   LEU A 712     -15.374  15.893  22.082  1.00 52.52           N  
ATOM   2101  CA  LEU A 712     -16.154  16.526  23.137  1.00 49.95           C  
ATOM   2102  C   LEU A 712     -16.365  15.649  24.359  1.00 49.71           C  
ATOM   2103  O   LEU A 712     -16.473  16.176  25.468  1.00 46.14           O  
ATOM   2104  CB  LEU A 712     -17.526  16.959  22.599  1.00 48.29           C  
ATOM   2105  CG  LEU A 712     -17.660  18.331  21.927  1.00 52.88           C  
ATOM   2106  CD1 LEU A 712     -16.665  18.524  20.786  1.00 51.42           C  
ATOM   2107  CD2 LEU A 712     -19.086  18.543  21.436  1.00 48.42           C  
ATOM   2108  N   GLY A 713     -16.428  14.331  24.188  1.00 46.26           N  
ATOM   2109  CA  GLY A 713     -16.675  13.441  25.305  1.00 41.65           C  
ATOM   2110  C   GLY A 713     -15.424  13.068  26.072  1.00 41.83           C  
ATOM   2111  O   GLY A 713     -15.429  13.049  27.307  1.00 39.73           O  
ATOM   2112  N   GLY A 714     -14.346  12.769  25.353  1.00 38.78           N  
ATOM   2113  CA  GLY A 714     -13.118  12.355  26.003  1.00 39.94           C  
ATOM   2114  C   GLY A 714     -13.172  10.970  26.606  1.00 46.31           C  
ATOM   2115  O   GLY A 714     -12.513  10.717  27.619  1.00 50.59           O  
ATOM   2116  N   PHE A 715     -13.950  10.068  26.021  1.00 42.68           N  
ATOM   2117  CA  PHE A 715     -14.025   8.674  26.435  1.00 39.56           C  
ATOM   2118  C   PHE A 715     -13.489   7.795  25.307  1.00 43.28           C  
ATOM   2119  O   PHE A 715     -13.116   8.281  24.237  1.00 45.03           O  
ATOM   2120  CB  PHE A 715     -15.460   8.289  26.808  1.00 33.34           C  
ATOM   2121  CG  PHE A 715     -15.845   8.656  28.216  1.00 35.50           C  
ATOM   2122  CD1 PHE A 715     -14.987   9.389  29.018  1.00 37.96           C  
ATOM   2123  CD2 PHE A 715     -17.069   8.266  28.736  1.00 36.39           C  
ATOM   2124  CE1 PHE A 715     -15.342   9.727  30.311  1.00 36.63           C  
ATOM   2125  CE2 PHE A 715     -17.429   8.600  30.029  1.00 30.05           C  
ATOM   2126  CZ  PHE A 715     -16.565   9.332  30.817  1.00 34.76           C  
ATOM   2127  N   GLN A 716     -13.456   6.486  25.548  1.00 43.67           N  
ATOM   2128  CA  GLN A 716     -12.845   5.557  24.603  1.00 42.97           C  
ATOM   2129  C   GLN A 716     -13.698   4.306  24.437  1.00 43.41           C  
ATOM   2130  O   GLN A 716     -13.179   3.189  24.341  1.00 53.66           O  
ATOM   2131  CB  GLN A 716     -11.429   5.185  25.041  1.00 44.06           C  
ATOM   2132  CG  GLN A 716     -11.232   5.193  26.551  1.00 52.26           C  
ATOM   2133  CD  GLN A 716      -9.772   5.132  26.959  1.00 56.17           C  
ATOM   2134  OE1 GLN A 716      -8.882   5.491  26.187  1.00 60.25           O  
ATOM   2135  NE2 GLN A 716      -9.518   4.675  28.181  1.00 51.59           N  
ATOM   2136  N   VAL A 717     -15.019   4.470  24.390  1.00 43.77           N  
ATOM   2137  CA  VAL A 717     -15.901   3.331  24.160  1.00 41.08           C  
ATOM   2138  C   VAL A 717     -15.799   2.921  22.696  1.00 41.28           C  
ATOM   2139  O   VAL A 717     -16.082   3.715  21.792  1.00 43.67           O  
ATOM   2140  CB  VAL A 717     -17.347   3.662  24.551  1.00 38.30           C  
ATOM   2141  CG1 VAL A 717     -18.272   2.522  24.165  1.00 32.84           C  
ATOM   2142  CG2 VAL A 717     -17.442   3.944  26.044  1.00 35.53           C  
ATOM   2143  N   THR A 718     -15.391   1.680  22.457  1.00 38.61           N  
ATOM   2144  CA  THR A 718     -15.157   1.192  21.109  1.00 42.33           C  
ATOM   2145  C   THR A 718     -16.470   0.814  20.429  1.00 44.99           C  
ATOM   2146  O   THR A 718     -17.493   0.630  21.091  1.00 43.82           O  
ATOM   2147  CB  THR A 718     -14.221  -0.011  21.149  1.00 49.08           C  
ATOM   2148  OG1 THR A 718     -14.910  -1.137  21.705  1.00 49.17           O  
ATOM   2149  CG2 THR A 718     -13.000   0.300  22.000  1.00 50.65           C  
ATOM   2150  N   PRO A 719     -16.473   0.716  19.095  1.00 45.73           N  
ATOM   2151  CA  PRO A 719     -17.685   0.236  18.408  1.00 44.79           C  
ATOM   2152  C   PRO A 719     -18.095  -1.171  18.810  1.00 45.70           C  
ATOM   2153  O   PRO A 719     -19.294  -1.482  18.816  1.00 45.67           O  
ATOM   2154  CB  PRO A 719     -17.304   0.311  16.919  1.00 48.43           C  
ATOM   2155  CG  PRO A 719     -15.815   0.532  16.887  1.00 43.51           C  
ATOM   2156  CD  PRO A 719     -15.484   1.253  18.147  1.00 42.90           C  
ATOM   2157  N   GLU A 720     -17.136  -2.036  19.147  1.00 44.41           N  
ATOM   2158  CA  GLU A 720     -17.488  -3.376  19.606  1.00 44.46           C  
ATOM   2159  C   GLU A 720     -18.167  -3.334  20.969  1.00 43.54           C  
ATOM   2160  O   GLU A 720     -19.045  -4.160  21.253  1.00 44.56           O  
ATOM   2161  CB  GLU A 720     -16.241  -4.261  19.652  1.00 47.59           C  
ATOM   2162  CG  GLU A 720     -15.579  -4.501  18.298  1.00 51.82           C  
ATOM   2163  CD  GLU A 720     -14.650  -3.373  17.887  1.00 56.34           C  
ATOM   2164  OE1 GLU A 720     -14.206  -2.616  18.776  1.00 53.06           O  
ATOM   2165  OE2 GLU A 720     -14.356  -3.248  16.679  1.00 60.30           O  
ATOM   2166  N   GLY A 721     -17.781  -2.379  21.819  1.00 42.68           N  
ATOM   2167  CA  GLY A 721     -18.476  -2.205  23.084  1.00 37.57           C  
ATOM   2168  C   GLY A 721     -19.915  -1.770  22.889  1.00 37.11           C  
ATOM   2169  O   GLY A 721     -20.831  -2.304  23.521  1.00 39.36           O  
ATOM   2170  N   TYR A 722     -20.132  -0.789  22.007  1.00 35.36           N  
ATOM   2171  CA  TYR A 722     -21.493  -0.410  21.639  1.00 33.72           C  
ATOM   2172  C   TYR A 722     -22.267  -1.611  21.115  1.00 33.42           C  
ATOM   2173  O   TYR A 722     -23.452  -1.786  21.432  1.00 34.45           O  
ATOM   2174  CB  TYR A 722     -21.465   0.703  20.589  1.00 35.59           C  
ATOM   2175  CG  TYR A 722     -21.161   2.078  21.140  1.00 36.45           C  
ATOM   2176  CD1 TYR A 722     -22.034   2.704  22.020  1.00 37.41           C  
ATOM   2177  CD2 TYR A 722     -20.005   2.756  20.770  1.00 38.28           C  
ATOM   2178  CE1 TYR A 722     -21.762   3.963  22.523  1.00 30.96           C  
ATOM   2179  CE2 TYR A 722     -19.726   4.016  21.267  1.00 36.19           C  
ATOM   2180  CZ  TYR A 722     -20.608   4.614  22.144  1.00 31.82           C  
ATOM   2181  OH  TYR A 722     -20.337   5.866  22.642  1.00 33.84           O  
ATOM   2182  N   ALA A 723     -21.610  -2.454  20.314  1.00 36.11           N  
ATOM   2183  CA  ALA A 723     -22.253  -3.672  19.839  1.00 34.19           C  
ATOM   2184  C   ALA A 723     -22.682  -4.556  21.002  1.00 33.63           C  
ATOM   2185  O   ALA A 723     -23.778  -5.129  20.984  1.00 29.73           O  
ATOM   2186  CB  ALA A 723     -21.315  -4.432  18.902  1.00 39.08           C  
ATOM   2187  N   HIS A 724     -21.839  -4.666  22.032  1.00 32.38           N  
ATOM   2188  CA  HIS A 724     -22.183  -5.526  23.161  1.00 32.98           C  
ATOM   2189  C   HIS A 724     -23.330  -4.943  23.983  1.00 31.34           C  
ATOM   2190  O   HIS A 724     -24.195  -5.687  24.460  1.00 37.87           O  
ATOM   2191  CB  HIS A 724     -20.953  -5.767  24.035  1.00 37.67           C  
