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Database: PDB
Entry: 2I4P
LinkDB: 2I4P
Original site: 2I4P 
HEADER    TRANSCRIPTION                           22-AUG-06   2I4P              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN PPARGAMMA AND THE            
TITLE    2 PARTIAL AGONIST LT127 (UREIDOFIBRATE DERIVATIVE).                    
TITLE    3 STRUCTURE OBTAINED FROM CRYSTALS OF THE APO-FORM SOAKED              
TITLE    4 FOR 30 DAYS.                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA;          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: LIGAND BINDING DOMAIN (LBD);                               
COMPND   5 SYNONYM: PPAR-GAMMA;                                                 
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PPARG;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    BUNDLE OF ALPHA-HELICES AND A SMALL FOUR-STRANDED BETA-               
KEYWDS   2 SHEET, TRANSCRIPTION                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.POCHETTI,F.MAZZA                                                    
REVDAT   3   24-FEB-09 2I4P    1       VERSN                                    
REVDAT   2   26-JUN-07 2I4P    1       JRNL                                     
REVDAT   1   17-APR-07 2I4P    0                                                
JRNL        AUTH   G.POCHETTI,C.GODIO,N.MITRO,D.CARUSO,A.GALMOZZI,              
JRNL        AUTH 2 S.SCURATI,F.LOIODICE,G.FRACCHIOLLA,P.TORTORELLA,             
JRNL        AUTH 3 A.LAGHEZZA,A.LAVECCHIA,E.NOVELLINO,F.MAZZA,                  
JRNL        AUTH 4 M.CRESTANI                                                   
JRNL        TITL   INSIGHTS INTO THE MECHANISM OF PARTIAL AGONISM:              
JRNL        TITL 2 CRYSTAL STRUCTURES OF THE PEROXISOME                         
JRNL        TITL 3 PROLIFERATOR-ACTIVATED RECEPTOR GAMMA                        
JRNL        TITL 4 LIGAND-BINDING DOMAIN IN THE COMPLEX WITH TWO                
JRNL        TITL 5 ENANTIOMERIC LIGANDS.                                        
JRNL        REF    J.BIOL.CHEM.                  V. 282 17314 2007              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17403688                                                     
JRNL        DOI    10.1074/JBC.M702316200                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.T.NOLTE,G.B.WISELY,S.WESTIN,J.E.COBB,M.H.LAMBERT,          
REMARK   1  AUTH 2 R.KUROKAWA,M.G.ROSENFELD,T.M.WILLSON,C.K.GLASS,              
REMARK   1  AUTH 3 M.V.MILBURN                                                  
REMARK   1  TITL   LIGAND BINDING AND CO-ACTIVATOR ASSEMBLY OF THE              
REMARK   1  TITL 2 PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR-GAMMA             
REMARK   1  REF    NATURE                        V. 395   137 1998              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  PMID   9744270                                                      
REMARK   1  DOI    10.1038/25931                                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.L.OBERFIELD,J.L.COLLINS,C.P.HOLMES,D.M.GOREHAM,            
REMARK   1  AUTH 2 J.P.COOPER,J.E.COBB,J.M.LENHARD,E.A.HULL-RYDE,               
REMARK   1  AUTH 3 C.P.MOHR,S.G.BLANCHARD,D.J.PARKS,L.B.MOORE,                  
REMARK   1  AUTH 4 J.M.LEHMANN,K.PLUNKET,A.B.MILLER,M.V.MILBURN,                
REMARK   1  AUTH 5 S.A.KLIEWER,T.M.WILLSON                                      
REMARK   1  TITL   A PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR                 
REMARK   1  TITL 2 LIGAND INHIBITS ADIPOCYTE DIFFERENTIATION                    
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  96  6102 1999              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1  PMID   10339548                                                     
REMARK   1  DOI    10.1073/PNAS.96.11.6102                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 35705                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.272                           
REMARK   3   FREE R VALUE                     : 0.295                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1777                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4332                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 113                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.85300                                              
REMARK   3    B22 (A**2) : -16.52600                                            
REMARK   3    B33 (A**2) : 13.67200                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.03600                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.360 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.167 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.071 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.966 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 98.34                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:DNA-RNA_REP.PARAM                   
REMARK   3  PARAMETER FILE  3  : CNS_TOPPAR:WATER_REP.PARAM                     
REMARK   3  PARAMETER FILE  4  : CNS_TOPPAR:ION.PARAM                           
REMARK   3  PARAMETER FILE  5  : LT127.PAR                                      
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : CNS_TOPPAR:PROTEIN.TOP                         
REMARK   3  TOPOLOGY FILE  2   : CNS_TOPPAR:DNA-RNA.TOP                         
REMARK   3  TOPOLOGY FILE  3   : CNS_TOPPAR:WATER.TOP                           
REMARK   3  TOPOLOGY FILE  4   : CNS_TOPPAR:ION.TOP                             
REMARK   3  TOPOLOGY FILE  5   : LT127.TOP                                      
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2I4P COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB039133.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-MAR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2                                
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200                                   (SI 111 AND SI 220)                
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36896                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.43300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M NACITRATE, 0.15 M TRIS, PH         
REMARK 280  8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       46.77000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.45500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       46.77000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       30.45500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     GLY A   191                                                      
REMARK 465     SER A   192                                                      
REMARK 465     HIS A   193                                                      
REMARK 465     MET A   194                                                      
REMARK 465     ALA A   195                                                      
REMARK 465     GLU A   196                                                      
REMARK 465     ILE A   197                                                      
REMARK 465     SER A   198                                                      
REMARK 465     SER A   199                                                      
REMARK 465     ASP A   200                                                      
REMARK 465     ILE A   201                                                      
REMARK 465     ASP A   202                                                      
REMARK 465     GLN A   203                                                      
REMARK 465     LEU A   204                                                      
REMARK 465     ASN A   205                                                      
REMARK 465     PRO A   206                                                      
REMARK 465     GLY B   191                                                      
REMARK 465     SER B   192                                                      
REMARK 465     HIS B   193                                                      
REMARK 465     MET B   194                                                      
REMARK 465     ALA B   195                                                      
REMARK 465     GLU B   196                                                      
REMARK 465     ILE B   197                                                      
REMARK 465     SER B   198                                                      
REMARK 465     SER B   199                                                      
REMARK 465     ASP B   200                                                      
REMARK 465     ILE B   201                                                      
REMARK 465     ASP B   202                                                      
REMARK 465     GLN B   203                                                      
REMARK 465     LEU B   204                                                      
REMARK 465     ASN B   205                                                      
REMARK 465     PRO B   206                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     ASP A  260                                                       
REMARK 475     PHE A  264                                                       
REMARK 475     HIS A  266                                                       
REMARK 475     LEU A  270                                                       
REMARK 475     GLN A  271                                                       
REMARK 475     GLU A  272                                                       
REMARK 475     GLN A  273                                                       
REMARK 475     SER A  274                                                       
REMARK 475     LYS B  261                                                       
REMARK 475     LYS B  265                                                       
REMARK 475     HIS B  266                                                       
REMARK 475     THR B  268                                                       
REMARK 475     GLN B  271                                                       
REMARK 475     GLU B  272                                                       
REMARK 475     GLN B  273                                                       
REMARK 475     SER B  274                                                       
REMARK 475     GLU B  276                                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ILE A  267   N     CA    C     O     CB    CG1   CG2             
REMARK 480     LEU A  476   OXT                                                 
REMARK 480     ASP B  260   CA    C     O     CB    CG    OD1   OD2             
REMARK 480     ILE B  262   CB    CG1   CG2                                     
REMARK 480     LYS B  263   CB    CG    CD    CE    NZ                          
REMARK 480     PHE B  264   CB    CG    CD1   CD2   CE1   CE2   CZ              
REMARK 480     ILE B  267   N     CA    C     O     CB    CG1   CG2             
REMARK 480     LEU B  476   OXT                                                 
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LEU A 476   C     LEU A 476   OXT     0.125                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 475   N   -  CA  -  C   ANGL. DEV. =  20.8 DEGREES          
REMARK 500    ASP A 475   C   -  N   -  CA  ANGL. DEV. =  20.3 DEGREES          
REMARK 500    LEU A 476   CA  -  C   -  O   ANGL. DEV. =  18.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 265       75.12   -105.45                                   
REMARK 500    HIS A 266     -142.45   -149.17                                   
REMARK 500    PRO A 269     -151.53    -56.46                                   
REMARK 500    SER A 274       81.23   -157.08                                   
REMARK 500    LYS A 275       82.69     50.40                                   
REMARK 500    GLU A 276      160.74    -43.96                                   
REMARK 500    SER A 342       72.20     42.10                                   
REMARK 500    GLU A 343       18.43     57.31                                   
REMARK 500    LYS A 358      -64.94    -10.12                                   
REMARK 500    LYS A 474       28.41    157.13                                   
REMARK 500    LEU B 237     -146.67    -63.98                                   
REMARK 500    THR B 238       94.84    -45.56                                   
REMARK 500    LYS B 240      -92.21    -66.05                                   
REMARK 500    THR B 242       95.18    -48.77                                   
REMARK 500    ASP B 243      145.78    173.29                                   
REMARK 500    LYS B 244       58.22     36.88                                   
REMARK 500    LYS B 263       88.47    -59.73                                   
REMARK 500    HIS B 266      -78.17   -165.88                                   
REMARK 500    PRO B 269       98.30    -61.76                                   
REMARK 500    GLU B 272       75.56   -168.26                                   
REMARK 500    SER B 274      113.91   -169.10                                   
REMARK 500    GLU B 276      156.01    -44.10                                   
REMARK 500    ARG B 357      168.59    -42.47                                   
REMARK 500    LEU B 393       50.72    -90.19                                   
REMARK 500    SER B 394      -94.21    -61.65                                   
REMARK 500    HIS B 425       59.11   -140.32                                   
REMARK 500    LYS B 458       32.20    -88.61                                   
REMARK 500    THR B 459      -43.87   -130.62                                   
REMARK 500    THR B 461      -69.04   -151.53                                   
REMARK 500    ASP B 462     -170.08    -51.59                                   
REMARK 500    MET B 463      128.26     77.16                                   
REMARK 500    SER B 464        7.92    -68.92                                   
REMARK 500    HIS B 466        4.91     89.53                                   
REMARK 500    LEU B 468      -31.24     71.30                                   
REMARK 500    LYS B 474      -85.24     67.82                                   
REMARK 500    ASP B 475      -20.45   -150.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DRH A 999                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1PRG   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN THE APO-FORM                                     
REMARK 900 RELATED ID: 2PRG   RELATED DB: PDB                                   
REMARK 900 THE TERNARY COMPLEX OF THE SAME PROTEIN WITH ROSIGLITAZONE           
REMARK 900 AND THE COACTIVATOR PEPTIDE SRC-1                                    
REMARK 900 RELATED ID: 4PRG   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH THE PARTIAL AGONIST GW0072           
DBREF  2I4P A  195   476  UNP    P37231   PPARG_HUMAN    223    504             
DBREF  2I4P B  195   476  UNP    P37231   PPARG_HUMAN    223    504             
SEQADV 2I4P GLY A  191  UNP  P37231              CLONING ARTIFACT               
SEQADV 2I4P SER A  192  UNP  P37231              CLONING ARTIFACT               
SEQADV 2I4P HIS A  193  UNP  P37231              CLONING ARTIFACT               
SEQADV 2I4P MET A  194  UNP  P37231              CLONING ARTIFACT               
SEQADV 2I4P GLY B  191  UNP  P37231              CLONING ARTIFACT               
SEQADV 2I4P SER B  192  UNP  P37231              CLONING ARTIFACT               
SEQADV 2I4P HIS B  193  UNP  P37231              CLONING ARTIFACT               
SEQADV 2I4P MET B  194  UNP  P37231              CLONING ARTIFACT               
SEQRES   1 A  286  GLY SER HIS MET ALA GLU ILE SER SER ASP ILE ASP GLN          
SEQRES   2 A  286  LEU ASN PRO GLU SER ALA ASP LEU ARG ALA LEU ALA LYS          
SEQRES   3 A  286  HIS LEU TYR ASP SER TYR ILE LYS SER PHE PRO LEU THR          
SEQRES   4 A  286  LYS ALA LYS ALA ARG ALA ILE LEU THR GLY LYS THR THR          
SEQRES   5 A  286  ASP LYS SER PRO PHE VAL ILE TYR ASP MET ASN SER LEU          
SEQRES   6 A  286  MET MET GLY GLU ASP LYS ILE LYS PHE LYS HIS ILE THR          
SEQRES   7 A  286  PRO LEU GLN GLU GLN SER LYS GLU VAL ALA ILE ARG ILE          
SEQRES   8 A  286  PHE GLN GLY CYS GLN PHE ARG SER VAL GLU ALA VAL GLN          
SEQRES   9 A  286  GLU ILE THR GLU TYR ALA LYS SER ILE PRO GLY PHE VAL          
SEQRES  10 A  286  ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS TYR          
SEQRES  11 A  286  GLY VAL HIS GLU ILE ILE TYR THR MET LEU ALA SER LEU          
SEQRES  12 A  286  MET ASN LYS ASP GLY VAL LEU ILE SER GLU GLY GLN GLY          
SEQRES  13 A  286  PHE MET THR ARG GLU PHE LEU LYS SER LEU ARG LYS PRO          
SEQRES  14 A  286  PHE GLY ASP PHE MET GLU PRO LYS PHE GLU PHE ALA VAL          
SEQRES  15 A  286  LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP LEU ALA          
SEQRES  16 A  286  ILE PHE ILE ALA VAL ILE ILE LEU SER GLY ASP ARG PRO          
SEQRES  17 A  286  GLY LEU LEU ASN VAL LYS PRO ILE GLU ASP ILE GLN ASP          
SEQRES  18 A  286  ASN LEU LEU GLN ALA LEU GLU LEU GLN LEU LYS LEU ASN          
SEQRES  19 A  286  HIS PRO GLU SER SER GLN LEU PHE ALA LYS LEU LEU GLN          
SEQRES  20 A  286  LYS MET THR ASP LEU ARG GLN ILE VAL THR GLU HIS VAL          
SEQRES  21 A  286  GLN LEU LEU GLN VAL ILE LYS LYS THR GLU THR ASP MET          
SEQRES  22 A  286  SER LEU HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP LEU          
SEQRES   1 B  286  GLY SER HIS MET ALA GLU ILE SER SER ASP ILE ASP GLN          
SEQRES   2 B  286  LEU ASN PRO GLU SER ALA ASP LEU ARG ALA LEU ALA LYS          
SEQRES   3 B  286  HIS LEU TYR ASP SER TYR ILE LYS SER PHE PRO LEU THR          
SEQRES   4 B  286  LYS ALA LYS ALA ARG ALA ILE LEU THR GLY LYS THR THR          
SEQRES   5 B  286  ASP LYS SER PRO PHE VAL ILE TYR ASP MET ASN SER LEU          
SEQRES   6 B  286  MET MET GLY GLU ASP LYS ILE LYS PHE LYS HIS ILE THR          
SEQRES   7 B  286  PRO LEU GLN GLU GLN SER LYS GLU VAL ALA ILE ARG ILE          
SEQRES   8 B  286  PHE GLN GLY CYS GLN PHE ARG SER VAL GLU ALA VAL GLN          
SEQRES   9 B  286  GLU ILE THR GLU TYR ALA LYS SER ILE PRO GLY PHE VAL          
SEQRES  10 B  286  ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS TYR          
SEQRES  11 B  286  GLY VAL HIS GLU ILE ILE TYR THR MET LEU ALA SER LEU          
SEQRES  12 B  286  MET ASN LYS ASP GLY VAL LEU ILE SER GLU GLY GLN GLY          
SEQRES  13 B  286  PHE MET THR ARG GLU PHE LEU LYS SER LEU ARG LYS PRO          
SEQRES  14 B  286  PHE GLY ASP PHE MET GLU PRO LYS PHE GLU PHE ALA VAL          
SEQRES  15 B  286  LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP LEU ALA          
SEQRES  16 B  286  ILE PHE ILE ALA VAL ILE ILE LEU SER GLY ASP ARG PRO          
SEQRES  17 B  286  GLY LEU LEU ASN VAL LYS PRO ILE GLU ASP ILE GLN ASP          
SEQRES  18 B  286  ASN LEU LEU GLN ALA LEU GLU LEU GLN LEU LYS LEU ASN          
SEQRES  19 B  286  HIS PRO GLU SER SER GLN LEU PHE ALA LYS LEU LEU GLN          
SEQRES  20 B  286  LYS MET THR ASP LEU ARG GLN ILE VAL THR GLU HIS VAL          
SEQRES  21 B  286  GLN LEU LEU GLN VAL ILE LYS LYS THR GLU THR ASP MET          
SEQRES  22 B  286  SER LEU HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP LEU          
HET    DRH  A 999      33                                                       
HETNAM     DRH (2S)-2-(4-{2-[1,3-BENZOXAZOL-2-YL(HEPTYL)                        
HETNAM   2 DRH  AMINO]ETHYL}PHENOXY)-2-METHYLBUTANOIC ACID                      
FORMUL   3  DRH    C27 H36 N2 O4                                                
FORMUL   4  HOH   *113(H2 O)                                                    
HELIX    1   1 GLU A  207  PHE A  226  1                                  20    
HELIX    2   2 THR A  229  THR A  238  1                                  10    
HELIX    3   3 ASP A  251  ILE A  262  1                                  12    
HELIX    4   4 GLU A  276  ILE A  303  1                                  28    
HELIX    5   5 GLY A  305  LEU A  309  5                                   5    
HELIX    6   6 ASP A  310  ALA A  331  1                                  22    
HELIX    7   7 SER A  342  GLY A  344  5                                   3    
HELIX    8   8 ARG A  350  SER A  355  1                                   6    
HELIX    9   9 PRO A  359  PHE A  363  5                                   5    
HELIX   10  10 MET A  364  ALA A  376  1                                  13    
HELIX   11  11 ASP A  380  LEU A  393  1                                  14    
HELIX   12  12 ASN A  402  HIS A  425  1                                  24    
HELIX   13  13 GLN A  430  GLU A  460  1                                  31    
HELIX   14  14 HIS A  466  TYR A  473  1                                   8    
HELIX   15  15 GLU B  207  PHE B  226  1                                  20    
HELIX   16  16 THR B  229  LEU B  237  1                                   9    
HELIX   17  17 ASP B  251  LYS B  261  1                                  11    
HELIX   18  18 GLU B  276  SER B  302  1                                  27    
HELIX   19  19 ASP B  310  ALA B  331  1                                  22    
HELIX   20  20 ARG B  350  LEU B  356  1                                   7    
HELIX   21  21 ARG B  357  ASP B  362  1                                   6    
HELIX   22  22 MET B  364  ALA B  376  1                                  13    
HELIX   23  23 ASP B  380  LEU B  393  1                                  14    
HELIX   24  24 ASN B  402  HIS B  425  1                                  24    
HELIX   25  25 GLN B  430  LYS B  438  1                                   9    
HELIX   26  26 LYS B  438  LYS B  458  1                                  21    
HELIX   27  27 LEU B  468  LYS B  474  1                                   7    
SHEET    1   A 4 PHE A 247  ILE A 249  0                                        
SHEET    2   A 4 GLY A 346  THR A 349  1  O  PHE A 347   N  ILE A 249           
SHEET    3   A 4 GLY A 338  ILE A 341 -1  N  VAL A 339   O  MET A 348           
SHEET    4   A 4 MET A 334  ASN A 335 -1  N  ASN A 335   O  GLY A 338           
SHEET    1   B 4 PHE B 247  ILE B 249  0                                        
SHEET    2   B 4 GLY B 346  THR B 349  1  O  PHE B 347   N  ILE B 249           
SHEET    3   B 4 GLY B 338  ILE B 341 -1  N  VAL B 339   O  MET B 348           
SHEET    4   B 4 MET B 334  ASN B 335 -1  N  ASN B 335   O  GLY B 338           
SITE     1 AC1 17 HOH A   1  HOH A  18  HOH A 116  PHE A 226                    
SITE     2 AC1 17 PHE A 282  CYS A 285  GLN A 286  ARG A 288                    
SITE     3 AC1 17 SER A 289  ALA A 292  ILE A 296  HIS A 323                    
SITE     4 AC1 17 ILE A 326  MET A 329  LEU A 330  HIS A 449                    
SITE     5 AC1 17 TYR A 473                                                     
CRYST1   93.540   60.910  118.350  90.00 103.08  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010691  0.000000  0.002484        0.00000                         
SCALE2      0.000000  0.016418  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008675        0.00000                         
ATOM      1  N   GLU A 207      -6.382 -10.976  27.899  1.00 56.40           N  
ATOM      2  CA  GLU A 207      -7.198 -10.926  26.649  1.00 54.86           C  
ATOM      3  C   GLU A 207      -6.487 -10.141  25.543  1.00 53.24           C  
ATOM      4  O   GLU A 207      -6.214  -8.950  25.685  1.00 53.51           O  
ATOM      5  CB  GLU A 207      -8.557 -10.283  26.950  1.00 55.54           C  
ATOM      6  CG  GLU A 207      -9.501 -10.198  25.762  1.00 57.42           C  
ATOM      7  CD  GLU A 207      -9.921 -11.565  25.238  1.00 59.55           C  
ATOM      8  OE1 GLU A 207      -9.601 -11.882  24.067  1.00 59.91           O  
ATOM      9  OE2 GLU A 207     -10.575 -12.318  25.995  1.00 60.06           O  
ATOM     10  N   SER A 208      -6.194 -10.815  24.440  1.00 52.15           N  
ATOM     11  CA  SER A 208      -5.527 -10.178  23.313  1.00 52.23           C  
ATOM     12  C   SER A 208      -6.419  -9.086  22.725  1.00 50.50           C  
ATOM     13  O   SER A 208      -5.955  -8.213  21.990  1.00 50.74           O  
ATOM     14  CB  SER A 208      -5.222 -11.214  22.232  1.00 53.53           C  
ATOM     15  OG  SER A 208      -6.421 -11.661  21.628  1.00 55.31           O  
ATOM     16  N   ALA A 209      -7.705  -9.152  23.041  1.00 49.00           N  
ATOM     17  CA  ALA A 209      -8.655  -8.171  22.552  1.00 48.33           C  
ATOM     18  C   ALA A 209      -8.341  -6.826  23.193  1.00 46.75           C  
ATOM     19  O   ALA A 209      -8.427  -5.790  22.543  1.00 46.83           O  
ATOM     20  CB  ALA A 209     -10.099  -8.605  22.888  1.00 47.67           C  
ATOM     21  N   ASP A 210      -7.965  -6.838  24.466  1.00 45.74           N  
ATOM     22  CA  ASP A 210      -7.650  -5.585  25.135  1.00 46.30           C  
ATOM     23  C   ASP A 210      -6.344  -5.010  24.622  1.00 45.88           C  
ATOM     24  O   ASP A 210      -6.195  -3.793  24.533  1.00 46.13           O  
ATOM     25  CB  ASP A 210      -7.567  -5.773  26.650  1.00 47.61           C  
ATOM     26  CG  ASP A 210      -8.927  -5.725  27.318  1.00 49.16           C  
ATOM     27  OD1 ASP A 210      -9.743  -4.861  26.930  1.00 49.08           O  
ATOM     28  OD2 ASP A 210      -9.176  -6.536  28.237  1.00 50.13           O  
ATOM     29  N   LEU A 211      -5.403  -5.890  24.279  1.00 45.69           N  
ATOM     30  CA  LEU A 211      -4.093  -5.473  23.765  1.00 45.61           C  
ATOM     31  C   LEU A 211      -4.205  -4.865  22.365  1.00 44.41           C  
ATOM     32  O   LEU A 211      -3.427  -3.980  21.997  1.00 44.41           O  
ATOM     33  CB  LEU A 211      -3.124  -6.664  23.728  1.00 42.53           C  
ATOM     34  CG  LEU A 211      -2.729  -7.284  25.074  1.00 42.56           C  
ATOM     35  CD1 LEU A 211      -1.954  -8.577  24.835  1.00 39.31           C  
ATOM     36  CD2 LEU A 211      -1.906  -6.291  25.886  1.00 39.28           C  
ATOM     37  N   ARG A 212      -5.165  -5.352  21.586  1.00 43.14           N  
ATOM     38  CA  ARG A 212      -5.378  -4.844  20.234  1.00 43.80           C  
ATOM     39  C   ARG A 212      -6.030  -3.468  20.312  1.00 42.83           C  
ATOM     40  O   ARG A 212      -5.751  -2.592  19.498  1.00 43.20           O  
ATOM     41  CB  ARG A 212      -6.270  -5.801  19.435  1.00 44.36           C  
ATOM     42  CG  ARG A 212      -5.636  -7.161  19.203  1.00 47.75           C  
ATOM     43  CD  ARG A 212      -4.263  -7.000  18.569  1.00 50.53           C  
ATOM     44  NE  ARG A 212      -4.330  -6.514  17.191  1.00 51.27           N  
ATOM     45  CZ  ARG A 212      -3.311  -5.940  16.559  1.00 53.21           C  
ATOM     46  NH1 ARG A 212      -2.154  -5.773  17.184  1.00 53.53           N  
ATOM     47  NH2 ARG A 212      -3.440  -5.547  15.298  1.00 53.12           N  
ATOM     48  N   ALA A 213      -6.898  -3.292  21.302  1.00 43.15           N  
ATOM     49  CA  ALA A 213      -7.583  -2.026  21.511  1.00 42.66           C  
ATOM     50  C   ALA A 213      -6.557  -0.973  21.932  1.00 43.12           C  
ATOM     51  O   ALA A 213      -6.627   0.179  21.505  1.00 42.52           O  
ATOM     52  CB  ALA A 213      -8.659  -2.189  22.588  1.00 43.37           C  
ATOM     53  N   LEU A 214      -5.597  -1.383  22.765  1.00 41.82           N  
ATOM     54  CA  LEU A 214      -4.544  -0.486  23.232  1.00 39.16           C  
ATOM     55  C   LEU A 214      -3.680  -0.068  22.035  1.00 36.78           C  
ATOM     56  O   LEU A 214      -3.278   1.093  21.913  1.00 32.98           O  
ATOM     57  CB  LEU A 214      -3.682  -1.189  24.293  1.00 37.89           C  
ATOM     58  CG  LEU A 214      -2.462  -0.427  24.814  1.00 38.34           C  
ATOM     59  CD1 LEU A 214      -2.896   0.900  25.454  1.00 33.95           C  
ATOM     60  CD2 LEU A 214      -1.733  -1.297  25.834  1.00 39.47           C  
ATOM     61  N   ALA A 215      -3.406  -1.023  21.154  1.00 35.65           N  
ATOM     62  CA  ALA A 215      -2.618  -0.765  19.948  1.00 37.73           C  
ATOM     63  C   ALA A 215      -3.320   0.257  19.035  1.00 37.36           C  
ATOM     64  O   ALA A 215      -2.689   1.180  18.523  1.00 38.59           O  
ATOM     65  CB  ALA A 215      -2.388  -2.060  19.186  1.00 33.55           C  
ATOM     66  N   LYS A 216      -4.621   0.088  18.828  1.00 38.34           N  
ATOM     67  CA  LYS A 216      -5.366   1.025  17.982  1.00 38.81           C  
ATOM     68  C   LYS A 216      -5.320   2.416  18.602  1.00 36.01           C  
ATOM     69  O   LYS A 216      -5.048   3.400  17.922  1.00 34.86           O  
ATOM     70  CB  LYS A 216      -6.833   0.602  17.844  1.00 42.38           C  
ATOM     71  CG  LYS A 216      -7.160  -0.254  16.629  1.00 46.41           C  
ATOM     72  CD  LYS A 216      -6.606  -1.661  16.749  1.00 49.05           C  
ATOM     73  CE  LYS A 216      -7.127  -2.537  15.613  1.00 51.88           C  
ATOM     74  NZ  LYS A 216      -6.957  -4.008  15.869  1.00 53.18           N  
ATOM     75  N   HIS A 217      -5.598   2.478  19.899  1.00 35.36           N  
ATOM     76  CA  HIS A 217      -5.600   3.732  20.633  1.00 36.84           C  
ATOM     77  C   HIS A 217      -4.286   4.500  20.487  1.00 36.60           C  
ATOM     78  O   HIS A 217      -4.288   5.700  20.187  1.00 38.12           O  
ATOM     79  CB  HIS A 217      -5.888   3.471  22.118  1.00 39.83           C  
ATOM     80  CG  HIS A 217      -5.551   4.629  23.007  1.00 41.41           C  
ATOM     81  ND1 HIS A 217      -6.269   5.806  23.005  1.00 43.19           N  
ATOM     82  CD2 HIS A 217      -4.528   4.815  23.872  1.00 41.99           C  
ATOM     83  CE1 HIS A 217      -5.699   6.669  23.827  1.00 43.51           C  
ATOM     84  NE2 HIS A 217      -4.639   6.093  24.365  1.00 43.31           N  
ATOM     85  N   LEU A 218      -3.169   3.815  20.713  1.00 35.00           N  
ATOM     86  CA  LEU A 218      -1.854   4.437  20.598  1.00 34.42           C  
ATOM     87  C   LEU A 218      -1.565   4.817  19.136  1.00 33.07           C  
ATOM     88  O   LEU A 218      -0.985   5.873  18.865  1.00 30.69           O  
ATOM     89  CB  LEU A 218      -0.770   3.484  21.131  1.00 35.51           C  
ATOM     90  CG  LEU A 218      -0.824   3.109  22.622  1.00 36.18           C  
ATOM     91  CD1 LEU A 218       0.192   2.006  22.904  1.00 35.48           C  
ATOM     92  CD2 LEU A 218      -0.519   4.328  23.485  1.00 34.99           C  
ATOM     93  N   TYR A 219      -1.957   3.966  18.189  1.00 32.95           N  
ATOM     94  CA  TYR A 219      -1.734   4.296  16.774  1.00 34.80           C  
ATOM     95  C   TYR A 219      -2.521   5.561  16.386  1.00 35.62           C  
ATOM     96  O   TYR A 219      -2.021   6.425  15.651  1.00 37.04           O  
ATOM     97  CB  TYR A 219      -2.156   3.134  15.865  1.00 34.53           C  
ATOM     98  CG  TYR A 219      -1.962   3.423  14.388  1.00 37.63           C  
ATOM     99  CD1 TYR A 219      -0.787   4.017  13.917  1.00 40.01           C  
ATOM    100  CD2 TYR A 219      -2.964   3.139  13.468  1.00 39.14           C  
ATOM    101  CE1 TYR A 219      -0.622   4.332  12.558  1.00 41.87           C  
ATOM    102  CE2 TYR A 219      -2.813   3.446  12.107  1.00 42.90           C  
ATOM    103  CZ  TYR A 219      -1.644   4.044  11.661  1.00 43.84           C  
ATOM    104  OH  TYR A 219      -1.515   4.380  10.330  1.00 44.62           O  
ATOM    105  N   ASP A 220      -3.750   5.650  16.897  1.00 34.60           N  
ATOM    106  CA  ASP A 220      -4.662   6.774  16.657  1.00 35.67           C  
ATOM    107  C   ASP A 220      -4.075   8.091  17.171  1.00 35.64           C  
ATOM    108  O   ASP A 220      -4.146   9.117  16.490  1.00 35.74           O  
ATOM    109  CB  ASP A 220      -6.000   6.489  17.361  1.00 33.61           C  
ATOM    110  CG  ASP A 220      -7.051   7.557  17.106  1.00 36.70           C  
ATOM    111  OD1 ASP A 220      -7.404   7.772  15.928  1.00 34.54           O  
ATOM    112  OD2 ASP A 220      -7.537   8.175  18.086  1.00 36.63           O  
ATOM    113  N   SER A 221      -3.478   8.047  18.365  1.00 35.32           N  
ATOM    114  CA  SER A 221      -2.897   9.232  18.993  1.00 32.52           C  
ATOM    115  C   SER A 221      -1.609   9.632  18.345  1.00 30.90           C  
ATOM    116  O   SER A 221      -1.203  10.797  18.380  1.00 31.14           O  
ATOM    117  CB  SER A 221      -2.622   8.974  20.471  1.00 32.59           C  
ATOM    118  OG  SER A 221      -3.640   8.177  21.024  1.00 37.26           O  
ATOM    119  N   TYR A 222      -0.927   8.636  17.807  1.00 29.93           N  
ATOM    120  CA  TYR A 222       0.332   8.855  17.125  1.00 30.67           C  
ATOM    121  C   TYR A 222       0.018   9.623  15.829  1.00 31.30           C  
ATOM    122  O   TYR A 222       0.695  10.599  15.495  1.00 30.76           O  
ATOM    123  CB  TYR A 222       0.947   7.492  16.826  1.00 29.00           C  
ATOM    124  CG  TYR A 222       2.127   7.470  15.908  1.00 28.72           C  
ATOM    125  CD1 TYR A 222       3.428   7.502  16.410  1.00 29.42           C  
ATOM    126  CD2 TYR A 222       1.952   7.312  14.533  1.00 28.54           C  
ATOM    127  CE1 TYR A 222       4.523   7.361  15.567  1.00 26.13           C  
ATOM    128  CE2 TYR A 222       3.042   7.176  13.684  1.00 30.70           C  
ATOM    129  CZ  TYR A 222       4.321   7.198  14.209  1.00 27.70           C  
ATOM    130  OH  TYR A 222       5.399   7.042  13.363  1.00 32.87           O  
ATOM    131  N   ILE A 223      -1.002   9.178  15.102  1.00 31.86           N  
ATOM    132  CA  ILE A 223      -1.385   9.859  13.869  1.00 35.43           C  
ATOM    133  C   ILE A 223      -1.772  11.288  14.202  1.00 35.92           C  
ATOM    134  O   ILE A 223      -1.389  12.213  13.506  1.00 36.10           O  
ATOM    135  CB  ILE A 223      -2.610   9.201  13.164  1.00 36.75           C  
ATOM    136  CG1 ILE A 223      -2.251   7.804  12.666  1.00 38.64           C  
ATOM    137  CG2 ILE A 223      -3.068  10.070  11.974  1.00 38.74           C  
ATOM    138  CD1 ILE A 223      -0.983   7.752  11.854  1.00 40.67           C  
ATOM    139  N   LYS A 224      -2.521  11.464  15.284  1.00 36.56           N  
ATOM    140  CA  LYS A 224      -2.968  12.789  15.669  1.00 36.89           C  
ATOM    141  C   LYS A 224      -1.868  13.679  16.239  1.00 38.48           C  
ATOM    142  O   LYS A 224      -1.973  14.903  16.210  1.00 39.44           O  
ATOM    143  CB  LYS A 224      -4.123  12.648  16.662  1.00 35.37           C  
ATOM    144  CG  LYS A 224      -5.343  11.953  16.059  1.00 33.06           C  
ATOM    145  CD  LYS A 224      -6.393  11.621  17.113  1.00 31.31           C  
ATOM    146  CE  LYS A 224      -7.604  10.955  16.483  1.00 32.48           C  
ATOM    147  NZ  LYS A 224      -8.647  10.584  17.467  1.00 32.27           N  
ATOM    148  N   SER A 225      -0.795  13.071  16.732  1.00 39.78           N  
ATOM    149  CA  SER A 225       0.298  13.832  17.330  1.00 37.52           C  
ATOM    150  C   SER A 225       1.458  14.211  16.424  1.00 37.40           C  
ATOM    151  O   SER A 225       2.073  15.258  16.615  1.00 37.47           O  
ATOM    152  CB  SER A 225       0.855  13.074  18.545  1.00 38.11           C  
ATOM    153  OG  SER A 225      -0.087  13.045  19.601  1.00 36.22           O  
ATOM    154  N   PHE A 226       1.780  13.366  15.451  1.00 38.60           N  
ATOM    155  CA  PHE A 226       2.912  13.640  14.565  1.00 38.98           C  
ATOM    156  C   PHE A 226       2.472  13.870  13.113  1.00 40.34           C  
ATOM    157  O   PHE A 226       2.009  12.949  12.443  1.00 42.63           O  
ATOM    158  CB  PHE A 226       3.919  12.478  14.636  1.00 36.31           C  
ATOM    159  CG  PHE A 226       4.312  12.095  16.049  1.00 35.00           C  
ATOM    160  CD1 PHE A 226       5.104  12.937  16.823  1.00 35.91           C  
ATOM    161  CD2 PHE A 226       3.867  10.900  16.610  1.00 36.54           C  
ATOM    162  CE1 PHE A 226       5.449  12.596  18.141  1.00 35.21           C  
ATOM    163  CE2 PHE A 226       4.202  10.546  17.924  1.00 33.42           C  
ATOM    164  CZ  PHE A 226       4.993  11.395  18.690  1.00 33.43           C  
ATOM    165  N   PRO A 227       2.634  15.108  12.612  1.00 40.95           N  
ATOM    166  CA  PRO A 227       2.286  15.568  11.261  1.00 41.71           C  
ATOM    167  C   PRO A 227       2.897  14.775  10.114  1.00 39.17           C  
ATOM    168  O   PRO A 227       2.258  14.584   9.088  1.00 41.16           O  
ATOM    169  CB  PRO A 227       2.766  17.019  11.255  1.00 42.24           C  
ATOM    170  CG  PRO A 227       2.570  17.430  12.682  1.00 43.77           C  
ATOM    171  CD  PRO A 227       3.156  16.232  13.408  1.00 43.76           C  
ATOM    172  N   LEU A 228       4.138  14.330  10.265  1.00 37.11           N  
ATOM    173  CA  LEU A 228       4.758  13.560   9.196  1.00 34.32           C  
ATOM    174  C   LEU A 228       4.962  12.114   9.643  1.00 34.87           C  
ATOM    175  O   LEU A 228       5.844  11.828  10.462  1.00 34.23           O  
ATOM    176  CB  LEU A 228       6.087  14.189   8.797  1.00 33.07           C  
ATOM    177  CG  LEU A 228       6.817  13.506   7.637  1.00 37.61           C  
ATOM    178  CD1 LEU A 228       5.964  13.532   6.382  1.00 35.79           C  
ATOM    179  CD2 LEU A 228       8.147  14.206   7.386  1.00 36.08           C  
ATOM    180  N   THR A 229       4.133  11.210   9.126  1.00 30.01           N  
ATOM    181  CA  THR A 229       4.234   9.798   9.489  1.00 29.59           C  
ATOM    182  C   THR A 229       5.278   9.111   8.598  1.00 29.56           C  
ATOM    183  O   THR A 229       5.753   9.684   7.610  1.00 28.32           O  
ATOM    184  CB  THR A 229       2.897   9.063   9.278  1.00 27.49           C  
ATOM    185  OG1 THR A 229       2.589   9.066   7.882  1.00 27.58           O  
ATOM    186  CG2 THR A 229       1.777   9.742  10.014  1.00 29.05           C  
ATOM    187  N   LYS A 230       5.642   7.880   8.940  1.00 30.37           N  
ATOM    188  CA  LYS A 230       6.600   7.154   8.104  1.00 29.05           C  
ATOM    189  C   LYS A 230       5.935   6.833   6.761  1.00 27.22           C  
ATOM    190  O   LYS A 230       6.587   6.859   5.718  1.00 27.64           O  
ATOM    191  CB  LYS A 230       7.047   5.851   8.774  1.00 30.28           C  
ATOM    192  CG  LYS A 230       8.145   5.118   7.984  1.00 34.18           C  
ATOM    193  CD  LYS A 230       8.611   3.859   8.697  1.00 33.98           C  
ATOM    194  CE  LYS A 230       9.871   3.290   8.051  1.00 37.18           C  
ATOM    195  NZ  LYS A 230      10.311   2.017   8.712  1.00 35.75           N  
ATOM    196  N   ALA A 231       4.634   6.545   6.782  1.00 29.52           N  
ATOM    197  CA  ALA A 231       3.901   6.227   5.543  1.00 30.75           C  
ATOM    198  C   ALA A 231       4.039   7.362   4.515  1.00 30.49           C  
ATOM    199  O   ALA A 231       4.296   7.119   3.336  1.00 33.00           O  
ATOM    200  CB  ALA A 231       2.428   5.979   5.853  1.00 30.58           C  
ATOM    201  N   LYS A 232       3.870   8.599   4.969  1.00 30.41           N  
ATOM    202  CA  LYS A 232       4.013   9.761   4.101  1.00 31.55           C  
ATOM    203  C   LYS A 232       5.479   9.987   3.756  1.00 30.85           C  
ATOM    204  O   LYS A 232       5.817  10.300   2.620  1.00 30.19           O  
ATOM    205  CB  LYS A 232       3.423  11.008   4.781  1.00 31.87           C  
ATOM    206  CG  LYS A 232       3.565  12.300   3.980  1.00 33.36           C  
ATOM    207  CD  LYS A 232       2.768  13.426   4.642  1.00 39.79           C  
ATOM    208  CE  LYS A 232       2.968  14.770   3.955  1.00 38.12           C  
ATOM    209  NZ  LYS A 232       2.614  14.693   2.519  1.00 46.46           N  
ATOM    210  N   ALA A 233       6.365   9.810   4.730  1.00 32.45           N  
ATOM    211  CA  ALA A 233       7.791   9.983   4.472  1.00 32.71           C  
ATOM    212  C   ALA A 233       8.267   9.007   3.380  1.00 33.90           C  
ATOM    213  O   ALA A 233       8.985   9.394   2.444  1.00 33.44           O  
ATOM    214  CB  ALA A 233       8.603   9.769   5.774  1.00 33.65           C  
ATOM    215  N   ARG A 234       7.870   7.743   3.487  1.00 33.21           N  
ATOM    216  CA  ARG A 234       8.292   6.770   2.493  1.00 34.38           C  
ATOM    217  C   ARG A 234       7.654   7.081   1.142  1.00 34.46           C  
ATOM    218  O   ARG A 234       8.279   6.900   0.106  1.00 35.89           O  
ATOM    219  CB  ARG A 234       7.932   5.329   2.918  1.00 36.02           C  
ATOM    220  CG  ARG A 234       8.349   4.891   4.347  1.00 38.69           C  
ATOM    221  CD  ARG A 234       9.754   5.351   4.812  1.00 40.08           C  
ATOM    222  NE  ARG A 234      10.821   5.086   3.851  1.00 41.36           N  
ATOM    223  CZ  ARG A 234      12.120   5.307   4.074  1.00 42.63           C  
ATOM    224  NH1 ARG A 234      12.545   5.796   5.240  1.00 34.94           N  
ATOM    225  NH2 ARG A 234      13.003   5.056   3.109  1.00 43.99           N  
ATOM    226  N   ALA A 235       6.409   7.551   1.140  1.00 35.74           N  
ATOM    227  CA  ALA A 235       5.760   7.857  -0.127  1.00 34.73           C  
ATOM    228  C   ALA A 235       6.534   8.968  -0.837  1.00 36.34           C  
ATOM    229  O   ALA A 235       6.687   8.954  -2.064  1.00 36.96           O  
ATOM    230  CB  ALA A 235       4.312   8.272   0.102  1.00 34.40           C  
ATOM    231  N   ILE A 236       7.033   9.925  -0.061  1.00 35.62           N  
ATOM    232  CA  ILE A 236       7.802  11.037  -0.614  1.00 36.33           C  
ATOM    233  C   ILE A 236       9.186  10.572  -1.093  1.00 38.13           C  
ATOM    234  O   ILE A 236       9.639  10.938  -2.185  1.00 38.23           O  
ATOM    235  CB  ILE A 236       7.957  12.169   0.446  1.00 35.25           C  
ATOM    236  CG1 ILE A 236       6.587  12.805   0.730  1.00 36.59           C  
ATOM    237  CG2 ILE A 236       8.944  13.226  -0.042  1.00 34.29           C  
ATOM    238  CD1 ILE A 236       6.578  13.790   1.896  1.00 37.36           C  
ATOM    239  N   LEU A 237       9.848   9.749  -0.283  1.00 37.78           N  
ATOM    240  CA  LEU A 237      11.177   9.254  -0.620  1.00 39.53           C  
ATOM    241  C   LEU A 237      11.219   8.299  -1.803  1.00 42.05           C  
ATOM    242  O   LEU A 237      12.142   8.342  -2.611  1.00 41.94           O  
ATOM    243  CB  LEU A 237      11.800   8.558   0.595  1.00 38.58           C  
ATOM    244  CG  LEU A 237      12.194   9.463   1.758  1.00 39.49           C  
ATOM    245  CD1 LEU A 237      12.586   8.608   2.957  1.00 40.59           C  
ATOM    246  CD2 LEU A 237      13.341  10.368   1.332  1.00 36.59           C  
ATOM    247  N   THR A 238      10.218   7.436  -1.912  1.00 45.14           N  
ATOM    248  CA  THR A 238      10.221   6.463  -2.984  1.00 47.06           C  
ATOM    249  C   THR A 238       9.664   7.000  -4.284  1.00 51.04           C  
ATOM    250  O   THR A 238       9.625   6.296  -5.293  1.00 52.67           O  
ATOM    251  CB  THR A 238       9.467   5.208  -2.560  1.00 46.18           C  
ATOM    252  OG1 THR A 238       8.126   5.557  -2.192  1.00 45.80           O  
ATOM    253  CG2 THR A 238      10.176   4.559  -1.371  1.00 44.85           C  
ATOM    254  N   GLY A 239       9.238   8.256  -4.256  1.00 53.88           N  
ATOM    255  CA  GLY A 239       8.717   8.888  -5.451  1.00 57.80           C  
ATOM    256  C   GLY A 239       7.466   8.272  -6.046  1.00 60.16           C  
ATOM    257  O   GLY A 239       6.484   8.020  -5.342  1.00 60.79           O  
ATOM    258  N   LYS A 240       7.510   8.032  -7.356  1.00 63.47           N  
ATOM    259  CA  LYS A 240       6.375   7.473  -8.085  1.00 65.43           C  
ATOM    260  C   LYS A 240       5.263   8.491  -7.910  1.00 65.97           C  
ATOM    261  O   LYS A 240       4.085   8.206  -8.125  1.00 68.36           O  
ATOM    262  CB  LYS A 240       5.955   6.128  -7.489  1.00 66.76           C  
ATOM    263  CG  LYS A 240       4.896   5.386  -8.295  1.00 68.55           C  
ATOM    264  CD  LYS A 240       4.545   4.064  -7.625  1.00 69.63           C  
ATOM    265  CE  LYS A 240       3.600   3.235  -8.478  1.00 69.72           C  
ATOM    266  NZ  LYS A 240       3.327   1.908  -7.855  1.00 71.60           N  
ATOM    267  N   THR A 241       5.671   9.692  -7.518  1.00 65.80           N  
ATOM    268  CA  THR A 241       4.760  10.793  -7.275  1.00 64.63           C  
ATOM    269  C   THR A 241       5.212  12.033  -8.030  1.00 64.05           C  
ATOM    270  O   THR A 241       6.381  12.164  -8.400  1.00 63.52           O  
ATOM    271  CB  THR A 241       4.700  11.136  -5.762  1.00 65.75           C  
ATOM    272  OG1 THR A 241       3.820  12.248  -5.552  1.00 66.76           O  
ATOM    273  CG2 THR A 241       6.097  11.493  -5.232  1.00 63.92           C  
ATOM    274  N   THR A 242       4.257  12.929  -8.251  1.00 62.68           N  
ATOM    275  CA  THR A 242       4.476  14.199  -8.929  1.00 62.19           C  
ATOM    276  C   THR A 242       3.866  15.243  -7.992  1.00 61.16           C  
ATOM    277  O   THR A 242       4.116  16.442  -8.108  1.00 59.95           O  
ATOM    278  CB  THR A 242       3.738  14.233 -10.296  1.00 62.23           C  
ATOM    279  OG1 THR A 242       4.427  13.397 -11.235  1.00 64.55           O  
ATOM    280  CG2 THR A 242       3.672  15.645 -10.839  1.00 62.93           C  
ATOM    281  N   ASP A 243       3.061  14.746  -7.057  1.00 59.00           N  
ATOM    282  CA  ASP A 243       2.371  15.568  -6.075  1.00 58.94           C  
ATOM    283  C   ASP A 243       3.279  16.065  -4.939  1.00 57.14           C  
ATOM    284  O   ASP A 243       3.188  17.220  -4.524  1.00 57.20           O  
ATOM    285  CB  ASP A 243       1.193  14.765  -5.492  1.00 59.15           C  
ATOM    286  CG  ASP A 243       0.404  15.545  -4.453  1.00 63.66           C  
ATOM    287  OD1 ASP A 243      -0.052  16.672  -4.760  1.00 66.67           O  
ATOM    288  OD2 ASP A 243       0.230  15.031  -3.324  1.00 63.69           O  
ATOM    289  N   LYS A 244       4.153  15.198  -4.436  1.00 55.23           N  
ATOM    290  CA  LYS A 244       5.019  15.589  -3.335  1.00 52.68           C  
ATOM    291  C   LYS A 244       6.503  15.291  -3.471  1.00 49.51           C  
ATOM    292  O   LYS A 244       7.106  14.700  -2.576  1.00 46.79           O  
ATOM    293  CB  LYS A 244       4.511  14.978  -2.032  1.00 54.76           C  
ATOM    294  CG  LYS A 244       4.257  13.494  -2.091  1.00 56.14           C  
ATOM    295  CD  LYS A 244       2.823  13.196  -2.459  1.00 55.99           C  
ATOM    296  CE  LYS A 244       2.348  11.969  -1.696  1.00 56.37           C  
ATOM    297  NZ  LYS A 244       2.356  12.165  -0.209  1.00 53.47           N  
ATOM    298  N   SER A 245       7.087  15.698  -4.592  1.00 46.95           N  
ATOM    299  CA  SER A 245       8.512  15.521  -4.811  1.00 45.90           C  
ATOM    300  C   SER A 245       9.173  16.650  -4.031  1.00 43.56           C  
ATOM    301  O   SER A 245       8.705  17.795  -4.079  1.00 42.86           O  
ATOM    302  CB  SER A 245       8.849  15.650  -6.302  1.00 48.42           C  
ATOM    303  OG  SER A 245       8.365  14.533  -7.032  1.00 53.46           O  
ATOM    304  N   PRO A 246      10.252  16.344  -3.285  1.00 40.16           N  
ATOM    305  CA  PRO A 246      10.975  17.342  -2.488  1.00 40.46           C  
ATOM    306  C   PRO A 246      12.108  18.016  -3.249  1.00 40.67           C  
ATOM    307  O   PRO A 246      12.637  17.457  -4.210  1.00 40.56           O  
ATOM    308  CB  PRO A 246      11.507  16.516  -1.333  1.00 41.20           C  
ATOM    309  CG  PRO A 246      11.920  15.237  -2.049  1.00 38.99           C  
ATOM    310  CD  PRO A 246      10.761  14.987  -3.012  1.00 38.12           C  
