HEADER    PHOTORECEPTOR                           27-DEC-95   2BRD              
TITLE     CRYSTAL STRUCTURE OF BACTERIORHODOPSIN IN PURPLE MEMBRANE             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BACTERIORHODOPSIN;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HALOBACTERIUM SALINARUM;                        
SOURCE   3 ORGANISM_TAXID: 2242;                                                
SOURCE   4 STRAIN: R1                                                           
KEYWDS    PROTON PUMP, MEMBRANE PROTEIN, RETINAL PROTEIN, TWO-DIMENSIONAL       
KEYWDS   2 CRYSTAL, PHOTORECEPTOR                                               
EXPDTA    ELECTRON CRYSTALLOGRAPHY                                              
AUTHOR    R.HENDERSON,N.GRIGORIEFF                                              
REVDAT   4   30-MAY-12 2BRD    1       EXPDTA REMARK                            
REVDAT   3   13-JUL-11 2BRD    1       VERSN                                    
REVDAT   2   24-FEB-09 2BRD    1       VERSN                                    
REVDAT   1   10-JUN-96 2BRD    0                                                
JRNL        AUTH   N.GRIGORIEFF,T.A.CESKA,K.H.DOWNING,J.M.BALDWIN,R.HENDERSON   
JRNL        TITL   ELECTRON-CRYSTALLOGRAPHIC REFINEMENT OF THE STRUCTURE OF     
JRNL        TITL 2 BACTERIORHODOPSIN.                                           
JRNL        REF    J.MOL.BIOL.                   V. 259   393 1996              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   8676377                                                      
JRNL        DOI    10.1006/JMBI.1996.0328                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.A.CESKA,R.HENDERSON                                        
REMARK   1  TITL   ANALYSIS OF HIGH-RESOLUTION ELECTRON DIFFRACTION PATTERNS    
REMARK   1  TITL 2 FROM PURPLE MEMBRANE LABELLED WITH HEAVY-ATOMS               
REMARK   1  REF    J.MOL.BIOL.                   V. 213   539 1990              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   R.HENDERSON,J.M.BALDWIN,T.A.CESKA,F.ZEMLIN,E.BECKMANN,       
REMARK   1  AUTH 2 K.H.DOWNING                                                  
REMARK   1  TITL   MODEL FOR THE STRUCTURE OF BACTERIORHODOPSIN BASED ON        
REMARK   1  TITL 2 HIGH-RESOLUTION ELECTRON CRYO-MICROSCOPY                     
REMARK   1  REF    J.MOL.BIOL.                   V. 213   899 1990              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   R.HENDERSON,P.N.UNWIN                                        
REMARK   1  TITL   THREE-DIMENSIONAL MODEL OF PURPLE MEMBRANE OBTAINED BY       
REMARK   1  TITL 2 ELECTRON MICROSCOPY                                          
REMARK   1  REF    NATURE                        V. 257    28 1975              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 85.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 4743                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.280                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1718                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 610                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 114.00                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.005 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.020 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.022 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.005 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.086 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.185 ; 0.300               
REMARK   3    MULTIPLE TORSION                (A) : 0.242 ; 0.300               
REMARK   3    H-BOND (X...Y)                  (A) : 0.127 ; 0.300               
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 0.865 ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : 20.400; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : 36.100; 20.000              
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2BRD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 240                                                                      
REMARK 240 EXPERIMENTAL DETAILS                                                 
REMARK 240   RECONSTRUCTION METHOD          : CRYSTALLOGRAPHY                   
REMARK 240   SAMPLE TYPE                    : 2D CRYSTAL                        
REMARK 240   SPECIMEN TYPE                  : NULL                              
REMARK 240 DATA ACQUISITION                                                     
REMARK 240   DATE OF DATA COLLECTION        : 01-JAN-86                         
REMARK 240   TEMPERATURE           (KELVIN) : NULL                              
REMARK 240   PH                             : NULL                              
REMARK 240   NUMBER OF CRYSTALS USED        : NULL                              
REMARK 240   MICROSCOPE MODEL               : NULL                              
REMARK 240   DETECTOR TYPE                  : NULL                              
REMARK 240   ACCELERATION VOLTAGE (KV)      : NULL                              
REMARK 240   NUMBER OF UNIQUE REFLECTIONS   : 6750                              
REMARK 240   RESOLUTION RANGE HIGH      (A) : 2.800                             
REMARK 240   RESOLUTION RANGE LOW       (A) : 54.000                            
REMARK 240   DATA SCALING SOFTWARE          : NULL                              
REMARK 240   COMPLETENESS FOR RANGE     (%) : 62.3                              
REMARK 240   DATA REDUNDANCY                : 18.000                            
REMARK 240 IN THE HIGHEST RESOLUTION SHELL                                      
REMARK 240   HIGHEST RESOLUTION SHELL, RANGE HIGH (A) :NULL                     
REMARK 240   HIGHEST RESOLUTION SHELL, RANGE LOW  (A) :NULL                     
REMARK 240   COMPLETENESS FOR SHELL     (%) : NULL                              
REMARK 240   DATA REDUNDANCY IN SHELL       : NULL                              
REMARK 240   R MERGE FOR SHELL          (I) : NULL                              
REMARK 240   METHOD USED TO DETERMINE THE STRUCTURE: NULL                       
REMARK 240   SOFTWARE USED                  : NULL                              
REMARK 240   STARTING MODEL                 : NULL                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 34840 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 35800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -277.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  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     PCA A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     ILE A   229                                                      
REMARK 465     PHE A   230                                                      
REMARK 465     GLY A   231                                                      
REMARK 465     GLU A   232                                                      
REMARK 465     ALA A   233                                                      
REMARK 465     GLU A   234                                                      
REMARK 465     ALA A   235                                                      
REMARK 465     PRO A   236                                                      
REMARK 465     GLU A   237                                                      
REMARK 465     PRO A   238                                                      
REMARK 465     SER A   239                                                      
REMARK 465     ALA A   240                                                      
REMARK 465     GLY A   241                                                      
REMARK 465     ASP A   242                                                      
REMARK 465     GLY A   243                                                      
REMARK 465     ALA A   244                                                      
REMARK 465     ALA A   245                                                      
REMARK 465     ALA A   246                                                      
REMARK 465     THR A   247                                                      
REMARK 465     SER A   248                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ALA A 228    CA   C    O    CB                                   
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    TRP A  80   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES          
REMARK 500    TYR A 133   CA  -  CB  -  CG  ANGL. DEV. =  14.6 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    GLU A   9      -41.19    -26.45                                   
REMARK 500    MET A  32      -89.28    -10.24                                   
REMARK 500    ASP A  36      -62.59   -132.17                                   
REMARK 500    PRO A  37     -118.09    -90.23                                   
REMARK 500    THR A  67       73.11   -116.15                                   
REMARK 500    PHE A  71       92.89   -171.60                                   
REMARK 500    GLN A  75      176.05    -53.88                                   
REMARK 500    THR A  89      -72.87    -42.50                                   
REMARK 500    VAL A 101      -89.22   -104.11                                   
REMARK 500    TYR A 133       -0.23   -173.72                                   
REMARK 500    ALA A 160     -141.06     42.32                                   
REMARK 500    GLU A 161      107.85    -45.90                                   
REMARK 500    MET A 163     -117.98    -99.74                                   
REMARK 500    TYR A 185      -71.49    -42.16                                   
REMARK 500    SER A 193     -101.25     12.74                                   
REMARK 500    PRO A 200      -91.57    -48.56                                   
REMARK 500    LEU A 201      -56.54   -154.37                                   
REMARK 500    ASP A 212      -73.64    -44.01                                   
REMARK 500    ARG A 227       99.21    -64.77                                   
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 DPG A 261                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPG A 262                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPG A 263                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPG A 264                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPG A 265                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPG A 266                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPG A 267                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPG A 268                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPG A 269                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPG A 270                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RET A 271                 
DBREF  2BRD A    2   248  UNP    P02945   BACR_HALN1      14    253             
SEQRES   1 A  248  PCA ALA GLN ILE THR GLY ARG PRO GLU TRP ILE TRP LEU          
SEQRES   2 A  248  ALA LEU GLY THR ALA LEU MET GLY LEU GLY THR LEU TYR          
SEQRES   3 A  248  PHE LEU VAL LYS GLY MET GLY VAL SER ASP PRO ASP ALA          
SEQRES   4 A  248  LYS LYS PHE TYR ALA ILE THR THR LEU VAL PRO ALA ILE          
SEQRES   5 A  248  ALA PHE THR MET TYR LEU SER MET LEU LEU GLY TYR GLY          
SEQRES   6 A  248  LEU THR MET VAL PRO PHE GLY GLY GLU GLN ASN PRO ILE          
SEQRES   7 A  248  TYR TRP ALA ARG TYR ALA ASP TRP LEU PHE THR THR PRO          
SEQRES   8 A  248  LEU LEU LEU LEU ASP LEU ALA LEU LEU VAL ASP ALA ASP          
SEQRES   9 A  248  GLN GLY THR ILE LEU ALA LEU VAL GLY ALA ASP GLY ILE          
SEQRES  10 A  248  MET ILE GLY THR GLY LEU VAL GLY ALA LEU THR LYS VAL          
SEQRES  11 A  248  TYR SER TYR ARG PHE VAL TRP TRP ALA ILE SER THR ALA          
SEQRES  12 A  248  ALA MET LEU TYR ILE LEU TYR VAL LEU PHE PHE GLY PHE          
SEQRES  13 A  248  THR SER LYS ALA GLU SER MET ARG PRO GLU VAL ALA SER          
SEQRES  14 A  248  THR PHE LYS VAL LEU ARG ASN VAL THR VAL VAL LEU TRP          
SEQRES  15 A  248  SER ALA TYR PRO VAL VAL TRP LEU ILE GLY SER GLU GLY          
SEQRES  16 A  248  ALA GLY ILE VAL PRO LEU ASN ILE GLU THR LEU LEU PHE          
SEQRES  17 A  248  MET VAL LEU ASP VAL SER ALA LYS VAL GLY PHE GLY LEU          
SEQRES  18 A  248  ILE LEU LEU ARG SER ARG ALA ILE PHE GLY GLU ALA GLU          
SEQRES  19 A  248  ALA PRO GLU PRO SER ALA GLY ASP GLY ALA ALA ALA THR          
SEQRES  20 A  248  SER                                                          
HET    DPG  A 261      59                                                       
HET    DPG  A 262      59                                                       
HET    DPG  A 263      59                                                       
HET    DPG  A 264      59                                                       
HET    DPG  A 265      59                                                       
HET    DPG  A 266      59                                                       
HET    DPG  A 267      59                                                       
HET    DPG  A 268      59                                                       
HET    DPG  A 269      59                                                       
HET    DPG  A 270      59                                                       
HET    RET  A 271      20                                                       
HETNAM     DPG PHOSPHORIC ACID 2,3-BIS-(3,7,11,15-TETRAMETHYL-                  
HETNAM   2 DPG  HEXADECYLOXY)-PROPYL ESTER 2-HYDROXO-3-PHOSPHONOOXY-            
HETNAM   3 DPG  PROPYL ESTER                                                    
HETNAM     RET RETINAL                                                          
HETSYN     DPG DPHPG                                                            
FORMUL   2  DPG    10(C46 H96 O11 P2)                                           
FORMUL  12  RET    C20 H28 O                                                    
HELIX    1   A GLU A    9  GLY A   31  1                                  23    
HELIX    2   B ASP A   38  LEU A   62  1                                  25    
HELIX    3   C PRO A   77  LEU A  100  1                                  24    
HELIX    4   D GLN A  105  LEU A  127  1                                  23    
HELIX    5   E ARG A  134  THR A  157  1                                  24    
HELIX    6   F GLU A  166  ILE A  191  1                                  26    
HELIX    7   G ILE A  203  SER A  226  1                                  24    
LINK         C15 RET A 271                 NZ  LYS A 216     1555   1555  1.31  
SITE     1 AC1 10 TYR A  64  LEU A  66  MET A  68  PRO A  70                    
SITE     2 AC1 10 TRP A  80  LEU A  87  PHE A  88  VAL A 124                    
SITE     3 AC1 10 LYS A 129  DPG A 266                                          
SITE     1 AC2  9 SER A 183  VAL A 187  ILE A 191  ALA A 196                    
SITE     2 AC2  9 ILE A 198  LEU A 207  DPG A 263  DPG A 267                    
SITE     3 AC2  9 DPG A 268                                                     
SITE     1 AC3 11 TRP A  12  PHE A 135  TRP A 138  ALA A 196                    
SITE     2 AC3 11 ILE A 203  LEU A 206  VAL A 210  DPG A 262                    
SITE     3 AC3 11 DPG A 264  DPG A 265  DPG A 268                               
SITE     1 AC4  8 ALA A  18  PHE A  54  LEU A  58  LEU A  61                    
SITE     2 AC4  8 VAL A 136  DPG A 263  DPG A 265  DPG A 270                    
SITE     1 AC5  5 ILE A  11  LEU A  15  ALA A  18  DPG A 263                    
SITE     2 AC5  5 DPG A 264                                                     
SITE     1 AC6 12 ILE A  52  PHE A  88  LEU A  92  LEU A  95                    
SITE     2 AC6 12 LEU A  99  ALA A 103  GLN A 105  ILE A 108                    
SITE     3 AC6 12 LEU A 109  GLY A 116  ILE A 117  DPG A 261                    
SITE     1 AC7  9 PHE A 156  LYS A 172  ARG A 175  ASN A 176                    
SITE     2 AC7  9 VAL A 180  ALA A 184  VAL A 187  DPG A 262                    
SITE     3 AC7  9 DPG A 268                                                     
SITE     1 AC8 18 TRP A 138  THR A 142  MET A 145  LEU A 149                    
SITE     2 AC8 18 TYR A 150  PHE A 153  THR A 157  SER A 169                    
SITE     3 AC8 18 LYS A 172  VAL A 173  VAL A 179  PRO A 186                    
SITE     4 AC8 18 VAL A 210  SER A 214  ARG A 225  DPG A 262                    
SITE     5 AC8 18 DPG A 263  DPG A 267                                          
SITE     1 AC9 10 LEU A  28  MET A  32  GLY A  33  LYS A  40                    
SITE     2 AC9 10 THR A  47  ALA A  51  TYR A 147  PHE A 154                    
SITE     3 AC9 10 LEU A 221  DPG A 270                                          
SITE     1 BC1  9 LEU A  22  TYR A  26  VAL A  29  LYS A  30                    
SITE     2 BC1  9 GLY A  33  LEU A 224  ARG A 227  DPG A 264                    
SITE     3 BC1  9 DPG A 269                                                     
SITE     1 BC2 11 TRP A  86  THR A  89  THR A  90  MET A 118                    
SITE     2 BC2 11 TRP A 138  SER A 141  TRP A 182  TYR A 185                    
SITE     3 BC2 11 TRP A 189  ASP A 212  LYS A 216                               
CRYST1   62.450   62.450  100.900  90.00  90.00 120.00 P 3           3          
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      0.016013  0.009245  0.000000        0.00000                         
SCALE2      0.000000  0.018490  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009911        0.00000                         
ATOM      1  N   ARG A   7      23.709  -2.251 -15.148  1.00105.67           N  
ATOM      2  CA  ARG A   7      24.318  -3.586 -15.161  1.00105.67           C  
ATOM      3  C   ARG A   7      25.040  -3.953 -13.872  1.00105.67           C  
ATOM      4  O   ARG A   7      24.733  -4.992 -13.256  1.00105.67           O  
ATOM      5  CB  ARG A   7      25.253  -3.702 -16.368  1.00 99.95           C  
ATOM      6  CG  ARG A   7      26.154  -4.923 -16.450  1.00119.68           C  
ATOM      7  CD  ARG A   7      27.359  -4.626 -17.276  1.00129.40           C  
ATOM      8  NE  ARG A   7      28.202  -5.785 -17.514  1.00164.78           N  
ATOM      9  CZ  ARG A   7      29.444  -5.714 -17.998  1.00127.09           C  
ATOM     10  NH1 ARG A   7      30.025  -4.554 -18.291  1.00170.55           N  
ATOM     11  NH2 ARG A   7      30.124  -6.843 -18.205  1.00170.55           N  
ATOM     12  N   PRO A   8      25.990  -3.121 -13.469  1.00 87.10           N  
ATOM     13  CA  PRO A   8      26.813  -3.320 -12.276  1.00 87.10           C  
ATOM     14  C   PRO A   8      26.107  -3.587 -10.971  1.00 87.10           C  
ATOM     15  O   PRO A   8      26.494  -4.488 -10.186  1.00 87.10           O  
ATOM     16  CB  PRO A   8      27.694  -2.063 -12.196  1.00 81.38           C  
ATOM     17  CG  PRO A   8      27.783  -1.604 -13.629  1.00 81.38           C  
ATOM     18  CD  PRO A   8      26.388  -1.887 -14.180  1.00 81.38           C  
ATOM     19  N   GLU A   9      25.053  -2.854 -10.688  1.00 59.83           N  
ATOM     20  CA  GLU A   9      24.216  -2.927  -9.497  1.00 59.83           C  
ATOM     21  C   GLU A   9      24.157  -4.262  -8.778  1.00 59.83           C  
ATOM     22  O   GLU A   9      24.187  -4.298  -7.526  1.00 59.83           O  
ATOM     23  CB  GLU A   9      22.775  -2.501  -9.814  1.00 54.11           C  
ATOM     24  CG  GLU A   9      22.514  -1.002  -9.923  1.00 73.84           C  
ATOM     25  CD  GLU A   9      21.156  -0.606 -10.423  1.00 83.56           C  
ATOM     26  OE1 GLU A   9      20.544  -1.230 -11.274  1.00118.94           O  
ATOM     27  OE2 GLU A   9      20.731   0.434  -9.875  1.00118.94           O  
ATOM     28  N   TRP A  10      24.082  -5.360  -9.500  1.00 36.30           N  
ATOM     29  CA  TRP A  10      24.019  -6.731  -9.022  1.00 36.30           C  
ATOM     30  C   TRP A  10      25.102  -7.099  -8.007  1.00 36.30           C  
ATOM     31  O   TRP A  10      24.773  -7.880  -7.090  1.00 36.30           O  
ATOM     32  CB  TRP A  10      23.966  -7.755 -10.146  1.00 30.58           C  
ATOM     33  CG  TRP A  10      25.105  -8.051 -11.039  1.00 46.70           C  
ATOM     34  CD1 TRP A  10      26.447  -8.021 -10.778  1.00 46.70           C  
ATOM     35  CD2 TRP A  10      24.996  -8.501 -12.408  1.00 46.70           C  
ATOM     36  NE1 TRP A  10      27.176  -8.388 -11.882  1.00 46.70           N  
ATOM     37  CE2 TRP A  10      26.309  -8.690 -12.895  1.00 46.70           C  
ATOM     38  CE3 TRP A  10      23.917  -8.747 -13.253  1.00 46.70           C  
ATOM     39  CZ2 TRP A  10      26.566  -9.112 -14.192  1.00 46.70           C  
ATOM     40  CZ3 TRP A  10      24.170  -9.164 -14.544  1.00 46.70           C  
ATOM     41  CH2 TRP A  10      25.470  -9.346 -15.010  1.00 46.70           C  