ATOM   2192  CG  HIS A 724     -20.158  -6.971  23.631  1.00 44.67           C  
ATOM   2193  ND1 HIS A 724     -19.973  -8.055  24.461  1.00 58.20           N  
ATOM   2194  CD2 HIS A 724     -19.508  -7.263  22.480  1.00 44.76           C  
ATOM   2195  CE1 HIS A 724     -19.239  -8.962  23.841  1.00 50.23           C  
ATOM   2196  NE2 HIS A 724     -18.943  -8.506  22.637  1.00 54.77           N  
ATOM   2197  N   LEU A 725     -23.358  -3.618  24.159  1.00 31.01           N  
ATOM   2198  CA  LEU A 725     -24.476  -3.000  24.870  1.00 26.10           C  
ATOM   2199  C   LEU A 725     -25.783  -3.197  24.114  1.00 25.94           C  
ATOM   2200  O   LEU A 725     -26.820  -3.508  24.715  1.00 25.60           O  
ATOM   2201  CB  LEU A 725     -24.210  -1.512  25.091  1.00 24.90           C  
ATOM   2202  CG  LEU A 725     -22.889  -1.108  25.745  1.00 27.65           C  
ATOM   2203  CD1 LEU A 725     -22.743   0.406  25.742  1.00 22.00           C  
ATOM   2204  CD2 LEU A 725     -22.800  -1.660  27.158  1.00 26.50           C  
ATOM   2205  N   THR A 726     -25.753  -3.012  22.792  1.00 23.02           N  
ATOM   2206  CA  THR A 726     -26.941  -3.265  21.983  1.00 25.07           C  
ATOM   2207  C   THR A 726     -27.393  -4.713  22.122  1.00 28.59           C  
ATOM   2208  O   THR A 726     -28.582  -4.991  22.330  1.00 26.67           O  
ATOM   2209  CB  THR A 726     -26.658  -2.932  20.519  1.00 24.79           C  
ATOM   2210  OG1 THR A 726     -26.129  -1.605  20.422  1.00 31.42           O  
ATOM   2211  CG2 THR A 726     -27.931  -3.026  19.699  1.00 26.80           C  
ATOM   2212  N   HIS A 727     -26.448  -5.652  22.019  1.00 27.97           N  
ATOM   2213  CA  HIS A 727     -26.785  -7.066  22.145  1.00 32.15           C  
ATOM   2214  C   HIS A 727     -27.407  -7.370  23.502  1.00 31.44           C  
ATOM   2215  O   HIS A 727     -28.330  -8.186  23.599  1.00 30.98           O  
ATOM   2216  CB  HIS A 727     -25.540  -7.923  21.921  1.00 29.62           C  
ATOM   2217  CG  HIS A 727     -25.807  -9.395  21.967  1.00 41.21           C  
ATOM   2218  ND1 HIS A 727     -26.179 -10.119  20.854  1.00 39.00           N  
ATOM   2219  CD2 HIS A 727     -25.764 -10.277  22.993  1.00 36.17           C  
ATOM   2220  CE1 HIS A 727     -26.349 -11.384  21.192  1.00 38.67           C  
ATOM   2221  NE2 HIS A 727     -26.103 -11.507  22.484  1.00 46.13           N  
ATOM   2222  N   GLN A 728     -26.921  -6.719  24.562  1.00 26.15           N  
ATOM   2223  CA  GLN A 728     -27.503  -6.941  25.882  1.00 25.35           C  
ATOM   2224  C   GLN A 728     -28.915  -6.373  25.969  1.00 25.83           C  
ATOM   2225  O   GLN A 728     -29.813  -7.016  26.524  1.00 30.69           O  
ATOM   2226  CB  GLN A 728     -26.609  -6.334  26.962  1.00 26.45           C  
ATOM   2227  CG  GLN A 728     -25.520  -7.274  27.456  1.00 23.45           C  
ATOM   2228  CD  GLN A 728     -24.684  -6.664  28.563  1.00 41.10           C  
ATOM   2229  OE1 GLN A 728     -24.934  -6.900  29.746  1.00 40.02           O  
ATOM   2230  NE2 GLN A 728     -23.688  -5.871  28.185  1.00 36.02           N  
ATOM   2231  N   LEU A 729     -29.132  -5.173  25.423  1.00 29.33           N  
ATOM   2232  CA  LEU A 729     -30.466  -4.582  25.447  1.00 28.06           C  
ATOM   2233  C   LEU A 729     -31.461  -5.358  24.594  1.00 27.99           C  
ATOM   2234  O   LEU A 729     -32.668  -5.285  24.853  1.00 29.20           O  
ATOM   2235  CB  LEU A 729     -30.410  -3.126  24.977  1.00 27.22           C  
ATOM   2236  CG  LEU A 729     -29.797  -2.123  25.956  1.00 24.99           C  
ATOM   2237  CD1 LEU A 729     -29.863  -0.711  25.396  1.00 18.56           C  
ATOM   2238  CD2 LEU A 729     -30.489  -2.203  27.307  1.00 23.04           C  
ATOM   2239  N   MET A 730     -30.987  -6.102  23.591  1.00 30.80           N  
ATOM   2240  CA  MET A 730     -31.895  -6.832  22.712  1.00 29.03           C  
ATOM   2241  C   MET A 730     -32.629  -7.962  23.423  1.00 30.45           C  
ATOM   2242  O   MET A 730     -33.674  -8.404  22.935  1.00 25.10           O  
ATOM   2243  CB  MET A 730     -31.130  -7.393  21.516  1.00 27.92           C  
ATOM   2244  CG  MET A 730     -30.824  -6.365  20.446  1.00 28.86           C  
ATOM   2245  SD  MET A 730     -29.783  -7.048  19.148  1.00 37.18           S  
ATOM   2246  CE  MET A 730     -30.777  -8.448  18.628  1.00 27.64           C  
ATOM   2247  N   SER A 731     -32.112  -8.442  24.554  1.00 29.51           N  
ATOM   2248  CA  SER A 731     -32.765  -9.513  25.298  1.00 30.54           C  
ATOM   2249  C   SER A 731     -33.952  -9.027  26.119  1.00 30.05           C  
ATOM   2250  O   SER A 731     -34.533  -9.822  26.866  1.00 31.09           O  
ATOM   2251  CB  SER A 731     -31.757 -10.209  26.215  1.00 23.51           C  
ATOM   2252  OG  SER A 731     -31.347  -9.351  27.265  1.00 34.98           O  
ATOM   2253  N   LEU A 732     -34.324  -7.757  26.000  1.00 30.06           N  
ATOM   2254  CA  LEU A 732     -35.435  -7.177  26.736  1.00 32.38           C  
ATOM   2255  C   LEU A 732     -36.609  -6.907  25.804  1.00 31.57           C  
ATOM   2256  O   LEU A 732     -36.445  -6.753  24.591  1.00 31.56           O  
ATOM   2257  CB  LEU A 732     -35.017  -5.872  27.421  1.00 27.01           C  
ATOM   2258  CG  LEU A 732     -33.927  -5.967  28.486  1.00 31.44           C  
ATOM   2259  CD1 LEU A 732     -33.294  -4.602  28.703  1.00 24.13           C  
ATOM   2260  CD2 LEU A 732     -34.499  -6.514  29.782  1.00 22.79           C  
ATOM   2261  N   ALA A 733     -37.803  -6.857  26.399  1.00 31.75           N  
ATOM   2262  CA  ALA A 733     -39.023  -6.436  25.707  1.00 38.19           C  
ATOM   2263  C   ALA A 733     -39.255  -7.235  24.428  1.00 35.30           C  
ATOM   2264  O   ALA A 733     -39.729  -6.708  23.419  1.00 39.35           O  
ATOM   2265  CB  ALA A 733     -38.989  -4.935  25.411  1.00 36.04           C  
ATOM   2266  N   ALA A 734     -38.909  -8.522  24.469  1.00 40.25           N  
ATOM   2267  CA  ALA A 734     -39.021  -9.428  23.327  1.00 36.23           C  
ATOM   2268  C   ALA A 734     -38.285  -8.910  22.092  1.00 38.13           C  
ATOM   2269  O   ALA A 734     -38.624  -9.280  20.964  1.00 40.98           O  
ATOM   2270  CB  ALA A 734     -40.489  -9.714  22.987  1.00 32.82           C  
ATOM   2271  N   GLY A 735     -37.280  -8.055  22.281  1.00 37.35           N  
ATOM   2272  CA  GLY A 735     -36.487  -7.548  21.184  1.00 35.89           C  
ATOM   2273  C   GLY A 735     -36.930  -6.218  20.614  1.00 38.57           C  
ATOM   2274  O   GLY A 735     -36.317  -5.744  19.648  1.00 38.16           O  
ATOM   2275  N   ARG A 736     -37.965  -5.596  21.176  1.00 37.96           N  
ATOM   2276  CA  ARG A 736     -38.492  -4.329  20.667  1.00 33.18           C  
ATOM   2277  C   ARG A 736     -37.582  -3.196  21.128  1.00 36.76           C  
ATOM   2278  O   ARG A 736     -37.754  -2.627  22.209  1.00 39.59           O  
ATOM   2279  CB  ARG A 736     -39.926  -4.120  21.136  1.00 33.15           C  
ATOM   2280  CG  ARG A 736     -40.865  -5.260  20.777  1.00 40.87           C  
ATOM   2281  CD  ARG A 736     -42.300  -4.957  21.176  1.00 44.21           C  
ATOM   2282  NE  ARG A 736     -43.242  -5.855  20.514  1.00 57.20           N  
ATOM   2283  CZ  ARG A 736     -44.520  -5.568  20.291  1.00 61.20           C  