ATOM    311  N   PHE A 247      12.471  19.226  -2.833  1.00 41.28           N  
ATOM    312  CA  PHE A 247      13.577  19.920  -3.472  1.00 41.32           C  
ATOM    313  C   PHE A 247      14.793  19.312  -2.786  1.00 41.16           C  
ATOM    314  O   PHE A 247      14.758  19.082  -1.580  1.00 41.19           O  
ATOM    315  CB  PHE A 247      13.529  21.429  -3.201  1.00 42.68           C  
ATOM    316  CG  PHE A 247      14.646  22.191  -3.861  1.00 41.82           C  
ATOM    317  CD1 PHE A 247      14.643  22.405  -5.238  1.00 42.97           C  
ATOM    318  CD2 PHE A 247      15.735  22.638  -3.117  1.00 44.19           C  
ATOM    319  CE1 PHE A 247      15.713  23.049  -5.868  1.00 41.83           C  
ATOM    320  CE2 PHE A 247      16.809  23.283  -3.734  1.00 43.31           C  
ATOM    321  CZ  PHE A 247      16.798  23.488  -5.111  1.00 43.58           C  
ATOM    322  N   VAL A 248      15.865  19.061  -3.529  1.00 40.41           N  
ATOM    323  CA  VAL A 248      17.038  18.446  -2.924  1.00 40.01           C  
ATOM    324  C   VAL A 248      18.231  19.368  -2.665  1.00 41.51           C  
ATOM    325  O   VAL A 248      18.701  20.069  -3.560  1.00 41.27           O  
ATOM    326  CB  VAL A 248      17.497  17.231  -3.758  1.00 38.82           C  
ATOM    327  CG1 VAL A 248      18.767  16.634  -3.161  1.00 37.18           C  
ATOM    328  CG2 VAL A 248      16.374  16.163  -3.779  1.00 34.96           C  
ATOM    329  N   ILE A 249      18.699  19.349  -1.417  1.00 41.07           N  
ATOM    330  CA  ILE A 249      19.834  20.150  -0.967  1.00 41.34           C  
ATOM    331  C   ILE A 249      21.039  19.218  -0.902  1.00 40.40           C  
ATOM    332  O   ILE A 249      21.119  18.372  -0.016  1.00 38.30           O  
ATOM    333  CB  ILE A 249      19.619  20.723   0.462  1.00 41.04           C  
ATOM    334  CG1 ILE A 249      18.305  21.506   0.558  1.00 43.84           C  
ATOM    335  CG2 ILE A 249      20.781  21.633   0.826  1.00 43.81           C  
ATOM    336  CD1 ILE A 249      18.276  22.781  -0.248  1.00 45.01           C  
ATOM    337  N   TYR A 250      21.970  19.385  -1.835  1.00 41.97           N  
ATOM    338  CA  TYR A 250      23.170  18.552  -1.903  1.00 43.62           C  
ATOM    339  C   TYR A 250      24.438  19.421  -1.928  1.00 45.26           C  
ATOM    340  O   TYR A 250      25.549  18.904  -2.061  1.00 43.64           O  
ATOM    341  CB  TYR A 250      23.108  17.678  -3.163  1.00 42.92           C  
ATOM    342  CG  TYR A 250      23.090  18.486  -4.441  1.00 42.96           C  
ATOM    343  CD1 TYR A 250      24.249  18.654  -5.201  1.00 41.29           C  
ATOM    344  CD2 TYR A 250      21.928  19.143  -4.857  1.00 43.17           C  
ATOM    345  CE1 TYR A 250      24.253  19.462  -6.340  1.00 43.37           C  
ATOM    346  CE2 TYR A 250      21.921  19.958  -5.998  1.00 41.17           C  
ATOM    347  CZ  TYR A 250      23.085  20.113  -6.727  1.00 43.40           C  
ATOM    348  OH  TYR A 250      23.095  20.946  -7.820  1.00 46.31           O  
ATOM    349  N   ASP A 251      24.256  20.739  -1.824  1.00 46.88           N  
ATOM    350  CA  ASP A 251      25.365  21.689  -1.815  1.00 49.88           C  
ATOM    351  C   ASP A 251      24.914  23.117  -1.494  1.00 51.73           C  
ATOM    352  O   ASP A 251      23.717  23.395  -1.376  1.00 51.69           O  
ATOM    353  CB  ASP A 251      26.106  21.685  -3.158  1.00 50.83           C  
ATOM    354  CG  ASP A 251      25.285  22.282  -4.291  1.00 51.94           C  
ATOM    355  OD1 ASP A 251      24.309  23.026  -4.032  1.00 52.92           O  
ATOM    356  OD2 ASP A 251      25.635  22.014  -5.457  1.00 53.77           O  
ATOM    357  N   MET A 252      25.883  24.021  -1.372  1.00 53.10           N  
ATOM    358  CA  MET A 252      25.609  25.418  -1.050  1.00 55.57           C  
ATOM    359  C   MET A 252      24.621  26.080  -1.993  1.00 55.69           C  
ATOM    360  O   MET A 252      23.724  26.802  -1.561  1.00 56.39           O  
ATOM    361  CB  MET A 252      26.914  26.218  -1.047  1.00 58.36           C  
ATOM    362  CG  MET A 252      27.916  25.742  -0.010  1.00 61.92           C  
ATOM    363  SD  MET A 252      27.162  25.637   1.635  1.00 66.07           S  
ATOM    364  CE  MET A 252      26.924  27.380   2.005  1.00 64.03           C  
ATOM    365  N   ASN A 253      24.798  25.839  -3.286  1.00 56.92           N  
ATOM    366  CA  ASN A 253      23.930  26.422  -4.295  1.00 57.32           C  
ATOM    367  C   ASN A 253      22.483  25.983  -4.088  1.00 56.65           C  
ATOM    368  O   ASN A 253      21.587  26.816  -3.911  1.00 56.47           O  
ATOM    369  CB  ASN A 253      24.401  26.004  -5.687  1.00 60.17           C  
ATOM    370  CG  ASN A 253      24.182  27.082  -6.720  1.00 64.00           C  
ATOM    371  OD1 ASN A 253      24.910  28.080  -6.753  1.00 66.98           O  
ATOM    372  ND2 ASN A 253      23.171  26.897  -7.567  1.00 64.65           N  
ATOM    373  N   SER A 254      22.252  24.673  -4.121  1.00 55.93           N  
ATOM    374  CA  SER A 254      20.907  24.151  -3.925  1.00 54.93           C  
ATOM    375  C   SER A 254      20.399  24.578  -2.545  1.00 54.79           C  
ATOM    376  O   SER A 254      19.202  24.799  -2.352  1.00 53.30           O  
ATOM    377  CB  SER A 254      20.900  22.621  -4.065  1.00 53.33           C  
ATOM    378  OG  SER A 254      21.960  22.025  -3.340  1.00 53.95           O  
ATOM    379  N   LEU A 255      21.313  24.704  -1.586  1.00 55.36           N  
ATOM    380  CA  LEU A 255      20.926  25.133  -0.247  1.00 56.88           C  
ATOM    381  C   LEU A 255      20.380  26.553  -0.350  1.00 58.01           C  
ATOM    382  O   LEU A 255      19.310  26.860   0.185  1.00 58.34           O  
ATOM    383  CB  LEU A 255      22.124  25.097   0.703  1.00 55.19           C  
ATOM    384  CG  LEU A 255      21.899  25.679   2.103  1.00 56.23           C  
ATOM    385  CD1 LEU A 255      20.687  25.037   2.772  1.00 56.13           C  
ATOM    386  CD2 LEU A 255      23.148  25.449   2.936  1.00 56.80           C  
ATOM    387  N   MET A 256      21.119  27.416  -1.044  1.00 60.00           N  
ATOM    388  CA  MET A 256      20.695  28.801  -1.236  1.00 62.56           C  
ATOM    389  C   MET A 256      19.305  28.815  -1.867  1.00 62.46           C  
ATOM    390  O   MET A 256      18.377  29.424  -1.334  1.00 62.09           O  
ATOM    391  CB  MET A 256      21.671  29.546  -2.154  1.00 64.92           C  
ATOM    392  CG  MET A 256      23.046  29.819  -1.556  1.00 68.28           C  
ATOM    393  SD  MET A 256      24.102  30.783  -2.687  1.00 72.23           S  
ATOM    394  CE  MET A 256      25.171  29.477  -3.383  1.00 71.66           C  
ATOM    395  N   MET A 257      19.173  28.135  -3.004  1.00 62.73           N  
ATOM    396  CA  MET A 257      17.901  28.058  -3.712  1.00 63.86           C  
ATOM    397  C   MET A 257      16.822  27.428  -2.833  1.00 64.26           C  
ATOM    398  O   MET A 257      15.648  27.792  -2.920  1.00 63.99           O  
ATOM    399  CB  MET A 257      18.054  27.238  -4.997  1.00 64.94           C  
ATOM    400  CG  MET A 257      19.017  27.831  -6.019  1.00 67.09           C  
ATOM    401  SD  MET A 257      18.260  28.035  -7.656  1.00 70.65           S  
ATOM    402  CE  MET A 257      17.985  26.306  -8.135  1.00 68.52           C  
ATOM    403  N   GLY A 258      17.230  26.485  -1.988  1.00 64.08           N  
ATOM    404  CA  GLY A 258      16.298  25.813  -1.100  1.00 64.36           C  
ATOM    405  C   GLY A 258      15.376  26.741  -0.327  1.00 65.52           C  
ATOM    406  O   GLY A 258      14.190  26.448  -0.168  1.00 63.54           O  
ATOM    407  N   GLU A 259      15.905  27.864   0.153  1.00 67.00           N  
ATOM    408  CA  GLU A 259      15.087  28.805   0.910  1.00 68.47           C  
ATOM    409  C   GLU A 259      14.152  29.573  -0.020  1.00 68.48           C  
ATOM    410  O   GLU A 259      13.478  30.515   0.399  1.00 69.65           O  
ATOM    411  CB  GLU A 259      15.979  29.778   1.697  1.00 70.29           C  
ATOM    412  CG  GLU A 259      15.275  30.432   2.891  1.00 74.31           C  
ATOM    413  CD  GLU A 259      16.233  31.151   3.836  1.00 76.54           C  
ATOM    414  OE1 GLU A 259      16.853  32.154   3.420  1.00 77.42           O  
ATOM    415  OE2 GLU A 259      16.366  30.710   4.999  1.00 78.62           O  
ATOM    416  N   ASP A 260      14.108  29.158  -1.283  0.00 67.95           N  
ATOM    417  CA  ASP A 260      13.252  29.796  -2.277  0.00 67.48           C  
ATOM    418  C   ASP A 260      12.057  28.900  -2.593  0.00 67.78           C  
ATOM    419  O   ASP A 260      10.967  29.390  -2.890  0.00 67.61           O  
ATOM    420  CB  ASP A 260      14.047  30.078  -3.557  0.00 66.60           C  
ATOM    421  CG  ASP A 260      13.241  30.840  -4.592  0.00 65.93           C  
ATOM    422  OD1 ASP A 260      12.221  30.303  -5.073  0.00 65.53           O  
ATOM    423  OD2 ASP A 260      13.629  31.980  -4.925  0.00 65.53           O  
ATOM    424  N   LYS A 261      12.265  27.587  -2.526  1.00 68.54           N  
ATOM    425  CA  LYS A 261      11.192  26.633  -2.801  1.00 69.10           C  
ATOM    426  C   LYS A 261      10.372  26.356  -1.538  1.00 69.72           C  
ATOM    427  O   LYS A 261       9.142  26.340  -1.582  1.00 70.24           O  
ATOM    428  CB  LYS A 261      11.761  25.317  -3.340  1.00 68.12           C  
ATOM    429  CG  LYS A 261      10.752  24.510  -4.165  1.00 68.90           C  
ATOM    430  CD  LYS A 261      10.547  23.088  -3.646  1.00 66.49           C  
ATOM    431  CE  LYS A 261       9.854  23.067  -2.284  1.00 67.01           C  
ATOM    432  NZ  LYS A 261       9.437  21.686  -1.881  1.00 63.20           N  
ATOM    433  N   ILE A 262      11.058  26.139  -0.418  1.00 70.56           N  
ATOM    434  CA  ILE A 262      10.395  25.872   0.858  1.00 71.55           C  
ATOM    435  C   ILE A 262      10.446  27.128   1.727  1.00 72.99           C  
ATOM    436  O   ILE A 262      11.205  28.059   1.447  1.00 74.01           O  
ATOM    437  CB  ILE A 262      11.095  24.735   1.653  1.00 70.96           C  
ATOM    438  CG1 ILE A 262      11.452  23.569   0.733  1.00 70.38           C  
ATOM    439  CG2 ILE A 262      10.189  24.247   2.771  1.00 71.00           C  
ATOM    440  CD1 ILE A 262      12.841  23.657   0.162  1.00 68.63           C  
ATOM    441  N   LYS A 263       9.644  27.147   2.787  1.00 74.08           N  
ATOM    442  CA  LYS A 263       9.621  28.288   3.697  1.00 74.49           C  
ATOM    443  C   LYS A 263      10.639  28.083   4.818  1.00 73.87           C  
ATOM    444  O   LYS A 263      10.415  27.282   5.729  1.00 75.23           O  
ATOM    445  CB  LYS A 263       8.224  28.465   4.304  1.00 74.70           C  
ATOM    446  CG  LYS A 263       8.136  29.609   5.303  1.00 75.14           C  
ATOM    447  CD  LYS A 263       6.785  29.668   5.993  1.00 74.49           C  
ATOM    448  CE  LYS A 263       6.722  30.857   6.939  1.00 74.64           C  
ATOM    449  NZ  LYS A 263       7.854  30.852   7.909  1.00 74.35           N  
ATOM    450  N   PHE A 264      11.754  28.804   4.751  0.00 72.35           N  
ATOM    451  CA  PHE A 264      12.792  28.688   5.768  0.00 70.89           C  
ATOM    452  C   PHE A 264      13.136  30.040   6.385  0.00 70.90           C  
ATOM    453  O   PHE A 264      13.199  31.052   5.688  0.00 70.74           O  
ATOM    454  CB  PHE A 264      14.062  28.070   5.171  0.00 69.18           C  
ATOM    455  CG  PHE A 264      13.884  26.661   4.672  0.00 67.48           C  
ATOM    456  CD1 PHE A 264      13.195  25.721   5.430  0.00 66.74           C  
ATOM    457  CD2 PHE A 264      14.445  26.263   3.462  0.00 66.74           C  
ATOM    458  CE1 PHE A 264      13.067  24.405   4.992  0.00 66.17           C  
ATOM    459  CE2 PHE A 264      14.323  24.948   3.015  0.00 66.17           C  
ATOM    460  CZ  PHE A 264      13.634  24.018   3.783  0.00 66.01           C  
ATOM    461  N   LYS A 265      13.356  30.052   7.697  1.00 71.55           N  
ATOM    462  CA  LYS A 265      13.710  31.281   8.400  1.00 71.13           C  
ATOM    463  C   LYS A 265      15.189  31.260   8.753  1.00 70.52           C  
ATOM    464  O   LYS A 265      15.563  31.036   9.907  1.00 71.55           O  
ATOM    465  CB  LYS A 265      12.882  31.435   9.677  1.00 71.69           C  
ATOM    466  CG  LYS A 265      11.395  31.584   9.430  1.00 73.17           C  
ATOM    467  CD  LYS A 265      10.657  31.932  10.710  1.00 73.47           C  
ATOM    468  CE  LYS A 265       9.211  32.263  10.409  1.00 74.47           C  
ATOM    469  NZ  LYS A 265       9.138  33.355   9.398  1.00 75.41           N  
ATOM    470  N   HIS A 266      16.024  31.482   7.745  0.00 68.67           N  
ATOM    471  CA  HIS A 266      17.470  31.507   7.916  0.00 66.97           C  
ATOM    472  C   HIS A 266      18.065  32.475   6.899  0.00 66.75           C  
ATOM    473  O   HIS A 266      17.477  33.517   6.610  0.00 66.50           O  
ATOM    474  CB  HIS A 266      18.058  30.106   7.716  0.00 65.52           C  
ATOM    475  CG  HIS A 266      17.624  29.114   8.751  0.00 64.07           C  
ATOM    476  ND1 HIS A 266      17.838  29.302  10.099  0.00 63.47           N  
ATOM    477  CD2 HIS A 266      16.991  27.922   8.634  0.00 63.47           C  
ATOM    478  CE1 HIS A 266      17.357  28.270  10.768  0.00 63.07           C  
ATOM    479  NE2 HIS A 266      16.838  27.418   9.902  0.00 63.07           N  
ATOM    480  N   ILE A 267      19.226  32.129   6.353  0.00 66.78           N  
ATOM    481  CA  ILE A 267      19.885  32.981   5.370  0.00 67.06           C  
ATOM    482  C   ILE A 267      20.111  32.225   4.064  0.00 67.67           C  
ATOM    483  O   ILE A 267      20.559  31.078   4.071  0.00 67.52           O  
ATOM    484  CB  ILE A 267      21.249  33.482   5.892  0.00 66.72           C  
ATOM    485  CG1 ILE A 267      21.080  34.106   7.280  0.00 66.60           C  
ATOM    486  CG2 ILE A 267      21.829  34.504   4.926  0.00 66.31           C  
ATOM    487  CD1 ILE A 267      22.388  34.514   7.941  1.00 67.53           C  
ATOM    488  N   THR A 268      19.797  32.871   2.945  1.00 68.86           N  
ATOM    489  CA  THR A 268      19.975  32.256   1.632  1.00 69.66           C  
ATOM    490  C   THR A 268      21.376  32.523   1.084  1.00 70.21           C  
ATOM    491  O   THR A 268      22.125  31.581   0.797  1.00 71.31           O  
ATOM    492  CB  THR A 268      18.938  32.786   0.602  1.00 69.90           C  
ATOM    493  OG1 THR A 268      17.621  32.361   0.976  1.00 71.51           O  
ATOM    494  CG2 THR A 268      19.258  32.273  -0.797  1.00 69.53           C  
ATOM    495  N   PRO A 269      21.755  33.814   0.947  1.00 69.59           N  
ATOM    496  CA  PRO A 269      23.067  34.223   0.429  1.00 67.75           C  
ATOM    497  C   PRO A 269      24.268  33.658   1.186  1.00 65.89           C  
ATOM    498  O   PRO A 269      24.191  32.576   1.767  1.00 67.79           O  
ATOM    499  CB  PRO A 269      22.998  35.748   0.498  1.00 68.62           C  
ATOM    500  CG  PRO A 269      22.121  35.985   1.689  1.00 69.03           C  
ATOM    501  CD  PRO A 269      21.014  34.991   1.441  1.00 69.30           C  
ATOM    502  N   LEU A 270      25.374  34.396   1.171  0.00 62.52           N  
ATOM    503  CA  LEU A 270      26.599  33.977   1.848  0.00 58.92           C  
ATOM    504  C   LEU A 270      26.352  33.744   3.338  0.00 56.91           C  
ATOM    505  O   LEU A 270      25.395  34.269   3.906  0.00 56.55           O  
ATOM    506  CB  LEU A 270      27.688  35.038   1.638  0.00 58.22           C  
ATOM    507  CG  LEU A 270      29.105  34.829   2.187  0.00 57.48           C  
ATOM    508  CD1 LEU A 270      29.149  35.162   3.668  0.00 57.10           C  
ATOM    509  CD2 LEU A 270      29.556  33.401   1.921  0.00 57.10           C  
ATOM    510  N   GLN A 271      27.220  32.954   3.965  0.00 54.64           N  
ATOM    511  CA  GLN A 271      27.082  32.640   5.384  0.00 52.49           C  
ATOM    512  C   GLN A 271      28.353  32.825   6.212  0.00 51.65           C  
ATOM    513  O   GLN A 271      28.286  32.943   7.436  0.00 51.38           O  
ATOM    514  CB  GLN A 271      26.562  31.207   5.541  0.00 51.61           C  
ATOM    515  CG  GLN A 271      27.116  30.218   4.519  0.00 50.32           C  
ATOM    516  CD  GLN A 271      28.567  29.845   4.763  0.00 49.70           C  
ATOM    517  OE1 GLN A 271      29.224  29.270   3.895  0.00 49.30           O  
ATOM    518  NE2 GLN A 271      29.070  30.157   5.952  0.00 49.30           N  
ATOM    519  N   GLU A 272      29.504  32.852   5.549  0.00 50.82           N  
ATOM    520  CA  GLU A 272      30.784  33.019   6.235  0.00 50.20           C  
ATOM    521  C   GLU A 272      30.758  34.084   7.328  0.00 50.47           C  
ATOM    522  O   GLU A 272      30.858  33.768   8.514  0.00 50.28           O  
ATOM    523  CB  GLU A 272      31.885  33.352   5.224  0.00 49.27           C  
ATOM    524  CG  GLU A 272      32.366  32.158   4.417  0.00 48.07           C  
ATOM    525  CD  GLU A 272      33.028  31.104   5.285  0.00 47.45           C  
ATOM    526  OE1 GLU A 272      34.038  31.426   5.945  0.00 47.08           O  
ATOM    527  OE2 GLU A 272      32.538  29.955   5.307  0.00 47.08           O  
ATOM    528  N   GLN A 273      30.628  35.345   6.927  0.00 51.05           N  
ATOM    529  CA  GLN A 273      30.600  36.450   7.879  0.00 51.90           C  
ATOM    530  C   GLN A 273      29.182  36.826   8.299  0.00 53.26           C  
ATOM    531  O   GLN A 273      28.933  37.954   8.725  0.00 53.15           O  
ATOM    532  CB  GLN A 273      31.298  37.676   7.282  0.00 50.91           C  
ATOM    533  CG  GLN A 273      32.783  37.484   7.008  0.00 49.76           C  
ATOM    534  CD  GLN A 273      33.590  37.269   8.275  0.00 49.15           C  
ATOM    535  OE1 GLN A 273      33.387  36.294   8.998  0.00 48.79           O  
ATOM    536  NE2 GLN A 273      34.512  38.185   8.550  0.00 48.79           N  
ATOM    537  N   SER A 274      28.256  35.878   8.180  0.00 55.20           N  
ATOM    538  CA  SER A 274      26.865  36.119   8.551  0.00 57.53           C  
ATOM    539  C   SER A 274      26.141  34.813   8.866  0.00 59.52           C  
ATOM    540  O   SER A 274      25.420  34.274   8.027  0.00 59.58           O  
ATOM    541  CB  SER A 274      26.140  36.853   7.419  0.00 56.97           C  
ATOM    542  OG  SER A 274      26.744  38.107   7.154  0.00 56.65           O  
ATOM    543  N   LYS A 275      26.336  34.317  10.085  1.00 62.80           N  
ATOM    544  CA  LYS A 275      25.717  33.071  10.536  1.00 64.47           C  
ATOM    545  C   LYS A 275      25.978  31.982   9.494  1.00 66.28           C  
ATOM    546  O   LYS A 275      25.134  31.707   8.638  1.00 67.66           O  
ATOM    547  CB  LYS A 275      24.212  33.276  10.735  1.00 64.52           C  
ATOM    548  CG  LYS A 275      23.611  32.441  11.856  1.00 63.29           C  
ATOM    549  CD  LYS A 275      22.225  32.945  12.211  1.00 63.27           C  
ATOM    550  CE  LYS A 275      21.774  32.434  13.572  1.00 64.40           C  
ATOM    551  NZ  LYS A 275      20.433  32.975  13.957  1.00 64.02           N  
ATOM    552  N   GLU A 276      27.161  31.374   9.577  1.00 66.74           N  
ATOM    553  CA  GLU A 276      27.580  30.329   8.647  1.00 66.45           C  
ATOM    554  C   GLU A 276      26.497  29.296   8.347  1.00 65.02           C  
ATOM    555  O   GLU A 276      25.534  29.145   9.101  1.00 64.79           O  
ATOM    556  CB  GLU A 276      28.815  29.611   9.191  1.00 67.11           C  
ATOM    557  CG  GLU A 276      28.500  28.637  10.304  1.00 68.73           C  
ATOM    558  CD  GLU A 276      29.742  28.021  10.900  1.00 70.19           C  
ATOM    559  OE1 GLU A 276      30.584  27.508  10.127  1.00 69.85           O  
ATOM    560  OE2 GLU A 276      29.870  28.048  12.144  1.00 71.08           O  
ATOM    561  N   VAL A 277      26.681  28.584   7.239  1.00 64.14           N  
ATOM    562  CA  VAL A 277      25.747  27.553   6.799  1.00 63.69           C  
ATOM    563  C   VAL A 277      25.540  26.468   7.852  1.00 62.57           C  
ATOM    564  O   VAL A 277      24.406  26.096   8.146  1.00 63.16           O  
ATOM    565  CB  VAL A 277      26.237  26.895   5.483  1.00 64.40           C  
ATOM    566  CG1 VAL A 277      27.716  26.541   5.600  1.00 65.90           C  
ATOM    567  CG2 VAL A 277      25.425  25.646   5.187  1.00 63.36           C  
ATOM    568  N   ALA A 278      26.632  25.962   8.416  1.00 61.39           N  
ATOM    569  CA  ALA A 278      26.548  24.923   9.435  1.00 60.88           C  
ATOM    570  C   ALA A 278      25.621  25.337  10.578  1.00 61.05           C  
ATOM    571  O   ALA A 278      24.622  24.672  10.851  1.00 61.93           O  
ATOM    572  CB  ALA A 278      27.937  24.610   9.975  1.00 59.71           C  
ATOM    573  N   ILE A 279      25.952  26.437  11.246  1.00 61.61           N  
ATOM    574  CA  ILE A 279      25.145  26.919  12.358  1.00 61.28           C  
ATOM    575  C   ILE A 279      23.732  27.190  11.887  1.00 61.28           C  
ATOM    576  O   ILE A 279      22.764  26.943  12.608  1.00 62.27           O  
ATOM    577  CB  ILE A 279      25.710  28.230  12.946  1.00 62.71           C  
ATOM    578  CG1 ILE A 279      27.090  27.980  13.553  1.00 62.86           C  
ATOM    579  CG2 ILE A 279      24.755  28.780  14.002  1.00 62.00           C  
ATOM    580  CD1 ILE A 279      27.748  29.238  14.093  1.00 66.68           C  
ATOM    581  N   ARG A 280      23.622  27.711  10.673  1.00 60.41           N  
ATOM    582  CA  ARG A 280      22.325  28.028  10.103  1.00 60.40           C  
ATOM    583  C   ARG A 280      21.461  26.774  10.072  1.00 58.91           C  
ATOM    584  O   ARG A 280      20.273  26.810  10.406  1.00 58.56           O  
ATOM    585  CB  ARG A 280      22.510  28.581   8.694  1.00 62.74           C  
ATOM    586  CG  ARG A 280      21.368  29.449   8.204  1.00 65.38           C  
ATOM    587  CD  ARG A 280      21.865  30.376   7.106  1.00 67.35           C  
ATOM    588  NE  ARG A 280      22.396  29.636   5.963  1.00 69.08           N  
ATOM    589  CZ  ARG A 280      23.221  30.152   5.058  1.00 69.39           C  
ATOM    590  NH1 ARG A 280      23.614  31.415   5.165  1.00 70.05           N  
ATOM    591  NH2 ARG A 280      23.648  29.409   4.044  1.00 68.13           N  
ATOM    592  N   ILE A 281      22.067  25.660   9.677  1.00 57.08           N  
ATOM    593  CA  ILE A 281      21.352  24.394   9.614  1.00 54.94           C  
ATOM    594  C   ILE A 281      21.209  23.798  11.012  1.00 53.52           C  
ATOM    595  O   ILE A 281      20.276  23.038  11.274  1.00 52.31           O  
ATOM    596  CB  ILE A 281      22.086  23.373   8.713  1.00 55.02           C  
ATOM    597  CG1 ILE A 281      22.360  23.985   7.338  1.00 55.11           C  
ATOM    598  CG2 ILE A 281      21.231  22.127   8.540  1.00 57.04           C  
ATOM    599  CD1 ILE A 281      23.080  23.051   6.382  1.00 55.40           C  
ATOM    600  N   PHE A 282      22.130  24.148  11.909  1.00 52.92           N  
ATOM    601  CA  PHE A 282      22.090  23.629  13.277  1.00 53.57           C  
ATOM    602  C   PHE A 282      20.885  24.163  14.047  1.00 52.85           C  
ATOM    603  O   PHE A 282      20.161  23.399  14.682  1.00 53.25           O  
ATOM    604  CB  PHE A 282      23.372  23.983  14.045  1.00 54.12           C  
ATOM    605  CG  PHE A 282      23.532  23.218  15.336  1.00 56.55           C  
ATOM    606  CD1 PHE A 282      24.197  21.994  15.360  1.00 58.40           C  
ATOM    607  CD2 PHE A 282      22.973  23.694  16.518  1.00 57.50           C  
ATOM    608  CE1 PHE A 282      24.302  21.252  16.545  1.00 58.28           C  
ATOM    609  CE2 PHE A 282      23.070  22.963  17.705  1.00 57.91           C  
ATOM    610  CZ  PHE A 282      23.736  21.739  17.717  1.00 58.06           C  
ATOM    611  N   GLN A 283      20.674  25.474  14.002  1.00 53.35           N  
ATOM    612  CA  GLN A 283      19.542  26.065  14.707  1.00 54.96           C  
ATOM    613  C   GLN A 283      18.227  25.658  14.056  1.00 54.95           C  
ATOM    614  O   GLN A 283      17.148  25.865  14.614  1.00 54.33           O  
ATOM    615  CB  GLN A 283      19.673  27.590  14.752  1.00 56.30           C  
ATOM    616  CG  GLN A 283      20.093  28.094  16.125  1.00 58.89           C  
ATOM    617  CD  GLN A 283      21.267  29.046  16.078  1.00 60.03           C  
ATOM    618  OE1 GLN A 283      21.835  29.396  17.116  1.00 60.76           O  
ATOM    619  NE2 GLN A 283      21.639  29.473  14.876  1.00 59.55           N  
ATOM    620  N   GLY A 284      18.327  25.077  12.867  1.00 54.92           N  
ATOM    621  CA  GLY A 284      17.141  24.613  12.177  1.00 55.67           C  
ATOM    622  C   GLY A 284      16.658  23.357  12.874  1.00 56.35           C  
ATOM    623  O   GLY A 284      15.470  23.213  13.162  1.00 55.29           O  
ATOM    624  N   CYS A 285      17.596  22.451  13.150  1.00 56.95           N  
ATOM    625  CA  CYS A 285      17.299  21.198  13.834  1.00 58.73           C  
ATOM    626  C   CYS A 285      16.848  21.532  15.239  1.00 57.52           C  
ATOM    627  O   CYS A 285      15.871  20.974  15.745  1.00 57.38           O  
ATOM    628  CB  CYS A 285      18.547  20.316  13.927  1.00 60.02           C  
ATOM    629  SG  CYS A 285      19.416  20.093  12.367  1.00 69.77           S  
ATOM    630  N   GLN A 286      17.580  22.451  15.859  1.00 57.12           N  
ATOM    631  CA  GLN A 286      17.296  22.883  17.215  1.00 57.42           C  
ATOM    632  C   GLN A 286      15.829  23.262  17.343  1.00 57.14           C  
ATOM    633  O   GLN A 286      15.167  22.858  18.296  1.00 58.50           O  
ATOM    634  CB  GLN A 286      18.185  24.074  17.584  1.00 58.88           C  
ATOM    635  CG  GLN A 286      18.448  24.223  19.079  1.00 62.02           C  
ATOM    636  CD  GLN A 286      19.284  25.450  19.411  1.00 64.15           C  
ATOM    637  OE1 GLN A 286      18.778  26.574  19.436  1.00 65.35           O  
ATOM    638  NE2 GLN A 286      20.574  25.240  19.656  1.00 64.86           N  
ATOM    639  N   PHE A 287      15.321  24.025  16.375  1.00 56.36           N  
ATOM    640  CA  PHE A 287      13.926  24.453  16.388  1.00 55.11           C  
ATOM    641  C   PHE A 287      12.967  23.288  16.169  1.00 54.14           C  
ATOM    642  O   PHE A 287      11.953  23.173  16.858  1.00 53.45           O  
ATOM    643  CB  PHE A 287      13.685  25.528  15.322  1.00 56.87           C  
ATOM    644  CG  PHE A 287      12.235  25.890  15.150  1.00 58.79           C  
ATOM    645  CD1 PHE A 287      11.502  25.393  14.075  1.00 59.54           C  
ATOM    646  CD2 PHE A 287      11.591  26.699  16.084  1.00 59.84           C  
ATOM    647  CE1 PHE A 287      10.141  25.697  13.933  1.00 60.67           C  
ATOM    648  CE2 PHE A 287      10.235  27.010  15.955  1.00 60.80           C  
ATOM    649  CZ  PHE A 287       9.507  26.506  14.875  1.00 61.16           C  
ATOM    650  N   ARG A 288      13.284  22.433  15.203  1.00 52.54           N  
ATOM    651  CA  ARG A 288      12.448  21.274  14.926  1.00 53.26           C  
ATOM    652  C   ARG A 288      12.447  20.340  16.143  1.00 53.24           C  
ATOM    653  O   ARG A 288      11.420  19.745  16.472  1.00 53.06           O  
ATOM    654  CB  ARG A 288      12.961  20.525  13.687  1.00 52.08           C  
ATOM    655  CG  ARG A 288      12.198  19.244  13.380  1.00 51.75           C  
ATOM    656  CD  ARG A 288      10.712  19.510  13.198  1.00 52.07           C  
ATOM    657  NE  ARG A 288       9.914  18.295  13.368  1.00 53.16           N  
ATOM    658  CZ  ARG A 288       8.734  18.265  13.982  1.00 53.57           C  
ATOM    659  NH1 ARG A 288       8.216  19.380  14.481  1.00 53.66           N  
ATOM    660  NH2 ARG A 288       8.075  17.123  14.116  1.00 52.03           N  
ATOM    661  N   SER A 289      13.596  20.222  16.813  1.00 52.11           N  
ATOM    662  CA  SER A 289      13.703  19.360  17.992  1.00 52.04           C  
ATOM    663  C   SER A 289      12.797  19.838  19.112  1.00 50.91           C  
ATOM    664  O   SER A 289      12.046  19.055  19.694  1.00 50.83           O  
ATOM    665  CB  SER A 289      15.145  19.305  18.501  1.00 51.66           C  
ATOM    666  OG  SER A 289      15.950  18.516  17.648  1.00 52.59           O  
ATOM    667  N   VAL A 290      12.880  21.127  19.416  1.00 50.94           N  
ATOM    668  CA  VAL A 290      12.056  21.712  20.465  1.00 53.29           C  
ATOM    669  C   VAL A 290      10.587  21.480  20.132  1.00 53.89           C  
ATOM    670  O   VAL A 290       9.742  21.336  21.020  1.00 55.32           O  
ATOM    671  CB  VAL A 290      12.335  23.233  20.603  1.00 52.24           C  
ATOM    672  CG1 VAL A 290      11.236  23.901  21.413  1.00 52.23           C  
ATOM    673  CG2 VAL A 290      13.689  23.446  21.289  1.00 53.09           C  
ATOM    674  N   GLU A 291      10.303  21.428  18.837  1.00 54.63           N  
ATOM    675  CA  GLU A 291       8.952  21.209  18.332  1.00 54.54           C  
ATOM    676  C   GLU A 291       8.570  19.727  18.525  1.00 52.75           C  
ATOM    677  O   GLU A 291       7.456  19.400  18.953  1.00 50.91           O  
ATOM    678  CB  GLU A 291       8.921  21.583  16.842  1.00 57.20           C  
ATOM    679  CG  GLU A 291       7.572  22.014  16.293  1.00 61.47           C  
ATOM    680  CD  GLU A 291       7.638  22.343  14.806  1.00 64.51           C  
ATOM    681  OE1 GLU A 291       8.495  23.169  14.416  1.00 65.95           O  
ATOM    682  OE2 GLU A 291       6.834  21.778  14.029  1.00 65.62           O  
ATOM    683  N   ALA A 292       9.503  18.835  18.202  1.00 50.07           N  
ATOM    684  CA  ALA A 292       9.265  17.406  18.346  1.00 48.60           C  
ATOM    685  C   ALA A 292       9.040  17.058  19.819  1.00 47.91           C  
ATOM    686  O   ALA A 292       8.314  16.119  20.143  1.00 46.85           O  
ATOM    687  CB  ALA A 292      10.447  16.621  17.787  1.00 47.40           C  
ATOM    688  N   VAL A 293       9.654  17.831  20.708  1.00 47.06           N  
ATOM    689  CA  VAL A 293       9.503  17.601  22.137  1.00 46.71           C  
ATOM    690  C   VAL A 293       8.062  17.862  22.567  1.00 46.53           C  
ATOM    691  O   VAL A 293       7.488  17.088  23.343  1.00 46.28           O  
ATOM    692  CB  VAL A 293      10.467  18.496  22.948  1.00 45.36           C  
ATOM    693  CG1 VAL A 293      10.231  18.316  24.439  1.00 46.80           C  
ATOM    694  CG2 VAL A 293      11.896  18.134  22.609  1.00 45.37           C  
ATOM    695  N   GLN A 294       7.468  18.942  22.062  1.00 45.85           N  
ATOM    696  CA  GLN A 294       6.083  19.250  22.419  1.00 44.65           C  
ATOM    697  C   GLN A 294       5.135  18.189  21.852  1.00 42.39           C  
ATOM    698  O   GLN A 294       4.148  17.815  22.488  1.00 43.01           O  
ATOM    699  CB  GLN A 294       5.693  20.642  21.912  1.00 47.90           C  
ATOM    700  CG  GLN A 294       4.259  21.042  22.266  1.00 50.48           C  
ATOM    701  CD  GLN A 294       3.947  20.875  23.750  1.00 54.14           C  
ATOM    702  OE1 GLN A 294       4.526  21.559  24.600  1.00 55.73           O  
ATOM    703  NE2 GLN A 294       3.031  19.958  24.068  1.00 52.33           N  
ATOM    704  N   GLU A 295       5.434  17.709  20.651  1.00 42.28           N  
ATOM    705  CA  GLU A 295       4.631  16.668  20.029  1.00 41.45           C  
ATOM    706  C   GLU A 295       4.732  15.375  20.841  1.00 40.55           C  
ATOM    707  O   GLU A 295       3.720  14.786  21.207  1.00 40.17           O  
ATOM    708  CB  GLU A 295       5.106  16.435  18.597  1.00 43.60           C  
ATOM    709  CG  GLU A 295       4.566  17.466  17.607  1.00 46.67           C  
ATOM    710  CD  GLU A 295       5.482  17.676  16.428  1.00 46.85           C  
ATOM    711  OE1 GLU A 295       5.999  16.671  15.897  1.00 47.17           O  
ATOM    712  OE2 GLU A 295       5.681  18.847  16.031  1.00 47.92           O  
ATOM    713  N   ILE A 296       5.955  14.943  21.132  1.00 39.93           N  
ATOM    714  CA  ILE A 296       6.158  13.720  21.908  1.00 38.41           C  
ATOM    715  C   ILE A 296       5.498  13.870  23.274  1.00 37.54           C  
ATOM    716  O   ILE A 296       4.904  12.920  23.801  1.00 36.53           O  
ATOM    717  CB  ILE A 296       7.664  13.421  22.084  1.00 38.03           C  
ATOM    718  CG1 ILE A 296       8.287  13.144  20.720  1.00 37.74           C  
ATOM    719  CG2 ILE A 296       7.866  12.221  23.007  1.00 39.08           C  
ATOM    720  CD1 ILE A 296       9.815  13.107  20.730  1.00 40.86           C  
ATOM    721  N   THR A 297       5.590  15.066  23.852  1.00 36.64           N  
ATOM    722  CA  THR A 297       4.974  15.297  25.151  1.00 37.91           C  
ATOM    723  C   THR A 297       3.462  15.138  25.038  1.00 39.02           C  
ATOM    724  O   THR A 297       2.815  14.588  25.935  1.00 37.71           O  
ATOM    725  CB  THR A 297       5.275  16.706  25.684  1.00 38.97           C  
ATOM    726  OG1 THR A 297       6.679  16.838  25.924  1.00 37.60           O  
ATOM    727  CG2 THR A 297       4.522  16.951  26.972  1.00 37.76           C  
ATOM    728  N   GLU A 298       2.892  15.614  23.932  1.00 39.56           N  
ATOM    729  CA  GLU A 298       1.451  15.489  23.751  1.00 38.71           C  
ATOM    730  C   GLU A 298       1.097  14.014  23.549  1.00 36.39           C  
ATOM    731  O   GLU A 298       0.067  13.547  24.019  1.00 34.54           O  
ATOM    732  CB  GLU A 298       0.975  16.311  22.543  1.00 43.32           C  
ATOM    733  CG  GLU A 298      -0.543  16.287  22.364  1.00 49.39           C  
ATOM    734  CD  GLU A 298      -0.975  16.341  20.900  1.00 53.46           C  
ATOM    735  OE1 GLU A 298      -0.916  17.426  20.285  1.00 54.96           O  
ATOM    736  OE2 GLU A 298      -1.366  15.282  20.360  1.00 56.68           O  
ATOM    737  N   TYR A 299       1.950  13.279  22.840  1.00 36.99           N  
ATOM    738  CA  TYR A 299       1.703  11.856  22.614  1.00 35.73           C  
ATOM    739  C   TYR A 299       1.764  11.097  23.945  1.00 34.55           C  
ATOM    740  O   TYR A 299       0.947  10.217  24.203  1.00 34.09           O  
ATOM    741  CB  TYR A 299       2.741  11.271  21.643  1.00 34.08           C  
ATOM    742  CG  TYR A 299       2.566   9.775  21.423  1.00 33.33           C  
ATOM    743  CD1 TYR A 299       1.420   9.274  20.803  1.00 30.75           C  
ATOM    744  CD2 TYR A 299       3.516   8.859  21.892  1.00 29.41           C  
ATOM    745  CE1 TYR A 299       1.215   7.900  20.657  1.00 30.86           C  
ATOM    746  CE2 TYR A 299       3.327   7.486  21.751  1.00 29.23           C  
ATOM    747  CZ  TYR A 299       2.174   7.006  21.134  1.00 33.92           C  
ATOM    748  OH  TYR A 299       1.973   5.635  21.003  1.00 33.50           O  
ATOM    749  N   ALA A 300       2.733  11.456  24.787  1.00 34.81           N  
ATOM    750  CA  ALA A 300       2.924  10.815  26.090  1.00 34.84           C  
ATOM    751  C   ALA A 300       1.651  10.827  26.920  1.00 34.65           C  
ATOM    752  O   ALA A 300       1.253   9.789  27.469  1.00 33.36           O  
ATOM    753  CB  ALA A 300       4.067  11.508  26.864  1.00 33.47           C  
ATOM    754  N   LYS A 301       1.004  11.993  26.989  1.00 33.19           N  
ATOM    755  CA  LYS A 301      -0.235  12.158  27.750  1.00 32.71           C  
ATOM    756  C   LYS A 301      -1.354  11.216  27.332  1.00 31.53           C  
ATOM    757  O   LYS A 301      -2.257  10.939  28.112  1.00 35.24           O  
ATOM    758  CB  LYS A 301      -0.708  13.613  27.659  1.00 36.79           C  
ATOM    759  CG  LYS A 301       0.319  14.594  28.192  1.00 40.89           C  
ATOM    760  CD  LYS A 301       0.121  16.003  27.651  1.00 46.77           C  
ATOM    761  CE  LYS A 301      -1.087  16.693  28.262  1.00 47.94           C  
ATOM    762  NZ  LYS A 301      -1.211  18.084  27.738  1.00 51.41           N  
ATOM    763  N   SER A 302      -1.304  10.717  26.106  1.00 30.93           N  
ATOM    764  CA  SER A 302      -2.316   9.786  25.632  1.00 30.93           C  
ATOM    765  C   SER A 302      -2.050   8.337  26.055  1.00 32.43           C  
ATOM    766  O   SER A 302      -2.939   7.482  25.940  1.00 32.22           O  
ATOM    767  CB  SER A 302      -2.384   9.835  24.115  1.00 31.19           C  
ATOM    768  OG  SER A 302      -1.161   9.378  23.562  1.00 35.14           O  
ATOM    769  N   ILE A 303      -0.832   8.048  26.515  1.00 32.38           N  
ATOM    770  CA  ILE A 303      -0.490   6.684  26.935  1.00 32.69           C  
ATOM    771  C   ILE A 303      -1.194   6.383  28.244  1.00 32.27           C  
ATOM    772  O   ILE A 303      -0.910   6.994  29.263  1.00 32.95           O  
ATOM    773  CB  ILE A 303       1.033   6.510  27.130  1.00 33.24           C  
ATOM    774  CG1 ILE A 303       1.764   6.846  25.826  1.00 30.23           C  
ATOM    775  CG2 ILE A 303       1.345   5.056  27.531  1.00 33.41           C  
ATOM    776  CD1 ILE A 303       3.283   6.783  25.927  1.00 33.44           C  
ATOM    777  N   PRO A 304      -2.132   5.433  28.230  1.00 30.99           N  
ATOM    778  CA  PRO A 304      -2.865   5.091  29.442  1.00 31.85           C  
ATOM    779  C   PRO A 304      -1.985   4.993  30.678  1.00 31.64           C  
ATOM    780  O   PRO A 304      -0.938   4.338  30.675  1.00 28.61           O  
ATOM    781  CB  PRO A 304      -3.534   3.774  29.071  1.00 33.46           C  
ATOM    782  CG  PRO A 304      -3.857   3.994  27.629  1.00 33.56           C  
ATOM    783  CD  PRO A 304      -2.553   4.578  27.110  1.00 31.41           C  
ATOM    784  N   GLY A 305      -2.430   5.672  31.723  1.00 29.34           N  
ATOM    785  CA  GLY A 305      -1.710   5.691  32.969  1.00 32.84           C  
ATOM    786  C   GLY A 305      -0.623   6.738  33.064  1.00 31.54           C  
ATOM    787  O   GLY A 305      -0.261   7.132  34.164  1.00 34.24           O  
ATOM    788  N   PHE A 306      -0.092   7.203  31.944  1.00 29.92           N  
ATOM    789  CA  PHE A 306       0.980   8.184  32.039  1.00 31.74           C  
ATOM    790  C   PHE A 306       0.680   9.428  32.893  1.00 34.38           C  
ATOM    791  O   PHE A 306       1.467   9.781  33.774  1.00 35.25           O  
ATOM    792  CB  PHE A 306       1.428   8.643  30.655  1.00 28.10           C  
ATOM    793  CG  PHE A 306       2.628   9.541  30.693  1.00 32.19           C  
ATOM    794  CD1 PHE A 306       3.911   9.004  30.807  1.00 33.05           C  
ATOM    795  CD2 PHE A 306       2.479  10.924  30.724  1.00 28.76           C  
ATOM    796  CE1 PHE A 306       5.011   9.826  30.958  1.00 31.48           C  
ATOM    797  CE2 PHE A 306       3.576  11.750  30.873  1.00 29.78           C  
ATOM    798  CZ  PHE A 306       4.847  11.203  30.993  1.00 31.07           C  
ATOM    799  N   VAL A 307      -0.445  10.097  32.639  1.00 34.28           N  
ATOM    800  CA  VAL A 307      -0.767  11.306  33.380  1.00 35.03           C  
ATOM    801  C   VAL A 307      -1.195  11.068  34.820  1.00 34.85           C  
ATOM    802  O   VAL A 307      -1.303  12.017  35.589  1.00 31.82           O  
ATOM    803  CB  VAL A 307      -1.853  12.157  32.657  1.00 35.89           C  
ATOM    804  CG1 VAL A 307      -1.289  12.709  31.372  1.00 37.97           C  
ATOM    805  CG2 VAL A 307      -3.099  11.327  32.388  1.00 35.48           C  
ATOM    806  N   ASN A 308      -1.431   9.808  35.185  1.00 35.81           N  
ATOM    807  CA  ASN A 308      -1.817   9.472  36.553  1.00 35.76           C  
ATOM    808  C   ASN A 308      -0.582   9.255  37.434  1.00 37.15           C  
ATOM    809  O   ASN A 308      -0.706   9.086  38.640  1.00 38.93           O  
ATOM    810  CB  ASN A 308      -2.657   8.189  36.596  1.00 38.79           C  
ATOM    811  CG  ASN A 308      -3.939   8.303  35.824  1.00 38.35           C  
ATOM    812  OD1 ASN A 308      -4.796   9.139  36.128  1.00 42.44           O  
ATOM    813  ND2 ASN A 308      -4.089   7.464  34.819  1.00 39.52           N  
ATOM    814  N   LEU A 309       0.600   9.252  36.830  1.00 37.62           N  
ATOM    815  CA  LEU A 309       1.844   9.046  37.565  1.00 38.59           C  
ATOM    816  C   LEU A 309       2.308  10.338  38.230  1.00 41.61           C  
ATOM    817  O   LEU A 309       1.864  11.429  37.870  1.00 41.93           O  
ATOM    818  CB  LEU A 309       2.957   8.563  36.619  1.00 34.42           C  
ATOM    819  CG  LEU A 309       2.827   7.202  35.924  1.00 37.24           C  
ATOM    820  CD1 LEU A 309       3.950   7.031  34.912  1.00 36.50           C  
ATOM    821  CD2 LEU A 309       2.869   6.087  36.953  1.00 34.71           C  
ATOM    822  N   ASP A 310       3.214  10.191  39.195  1.00 42.88           N  
ATOM    823  CA  ASP A 310       3.813  11.309  39.920  1.00 43.74           C  
ATOM    824  C   ASP A 310       4.312  12.318  38.894  1.00 42.46           C  
ATOM    825  O   ASP A 310       4.966  11.956  37.916  1.00 44.01           O  
ATOM    826  CB  ASP A 310       5.002  10.818  40.755  1.00 43.82           C  
ATOM    827  CG  ASP A 310       5.504  11.866  41.738  1.00 48.54           C  
ATOM    828  OD1 ASP A 310       4.983  11.933  42.876  1.00 50.45           O  
ATOM    829  OD2 ASP A 310       6.416  12.634  41.371  1.00 50.62           O  
ATOM    830  N   LEU A 311       4.023  13.587  39.124  1.00 42.66           N  
ATOM    831  CA  LEU A 311       4.440  14.615  38.191  1.00 44.44           C  
ATOM    832  C   LEU A 311       5.940  14.588  37.944  1.00 45.23           C  
ATOM    833  O   LEU A 311       6.392  14.700  36.805  1.00 46.40           O  
ATOM    834  CB  LEU A 311       4.013  15.988  38.703  1.00 44.80           C  
ATOM    835  CG  LEU A 311       4.378  17.164  37.796  1.00 45.79           C  
ATOM    836  CD1 LEU A 311       3.463  18.342  38.091  1.00 46.11           C  
ATOM    837  CD2 LEU A 311       5.837  17.535  38.013  1.00 46.27           C  
ATOM    838  N   ASN A 312       6.715  14.441  39.010  1.00 45.37           N  
ATOM    839  CA  ASN A 312       8.163  14.413  38.886  1.00 44.51           C  
ATOM    840  C   ASN A 312       8.599  13.277  37.972  1.00 43.17           C  
ATOM    841  O   ASN A 312       9.528  13.422  37.183  1.00 43.48           O  
ATOM    842  CB  ASN A 312       8.795  14.242  40.270  1.00 48.27           C  
ATOM    843  CG  ASN A 312       8.397  15.346  41.231  1.00 50.72           C  
ATOM    844  OD1 ASN A 312       8.794  16.503  41.066  1.00 53.79           O  
ATOM    845  ND2 ASN A 312       7.600  14.998  42.236  1.00 50.90           N  
ATOM    846  N   ASP A 313       7.925  12.139  38.079  1.00 41.71           N  
ATOM    847  CA  ASP A 313       8.270  10.998  37.251  1.00 40.63           C  
ATOM    848  C   ASP A 313       7.875  11.218  35.789  1.00 40.02           C  
ATOM    849  O   ASP A 313       8.597  10.802  34.885  1.00 39.85           O  
ATOM    850  CB  ASP A 313       7.626   9.727  37.811  1.00 39.58           C  
ATOM    851  CG  ASP A 313       8.360   9.194  39.037  1.00 40.72           C  
ATOM    852  OD1 ASP A 313       9.485   9.667  39.317  1.00 39.82           O  
ATOM    853  OD2 ASP A 313       7.820   8.294  39.712  1.00 39.16           O  
ATOM    854  N   GLN A 314       6.736  11.873  35.565  1.00 39.66           N  
ATOM    855  CA  GLN A 314       6.281  12.175  34.210  1.00 40.03           C  
ATOM    856  C   GLN A 314       7.384  13.006  33.576  1.00 40.25           C  
ATOM    857  O   GLN A 314       7.821  12.749  32.452  1.00 39.62           O  
ATOM    858  CB  GLN A 314       4.975  12.995  34.225  1.00 38.91           C  
ATOM    859  CG  GLN A 314       3.748  12.272  34.796  1.00 38.22           C  
ATOM    860  CD  GLN A 314       2.466  13.107  34.715  1.00 40.20           C  
ATOM    861  OE1 GLN A 314       1.649  13.102  35.638  1.00 40.74           O  
ATOM    862  NE2 GLN A 314       2.280  13.810  33.603  1.00 36.85           N  
ATOM    863  N   VAL A 315       7.835  14.011  34.313  1.00 41.45           N  
ATOM    864  CA  VAL A 315       8.901  14.877  33.833  1.00 42.25           C  
ATOM    865  C   VAL A 315      10.174  14.078  33.546  1.00 41.79           C  
ATOM    866  O   VAL A 315      10.797  14.234  32.492  1.00 42.66           O  
ATOM    867  CB  VAL A 315       9.182  15.991  34.862  1.00 42.91           C  
ATOM    868  CG1 VAL A 315      10.518  16.667  34.576  1.00 42.80           C  
ATOM    869  CG2 VAL A 315       8.046  17.020  34.804  1.00 43.92           C  
ATOM    870  N   THR A 316      10.546  13.206  34.474  1.00 41.34           N  
ATOM    871  CA  THR A 316      11.748  12.397  34.304  1.00 42.17           C  
ATOM    872  C   THR A 316      11.650  11.434  33.117  1.00 39.55           C  
ATOM    873  O   THR A 316      12.628  11.214  32.405  1.00 39.94           O  
ATOM    874  CB  THR A 316      12.076  11.614  35.610  1.00 41.73           C  
ATOM    875  OG1 THR A 316      12.505  12.545  36.610  1.00 43.10           O  
ATOM    876  CG2 THR A 316      13.187  10.593  35.387  1.00 40.77           C  
ATOM    877  N   LEU A 317      10.474  10.859  32.903  1.00 39.74           N  
ATOM    878  CA  LEU A 317      10.310   9.944  31.785  1.00 38.35           C  
ATOM    879  C   LEU A 317      10.475  10.700  30.476  1.00 38.21           C  
ATOM    880  O   LEU A 317      11.092  10.198  29.529  1.00 37.32           O  
ATOM    881  CB  LEU A 317       8.940   9.276  31.843  1.00 37.28           C  
ATOM    882  CG  LEU A 317       8.758   8.317  33.025  1.00 38.40           C  
ATOM    883  CD1 LEU A 317       7.360   7.741  32.965  1.00 37.23           C  
ATOM    884  CD2 LEU A 317       9.817   7.190  32.975  1.00 33.92           C  
ATOM    885  N   LEU A 318       9.939  11.917  30.418  1.00 38.03           N  
ATOM    886  CA  LEU A 318      10.057  12.712  29.194  1.00 38.19           C  
ATOM    887  C   LEU A 318      11.488  13.150  28.966  1.00 36.78           C  
ATOM    888  O   LEU A 318      12.015  13.028  27.864  1.00 35.99           O  
ATOM    889  CB  LEU A 318       9.140  13.938  29.251  1.00 36.10           C  
ATOM    890  CG  LEU A 318       7.668  13.605  29.009  1.00 37.82           C  
ATOM    891  CD1 LEU A 318       6.783  14.775  29.456  1.00 38.19           C  
ATOM    892  CD2 LEU A 318       7.468  13.287  27.516  1.00 37.47           C  
ATOM    893  N   LYS A 319      12.111  13.664  30.018  1.00 40.14           N  
ATOM    894  CA  LYS A 319      13.490  14.138  29.959  1.00 42.46           C  
ATOM    895  C   LYS A 319      14.458  13.113  29.351  1.00 42.43           C  
ATOM    896  O   LYS A 319      15.301  13.453  28.521  1.00 42.30           O  
ATOM    897  CB  LYS A 319      13.949  14.517  31.368  1.00 44.35           C  
ATOM    898  CG  LYS A 319      15.416  14.864  31.475  1.00 46.59           C  
ATOM    899  CD  LYS A 319      15.866  14.863  32.928  1.00 50.18           C  
ATOM    900  CE  LYS A 319      17.360  15.112  33.031  1.00 50.85           C  
ATOM    901  NZ  LYS A 319      17.737  16.404  32.384  1.00 53.87           N  
ATOM    902  N   TYR A 320      14.328  11.858  29.760  1.00 44.41           N  
ATOM    903  CA  TYR A 320      15.205  10.807  29.254  1.00 46.00           C  
ATOM    904  C   TYR A 320      14.673  10.090  28.034  1.00 45.56           C  
ATOM    905  O   TYR A 320      15.435   9.409  27.348  1.00 46.20           O  
ATOM    906  CB  TYR A 320      15.475   9.751  30.330  1.00 47.95           C  
ATOM    907  CG  TYR A 320      16.395  10.213  31.428  1.00 49.38           C  
ATOM    908  CD1 TYR A 320      15.886  10.719  32.622  1.00 49.63           C  
ATOM    909  CD2 TYR A 320      17.783  10.145  31.271  1.00 50.31           C  
ATOM    910  CE1 TYR A 320      16.733  11.144  33.638  1.00 51.91           C  