ATOM     42  N   ILE A  11      26.315  -6.602  -8.171  1.00 25.63           N  
ATOM     43  CA  ILE A  11      27.384  -6.940  -7.214  1.00 25.63           C  
ATOM     44  C   ILE A  11      27.085  -6.314  -5.852  1.00 25.63           C  
ATOM     45  O   ILE A  11      27.122  -6.986  -4.807  1.00 25.63           O  
ATOM     46  CB  ILE A  11      28.801  -6.586  -7.777  1.00 19.91           C  
ATOM     47  CG1 ILE A  11      29.888  -7.041  -6.766  1.00 39.64           C  
ATOM     48  CG2 ILE A  11      28.977  -5.090  -8.150  1.00 39.64           C  
ATOM     49  CD1 ILE A  11      29.936  -8.575  -6.523  1.00 49.36           C  
ATOM     50  N   TRP A  12      26.773  -5.031  -5.884  1.00 23.84           N  
ATOM     51  CA  TRP A  12      26.459  -4.230  -4.700  1.00 23.84           C  
ATOM     52  C   TRP A  12      25.253  -4.811  -3.949  1.00 23.84           C  
ATOM     53  O   TRP A  12      25.295  -5.015  -2.725  1.00 23.84           O  
ATOM     54  CB  TRP A  12      26.200  -2.769  -5.030  1.00 18.12           C  
ATOM     55  CG  TRP A  12      26.947  -2.071  -6.100  1.00 34.24           C  
ATOM     56  CD1 TRP A  12      26.436  -1.589  -7.280  1.00 34.24           C  
ATOM     57  CD2 TRP A  12      28.345  -1.736  -6.120  1.00 34.24           C  
ATOM     58  NE1 TRP A  12      27.422  -0.990  -8.027  1.00 34.24           N  
ATOM     59  CE2 TRP A  12      28.601  -1.066  -7.338  1.00 34.24           C  
ATOM     60  CE3 TRP A  12      29.386  -1.952  -5.224  1.00 34.24           C  
ATOM     61  CZ2 TRP A  12      29.866  -0.609  -7.678  1.00 34.24           C  
ATOM     62  CZ3 TRP A  12      30.648  -1.503  -5.559  1.00 34.24           C  
ATOM     63  CH2 TRP A  12      30.882  -0.844  -6.762  1.00 34.24           C  
ATOM     64  N   LEU A  13      24.208  -5.039  -4.728  1.00 23.60           N  
ATOM     65  CA  LEU A  13      22.939  -5.588  -4.224  1.00 23.60           C  
ATOM     66  C   LEU A  13      23.087  -7.010  -3.706  1.00 23.60           C  
ATOM     67  O   LEU A  13      22.461  -7.324  -2.671  1.00 23.60           O  
ATOM     68  CB  LEU A  13      21.862  -5.339  -5.282  1.00 17.88           C  
ATOM     69  CG  LEU A  13      20.852  -4.223  -5.081  1.00 37.61           C  
ATOM     70  CD1 LEU A  13      21.336  -3.075  -4.203  1.00 47.33           C  
ATOM     71  CD2 LEU A  13      20.504  -3.658  -6.465  1.00 47.33           C  
ATOM     72  N   ALA A  14      23.881  -7.832  -4.374  1.00 19.45           N  
ATOM     73  CA  ALA A  14      24.106  -9.226  -3.937  1.00 19.45           C  
ATOM     74  C   ALA A  14      24.866  -9.182  -2.611  1.00 19.45           C  
ATOM     75  O   ALA A  14      24.510  -9.857  -1.625  1.00 19.45           O  
ATOM     76  CB  ALA A  14      24.779 -10.059  -5.009  1.00 13.73           C  
ATOM     77  N   LEU A  15      25.885  -8.334  -2.580  1.00 13.21           N  
ATOM     78  CA  LEU A  15      26.738  -8.094  -1.410  1.00 13.21           C  
ATOM     79  C   LEU A  15      25.861  -7.720  -0.206  1.00 13.21           C  
ATOM     80  O   LEU A  15      26.057  -8.205   0.916  1.00 13.21           O  
ATOM     81  CB  LEU A  15      27.728  -6.979  -1.766  1.00  7.49           C  
ATOM     82  CG  LEU A  15      28.997  -6.895  -0.934  1.00 27.22           C  
ATOM     83  CD1 LEU A  15      30.207  -7.294  -1.769  1.00 36.94           C  
ATOM     84  CD2 LEU A  15      29.133  -5.470  -0.410  1.00 36.94           C  
ATOM     85  N   GLY A  16      24.916  -6.838  -0.494  1.00  8.52           N  
ATOM     86  CA  GLY A  16      23.929  -6.328   0.453  1.00  8.52           C  
ATOM     87  C   GLY A  16      23.013  -7.448   0.941  1.00  8.52           C  
ATOM     88  O   GLY A  16      22.785  -7.573   2.154  1.00  8.52           O  
ATOM     89  N   THR A  17      22.506  -8.241   0.012  1.00  9.03           N  
ATOM     90  CA  THR A  17      21.609  -9.364   0.317  1.00  9.03           C  
ATOM     91  C   THR A  17      22.282 -10.291   1.331  1.00  9.03           C  
ATOM     92  O   THR A  17      21.701 -10.629   2.374  1.00  9.03           O  
ATOM     93  CB  THR A  17      21.136 -10.171  -0.951  1.00  5.00           C  
ATOM     94  OG1 THR A  17      20.484  -9.228  -1.858  1.00 23.04           O  
ATOM     95  CG2 THR A  17      20.203 -11.347  -0.630  1.00 23.04           C  
ATOM     96  N   ALA A  18      23.499 -10.675   0.983  1.00 16.73           N  
ATOM     97  CA  ALA A  18      24.325 -11.552   1.815  1.00 16.73           C  
ATOM     98  C   ALA A  18      24.600 -10.941   3.190  1.00 16.73           C  
ATOM     99  O   ALA A  18      24.337 -11.573   4.227  1.00 16.73           O  
ATOM    100  CB  ALA A  18      25.658 -11.826   1.115  1.00 11.01           C  
ATOM    101  N   LEU A  19      25.132  -9.730   3.157  1.00 27.10           N  
ATOM    102  CA  LEU A  19      25.496  -8.971   4.360  1.00 27.10           C  
ATOM    103  C   LEU A  19      24.331  -8.858   5.341  1.00 27.10           C  
ATOM    104  O   LEU A  19      24.415  -9.293   6.503  1.00 27.10           O  
ATOM    105  CB  LEU A  19      26.055  -7.621   3.904  1.00 21.38           C  
ATOM    106  CG  LEU A  19      27.286  -7.035   4.568  1.00 41.11           C  
ATOM    107  CD1 LEU A  19      27.223  -7.070   6.089  1.00 50.83           C  
ATOM    108  CD2 LEU A  19      28.505  -7.815   4.073  1.00 50.83           C  
ATOM    109  N   MET A  20      23.259  -8.270   4.849  1.00 33.95           N  
ATOM    110  CA  MET A  20      22.015  -8.040   5.593  1.00 33.95           C  
ATOM    111  C   MET A  20      21.415  -9.346   6.089  1.00 33.95           C  
ATOM    112  O   MET A  20      21.105  -9.467   7.291  1.00 33.95           O  
ATOM    113  CB  MET A  20      21.054  -7.194   4.762  1.00 28.23           C  
ATOM    114  CG  MET A  20      21.605  -5.779   4.716  1.00 47.96           C  
ATOM    115  SD  MET A  20      20.248  -4.702   4.136  1.00 57.68           S  
ATOM    116  CE  MET A  20      20.864  -3.108   4.702  1.00 93.06           C  
ATOM    117  N   GLY A  21      21.303 -10.315   5.196  1.00 33.34           N  
ATOM    118  CA  GLY A  21      20.763 -11.649   5.530  1.00 33.34           C  
ATOM    119  C   GLY A  21      21.539 -12.167   6.747  1.00 33.34           C  
ATOM    120  O   GLY A  21      20.959 -12.594   7.757  1.00 33.34           O  
ATOM    121  N   LEU A  22      22.857 -12.086   6.619  1.00 30.36           N  
ATOM    122  CA  LEU A  22      23.806 -12.491   7.658  1.00 30.36           C  
ATOM    123  C   LEU A  22      23.490 -11.762   8.963  1.00 30.36           C  
ATOM    124  O   LEU A  22      23.408 -12.409  10.025  1.00 30.36           O  
ATOM    125  CB  LEU A  22      25.236 -12.302   7.133  1.00 24.64           C  
ATOM    126  CG  LEU A  22      26.320 -12.887   8.036  1.00 44.37           C  
ATOM    127  CD1 LEU A  22      27.326 -13.680   7.216  1.00 54.09           C  
ATOM    128  CD2 LEU A  22      26.995 -11.735   8.777  1.00 54.09           C  
ATOM    129  N   GLY A  23      23.287 -10.457   8.879  1.00 32.35           N  
ATOM    130  CA  GLY A  23      22.945  -9.620  10.038  1.00 32.35           C  
ATOM    131  C   GLY A  23      21.701 -10.184  10.732  1.00 32.35           C  
ATOM    132  O   GLY A  23      21.689 -10.315  11.967  1.00 32.35           O  
ATOM    133  N   THR A  24      20.692 -10.503   9.944  1.00 43.60           N  
ATOM    134  CA  THR A  24      19.417 -11.065  10.367  1.00 43.60           C  
ATOM    135  C   THR A  24      19.564 -12.379  11.141  1.00 43.60           C  
ATOM    136  O   THR A  24      19.125 -12.519  12.292  1.00 43.60           O  
ATOM    137  CB  THR A  24      18.459 -11.386   9.139  1.00 37.88           C  
ATOM    138  OG1 THR A  24      18.549 -10.270   8.211  1.00 57.61           O  
ATOM    139  CG2 THR A  24      17.015 -11.677   9.559  1.00 57.61           C  
ATOM    140  N   LEU A  25      20.168 -13.328  10.442  1.00 56.22           N  
ATOM    141  CA  LEU A  25      20.415 -14.677  10.975  1.00 56.22           C  
ATOM    142  C   LEU A  25      21.169 -14.577  12.299  1.00 56.22           C  
ATOM    143  O   LEU A  25      20.722 -14.997  13.387  1.00 56.22           O  
ATOM    144  CB  LEU A  25      21.153 -15.447   9.876  1.00 50.50           C  
ATOM    145  CG  LEU A  25      20.505 -15.515   8.504  1.00 70.23           C  
ATOM    146  CD1 LEU A  25      21.483 -16.069   7.472  1.00 79.95           C  
ATOM    147  CD2 LEU A  25      19.263 -16.401   8.578  1.00 79.95           C  
ATOM    148  N   TYR A  26      22.335 -13.953  12.172  1.00 59.31           N  
ATOM    149  CA  TYR A  26      23.261 -13.708  13.278  1.00 59.31           C  
ATOM    150  C   TYR A  26      22.493 -13.144  14.472  1.00 59.31           C  
ATOM    151  O   TYR A  26      22.621 -13.683  15.581  1.00 59.31           O  
ATOM    152  CB  TYR A  26      24.424 -12.776  12.892  1.00 53.59           C  
ATOM    153  CG  TYR A  26      25.342 -12.459  14.055  1.00 69.71           C  
ATOM    154  CD1 TYR A  26      26.391 -13.318  14.399  1.00 69.71           C  
ATOM    155  CD2 TYR A  26      25.153 -11.308  14.820  1.00 69.71           C  
ATOM    156  CE1 TYR A  26      27.231 -13.033  15.473  1.00 69.71           C  
ATOM    157  CE2 TYR A  26      25.981 -11.011  15.897  1.00 69.71           C  
ATOM    158  CZ  TYR A  26      27.019 -11.875  16.219  1.00 69.71           C  
ATOM    159  OH  TYR A  26      27.817 -11.554  17.281  1.00 83.04           O  
ATOM    160  N   PHE A  27      21.719 -12.100  14.217  1.00 47.13           N  
ATOM    161  CA  PHE A  27      20.916 -11.454  15.259  1.00 47.13           C  
ATOM    162  C   PHE A  27      19.876 -12.408  15.844  1.00 47.13           C  
ATOM    163  O   PHE A  27      19.601 -12.272  17.054  1.00 47.13           O  
ATOM    164  CB  PHE A  27      20.310 -10.113  14.840  1.00 41.41           C  
ATOM    165  CG  PHE A  27      20.507  -9.123  15.959  1.00 57.53           C  
ATOM    166  CD1 PHE A  27      19.641  -9.100  17.047  1.00 57.53           C  
ATOM    167  CD2 PHE A  27      21.599  -8.254  15.917  1.00 57.53           C  
ATOM    168  CE1 PHE A  27      19.844  -8.183  18.084  1.00 57.53           C  
ATOM    169  CE2 PHE A  27      21.813  -7.344  16.940  1.00 57.53           C  
ATOM    170  CZ  PHE A  27      20.937  -7.298  18.027  1.00 57.53           C  
ATOM    171  N   LEU A  28      19.331 -13.314  15.041  1.00 34.74           N  
ATOM    172  CA  LEU A  28      18.347 -14.279  15.558  1.00 34.74           C  
ATOM    173  C   LEU A  28      19.081 -15.101  16.630  1.00 34.74           C  
ATOM    174  O   LEU A  28      18.554 -15.237  17.744  1.00 34.74           O  
ATOM    175  CB  LEU A  28      17.723 -15.117  14.450  1.00 29.02           C  
ATOM    176  CG  LEU A  28      16.527 -15.994  14.796  1.00 48.75           C  
ATOM    177  CD1 LEU A  28      15.808 -16.480  13.538  1.00 58.47           C  
ATOM    178  CD2 LEU A  28      16.956 -17.223  15.599  1.00 58.47           C  
ATOM    179  N   VAL A  29      20.247 -15.599  16.241  1.00 42.41           N  
ATOM    180  CA  VAL A  29      21.067 -16.405  17.167  1.00 42.41           C  
ATOM    181  C   VAL A  29      21.456 -15.625  18.422  1.00 42.41           C  
ATOM    182  O   VAL A  29      21.032 -15.926  19.552  1.00 42.41           O  
ATOM    183  CB  VAL A  29      22.282 -16.980  16.411  1.00 36.69           C  
ATOM    184  CG1 VAL A  29      23.252 -17.721  17.326  1.00 56.42           C  
ATOM    185  CG2 VAL A  29      21.859 -17.858  15.243  1.00 56.42           C  
ATOM    186  N   LYS A  30      22.269 -14.608  18.228  1.00 84.32           N  
ATOM    187  CA  LYS A  30      22.788 -13.717  19.266  1.00 84.32           C  
ATOM    188  C   LYS A  30      21.673 -13.171  20.156  1.00 84.32           C  
ATOM    189  O   LYS A  30      21.725 -13.265  21.392  1.00 84.32           O  
ATOM    190  CB  LYS A  30      23.537 -12.532  18.654  1.00 78.60           C  
ATOM    191  CG  LYS A  30      24.516 -11.842  19.607  1.00 98.33           C  
ATOM    192  CD  LYS A  30      25.740 -12.720  19.828  1.00108.05           C  
ATOM    193  CE  LYS A  30      26.621 -12.212  20.946  1.00143.43           C  
ATOM    194  NZ  LYS A  30      27.833 -13.061  21.076  1.00105.74           N  
ATOM    195  N   GLY A  31      20.687 -12.595  19.496  1.00150.37           N  
ATOM    196  CA  GLY A  31      19.508 -11.995  20.107  1.00150.37           C  
ATOM    197  C   GLY A  31      18.785 -12.942  21.056  1.00150.37           C  
ATOM    198  O   GLY A  31      18.856 -12.760  22.282  1.00150.37           O  
ATOM    199  N   MET A  32      18.106 -13.915  20.490  1.00224.40           N  
ATOM    200  CA  MET A  32      17.329 -14.937  21.201  1.00224.40           C  
ATOM    201  C   MET A  32      17.598 -14.896  22.704  1.00224.40           C  
ATOM    202  O   MET A  32      16.907 -14.187  23.455  1.00224.40           O  
ATOM    203  CB  MET A  32      17.590 -16.306  20.581  1.00218.68           C  
ATOM    204  CG  MET A  32      16.423 -17.241  20.764  1.00238.41           C  
ATOM    205  SD  MET A  32      16.668 -18.656  19.629  1.00248.13           S  
ATOM    206  CE  MET A  32      15.072 -19.475  19.799  1.00283.51           C  
ATOM    207  N   GLY A  33      18.595 -15.640  23.124  1.00290.22           N  
ATOM    208  CA  GLY A  33      19.072 -15.779  24.484  1.00290.22           C  
ATOM    209  C   GLY A  33      18.086 -15.479  25.597  1.00290.22           C  
ATOM    210  O   GLY A  33      16.899 -15.835  25.560  1.00290.22           O  
ATOM    211  N   VAL A  34      18.625 -14.824  26.614  1.00333.81           N  
ATOM    212  CA  VAL A  34      17.896 -14.419  27.824  1.00333.81           C  
ATOM    213  C   VAL A  34      17.170 -13.098  27.575  1.00333.81           C  
ATOM    214  O   VAL A  34      17.769 -12.014  27.644  1.00333.81           O  
ATOM    215  CB  VAL A  34      18.845 -14.403  29.035  1.00328.09           C  
ATOM    216  CG1 VAL A  34      19.188 -15.806  29.527  1.00347.82           C  
ATOM    217  CG2 VAL A  34      20.119 -13.615  28.772  1.00347.82           C  
ATOM    218  N   SER A  35      15.884 -13.241  27.291  1.00349.55           N  
ATOM    219  CA  SER A  35      15.024 -12.083  27.011  1.00349.55           C  
ATOM    220  C   SER A  35      13.547 -12.463  26.986  1.00349.55           C  
ATOM    221  O   SER A  35      13.134 -13.449  26.360  1.00349.55           O  
ATOM    222  CB  SER A  35      15.434 -11.451  25.686  1.00343.83           C  
ATOM    223  OG  SER A  35      15.271 -12.354  24.608  1.00363.56           O  
ATOM    224  N   ASP A  36      12.780 -11.638  27.674  1.00334.00           N  
ATOM    225  CA  ASP A  36      11.319 -11.776  27.788  1.00334.00           C  
ATOM    226  C   ASP A  36      10.705 -10.398  27.507  1.00334.00           C  
ATOM    227  O   ASP A  36       9.970 -10.240  26.520  1.00334.00           O  
ATOM    228  CB  ASP A  36      10.879 -12.429  29.085  1.00328.28           C  
ATOM    229  CG  ASP A  36      10.769 -13.941  29.023  1.00348.01           C  
ATOM    230  OD1 ASP A  36      11.832 -14.585  29.150  1.00357.73           O  
ATOM    231  OD2 ASP A  36       9.667 -14.488  28.856  1.00357.73           O  
ATOM    232  N   PRO A  37      11.045  -9.451  28.364  1.00287.15           N  
ATOM    233  CA  PRO A  37      10.551  -8.074  28.241  1.00287.15           C  
ATOM    234  C   PRO A  37      11.450  -7.185  27.402  1.00287.15           C  
ATOM    235  O   PRO A  37      11.718  -7.440  26.213  1.00287.15           O  
ATOM    236  CB  PRO A  37      10.450  -7.658  29.712  1.00281.43           C  
ATOM    237  CG  PRO A  37      11.622  -8.337  30.370  1.00281.43           C  
ATOM    238  CD  PRO A  37      11.912  -9.585  29.545  1.00281.43           C  
ATOM    239  N   ASP A  38      11.970  -6.154  28.042  1.00222.99           N  
ATOM    240  CA  ASP A  38      12.856  -5.135  27.481  1.00222.99           C  
ATOM    241  C   ASP A  38      13.833  -5.725  26.464  1.00222.99           C  
ATOM    242  O   ASP A  38      13.770  -5.410  25.264  1.00222.99           O  
ATOM    243  CB  ASP A  38      13.579  -4.377  28.597  1.00217.27           C  
ATOM    244  CG  ASP A  38      12.679  -3.522  29.464  1.00237.00           C  
ATOM    245  OD1 ASP A  38      11.483  -3.351  29.185  1.00246.72           O  
ATOM    246  OD2 ASP A  38      13.216  -3.003  30.469  1.00246.72           O  
ATOM    247  N   ALA A  39      14.705  -6.581  26.963  1.00158.96           N  
ATOM    248  CA  ALA A  39      15.727  -7.257  26.159  1.00158.96           C  
ATOM    249  C   ALA A  39      15.139  -7.830  24.875  1.00158.96           C  
ATOM    250  O   ALA A  39      15.645  -7.524  23.779  1.00158.96           O  
ATOM    251  CB  ALA A  39      16.419  -8.329  26.992  1.00153.24           C  
ATOM    252  N   LYS A  40      14.090  -8.627  25.010  1.00109.44           N  
ATOM    253  CA  LYS A  40      13.409  -9.264  23.875  1.00109.44           C  
ATOM    254  C   LYS A  40      12.768  -8.230  22.955  1.00109.44           C  
ATOM    255  O   LYS A  40      12.738  -8.442  21.733  1.00109.44           O  
ATOM    256  CB  LYS A  40      12.360 -10.279  24.294  1.00103.72           C  
ATOM    257  CG  LYS A  40      11.842 -11.187  23.181  1.00123.45           C  
ATOM    258  CD  LYS A  40      11.102 -12.388  23.756  1.00133.17           C  
ATOM    259  CE  LYS A  40      10.486 -13.268  22.690  1.00168.55           C  
ATOM    260  NZ  LYS A  40       9.869 -14.484  23.278  1.00130.86           N  
ATOM    261  N   LYS A  41      12.264  -7.163  23.545  1.00 76.57           N  
ATOM    262  CA  LYS A  41      11.629  -6.062  22.802  1.00 76.57           C  
ATOM    263  C   LYS A  41      12.672  -5.470  21.852  1.00 76.57           C  
ATOM    264  O   LYS A  41      12.456  -5.367  20.634  1.00 76.57           O  
ATOM    265  CB  LYS A  41      11.096  -5.000  23.745  1.00 70.85           C  
ATOM    266  CG  LYS A  41      10.610  -3.704  23.104  1.00 90.58           C  
ATOM    267  CD  LYS A  41      10.722  -2.551  24.094  1.00100.30           C  
ATOM    268  CE  LYS A  41      12.154  -2.113  24.318  1.00135.68           C  
ATOM    269  NZ  LYS A  41      12.225  -0.913  25.189  1.00 97.99           N  
ATOM    270  N   PHE A  42      13.802  -5.119  22.448  1.00 59.41           N  
ATOM    271  CA  PHE A  42      14.952  -4.542  21.738  1.00 59.41           C  
ATOM    272  C   PHE A  42      15.408  -5.503  20.636  1.00 59.41           C  
ATOM    273  O   PHE A  42      15.541  -5.082  19.474  1.00 59.41           O  
ATOM    274  CB  PHE A  42      16.087  -4.142  22.675  1.00 53.69           C  
ATOM    275  CG  PHE A  42      15.871  -2.849  23.405  1.00 69.81           C  
ATOM    276  CD1 PHE A  42      15.742  -1.657  22.694  1.00 69.81           C  
ATOM    277  CD2 PHE A  42      15.785  -2.826  24.797  1.00 69.81           C  
ATOM    278  CE1 PHE A  42      15.533  -0.446  23.360  1.00 69.81           C  
ATOM    279  CE2 PHE A  42      15.581  -1.638  25.482  1.00 69.81           C  
ATOM    280  CZ  PHE A  42      15.454  -0.448  24.763  1.00 69.81           C  
ATOM    281  N   TYR A  43      15.618  -6.748  21.022  1.00 56.11           N  
ATOM    282  CA  TYR A  43      16.054  -7.809  20.109  1.00 56.11           C  
ATOM    283  C   TYR A  43      15.135  -7.951  18.899  1.00 56.11           C  
ATOM    284  O   TYR A  43      15.596  -7.847  17.751  1.00 56.11           O  
ATOM    285  CB  TYR A  43      16.216  -9.161  20.829  1.00 50.39           C  
ATOM    286  CG  TYR A  43      17.483  -9.307  21.638  1.00 66.51           C  
ATOM    287  CD1 TYR A  43      18.717  -8.861  21.156  1.00 66.51           C  
ATOM    288  CD2 TYR A  43      17.462  -9.915  22.894  1.00 66.51           C  
ATOM    289  CE1 TYR A  43      19.888  -8.999  21.895  1.00 66.51           C  
ATOM    290  CE2 TYR A  43      18.619 -10.060  23.653  1.00 66.51           C  
ATOM    291  CZ  TYR A  43      19.831  -9.605  23.148  1.00 66.51           C  
ATOM    292  OH  TYR A  43      20.948  -9.769  23.919  1.00 79.84           O  
ATOM    293  N   ALA A  44      13.865  -8.182  19.153  1.00 61.21           N  
ATOM    294  CA  ALA A  44      12.824  -8.348  18.136  1.00 61.21           C  
ATOM    295  C   ALA A  44      12.778  -7.150  17.190  1.00 61.21           C  
ATOM    296  O   ALA A  44      12.896  -7.288  15.959  1.00 61.21           O  
ATOM    297  CB  ALA A  44      11.466  -8.539  18.806  1.00 55.49           C  
ATOM    298  N   ILE A  45      12.622  -5.986  17.809  1.00 68.36           N  
ATOM    299  CA  ILE A  45      12.555  -4.718  17.073  1.00 68.36           C  
ATOM    300  C   ILE A  45      13.761  -4.565  16.153  1.00 68.36           C  
ATOM    301  O   ILE A  45      13.572  -4.243  14.967  1.00 68.36           O  
ATOM    302  CB  ILE A  45      12.332  -3.498  18.034  1.00 62.64           C  