ATOM   2284  NH1 ARG A 736     -45.019  -4.402  20.678  1.00 52.41           N  
ATOM   2285  NH2 ARG A 736     -45.301  -6.448  19.678  1.00 61.96           N  
ATOM   2286  N   VAL A 737     -36.601  -2.855  20.292  1.00 32.57           N  
ATOM   2287  CA  VAL A 737     -35.602  -1.840  20.612  1.00 33.29           C  
ATOM   2288  C   VAL A 737     -35.534  -0.833  19.471  1.00 27.07           C  
ATOM   2289  O   VAL A 737     -35.422  -1.219  18.303  1.00 27.08           O  
ATOM   2290  CB  VAL A 737     -34.212  -2.461  20.859  1.00 33.30           C  
ATOM   2291  CG1 VAL A 737     -33.219  -1.389  21.286  1.00 25.75           C  
ATOM   2292  CG2 VAL A 737     -34.295  -3.560  21.905  1.00 29.27           C  
ATOM   2293  N   LEU A 738     -35.590   0.454  19.812  1.00 29.91           N  
ATOM   2294  CA  LEU A 738     -35.420   1.543  18.856  1.00 26.48           C  
ATOM   2295  C   LEU A 738     -34.173   2.328  19.237  1.00 24.09           C  
ATOM   2296  O   LEU A 738     -34.066   2.816  20.367  1.00 24.32           O  
ATOM   2297  CB  LEU A 738     -36.650   2.453  18.834  1.00 25.33           C  
ATOM   2298  CG  LEU A 738     -36.582   3.695  17.943  1.00 25.71           C  
ATOM   2299  CD1 LEU A 738     -36.107   3.343  16.540  1.00 22.31           C  
ATOM   2300  CD2 LEU A 738     -37.936   4.382  17.900  1.00 25.54           C  
ATOM   2301  N   ILE A 739     -33.238   2.450  18.299  1.00 24.03           N  
ATOM   2302  CA  ILE A 739     -31.939   3.068  18.550  1.00 28.19           C  
ATOM   2303  C   ILE A 739     -31.961   4.464  17.936  1.00 27.06           C  
ATOM   2304  O   ILE A 739     -31.714   4.627  16.741  1.00 28.59           O  
ATOM   2305  CB  ILE A 739     -30.796   2.225  17.977  1.00 25.36           C  
ATOM   2306  CG1 ILE A 739     -30.880   0.782  18.479  1.00 32.33           C  
ATOM   2307  CG2 ILE A 739     -29.454   2.846  18.320  1.00 24.41           C  
ATOM   2308  CD1 ILE A 739     -30.162   0.537  19.787  1.00 33.72           C  
ATOM   2309  N   ILE A 740     -32.219   5.484  18.753  1.00 26.28           N  
ATOM   2310  CA  ILE A 740     -32.352   6.860  18.279  1.00 26.13           C  
ATOM   2311  C   ILE A 740     -31.000   7.557  18.382  1.00 27.43           C  
ATOM   2312  O   ILE A 740     -30.417   7.636  19.470  1.00 31.45           O  
ATOM   2313  CB  ILE A 740     -33.415   7.627  19.078  1.00 27.07           C  
ATOM   2314  CG1 ILE A 740     -34.738   6.862  19.090  1.00 27.11           C  
ATOM   2315  CG2 ILE A 740     -33.601   9.027  18.508  1.00 30.48           C  
ATOM   2316  CD1 ILE A 740     -35.764   7.449  20.035  1.00 22.47           C  
ATOM   2317  N   LEU A 741     -30.512   8.087  17.261  1.00 27.98           N  
ATOM   2318  CA  LEU A 741     -29.249   8.819  17.278  1.00 29.46           C  
ATOM   2319  C   LEU A 741     -29.387  10.130  18.047  1.00 32.83           C  
ATOM   2320  O   LEU A 741     -30.393  10.835  17.932  1.00 32.26           O  
ATOM   2321  CB  LEU A 741     -28.774   9.103  15.853  1.00 31.22           C  
ATOM   2322  CG  LEU A 741     -27.547  10.013  15.726  1.00 33.91           C  
ATOM   2323  CD1 LEU A 741     -26.306   9.333  16.287  1.00 32.44           C  
ATOM   2324  CD2 LEU A 741     -27.324  10.438  14.282  1.00 33.49           C  
ATOM   2325  N   GLU A 742     -28.360  10.456  18.836  1.00 33.09           N  
ATOM   2326  CA  GLU A 742     -28.323  11.714  19.574  1.00 32.50           C  
ATOM   2327  C   GLU A 742     -27.028  12.471  19.294  1.00 35.15           C  
ATOM   2328  O   GLU A 742     -26.890  13.108  18.245  1.00 33.34           O  
ATOM   2329  CB  GLU A 742     -28.477  11.462  21.076  1.00 31.68           C  
ATOM   2330  CG  GLU A 742     -29.787  10.794  21.468  1.00 31.14           C  
ATOM   2331  CD  GLU A 742     -30.830  11.787  21.944  1.00 31.69           C  
ATOM   2332  OE1 GLU A 742     -30.573  13.006  21.857  1.00 41.80           O  
ATOM   2333  OE2 GLU A 742     -31.905  11.352  22.408  1.00 30.98           O  
ATOM   2334  N   GLY A 743     -26.074  12.406  20.223  1.00 32.85           N  
ATOM   2335  CA  GLY A 743     -24.797  13.069  20.069  1.00 35.20           C  
ATOM   2336  C   GLY A 743     -23.764  12.196  19.379  1.00 42.28           C  
ATOM   2337  O   GLY A 743     -24.041  11.088  18.916  1.00 44.00           O  
ATOM   2338  N   GLY A 744     -22.539  12.717  19.322  1.00 41.69           N  
ATOM   2339  CA  GLY A 744     -21.448  12.039  18.647  1.00 42.38           C  
ATOM   2340  C   GLY A 744     -20.894  12.871  17.510  1.00 47.82           C  
ATOM   2341  O   GLY A 744     -21.581  13.086  16.507  1.00 50.51           O  
ATOM   2342  N   TYR A 745     -19.652  13.340  17.643  1.00 47.48           N  
ATOM   2343  CA  TYR A 745     -19.141  14.385  16.763  1.00 43.72           C  
ATOM   2344  C   TYR A 745     -17.821  13.995  16.109  1.00 46.89           C  
ATOM   2345  O   TYR A 745     -17.005  14.859  15.780  1.00 54.69           O  
ATOM   2346  CB  TYR A 745     -19.011  15.699  17.527  1.00 41.89           C  
ATOM   2347  CG  TYR A 745     -20.255  16.007  18.325  1.00 46.22           C  
ATOM   2348  CD1 TYR A 745     -21.374  16.556  17.714  1.00 42.16           C  
ATOM   2349  CD2 TYR A 745     -20.325  15.714  19.680  1.00 46.66           C  
ATOM   2350  CE1 TYR A 745     -22.520  16.826  18.434  1.00 40.53           C  
ATOM   2351  CE2 TYR A 745     -21.466  15.979  20.408  1.00 38.39           C  
ATOM   2352  CZ  TYR A 745     -22.561  16.535  19.780  1.00 40.51           C  
ATOM   2353  OH  TYR A 745     -23.702  16.801  20.500  1.00 39.04           O  
ATOM   2354  N   ASN A 746     -17.597  12.699  15.913  1.00 42.48           N  
ATOM   2355  CA  ASN A 746     -16.562  12.200  15.013  1.00 38.99           C  
ATOM   2356  C   ASN A 746     -17.274  11.360  13.963  1.00 46.34           C  
ATOM   2357  O   ASN A 746     -17.866  10.326  14.290  1.00 50.26           O  
ATOM   2358  CB  ASN A 746     -15.504  11.390  15.762  1.00 46.34           C  
ATOM   2359  CG  ASN A 746     -14.355  10.945  14.865  1.00 47.55           C  
ATOM   2360  OD1 ASN A 746     -14.554  10.570  13.708  1.00 45.99           O  
ATOM   2361  ND2 ASN A 746     -13.141  10.988  15.401  1.00 43.52           N  
ATOM   2362  N   LEU A 747     -17.216  11.808  12.707  1.00 47.00           N  
ATOM   2363  CA  LEU A 747     -17.987  11.172  11.641  1.00 48.66           C  
ATOM   2364  C   LEU A 747     -17.660   9.685  11.530  1.00 47.65           C  
ATOM   2365  O   LEU A 747     -18.562   8.838  11.465  1.00 43.82           O  
ATOM   2366  CB  LEU A 747     -17.718  11.887  10.314  1.00 46.21           C  
ATOM   2367  CG  LEU A 747     -18.293  13.290  10.063  1.00 43.45           C  
ATOM   2368  CD1 LEU A 747     -19.786  13.320  10.331  1.00 46.79           C  
ATOM   2369  CD2 LEU A 747     -17.579  14.370  10.869  1.00 38.53           C  
ATOM   2370  N   THR A 748     -16.369   9.351  11.516  1.00 48.01           N  
ATOM   2371  CA  THR A 748     -15.963   7.952  11.421  1.00 48.18           C  
ATOM   2372  C   THR A 748     -16.391   7.166  12.656  1.00 50.15           C  
ATOM   2373  O   THR A 748     -16.923   6.054  12.538  1.00 47.39           O  
ATOM   2374  CB  THR A 748     -14.449   7.867  11.221  1.00 43.86           C  
ATOM   2375  OG1 THR A 748     -14.131   8.165   9.857  1.00 45.86           O  