ATOM    911  CE2 TYR A 320      18.641  10.569  32.278  1.00 51.48           C  
ATOM    912  CZ  TYR A 320      18.110  11.066  33.461  1.00 52.22           C  
ATOM    913  OH  TYR A 320      18.954  11.479  34.465  1.00 53.27           O  
ATOM    914  N   GLY A 321      13.380  10.233  27.757  1.00 43.50           N  
ATOM    915  CA  GLY A 321      12.811   9.532  26.614  1.00 43.20           C  
ATOM    916  C   GLY A 321      12.740  10.283  25.300  1.00 42.05           C  
ATOM    917  O   GLY A 321      12.901   9.699  24.232  1.00 41.73           O  
ATOM    918  N   VAL A 322      12.503  11.583  25.383  1.00 42.66           N  
ATOM    919  CA  VAL A 322      12.376  12.430  24.204  1.00 42.61           C  
ATOM    920  C   VAL A 322      13.438  12.243  23.125  1.00 42.05           C  
ATOM    921  O   VAL A 322      13.107  12.000  21.964  1.00 39.56           O  
ATOM    922  CB  VAL A 322      12.318  13.927  24.620  1.00 43.51           C  
ATOM    923  CG1 VAL A 322      12.631  14.824  23.433  1.00 46.30           C  
ATOM    924  CG2 VAL A 322      10.925  14.253  25.162  1.00 44.27           C  
ATOM    925  N   HIS A 323      14.712  12.349  23.488  1.00 42.37           N  
ATOM    926  CA  HIS A 323      15.744  12.201  22.474  1.00 42.37           C  
ATOM    927  C   HIS A 323      15.837  10.824  21.860  1.00 40.60           C  
ATOM    928  O   HIS A 323      16.214  10.693  20.703  1.00 41.21           O  
ATOM    929  CB  HIS A 323      17.102  12.643  23.001  1.00 46.15           C  
ATOM    930  CG  HIS A 323      17.371  14.094  22.772  1.00 48.11           C  
ATOM    931  ND1 HIS A 323      16.972  15.073  23.655  1.00 51.72           N  
ATOM    932  CD2 HIS A 323      17.901  14.739  21.708  1.00 51.34           C  
ATOM    933  CE1 HIS A 323      17.241  16.261  23.142  1.00 51.87           C  
ATOM    934  NE2 HIS A 323      17.806  16.086  21.961  1.00 54.11           N  
ATOM    935  N   GLU A 324      15.486   9.797  22.620  1.00 39.74           N  
ATOM    936  CA  GLU A 324      15.513   8.437  22.093  1.00 39.74           C  
ATOM    937  C   GLU A 324      14.376   8.268  21.079  1.00 38.75           C  
ATOM    938  O   GLU A 324      14.518   7.566  20.073  1.00 37.45           O  
ATOM    939  CB  GLU A 324      15.381   7.428  23.239  1.00 41.12           C  
ATOM    940  CG  GLU A 324      16.712   7.161  23.954  1.00 43.07           C  
ATOM    941  CD  GLU A 324      16.561   6.394  25.255  1.00 42.76           C  
ATOM    942  OE1 GLU A 324      15.547   5.695  25.438  1.00 45.85           O  
ATOM    943  OE2 GLU A 324      17.475   6.476  26.100  1.00 46.23           O  
ATOM    944  N   ILE A 325      13.246   8.914  21.355  1.00 37.81           N  
ATOM    945  CA  ILE A 325      12.095   8.874  20.461  1.00 34.88           C  
ATOM    946  C   ILE A 325      12.422   9.660  19.198  1.00 33.66           C  
ATOM    947  O   ILE A 325      12.117   9.227  18.088  1.00 34.59           O  
ATOM    948  CB  ILE A 325      10.846   9.466  21.155  1.00 35.00           C  
ATOM    949  CG1 ILE A 325      10.352   8.475  22.207  1.00 34.61           C  
ATOM    950  CG2 ILE A 325       9.743   9.786  20.125  1.00 32.02           C  
ATOM    951  CD1 ILE A 325       9.207   8.986  23.061  1.00 37.51           C  
ATOM    952  N   ILE A 326      13.074  10.805  19.369  1.00 33.68           N  
ATOM    953  CA  ILE A 326      13.437  11.643  18.237  1.00 34.81           C  
ATOM    954  C   ILE A 326      14.295  10.913  17.203  1.00 35.57           C  
ATOM    955  O   ILE A 326      14.050  11.020  15.999  1.00 35.30           O  
ATOM    956  CB  ILE A 326      14.173  12.944  18.709  1.00 34.05           C  
ATOM    957  CG1 ILE A 326      13.152  13.961  19.234  1.00 35.99           C  
ATOM    958  CG2 ILE A 326      14.989  13.535  17.562  1.00 31.28           C  
ATOM    959  CD1 ILE A 326      13.771  15.295  19.728  1.00 34.51           C  
ATOM    960  N   TYR A 327      15.304  10.174  17.659  1.00 36.06           N  
ATOM    961  CA  TYR A 327      16.159   9.456  16.720  1.00 37.05           C  
ATOM    962  C   TYR A 327      15.440   8.263  16.114  1.00 32.87           C  
ATOM    963  O   TYR A 327      15.710   7.891  14.980  1.00 32.25           O  
ATOM    964  CB  TYR A 327      17.457   9.020  17.407  1.00 40.16           C  
ATOM    965  CG  TYR A 327      18.284  10.203  17.841  1.00 47.22           C  
ATOM    966  CD1 TYR A 327      18.705  11.157  16.915  1.00 49.96           C  
ATOM    967  CD2 TYR A 327      18.617  10.395  19.181  1.00 50.60           C  
ATOM    968  CE1 TYR A 327      19.433  12.271  17.313  1.00 53.68           C  
ATOM    969  CE2 TYR A 327      19.346  11.507  19.589  1.00 53.09           C  
ATOM    970  CZ  TYR A 327      19.750  12.439  18.648  1.00 54.56           C  
ATOM    971  OH  TYR A 327      20.486  13.539  19.039  1.00 60.22           O  
ATOM    972  N   THR A 328      14.519   7.669  16.861  1.00 30.62           N  
ATOM    973  CA  THR A 328      13.756   6.534  16.331  1.00 33.70           C  
ATOM    974  C   THR A 328      12.853   6.993  15.185  1.00 32.55           C  
ATOM    975  O   THR A 328      12.730   6.323  14.164  1.00 32.64           O  
ATOM    976  CB  THR A 328      12.844   5.902  17.400  1.00 33.04           C  
ATOM    977  OG1 THR A 328      13.646   5.321  18.432  1.00 38.90           O  
ATOM    978  CG2 THR A 328      11.976   4.826  16.790  1.00 32.81           C  
ATOM    979  N   MET A 329      12.212   8.140  15.368  1.00 33.69           N  
ATOM    980  CA  MET A 329      11.315   8.662  14.353  1.00 33.50           C  
ATOM    981  C   MET A 329      12.070   9.293  13.208  1.00 33.57           C  
ATOM    982  O   MET A 329      11.632   9.233  12.064  1.00 34.59           O  
ATOM    983  CB  MET A 329      10.332   9.638  14.996  1.00 34.41           C  
ATOM    984  CG  MET A 329       9.326   8.897  15.855  1.00 31.68           C  
ATOM    985  SD  MET A 329       8.089   9.922  16.587  1.00 41.31           S  
ATOM    986  CE  MET A 329       6.894  10.094  15.230  1.00 39.29           C  
ATOM    987  N   LEU A 330      13.225   9.872  13.513  1.00 34.36           N  
ATOM    988  CA  LEU A 330      14.063  10.485  12.491  1.00 33.40           C  
ATOM    989  C   LEU A 330      14.436   9.446  11.419  1.00 33.60           C  
ATOM    990  O   LEU A 330      14.632   9.785  10.248  1.00 32.51           O  
ATOM    991  CB  LEU A 330      15.330  11.040  13.137  1.00 35.44           C  
ATOM    992  CG  LEU A 330      16.375  11.565  12.168  1.00 36.43           C  
ATOM    993  CD1 LEU A 330      15.833  12.833  11.528  1.00 39.67           C  
ATOM    994  CD2 LEU A 330      17.695  11.808  12.889  1.00 39.76           C  
ATOM    995  N   ALA A 331      14.537   8.182  11.827  1.00 32.70           N  
ATOM    996  CA  ALA A 331      14.875   7.093  10.897  1.00 32.54           C  
ATOM    997  C   ALA A 331      13.797   6.982   9.821  1.00 31.27           C  
ATOM    998  O   ALA A 331      14.082   6.606   8.698  1.00 31.19           O  
ATOM    999  CB  ALA A 331      14.997   5.747  11.655  1.00 29.78           C  
ATOM   1000  N   SER A 332      12.559   7.310  10.179  1.00 32.99           N  
ATOM   1001  CA  SER A 332      11.449   7.252   9.225  1.00 34.97           C  
ATOM   1002  C   SER A 332      11.668   8.219   8.079  1.00 34.47           C  
ATOM   1003  O   SER A 332      11.197   7.992   6.973  1.00 35.67           O  
ATOM   1004  CB  SER A 332      10.135   7.615   9.902  1.00 34.49           C  
ATOM   1005  OG  SER A 332       9.818   6.710  10.926  1.00 36.95           O  
ATOM   1006  N   LEU A 333      12.397   9.297   8.350  1.00 36.28           N  
ATOM   1007  CA  LEU A 333      12.651  10.314   7.341  1.00 36.22           C  
ATOM   1008  C   LEU A 333      13.954  10.102   6.595  1.00 36.11           C  
ATOM   1009  O   LEU A 333      14.316  10.913   5.750  1.00 38.74           O  
ATOM   1010  CB  LEU A 333      12.694  11.696   7.994  1.00 37.27           C  
ATOM   1011  CG  LEU A 333      11.644  12.005   9.056  1.00 38.36           C  
ATOM   1012  CD1 LEU A 333      11.756  13.464   9.484  1.00 37.91           C  
ATOM   1013  CD2 LEU A 333      10.269  11.717   8.511  1.00 39.36           C  
ATOM   1014  N   MET A 334      14.655   9.015   6.895  1.00 36.25           N  
ATOM   1015  CA  MET A 334      15.943   8.746   6.263  1.00 36.23           C  
ATOM   1016  C   MET A 334      16.071   7.509   5.364  1.00 34.90           C  
ATOM   1017  O   MET A 334      15.328   6.547   5.476  1.00 35.69           O  
ATOM   1018  CB  MET A 334      17.026   8.617   7.350  1.00 34.43           C  
ATOM   1019  CG  MET A 334      17.091   9.747   8.357  1.00 37.30           C  
ATOM   1020  SD  MET A 334      18.314   9.410   9.656  1.00 38.21           S  
ATOM   1021  CE  MET A 334      19.361  10.885   9.515  1.00 38.81           C  
ATOM   1022  N   ASN A 335      17.046   7.570   4.468  1.00 37.36           N  
ATOM   1023  CA  ASN A 335      17.422   6.451   3.617  1.00 38.95           C  
ATOM   1024  C   ASN A 335      18.928   6.634   3.549  1.00 41.44           C  
ATOM   1025  O   ASN A 335      19.456   7.591   4.122  1.00 40.64           O  
ATOM   1026  CB  ASN A 335      16.784   6.479   2.214  1.00 38.36           C  
ATOM   1027  CG  ASN A 335      17.085   7.732   1.438  1.00 40.20           C  
ATOM   1028  OD1 ASN A 335      18.110   8.392   1.632  1.00 40.15           O  
ATOM   1029  ND2 ASN A 335      16.186   8.060   0.519  1.00 41.21           N  
ATOM   1030  N   LYS A 336      19.625   5.732   2.877  1.00 42.76           N  
ATOM   1031  CA  LYS A 336      21.077   5.817   2.783  1.00 44.83           C  
ATOM   1032  C   LYS A 336      21.626   7.113   2.198  1.00 45.20           C  
ATOM   1033  O   LYS A 336      22.768   7.484   2.484  1.00 45.85           O  
ATOM   1034  CB  LYS A 336      21.608   4.645   1.956  1.00 47.97           C  
ATOM   1035  CG  LYS A 336      22.100   3.474   2.782  1.00 49.29           C  
ATOM   1036  CD  LYS A 336      23.372   3.863   3.524  1.00 53.88           C  
ATOM   1037  CE  LYS A 336      23.981   2.707   4.298  1.00 53.98           C  
ATOM   1038  NZ  LYS A 336      25.068   3.203   5.191  1.00 54.74           N  
ATOM   1039  N   ASP A 337      20.825   7.804   1.389  1.00 44.23           N  
ATOM   1040  CA  ASP A 337      21.285   9.030   0.737  1.00 42.79           C  
ATOM   1041  C   ASP A 337      20.974  10.349   1.421  1.00 40.58           C  
ATOM   1042  O   ASP A 337      21.535  11.377   1.045  1.00 39.91           O  
ATOM   1043  CB  ASP A 337      20.730   9.112  -0.688  1.00 45.43           C  
ATOM   1044  CG  ASP A 337      20.928   7.833  -1.471  1.00 48.16           C  
ATOM   1045  OD1 ASP A 337      22.063   7.306  -1.479  1.00 47.65           O  
ATOM   1046  OD2 ASP A 337      19.945   7.365  -2.086  1.00 50.42           O  
ATOM   1047  N   GLY A 338      20.066  10.349   2.389  1.00 39.91           N  
ATOM   1048  CA  GLY A 338      19.750  11.611   3.029  1.00 38.55           C  
ATOM   1049  C   GLY A 338      18.534  11.609   3.922  1.00 38.04           C  
ATOM   1050  O   GLY A 338      17.995  10.550   4.272  1.00 38.79           O  
ATOM   1051  N   VAL A 339      18.092  12.813   4.276  1.00 34.83           N  
ATOM   1052  CA  VAL A 339      16.964  12.975   5.173  1.00 33.55           C  
ATOM   1053  C   VAL A 339      15.995  14.063   4.739  1.00 35.11           C  
ATOM   1054  O   VAL A 339      16.404  15.122   4.255  1.00 35.61           O  
ATOM   1055  CB  VAL A 339      17.480  13.291   6.612  1.00 31.57           C  
ATOM   1056  CG1 VAL A 339      18.276  14.577   6.609  1.00 29.10           C  
ATOM   1057  CG2 VAL A 339      16.327  13.390   7.586  1.00 25.40           C  
ATOM   1058  N   LEU A 340      14.704  13.793   4.915  1.00 35.99           N  
ATOM   1059  CA  LEU A 340      13.658  14.751   4.569  1.00 35.55           C  
ATOM   1060  C   LEU A 340      13.671  15.881   5.581  1.00 36.36           C  
ATOM   1061  O   LEU A 340      13.924  15.646   6.758  1.00 35.24           O  
ATOM   1062  CB  LEU A 340      12.285  14.083   4.623  1.00 35.77           C  
ATOM   1063  CG  LEU A 340      11.985  13.119   3.478  1.00 37.28           C  
ATOM   1064  CD1 LEU A 340      10.682  12.393   3.759  1.00 37.96           C  
ATOM   1065  CD2 LEU A 340      11.913  13.900   2.174  1.00 37.16           C  
ATOM   1066  N   ILE A 341      13.394  17.099   5.127  1.00 36.65           N  
ATOM   1067  CA  ILE A 341      13.350  18.251   6.021  1.00 37.87           C  
ATOM   1068  C   ILE A 341      12.106  19.101   5.753  1.00 39.20           C  
ATOM   1069  O   ILE A 341      11.451  18.959   4.715  1.00 35.85           O  
ATOM   1070  CB  ILE A 341      14.610  19.145   5.892  1.00 40.01           C  
ATOM   1071  CG1 ILE A 341      14.646  19.847   4.534  1.00 41.06           C  
ATOM   1072  CG2 ILE A 341      15.862  18.303   6.089  1.00 40.27           C  
ATOM   1073  CD1 ILE A 341      15.726  20.935   4.446  1.00 41.47           C  
ATOM   1074  N   SER A 342      11.794  19.977   6.706  1.00 39.73           N  
ATOM   1075  CA  SER A 342      10.636  20.860   6.647  1.00 40.77           C  
ATOM   1076  C   SER A 342       9.385  20.168   6.131  1.00 40.57           C  
ATOM   1077  O   SER A 342       8.942  20.415   5.003  1.00 39.83           O  
ATOM   1078  CB  SER A 342      10.936  22.078   5.783  1.00 40.11           C  
ATOM   1079  OG  SER A 342      11.200  21.692   4.456  1.00 49.89           O  
ATOM   1080  N   GLU A 343       8.824  19.302   6.967  1.00 40.66           N  
ATOM   1081  CA  GLU A 343       7.604  18.559   6.636  1.00 44.78           C  
ATOM   1082  C   GLU A 343       7.680  17.704   5.363  1.00 43.13           C  
ATOM   1083  O   GLU A 343       6.653  17.319   4.809  1.00 46.04           O  
ATOM   1084  CB  GLU A 343       6.421  19.524   6.516  1.00 48.01           C  
ATOM   1085  CG  GLU A 343       6.136  20.341   7.772  1.00 54.21           C  
ATOM   1086  CD  GLU A 343       5.283  21.579   7.486  1.00 57.56           C  
ATOM   1087  OE1 GLU A 343       5.816  22.547   6.896  1.00 58.79           O  
ATOM   1088  OE2 GLU A 343       4.081  21.580   7.842  1.00 60.13           O  
ATOM   1089  N   GLY A 344       8.888  17.408   4.900  1.00 42.19           N  
ATOM   1090  CA  GLY A 344       9.036  16.585   3.715  1.00 39.89           C  
ATOM   1091  C   GLY A 344       9.126  17.317   2.386  1.00 38.37           C  
ATOM   1092  O   GLY A 344       9.187  16.670   1.339  1.00 37.05           O  
ATOM   1093  N   GLN A 345       9.135  18.650   2.414  1.00 37.83           N  
ATOM   1094  CA  GLN A 345       9.226  19.441   1.186  1.00 37.55           C  
ATOM   1095  C   GLN A 345      10.668  19.495   0.715  1.00 36.79           C  
ATOM   1096  O   GLN A 345      10.940  19.813  -0.442  1.00 37.78           O  
ATOM   1097  CB  GLN A 345       8.744  20.868   1.409  1.00 37.37           C  
ATOM   1098  CG  GLN A 345       7.389  20.990   2.046  1.00 42.23           C  
ATOM   1099  CD  GLN A 345       7.096  22.423   2.424  1.00 44.77           C  
ATOM   1100  OE1 GLN A 345       6.899  23.272   1.559  1.00 47.75           O  
ATOM   1101  NE2 GLN A 345       7.092  22.705   3.721  1.00 44.81           N  
ATOM   1102  N   GLY A 346      11.595  19.185   1.616  1.00 34.64           N  
ATOM   1103  CA  GLY A 346      12.995  19.205   1.243  1.00 32.56           C  
ATOM   1104  C   GLY A 346      13.679  17.880   1.541  1.00 34.84           C  
ATOM   1105  O   GLY A 346      13.139  17.022   2.235  1.00 33.58           O  
ATOM   1106  N   PHE A 347      14.870  17.705   0.988  1.00 35.31           N  
ATOM   1107  CA  PHE A 347      15.652  16.503   1.229  1.00 37.55           C  
ATOM   1108  C   PHE A 347      17.097  16.955   1.223  1.00 37.48           C  
ATOM   1109  O   PHE A 347      17.581  17.472   0.224  1.00 38.84           O  
ATOM   1110  CB  PHE A 347      15.428  15.471   0.128  1.00 36.44           C  
ATOM   1111  CG  PHE A 347      16.175  14.182   0.340  1.00 35.96           C  
ATOM   1112  CD1 PHE A 347      15.672  13.200   1.195  1.00 34.92           C  
ATOM   1113  CD2 PHE A 347      17.357  13.926  -0.357  1.00 34.77           C  
ATOM   1114  CE1 PHE A 347      16.327  11.979   1.345  1.00 34.77           C  
ATOM   1115  CE2 PHE A 347      18.021  12.708  -0.215  1.00 35.31           C  
ATOM   1116  CZ  PHE A 347      17.504  11.728   0.636  1.00 34.80           C  
ATOM   1117  N   MET A 348      17.777  16.772   2.348  1.00 39.76           N  
ATOM   1118  CA  MET A 348      19.174  17.174   2.466  1.00 41.09           C  
ATOM   1119  C   MET A 348      20.054  15.930   2.395  1.00 41.10           C  
ATOM   1120  O   MET A 348      19.924  15.006   3.208  1.00 41.16           O  
ATOM   1121  CB  MET A 348      19.383  17.927   3.789  1.00 43.53           C  
ATOM   1122  CG  MET A 348      20.687  18.703   3.884  1.00 47.44           C  
ATOM   1123  SD  MET A 348      20.650  19.931   5.214  1.00 52.31           S  
ATOM   1124  CE  MET A 348      19.986  21.350   4.345  1.00 49.87           C  
ATOM   1125  N   THR A 349      20.945  15.917   1.410  1.00 40.36           N  
ATOM   1126  CA  THR A 349      21.836  14.791   1.183  1.00 42.11           C  
ATOM   1127  C   THR A 349      22.747  14.461   2.366  1.00 41.14           C  
ATOM   1128  O   THR A 349      23.200  15.351   3.084  1.00 39.68           O  
ATOM   1129  CB  THR A 349      22.694  15.041  -0.074  1.00 43.54           C  
ATOM   1130  OG1 THR A 349      21.839  15.092  -1.231  1.00 47.34           O  
ATOM   1131  CG2 THR A 349      23.699  13.928  -0.257  1.00 47.14           C  
ATOM   1132  N   ARG A 350      22.998  13.168   2.553  1.00 40.12           N  
ATOM   1133  CA  ARG A 350      23.855  12.670   3.619  1.00 42.58           C  
ATOM   1134  C   ARG A 350      25.290  13.150   3.426  1.00 44.77           C  
ATOM   1135  O   ARG A 350      25.995  13.426   4.399  1.00 44.39           O  
ATOM   1136  CB  ARG A 350      23.841  11.143   3.626  1.00 42.68           C  
ATOM   1137  CG  ARG A 350      24.839  10.504   4.577  1.00 41.40           C  
ATOM   1138  CD  ARG A 350      24.777   8.996   4.438  1.00 43.11           C  
ATOM   1139  NE  ARG A 350      25.470   8.306   5.518  1.00 44.63           N  
ATOM   1140  CZ  ARG A 350      25.341   7.005   5.760  1.00 47.91           C  
ATOM   1141  NH1 ARG A 350      24.548   6.269   4.991  1.00 47.10           N  
ATOM   1142  NH2 ARG A 350      25.991   6.440   6.771  1.00 47.92           N  
ATOM   1143  N   GLU A 351      25.714  13.232   2.167  1.00 46.01           N  
ATOM   1144  CA  GLU A 351      27.062  13.672   1.829  1.00 48.39           C  
ATOM   1145  C   GLU A 351      27.240  15.164   2.138  1.00 48.44           C  
ATOM   1146  O   GLU A 351      28.289  15.585   2.629  1.00 48.09           O  
ATOM   1147  CB  GLU A 351      27.338  13.409   0.345  1.00 50.74           C  
ATOM   1148  CG  GLU A 351      28.744  12.938   0.056  1.00 53.68           C  
ATOM   1149  CD  GLU A 351      28.966  11.506   0.501  1.00 57.66           C  
ATOM   1150  OE1 GLU A 351      28.625  10.587  -0.279  1.00 58.28           O  
ATOM   1151  OE2 GLU A 351      29.464  11.301   1.632  1.00 58.04           O  
ATOM   1152  N   PHE A 352      26.212  15.957   1.848  1.00 48.14           N  
ATOM   1153  CA  PHE A 352      26.270  17.391   2.107  1.00 47.69           C  
ATOM   1154  C   PHE A 352      26.475  17.621   3.601  1.00 49.02           C  
ATOM   1155  O   PHE A 352      27.360  18.372   4.006  1.00 50.18           O  
ATOM   1156  CB  PHE A 352      24.976  18.069   1.647  1.00 45.67           C  
ATOM   1157  CG  PHE A 352      24.906  19.541   1.973  1.00 44.72           C  
ATOM   1158  CD1 PHE A 352      25.861  20.423   1.485  1.00 45.69           C  
ATOM   1159  CD2 PHE A 352      23.877  20.044   2.764  1.00 44.27           C  
ATOM   1160  CE1 PHE A 352      25.795  21.787   1.781  1.00 46.16           C  
ATOM   1161  CE2 PHE A 352      23.800  21.401   3.067  1.00 45.80           C  
ATOM   1162  CZ  PHE A 352      24.761  22.275   2.575  1.00 46.66           C  
ATOM   1163  N   LEU A 353      25.659  16.957   4.416  1.00 48.31           N  
ATOM   1164  CA  LEU A 353      25.751  17.087   5.860  1.00 48.93           C  
ATOM   1165  C   LEU A 353      27.124  16.696   6.388  1.00 50.67           C  
ATOM   1166  O   LEU A 353      27.650  17.338   7.299  1.00 50.82           O  
ATOM   1167  CB  LEU A 353      24.690  16.222   6.532  1.00 46.70           C  
ATOM   1168  CG  LEU A 353      23.271  16.716   6.294  1.00 46.60           C  
ATOM   1169  CD1 LEU A 353      22.269  15.776   6.913  1.00 45.24           C  
ATOM   1170  CD2 LEU A 353      23.145  18.110   6.888  1.00 48.88           C  
ATOM   1171  N   LYS A 354      27.693  15.639   5.818  1.00 51.06           N  
ATOM   1172  CA  LYS A 354      28.997  15.150   6.245  1.00 52.46           C  
ATOM   1173  C   LYS A 354      30.114  16.097   5.817  1.00 52.37           C  
ATOM   1174  O   LYS A 354      31.227  16.029   6.330  1.00 52.98           O  
ATOM   1175  CB  LYS A 354      29.242  13.750   5.671  1.00 53.11           C  
ATOM   1176  CG  LYS A 354      30.420  13.009   6.299  1.00 54.29           C  
ATOM   1177  CD  LYS A 354      30.447  11.538   5.880  1.00 54.03           C  
ATOM   1178  CE  LYS A 354      30.606  11.394   4.371  1.00 56.89           C  
ATOM   1179  NZ  LYS A 354      30.622   9.975   3.925  1.00 57.12           N  
ATOM   1180  N   SER A 355      29.807  16.993   4.889  1.00 52.83           N  
ATOM   1181  CA  SER A 355      30.799  17.940   4.402  1.00 54.14           C  
ATOM   1182  C   SER A 355      30.806  19.247   5.191  1.00 55.14           C  
ATOM   1183  O   SER A 355      31.491  20.197   4.810  1.00 55.57           O  
ATOM   1184  CB  SER A 355      30.536  18.259   2.937  1.00 54.11           C  
ATOM   1185  OG  SER A 355      29.393  19.086   2.820  1.00 57.08           O  
ATOM   1186  N   LEU A 356      30.039  19.307   6.274  1.00 55.21           N  
ATOM   1187  CA  LEU A 356      29.986  20.522   7.084  1.00 56.63           C  
ATOM   1188  C   LEU A 356      31.249  20.668   7.941  1.00 57.17           C  
ATOM   1189  O   LEU A 356      32.034  19.726   8.063  1.00 57.87           O  
ATOM   1190  CB  LEU A 356      28.731  20.514   7.969  1.00 54.19           C  
ATOM   1191  CG  LEU A 356      27.384  20.444   7.232  1.00 53.07           C  
ATOM   1192  CD1 LEU A 356      26.234  20.313   8.230  1.00 50.90           C  
ATOM   1193  CD2 LEU A 356      27.206  21.689   6.370  1.00 53.31           C  
ATOM   1194  N   ARG A 357      31.436  21.855   8.520  1.00 59.13           N  
ATOM   1195  CA  ARG A 357      32.595  22.166   9.365  1.00 59.66           C  
ATOM   1196  C   ARG A 357      32.919  21.109  10.423  1.00 59.65           C  
ATOM   1197  O   ARG A 357      32.027  20.587  11.091  1.00 58.77           O  
ATOM   1198  CB  ARG A 357      32.391  23.510  10.067  1.00 60.43           C  
ATOM   1199  CG  ARG A 357      33.462  23.804  11.109  1.00 63.95           C  
ATOM   1200  CD  ARG A 357      32.975  24.805  12.135  1.00 65.29           C  
ATOM   1201  NE  ARG A 357      32.912  26.158  11.598  1.00 66.11           N  
ATOM   1202  CZ  ARG A 357      32.408  27.191  12.261  1.00 66.80           C  
ATOM   1203  NH1 ARG A 357      31.917  27.015  13.481  1.00 65.97           N  
ATOM   1204  NH2 ARG A 357      32.418  28.404  11.719  1.00 67.29           N  
ATOM   1205  N   LYS A 358      34.214  20.847  10.580  1.00 61.40           N  
ATOM   1206  CA  LYS A 358      34.762  19.864  11.518  1.00 63.03           C  
ATOM   1207  C   LYS A 358      33.792  19.266  12.533  1.00 63.26           C  
ATOM   1208  O   LYS A 358      33.523  18.063  12.504  1.00 65.32           O  
ATOM   1209  CB  LYS A 358      35.965  20.454  12.266  1.00 63.50           C  
ATOM   1210  CG  LYS A 358      37.065  21.011  11.376  1.00 64.88           C  
ATOM   1211  CD  LYS A 358      37.689  19.949  10.476  1.00 65.92           C  
ATOM   1212  CE  LYS A 358      38.840  20.540   9.662  1.00 65.95           C  
ATOM   1213  NZ  LYS A 358      39.413  19.572   8.681  1.00 67.44           N  
ATOM   1214  N   PRO A 359      33.256  20.090  13.450  1.00 62.29           N  
ATOM   1215  CA  PRO A 359      32.325  19.522  14.429  1.00 61.33           C  
ATOM   1216  C   PRO A 359      30.958  19.118  13.857  1.00 60.75           C  
ATOM   1217  O   PRO A 359      30.518  17.982  14.041  1.00 59.81           O  
ATOM   1218  CB  PRO A 359      32.224  20.625  15.482  1.00 60.67           C  
ATOM   1219  CG  PRO A 359      32.355  21.867  14.660  1.00 61.60           C  
ATOM   1220  CD  PRO A 359      33.473  21.528  13.696  1.00 60.66           C  
ATOM   1221  N   PHE A 360      30.296  20.040  13.161  1.00 59.35           N  
ATOM   1222  CA  PHE A 360      28.979  19.759  12.599  1.00 58.87           C  
ATOM   1223  C   PHE A 360      28.988  18.651  11.546  1.00 59.12           C  
ATOM   1224  O   PHE A 360      28.029  17.887  11.420  1.00 58.71           O  
ATOM   1225  CB  PHE A 360      28.389  21.021  11.981  1.00 58.17           C  
ATOM   1226  CG  PHE A 360      28.362  22.197  12.907  1.00 58.64           C  
ATOM   1227  CD1 PHE A 360      29.452  23.060  12.984  1.00 57.98           C  
ATOM   1228  CD2 PHE A 360      27.244  22.450  13.696  1.00 58.54           C  
ATOM   1229  CE1 PHE A 360      29.429  24.159  13.831  1.00 58.92           C  
ATOM   1230  CE2 PHE A 360      27.208  23.546  14.549  1.00 59.43           C  
ATOM   1231  CZ  PHE A 360      28.304  24.405  14.618  1.00 59.99           C  
ATOM   1232  N   GLY A 361      30.079  18.571  10.794  1.00 58.49           N  
ATOM   1233  CA  GLY A 361      30.193  17.571   9.751  1.00 59.29           C  
ATOM   1234  C   GLY A 361      29.930  16.136  10.163  1.00 59.58           C  
ATOM   1235  O   GLY A 361      29.675  15.288   9.310  1.00 59.53           O  
ATOM   1236  N   ASP A 362      29.987  15.844  11.458  1.00 60.47           N  
ATOM   1237  CA  ASP A 362      29.753  14.476  11.905  1.00 60.75           C  
ATOM   1238  C   ASP A 362      28.647  14.325  12.937  1.00 58.95           C  
ATOM   1239  O   ASP A 362      28.590  13.334  13.659  1.00 58.64           O  
ATOM   1240  CB  ASP A 362      31.058  13.862  12.429  1.00 64.04           C  
ATOM   1241  CG  ASP A 362      31.906  14.856  13.191  1.00 65.39           C  
ATOM   1242  OD1 ASP A 362      31.364  15.528  14.097  1.00 67.51           O  
ATOM   1243  OD2 ASP A 362      33.116  14.958  12.886  1.00 66.75           O  
ATOM   1244  N   PHE A 363      27.761  15.310  12.999  1.00 57.75           N  
ATOM   1245  CA  PHE A 363      26.638  15.260  13.925  1.00 58.00           C  
ATOM   1246  C   PHE A 363      25.594  14.224  13.495  1.00 57.13           C  
ATOM   1247  O   PHE A 363      25.006  13.543  14.337  1.00 56.36           O  
ATOM   1248  CB  PHE A 363      25.957  16.630  14.004  1.00 60.56           C  
ATOM   1249  CG  PHE A 363      26.117  17.311  15.327  1.00 62.90           C  
ATOM   1250  CD1 PHE A 363      25.520  16.784  16.468  1.00 62.80           C  
ATOM   1251  CD2 PHE A 363      26.900  18.459  15.443  1.00 63.34           C  
ATOM   1252  CE1 PHE A 363      25.705  17.389  17.712  1.00 64.72           C  
ATOM   1253  CE2 PHE A 363      27.092  19.072  16.684  1.00 64.60           C  
ATOM   1254  CZ  PHE A 363      26.495  18.536  17.820  1.00 63.78           C  
ATOM   1255  N   MET A 364      25.369  14.111  12.186  1.00 56.41           N  
ATOM   1256  CA  MET A 364      24.362  13.192  11.655  1.00 56.35           C  
ATOM   1257  C   MET A 364      24.828  11.823  11.181  1.00 55.22           C  
ATOM   1258  O   MET A 364      24.047  10.874  11.185  1.00 54.87           O  
ATOM   1259  CB  MET A 364      23.596  13.858  10.509  1.00 57.12           C  
ATOM   1260  CG  MET A 364      22.737  15.041  10.924  1.00 59.90           C  
ATOM   1261  SD  MET A 364      21.392  14.582  12.038  1.00 64.64           S  
ATOM   1262  CE  MET A 364      20.147  14.068  10.875  1.00 61.81           C  
ATOM   1263  N   GLU A 365      26.082  11.706  10.770  1.00 54.60           N  
ATOM   1264  CA  GLU A 365      26.563  10.418  10.287  1.00 55.27           C  
ATOM   1265  C   GLU A 365      26.100   9.244  11.166  1.00 54.41           C  
ATOM   1266  O   GLU A 365      25.546   8.262  10.665  1.00 54.75           O  
ATOM   1267  CB  GLU A 365      28.089  10.433  10.184  1.00 56.36           C  
ATOM   1268  CG  GLU A 365      28.657   9.301   9.349  1.00 58.13           C  
ATOM   1269  CD  GLU A 365      28.051   9.257   7.962  1.00 58.95           C  
ATOM   1270  OE1 GLU A 365      27.772  10.337   7.406  1.00 59.72           O  
ATOM   1271  OE2 GLU A 365      27.861   8.149   7.421  1.00 60.58           O  
ATOM   1272  N   PRO A 366      26.313   9.329  12.490  1.00 53.05           N  
ATOM   1273  CA  PRO A 366      25.873   8.212  13.332  1.00 52.21           C  
ATOM   1274  C   PRO A 366      24.367   7.947  13.303  1.00 51.08           C  
ATOM   1275  O   PRO A 366      23.931   6.819  13.555  1.00 50.30           O  
ATOM   1276  CB  PRO A 366      26.382   8.600  14.727  1.00 51.16           C  
ATOM   1277  CG  PRO A 366      26.424  10.098  14.678  1.00 52.68           C  
ATOM   1278  CD  PRO A 366      26.977  10.369  13.298  1.00 52.72           C  
ATOM   1279  N   LYS A 367      23.573   8.977  13.000  1.00 48.93           N  
ATOM   1280  CA  LYS A 367      22.121   8.812  12.939  1.00 46.72           C  
ATOM   1281  C   LYS A 367      21.771   8.018  11.674  1.00 45.04           C  
ATOM   1282  O   LYS A 367      20.890   7.157  11.696  1.00 43.45           O  
ATOM   1283  CB  LYS A 367      21.408  10.173  12.905  1.00 48.99           C  
ATOM   1284  CG  LYS A 367      21.970  11.224  13.864  1.00 51.79           C  
ATOM   1285  CD  LYS A 367      21.813  10.840  15.315  1.00 52.76           C  
ATOM   1286  CE  LYS A 367      22.823  11.582  16.194  1.00 54.81           C  
ATOM   1287  NZ  LYS A 367      22.802  13.063  16.007  1.00 56.08           N  
ATOM   1288  N   PHE A 368      22.468   8.309  10.578  1.00 42.48           N  
ATOM   1289  CA  PHE A 368      22.230   7.609   9.326  1.00 42.71           C  
ATOM   1290  C   PHE A 368      22.563   6.137   9.495  1.00 44.66           C  
ATOM   1291  O   PHE A 368      21.791   5.271   9.072  1.00 43.42           O  
ATOM   1292  CB  PHE A 368      23.081   8.195   8.199  1.00 40.25           C  
ATOM   1293  CG  PHE A 368      22.525   9.465   7.607  1.00 41.98           C  
ATOM   1294  CD1 PHE A 368      21.390   9.432   6.797  1.00 41.24           C  
ATOM   1295  CD2 PHE A 368      23.134  10.695   7.860  1.00 42.43           C  
ATOM   1296  CE1 PHE A 368      20.863  10.607   6.241  1.00 40.05           C  
ATOM   1297  CE2 PHE A 368      22.618  11.881   7.314  1.00 43.64           C  
ATOM   1298  CZ  PHE A 368      21.477  11.833   6.500  1.00 43.01           C  
ATOM   1299  N   GLU A 369      23.708   5.853  10.119  1.00 45.25           N  
ATOM   1300  CA  GLU A 369      24.139   4.472  10.335  1.00 44.75           C  
ATOM   1301  C   GLU A 369      23.086   3.696  11.104  1.00 43.34           C  
ATOM   1302  O   GLU A 369      22.793   2.537  10.797  1.00 43.11           O  
ATOM   1303  CB  GLU A 369      25.480   4.435  11.086  1.00 47.65           C  
ATOM   1304  CG  GLU A 369      26.643   4.974  10.256  1.00 53.27           C  
ATOM   1305  CD  GLU A 369      28.007   4.755  10.900  1.00 57.77           C  
ATOM   1306  OE1 GLU A 369      28.385   3.585  11.142  1.00 59.92           O  
ATOM   1307  OE2 GLU A 369      28.706   5.759  11.153  1.00 60.34           O  
ATOM   1308  N   PHE A 370      22.509   4.342  12.107  1.00 41.81           N  
ATOM   1309  CA  PHE A 370      21.473   3.703  12.894  1.00 39.70           C  
ATOM   1310  C   PHE A 370      20.201   3.548  12.061  1.00 38.66           C  
ATOM   1311  O   PHE A 370      19.563   2.495  12.067  1.00 36.60           O  
ATOM   1312  CB  PHE A 370      21.169   4.533  14.140  1.00 38.59           C  
ATOM   1313  CG  PHE A 370      19.841   4.217  14.760  1.00 39.33           C  
ATOM   1314  CD1 PHE A 370      19.636   3.011  15.426  1.00 38.83           C  
ATOM   1315  CD2 PHE A 370      18.786   5.116  14.656  1.00 36.83           C  
ATOM   1316  CE1 PHE A 370      18.399   2.704  15.979  1.00 38.13           C  
ATOM   1317  CE2 PHE A 370      17.546   4.821  15.204  1.00 39.53           C  
ATOM   1318  CZ  PHE A 370      17.352   3.608  15.868  1.00 40.13           C  
ATOM   1319  N   ALA A 371      19.840   4.603  11.343  1.00 38.78           N  
ATOM   1320  CA  ALA A 371      18.627   4.591  10.529  1.00 39.20           C  
ATOM   1321  C   ALA A 371      18.566   3.453   9.511  1.00 39.57           C  
ATOM   1322  O   ALA A 371      17.553   2.760   9.412  1.00 40.90           O  
ATOM   1323  CB  ALA A 371      18.465   5.941   9.821  1.00 38.53           C  
ATOM   1324  N   VAL A 372      19.641   3.268   8.750  1.00 41.50           N  
ATOM   1325  CA  VAL A 372      19.688   2.217   7.735  1.00 42.74           C  
ATOM   1326  C   VAL A 372      19.518   0.822   8.329  1.00 41.83           C  
ATOM   1327  O   VAL A 372      18.926  -0.052   7.704  1.00 42.13           O  
ATOM   1328  CB  VAL A 372      21.014   2.255   6.942  1.00 43.93           C  
ATOM   1329  CG1 VAL A 372      21.035   1.143   5.916  1.00 45.20           C  
ATOM   1330  CG2 VAL A 372      21.174   3.592   6.263  1.00 43.68           C  
ATOM   1331  N   LYS A 373      20.051   0.617   9.526  1.00 42.38           N  
ATOM   1332  CA  LYS A 373      19.940  -0.672  10.207  1.00 43.59           C  
ATOM   1333  C   LYS A 373      18.522  -0.800  10.766  1.00 43.43           C  
ATOM   1334  O   LYS A 373      17.853  -1.828  10.603  1.00 45.42           O  
ATOM   1335  CB  LYS A 373      20.940  -0.753  11.368  1.00 44.95           C  
ATOM   1336  CG  LYS A 373      22.401  -0.482  10.988  1.00 50.94           C  
ATOM   1337  CD  LYS A 373      23.332  -0.497  12.217  1.00 53.41           C  
ATOM   1338  CE  LYS A 373      22.988   0.629  13.209  1.00 59.15           C  
ATOM   1339  NZ  LYS A 373      23.857   0.692  14.432  1.00 58.36           N  
ATOM   1340  N   PHE A 374      18.067   0.257  11.425  1.00 39.49           N  
ATOM   1341  CA  PHE A 374      16.738   0.262  12.018  1.00 37.66           C  
ATOM   1342  C   PHE A 374      15.684   0.102  10.930  1.00 35.62           C  
ATOM   1343  O   PHE A 374      14.742  -0.672  11.080  1.00 35.69           O  
ATOM   1344  CB  PHE A 374      16.512   1.569  12.773  1.00 37.52           C  
ATOM   1345  CG  PHE A 374      15.278   1.571  13.633  1.00 36.87           C  
ATOM   1346  CD1 PHE A 374      15.281   0.935  14.869  1.00 33.85           C  
ATOM   1347  CD2 PHE A 374      14.116   2.218  13.209  1.00 35.61           C  
ATOM   1348  CE1 PHE A 374      14.150   0.937  15.678  1.00 36.12           C  
ATOM   1349  CE2 PHE A 374      12.978   2.226  14.010  1.00 35.72           C  
ATOM   1350  CZ  PHE A 374      12.995   1.585  15.245  1.00 36.12           C  
ATOM   1351  N   ASN A 375      15.851   0.815   9.823  1.00 34.01           N  
ATOM   1352  CA  ASN A 375      14.875   0.728   8.753  1.00 36.36           C  
ATOM   1353  C   ASN A 375      14.803  -0.658   8.133  1.00 37.54           C  
ATOM   1354  O   ASN A 375      13.785  -1.021   7.528  1.00 34.41           O  
ATOM   1355  CB  ASN A 375      15.152   1.783   7.673  1.00 36.28           C  
ATOM   1356  CG  ASN A 375      14.859   3.203   8.159  1.00 34.45           C  
ATOM   1357  OD1 ASN A 375      14.224   3.395   9.190  1.00 34.58           O  
ATOM   1358  ND2 ASN A 375      15.316   4.189   7.417  1.00 34.22           N  
ATOM   1359  N   ALA A 376      15.870  -1.439   8.293  1.00 37.62           N  
ATOM   1360  CA  ALA A 376      15.882  -2.788   7.740  1.00 39.70           C  
ATOM   1361  C   ALA A 376      14.823  -3.641   8.435  1.00 39.51           C  
ATOM   1362  O   ALA A 376      14.408  -4.676   7.912  1.00 42.23           O  
ATOM   1363  CB  ALA A 376      17.266  -3.416   7.897  1.00 41.76           C  
ATOM   1364  N   LEU A 377      14.378  -3.206   9.610  1.00 38.09           N  
ATOM   1365  CA  LEU A 377      13.343  -3.944  10.332  1.00 39.11           C  
ATOM   1366  C   LEU A 377      11.970  -3.808   9.652  1.00 39.43           C  
ATOM   1367  O   LEU A 377      11.058  -4.608   9.897  1.00 39.53           O  
ATOM   1368  CB  LEU A 377      13.261  -3.469  11.786  1.00 36.40           C  
ATOM   1369  CG  LEU A 377      14.487  -3.727  12.668  1.00 39.00           C  
ATOM   1370  CD1 LEU A 377      14.189  -3.290  14.113  1.00 34.64           C  
ATOM   1371  CD2 LEU A 377      14.853  -5.211  12.620  1.00 38.36           C  
ATOM   1372  N   GLU A 378      11.839  -2.796   8.796  1.00 39.52           N  
ATOM   1373  CA  GLU A 378      10.605  -2.526   8.051  1.00 39.21           C  
ATOM   1374  C   GLU A 378       9.366  -2.317   8.919  1.00 37.67           C  
ATOM   1375  O   GLU A 378       8.301  -2.898   8.683  1.00 35.20           O  
ATOM   1376  CB  GLU A 378      10.353  -3.650   7.046  1.00 42.91           C  
ATOM   1377  CG  GLU A 378      11.500  -3.837   6.056  1.00 46.94           C  
ATOM   1378  CD  GLU A 378      11.114  -4.720   4.886  1.00 51.25           C  
ATOM   1379  OE1 GLU A 378      10.272  -4.284   4.078  1.00 55.76           O  
ATOM   1380  OE2 GLU A 378      11.641  -5.846   4.773  1.00 52.92           O  
ATOM   1381  N   LEU A 379       9.500  -1.475   9.930  1.00 35.63           N  
ATOM   1382  CA  LEU A 379       8.371  -1.211  10.799  1.00 35.93           C  
ATOM   1383  C   LEU A 379       7.502  -0.099  10.200  1.00 35.77           C  
ATOM   1384  O   LEU A 379       8.003   0.798   9.524  1.00 33.90           O  
ATOM   1385  CB  LEU A 379       8.864  -0.796  12.187  1.00 35.88           C  
ATOM   1386  CG  LEU A 379       9.727  -1.812  12.957  1.00 36.23           C  
ATOM   1387  CD1 LEU A 379      10.161  -1.186  14.260  1.00 35.33           C  
ATOM   1388  CD2 LEU A 379       8.943  -3.096  13.233  1.00 34.33           C  
ATOM   1389  N   ASP A 380       6.196  -0.180  10.424  1.00 36.87           N  
ATOM   1390  CA  ASP A 380       5.312   0.870   9.940  1.00 37.25           C  
ATOM   1391  C   ASP A 380       4.856   1.664  11.158  1.00 36.28           C  
ATOM   1392  O   ASP A 380       5.268   1.371  12.284  1.00 36.45           O  
ATOM   1393  CB  ASP A 380       4.114   0.305   9.155  1.00 37.67           C  
ATOM   1394  CG  ASP A 380       3.264  -0.638   9.964  1.00 35.67           C  
ATOM   1395  OD1 ASP A 380       3.107  -0.416  11.170  1.00 36.75           O  
ATOM   1396  OD2 ASP A 380       2.733  -1.604   9.377  1.00 41.06           O  
ATOM   1397  N   ASP A 381       4.018   2.667  10.933  1.00 33.38           N  
ATOM   1398  CA  ASP A 381       3.554   3.524  12.002  1.00 30.54           C  
ATOM   1399  C   ASP A 381       2.822   2.832  13.123  1.00 31.01           C  
ATOM   1400  O   ASP A 381       2.982   3.203  14.283  1.00 29.29           O  
ATOM   1401  CB  ASP A 381       2.684   4.647  11.424  1.00 31.43           C  
ATOM   1402  CG  ASP A 381       3.461   5.559  10.508  1.00 28.86           C  
ATOM   1403  OD1 ASP A 381       4.435   6.193  10.964  1.00 32.73           O  
ATOM   1404  OD2 ASP A 381       3.109   5.646   9.326  1.00 31.32           O  
ATOM   1405  N   SER A 382       2.002   1.839  12.800  1.00 29.11           N  
ATOM   1406  CA  SER A 382       1.290   1.152  13.858  1.00 31.18           C  
ATOM   1407  C   SER A 382       2.280   0.460  14.810  1.00 31.72           C  
ATOM   1408  O   SER A 382       1.992   0.317  16.003  1.00 31.99           O  
ATOM   1409  CB  SER A 382       0.312   0.142  13.267  1.00 31.61           C  
ATOM   1410  OG  SER A 382       1.000  -0.730  12.394  1.00 38.99           O  
ATOM   1411  N   ASP A 383       3.440   0.033  14.294  1.00 31.17           N  
ATOM   1412  CA  ASP A 383       4.445  -0.619  15.145  1.00 31.59           C  
ATOM   1413  C   ASP A 383       5.149   0.430  16.006  1.00 29.66           C  
ATOM   1414  O   ASP A 383       5.231   0.302  17.225  1.00 28.41           O  
ATOM   1415  CB  ASP A 383       5.518  -1.357  14.308  1.00 29.71           C  
ATOM   1416  CG  ASP A 383       4.930  -2.401  13.376  1.00 28.67           C  
ATOM   1417  OD1 ASP A 383       4.048  -3.163  13.822  1.00 32.68           O  
ATOM   1418  OD2 ASP A 383       5.358  -2.468  12.198  1.00 29.37           O  
ATOM   1419  N   LEU A 384       5.665   1.464  15.347  1.00 31.68           N  
ATOM   1420  CA  LEU A 384       6.380   2.560  16.004  1.00 30.88           C  
ATOM   1421  C   LEU A 384       5.583   3.248  17.112  1.00 32.70           C  
ATOM   1422  O   LEU A 384       6.144   3.666  18.138  1.00 34.38           O  
ATOM   1423  CB  LEU A 384       6.821   3.580  14.942  1.00 29.57           C  
ATOM   1424  CG  LEU A 384       7.878   3.035  13.976  1.00 29.29           C  
ATOM   1425  CD1 LEU A 384       7.989   3.896  12.707  1.00 27.34           C  
ATOM   1426  CD2 LEU A 384       9.212   2.968  14.722  1.00 28.54           C  
ATOM   1427  N   ALA A 385       4.277   3.372  16.923  1.00 32.49           N  
ATOM   1428  CA  ALA A 385       3.464   4.009  17.949  1.00 33.65           C  
ATOM   1429  C   ALA A 385       3.566   3.239  19.266  1.00 31.71           C  
ATOM   1430  O   ALA A 385       3.653   3.841  20.333  1.00 31.69           O  
ATOM   1431  CB  ALA A 385       2.003   4.111  17.493  1.00 31.74           C  
ATOM   1432  N   ILE A 386       3.548   1.910  19.213  1.00 33.93           N  
ATOM   1433  CA  ILE A 386       3.652   1.146  20.462  1.00 33.71           C  
ATOM   1434  C   ILE A 386       5.089   1.178  20.977  1.00 32.77           C  
ATOM   1435  O   ILE A 386       5.316   1.290  22.178  1.00 34.93           O  
ATOM   1436  CB  ILE A 386       3.265  -0.357  20.317  1.00 35.81           C  
ATOM   1437  CG1 ILE A 386       2.048  -0.535  19.409  1.00 35.92           C  
ATOM   1438  CG2 ILE A 386       2.946  -0.928  21.715  1.00 32.12           C  
ATOM   1439  CD1 ILE A 386       0.785   0.060  19.956  1.00 42.40           C  
ATOM   1440  N   PHE A 387       6.053   1.075  20.064  1.00 32.78           N  
ATOM   1441  CA  PHE A 387       7.463   1.073  20.435  1.00 34.14           C  
ATOM   1442  C   PHE A 387       7.860   2.361  21.142  1.00 34.98           C  
ATOM   1443  O   PHE A 387       8.570   2.347  22.156  1.00 33.59           O  
ATOM   1444  CB  PHE A 387       8.349   0.878  19.202  1.00 34.62           C  
ATOM   1445  CG  PHE A 387       9.831   0.916  19.509  1.00 35.42           C  
ATOM   1446  CD1 PHE A 387      10.388   0.027  20.429  1.00 35.27           C  
ATOM   1447  CD2 PHE A 387      10.659   1.847  18.897  1.00 35.93           C  
ATOM   1448  CE1 PHE A 387      11.739   0.065  20.734  1.00 34.19           C  
ATOM   1449  CE2 PHE A 387      12.027   1.899  19.197  1.00 38.28           C  
ATOM   1450  CZ  PHE A 387      12.566   1.005  20.119  1.00 36.74           C  
ATOM   1451  N   ILE A 388       7.406   3.479  20.600  1.00 31.88           N  
ATOM   1452  CA  ILE A 388       7.698   4.780  21.184  1.00 33.22           C  
ATOM   1453  C   ILE A 388       7.121   4.888  22.595  1.00 32.37           C  
ATOM   1454  O   ILE A 388       7.724   5.498  23.483  1.00 32.15           O  
ATOM   1455  CB  ILE A 388       7.123   5.873  20.282  1.00 37.11           C  
ATOM   1456  CG1 ILE A 388       8.018   6.007  19.052  1.00 40.47           C  
ATOM   1457  CG2 ILE A 388       6.966   7.170  21.037  1.00 40.51           C  
ATOM   1458  CD1 ILE A 388       7.297   6.588  17.845  1.00 46.48           C  
ATOM   1459  N   ALA A 389       5.955   4.286  22.799  1.00 32.20           N  
ATOM   1460  CA  ALA A 389       5.295   4.295  24.101  1.00 33.47           C  
ATOM   1461  C   ALA A 389       6.113   3.459  25.091  1.00 34.48           C  
ATOM   1462  O   ALA A 389       6.220   3.812  26.258  1.00 35.08           O  
ATOM   1463  CB  ALA A 389       3.879   3.725  23.979  1.00 31.12           C  
ATOM   1464  N   VAL A 390       6.674   2.348  24.616  1.00 34.77           N  
ATOM   1465  CA  VAL A 390       7.498   1.472  25.455  1.00 35.28           C  
ATOM   1466  C   VAL A 390       8.717   2.249  25.935  1.00 33.91           C  
ATOM   1467  O   VAL A 390       9.040   2.239  27.112  1.00 34.65           O  
ATOM   1468  CB  VAL A 390       7.951   0.221  24.662  1.00 35.04           C  
ATOM   1469  CG1 VAL A 390       9.108  -0.481  25.363  1.00 34.45           C  
ATOM   1470  CG2 VAL A 390       6.775  -0.725  24.508  1.00 33.36           C  
ATOM   1471  N   ILE A 391       9.371   2.942  25.009  1.00 35.79           N  
ATOM   1472  CA  ILE A 391      10.552   3.745  25.316  1.00 35.85           C  
ATOM   1473  C   ILE A 391      10.283   4.725  26.449  1.00 37.15           C  
ATOM   1474  O   ILE A 391      11.101   4.870  27.356  1.00 37.01           O  
ATOM   1475  CB  ILE A 391      11.015   4.568  24.093  1.00 36.96           C  
ATOM   1476  CG1 ILE A 391      11.467   3.639  22.963  1.00 39.80           C  
ATOM   1477  CG2 ILE A 391      12.114   5.538  24.493  1.00 36.84           C  
ATOM   1478  CD1 ILE A 391      12.549   2.670  23.362  1.00 47.19           C  
ATOM   1479  N   ILE A 392       9.140   5.406  26.392  1.00 34.68           N  
ATOM   1480  CA  ILE A 392       8.800   6.383  27.410  1.00 34.61           C  
ATOM   1481  C   ILE A 392       8.612   5.797  28.805  1.00 33.54           C  
ATOM   1482  O   ILE A 392       9.102   6.352  29.781  1.00 33.80           O  
ATOM   1483  CB  ILE A 392       7.504   7.175  27.040  1.00 35.71           C  
ATOM   1484  CG1 ILE A 392       7.685   7.890  25.695  1.00 32.95           C  
ATOM   1485  CG2 ILE A 392       7.192   8.181  28.138  1.00 33.74           C  
ATOM   1486  CD1 ILE A 392       6.458   8.694  25.244  1.00 36.12           C  
ATOM   1487  N   LEU A 393       7.896   4.684  28.902  1.00 34.60           N  
ATOM   1488  CA  LEU A 393       7.644   4.078  30.194  1.00 34.54           C  
ATOM   1489  C   LEU A 393       8.756   3.121  30.631  1.00 35.96           C  
ATOM   1490  O   LEU A 393       8.520   1.936  30.896  1.00 33.23           O  
ATOM   1491  CB  LEU A 393       6.287   3.374  30.169  1.00 34.15           C  
ATOM   1492  CG  LEU A 393       5.072   4.315  30.283  1.00 36.61           C  
ATOM   1493  CD1 LEU A 393       4.919   4.770  31.715  1.00 36.19           C  
ATOM   1494  CD2 LEU A 393       5.239   5.525  29.357  1.00 35.29           C  
ATOM   1495  N   SER A 394       9.968   3.661  30.690  1.00 37.96           N  
ATOM   1496  CA  SER A 394      11.149   2.913  31.103  1.00 40.77           C  
ATOM   1497  C   SER A 394      11.338   3.109  32.593  1.00 40.91           C  
ATOM   1498  O   SER A 394      11.737   4.185  33.037  1.00 40.26           O  
ATOM   1499  CB  SER A 394      12.377   3.441  30.377  1.00 42.12           C  
ATOM   1500  OG  SER A 394      12.234   3.292  28.981  1.00 46.70           O  
ATOM   1501  N   GLY A 395      11.054   2.071  33.366  1.00 44.00           N  
ATOM   1502  CA  GLY A 395      11.193   2.183  34.807  1.00 46.68           C  
ATOM   1503  C   GLY A 395      12.624   2.293  35.302  1.00 48.42           C  
ATOM   1504  O   GLY A 395      12.860   2.422  36.503  1.00 50.10           O  
ATOM   1505  N   ASP A 396      13.588   2.260  34.392  1.00 49.56           N  
ATOM   1506  CA  ASP A 396      14.980   2.331  34.805  1.00 51.91           C  
ATOM   1507  C   ASP A 396      15.663   3.664  34.531  1.00 51.54           C  
ATOM   1508  O   ASP A 396      16.884   3.720  34.393  1.00 51.60           O  
ATOM   1509  CB  ASP A 396      15.761   1.184  34.161  1.00 55.19           C  
ATOM   1510  CG  ASP A 396      15.260  -0.183  34.620  1.00 59.73           C  
ATOM   1511  OD1 ASP A 396      14.030  -0.422  34.541  1.00 61.39           O  