ATOM    303  CG1 ILE A  45      10.915  -3.588  18.656  1.00 82.37           C  
ATOM    304  CG2 ILE A  45      12.554  -2.130  17.336  1.00 82.37           C  
ATOM    305  CD1 ILE A  45      10.592  -2.518  19.732  1.00 92.09           C  
ATOM    306  N   THR A  46      14.950  -4.801  16.675  1.00 72.18           N  
ATOM    307  CA  THR A  46      16.202  -4.687  15.923  1.00 72.18           C  
ATOM    308  C   THR A  46      16.530  -5.867  15.023  1.00 72.18           C  
ATOM    309  O   THR A  46      17.530  -5.783  14.278  1.00 72.18           O  
ATOM    310  CB  THR A  46      17.402  -4.293  16.878  1.00 66.46           C  
ATOM    311  OG1 THR A  46      18.432  -3.707  16.018  1.00 86.19           O  
ATOM    312  CG2 THR A  46      17.955  -5.442  17.718  1.00 86.19           C  
ATOM    313  N   THR A  47      15.776  -6.943  15.075  1.00 71.42           N  
ATOM    314  CA  THR A  47      16.000  -8.131  14.242  1.00 71.42           C  
ATOM    315  C   THR A  47      15.108  -8.066  13.001  1.00 71.42           C  
ATOM    316  O   THR A  47      15.495  -8.416  11.863  1.00 71.42           O  
ATOM    317  CB  THR A  47      15.816  -9.482  15.027  1.00 65.70           C  
ATOM    318  OG1 THR A  47      16.935  -9.578  15.962  1.00 85.43           O  
ATOM    319  CG2 THR A  47      15.758 -10.725  14.128  1.00 85.43           C  
ATOM    320  N   LEU A  48      13.913  -7.553  13.257  1.00 65.78           N  
ATOM    321  CA  LEU A  48      12.896  -7.389  12.199  1.00 65.78           C  
ATOM    322  C   LEU A  48      13.463  -6.521  11.081  1.00 65.78           C  
ATOM    323  O   LEU A  48      13.335  -6.886   9.896  1.00 65.78           O  
ATOM    324  CB  LEU A  48      11.621  -6.908  12.889  1.00 60.06           C  
ATOM    325  CG  LEU A  48      10.310  -7.504  12.400  1.00 79.79           C  
ATOM    326  CD1 LEU A  48       9.462  -7.958  13.585  1.00 89.51           C  
ATOM    327  CD2 LEU A  48       9.558  -6.445  11.599  1.00 89.51           C  
ATOM    328  N   VAL A  49      14.084  -5.416  11.458  1.00 55.57           N  
ATOM    329  CA  VAL A  49      14.699  -4.463  10.521  1.00 55.57           C  
ATOM    330  C   VAL A  49      15.521  -5.230   9.489  1.00 55.57           C  
ATOM    331  O   VAL A  49      15.118  -5.321   8.310  1.00 55.57           O  
ATOM    332  CB  VAL A  49      15.448  -3.346  11.263  1.00 49.85           C  
ATOM    333  CG1 VAL A  49      15.630  -2.102  10.400  1.00 69.58           C  
ATOM    334  CG2 VAL A  49      14.801  -2.974  12.586  1.00 69.58           C  
ATOM    335  N   PRO A  50      16.624  -5.814   9.943  1.00 43.31           N  
ATOM    336  CA  PRO A  50      17.510  -6.609   9.088  1.00 43.31           C  
ATOM    337  C   PRO A  50      16.686  -7.578   8.252  1.00 43.31           C  
ATOM    338  O   PRO A  50      16.915  -7.612   7.029  1.00 43.31           O  
ATOM    339  CB  PRO A  50      18.494  -7.320  10.000  1.00 37.59           C  
ATOM    340  CG  PRO A  50      18.137  -6.934  11.399  1.00 37.59           C  
ATOM    341  CD  PRO A  50      17.164  -5.769  11.303  1.00 37.59           C  
ATOM    342  N   ALA A  51      15.784  -8.321   8.892  1.00 32.06           N  
ATOM    343  CA  ALA A  51      14.946  -9.260   8.111  1.00 32.06           C  
ATOM    344  C   ALA A  51      14.424  -8.556   6.855  1.00 32.06           C  
ATOM    345  O   ALA A  51      14.766  -8.877   5.694  1.00 32.06           O  
ATOM    346  CB  ALA A  51      13.818  -9.788   8.987  1.00 26.34           C  
ATOM    347  N   ILE A  52      13.605  -7.540   7.106  1.00 24.92           N  
ATOM    348  CA  ILE A  52      12.978  -6.721   6.064  1.00 24.92           C  
ATOM    349  C   ILE A  52      13.974  -6.318   4.991  1.00 24.92           C  
ATOM    350  O   ILE A  52      13.793  -6.619   3.799  1.00 24.92           O  
ATOM    351  CB  ILE A  52      12.252  -5.488   6.704  1.00 19.20           C  
ATOM    352  CG1 ILE A  52      11.268  -6.020   7.780  1.00 38.93           C  
ATOM    353  CG2 ILE A  52      11.532  -4.611   5.650  1.00 38.93           C  
ATOM    354  CD1 ILE A  52      10.931  -4.974   8.876  1.00 48.65           C  
ATOM    355  N   ALA A  53      15.032  -5.670   5.445  1.00 24.16           N  
ATOM    356  CA  ALA A  53      16.111  -5.190   4.564  1.00 24.16           C  
ATOM    357  C   ALA A  53      16.637  -6.302   3.664  1.00 24.16           C  
ATOM    358  O   ALA A  53      16.877  -6.042   2.470  1.00 24.16           O  
ATOM    359  CB  ALA A  53      17.197  -4.501   5.374  1.00 18.44           C  
ATOM    360  N   PHE A  54      16.817  -7.491   4.207  1.00 28.92           N  
ATOM    361  CA  PHE A  54      17.291  -8.654   3.459  1.00 28.92           C  
ATOM    362  C   PHE A  54      16.284  -8.949   2.333  1.00 28.92           C  
ATOM    363  O   PHE A  54      16.660  -8.952   1.150  1.00 28.92           O  
ATOM    364  CB  PHE A  54      17.497  -9.912   4.308  1.00 23.20           C  
ATOM    365  CG  PHE A  54      17.439 -11.186   3.504  1.00 39.32           C  
ATOM    366  CD1 PHE A  54      18.551 -11.592   2.766  1.00 39.32           C  
ATOM    367  CD2 PHE A  54      16.268 -11.938   3.465  1.00 39.32           C  
ATOM    368  CE1 PHE A  54      18.513 -12.750   2.009  1.00 39.32           C  
ATOM    369  CE2 PHE A  54      16.208 -13.104   2.701  1.00 39.32           C  
ATOM    370  CZ  PHE A  54      17.340 -13.509   1.973  1.00 39.32           C  
ATOM    371  N   THR A  55      15.046  -9.187   2.768  1.00 37.54           N  
ATOM    372  CA  THR A  55      13.974  -9.517   1.802  1.00 37.54           C  
ATOM    373  C   THR A  55      14.029  -8.543   0.626  1.00 37.54           C  
ATOM    374  O   THR A  55      14.258  -8.899  -0.545  1.00 37.54           O  
ATOM    375  CB  THR A  55      12.531  -9.582   2.436  1.00 31.82           C  
ATOM    376  OG1 THR A  55      12.698  -9.684   3.886  1.00 51.55           O  
ATOM    377  CG2 THR A  55      11.673 -10.739   1.904  1.00 51.55           C  
ATOM    378  N   MET A  56      13.861  -7.283   1.002  1.00 47.76           N  
ATOM    379  CA  MET A  56      13.877  -6.161   0.062  1.00 47.76           C  
ATOM    380  C   MET A  56      15.110  -6.221  -0.827  1.00 47.76           C  
ATOM    381  O   MET A  56      14.957  -6.052  -2.049  1.00 47.76           O  
ATOM    382  CB  MET A  56      13.717  -4.837   0.802  1.00 42.04           C  
ATOM    383  CG  MET A  56      12.782  -3.961  -0.002  1.00 61.77           C  
ATOM    384  SD  MET A  56      11.174  -4.826  -0.084  1.00 71.49           S  
ATOM    385  CE  MET A  56      10.511  -4.126  -1.605  1.00106.87           C  
ATOM    386  N   TYR A  57      16.277  -6.468  -0.265  1.00 55.00           N  
ATOM    387  CA  TYR A  57      17.543  -6.566  -0.997  1.00 55.00           C  
ATOM    388  C   TYR A  57      17.512  -7.671  -2.046  1.00 55.00           C  
ATOM    389  O   TYR A  57      18.087  -7.482  -3.136  1.00 55.00           O  
ATOM    390  CB  TYR A  57      18.758  -6.681  -0.058  1.00 49.28           C  
ATOM    391  CG  TYR A  57      19.438  -5.340   0.139  1.00 65.40           C  
ATOM    392  CD1 TYR A  57      18.863  -4.343   0.930  1.00 65.40           C  
ATOM    393  CD2 TYR A  57      20.653  -5.059  -0.485  1.00 65.40           C  
ATOM    394  CE1 TYR A  57      19.486  -3.112   1.104  1.00 65.40           C  
ATOM    395  CE2 TYR A  57      21.294  -3.835  -0.320  1.00 65.40           C  
ATOM    396  CZ  TYR A  57      20.706  -2.860   0.475  1.00 65.40           C  
ATOM    397  OH  TYR A  57      21.354  -1.663   0.616  1.00 78.73           O  
ATOM    398  N   LEU A  58      16.859  -8.777  -1.723  1.00 54.09           N  
ATOM    399  CA  LEU A  58      16.719  -9.911  -2.652  1.00 54.09           C  
ATOM    400  C   LEU A  58      15.779  -9.480  -3.782  1.00 54.09           C  
ATOM    401  O   LEU A  58      15.977  -9.836  -4.958  1.00 54.09           O  
ATOM    402  CB  LEU A  58      16.299 -11.154  -1.883  1.00 48.37           C  
ATOM    403  CG  LEU A  58      16.055 -12.451  -2.627  1.00 68.10           C  
ATOM    404  CD1 LEU A  58      17.168 -12.793  -3.606  1.00 77.82           C  
ATOM    405  CD2 LEU A  58      15.960 -13.568  -1.584  1.00 77.82           C  
ATOM    406  N   SER A  59      14.777  -8.698  -3.399  1.00 42.65           N  
ATOM    407  CA  SER A  59      13.774  -8.144  -4.310  1.00 42.65           C  
ATOM    408  C   SER A  59      14.403  -7.149  -5.296  1.00 42.65           C  
ATOM    409  O   SER A  59      13.982  -7.018  -6.449  1.00 42.65           O  
ATOM    410  CB  SER A  59      12.662  -7.394  -3.588  1.00 36.93           C  
ATOM    411  OG  SER A  59      12.282  -7.973  -2.363  1.00 56.66           O  
ATOM    412  N   MET A  60      15.373  -6.424  -4.796  1.00 29.63           N  
ATOM    413  CA  MET A  60      16.152  -5.393  -5.476  1.00 29.63           C  
ATOM    414  C   MET A  60      17.140  -6.029  -6.450  1.00 29.63           C  
ATOM    415  O   MET A  60      17.279  -5.594  -7.604  1.00 29.63           O  
ATOM    416  CB  MET A  60      16.827  -4.530  -4.417  1.00 23.91           C  
ATOM    417  CG  MET A  60      17.107  -3.128  -4.888  1.00 43.64           C  
ATOM    418  SD  MET A  60      16.804  -2.000  -3.478  1.00 53.36           S  
ATOM    419  CE  MET A  60      18.080  -2.543  -2.330  1.00 88.74           C  
ATOM    420  N   LEU A  61      17.801  -7.056  -5.951  1.00 26.77           N  
ATOM    421  CA  LEU A  61      18.798  -7.835  -6.693  1.00 26.77           C  
ATOM    422  C   LEU A  61      18.171  -8.583  -7.871  1.00 26.77           C  
ATOM    423  O   LEU A  61      18.730  -8.595  -8.984  1.00 26.77           O  
ATOM    424  CB  LEU A  61      19.525  -8.742  -5.689  1.00 21.05           C  
ATOM    425  CG  LEU A  61      20.486  -9.775  -6.256  1.00 40.78           C  
ATOM    426  CD1 LEU A  61      21.614  -9.121  -7.046  1.00 50.50           C  
ATOM    427  CD2 LEU A  61      21.067 -10.572  -5.089  1.00 50.50           C  
ATOM    428  N   LEU A  62      17.033  -9.205  -7.601  1.00 42.46           N  
ATOM    429  CA  LEU A  62      16.286  -9.968  -8.623  1.00 42.46           C  
ATOM    430  C   LEU A  62      15.515  -9.000  -9.518  1.00 42.46           C  
ATOM    431  O   LEU A  62      15.402  -9.187 -10.741  1.00 42.46           O  
ATOM    432  CB  LEU A  62      15.497 -11.051  -7.892  1.00 36.74           C  
ATOM    433  CG  LEU A  62      16.174 -12.373  -7.570  1.00 56.47           C  
ATOM    434  CD1 LEU A  62      17.583 -12.221  -7.009  1.00 66.19           C  
ATOM    435  CD2 LEU A  62      15.332 -13.117  -6.529  1.00 66.19           C  
ATOM    436  N   GLY A  63      14.995  -7.958  -8.908  1.00 71.69           N  
ATOM    437  CA  GLY A  63      14.231  -6.868  -9.493  1.00 71.69           C  
ATOM    438  C   GLY A  63      12.979  -7.281 -10.247  1.00 71.69           C  
ATOM    439  O   GLY A  63      12.968  -7.240 -11.491  1.00 71.69           O  
ATOM    440  N   TYR A  64      11.948  -7.644  -9.505  1.00106.06           N  
ATOM    441  CA  TYR A  64      10.662  -8.081 -10.069  1.00106.06           C  
ATOM    442  C   TYR A  64       9.821  -6.888 -10.518  1.00106.06           C  
ATOM    443  O   TYR A  64      10.287  -5.739 -10.515  1.00106.06           O  
ATOM    444  CB  TYR A  64       9.904  -8.975  -9.076  1.00100.34           C  
ATOM    445  CG  TYR A  64       9.067  -8.270  -8.037  1.00116.46           C  
ATOM    446  CD1 TYR A  64       9.635  -7.471  -7.041  1.00116.46           C  
ATOM    447  CD2 TYR A  64       7.678  -8.408  -8.051  1.00116.46           C  
ATOM    448  CE1 TYR A  64       8.844  -6.830  -6.089  1.00116.46           C  
ATOM    449  CE2 TYR A  64       6.872  -7.776  -7.109  1.00116.46           C  
ATOM    450  CZ  TYR A  64       7.460  -6.988  -6.129  1.00116.46           C  
ATOM    451  OH  TYR A  64       6.641  -6.380  -5.220  1.00129.79           O  
ATOM    452  N   GLY A  65       8.593  -7.196 -10.897  1.00137.97           N  
ATOM    453  CA  GLY A  65       7.610  -6.210 -11.360  1.00137.97           C  
ATOM    454  C   GLY A  65       7.723  -6.026 -12.873  1.00137.97           C  
ATOM    455  O   GLY A  65       7.387  -6.921 -13.661  1.00137.97           O  
ATOM    456  N   LEU A  66       8.193  -4.844 -13.227  1.00162.87           N  
ATOM    457  CA  LEU A  66       8.393  -4.436 -14.626  1.00162.87           C  
ATOM    458  C   LEU A  66       9.553  -3.440 -14.682  1.00162.87           C  
ATOM    459  O   LEU A  66      10.017  -2.969 -13.629  1.00162.87           O  
ATOM    460  CB  LEU A  66       7.065  -3.980 -15.204  1.00157.15           C  
ATOM    461  CG  LEU A  66       6.359  -2.729 -14.740  1.00176.88           C  
ATOM    462  CD1 LEU A  66       5.195  -2.393 -15.675  1.00186.60           C  
ATOM    463  CD2 LEU A  66       5.808  -2.919 -13.329  1.00186.60           C  
ATOM    464  N   THR A  67      10.001  -3.157 -15.893  1.00176.97           N  
ATOM    465  CA  THR A  67      11.118  -2.234 -16.128  1.00176.97           C  
ATOM    466  C   THR A  67      10.698  -0.994 -16.908  1.00176.97           C  
ATOM    467  O   THR A  67      11.019  -0.827 -18.095  1.00176.97           O  
ATOM    468  CB  THR A  67      12.339  -2.969 -16.813  1.00171.25           C  
ATOM    469  OG1 THR A  67      12.638  -4.133 -15.978  1.00190.98           O  
ATOM    470  CG2 THR A  67      13.582  -2.094 -17.005  1.00190.98           C  
ATOM    471  N   MET A  68       9.981  -0.133 -16.208  1.00176.47           N  
ATOM    472  CA  MET A  68       9.478   1.142 -16.749  1.00176.47           C  
ATOM    473  C   MET A  68      10.249   2.268 -16.052  1.00176.47           C  
ATOM    474  O   MET A  68      10.741   2.061 -14.929  1.00176.47           O  
ATOM    475  CB  MET A  68       7.971   1.257 -16.604  1.00170.75           C  
ATOM    476  CG  MET A  68       7.252   0.348 -17.570  1.00190.48           C  
ATOM    477  SD  MET A  68       5.456   0.623 -17.375  1.00200.20           S  
ATOM    478  CE  MET A  68       4.829  -0.487 -18.650  1.00235.58           C  
ATOM    479  N   VAL A  69      10.346   3.401 -16.722  1.00162.43           N  
ATOM    480  CA  VAL A  69      11.063   4.568 -16.193  1.00162.43           C  
ATOM    481  C   VAL A  69      10.111   5.697 -15.792  1.00162.43           C  
ATOM    482  O   VAL A  69       9.247   6.116 -16.576  1.00162.43           O  
ATOM    483  CB  VAL A  69      12.136   5.053 -17.191  1.00156.71           C  
ATOM    484  CG1 VAL A  69      13.295   4.078 -17.352  1.00176.44           C  
ATOM    485  CG2 VAL A  69      11.544   5.403 -18.548  1.00176.44           C  
ATOM    486  N   PRO A  70      10.322   6.167 -14.568  1.00155.25           N  
ATOM    487  CA  PRO A  70       9.526   7.266 -14.004  1.00155.25           C  
ATOM    488  C   PRO A  70      10.000   8.584 -14.610  1.00155.25           C  
ATOM    489  O   PRO A  70       9.204   9.434 -15.032  1.00155.25           O  
ATOM    490  CB  PRO A  70       9.739   7.165 -12.504  1.00149.53           C  
ATOM    491  CG  PRO A  70      11.043   6.448 -12.319  1.00149.53           C  
ATOM    492  CD  PRO A  70      11.337   5.704 -13.610  1.00149.53           C  
ATOM    493  N   PHE A  71      11.315   8.710 -14.645  1.00180.18           N  
ATOM    494  CA  PHE A  71      12.020   9.881 -15.187  1.00180.18           C  
ATOM    495  C   PHE A  71      13.522   9.572 -15.247  1.00180.18           C  
ATOM    496  O   PHE A  71      14.262   9.777 -14.274  1.00180.18           O  
ATOM    497  CB  PHE A  71      11.710  11.159 -14.422  1.00174.46           C  
ATOM    498  CG  PHE A  71      12.500  12.368 -14.825  1.00190.58           C  
ATOM    499  CD1 PHE A  71      12.211  13.023 -16.023  1.00190.58           C  
ATOM    500  CD2 PHE A  71      13.526  12.846 -14.011  1.00190.58           C  
ATOM    501  CE1 PHE A  71      12.931  14.142 -16.413  1.00190.58           C  
ATOM    502  CE2 PHE A  71      14.265  13.974 -14.384  1.00190.58           C  
ATOM    503  CZ  PHE A  71      13.958  14.620 -15.595  1.00190.58           C  
ATOM    504  N   GLY A  72      13.920   9.084 -16.408  1.00249.77           N  
ATOM    505  CA  GLY A  72      15.316   8.720 -16.687  1.00249.77           C  
ATOM    506  C   GLY A  72      15.367   7.506 -17.616  1.00249.77           C  
ATOM    507  O   GLY A  72      14.401   7.201 -18.331  1.00249.77           O  
ATOM    508  N   GLY A  73      16.511   6.847 -17.573  1.00325.94           N  
ATOM    509  CA  GLY A  73      16.784   5.650 -18.380  1.00325.94           C  
ATOM    510  C   GLY A  73      17.242   4.508 -17.470  1.00325.94           C  
ATOM    511  O   GLY A  73      17.939   3.578 -17.900  1.00325.94           O  
ATOM    512  N   GLU A  74      16.829   4.621 -16.222  1.00357.88           N  
ATOM    513  CA  GLU A  74      17.139   3.652 -15.164  1.00357.88           C  
ATOM    514  C   GLU A  74      15.848   3.015 -14.662  1.00357.88           C  
ATOM    515  O   GLU A  74      14.792   3.665 -14.610  1.00357.88           O  
ATOM    516  CB  GLU A  74      17.868   4.313 -14.000  1.00352.16           C  
ATOM    517  CG  GLU A  74      19.126   5.117 -14.303  1.00371.89           C  
ATOM    518  CD  GLU A  74      19.496   6.207 -13.346  1.00381.61           C  
ATOM    519  OE1 GLU A  74      18.512   6.894 -12.993  1.00416.99           O  
ATOM    520  OE2 GLU A  74      20.632   6.419 -12.952  1.00416.99           O  
ATOM    521  N   GLN A  75      15.949   1.753 -14.304  1.00311.21           N  
ATOM    522  CA  GLN A  75      14.851   0.916 -13.807  1.00311.21           C  
ATOM    523  C   GLN A  75      14.117   1.529 -12.620  1.00311.21           C  
ATOM    524  O   GLN A  75      14.496   2.589 -12.103  1.00311.21           O  
ATOM    525  CB  GLN A  75      15.356  -0.500 -13.494  1.00305.49           C  
ATOM    526  CG  GLN A  75      16.041  -1.150 -14.683  1.00325.22           C  
ATOM    527  CD  GLN A  75      16.420  -2.591 -14.460  1.00334.94           C  
ATOM    528  OE1 GLN A  75      17.543  -2.924 -14.091  1.00370.32           O  
ATOM    529  NE2 GLN A  75      15.453  -3.475 -14.697  1.00370.32           N  
ATOM    530  N   ASN A  76      13.064   0.835 -12.197  1.00217.07           N  
ATOM    531  CA  ASN A  76      12.219   1.260 -11.078  1.00217.07           C  
ATOM    532  C   ASN A  76      12.049   0.311  -9.902  1.00217.07           C  
ATOM    533  O   ASN A  76      11.598   0.786  -8.834  1.00217.07           O  
ATOM    534  CB  ASN A  76      10.862   1.748 -11.605  1.00211.35           C  
ATOM    535  CG  ASN A  76       9.934   0.679 -12.133  1.00231.08           C  
ATOM    536  OD1 ASN A  76      10.332  -0.455 -12.431  1.00240.80           O  
ATOM    537  ND2 ASN A  76       8.653   1.035 -12.264  1.00240.80           N  
ATOM    538  N   PRO A  77      12.381  -0.956 -10.053  1.00122.99           N  
ATOM    539  CA  PRO A  77      12.249  -1.940  -8.972  1.00122.99           C  
ATOM    540  C   PRO A  77      13.145  -1.609  -7.788  1.00122.99           C  
ATOM    541  O   PRO A  77      12.729  -1.647  -6.619  1.00122.99           O  
ATOM    542  CB  PRO A  77      12.611  -3.278  -9.612  1.00117.27           C  
ATOM    543  CG  PRO A  77      13.495  -2.906 -10.775  1.00117.27           C  
ATOM    544  CD  PRO A  77      12.911  -1.589 -11.268  1.00117.27           C  
ATOM    545  N   ILE A  78      14.379  -1.289  -8.125  1.00 66.05           N  
ATOM    546  CA  ILE A  78      15.435  -0.923  -7.173  1.00 66.05           C  
ATOM    547  C   ILE A  78      14.925   0.129  -6.195  1.00 66.05           C  
ATOM    548  O   ILE A  78      14.761  -0.132  -4.989  1.00 66.05           O  
ATOM    549  CB  ILE A  78      16.703  -0.461  -7.983  1.00 60.33           C  
ATOM    550  CG1 ILE A  78      17.155  -1.649  -8.873  1.00 80.06           C  
ATOM    551  CG2 ILE A  78      17.849   0.075  -7.096  1.00 80.06           C  
ATOM    552  CD1 ILE A  78      17.633  -1.247 -10.292  1.00 89.78           C  
ATOM    553  N   TYR A  79      14.652   1.300  -6.750  1.00 41.46           N  
ATOM    554  CA  TYR A  79      14.153   2.433  -5.970  1.00 41.46           C  
ATOM    555  C   TYR A  79      12.984   1.997  -5.084  1.00 41.46           C  
ATOM    556  O   TYR A  79      13.084   2.064  -3.842  1.00 41.46           O  
ATOM    557  CB  TYR A  79      13.726   3.624  -6.822  1.00 35.74           C  
ATOM    558  CG  TYR A  79      14.461   4.005  -8.073  1.00 51.86           C  
ATOM    559  CD1 TYR A  79      15.818   3.758  -8.283  1.00 51.86           C  
ATOM    560  CD2 TYR A  79      13.754   4.679  -9.078  1.00 51.86           C  
ATOM    561  CE1 TYR A  79      16.446   4.145  -9.464  1.00 51.86           C  
ATOM    562  CE2 TYR A  79      14.365   5.075 -10.261  1.00 51.86           C  
ATOM    563  CZ  TYR A  79      15.714   4.807 -10.447  1.00 51.86           C  