ATOM   2376  CG2 THR A 748     -13.934   6.478  11.561  1.00 49.91           C  
ATOM   2377  N   SER A 749     -16.181   7.737  13.846  1.00 43.68           N  
ATOM   2378  CA  SER A 749     -16.540   7.048  15.082  1.00 43.52           C  
ATOM   2379  C   SER A 749     -18.029   6.728  15.124  1.00 46.20           C  
ATOM   2380  O   SER A 749     -18.424   5.597  15.430  1.00 51.75           O  
ATOM   2381  CB  SER A 749     -16.139   7.895  16.290  1.00 44.36           C  
ATOM   2382  OG  SER A 749     -14.730   7.978  16.414  1.00 50.51           O  
ATOM   2383  N   ILE A 750     -18.873   7.713  14.807  1.00 39.15           N  
ATOM   2384  CA  ILE A 750     -20.314   7.503  14.906  1.00 39.84           C  
ATOM   2385  C   ILE A 750     -20.804   6.576  13.799  1.00 43.77           C  
ATOM   2386  O   ILE A 750     -21.696   5.745  14.020  1.00 44.25           O  
ATOM   2387  CB  ILE A 750     -21.059   8.852  14.905  1.00 39.93           C  
ATOM   2388  CG1 ILE A 750     -20.897   9.577  13.567  1.00 39.95           C  
ATOM   2389  CG2 ILE A 750     -20.565   9.726  16.044  1.00 41.35           C  
ATOM   2390  CD1 ILE A 750     -21.582  10.921  13.519  1.00 41.82           C  
ATOM   2391  N   SER A 751     -20.226   6.687  12.598  1.00 43.28           N  
ATOM   2392  CA  SER A 751     -20.614   5.791  11.512  1.00 45.76           C  
ATOM   2393  C   SER A 751     -20.307   4.341  11.868  1.00 46.44           C  
ATOM   2394  O   SER A 751     -21.168   3.458  11.748  1.00 44.45           O  
ATOM   2395  CB  SER A 751     -19.903   6.195  10.219  1.00 48.23           C  
ATOM   2396  OG  SER A 751     -20.269   7.505   9.821  1.00 48.04           O  
ATOM   2397  N   GLU A 752     -19.081   4.083  12.329  1.00 50.11           N  
ATOM   2398  CA  GLU A 752     -18.695   2.727  12.706  1.00 43.33           C  
ATOM   2399  C   GLU A 752     -19.538   2.214  13.869  1.00 45.79           C  
ATOM   2400  O   GLU A 752     -20.055   1.090  13.829  1.00 43.57           O  
ATOM   2401  CB  GLU A 752     -17.208   2.692  13.062  1.00 48.03           C  
ATOM   2402  CG  GLU A 752     -16.296   2.368  11.891  1.00 57.19           C  
ATOM   2403  CD  GLU A 752     -16.376   0.909  11.480  1.00 69.61           C  
ATOM   2404  OE1 GLU A 752     -16.691   0.637  10.302  1.00 63.20           O  
ATOM   2405  OE2 GLU A 752     -16.127   0.035  12.339  1.00 61.85           O  
ATOM   2406  N   SER A 753     -19.695   3.032  14.912  1.00 44.48           N  
ATOM   2407  CA  SER A 753     -20.391   2.583  16.115  1.00 41.31           C  
ATOM   2408  C   SER A 753     -21.854   2.263  15.825  1.00 41.32           C  
ATOM   2409  O   SER A 753     -22.337   1.163  16.133  1.00 43.19           O  
ATOM   2410  CB  SER A 753     -20.273   3.643  17.210  1.00 40.04           C  
ATOM   2411  OG  SER A 753     -18.914   3.930  17.495  1.00 39.30           O  
ATOM   2412  N   MET A 754     -22.580   3.213  15.228  1.00 39.48           N  
ATOM   2413  CA  MET A 754     -23.988   2.950  14.952  1.00 36.27           C  
ATOM   2414  C   MET A 754     -24.158   1.851  13.913  1.00 42.82           C  
ATOM   2415  O   MET A 754     -25.161   1.126  13.941  1.00 39.68           O  
ATOM   2416  CB  MET A 754     -24.703   4.222  14.504  1.00 33.00           C  
ATOM   2417  CG  MET A 754     -26.199   4.160  14.759  1.00 30.52           C  
ATOM   2418  SD  MET A 754     -27.105   5.621  14.238  1.00 44.75           S  
ATOM   2419  CE  MET A 754     -28.462   5.585  15.405  1.00 33.30           C  
ATOM   2420  N   SER A 755     -23.194   1.701  13.000  1.00 44.24           N  
ATOM   2421  CA  SER A 755     -23.236   0.560  12.092  1.00 42.79           C  
ATOM   2422  C   SER A 755     -23.131  -0.753  12.860  1.00 38.62           C  
ATOM   2423  O   SER A 755     -23.819  -1.727  12.536  1.00 39.41           O  
ATOM   2424  CB  SER A 755     -22.124   0.674  11.051  1.00 43.26           C  
ATOM   2425  OG  SER A 755     -22.537   1.481   9.962  1.00 46.85           O  
ATOM   2426  N   MET A 756     -22.279  -0.792  13.888  1.00 38.43           N  
ATOM   2427  CA  MET A 756     -22.182  -1.979  14.733  1.00 44.14           C  
ATOM   2428  C   MET A 756     -23.507  -2.262  15.431  1.00 41.94           C  
ATOM   2429  O   MET A 756     -23.979  -3.408  15.460  1.00 43.50           O  
ATOM   2430  CB  MET A 756     -21.062  -1.800  15.758  1.00 45.61           C  
ATOM   2431  CG  MET A 756     -19.668  -2.073  15.221  1.00 48.24           C  
ATOM   2432  SD  MET A 756     -19.195  -3.801  15.412  1.00 60.62           S  
ATOM   2433  CE  MET A 756     -17.544  -3.779  14.719  1.00 54.12           C  
ATOM   2434  N   CYS A 757     -24.125  -1.222  16.002  1.00 34.36           N  
ATOM   2435  CA  CYS A 757     -25.426  -1.405  16.643  1.00 34.88           C  
ATOM   2436  C   CYS A 757     -26.453  -1.961  15.664  1.00 36.07           C  
ATOM   2437  O   CYS A 757     -27.226  -2.864  16.008  1.00 33.31           O  
ATOM   2438  CB  CYS A 757     -25.910  -0.084  17.238  1.00 29.49           C  
ATOM   2439  SG  CYS A 757     -24.824   0.589  18.512  1.00 37.10           S  
ATOM   2440  N   THR A 758     -26.472  -1.440  14.434  1.00 38.11           N  
ATOM   2441  CA  THR A 758     -27.385  -1.971  13.427  1.00 39.36           C  
ATOM   2442  C   THR A 758     -27.066  -3.423  13.095  1.00 40.25           C  
ATOM   2443  O   THR A 758     -27.980  -4.215  12.838  1.00 39.22           O  
ATOM   2444  CB  THR A 758     -27.335  -1.109  12.164  1.00 39.43           C  
ATOM   2445  OG1 THR A 758     -27.597   0.256  12.510  1.00 41.30           O  
ATOM   2446  CG2 THR A 758     -28.378  -1.572  11.158  1.00 38.64           C  
ATOM   2447  N   SER A 759     -25.783  -3.793  13.102  1.00 41.77           N  
ATOM   2448  CA  SER A 759     -25.416  -5.187  12.875  1.00 40.16           C  
ATOM   2449  C   SER A 759     -25.997  -6.083  13.961  1.00 39.45           C  
ATOM   2450  O   SER A 759     -26.565  -7.142  13.670  1.00 44.53           O  
ATOM   2451  CB  SER A 759     -23.896  -5.335  12.813  1.00 39.69           C  
ATOM   2452  OG  SER A 759     -23.361  -4.659  11.689  1.00 53.68           O  
ATOM   2453  N   MET A 760     -25.868  -5.669  15.224  1.00 41.61           N  
ATOM   2454  CA  MET A 760     -26.460  -6.449  16.307  1.00 35.66           C  
ATOM   2455  C   MET A 760     -27.973  -6.534  16.159  1.00 28.51           C  
ATOM   2456  O   MET A 760     -28.565  -7.599  16.369  1.00 35.29           O  
ATOM   2457  CB  MET A 760     -26.082  -5.847  17.659  1.00 32.59           C  
ATOM   2458  CG  MET A 760     -24.590  -5.813  17.905  1.00 33.12           C  
ATOM   2459  SD  MET A 760     -23.861  -7.454  17.791  1.00 42.49           S  
ATOM   2460  CE  MET A 760     -22.695  -7.201  16.457  1.00 43.74           C  
ATOM   2461  N   LEU A 761     -28.617  -5.425  15.787  1.00 34.42           N  
ATOM   2462  CA  LEU A 761     -30.060  -5.454  15.574  1.00 36.65           C  
ATOM   2463  C   LEU A 761     -30.445  -6.414  14.457  1.00 38.20           C  
ATOM   2464  O   LEU A 761     -31.511  -7.038  14.514  1.00 29.71           O  
ATOM   2465  CB  LEU A 761     -30.576  -4.049  15.262  1.00 31.35           C  
ATOM   2466  CG  LEU A 761     -30.580  -3.042  16.410  1.00 31.67           C  
ATOM   2467  CD1 LEU A 761     -31.541  -1.903  16.106  1.00 24.67           C  
ATOM   2468  CD2 LEU A 761     -30.945  -3.721  17.721  1.00 30.55           C  