ATOM   1512  OD2 ASP A 396      16.086  -1.017  35.060  1.00 61.53           O  
ATOM   1513  N   ARG A 397      14.876   4.735  34.462  1.00 49.04           N  
ATOM   1514  CA  ARG A 397      15.432   6.064  34.232  1.00 47.02           C  
ATOM   1515  C   ARG A 397      15.952   6.601  35.562  1.00 47.15           C  
ATOM   1516  O   ARG A 397      15.362   6.352  36.613  1.00 48.49           O  
ATOM   1517  CB  ARG A 397      14.363   7.020  33.686  1.00 45.49           C  
ATOM   1518  CG  ARG A 397      13.682   6.553  32.398  1.00 43.61           C  
ATOM   1519  CD  ARG A 397      14.682   6.379  31.255  1.00 42.66           C  
ATOM   1520  NE  ARG A 397      14.011   6.354  29.953  1.00 41.78           N  
ATOM   1521  CZ  ARG A 397      14.635   6.229  28.785  1.00 42.67           C  
ATOM   1522  NH1 ARG A 397      15.957   6.107  28.746  1.00 38.91           N  
ATOM   1523  NH2 ARG A 397      13.943   6.249  27.649  1.00 41.44           N  
ATOM   1524  N   PRO A 398      17.072   7.340  35.535  1.00 46.14           N  
ATOM   1525  CA  PRO A 398      17.652   7.904  36.759  1.00 45.96           C  
ATOM   1526  C   PRO A 398      16.721   8.872  37.490  1.00 46.13           C  
ATOM   1527  O   PRO A 398      16.109   9.744  36.869  1.00 48.24           O  
ATOM   1528  CB  PRO A 398      18.914   8.610  36.252  1.00 45.23           C  
ATOM   1529  CG  PRO A 398      19.309   7.788  35.071  1.00 45.48           C  
ATOM   1530  CD  PRO A 398      17.977   7.533  34.389  1.00 44.61           C  
ATOM   1531  N   GLY A 399      16.621   8.713  38.808  1.00 44.89           N  
ATOM   1532  CA  GLY A 399      15.801   9.600  39.612  1.00 44.38           C  
ATOM   1533  C   GLY A 399      14.320   9.296  39.762  1.00 44.66           C  
ATOM   1534  O   GLY A 399      13.594  10.099  40.350  1.00 45.19           O  
ATOM   1535  N   LEU A 400      13.864   8.151  39.264  1.00 43.58           N  
ATOM   1536  CA  LEU A 400      12.452   7.797  39.362  1.00 44.00           C  
ATOM   1537  C   LEU A 400      12.006   7.506  40.788  1.00 45.86           C  
ATOM   1538  O   LEU A 400      12.638   6.731  41.502  1.00 47.73           O  
ATOM   1539  CB  LEU A 400      12.142   6.591  38.466  1.00 43.09           C  
ATOM   1540  CG  LEU A 400      12.159   6.830  36.949  1.00 42.72           C  
ATOM   1541  CD1 LEU A 400      11.907   5.510  36.208  1.00 40.50           C  
ATOM   1542  CD2 LEU A 400      11.094   7.861  36.582  1.00 41.89           C  
ATOM   1543  N   LEU A 401      10.896   8.116  41.191  1.00 46.85           N  
ATOM   1544  CA  LEU A 401      10.369   7.929  42.532  1.00 47.63           C  
ATOM   1545  C   LEU A 401       9.581   6.635  42.692  1.00 48.98           C  
ATOM   1546  O   LEU A 401       9.888   5.826  43.568  1.00 48.98           O  
ATOM   1547  CB  LEU A 401       9.479   9.111  42.917  1.00 46.90           C  
ATOM   1548  CG  LEU A 401      10.120  10.500  42.900  1.00 47.77           C  
ATOM   1549  CD1 LEU A 401       9.076  11.520  43.322  1.00 46.93           C  
ATOM   1550  CD2 LEU A 401      11.325  10.548  43.840  1.00 48.76           C  
ATOM   1551  N   ASN A 402       8.565   6.445  41.851  1.00 48.82           N  
ATOM   1552  CA  ASN A 402       7.719   5.255  41.917  1.00 49.58           C  
ATOM   1553  C   ASN A 402       7.896   4.411  40.667  1.00 48.66           C  
ATOM   1554  O   ASN A 402       7.182   4.590  39.675  1.00 47.50           O  
ATOM   1555  CB  ASN A 402       6.248   5.656  42.043  1.00 51.83           C  
ATOM   1556  CG  ASN A 402       6.004   6.660  43.152  1.00 56.23           C  
ATOM   1557  OD1 ASN A 402       4.974   7.344  43.167  1.00 59.32           O  
ATOM   1558  ND2 ASN A 402       6.940   6.753  44.093  1.00 57.18           N  
ATOM   1559  N   VAL A 403       8.837   3.478  40.727  1.00 46.41           N  
ATOM   1560  CA  VAL A 403       9.139   2.607  39.604  1.00 46.09           C  
ATOM   1561  C   VAL A 403       8.092   1.543  39.277  1.00 45.13           C  
ATOM   1562  O   VAL A 403       7.909   1.199  38.112  1.00 44.85           O  
ATOM   1563  CB  VAL A 403      10.500   1.913  39.830  1.00 46.53           C  
ATOM   1564  CG1 VAL A 403      10.797   0.934  38.722  1.00 47.01           C  
ATOM   1565  CG2 VAL A 403      11.585   2.958  39.907  1.00 48.82           C  
ATOM   1566  N   LYS A 404       7.399   1.034  40.289  1.00 44.98           N  
ATOM   1567  CA  LYS A 404       6.412  -0.027  40.074  1.00 45.86           C  
ATOM   1568  C   LYS A 404       5.259   0.326  39.145  1.00 44.71           C  
ATOM   1569  O   LYS A 404       4.959  -0.421  38.213  1.00 45.27           O  
ATOM   1570  CB  LYS A 404       5.828  -0.515  41.404  1.00 46.88           C  
ATOM   1571  CG  LYS A 404       4.982  -1.773  41.235  1.00 49.53           C  
ATOM   1572  CD  LYS A 404       3.877  -1.883  42.275  1.00 52.91           C  
ATOM   1573  CE  LYS A 404       4.417  -2.073  43.684  1.00 52.70           C  
ATOM   1574  NZ  LYS A 404       3.294  -2.206  44.653  1.00 54.03           N  
ATOM   1575  N   PRO A 405       4.577   1.453  39.402  1.00 43.16           N  
ATOM   1576  CA  PRO A 405       3.457   1.833  38.529  1.00 41.65           C  
ATOM   1577  C   PRO A 405       3.936   2.038  37.095  1.00 40.70           C  
ATOM   1578  O   PRO A 405       3.213   1.757  36.141  1.00 40.33           O  
ATOM   1579  CB  PRO A 405       2.938   3.119  39.172  1.00 41.73           C  
ATOM   1580  CG  PRO A 405       4.181   3.712  39.788  1.00 43.11           C  
ATOM   1581  CD  PRO A 405       4.839   2.493  40.411  1.00 42.31           C  
ATOM   1582  N   ILE A 406       5.168   2.513  36.950  1.00 39.91           N  
ATOM   1583  CA  ILE A 406       5.742   2.728  35.633  1.00 39.56           C  
ATOM   1584  C   ILE A 406       5.958   1.414  34.873  1.00 40.72           C  
ATOM   1585  O   ILE A 406       5.624   1.314  33.688  1.00 37.26           O  
ATOM   1586  CB  ILE A 406       7.074   3.487  35.737  1.00 38.15           C  
ATOM   1587  CG1 ILE A 406       6.799   4.935  36.142  1.00 35.86           C  
ATOM   1588  CG2 ILE A 406       7.819   3.425  34.409  1.00 37.44           C  
ATOM   1589  CD1 ILE A 406       8.051   5.792  36.271  1.00 34.31           C  
ATOM   1590  N   GLU A 407       6.514   0.412  35.558  1.00 41.08           N  
ATOM   1591  CA  GLU A 407       6.768  -0.896  34.953  1.00 41.17           C  
ATOM   1592  C   GLU A 407       5.474  -1.640  34.664  1.00 40.16           C  
ATOM   1593  O   GLU A 407       5.417  -2.461  33.750  1.00 42.49           O  
ATOM   1594  CB  GLU A 407       7.639  -1.761  35.871  1.00 43.69           C  
ATOM   1595  CG  GLU A 407       8.931  -1.114  36.304  1.00 46.42           C  
ATOM   1596  CD  GLU A 407       9.853  -2.080  37.055  1.00 50.21           C  
ATOM   1597  OE1 GLU A 407       9.349  -2.920  37.835  1.00 49.78           O  
ATOM   1598  OE2 GLU A 407      11.086  -1.983  36.873  1.00 49.00           O  
ATOM   1599  N   ASP A 408       4.436  -1.382  35.453  1.00 39.58           N  
ATOM   1600  CA  ASP A 408       3.160  -2.047  35.208  1.00 39.88           C  
ATOM   1601  C   ASP A 408       2.596  -1.567  33.865  1.00 38.71           C  
ATOM   1602  O   ASP A 408       1.969  -2.327  33.133  1.00 38.86           O  
ATOM   1603  CB  ASP A 408       2.158  -1.750  36.329  1.00 41.01           C  
ATOM   1604  CG  ASP A 408       2.533  -2.418  37.647  1.00 46.10           C  
ATOM   1605  OD1 ASP A 408       3.160  -3.508  37.621  1.00 46.69           O  
ATOM   1606  OD2 ASP A 408       2.181  -1.860  38.709  1.00 47.10           O  
ATOM   1607  N   ILE A 409       2.823  -0.300  33.543  1.00 36.01           N  
ATOM   1608  CA  ILE A 409       2.342   0.231  32.288  1.00 36.56           C  
ATOM   1609  C   ILE A 409       3.194  -0.318  31.154  1.00 36.85           C  
ATOM   1610  O   ILE A 409       2.658  -0.796  30.141  1.00 35.12           O  
ATOM   1611  CB  ILE A 409       2.400   1.782  32.259  1.00 35.76           C  
ATOM   1612  CG1 ILE A 409       1.404   2.359  33.276  1.00 35.50           C  
ATOM   1613  CG2 ILE A 409       2.050   2.281  30.850  1.00 35.95           C  
ATOM   1614  CD1 ILE A 409       1.613   3.837  33.599  1.00 36.51           C  
ATOM   1615  N   GLN A 410       4.517  -0.280  31.327  1.00 36.23           N  
ATOM   1616  CA  GLN A 410       5.392  -0.766  30.275  1.00 36.81           C  
ATOM   1617  C   GLN A 410       5.122  -2.222  29.949  1.00 37.91           C  
ATOM   1618  O   GLN A 410       5.161  -2.612  28.788  1.00 38.88           O  
ATOM   1619  CB  GLN A 410       6.876  -0.594  30.624  1.00 35.30           C  
ATOM   1620  CG  GLN A 410       7.712  -0.375  29.347  1.00 38.36           C  
ATOM   1621  CD  GLN A 410       9.197  -0.648  29.507  1.00 42.78           C  
ATOM   1622  OE1 GLN A 410      10.019  -0.144  28.732  1.00 43.64           O  
ATOM   1623  NE2 GLN A 410       9.549  -1.457  30.497  1.00 43.30           N  
ATOM   1624  N   ASP A 411       4.837  -3.029  30.966  1.00 41.59           N  
ATOM   1625  CA  ASP A 411       4.567  -4.445  30.728  1.00 42.87           C  
ATOM   1626  C   ASP A 411       3.337  -4.611  29.843  1.00 40.88           C  
ATOM   1627  O   ASP A 411       3.296  -5.492  28.983  1.00 40.68           O  
ATOM   1628  CB  ASP A 411       4.375  -5.195  32.057  1.00 48.56           C  
ATOM   1629  CG  ASP A 411       5.626  -5.151  32.944  1.00 53.79           C  
ATOM   1630  OD1 ASP A 411       6.755  -5.048  32.402  1.00 56.37           O  
ATOM   1631  OD2 ASP A 411       5.483  -5.232  34.185  1.00 57.06           O  
ATOM   1632  N   ASN A 412       2.336  -3.760  30.053  1.00 40.95           N  
ATOM   1633  CA  ASN A 412       1.102  -3.793  29.257  1.00 40.91           C  
ATOM   1634  C   ASN A 412       1.429  -3.384  27.806  1.00 38.02           C  
ATOM   1635  O   ASN A 412       0.967  -3.994  26.843  1.00 36.82           O  
ATOM   1636  CB  ASN A 412       0.074  -2.828  29.863  1.00 44.82           C  
ATOM   1637  CG  ASN A 412      -1.343  -3.100  29.391  1.00 49.59           C  
ATOM   1638  OD1 ASN A 412      -2.247  -2.291  29.615  1.00 54.32           O  
ATOM   1639  ND2 ASN A 412      -1.551  -4.246  28.747  1.00 52.31           N  
ATOM   1640  N   LEU A 413       2.240  -2.343  27.669  1.00 36.00           N  
ATOM   1641  CA  LEU A 413       2.659  -1.850  26.366  1.00 34.64           C  
ATOM   1642  C   LEU A 413       3.499  -2.921  25.644  1.00 36.17           C  
ATOM   1643  O   LEU A 413       3.383  -3.102  24.426  1.00 33.15           O  
ATOM   1644  CB  LEU A 413       3.481  -0.559  26.551  1.00 34.00           C  
ATOM   1645  CG  LEU A 413       2.729   0.665  27.114  1.00 33.84           C  
ATOM   1646  CD1 LEU A 413       3.730   1.793  27.390  1.00 30.87           C  
ATOM   1647  CD2 LEU A 413       1.657   1.148  26.108  1.00 31.11           C  
ATOM   1648  N   LEU A 414       4.354  -3.623  26.394  1.00 35.77           N  
ATOM   1649  CA  LEU A 414       5.193  -4.671  25.797  1.00 35.57           C  
ATOM   1650  C   LEU A 414       4.317  -5.823  25.308  1.00 35.14           C  
ATOM   1651  O   LEU A 414       4.571  -6.388  24.250  1.00 36.91           O  
ATOM   1652  CB  LEU A 414       6.244  -5.168  26.807  1.00 32.48           C  
ATOM   1653  CG  LEU A 414       7.402  -4.191  27.082  1.00 31.72           C  
ATOM   1654  CD1 LEU A 414       8.098  -4.550  28.382  1.00 30.20           C  
ATOM   1655  CD2 LEU A 414       8.384  -4.217  25.910  1.00 28.92           C  
ATOM   1656  N   GLN A 415       3.282  -6.171  26.064  1.00 36.77           N  
ATOM   1657  CA  GLN A 415       2.384  -7.235  25.618  1.00 38.53           C  
ATOM   1658  C   GLN A 415       1.698  -6.801  24.310  1.00 38.74           C  
ATOM   1659  O   GLN A 415       1.488  -7.617  23.405  1.00 39.51           O  
ATOM   1660  CB  GLN A 415       1.309  -7.528  26.669  1.00 37.88           C  
ATOM   1661  CG  GLN A 415       1.811  -8.161  27.949  1.00 40.08           C  
ATOM   1662  CD  GLN A 415       0.697  -8.385  28.960  1.00 42.29           C  
ATOM   1663  OE1 GLN A 415       0.783  -7.929  30.103  1.00 44.10           O  
ATOM   1664  NE2 GLN A 415      -0.354  -9.092  28.544  1.00 41.12           N  
ATOM   1665  N   ALA A 416       1.341  -5.516  24.230  1.00 36.47           N  
ATOM   1666  CA  ALA A 416       0.685  -4.950  23.044  1.00 37.12           C  
ATOM   1667  C   ALA A 416       1.629  -4.940  21.841  1.00 34.92           C  
ATOM   1668  O   ALA A 416       1.247  -5.339  20.742  1.00 35.60           O  
ATOM   1669  CB  ALA A 416       0.187  -3.504  23.344  1.00 34.95           C  
ATOM   1670  N   LEU A 417       2.862  -4.477  22.055  1.00 35.31           N  
ATOM   1671  CA  LEU A 417       3.874  -4.436  21.001  1.00 35.35           C  
ATOM   1672  C   LEU A 417       4.141  -5.830  20.444  1.00 36.87           C  
ATOM   1673  O   LEU A 417       4.209  -6.025  19.230  1.00 36.24           O  
ATOM   1674  CB  LEU A 417       5.183  -3.864  21.542  1.00 35.43           C  
ATOM   1675  CG  LEU A 417       6.348  -3.729  20.550  1.00 35.59           C  
ATOM   1676  CD1 LEU A 417       5.910  -2.975  19.284  1.00 34.77           C  
ATOM   1677  CD2 LEU A 417       7.487  -2.991  21.227  1.00 34.48           C  
ATOM   1678  N   GLU A 418       4.296  -6.796  21.343  1.00 37.93           N  
ATOM   1679  CA  GLU A 418       4.565  -8.178  20.950  1.00 40.91           C  
ATOM   1680  C   GLU A 418       3.451  -8.750  20.072  1.00 40.01           C  
ATOM   1681  O   GLU A 418       3.713  -9.330  19.023  1.00 41.80           O  
ATOM   1682  CB  GLU A 418       4.744  -9.044  22.204  1.00 41.99           C  
ATOM   1683  CG  GLU A 418       4.891 -10.537  21.940  1.00 44.09           C  
ATOM   1684  CD  GLU A 418       5.129 -11.314  23.217  1.00 43.78           C  
ATOM   1685  OE1 GLU A 418       4.352 -11.128  24.171  1.00 45.87           O  
ATOM   1686  OE2 GLU A 418       6.089 -12.105  23.270  1.00 45.62           O  
ATOM   1687  N   LEU A 419       2.207  -8.596  20.508  1.00 40.89           N  
ATOM   1688  CA  LEU A 419       1.075  -9.098  19.735  1.00 40.33           C  
ATOM   1689  C   LEU A 419       0.994  -8.392  18.380  1.00 41.03           C  
ATOM   1690  O   LEU A 419       0.723  -9.012  17.346  1.00 41.69           O  
ATOM   1691  CB  LEU A 419      -0.228  -8.880  20.506  1.00 40.91           C  
ATOM   1692  CG  LEU A 419      -1.459  -9.439  19.789  1.00 41.08           C  
ATOM   1693  CD1 LEU A 419      -1.214 -10.903  19.429  1.00 42.21           C  
ATOM   1694  CD2 LEU A 419      -2.684  -9.299  20.674  1.00 41.32           C  
ATOM   1695  N   GLN A 420       1.237  -7.086  18.399  1.00 40.86           N  
ATOM   1696  CA  GLN A 420       1.208  -6.259  17.196  1.00 37.95           C  
ATOM   1697  C   GLN A 420       2.247  -6.722  16.185  1.00 38.50           C  
ATOM   1698  O   GLN A 420       1.985  -6.791  14.987  1.00 39.32           O  
ATOM   1699  CB  GLN A 420       1.474  -4.800  17.590  1.00 35.34           C  
ATOM   1700  CG  GLN A 420       1.817  -3.875  16.442  1.00 33.37           C  
ATOM   1701  CD  GLN A 420       0.674  -3.710  15.475  1.00 32.20           C  
ATOM   1702  OE1 GLN A 420      -0.477  -3.947  15.821  1.00 36.94           O  
ATOM   1703  NE2 GLN A 420       0.982  -3.289  14.262  1.00 33.58           N  
ATOM   1704  N   LEU A 421       3.444  -7.035  16.661  1.00 40.73           N  
ATOM   1705  CA  LEU A 421       4.498  -7.478  15.755  1.00 41.30           C  
ATOM   1706  C   LEU A 421       4.207  -8.878  15.229  1.00 42.38           C  
ATOM   1707  O   LEU A 421       4.506  -9.194  14.088  1.00 43.15           O  
ATOM   1708  CB  LEU A 421       5.860  -7.440  16.466  1.00 40.54           C  
ATOM   1709  CG  LEU A 421       6.327  -6.041  16.905  1.00 38.83           C  
ATOM   1710  CD1 LEU A 421       7.667  -6.137  17.640  1.00 36.70           C  
ATOM   1711  CD2 LEU A 421       6.454  -5.141  15.676  1.00 36.96           C  
ATOM   1712  N   LYS A 422       3.597  -9.709  16.059  1.00 44.42           N  
ATOM   1713  CA  LYS A 422       3.283 -11.076  15.657  1.00 47.34           C  
ATOM   1714  C   LYS A 422       2.223 -11.112  14.567  1.00 46.31           C  
ATOM   1715  O   LYS A 422       2.296 -11.919  13.647  1.00 47.24           O  
ATOM   1716  CB  LYS A 422       2.797 -11.874  16.868  1.00 51.11           C  
ATOM   1717  CG  LYS A 422       2.396 -13.305  16.562  1.00 54.72           C  
ATOM   1718  CD  LYS A 422       1.815 -13.987  17.796  1.00 56.80           C  
ATOM   1719  CE  LYS A 422       1.346 -15.399  17.462  1.00 59.09           C  
ATOM   1720  NZ  LYS A 422       0.767 -16.085  18.648  1.00 60.37           N  
ATOM   1721  N   LEU A 423       1.238 -10.229  14.681  1.00 46.29           N  
ATOM   1722  CA  LEU A 423       0.149 -10.148  13.713  1.00 44.64           C  
ATOM   1723  C   LEU A 423       0.539  -9.372  12.464  1.00 44.26           C  
ATOM   1724  O   LEU A 423       0.159  -9.748  11.356  1.00 44.51           O  
ATOM   1725  CB  LEU A 423      -1.077  -9.478  14.356  1.00 44.84           C  
ATOM   1726  CG  LEU A 423      -1.794 -10.206  15.502  1.00 46.34           C  
ATOM   1727  CD1 LEU A 423      -2.773  -9.259  16.206  1.00 44.44           C  
ATOM   1728  CD2 LEU A 423      -2.523 -11.430  14.950  1.00 45.73           C  
ATOM   1729  N   ASN A 424       1.306  -8.296  12.645  1.00 43.74           N  
ATOM   1730  CA  ASN A 424       1.711  -7.440  11.537  1.00 43.24           C  
ATOM   1731  C   ASN A 424       2.911  -7.956  10.749  1.00 45.20           C  
ATOM   1732  O   ASN A 424       3.075  -7.614   9.579  1.00 43.93           O  
ATOM   1733  CB  ASN A 424       1.979  -6.017  12.060  1.00 44.75           C  
ATOM   1734  CG  ASN A 424       1.938  -4.961  10.958  1.00 44.02           C  
ATOM   1735  OD1 ASN A 424       1.081  -5.006  10.079  1.00 43.46           O  
ATOM   1736  ND2 ASN A 424       2.856  -3.998  11.014  1.00 44.01           N  
ATOM   1737  N   HIS A 425       3.750  -8.776  11.384  1.00 45.67           N  
ATOM   1738  CA  HIS A 425       4.922  -9.344  10.717  1.00 45.21           C  
ATOM   1739  C   HIS A 425       5.057 -10.838  11.022  1.00 47.73           C  
ATOM   1740  O   HIS A 425       6.066 -11.284  11.580  1.00 46.15           O  
ATOM   1741  CB  HIS A 425       6.200  -8.635  11.163  1.00 44.16           C  
ATOM   1742  CG  HIS A 425       6.261  -7.191  10.784  1.00 42.40           C  
ATOM   1743  ND1 HIS A 425       5.577  -6.210  11.471  1.00 42.31           N  
ATOM   1744  CD2 HIS A 425       6.957  -6.555   9.812  1.00 42.57           C  
ATOM   1745  CE1 HIS A 425       5.854  -5.032  10.943  1.00 39.20           C  
ATOM   1746  NE2 HIS A 425       6.688  -5.212   9.935  1.00 42.66           N  
ATOM   1747  N   PRO A 426       4.049 -11.632  10.632  1.00 49.46           N  
ATOM   1748  CA  PRO A 426       3.990 -13.083  10.841  1.00 52.00           C  
ATOM   1749  C   PRO A 426       5.250 -13.829  10.430  1.00 52.56           C  
ATOM   1750  O   PRO A 426       5.611 -14.834  11.038  1.00 54.73           O  
ATOM   1751  CB  PRO A 426       2.797 -13.509   9.984  1.00 50.96           C  
ATOM   1752  CG  PRO A 426       1.939 -12.298   9.966  1.00 52.49           C  
ATOM   1753  CD  PRO A 426       2.944 -11.198   9.760  1.00 52.13           C  
ATOM   1754  N   GLU A 427       5.915 -13.323   9.400  1.00 53.11           N  
ATOM   1755  CA  GLU A 427       7.111 -13.950   8.862  1.00 52.98           C  
ATOM   1756  C   GLU A 427       8.441 -13.383   9.358  1.00 52.35           C  
ATOM   1757  O   GLU A 427       9.496 -13.757   8.846  1.00 53.33           O  
ATOM   1758  CB  GLU A 427       7.070 -13.857   7.339  1.00 53.13           C  
ATOM   1759  CG  GLU A 427       7.441 -12.478   6.775  1.00 56.49           C  
ATOM   1760  CD  GLU A 427       6.789 -11.308   7.513  1.00 56.33           C  
ATOM   1761  OE1 GLU A 427       5.560 -11.335   7.739  1.00 56.64           O  
ATOM   1762  OE2 GLU A 427       7.515 -10.349   7.856  1.00 57.95           O  
ATOM   1763  N   SER A 428       8.406 -12.479  10.329  1.00 50.04           N  
ATOM   1764  CA  SER A 428       9.645 -11.900  10.831  1.00 49.43           C  
ATOM   1765  C   SER A 428       9.942 -12.463  12.210  1.00 48.47           C  
ATOM   1766  O   SER A 428       9.451 -11.960  13.224  1.00 48.42           O  
ATOM   1767  CB  SER A 428       9.539 -10.377  10.896  1.00 50.64           C  
ATOM   1768  OG  SER A 428      10.772  -9.813  11.322  1.00 54.72           O  
ATOM   1769  N   SER A 429      10.770 -13.503  12.234  1.00 46.24           N  
ATOM   1770  CA  SER A 429      11.112 -14.189  13.469  1.00 44.53           C  
ATOM   1771  C   SER A 429      11.873 -13.379  14.501  1.00 42.30           C  
ATOM   1772  O   SER A 429      12.925 -12.802  14.222  1.00 41.86           O  
ATOM   1773  CB  SER A 429      11.904 -15.467  13.157  1.00 46.14           C  
ATOM   1774  OG  SER A 429      12.017 -16.281  14.319  1.00 48.35           O  
ATOM   1775  N   GLN A 430      11.323 -13.340  15.704  1.00 42.60           N  
ATOM   1776  CA  GLN A 430      11.970 -12.648  16.800  1.00 44.13           C  
ATOM   1777  C   GLN A 430      12.104 -11.135  16.560  1.00 41.88           C  
ATOM   1778  O   GLN A 430      12.987 -10.493  17.129  1.00 41.51           O  
ATOM   1779  CB  GLN A 430      13.352 -13.288  17.010  1.00 45.48           C  
ATOM   1780  CG  GLN A 430      13.818 -13.391  18.445  1.00 48.56           C  
ATOM   1781  CD  GLN A 430      12.941 -14.286  19.292  1.00 47.42           C  
ATOM   1782  OE1 GLN A 430      12.370 -15.265  18.808  1.00 48.58           O  
ATOM   1783  NE2 GLN A 430      12.849 -13.967  20.573  1.00 49.23           N  
ATOM   1784  N   LEU A 431      11.228 -10.565  15.734  1.00 39.89           N  
ATOM   1785  CA  LEU A 431      11.285  -9.128  15.461  1.00 38.12           C  
ATOM   1786  C   LEU A 431      11.242  -8.366  16.779  1.00 34.81           C  
ATOM   1787  O   LEU A 431      12.004  -7.419  16.994  1.00 35.66           O  
ATOM   1788  CB  LEU A 431      10.110  -8.690  14.569  1.00 37.35           C  
ATOM   1789  CG  LEU A 431      10.086  -7.203  14.182  1.00 36.15           C  
ATOM   1790  CD1 LEU A 431      11.391  -6.817  13.457  1.00 32.93           C  
ATOM   1791  CD2 LEU A 431       8.878  -6.933  13.292  1.00 34.92           C  
ATOM   1792  N   PHE A 432      10.345  -8.793  17.656  1.00 35.20           N  
ATOM   1793  CA  PHE A 432      10.180  -8.182  18.973  1.00 36.51           C  
ATOM   1794  C   PHE A 432      11.531  -8.065  19.688  1.00 36.97           C  
ATOM   1795  O   PHE A 432      11.925  -6.979  20.115  1.00 37.35           O  
ATOM   1796  CB  PHE A 432       9.195  -9.018  19.798  1.00 33.54           C  
ATOM   1797  CG  PHE A 432       8.859  -8.430  21.144  1.00 35.95           C  
ATOM   1798  CD1 PHE A 432       8.468  -7.092  21.268  1.00 35.86           C  
ATOM   1799  CD2 PHE A 432       8.858  -9.233  22.283  1.00 33.38           C  
ATOM   1800  CE1 PHE A 432       8.076  -6.569  22.506  1.00 34.10           C  
ATOM   1801  CE2 PHE A 432       8.466  -8.723  23.525  1.00 35.39           C  
ATOM   1802  CZ  PHE A 432       8.071  -7.383  23.639  1.00 34.13           C  
ATOM   1803  N   ALA A 433      12.249  -9.178  19.808  1.00 38.33           N  
ATOM   1804  CA  ALA A 433      13.555  -9.151  20.466  1.00 38.62           C  
ATOM   1805  C   ALA A 433      14.500  -8.238  19.691  1.00 37.49           C  
ATOM   1806  O   ALA A 433      15.219  -7.420  20.282  1.00 37.99           O  
ATOM   1807  CB  ALA A 433      14.137 -10.562  20.548  1.00 38.93           C  
ATOM   1808  N   LYS A 434      14.489  -8.366  18.365  1.00 37.05           N  
ATOM   1809  CA  LYS A 434      15.361  -7.554  17.519  1.00 37.61           C  
ATOM   1810  C   LYS A 434      15.104  -6.067  17.712  1.00 37.41           C  
ATOM   1811  O   LYS A 434      16.051  -5.280  17.775  1.00 35.81           O  
ATOM   1812  CB  LYS A 434      15.186  -7.925  16.042  1.00 40.87           C  
ATOM   1813  CG  LYS A 434      15.629  -9.348  15.683  1.00 46.77           C  
ATOM   1814  CD  LYS A 434      17.103  -9.579  15.994  1.00 49.60           C  
ATOM   1815  CE  LYS A 434      17.551 -10.992  15.610  1.00 53.55           C  
ATOM   1816  NZ  LYS A 434      19.001 -11.265  15.891  1.00 52.30           N  
ATOM   1817  N   LEU A 435      13.829  -5.681  17.818  1.00 36.73           N  
ATOM   1818  CA  LEU A 435      13.489  -4.271  18.021  1.00 35.57           C  
ATOM   1819  C   LEU A 435      13.943  -3.792  19.389  1.00 35.93           C  
ATOM   1820  O   LEU A 435      14.529  -2.714  19.507  1.00 37.77           O  
ATOM   1821  CB  LEU A 435      11.981  -4.043  17.877  1.00 34.95           C  
ATOM   1822  CG  LEU A 435      11.478  -2.607  18.110  1.00 33.54           C  
ATOM   1823  CD1 LEU A 435      12.221  -1.649  17.205  1.00 31.06           C  
ATOM   1824  CD2 LEU A 435       9.972  -2.535  17.838  1.00 33.45           C  
ATOM   1825  N   LEU A 436      13.684  -4.593  20.422  1.00 35.47           N  
ATOM   1826  CA  LEU A 436      14.080  -4.230  21.783  1.00 35.01           C  
ATOM   1827  C   LEU A 436      15.578  -3.999  21.923  1.00 35.93           C  
ATOM   1828  O   LEU A 436      16.002  -3.156  22.708  1.00 35.07           O  
ATOM   1829  CB  LEU A 436      13.621  -5.298  22.775  1.00 33.48           C  
ATOM   1830  CG  LEU A 436      12.106  -5.376  22.957  1.00 36.23           C  
ATOM   1831  CD1 LEU A 436      11.736  -6.649  23.691  1.00 36.17           C  
ATOM   1832  CD2 LEU A 436      11.608  -4.131  23.710  1.00 38.00           C  
ATOM   1833  N   GLN A 437      16.372  -4.743  21.151  1.00 38.90           N  
ATOM   1834  CA  GLN A 437      17.825  -4.615  21.172  1.00 38.61           C  
ATOM   1835  C   GLN A 437      18.252  -3.299  20.553  1.00 39.78           C  
ATOM   1836  O   GLN A 437      19.297  -2.753  20.897  1.00 39.58           O  
ATOM   1837  CB  GLN A 437      18.487  -5.762  20.406  1.00 39.56           C  
ATOM   1838  CG  GLN A 437      18.191  -7.147  20.958  1.00 43.20           C  
ATOM   1839  CD  GLN A 437      19.234  -8.165  20.544  1.00 46.32           C  
ATOM   1840  OE1 GLN A 437      20.375  -8.118  21.012  1.00 49.70           O  
ATOM   1841  NE2 GLN A 437      18.857  -9.085  19.658  1.00 44.87           N  
ATOM   1842  N   LYS A 438      17.448  -2.793  19.626  1.00 40.20           N  
ATOM   1843  CA  LYS A 438      17.752  -1.524  18.983  1.00 41.72           C  
ATOM   1844  C   LYS A 438      17.764  -0.435  20.036  1.00 42.58           C  
ATOM   1845  O   LYS A 438      18.325   0.643  19.830  1.00 43.92           O  
ATOM   1846  CB  LYS A 438      16.700  -1.198  17.914  1.00 41.47           C  
ATOM   1847  CG  LYS A 438      16.865  -2.006  16.636  1.00 41.72           C  
ATOM   1848  CD  LYS A 438      18.192  -1.680  15.950  1.00 42.49           C  
ATOM   1849  CE  LYS A 438      18.378  -2.533  14.720  1.00 42.46           C  
ATOM   1850  NZ  LYS A 438      18.322  -3.972  15.104  1.00 47.21           N  
ATOM   1851  N   MET A 439      17.130  -0.726  21.166  1.00 44.01           N  
ATOM   1852  CA  MET A 439      17.054   0.223  22.260  1.00 45.63           C  
ATOM   1853  C   MET A 439      18.435   0.580  22.786  1.00 46.24           C  
ATOM   1854  O   MET A 439      18.614   1.632  23.395  1.00 46.59           O  
ATOM   1855  CB  MET A 439      16.177  -0.344  23.383  1.00 46.58           C  
ATOM   1856  CG  MET A 439      14.692  -0.373  23.032  1.00 48.98           C  
ATOM   1857  SD  MET A 439      13.595  -0.861  24.390  1.00 53.41           S  
ATOM   1858  CE  MET A 439      13.829   0.513  25.541  1.00 50.81           C  
ATOM   1859  N   THR A 440      19.414  -0.286  22.530  1.00 47.36           N  
ATOM   1860  CA  THR A 440      20.780  -0.054  22.993  1.00 46.90           C  
ATOM   1861  C   THR A 440      21.489   0.897  22.046  1.00 45.67           C  
ATOM   1862  O   THR A 440      22.315   1.701  22.458  1.00 45.62           O  
ATOM   1863  CB  THR A 440      21.588  -1.391  23.097  1.00 48.63           C  
ATOM   1864  OG1 THR A 440      22.744  -1.193  23.920  1.00 51.91           O  
ATOM   1865  CG2 THR A 440      22.059  -1.853  21.729  1.00 49.70           C  
ATOM   1866  N   ASP A 441      21.151   0.809  20.767  1.00 45.66           N  
ATOM   1867  CA  ASP A 441      21.752   1.674  19.763  1.00 46.03           C  
ATOM   1868  C   ASP A 441      21.323   3.121  19.993  1.00 44.41           C  
ATOM   1869  O   ASP A 441      22.107   4.043  19.796  1.00 44.09           O  
ATOM   1870  CB  ASP A 441      21.335   1.218  18.363  1.00 47.60           C  
ATOM   1871  CG  ASP A 441      21.870  -0.160  18.015  1.00 49.99           C  
ATOM   1872  OD1 ASP A 441      23.081  -0.275  17.728  1.00 54.26           O  
ATOM   1873  OD2 ASP A 441      21.085  -1.130  18.038  1.00 50.63           O  
ATOM   1874  N   LEU A 442      20.076   3.318  20.409  1.00 45.05           N  
ATOM   1875  CA  LEU A 442      19.578   4.666  20.664  1.00 45.91           C  
ATOM   1876  C   LEU A 442      20.372   5.317  21.789  1.00 45.76           C  
ATOM   1877  O   LEU A 442      20.835   6.450  21.648  1.00 44.38           O  
ATOM   1878  CB  LEU A 442      18.087   4.635  21.021  1.00 44.72           C  
ATOM   1879  CG  LEU A 442      17.135   4.217  19.892  1.00 44.83           C  
ATOM   1880  CD1 LEU A 442      15.740   4.040  20.442  1.00 43.23           C  
ATOM   1881  CD2 LEU A 442      17.143   5.262  18.786  1.00 43.50           C  
ATOM   1882  N   ARG A 443      20.525   4.598  22.902  1.00 47.36           N  
ATOM   1883  CA  ARG A 443      21.275   5.104  24.054  1.00 48.95           C  
ATOM   1884  C   ARG A 443      22.645   5.609  23.601  1.00 49.33           C  
ATOM   1885  O   ARG A 443      23.071   6.707  23.972  1.00 50.13           O  
ATOM   1886  CB  ARG A 443      21.456   3.999  25.116  1.00 50.71           C  
ATOM   1887  CG  ARG A 443      20.371   3.942  26.202  1.00 52.55           C  
ATOM   1888  CD  ARG A 443      20.364   5.195  27.081  1.00 52.81           C  
ATOM   1889  NE  ARG A 443      19.466   5.083  28.236  1.00 55.75           N  
ATOM   1890  CZ  ARG A 443      19.287   6.043  29.154  1.00 57.82           C  
ATOM   1891  NH1 ARG A 443      19.942   7.198  29.054  1.00 57.33           N  
ATOM   1892  NH2 ARG A 443      18.465   5.853  30.188  1.00 55.49           N  
ATOM   1893  N   GLN A 444      23.329   4.805  22.792  1.00 49.72           N  
ATOM   1894  CA  GLN A 444      24.647   5.170  22.284  1.00 49.42           C  
ATOM   1895  C   GLN A 444      24.551   6.465  21.481  1.00 47.99           C  
ATOM   1896  O   GLN A 444      25.366   7.373  21.658  1.00 46.47           O  
ATOM   1897  CB  GLN A 444      25.196   4.053  21.391  1.00 52.80           C  
ATOM   1898  CG  GLN A 444      24.996   2.643  21.950  1.00 58.07           C  
ATOM   1899  CD  GLN A 444      25.674   2.427  23.296  1.00 60.45           C  
ATOM   1900  OE1 GLN A 444      26.877   2.655  23.444  1.00 64.26           O  
ATOM   1901  NE2 GLN A 444      24.903   1.976  24.283  1.00 61.99           N  
ATOM   1902  N   ILE A 445      23.558   6.541  20.594  1.00 45.68           N  
ATOM   1903  CA  ILE A 445      23.356   7.739  19.779  1.00 45.38           C  
ATOM   1904  C   ILE A 445      23.200   8.970  20.675  1.00 43.57           C  
ATOM   1905  O   ILE A 445      23.886   9.970  20.492  1.00 41.53           O  
ATOM   1906  CB  ILE A 445      22.089   7.628  18.910  1.00 45.30           C  
ATOM   1907  CG1 ILE A 445      22.193   6.416  17.986  1.00 45.74           C  
ATOM   1908  CG2 ILE A 445      21.905   8.897  18.092  1.00 46.11           C  
ATOM   1909  CD1 ILE A 445      23.227   6.561  16.903  1.00 47.69           C  
ATOM   1910  N   VAL A 446      22.295   8.881  21.642  1.00 43.53           N  
ATOM   1911  CA  VAL A 446      22.046   9.986  22.553  1.00 46.91           C  
ATOM   1912  C   VAL A 446      23.317  10.442  23.274  1.00 49.52           C  
ATOM   1913  O   VAL A 446      23.725  11.609  23.171  1.00 48.75           O  
ATOM   1914  CB  VAL A 446      20.986   9.606  23.607  1.00 46.60           C  
ATOM   1915  CG1 VAL A 446      20.802  10.757  24.590  1.00 48.05           C  
ATOM   1916  CG2 VAL A 446      19.655   9.271  22.922  1.00 46.66           C  
ATOM   1917  N   THR A 447      23.941   9.522  24.002  1.00 51.45           N  
ATOM   1918  CA  THR A 447      25.159   9.848  24.735  1.00 54.71           C  
ATOM   1919  C   THR A 447      26.167  10.474  23.781  1.00 56.35           C  
ATOM   1920  O   THR A 447      26.729  11.535  24.055  1.00 56.84           O  
ATOM   1921  CB  THR A 447      25.786   8.599  25.359  1.00 54.61           C  
ATOM   1922  OG1 THR A 447      24.819   7.937  26.183  1.00 55.19           O  
ATOM   1923  CG2 THR A 447      26.981   8.983  26.210  1.00 57.05           C  
ATOM   1924  N   GLU A 448      26.374   9.813  22.649  1.00 57.76           N  
ATOM   1925  CA  GLU A 448      27.311  10.289  21.645  1.00 58.44           C  
ATOM   1926  C   GLU A 448      26.957  11.718  21.268  1.00 58.22           C  
ATOM   1927  O   GLU A 448      27.830  12.577  21.153  1.00 59.25           O  
ATOM   1928  CB  GLU A 448      27.242   9.385  20.414  1.00 60.81           C  
ATOM   1929  CG  GLU A 448      28.469   9.429  19.522  1.00 64.12           C  
ATOM   1930  CD  GLU A 448      28.429   8.362  18.444  1.00 64.55           C  
ATOM   1931  OE1 GLU A 448      27.656   8.514  17.478  1.00 64.57           O  
ATOM   1932  OE2 GLU A 448      29.164   7.362  18.576  1.00 66.86           O  
ATOM   1933  N   HIS A 449      25.665  11.968  21.087  1.00 57.54           N  
ATOM   1934  CA  HIS A 449      25.178  13.294  20.717  1.00 57.44           C  
ATOM   1935  C   HIS A 449      25.522  14.315  21.804  1.00 56.66           C  
ATOM   1936  O   HIS A 449      25.985  15.415  21.516  1.00 56.49           O  
ATOM   1937  CB  HIS A 449      23.657  13.254  20.508  1.00 57.03           C  
ATOM   1938  CG  HIS A 449      23.084  14.535  19.985  1.00 57.07           C  
ATOM   1939  ND1 HIS A 449      23.163  14.897  18.658  1.00 57.11           N  
ATOM   1940  CD2 HIS A 449      22.453  15.554  20.617  1.00 56.76           C  
ATOM   1941  CE1 HIS A 449      22.606  16.084  18.494  1.00 56.30           C  
ATOM   1942  NE2 HIS A 449      22.167  16.504  19.668  1.00 56.60           N  
ATOM   1943  N   VAL A 450      25.285  13.935  23.054  1.00 57.53           N  
ATOM   1944  CA  VAL A 450      25.567  14.798  24.193  1.00 57.79           C  
ATOM   1945  C   VAL A 450      27.015  15.290  24.218  1.00 58.64           C  
ATOM   1946  O   VAL A 450      27.262  16.490  24.308  1.00 59.00           O  
ATOM   1947  CB  VAL A 450      25.258  14.065  25.520  1.00 57.96           C  
ATOM   1948  CG1 VAL A 450      25.819  14.845  26.699  1.00 58.10           C  
ATOM   1949  CG2 VAL A 450      23.753  13.902  25.680  1.00 57.16           C  
ATOM   1950  N   GLN A 451      27.970  14.369  24.129  1.00 59.92           N  
ATOM   1951  CA  GLN A 451      29.382  14.742  24.159  1.00 61.49           C  
ATOM   1952  C   GLN A 451      29.696  15.787  23.099  1.00 61.66           C  
ATOM   1953  O   GLN A 451      30.240  16.853  23.398  1.00 63.57           O  
ATOM   1954  CB  GLN A 451      30.279  13.532  23.906  1.00 62.45           C  
ATOM   1955  CG  GLN A 451      29.601  12.191  24.016  1.00 65.23           C  
ATOM   1956  CD  GLN A 451      30.451  11.077  23.432  1.00 65.96           C  
ATOM   1957  OE1 GLN A 451      30.048   9.915  23.420  1.00 67.30           O  
ATOM   1958  NE2 GLN A 451      31.634  11.430  22.940  1.00 65.76           N  
ATOM   1959  N   LEU A 452      29.362  15.466  21.855  1.00 60.72           N  
ATOM   1960  CA  LEU A 452      29.614  16.366  20.745  1.00 59.24           C  
ATOM   1961  C   LEU A 452      29.002  17.727  21.036  1.00 59.27           C  
ATOM   1962  O   LEU A 452      29.561  18.766  20.681  1.00 58.10           O  
ATOM   1963  CB  LEU A 452      29.022  15.784  19.462  1.00 60.32           C  
ATOM   1964  CG  LEU A 452      29.270  16.547  18.160  1.00 60.41           C  
ATOM   1965  CD1 LEU A 452      30.760  16.771  17.960  1.00 60.35           C  
ATOM   1966  CD2 LEU A 452      28.689  15.755  17.000  1.00 61.37           C  
ATOM   1967  N   LEU A 453      27.850  17.718  21.696  1.00 58.53           N  
ATOM   1968  CA  LEU A 453      27.172  18.957  22.032  1.00 59.32           C  
ATOM   1969  C   LEU A 453      28.051  19.794  22.971  1.00 60.33           C  
ATOM   1970  O   LEU A 453      28.087  21.023  22.875  1.00 61.90           O  
ATOM   1971  CB  LEU A 453      25.829  18.644  22.685  1.00 58.60           C  
ATOM   1972  CG  LEU A 453      24.773  19.738  22.563  1.00 59.64           C  
ATOM   1973  CD1 LEU A 453      24.495  20.032  21.094  1.00 59.46           C  
ATOM   1974  CD2 LEU A 453      23.506  19.282  23.264  1.00 60.73           C  
ATOM   1975  N   GLN A 454      28.764  19.123  23.874  1.00 60.25           N  
ATOM   1976  CA  GLN A 454      29.657  19.805  24.806  1.00 60.71           C  
ATOM   1977  C   GLN A 454      30.825  20.444  24.059  1.00 59.83           C  
ATOM   1978  O   GLN A 454      31.361  21.468  24.481  1.00 60.02           O  
ATOM   1979  CB  GLN A 454      30.183  18.821  25.851  1.00 61.35           C  
ATOM   1980  CG  GLN A 454      29.157  18.435  26.914  1.00 64.47           C  
ATOM   1981  CD  GLN A 454      28.827  19.581  27.865  1.00 67.08           C  
ATOM   1982  OE1 GLN A 454      27.913  19.478  28.687  1.00 68.13           O  
ATOM   1983  NE2 GLN A 454      29.579  20.677  27.762  1.00 69.04           N  
ATOM   1984  N   VAL A 455      31.215  19.836  22.943  1.00 59.19           N  
ATOM   1985  CA  VAL A 455      32.306  20.362  22.132  1.00 59.04           C  
ATOM   1986  C   VAL A 455      31.861  21.661  21.466  1.00 59.38           C  
ATOM   1987  O   VAL A 455      32.608  22.641  21.424  1.00 59.20           O  
ATOM   1988  CB  VAL A 455      32.731  19.355  21.037  1.00 57.96           C  
ATOM   1989  CG1 VAL A 455      33.739  19.996  20.104  1.00 56.61           C  
ATOM   1990  CG2 VAL A 455      33.334  18.119  21.677  1.00 58.43           C  
ATOM   1991  N   ILE A 456      30.637  21.660  20.947  1.00 59.96           N  
ATOM   1992  CA  ILE A 456      30.071  22.836  20.287  1.00 61.00           C  
ATOM   1993  C   ILE A 456      30.081  24.040  21.231  1.00 60.47           C  
ATOM   1994  O   ILE A 456      30.552  25.124  20.883  1.00 60.96           O  
ATOM   1995  CB  ILE A 456      28.613  22.563  19.840  1.00 60.98           C  
ATOM   1996  CG1 ILE A 456      28.584  21.429  18.811  1.00 61.83           C  
ATOM   1997  CG2 ILE A 456      27.998  23.824  19.248  1.00 62.76           C  
ATOM   1998  CD1 ILE A 456      29.390  21.713  17.552  1.00 61.91           C  
ATOM   1999  N   LYS A 457      29.553  23.833  22.430  1.00 60.78           N  
ATOM   2000  CA  LYS A 457      29.486  24.875  23.445  1.00 61.21           C  
ATOM   2001  C   LYS A 457      30.832  25.557  23.691  1.00 60.66           C  
ATOM   2002  O   LYS A 457      30.889  26.759  23.948  1.00 61.52           O  
ATOM   2003  CB  LYS A 457      28.963  24.274  24.754  1.00 62.58           C  
ATOM   2004  CG  LYS A 457      28.957  25.225  25.940  1.00 65.60           C  
ATOM   2005  CD  LYS A 457      27.587  25.263  26.607  1.00 68.15           C  
ATOM   2006  CE  LYS A 457      27.616  26.066  27.900  1.00 69.15           C  
ATOM   2007  NZ  LYS A 457      28.147  27.448  27.700  1.00 71.72           N  
ATOM   2008  N   LYS A 458      31.916  24.796  23.600  1.00 59.30           N  
ATOM   2009  CA  LYS A 458      33.242  25.346  23.843  1.00 58.34           C  
ATOM   2010  C   LYS A 458      33.896  25.982  22.628  1.00 58.51           C  
ATOM   2011  O   LYS A 458      34.699  26.903  22.769  1.00 58.95           O  
ATOM   2012  CB  LYS A 458      34.158  24.264  24.406  1.00 57.61           C  
ATOM   2013  CG  LYS A 458      33.814  23.849  25.825  1.00 56.80           C  
ATOM   2014  CD  LYS A 458      34.674  22.677  26.260  1.00 58.05           C  
ATOM   2015  CE  LYS A 458      34.404  22.286  27.702  1.00 58.13           C  
ATOM   2016  NZ  LYS A 458      34.895  23.312  28.664  1.00 59.63           N  
ATOM   2017  N   THR A 459      33.556  25.499  21.438  1.00 58.15           N  
ATOM   2018  CA  THR A 459      34.140  26.043  20.222  1.00 59.08           C  
ATOM   2019  C   THR A 459      33.247  27.112  19.594  1.00 59.61           C  
ATOM   2020  O   THR A 459      33.709  27.925  18.794  1.00 58.73           O  
ATOM   2021  CB  THR A 459      34.422  24.923  19.190  1.00 59.59           C  
ATOM   2022  OG1 THR A 459      33.211  24.210  18.894  1.00 60.45           O  
ATOM   2023  CG2 THR A 459      35.455  23.948  19.748  1.00 59.63           C  
ATOM   2024  N   GLU A 460      31.970  27.105  19.964  1.00 60.27           N  
ATOM   2025  CA  GLU A 460      31.015  28.079  19.448  1.00 61.21           C  
ATOM   2026  C   GLU A 460      30.335  28.820  20.599  1.00 60.54           C  
ATOM   2027  O   GLU A 460      29.133  28.675  20.813  1.00 61.10           O  
ATOM   2028  CB  GLU A 460      29.950  27.380  18.599  1.00 63.00           C  
ATOM   2029  CG  GLU A 460      29.874  27.875  17.163  1.00 64.27           C  
ATOM   2030  CD  GLU A 460      31.082  27.464  16.351  1.00 64.65           C  
ATOM   2031  OE1 GLU A 460      31.297  26.246  16.193  1.00 64.32           O  
ATOM   2032  OE2 GLU A 460      31.820  28.352  15.877  1.00 66.36           O  
ATOM   2033  N   THR A 461      31.100  29.616  21.340  1.00 60.04           N  
ATOM   2034  CA  THR A 461      30.543  30.362  22.469  1.00 59.71           C  
ATOM   2035  C   THR A 461      29.564  31.442  22.027  1.00 58.36           C  
ATOM   2036  O   THR A 461      28.970  32.131  22.857  1.00 56.72           O  
ATOM   2037  CB  THR A 461      31.653  31.023  23.305  1.00 59.97           C  
ATOM   2038  OG1 THR A 461      32.587  31.673  22.432  1.00 60.55           O  
ATOM   2039  CG2 THR A 461      32.368  29.980  24.160  1.00 59.94           C  
ATOM   2040  N   ASP A 462      29.395  31.574  20.717  1.00 57.85           N  
ATOM   2041  CA  ASP A 462      28.493  32.560  20.156  1.00 58.83           C  
ATOM   2042  C   ASP A 462      27.191  31.921  19.692  1.00 59.46           C  
ATOM   2043  O   ASP A 462      26.241  32.621  19.344  1.00 60.29           O  
ATOM   2044  CB  ASP A 462      29.164  33.271  18.980  1.00 61.17           C  
ATOM   2045  CG  ASP A 462      29.667  32.305  17.922  1.00 62.07           C  
ATOM   2046  OD1 ASP A 462      30.481  31.417  18.261  1.00 63.15           O  
ATOM   2047  OD2 ASP A 462      29.249  32.439  16.754  1.00 62.38           O  
ATOM   2048  N   MET A 463      27.140  30.595  19.690  1.00 59.65           N  
ATOM   2049  CA  MET A 463      25.932  29.906  19.252  1.00 60.24           C  
ATOM   2050  C   MET A 463      25.047  29.567  20.443  1.00 59.01           C  
ATOM   2051  O   MET A 463      25.509  29.003  21.432  1.00 59.22           O  
ATOM   2052  CB  MET A 463      26.288  28.635  18.489  1.00 62.64           C  
ATOM   2053  CG  MET A 463      25.182  28.185  17.564  1.00 65.51           C  
ATOM   2054  SD  MET A 463      25.434  26.506  17.033  1.00 70.18           S  
ATOM   2055  CE  MET A 463      24.653  25.670  18.366  1.00 68.05           C  
ATOM   2056  N   SER A 464      23.767  29.904  20.335  1.00 58.10           N  
ATOM   2057  CA  SER A 464      22.832  29.678  21.421  1.00 57.32           C  
ATOM   2058  C   SER A 464      22.025  28.395  21.334  1.00 57.48           C  
ATOM   2059  O   SER A 464      21.744  27.894  20.245  1.00 58.03           O  
ATOM   2060  CB  SER A 464      21.883  30.868  21.524  1.00 56.45           C  
ATOM   2061  OG  SER A 464      21.268  31.116  20.276  1.00 57.82           O  
ATOM   2062  N   LEU A 465      21.656  27.872  22.499  1.00 56.81           N  
ATOM   2063  CA  LEU A 465      20.863  26.656  22.579  1.00 57.09           C  
ATOM   2064  C   LEU A 465      19.556  26.960  23.300  1.00 57.50           C  
ATOM   2065  O   LEU A 465      19.536  27.726  24.266  1.00 58.14           O  
ATOM   2066  CB  LEU A 465      21.627  25.563  23.332  1.00 55.57           C  
ATOM   2067  CG  LEU A 465      23.035  25.227  22.835  1.00 54.98           C  
ATOM   2068  CD1 LEU A 465      23.409  23.845  23.351  1.00 56.40           C  
ATOM   2069  CD2 LEU A 465      23.093  25.234  21.312  1.00 54.16           C  
ATOM   2070  N   HIS A 466      18.467  26.361  22.829  1.00 57.80           N  
ATOM   2071  CA  HIS A 466      17.162  26.582  23.442  1.00 59.91           C  
ATOM   2072  C   HIS A 466      17.148  26.038  24.876  1.00 60.18           C  
ATOM   2073  O   HIS A 466      17.633  24.934  25.136  1.00 60.58           O  
ATOM   2074  CB  HIS A 466      16.073  25.908  22.606  1.00 60.96           C  
ATOM   2075  CG  HIS A 466      14.685  26.323  22.977  1.00 62.58           C  
ATOM   2076  ND1 HIS A 466      14.197  26.223  24.262  1.00 63.18           N  
ATOM   2077  CD2 HIS A 466      13.674  26.822  22.228  1.00 64.34           C  
ATOM   2078  CE1 HIS A 466      12.945  26.640  24.289  1.00 63.72           C  
ATOM   2079  NE2 HIS A 466      12.602  27.009  23.067  1.00 65.11           N  
ATOM   2080  N   PRO A 467      16.589  26.810  25.825  1.00 60.01           N  
ATOM   2081  CA  PRO A 467      16.503  26.436  27.244  1.00 59.41           C  
ATOM   2082  C   PRO A 467      15.926  25.036  27.483  1.00 58.93           C  
ATOM   2083  O   PRO A 467      16.445  24.261  28.294  1.00 59.11           O  
ATOM   2084  CB  PRO A 467      15.614  27.530  27.832  1.00 59.59           C  
ATOM   2085  CG  PRO A 467      15.918  28.708  26.972  1.00 59.65           C  
ATOM   2086  CD  PRO A 467      15.935  28.110  25.592  1.00 59.00           C  
ATOM   2087  N   LEU A 468      14.842  24.728  26.782  1.00 57.05           N  
ATOM   2088  CA  LEU A 468      14.193  23.432  26.900  1.00 57.71           C  
ATOM   2089  C   LEU A 468      15.196  22.299  26.666  1.00 57.66           C  
ATOM   2090  O   LEU A 468      15.413  21.454  27.541  1.00 58.24           O  
ATOM   2091  CB  LEU A 468      13.046  23.339  25.891  1.00 55.79           C  
ATOM   2092  CG  LEU A 468      12.431  21.951  25.726  1.00 58.01           C  
ATOM   2093  CD1 LEU A 468      11.905  21.465  27.066  1.00 57.33           C  
ATOM   2094  CD2 LEU A 468      11.318  22.002  24.684  1.00 56.13           C  
ATOM   2095  N   LEU A 469      15.809  22.293  25.485  1.00 57.47           N  
ATOM   2096  CA  LEU A 469      16.789  21.273  25.128  1.00 56.94           C  
ATOM   2097  C   LEU A 469      17.939  21.230  26.125  1.00 58.44           C  
ATOM   2098  O   LEU A 469      18.425  20.161  26.487  1.00 57.78           O  
ATOM   2099  CB  LEU A 469      17.340  21.543  23.731  1.00 54.82           C  
ATOM   2100  CG  LEU A 469      16.340  21.487  22.576  1.00 53.98           C  
ATOM   2101  CD1 LEU A 469      17.072  21.744  21.273  1.00 52.33           C  
ATOM   2102  CD2 LEU A 469      15.659  20.127  22.545  1.00 53.10           C  
ATOM   2103  N   GLN A 470      18.363  22.405  26.573  1.00 59.77           N  
ATOM   2104  CA  GLN A 470      19.457  22.511  27.519  1.00 60.94           C  
ATOM   2105  C   GLN A 470      19.111  21.846  28.852  1.00 61.70           C  
ATOM   2106  O   GLN A 470      19.964  21.232  29.493  1.00 60.83           O  
ATOM   2107  CB  GLN A 470      19.794  23.985  27.737  1.00 61.24           C  
ATOM   2108  CG  GLN A 470      21.270  24.290  27.633  1.00 64.05           C  
ATOM   2109  CD  GLN A 470      21.558  25.779  27.589  1.00 65.43           C  
ATOM   2110  OE1 GLN A 470      22.714  26.193  27.495  1.00 68.05           O  
ATOM   2111  NE2 GLN A 470      20.508  26.591  27.652  1.00 64.22           N  
ATOM   2112  N   GLU A 471      17.853  21.965  29.264  1.00 63.14           N  