ATOM    564  OH  TYR A  79      16.274   5.215 -11.624  1.00 65.19           O  
ATOM    565  N   TRP A  80      11.913   1.537  -5.718  1.00 33.97           N  
ATOM    566  CA  TRP A  80      10.692   1.095  -5.011  1.00 33.97           C  
ATOM    567  C   TRP A  80      11.086   0.279  -3.777  1.00 33.97           C  
ATOM    568  O   TRP A  80      10.670   0.575  -2.636  1.00 33.97           O  
ATOM    569  CB  TRP A  80       9.670   0.464  -5.921  1.00 28.25           C  
ATOM    570  CG  TRP A  80       9.279  -0.956  -5.999  1.00 44.37           C  
ATOM    571  CD1 TRP A  80       9.276  -1.913  -5.015  1.00 44.37           C  
ATOM    572  CD2 TRP A  80       8.737  -1.625  -7.160  1.00 44.37           C  
ATOM    573  NE1 TRP A  80       8.814  -3.117  -5.483  1.00 44.37           N  
ATOM    574  CE2 TRP A  80       8.471  -2.966  -6.797  1.00 44.37           C  
ATOM    575  CE3 TRP A  80       8.472  -1.212  -8.463  1.00 44.37           C  
ATOM    576  CZ2 TRP A  80       7.953  -3.893  -7.691  1.00 44.37           C  
ATOM    577  CZ3 TRP A  80       7.958  -2.137  -9.352  1.00 44.37           C  
ATOM    578  CH2 TRP A  80       7.700  -3.455  -8.983  1.00 44.37           C  
ATOM    579  N   ALA A  81      11.900  -0.737  -4.026  1.00 30.92           N  
ATOM    580  CA  ALA A  81      12.399  -1.624  -2.969  1.00 30.92           C  
ATOM    581  C   ALA A  81      13.011  -0.770  -1.859  1.00 30.92           C  
ATOM    582  O   ALA A  81      12.596  -0.883  -0.684  1.00 30.92           O  
ATOM    583  CB  ALA A  81      13.366  -2.640  -3.554  1.00 25.20           C  
ATOM    584  N   ARG A  82      13.947   0.091  -2.240  1.00 29.98           N  
ATOM    585  CA  ARG A  82      14.608   0.973  -1.267  1.00 29.98           C  
ATOM    586  C   ARG A  82      13.558   1.623  -0.366  1.00 29.98           C  
ATOM    587  O   ARG A  82      13.600   1.434   0.866  1.00 29.98           O  
ATOM    588  CB  ARG A  82      15.482   2.045  -1.901  1.00 24.26           C  
ATOM    589  CG  ARG A  82      16.446   1.564  -2.970  1.00 43.99           C  
ATOM    590  CD  ARG A  82      17.530   2.554  -3.233  1.00 53.71           C  
ATOM    591  NE  ARG A  82      17.966   2.516  -4.621  1.00 89.09           N  
ATOM    592  CZ  ARG A  82      19.213   2.739  -5.035  1.00 51.40           C  
ATOM    593  NH1 ARG A  82      20.214   3.006  -4.201  1.00 94.86           N  
ATOM    594  NH2 ARG A  82      19.460   2.697  -6.345  1.00 94.86           N  
ATOM    595  N   TYR A  83      12.625   2.335  -0.992  1.00 31.39           N  
ATOM    596  CA  TYR A  83      11.558   3.014  -0.235  1.00 31.39           C  
ATOM    597  C   TYR A  83      10.818   2.057   0.679  1.00 31.39           C  
ATOM    598  O   TYR A  83      10.547   2.519   1.802  1.00 31.39           O  
ATOM    599  CB  TYR A  83      10.643   3.901  -1.101  1.00 25.67           C  
ATOM    600  CG  TYR A  83      11.492   4.885  -1.887  1.00 41.79           C  
ATOM    601  CD1 TYR A  83      12.232   5.888  -1.261  1.00 41.79           C  
ATOM    602  CD2 TYR A  83      11.570   4.778  -3.272  1.00 41.79           C  
ATOM    603  CE1 TYR A  83      13.024   6.764  -2.002  1.00 41.79           C  
ATOM    604  CE2 TYR A  83      12.357   5.639  -4.028  1.00 41.79           C  
ATOM    605  CZ  TYR A  83      13.085   6.631  -3.385  1.00 41.79           C  
ATOM    606  OH  TYR A  83      13.835   7.455  -4.175  1.00 55.12           O  
ATOM    607  N   ALA A  84      10.524   0.832   0.283  1.00 35.39           N  
ATOM    608  CA  ALA A  84       9.832  -0.113   1.188  1.00 35.39           C  
ATOM    609  C   ALA A  84      10.693  -0.342   2.438  1.00 35.39           C  
ATOM    610  O   ALA A  84      10.270  -0.230   3.610  1.00 35.39           O  
ATOM    611  CB  ALA A  84       9.529  -1.413   0.459  1.00 29.67           C  
ATOM    612  N   ASP A  85      11.948  -0.650   2.135  1.00 41.43           N  
ATOM    613  CA  ASP A  85      12.998  -0.922   3.126  1.00 41.43           C  
ATOM    614  C   ASP A  85      13.035   0.178   4.188  1.00 41.43           C  
ATOM    615  O   ASP A  85      12.775  -0.090   5.371  1.00 41.43           O  
ATOM    616  CB  ASP A  85      14.346  -1.125   2.439  1.00 35.71           C  
ATOM    617  CG  ASP A  85      15.445  -1.663   3.329  1.00 55.44           C  
ATOM    618  OD1 ASP A  85      15.121  -2.089   4.457  1.00 65.16           O  
ATOM    619  OD2 ASP A  85      16.621  -1.676   2.930  1.00 65.16           O  
ATOM    620  N   TRP A  86      13.329   1.380   3.726  1.00 45.78           N  
ATOM    621  CA  TRP A  86      13.422   2.562   4.601  1.00 45.78           C  
ATOM    622  C   TRP A  86      12.092   2.830   5.293  1.00 45.78           C  
ATOM    623  O   TRP A  86      12.061   3.125   6.502  1.00 45.78           O  
ATOM    624  CB  TRP A  86      14.013   3.759   3.860  1.00 40.06           C  
ATOM    625  CG  TRP A  86      15.189   3.461   2.993  1.00 56.18           C  
ATOM    626  CD1 TRP A  86      16.112   2.459   3.133  1.00 56.18           C  
ATOM    627  CD2 TRP A  86      15.594   4.194   1.824  1.00 56.18           C  
ATOM    628  NE1 TRP A  86      17.051   2.513   2.134  1.00 56.18           N  
ATOM    629  CE2 TRP A  86      16.755   3.568   1.318  1.00 56.18           C  
ATOM    630  CE3 TRP A  86      15.078   5.305   1.168  1.00 56.18           C  
ATOM    631  CZ2 TRP A  86      17.412   4.022   0.183  1.00 56.18           C  
ATOM    632  CZ3 TRP A  86      15.728   5.761   0.038  1.00 56.18           C  
ATOM    633  CH2 TRP A  86      16.871   5.134  -0.448  1.00 56.18           C  
ATOM    634  N   LEU A  87      11.000   2.694   4.568  1.00 43.87           N  
ATOM    635  CA  LEU A  87       9.636   2.895   5.040  1.00 43.87           C  
ATOM    636  C   LEU A  87       9.292   2.046   6.263  1.00 43.87           C  
ATOM    637  O   LEU A  87       8.488   2.571   7.063  1.00 43.87           O  
ATOM    638  CB  LEU A  87       8.629   2.700   3.902  1.00 38.15           C  
ATOM    639  CG  LEU A  87       7.148   2.833   4.205  1.00 57.88           C  
ATOM    640  CD1 LEU A  87       6.788   4.237   4.678  1.00 67.60           C  
ATOM    641  CD2 LEU A  87       6.365   2.498   2.934  1.00 67.60           C  
ATOM    642  N   PHE A  88       9.817   0.836   6.377  1.00 33.39           N  
ATOM    643  CA  PHE A  88       9.470   0.045   7.596  1.00 33.39           C  
ATOM    644  C   PHE A  88      10.606   0.218   8.611  1.00 33.39           C  
ATOM    645  O   PHE A  88      10.431   0.542   9.809  1.00 33.39           O  
ATOM    646  CB  PHE A  88       9.092  -1.384   7.250  1.00 27.67           C  
ATOM    647  CG  PHE A  88       7.834  -1.498   6.433  1.00 43.79           C  
ATOM    648  CD1 PHE A  88       6.584  -1.445   7.058  1.00 43.79           C  
ATOM    649  CD2 PHE A  88       7.900  -1.650   5.048  1.00 43.79           C  
ATOM    650  CE1 PHE A  88       5.414  -1.549   6.319  1.00 43.79           C  
ATOM    651  CE2 PHE A  88       6.731  -1.756   4.283  1.00 43.79           C  
ATOM    652  CZ  PHE A  88       5.486  -1.700   4.932  1.00 43.79           C  
ATOM    653  N   THR A  89      11.798   0.029   8.061  1.00 20.79           N  
ATOM    654  CA  THR A  89      13.050   0.140   8.800  1.00 20.79           C  
ATOM    655  C   THR A  89      13.029   1.353   9.732  1.00 20.79           C  
ATOM    656  O   THR A  89      12.928   1.214  10.956  1.00 20.79           O  
ATOM    657  CB  THR A  89      14.342   0.231   7.890  1.00 15.07           C  
ATOM    658  OG1 THR A  89      14.571  -1.106   7.347  1.00 34.80           O  
ATOM    659  CG2 THR A  89      15.564   0.777   8.643  1.00 34.80           C  
ATOM    660  N   THR A  90      13.133   2.508   9.091  1.00 14.76           N  
ATOM    661  CA  THR A  90      13.169   3.812   9.780  1.00 14.76           C  
ATOM    662  C   THR A  90      12.265   3.776  10.999  1.00 14.76           C  
ATOM    663  O   THR A  90      12.766   3.752  12.140  1.00 14.76           O  
ATOM    664  CB  THR A  90      12.974   5.033   8.813  1.00  9.04           C  
ATOM    665  OG1 THR A  90      13.945   4.867   7.721  1.00 28.77           O  
ATOM    666  CG2 THR A  90      13.190   6.398   9.472  1.00 28.77           C  
ATOM    667  N   PRO A  91      10.965   3.725  10.763  1.00 21.51           N  
ATOM    668  CA  PRO A  91       9.978   3.646  11.840  1.00 21.51           C  
ATOM    669  C   PRO A  91      10.455   2.751  12.976  1.00 21.51           C  
ATOM    670  O   PRO A  91      10.585   3.251  14.107  1.00 21.51           O  
ATOM    671  CB  PRO A  91       8.738   3.042  11.170  1.00 15.79           C  
ATOM    672  CG  PRO A  91       8.824   3.531   9.756  1.00 15.79           C  
ATOM    673  CD  PRO A  91      10.303   3.737   9.450  1.00 15.79           C  
ATOM    674  N   LEU A  92      10.707   1.483  12.651  1.00 37.30           N  
ATOM    675  CA  LEU A  92      11.156   0.527  13.682  1.00 37.30           C  
ATOM    676  C   LEU A  92      12.402   0.941  14.450  1.00 37.30           C  
ATOM    677  O   LEU A  92      12.440   0.792  15.691  1.00 37.30           O  
ATOM    678  CB  LEU A  92      11.231  -0.867  13.038  1.00 31.58           C  
ATOM    679  CG  LEU A  92       9.931  -1.658  12.991  1.00 51.31           C  
ATOM    680  CD1 LEU A  92       8.886  -0.961  12.130  1.00 61.03           C  
ATOM    681  CD2 LEU A  92      10.223  -3.050  12.437  1.00 61.03           C  
ATOM    682  N   LEU A  93      13.396   1.441  13.753  1.00 55.94           N  
ATOM    683  CA  LEU A  93      14.678   1.900  14.300  1.00 55.94           C  
ATOM    684  C   LEU A  93      14.481   3.045  15.294  1.00 55.94           C  
ATOM    685  O   LEU A  93      15.001   3.077  16.425  1.00 55.94           O  
ATOM    686  CB  LEU A  93      15.560   2.285  13.103  1.00 50.22           C  
ATOM    687  CG  LEU A  93      17.056   2.055  13.232  1.00 69.95           C  
ATOM    688  CD1 LEU A  93      17.411   0.631  12.812  1.00 79.67           C  
ATOM    689  CD2 LEU A  93      17.788   3.076  12.363  1.00 79.67           C  
ATOM    690  N   LEU A  94      13.685   3.996  14.827  1.00 71.61           N  
ATOM    691  CA  LEU A  94      13.301   5.208  15.556  1.00 71.61           C  
ATOM    692  C   LEU A  94      12.566   4.788  16.832  1.00 71.61           C  
ATOM    693  O   LEU A  94      12.795   5.323  17.922  1.00 71.61           O  
ATOM    694  CB  LEU A  94      12.464   6.093  14.632  1.00 65.89           C  
ATOM    695  CG  LEU A  94      12.600   7.599  14.731  1.00 85.62           C  
ATOM    696  CD1 LEU A  94      12.718   8.084  16.168  1.00 95.34           C  
ATOM    697  CD2 LEU A  94      13.853   8.013  13.963  1.00 95.34           C  
ATOM    698  N   LEU A  95      11.689   3.817  16.649  1.00 79.99           N  
ATOM    699  CA  LEU A  95      10.879   3.220  17.701  1.00 79.99           C  
ATOM    700  C   LEU A  95      11.804   2.671  18.792  1.00 79.99           C  
ATOM    701  O   LEU A  95      11.596   2.997  19.962  1.00 79.99           O  
ATOM    702  CB  LEU A  95       9.981   2.124  17.110  1.00 74.27           C  
ATOM    703  CG  LEU A  95       9.439   1.138  18.143  1.00 94.00           C  
ATOM    704  CD1 LEU A  95       8.237   1.734  18.859  1.00103.72           C  
ATOM    705  CD2 LEU A  95       9.096  -0.163  17.436  1.00103.72           C  
ATOM    706  N   ASP A  96      12.761   1.867  18.366  1.00 77.15           N  
ATOM    707  CA  ASP A  96      13.734   1.251  19.282  1.00 77.15           C  
ATOM    708  C   ASP A  96      14.500   2.308  20.081  1.00 77.15           C  
ATOM    709  O   ASP A  96      14.477   2.271  21.331  1.00 77.15           O  
ATOM    710  CB  ASP A  96      14.654   0.302  18.513  1.00 71.43           C  
ATOM    711  CG  ASP A  96      15.468  -0.594  19.427  1.00 91.16           C  
ATOM    712  OD1 ASP A  96      16.333  -0.025  20.130  1.00100.88           O  
ATOM    713  OD2 ASP A  96      15.273  -1.817  19.463  1.00100.88           O  
ATOM    714  N   LEU A  97      15.146   3.207  19.344  1.00 62.35           N  
ATOM    715  CA  LEU A  97      15.933   4.275  20.006  1.00 62.35           C  
ATOM    716  C   LEU A  97      15.055   5.043  20.990  1.00 62.35           C  
ATOM    717  O   LEU A  97      15.390   5.124  22.193  1.00 62.35           O  
ATOM    718  CB  LEU A  97      16.707   5.056  18.963  1.00 56.63           C  
ATOM    719  CG  LEU A  97      16.080   5.789  17.805  1.00 76.36           C  
ATOM    720  CD1 LEU A  97      15.394   7.078  18.245  1.00 86.08           C  
ATOM    721  CD2 LEU A  97      17.181   6.136  16.794  1.00 86.08           C  
ATOM    722  N   ALA A  98      13.932   5.556  20.518  1.00 47.55           N  
ATOM    723  CA  ALA A  98      12.970   6.306  21.338  1.00 47.55           C  
ATOM    724  C   ALA A  98      12.631   5.506  22.592  1.00 47.55           C  
ATOM    725  O   ALA A  98      12.758   5.982  23.730  1.00 47.55           O  
ATOM    726  CB  ALA A  98      11.720   6.651  20.542  1.00 41.83           C  
ATOM    727  N   LEU A  99      12.242   4.263  22.399  1.00 47.92           N  
ATOM    728  CA  LEU A  99      11.875   3.280  23.417  1.00 47.92           C  
ATOM    729  C   LEU A  99      12.946   3.173  24.500  1.00 47.92           C  
ATOM    730  O   LEU A  99      12.592   3.039  25.687  1.00 47.92           O  
ATOM    731  CB  LEU A  99      11.591   1.956  22.706  1.00 42.20           C  
ATOM    732  CG  LEU A  99      10.553   0.984  23.217  1.00 61.93           C  
ATOM    733  CD1 LEU A  99       9.290   1.674  23.721  1.00 71.65           C  
ATOM    734  CD2 LEU A  99      10.174   0.065  22.047  1.00 71.65           C  
ATOM    735  N   LEU A 100      14.206   3.245  24.083  1.00 73.36           N  
ATOM    736  CA  LEU A 100      15.328   3.170  25.030  1.00 73.36           C  
ATOM    737  C   LEU A 100      15.291   4.317  26.039  1.00 73.36           C  
ATOM    738  O   LEU A 100      15.615   4.099  27.220  1.00 73.36           O  
ATOM    739  CB  LEU A 100      16.623   3.116  24.212  1.00 67.64           C  
ATOM    740  CG  LEU A 100      17.938   2.965  24.953  1.00 87.37           C  
ATOM    741  CD1 LEU A 100      18.003   1.653  25.726  1.00 97.09           C  
ATOM    742  CD2 LEU A 100      19.072   3.016  23.928  1.00 97.09           C  
ATOM    743  N   VAL A 101      14.906   5.494  25.579  1.00112.74           N  
ATOM    744  CA  VAL A 101      14.822   6.694  26.419  1.00112.74           C  
ATOM    745  C   VAL A 101      13.375   7.038  26.781  1.00112.74           C  
ATOM    746  O   VAL A 101      12.832   6.597  27.804  1.00112.74           O  
ATOM    747  CB  VAL A 101      15.567   7.862  25.740  1.00107.02           C  
ATOM    748  CG1 VAL A 101      15.691   9.078  26.654  1.00126.75           C  
ATOM    749  CG2 VAL A 101      16.928   7.468  25.194  1.00126.75           C  
ATOM    750  N   ASP A 102      12.771   7.830  25.918  1.00149.66           N  
ATOM    751  CA  ASP A 102      11.403   8.332  26.018  1.00149.66           C  
ATOM    752  C   ASP A 102      10.337   7.251  25.832  1.00149.66           C  
ATOM    753  O   ASP A 102      10.363   6.472  24.871  1.00149.66           O  
ATOM    754  CB  ASP A 102      11.191   9.481  25.023  1.00143.94           C  
ATOM    755  CG  ASP A 102      11.563  10.849  25.551  1.00163.67           C  
ATOM    756  OD1 ASP A 102      12.562  11.022  26.263  1.00173.39           O  
ATOM    757  OD2 ASP A 102      10.799  11.784  25.222  1.00173.39           O  
ATOM    758  N   ALA A 103       9.395   7.263  26.759  1.00167.75           N  
ATOM    759  CA  ALA A 103       8.265   6.322  26.768  1.00167.75           C  
ATOM    760  C   ALA A 103       6.952   7.108  26.754  1.00167.75           C  
ATOM    761  O   ALA A 103       5.922   6.663  27.280  1.00167.75           O  
ATOM    762  CB  ALA A 103       8.356   5.383  27.960  1.00162.03           C  
ATOM    763  N   ASP A 104       7.040   8.275  26.140  1.00156.12           N  
ATOM    764  CA  ASP A 104       5.910   9.205  26.003  1.00156.12           C  
ATOM    765  C   ASP A 104       5.166   8.902  24.699  1.00156.12           C  
ATOM    766  O   ASP A 104       5.711   9.050  23.594  1.00156.12           O  
ATOM    767  CB  ASP A 104       6.388  10.650  26.108  1.00150.40           C  
ATOM    768  CG  ASP A 104       7.229  10.926  27.340  1.00170.13           C  
ATOM    769  OD1 ASP A 104       6.745  10.823  28.477  1.00179.85           O  
ATOM    770  OD2 ASP A 104       8.417  11.257  27.135  1.00179.85           O  
ATOM    771  N   GLN A 105       3.921   8.497  24.874  1.00125.96           N  
ATOM    772  CA  GLN A 105       3.014   8.149  23.770  1.00125.96           C  
ATOM    773  C   GLN A 105       3.055   9.243  22.702  1.00125.96           C  
ATOM    774  O   GLN A 105       3.395   8.976  21.540  1.00125.96           O  
ATOM    775  CB  GLN A 105       1.582   7.906  24.240  1.00120.24           C  
ATOM    776  CG  GLN A 105       0.646   7.419  23.149  1.00139.97           C  
ATOM    777  CD  GLN A 105      -0.812   7.626  23.474  1.00149.69           C  
ATOM    778  OE1 GLN A 105      -1.184   8.148  24.522  1.00185.07           O  
ATOM    779  NE2 GLN A 105      -1.671   7.208  22.546  1.00185.07           N  
ATOM    780  N   GLY A 106       2.720  10.449  23.127  1.00 93.96           N  
ATOM    781  CA  GLY A 106       2.703  11.629  22.255  1.00 93.96           C  
ATOM    782  C   GLY A 106       4.013  11.695  21.468  1.00 93.96           C  
ATOM    783  O   GLY A 106       3.999  11.622  20.230  1.00 93.96           O  
ATOM    784  N   THR A 107       5.100  11.808  22.208  1.00 73.21           N  
ATOM    785  CA  THR A 107       6.453  11.893  21.642  1.00 73.21           C  
ATOM    786  C   THR A 107       6.645  10.865  20.530  1.00 73.21           C  
ATOM    787  O   THR A 107       6.754  11.229  19.343  1.00 73.21           O  
ATOM    788  CB  THR A 107       7.558  11.774  22.765  1.00 67.49           C  
ATOM    789  OG1 THR A 107       7.162  12.693  23.834  1.00 87.22           O  
ATOM    790  CG2 THR A 107       8.984  12.069  22.291  1.00 87.22           C  
ATOM    791  N   ILE A 108       6.653   9.601  20.922  1.00 62.27           N  
ATOM    792  CA  ILE A 108       6.833   8.476  20.003  1.00 62.27           C  
ATOM    793  C   ILE A 108       5.935   8.565  18.774  1.00 62.27           C  
ATOM    794  O   ILE A 108       6.437   8.628  17.640  1.00 62.27           O  
ATOM    795  CB  ILE A 108       6.646   7.095  20.734  1.00 56.55           C  
ATOM    796  CG1 ILE A 108       7.532   7.024  21.999  1.00 76.28           C  
ATOM    797  CG2 ILE A 108       6.913   5.899  19.779  1.00 76.28           C  
ATOM    798  CD1 ILE A 108       7.257   5.796  22.911  1.00 86.00           C  
ATOM    799  N   LEU A 109       4.635   8.580  18.998  1.00 56.10           N  
ATOM    800  CA  LEU A 109       3.606   8.644  17.950  1.00 56.10           C  
ATOM    801  C   LEU A 109       3.913   9.740  16.931  1.00 56.10           C  
ATOM    802  O   LEU A 109       3.969   9.507  15.709  1.00 56.10           O  
ATOM    803  CB  LEU A 109       2.244   8.780  18.641  1.00 50.38           C  
ATOM    804  CG  LEU A 109       1.058   7.977  18.145  1.00 70.11           C  
ATOM    805  CD1 LEU A 109      -0.210   8.371  18.900  1.00 79.83           C  
ATOM    806  CD2 LEU A 109       0.850   8.211  16.651  1.00 79.83           C  
ATOM    807  N   ALA A 110       4.119  10.933  17.460  1.00 50.75           N  
ATOM    808  CA  ALA A 110       4.443  12.130  16.687  1.00 50.75           C  
ATOM    809  C   ALA A 110       5.654  11.857  15.796  1.00 50.75           C  
ATOM    810  O   ALA A 110       5.635  12.038  14.574  1.00 50.75           O  
ATOM    811  CB  ALA A 110       4.739  13.283  17.642  1.00 45.03           C  
ATOM    812  N   LEU A 111       6.694  11.403  16.462  1.00 46.68           N  
ATOM    813  CA  LEU A 111       8.004  11.059  15.881  1.00 46.68           C  
ATOM    814  C   LEU A 111       7.892  10.070  14.734  1.00 46.68           C  
ATOM    815  O   LEU A 111       8.479  10.291  13.650  1.00 46.68           O  
ATOM    816  CB  LEU A 111       8.836  10.728  17.109  1.00 40.96           C  
ATOM    817  CG  LEU A 111      10.022   9.818  17.171  1.00 60.69           C  
ATOM    818  CD1 LEU A 111      10.982  10.263  18.276  1.00 70.41           C  
ATOM    819  CD2 LEU A 111       9.530   8.401  17.490  1.00 70.41           C  
ATOM    820  N   VAL A 112       7.132   9.010  14.928  1.00 45.42           N  
ATOM    821  CA  VAL A 112       6.883   7.947  13.948  1.00 45.42           C  
ATOM    822  C   VAL A 112       6.017   8.442  12.787  1.00 45.42           C  
ATOM    823  O   VAL A 112       6.164   7.945  11.654  1.00 45.42           O  
ATOM    824  CB  VAL A 112       6.340   6.679  14.634  1.00 39.70           C  