ATOM   2469  N   LEU A 762     -29.592  -6.552  13.440  1.00 35.42           N  
ATOM   2470  CA  LEU A 762     -29.876  -7.425  12.310  1.00 36.89           C  
ATOM   2471  C   LEU A 762     -29.680  -8.900  12.633  1.00 43.06           C  
ATOM   2472  O   LEU A 762     -30.136  -9.751  11.863  1.00 46.33           O  
ATOM   2473  CB  LEU A 762     -29.001  -7.035  11.116  1.00 38.03           C  
ATOM   2474  CG  LEU A 762     -29.446  -5.787  10.347  1.00 37.46           C  
ATOM   2475  CD1 LEU A 762     -28.364  -5.321   9.388  1.00 41.47           C  
ATOM   2476  CD2 LEU A 762     -30.745  -6.047   9.601  1.00 38.09           C  
ATOM   2477  N   GLY A 763     -29.017  -9.222  13.742  1.00 39.04           N  
ATOM   2478  CA  GLY A 763     -28.850 -10.595  14.171  1.00 36.75           C  
ATOM   2479  C   GLY A 763     -27.435 -11.125  14.104  1.00 45.50           C  
ATOM   2480  O   GLY A 763     -27.224 -12.301  14.425  1.00 54.55           O  
ATOM   2481  N   ASP A 764     -26.461 -10.314  13.701  1.00 39.36           N  
ATOM   2482  CA  ASP A 764     -25.086 -10.784  13.634  1.00 43.76           C  
ATOM   2483  C   ASP A 764     -24.540 -11.047  15.036  1.00 47.41           C  
ATOM   2484  O   ASP A 764     -25.027 -10.511  16.036  1.00 47.77           O  
ATOM   2485  CB  ASP A 764     -24.204  -9.770  12.904  1.00 41.32           C  
ATOM   2486  CG  ASP A 764     -24.751  -9.397  11.539  1.00 48.73           C  
ATOM   2487  OD1 ASP A 764     -25.765  -9.992  11.116  1.00 47.56           O  
ATOM   2488  OD2 ASP A 764     -24.165  -8.504  10.890  1.00 52.00           O  
ATOM   2489  N   SER A 765     -23.514 -11.892  15.099  1.00 48.61           N  
ATOM   2490  CA  SER A 765     -22.937 -12.265  16.380  1.00 52.19           C  
ATOM   2491  C   SER A 765     -21.968 -11.189  16.872  1.00 49.24           C  
ATOM   2492  O   SER A 765     -21.277 -10.552  16.072  1.00 50.04           O  
ATOM   2493  CB  SER A 765     -22.222 -13.607  16.269  1.00 58.52           C  
ATOM   2494  OG  SER A 765     -23.158 -14.669  16.162  1.00 66.18           O  
ATOM   2495  N   PRO A 766     -21.905 -10.969  18.183  1.00 50.34           N  
ATOM   2496  CA  PRO A 766     -21.123  -9.850  18.717  1.00 54.51           C  
ATOM   2497  C   PRO A 766     -19.635 -10.104  18.579  1.00 52.61           C  
ATOM   2498  O   PRO A 766     -19.145 -11.186  18.934  1.00 63.32           O  
ATOM   2499  CB  PRO A 766     -21.539  -9.802  20.197  1.00 50.65           C  
ATOM   2500  CG  PRO A 766     -22.804 -10.621  20.272  1.00 49.88           C  
ATOM   2501  CD  PRO A 766     -22.605 -11.693  19.254  1.00 46.95           C  
ATOM   2502  N   PRO A 767     -18.881  -9.128  18.079  1.00 52.84           N  
ATOM   2503  CA  PRO A 767     -17.424  -9.278  18.045  1.00 57.13           C  
ATOM   2504  C   PRO A 767     -16.855  -9.417  19.447  1.00 57.23           C  
ATOM   2505  O   PRO A 767     -17.337  -8.800  20.402  1.00 57.73           O  
ATOM   2506  CB  PRO A 767     -16.947  -7.983  17.376  1.00 59.46           C  
ATOM   2507  CG  PRO A 767     -18.058  -7.004  17.616  1.00 51.27           C  
ATOM   2508  CD  PRO A 767     -19.315  -7.820  17.558  1.00 57.01           C  
ATOM   2509  N   SER A 768     -15.817 -10.247  19.558  1.00 64.05           N  
ATOM   2510  CA  SER A 768     -15.097 -10.388  20.814  1.00 67.16           C  
ATOM   2511  C   SER A 768     -14.527  -9.038  21.222  1.00 63.06           C  
ATOM   2512  O   SER A 768     -14.228  -8.187  20.379  1.00 66.56           O  
ATOM   2513  CB  SER A 768     -13.974 -11.421  20.678  1.00 67.54           C  
ATOM   2514  OG  SER A 768     -13.730 -12.103  21.898  1.00 60.18           O  
ATOM   2515  N   LEU A 769     -14.368  -8.848  22.528  1.00 58.30           N  
ATOM   2516  CA  LEU A 769     -14.025  -7.551  23.093  1.00 66.38           C  
ATOM   2517  C   LEU A 769     -12.849  -7.667  24.041  1.00 75.16           C  
ATOM   2518  O   LEU A 769     -12.930  -8.399  25.031  1.00 70.74           O  
ATOM   2519  CB  LEU A 769     -15.209  -6.944  23.845  1.00 58.31           C  
ATOM   2520  CG  LEU A 769     -14.874  -5.504  24.209  1.00 56.57           C  
ATOM   2521  CD1 LEU A 769     -14.946  -4.747  22.913  1.00 58.95           C  
ATOM   2522  CD2 LEU A 769     -15.851  -4.921  25.229  1.00 56.51           C  
ATOM   2523  N   ASP A 770     -11.779  -6.926  23.737  1.00 83.07           N  
ATOM   2524  CA  ASP A 770     -10.657  -6.657  24.637  1.00 87.14           C  
ATOM   2525  C   ASP A 770     -10.319  -7.710  25.692  1.00 87.53           C  
ATOM   2526  O   ASP A 770     -10.447  -8.918  25.467  1.00 87.25           O  
ATOM   2527  CB  ASP A 770     -10.907  -5.321  25.352  1.00 79.94           C  
ATOM   2528  N   HIS A 771      -9.818  -7.225  26.831  1.00 86.92           N  
ATOM   2529  CA  HIS A 771      -9.667  -7.999  28.055  1.00 94.98           C  
ATOM   2530  C   HIS A 771     -10.143  -7.186  29.249  1.00 87.43           C  
ATOM   2531  O   HIS A 771      -9.963  -7.616  30.398  1.00 92.71           O  
ATOM   2532  CB  HIS A 771      -8.211  -8.436  28.265  1.00 95.37           C  
ATOM   2533  N   LEU A 772     -10.733  -6.017  28.994  1.00 79.05           N  
ATOM   2534  CA  LEU A 772     -11.113  -5.031  30.001  1.00 85.53           C  
ATOM   2535  C   LEU A 772      -9.924  -4.630  30.867  1.00 86.04           C  
ATOM   2536  O   LEU A 772      -9.550  -3.451  30.899  1.00 77.25           O  
ATOM   2537  CB  LEU A 772     -12.256  -5.542  30.889  1.00 92.08           C  
ATOM   2538  CG  LEU A 772     -13.516  -6.227  30.336  1.00 73.49           C  
ATOM   2539  CD1 LEU A 772     -13.929  -5.716  28.958  1.00 62.38           C  
ATOM   2540  CD2 LEU A 772     -13.379  -7.745  30.331  1.00 86.16           C  
ATOM   2541  N   THR A 773      -9.321  -5.626  31.545  1.00 93.75           N  
ATOM   2542  CA  THR A 773      -8.340  -5.544  32.625  1.00 85.51           C  
ATOM   2543  C   THR A 773      -9.187  -5.336  33.886  1.00 74.89           C  
ATOM   2544  O   THR A 773     -10.122  -6.123  34.084  1.00 79.10           O  
ATOM   2545  CB  THR A 773      -7.276  -4.480  32.321  1.00 94.07           C  
ATOM   2546  N   PRO A 774      -8.944  -4.343  34.781  1.00 70.29           N  
ATOM   2547  CA  PRO A 774     -10.038  -3.982  35.691  1.00 70.17           C  
ATOM   2548  C   PRO A 774     -10.704  -2.670  35.315  1.00 59.42           C  
ATOM   2549  O   PRO A 774     -10.592  -2.206  34.177  1.00 61.60           O  
ATOM   2550  CB  PRO A 774      -9.354  -3.900  37.065  1.00 73.02           C  
ATOM   2551  CG  PRO A 774      -7.874  -3.911  36.799  1.00 81.93           C  
ATOM   2552  CD  PRO A 774      -7.671  -3.836  35.328  1.00 74.87           C  
ATOM   2553  N   LEU A 775     -11.411  -2.070  36.264  1.00 55.39           N  
ATOM   2554  CA  LEU A 775     -12.051  -0.780  36.067  1.00 54.01           C  
ATOM   2555  C   LEU A 775     -11.309   0.295  36.848  1.00 55.12           C  
ATOM   2556  O   LEU A 775     -10.724   0.026  37.903  1.00 58.89           O  
ATOM   2557  CB  LEU A 775     -13.514  -0.794  36.525  1.00 52.89           C  
ATOM   2558  CG  LEU A 775     -14.391  -2.028  36.332  1.00 40.28           C  
ATOM   2559  CD1 LEU A 775     -15.794  -1.747  36.845  1.00 39.91           C  
ATOM   2560  CD2 LEU A 775     -14.426  -2.454  34.881  1.00 39.51           C  