ATOM   2113  CA  GLU A 471      17.417  21.383  30.526  1.00 64.41           C  
ATOM   2114  C   GLU A 471      17.370  19.866  30.437  1.00 65.13           C  
ATOM   2115  O   GLU A 471      17.862  19.171  31.325  1.00 65.72           O  
ATOM   2116  CB  GLU A 471      16.040  21.922  30.912  1.00 64.77           C  
ATOM   2117  CG  GLU A 471      15.585  21.532  32.316  1.00 66.27           C  
ATOM   2118  CD  GLU A 471      16.525  22.036  33.407  1.00 66.92           C  
ATOM   2119  OE1 GLU A 471      16.806  23.257  33.450  1.00 67.24           O  
ATOM   2120  OE2 GLU A 471      16.976  21.207  34.226  1.00 65.46           O  
ATOM   2121  N   ILE A 472      16.774  19.355  29.365  1.00 65.40           N  
ATOM   2122  CA  ILE A 472      16.692  17.917  29.177  1.00 66.55           C  
ATOM   2123  C   ILE A 472      18.099  17.289  29.291  1.00 68.34           C  
ATOM   2124  O   ILE A 472      18.200  16.192  29.843  1.00 68.70           O  
ATOM   2125  CB  ILE A 472      16.014  17.556  27.838  1.00 65.03           C  
ATOM   2126  CG1 ILE A 472      14.508  17.802  27.957  1.00 63.41           C  
ATOM   2127  CG2 ILE A 472      16.287  16.095  27.470  1.00 64.87           C  
ATOM   2128  CD1 ILE A 472      13.750  17.580  26.684  1.00 62.60           C  
ATOM   2129  N   TYR A 473      19.206  17.898  28.868  1.00 70.06           N  
ATOM   2130  CA  TYR A 473      20.555  17.290  29.091  1.00 71.91           C  
ATOM   2131  C   TYR A 473      21.043  17.692  30.578  1.00 72.76           C  
ATOM   2132  O   TYR A 473      20.938  18.862  30.955  1.00 72.58           O  
ATOM   2133  CB  TYR A 473      21.494  17.698  27.921  1.00 73.08           C  
ATOM   2134  CG  TYR A 473      20.877  17.929  26.504  1.00 74.89           C  
ATOM   2135  CD1 TYR A 473      20.910  19.206  25.984  1.00 75.44           C  
ATOM   2136  CD2 TYR A 473      20.334  16.901  25.711  1.00 75.40           C  
ATOM   2137  CE1 TYR A 473      20.445  19.490  24.723  1.00 76.98           C  
ATOM   2138  CE2 TYR A 473      19.860  17.176  24.428  1.00 75.81           C  
ATOM   2139  CZ  TYR A 473      19.918  18.476  23.944  1.00 76.39           C  
ATOM   2140  OH  TYR A 473      19.442  18.773  22.688  1.00 76.73           O  
ATOM   2141  N   LYS A 474      21.576  16.748  31.369  1.00 74.62           N  
ATOM   2142  CA  LYS A 474      22.049  16.870  32.779  1.00 74.93           C  
ATOM   2143  C   LYS A 474      21.922  15.388  33.135  1.00 74.91           C  
ATOM   2144  O   LYS A 474      21.685  14.918  34.245  1.00 74.83           O  
ATOM   2145  CB  LYS A 474      21.181  17.842  33.617  1.00 74.81           C  
ATOM   2146  CG  LYS A 474      21.282  19.326  33.254  1.00 75.10           C  
ATOM   2147  CD  LYS A 474      20.680  20.208  34.340  1.00 75.14           C  
ATOM   2148  CE  LYS A 474      21.186  19.823  35.719  1.00 74.71           C  
ATOM   2149  NZ  LYS A 474      22.684  19.800  35.775  1.00 75.33           N  
ATOM   2150  N   ASP A 475      22.096  14.767  31.998  1.00 74.64           N  
ATOM   2151  CA  ASP A 475      21.994  13.460  31.384  1.00 74.72           C  
ATOM   2152  C   ASP A 475      22.994  12.349  31.222  1.00 74.99           C  
ATOM   2153  O   ASP A 475      23.629  12.408  30.175  1.00 74.49           O  
ATOM   2154  CB  ASP A 475      21.806  13.851  29.960  1.00 75.26           C  
ATOM   2155  CG  ASP A 475      20.551  13.301  29.404  1.00 75.40           C  
ATOM   2156  OD1 ASP A 475      19.568  13.180  30.156  1.00 75.05           O  
ATOM   2157  OD2 ASP A 475      20.518  12.972  28.206  1.00 74.75           O  
ATOM   2158  N   LEU A 476      23.268  11.402  32.046  1.00 73.26           N  
ATOM   2159  CA  LEU A 476      24.074  10.420  31.354  1.00 72.80           C  
ATOM   2160  C   LEU A 476      25.463   9.999  31.806  1.00 72.59           C  
ATOM   2161  O   LEU A 476      26.445  10.496  32.352  1.00 72.68           O  
ATOM   2162  CB  LEU A 476      24.129  10.856  29.871  1.00 72.75           C  
ATOM   2163  CG  LEU A 476      22.887  10.518  29.016  1.00 72.62           C  
ATOM   2164  CD1 LEU A 476      23.308  10.186  27.598  1.00 72.66           C  
ATOM   2165  CD2 LEU A 476      22.088   9.370  29.614  1.00 72.43           C  
ATOM   2166  OXT LEU A 476      25.742  10.357  30.530  0.00 72.10           O  
TER    2167      LEU A 476                                                      
ATOM   2168  N   GLU B 207      10.594 -26.834  16.328  1.00 71.00           N  
ATOM   2169  CA  GLU B 207       9.741 -27.425  17.400  1.00 70.65           C  
ATOM   2170  C   GLU B 207      10.258 -27.079  18.792  1.00 69.60           C  
ATOM   2171  O   GLU B 207      11.422 -26.715  18.962  1.00 69.60           O  
ATOM   2172  CB  GLU B 207       9.680 -28.948  17.240  1.00 71.24           C  
ATOM   2173  CG  GLU B 207       9.045 -29.397  15.933  1.00 72.05           C  
ATOM   2174  CD  GLU B 207       7.687 -28.753  15.695  1.00 71.98           C  
ATOM   2175  OE1 GLU B 207       6.792 -28.910  16.553  1.00 72.63           O  
ATOM   2176  OE2 GLU B 207       7.517 -28.089  14.650  1.00 71.81           O  
ATOM   2177  N   SER B 208       9.384 -27.195  19.787  1.00 68.65           N  
ATOM   2178  CA  SER B 208       9.759 -26.900  21.161  1.00 67.71           C  
ATOM   2179  C   SER B 208      10.711 -27.972  21.682  1.00 67.54           C  
ATOM   2180  O   SER B 208      11.196 -27.885  22.812  1.00 68.34           O  
ATOM   2181  CB  SER B 208       8.514 -26.845  22.049  1.00 67.82           C  
ATOM   2182  OG  SER B 208       7.877 -28.110  22.117  1.00 68.48           O  
ATOM   2183  N   ALA B 209      10.976 -28.980  20.853  1.00 66.14           N  
ATOM   2184  CA  ALA B 209      11.866 -30.074  21.228  1.00 64.77           C  
ATOM   2185  C   ALA B 209      13.323 -29.682  21.025  1.00 63.72           C  
ATOM   2186  O   ALA B 209      14.178 -30.001  21.850  1.00 64.24           O  
ATOM   2187  CB  ALA B 209      11.539 -31.322  20.406  1.00 65.92           C  
ATOM   2188  N   ASP B 210      13.602 -29.000  19.918  1.00 62.04           N  
ATOM   2189  CA  ASP B 210      14.956 -28.552  19.613  1.00 59.88           C  
ATOM   2190  C   ASP B 210      15.326 -27.425  20.564  1.00 57.40           C  
ATOM   2191  O   ASP B 210      16.488 -27.275  20.946  1.00 56.60           O  
ATOM   2192  CB  ASP B 210      15.041 -28.029  18.179  1.00 61.51           C  
ATOM   2193  CG  ASP B 210      14.599 -29.047  17.163  1.00 64.77           C  
ATOM   2194  OD1 ASP B 210      13.450 -29.535  17.263  1.00 67.05           O  
ATOM   2195  OD2 ASP B 210      15.403 -29.359  16.259  1.00 67.43           O  
ATOM   2196  N   LEU B 211      14.327 -26.632  20.939  1.00 54.45           N  
ATOM   2197  CA  LEU B 211      14.542 -25.507  21.841  1.00 53.31           C  
ATOM   2198  C   LEU B 211      14.833 -25.954  23.273  1.00 52.20           C  
ATOM   2199  O   LEU B 211      15.651 -25.347  23.964  1.00 52.38           O  
ATOM   2200  CB  LEU B 211      13.326 -24.570  21.813  1.00 51.10           C  
ATOM   2201  CG  LEU B 211      13.051 -23.875  20.471  1.00 51.32           C  
ATOM   2202  CD1 LEU B 211      11.774 -23.055  20.567  1.00 47.44           C  
ATOM   2203  CD2 LEU B 211      14.238 -22.989  20.094  1.00 49.91           C  
ATOM   2204  N   ARG B 212      14.157 -27.004  23.725  1.00 52.10           N  
ATOM   2205  CA  ARG B 212      14.381 -27.512  25.074  1.00 51.36           C  
ATOM   2206  C   ARG B 212      15.705 -28.258  25.123  1.00 50.29           C  
ATOM   2207  O   ARG B 212      16.368 -28.301  26.160  1.00 50.36           O  
ATOM   2208  CB  ARG B 212      13.244 -28.444  25.497  1.00 53.14           C  
ATOM   2209  CG  ARG B 212      11.967 -27.719  25.868  1.00 56.48           C  
ATOM   2210  CD  ARG B 212      12.198 -26.819  27.074  1.00 59.72           C  
ATOM   2211  NE  ARG B 212      11.532 -27.310  28.279  1.00 64.25           N  
ATOM   2212  CZ  ARG B 212      11.792 -28.473  28.871  1.00 64.96           C  
ATOM   2213  NH1 ARG B 212      12.715 -29.290  28.375  1.00 66.04           N  
ATOM   2214  NH2 ARG B 212      11.128 -28.818  29.968  1.00 66.18           N  
ATOM   2215  N   ALA B 213      16.076 -28.858  23.998  1.00 48.96           N  
ATOM   2216  CA  ALA B 213      17.333 -29.584  23.901  1.00 47.97           C  
ATOM   2217  C   ALA B 213      18.450 -28.542  23.971  1.00 47.20           C  
ATOM   2218  O   ALA B 213      19.385 -28.666  24.763  1.00 46.09           O  
ATOM   2219  CB  ALA B 213      17.400 -30.345  22.583  1.00 46.89           C  
ATOM   2220  N   LEU B 214      18.335 -27.511  23.137  1.00 45.23           N  
ATOM   2221  CA  LEU B 214      19.308 -26.426  23.110  1.00 44.23           C  
ATOM   2222  C   LEU B 214      19.504 -25.867  24.517  1.00 41.92           C  
ATOM   2223  O   LEU B 214      20.630 -25.699  24.970  1.00 43.10           O  
ATOM   2224  CB  LEU B 214      18.820 -25.309  22.181  1.00 43.90           C  
ATOM   2225  CG  LEU B 214      19.714 -24.085  22.004  1.00 43.53           C  
ATOM   2226  CD1 LEU B 214      21.092 -24.505  21.503  1.00 41.01           C  
ATOM   2227  CD2 LEU B 214      19.052 -23.128  21.019  1.00 42.88           C  
ATOM   2228  N   ALA B 215      18.396 -25.589  25.202  1.00 42.07           N  
ATOM   2229  CA  ALA B 215      18.421 -25.039  26.561  1.00 42.32           C  
ATOM   2230  C   ALA B 215      19.124 -25.966  27.551  1.00 42.73           C  
ATOM   2231  O   ALA B 215      19.934 -25.529  28.369  1.00 42.34           O  
ATOM   2232  CB  ALA B 215      16.998 -24.772  27.040  1.00 39.83           C  
ATOM   2233  N   LYS B 216      18.787 -27.248  27.487  1.00 42.60           N  
ATOM   2234  CA  LYS B 216      19.393 -28.239  28.368  1.00 42.17           C  
ATOM   2235  C   LYS B 216      20.897 -28.293  28.087  1.00 39.78           C  
ATOM   2236  O   LYS B 216      21.718 -28.268  28.997  1.00 39.93           O  
ATOM   2237  CB  LYS B 216      18.756 -29.614  28.111  1.00 44.04           C  
ATOM   2238  CG  LYS B 216      18.478 -30.425  29.376  1.00 47.19           C  
ATOM   2239  CD  LYS B 216      19.751 -30.765  30.120  1.00 47.93           C  
ATOM   2240  CE  LYS B 216      19.454 -31.469  31.442  1.00 50.22           C  
ATOM   2241  NZ  LYS B 216      20.723 -31.814  32.159  1.00 51.39           N  
ATOM   2242  N   HIS B 217      21.240 -28.349  26.805  1.00 40.00           N  
ATOM   2243  CA  HIS B 217      22.627 -28.421  26.358  1.00 40.16           C  
ATOM   2244  C   HIS B 217      23.483 -27.267  26.891  1.00 41.77           C  
ATOM   2245  O   HIS B 217      24.584 -27.479  27.420  1.00 41.17           O  
ATOM   2246  CB  HIS B 217      22.656 -28.449  24.824  1.00 39.20           C  
ATOM   2247  CG  HIS B 217      24.022 -28.637  24.239  1.00 41.19           C  
ATOM   2248  ND1 HIS B 217      24.895 -27.592  24.027  1.00 41.97           N  
ATOM   2249  CD2 HIS B 217      24.667 -29.753  23.827  1.00 39.42           C  
ATOM   2250  CE1 HIS B 217      26.017 -28.055  23.507  1.00 37.91           C  
ATOM   2251  NE2 HIS B 217      25.904 -29.363  23.376  1.00 40.04           N  
ATOM   2252  N   LEU B 218      22.971 -26.046  26.755  1.00 40.75           N  
ATOM   2253  CA  LEU B 218      23.689 -24.860  27.214  1.00 38.12           C  
ATOM   2254  C   LEU B 218      23.822 -24.883  28.727  1.00 36.90           C  
ATOM   2255  O   LEU B 218      24.872 -24.567  29.272  1.00 36.60           O  
ATOM   2256  CB  LEU B 218      22.946 -23.604  26.752  1.00 37.01           C  
ATOM   2257  CG  LEU B 218      22.817 -23.494  25.226  1.00 37.24           C  
ATOM   2258  CD1 LEU B 218      21.804 -22.424  24.857  1.00 39.05           C  
ATOM   2259  CD2 LEU B 218      24.184 -23.181  24.617  1.00 36.19           C  
ATOM   2260  N   TYR B 219      22.747 -25.259  29.405  1.00 39.73           N  
ATOM   2261  CA  TYR B 219      22.768 -25.341  30.854  1.00 42.35           C  
ATOM   2262  C   TYR B 219      23.876 -26.282  31.315  1.00 42.91           C  
ATOM   2263  O   TYR B 219      24.687 -25.920  32.173  1.00 43.75           O  
ATOM   2264  CB  TYR B 219      21.429 -25.851  31.391  1.00 43.24           C  
ATOM   2265  CG  TYR B 219      21.431 -26.010  32.896  1.00 45.41           C  
ATOM   2266  CD1 TYR B 219      21.507 -24.896  33.735  1.00 44.48           C  
ATOM   2267  CD2 TYR B 219      21.395 -27.278  33.484  1.00 45.52           C  
ATOM   2268  CE1 TYR B 219      21.548 -25.041  35.125  1.00 44.69           C  
ATOM   2269  CE2 TYR B 219      21.437 -27.431  34.867  1.00 46.06           C  
ATOM   2270  CZ  TYR B 219      21.513 -26.310  35.678  1.00 45.72           C  
ATOM   2271  OH  TYR B 219      21.557 -26.464  37.041  1.00 47.33           O  
ATOM   2272  N   ASP B 220      23.906 -27.491  30.754  1.00 42.88           N  
ATOM   2273  CA  ASP B 220      24.930 -28.464  31.135  1.00 43.40           C  
ATOM   2274  C   ASP B 220      26.310 -27.883  30.936  1.00 41.42           C  
ATOM   2275  O   ASP B 220      27.129 -27.904  31.843  1.00 42.15           O  
ATOM   2276  CB  ASP B 220      24.820 -29.750  30.313  1.00 42.88           C  
ATOM   2277  CG  ASP B 220      23.576 -30.539  30.632  1.00 44.98           C  
ATOM   2278  OD1 ASP B 220      23.081 -30.453  31.778  1.00 44.52           O  
ATOM   2279  OD2 ASP B 220      23.097 -31.262  29.732  1.00 49.63           O  
ATOM   2280  N   SER B 221      26.554 -27.359  29.744  1.00 38.80           N  
ATOM   2281  CA  SER B 221      27.846 -26.774  29.405  1.00 39.53           C  
ATOM   2282  C   SER B 221      28.253 -25.624  30.308  1.00 40.64           C  
ATOM   2283  O   SER B 221      29.440 -25.430  30.584  1.00 41.21           O  
ATOM   2284  CB  SER B 221      27.831 -26.279  27.962  1.00 38.28           C  
ATOM   2285  OG  SER B 221      28.989 -25.505  27.697  1.00 40.66           O  
ATOM   2286  N   TYR B 222      27.256 -24.855  30.747  1.00 41.12           N  
ATOM   2287  CA  TYR B 222      27.458 -23.701  31.614  1.00 41.21           C  
ATOM   2288  C   TYR B 222      27.903 -24.171  33.001  1.00 41.43           C  
ATOM   2289  O   TYR B 222      28.814 -23.597  33.604  1.00 39.36           O  
ATOM   2290  CB  TYR B 222      26.143 -22.899  31.662  1.00 42.26           C  
ATOM   2291  CG  TYR B 222      26.027 -21.815  32.704  1.00 42.38           C  
ATOM   2292  CD1 TYR B 222      25.487 -22.094  33.955  1.00 44.94           C  
ATOM   2293  CD2 TYR B 222      26.403 -20.498  32.426  1.00 45.55           C  
ATOM   2294  CE1 TYR B 222      25.309 -21.098  34.908  1.00 47.65           C  
ATOM   2295  CE2 TYR B 222      26.232 -19.476  33.385  1.00 46.97           C  
ATOM   2296  CZ  TYR B 222      25.678 -19.792  34.622  1.00 49.08           C  
ATOM   2297  OH  TYR B 222      25.458 -18.816  35.577  1.00 53.45           O  
ATOM   2298  N   ILE B 223      27.270 -25.232  33.488  1.00 41.22           N  
ATOM   2299  CA  ILE B 223      27.613 -25.794  34.792  1.00 43.64           C  
ATOM   2300  C   ILE B 223      29.044 -26.320  34.773  1.00 43.72           C  
ATOM   2301  O   ILE B 223      29.810 -26.122  35.720  1.00 43.79           O  
ATOM   2302  CB  ILE B 223      26.667 -26.966  35.169  1.00 44.07           C  
ATOM   2303  CG1 ILE B 223      25.291 -26.424  35.519  1.00 43.46           C  
ATOM   2304  CG2 ILE B 223      27.233 -27.753  36.340  1.00 44.71           C  
ATOM   2305  CD1 ILE B 223      25.319 -25.361  36.581  1.00 46.29           C  
ATOM   2306  N   LYS B 224      29.393 -26.990  33.683  1.00 43.90           N  
ATOM   2307  CA  LYS B 224      30.718 -27.568  33.524  1.00 46.14           C  
ATOM   2308  C   LYS B 224      31.817 -26.528  33.352  1.00 45.16           C  
ATOM   2309  O   LYS B 224      32.933 -26.710  33.842  1.00 45.91           O  
ATOM   2310  CB  LYS B 224      30.719 -28.514  32.319  1.00 47.36           C  
ATOM   2311  CG  LYS B 224      32.107 -28.974  31.883  1.00 51.95           C  
ATOM   2312  CD  LYS B 224      32.037 -29.858  30.644  1.00 53.49           C  
ATOM   2313  CE  LYS B 224      33.424 -30.120  30.057  1.00 55.70           C  
ATOM   2314  NZ  LYS B 224      34.342 -30.858  30.988  1.00 57.76           N  
ATOM   2315  N   SER B 225      31.487 -25.432  32.673  1.00 43.03           N  
ATOM   2316  CA  SER B 225      32.440 -24.368  32.377  1.00 38.88           C  
ATOM   2317  C   SER B 225      32.806 -23.348  33.452  1.00 36.54           C  
ATOM   2318  O   SER B 225      33.932 -22.846  33.476  1.00 33.18           O  
ATOM   2319  CB  SER B 225      31.972 -23.616  31.126  1.00 39.07           C  
ATOM   2320  OG  SER B 225      32.453 -24.243  29.951  1.00 41.62           O  
ATOM   2321  N   PHE B 226      31.874 -23.026  34.335  1.00 36.89           N  
ATOM   2322  CA  PHE B 226      32.151 -22.028  35.362  1.00 38.41           C  
ATOM   2323  C   PHE B 226      32.293 -22.627  36.756  1.00 39.03           C  
ATOM   2324  O   PHE B 226      31.643 -23.609  37.086  1.00 41.13           O  
ATOM   2325  CB  PHE B 226      31.069 -20.941  35.304  1.00 35.45           C  
ATOM   2326  CG  PHE B 226      30.962 -20.296  33.947  1.00 38.74           C  
ATOM   2327  CD1 PHE B 226      31.987 -19.482  33.469  1.00 40.10           C  
ATOM   2328  CD2 PHE B 226      29.889 -20.573  33.108  1.00 38.04           C  
ATOM   2329  CE1 PHE B 226      31.947 -18.960  32.173  1.00 40.69           C  
ATOM   2330  CE2 PHE B 226      29.838 -20.058  31.811  1.00 36.63           C  
ATOM   2331  CZ  PHE B 226      30.868 -19.252  31.341  1.00 38.58           C  
ATOM   2332  N   PRO B 227      33.161 -22.033  37.591  1.00 40.86           N  
ATOM   2333  CA  PRO B 227      33.423 -22.493  38.962  1.00 42.37           C  
ATOM   2334  C   PRO B 227      32.231 -22.457  39.898  1.00 43.75           C  
ATOM   2335  O   PRO B 227      31.856 -23.479  40.476  1.00 44.58           O  
ATOM   2336  CB  PRO B 227      34.525 -21.557  39.440  1.00 42.17           C  
ATOM   2337  CG  PRO B 227      35.168 -21.082  38.164  1.00 43.50           C  
ATOM   2338  CD  PRO B 227      33.989 -20.859  37.277  1.00 39.48           C  
ATOM   2339  N   LEU B 228      31.641 -21.276  40.059  1.00 43.19           N  
ATOM   2340  CA  LEU B 228      30.507 -21.134  40.957  1.00 43.41           C  
ATOM   2341  C   LEU B 228      29.208 -20.781  40.246  1.00 43.85           C  
ATOM   2342  O   LEU B 228      29.137 -19.802  39.501  1.00 43.95           O  
ATOM   2343  CB  LEU B 228      30.833 -20.084  42.021  1.00 44.56           C  
ATOM   2344  CG  LEU B 228      30.425 -20.463  43.451  1.00 47.18           C  
ATOM   2345  CD1 LEU B 228      31.370 -19.837  44.454  1.00 49.93           C  
ATOM   2346  CD2 LEU B 228      29.009 -20.019  43.710  1.00 47.69           C  
ATOM   2347  N   THR B 229      28.185 -21.595  40.478  1.00 43.32           N  
ATOM   2348  CA  THR B 229      26.880 -21.374  39.883  1.00 41.13           C  
ATOM   2349  C   THR B 229      26.163 -20.336  40.732  1.00 40.30           C  
ATOM   2350  O   THR B 229      26.538 -20.093  41.876  1.00 39.42           O  
ATOM   2351  CB  THR B 229      26.034 -22.637  39.905  1.00 42.04           C  
ATOM   2352  OG1 THR B 229      25.788 -23.005  41.264  1.00 43.45           O  
ATOM   2353  CG2 THR B 229      26.739 -23.767  39.189  1.00 42.91           C  
ATOM   2354  N   LYS B 230      25.118 -19.735  40.179  1.00 39.80           N  
ATOM   2355  CA  LYS B 230      24.377 -18.729  40.921  1.00 39.14           C  
ATOM   2356  C   LYS B 230      23.658 -19.364  42.103  1.00 37.99           C  
ATOM   2357  O   LYS B 230      23.545 -18.760  43.165  1.00 37.87           O  
ATOM   2358  CB  LYS B 230      23.354 -18.023  40.015  1.00 36.93           C  
ATOM   2359  CG  LYS B 230      22.514 -16.994  40.767  1.00 37.72           C  
ATOM   2360  CD  LYS B 230      21.579 -16.220  39.857  1.00 35.78           C  
ATOM   2361  CE  LYS B 230      20.712 -15.267  40.676  1.00 38.43           C  
ATOM   2362  NZ  LYS B 230      19.754 -14.512  39.819  1.00 32.58           N  
ATOM   2363  N   ALA B 231      23.160 -20.579  41.913  1.00 38.82           N  
ATOM   2364  CA  ALA B 231      22.444 -21.267  42.977  1.00 40.08           C  
ATOM   2365  C   ALA B 231      23.372 -21.385  44.178  1.00 43.16           C  
ATOM   2366  O   ALA B 231      22.978 -21.134  45.316  1.00 45.50           O  
ATOM   2367  CB  ALA B 231      22.011 -22.642  42.506  1.00 38.30           C  
ATOM   2368  N   LYS B 232      24.616 -21.751  43.898  1.00 45.34           N  
ATOM   2369  CA  LYS B 232      25.646 -21.910  44.913  1.00 48.85           C  
ATOM   2370  C   LYS B 232      25.983 -20.559  45.555  1.00 48.42           C  
ATOM   2371  O   LYS B 232      26.007 -20.430  46.776  1.00 49.11           O  
ATOM   2372  CB  LYS B 232      26.900 -22.498  44.255  1.00 51.35           C  
ATOM   2373  CG  LYS B 232      27.711 -23.464  45.112  1.00 57.78           C  
ATOM   2374  CD  LYS B 232      28.305 -22.804  46.355  1.00 60.46           C  
ATOM   2375  CE  LYS B 232      29.206 -23.787  47.095  1.00 61.52           C  
ATOM   2376  NZ  LYS B 232      28.494 -25.065  47.397  1.00 61.64           N  
ATOM   2377  N   ALA B 233      26.242 -19.555  44.721  1.00 47.42           N  
ATOM   2378  CA  ALA B 233      26.604 -18.230  45.206  1.00 46.83           C  
ATOM   2379  C   ALA B 233      25.530 -17.641  46.098  1.00 46.44           C  
ATOM   2380  O   ALA B 233      25.840 -16.967  47.078  1.00 46.91           O  
ATOM   2381  CB  ALA B 233      26.879 -17.294  44.033  1.00 45.73           C  
ATOM   2382  N   ARG B 234      24.269 -17.888  45.753  1.00 46.44           N  
ATOM   2383  CA  ARG B 234      23.153 -17.375  46.537  1.00 44.73           C  
ATOM   2384  C   ARG B 234      23.127 -18.061  47.898  1.00 44.42           C  
ATOM   2385  O   ARG B 234      22.948 -17.406  48.920  1.00 42.71           O  
ATOM   2386  CB  ARG B 234      21.821 -17.612  45.809  1.00 44.99           C  
ATOM   2387  CG  ARG B 234      21.620 -16.787  44.519  1.00 46.87           C  
ATOM   2388  CD  ARG B 234      21.485 -15.293  44.821  1.00 45.04           C  
ATOM   2389  NE  ARG B 234      22.619 -14.531  44.319  1.00 44.85           N  
ATOM   2390  CZ  ARG B 234      22.812 -13.232  44.543  1.00 45.02           C  
ATOM   2391  NH1 ARG B 234      21.942 -12.533  45.272  1.00 42.68           N  
ATOM   2392  NH2 ARG B 234      23.873 -12.626  44.024  1.00 39.72           N  
ATOM   2393  N   ALA B 235      23.299 -19.380  47.903  1.00 44.07           N  
ATOM   2394  CA  ALA B 235      23.302 -20.142  49.146  1.00 45.64           C  
ATOM   2395  C   ALA B 235      24.318 -19.531  50.103  1.00 44.82           C  
ATOM   2396  O   ALA B 235      24.051 -19.380  51.292  1.00 44.71           O  
ATOM   2397  CB  ALA B 235      23.650 -21.600  48.869  1.00 44.06           C  
ATOM   2398  N   ILE B 236      25.480 -19.176  49.570  1.00 46.69           N  
ATOM   2399  CA  ILE B 236      26.543 -18.575  50.365  1.00 49.91           C  
ATOM   2400  C   ILE B 236      26.228 -17.141  50.797  1.00 52.41           C  
ATOM   2401  O   ILE B 236      26.397 -16.787  51.964  1.00 53.27           O  
ATOM   2402  CB  ILE B 236      27.883 -18.574  49.587  1.00 49.12           C  
ATOM   2403  CG1 ILE B 236      28.353 -20.010  49.363  1.00 50.25           C  
ATOM   2404  CG2 ILE B 236      28.937 -17.810  50.358  1.00 48.41           C  
ATOM   2405  CD1 ILE B 236      29.577 -20.133  48.485  1.00 51.22           C  
ATOM   2406  N   LEU B 237      25.766 -16.318  49.862  1.00 54.39           N  
ATOM   2407  CA  LEU B 237      25.457 -14.924  50.167  1.00 56.96           C  
ATOM   2408  C   LEU B 237      24.324 -14.787  51.169  1.00 60.53           C  
ATOM   2409  O   LEU B 237      24.177 -15.603  52.075  1.00 61.52           O  
ATOM   2410  CB  LEU B 237      25.095 -14.174  48.886  1.00 54.17           C  
ATOM   2411  CG  LEU B 237      26.247 -13.866  47.929  1.00 53.78           C  
ATOM   2412  CD1 LEU B 237      25.689 -13.302  46.624  1.00 53.33           C  
ATOM   2413  CD2 LEU B 237      27.203 -12.872  48.579  1.00 52.50           C  
ATOM   2414  N   THR B 238      23.538 -13.728  51.010  1.00 64.68           N  
ATOM   2415  CA  THR B 238      22.397 -13.495  51.875  1.00 67.88           C  
ATOM   2416  C   THR B 238      21.655 -14.824  52.010  1.00 70.54           C  
ATOM   2417  O   THR B 238      20.828 -15.193  51.169  1.00 70.77           O  
ATOM   2418  CB  THR B 238      21.465 -12.407  51.280  1.00 68.27           C  
ATOM   2419  OG1 THR B 238      20.154 -12.535  51.845  1.00 70.22           O  
ATOM   2420  CG2 THR B 238      21.395 -12.521  49.756  1.00 67.18           C  
ATOM   2421  N   GLY B 239      21.981 -15.546  53.076  1.00 72.98           N  
ATOM   2422  CA  GLY B 239      21.377 -16.838  53.328  1.00 75.58           C  
ATOM   2423  C   GLY B 239      22.317 -17.599  54.235  1.00 77.16           C  
ATOM   2424  O   GLY B 239      23.535 -17.467  54.108  1.00 76.95           O  
ATOM   2425  N   LYS B 240      21.765 -18.392  55.149  1.00 78.93           N  
ATOM   2426  CA  LYS B 240      22.591 -19.146  56.082  1.00 79.54           C  
ATOM   2427  C   LYS B 240      23.450 -20.224  55.431  1.00 79.98           C  
ATOM   2428  O   LYS B 240      24.565 -19.939  54.990  1.00 80.23           O  
ATOM   2429  CB  LYS B 240      21.729 -19.749  57.204  1.00 79.97           C  
ATOM   2430  CG  LYS B 240      20.466 -20.472  56.749  1.00 80.77           C  
ATOM   2431  CD  LYS B 240      19.618 -20.881  57.950  1.00 80.65           C  
ATOM   2432  CE  LYS B 240      18.288 -21.496  57.526  1.00 81.36           C  
ATOM   2433  NZ  LYS B 240      17.396 -21.765  58.694  1.00 81.06           N  
ATOM   2434  N   THR B 241      22.940 -21.451  55.351  1.00 80.25           N  
ATOM   2435  CA  THR B 241      23.727 -22.540  54.781  1.00 79.42           C  
ATOM   2436  C   THR B 241      24.958 -22.554  55.674  1.00 79.51           C  
ATOM   2437  O   THR B 241      26.095 -22.663  55.213  1.00 79.58           O  
ATOM   2438  CB  THR B 241      24.148 -22.235  53.342  1.00 78.45           C  
ATOM   2439  OG1 THR B 241      22.989 -21.893  52.576  1.00 77.82           O  
ATOM   2440  CG2 THR B 241      24.830 -23.443  52.720  1.00 78.33           C  
ATOM   2441  N   THR B 242      24.689 -22.411  56.969  1.00 79.89           N  
ATOM   2442  CA  THR B 242      25.703 -22.360  58.015  1.00 79.48           C  
ATOM   2443  C   THR B 242      26.763 -23.460  57.972  1.00 78.43           C  
ATOM   2444  O   THR B 242      26.565 -24.563  58.490  1.00 78.07           O  
ATOM   2445  CB  THR B 242      25.032 -22.367  59.409  1.00 80.11           C  
ATOM   2446  OG1 THR B 242      23.984 -21.386  59.433  1.00 80.33           O  
ATOM   2447  CG2 THR B 242      26.055 -22.041  60.503  1.00 79.14           C  
ATOM   2448  N   ASP B 243      27.888 -23.129  57.343  1.00 77.05           N  
ATOM   2449  CA  ASP B 243      29.046 -24.010  57.213  1.00 75.63           C  
ATOM   2450  C   ASP B 243      30.032 -23.308  56.288  1.00 74.48           C  
ATOM   2451  O   ASP B 243      29.627 -22.600  55.366  1.00 75.12           O  
ATOM   2452  CB  ASP B 243      28.665 -25.385  56.637  1.00 75.27           C  
ATOM   2453  CG  ASP B 243      28.206 -25.315  55.194  1.00 75.60           C  
ATOM   2454  OD1 ASP B 243      27.075 -24.843  54.945  1.00 75.10           O  
ATOM   2455  OD2 ASP B 243      28.983 -25.733  54.306  1.00 76.08           O  
ATOM   2456  N   LYS B 244      31.322 -23.499  56.550  1.00 72.94           N  
ATOM   2457  CA  LYS B 244      32.385 -22.880  55.763  1.00 70.24           C  
ATOM   2458  C   LYS B 244      32.041 -21.464  55.308  1.00 68.09           C  
ATOM   2459  O   LYS B 244      32.024 -21.173  54.116  1.00 68.35           O  
ATOM   2460  CB  LYS B 244      32.732 -23.749  54.546  1.00 71.26           C  
ATOM   2461  CG  LYS B 244      31.566 -24.063  53.612  1.00 72.18           C  
ATOM   2462  CD  LYS B 244      32.057 -24.688  52.305  1.00 73.42           C  
ATOM   2463  CE  LYS B 244      32.835 -25.985  52.542  1.00 73.87           C  
ATOM   2464  NZ  LYS B 244      33.265 -26.630  51.263  1.00 73.59           N  
ATOM   2465  N   SER B 245      31.762 -20.582  56.262  1.00 65.81           N  
ATOM   2466  CA  SER B 245      31.436 -19.196  55.940  1.00 63.63           C  
ATOM   2467  C   SER B 245      32.665 -18.535  55.295  1.00 60.85           C  
ATOM   2468  O   SER B 245      33.793 -18.730  55.749  1.00 61.66           O  
ATOM   2469  CB  SER B 245      31.029 -18.449  57.212  1.00 64.15           C  
ATOM   2470  OG  SER B 245      30.407 -17.214  56.908  1.00 64.11           O  
ATOM   2471  N   PRO B 246      32.458 -17.745  54.226  1.00 57.87           N  
ATOM   2472  CA  PRO B 246      33.531 -17.056  53.498  1.00 54.42           C  
ATOM   2473  C   PRO B 246      34.339 -16.071  54.331  1.00 51.89           C  
ATOM   2474  O   PRO B 246      33.822 -15.466  55.264  1.00 51.51           O  
ATOM   2475  CB  PRO B 246      32.784 -16.345  52.372  1.00 55.60           C  
ATOM   2476  CG  PRO B 246      31.537 -17.146  52.211  1.00 56.35           C  
ATOM   2477  CD  PRO B 246      31.152 -17.424  53.628  1.00 56.57           C  
ATOM   2478  N   PHE B 247      35.612 -15.909  53.994  1.00 48.86           N  
ATOM   2479  CA  PHE B 247      36.444 -14.957  54.710  1.00 47.52           C  
ATOM   2480  C   PHE B 247      36.020 -13.586  54.196  1.00 47.03           C  
ATOM   2481  O   PHE B 247      35.998 -13.362  52.988  1.00 45.34           O  
ATOM   2482  CB  PHE B 247      37.922 -15.175  54.401  1.00 46.35           C  
ATOM   2483  CG  PHE B 247      38.826 -14.270  55.179  1.00 47.51           C  
ATOM   2484  CD1 PHE B 247      39.178 -14.577  56.492  1.00 48.13           C  
ATOM   2485  CD2 PHE B 247      39.270 -13.074  54.629  1.00 46.20           C  
ATOM   2486  CE1 PHE B 247      39.957 -13.701  57.245  1.00 46.69           C  
ATOM   2487  CE2 PHE B 247      40.044 -12.197  55.373  1.00 46.81           C  
ATOM   2488  CZ  PHE B 247      40.388 -12.512  56.686  1.00 46.00           C  
ATOM   2489  N   VAL B 248      35.692 -12.674  55.105  1.00 45.90           N  
ATOM   2490  CA  VAL B 248      35.230 -11.341  54.724  1.00 45.20           C  
ATOM   2491  C   VAL B 248      36.319 -10.279  54.689  1.00 46.64           C  
ATOM   2492  O   VAL B 248      37.075 -10.116  55.646  1.00 46.22           O  
ATOM   2493  CB  VAL B 248      34.104 -10.856  55.680  1.00 45.33           C  
ATOM   2494  CG1 VAL B 248      33.614  -9.464  55.269  1.00 42.36           C  
ATOM   2495  CG2 VAL B 248      32.947 -11.863  55.677  1.00 42.49           C  
ATOM   2496  N   ILE B 249      36.396  -9.557  53.575  1.00 47.96           N  
ATOM   2497  CA  ILE B 249      37.377  -8.486  53.413  1.00 49.97           C  
ATOM   2498  C   ILE B 249      36.591  -7.185  53.562  1.00 50.99           C  
ATOM   2499  O   ILE B 249      35.821  -6.822  52.676  1.00 53.01           O  
ATOM   2500  CB  ILE B 249      38.026  -8.513  52.009  1.00 49.47           C  
ATOM   2501  CG1 ILE B 249      38.519  -9.925  51.673  1.00 50.76           C  
ATOM   2502  CG2 ILE B 249      39.176  -7.514  51.952  1.00 47.98           C  
ATOM   2503  CD1 ILE B 249      39.751 -10.370  52.422  1.00 53.43           C  
ATOM   2504  N   TYR B 250      36.779  -6.485  54.676  1.00 51.94           N  
ATOM   2505  CA  TYR B 250      36.040  -5.250  54.927  1.00 53.21           C  
ATOM   2506  C   TYR B 250      36.927  -4.034  55.185  1.00 54.54           C  
ATOM   2507  O   TYR B 250      36.430  -2.914  55.286  1.00 54.26           O  
ATOM   2508  CB  TYR B 250      35.100  -5.464  56.119  1.00 53.87           C  
ATOM   2509  CG  TYR B 250      35.831  -5.853  57.385  1.00 55.76           C  
ATOM   2510  CD1 TYR B 250      36.446  -4.888  58.184  1.00 57.01           C  
ATOM   2511  CD2 TYR B 250      35.955  -7.193  57.758  1.00 56.18           C  
ATOM   2512  CE1 TYR B 250      37.170  -5.248  59.326  1.00 58.40           C  
ATOM   2513  CE2 TYR B 250      36.679  -7.564  58.895  1.00 56.73           C  
ATOM   2514  CZ  TYR B 250      37.283  -6.587  59.673  1.00 57.59           C  
ATOM   2515  OH  TYR B 250      38.002  -6.950  60.790  1.00 56.87           O  
ATOM   2516  N   ASP B 251      38.233  -4.270  55.299  1.00 57.16           N  
ATOM   2517  CA  ASP B 251      39.226  -3.220  55.553  1.00 59.56           C  
ATOM   2518  C   ASP B 251      40.597  -3.653  55.042  1.00 59.28           C  
ATOM   2519  O   ASP B 251      40.739  -4.727  54.461  1.00 59.26           O  
ATOM   2520  CB  ASP B 251      39.357  -2.936  57.055  1.00 63.04           C  
ATOM   2521  CG  ASP B 251      38.262  -2.035  57.584  1.00 67.09           C  
ATOM   2522  OD1 ASP B 251      37.788  -1.156  56.825  1.00 68.34           O  
ATOM   2523  OD2 ASP B 251      37.895  -2.190  58.772  1.00 70.14           O  
ATOM   2524  N   MET B 252      41.610  -2.825  55.284  1.00 59.44           N  
ATOM   2525  CA  MET B 252      42.969  -3.142  54.859  1.00 60.33           C  
ATOM   2526  C   MET B 252      43.503  -4.383  55.577  1.00 60.23           C  
ATOM   2527  O   MET B 252      43.995  -5.320  54.939  1.00 60.20           O  
ATOM   2528  CB  MET B 252      43.900  -1.962  55.131  1.00 63.16           C  
ATOM   2529  CG  MET B 252      44.443  -1.288  53.878  1.00 68.28           C  
ATOM   2530  SD  MET B 252      43.189  -0.404  52.917  1.00 73.50           S  
ATOM   2531  CE  MET B 252      43.492   1.296  53.460  1.00 72.18           C  
ATOM   2532  N   ASN B 253      43.406  -4.387  56.904  1.00 59.18           N  
ATOM   2533  CA  ASN B 253      43.881  -5.513  57.705  1.00 58.60           C  
ATOM   2534  C   ASN B 253      43.210  -6.829  57.315  1.00 57.41           C  
ATOM   2535  O   ASN B 253      43.872  -7.873  57.234  1.00 55.67           O  
ATOM   2536  CB  ASN B 253      43.652  -5.229  59.195  1.00 60.88           C  
ATOM   2537  CG  ASN B 253      44.642  -4.217  59.758  1.00 62.73           C  
ATOM   2538  OD1 ASN B 253      44.380  -3.574  60.780  1.00 65.36           O  
ATOM   2539  ND2 ASN B 253      45.790  -4.083  59.102  1.00 61.35           N  
ATOM   2540  N   SER B 254      41.899  -6.780  57.077  1.00 56.47           N  
ATOM   2541  CA  SER B 254      41.151  -7.977  56.687  1.00 56.71           C  
ATOM   2542  C   SER B 254      41.595  -8.450  55.300  1.00 56.73           C  
ATOM   2543  O   SER B 254      41.538  -9.641  54.983  1.00 55.90           O  
ATOM   2544  CB  SER B 254      39.638  -7.702  56.708  1.00 56.08           C  
ATOM   2545  OG  SER B 254      39.303  -6.538  55.976  1.00 55.78           O  
ATOM   2546  N   LEU B 255      42.050  -7.512  54.479  1.00 57.63           N  
ATOM   2547  CA  LEU B 255      42.537  -7.855  53.149  1.00 59.22           C  
ATOM   2548  C   LEU B 255      43.844  -8.624  53.321  1.00 60.49           C  
ATOM   2549  O   LEU B 255      43.984  -9.757  52.853  1.00 59.97           O  
ATOM   2550  CB  LEU B 255      42.801  -6.591  52.330  1.00 58.18           C  
ATOM   2551  CG  LEU B 255      43.399  -6.837  50.940  1.00 58.50           C  
ATOM   2552  CD1 LEU B 255      42.424  -7.657  50.107  1.00 56.67           C  
ATOM   2553  CD2 LEU B 255      43.704  -5.513  50.262  1.00 57.21           C  
ATOM   2554  N   MET B 256      44.795  -7.987  54.001  1.00 62.38           N  
ATOM   2555  CA  MET B 256      46.104  -8.578  54.263  1.00 64.28           C  
ATOM   2556  C   MET B 256      45.943 -10.022  54.737  1.00 63.80           C  
ATOM   2557  O   MET B 256      46.615 -10.932  54.251  1.00 63.03           O  
ATOM   2558  CB  MET B 256      46.836  -7.783  55.348  1.00 66.84           C  
ATOM   2559  CG  MET B 256      46.892  -6.270  55.139  1.00 71.11           C  
ATOM   2560  SD  MET B 256      47.862  -5.722  53.717  1.00 76.85           S  
ATOM   2561  CE  MET B 256      46.713  -4.567  52.945  1.00 74.71           C  
ATOM   2562  N   MET B 257      45.039 -10.222  55.690  1.00 63.59           N  
ATOM   2563  CA  MET B 257      44.800 -11.545  56.242  1.00 62.50           C  
ATOM   2564  C   MET B 257      44.273 -12.532  55.215  1.00 61.58           C  
ATOM   2565  O   MET B 257      44.804 -13.636  55.083  1.00 61.20           O  
ATOM   2566  CB  MET B 257      43.829 -11.465  57.421  1.00 62.67           C  
ATOM   2567  CG  MET B 257      43.660 -12.795  58.133  1.00 64.20           C  
ATOM   2568  SD  MET B 257      43.292 -12.611  59.880  1.00 65.24           S  
ATOM   2569  CE  MET B 257      41.955 -13.799  60.090  1.00 63.23           C  
ATOM   2570  N   GLY B 258      43.234 -12.140  54.487  1.00 60.93           N  
ATOM   2571  CA  GLY B 258      42.668 -13.035  53.493  1.00 60.79           C  
ATOM   2572  C   GLY B 258      43.646 -13.333  52.376  1.00 61.47           C  
ATOM   2573  O   GLY B 258      43.740 -14.462  51.885  1.00 60.30           O  
ATOM   2574  N   GLU B 259      44.385 -12.305  51.981  1.00 62.32           N  
ATOM   2575  CA  GLU B 259      45.366 -12.417  50.910  1.00 63.68           C  
ATOM   2576  C   GLU B 259      46.441 -13.449  51.255  1.00 63.24           C  
ATOM   2577  O   GLU B 259      47.025 -14.071  50.366  1.00 64.04           O  
ATOM   2578  CB  GLU B 259      45.997 -11.040  50.664  1.00 64.23           C  
ATOM   2579  CG  GLU B 259      46.925 -10.953  49.472  1.00 65.62           C  
ATOM   2580  CD  GLU B 259      47.421  -9.539  49.246  1.00 66.77           C  
ATOM   2581  OE1 GLU B 259      47.946  -8.937  50.203  1.00 67.93           O  
ATOM   2582  OE2 GLU B 259      47.289  -9.026  48.115  1.00 68.49           O  
ATOM   2583  N   ASP B 260      46.688 -13.629  52.549  1.00 62.11           N  
ATOM   2584  CA  ASP B 260      47.692 -14.574  53.021  0.00 60.60           C  
ATOM   2585  C   ASP B 260      47.026 -15.844  53.549  0.00 60.18           C  
ATOM   2586  O   ASP B 260      47.701 -16.807  53.910  0.00 59.92           O  
ATOM   2587  CB  ASP B 260      48.534 -13.923  54.125  0.00 59.80           C  
ATOM   2588  CG  ASP B 260      49.787 -14.715  54.456  0.00 59.11           C  
ATOM   2589  OD1 ASP B 260      49.669 -15.832  54.999  0.00 58.72           O  
ATOM   2590  OD2 ASP B 260      50.895 -14.215  54.169  0.00 58.72           O  
ATOM   2591  N   LYS B 261      45.696 -15.843  53.582  0.00 59.86           N  
ATOM   2592  CA  LYS B 261      44.947 -16.996  54.071  0.00 59.85           C  
ATOM   2593  C   LYS B 261      43.835 -17.410  53.114  0.00 60.53           C  
ATOM   2594  O   LYS B 261      42.710 -17.684  53.534  0.00 60.46           O  
ATOM   2595  CB  LYS B 261      44.352 -16.688  55.446  0.00 58.77           C  
ATOM   2596  CG  LYS B 261      45.384 -16.279  56.481  0.00 57.56           C  
ATOM   2597  CD  LYS B 261      44.736 -15.986  57.822  0.00 56.61           C  
ATOM   2598  CE  LYS B 261      45.759 -15.474  58.822  0.00 56.04           C  
ATOM   2599  NZ  LYS B 261      46.862 -16.450  59.035  0.00 55.59           N  
ATOM   2600  N   ILE B 262      44.155 -17.456  51.826  1.00 62.03           N  
ATOM   2601  CA  ILE B 262      43.187 -17.846  50.808  1.00 62.17           C  
ATOM   2602  C   ILE B 262      43.939 -18.180  49.526  1.00 62.60           C  
ATOM   2603  O   ILE B 262      45.063 -17.720  49.329  1.00 63.75           O  
ATOM   2604  CB  ILE B 262      42.181 -16.709  50.533  0.00 61.92           C  
ATOM   2605  CG1 ILE B 262      40.891 -17.288  49.961  0.00 61.86           C  
ATOM   2606  CG2 ILE B 262      42.771 -15.708  49.544  0.00 61.54           C  
ATOM   2607  CD1 ILE B 262      39.740 -16.322  50.005  1.00 62.85           C  
ATOM   2608  N   LYS B 263      43.321 -18.984  48.665  1.00 62.89           N  
ATOM   2609  CA  LYS B 263      43.930 -19.382  47.394  1.00 62.20           C  
ATOM   2610  C   LYS B 263      44.235 -18.160  46.522  1.00 61.75           C  
ATOM   2611  O   LYS B 263      43.400 -17.747  45.708  1.00 63.86           O  
ATOM   2612  CB  LYS B 263      42.984 -20.327  46.643  0.00 61.02           C  
ATOM   2613  CG  LYS B 263      43.486 -20.824  45.287  0.00 59.87           C  
ATOM   2614  CD  LYS B 263      44.558 -21.904  45.411  0.00 58.93           C  
ATOM   2615  CE  LYS B 263      45.914 -21.333  45.797  0.00 58.37           C  
ATOM   2616  NZ  LYS B 263      46.952 -22.397  45.885  0.00 57.93           N  
ATOM   2617  N   PHE B 264      45.422 -17.580  46.694  1.00 59.53           N  
ATOM   2618  CA  PHE B 264      45.815 -16.409  45.914  1.00 57.79           C  
ATOM   2619  C   PHE B 264      47.161 -16.667  45.246  1.00 56.79           C  
ATOM   2620  O   PHE B 264      48.049 -17.269  45.846  1.00 59.47           O  
ATOM   2621  CB  PHE B 264      45.908 -15.176  46.816  0.00 56.21           C  
ATOM   2622  CG  PHE B 264      46.092 -13.890  46.064  0.00 54.79           C  
ATOM   2623  CD1 PHE B 264      45.128 -13.456  45.159  0.00 54.16           C  
ATOM   2624  CD2 PHE B 264      47.228 -13.111  46.257  0.00 54.16           C  
ATOM   2625  CE1 PHE B 264      45.292 -12.265  44.456  0.00 53.68           C  
ATOM   2626  CE2 PHE B 264      47.402 -11.918  45.559  0.00 53.68           C  
ATOM   2627  CZ  PHE B 264      46.432 -11.495  44.657  0.00 53.54           C  
ATOM   2628  N   LYS B 265      47.315 -16.224  44.004  0.00 55.32           N  
ATOM   2629  CA  LYS B 265      48.569 -16.429  43.292  0.00 53.40           C  
ATOM   2630  C   LYS B 265      48.991 -15.191  42.512  0.00 52.85           C  
ATOM   2631  O   LYS B 265      48.709 -15.062  41.320  0.00 52.58           O  
ATOM   2632  CB  LYS B 265      48.446 -17.640  42.360  0.00 52.51           C  
ATOM   2633  CG  LYS B 265      47.179 -17.664  41.520  0.00 51.31           C  
ATOM   2634  CD  LYS B 265      47.017 -18.996  40.796  0.00 50.43           C  
ATOM   2635  CE  LYS B 265      46.811 -20.146  41.773  0.00 49.87           C  
ATOM   2636  NZ  LYS B 265      45.568 -19.982  42.578  0.00 49.45           N  
ATOM   2637  N   HIS B 266      49.674 -14.280  43.201  0.00 52.34           N  
ATOM   2638  CA  HIS B 266      50.141 -13.043  42.590  0.00 52.12           C  
ATOM   2639  C   HIS B 266      51.177 -12.327  43.455  0.00 52.81           C  
ATOM   2640  O   HIS B 266      52.376 -12.399  43.184  0.00 52.65           O  
ATOM   2641  CB  HIS B 266      48.955 -12.113  42.323  0.00 50.84           C  
ATOM   2642  CG  HIS B 266      49.347 -10.768  41.796  0.00 49.65           C  
ATOM   2643  ND1 HIS B 266      50.156 -10.609  40.691  0.00 49.14           N  
ATOM   2644  CD2 HIS B 266      49.036  -9.520  42.217  0.00 49.14           C  
ATOM   2645  CE1 HIS B 266      50.327  -9.320  40.455  0.00 48.82           C  
ATOM   2646  NE2 HIS B 266      49.657  -8.638  41.367  0.00 48.82           N  
ATOM   2647  N   ILE B 267      50.713 -11.639  44.494  0.00 53.97           N  
ATOM   2648  CA  ILE B 267      51.611 -10.905  45.380  0.00 55.39           C  
ATOM   2649  C   ILE B 267      51.221 -11.109  46.847  0.00 56.46           C  
ATOM   2650  O   ILE B 267      50.219 -11.758  47.146  0.00 56.31           O  
ATOM   2651  CB  ILE B 267      51.587  -9.390  45.052  0.00 55.63           C  
ATOM   2652  CG1 ILE B 267      52.893  -8.730  45.503  0.00 56.09           C  
ATOM   2653  CG2 ILE B 267      50.392  -8.726  45.722  0.00 55.21           C  
ATOM   2654  CD1 ILE B 267      54.102  -9.119  44.661  1.00 58.80           C  
ATOM   2655  N   THR B 268      52.019 -10.551  47.754  0.00 58.07           N  
ATOM   2656  CA  THR B 268      51.763 -10.666  49.187  0.00 60.00           C  
ATOM   2657  C   THR B 268      51.430  -9.299  49.793  0.00 62.04           C  
ATOM   2658  O   THR B 268      51.801  -8.263  49.241  0.00 61.94           O  
ATOM   2659  CB  THR B 268      52.986 -11.257  49.921  0.00 59.39           C  
ATOM   2660  OG1 THR B 268      54.124 -10.409  49.717  0.00 59.04           O  
ATOM   2661  CG2 THR B 268      53.299 -12.651  49.396  0.00 59.04           C  
ATOM   2662  N   PRO B 269      50.729  -9.282  50.941  1.00 64.85           N  
ATOM   2663  CA  PRO B 269      50.340  -8.041  51.627  1.00 65.32           C  
ATOM   2664  C   PRO B 269      51.513  -7.181  52.090  1.00 66.59           C  
ATOM   2665  O   PRO B 269      52.100  -7.428  53.147  1.00 67.99           O  
ATOM   2666  CB  PRO B 269      49.497  -8.543  52.795  1.00 64.41           C  
ATOM   2667  CG  PRO B 269      50.128  -9.862  53.113  1.00 64.67           C  
ATOM   2668  CD  PRO B 269      50.326 -10.458  51.735  1.00 65.40           C  
ATOM   2669  N   LEU B 270      51.838  -6.167  51.291  1.00 66.50           N  
ATOM   2670  CA  LEU B 270      52.933  -5.242  51.583  1.00 64.81           C  
ATOM   2671  C   LEU B 270      52.528  -3.804  51.251  1.00 62.78           C  
ATOM   2672  O   LEU B 270      52.657  -3.359  50.107  1.00 63.12           O  
ATOM   2673  CB  LEU B 270      54.181  -5.625  50.775  1.00 66.03           C  
ATOM   2674  CG  LEU B 270      55.055  -6.764  51.312  1.00 66.95           C  
ATOM   2675  CD1 LEU B 270      56.125  -7.143  50.287  1.00 66.50           C  
ATOM   2676  CD2 LEU B 270      55.701  -6.319  52.623  1.00 67.12           C  
ATOM   2677  N   GLN B 271      52.053  -3.078  52.259  0.00 60.15           N  
ATOM   2678  CA  GLN B 271      51.620  -1.697  52.072  0.00 57.55           C  
ATOM   2679  C   GLN B 271      52.571  -0.677  52.696  0.00 56.40           C  
ATOM   2680  O   GLN B 271      52.505  -0.405  53.895  0.00 56.10           O  
ATOM   2681  CB  GLN B 271      50.217  -1.509  52.657  0.00 56.66           C  
ATOM   2682  CG  GLN B 271      49.677  -0.089  52.553  0.00 55.33           C  
ATOM   2683  CD  GLN B 271      49.413   0.343  51.122  0.00 54.68           C  
ATOM   2684  OE1 GLN B 271      49.070   1.497  50.866  0.00 54.27           O  
ATOM   2685  NE2 GLN B 271      49.565  -0.583  50.182  0.00 54.27           N  
ATOM   2686  N   GLU B 272      53.451  -0.116  51.873  0.00 55.20           N  
ATOM   2687  CA  GLU B 272      54.408   0.889  52.323  0.00 54.20           C  
ATOM   2688  C   GLU B 272      55.085   1.559  51.130  0.00 54.22           C  
ATOM   2689  O   GLU B 272      56.243   1.281  50.817  0.00 54.00           O  
ATOM   2690  CB  GLU B 272      55.465   0.263  53.244  0.00 53.22           C  
ATOM   2691  CG  GLU B 272      56.208  -0.934  52.666  0.00 51.93           C  
ATOM   2692  CD  GLU B 272      55.350  -2.180  52.594  0.00 51.28           C  
ATOM   2693  OE1 GLU B 272      54.837  -2.610  53.649  0.00 50.87           O  
ATOM   2694  OE2 GLU B 272      55.191  -2.732  51.486  0.00 50.87           O  
ATOM   2695  N   GLN B 273      54.349   2.448  50.468  0.00 54.50           N  
ATOM   2696  CA  GLN B 273      54.858   3.162  49.302  0.00 55.06           C  
ATOM   2697  C   GLN B 273      55.297   2.188  48.212  0.00 56.26           C  
ATOM   2698  O   GLN B 273      56.370   2.339  47.627  0.00 56.12           O  
ATOM   2699  CB  GLN B 273      56.037   4.061  49.695  0.00 54.01           C  
ATOM   2700  CG  GLN B 273      55.657   5.345  50.426  0.00 52.75           C  
ATOM   2701  CD  GLN B 273      54.996   5.098  51.769  0.00 52.10           C  
ATOM   2702  OE1 GLN B 273      53.881   4.583  51.842  0.00 51.70           O  
ATOM   2703  NE2 GLN B 273      55.686   5.466  52.842  0.00 51.70           N  
ATOM   2704  N   SER B 274      54.459   1.191  47.941  0.00 58.01           N  
ATOM   2705  CA  SER B 274      54.759   0.189  46.922  0.00 60.13           C  
ATOM   2706  C   SER B 274      53.534  -0.673  46.624  0.00 62.02           C  
ATOM   2707  O   SER B 274      53.078  -1.429  47.481  0.00 62.02           O  
ATOM   2708  CB  SER B 274      55.913  -0.702  47.389  0.00 59.57           C  
ATOM   2709  OG  SER B 274      56.220  -1.691  46.422  0.00 59.22           O  
ATOM   2710  N   LYS B 275      53.009  -0.559  45.406  1.00 64.99           N  
ATOM   2711  CA  LYS B 275      51.833  -1.332  45.003  1.00 67.03           C  
ATOM   2712  C   LYS B 275      50.694  -1.168  46.013  1.00 67.17           C  
ATOM   2713  O   LYS B 275      50.298  -2.129  46.674  1.00 69.53           O  