ATOM    825  CG1 VAL A 112       6.125   5.534  13.649  1.00 59.43           C  
ATOM    826  CG2 VAL A 112       7.225   6.223  15.783  1.00 59.43           C  
ATOM    827  N   GLY A 113       5.135   9.383  13.072  1.00 47.58           N  
ATOM    828  CA  GLY A 113       4.240   9.990  12.068  1.00 47.58           C  
ATOM    829  C   GLY A 113       5.086  10.868  11.136  1.00 47.58           C  
ATOM    830  O   GLY A 113       4.989  10.836   9.896  1.00 47.58           O  
ATOM    831  N   ALA A 114       5.951  11.643  11.774  1.00 49.88           N  
ATOM    832  CA  ALA A 114       6.899  12.561  11.126  1.00 49.88           C  
ATOM    833  C   ALA A 114       7.816  11.735  10.220  1.00 49.88           C  
ATOM    834  O   ALA A 114       8.094  12.070   9.058  1.00 49.88           O  
ATOM    835  CB  ALA A 114       7.676  13.363  12.157  1.00 44.16           C  
ATOM    836  N   ASP A 115       8.264  10.630  10.789  1.00 48.10           N  
ATOM    837  CA  ASP A 115       9.127   9.638  10.129  1.00 48.10           C  
ATOM    838  C   ASP A 115       8.414   9.147   8.861  1.00 48.10           C  
ATOM    839  O   ASP A 115       8.922   9.159   7.727  1.00 48.10           O  
ATOM    840  CB  ASP A 115       9.393   8.522  11.132  1.00 42.38           C  
ATOM    841  CG  ASP A 115      10.237   7.374  10.635  1.00 62.11           C  
ATOM    842  OD1 ASP A 115      10.180   6.962   9.467  1.00 71.83           O  
ATOM    843  OD2 ASP A 115      11.001   6.871  11.494  1.00 71.83           O  
ATOM    844  N   GLY A 116       7.187   8.717   9.118  1.00 39.39           N  
ATOM    845  CA  GLY A 116       6.240   8.191   8.134  1.00 39.39           C  
ATOM    846  C   GLY A 116       6.203   9.095   6.904  1.00 39.39           C  
ATOM    847  O   GLY A 116       6.492   8.636   5.782  1.00 39.39           O  
ATOM    848  N   ILE A 117       5.877  10.364   7.152  1.00 26.42           N  
ATOM    849  CA  ILE A 117       5.828  11.327   6.033  1.00 26.42           C  
ATOM    850  C   ILE A 117       7.229  11.533   5.463  1.00 26.42           C  
ATOM    851  O   ILE A 117       7.305  11.814   4.253  1.00 26.42           O  
ATOM    852  CB  ILE A 117       5.036  12.635   6.346  1.00 20.70           C  
ATOM    853  CG1 ILE A 117       5.969  13.828   6.669  1.00 40.43           C  
ATOM    854  CG2 ILE A 117       3.964  12.432   7.457  1.00 40.43           C  
ATOM    855  CD1 ILE A 117       6.457  14.610   5.416  1.00 50.15           C  
ATOM    856  N   MET A 118       8.280  11.429   6.260  1.00 13.21           N  
ATOM    857  CA  MET A 118       9.650  11.606   5.743  1.00 13.21           C  
ATOM    858  C   MET A 118       9.849  10.638   4.565  1.00 13.21           C  
ATOM    859  O   MET A 118       9.987  11.073   3.402  1.00 13.21           O  
ATOM    860  CB  MET A 118      10.698  11.394   6.821  1.00  7.49           C  
ATOM    861  CG  MET A 118      12.101  11.423   6.266  1.00 27.22           C  
ATOM    862  SD  MET A 118      13.077  10.181   7.196  1.00 36.94           S  
ATOM    863  CE  MET A 118      14.638  11.069   7.332  1.00 72.32           C  
ATOM    864  N   ILE A 119       9.833   9.353   4.925  1.00  5.00           N  
ATOM    865  CA  ILE A 119      10.013   8.306   3.905  1.00  5.00           C  
ATOM    866  C   ILE A 119       8.960   8.445   2.799  1.00  5.00           C  
ATOM    867  O   ILE A 119       9.309   8.680   1.631  1.00  5.00           O  
ATOM    868  CB  ILE A 119       9.995   6.840   4.461  1.00  5.00           C  
ATOM    869  CG1 ILE A 119      10.967   6.641   5.641  1.00 18.75           C  
ATOM    870  CG2 ILE A 119      10.274   5.824   3.314  1.00 18.75           C  
ATOM    871  CD1 ILE A 119      12.482   6.647   5.300  1.00 28.47           C  
ATOM    872  N   GLY A 120       7.707   8.302   3.194  1.00  5.00           N  
ATOM    873  CA  GLY A 120       6.547   8.385   2.310  1.00  5.00           C  
ATOM    874  C   GLY A 120       6.636   9.483   1.266  1.00  5.00           C  
ATOM    875  O   GLY A 120       6.575   9.218   0.049  1.00  5.00           O  
ATOM    876  N   THR A 121       6.797  10.716   1.714  1.00  7.12           N  
ATOM    877  CA  THR A 121       6.913  11.914   0.876  1.00  7.12           C  
ATOM    878  C   THR A 121       8.153  11.811  -0.007  1.00  7.12           C  
ATOM    879  O   THR A 121       8.128  12.256  -1.172  1.00  7.12           O  
ATOM    880  CB  THR A 121       6.852  13.250   1.701  1.00  5.00           C  
ATOM    881  OG1 THR A 121       5.599  13.211   2.461  1.00 21.13           O  
ATOM    882  CG2 THR A 121       6.941  14.511   0.838  1.00 21.13           C  
ATOM    883  N   GLY A 122       9.193  11.204   0.560  1.00 20.34           N  
ATOM    884  CA  GLY A 122      10.456  10.973  -0.180  1.00 20.34           C  
ATOM    885  C   GLY A 122      10.096  10.148  -1.428  1.00 20.34           C  
ATOM    886  O   GLY A 122      10.496  10.468  -2.558  1.00 20.34           O  
ATOM    887  N   LEU A 123       9.318   9.102  -1.200  1.00 39.89           N  
ATOM    888  CA  LEU A 123       8.805   8.177  -2.217  1.00 39.89           C  
ATOM    889  C   LEU A 123       7.964   8.952  -3.233  1.00 39.89           C  
ATOM    890  O   LEU A 123       8.123   8.782  -4.455  1.00 39.89           O  
ATOM    891  CB  LEU A 123       8.063   7.044  -1.503  1.00 34.17           C  
ATOM    892  CG  LEU A 123       7.105   6.172  -2.293  1.00 53.90           C  
ATOM    893  CD1 LEU A 123       7.824   5.012  -2.965  1.00 63.62           C  
ATOM    894  CD2 LEU A 123       6.040   5.649  -1.332  1.00 63.62           C  
ATOM    895  N   VAL A 124       7.098   9.813  -2.720  1.00 59.32           N  
ATOM    896  CA  VAL A 124       6.225  10.657  -3.551  1.00 59.32           C  
ATOM    897  C   VAL A 124       7.092  11.366  -4.598  1.00 59.32           C  
ATOM    898  O   VAL A 124       6.889  11.255  -5.817  1.00 59.32           O  
ATOM    899  CB  VAL A 124       5.427  11.647  -2.683  1.00 53.60           C  
ATOM    900  CG1 VAL A 124       4.589  12.606  -3.523  1.00 73.33           C  
ATOM    901  CG2 VAL A 124       4.559  10.962  -1.641  1.00 73.33           C  
ATOM    902  N   GLY A 125       8.074  12.078  -4.063  1.00 70.90           N  
ATOM    903  CA  GLY A 125       9.054  12.845  -4.837  1.00 70.90           C  
ATOM    904  C   GLY A 125       9.793  11.970  -5.840  1.00 70.90           C  
ATOM    905  O   GLY A 125       9.993  12.350  -7.004  1.00 70.90           O  
ATOM    906  N   ALA A 126      10.186  10.797  -5.384  1.00 69.59           N  
ATOM    907  CA  ALA A 126      10.904   9.786  -6.151  1.00 69.59           C  
ATOM    908  C   ALA A 126      10.146   9.333  -7.395  1.00 69.59           C  
ATOM    909  O   ALA A 126      10.740   9.120  -8.461  1.00 69.59           O  
ATOM    910  CB  ALA A 126      11.158   8.564  -5.271  1.00 63.87           C  
ATOM    911  N   LEU A 127       8.851   9.159  -7.209  1.00 61.08           N  
ATOM    912  CA  LEU A 127       7.955   8.708  -8.274  1.00 61.08           C  
ATOM    913  C   LEU A 127       7.358   9.817  -9.120  1.00 61.08           C  
ATOM    914  O   LEU A 127       6.842   9.454 -10.203  1.00 61.08           O  
ATOM    915  CB  LEU A 127       6.948   7.755  -7.606  1.00 55.36           C  
ATOM    916  CG  LEU A 127       7.563   6.638  -6.769  1.00 75.09           C  
ATOM    917  CD1 LEU A 127       6.483   5.843  -6.050  1.00 84.81           C  
ATOM    918  CD2 LEU A 127       8.369   5.711  -7.675  1.00 84.81           C  
ATOM    919  N   THR A 128       7.406  11.065  -8.673  1.00 53.78           N  
ATOM    920  CA  THR A 128       6.824  12.149  -9.490  1.00 53.78           C  
ATOM    921  C   THR A 128       7.437  12.170 -10.894  1.00 53.78           C  
ATOM    922  O   THR A 128       8.651  12.244 -11.119  1.00 53.78           O  
ATOM    923  CB  THR A 128       6.832  13.578  -8.835  1.00 48.06           C  
ATOM    924  OG1 THR A 128       5.992  14.384  -9.733  1.00 67.79           O  
ATOM    925  CG2 THR A 128       8.207  14.214  -8.641  1.00 67.79           C  
ATOM    926  N   LYS A 129       6.529  12.111 -11.850  1.00 53.73           N  
ATOM    927  CA  LYS A 129       6.761  12.091 -13.294  1.00 53.73           C  
ATOM    928  C   LYS A 129       7.243  13.409 -13.872  1.00 53.73           C  
ATOM    929  O   LYS A 129       8.028  13.390 -14.839  1.00 53.73           O  
ATOM    930  CB  LYS A 129       5.489  11.614 -13.996  1.00 48.01           C  
ATOM    931  CG  LYS A 129       4.904  12.493 -15.096  1.00 67.74           C  
ATOM    932  CD  LYS A 129       3.386  12.554 -14.963  1.00 77.46           C  
ATOM    933  CE  LYS A 129       2.796  13.800 -15.588  1.00112.84           C  
ATOM    934  NZ  LYS A 129       1.390  13.984 -15.141  1.00 75.15           N  
ATOM    935  N   VAL A 130       6.775  14.505 -13.309  1.00 57.52           N  
ATOM    936  CA  VAL A 130       7.161  15.852 -13.788  1.00 57.52           C  
ATOM    937  C   VAL A 130       8.683  15.963 -13.734  1.00 57.52           C  
ATOM    938  O   VAL A 130       9.396  15.153 -13.122  1.00 57.52           O  
ATOM    939  CB  VAL A 130       6.328  16.922 -13.073  1.00 51.80           C  
ATOM    940  CG1 VAL A 130       6.602  18.357 -13.504  1.00 71.53           C  
ATOM    941  CG2 VAL A 130       4.834  16.624 -13.224  1.00 71.53           C  
ATOM    942  N   TYR A 131       9.165  16.980 -14.413  1.00 59.40           N  
ATOM    943  CA  TYR A 131      10.576  17.315 -14.570  1.00 59.40           C  
ATOM    944  C   TYR A 131      11.230  17.946 -13.354  1.00 59.40           C  
ATOM    945  O   TYR A 131      12.158  17.329 -12.790  1.00 59.40           O  
ATOM    946  CB  TYR A 131      10.728  18.181 -15.850  1.00 53.68           C  
ATOM    947  CG  TYR A 131      10.079  17.542 -17.064  1.00 69.80           C  
ATOM    948  CD1 TYR A 131      10.781  16.662 -17.893  1.00 69.80           C  
ATOM    949  CD2 TYR A 131       8.747  17.811 -17.384  1.00 69.80           C  
ATOM    950  CE1 TYR A 131      10.178  16.074 -19.003  1.00 69.80           C  
ATOM    951  CE2 TYR A 131       8.128  17.232 -18.487  1.00 69.80           C  
ATOM    952  CZ  TYR A 131       8.847  16.363 -19.297  1.00 69.80           C  
ATOM    953  OH  TYR A 131       8.207  15.814 -20.374  1.00 83.13           O  
ATOM    954  N   SER A 132      10.777  19.126 -12.966  1.00 55.17           N  
ATOM    955  CA  SER A 132      11.359  19.832 -11.819  1.00 55.17           C  
ATOM    956  C   SER A 132      10.373  20.232 -10.730  1.00 55.17           C  
ATOM    957  O   SER A 132       9.793  21.330 -10.752  1.00 55.17           O  
ATOM    958  CB  SER A 132      12.127  21.071 -12.283  1.00 49.45           C  
ATOM    959  OG  SER A 132      12.593  21.831 -11.181  1.00 69.18           O  
ATOM    960  N   TYR A 133      10.231  19.328  -9.779  1.00 46.69           N  
ATOM    961  CA  TYR A 133       9.360  19.512  -8.607  1.00 46.69           C  
ATOM    962  C   TYR A 133       9.581  18.331  -7.665  1.00 46.69           C  
ATOM    963  O   TYR A 133       9.031  18.281  -6.556  1.00 46.69           O  
ATOM    964  CB  TYR A 133       7.928  19.866  -8.911  1.00 40.97           C  
ATOM    965  CG  TYR A 133       6.771  18.941  -9.088  1.00 57.09           C  
ATOM    966  CD1 TYR A 133       6.530  17.841  -8.260  1.00 57.09           C  
ATOM    967  CD2 TYR A 133       5.827  19.193 -10.094  1.00 57.09           C  
ATOM    968  CE1 TYR A 133       5.433  17.006  -8.433  1.00 57.09           C  
ATOM    969  CE2 TYR A 133       4.718  18.373 -10.286  1.00 57.09           C  
ATOM    970  CZ  TYR A 133       4.526  17.275  -9.456  1.00 57.09           C  
ATOM    971  OH  TYR A 133       3.428  16.491  -9.672  1.00 70.42           O  
ATOM    972  N   ARG A 134      10.462  17.433  -8.083  1.00 37.40           N  
ATOM    973  CA  ARG A 134      10.851  16.234  -7.324  1.00 37.40           C  
ATOM    974  C   ARG A 134      11.583  16.670  -6.048  1.00 37.40           C  
ATOM    975  O   ARG A 134      11.572  16.010  -4.999  1.00 37.40           O  
ATOM    976  CB  ARG A 134      11.745  15.296  -8.125  1.00 31.68           C  
ATOM    977  CG  ARG A 134      11.461  15.151  -9.609  1.00 51.41           C  
ATOM    978  CD  ARG A 134      12.351  14.144 -10.252  1.00 61.13           C  
ATOM    979  NE  ARG A 134      11.791  12.807 -10.335  1.00 96.51           N  
ATOM    980  CZ  ARG A 134      12.480  11.683 -10.537  1.00 58.82           C  
ATOM    981  NH1 ARG A 134      13.806  11.658 -10.659  1.00102.28           N  
ATOM    982  NH2 ARG A 134      11.826  10.524 -10.649  1.00102.28           N  
ATOM    983  N   PHE A 135      12.218  17.821  -6.167  1.00 30.70           N  
ATOM    984  CA  PHE A 135      12.990  18.563  -5.182  1.00 30.70           C  
ATOM    985  C   PHE A 135      12.056  19.345  -4.249  1.00 30.70           C  
ATOM    986  O   PHE A 135      12.516  19.761  -3.171  1.00 30.70           O  
ATOM    987  CB  PHE A 135      14.052  19.473  -5.798  1.00 24.98           C  
ATOM    988  CG  PHE A 135      14.906  18.838  -6.854  1.00 41.10           C  
ATOM    989  CD1 PHE A 135      15.933  17.962  -6.498  1.00 41.10           C  
ATOM    990  CD2 PHE A 135      14.676  19.117  -8.202  1.00 41.10           C  
ATOM    991  CE1 PHE A 135      16.722  17.370  -7.473  1.00 41.10           C  
ATOM    992  CE2 PHE A 135      15.462  18.534  -9.202  1.00 41.10           C  
ATOM    993  CZ  PHE A 135      16.490  17.656  -8.822  1.00 41.10           C  
ATOM    994  N   VAL A 136      10.815  19.535  -4.678  1.00 29.28           N  
ATOM    995  CA  VAL A 136       9.830  20.253  -3.830  1.00 29.28           C  
ATOM    996  C   VAL A 136       9.557  19.272  -2.676  1.00 29.28           C  
ATOM    997  O   VAL A 136       9.660  19.559  -1.471  1.00 29.28           O  
ATOM    998  CB  VAL A 136       8.626  20.753  -4.624  1.00 23.56           C  
ATOM    999  CG1 VAL A 136       7.375  19.886  -4.581  1.00 43.29           C  
ATOM   1000  CG2 VAL A 136       8.251  22.180  -4.219  1.00 43.29           C  
ATOM   1001  N   TRP A 137       9.257  18.066  -3.151  1.00 32.79           N  
ATOM   1002  CA  TRP A 137       8.981  16.911  -2.287  1.00 32.79           C  
ATOM   1003  C   TRP A 137      10.262  16.690  -1.476  1.00 32.79           C  
ATOM   1004  O   TRP A 137      10.210  16.654  -0.236  1.00 32.79           O  
ATOM   1005  CB  TRP A 137       8.528  15.704  -3.078  1.00 27.07           C  
ATOM   1006  CG  TRP A 137       7.197  15.774  -3.734  1.00 43.19           C  
ATOM   1007  CD1 TRP A 137       6.914  15.595  -5.062  1.00 43.19           C  
ATOM   1008  CD2 TRP A 137       5.937  16.040  -3.099  1.00 43.19           C  
ATOM   1009  NE1 TRP A 137       5.566  15.732  -5.293  1.00 43.19           N  
ATOM   1010  CE2 TRP A 137       4.947  16.008  -4.106  1.00 43.19           C  
ATOM   1011  CE3 TRP A 137       5.570  16.305  -1.785  1.00 43.19           C  
ATOM   1012  CZ2 TRP A 137       3.603  16.229  -3.835  1.00 43.19           C  
ATOM   1013  CZ3 TRP A 137       4.233  16.524  -1.513  1.00 43.19           C  
ATOM   1014  CH2 TRP A 137       3.264  16.488  -2.514  1.00 43.19           C  
ATOM   1015  N   TRP A 138      11.389  16.617  -2.178  1.00 40.16           N  
ATOM   1016  CA  TRP A 138      12.694  16.429  -1.523  1.00 40.16           C  
ATOM   1017  C   TRP A 138      12.821  17.400  -0.348  1.00 40.16           C  
ATOM   1018  O   TRP A 138      13.175  16.976   0.763  1.00 40.16           O  
ATOM   1019  CB  TRP A 138      13.865  16.523  -2.496  1.00 34.44           C  
ATOM   1020  CG  TRP A 138      15.197  16.417  -1.833  1.00 50.56           C  
ATOM   1021  CD1 TRP A 138      15.896  15.290  -1.513  1.00 50.56           C  
ATOM   1022  CD2 TRP A 138      15.999  17.513  -1.364  1.00 50.56           C  
ATOM   1023  NE1 TRP A 138      17.085  15.603  -0.899  1.00 50.56           N  
ATOM   1024  CE2 TRP A 138      17.167  16.961  -0.791  1.00 50.56           C  
ATOM   1025  CE3 TRP A 138      15.825  18.893  -1.382  1.00 50.56           C  
ATOM   1026  CZ2 TRP A 138      18.168  17.748  -0.242  1.00 50.56           C  
ATOM   1027  CZ3 TRP A 138      16.818  19.679  -0.834  1.00 50.56           C  
ATOM   1028  CH2 TRP A 138      17.965  19.120  -0.274  1.00 50.56           C  
ATOM   1029  N   ALA A 139      12.533  18.661  -0.583  1.00 49.67           N  
ATOM   1030  CA  ALA A 139      12.559  19.762   0.375  1.00 49.67           C  
ATOM   1031  C   ALA A 139      11.677  19.469   1.590  1.00 49.67           C  
ATOM   1032  O   ALA A 139      12.094  19.695   2.747  1.00 49.67           O  
ATOM   1033  CB  ALA A 139      12.130  21.055  -0.313  1.00 43.95           C  
ATOM   1034  N   ILE A 140      10.479  18.961   1.308  1.00 56.92           N  
ATOM   1035  CA  ILE A 140       9.528  18.603   2.384  1.00 56.92           C  
ATOM   1036  C   ILE A 140      10.088  17.463   3.229  1.00 56.92           C  
ATOM   1037  O   ILE A 140       9.988  17.421   4.473  1.00 56.92           O  
ATOM   1038  CB  ILE A 140       8.099  18.359   1.791  1.00 51.20           C  
ATOM   1039  CG1 ILE A 140       7.521  19.734   1.362  1.00 70.93           C  
ATOM   1040  CG2 ILE A 140       7.145  17.604   2.750  1.00 70.93           C  
ATOM   1041  CD1 ILE A 140       6.123  19.678   0.695  1.00 80.65           C  
ATOM   1042  N   SER A 141      10.723  16.525   2.548  1.00 56.90           N  
ATOM   1043  CA  SER A 141      11.373  15.335   3.102  1.00 56.90           C  
ATOM   1044  C   SER A 141      12.507  15.773   4.034  1.00 56.90           C  
ATOM   1045  O   SER A 141      12.746  15.199   5.104  1.00 56.90           O  
ATOM   1046  CB  SER A 141      11.900  14.431   2.004  1.00 51.18           C  
ATOM   1047  OG  SER A 141      10.951  14.188   0.986  1.00 70.91           O  
ATOM   1048  N   THR A 142      13.196  16.803   3.587  1.00 46.66           N  
ATOM   1049  CA  THR A 142      14.314  17.477   4.246  1.00 46.66           C  
ATOM   1050  C   THR A 142      13.808  18.044   5.577  1.00 46.66           C  
ATOM   1051  O   THR A 142      14.400  17.824   6.648  1.00 46.66           O  
ATOM   1052  CB  THR A 142      14.924  18.610   3.327  1.00 40.94           C  
ATOM   1053  OG1 THR A 142      15.498  17.933   2.162  1.00 60.67           O  
ATOM   1054  CG2 THR A 142      15.933  19.539   4.010  1.00 60.67           C  
ATOM   1055  N   ALA A 143      12.693  18.759   5.449  1.00 31.69           N  
ATOM   1056  CA  ALA A 143      12.030  19.371   6.613  1.00 31.69           C  
ATOM   1057  C   ALA A 143      11.733  18.288   7.653  1.00 31.69           C  
ATOM   1058  O   ALA A 143      12.172  18.397   8.812  1.00 31.69           O  
ATOM   1059  CB  ALA A 143      10.767  20.098   6.177  1.00 25.97           C  
ATOM   1060  N   ALA A 144      11.018  17.263   7.206  1.00 19.57           N  
ATOM   1061  CA  ALA A 144      10.631  16.115   8.044  1.00 19.57           C  
ATOM   1062  C   ALA A 144      11.836  15.491   8.744  1.00 19.57           C  
ATOM   1063  O   ALA A 144      11.853  15.311   9.982  1.00 19.57           O  
ATOM   1064  CB  ALA A 144       9.867  15.091   7.208  1.00 13.85           C  
ATOM   1065  N   MET A 145      12.859  15.181   7.959  1.00 15.86           N  
ATOM   1066  CA  MET A 145      14.110  14.581   8.445  1.00 15.86           C  
ATOM   1067  C   MET A 145      14.648  15.428   9.602  1.00 15.86           C  
ATOM   1068  O   MET A 145      14.934  14.939  10.707  1.00 15.86           O  
ATOM   1069  CB  MET A 145      15.144  14.451   7.334  1.00 10.14           C  
ATOM   1070  CG  MET A 145      16.451  13.954   7.914  1.00 29.87           C  
ATOM   1071  SD  MET A 145      17.690  14.002   6.575  1.00 39.59           S  
ATOM   1072  CE  MET A 145      19.122  14.592   7.501  1.00 74.97           C  
ATOM   1073  N   LEU A 146      14.748  16.714   9.286  1.00 18.09           N  
ATOM   1074  CA  LEU A 146      15.225  17.726  10.245  1.00 18.09           C  
ATOM   1075  C   LEU A 146      14.414  17.566  11.528  1.00 18.09           C  
ATOM   1076  O   LEU A 146      15.028  17.428  12.601  1.00 18.09           O  
ATOM   1077  CB  LEU A 146      15.202  19.086   9.566  1.00 12.37           C  
ATOM   1078  CG  LEU A 146      15.872  20.304  10.173  1.00 32.10           C  
ATOM   1079  CD1 LEU A 146      15.077  20.881  11.341  1.00 41.82           C  
ATOM   1080  CD2 LEU A 146      17.280  19.932  10.644  1.00 41.82           C  
ATOM   1081  N   TYR A 147      13.092  17.538  11.412  1.00 21.72           N  
ATOM   1082  CA  TYR A 147      12.225  17.372  12.584  1.00 21.72           C  
ATOM   1083  C   TYR A 147      12.629  16.143  13.396  1.00 21.72           C  
ATOM   1084  O   TYR A 147      12.794  16.249  14.629  1.00 21.72           O  
ATOM   1085  CB  TYR A 147      10.720  17.337  12.246  1.00 16.00           C  