ATOM   2561  N   LYS A 776     -11.351   1.518  36.322  1.00 49.91           N  
ATOM   2562  CA  LYS A 776     -10.979   2.677  37.119  1.00 51.03           C  
ATOM   2563  C   LYS A 776     -11.746   2.643  38.436  1.00 48.89           C  
ATOM   2564  O   LYS A 776     -12.972   2.507  38.446  1.00 48.57           O  
ATOM   2565  CB  LYS A 776     -11.287   3.965  36.353  1.00 46.40           C  
ATOM   2566  CG  LYS A 776     -10.101   4.575  35.613  1.00 50.92           C  
ATOM   2567  CD  LYS A 776     -10.374   4.669  34.117  1.00 43.45           C  
ATOM   2568  N   THR A 777     -11.011   2.742  39.549  1.00 44.14           N  
ATOM   2569  CA  THR A 777     -11.625   2.611  40.869  1.00 44.01           C  
ATOM   2570  C   THR A 777     -12.819   3.544  41.027  1.00 43.17           C  
ATOM   2571  O   THR A 777     -13.840   3.169  41.616  1.00 44.64           O  
ATOM   2572  CB  THR A 777     -10.582   2.883  41.957  1.00 49.29           C  
ATOM   2573  OG1 THR A 777      -9.539   1.904  41.874  1.00 68.77           O  
ATOM   2574  CG2 THR A 777     -11.213   2.823  43.339  1.00 44.22           C  
ATOM   2575  N   SER A 778     -12.719   4.756  40.475  1.00 48.35           N  
ATOM   2576  CA  SER A 778     -13.816   5.715  40.561  1.00 44.67           C  
ATOM   2577  C   SER A 778     -15.086   5.185  39.907  1.00 43.28           C  
ATOM   2578  O   SER A 778     -16.193   5.534  40.332  1.00 40.17           O  
ATOM   2579  CB  SER A 778     -13.398   7.038  39.919  1.00 39.56           C  
ATOM   2580  OG  SER A 778     -12.876   6.828  38.617  1.00 43.63           O  
ATOM   2581  N   ALA A 779     -14.952   4.342  38.879  1.00 40.80           N  
ATOM   2582  CA  ALA A 779     -16.132   3.762  38.243  1.00 40.04           C  
ATOM   2583  C   ALA A 779     -16.798   2.730  39.145  1.00 40.73           C  
ATOM   2584  O   ALA A 779     -18.031   2.677  39.229  1.00 36.13           O  
ATOM   2585  CB  ALA A 779     -15.754   3.140  36.902  1.00 35.20           C  
ATOM   2586  N   THR A 780     -16.004   1.894  39.819  1.00 36.46           N  
ATOM   2587  CA  THR A 780     -16.571   0.975  40.802  1.00 33.35           C  
ATOM   2588  C   THR A 780     -17.245   1.739  41.935  1.00 33.37           C  
ATOM   2589  O   THR A 780     -18.308   1.335  42.424  1.00 29.66           O  
ATOM   2590  CB  THR A 780     -15.484   0.047  41.347  1.00 36.16           C  
ATOM   2591  OG1 THR A 780     -14.901  -0.695  40.269  1.00 31.42           O  
ATOM   2592  CG2 THR A 780     -16.068  -0.923  42.361  1.00 29.50           C  
ATOM   2593  N   VAL A 781     -16.646   2.859  42.354  1.00 39.66           N  
ATOM   2594  CA  VAL A 781     -17.254   3.694  43.388  1.00 37.81           C  
ATOM   2595  C   VAL A 781     -18.576   4.272  42.899  1.00 35.83           C  
ATOM   2596  O   VAL A 781     -19.555   4.353  43.654  1.00 34.45           O  
ATOM   2597  CB  VAL A 781     -16.277   4.805  43.817  1.00 39.74           C  
ATOM   2598  CG1 VAL A 781     -16.921   5.703  44.862  1.00 34.69           C  
ATOM   2599  CG2 VAL A 781     -14.986   4.204  44.348  1.00 36.03           C  
ATOM   2600  N   SER A 782     -18.623   4.687  41.631  1.00 33.87           N  
ATOM   2601  CA  SER A 782     -19.863   5.202  41.061  1.00 32.19           C  
ATOM   2602  C   SER A 782     -20.940   4.126  41.042  1.00 35.47           C  
ATOM   2603  O   SER A 782     -22.070   4.354  41.494  1.00 35.88           O  
ATOM   2604  CB  SER A 782     -19.608   5.734  39.650  1.00 33.53           C  
ATOM   2605  OG  SER A 782     -18.631   6.761  39.657  1.00 36.73           O  
ATOM   2606  N   ILE A 783     -20.600   2.939  40.531  1.00 31.71           N  
ATOM   2607  CA  ILE A 783     -21.562   1.842  40.470  1.00 28.67           C  
ATOM   2608  C   ILE A 783     -22.075   1.507  41.864  1.00 32.33           C  
ATOM   2609  O   ILE A 783     -23.274   1.275  42.061  1.00 31.34           O  
ATOM   2610  CB  ILE A 783     -20.931   0.613  39.789  1.00 32.01           C  
ATOM   2611  CG1 ILE A 783     -20.582   0.927  38.333  1.00 28.19           C  
ATOM   2612  CG2 ILE A 783     -21.866  -0.587  39.865  1.00 24.42           C  
ATOM   2613  CD1 ILE A 783     -19.962  -0.237  37.595  1.00 28.77           C  
ATOM   2614  N   ASN A 784     -21.180   1.489  42.855  1.00 32.61           N  
ATOM   2615  CA  ASN A 784     -21.610   1.195  44.217  1.00 36.92           C  
ATOM   2616  C   ASN A 784     -22.507   2.294  44.773  1.00 37.19           C  
ATOM   2617  O   ASN A 784     -23.445   2.004  45.526  1.00 39.51           O  
ATOM   2618  CB  ASN A 784     -20.392   0.982  45.114  1.00 41.12           C  
ATOM   2619  CG  ASN A 784     -19.778  -0.393  44.939  1.00 41.96           C  
ATOM   2620  OD1 ASN A 784     -18.623  -0.524  44.535  1.00 42.37           O  
ATOM   2621  ND2 ASN A 784     -20.555  -1.429  45.234  1.00 42.11           N  
ATOM   2622  N   ASN A 785     -22.249   3.552  44.405  1.00 34.00           N  
ATOM   2623  CA  ASN A 785     -23.114   4.643  44.845  1.00 39.41           C  
ATOM   2624  C   ASN A 785     -24.513   4.505  44.256  1.00 37.47           C  
ATOM   2625  O   ASN A 785     -25.516   4.647  44.969  1.00 34.63           O  
ATOM   2626  CB  ASN A 785     -22.493   5.987  44.463  1.00 38.20           C  
ATOM   2627  CG  ASN A 785     -21.446   6.446  45.457  1.00 37.99           C  
ATOM   2628  OD1 ASN A 785     -21.630   6.324  46.668  1.00 45.10           O  
ATOM   2629  ND2 ASN A 785     -20.338   6.973  44.950  1.00 32.53           N  
ATOM   2630  N   VAL A 786     -24.598   4.224  42.951  1.00 37.72           N  
ATOM   2631  CA  VAL A 786     -25.894   3.999  42.313  1.00 35.85           C  
ATOM   2632  C   VAL A 786     -26.613   2.831  42.976  1.00 34.60           C  
ATOM   2633  O   VAL A 786     -27.807   2.909  43.291  1.00 33.59           O  
ATOM   2634  CB  VAL A 786     -25.717   3.759  40.802  1.00 33.03           C  
ATOM   2635  CG1 VAL A 786     -27.072   3.598  40.128  1.00 23.95           C  
ATOM   2636  CG2 VAL A 786     -24.927   4.890  40.166  1.00 28.10           C  
ATOM   2637  N   LEU A 787     -25.890   1.729  43.197  1.00 36.41           N  
ATOM   2638  CA  LEU A 787     -26.492   0.549  43.808  1.00 34.44           C  
ATOM   2639  C   LEU A 787     -27.053   0.869  45.185  1.00 36.26           C  
ATOM   2640  O   LEU A 787     -28.168   0.454  45.522  1.00 30.65           O  
ATOM   2641  CB  LEU A 787     -25.462  -0.577  43.899  1.00 34.81           C  
ATOM   2642  CG  LEU A 787     -25.303  -1.473  42.670  1.00 36.13           C  
ATOM   2643  CD1 LEU A 787     -23.894  -2.039  42.603  1.00 34.33           C  
ATOM   2644  CD2 LEU A 787     -26.340  -2.587  42.685  1.00 36.26           C  
ATOM   2645  N   ARG A 788     -26.296   1.614  45.995  1.00 39.51           N  
ATOM   2646  CA  ARG A 788     -26.801   2.004  47.305  1.00 38.72           C  
ATOM   2647  C   ARG A 788     -28.015   2.914  47.181  1.00 42.77           C  
ATOM   2648  O   ARG A 788     -28.930   2.845  48.009  1.00 46.83           O  
ATOM   2649  CB  ARG A 788     -25.699   2.691  48.110  1.00 39.71           C  
ATOM   2650  CG  ARG A 788     -26.035   2.888  49.579  1.00 42.37           C  
ATOM   2651  CD  ARG A 788     -24.776   2.899  50.425  1.00 41.73           C  
ATOM   2652  NE  ARG A 788     -23.652   3.479  49.699  1.00 46.76           N  