ATOM   2714  CB  LYS B 275      52.196  -2.816  44.883  1.00 67.70           C  
ATOM   2715  CG  LYS B 275      52.166  -3.387  43.461  1.00 69.83           C  
ATOM   2716  CD  LYS B 275      53.309  -2.884  42.582  1.00 70.61           C  
ATOM   2717  CE  LYS B 275      53.075  -1.468  42.081  1.00 70.88           C  
ATOM   2718  NZ  LYS B 275      54.169  -1.040  41.168  1.00 70.87           N  
ATOM   2719  N   GLU B 276      50.172   0.051  46.125  0.00 66.17           N  
ATOM   2720  CA  GLU B 276      49.087   0.352  47.057  0.00 65.03           C  
ATOM   2721  C   GLU B 276      47.980  -0.704  47.053  0.00 64.91           C  
ATOM   2722  O   GLU B 276      47.796  -1.425  46.073  0.00 64.77           O  
ATOM   2723  CB  GLU B 276      48.489   1.725  46.733  0.00 64.08           C  
ATOM   2724  CG  GLU B 276      49.484   2.875  46.825  0.00 62.83           C  
ATOM   2725  CD  GLU B 276      49.981   3.111  48.239  0.00 62.20           C  
ATOM   2726  OE1 GLU B 276      49.162   3.485  49.104  0.00 61.80           O  
ATOM   2727  OE2 GLU B 276      51.192   2.923  48.485  0.00 61.80           O  
ATOM   2728  N   VAL B 277      47.249  -0.781  48.162  1.00 65.35           N  
ATOM   2729  CA  VAL B 277      46.154  -1.736  48.333  1.00 64.61           C  
ATOM   2730  C   VAL B 277      45.259  -1.845  47.095  1.00 64.38           C  
ATOM   2731  O   VAL B 277      45.073  -2.935  46.546  1.00 63.91           O  
ATOM   2732  CB  VAL B 277      45.270  -1.344  49.548  1.00 64.58           C  
ATOM   2733  CG1 VAL B 277      44.166  -2.369  49.747  1.00 64.21           C  
ATOM   2734  CG2 VAL B 277      46.129  -1.227  50.804  1.00 65.32           C  
ATOM   2735  N   ALA B 278      44.709  -0.710  46.668  1.00 63.86           N  
ATOM   2736  CA  ALA B 278      43.826  -0.654  45.506  1.00 63.21           C  
ATOM   2737  C   ALA B 278      44.415  -1.368  44.295  1.00 63.49           C  
ATOM   2738  O   ALA B 278      43.706  -2.074  43.578  1.00 63.86           O  
ATOM   2739  CB  ALA B 278      43.525   0.790  45.157  1.00 62.74           C  
ATOM   2740  N   ILE B 279      45.712  -1.174  44.070  1.00 63.78           N  
ATOM   2741  CA  ILE B 279      46.409  -1.798  42.952  1.00 63.63           C  
ATOM   2742  C   ILE B 279      46.434  -3.314  43.097  1.00 63.46           C  
ATOM   2743  O   ILE B 279      46.266  -4.044  42.121  1.00 63.46           O  
ATOM   2744  CB  ILE B 279      47.863  -1.282  42.846  1.00 63.96           C  
ATOM   2745  CG1 ILE B 279      47.884   0.058  42.106  1.00 64.84           C  
ATOM   2746  CG2 ILE B 279      48.733  -2.300  42.116  1.00 64.62           C  
ATOM   2747  CD1 ILE B 279      47.003   1.130  42.730  1.00 65.36           C  
ATOM   2748  N   ARG B 280      46.644  -3.782  44.321  1.00 62.64           N  
ATOM   2749  CA  ARG B 280      46.688  -5.210  44.579  1.00 61.57           C  
ATOM   2750  C   ARG B 280      45.326  -5.836  44.330  1.00 59.79           C  
ATOM   2751  O   ARG B 280      45.239  -6.955  43.832  1.00 60.31           O  
ATOM   2752  CB  ARG B 280      47.144  -5.470  46.016  1.00 63.36           C  
ATOM   2753  CG  ARG B 280      48.655  -5.367  46.209  1.00 64.50           C  
ATOM   2754  CD  ARG B 280      49.006  -5.012  47.652  1.00 66.12           C  
ATOM   2755  NE  ARG B 280      48.418  -5.931  48.623  1.00 66.23           N  
ATOM   2756  CZ  ARG B 280      48.277  -5.653  49.914  1.00 66.44           C  
ATOM   2757  NH1 ARG B 280      48.681  -4.481  50.385  1.00 68.56           N  
ATOM   2758  NH2 ARG B 280      47.726  -6.539  50.734  1.00 65.41           N  
ATOM   2759  N   ILE B 281      44.264  -5.112  44.668  1.00 58.38           N  
ATOM   2760  CA  ILE B 281      42.914  -5.623  44.451  1.00 57.79           C  
ATOM   2761  C   ILE B 281      42.638  -5.666  42.945  1.00 57.75           C  
ATOM   2762  O   ILE B 281      42.103  -6.645  42.428  1.00 57.64           O  
ATOM   2763  CB  ILE B 281      41.842  -4.724  45.116  1.00 57.34           C  
ATOM   2764  CG1 ILE B 281      42.147  -4.529  46.603  1.00 57.05           C  
ATOM   2765  CG2 ILE B 281      40.475  -5.362  44.962  1.00 56.07           C  
ATOM   2766  CD1 ILE B 281      42.107  -5.803  47.401  1.00 56.68           C  
ATOM   2767  N   PHE B 282      43.015  -4.593  42.254  1.00 57.13           N  
ATOM   2768  CA  PHE B 282      42.831  -4.474  40.811  1.00 57.37           C  
ATOM   2769  C   PHE B 282      43.474  -5.646  40.070  1.00 56.67           C  
ATOM   2770  O   PHE B 282      42.880  -6.227  39.165  1.00 55.70           O  
ATOM   2771  CB  PHE B 282      43.449  -3.157  40.325  1.00 58.36           C  
ATOM   2772  CG  PHE B 282      43.363  -2.952  38.838  1.00 60.85           C  
ATOM   2773  CD1 PHE B 282      42.135  -2.730  38.223  1.00 61.23           C  
ATOM   2774  CD2 PHE B 282      44.514  -2.969  38.052  1.00 61.38           C  
ATOM   2775  CE1 PHE B 282      42.054  -2.524  36.842  1.00 63.22           C  
ATOM   2776  CE2 PHE B 282      44.444  -2.766  36.674  1.00 62.01           C  
ATOM   2777  CZ  PHE B 282      43.212  -2.542  36.067  1.00 62.21           C  
ATOM   2778  N   GLN B 283      44.699  -5.979  40.462  1.00 56.45           N  
ATOM   2779  CA  GLN B 283      45.444  -7.074  39.856  1.00 56.38           C  
ATOM   2780  C   GLN B 283      44.735  -8.403  40.108  1.00 54.26           C  
ATOM   2781  O   GLN B 283      44.736  -9.291  39.255  1.00 53.71           O  
ATOM   2782  CB  GLN B 283      46.866  -7.111  40.431  1.00 59.19           C  
ATOM   2783  CG  GLN B 283      47.678  -5.842  40.143  1.00 63.51           C  
ATOM   2784  CD  GLN B 283      49.003  -5.791  40.895  1.00 65.47           C  
ATOM   2785  OE1 GLN B 283      49.030  -5.736  42.126  1.00 67.38           O  
ATOM   2786  NE2 GLN B 283      50.108  -5.806  40.153  1.00 66.93           N  
ATOM   2787  N   GLY B 284      44.128  -8.532  41.284  1.00 52.35           N  
ATOM   2788  CA  GLY B 284      43.410  -9.751  41.613  1.00 47.99           C  
ATOM   2789  C   GLY B 284      42.216  -9.936  40.696  1.00 46.59           C  
ATOM   2790  O   GLY B 284      41.930 -11.053  40.247  1.00 44.53           O  
ATOM   2791  N   CYS B 285      41.514  -8.840  40.414  0.50 44.54           N  
ATOM   2792  CA  CYS B 285      40.350  -8.885  39.538  0.50 44.07           C  
ATOM   2793  C   CYS B 285      40.780  -9.215  38.118  0.50 42.30           C  
ATOM   2794  O   CYS B 285      40.098  -9.949  37.406  0.50 41.03           O  
ATOM   2795  CB  CYS B 285      39.607  -7.547  39.561  0.50 45.30           C  
ATOM   2796  SG  CYS B 285      38.826  -7.176  41.146  0.50 52.50           S  
ATOM   2797  N   GLN B 286      41.917  -8.668  37.709  1.00 42.75           N  
ATOM   2798  CA  GLN B 286      42.440  -8.933  36.376  1.00 43.28           C  
ATOM   2799  C   GLN B 286      42.801 -10.413  36.238  1.00 44.07           C  
ATOM   2800  O   GLN B 286      42.418 -11.064  35.267  1.00 44.77           O  
ATOM   2801  CB  GLN B 286      43.658  -8.053  36.107  1.00 44.87           C  
ATOM   2802  CG  GLN B 286      43.302  -6.600  35.812  1.00 49.08           C  
ATOM   2803  CD  GLN B 286      42.516  -6.447  34.518  1.00 52.22           C  
ATOM   2804  OE1 GLN B 286      43.070  -6.566  33.421  1.00 56.76           O  
ATOM   2805  NE2 GLN B 286      41.219  -6.198  34.638  1.00 54.17           N  
ATOM   2806  N   PHE B 287      43.513 -10.952  37.222  1.00 42.27           N  
ATOM   2807  CA  PHE B 287      43.899 -12.357  37.182  1.00 41.05           C  
ATOM   2808  C   PHE B 287      42.672 -13.249  37.017  1.00 40.30           C  
ATOM   2809  O   PHE B 287      42.672 -14.150  36.181  1.00 41.39           O  
ATOM   2810  CB  PHE B 287      44.667 -12.744  38.459  1.00 38.18           C  
ATOM   2811  CG  PHE B 287      45.179 -14.162  38.455  1.00 38.94           C  
ATOM   2812  CD1 PHE B 287      44.334 -15.228  38.757  1.00 37.07           C  
ATOM   2813  CD2 PHE B 287      46.507 -14.433  38.125  1.00 38.81           C  
ATOM   2814  CE1 PHE B 287      44.806 -16.545  38.729  1.00 38.75           C  
ATOM   2815  CE2 PHE B 287      46.993 -15.752  38.092  1.00 38.26           C  
ATOM   2816  CZ  PHE B 287      46.145 -16.804  38.393  1.00 36.23           C  
ATOM   2817  N   ARG B 288      41.629 -13.003  37.807  1.00 39.98           N  
ATOM   2818  CA  ARG B 288      40.410 -13.808  37.714  1.00 39.95           C  
ATOM   2819  C   ARG B 288      39.707 -13.570  36.370  1.00 38.48           C  
ATOM   2820  O   ARG B 288      39.085 -14.484  35.823  1.00 34.25           O  
ATOM   2821  CB  ARG B 288      39.455 -13.494  38.875  1.00 41.00           C  
ATOM   2822  CG  ARG B 288      40.108 -13.571  40.268  1.00 51.06           C  
ATOM   2823  CD  ARG B 288      40.448 -15.016  40.734  1.00 56.01           C  
ATOM   2824  NE  ARG B 288      39.294 -15.714  41.311  1.00 58.59           N  
ATOM   2825  CZ  ARG B 288      39.186 -17.040  41.410  1.00 59.52           C  
ATOM   2826  NH1 ARG B 288      40.167 -17.825  40.970  1.00 56.77           N  
ATOM   2827  NH2 ARG B 288      38.085 -17.582  41.926  1.00 57.20           N  
ATOM   2828  N   SER B 289      39.821 -12.348  35.841  1.00 36.70           N  
ATOM   2829  CA  SER B 289      39.216 -11.995  34.551  1.00 37.92           C  
ATOM   2830  C   SER B 289      39.894 -12.712  33.393  1.00 37.36           C  
ATOM   2831  O   SER B 289      39.234 -13.113  32.435  1.00 40.71           O  
ATOM   2832  CB  SER B 289      39.281 -10.487  34.312  1.00 37.78           C  
ATOM   2833  OG  SER B 289      38.365  -9.817  35.153  1.00 41.03           O  
ATOM   2834  N   VAL B 290      41.213 -12.863  33.466  1.00 36.71           N  
ATOM   2835  CA  VAL B 290      41.921 -13.573  32.419  1.00 35.85           C  
ATOM   2836  C   VAL B 290      41.423 -15.016  32.428  1.00 36.86           C  
ATOM   2837  O   VAL B 290      41.285 -15.626  31.379  1.00 36.35           O  
ATOM   2838  CB  VAL B 290      43.443 -13.531  32.636  1.00 36.82           C  
ATOM   2839  CG1 VAL B 290      44.131 -14.589  31.781  1.00 34.92           C  
ATOM   2840  CG2 VAL B 290      43.974 -12.143  32.262  1.00 37.20           C  
ATOM   2841  N   GLU B 291      41.141 -15.555  33.614  1.00 38.40           N  
ATOM   2842  CA  GLU B 291      40.630 -16.929  33.724  1.00 39.18           C  
ATOM   2843  C   GLU B 291      39.218 -17.012  33.154  1.00 39.07           C  
ATOM   2844  O   GLU B 291      38.904 -17.911  32.375  1.00 42.14           O  
ATOM   2845  CB  GLU B 291      40.562 -17.379  35.180  1.00 36.83           C  
ATOM   2846  CG  GLU B 291      41.876 -17.441  35.918  1.00 39.49           C  
ATOM   2847  CD  GLU B 291      41.682 -17.973  37.322  1.00 40.37           C  
ATOM   2848  OE1 GLU B 291      40.934 -17.334  38.098  1.00 39.61           O  
ATOM   2849  OE2 GLU B 291      42.259 -19.035  37.642  1.00 40.99           O  
ATOM   2850  N   ALA B 292      38.355 -16.092  33.582  1.00 39.00           N  
ATOM   2851  CA  ALA B 292      36.974 -16.054  33.104  1.00 38.36           C  
ATOM   2852  C   ALA B 292      36.937 -16.029  31.573  1.00 36.57           C  
ATOM   2853  O   ALA B 292      36.106 -16.697  30.950  1.00 38.22           O  
ATOM   2854  CB  ALA B 292      36.247 -14.824  33.681  1.00 37.70           C  
ATOM   2855  N   VAL B 293      37.843 -15.272  30.965  1.00 35.97           N  
ATOM   2856  CA  VAL B 293      37.891 -15.202  29.506  1.00 36.12           C  
ATOM   2857  C   VAL B 293      38.074 -16.576  28.870  1.00 35.82           C  
ATOM   2858  O   VAL B 293      37.457 -16.882  27.848  1.00 33.36           O  
ATOM   2859  CB  VAL B 293      39.028 -14.294  29.027  1.00 36.75           C  
ATOM   2860  CG1 VAL B 293      39.269 -14.491  27.515  1.00 35.54           C  
ATOM   2861  CG2 VAL B 293      38.679 -12.843  29.337  1.00 38.21           C  
ATOM   2862  N   GLN B 294      38.925 -17.405  29.466  1.00 34.22           N  
ATOM   2863  CA  GLN B 294      39.163 -18.735  28.910  1.00 33.09           C  
ATOM   2864  C   GLN B 294      37.957 -19.618  29.155  1.00 29.75           C  
ATOM   2865  O   GLN B 294      37.591 -20.421  28.320  1.00 29.80           O  
ATOM   2866  CB  GLN B 294      40.428 -19.361  29.521  1.00 33.81           C  
ATOM   2867  CG  GLN B 294      41.725 -18.689  29.070  1.00 35.80           C  
ATOM   2868  CD  GLN B 294      41.763 -18.432  27.563  1.00 39.98           C  
ATOM   2869  OE1 GLN B 294      41.414 -19.300  26.759  1.00 40.47           O  
ATOM   2870  NE2 GLN B 294      42.200 -17.240  27.179  1.00 40.39           N  
ATOM   2871  N   GLU B 295      37.333 -19.467  30.310  1.00 30.72           N  
ATOM   2872  CA  GLU B 295      36.146 -20.248  30.614  1.00 31.64           C  
ATOM   2873  C   GLU B 295      34.973 -19.851  29.706  1.00 32.06           C  
ATOM   2874  O   GLU B 295      34.200 -20.709  29.268  1.00 29.34           O  
ATOM   2875  CB  GLU B 295      35.776 -20.058  32.077  1.00 32.99           C  
ATOM   2876  CG  GLU B 295      36.779 -20.683  33.036  1.00 35.57           C  
ATOM   2877  CD  GLU B 295      36.702 -20.076  34.416  1.00 36.20           C  
ATOM   2878  OE1 GLU B 295      35.580 -19.735  34.845  1.00 38.50           O  
ATOM   2879  OE2 GLU B 295      37.755 -19.943  35.076  1.00 40.49           O  
ATOM   2880  N   ILE B 296      34.820 -18.556  29.433  1.00 31.74           N  
ATOM   2881  CA  ILE B 296      33.740 -18.114  28.543  1.00 32.12           C  
ATOM   2882  C   ILE B 296      34.032 -18.619  27.122  1.00 32.98           C  
ATOM   2883  O   ILE B 296      33.123 -19.005  26.376  1.00 32.30           O  
ATOM   2884  CB  ILE B 296      33.633 -16.583  28.508  1.00 32.59           C  
ATOM   2885  CG1 ILE B 296      33.166 -16.067  29.873  1.00 31.48           C  
ATOM   2886  CG2 ILE B 296      32.678 -16.155  27.388  1.00 32.52           C  
ATOM   2887  CD1 ILE B 296      33.446 -14.595  30.073  1.00 35.80           C  
ATOM   2888  N   THR B 297      35.311 -18.622  26.757  1.00 31.06           N  
ATOM   2889  CA  THR B 297      35.721 -19.094  25.435  1.00 32.27           C  
ATOM   2890  C   THR B 297      35.348 -20.566  25.217  1.00 32.13           C  
ATOM   2891  O   THR B 297      34.965 -20.959  24.118  1.00 33.49           O  
ATOM   2892  CB  THR B 297      37.235 -18.940  25.244  1.00 30.32           C  
ATOM   2893  OG1 THR B 297      37.560 -17.546  25.200  1.00 34.80           O  
ATOM   2894  CG2 THR B 297      37.699 -19.624  23.952  1.00 26.95           C  
ATOM   2895  N   GLU B 298      35.458 -21.376  26.262  1.00 32.59           N  
ATOM   2896  CA  GLU B 298      35.129 -22.791  26.142  1.00 35.95           C  
ATOM   2897  C   GLU B 298      33.624 -22.950  26.054  1.00 34.76           C  
ATOM   2898  O   GLU B 298      33.119 -23.712  25.239  1.00 37.57           O  
ATOM   2899  CB  GLU B 298      35.661 -23.587  27.345  1.00 38.21           C  
ATOM   2900  CG  GLU B 298      35.263 -25.052  27.283  1.00 43.75           C  
ATOM   2901  CD  GLU B 298      35.708 -25.836  28.498  1.00 49.58           C  
ATOM   2902  OE1 GLU B 298      35.197 -25.567  29.608  1.00 50.08           O  
ATOM   2903  OE2 GLU B 298      36.571 -26.727  28.338  1.00 53.26           O  
ATOM   2904  N   TYR B 299      32.906 -22.237  26.916  1.00 35.14           N  
ATOM   2905  CA  TYR B 299      31.452 -22.278  26.898  1.00 33.21           C  
ATOM   2906  C   TYR B 299      30.943 -21.934  25.490  1.00 33.39           C  
ATOM   2907  O   TYR B 299      30.025 -22.579  24.976  1.00 32.46           O  
ATOM   2908  CB  TYR B 299      30.882 -21.268  27.899  1.00 34.65           C  
ATOM   2909  CG  TYR B 299      29.381 -21.210  27.865  1.00 34.57           C  
ATOM   2910  CD1 TYR B 299      28.617 -22.311  28.265  1.00 31.16           C  
ATOM   2911  CD2 TYR B 299      28.716 -20.085  27.368  1.00 36.68           C  
ATOM   2912  CE1 TYR B 299      27.253 -22.309  28.169  1.00 32.98           C  
ATOM   2913  CE2 TYR B 299      27.316 -20.071  27.269  1.00 35.11           C  
ATOM   2914  CZ  TYR B 299      26.597 -21.195  27.674  1.00 36.45           C  
ATOM   2915  OH  TYR B 299      25.223 -21.227  27.566  1.00 37.96           O  
ATOM   2916  N   ALA B 300      31.544 -20.911  24.880  1.00 32.03           N  
ATOM   2917  CA  ALA B 300      31.156 -20.460  23.542  1.00 35.12           C  
ATOM   2918  C   ALA B 300      31.269 -21.578  22.519  1.00 36.54           C  
ATOM   2919  O   ALA B 300      30.391 -21.759  21.670  1.00 34.85           O  
ATOM   2920  CB  ALA B 300      32.033 -19.282  23.111  1.00 33.66           C  
ATOM   2921  N   LYS B 301      32.362 -22.326  22.607  1.00 37.29           N  
ATOM   2922  CA  LYS B 301      32.594 -23.419  21.684  1.00 39.98           C  
ATOM   2923  C   LYS B 301      31.518 -24.499  21.753  1.00 38.54           C  
ATOM   2924  O   LYS B 301      31.379 -25.282  20.822  1.00 40.54           O  
ATOM   2925  CB  LYS B 301      33.991 -24.016  21.919  1.00 42.03           C  
ATOM   2926  CG  LYS B 301      35.106 -23.012  21.648  1.00 44.64           C  
ATOM   2927  CD  LYS B 301      36.497 -23.630  21.743  1.00 47.83           C  
ATOM   2928  CE  LYS B 301      37.552 -22.634  21.271  1.00 48.62           C  
ATOM   2929  NZ  LYS B 301      38.937 -23.180  21.320  1.00 50.15           N  
ATOM   2930  N   SER B 302      30.733 -24.520  22.825  1.00 39.37           N  
ATOM   2931  CA  SER B 302      29.665 -25.519  22.961  1.00 41.54           C  
ATOM   2932  C   SER B 302      28.318 -25.035  22.422  1.00 42.42           C  
ATOM   2933  O   SER B 302      27.349 -25.796  22.364  1.00 42.70           O  
ATOM   2934  CB  SER B 302      29.481 -25.915  24.421  1.00 40.89           C  
ATOM   2935  OG  SER B 302      28.912 -24.847  25.149  1.00 46.64           O  
ATOM   2936  N   ILE B 303      28.241 -23.762  22.052  1.00 42.45           N  
ATOM   2937  CA  ILE B 303      26.997 -23.239  21.509  1.00 40.37           C  
ATOM   2938  C   ILE B 303      26.895 -23.772  20.090  1.00 37.49           C  
ATOM   2939  O   ILE B 303      27.781 -23.534  19.277  1.00 38.53           O  
ATOM   2940  CB  ILE B 303      27.002 -21.699  21.475  1.00 38.69           C  
ATOM   2941  CG1 ILE B 303      27.149 -21.156  22.898  1.00 36.12           C  
ATOM   2942  CG2 ILE B 303      25.716 -21.190  20.830  1.00 34.22           C  
ATOM   2943  CD1 ILE B 303      27.490 -19.676  22.960  1.00 32.68           C  
ATOM   2944  N   PRO B 304      25.811 -24.501  19.775  1.00 39.00           N  
ATOM   2945  CA  PRO B 304      25.619 -25.065  18.434  1.00 38.92           C  
ATOM   2946  C   PRO B 304      25.808 -24.042  17.323  1.00 39.71           C  
ATOM   2947  O   PRO B 304      25.140 -22.993  17.308  1.00 40.93           O  
ATOM   2948  CB  PRO B 304      24.189 -25.604  18.485  1.00 38.42           C  
ATOM   2949  CG  PRO B 304      24.048 -26.018  19.914  1.00 38.76           C  
ATOM   2950  CD  PRO B 304      24.704 -24.886  20.670  1.00 37.03           C  
ATOM   2951  N   GLY B 305      26.727 -24.354  16.409  1.00 36.33           N  
ATOM   2952  CA  GLY B 305      27.010 -23.486  15.283  1.00 33.77           C  
ATOM   2953  C   GLY B 305      28.170 -22.533  15.477  1.00 34.41           C  
ATOM   2954  O   GLY B 305      28.713 -22.027  14.504  1.00 33.16           O  
ATOM   2955  N   PHE B 306      28.571 -22.292  16.725  1.00 35.37           N  
ATOM   2956  CA  PHE B 306      29.651 -21.343  16.986  1.00 34.38           C  
ATOM   2957  C   PHE B 306      30.980 -21.631  16.308  1.00 36.56           C  
ATOM   2958  O   PHE B 306      31.521 -20.768  15.610  1.00 37.56           O  
ATOM   2959  CB  PHE B 306      29.895 -21.191  18.490  1.00 34.38           C  
ATOM   2960  CG  PHE B 306      30.902 -20.112  18.829  1.00 34.33           C  
ATOM   2961  CD1 PHE B 306      30.545 -18.767  18.786  1.00 32.55           C  
ATOM   2962  CD2 PHE B 306      32.221 -20.442  19.128  1.00 34.10           C  
ATOM   2963  CE1 PHE B 306      31.479 -17.776  19.031  1.00 29.15           C  
ATOM   2964  CE2 PHE B 306      33.166 -19.458  19.373  1.00 30.52           C  
ATOM   2965  CZ  PHE B 306      32.791 -18.116  19.324  1.00 34.11           C  
ATOM   2966  N   VAL B 307      31.522 -22.827  16.520  1.00 36.65           N  
ATOM   2967  CA  VAL B 307      32.810 -23.186  15.928  1.00 37.98           C  
ATOM   2968  C   VAL B 307      32.744 -23.285  14.412  1.00 38.03           C  
ATOM   2969  O   VAL B 307      33.764 -23.257  13.738  1.00 36.77           O  
ATOM   2970  CB  VAL B 307      33.343 -24.525  16.499  1.00 37.26           C  
ATOM   2971  CG1 VAL B 307      33.602 -24.372  17.992  1.00 37.34           C  
ATOM   2972  CG2 VAL B 307      32.342 -25.639  16.252  1.00 37.60           C  
ATOM   2973  N   ASN B 308      31.534 -23.388  13.880  1.00 39.37           N  
ATOM   2974  CA  ASN B 308      31.336 -23.485  12.442  1.00 39.58           C  
ATOM   2975  C   ASN B 308      31.390 -22.117  11.764  1.00 40.01           C  
ATOM   2976  O   ASN B 308      31.311 -22.006  10.543  1.00 41.12           O  
ATOM   2977  CB  ASN B 308      30.001 -24.170  12.172  1.00 41.32           C  
ATOM   2978  CG  ASN B 308      30.090 -25.674  12.330  1.00 43.08           C  
ATOM   2979  OD1 ASN B 308      29.106 -26.343  12.623  1.00 47.15           O  
ATOM   2980  ND2 ASN B 308      31.281 -26.213  12.122  1.00 41.53           N  
ATOM   2981  N   LEU B 309      31.554 -21.072  12.561  1.00 38.37           N  
ATOM   2982  CA  LEU B 309      31.617 -19.729  12.016  1.00 36.37           C  
ATOM   2983  C   LEU B 309      33.033 -19.384  11.571  1.00 36.92           C  
ATOM   2984  O   LEU B 309      33.999 -19.976  12.044  1.00 40.19           O  
ATOM   2985  CB  LEU B 309      31.163 -18.719  13.082  1.00 34.83           C  
ATOM   2986  CG  LEU B 309      29.743 -18.806  13.646  1.00 32.33           C  
ATOM   2987  CD1 LEU B 309      29.666 -17.968  14.940  1.00 33.61           C  
ATOM   2988  CD2 LEU B 309      28.734 -18.305  12.597  1.00 34.37           C  
ATOM   2989  N   ASP B 310      33.142 -18.427  10.660  1.00 35.37           N  
ATOM   2990  CA  ASP B 310      34.423 -17.926  10.181  1.00 36.28           C  
ATOM   2991  C   ASP B 310      35.300 -17.766  11.434  1.00 37.97           C  
ATOM   2992  O   ASP B 310      34.859 -17.191  12.433  1.00 36.97           O  
ATOM   2993  CB  ASP B 310      34.183 -16.564   9.522  1.00 38.68           C  
ATOM   2994  CG  ASP B 310      35.459 -15.876   9.084  1.00 40.50           C  
ATOM   2995  OD1 ASP B 310      35.798 -15.980   7.889  1.00 42.27           O  
ATOM   2996  OD2 ASP B 310      36.119 -15.222   9.928  1.00 41.85           O  
ATOM   2997  N   LEU B 311      36.530 -18.267  11.404  1.00 36.95           N  
ATOM   2998  CA  LEU B 311      37.386 -18.154  12.589  1.00 38.61           C  
ATOM   2999  C   LEU B 311      37.573 -16.718  13.094  1.00 35.63           C  
ATOM   3000  O   LEU B 311      37.516 -16.466  14.294  1.00 33.82           O  
ATOM   3001  CB  LEU B 311      38.750 -18.803  12.330  1.00 39.60           C  
ATOM   3002  CG  LEU B 311      38.782 -20.326  12.526  1.00 43.53           C  
ATOM   3003  CD1 LEU B 311      37.771 -20.987  11.624  1.00 45.48           C  
ATOM   3004  CD2 LEU B 311      40.173 -20.853  12.214  1.00 46.67           C  
ATOM   3005  N   ASN B 312      37.800 -15.785  12.178  1.00 34.50           N  
ATOM   3006  CA  ASN B 312      37.978 -14.382  12.550  1.00 34.08           C  
ATOM   3007  C   ASN B 312      36.751 -13.857  13.294  1.00 33.60           C  
ATOM   3008  O   ASN B 312      36.870 -13.090  14.252  1.00 28.57           O  
ATOM   3009  CB  ASN B 312      38.201 -13.536  11.303  1.00 34.73           C  
ATOM   3010  CG  ASN B 312      39.592 -13.676  10.746  1.00 36.98           C  
ATOM   3011  OD1 ASN B 312      40.570 -13.412  11.435  1.00 41.62           O  
ATOM   3012  ND2 ASN B 312      39.691 -14.075   9.491  1.00 36.21           N  
ATOM   3013  N   ASP B 313      35.571 -14.280  12.847  1.00 32.61           N  
ATOM   3014  CA  ASP B 313      34.334 -13.847  13.466  1.00 33.05           C  
ATOM   3015  C   ASP B 313      34.232 -14.401  14.888  1.00 35.07           C  
ATOM   3016  O   ASP B 313      33.776 -13.712  15.800  1.00 32.68           O  
ATOM   3017  CB  ASP B 313      33.140 -14.287  12.615  1.00 32.89           C  
ATOM   3018  CG  ASP B 313      32.862 -13.330  11.460  1.00 34.09           C  
ATOM   3019  OD1 ASP B 313      33.660 -12.393  11.252  1.00 33.21           O  
ATOM   3020  OD2 ASP B 313      31.846 -13.508  10.764  1.00 33.36           O  
ATOM   3021  N   GLN B 314      34.666 -15.646  15.078  1.00 33.33           N  
ATOM   3022  CA  GLN B 314      34.633 -16.256  16.402  1.00 32.16           C  
ATOM   3023  C   GLN B 314      35.452 -15.392  17.370  1.00 29.82           C  
ATOM   3024  O   GLN B 314      35.006 -15.070  18.468  1.00 27.40           O  
ATOM   3025  CB  GLN B 314      35.237 -17.669  16.360  1.00 31.73           C  
ATOM   3026  CG  GLN B 314      34.471 -18.683  15.518  1.00 29.57           C  
ATOM   3027  CD  GLN B 314      35.092 -20.080  15.612  1.00 30.55           C  
ATOM   3028  OE1 GLN B 314      35.525 -20.490  16.681  1.00 30.16           O  
ATOM   3029  NE2 GLN B 314      35.124 -20.812  14.493  1.00 30.50           N  
ATOM   3030  N   VAL B 315      36.662 -15.032  16.947  1.00 30.85           N  
ATOM   3031  CA  VAL B 315      37.549 -14.227  17.764  1.00 32.36           C  
ATOM   3032  C   VAL B 315      36.926 -12.858  18.028  1.00 33.37           C  
ATOM   3033  O   VAL B 315      37.005 -12.341  19.136  1.00 33.20           O  
ATOM   3034  CB  VAL B 315      38.939 -14.069  17.082  1.00 33.56           C  
ATOM   3035  CG1 VAL B 315      39.823 -13.088  17.871  1.00 32.32           C  
ATOM   3036  CG2 VAL B 315      39.637 -15.439  17.014  1.00 30.46           C  
ATOM   3037  N   THR B 316      36.289 -12.290  17.011  1.00 33.44           N  
ATOM   3038  CA  THR B 316      35.649 -10.989  17.138  1.00 32.66           C  
ATOM   3039  C   THR B 316      34.503 -11.033  18.144  1.00 31.97           C  
ATOM   3040  O   THR B 316      34.380 -10.138  19.001  1.00 29.62           O  
ATOM   3041  CB  THR B 316      35.112 -10.506  15.767  1.00 32.05           C  
ATOM   3042  OG1 THR B 316      36.218 -10.267  14.894  1.00 32.38           O  
ATOM   3043  CG2 THR B 316      34.287  -9.217  15.918  1.00 31.71           C  
ATOM   3044  N   LEU B 317      33.678 -12.078  18.046  1.00 28.38           N  
ATOM   3045  CA  LEU B 317      32.536 -12.242  18.949  1.00 28.69           C  
ATOM   3046  C   LEU B 317      32.977 -12.392  20.406  1.00 28.61           C  
ATOM   3047  O   LEU B 317      32.332 -11.872  21.322  1.00 26.23           O  
ATOM   3048  CB  LEU B 317      31.680 -13.457  18.529  1.00 29.51           C  
ATOM   3049  CG  LEU B 317      30.867 -13.382  17.211  1.00 30.31           C  
ATOM   3050  CD1 LEU B 317      30.178 -14.716  16.957  1.00 25.21           C  
ATOM   3051  CD2 LEU B 317      29.808 -12.257  17.282  1.00 26.05           C  
ATOM   3052  N   LEU B 318      34.077 -13.103  20.632  1.00 30.52           N  
ATOM   3053  CA  LEU B 318      34.563 -13.287  21.993  1.00 29.75           C  
ATOM   3054  C   LEU B 318      35.192 -11.996  22.484  1.00 29.23           C  
ATOM   3055  O   LEU B 318      35.003 -11.600  23.627  1.00 30.77           O  
ATOM   3056  CB  LEU B 318      35.583 -14.438  22.043  1.00 31.00           C  
ATOM   3057  CG  LEU B 318      35.012 -15.809  22.437  1.00 29.89           C  
ATOM   3058  CD1 LEU B 318      33.561 -15.894  22.075  1.00 36.68           C  
ATOM   3059  CD2 LEU B 318      35.795 -16.913  21.748  1.00 28.88           C  
ATOM   3060  N   LYS B 319      35.913 -11.325  21.601  1.00 30.34           N  
ATOM   3061  CA  LYS B 319      36.579 -10.089  21.964  1.00 36.30           C  
ATOM   3062  C   LYS B 319      35.634  -9.036  22.537  1.00 37.80           C  
ATOM   3063  O   LYS B 319      35.953  -8.394  23.543  1.00 36.73           O  
ATOM   3064  CB  LYS B 319      37.307  -9.512  20.750  1.00 39.24           C  
ATOM   3065  CG  LYS B 319      38.042  -8.206  21.048  1.00 44.22           C  
ATOM   3066  CD  LYS B 319      38.791  -7.685  19.828  1.00 46.53           C  
ATOM   3067  CE  LYS B 319      39.556  -6.412  20.166  1.00 49.78           C  
ATOM   3068  NZ  LYS B 319      38.647  -5.324  20.642  1.00 53.03           N  
ATOM   3069  N   TYR B 320      34.476  -8.862  21.899  1.00 36.74           N  
ATOM   3070  CA  TYR B 320      33.509  -7.860  22.348  1.00 38.33           C  
ATOM   3071  C   TYR B 320      32.451  -8.354  23.318  1.00 38.80           C  
ATOM   3072  O   TYR B 320      31.750  -7.544  23.924  1.00 43.41           O  
ATOM   3073  CB  TYR B 320      32.801  -7.216  21.145  1.00 36.56           C  
ATOM   3074  CG  TYR B 320      33.727  -6.441  20.241  1.00 38.69           C  
ATOM   3075  CD1 TYR B 320      34.311  -7.043  19.124  1.00 39.75           C  
ATOM   3076  CD2 TYR B 320      34.063  -5.117  20.531  1.00 40.86           C  
ATOM   3077  CE1 TYR B 320      35.213  -6.347  18.317  1.00 42.21           C  
ATOM   3078  CE2 TYR B 320      34.964  -4.408  19.731  1.00 41.93           C  
ATOM   3079  CZ  TYR B 320      35.533  -5.029  18.629  1.00 44.58           C  
ATOM   3080  OH  TYR B 320      36.417  -4.340  17.835  1.00 47.80           O  
ATOM   3081  N   GLY B 321      32.330  -9.665  23.484  1.00 35.94           N  
ATOM   3082  CA  GLY B 321      31.301 -10.167  24.370  1.00 36.96           C  
ATOM   3083  C   GLY B 321      31.721 -10.564  25.769  1.00 38.18           C  
ATOM   3084  O   GLY B 321      30.870 -10.675  26.657  1.00 36.65           O  
ATOM   3085  N   VAL B 322      33.024 -10.765  25.972  1.00 38.65           N  
ATOM   3086  CA  VAL B 322      33.551 -11.196  27.270  1.00 37.64           C  
ATOM   3087  C   VAL B 322      33.223 -10.243  28.414  1.00 37.00           C  
ATOM   3088  O   VAL B 322      32.775 -10.680  29.474  1.00 35.07           O  
ATOM   3089  CB  VAL B 322      35.105 -11.439  27.190  1.00 37.14           C  
ATOM   3090  CG1 VAL B 322      35.777 -10.313  26.426  1.00 42.19           C  
ATOM   3091  CG2 VAL B 322      35.698 -11.521  28.568  1.00 40.85           C  
ATOM   3092  N   HIS B 323      33.440  -8.946  28.209  1.00 36.68           N  
ATOM   3093  CA  HIS B 323      33.145  -7.973  29.260  1.00 37.86           C  
ATOM   3094  C   HIS B 323      31.675  -7.944  29.640  1.00 36.49           C  
ATOM   3095  O   HIS B 323      31.343  -7.811  30.819  1.00 37.83           O  
ATOM   3096  CB  HIS B 323      33.558  -6.556  28.851  1.00 39.75           C  
ATOM   3097  CG  HIS B 323      35.036  -6.338  28.819  1.00 43.14           C  
ATOM   3098  ND1 HIS B 323      35.821  -6.701  27.744  1.00 45.76           N  
ATOM   3099  CD2 HIS B 323      35.874  -5.788  29.729  1.00 45.48           C  
ATOM   3100  CE1 HIS B 323      37.078  -6.382  27.994  1.00 46.24           C  
ATOM   3101  NE2 HIS B 323      37.138  -5.827  29.192  1.00 46.73           N  
ATOM   3102  N   GLU B 324      30.799  -8.058  28.643  1.00 33.88           N  
ATOM   3103  CA  GLU B 324      29.360  -8.028  28.880  1.00 33.79           C  
ATOM   3104  C   GLU B 324      28.950  -9.233  29.700  1.00 33.28           C  
ATOM   3105  O   GLU B 324      28.131  -9.137  30.617  1.00 31.35           O  
ATOM   3106  CB  GLU B 324      28.599  -8.011  27.544  1.00 33.29           C  
ATOM   3107  CG  GLU B 324      28.530  -6.632  26.892  1.00 34.52           C  
ATOM   3108  CD  GLU B 324      27.887  -6.646  25.514  1.00 34.11           C  
ATOM   3109  OE1 GLU B 324      27.088  -7.564  25.204  1.00 33.23           O  
ATOM   3110  OE2 GLU B 324      28.184  -5.722  24.740  1.00 34.34           O  
ATOM   3111  N   ILE B 325      29.525 -10.373  29.341  1.00 33.50           N  
ATOM   3112  CA  ILE B 325      29.278 -11.628  30.031  1.00 32.99           C  
ATOM   3113  C   ILE B 325      29.839 -11.554  31.455  1.00 32.58           C  
ATOM   3114  O   ILE B 325      29.196 -11.996  32.403  1.00 32.76           O  
ATOM   3115  CB  ILE B 325      29.958 -12.775  29.261  1.00 35.14           C  
ATOM   3116  CG1 ILE B 325      29.265 -12.926  27.902  1.00 36.26           C  
ATOM   3117  CG2 ILE B 325      29.917 -14.076  30.075  1.00 32.82           C  
ATOM   3118  CD1 ILE B 325      30.093 -13.613  26.853  1.00 38.17           C  
ATOM   3119  N   ILE B 326      31.029 -10.983  31.614  1.00 31.84           N  
ATOM   3120  CA  ILE B 326      31.612 -10.897  32.950  1.00 33.60           C  
ATOM   3121  C   ILE B 326      30.734 -10.102  33.912  1.00 35.64           C  
ATOM   3122  O   ILE B 326      30.433 -10.563  35.017  1.00 33.94           O  
ATOM   3123  CB  ILE B 326      33.042 -10.321  32.885  1.00 32.15           C  
ATOM   3124  CG1 ILE B 326      33.986 -11.432  32.407  1.00 30.85           C  
ATOM   3125  CG2 ILE B 326      33.478  -9.765  34.263  1.00 34.38           C  
ATOM   3126  CD1 ILE B 326      35.400 -10.979  32.094  1.00 29.55           C  
ATOM   3127  N   TYR B 327      30.287  -8.922  33.493  1.00 38.03           N  
ATOM   3128  CA  TYR B 327      29.437  -8.124  34.361  1.00 38.30           C  
ATOM   3129  C   TYR B 327      28.087  -8.774  34.599  1.00 36.50           C  
ATOM   3130  O   TYR B 327      27.535  -8.668  35.690  1.00 36.14           O  
ATOM   3131  CB  TYR B 327      29.311  -6.702  33.806  1.00 41.24           C  
ATOM   3132  CG  TYR B 327      30.617  -5.976  33.998  1.00 46.09           C  
ATOM   3133  CD1 TYR B 327      31.155  -5.826  35.279  1.00 50.31           C  
ATOM   3134  CD2 TYR B 327      31.377  -5.553  32.912  1.00 49.05           C  
ATOM   3135  CE1 TYR B 327      32.427  -5.286  35.475  1.00 54.04           C  
ATOM   3136  CE2 TYR B 327      32.654  -5.009  33.094  1.00 52.11           C  
ATOM   3137  CZ  TYR B 327      33.171  -4.882  34.380  1.00 54.00           C  
ATOM   3138  OH  TYR B 327      34.433  -4.372  34.582  1.00 55.89           O  
ATOM   3139  N   THR B 328      27.566  -9.467  33.594  1.00 34.77           N  
ATOM   3140  CA  THR B 328      26.290 -10.161  33.741  1.00 35.71           C  
ATOM   3141  C   THR B 328      26.416 -11.275  34.784  1.00 36.09           C  
ATOM   3142  O   THR B 328      25.626 -11.360  35.730  1.00 35.28           O  
ATOM   3143  CB  THR B 328      25.842 -10.783  32.396  1.00 35.72           C  
ATOM   3144  OG1 THR B 328      25.534  -9.734  31.475  1.00 38.34           O  
ATOM   3145  CG2 THR B 328      24.601 -11.667  32.573  1.00 34.29           C  
ATOM   3146  N   MET B 329      27.414 -12.134  34.621  1.00 36.42           N  
ATOM   3147  CA  MET B 329      27.582 -13.233  35.573  1.00 37.29           C  
ATOM   3148  C   MET B 329      28.062 -12.760  36.947  1.00 34.78           C  
ATOM   3149  O   MET B 329      27.774 -13.393  37.959  1.00 33.45           O  
ATOM   3150  CB  MET B 329      28.542 -14.276  35.005  1.00 39.21           C  
ATOM   3151  CG  MET B 329      28.044 -14.915  33.728  1.00 40.72           C  
ATOM   3152  SD  MET B 329      29.081 -16.292  33.250  1.00 44.14           S  
ATOM   3153  CE  MET B 329      30.575 -15.489  32.938  1.00 43.71           C  
ATOM   3154  N   LEU B 330      28.781 -11.643  36.976  1.00 34.65           N  
ATOM   3155  CA  LEU B 330      29.287 -11.080  38.230  1.00 36.93           C  
ATOM   3156  C   LEU B 330      28.132 -10.816  39.200  1.00 37.50           C  
ATOM   3157  O   LEU B 330      28.249 -10.998  40.418  1.00 36.21           O  
ATOM   3158  CB  LEU B 330      30.005  -9.764  37.949  1.00 37.83           C  
ATOM   3159  CG  LEU B 330      31.481  -9.620  38.311  1.00 42.87           C  
ATOM   3160  CD1 LEU B 330      31.951  -8.222  37.913  1.00 45.20           C  
ATOM   3161  CD2 LEU B 330      31.691  -9.855  39.799  1.00 39.40           C  
ATOM   3162  N   ALA B 331      27.014 -10.375  38.640  1.00 38.30           N  
ATOM   3163  CA  ALA B 331      25.827 -10.072  39.421  1.00 37.53           C  
ATOM   3164  C   ALA B 331      25.363 -11.299  40.186  1.00 37.85           C  
ATOM   3165  O   ALA B 331      24.806 -11.177  41.270  1.00 39.41           O  
ATOM   3166  CB  ALA B 331      24.709  -9.560  38.497  1.00 35.56           C  
ATOM   3167  N   SER B 332      25.585 -12.482  39.623  1.00 38.60           N  
ATOM   3168  CA  SER B 332      25.179 -13.718  40.293  1.00 39.22           C  
ATOM   3169  C   SER B 332      25.945 -13.868  41.597  1.00 40.15           C  
ATOM   3170  O   SER B 332      25.510 -14.576  42.505  1.00 40.86           O  
ATOM   3171  CB  SER B 332      25.476 -14.944  39.420  1.00 38.51           C  
ATOM   3172  OG  SER B 332      24.666 -14.988  38.262  1.00 38.73           O  
ATOM   3173  N   LEU B 333      27.084 -13.191  41.685  1.00 41.55           N  
ATOM   3174  CA  LEU B 333      27.923 -13.270  42.870  1.00 42.91           C  
ATOM   3175  C   LEU B 333      27.814 -12.023  43.743  1.00 44.61           C  
ATOM   3176  O   LEU B 333      28.503 -11.910  44.758  1.00 45.38           O  
ATOM   3177  CB  LEU B 333      29.385 -13.484  42.456  1.00 41.35           C  
ATOM   3178  CG  LEU B 333      29.673 -14.572  41.413  1.00 41.93           C  
ATOM   3179  CD1 LEU B 333      31.171 -14.625  41.139  1.00 39.46           C  
ATOM   3180  CD2 LEU B 333      29.168 -15.934  41.890  1.00 39.98           C  
ATOM   3181  N   MET B 334      26.938 -11.097  43.359  1.00 45.39           N  
ATOM   3182  CA  MET B 334      26.762  -9.859  44.112  1.00 44.90           C  
ATOM   3183  C   MET B 334      25.385  -9.666  44.749  1.00 45.13           C  
ATOM   3184  O   MET B 334      24.376 -10.207  44.290  1.00 42.28           O  
ATOM   3185  CB  MET B 334      27.003  -8.650  43.215  1.00 44.62           C  
ATOM   3186  CG  MET B 334      28.369  -8.546  42.579  1.00 48.41           C  
ATOM   3187  SD  MET B 334      28.351  -7.132  41.445  1.00 50.19           S  
ATOM   3188  CE  MET B 334      29.705  -6.179  42.020  1.00 49.53           C  
ATOM   3189  N   ASN B 335      25.373  -8.890  45.827  1.00 43.73           N  
ATOM   3190  CA  ASN B 335      24.148  -8.521  46.507  1.00 44.07           C  
ATOM   3191  C   ASN B 335      24.386  -7.054  46.794  1.00 43.80           C  
ATOM   3192  O   ASN B 335      25.448  -6.539  46.461  1.00 41.47           O  
ATOM   3193  CB  ASN B 335      23.912  -9.342  47.789  1.00 44.37           C  
ATOM   3194  CG  ASN B 335      24.936  -9.078  48.880  1.00 43.65           C  
ATOM   3195  OD1 ASN B 335      24.980  -9.808  49.862  1.00 46.35           O  
ATOM   3196  ND2 ASN B 335      25.748  -8.047  48.723  1.00 45.97           N  
ATOM   3197  N   LYS B 336      23.421  -6.382  47.405  1.00 45.70           N  
ATOM   3198  CA  LYS B 336      23.551  -4.957  47.681  1.00 48.21           C  
ATOM   3199  C   LYS B 336      24.646  -4.598  48.683  1.00 48.45           C  
ATOM   3200  O   LYS B 336      24.946  -3.420  48.873  1.00 50.39           O  
ATOM   3201  CB  LYS B 336      22.197  -4.414  48.151  1.00 50.93           C  
ATOM   3202  CG  LYS B 336      21.032  -4.957  47.319  1.00 53.98           C  
ATOM   3203  CD  LYS B 336      19.709  -4.230  47.561  1.00 54.98           C  
ATOM   3204  CE  LYS B 336      19.751  -2.807  47.023  1.00 56.02           C  
ATOM   3205  NZ  LYS B 336      18.405  -2.167  47.051  1.00 57.11           N  
ATOM   3206  N   ASP B 337      25.264  -5.605  49.299  1.00 48.74           N  
ATOM   3207  CA  ASP B 337      26.314  -5.360  50.290  1.00 47.90           C  
ATOM   3208  C   ASP B 337      27.703  -5.911  49.991  1.00 47.58           C  
ATOM   3209  O   ASP B 337      28.620  -5.726  50.794  1.00 47.38           O  
ATOM   3210  CB  ASP B 337      25.874  -5.884  51.657  1.00 48.53           C  
ATOM   3211  CG  ASP B 337      24.729  -5.093  52.235  1.00 47.94           C  
ATOM   3212  OD1 ASP B 337      24.904  -3.875  52.459  1.00 49.72           O  
ATOM   3213  OD2 ASP B 337      23.656  -5.685  52.459  1.00 47.34           O  
ATOM   3214  N   GLY B 338      27.875  -6.590  48.860  1.00 45.97           N  
ATOM   3215  CA  GLY B 338      29.196  -7.121  48.554  1.00 45.37           C  
ATOM   3216  C   GLY B 338      29.264  -8.170  47.462  1.00 43.60           C  
ATOM   3217  O   GLY B 338      28.242  -8.601  46.944  1.00 44.24           O  
ATOM   3218  N   VAL B 339      30.479  -8.590  47.119  1.00 43.84           N  
ATOM   3219  CA  VAL B 339      30.673  -9.578  46.068  1.00 43.10           C  
ATOM   3220  C   VAL B 339      31.562 -10.743  46.502  1.00 42.85           C  
ATOM   3221  O   VAL B 339      32.592 -10.544  47.141  1.00 42.40           O  
ATOM   3222  CB  VAL B 339      31.280  -8.898  44.811  1.00 43.00           C  
ATOM   3223  CG1 VAL B 339      32.496  -8.074  45.204  1.00 43.27           C  
ATOM   3224  CG2 VAL B 339      31.657  -9.936  43.772  1.00 43.79           C  
ATOM   3225  N   LEU B 340      31.141 -11.960  46.168  1.00 43.32           N  
ATOM   3226  CA  LEU B 340      31.910 -13.155  46.490  1.00 43.02           C  
ATOM   3227  C   LEU B 340      33.146 -13.167  45.616  1.00 45.76           C  
ATOM   3228  O   LEU B 340      33.077 -12.867  44.420  1.00 46.72           O  
ATOM   3229  CB  LEU B 340      31.094 -14.412  46.214  1.00 41.29           C  
ATOM   3230  CG  LEU B 340      29.840 -14.567  47.066  1.00 41.08           C  
ATOM   3231  CD1 LEU B 340      29.070 -15.795  46.616  1.00 40.40           C  
ATOM   3232  CD2 LEU B 340      30.237 -14.689  48.529  1.00 43.51           C  
ATOM   3233  N   ILE B 341      34.275 -13.531  46.211  1.00 47.43           N  
ATOM   3234  CA  ILE B 341      35.539 -13.564  45.498  1.00 48.93           C  
ATOM   3235  C   ILE B 341      36.187 -14.934  45.694  1.00 49.69           C  
ATOM   3236  O   ILE B 341      35.759 -15.724  46.539  1.00 49.10           O  
ATOM   3237  CB  ILE B 341      36.478 -12.437  46.035  1.00 50.89           C  
ATOM   3238  CG1 ILE B 341      37.215 -11.763  44.880  1.00 52.74           C  
ATOM   3239  CG2 ILE B 341      37.449 -12.987  47.080  1.00 49.61           C  
ATOM   3240  CD1 ILE B 341      38.081 -12.683  44.024  1.00 56.03           C  
ATOM   3241  N   SER B 342      37.191 -15.221  44.878  1.00 49.48           N  
ATOM   3242  CA  SER B 342      37.935 -16.465  44.979  1.00 51.69           C  
ATOM   3243  C   SER B 342      37.118 -17.751  45.079  1.00 51.06           C  
ATOM   3244  O   SER B 342      37.244 -18.493  46.052  1.00 50.52           O  
ATOM   3245  CB  SER B 342      38.879 -16.374  46.180  1.00 51.06           C  
ATOM   3246  OG  SER B 342      39.634 -17.559  46.312  1.00 56.83           O  
ATOM   3247  N   GLU B 343      36.282 -18.022  44.084  1.00 52.84           N  
ATOM   3248  CA  GLU B 343      35.495 -19.258  44.095  1.00 53.93           C  
ATOM   3249  C   GLU B 343      34.494 -19.249  45.244  1.00 53.27           C  
ATOM   3250  O   GLU B 343      34.043 -20.302  45.708  1.00 51.72           O  
ATOM   3251  CB  GLU B 343      36.442 -20.457  44.245  1.00 57.62           C  
ATOM   3252  CG  GLU B 343      35.801 -21.830  44.110  1.00 61.59           C  
ATOM   3253  CD  GLU B 343      35.511 -22.198  42.673  1.00 62.96           C  
ATOM   3254  OE1 GLU B 343      36.467 -22.249  41.867  1.00 63.67           O  
ATOM   3255  OE2 GLU B 343      34.327 -22.439  42.356  1.00 66.06           O  
ATOM   3256  N   GLY B 344      34.152 -18.053  45.706  1.00 52.93           N  
ATOM   3257  CA  GLY B 344      33.206 -17.937  46.797  1.00 52.69           C  
ATOM   3258  C   GLY B 344      33.850 -18.121  48.159  1.00 52.55           C  
ATOM   3259  O   GLY B 344      33.173 -18.036  49.183  1.00 52.79           O  
ATOM   3260  N   GLN B 345      35.154 -18.375  48.184  1.00 51.70           N  
ATOM   3261  CA  GLN B 345      35.847 -18.556  49.457  1.00 51.73           C  
ATOM   3262  C   GLN B 345      35.974 -17.216  50.173  1.00 49.40           C  
ATOM   3263  O   GLN B 345      36.286 -17.163  51.359  1.00 49.32           O  
ATOM   3264  CB  GLN B 345      37.242 -19.151  49.243  1.00 51.86           C  
ATOM   3265  CG  GLN B 345      37.254 -20.456  48.473  1.00 57.43           C  
ATOM   3266  CD  GLN B 345      36.037 -21.313  48.756  1.00 60.67           C  
ATOM   3267  OE1 GLN B 345      35.722 -21.614  49.911  1.00 64.11           O  
ATOM   3268  NE2 GLN B 345      35.341 -21.715  47.694  1.00 63.25           N  
ATOM   3269  N   GLY B 346      35.728 -16.134  49.444  1.00 46.95           N  
ATOM   3270  CA  GLY B 346      35.821 -14.818  50.041  1.00 43.83           C  
ATOM   3271  C   GLY B 346      34.619 -13.930  49.771  1.00 45.01           C  
ATOM   3272  O   GLY B 346      33.759 -14.243  48.944  1.00 42.21           O  
ATOM   3273  N   PHE B 347      34.566 -12.814  50.490  1.00 44.65           N  
ATOM   3274  CA  PHE B 347      33.491 -11.847  50.353  1.00 46.68           C  
ATOM   3275  C   PHE B 347      34.078 -10.467  50.587  1.00 46.99           C  
ATOM   3276  O   PHE B 347      34.580 -10.175  51.671  1.00 47.28           O  
ATOM   3277  CB  PHE B 347      32.393 -12.106  51.388  1.00 46.58           C  
ATOM   3278  CG  PHE B 347      31.223 -11.167  51.273  1.00 46.24           C  
ATOM   3279  CD1 PHE B 347      30.302 -11.303  50.238  1.00 47.15           C  
ATOM   3280  CD2 PHE B 347      31.059 -10.127  52.181  1.00 47.48           C  
ATOM   3281  CE1 PHE B 347      29.235 -10.416  50.110  1.00 48.03           C  
ATOM   3282  CE2 PHE B 347      29.997  -9.231  52.064  1.00 47.47           C  
ATOM   3283  CZ  PHE B 347      29.082  -9.375  51.027  1.00 49.24           C  
ATOM   3284  N   MET B 348      34.017  -9.617  49.571  1.00 48.25           N  
ATOM   3285  CA  MET B 348      34.558  -8.267  49.684  1.00 48.90           C  
ATOM   3286  C   MET B 348      33.384  -7.298  49.764  1.00 48.79           C  
ATOM   3287  O   MET B 348      32.624  -7.159  48.806  1.00 48.98           O  
ATOM   3288  CB  MET B 348      35.433  -7.972  48.467  1.00 51.32           C  
ATOM   3289  CG  MET B 348      36.493  -6.912  48.686  1.00 54.06           C  
ATOM   3290  SD  MET B 348      37.678  -6.930  47.337  1.00 58.40           S  
ATOM   3291  CE  MET B 348      38.691  -8.329  47.793  1.00 56.07           C  
ATOM   3292  N   THR B 349      33.239  -6.628  50.906  1.00 48.96           N  
ATOM   3293  CA  THR B 349      32.124  -5.702  51.120  1.00 48.53           C  
ATOM   3294  C   THR B 349      32.094  -4.536  50.144  1.00 48.94           C  
ATOM   3295  O   THR B 349      33.132  -4.070  49.673  1.00 49.39           O  
ATOM   3296  CB  THR B 349      32.118  -5.112  52.569  1.00 46.90           C  
ATOM   3297  OG1 THR B 349      33.076  -4.050  52.667  1.00 47.22           O  
ATOM   3298  CG2 THR B 349      32.476  -6.188  53.583  1.00 47.98           C  
ATOM   3299  N   ARG B 350      30.884  -4.071  49.857  1.00 49.34           N  
ATOM   3300  CA  ARG B 350      30.652  -2.949  48.959  1.00 50.55           C  
ATOM   3301  C   ARG B 350      31.277  -1.684  49.534  1.00 52.23           C  
ATOM   3302  O   ARG B 350      31.817  -0.857  48.794  1.00 51.49           O  
ATOM   3303  CB  ARG B 350      29.145  -2.753  48.787  1.00 50.74           C  
ATOM   3304  CG  ARG B 350      28.722  -1.620  47.871  1.00 49.35           C  
ATOM   3305  CD  ARG B 350      27.236  -1.720  47.637  1.00 49.44           C  
ATOM   3306  NE  ARG B 350      26.729  -0.778  46.646  1.00 52.21           N  
ATOM   3307  CZ  ARG B 350      25.451  -0.721  46.289  1.00 53.09           C  
ATOM   3308  NH1 ARG B 350      24.583  -1.552  46.849  1.00 53.51           N  
ATOM   3309  NH2 ARG B 350      25.037   0.157  45.385  1.00 53.48           N  
ATOM   3310  N   GLU B 351      31.185  -1.547  50.858  1.00 54.79           N  
ATOM   3311  CA  GLU B 351      31.723  -0.400  51.591  1.00 56.47           C  
ATOM   3312  C   GLU B 351      33.228  -0.316  51.394  1.00 55.60           C  
ATOM   3313  O   GLU B 351      33.756   0.729  51.013  1.00 56.42           O  
ATOM   3314  CB  GLU B 351      31.381  -0.534  53.085  1.00 59.66           C  