ATOM   1086  CG  TYR A 147       9.905  17.808  13.438  1.00 32.12           C  
ATOM   1087  CD1 TYR A 147       9.848  19.175  13.722  1.00 32.12           C  
ATOM   1088  CD2 TYR A 147       9.231  16.927  14.284  1.00 32.12           C  
ATOM   1089  CE1 TYR A 147       9.126  19.661  14.808  1.00 32.12           C  
ATOM   1090  CE2 TYR A 147       8.503  17.399  15.374  1.00 32.12           C  
ATOM   1091  CZ  TYR A 147       8.456  18.768  15.633  1.00 32.12           C  
ATOM   1092  OH  TYR A 147       7.760  19.286  16.689  1.00 45.45           O  
ATOM   1093  N   ILE A 148      12.802  15.017  12.716  1.00 23.54           N  
ATOM   1094  CA  ILE A 148      13.209  13.771  13.389  1.00 23.54           C  
ATOM   1095  C   ILE A 148      14.470  14.026  14.223  1.00 23.54           C  
ATOM   1096  O   ILE A 148      14.533  13.694  15.423  1.00 23.54           O  
ATOM   1097  CB  ILE A 148      13.388  12.584  12.381  1.00 17.82           C  
ATOM   1098  CG1 ILE A 148      12.052  12.252  11.672  1.00 37.55           C  
ATOM   1099  CG2 ILE A 148      14.002  11.323  13.051  1.00 37.55           C  
ATOM   1100  CD1 ILE A 148      12.148  11.149  10.580  1.00 47.27           C  
ATOM   1101  N   LEU A 149      15.457  14.620  13.567  1.00 25.39           N  
ATOM   1102  CA  LEU A 149      16.751  14.951  14.178  1.00 25.39           C  
ATOM   1103  C   LEU A 149      16.652  15.890  15.371  1.00 25.39           C  
ATOM   1104  O   LEU A 149      17.289  15.628  16.413  1.00 25.39           O  
ATOM   1105  CB  LEU A 149      17.678  15.418  13.046  1.00 19.67           C  
ATOM   1106  CG  LEU A 149      18.504  14.352  12.340  1.00 39.40           C  
ATOM   1107  CD1 LEU A 149      17.642  13.283  11.677  1.00 49.12           C  
ATOM   1108  CD2 LEU A 149      19.374  15.043  11.286  1.00 49.12           C  
ATOM   1109  N   TYR A 150      15.876  16.946  15.257  1.00 30.40           N  
ATOM   1110  CA  TYR A 150      15.636  17.968  16.286  1.00 30.40           C  
ATOM   1111  C   TYR A 150      15.031  17.308  17.525  1.00 30.40           C  
ATOM   1112  O   TYR A 150      15.433  17.521  18.687  1.00 30.40           O  
ATOM   1113  CB  TYR A 150      14.722  19.070  15.730  1.00 24.68           C  
ATOM   1114  CG  TYR A 150      15.102  20.493  16.045  1.00 40.80           C  
ATOM   1115  CD1 TYR A 150      14.925  21.053  17.314  1.00 40.80           C  
ATOM   1116  CD2 TYR A 150      15.643  21.304  15.044  1.00 40.80           C  
ATOM   1117  CE1 TYR A 150      15.282  22.374  17.580  1.00 40.80           C  
ATOM   1118  CE2 TYR A 150      16.007  22.625  15.294  1.00 40.80           C  
ATOM   1119  CZ  TYR A 150      15.826  23.159  16.564  1.00 40.80           C  
ATOM   1120  OH  TYR A 150      16.196  24.461  16.763  1.00 54.13           O  
ATOM   1121  N   VAL A 151      14.061  16.442  17.236  1.00 40.55           N  
ATOM   1122  CA  VAL A 151      13.345  15.654  18.256  1.00 40.55           C  
ATOM   1123  C   VAL A 151      14.330  14.690  18.915  1.00 40.55           C  
ATOM   1124  O   VAL A 151      14.161  14.364  20.105  1.00 40.55           O  
ATOM   1125  CB  VAL A 151      12.061  15.057  17.679  1.00 34.83           C  
ATOM   1126  CG1 VAL A 151      11.351  14.114  18.643  1.00 54.56           C  
ATOM   1127  CG2 VAL A 151      11.113  16.160  17.224  1.00 54.56           C  
ATOM   1128  N   LEU A 152      15.335  14.260  18.162  1.00 53.12           N  
ATOM   1129  CA  LEU A 152      16.390  13.381  18.692  1.00 53.12           C  
ATOM   1130  C   LEU A 152      17.278  14.226  19.611  1.00 53.12           C  
ATOM   1131  O   LEU A 152      17.765  13.727  20.647  1.00 53.12           O  
ATOM   1132  CB  LEU A 152      17.070  12.590  17.581  1.00 47.40           C  
ATOM   1133  CG  LEU A 152      16.787  11.086  17.592  1.00 67.13           C  
ATOM   1134  CD1 LEU A 152      15.352  10.775  17.189  1.00 76.85           C  
ATOM   1135  CD2 LEU A 152      17.771  10.385  16.659  1.00 76.85           C  
ATOM   1136  N   PHE A 153      17.444  15.501  19.266  1.00 64.26           N  
ATOM   1137  CA  PHE A 153      18.230  16.442  20.086  1.00 64.26           C  
ATOM   1138  C   PHE A 153      17.536  16.409  21.475  1.00 64.26           C  
ATOM   1139  O   PHE A 153      18.209  16.210  22.495  1.00 64.26           O  
ATOM   1140  CB  PHE A 153      18.363  17.868  19.645  1.00 58.54           C  
ATOM   1141  CG  PHE A 153      18.666  18.379  18.286  1.00 74.66           C  
ATOM   1142  CD1 PHE A 153      19.406  17.642  17.359  1.00 74.66           C  
ATOM   1143  CD2 PHE A 153      18.230  19.664  17.927  1.00 74.66           C  
ATOM   1144  CE1 PHE A 153      19.682  18.145  16.098  1.00 74.66           C  
ATOM   1145  CE2 PHE A 153      18.504  20.196  16.662  1.00 74.66           C  
ATOM   1146  CZ  PHE A 153      19.236  19.421  15.746  1.00 74.66           C  
ATOM   1147  N   PHE A 154      16.219  16.602  21.423  1.00 70.10           N  
ATOM   1148  CA  PHE A 154      15.409  16.568  22.659  1.00 70.10           C  
ATOM   1149  C   PHE A 154      15.616  15.230  23.382  1.00 70.10           C  
ATOM   1150  O   PHE A 154      15.890  15.206  24.593  1.00 70.10           O  
ATOM   1151  CB  PHE A 154      13.923  16.835  22.430  1.00 64.38           C  
ATOM   1152  CG  PHE A 154      13.004  16.324  23.507  1.00 80.50           C  
ATOM   1153  CD1 PHE A 154      12.850  17.043  24.693  1.00 80.50           C  
ATOM   1154  CD2 PHE A 154      12.314  15.123  23.335  1.00 80.50           C  
ATOM   1155  CE1 PHE A 154      12.013  16.586  25.699  1.00 80.50           C  
ATOM   1156  CE2 PHE A 154      11.465  14.642  24.337  1.00 80.50           C  
ATOM   1157  CZ  PHE A 154      11.321  15.384  25.523  1.00 80.50           C  
ATOM   1158  N   GLY A 155      15.469  14.147  22.640  1.00 70.46           N  
ATOM   1159  CA  GLY A 155      15.633  12.780  23.157  1.00 70.46           C  
ATOM   1160  C   GLY A 155      16.860  12.747  24.072  1.00 70.46           C  
ATOM   1161  O   GLY A 155      16.725  12.443  25.269  1.00 70.46           O  
ATOM   1162  N   PHE A 156      18.005  13.077  23.487  1.00 79.83           N  
ATOM   1163  CA  PHE A 156      19.261  13.108  24.255  1.00 79.83           C  
ATOM   1164  C   PHE A 156      19.086  14.035  25.466  1.00 79.83           C  
ATOM   1165  O   PHE A 156      19.171  13.594  26.621  1.00 79.83           O  
ATOM   1166  CB  PHE A 156      20.471  13.533  23.425  1.00 74.11           C  
ATOM   1167  CG  PHE A 156      21.716  13.744  24.240  1.00 90.23           C  
ATOM   1168  CD1 PHE A 156      22.440  12.661  24.732  1.00 90.23           C  
ATOM   1169  CD2 PHE A 156      22.138  15.045  24.526  1.00 90.23           C  
ATOM   1170  CE1 PHE A 156      23.593  12.870  25.498  1.00 90.23           C  
ATOM   1171  CE2 PHE A 156      23.277  15.275  25.282  1.00 90.23           C  
ATOM   1172  CZ  PHE A 156      24.006  14.187  25.769  1.00 90.23           C  
ATOM   1173  N   THR A 157      18.836  15.294  25.154  1.00116.41           N  
ATOM   1174  CA  THR A 157      18.649  16.365  26.135  1.00116.41           C  
ATOM   1175  C   THR A 157      17.858  15.912  27.355  1.00116.41           C  
ATOM   1176  O   THR A 157      18.386  15.970  28.482  1.00116.41           O  
ATOM   1177  CB  THR A 157      18.026  17.664  25.485  1.00110.69           C  
ATOM   1178  OG1 THR A 157      18.985  18.115  24.475  1.00130.42           O  
ATOM   1179  CG2 THR A 157      17.706  18.778  26.486  1.00130.42           C  
ATOM   1180  N   SER A 158      16.631  15.483  27.127  1.00189.78           N  
ATOM   1181  CA  SER A 158      15.745  15.003  28.200  1.00189.78           C  
ATOM   1182  C   SER A 158      16.235  13.622  28.645  1.00189.78           C  
ATOM   1183  O   SER A 158      15.897  12.601  28.028  1.00189.78           O  
ATOM   1184  CB  SER A 158      14.296  14.967  27.758  1.00184.06           C  
ATOM   1185  OG  SER A 158      13.431  14.571  28.806  1.00203.79           O  
ATOM   1186  N   LYS A 159      17.027  13.642  29.701  1.00275.12           N  
ATOM   1187  CA  LYS A 159      17.610  12.426  30.284  1.00275.12           C  
ATOM   1188  C   LYS A 159      16.543  11.687  31.087  1.00275.12           C  
ATOM   1189  O   LYS A 159      16.204  10.534  30.777  1.00275.12           O  
ATOM   1190  CB  LYS A 159      18.819  12.734  31.153  1.00269.40           C  
ATOM   1191  CG  LYS A 159      19.669  11.512  31.501  1.00289.13           C  
ATOM   1192  CD  LYS A 159      20.982  11.924  32.150  1.00298.85           C  
ATOM   1193  CE  LYS A 159      21.884  10.736  32.413  1.00334.23           C  
ATOM   1194  NZ  LYS A 159      23.185  11.184  32.972  1.00296.54           N  
ATOM   1195  N   ALA A 160      16.038  12.371  32.094  1.00339.04           N  
ATOM   1196  CA  ALA A 160      14.995  11.852  32.990  1.00339.04           C  
ATOM   1197  C   ALA A 160      15.271  10.400  33.363  1.00339.04           C  
ATOM   1198  O   ALA A 160      16.434  10.022  33.590  1.00339.04           O  
ATOM   1199  CB  ALA A 160      13.630  12.048  32.341  1.00333.32           C  
ATOM   1200  N   GLU A 161      14.214   9.612  33.429  1.00357.97           N  
ATOM   1201  CA  GLU A 161      14.267   8.191  33.772  1.00357.97           C  
ATOM   1202  C   GLU A 161      15.385   7.478  33.011  1.00357.97           C  
ATOM   1203  O   GLU A 161      15.290   7.246  31.796  1.00357.97           O  
ATOM   1204  CB  GLU A 161      12.974   7.441  33.479  1.00352.25           C  
ATOM   1205  CG  GLU A 161      11.791   7.552  34.423  1.00371.98           C  
ATOM   1206  CD  GLU A 161      10.891   8.740  34.289  1.00381.70           C  
ATOM   1207  OE1 GLU A 161      10.581   8.975  33.100  1.00417.08           O  
ATOM   1208  OE2 GLU A 161      10.491   9.407  35.228  1.00417.08           O  
ATOM   1209  N   SER A 162      16.417   7.143  33.763  1.00347.68           N  
ATOM   1210  CA  SER A 162      17.602   6.447  33.243  1.00347.68           C  
ATOM   1211  C   SER A 162      18.086   5.430  34.278  1.00347.68           C  
ATOM   1212  O   SER A 162      18.003   5.669  35.492  1.00347.68           O  
ATOM   1213  CB  SER A 162      18.704   7.422  32.869  1.00341.96           C  
ATOM   1214  OG  SER A 162      19.132   8.189  33.979  1.00361.69           O  
ATOM   1215  N   MET A 163      18.575   4.321  33.755  1.00333.78           N  
ATOM   1216  CA  MET A 163      19.097   3.215  34.575  1.00333.78           C  
ATOM   1217  C   MET A 163      20.623   3.310  34.611  1.00333.78           C  
ATOM   1218  O   MET A 163      21.188   4.304  35.100  1.00333.78           O  
ATOM   1219  CB  MET A 163      18.569   1.879  34.076  1.00328.06           C  
ATOM   1220  CG  MET A 163      17.074   1.760  34.229  1.00347.79           C  
ATOM   1221  SD  MET A 163      16.581   0.110  33.610  1.00357.51           S  
ATOM   1222  CE  MET A 163      14.798   0.209  33.853  1.00392.89           C  
ATOM   1223  N   ARG A 164      21.263   2.285  34.093  1.00334.11           N  
ATOM   1224  CA  ARG A 164      22.720   2.154  34.017  1.00334.11           C  
ATOM   1225  C   ARG A 164      23.300   3.223  33.093  1.00334.11           C  
ATOM   1226  O   ARG A 164      22.559   3.897  32.361  1.00334.11           O  
ATOM   1227  CB  ARG A 164      23.098   0.759  33.508  1.00328.39           C  
ATOM   1228  CG  ARG A 164      22.498  -0.405  34.283  1.00348.12           C  
ATOM   1229  CD  ARG A 164      22.643  -1.695  33.549  1.00357.84           C  
ATOM   1230  NE  ARG A 164      22.041  -2.813  34.259  1.00393.22           N  
ATOM   1231  CZ  ARG A 164      21.891  -4.040  33.759  1.00355.53           C  
ATOM   1232  NH1 ARG A 164      22.288  -4.359  32.531  1.00398.99           N  
ATOM   1233  NH2 ARG A 164      21.322  -4.982  34.513  1.00398.99           N  
ATOM   1234  N   PRO A 165      24.621   3.340  33.139  1.00335.38           N  
ATOM   1235  CA  PRO A 165      25.353   4.310  32.317  1.00335.38           C  
ATOM   1236  C   PRO A 165      25.458   3.870  30.867  1.00335.38           C  
ATOM   1237  O   PRO A 165      25.406   4.688  29.930  1.00335.38           O  
ATOM   1238  CB  PRO A 165      26.708   4.430  33.011  1.00329.66           C  
ATOM   1239  CG  PRO A 165      26.926   3.086  33.648  1.00329.66           C  
ATOM   1240  CD  PRO A 165      25.538   2.565  33.992  1.00329.66           C  
ATOM   1241  N   GLU A 166      25.574   2.570  30.669  1.00316.52           N  
ATOM   1242  CA  GLU A 166      25.695   1.900  29.378  1.00316.52           C  
ATOM   1243  C   GLU A 166      24.700   2.362  28.325  1.00316.52           C  
ATOM   1244  O   GLU A 166      25.082   2.565  27.155  1.00316.52           O  
ATOM   1245  CB  GLU A 166      25.561   0.380  29.506  1.00310.80           C  
ATOM   1246  CG  GLU A 166      26.782  -0.426  29.923  1.00330.53           C  
ATOM   1247  CD  GLU A 166      27.381  -0.127  31.262  1.00340.25           C  
ATOM   1248  OE1 GLU A 166      26.874  -0.430  32.329  1.00375.63           O  
ATOM   1249  OE2 GLU A 166      28.475   0.471  31.169  1.00375.63           O  
ATOM   1250  N   VAL A 167      23.451   2.529  28.718  1.00263.48           N  
ATOM   1251  CA  VAL A 167      22.361   2.977  27.846  1.00263.48           C  
ATOM   1252  C   VAL A 167      22.634   4.386  27.314  1.00263.48           C  
ATOM   1253  O   VAL A 167      22.351   4.675  26.137  1.00263.48           O  
ATOM   1254  CB  VAL A 167      21.002   2.839  28.557  1.00257.76           C  
ATOM   1255  CG1 VAL A 167      20.694   1.399  28.954  1.00277.49           C  
ATOM   1256  CG2 VAL A 167      20.874   3.768  29.752  1.00277.49           C  
ATOM   1257  N   ALA A 168      23.174   5.228  28.177  1.00190.26           N  
ATOM   1258  CA  ALA A 168      23.512   6.616  27.845  1.00190.26           C  
ATOM   1259  C   ALA A 168      24.560   6.663  26.735  1.00190.26           C  
ATOM   1260  O   ALA A 168      24.403   7.408  25.753  1.00190.26           O  
ATOM   1261  CB  ALA A 168      23.977   7.360  29.089  1.00184.54           C  
ATOM   1262  N   SER A 169      25.604   5.872  26.908  1.00117.87           N  
ATOM   1263  CA  SER A 169      26.718   5.766  25.955  1.00117.87           C  
ATOM   1264  C   SER A 169      26.232   5.176  24.632  1.00117.87           C  
ATOM   1265  O   SER A 169      26.516   5.727  23.549  1.00117.87           O  
ATOM   1266  CB  SER A 169      27.872   4.963  26.530  1.00112.15           C  
ATOM   1267  OG  SER A 169      28.990   4.952  25.660  1.00131.88           O  
ATOM   1268  N   THR A 170      25.489   4.079  24.742  1.00 67.33           N  
ATOM   1269  CA  THR A 170      24.928   3.395  23.566  1.00 67.33           C  
ATOM   1270  C   THR A 170      24.128   4.414  22.754  1.00 67.33           C  
ATOM   1271  O   THR A 170      24.340   4.527  21.537  1.00 67.33           O  
ATOM   1272  CB  THR A 170      24.079   2.113  23.896  1.00 61.61           C  
ATOM   1273  OG1 THR A 170      25.009   1.131  24.454  1.00 81.34           O  
ATOM   1274  CG2 THR A 170      23.317   1.553  22.686  1.00 81.34           C  
ATOM   1275  N   PHE A 171      23.257   5.134  23.448  1.00 52.72           N  
ATOM   1276  CA  PHE A 171      22.430   6.175  22.830  1.00 52.72           C  
ATOM   1277  C   PHE A 171      23.345   7.226  22.185  1.00 52.72           C  
ATOM   1278  O   PHE A 171      23.080   7.628  21.042  1.00 52.72           O  
ATOM   1279  CB  PHE A 171      21.415   6.836  23.767  1.00 47.00           C  
ATOM   1280  CG  PHE A 171      20.688   7.980  23.108  1.00 63.12           C  
ATOM   1281  CD1 PHE A 171      19.536   7.745  22.359  1.00 63.12           C  
ATOM   1282  CD2 PHE A 171      21.184   9.282  23.221  1.00 63.12           C  
ATOM   1283  CE1 PHE A 171      18.869   8.805  21.733  1.00 63.12           C  
ATOM   1284  CE2 PHE A 171      20.540  10.339  22.604  1.00 63.12           C  
ATOM   1285  CZ  PHE A 171      19.380  10.108  21.863  1.00 63.12           C  
ATOM   1286  N   LYS A 172      24.364   7.650  22.907  1.00 60.34           N  
ATOM   1287  CA  LYS A 172      25.328   8.647  22.445  1.00 60.34           C  
ATOM   1288  C   LYS A 172      25.947   8.280  21.097  1.00 60.34           C  
ATOM   1289  O   LYS A 172      26.013   9.150  20.208  1.00 60.34           O  
ATOM   1290  CB  LYS A 172      26.464   8.895  23.442  1.00 54.62           C  
ATOM   1291  CG  LYS A 172      27.304  10.120  23.062  1.00 74.35           C  
ATOM   1292  CD  LYS A 172      28.794   9.906  23.270  1.00 84.07           C  
ATOM   1293  CE  LYS A 172      29.625  11.008  22.641  1.00119.45           C  
ATOM   1294  NZ  LYS A 172      31.009  10.534  22.385  1.00 81.76           N  
ATOM   1295  N   VAL A 173      26.397   7.041  20.964  1.00 69.58           N  
ATOM   1296  CA  VAL A 173      27.011   6.581  19.700  1.00 69.58           C  
ATOM   1297  C   VAL A 173      25.936   6.422  18.624  1.00 69.58           C  
ATOM   1298  O   VAL A 173      26.121   6.763  17.441  1.00 69.58           O  
ATOM   1299  CB  VAL A 173      27.891   5.345  19.948  1.00 63.86           C  
ATOM   1300  CG1 VAL A 173      27.114   4.079  20.277  1.00 83.59           C  
ATOM   1301  CG2 VAL A 173      28.846   5.111  18.785  1.00 83.59           C  
ATOM   1302  N   LEU A 174      24.798   5.918  19.062  1.00 65.39           N  
ATOM   1303  CA  LEU A 174      23.606   5.665  18.255  1.00 65.39           C  
ATOM   1304  C   LEU A 174      23.095   6.916  17.550  1.00 65.39           C  
ATOM   1305  O   LEU A 174      22.736   6.837  16.362  1.00 65.39           O  
ATOM   1306  CB  LEU A 174      22.583   5.005  19.187  1.00 59.67           C  
ATOM   1307  CG  LEU A 174      21.506   4.120  18.598  1.00 79.40           C  
ATOM   1308  CD1 LEU A 174      21.054   3.070  19.609  1.00 89.12           C  
ATOM   1309  CD2 LEU A 174      20.318   4.992  18.193  1.00 89.12           C  
ATOM   1310  N   ARG A 175      23.059   8.032  18.250  1.00 55.13           N  
ATOM   1311  CA  ARG A 175      22.604   9.332  17.757  1.00 55.13           C  
ATOM   1312  C   ARG A 175      23.559   9.894  16.704  1.00 55.13           C  
ATOM   1313  O   ARG A 175      23.105  10.482  15.710  1.00 55.13           O  
ATOM   1314  CB  ARG A 175      22.397  10.369  18.869  1.00 49.41           C  
ATOM   1315  CG  ARG A 175      23.662  10.858  19.540  1.00 69.14           C  
ATOM   1316  CD  ARG A 175      23.486  11.833  20.644  1.00 78.86           C  
ATOM   1317  NE  ARG A 175      24.714  11.968  21.425  1.00114.24           N  
ATOM   1318  CZ  ARG A 175      25.042  13.029  22.159  1.00 76.55           C  
ATOM   1319  NH1 ARG A 175      24.256  14.099  22.238  1.00120.01           N  
ATOM   1320  NH2 ARG A 175      26.187  13.029  22.843  1.00120.01           N  
ATOM   1321  N   ASN A 176      24.844   9.711  16.946  1.00 51.74           N  
ATOM   1322  CA  ASN A 176      25.904  10.182  16.036  1.00 51.74           C  
ATOM   1323  C   ASN A 176      25.768   9.414  14.717  1.00 51.74           C  
ATOM   1324  O   ASN A 176      25.617  10.026  13.644  1.00 51.74           O  
ATOM   1325  CB  ASN A 176      27.270  10.089  16.695  1.00 46.02           C  
ATOM   1326  CG  ASN A 176      27.407  10.879  17.982  1.00 65.75           C  
ATOM   1327  OD1 ASN A 176      26.646  11.817  18.265  1.00 75.47           O  
ATOM   1328  ND2 ASN A 176      28.400  10.502  18.791  1.00 75.47           N  
ATOM   1329  N   VAL A 177      25.795   8.092  14.852  1.00 63.74           N  
ATOM   1330  CA  VAL A 177      25.659   7.193  13.686  1.00 63.74           C  
ATOM   1331  C   VAL A 177      24.391   7.586  12.918  1.00 63.74           C  
ATOM   1332  O   VAL A 177      24.442   7.902  11.717  1.00 63.74           O  
ATOM   1333  CB  VAL A 177      25.700   5.719  14.122  1.00 58.02           C  
ATOM   1334  CG1 VAL A 177      25.410   4.742  12.983  1.00 77.75           C  
ATOM   1335  CG2 VAL A 177      27.012   5.344  14.796  1.00 77.75           C  
ATOM   1336  N   THR A 178      23.283   7.573  13.641  1.00 82.00           N  
ATOM   1337  CA  THR A 178      21.959   7.928  13.116  1.00 82.00           C  
ATOM   1338  C   THR A 178      22.046   9.215  12.306  1.00 82.00           C  
ATOM   1339  O   THR A 178      21.847   9.182  11.080  1.00 82.00           O  
ATOM   1340  CB  THR A 178      20.875   7.988  14.262  1.00 76.28           C  
ATOM   1341  OG1 THR A 178      20.529   6.594  14.566  1.00 96.01           O  
ATOM   1342  CG2 THR A 178      19.625   8.814  13.956  1.00 96.01           C  
ATOM   1343  N   VAL A 179      22.370  10.311  12.966  1.00 92.98           N  
ATOM   1344  CA  VAL A 179      22.496  11.630  12.326  1.00 92.98           C  
ATOM   1345  C   VAL A 179      23.304  11.528  11.031  1.00 92.98           C  
ATOM   1346  O   VAL A 179      22.790  11.834   9.940  1.00 92.98           O  