ATOM   2653  CZ  ARG A 788     -22.511   2.844  49.456  1.00 50.08           C  
ATOM   2654  NH1 ARG A 788     -22.336   1.601  49.883  1.00 50.76           N  
ATOM   2655  NH2 ARG A 788     -21.545   3.454  48.783  1.00 52.06           N  
ATOM   2656  N   ALA A 789     -28.051   3.759  46.147  1.00 39.98           N  
ATOM   2657  CA  ALA A 789     -29.170   4.682  45.994  1.00 35.59           C  
ATOM   2658  C   ALA A 789     -30.444   3.974  45.550  1.00 34.09           C  
ATOM   2659  O   ALA A 789     -31.543   4.382  45.943  1.00 34.24           O  
ATOM   2660  CB  ALA A 789     -28.807   5.785  45.000  1.00 34.74           C  
ATOM   2661  N   HIS A 790     -30.328   2.917  44.744  1.00 38.25           N  
ATOM   2662  CA  HIS A 790     -31.495   2.293  44.135  1.00 37.86           C  
ATOM   2663  C   HIS A 790     -31.849   0.929  44.705  1.00 38.06           C  
ATOM   2664  O   HIS A 790     -32.871   0.361  44.305  1.00 48.05           O  
ATOM   2665  CB  HIS A 790     -31.294   2.163  42.620  1.00 30.85           C  
ATOM   2666  CG  HIS A 790     -31.706   3.381  41.861  1.00 29.89           C  
ATOM   2667  ND1 HIS A 790     -33.013   3.622  41.495  1.00 32.89           N  
ATOM   2668  CD2 HIS A 790     -30.989   4.441  41.419  1.00 31.39           C  
ATOM   2669  CE1 HIS A 790     -33.081   4.773  40.851  1.00 38.20           C  
ATOM   2670  NE2 HIS A 790     -31.867   5.290  40.790  1.00 36.64           N  
ATOM   2671  N   ALA A 791     -31.043   0.387  45.615  1.00 40.38           N  
ATOM   2672  CA  ALA A 791     -31.383  -0.897  46.222  1.00 43.43           C  
ATOM   2673  C   ALA A 791     -32.735  -0.898  46.932  1.00 45.39           C  
ATOM   2674  O   ALA A 791     -33.434  -1.924  46.852  1.00 44.07           O  
ATOM   2675  CB  ALA A 791     -30.264  -1.331  47.178  1.00 40.83           C  
ATOM   2676  N   PRO A 792     -33.164   0.164  47.631  1.00 46.21           N  
ATOM   2677  CA  PRO A 792     -34.500   0.122  48.253  1.00 45.26           C  
ATOM   2678  C   PRO A 792     -35.639  -0.077  47.267  1.00 47.66           C  
ATOM   2679  O   PRO A 792     -36.690  -0.604  47.655  1.00 50.19           O  
ATOM   2680  CB  PRO A 792     -34.608   1.483  48.960  1.00 42.82           C  
ATOM   2681  CG  PRO A 792     -33.460   2.301  48.458  1.00 43.42           C  
ATOM   2682  CD  PRO A 792     -32.395   1.328  48.105  1.00 41.20           C  
ATOM   2683  N   PHE A 793     -35.470   0.319  46.005  1.00 44.23           N  
ATOM   2684  CA  PHE A 793     -36.551   0.235  45.031  1.00 42.23           C  
ATOM   2685  C   PHE A 793     -36.514  -1.023  44.177  1.00 40.57           C  
ATOM   2686  O   PHE A 793     -37.558  -1.422  43.649  1.00 42.07           O  
ATOM   2687  CB  PHE A 793     -36.530   1.459  44.107  1.00 41.68           C  
ATOM   2688  CG  PHE A 793     -36.423   2.762  44.838  1.00 39.88           C  
ATOM   2689  CD1 PHE A 793     -37.544   3.348  45.399  1.00 39.21           C  
ATOM   2690  CD2 PHE A 793     -35.200   3.399  44.969  1.00 44.84           C  
ATOM   2691  CE1 PHE A 793     -37.449   4.547  46.075  1.00 45.78           C  
ATOM   2692  CE2 PHE A 793     -35.098   4.599  45.646  1.00 39.73           C  
ATOM   2693  CZ  PHE A 793     -36.225   5.174  46.200  1.00 42.94           C  
ATOM   2694  N   TRP A 794     -35.353  -1.659  44.029  1.00 42.91           N  
ATOM   2695  CA  TRP A 794     -35.192  -2.798  43.130  1.00 42.74           C  
ATOM   2696  C   TRP A 794     -34.655  -3.987  43.915  1.00 44.01           C  
ATOM   2697  O   TRP A 794     -33.506  -3.970  44.371  1.00 44.61           O  
ATOM   2698  CB  TRP A 794     -34.273  -2.434  41.968  1.00 37.90           C  
ATOM   2699  CG  TRP A 794     -34.766  -1.238  41.222  1.00 39.99           C  
ATOM   2700  CD1 TRP A 794     -34.346   0.052  41.370  1.00 35.87           C  
ATOM   2701  CD2 TRP A 794     -35.794  -1.214  40.225  1.00 38.16           C  
ATOM   2702  NE1 TRP A 794     -35.042   0.876  40.520  1.00 29.13           N  
ATOM   2703  CE2 TRP A 794     -35.937   0.123  39.805  1.00 33.96           C  
ATOM   2704  CE3 TRP A 794     -36.604  -2.194  39.643  1.00 36.67           C  
ATOM   2705  CZ2 TRP A 794     -36.855   0.505  38.830  1.00 32.85           C  
ATOM   2706  CZ3 TRP A 794     -37.515  -1.813  38.675  1.00 39.60           C  
ATOM   2707  CH2 TRP A 794     -37.633  -0.475  38.278  1.00 31.94           C  
ATOM   2708  N   SER A 795     -35.489  -5.021  44.059  1.00 42.17           N  
ATOM   2709  CA  SER A 795     -35.095  -6.199  44.824  1.00 41.41           C  
ATOM   2710  C   SER A 795     -33.925  -6.928  44.176  1.00 42.76           C  
ATOM   2711  O   SER A 795     -33.063  -7.464  44.881  1.00 41.84           O  
ATOM   2712  CB  SER A 795     -36.288  -7.143  44.980  1.00 44.88           C  
ATOM   2713  OG  SER A 795     -36.628  -7.747  43.744  1.00 49.41           O  
ATOM   2714  N   SER A 796     -33.868  -6.951  42.843  1.00 42.97           N  
ATOM   2715  CA  SER A 796     -32.762  -7.593  42.141  1.00 45.09           C  
ATOM   2716  C   SER A 796     -31.419  -6.913  42.397  1.00 39.62           C  
ATOM   2717  O   SER A 796     -30.391  -7.419  41.934  1.00 46.19           O  
ATOM   2718  CB  SER A 796     -33.049  -7.629  40.640  1.00 43.42           C  
ATOM   2719  OG  SER A 796     -33.486  -6.367  40.172  1.00 45.33           O  
ATOM   2720  N   LEU A 797     -31.396  -5.788  43.109  1.00 36.47           N  
ATOM   2721  CA  LEU A 797     -30.151  -5.173  43.544  1.00 38.90           C  
ATOM   2722  C   LEU A 797     -29.773  -5.565  44.964  1.00 40.90           C  
ATOM   2723  O   LEU A 797     -28.656  -5.264  45.399  1.00 38.75           O  
ATOM   2724  CB  LEU A 797     -30.255  -3.647  43.450  1.00 40.29           C  
ATOM   2725  CG  LEU A 797     -30.421  -3.014  42.064  1.00 38.25           C  
ATOM   2726  CD1 LEU A 797     -30.155  -1.514  42.113  1.00 36.21           C  
ATOM   2727  CD2 LEU A 797     -29.518  -3.685  41.040  1.00 28.09           C  
ATOM   2728  N   ARG A 798     -30.673  -6.229  45.687  1.00 44.49           N  
ATOM   2729  CA  ARG A 798     -30.463  -6.568  47.090  1.00 44.90           C  
ATOM   2730  C   ARG A 798     -29.944  -7.990  47.279  1.00 57.34           C  
ATOM   2731  O   ARG A 798     -28.964  -8.208  47.989  1.00 61.26           O  
ATOM   2732  CB  ARG A 798     -31.762  -6.404  47.876  1.00 45.31           C  
ATOM   2733  CG  ARG A 798     -32.175  -4.973  48.134  1.00 47.47           C  
ATOM   2734  CD  ARG A 798     -33.516  -4.947  48.834  1.00 46.09           C  
ATOM   2735  NE  ARG A 798     -34.448  -4.030  48.193  1.00 53.82           N  
ATOM   2736  CZ  ARG A 798     -35.713  -4.332  47.928  1.00 55.29           C  
ATOM   2737  NH1 ARG A 798     -36.184  -5.531  48.244  1.00 49.63           N  
ATOM   2738  NH2 ARG A 798     -36.504  -3.442  47.342  1.00 50.66           N  
ATOM   2739  OXT ARG A 798     -30.500  -8.954  46.749  1.00 57.25           O  
TER    2740      ARG A 798                                                      
HETATM 2741  K     K A 801     -26.634   9.724  28.967  1.00 21.45           K  
HETATM 2742  K     K A 802     -39.010   7.939  35.338  1.00 43.09           K  
HETATM 2743 ZN    ZN A 803     -23.878  14.229  24.130  1.00 35.02          ZN  
HETATM 2744  C10 F1Y A 804     -23.489  19.130  23.749  1.00 44.42           C  