ATOM   3315  CG  GLU B 351      32.001   0.519  54.026  1.00 65.03           C  
ATOM   3316  CD  GLU B 351      33.479   0.263  54.345  1.00 68.62           C  
ATOM   3317  OE1 GLU B 351      33.827  -0.883  54.719  1.00 70.62           O  
ATOM   3318  OE2 GLU B 351      34.293   1.210  54.234  1.00 69.59           O  
ATOM   3319  N   PHE B 352      33.916  -1.424  51.652  1.00 55.60           N  
ATOM   3320  CA  PHE B 352      35.363  -1.473  51.485  1.00 55.36           C  
ATOM   3321  C   PHE B 352      35.780  -1.065  50.074  1.00 56.16           C  
ATOM   3322  O   PHE B 352      36.630  -0.198  49.907  1.00 58.40           O  
ATOM   3323  CB  PHE B 352      35.889  -2.879  51.774  1.00 54.17           C  
ATOM   3324  CG  PHE B 352      37.373  -3.026  51.559  1.00 54.71           C  
ATOM   3325  CD1 PHE B 352      38.274  -2.230  52.263  1.00 52.80           C  
ATOM   3326  CD2 PHE B 352      37.871  -3.963  50.655  1.00 54.79           C  
ATOM   3327  CE1 PHE B 352      39.656  -2.367  52.073  1.00 53.72           C  
ATOM   3328  CE2 PHE B 352      39.251  -4.109  50.455  1.00 54.19           C  
ATOM   3329  CZ  PHE B 352      40.143  -3.308  51.168  1.00 54.88           C  
ATOM   3330  N   LEU B 353      35.181  -1.691  49.064  1.00 56.24           N  
ATOM   3331  CA  LEU B 353      35.501  -1.392  47.670  1.00 56.29           C  
ATOM   3332  C   LEU B 353      35.310   0.076  47.328  1.00 58.08           C  
ATOM   3333  O   LEU B 353      36.131   0.670  46.627  1.00 58.59           O  
ATOM   3334  CB  LEU B 353      34.640  -2.243  46.732  1.00 54.40           C  
ATOM   3335  CG  LEU B 353      34.964  -3.738  46.729  1.00 53.03           C  
ATOM   3336  CD1 LEU B 353      33.931  -4.495  45.921  1.00 52.49           C  
ATOM   3337  CD2 LEU B 353      36.356  -3.946  46.161  1.00 52.92           C  
ATOM   3338  N   LYS B 354      34.224   0.656  47.825  1.00 60.04           N  
ATOM   3339  CA  LYS B 354      33.922   2.054  47.558  1.00 61.92           C  
ATOM   3340  C   LYS B 354      34.832   2.998  48.338  1.00 63.24           C  
ATOM   3341  O   LYS B 354      35.082   4.122  47.906  1.00 65.49           O  
ATOM   3342  CB  LYS B 354      32.451   2.340  47.886  1.00 61.33           C  
ATOM   3343  CG  LYS B 354      32.003   3.752  47.549  1.00 61.23           C  
ATOM   3344  CD  LYS B 354      30.482   3.856  47.490  1.00 62.64           C  
ATOM   3345  CE  LYS B 354      29.837   3.579  48.835  1.00 62.45           C  
ATOM   3346  NZ  LYS B 354      28.347   3.565  48.752  1.00 62.34           N  
ATOM   3347  N   SER B 355      35.340   2.541  49.478  1.00 64.30           N  
ATOM   3348  CA  SER B 355      36.214   3.372  50.299  1.00 64.71           C  
ATOM   3349  C   SER B 355      37.575   3.582  49.645  1.00 65.54           C  
ATOM   3350  O   SER B 355      38.347   4.437  50.070  1.00 66.83           O  
ATOM   3351  CB  SER B 355      36.414   2.741  51.681  1.00 64.19           C  
ATOM   3352  OG  SER B 355      37.380   1.707  51.640  1.00 62.67           O  
ATOM   3353  N   LEU B 356      37.873   2.796  48.617  1.00 66.20           N  
ATOM   3354  CA  LEU B 356      39.149   2.919  47.923  1.00 65.94           C  
ATOM   3355  C   LEU B 356      39.303   4.302  47.298  1.00 67.32           C  
ATOM   3356  O   LEU B 356      38.318   5.018  47.104  1.00 67.26           O  
ATOM   3357  CB  LEU B 356      39.259   1.846  46.844  1.00 64.58           C  
ATOM   3358  CG  LEU B 356      39.269   0.406  47.358  1.00 63.23           C  
ATOM   3359  CD1 LEU B 356      39.162  -0.547  46.188  1.00 63.56           C  
ATOM   3360  CD2 LEU B 356      40.541   0.145  48.140  1.00 62.01           C  
ATOM   3361  N   ARG B 357      40.544   4.665  46.983  1.00 68.93           N  
ATOM   3362  CA  ARG B 357      40.861   5.964  46.392  1.00 71.20           C  
ATOM   3363  C   ARG B 357      39.904   6.431  45.299  1.00 72.49           C  
ATOM   3364  O   ARG B 357      39.067   5.669  44.812  1.00 73.71           O  
ATOM   3365  CB  ARG B 357      42.298   5.956  45.862  1.00 71.50           C  
ATOM   3366  CG  ARG B 357      43.327   5.770  46.969  1.00 72.51           C  
ATOM   3367  CD  ARG B 357      44.758   5.896  46.476  1.00 72.90           C  
ATOM   3368  NE  ARG B 357      45.076   4.918  45.442  1.00 74.22           N  
ATOM   3369  CZ  ARG B 357      46.310   4.519  45.149  1.00 76.32           C  
ATOM   3370  NH1 ARG B 357      47.350   5.011  45.816  1.00 77.54           N  
ATOM   3371  NH2 ARG B 357      46.508   3.628  44.188  1.00 76.91           N  
ATOM   3372  N   LYS B 358      40.035   7.697  44.920  1.00 73.07           N  
ATOM   3373  CA  LYS B 358      39.175   8.288  43.905  1.00 73.39           C  
ATOM   3374  C   LYS B 358      39.074   7.453  42.634  1.00 73.32           C  
ATOM   3375  O   LYS B 358      37.972   7.206  42.141  1.00 74.75           O  
ATOM   3376  CB  LYS B 358      39.655   9.699  43.545  1.00 73.41           C  
ATOM   3377  CG  LYS B 358      39.591  10.723  44.680  1.00 73.91           C  
ATOM   3378  CD  LYS B 358      40.719  10.556  45.697  1.00 73.90           C  
ATOM   3379  CE  LYS B 358      40.307   9.701  46.885  1.00 74.26           C  
ATOM   3380  NZ  LYS B 358      41.428   9.547  47.859  1.00 74.86           N  
ATOM   3381  N   PRO B 359      40.218   6.995  42.092  1.00 72.30           N  
ATOM   3382  CA  PRO B 359      40.223   6.188  40.864  1.00 71.43           C  
ATOM   3383  C   PRO B 359      39.515   4.836  40.985  1.00 70.46           C  
ATOM   3384  O   PRO B 359      38.550   4.557  40.269  1.00 69.20           O  
ATOM   3385  CB  PRO B 359      41.714   6.008  40.567  1.00 71.33           C  
ATOM   3386  CG  PRO B 359      42.372   7.139  41.306  1.00 72.09           C  
ATOM   3387  CD  PRO B 359      41.592   7.198  42.579  1.00 71.62           C  
ATOM   3388  N   PHE B 360      40.008   4.007  41.902  1.00 69.52           N  
ATOM   3389  CA  PHE B 360      39.483   2.662  42.119  1.00 68.91           C  
ATOM   3390  C   PHE B 360      38.186   2.552  42.915  1.00 68.45           C  
ATOM   3391  O   PHE B 360      37.503   1.529  42.852  1.00 68.24           O  
ATOM   3392  CB  PHE B 360      40.561   1.810  42.784  1.00 67.40           C  
ATOM   3393  CG  PHE B 360      41.764   1.568  41.914  1.00 67.43           C  
ATOM   3394  CD1 PHE B 360      41.722   0.624  40.891  1.00 67.24           C  
ATOM   3395  CD2 PHE B 360      42.944   2.276  42.123  1.00 67.08           C  
ATOM   3396  CE1 PHE B 360      42.841   0.387  40.094  1.00 66.33           C  
ATOM   3397  CE2 PHE B 360      44.066   2.047  41.330  1.00 65.92           C  
ATOM   3398  CZ  PHE B 360      44.013   1.101  40.316  1.00 66.15           C  
ATOM   3399  N   GLY B 361      37.843   3.600  43.656  1.00 68.36           N  
ATOM   3400  CA  GLY B 361      36.630   3.572  44.455  1.00 68.84           C  
ATOM   3401  C   GLY B 361      35.342   3.566  43.652  1.00 69.52           C  
ATOM   3402  O   GLY B 361      34.331   3.015  44.088  1.00 69.79           O  
ATOM   3403  N   ASP B 362      35.371   4.182  42.478  1.00 70.35           N  
ATOM   3404  CA  ASP B 362      34.192   4.244  41.620  1.00 71.28           C  
ATOM   3405  C   ASP B 362      34.284   3.216  40.499  1.00 70.68           C  
ATOM   3406  O   ASP B 362      33.709   3.390  39.424  1.00 71.22           O  
ATOM   3407  CB  ASP B 362      34.059   5.651  41.039  1.00 72.71           C  
ATOM   3408  CG  ASP B 362      35.404   6.274  40.727  1.00 74.75           C  
ATOM   3409  OD1 ASP B 362      36.196   5.645  39.989  1.00 76.47           O  
ATOM   3410  OD2 ASP B 362      35.669   7.392  41.221  1.00 75.34           O  
ATOM   3411  N   PHE B 363      35.009   2.136  40.769  1.00 70.10           N  
ATOM   3412  CA  PHE B 363      35.205   1.069  39.801  1.00 69.07           C  
ATOM   3413  C   PHE B 363      34.114   0.004  39.925  1.00 68.43           C  
ATOM   3414  O   PHE B 363      33.586  -0.477  38.919  1.00 68.71           O  
ATOM   3415  CB  PHE B 363      36.579   0.427  40.023  1.00 70.83           C  
ATOM   3416  CG  PHE B 363      37.061  -0.406  38.869  1.00 71.49           C  
ATOM   3417  CD1 PHE B 363      37.499   0.197  37.694  1.00 71.62           C  
ATOM   3418  CD2 PHE B 363      37.086  -1.797  38.960  1.00 72.66           C  
ATOM   3419  CE1 PHE B 363      37.955  -0.570  36.625  1.00 73.03           C  
ATOM   3420  CE2 PHE B 363      37.540  -2.577  37.897  1.00 72.80           C  
ATOM   3421  CZ  PHE B 363      37.977  -1.963  36.727  1.00 73.92           C  
ATOM   3422  N   MET B 364      33.763  -0.352  41.158  1.00 66.66           N  
ATOM   3423  CA  MET B 364      32.754  -1.388  41.373  1.00 65.18           C  
ATOM   3424  C   MET B 364      31.339  -0.930  41.730  1.00 63.47           C  
ATOM   3425  O   MET B 364      30.399  -1.718  41.628  1.00 63.44           O  
ATOM   3426  CB  MET B 364      33.245  -2.375  42.436  1.00 65.25           C  
ATOM   3427  CG  MET B 364      34.433  -3.227  42.011  1.00 65.08           C  
ATOM   3428  SD  MET B 364      34.052  -4.328  40.628  1.00 66.78           S  
ATOM   3429  CE  MET B 364      32.827  -5.395  41.379  1.00 62.11           C  
ATOM   3430  N   GLU B 365      31.173   0.325  42.140  1.00 61.84           N  
ATOM   3431  CA  GLU B 365      29.841   0.818  42.503  1.00 60.55           C  
ATOM   3432  C   GLU B 365      28.818   0.710  41.378  1.00 59.48           C  
ATOM   3433  O   GLU B 365      27.697   0.233  41.589  1.00 59.32           O  
ATOM   3434  CB  GLU B 365      29.902   2.272  42.983  1.00 60.79           C  
ATOM   3435  CG  GLU B 365      29.910   2.413  44.493  1.00 60.43           C  
ATOM   3436  CD  GLU B 365      28.717   1.735  45.154  1.00 60.00           C  
ATOM   3437  OE1 GLU B 365      27.589   2.266  45.074  1.00 59.49           O  
ATOM   3438  OE2 GLU B 365      28.906   0.659  45.756  1.00 60.51           O  
ATOM   3439  N   PRO B 366      29.179   1.169  40.169  1.00 57.99           N  
ATOM   3440  CA  PRO B 366      28.219   1.075  39.066  1.00 57.45           C  
ATOM   3441  C   PRO B 366      27.808  -0.378  38.786  1.00 56.40           C  
ATOM   3442  O   PRO B 366      26.696  -0.639  38.320  1.00 56.96           O  
ATOM   3443  CB  PRO B 366      28.963   1.734  37.901  1.00 56.96           C  
ATOM   3444  CG  PRO B 366      30.407   1.506  38.238  1.00 58.54           C  
ATOM   3445  CD  PRO B 366      30.452   1.759  39.719  1.00 56.83           C  
ATOM   3446  N   LYS B 367      28.698  -1.321  39.083  1.00 54.87           N  
ATOM   3447  CA  LYS B 367      28.384  -2.732  38.866  1.00 54.12           C  
ATOM   3448  C   LYS B 367      27.354  -3.160  39.906  1.00 51.75           C  
ATOM   3449  O   LYS B 367      26.432  -3.920  39.602  1.00 51.52           O  
ATOM   3450  CB  LYS B 367      29.635  -3.611  39.005  1.00 54.16           C  
ATOM   3451  CG  LYS B 367      30.919  -3.004  38.464  1.00 56.41           C  
ATOM   3452  CD  LYS B 367      30.874  -2.729  36.978  1.00 58.00           C  
ATOM   3453  CE  LYS B 367      32.163  -2.040  36.530  1.00 60.64           C  
ATOM   3454  NZ  LYS B 367      32.257  -1.861  35.047  1.00 62.68           N  
ATOM   3455  N   PHE B 368      27.515  -2.661  41.131  1.00 50.52           N  
ATOM   3456  CA  PHE B 368      26.610  -2.985  42.233  1.00 49.41           C  
ATOM   3457  C   PHE B 368      25.192  -2.538  41.941  1.00 48.73           C  
ATOM   3458  O   PHE B 368      24.238  -3.273  42.193  1.00 49.10           O  
ATOM   3459  CB  PHE B 368      27.094  -2.338  43.538  1.00 49.49           C  
ATOM   3460  CG  PHE B 368      28.173  -3.120  44.232  1.00 49.99           C  
ATOM   3461  CD1 PHE B 368      27.883  -4.340  44.834  1.00 49.83           C  
ATOM   3462  CD2 PHE B 368      29.487  -2.669  44.239  1.00 49.77           C  
ATOM   3463  CE1 PHE B 368      28.883  -5.099  45.425  1.00 48.77           C  
ATOM   3464  CE2 PHE B 368      30.494  -3.425  44.829  1.00 48.91           C  
ATOM   3465  CZ  PHE B 368      30.189  -4.640  45.420  1.00 48.06           C  
ATOM   3466  N   GLU B 369      25.058  -1.327  41.415  1.00 49.04           N  
ATOM   3467  CA  GLU B 369      23.746  -0.788  41.080  1.00 49.16           C  
ATOM   3468  C   GLU B 369      23.106  -1.635  39.981  1.00 46.55           C  
ATOM   3469  O   GLU B 369      21.928  -1.979  40.052  1.00 45.84           O  
ATOM   3470  CB  GLU B 369      23.873   0.665  40.616  1.00 51.79           C  
ATOM   3471  CG  GLU B 369      24.268   1.627  41.718  1.00 56.53           C  
ATOM   3472  CD  GLU B 369      24.176   3.075  41.280  1.00 59.89           C  
ATOM   3473  OE1 GLU B 369      24.904   3.459  40.341  1.00 61.62           O  
ATOM   3474  OE2 GLU B 369      23.370   3.828  41.872  1.00 63.45           O  
ATOM   3475  N   PHE B 370      23.898  -1.976  38.973  1.00 45.88           N  
ATOM   3476  CA  PHE B 370      23.413  -2.792  37.876  1.00 44.73           C  
ATOM   3477  C   PHE B 370      22.964  -4.145  38.410  1.00 43.99           C  
ATOM   3478  O   PHE B 370      21.862  -4.606  38.108  1.00 43.97           O  
ATOM   3479  CB  PHE B 370      24.517  -3.001  36.835  1.00 45.95           C  
ATOM   3480  CG  PHE B 370      24.145  -3.980  35.752  1.00 47.86           C  
ATOM   3481  CD1 PHE B 370      23.284  -3.608  34.724  1.00 47.47           C  
ATOM   3482  CD2 PHE B 370      24.615  -5.286  35.791  1.00 47.23           C  
ATOM   3483  CE1 PHE B 370      22.893  -4.529  33.752  1.00 50.60           C  
ATOM   3484  CE2 PHE B 370      24.231  -6.212  34.825  1.00 48.14           C  
ATOM   3485  CZ  PHE B 370      23.370  -5.836  33.806  1.00 49.15           C  
ATOM   3486  N   ALA B 371      23.831  -4.766  39.210  1.00 43.26           N  
ATOM   3487  CA  ALA B 371      23.580  -6.079  39.803  1.00 41.79           C  
ATOM   3488  C   ALA B 371      22.280  -6.126  40.578  1.00 41.87           C  
ATOM   3489  O   ALA B 371      21.481  -7.069  40.446  1.00 40.03           O  
ATOM   3490  CB  ALA B 371      24.731  -6.450  40.724  1.00 40.95           C  
ATOM   3491  N   VAL B 372      22.090  -5.109  41.411  1.00 43.52           N  
ATOM   3492  CA  VAL B 372      20.898  -5.001  42.237  1.00 44.64           C  
ATOM   3493  C   VAL B 372      19.647  -5.044  41.373  1.00 42.62           C  
ATOM   3494  O   VAL B 372      18.720  -5.794  41.654  1.00 43.00           O  
ATOM   3495  CB  VAL B 372      20.926  -3.696  43.076  1.00 46.51           C  
ATOM   3496  CG1 VAL B 372      19.568  -3.447  43.708  1.00 48.76           C  
ATOM   3497  CG2 VAL B 372      21.985  -3.814  44.168  1.00 46.17           C  
ATOM   3498  N   LYS B 373      19.624  -4.254  40.309  1.00 44.11           N  
ATOM   3499  CA  LYS B 373      18.465  -4.253  39.422  1.00 45.95           C  
ATOM   3500  C   LYS B 373      18.354  -5.581  38.669  1.00 44.40           C  
ATOM   3501  O   LYS B 373      17.288  -6.200  38.632  1.00 45.46           O  
ATOM   3502  CB  LYS B 373      18.559  -3.098  38.417  1.00 48.35           C  
ATOM   3503  CG  LYS B 373      18.432  -1.709  39.030  1.00 51.74           C  
ATOM   3504  CD  LYS B 373      18.760  -0.624  38.012  1.00 51.88           C  
ATOM   3505  CE  LYS B 373      20.222  -0.706  37.586  1.00 53.30           C  
ATOM   3506  NZ  LYS B 373      20.587   0.332  36.570  1.00 55.18           N  
ATOM   3507  N   PHE B 374      19.460  -6.015  38.074  1.00 42.37           N  
ATOM   3508  CA  PHE B 374      19.485  -7.262  37.307  1.00 42.02           C  
ATOM   3509  C   PHE B 374      19.000  -8.459  38.130  1.00 39.37           C  
ATOM   3510  O   PHE B 374      18.210  -9.273  37.649  1.00 38.54           O  
ATOM   3511  CB  PHE B 374      20.907  -7.530  36.782  1.00 40.68           C  
ATOM   3512  CG  PHE B 374      20.994  -8.685  35.819  1.00 41.35           C  
ATOM   3513  CD1 PHE B 374      20.461  -8.578  34.535  1.00 40.08           C  
ATOM   3514  CD2 PHE B 374      21.612  -9.882  36.194  1.00 40.36           C  
ATOM   3515  CE1 PHE B 374      20.539  -9.640  33.630  1.00 40.75           C  
ATOM   3516  CE2 PHE B 374      21.696 -10.952  35.302  1.00 40.35           C  
ATOM   3517  CZ  PHE B 374      21.160 -10.832  34.014  1.00 41.21           C  
ATOM   3518  N   ASN B 375      19.469  -8.566  39.371  1.00 40.23           N  
ATOM   3519  CA  ASN B 375      19.067  -9.678  40.232  1.00 39.63           C  
ATOM   3520  C   ASN B 375      17.583  -9.676  40.625  1.00 40.37           C  
ATOM   3521  O   ASN B 375      17.046 -10.703  41.051  1.00 37.71           O  
ATOM   3522  CB  ASN B 375      19.939  -9.712  41.487  1.00 39.80           C  
ATOM   3523  CG  ASN B 375      21.369 -10.138  41.186  1.00 39.79           C  
ATOM   3524  OD1 ASN B 375      21.621 -10.845  40.209  1.00 37.97           O  
ATOM   3525  ND2 ASN B 375      22.307  -9.721  42.031  1.00 39.55           N  
ATOM   3526  N   ALA B 376      16.922  -8.529  40.473  1.00 40.63           N  
ATOM   3527  CA  ALA B 376      15.507  -8.420  40.801  1.00 40.86           C  
ATOM   3528  C   ALA B 376      14.699  -9.280  39.834  1.00 41.40           C  
ATOM   3529  O   ALA B 376      13.541  -9.602  40.089  1.00 43.05           O  
ATOM   3530  CB  ALA B 376      15.057  -6.962  40.700  1.00 42.25           C  
ATOM   3531  N   LEU B 377      15.321  -9.645  38.719  1.00 40.46           N  
ATOM   3532  CA  LEU B 377      14.671 -10.464  37.711  1.00 40.50           C  
ATOM   3533  C   LEU B 377      14.628 -11.930  38.143  1.00 38.56           C  
ATOM   3534  O   LEU B 377      13.960 -12.748  37.524  1.00 39.54           O  
ATOM   3535  CB  LEU B 377      15.412 -10.329  36.376  1.00 40.16           C  
ATOM   3536  CG  LEU B 377      15.492  -8.925  35.766  1.00 42.67           C  
ATOM   3537  CD1 LEU B 377      16.164  -9.002  34.412  1.00 41.19           C  
ATOM   3538  CD2 LEU B 377      14.090  -8.343  35.608  1.00 42.80           C  
ATOM   3539  N   GLU B 378      15.347 -12.250  39.211  1.00 39.82           N  
ATOM   3540  CA  GLU B 378      15.396 -13.613  39.730  1.00 41.03           C  
ATOM   3541  C   GLU B 378      15.650 -14.709  38.693  1.00 38.07           C  
ATOM   3542  O   GLU B 378      14.989 -15.741  38.674  1.00 36.41           O  
ATOM   3543  CB  GLU B 378      14.118 -13.922  40.511  1.00 44.15           C  
ATOM   3544  CG  GLU B 378      14.017 -13.158  41.814  1.00 47.68           C  
ATOM   3545  CD  GLU B 378      12.815 -13.578  42.646  1.00 52.19           C  
ATOM   3546  OE1 GLU B 378      12.816 -14.706  43.193  1.00 55.26           O  
ATOM   3547  OE2 GLU B 378      11.862 -12.781  42.748  1.00 54.61           O  
ATOM   3548  N   LEU B 379      16.618 -14.476  37.821  1.00 38.57           N  
ATOM   3549  CA  LEU B 379      16.979 -15.477  36.826  1.00 38.34           C  
ATOM   3550  C   LEU B 379      17.800 -16.561  37.537  1.00 37.34           C  
ATOM   3551  O   LEU B 379      18.423 -16.288  38.552  1.00 35.48           O  
ATOM   3552  CB  LEU B 379      17.845 -14.835  35.735  1.00 36.68           C  
ATOM   3553  CG  LEU B 379      17.174 -14.233  34.490  1.00 39.69           C  
ATOM   3554  CD1 LEU B 379      15.923 -13.490  34.854  1.00 37.47           C  
ATOM   3555  CD2 LEU B 379      18.161 -13.333  33.778  1.00 34.47           C  
ATOM   3556  N   ASP B 380      17.771 -17.791  37.033  1.00 38.55           N  
ATOM   3557  CA  ASP B 380      18.607 -18.834  37.615  1.00 39.54           C  
ATOM   3558  C   ASP B 380      19.599 -19.280  36.554  1.00 38.67           C  
ATOM   3559  O   ASP B 380      19.582 -18.774  35.429  1.00 37.78           O  
ATOM   3560  CB  ASP B 380      17.794 -20.028  38.143  1.00 40.32           C  
ATOM   3561  CG  ASP B 380      16.870 -20.626  37.119  1.00 40.54           C  
ATOM   3562  OD1 ASP B 380      17.272 -20.808  35.949  1.00 41.70           O  
ATOM   3563  OD2 ASP B 380      15.726 -20.939  37.511  1.00 44.70           O  
ATOM   3564  N   ASP B 381      20.467 -20.216  36.913  1.00 38.84           N  
ATOM   3565  CA  ASP B 381      21.490 -20.712  36.001  1.00 37.91           C  
ATOM   3566  C   ASP B 381      20.974 -21.201  34.644  1.00 37.79           C  
ATOM   3567  O   ASP B 381      21.614 -20.965  33.618  1.00 38.25           O  
ATOM   3568  CB  ASP B 381      22.307 -21.822  36.682  1.00 38.46           C  
ATOM   3569  CG  ASP B 381      23.021 -21.344  37.950  1.00 38.86           C  
ATOM   3570  OD1 ASP B 381      22.626 -21.783  39.053  1.00 38.97           O  
ATOM   3571  OD2 ASP B 381      23.976 -20.533  37.849  1.00 40.41           O  
ATOM   3572  N   SER B 382      19.831 -21.877  34.619  1.00 37.17           N  
ATOM   3573  CA  SER B 382      19.299 -22.362  33.345  1.00 38.36           C  
ATOM   3574  C   SER B 382      18.872 -21.192  32.450  1.00 37.32           C  
ATOM   3575  O   SER B 382      18.982 -21.274  31.223  1.00 36.77           O  
ATOM   3576  CB  SER B 382      18.120 -23.307  33.582  1.00 39.33           C  
ATOM   3577  OG  SER B 382      17.107 -22.656  34.317  1.00 44.99           O  
ATOM   3578  N   ASP B 383      18.391 -20.107  33.058  1.00 35.63           N  
ATOM   3579  CA  ASP B 383      18.005 -18.928  32.278  1.00 34.82           C  
ATOM   3580  C   ASP B 383      19.276 -18.218  31.808  1.00 33.03           C  
ATOM   3581  O   ASP B 383      19.453 -17.943  30.622  1.00 33.18           O  
ATOM   3582  CB  ASP B 383      17.195 -17.926  33.115  1.00 31.67           C  
ATOM   3583  CG  ASP B 383      15.982 -18.538  33.756  1.00 33.34           C  
ATOM   3584  OD1 ASP B 383      15.270 -19.325  33.077  1.00 35.49           O  
ATOM   3585  OD2 ASP B 383      15.733 -18.206  34.942  1.00 33.82           O  
ATOM   3586  N   LEU B 384      20.156 -17.906  32.753  1.00 34.31           N  
ATOM   3587  CA  LEU B 384      21.406 -17.219  32.430  1.00 34.57           C  
ATOM   3588  C   LEU B 384      22.255 -17.936  31.386  1.00 36.70           C  
ATOM   3589  O   LEU B 384      22.943 -17.288  30.579  1.00 36.50           O  
ATOM   3590  CB  LEU B 384      22.225 -17.008  33.698  1.00 33.61           C  
ATOM   3591  CG  LEU B 384      21.652 -15.982  34.667  1.00 36.17           C  
ATOM   3592  CD1 LEU B 384      22.413 -16.026  35.994  1.00 35.23           C  
ATOM   3593  CD2 LEU B 384      21.746 -14.601  34.024  1.00 34.86           C  
ATOM   3594  N   ALA B 385      22.220 -19.269  31.391  1.00 36.48           N  
ATOM   3595  CA  ALA B 385      23.004 -20.031  30.413  1.00 36.17           C  
ATOM   3596  C   ALA B 385      22.617 -19.625  28.986  1.00 34.20           C  
ATOM   3597  O   ALA B 385      23.487 -19.440  28.130  1.00 33.04           O  
ATOM   3598  CB  ALA B 385      22.791 -21.549  30.607  1.00 33.57           C  
ATOM   3599  N   ILE B 386      21.318 -19.492  28.729  1.00 33.84           N  
ATOM   3600  CA  ILE B 386      20.857 -19.113  27.395  1.00 34.47           C  
ATOM   3601  C   ILE B 386      21.169 -17.641  27.107  1.00 32.83           C  
ATOM   3602  O   ILE B 386      21.606 -17.293  26.017  1.00 34.94           O  
ATOM   3603  CB  ILE B 386      19.343 -19.284  27.234  1.00 36.60           C  
ATOM   3604  CG1 ILE B 386      18.855 -20.558  27.938  1.00 41.98           C  
ATOM   3605  CG2 ILE B 386      19.004 -19.317  25.745  1.00 36.03           C  
ATOM   3606  CD1 ILE B 386      19.017 -21.823  27.144  1.00 44.88           C  
ATOM   3607  N   PHE B 387      20.920 -16.785  28.090  1.00 33.05           N  
ATOM   3608  CA  PHE B 387      21.177 -15.353  27.963  1.00 32.65           C  
ATOM   3609  C   PHE B 387      22.619 -15.065  27.551  1.00 31.75           C  
ATOM   3610  O   PHE B 387      22.878 -14.282  26.644  1.00 31.58           O  
ATOM   3611  CB  PHE B 387      20.888 -14.648  29.293  1.00 30.21           C  
ATOM   3612  CG  PHE B 387      21.055 -13.149  29.228  1.00 33.08           C  
ATOM   3613  CD1 PHE B 387      20.439 -12.414  28.216  1.00 31.57           C  
ATOM   3614  CD2 PHE B 387      21.831 -12.478  30.163  1.00 29.18           C  
ATOM   3615  CE1 PHE B 387      20.599 -11.034  28.140  1.00 32.14           C  
ATOM   3616  CE2 PHE B 387      21.994 -11.101  30.092  1.00 29.49           C  
ATOM   3617  CZ  PHE B 387      21.381 -10.382  29.083  1.00 29.38           C  
ATOM   3618  N   ILE B 388      23.566 -15.710  28.218  1.00 32.61           N  
ATOM   3619  CA  ILE B 388      24.974 -15.488  27.908  1.00 32.39           C  
ATOM   3620  C   ILE B 388      25.279 -15.848  26.462  1.00 29.93           C  
ATOM   3621  O   ILE B 388      26.070 -15.188  25.796  1.00 28.71           O  
ATOM   3622  CB  ILE B 388      25.852 -16.304  28.871  1.00 37.36           C  
ATOM   3623  CG1 ILE B 388      25.574 -15.838  30.296  1.00 39.11           C  
ATOM   3624  CG2 ILE B 388      27.324 -16.134  28.538  1.00 36.10           C  
ATOM   3625  CD1 ILE B 388      26.101 -16.792  31.357  1.00 50.65           C  
ATOM   3626  N   ALA B 389      24.640 -16.905  25.983  1.00 28.39           N  
ATOM   3627  CA  ALA B 389      24.819 -17.351  24.622  1.00 29.14           C  
ATOM   3628  C   ALA B 389      24.273 -16.286  23.656  1.00 28.89           C  
ATOM   3629  O   ALA B 389      24.848 -16.051  22.596  1.00 30.29           O  
ATOM   3630  CB  ALA B 389      24.095 -18.686  24.421  1.00 25.83           C  
ATOM   3631  N   VAL B 390      23.150 -15.666  24.009  1.00 29.41           N  
ATOM   3632  CA  VAL B 390      22.579 -14.603  23.164  1.00 29.25           C  
ATOM   3633  C   VAL B 390      23.618 -13.489  23.060  1.00 27.28           C  
ATOM   3634  O   VAL B 390      23.952 -13.025  21.973  1.00 27.43           O  
ATOM   3635  CB  VAL B 390      21.275 -14.045  23.793  1.00 29.94           C  
ATOM   3636  CG1 VAL B 390      20.853 -12.734  23.116  1.00 30.99           C  
ATOM   3637  CG2 VAL B 390      20.184 -15.080  23.659  1.00 28.02           C  
ATOM   3638  N   ILE B 391      24.157 -13.080  24.202  1.00 26.95           N  
ATOM   3639  CA  ILE B 391      25.157 -12.018  24.224  1.00 27.24           C  
ATOM   3640  C   ILE B 391      26.324 -12.291  23.274  1.00 29.34           C  
ATOM   3641  O   ILE B 391      26.763 -11.403  22.528  1.00 25.97           O  
ATOM   3642  CB  ILE B 391      25.705 -11.817  25.656  1.00 24.93           C  
ATOM   3643  CG1 ILE B 391      24.617 -11.230  26.550  1.00 25.37           C  
ATOM   3644  CG2 ILE B 391      26.920 -10.936  25.628  1.00 28.47           C  
ATOM   3645  CD1 ILE B 391      25.061 -10.968  27.992  1.00 27.70           C  
ATOM   3646  N   ILE B 392      26.812 -13.532  23.287  1.00 30.86           N  
ATOM   3647  CA  ILE B 392      27.939 -13.910  22.449  1.00 28.39           C  
ATOM   3648  C   ILE B 392      27.617 -13.872  20.954  1.00 29.53           C  
ATOM   3649  O   ILE B 392      28.445 -13.441  20.159  1.00 28.17           O  
ATOM   3650  CB  ILE B 392      28.478 -15.332  22.839  1.00 27.97           C  
ATOM   3651  CG1 ILE B 392      29.126 -15.280  24.220  1.00 31.05           C  
ATOM   3652  CG2 ILE B 392      29.522 -15.793  21.832  1.00 28.31           C  
ATOM   3653  CD1 ILE B 392      29.291 -16.631  24.895  1.00 32.82           C  
ATOM   3654  N   LEU B 393      26.425 -14.321  20.572  1.00 30.13           N  
ATOM   3655  CA  LEU B 393      26.037 -14.335  19.160  1.00 31.79           C  
ATOM   3656  C   LEU B 393      25.346 -13.028  18.755  1.00 34.69           C  
ATOM   3657  O   LEU B 393      24.266 -13.031  18.147  1.00 33.77           O  
ATOM   3658  CB  LEU B 393      25.100 -15.517  18.874  1.00 29.46           C  
ATOM   3659  CG  LEU B 393      25.737 -16.901  18.687  1.00 32.87           C  
ATOM   3660  CD1 LEU B 393      26.515 -16.920  17.370  1.00 32.02           C  
ATOM   3661  CD2 LEU B 393      26.653 -17.240  19.879  1.00 30.37           C  
ATOM   3662  N   SER B 394      25.967 -11.902  19.068  1.00 33.41           N  
ATOM   3663  CA  SER B 394      25.315 -10.656  18.722  1.00 40.48           C  
ATOM   3664  C   SER B 394      25.094 -10.471  17.225  1.00 43.00           C  
ATOM   3665  O   SER B 394      24.098 -10.955  16.676  1.00 50.25           O  
ATOM   3666  CB  SER B 394      26.068  -9.476  19.325  1.00 37.79           C  
ATOM   3667  OG  SER B 394      25.788  -9.429  20.713  1.00 37.66           O  
ATOM   3668  N   GLY B 395      26.006  -9.802  16.546  1.00 42.47           N  
ATOM   3669  CA  GLY B 395      25.795  -9.592  15.124  1.00 40.43           C  
ATOM   3670  C   GLY B 395      26.190  -8.177  14.778  1.00 39.66           C  
ATOM   3671  O   GLY B 395      26.601  -7.889  13.655  1.00 41.00           O  
ATOM   3672  N   ASP B 396      26.103  -7.294  15.766  1.00 40.85           N  
ATOM   3673  CA  ASP B 396      26.452  -5.894  15.564  1.00 41.94           C  
ATOM   3674  C   ASP B 396      27.872  -5.598  16.016  1.00 41.72           C  
ATOM   3675  O   ASP B 396      28.274  -4.437  16.100  1.00 43.90           O  
ATOM   3676  CB  ASP B 396      25.455  -4.983  16.303  1.00 44.29           C  
ATOM   3677  CG  ASP B 396      25.533  -5.126  17.818  1.00 47.56           C  
ATOM   3678  OD1 ASP B 396      26.262  -6.019  18.302  1.00 50.70           O  
ATOM   3679  OD2 ASP B 396      24.863  -4.345  18.529  1.00 47.51           O  
ATOM   3680  N   ARG B 397      28.644  -6.640  16.310  1.00 39.76           N  
ATOM   3681  CA  ARG B 397      30.019  -6.416  16.731  1.00 37.50           C  
ATOM   3682  C   ARG B 397      30.730  -5.893  15.510  1.00 37.05           C  
ATOM   3683  O   ARG B 397      30.496  -6.377  14.406  1.00 36.86           O  
ATOM   3684  CB  ARG B 397      30.702  -7.717  17.172  1.00 34.65           C  
ATOM   3685  CG  ARG B 397      29.981  -8.440  18.258  1.00 31.78           C  
ATOM   3686  CD  ARG B 397      29.779  -7.557  19.476  1.00 30.44           C  
ATOM   3687  NE  ARG B 397      29.286  -8.352  20.592  1.00 30.93           N  
ATOM   3688  CZ  ARG B 397      28.818  -7.868  21.732  1.00 31.17           C  
ATOM   3689  NH1 ARG B 397      28.768  -6.558  21.944  1.00 29.08           N  
ATOM   3690  NH2 ARG B 397      28.388  -8.712  22.660  1.00 30.78           N  
ATOM   3691  N   PRO B 398      31.609  -4.899  15.688  1.00 35.32           N  
ATOM   3692  CA  PRO B 398      32.324  -4.360  14.536  1.00 36.13           C  
ATOM   3693  C   PRO B 398      33.346  -5.331  13.959  1.00 36.45           C  
ATOM   3694  O   PRO B 398      33.944  -6.133  14.689  1.00 39.35           O  
ATOM   3695  CB  PRO B 398      32.966  -3.077  15.087  1.00 35.07           C  
ATOM   3696  CG  PRO B 398      33.149  -3.367  16.528  1.00 36.19           C  
ATOM   3697  CD  PRO B 398      31.880  -4.111  16.905  1.00 35.70           C  
ATOM   3698  N   GLY B 399      33.524  -5.258  12.644  1.00 33.64           N  
ATOM   3699  CA  GLY B 399      34.485  -6.096  11.956  1.00 34.32           C  
ATOM   3700  C   GLY B 399      34.038  -7.492  11.567  1.00 34.62           C  
ATOM   3701  O   GLY B 399      34.824  -8.239  10.995  1.00 35.92           O  
ATOM   3702  N   LEU B 400      32.797  -7.858  11.861  1.00 33.62           N  
ATOM   3703  CA  LEU B 400      32.322  -9.197  11.516  1.00 35.71           C  
ATOM   3704  C   LEU B 400      32.335  -9.358  10.004  1.00 37.86           C  
ATOM   3705  O   LEU B 400      32.126  -8.389   9.273  1.00 38.58           O  
ATOM   3706  CB  LEU B 400      30.912  -9.438  12.079  1.00 30.90           C  
ATOM   3707  CG  LEU B 400      30.827  -9.516  13.608  1.00 32.22           C  
ATOM   3708  CD1 LEU B 400      29.360  -9.638  14.073  1.00 29.53           C  
ATOM   3709  CD2 LEU B 400      31.651 -10.711  14.080  1.00 32.06           C  
ATOM   3710  N   LEU B 401      32.582 -10.577   9.532  1.00 37.89           N  
ATOM   3711  CA  LEU B 401      32.652 -10.823   8.098  1.00 38.32           C  
ATOM   3712  C   LEU B 401      31.426 -11.509   7.496  1.00 38.11           C  
ATOM   3713  O   LEU B 401      31.146 -11.352   6.311  1.00 39.16           O  
ATOM   3714  CB  LEU B 401      33.898 -11.653   7.783  1.00 39.76           C  
ATOM   3715  CG  LEU B 401      35.273 -11.068   8.108  1.00 42.74           C  
ATOM   3716  CD1 LEU B 401      36.314 -12.180   8.047  1.00 41.28           C  
ATOM   3717  CD2 LEU B 401      35.611  -9.941   7.125  1.00 42.32           C  
ATOM   3718  N   ASN B 402      30.697 -12.268   8.303  1.00 37.20           N  
ATOM   3719  CA  ASN B 402      29.520 -12.975   7.813  1.00 36.95           C  
ATOM   3720  C   ASN B 402      28.443 -12.998   8.889  1.00 37.71           C  
ATOM   3721  O   ASN B 402      28.272 -13.999   9.593  1.00 39.10           O  
ATOM   3722  CB  ASN B 402      29.901 -14.408   7.424  1.00 36.48           C  
ATOM   3723  CG  ASN B 402      28.745 -15.170   6.809  1.00 39.00           C  
ATOM   3724  OD1 ASN B 402      27.630 -14.648   6.694  1.00 37.71           O  
ATOM   3725  ND2 ASN B 402      29.001 -16.413   6.415  1.00 38.16           N  
ATOM   3726  N   VAL B 403      27.700 -11.897   8.979  1.00 36.15           N  
ATOM   3727  CA  VAL B 403      26.657 -11.709   9.980  1.00 35.81           C  
ATOM   3728  C   VAL B 403      25.468 -12.639   9.922  1.00 35.69           C  
ATOM   3729  O   VAL B 403      24.884 -12.959  10.960  1.00 34.65           O  
ATOM   3730  CB  VAL B 403      26.141 -10.249   9.943  1.00 34.58           C  
ATOM   3731  CG1 VAL B 403      25.026 -10.057  10.944  1.00 34.83           C  
ATOM   3732  CG2 VAL B 403      27.293  -9.301  10.221  1.00 34.92           C  
ATOM   3733  N   LYS B 404      25.106 -13.082   8.725  1.00 35.91           N  
ATOM   3734  CA  LYS B 404      23.948 -13.958   8.576  1.00 37.95           C  
ATOM   3735  C   LYS B 404      23.887 -15.161   9.528  1.00 36.96           C  
ATOM   3736  O   LYS B 404      22.943 -15.287  10.306  1.00 38.28           O  
ATOM   3737  CB  LYS B 404      23.830 -14.434   7.121  1.00 38.32           C  
ATOM   3738  CG  LYS B 404      22.705 -15.444   6.882  1.00 41.83           C  
ATOM   3739  CD  LYS B 404      22.489 -15.691   5.388  1.00 44.62           C  
ATOM   3740  CE  LYS B 404      21.507 -16.831   5.131  1.00 44.71           C  
ATOM   3741  NZ  LYS B 404      20.293 -16.755   5.988  1.00 44.23           N  
ATOM   3742  N   PRO B 405      24.891 -16.059   9.486  1.00 37.33           N  
ATOM   3743  CA  PRO B 405      24.879 -17.235  10.371  1.00 34.62           C  
ATOM   3744  C   PRO B 405      24.898 -16.883  11.853  1.00 33.18           C  
ATOM   3745  O   PRO B 405      24.371 -17.614  12.681  1.00 32.62           O  
ATOM   3746  CB  PRO B 405      26.115 -18.023   9.916  1.00 35.78           C  
ATOM   3747  CG  PRO B 405      27.051 -16.941   9.438  1.00 36.37           C  
ATOM   3748  CD  PRO B 405      26.115 -16.026   8.667  1.00 35.47           C  
ATOM   3749  N   ILE B 406      25.501 -15.753  12.191  1.00 33.62           N  
ATOM   3750  CA  ILE B 406      25.548 -15.308  13.581  1.00 34.79           C  
ATOM   3751  C   ILE B 406      24.138 -14.943  14.054  1.00 34.97           C  
ATOM   3752  O   ILE B 406      23.665 -15.428  15.091  1.00 34.58           O  
ATOM   3753  CB  ILE B 406      26.480 -14.080  13.723  1.00 34.47           C  
ATOM   3754  CG1 ILE B 406      27.926 -14.514  13.480  1.00 31.74           C  
ATOM   3755  CG2 ILE B 406      26.301 -13.432  15.090  1.00 34.35           C  
ATOM   3756  CD1 ILE B 406      28.896 -13.382  13.311  1.00 28.06           C  
ATOM   3757  N   GLU B 407      23.456 -14.091  13.290  1.00 36.54           N  
ATOM   3758  CA  GLU B 407      22.091 -13.689  13.656  1.00 36.09           C  
ATOM   3759  C   GLU B 407      21.134 -14.873  13.538  1.00 34.84           C  
ATOM   3760  O   GLU B 407      20.125 -14.928  14.228  1.00 34.50           O  
ATOM   3761  CB  GLU B 407      21.609 -12.540  12.775  1.00 37.69           C  
ATOM   3762  CG  GLU B 407      22.507 -11.325  12.827  1.00 43.95           C  
ATOM   3763  CD  GLU B 407      21.916 -10.126  12.102  1.00 47.67           C  
ATOM   3764  OE1 GLU B 407      21.467 -10.283  10.944  1.00 48.17           O  
ATOM   3765  OE2 GLU B 407      21.914  -9.026  12.692  1.00 49.19           O  
ATOM   3766  N   ASP B 408      21.444 -15.830  12.670  1.00 36.06           N  
ATOM   3767  CA  ASP B 408      20.576 -16.994  12.559  1.00 38.13           C  
ATOM   3768  C   ASP B 408      20.686 -17.836  13.827  1.00 38.13           C  
ATOM   3769  O   ASP B 408      19.697 -18.425  14.279  1.00 38.96           O  
ATOM   3770  CB  ASP B 408      20.927 -17.836  11.333  1.00 39.83           C  
ATOM   3771  CG  ASP B 408      20.519 -17.169  10.032  1.00 40.87           C  
ATOM   3772  OD1 ASP B 408      19.468 -16.496   9.998  1.00 44.72           O  
ATOM   3773  OD2 ASP B 408      21.241 -17.327   9.036  1.00 43.98           O  
ATOM   3774  N   ILE B 409      21.880 -17.889  14.417  1.00 38.21           N  
ATOM   3775  CA  ILE B 409      22.053 -18.659  15.654  1.00 34.99           C  
ATOM   3776  C   ILE B 409      21.386 -17.909  16.823  1.00 34.60           C  
ATOM   3777  O   ILE B 409      20.646 -18.500  17.620  1.00 35.37           O  
ATOM   3778  CB  ILE B 409      23.564 -18.920  15.945  1.00 35.96           C  
ATOM   3779  CG1 ILE B 409      24.125 -19.881  14.889  1.00 37.67           C  
ATOM   3780  CG2 ILE B 409      23.749 -19.512  17.352  1.00 30.93           C  
ATOM   3781  CD1 ILE B 409      25.667 -20.026  14.889  1.00 39.75           C  
ATOM   3782  N   GLN B 410      21.610 -16.601  16.908  1.00 34.02           N  
ATOM   3783  CA  GLN B 410      21.011 -15.821  17.986  1.00 33.29           C  
ATOM   3784  C   GLN B 410      19.483 -15.926  17.931  1.00 33.65           C  
ATOM   3785  O   GLN B 410      18.827 -16.032  18.966  1.00 34.29           O  
ATOM   3786  CB  GLN B 410      21.442 -14.348  17.905  1.00 32.36           C  
ATOM   3787  CG  GLN B 410      21.402 -13.645  19.276  1.00 34.20           C  
ATOM   3788  CD  GLN B 410      21.503 -12.136  19.180  1.00 36.93           C  
ATOM   3789  OE1 GLN B 410      22.196 -11.499  19.976  1.00 39.88           O  
ATOM   3790  NE2 GLN B 410      20.802 -11.551  18.209  1.00 36.46           N  
ATOM   3791  N   ASP B 411      18.915 -15.889  16.729  1.00 34.18           N  
ATOM   3792  CA  ASP B 411      17.470 -16.025  16.599  1.00 37.23           C  
ATOM   3793  C   ASP B 411      17.082 -17.327  17.288  1.00 36.86           C  
ATOM   3794  O   ASP B 411      16.165 -17.368  18.106  1.00 36.99           O  
ATOM   3795  CB  ASP B 411      17.053 -16.089  15.125  1.00 39.66           C  
ATOM   3796  CG  ASP B 411      15.556 -16.329  14.953  1.00 45.77           C  
ATOM   3797  OD1 ASP B 411      14.770 -15.374  15.137  1.00 47.60           O  
ATOM   3798  OD2 ASP B 411      15.157 -17.477  14.647  1.00 48.16           O  
ATOM   3799  N   ASN B 412      17.804 -18.395  16.962  1.00 39.34           N  
ATOM   3800  CA  ASN B 412      17.525 -19.700  17.549  1.00 40.49           C  
ATOM   3801  C   ASN B 412      17.714 -19.636  19.068  1.00 39.71           C  
ATOM   3802  O   ASN B 412      16.931 -20.211  19.827  1.00 38.92           O  
ATOM   3803  CB  ASN B 412      18.453 -20.745  16.925  1.00 46.52           C  
ATOM   3804  CG  ASN B 412      17.951 -22.165  17.109  1.00 52.19           C  
ATOM   3805  OD1 ASN B 412      18.508 -23.109  16.540  1.00 57.65           O  
ATOM   3806  ND2 ASN B 412      16.897 -22.327  17.903  1.00 54.87           N  
ATOM   3807  N   LEU B 413      18.749 -18.925  19.511  1.00 37.12           N  
ATOM   3808  CA  LEU B 413      19.004 -18.784  20.938  1.00 35.80           C  
ATOM   3809  C   LEU B 413      17.901 -17.971  21.623  1.00 35.28           C  
ATOM   3810  O   LEU B 413      17.479 -18.296  22.731  1.00 33.95           O  
ATOM   3811  CB  LEU B 413      20.363 -18.114  21.166  1.00 36.02           C  
ATOM   3812  CG  LEU B 413      21.567 -18.973  20.771  1.00 35.36           C  
ATOM   3813  CD1 LEU B 413      22.834 -18.160  20.851  1.00 33.47           C  
ATOM   3814  CD2 LEU B 413      21.633 -20.187  21.698  1.00 36.76           C  
ATOM   3815  N   LEU B 414      17.430 -16.914  20.964  1.00 35.39           N  
ATOM   3816  CA  LEU B 414      16.365 -16.072  21.538  1.00 35.74           C  
ATOM   3817  C   LEU B 414      15.066 -16.860  21.680  1.00 34.99           C  
ATOM   3818  O   LEU B 414      14.360 -16.742  22.686  1.00 35.32           O  
ATOM   3819  CB  LEU B 414      16.130 -14.847  20.654  1.00 34.71           C  
ATOM   3820  CG  LEU B 414      17.236 -13.803  20.682  1.00 35.03           C  
ATOM   3821  CD1 LEU B 414      17.250 -13.026  19.380  1.00 33.76           C  
ATOM   3822  CD2 LEU B 414      17.025 -12.905  21.896  1.00 33.95           C  
ATOM   3823  N   GLN B 415      14.746 -17.663  20.670  1.00 37.58           N  
ATOM   3824  CA  GLN B 415      13.538 -18.478  20.740  1.00 39.77           C  
ATOM   3825  C   GLN B 415      13.663 -19.383  21.956  1.00 39.45           C  
ATOM   3826  O   GLN B 415      12.702 -19.561  22.702  1.00 40.16           O  
ATOM   3827  CB  GLN B 415      13.372 -19.355  19.494  1.00 40.14           C  
ATOM   3828  CG  GLN B 415      13.014 -18.618  18.231  1.00 44.09           C  
ATOM   3829  CD  GLN B 415      12.713 -19.567  17.091  1.00 45.99           C  
ATOM   3830  OE1 GLN B 415      11.805 -20.390  17.183  1.00 50.02           O  
ATOM   3831  NE2 GLN B 415      13.473 -19.460  16.013  1.00 46.74           N  
ATOM   3832  N   ALA B 416      14.852 -19.946  22.160  1.00 38.68           N  
ATOM   3833  CA  ALA B 416      15.075 -20.850  23.292  1.00 38.16           C  
ATOM   3834  C   ALA B 416      14.999 -20.117  24.619  1.00 36.44           C  
ATOM   3835  O   ALA B 416      14.521 -20.662  25.614  1.00 36.47           O  
ATOM   3836  CB  ALA B 416      16.437 -21.562  23.151  1.00 36.11           C  
ATOM   3837  N   LEU B 417      15.461 -18.872  24.633  1.00 36.16           N  
ATOM   3838  CA  LEU B 417      15.435 -18.079  25.854  1.00 36.04           C  
ATOM   3839  C   LEU B 417      14.006 -17.741  26.247  1.00 36.79           C  
ATOM   3840  O   LEU B 417      13.635 -17.813  27.421  1.00 36.41           O  
ATOM   3841  CB  LEU B 417      16.227 -16.777  25.664  1.00 35.38           C  
ATOM   3842  CG  LEU B 417      16.237 -15.848  26.886  1.00 35.61           C  
ATOM   3843  CD1 LEU B 417      16.749 -16.631  28.110  1.00 33.31           C  
ATOM   3844  CD2 LEU B 417      17.117 -14.623  26.613  1.00 33.47           C  
ATOM   3845  N   GLU B 418      13.208 -17.370  25.254  1.00 38.80           N  
ATOM   3846  CA  GLU B 418      11.816 -16.996  25.489  1.00 39.72           C  
ATOM   3847  C   GLU B 418      11.013 -18.174  26.043  1.00 39.59           C  
ATOM   3848  O   GLU B 418      10.300 -18.034  27.036  1.00 37.74           O  
ATOM   3849  CB  GLU B 418      11.201 -16.467  24.185  1.00 41.03           C  
ATOM   3850  CG  GLU B 418       9.725 -16.100  24.287  1.00 43.67           C  
ATOM   3851  CD  GLU B 418       9.218 -15.375  23.056  1.00 44.95           C  
ATOM   3852  OE1 GLU B 418       9.520 -15.816  21.923  1.00 42.11           O  
ATOM   3853  OE2 GLU B 418       8.507 -14.359  23.228  1.00 52.35           O  
ATOM   3854  N   LEU B 419      11.151 -19.341  25.420  1.00 41.43           N  
ATOM   3855  CA  LEU B 419      10.434 -20.525  25.883  1.00 41.48           C  
ATOM   3856  C   LEU B 419      10.866 -20.857  27.310  1.00 41.92           C  
ATOM   3857  O   LEU B 419      10.036 -21.149  28.170  1.00 42.05           O  
ATOM   3858  CB  LEU B 419      10.713 -21.713  24.952  1.00 43.27           C  
ATOM   3859  CG  LEU B 419      10.028 -23.047  25.276  1.00 41.89           C  
ATOM   3860  CD1 LEU B 419       8.542 -22.836  25.449  1.00 42.37           C  
ATOM   3861  CD2 LEU B 419      10.292 -24.044  24.158  1.00 43.00           C  
ATOM   3862  N   GLN B 420      12.171 -20.789  27.554  1.00 42.12           N  
ATOM   3863  CA  GLN B 420      12.740 -21.073  28.863  1.00 41.13           C  
ATOM   3864  C   GLN B 420      12.139 -20.183  29.943  1.00 42.36           C  
ATOM   3865  O   GLN B 420      11.678 -20.669  30.977  1.00 43.30           O  
ATOM   3866  CB  GLN B 420      14.261 -20.890  28.802  1.00 42.48           C  
ATOM   3867  CG  GLN B 420      15.002 -20.905  30.147  1.00 42.47           C  
ATOM   3868  CD  GLN B 420      14.863 -22.213  30.909  1.00 42.15           C  
ATOM   3869  OE1 GLN B 420      14.697 -23.285  30.313  1.00 41.62           O  
ATOM   3870  NE2 GLN B 420      14.949 -22.133  32.235  1.00 38.85           N  
ATOM   3871  N   LEU B 421      12.143 -18.874  29.709  1.00 42.33           N  
ATOM   3872  CA  LEU B 421      11.582 -17.942  30.680  1.00 41.79           C  
ATOM   3873  C   LEU B 421      10.075 -18.153  30.871  1.00 41.34           C  
ATOM   3874  O   LEU B 421       9.557 -17.983  31.968  1.00 39.82           O  
ATOM   3875  CB  LEU B 421      11.868 -16.497  30.254  1.00 41.19           C  
ATOM   3876  CG  LEU B 421      13.364 -16.163  30.137  1.00 40.28           C  
ATOM   3877  CD1 LEU B 421      13.537 -14.723  29.675  1.00 39.05           C  
ATOM   3878  CD2 LEU B 421      14.056 -16.379  31.490  1.00 36.60           C  
ATOM   3879  N   LYS B 422       9.374 -18.543  29.813  1.00 43.99           N  
ATOM   3880  CA  LYS B 422       7.937 -18.769  29.920  1.00 46.42           C  
ATOM   3881  C   LYS B 422       7.617 -20.035  30.709  1.00 46.76           C  
ATOM   3882  O   LYS B 422       6.631 -20.085  31.449  1.00 47.46           O  
ATOM   3883  CB  LYS B 422       7.303 -18.841  28.528  1.00 48.01           C  
ATOM   3884  CG  LYS B 422       7.385 -17.534  27.774  1.00 49.01           C  
ATOM   3885  CD  LYS B 422       6.370 -17.458  26.652  1.00 50.96           C  
ATOM   3886  CE  LYS B 422       6.245 -16.025  26.141  1.00 50.79           C  
ATOM   3887  NZ  LYS B 422       5.072 -15.833  25.249  1.00 52.57           N  
ATOM   3888  N   LEU B 423       8.452 -21.057  30.552  1.00 47.36           N  
ATOM   3889  CA  LEU B 423       8.238 -22.310  31.262  1.00 46.99           C  
ATOM   3890  C   LEU B 423       8.808 -22.263  32.667  1.00 46.96           C  
ATOM   3891  O   LEU B 423       8.300 -22.922  33.567  1.00 48.22           O  
ATOM   3892  CB  LEU B 423       8.878 -23.473  30.501  1.00 46.62           C  
ATOM   3893  CG  LEU B 423       8.209 -23.904  29.195  1.00 47.65           C  
ATOM   3894  CD1 LEU B 423       8.955 -25.090  28.605  1.00 47.56           C  
ATOM   3895  CD2 LEU B 423       6.755 -24.267  29.459  1.00 48.27           C  
ATOM   3896  N   ASN B 424       9.859 -21.472  32.858  1.00 46.78           N  
ATOM   3897  CA  ASN B 424      10.502 -21.383  34.158  1.00 46.01           C  
ATOM   3898  C   ASN B 424       9.958 -20.271  35.051  1.00 45.66           C  
ATOM   3899  O   ASN B 424      10.144 -20.296  36.265  1.00 45.11           O  
ATOM   3900  CB  ASN B 424      12.020 -21.229  33.965  1.00 46.73           C  
ATOM   3901  CG  ASN B 424      12.795 -21.434  35.252  1.00 47.59           C  
ATOM   3902  OD1 ASN B 424      12.383 -22.217  36.110  1.00 50.30           O  
ATOM   3903  ND2 ASN B 424      13.926 -20.746  35.390  1.00 47.17           N  
ATOM   3904  N   HIS B 425       9.278 -19.298  34.458  1.00 46.18           N  
ATOM   3905  CA  HIS B 425       8.719 -18.190  35.233  1.00 45.88           C  
ATOM   3906  C   HIS B 425       7.347 -17.855  34.674  1.00 48.27           C  
ATOM   3907  O   HIS B 425       7.105 -16.727  34.235  1.00 49.78           O  
ATOM   3908  CB  HIS B 425       9.604 -16.952  35.111  1.00 44.28           C  
ATOM   3909  CG  HIS B 425      11.033 -17.180  35.475  1.00 40.67           C  
ATOM   3910  ND1 HIS B 425      11.505 -17.037  36.760  1.00 41.82           N  
ATOM   3911  CD2 HIS B 425      12.105 -17.503  34.713  1.00 41.02           C  
ATOM   3912  CE1 HIS B 425      12.808 -17.259  36.775  1.00 42.65           C  
ATOM   3913  NE2 HIS B 425      13.196 -17.542  35.545  1.00 40.84           N  
ATOM   3914  N   PRO B 426       6.427 -18.829  34.677  1.00 50.09           N  
ATOM   3915  CA  PRO B 426       5.078 -18.604  34.154  1.00 51.00           C  