ATOM   1347  CB  VAL A 179      23.051  12.665  13.324  1.00 87.26           C  
ATOM   1348  CG1 VAL A 179      23.572  13.937  12.660  1.00106.99           C  
ATOM   1349  CG2 VAL A 179      22.029  13.026  14.394  1.00106.99           C  
ATOM   1350  N   VAL A 180      24.542  11.098  11.177  1.00 86.88           N  
ATOM   1351  CA  VAL A 180      25.479  10.936  10.055  1.00 86.88           C  
ATOM   1352  C   VAL A 180      24.842  10.258   8.846  1.00 86.88           C  
ATOM   1353  O   VAL A 180      24.616  10.860   7.775  1.00 86.88           O  
ATOM   1354  CB  VAL A 180      26.729  10.206  10.597  1.00 81.16           C  
ATOM   1355  CG1 VAL A 180      27.589   9.553   9.525  1.00100.89           C  
ATOM   1356  CG2 VAL A 180      27.566  11.143  11.459  1.00100.89           C  
ATOM   1357  N   LEU A 181      24.543   8.986   9.039  1.00 68.77           N  
ATOM   1358  CA  LEU A 181      23.936   8.110   8.031  1.00 68.77           C  
ATOM   1359  C   LEU A 181      22.723   8.759   7.377  1.00 68.77           C  
ATOM   1360  O   LEU A 181      22.592   8.857   6.141  1.00 68.77           O  
ATOM   1361  CB  LEU A 181      23.642   6.773   8.723  1.00 63.05           C  
ATOM   1362  CG  LEU A 181      24.723   5.722   8.858  1.00 82.78           C  
ATOM   1363  CD1 LEU A 181      25.027   5.085   7.504  1.00 92.50           C  
ATOM   1364  CD2 LEU A 181      26.000   6.328   9.443  1.00 92.50           C  
ATOM   1365  N   TRP A 182      21.831   9.224   8.229  1.00 47.49           N  
ATOM   1366  CA  TRP A 182      20.570   9.882   7.880  1.00 47.49           C  
ATOM   1367  C   TRP A 182      20.742  11.210   7.156  1.00 47.49           C  
ATOM   1368  O   TRP A 182      19.747  11.645   6.532  1.00 47.49           O  
ATOM   1369  CB  TRP A 182      19.648   9.891   9.101  1.00 41.77           C  
ATOM   1370  CG  TRP A 182      19.212   8.548   9.585  1.00 57.89           C  
ATOM   1371  CD1 TRP A 182      19.908   7.369   9.556  1.00 57.89           C  
ATOM   1372  CD2 TRP A 182      17.959   8.233  10.218  1.00 57.89           C  
ATOM   1373  NE1 TRP A 182      19.176   6.349  10.109  1.00 57.89           N  
ATOM   1374  CE2 TRP A 182      17.977   6.854  10.524  1.00 57.89           C  
ATOM   1375  CE3 TRP A 182      16.838   8.990  10.541  1.00 57.89           C  
ATOM   1376  CZ2 TRP A 182      16.912   6.212  11.140  1.00 57.89           C  
ATOM   1377  CZ3 TRP A 182      15.777   8.356  11.153  1.00 57.89           C  
ATOM   1378  CH2 TRP A 182      15.813   6.995  11.450  1.00 57.89           C  
ATOM   1379  N   SER A 183      21.886  11.862   7.212  1.00 30.28           N  
ATOM   1380  CA  SER A 183      22.153  13.130   6.503  1.00 30.28           C  
ATOM   1381  C   SER A 183      22.668  12.737   5.106  1.00 30.28           C  
ATOM   1382  O   SER A 183      22.339  13.259   4.014  1.00 30.28           O  
ATOM   1383  CB  SER A 183      23.132  14.016   7.240  1.00 24.56           C  
ATOM   1384  OG  SER A 183      22.679  14.326   8.546  1.00 44.29           O  
ATOM   1385  N   ALA A 184      23.489  11.685   5.202  1.00 18.13           N  
ATOM   1386  CA  ALA A 184      24.107  11.070   4.013  1.00 18.13           C  
ATOM   1387  C   ALA A 184      22.993  10.686   3.035  1.00 18.13           C  
ATOM   1388  O   ALA A 184      23.108  10.996   1.835  1.00 18.13           O  
ATOM   1389  CB  ALA A 184      24.998   9.908   4.403  1.00 12.41           C  
ATOM   1390  N   TYR A 185      21.949  10.048   3.552  1.00 10.46           N  
ATOM   1391  CA  TYR A 185      20.805   9.640   2.720  1.00 10.46           C  
ATOM   1392  C   TYR A 185      20.419  10.732   1.737  1.00 10.46           C  
ATOM   1393  O   TYR A 185      20.690  10.586   0.530  1.00 10.46           O  
ATOM   1394  CB  TYR A 185      19.629   9.121   3.560  1.00  5.00           C  
ATOM   1395  CG  TYR A 185      19.876   7.712   4.051  1.00 20.86           C  
ATOM   1396  CD1 TYR A 185      20.030   6.683   3.119  1.00 20.86           C  
ATOM   1397  CD2 TYR A 185      19.971   7.406   5.406  1.00 20.86           C  
ATOM   1398  CE1 TYR A 185      20.270   5.375   3.524  1.00 20.86           C  
ATOM   1399  CE2 TYR A 185      20.218   6.101   5.829  1.00 20.86           C  
ATOM   1400  CZ  TYR A 185      20.363   5.088   4.880  1.00 20.86           C  
ATOM   1401  OH  TYR A 185      20.585   3.789   5.246  1.00 34.19           O  
ATOM   1402  N   PRO A 186      19.839  11.810   2.238  1.00  6.67           N  
ATOM   1403  CA  PRO A 186      19.420  12.946   1.414  1.00  6.67           C  
ATOM   1404  C   PRO A 186      20.524  13.468   0.507  1.00  6.67           C  
ATOM   1405  O   PRO A 186      20.155  13.720  -0.667  1.00  6.67           O  
ATOM   1406  CB  PRO A 186      18.899  14.017   2.366  1.00  5.00           C  
ATOM   1407  CG  PRO A 186      19.339  13.576   3.732  1.00  5.00           C  
ATOM   1408  CD  PRO A 186      19.487  12.062   3.639  1.00  5.00           C  
ATOM   1409  N   VAL A 187      21.758  13.607   1.014  1.00  6.56           N  
ATOM   1410  CA  VAL A 187      22.771  14.119   0.043  1.00  6.56           C  
ATOM   1411  C   VAL A 187      22.916  13.171  -1.151  1.00  6.56           C  
ATOM   1412  O   VAL A 187      22.798  13.620  -2.319  1.00  6.56           O  
ATOM   1413  CB  VAL A 187      24.084  14.552   0.698  1.00  5.00           C  
ATOM   1414  CG1 VAL A 187      25.249  14.629  -0.288  1.00 20.57           C  
ATOM   1415  CG2 VAL A 187      23.932  15.900   1.395  1.00 20.57           C  
ATOM   1416  N   VAL A 188      23.146  11.896  -0.874  1.00 11.37           N  
ATOM   1417  CA  VAL A 188      23.307  10.887  -1.936  1.00 11.37           C  
ATOM   1418  C   VAL A 188      22.089  10.892  -2.862  1.00 11.37           C  
ATOM   1419  O   VAL A 188      22.262  10.901  -4.095  1.00 11.37           O  
ATOM   1420  CB  VAL A 188      23.664   9.502  -1.378  1.00  5.65           C  
ATOM   1421  CG1 VAL A 188      23.701   8.425  -2.463  1.00 25.38           C  
ATOM   1422  CG2 VAL A 188      24.982   9.505  -0.613  1.00 25.38           C  
ATOM   1423  N   TRP A 189      20.910  10.892  -2.274  1.00 22.71           N  
ATOM   1424  CA  TRP A 189      19.645  10.911  -3.021  1.00 22.71           C  
ATOM   1425  C   TRP A 189      19.681  12.079  -4.012  1.00 22.71           C  
ATOM   1426  O   TRP A 189      19.653  11.868  -5.235  1.00 22.71           O  
ATOM   1427  CB  TRP A 189      18.453  11.000  -2.087  1.00 16.99           C  
ATOM   1428  CG  TRP A 189      17.095  10.743  -2.632  1.00 33.11           C  
ATOM   1429  CD1 TRP A 189      16.375   9.580  -2.560  1.00 33.11           C  
ATOM   1430  CD2 TRP A 189      16.256  11.678  -3.330  1.00 33.11           C  
ATOM   1431  NE1 TRP A 189      15.152   9.737  -3.162  1.00 33.11           N  
ATOM   1432  CE2 TRP A 189      15.053  11.010  -3.646  1.00 33.11           C  
ATOM   1433  CE3 TRP A 189      16.420  13.000  -3.725  1.00 33.11           C  
ATOM   1434  CZ2 TRP A 189      14.019  11.631  -4.331  1.00 33.11           C  
ATOM   1435  CZ3 TRP A 189      15.389  13.622  -4.401  1.00 33.11           C  
ATOM   1436  CH2 TRP A 189      14.207  12.954  -4.703  1.00 33.11           C  
ATOM   1437  N   LEU A 190      19.765  13.279  -3.463  1.00 40.13           N  
ATOM   1438  CA  LEU A 190      19.803  14.491  -4.285  1.00 40.13           C  
ATOM   1439  C   LEU A 190      20.787  14.368  -5.447  1.00 40.13           C  
ATOM   1440  O   LEU A 190      20.373  14.449  -6.618  1.00 40.13           O  
ATOM   1441  CB  LEU A 190      20.086  15.692  -3.375  1.00 34.41           C  
ATOM   1442  CG  LEU A 190      20.571  16.980  -4.025  1.00 54.14           C  
ATOM   1443  CD1 LEU A 190      19.623  17.470  -5.114  1.00 63.86           C  
ATOM   1444  CD2 LEU A 190      20.707  18.045  -2.935  1.00 63.86           C  
ATOM   1445  N   ILE A 191      22.049  14.181  -5.101  1.00 54.89           N  
ATOM   1446  CA  ILE A 191      23.113  14.076  -6.114  1.00 54.89           C  
ATOM   1447  C   ILE A 191      22.940  12.994  -7.159  1.00 54.89           C  
ATOM   1448  O   ILE A 191      23.021  13.323  -8.367  1.00 54.89           O  
ATOM   1449  CB  ILE A 191      24.500  14.107  -5.366  1.00 49.17           C  
ATOM   1450  CG1 ILE A 191      24.918  15.601  -5.277  1.00 68.90           C  
ATOM   1451  CG2 ILE A 191      25.592  13.211  -5.986  1.00 68.90           C  
ATOM   1452  CD1 ILE A 191      26.132  15.906  -4.369  1.00 78.62           C  
ATOM   1453  N   GLY A 192      22.714  11.754  -6.775  1.00 56.19           N  
ATOM   1454  CA  GLY A 192      22.554  10.648  -7.721  1.00 56.19           C  
ATOM   1455  C   GLY A 192      21.117  10.241  -8.006  1.00 56.19           C  
ATOM   1456  O   GLY A 192      20.238  11.038  -8.359  1.00 56.19           O  
ATOM   1457  N   SER A 193      20.910   8.949  -7.858  1.00 38.64           N  
ATOM   1458  CA  SER A 193      19.676   8.204  -8.042  1.00 38.64           C  
ATOM   1459  C   SER A 193      18.552   8.961  -8.746  1.00 38.64           C  
ATOM   1460  O   SER A 193      18.541   9.082  -9.984  1.00 38.64           O  
ATOM   1461  CB  SER A 193      19.168   7.613  -6.724  1.00 32.92           C  
ATOM   1462  OG  SER A 193      19.761   6.361  -6.441  1.00 52.65           O  
ATOM   1463  N   GLU A 194      17.617   9.436  -7.944  1.00 18.59           N  
ATOM   1464  CA  GLU A 194      16.435  10.165  -8.398  1.00 18.59           C  
ATOM   1465  C   GLU A 194      16.419  11.664  -8.183  1.00 18.59           C  
ATOM   1466  O   GLU A 194      15.338  12.279  -8.072  1.00 18.59           O  
ATOM   1467  CB  GLU A 194      15.206   9.577  -7.675  1.00 12.87           C  
ATOM   1468  CG  GLU A 194      14.684   8.254  -8.251  1.00 32.60           C  
ATOM   1469  CD  GLU A 194      14.026   8.414  -9.594  1.00 42.32           C  
ATOM   1470  OE1 GLU A 194      14.587   8.879 -10.573  1.00 77.70           O  
ATOM   1471  OE2 GLU A 194      12.835   8.033  -9.585  1.00 77.70           O  
ATOM   1472  N   GLY A 195      17.598  12.253  -8.142  1.00 17.82           N  
ATOM   1473  CA  GLY A 195      17.751  13.701  -7.936  1.00 17.82           C  
ATOM   1474  C   GLY A 195      18.120  14.366  -9.262  1.00 17.82           C  
ATOM   1475  O   GLY A 195      17.252  14.613 -10.114  1.00 17.82           O  
ATOM   1476  N   ALA A 196      19.408  14.638  -9.377  1.00 50.57           N  
ATOM   1477  CA  ALA A 196      19.976  15.284 -10.566  1.00 50.57           C  
ATOM   1478  C   ALA A 196      20.521  14.239 -11.539  1.00 50.57           C  
ATOM   1479  O   ALA A 196      20.129  14.184 -12.715  1.00 50.57           O  
ATOM   1480  CB  ALA A 196      21.071  16.263 -10.159  1.00 44.85           C  
ATOM   1481  N   GLY A 197      21.420  13.442 -10.991  1.00101.08           N  
ATOM   1482  CA  GLY A 197      22.089  12.366 -11.738  1.00101.08           C  
ATOM   1483  C   GLY A 197      23.542  12.792 -11.978  1.00101.08           C  
ATOM   1484  O   GLY A 197      24.077  12.679 -13.090  1.00101.08           O  
ATOM   1485  N   ILE A 198      24.137  13.274 -10.898  1.00146.07           N  
ATOM   1486  CA  ILE A 198      25.534  13.735 -10.894  1.00146.07           C  
ATOM   1487  C   ILE A 198      26.453  12.516 -10.977  1.00146.07           C  
ATOM   1488  O   ILE A 198      27.480  12.560 -11.672  1.00146.07           O  
ATOM   1489  CB  ILE A 198      25.825  14.681  -9.684  1.00140.35           C  
ATOM   1490  CG1 ILE A 198      24.833  15.871  -9.696  1.00160.08           C  
ATOM   1491  CG2 ILE A 198      27.297  15.168  -9.637  1.00160.08           C  
ATOM   1492  CD1 ILE A 198      24.889  16.774 -10.957  1.00169.80           C  
ATOM   1493  N   VAL A 199      26.061  11.465 -10.278  1.00167.12           N  
ATOM   1494  CA  VAL A 199      26.801  10.195 -10.257  1.00167.12           C  
ATOM   1495  C   VAL A 199      26.185   9.307 -11.350  1.00167.12           C  
ATOM   1496  O   VAL A 199      24.980   9.433 -11.616  1.00167.12           O  
ATOM   1497  CB  VAL A 199      26.784   9.533  -8.871  1.00161.40           C  
ATOM   1498  CG1 VAL A 199      27.236  10.463  -7.750  1.00181.13           C  
ATOM   1499  CG2 VAL A 199      25.438   8.912  -8.527  1.00181.13           C  
ATOM   1500  N   PRO A 200      27.023   8.460 -11.922  1.00165.24           N  
ATOM   1501  CA  PRO A 200      26.599   7.537 -12.978  1.00165.24           C  
ATOM   1502  C   PRO A 200      25.327   6.787 -12.603  1.00165.24           C  
ATOM   1503  O   PRO A 200      24.203   7.250 -12.866  1.00165.24           O  
ATOM   1504  CB  PRO A 200      27.799   6.618 -13.191  1.00159.52           C  
ATOM   1505  CG  PRO A 200      28.989   7.392 -12.697  1.00159.52           C  
ATOM   1506  CD  PRO A 200      28.454   8.312 -11.610  1.00159.52           C  
ATOM   1507  N   LEU A 201      25.509   5.627 -11.999  1.00146.27           N  
ATOM   1508  CA  LEU A 201      24.411   4.751 -11.562  1.00146.27           C  
ATOM   1509  C   LEU A 201      24.884   3.880 -10.403  1.00146.27           C  
ATOM   1510  O   LEU A 201      24.329   3.866  -9.298  1.00146.27           O  
ATOM   1511  CB  LEU A 201      23.913   3.981 -12.786  1.00140.55           C  
ATOM   1512  CG  LEU A 201      22.756   3.012 -12.635  1.00160.28           C  
ATOM   1513  CD1 LEU A 201      22.082   2.757 -13.982  1.00170.00           C  
ATOM   1514  CD2 LEU A 201      23.272   1.683 -12.085  1.00170.00           C  
ATOM   1515  N   ASN A 202      25.949   3.156 -10.674  1.00116.41           N  
ATOM   1516  CA  ASN A 202      26.633   2.233  -9.758  1.00116.41           C  
ATOM   1517  C   ASN A 202      26.636   2.828  -8.347  1.00116.41           C  
ATOM   1518  O   ASN A 202      26.088   2.321  -7.356  1.00116.41           O  
ATOM   1519  CB  ASN A 202      28.045   1.954 -10.280  1.00110.69           C  
ATOM   1520  CG  ASN A 202      28.228   2.245 -11.758  1.00130.42           C  
ATOM   1521  OD1 ASN A 202      28.051   1.374 -12.620  1.00140.14           O  
ATOM   1522  ND2 ASN A 202      28.578   3.494 -12.073  1.00140.14           N  
ATOM   1523  N   ILE A 203      27.278   3.981  -8.297  1.00 83.15           N  
ATOM   1524  CA  ILE A 203      27.473   4.845  -7.144  1.00 83.15           C  
ATOM   1525  C   ILE A 203      26.225   4.921  -6.274  1.00 83.15           C  
ATOM   1526  O   ILE A 203      26.327   4.705  -5.055  1.00 83.15           O  
ATOM   1527  CB  ILE A 203      27.923   6.273  -7.637  1.00 77.43           C  
ATOM   1528  CG1 ILE A 203      29.087   6.151  -8.648  1.00 97.16           C  
ATOM   1529  CG2 ILE A 203      28.259   7.233  -6.469  1.00 97.16           C  
ATOM   1530  CD1 ILE A 203      30.365   5.439  -8.139  1.00106.88           C  
ATOM   1531  N   GLU A 204      25.080   5.204  -6.877  1.00 54.32           N  
ATOM   1532  CA  GLU A 204      23.808   5.300  -6.147  1.00 54.32           C  
ATOM   1533  C   GLU A 204      23.655   4.081  -5.240  1.00 54.32           C  
ATOM   1534  O   GLU A 204      23.527   4.181  -4.007  1.00 54.32           O  
ATOM   1535  CB  GLU A 204      22.601   5.435  -7.066  1.00 48.60           C  
ATOM   1536  CG  GLU A 204      21.887   4.238  -7.643  1.00 68.33           C  
ATOM   1537  CD  GLU A 204      20.894   4.329  -8.746  1.00 78.05           C  
ATOM   1538  OE1 GLU A 204      19.735   4.685  -8.608  1.00113.43           O  
ATOM   1539  OE2 GLU A 204      21.368   3.971  -9.850  1.00113.43           O  
ATOM   1540  N   THR A 205      23.715   2.922  -5.864  1.00 37.75           N  
ATOM   1541  CA  THR A 205      23.587   1.608  -5.255  1.00 37.75           C  
ATOM   1542  C   THR A 205      24.633   1.367  -4.174  1.00 37.75           C  
ATOM   1543  O   THR A 205      24.251   0.945  -3.071  1.00 37.75           O  
ATOM   1544  CB  THR A 205      23.644   0.459  -6.341  1.00 32.03           C  
ATOM   1545  OG1 THR A 205      22.731   0.883  -7.402  1.00 51.76           O  
ATOM   1546  CG2 THR A 205      23.299  -0.924  -5.787  1.00 51.76           C  
ATOM   1547  N   LEU A 206      25.879   1.636  -4.532  1.00 37.93           N  
ATOM   1548  CA  LEU A 206      26.993   1.444  -3.593  1.00 37.93           C  
ATOM   1549  C   LEU A 206      26.875   2.296  -2.331  1.00 37.93           C  
ATOM   1550  O   LEU A 206      26.929   1.765  -1.210  1.00 37.93           O  
ATOM   1551  CB  LEU A 206      28.321   1.660  -4.342  1.00 32.21           C  
ATOM   1552  CG  LEU A 206      29.560   1.707  -3.450  1.00 51.94           C  
ATOM   1553  CD1 LEU A 206      29.761   0.382  -2.722  1.00 61.66           C  
ATOM   1554  CD2 LEU A 206      30.775   2.034  -4.312  1.00 61.66           C  
ATOM   1555  N   LEU A 207      26.735   3.590  -2.507  1.00 46.08           N  
ATOM   1556  CA  LEU A 207      26.611   4.586  -1.441  1.00 46.08           C  
ATOM   1557  C   LEU A 207      25.416   4.307  -0.534  1.00 46.08           C  
ATOM   1558  O   LEU A 207      25.527   4.156   0.699  1.00 46.08           O  
ATOM   1559  CB  LEU A 207      26.565   5.961  -2.124  1.00 40.36           C  
ATOM   1560  CG  LEU A 207      27.894   6.625  -2.445  1.00 60.09           C  
ATOM   1561  CD1 LEU A 207      28.746   5.797  -3.398  1.00 69.81           C  
ATOM   1562  CD2 LEU A 207      27.595   7.993  -3.060  1.00 69.81           C  
ATOM   1563  N   PHE A 208      24.275   4.222  -1.204  1.00 50.08           N  
ATOM   1564  CA  PHE A 208      22.991   3.946  -0.523  1.00 50.08           C  
ATOM   1565  C   PHE A 208      23.088   2.630   0.246  1.00 50.08           C  
ATOM   1566  O   PHE A 208      22.629   2.592   1.410  1.00 50.08           O  
ATOM   1567  CB  PHE A 208      21.832   4.122  -1.485  1.00 44.36           C  
ATOM   1568  CG  PHE A 208      21.097   5.428  -1.449  1.00 60.48           C  
ATOM   1569  CD1 PHE A 208      21.451   6.459  -0.582  1.00 60.48           C  
ATOM   1570  CD2 PHE A 208      19.993   5.602  -2.293  1.00 60.48           C  
ATOM   1571  CE1 PHE A 208      20.734   7.656  -0.564  1.00 60.48           C  
ATOM   1572  CE2 PHE A 208      19.268   6.784  -2.297  1.00 60.48           C  
ATOM   1573  CZ  PHE A 208      19.638   7.812  -1.428  1.00 60.48           C  
ATOM   1574  N   MET A 209      23.677   1.597  -0.338  1.00 41.48           N  
ATOM   1575  CA  MET A 209      23.850   0.297   0.333  1.00 41.48           C  
ATOM   1576  C   MET A 209      24.784   0.468   1.535  1.00 41.48           C  
ATOM   1577  O   MET A 209      24.470  -0.047   2.625  1.00 41.48           O  
ATOM   1578  CB  MET A 209      24.318  -0.795  -0.611  1.00 35.76           C  
ATOM   1579  CG  MET A 209      24.557  -2.111   0.085  1.00 55.49           C  
ATOM   1580  SD  MET A 209      26.316  -2.165   0.582  1.00 65.21           S  
ATOM   1581  CE  MET A 209      26.266  -3.479   1.808  1.00100.59           C  
ATOM   1582  N   VAL A 210      25.882   1.179   1.335  1.00 26.44           N  
ATOM   1583  CA  VAL A 210      26.883   1.453   2.379  1.00 26.44           C  
ATOM   1584  C   VAL A 210      26.121   1.935   3.625  1.00 26.44           C  
ATOM   1585  O   VAL A 210      26.197   1.335   4.709  1.00 26.44           O  
ATOM   1586  CB  VAL A 210      27.977   2.440   1.937  1.00 20.72           C  
ATOM   1587  CG1 VAL A 210      28.775   3.021   3.109  1.00 40.45           C  
ATOM   1588  CG2 VAL A 210      28.972   1.870   0.937  1.00 40.45           C  
ATOM   1589  N   LEU A 211      25.392   3.020   3.388  1.00 14.81           N  
ATOM   1590  CA  LEU A 211      24.575   3.629   4.448  1.00 14.81           C  
ATOM   1591  C   LEU A 211      23.622   2.596   5.045  1.00 14.81           C  
ATOM   1592  O   LEU A 211      23.618   2.409   6.273  1.00 14.81           O  
ATOM   1593  CB  LEU A 211      23.887   4.863   3.870  1.00  9.09           C  
ATOM   1594  CG  LEU A 211      24.666   6.163   3.822  1.00 28.82           C  
ATOM   1595  CD1 LEU A 211      26.125   5.977   3.420  1.00 38.54           C  
ATOM   1596  CD2 LEU A 211      23.981   7.067   2.790  1.00 38.54           C  
ATOM   1597  N   ASP A 212      22.840   1.960   4.190  1.00 13.94           N  
ATOM   1598  CA  ASP A 212      21.864   0.949   4.620  1.00 13.94           C  
ATOM   1599  C   ASP A 212      22.475   0.003   5.653  1.00 13.94           C  
ATOM   1600  O   ASP A 212      22.188   0.082   6.860  1.00 13.94           O  
ATOM   1601  CB  ASP A 212      21.265   0.205   3.427  1.00  8.22           C  
ATOM   1602  CG  ASP A 212      20.137   0.947   2.736  1.00 27.95           C  
ATOM   1603  OD1 ASP A 212      19.626   1.958   3.243  1.00 37.67           O  
ATOM   1604  OD2 ASP A 212      19.752   0.484   1.638  1.00 37.67           O  
ATOM   1605  N   VAL A 213      23.337  -0.863   5.146  1.00 21.37           N  
ATOM   1606  CA  VAL A 213      24.027  -1.889   5.946  1.00 21.37           C  
ATOM   1607  C   VAL A 213      24.689  -1.313   7.192  1.00 21.37           C  