HETATM 2745  C13 F1Y A 804     -24.063  17.786  23.456  1.00 43.88           C  
HETATM 2746  C20 F1Y A 804     -17.673  23.054  27.660  1.00 57.29           C  
HETATM 2747  C21 F1Y A 804     -17.369  23.477  26.389  1.00 49.40           C  
HETATM 2748  C22 F1Y A 804     -18.430  23.534  25.408  1.00 54.61           C  
HETATM 2749  C01 F1Y A 804     -18.539  22.170  21.240  1.00 54.72           C  
HETATM 2750  C02 F1Y A 804     -19.468  23.362  20.944  1.00 56.55           C  
HETATM 2751  C03 F1Y A 804     -20.105  24.111  22.155  1.00 56.39           C  
HETATM 2752  C04 F1Y A 804     -19.696  23.779  23.600  1.00 57.09           C  
HETATM 2753  C05 F1Y A 804     -20.542  23.321  24.633  1.00 54.81           C  
HETATM 2754  C07 F1Y A 804     -22.415  21.744  24.326  1.00 47.95           C  
HETATM 2755  C08 F1Y A 804     -23.784  21.467  24.458  1.00 47.15           C  
HETATM 2756  C09 F1Y A 804     -24.294  20.189  24.173  1.00 46.18           C  
HETATM 2757  C11 F1Y A 804     -22.123  19.432  23.624  1.00 43.94           C  
HETATM 2758  C12 F1Y A 804     -21.599  20.694  23.901  1.00 45.64           C  
HETATM 2759  C18 F1Y A 804     -20.015  22.729  27.083  1.00 55.02           C  
HETATM 2760  C19 F1Y A 804     -18.989  22.681  28.007  1.00 54.99           C  
HETATM 2761  N06 F1Y A 804     -21.922  23.031  24.617  1.00 51.79           N  
HETATM 2762  N15 F1Y A 804     -23.330  16.740  22.832  1.00 46.35           N  
HETATM 2763  N17 F1Y A 804     -19.714  23.163  25.775  1.00 55.53           N  
HETATM 2764  N23 F1Y A 804     -18.386  23.920  24.084  1.00 55.30           N  
HETATM 2765  O14 F1Y A 804     -25.250  17.532  23.761  1.00 50.22           O  
HETATM 2766  O16 F1Y A 804     -23.981  15.552  22.618  1.00 48.29           O  
HETATM 2767  C1  EDO A 805     -20.886  26.848  27.150  1.00 54.48           C  
HETATM 2768  O1  EDO A 805     -19.606  26.554  26.579  1.00 53.64           O  
HETATM 2769  C2  EDO A 805     -21.863  25.733  26.803  1.00 51.11           C  
HETATM 2770  O2  EDO A 805     -23.192  26.265  26.739  1.00 51.07           O  
HETATM 2771  O   HOH A 901     -22.121   7.552  23.949  1.00 33.87           O  
HETATM 2772  O   HOH A 902     -38.385   8.937  38.074  1.00 40.24           O  
HETATM 2773  O   HOH A 903     -25.766  15.286  24.665  1.00 27.42           O  
HETATM 2774  O   HOH A 904     -36.941  27.076  11.875  1.00 44.21           O  
HETATM 2775  O   HOH A 905     -22.530   7.734  28.466  1.00 27.63           O  
HETATM 2776  O   HOH A 906     -16.904   7.119  37.879  1.00 33.99           O  
HETATM 2777  O   HOH A 907     -34.140  12.555  22.698  1.00 31.28           O  
HETATM 2778  O   HOH A 908     -30.113   7.808  40.363  1.00 30.46           O  
HETATM 2779  O   HOH A 909     -32.977  10.592  26.838  1.00 30.58           O  
HETATM 2780  O   HOH A 910     -29.311  30.986  16.381  1.00 42.91           O  
HETATM 2781  O   HOH A 911     -28.649  13.714  16.312  1.00 33.14           O  
HETATM 2782  O   HOH A 912     -15.621  10.229  23.913  1.00 36.52           O  
HETATM 2783  O   HOH A 913     -33.945  -7.185  19.088  1.00 33.89           O  
HETATM 2784  O   HOH A 914     -37.109  10.149  34.995  1.00 39.48           O  
CONECT 1307 2741                                                                
CONECT 1310 2741                                                                
CONECT 1329 2741                                                                
CONECT 1332 2743                                                                
CONECT 1333 2743                                                                
CONECT 1344 2741                                                                
CONECT 1347 2743                                                                
CONECT 1414 2742                                                                
CONECT 1443 2742                                                                
CONECT 1465 2742                                                                
CONECT 1502 2741                                                                
CONECT 1506 2741                                                                
CONECT 1720 2742                                                                
CONECT 2059 2743                                                                
CONECT 2741 1307 1310 1329 1344                                                 
CONECT 2741 1502 1506                                                           
CONECT 2742 1414 1443 1465 1720                                                 
CONECT 2742 2772 2784                                                           
CONECT 2743 1332 1333 1347 2059                                                 
CONECT 2743 2766 2773                                                           
CONECT 2744 2745 2756 2757                                                      
CONECT 2745 2744 2762 2765                                                      
CONECT 2746 2747 2760                                                           
CONECT 2747 2746 2748                                                           
CONECT 2748 2747 2763 2764                                                      
CONECT 2749 2750                                                                
CONECT 2750 2749 2751                                                           
CONECT 2751 2750 2752                                                           
CONECT 2752 2751 2753 2764                                                      
CONECT 2753 2752 2761 2763                                                      
CONECT 2754 2755 2758 2761                                                      
CONECT 2755 2754 2756                                                           
CONECT 2756 2744 2755                                                           
CONECT 2757 2744 2758                                                           
CONECT 2758 2754 2757                                                           
CONECT 2759 2760 2763                                                           
CONECT 2760 2746 2759                                                           
CONECT 2761 2753 2754                                                           
CONECT 2762 2745 2766                                                           
CONECT 2763 2748 2753 2759                                                      
CONECT 2764 2748 2752                                                           
CONECT 2765 2745                                                                
CONECT 2766 2743 2762                                                           
CONECT 2767 2768 2769                                                           
CONECT 2768 2767                                                                
CONECT 2769 2767 2770                                                           
CONECT 2770 2769                                                                
CONECT 2772 2742                                                                
CONECT 2773 2743                                                                
CONECT 2784 2742                                                                
MASTER      317    0    5   18    8    0   12    6 2783    1   50   28          
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: April 25th, 2023.