ATOM   3916  C   PRO B 426       4.350 -17.409  34.752  1.00 51.67           C  
ATOM   3917  O   PRO B 426       3.467 -16.848  34.119  1.00 53.51           O  
ATOM   3918  CB  PRO B 426       4.369 -19.922  34.455  1.00 51.60           C  
ATOM   3919  CG  PRO B 426       5.071 -20.400  35.699  1.00 51.58           C  
ATOM   3920  CD  PRO B 426       6.512 -20.137  35.348  1.00 50.26           C  
ATOM   3921  N   GLU B 427       4.730 -17.014  35.961  1.00 52.63           N  
ATOM   3922  CA  GLU B 427       4.087 -15.893  36.641  1.00 54.15           C  
ATOM   3923  C   GLU B 427       4.787 -14.559  36.398  1.00 52.58           C  
ATOM   3924  O   GLU B 427       4.313 -13.515  36.845  1.00 53.12           O  
ATOM   3925  CB  GLU B 427       4.044 -16.151  38.152  1.00 55.20           C  
ATOM   3926  CG  GLU B 427       3.586 -17.552  38.548  1.00 61.39           C  
ATOM   3927  CD  GLU B 427       2.150 -17.842  38.157  1.00 64.07           C  
ATOM   3928  OE1 GLU B 427       1.852 -17.873  36.943  1.00 67.31           O  
ATOM   3929  OE2 GLU B 427       1.316 -18.038  39.066  1.00 65.23           O  
ATOM   3930  N   SER B 428       5.915 -14.588  35.697  1.00 51.12           N  
ATOM   3931  CA  SER B 428       6.658 -13.364  35.441  1.00 49.03           C  
ATOM   3932  C   SER B 428       6.375 -12.836  34.042  1.00 47.67           C  
ATOM   3933  O   SER B 428       7.037 -13.212  33.071  1.00 46.69           O  
ATOM   3934  CB  SER B 428       8.154 -13.615  35.616  1.00 49.86           C  
ATOM   3935  OG  SER B 428       8.862 -12.387  35.657  1.00 51.21           O  
ATOM   3936  N   SER B 429       5.389 -11.948  33.956  1.00 46.21           N  
ATOM   3937  CA  SER B 429       4.970 -11.362  32.685  1.00 43.85           C  
ATOM   3938  C   SER B 429       6.039 -10.549  31.976  1.00 42.28           C  
ATOM   3939  O   SER B 429       6.654  -9.653  32.552  1.00 41.89           O  
ATOM   3940  CB  SER B 429       3.731 -10.481  32.896  1.00 45.39           C  
ATOM   3941  OG  SER B 429       3.246  -9.987  31.661  1.00 45.48           O  
ATOM   3942  N   GLN B 430       6.253 -10.876  30.710  1.00 41.28           N  
ATOM   3943  CA  GLN B 430       7.225 -10.172  29.888  1.00 42.32           C  
ATOM   3944  C   GLN B 430       8.662 -10.196  30.408  1.00 40.52           C  
ATOM   3945  O   GLN B 430       9.428  -9.263  30.168  1.00 41.86           O  
ATOM   3946  CB  GLN B 430       6.778  -8.720  29.692  1.00 43.05           C  
ATOM   3947  CG  GLN B 430       7.358  -8.116  28.435  1.00 47.50           C  
ATOM   3948  CD  GLN B 430       7.066  -8.980  27.225  1.00 47.40           C  
ATOM   3949  OE1 GLN B 430       5.945  -8.989  26.723  1.00 46.18           O  
ATOM   3950  NE2 GLN B 430       8.075  -9.746  26.769  1.00 47.82           N  
ATOM   3951  N   LEU B 431       9.030 -11.263  31.109  1.00 38.46           N  
ATOM   3952  CA  LEU B 431      10.382 -11.391  31.639  1.00 37.22           C  
ATOM   3953  C   LEU B 431      11.387 -11.330  30.494  1.00 35.04           C  
ATOM   3954  O   LEU B 431      12.451 -10.721  30.609  1.00 34.52           O  
ATOM   3955  CB  LEU B 431      10.541 -12.716  32.401  1.00 34.50           C  
ATOM   3956  CG  LEU B 431      11.863 -12.857  33.165  1.00 37.39           C  
ATOM   3957  CD1 LEU B 431      12.055 -11.658  34.099  1.00 32.79           C  
ATOM   3958  CD2 LEU B 431      11.868 -14.161  33.959  1.00 35.61           C  
ATOM   3959  N   PHE B 432      11.038 -11.966  29.386  1.00 33.60           N  
ATOM   3960  CA  PHE B 432      11.884 -11.986  28.203  1.00 34.31           C  
ATOM   3961  C   PHE B 432      12.279 -10.558  27.803  1.00 36.25           C  
ATOM   3962  O   PHE B 432      13.473 -10.216  27.684  1.00 33.88           O  
ATOM   3963  CB  PHE B 432      11.107 -12.660  27.072  1.00 34.48           C  
ATOM   3964  CG  PHE B 432      11.889 -12.842  25.801  1.00 36.45           C  
ATOM   3965  CD1 PHE B 432      13.161 -13.401  25.822  1.00 34.39           C  
ATOM   3966  CD2 PHE B 432      11.327 -12.496  24.570  1.00 36.00           C  
ATOM   3967  CE1 PHE B 432      13.870 -13.620  24.639  1.00 33.28           C  
ATOM   3968  CE2 PHE B 432      12.026 -12.710  23.377  1.00 34.80           C  
ATOM   3969  CZ  PHE B 432      13.302 -13.277  23.414  1.00 35.91           C  
ATOM   3970  N   ALA B 433      11.260  -9.726  27.604  1.00 36.34           N  
ATOM   3971  CA  ALA B 433      11.468  -8.342  27.201  1.00 37.35           C  
ATOM   3972  C   ALA B 433      12.275  -7.555  28.225  1.00 35.30           C  
ATOM   3973  O   ALA B 433      13.165  -6.814  27.854  1.00 35.00           O  
ATOM   3974  CB  ALA B 433      10.125  -7.663  26.955  1.00 35.65           C  
ATOM   3975  N   LYS B 434      11.980  -7.717  29.511  1.00 36.82           N  
ATOM   3976  CA  LYS B 434      12.729  -6.972  30.531  1.00 37.07           C  
ATOM   3977  C   LYS B 434      14.217  -7.307  30.521  1.00 36.43           C  
ATOM   3978  O   LYS B 434      15.072  -6.416  30.675  1.00 34.10           O  
ATOM   3979  CB  LYS B 434      12.169  -7.236  31.930  1.00 37.80           C  
ATOM   3980  CG  LYS B 434      10.726  -6.793  32.131  1.00 42.02           C  
ATOM   3981  CD  LYS B 434      10.297  -7.049  33.562  1.00 43.52           C  
ATOM   3982  CE  LYS B 434       8.803  -6.925  33.741  1.00 46.31           C  
ATOM   3983  NZ  LYS B 434       8.466  -6.844  35.197  1.00 51.04           N  
ATOM   3984  N   LEU B 435      14.519  -8.594  30.353  1.00 35.37           N  
ATOM   3985  CA  LEU B 435      15.902  -9.058  30.319  1.00 34.08           C  
ATOM   3986  C   LEU B 435      16.629  -8.457  29.125  1.00 33.61           C  
ATOM   3987  O   LEU B 435      17.758  -7.948  29.251  1.00 33.08           O  
ATOM   3988  CB  LEU B 435      15.943 -10.598  30.255  1.00 33.59           C  
ATOM   3989  CG  LEU B 435      17.305 -11.295  30.112  1.00 31.24           C  
ATOM   3990  CD1 LEU B 435      18.312 -10.731  31.123  1.00 29.91           C  
ATOM   3991  CD2 LEU B 435      17.115 -12.805  30.359  1.00 31.75           C  
ATOM   3992  N   LEU B 436      15.985  -8.502  27.965  1.00 33.63           N  
ATOM   3993  CA  LEU B 436      16.586  -7.948  26.766  1.00 35.59           C  
ATOM   3994  C   LEU B 436      16.885  -6.469  26.931  1.00 36.59           C  
ATOM   3995  O   LEU B 436      17.923  -5.998  26.471  1.00 36.35           O  
ATOM   3996  CB  LEU B 436      15.685  -8.162  25.548  1.00 36.14           C  
ATOM   3997  CG  LEU B 436      15.491  -9.615  25.097  1.00 38.52           C  
ATOM   3998  CD1 LEU B 436      14.596  -9.649  23.877  1.00 35.25           C  
ATOM   3999  CD2 LEU B 436      16.847 -10.266  24.796  1.00 35.03           C  
ATOM   4000  N   GLN B 437      16.005  -5.721  27.586  1.00 37.69           N  
ATOM   4001  CA  GLN B 437      16.304  -4.305  27.736  1.00 41.22           C  
ATOM   4002  C   GLN B 437      17.465  -4.054  28.690  1.00 40.91           C  
ATOM   4003  O   GLN B 437      18.054  -2.974  28.684  1.00 40.08           O  
ATOM   4004  CB  GLN B 437      15.057  -3.492  28.140  1.00 44.95           C  
ATOM   4005  CG  GLN B 437      14.059  -4.165  29.047  1.00 50.04           C  
ATOM   4006  CD  GLN B 437      12.853  -3.272  29.348  1.00 53.25           C  
ATOM   4007  OE1 GLN B 437      12.266  -2.657  28.444  1.00 50.60           O  
ATOM   4008  NE2 GLN B 437      12.473  -3.207  30.623  1.00 55.03           N  
ATOM   4009  N   LYS B 438      17.818  -5.060  29.489  1.00 41.44           N  
ATOM   4010  CA  LYS B 438      18.937  -4.926  30.412  1.00 41.97           C  
ATOM   4011  C   LYS B 438      20.245  -4.847  29.630  1.00 44.19           C  
ATOM   4012  O   LYS B 438      21.268  -4.410  30.161  1.00 43.62           O  
ATOM   4013  CB  LYS B 438      18.989  -6.112  31.377  1.00 41.95           C  
ATOM   4014  CG  LYS B 438      18.684  -5.751  32.825  1.00 44.39           C  
ATOM   4015  CD  LYS B 438      17.314  -5.128  32.968  1.00 43.59           C  
ATOM   4016  CE  LYS B 438      16.963  -4.887  34.429  1.00 43.11           C  
ATOM   4017  NZ  LYS B 438      17.870  -3.881  35.041  1.00 47.99           N  
ATOM   4018  N   MET B 439      20.214  -5.271  28.367  1.00 45.46           N  
ATOM   4019  CA  MET B 439      21.412  -5.224  27.539  1.00 48.46           C  
ATOM   4020  C   MET B 439      21.871  -3.785  27.326  1.00 49.49           C  
ATOM   4021  O   MET B 439      23.056  -3.533  27.105  1.00 50.09           O  
ATOM   4022  CB  MET B 439      21.164  -5.928  26.199  1.00 49.76           C  
ATOM   4023  CG  MET B 439      20.812  -7.413  26.380  1.00 55.39           C  
ATOM   4024  SD  MET B 439      20.753  -8.452  24.889  1.00 61.49           S  
ATOM   4025  CE  MET B 439      19.219  -7.852  24.124  1.00 60.12           C  
ATOM   4026  N   THR B 440      20.940  -2.839  27.424  1.00 51.09           N  
ATOM   4027  CA  THR B 440      21.276  -1.428  27.249  1.00 53.11           C  
ATOM   4028  C   THR B 440      22.040  -0.946  28.477  1.00 53.40           C  
ATOM   4029  O   THR B 440      22.844  -0.017  28.397  1.00 54.89           O  
ATOM   4030  CB  THR B 440      20.014  -0.547  27.068  1.00 53.86           C  
ATOM   4031  OG1 THR B 440      19.433  -0.266  28.346  1.00 56.65           O  
ATOM   4032  CG2 THR B 440      18.983  -1.266  26.212  1.00 51.17           C  
ATOM   4033  N   ASP B 441      21.787  -1.591  29.613  1.00 53.39           N  
ATOM   4034  CA  ASP B 441      22.462  -1.243  30.856  1.00 52.06           C  
ATOM   4035  C   ASP B 441      23.894  -1.773  30.814  1.00 50.45           C  
ATOM   4036  O   ASP B 441      24.834  -1.052  31.151  1.00 48.86           O  
ATOM   4037  CB  ASP B 441      21.729  -1.848  32.051  1.00 55.27           C  
ATOM   4038  CG  ASP B 441      20.244  -1.534  32.047  1.00 59.04           C  
ATOM   4039  OD1 ASP B 441      19.557  -1.923  31.077  1.00 61.49           O  
ATOM   4040  OD2 ASP B 441      19.760  -0.906  33.014  1.00 62.02           O  
ATOM   4041  N   LEU B 442      24.052  -3.033  30.403  1.00 48.25           N  
ATOM   4042  CA  LEU B 442      25.374  -3.657  30.305  1.00 46.60           C  
ATOM   4043  C   LEU B 442      26.299  -2.849  29.412  1.00 45.35           C  
ATOM   4044  O   LEU B 442      27.409  -2.501  29.803  1.00 44.62           O  
ATOM   4045  CB  LEU B 442      25.273  -5.073  29.726  1.00 46.51           C  
ATOM   4046  CG  LEU B 442      24.816  -6.215  30.629  1.00 48.19           C  
ATOM   4047  CD1 LEU B 442      24.569  -7.448  29.781  1.00 46.46           C  
ATOM   4048  CD2 LEU B 442      25.869  -6.482  31.701  1.00 46.54           C  
ATOM   4049  N   ARG B 443      25.821  -2.580  28.201  1.00 45.36           N  
ATOM   4050  CA  ARG B 443      26.547  -1.823  27.189  1.00 47.04           C  
ATOM   4051  C   ARG B 443      27.118  -0.535  27.764  1.00 47.24           C  
ATOM   4052  O   ARG B 443      28.261  -0.166  27.486  1.00 46.90           O  
ATOM   4053  CB  ARG B 443      25.605  -1.492  26.030  1.00 46.32           C  
ATOM   4054  CG  ARG B 443      26.069  -1.971  24.675  1.00 48.43           C  
ATOM   4055  CD  ARG B 443      25.846  -3.463  24.463  1.00 49.68           C  
ATOM   4056  NE  ARG B 443      25.916  -3.795  23.039  1.00 50.23           N  
ATOM   4057  CZ  ARG B 443      25.683  -5.001  22.527  1.00 53.42           C  
ATOM   4058  NH1 ARG B 443      25.361  -6.021  23.320  1.00 54.16           N  
ATOM   4059  NH2 ARG B 443      25.765  -5.185  21.215  1.00 52.56           N  
ATOM   4060  N   GLN B 444      26.309   0.156  28.558  1.00 49.04           N  
ATOM   4061  CA  GLN B 444      26.748   1.395  29.180  1.00 51.23           C  
ATOM   4062  C   GLN B 444      27.832   1.104  30.210  1.00 51.51           C  
ATOM   4063  O   GLN B 444      28.847   1.800  30.265  1.00 50.43           O  
ATOM   4064  CB  GLN B 444      25.566   2.106  29.842  1.00 53.00           C  
ATOM   4065  CG  GLN B 444      24.799   3.020  28.901  1.00 56.08           C  
ATOM   4066  CD  GLN B 444      25.605   4.246  28.482  1.00 58.78           C  
ATOM   4067  OE1 GLN B 444      25.171   5.025  27.624  1.00 60.88           O  
ATOM   4068  NE2 GLN B 444      26.778   4.427  29.092  1.00 56.86           N  
ATOM   4069  N   ILE B 445      27.603   0.079  31.030  1.00 52.11           N  
ATOM   4070  CA  ILE B 445      28.562  -0.330  32.054  1.00 52.30           C  
ATOM   4071  C   ILE B 445      29.898  -0.603  31.391  1.00 50.52           C  
ATOM   4072  O   ILE B 445      30.922  -0.063  31.794  1.00 51.28           O  
ATOM   4073  CB  ILE B 445      28.132  -1.638  32.767  1.00 53.98           C  
ATOM   4074  CG1 ILE B 445      26.747  -1.478  33.384  1.00 54.68           C  
ATOM   4075  CG2 ILE B 445      29.128  -1.985  33.862  1.00 55.71           C  
ATOM   4076  CD1 ILE B 445      26.686  -0.436  34.480  1.00 58.88           C  
ATOM   4077  N   VAL B 446      29.879  -1.441  30.359  1.00 49.24           N  
ATOM   4078  CA  VAL B 446      31.101  -1.797  29.650  1.00 48.85           C  
ATOM   4079  C   VAL B 446      31.801  -0.578  29.061  1.00 49.37           C  
ATOM   4080  O   VAL B 446      33.002  -0.401  29.240  1.00 49.15           O  
ATOM   4081  CB  VAL B 446      30.813  -2.799  28.529  1.00 47.23           C  
ATOM   4082  CG1 VAL B 446      32.095  -3.154  27.809  1.00 45.67           C  
ATOM   4083  CG2 VAL B 446      30.167  -4.043  29.112  1.00 47.70           C  
ATOM   4084  N   THR B 447      31.051   0.256  28.351  1.00 51.19           N  
ATOM   4085  CA  THR B 447      31.623   1.460  27.755  1.00 53.58           C  
ATOM   4086  C   THR B 447      32.300   2.276  28.853  1.00 54.65           C  
ATOM   4087  O   THR B 447      33.471   2.641  28.752  1.00 54.47           O  
ATOM   4088  CB  THR B 447      30.537   2.330  27.102  1.00 53.74           C  
ATOM   4089  OG1 THR B 447      29.917   1.605  26.033  1.00 54.21           O  
ATOM   4090  CG2 THR B 447      31.144   3.614  26.559  1.00 55.04           C  
ATOM   4091  N   GLU B 448      31.542   2.542  29.906  1.00 55.83           N  
ATOM   4092  CA  GLU B 448      32.019   3.299  31.052  1.00 57.38           C  
ATOM   4093  C   GLU B 448      33.230   2.604  31.687  1.00 57.38           C  
ATOM   4094  O   GLU B 448      34.084   3.253  32.294  1.00 57.39           O  
ATOM   4095  CB  GLU B 448      30.879   3.423  32.071  1.00 57.86           C  
ATOM   4096  CG  GLU B 448      31.141   4.346  33.246  1.00 58.90           C  
ATOM   4097  CD  GLU B 448      29.954   4.415  34.197  1.00 60.20           C  
ATOM   4098  OE1 GLU B 448      29.615   3.377  34.810  1.00 59.09           O  
ATOM   4099  OE2 GLU B 448      29.357   5.507  34.325  1.00 61.65           O  
ATOM   4100  N   HIS B 449      33.305   1.285  31.538  1.00 57.63           N  
ATOM   4101  CA  HIS B 449      34.411   0.515  32.111  1.00 58.39           C  
ATOM   4102  C   HIS B 449      35.751   0.786  31.412  1.00 58.14           C  
ATOM   4103  O   HIS B 449      36.772   0.991  32.074  1.00 56.93           O  
ATOM   4104  CB  HIS B 449      34.091  -0.988  32.064  1.00 57.84           C  
ATOM   4105  CG  HIS B 449      35.147  -1.854  32.683  1.00 59.66           C  
ATOM   4106  ND1 HIS B 449      35.702  -2.934  32.030  1.00 60.27           N  
ATOM   4107  CD2 HIS B 449      35.743  -1.803  33.898  1.00 60.06           C  
ATOM   4108  CE1 HIS B 449      36.595  -3.511  32.814  1.00 59.98           C  
ATOM   4109  NE2 HIS B 449      36.639  -2.845  33.954  1.00 60.84           N  
ATOM   4110  N   VAL B 450      35.753   0.782  30.082  1.00 58.16           N  
ATOM   4111  CA  VAL B 450      36.986   1.030  29.344  1.00 60.04           C  
ATOM   4112  C   VAL B 450      37.455   2.462  29.596  1.00 61.21           C  
ATOM   4113  O   VAL B 450      38.639   2.781  29.453  1.00 60.61           O  
ATOM   4114  CB  VAL B 450      36.792   0.815  27.826  1.00 59.74           C  
ATOM   4115  CG1 VAL B 450      36.213  -0.560  27.574  1.00 59.35           C  
ATOM   4116  CG2 VAL B 450      35.895   1.891  27.248  1.00 61.75           C  
ATOM   4117  N   GLN B 451      36.515   3.317  29.981  1.00 62.38           N  
ATOM   4118  CA  GLN B 451      36.816   4.712  30.266  1.00 64.57           C  
ATOM   4119  C   GLN B 451      37.732   4.788  31.482  1.00 64.51           C  
ATOM   4120  O   GLN B 451      38.792   5.407  31.431  1.00 65.11           O  
ATOM   4121  CB  GLN B 451      35.529   5.487  30.557  1.00 66.40           C  
ATOM   4122  CG  GLN B 451      35.682   6.998  30.475  1.00 68.75           C  
ATOM   4123  CD  GLN B 451      34.779   7.728  31.456  1.00 70.69           C  
ATOM   4124  OE1 GLN B 451      35.068   7.790  32.653  1.00 71.11           O  
ATOM   4125  NE2 GLN B 451      33.673   8.274  30.956  1.00 70.48           N  
ATOM   4126  N   LEU B 452      37.316   4.167  32.582  1.00 64.56           N  
ATOM   4127  CA  LEU B 452      38.124   4.175  33.794  1.00 65.49           C  
ATOM   4128  C   LEU B 452      39.417   3.406  33.537  1.00 66.08           C  
ATOM   4129  O   LEU B 452      40.453   3.672  34.147  1.00 66.24           O  
ATOM   4130  CB  LEU B 452      37.359   3.534  34.958  1.00 66.10           C  
ATOM   4131  CG  LEU B 452      36.181   4.305  35.570  1.00 66.56           C  
ATOM   4132  CD1 LEU B 452      35.499   3.438  36.617  1.00 66.54           C  
ATOM   4133  CD2 LEU B 452      36.668   5.601  36.199  1.00 66.08           C  
ATOM   4134  N   LEU B 453      39.347   2.455  32.618  1.00 65.84           N  
ATOM   4135  CA  LEU B 453      40.501   1.645  32.282  1.00 67.14           C  
ATOM   4136  C   LEU B 453      41.566   2.493  31.593  1.00 68.29           C  
ATOM   4137  O   LEU B 453      42.754   2.387  31.899  1.00 68.17           O  
ATOM   4138  CB  LEU B 453      40.073   0.505  31.366  1.00 67.00           C  
ATOM   4139  CG  LEU B 453      41.028  -0.675  31.268  1.00 66.67           C  
ATOM   4140  CD1 LEU B 453      41.029  -1.426  32.589  1.00 67.49           C  
ATOM   4141  CD2 LEU B 453      40.583  -1.588  30.138  1.00 68.42           C  
ATOM   4142  N   GLN B 454      41.136   3.336  30.659  1.00 69.42           N  
ATOM   4143  CA  GLN B 454      42.069   4.193  29.935  1.00 70.72           C  
ATOM   4144  C   GLN B 454      42.770   5.122  30.922  1.00 70.26           C  
ATOM   4145  O   GLN B 454      43.917   5.514  30.714  1.00 69.72           O  
ATOM   4146  CB  GLN B 454      41.336   5.023  28.868  1.00 71.63           C  
ATOM   4147  CG  GLN B 454      40.617   6.264  29.400  1.00 73.14           C  
ATOM   4148  CD  GLN B 454      40.050   7.140  28.292  1.00 73.62           C  
ATOM   4149  OE1 GLN B 454      39.076   6.777  27.626  1.00 74.32           O  
ATOM   4150  NE2 GLN B 454      40.669   8.299  28.083  1.00 73.70           N  
ATOM   4151  N   VAL B 455      42.064   5.466  31.996  1.00 70.69           N  
ATOM   4152  CA  VAL B 455      42.599   6.343  33.033  1.00 71.51           C  
ATOM   4153  C   VAL B 455      43.667   5.632  33.861  1.00 72.50           C  
ATOM   4154  O   VAL B 455      44.709   6.213  34.174  1.00 73.02           O  
ATOM   4155  CB  VAL B 455      41.483   6.832  33.980  1.00 70.63           C  
ATOM   4156  CG1 VAL B 455      42.078   7.708  35.077  1.00 69.88           C  
ATOM   4157  CG2 VAL B 455      40.429   7.600  33.189  1.00 70.00           C  
ATOM   4158  N   ILE B 456      43.404   4.378  34.223  1.00 73.04           N  
ATOM   4159  CA  ILE B 456      44.363   3.602  35.001  1.00 73.38           C  
ATOM   4160  C   ILE B 456      45.665   3.549  34.205  1.00 74.52           C  
ATOM   4161  O   ILE B 456      46.752   3.658  34.765  1.00 75.14           O  
ATOM   4162  CB  ILE B 456      43.859   2.158  35.254  1.00 72.80           C  
ATOM   4163  CG1 ILE B 456      42.509   2.195  35.971  1.00 72.41           C  
ATOM   4164  CG2 ILE B 456      44.865   1.392  36.108  1.00 72.48           C  
ATOM   4165  CD1 ILE B 456      41.899   0.828  36.199  1.00 71.68           C  
ATOM   4166  N   LYS B 457      45.544   3.381  32.892  1.00 75.66           N  
ATOM   4167  CA  LYS B 457      46.706   3.337  32.015  1.00 76.52           C  
ATOM   4168  C   LYS B 457      47.571   4.565  32.290  1.00 77.47           C  
ATOM   4169  O   LYS B 457      48.797   4.477  32.340  1.00 77.67           O  
ATOM   4170  CB  LYS B 457      46.250   3.328  30.552  1.00 76.26           C  
ATOM   4171  CG  LYS B 457      47.330   3.678  29.526  1.00 77.08           C  
ATOM   4172  CD  LYS B 457      48.463   2.659  29.493  1.00 77.13           C  
ATOM   4173  CE  LYS B 457      49.496   3.007  28.419  1.00 76.08           C  
ATOM   4174  NZ  LYS B 457      50.150   4.336  28.633  1.00 74.85           N  
ATOM   4175  N   LYS B 458      46.915   5.706  32.478  1.00 78.56           N  
ATOM   4176  CA  LYS B 458      47.606   6.963  32.750  1.00 79.55           C  
ATOM   4177  C   LYS B 458      47.816   7.121  34.253  1.00 80.42           C  
ATOM   4178  O   LYS B 458      47.808   8.232  34.790  1.00 80.64           O  
ATOM   4179  CB  LYS B 458      46.785   8.134  32.205  1.00 79.07           C  
ATOM   4180  CG  LYS B 458      46.326   7.942  30.760  1.00 78.41           C  
ATOM   4181  CD  LYS B 458      45.660   9.196  30.203  1.00 78.26           C  
ATOM   4182  CE  LYS B 458      44.431   9.589  31.004  1.00 77.96           C  
ATOM   4183  NZ  LYS B 458      43.857  10.875  30.523  1.00 78.52           N  
ATOM   4184  N   THR B 459      47.997   5.988  34.924  1.00 81.43           N  
ATOM   4185  CA  THR B 459      48.214   5.952  36.365  1.00 82.30           C  
ATOM   4186  C   THR B 459      49.437   5.074  36.640  1.00 82.87           C  
ATOM   4187  O   THR B 459      50.299   5.419  37.444  1.00 83.33           O  
ATOM   4188  CB  THR B 459      46.984   5.354  37.093  1.00 82.59           C  
ATOM   4189  OG1 THR B 459      45.788   5.974  36.600  1.00 82.85           O  
ATOM   4190  CG2 THR B 459      47.077   5.590  38.594  1.00 82.21           C  
ATOM   4191  N   GLU B 460      49.499   3.937  35.955  1.00 83.94           N  
ATOM   4192  CA  GLU B 460      50.601   2.992  36.095  1.00 85.02           C  
ATOM   4193  C   GLU B 460      51.079   2.603  34.693  1.00 85.91           C  
ATOM   4194  O   GLU B 460      50.291   2.116  33.875  1.00 86.07           O  
ATOM   4195  CB  GLU B 460      50.122   1.752  36.864  1.00 85.30           C  
ATOM   4196  CG  GLU B 460      51.192   0.699  37.111  1.00 85.75           C  
ATOM   4197  CD  GLU B 460      51.045  -0.513  36.207  1.00 86.52           C  
ATOM   4198  OE1 GLU B 460      51.088  -0.348  34.966  1.00 86.20           O  
ATOM   4199  OE2 GLU B 460      50.886  -1.632  36.743  1.00 86.77           O  
ATOM   4200  N   THR B 461      52.363   2.824  34.412  1.00 86.09           N  
ATOM   4201  CA  THR B 461      52.908   2.503  33.093  1.00 86.27           C  
ATOM   4202  C   THR B 461      54.393   2.144  33.045  1.00 86.52           C  
ATOM   4203  O   THR B 461      54.753   0.995  32.779  1.00 87.02           O  
ATOM   4204  CB  THR B 461      52.671   3.668  32.102  1.00 86.03           C  
ATOM   4205  OG1 THR B 461      52.630   4.910  32.820  1.00 86.17           O  
ATOM   4206  CG2 THR B 461      51.374   3.466  31.337  1.00 84.75           C  
ATOM   4207  N   ASP B 462      55.241   3.140  33.294  1.00 86.65           N  
ATOM   4208  CA  ASP B 462      56.700   2.993  33.261  1.00 86.62           C  
ATOM   4209  C   ASP B 462      57.294   1.842  34.085  1.00 87.02           C  
ATOM   4210  O   ASP B 462      56.578   0.974  34.595  1.00 87.13           O  
ATOM   4211  CB  ASP B 462      57.353   4.307  33.709  1.00 85.51           C  
ATOM   4212  CG  ASP B 462      58.453   4.766  32.773  1.00 84.24           C  
ATOM   4213  OD1 ASP B 462      59.367   3.968  32.478  1.00 84.72           O  
ATOM   4214  OD2 ASP B 462      58.405   5.934  32.337  1.00 82.91           O  
ATOM   4215  N   MET B 463      58.621   1.864  34.199  1.00 87.46           N  
ATOM   4216  CA  MET B 463      59.399   0.869  34.939  1.00 88.05           C  
ATOM   4217  C   MET B 463      59.565  -0.445  34.184  1.00 87.49           C  
ATOM   4218  O   MET B 463      58.587  -1.039  33.721  1.00 87.85           O  
ATOM   4219  CB  MET B 463      58.775   0.600  36.314  1.00 89.57           C  
ATOM   4220  CG  MET B 463      59.629  -0.294  37.200  1.00 91.15           C  
ATOM   4221  SD  MET B 463      61.340   0.282  37.276  1.00 94.13           S  
ATOM   4222  CE  MET B 463      61.223   1.538  38.567  1.00 92.75           C  
ATOM   4223  N   SER B 464      60.813  -0.894  34.069  1.00 86.94           N  
ATOM   4224  CA  SER B 464      61.135  -2.137  33.369  1.00 85.92           C  
ATOM   4225  C   SER B 464      60.626  -3.360  34.129  1.00 85.65           C  
ATOM   4226  O   SER B 464      60.933  -4.500  33.773  1.00 85.60           O  
ATOM   4227  CB  SER B 464      62.649  -2.252  33.164  1.00 85.45           C  
ATOM   4228  OG  SER B 464      62.973  -3.415  32.422  1.00 84.58           O  
ATOM   4229  N   LEU B 465      59.852  -3.114  35.181  1.00 85.17           N  
ATOM   4230  CA  LEU B 465      59.285  -4.189  35.983  1.00 83.97           C  
ATOM   4231  C   LEU B 465      57.863  -4.455  35.489  1.00 83.13           C  
ATOM   4232  O   LEU B 465      57.173  -3.533  35.043  1.00 82.99           O  
ATOM   4233  CB  LEU B 465      59.267  -3.800  37.466  1.00 83.38           C  
ATOM   4234  CG  LEU B 465      58.885  -4.913  38.449  1.00 83.75           C  
ATOM   4235  CD1 LEU B 465      59.907  -6.046  38.371  1.00 83.03           C  
ATOM   4236  CD2 LEU B 465      58.820  -4.350  39.861  1.00 83.03           C  
ATOM   4237  N   HIS B 466      57.448  -5.721  35.562  1.00 81.96           N  
ATOM   4238  CA  HIS B 466      56.125  -6.177  35.126  1.00 80.01           C  
ATOM   4239  C   HIS B 466      56.078  -6.598  33.649  1.00 78.93           C  
ATOM   4240  O   HIS B 466      55.005  -6.913  33.130  1.00 78.74           O  
ATOM   4241  CB  HIS B 466      55.066  -5.091  35.364  1.00 80.15           C  
ATOM   4242  CG  HIS B 466      53.780  -5.608  35.933  1.00 80.13           C  
ATOM   4243  ND1 HIS B 466      52.574  -4.966  35.746  1.00 79.93           N  
ATOM   4244  CD2 HIS B 466      53.517  -6.680  36.717  1.00 79.85           C  
ATOM   4245  CE1 HIS B 466      51.624  -5.621  36.391  1.00 80.13           C  
ATOM   4246  NE2 HIS B 466      52.170  -6.665  36.989  1.00 80.01           N  
ATOM   4247  N   PRO B 467      57.230  -6.609  32.947  1.00 77.82           N  
ATOM   4248  CA  PRO B 467      57.135  -7.015  31.542  1.00 76.79           C  
ATOM   4249  C   PRO B 467      56.678  -8.465  31.430  1.00 76.26           C  
ATOM   4250  O   PRO B 467      56.766  -9.224  32.397  1.00 76.76           O  
ATOM   4251  CB  PRO B 467      58.554  -6.798  31.028  1.00 76.07           C  
ATOM   4252  CG  PRO B 467      59.382  -7.123  32.218  1.00 76.53           C  
ATOM   4253  CD  PRO B 467      58.642  -6.421  33.333  1.00 77.64           C  
ATOM   4254  N   LEU B 468      56.182  -8.840  30.255  1.00 75.08           N  
ATOM   4255  CA  LEU B 468      55.689 -10.195  30.021  1.00 74.44           C  
ATOM   4256  C   LEU B 468      54.379 -10.365  30.790  1.00 73.79           C  
ATOM   4257  O   LEU B 468      53.489 -11.106  30.372  1.00 73.13           O  
ATOM   4258  CB  LEU B 468      56.725 -11.232  30.480  1.00 74.11           C  
ATOM   4259  CG  LEU B 468      56.537 -12.690  30.044  1.00 73.45           C  
ATOM   4260  CD1 LEU B 468      56.394 -12.764  28.533  1.00 72.34           C  
ATOM   4261  CD2 LEU B 468      57.734 -13.518  30.504  1.00 73.04           C  
ATOM   4262  N   LEU B 469      54.273  -9.669  31.918  1.00 73.54           N  
ATOM   4263  CA  LEU B 469      53.066  -9.706  32.734  1.00 74.25           C  
ATOM   4264  C   LEU B 469      52.071  -8.780  32.037  1.00 74.62           C  
ATOM   4265  O   LEU B 469      50.876  -9.064  31.961  1.00 74.73           O  
ATOM   4266  CB  LEU B 469      53.368  -9.199  34.146  1.00 74.47           C  
ATOM   4267  CG  LEU B 469      52.352  -9.532  35.242  1.00 74.87           C  
ATOM   4268  CD1 LEU B 469      51.030  -8.818  34.980  1.00 75.11           C  
ATOM   4269  CD2 LEU B 469      52.155 -11.040  35.293  1.00 74.45           C  
ATOM   4270  N   GLN B 470      52.585  -7.665  31.526  1.00 75.15           N  
ATOM   4271  CA  GLN B 470      51.768  -6.706  30.797  1.00 75.76           C  
ATOM   4272  C   GLN B 470      51.240  -7.420  29.556  1.00 75.70           C  
ATOM   4273  O   GLN B 470      50.187  -7.076  29.018  1.00 75.74           O  
ATOM   4274  CB  GLN B 470      52.618  -5.502  30.389  1.00 76.12           C  
ATOM   4275  CG  GLN B 470      51.963  -4.594  29.358  1.00 78.49           C  
ATOM   4276  CD  GLN B 470      52.843  -3.414  28.981  1.00 79.91           C  
ATOM   4277  OE1 GLN B 470      52.548  -2.680  28.035  1.00 80.78           O  
ATOM   4278  NE2 GLN B 470      53.929  -3.223  29.727  1.00 80.22           N  
ATOM   4279  N   GLU B 471      51.994  -8.419  29.108  1.00 75.52           N  
ATOM   4280  CA  GLU B 471      51.620  -9.215  27.948  1.00 74.76           C  
ATOM   4281  C   GLU B 471      50.372 -10.010  28.300  1.00 74.72           C  
ATOM   4282  O   GLU B 471      49.327  -9.879  27.660  1.00 75.28           O  
ATOM   4283  CB  GLU B 471      52.749 -10.190  27.587  1.00 73.88           C  
ATOM   4284  CG  GLU B 471      53.498  -9.860  26.308  1.00 72.43           C  
ATOM   4285  CD  GLU B 471      54.085  -8.470  26.326  1.00 71.19           C  
ATOM   4286  OE1 GLU B 471      54.831  -8.160  27.275  1.00 71.57           O  
ATOM   4287  OE2 GLU B 471      53.803  -7.687  25.394  1.00 71.42           O  
ATOM   4288  N   ILE B 472      50.497 -10.832  29.336  1.00 74.88           N  
ATOM   4289  CA  ILE B 472      49.404 -11.679  29.790  1.00 75.26           C  
ATOM   4290  C   ILE B 472      48.105 -10.901  29.960  1.00 75.71           C  
ATOM   4291  O   ILE B 472      47.019 -11.475  29.871  1.00 75.42           O  
ATOM   4292  CB  ILE B 472      49.753 -12.372  31.135  1.00 74.01           C  
ATOM   4293  CG1 ILE B 472      51.126 -13.044  31.038  1.00 72.31           C  
ATOM   4294  CG2 ILE B 472      48.698 -13.422  31.467  1.00 74.36           C  
ATOM   4295  CD1 ILE B 472      51.573 -13.720  32.313  1.00 69.33           C  
ATOM   4296  N   TYR B 473      48.218  -9.596  30.192  1.00 77.05           N  
ATOM   4297  CA  TYR B 473      47.035  -8.763  30.388  1.00 78.69           C  
ATOM   4298  C   TYR B 473      46.740  -7.755  29.273  1.00 79.82           C  
ATOM   4299  O   TYR B 473      45.742  -7.892  28.559  1.00 80.04           O  
ATOM   4300  CB  TYR B 473      47.139  -8.039  31.730  1.00 77.92           C  
ATOM   4301  CG  TYR B 473      47.190  -8.982  32.912  1.00 78.04           C  
ATOM   4302  CD1 TYR B 473      48.273  -9.840  33.099  1.00 78.26           C  
ATOM   4303  CD2 TYR B 473      46.152  -9.025  33.837  1.00 78.11           C  
ATOM   4304  CE1 TYR B 473      48.320 -10.717  34.182  1.00 78.73           C  
ATOM   4305  CE2 TYR B 473      46.188  -9.897  34.922  1.00 78.63           C  
ATOM   4306  CZ  TYR B 473      47.274 -10.739  35.090  1.00 78.62           C  
ATOM   4307  OH  TYR B 473      47.313 -11.594  36.169  1.00 78.97           O  
ATOM   4308  N   LYS B 474      47.601  -6.751  29.123  1.00 80.95           N  
ATOM   4309  CA  LYS B 474      47.408  -5.721  28.100  1.00 81.84           C  
ATOM   4310  C   LYS B 474      46.185  -4.868  28.436  1.00 83.15           C  
ATOM   4311  O   LYS B 474      46.304  -3.804  29.052  1.00 82.84           O  
ATOM   4312  CB  LYS B 474      47.220  -6.363  26.721  1.00 80.75           C  
ATOM   4313  CG  LYS B 474      48.507  -6.733  26.015  1.00 79.58           C  
ATOM   4314  CD  LYS B 474      49.253  -5.490  25.571  1.00 79.42           C  
ATOM   4315  CE  LYS B 474      50.372  -5.850  24.616  1.00 80.06           C  
ATOM   4316  NZ  LYS B 474      49.851  -6.601  23.435  1.00 80.78           N  
ATOM   4317  N   ASP B 475      45.012  -5.341  28.026  1.00 84.69           N  
ATOM   4318  CA  ASP B 475      43.762  -4.637  28.290  1.00 86.18           C  
ATOM   4319  C   ASP B 475      42.611  -5.622  28.410  1.00 86.38           C  
ATOM   4320  O   ASP B 475      41.571  -5.303  28.990  1.00 87.31           O  
ATOM   4321  CB  ASP B 475      43.461  -3.624  27.175  1.00 87.13           C  
ATOM   4322  CG  ASP B 475      44.367  -2.402  27.232  1.00 88.47           C  
ATOM   4323  OD1 ASP B 475      44.422  -1.749  28.298  1.00 89.76           O  
ATOM   4324  OD2 ASP B 475      45.020  -2.090  26.212  1.00 88.44           O  
ATOM   4325  N   LEU B 476      42.804  -6.819  27.863  1.00 86.26           N  
ATOM   4326  CA  LEU B 476      41.783  -7.861  27.900  1.00 86.03           C  
ATOM   4327  C   LEU B 476      40.601  -7.496  27.001  1.00 85.80           C  
ATOM   4328  O   LEU B 476      40.263  -8.306  26.110  1.00 86.68           O  
ATOM   4329  CB  LEU B 476      41.293  -8.076  29.337  1.00 84.94           C  
ATOM   4330  CG  LEU B 476      40.364  -9.267  29.565  1.00 84.57           C  
ATOM   4331  CD1 LEU B 476      41.107 -10.552  29.236  1.00 83.08           C  
ATOM   4332  CD2 LEU B 476      39.883  -9.276  31.009  1.00 84.24           C  
ATOM   4333  OXT LEU B 476      40.026  -6.406  27.199  0.00 85.63           O  
TER    4334      LEU B 476                                                      
HETATM 4335  CAB DRH A 999      19.957  20.967  17.201  1.00 67.53           C  
HETATM 4336  CAO DRH A 999      19.055  19.969  17.936  1.00 69.01           C  
HETATM 4337  CBG DRH A 999      19.809  18.716  18.392  1.00 70.28           C  
HETATM 4338  CAZ DRH A 999      18.936  17.933  19.380  1.00 70.13           C  
HETATM 4339  OAE DRH A 999      19.404  17.692  20.503  1.00 70.14           O  
HETATM 4340  OAD DRH A 999      17.779  17.612  18.995  1.00 70.62           O  
HETATM 4341  CAC DRH A 999      21.094  19.113  19.123  1.00 70.18           C  
HETATM 4342  OAX DRH A 999      20.217  17.938  17.256  1.00 71.42           O  
HETATM 4343  CBB DRH A 999      19.390  17.184  16.465  1.00 72.12           C  
HETATM 4344  CAK DRH A 999      18.343  16.441  16.985  1.00 71.52           C  
HETATM 4345  CAI DRH A 999      17.564  15.626  16.151  1.00 71.23           C  
HETATM 4346  CAJ DRH A 999      19.649  17.136  15.104  1.00 72.50           C  
HETATM 4347  CAH DRH A 999      18.873  16.323  14.266  1.00 72.47           C  
HETATM 4348  CBA DRH A 999      17.835  15.578  14.793  1.00 71.73           C  
HETATM 4349  CAT DRH A 999      17.037  14.642  13.865  1.00 71.80           C  
HETATM 4350  CAV DRH A 999      15.521  14.704  14.044  1.00 70.61           C  
HETATM 4351  NBF DRH A 999      14.850  15.834  13.370  1.00 71.25           N  
HETATM 4352  CAU DRH A 999      13.390  15.775  13.208  1.00 68.15           C  
HETATM 4353  CAS DRH A 999      12.702  15.156  14.428  1.00 67.24           C  
HETATM 4354  CAR DRH A 999      11.242  14.835  14.119  1.00 63.88           C  
HETATM 4355  CAQ DRH A 999      10.597  14.302  15.400  1.00 64.40           C  
HETATM 4356  CAP DRH A 999       9.161  13.824  15.188  1.00 64.56           C  
HETATM 4357  CAN DRH A 999       8.548  13.421  16.527  1.00 65.02           C  
HETATM 4358  CAA DRH A 999       9.418  12.389  17.258  1.00 65.22           C  
HETATM 4359  CBC DRH A 999      15.470  16.713  12.587  1.00 71.98           C  
HETATM 4360  OAY DRH A 999      16.754  16.614  12.114  1.00 72.29           O  
HETATM 4361  CBE DRH A 999      16.890  17.619  11.197  1.00 71.78           C  
HETATM 4362  CAM DRH A 999      17.928  17.998  10.362  1.00 72.18           C  
HETATM 4363  CAG DRH A 999      17.764  19.065   9.483  1.00 72.52           C  
HETATM 4364  CAF DRH A 999      16.551  19.759   9.443  1.00 72.25           C  
HETATM 4365  CAL DRH A 999      15.513  19.378  10.280  1.00 72.67           C  
HETATM 4366  CBD DRH A 999      15.676  18.310  11.155  1.00 72.57           C  
HETATM 4367  NAW DRH A 999      14.844  17.731  12.015  1.00 72.66           N  
HETATM 4368  O   HOH A   1      21.163  20.329  21.937  1.00 75.08           O  
HETATM 4369  O   HOH A   2      16.221  12.977  25.993  1.00 40.96           O  
HETATM 4370  O   HOH A   3      17.434  10.682  25.663  1.00 51.55           O  
HETATM 4371  O   HOH A   4      19.026   8.141  26.771  1.00 49.13           O  
HETATM 4372  O   HOH A   7      11.071 -11.810  19.966  1.00 41.83           O  
HETATM 4373  O   HOH A   8      -0.155  12.470  -2.080  1.00 38.71           O  
HETATM 4374  O   HOH A  10      -2.022   9.346  30.275  1.00 34.87           O  
HETATM 4375  O   HOH A  12      -0.727  -0.055  16.849  1.00 41.89           O  
HETATM 4376  O   HOH A  14      12.802  15.409  -5.761  1.00 37.61           O  
HETATM 4377  O   HOH A  15       3.457   8.867  -4.678  1.00 85.08           O  
HETATM 4378  O   HOH A  16      -0.589   5.358  36.239  1.00 39.81           O  
HETATM 4379  O   HOH A  18      15.030  17.704  14.939  1.00 84.16           O  
HETATM 4380  O   HOH A  19      11.459   7.633  29.692  1.00 38.00           O  
HETATM 4381  O   HOH A  20       3.882   4.641   1.975  1.00 40.92           O  
HETATM 4382  O   HOH A  25      11.983   3.014  10.588  1.00 38.13           O  
HETATM 4383  O   HOH A  26      11.867   0.068  10.587  1.00 36.23           O  
HETATM 4384  O   HOH A  27      11.220   3.473   1.792  1.00 58.27           O  
HETATM 4385  O   HOH A  30       7.507 -12.910  25.400  1.00 62.40           O  
HETATM 4386  O   HOH A  32       3.301   3.080   8.282  1.00 35.76           O  
HETATM 4387  O   HOH A  34      11.502   4.855  12.570  1.00 34.91           O  
HETATM 4388  O   HOH A  35       7.789   7.743  12.422  1.00 37.57           O  
HETATM 4389  O   HOH A  36      17.546   0.060   5.503  1.00 50.40           O  
HETATM 4390  O   HOH A  38      18.432   2.806  28.560  1.00 54.08           O  
HETATM 4391  O   HOH A  43      -6.894  -1.826  26.338  1.00 46.38           O  
HETATM 4392  O   HOH A  47       5.241   6.704  39.192  1.00 43.67           O  
HETATM 4393  O   HOH A  53      -3.839  17.840  28.146  1.00 47.20           O  
HETATM 4394  O   HOH A  54      11.157  11.566  39.196  1.00 46.43           O  
HETATM 4395  O   HOH A  56      -9.052   5.409  24.402  1.00 58.65           O  
HETATM 4396  O   HOH A  60       8.194  -7.660   7.037  1.00 74.80           O  
HETATM 4397  O   HOH A  62       6.539  13.858  12.429  1.00 41.51           O  
HETATM 4398  O   HOH A  63       1.858   5.881  -6.801  1.00 46.98           O  
HETATM 4399  O   HOH A  64      18.539  20.456  -6.449  1.00 42.33           O  
HETATM 4400  O   HOH A  65      11.818   0.656   6.725  1.00 41.08           O  
HETATM 4401  O   HOH A  69       7.715  10.135  11.229  1.00 53.23           O  
HETATM 4402  O   HOH A  71       3.720  -3.697   6.993  1.00 59.01           O  
HETATM 4403  O   HOH A  73      24.296  11.101   0.074  1.00 45.10           O  
HETATM 4404  O   HOH A  75      -6.027  -6.694  14.753  1.00 59.59           O  
HETATM 4405  O   HOH A  76      25.612  15.984  10.216  1.00 56.75           O  
HETATM 4406  O   HOH A  78      30.432  24.084   7.168  1.00 63.11           O  
HETATM 4407  O   HOH A  79      -3.276  16.504  18.362  1.00 79.16           O  
HETATM 4408  O   HOH A  80      16.572   3.298   4.576  1.00 40.54           O  
HETATM 4409  O   HOH A  81       7.012  16.314  -0.540  1.00 47.66           O  
HETATM 4410  O   HOH A  83       0.900   1.686  10.126  1.00 41.64           O  
HETATM 4411  O   HOH A  85      29.377  11.412  31.625  1.00 75.97           O  
HETATM 4412  O   HOH A  86       7.733  25.561   4.311  1.00 62.71           O  
HETATM 4413  O   HOH A  87       0.450   5.576   8.914  1.00 48.63           O  
HETATM 4414  O   HOH A  88      16.147  -2.435  31.861  1.00 60.63           O  
HETATM 4415  O   HOH A  90      -7.374 -13.585  25.013  1.00 66.71           O  
HETATM 4416  O   HOH A  91      25.185  15.565  -2.200  1.00 73.92           O  
HETATM 4417  O   HOH A  93       8.351 -10.608  16.908  1.00 43.48           O  
HETATM 4418  O   HOH A  97      26.167  12.684   6.990  1.00 49.80           O  
HETATM 4419  O   HOH A  99      -8.452  11.537  20.132  1.00 58.86           O  
HETATM 4420  O   HOH A 100      -1.616  -5.831  20.138  1.00 42.65           O  
HETATM 4421  O   HOH A 102      -6.436   2.950  15.531  1.00 59.67           O  
HETATM 4422  O   HOH A 104      23.337  28.423  25.184  1.00 56.91           O  
HETATM 4423  O   HOH A 105      27.326  28.251  30.357  1.00 72.51           O  
HETATM 4424  O   HOH A 106      10.883  -7.327   9.677  1.00 48.01           O  
HETATM 4425  O   HOH A 107      10.276  23.300  12.429  1.00 81.26           O  
HETATM 4426  O   HOH A 108       8.664  -3.146  32.429  1.00 52.75           O  
HETATM 4427  O   HOH A 109      25.022  10.561  18.053  1.00 60.16           O  
HETATM 4428  O   HOH A 110      -7.895   5.432  13.945  1.00 52.20           O  
HETATM 4429  O   HOH A 111      11.141  22.093  10.361  1.00 74.07           O  
HETATM 4430  O   HOH A 112       9.243  12.492  12.093  1.00 63.66           O  
HETATM 4431  O   HOH A 113      13.198  23.907  11.440  1.00 75.07           O  
HETATM 4432  O   HOH A 114       8.395  21.547  11.397  1.00 62.17           O  
HETATM 4433  O   HOH A 115       8.585  16.435  10.468  1.00 63.92           O  
HETATM 4434  O   HOH A 116      12.857  20.417   9.440  1.00 62.31           O  
HETATM 4435  O   HOH B   5      30.448 -15.510  10.832  1.00 31.89           O  
HETATM 4436  O   HOH B   6      37.185 -14.168  41.954  1.00 55.68           O  
HETATM 4437  O   HOH B   9      20.824  -8.658  44.837  1.00 36.41           O  
HETATM 4438  O   HOH B  11      23.700 -12.804  36.734  1.00 36.08           O  
HETATM 4439  O   HOH B  13      37.390 -15.713  38.356  1.00 40.81           O  
HETATM 4440  O   HOH B  17      35.556 -10.808  12.263  1.00 35.57           O  
HETATM 4441  O   HOH B  21      42.361 -15.246  28.741  1.00 48.85           O  
HETATM 4442  O   HOH B  22      17.739 -13.412  14.012  1.00 66.22           O  
HETATM 4443  O   HOH B  23      40.196  -5.198  58.740  1.00 90.73           O  
HETATM 4444  O   HOH B  24      39.951 -21.406  33.960  1.00 51.98           O  
HETATM 4445  O   HOH B  28      22.748 -19.519   8.894  1.00 47.19           O  
HETATM 4446  O   HOH B  29      44.791 -15.733  35.125  1.00 32.00           O  
HETATM 4447  O   HOH B  31      29.748 -11.131  21.069  1.00 38.80           O  
HETATM 4448  O   HOH B  33      18.484 -13.052  41.695  1.00 40.86           O  
HETATM 4449  O   HOH B  39      20.051  -3.424  24.542  1.00 83.11           O  
HETATM 4450  O   HOH B  40      28.857 -16.185  37.942  1.00 40.68           O  
HETATM 4451  O   HOH B  41      36.963  -7.180  14.735  1.00 44.61           O  
HETATM 4452  O   HOH B  42      39.151 -10.978  14.539  1.00 42.13           O  
HETATM 4453  O   HOH B  44      58.441  -9.519  34.634  1.00 59.64           O  
HETATM 4454  O   HOH B  45      14.070 -23.380  25.679  1.00 37.77           O  
HETATM 4455  O   HOH B  46       0.641  -8.804  33.670  1.00 49.11           O  
HETATM 4456  O   HOH B  48      38.133 -13.151  23.650  1.00 48.17           O  
HETATM 4457  O   HOH B  49      50.605 -13.396  50.820  1.00 91.72           O  
HETATM 4458  O   HOH B  50      18.404 -12.234  37.775  1.00 39.94           O  
HETATM 4459  O   HOH B  51      41.295 -12.847  14.039  1.00 53.53           O  
HETATM 4460  O   HOH B  52      20.535   0.153  41.011  1.00 57.73           O  
HETATM 4461  O   HOH B  55      21.585 -12.461  38.271  1.00 45.36           O  
HETATM 4462  O   HOH B  57      18.992 -23.876  30.235  1.00 48.19           O  
HETATM 4463  O   HOH B  58      19.539 -14.462  46.783  1.00 60.47           O  
HETATM 4464  O   HOH B  59      28.053  -6.819  37.720  1.00 56.22           O  
HETATM 4465  O   HOH B  61      26.490 -19.480  57.349  1.00 77.04           O  
HETATM 4466  O   HOH B  66      37.238  -3.997  23.171  1.00 60.84           O  
HETATM 4467  O   HOH B  68      38.653 -13.146  20.976  1.00 51.13           O  
HETATM 4468  O   HOH B  70      21.920 -24.755  39.153  1.00 61.95           O  
HETATM 4469  O   HOH B  72       6.602 -17.708  37.796  1.00 55.73           O  
HETATM 4470  O   HOH B  74      13.532   0.182  28.505  1.00 68.90           O  
HETATM 4471  O   HOH B  77      13.058 -25.147  29.203  1.00 64.91           O  
HETATM 4472  O   HOH B  82      38.526  -6.031  33.523  1.00 70.71           O  
HETATM 4473  O   HOH B  84      14.703 -15.917  34.261  1.00 84.63           O  
HETATM 4474  O   HOH B  89      23.561   6.254  40.691  1.00 74.14           O  
HETATM 4475  O   HOH B  92      26.514 -29.863  26.749  1.00 53.38           O  
HETATM 4476  O   HOH B  94      41.408 -18.148  55.844  1.00 90.30           O  
HETATM 4477  O   HOH B  95      30.258 -24.439  18.455  1.00 54.33           O  
HETATM 4478  O   HOH B  96      49.343  -2.356  33.288  1.00 66.81           O  
HETATM 4479  O   HOH B 101      10.090 -18.800  22.057  1.00 52.45           O  
HETATM 4480  O   HOH B 103      20.330 -21.201  39.655  1.00 42.43           O  
CONECT 4335 4336                                                                
CONECT 4336 4335 4337                                                           
CONECT 4337 4336 4338 4341 4342                                                 
CONECT 4338 4337 4339 4340                                                      
CONECT 4339 4338                                                                
CONECT 4340 4338                                                                
CONECT 4341 4337                                                                
CONECT 4342 4337 4343                                                           
CONECT 4343 4342 4344 4346                                                      
CONECT 4344 4343 4345                                                           
CONECT 4345 4344 4348                                                           
CONECT 4346 4343 4347                                                           
CONECT 4347 4346 4348                                                           
CONECT 4348 4345 4347 4349                                                      
CONECT 4349 4348 4350                                                           
CONECT 4350 4349 4351                                                           
CONECT 4351 4350 4352 4359                                                      
CONECT 4352 4351 4353                                                           
CONECT 4353 4352 4354                                                           
CONECT 4354 4353 4355                                                           
CONECT 4355 4354 4356                                                           
CONECT 4356 4355 4357                                                           
CONECT 4357 4356 4358                                                           
CONECT 4358 4357                                                                
CONECT 4359 4351 4360 4367                                                      
CONECT 4360 4359 4361                                                           
CONECT 4361 4360 4362 4366                                                      
CONECT 4362 4361 4363                                                           
CONECT 4363 4362 4364                                                           
CONECT 4364 4363 4365                                                           
CONECT 4365 4364 4366                                                           
CONECT 4366 4361 4365 4367                                                      
CONECT 4367 4359 4366                                                           
MASTER      427    0    1   27    8    0    5    6 4478    2   33   44          
END                                                                             
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