ATOM   1608  O   VAL A 213      24.561  -1.942   8.265  1.00 21.37           O  
ATOM   1609  CB  VAL A 213      24.922  -2.766   5.047  1.00 15.65           C  
ATOM   1610  CG1 VAL A 213      26.406  -2.448   5.110  1.00 35.38           C  
ATOM   1611  CG2 VAL A 213      24.662  -4.248   5.305  1.00 35.38           C  
ATOM   1612  N   SER A 214      25.351  -0.178   7.049  1.00 32.15           N  
ATOM   1613  CA  SER A 214      26.023   0.482   8.176  1.00 32.15           C  
ATOM   1614  C   SER A 214      25.039   0.880   9.277  1.00 32.15           C  
ATOM   1615  O   SER A 214      25.298   0.639  10.468  1.00 32.15           O  
ATOM   1616  CB  SER A 214      26.824   1.701   7.738  1.00 26.43           C  
ATOM   1617  OG  SER A 214      27.954   1.336   6.966  1.00 46.16           O  
ATOM   1618  N   ALA A 215      23.947   1.499   8.880  1.00 41.64           N  
ATOM   1619  CA  ALA A 215      22.899   1.973   9.782  1.00 41.64           C  
ATOM   1620  C   ALA A 215      22.186   0.817  10.477  1.00 41.64           C  
ATOM   1621  O   ALA A 215      22.138   0.816  11.721  1.00 41.64           O  
ATOM   1622  CB  ALA A 215      21.930   2.893   9.048  1.00 35.92           C  
ATOM   1623  N   LYS A 216      21.672  -0.123   9.703  1.00 46.22           N  
ATOM   1624  CA  LYS A 216      20.941  -1.279  10.236  1.00 46.22           C  
ATOM   1625  C   LYS A 216      21.774  -2.281  11.020  1.00 46.22           C  
ATOM   1626  O   LYS A 216      21.417  -2.603  12.179  1.00 46.22           O  
ATOM   1627  CB  LYS A 216      20.177  -1.995   9.128  1.00 40.50           C  
ATOM   1628  CG  LYS A 216      18.702  -1.589   9.090  1.00 17.34           C  
ATOM   1629  CD  LYS A 216      17.913  -2.110   7.892  1.00 17.34           C  
ATOM   1630  CE  LYS A 216      18.418  -1.619   6.549  1.00 17.34           C  
ATOM   1631  NZ  LYS A 216      18.077  -0.337   6.073  1.00 17.34           N  
ATOM   1632  N   VAL A 217      22.843  -2.757  10.394  1.00 42.58           N  
ATOM   1633  CA  VAL A 217      23.719  -3.751  11.058  1.00 42.58           C  
ATOM   1634  C   VAL A 217      24.536  -3.057  12.148  1.00 42.58           C  
ATOM   1635  O   VAL A 217      24.736  -3.643  13.229  1.00 42.58           O  
ATOM   1636  CB  VAL A 217      24.472  -4.607  10.033  1.00 36.86           C  
ATOM   1637  CG1 VAL A 217      25.980  -4.417  10.019  1.00 56.59           C  
ATOM   1638  CG2 VAL A 217      24.134  -6.086  10.196  1.00 56.59           C  
ATOM   1639  N   GLY A 218      24.970  -1.843  11.864  1.00 29.75           N  
ATOM   1640  CA  GLY A 218      25.756  -1.034  12.808  1.00 29.75           C  
ATOM   1641  C   GLY A 218      24.944  -0.770  14.073  1.00 29.75           C  
ATOM   1642  O   GLY A 218      25.391  -1.123  15.181  1.00 29.75           O  
ATOM   1643  N   PHE A 219      23.764  -0.191  13.890  1.00 16.29           N  
ATOM   1644  CA  PHE A 219      22.858   0.116  15.024  1.00 16.29           C  
ATOM   1645  C   PHE A 219      22.518  -1.191  15.744  1.00 16.29           C  
ATOM   1646  O   PHE A 219      22.499  -1.219  16.991  1.00 16.29           O  
ATOM   1647  CB  PHE A 219      21.674   0.959  14.609  1.00 10.57           C  
ATOM   1648  CG  PHE A 219      20.427   0.967  15.428  1.00 26.69           C  
ATOM   1649  CD1 PHE A 219      19.580  -0.149  15.405  1.00 26.69           C  
ATOM   1650  CD2 PHE A 219      20.065   2.072  16.198  1.00 26.69           C  
ATOM   1651  CE1 PHE A 219      18.407  -0.192  16.143  1.00 26.69           C  
ATOM   1652  CE2 PHE A 219      18.883   2.062  16.952  1.00 26.69           C  
ATOM   1653  CZ  PHE A 219      18.058   0.920  16.916  1.00 26.69           C  
ATOM   1654  N   GLY A 220      22.271  -2.244  14.973  1.00 13.10           N  
ATOM   1655  CA  GLY A 220      21.961  -3.567  15.536  1.00 13.10           C  
ATOM   1656  C   GLY A 220      23.079  -3.995  16.490  1.00 13.10           C  
ATOM   1657  O   GLY A 220      22.809  -4.495  17.596  1.00 13.10           O  
ATOM   1658  N   LEU A 221      24.309  -3.805  16.060  1.00 31.10           N  
ATOM   1659  CA  LEU A 221      25.535  -4.126  16.788  1.00 31.10           C  
ATOM   1660  C   LEU A 221      25.764  -3.233  18.004  1.00 31.10           C  
ATOM   1661  O   LEU A 221      26.305  -3.703  19.024  1.00 31.10           O  
ATOM   1662  CB  LEU A 221      26.683  -4.083  15.770  1.00 25.38           C  
ATOM   1663  CG  LEU A 221      27.721  -5.191  15.834  1.00 45.11           C  
ATOM   1664  CD1 LEU A 221      27.092  -6.554  15.552  1.00 54.83           C  
ATOM   1665  CD2 LEU A 221      28.807  -4.867  14.806  1.00 54.83           C  
ATOM   1666  N   ILE A 222      25.360  -1.980  17.906  1.00 75.50           N  
ATOM   1667  CA  ILE A 222      25.481  -0.993  18.990  1.00 75.50           C  
ATOM   1668  C   ILE A 222      24.507  -1.373  20.106  1.00 75.50           C  
ATOM   1669  O   ILE A 222      24.780  -1.230  21.309  1.00 75.50           O  
ATOM   1670  CB  ILE A 222      25.302   0.467  18.453  1.00 69.78           C  
ATOM   1671  CG1 ILE A 222      26.568   0.885  17.660  1.00 89.51           C  
ATOM   1672  CG2 ILE A 222      24.953   1.491  19.565  1.00 89.51           C  
ATOM   1673  CD1 ILE A 222      26.443   2.225  16.883  1.00 99.23           C  
ATOM   1674  N   LEU A 223      23.363  -1.877  19.670  1.00128.75           N  
ATOM   1675  CA  LEU A 223      22.260  -2.347  20.520  1.00128.75           C  
ATOM   1676  C   LEU A 223      22.622  -3.707  21.122  1.00128.75           C  
ATOM   1677  O   LEU A 223      22.154  -4.111  22.200  1.00128.75           O  
ATOM   1678  CB  LEU A 223      20.985  -2.297  19.681  1.00123.03           C  
ATOM   1679  CG  LEU A 223      19.708  -1.823  20.355  1.00142.76           C  
ATOM   1680  CD1 LEU A 223      19.800  -0.353  20.750  1.00152.48           C  
ATOM   1681  CD2 LEU A 223      18.558  -2.036  19.372  1.00152.48           C  
ATOM   1682  N   LEU A 224      23.475  -4.411  20.397  1.00167.55           N  
ATOM   1683  CA  LEU A 224      24.025  -5.726  20.762  1.00167.55           C  
ATOM   1684  C   LEU A 224      25.011  -5.475  21.910  1.00167.55           C  
ATOM   1685  O   LEU A 224      25.088  -6.222  22.893  1.00167.55           O  
ATOM   1686  CB  LEU A 224      24.580  -6.367  19.504  1.00161.83           C  
ATOM   1687  CG  LEU A 224      25.678  -7.401  19.481  1.00181.56           C  
ATOM   1688  CD1 LEU A 224      27.044  -6.789  19.785  1.00191.28           C  
ATOM   1689  CD2 LEU A 224      25.375  -8.510  20.486  1.00191.28           C  
ATOM   1690  N   ARG A 225      25.752  -4.394  21.746  1.00182.10           N  
ATOM   1691  CA  ARG A 225      26.754  -3.903  22.696  1.00182.10           C  
ATOM   1692  C   ARG A 225      26.045  -3.472  23.984  1.00182.10           C  
ATOM   1693  O   ARG A 225      26.463  -3.832  25.094  1.00182.10           O  
ATOM   1694  CB  ARG A 225      27.543  -2.735  22.109  1.00176.38           C  
ATOM   1695  CG  ARG A 225      28.333  -1.891  23.098  1.00196.11           C  
ATOM   1696  CD  ARG A 225      28.609  -0.530  22.555  1.00205.83           C  
ATOM   1697  NE  ARG A 225      29.134   0.372  23.569  1.00241.21           N  
ATOM   1698  CZ  ARG A 225      29.350   1.673  23.376  1.00203.52           C  
ATOM   1699  NH1 ARG A 225      29.095   2.268  22.214  1.00246.98           N  
ATOM   1700  NH2 ARG A 225      29.836   2.404  24.380  1.00246.98           N  
ATOM   1701  N   SER A 226      24.988  -2.701  23.785  1.00216.48           N  
ATOM   1702  CA  SER A 226      24.159  -2.184  24.881  1.00216.48           C  
ATOM   1703  C   SER A 226      23.589  -3.347  25.698  1.00216.48           C  
ATOM   1704  O   SER A 226      23.872  -3.470  26.899  1.00216.48           O  
ATOM   1705  CB  SER A 226      23.028  -1.314  24.362  1.00210.76           C  
ATOM   1706  OG  SER A 226      22.225  -0.811  25.413  1.00230.49           O  
ATOM   1707  N   ARG A 227      22.799  -4.158  25.012  1.00328.23           N  
ATOM   1708  CA  ARG A 227      22.156  -5.332  25.620  1.00328.23           C  
ATOM   1709  C   ARG A 227      23.200  -6.357  26.059  1.00328.23           C  
ATOM   1710  O   ARG A 227      23.708  -7.125  25.197  1.00342.24           O  
ATOM   1711  CB  ARG A 227      21.136  -5.976  24.679  1.00322.51           C  
ATOM   1712  CG  ARG A 227      19.758  -5.319  24.715  1.00342.24           C  
ATOM   1713  CD  ARG A 227      18.986  -5.765  25.909  1.00351.96           C  
ATOM   1714  NE  ARG A 227      18.106  -4.731  26.433  1.00387.34           N  
ATOM   1715  CZ  ARG A 227      18.532  -3.691  27.152  1.00349.65           C  
ATOM   1716  NH1 ARG A 227      19.818  -3.518  27.445  1.00393.11           N  
ATOM   1717  NH2 ARG A 227      17.648  -2.800  27.598  1.00393.11           N  
ATOM   1718  N   ALA A 228      23.504  -6.339  27.318  1.00328.23           N  
TER    1719      ALA A 228                                                      
HETATM 1720  C1  DPG A 261       2.744   1.291 -13.544  1.00237.46           C  
HETATM 1721  C2  DPG A 261       4.096   1.770 -13.022  1.00224.93           C  
HETATM 1722  C3  DPG A 261       4.781   2.723 -13.988  1.00248.36           C  
HETATM 1723  C4  DPG A 261       2.674   6.710 -16.636  1.00317.24           C  
HETATM 1724  C5  DPG A 261       3.323   6.458 -18.063  1.00356.30           C  
HETATM 1725  C6  DPG A 261       3.762   7.822 -18.665  1.00373.01           C  
HETATM 1726  C11 DPG A 261       1.435   2.763 -12.120  1.00204.10           C  
HETATM 1727  C12 DPG A 261       1.885   4.217 -11.937  1.00200.01           C  
HETATM 1728  C13 DPG A 261       2.736   4.406 -10.710  1.00173.88           C  
HETATM 1729  C14 DPG A 261       3.973   5.096 -11.192  1.00183.86           C  
HETATM 1730  C15 DPG A 261       2.009   5.227  -9.678  1.00153.83           C  
HETATM 1731  C16 DPG A 261       2.492   5.118  -8.223  1.00128.95           C  
HETATM 1732  C17 DPG A 261       1.637   5.781  -7.114  1.00112.97           C  
HETATM 1733  C18 DPG A 261       1.881   5.396  -5.614  1.00 95.93           C  
HETATM 1734  C19 DPG A 261       1.715   3.900  -5.348  1.00 93.50           C  
HETATM 1735  C20 DPG A 261       1.002   6.157  -4.602  1.00 87.68           C  
HETATM 1736  C21 DPG A 261       1.750   6.339  -3.286  1.00 81.22           C  
HETATM 1737  C22 DPG A 261       1.352   7.635  -2.525  1.00 79.84           C  
HETATM 1738  C23 DPG A 261       1.084   7.785  -0.958  1.00 82.81           C  
HETATM 1739  C24 DPG A 261       1.327   6.459  -0.234  1.00 86.99           C  
HETATM 1740  C25 DPG A 261       1.993   8.849  -0.256  1.00 86.83           C  
HETATM 1741  C26 DPG A 261       1.554   9.440   1.067  1.00 99.22           C  
HETATM 1742  C27 DPG A 261       2.789   9.854   1.784  1.00108.69           C  
HETATM 1743  C28 DPG A 261       2.662   9.788   3.256  1.00134.51           C  
HETATM 1744  C29 DPG A 261       2.669   8.358   3.740  1.00144.95           C  
HETATM 1745  C30 DPG A 261       1.560  10.644   3.878  1.00148.12           C  
HETATM 1746  C41 DPG A 261       4.598  -0.163 -11.629  1.00193.23           C  
HETATM 1747  C42 DPG A 261       5.065   0.575 -10.343  1.00166.53           C  
HETATM 1748  C43 DPG A 261       4.264   0.424  -9.013  1.00141.94           C  
HETATM 1749  C44 DPG A 261       4.391  -1.083  -8.603  1.00135.04           C  
HETATM 1750  C45 DPG A 261       4.718   1.492  -7.924  1.00124.38           C  
HETATM 1751  C46 DPG A 261       4.476   1.231  -6.384  1.00103.99           C  
HETATM 1752  C47 DPG A 261       5.544   1.712  -5.358  1.00 93.58           C  
HETATM 1753  C48 DPG A 261       5.925   0.831  -4.147  1.00 84.88           C  
HETATM 1754  C49 DPG A 261       6.124  -0.642  -4.564  1.00 87.42           C  
HETATM 1755  C50 DPG A 261       4.801   0.942  -3.113  1.00 80.75           C  
HETATM 1756  C51 DPG A 261       5.169   0.429  -1.718  1.00 80.36           C  
HETATM 1757  C52 DPG A 261       3.993  -0.180  -0.951  1.00 82.84           C  
HETATM 1758  C53 DPG A 261       3.977  -0.007   0.627  1.00 94.39           C  
HETATM 1759  C54 DPG A 261       5.244  -0.461   1.454  1.00104.09           C  
HETATM 1760  C55 DPG A 261       3.541   1.462   0.986  1.00 98.28           C  
HETATM 1761  C56 DPG A 261       2.928   1.679   2.385  1.00118.17           C  
HETATM 1762  C57 DPG A 261       1.915   2.819   2.505  1.00120.24           C  
HETATM 1763  C58 DPG A 261       1.447   2.806   3.968  1.00150.22           C  
HETATM 1764  C59 DPG A 261       1.830   4.067   4.761  1.00170.30           C  
HETATM 1765  C60 DPG A 261       0.009   2.335   4.238  1.00156.75           C  
HETATM 1766  O1  DPG A 261       1.756   2.347 -13.479  1.00235.88           O  
HETATM 1767  O2  DPG A 261       4.974   0.698 -12.720  1.00217.84           O  
HETATM 1768  O3  DPG A 261       3.907   3.847 -14.226  1.00254.30           O  
HETATM 1769  O4  DPG A 261       2.356   3.306 -16.056  1.00301.68           O  
HETATM 1770  O5  DPG A 261       4.648   4.075 -16.769  1.00320.84           O  
HETATM 1771  O6  DPG A 261       3.011   5.752 -15.565  1.00288.69           O  
HETATM 1772  O7  DPG A 261       2.468   5.783 -19.035  1.00383.32           O  
HETATM 1773  O8  DPG A 261       4.696   8.492 -17.784  1.00348.59           O  
HETATM 1774  O9  DPG A 261       6.418  10.288 -17.121  1.00330.41           O  
HETATM 1775  O10 DPG A 261       6.278   9.522 -19.522  1.00396.93           O  
HETATM 1776  O11 DPG A 261       4.465  10.881 -18.580  1.00370.64           O  
HETATM 1777  P1  DPG A 261       3.513   4.178 -15.775  1.00294.23           P  
HETATM 1778  P2  DPG A 261       5.503   9.837 -18.257  1.00361.67           P  
HETATM 1779  C1  DPG A 262      30.521  12.854 -11.219  1.00238.93           C  
HETATM 1780  C2  DPG A 262      31.524  12.490 -12.313  1.00253.66           C  
HETATM 1781  C3  DPG A 262      30.944  12.785 -13.693  1.00271.62           C  
HETATM 1782  C4  DPG A 262      29.779  12.214 -16.789  1.00305.61           C  
HETATM 1783  C5  DPG A 262      29.917  10.645 -16.998  1.00307.43           C  
HETATM 1784  C6  DPG A 262      28.558  10.072 -17.494  1.00311.44           C  
HETATM 1785  C11 DPG A 262      31.894  14.026  -9.573  1.00216.87           C  
HETATM 1786  C12 DPG A 262      31.417  13.177  -8.401  1.00201.87           C  
HETATM 1787  C13 DPG A 262      31.678  13.705  -7.034  1.00185.85           C  
HETATM 1788  C14 DPG A 262      33.145  13.967  -6.900  1.00184.39           C  
HETATM 1789  C15 DPG A 262      30.865  14.954  -6.751  1.00182.79           C  
HETATM 1790  C16 DPG A 262      30.844  15.435  -5.297  1.00168.90           C  
HETATM 1791  C17 DPG A 262      29.632  16.200  -4.709  1.00164.28           C  
HETATM 1792  C18 DPG A 262      29.494  16.282  -3.149  1.00155.40           C  
HETATM 1793  C19 DPG A 262      28.995  14.978  -2.530  1.00153.42           C  
HETATM 1794  C20 DPG A 262      28.635  17.445  -2.619  1.00153.65           C  
HETATM 1795  C21 DPG A 262      29.048  17.749  -1.182  1.00152.61           C  
HETATM 1796  C22 DPG A 262      27.940  18.494  -0.383  1.00154.62           C  
HETATM 1797  C23 DPG A 262      27.562  18.197   1.150  1.00164.34           C  
HETATM 1798  C24 DPG A 262      27.569  16.674   1.352  1.00166.24           C  
HETATM 1799  C25 DPG A 262      28.599  18.804   2.155  1.00175.31           C  
HETATM 1800  C26 DPG A 262      28.644  18.359   3.595  1.00198.06           C  
HETATM 1801  C27 DPG A 262      29.070  19.538   4.403  1.00214.75           C  
HETATM 1802  C28 DPG A 262      28.804  19.260   5.843  1.00252.07           C  
HETATM 1803  C29 DPG A 262      30.023  19.644   6.654  1.00277.64           C  
HETATM 1804  C30 DPG A 262      27.524  19.920   6.368  1.00268.24           C  
HETATM 1805  C41 DPG A 262      32.916  10.734 -11.397  1.00241.34           C  
HETATM 1806  C42 DPG A 262      32.523   9.337 -10.836  1.00233.75           C  
HETATM 1807  C43 DPG A 262      32.978   8.878  -9.417  1.00214.82           C  
HETATM 1808  C44 DPG A 262      34.542   8.833  -9.457  1.00215.35           C  
HETATM 1809  C45 DPG A 262      32.309   9.762  -8.283  1.00200.42           C  
HETATM 1810  C46 DPG A 262      32.363   9.323  -6.768  1.00182.97           C  
HETATM 1811  C47 DPG A 262      31.562  10.222  -5.779  1.00173.14           C  
HETATM 1812  C48 DPG A 262      31.240   9.705  -4.358  1.00161.84           C  
HETATM 1813  C49 DPG A 262      30.044  10.480  -3.765  1.00158.28           C  
HETATM 1814  C50 DPG A 262      32.512   9.858  -3.529  1.00157.08           C  
HETATM 1815  C51 DPG A 262      32.361   9.737  -2.014  1.00152.52           C  
HETATM 1816  C52 DPG A 262      33.401  10.537  -1.229  1.00152.55           C  
HETATM 1817  C53 DPG A 262      32.962  11.212   0.137  1.00157.02           C  
HETATM 1818  C54 DPG A 262      31.442  11.598   0.345  1.00158.24           C  
HETATM 1819  C55 DPG A 262      33.508  10.363   1.345  1.00166.17           C  
HETATM 1820  C56 DPG A 262      33.516  11.086   2.710  1.00183.06           C  
HETATM 1821  C57 DPG A 262      34.488  10.529   3.749  1.00201.02           C  
HETATM 1822  C58 DPG A 262      34.472  11.539   4.912  1.00226.80           C  
HETATM 1823  C59 DPG A 262      35.861  12.119   5.241  1.00235.25           C  
HETATM 1824  C60 DPG A 262      33.698  11.100   6.170  1.00261.98           C  
HETATM 1825  O1  DPG A 262      30.859  14.104 -10.580  1.00230.30           O  
HETATM 1826  O2  DPG A 262      31.813  11.093 -12.254  1.00252.87           O  
HETATM 1827  O3  DPG A 262      31.735  13.809 -14.328  1.00279.46           O  
HETATM 1828  O4  DPG A 262      32.351  15.174 -16.273  1.00300.81           O  
HETATM 1829  O5  DPG A 262      29.905  15.202 -15.665  1.00294.65           O  
HETATM 1830  O6  DPG A 262      31.015  12.986 -16.570  1.00303.62           O  
HETATM 1831  O7  DPG A 262      30.321   9.885 -15.818  1.00296.25           O  
HETATM 1832  O8  DPG A 262      28.490   8.645 -17.260  1.00309.60           O  
HETATM 1833  O9  DPG A 262      27.102   6.478 -17.150  1.00308.70           O  
HETATM 1834  O10 DPG A 262      26.154   8.506 -18.318  1.00317.07           O  
HETATM 1835  O11 DPG A 262      28.020   7.285 -19.341  1.00322.04           O  
HETATM 1836  P1  DPG A 262      31.197  14.420 -15.745  1.00295.49           P  
HETATM 1837  P2  DPG A 262      27.400   7.692 -18.027  1.00315.24           P  
HETATM 1838  C1  DPG A 263      33.521   1.934 -12.702  1.00224.36           C  
HETATM 1839  C2  DPG A 263      33.606   3.429 -12.384  1.00215.74           C  
HETATM 1840  C3  DPG A 263      35.015   3.952 -12.650  1.00222.93           C  
HETATM 1841  C4  DPG A 263      36.590   6.606 -15.410  1.00305.45           C  
HETATM 1842  C5  DPG A 263      35.825   6.724 -16.797  1.00350.99           C  
HETATM 1843  C6  DPG A 263      35.252   5.330 -17.180  1.00363.89           C  
HETATM 1844  C11 DPG A 263      33.500   0.540 -10.741  1.00175.00           C  
HETATM 1845  C12 DPG A 263      32.898   0.824  -9.357  1.00146.37           C  
HETATM 1846  C13 DPG A 263      33.974   0.861  -8.306  1.00128.64           C  
HETATM 1847  C14 DPG A 263      33.412   1.719  -7.217  1.00114.37           C  
HETATM 1848  C15 DPG A 263      34.273  -0.542  -7.843  1.00122.04           C  
HETATM 1849  C16 DPG A 263      35.090  -0.757  -6.566  1.00107.99           C  
HETATM 1850  C17 DPG A 263      34.885  -2.021  -5.696  1.00102.17           C  
HETATM 1851  C18 DPG A 263      34.953  -1.960  -4.134  1.00100.07           C  
HETATM 1852  C19 DPG A 263      35.813  -0.819  -3.593  1.00102.02           C  
HETATM 1853  C20 DPG A 263      35.399  -3.269  -3.440  1.00102.83           C  
HETATM 1854  C21 DPG A 263      34.850  -3.284  -2.019  1.00116.18           C  
HETATM 1855  C22 DPG A 263      35.793  -3.959  -0.979  1.00132.92           C  
HETATM 1856  C23 DPG A 263      35.995  -3.411   0.519  1.00168.18           C  
HETATM 1857  C24 DPG A 263      34.627  -3.024   1.099  1.00185.55           C  
HETATM 1858  C25 DPG A 263      36.588  -4.496   1.479  1.00198.11           C  
HETATM 1859  C26 DPG A 263      37.210  -4.069   2.791  1.00248.90           C  
HETATM 1860  C27 DPG A 263      37.478  -5.339   3.524  1.00282.47           C  
HETATM 1861  C28 DPG A 263      38.469  -5.102   4.612  1.00339.50           C  
HETATM 1862  C29 DPG A 263      38.158  -6.035   5.766  1.00409.79           C  
HETATM 1863  C30 DPG A 263      39.922  -5.247   4.138  1.00313.58           C  
HETATM 1864  C41 DPG A 263      34.425   4.139 -10.239  1.00163.96           C  
HETATM 1865  C42 DPG A 263      33.784   4.938  -9.069  1.00141.15           C  
HETATM 1866  C43 DPG A 263      34.478   5.008  -7.674  1.00119.83           C  
HETATM 1867  C44 DPG A 263      35.631   6.057  -7.809  1.00121.59           C  
HETATM 1868  C45 DPG A 263      33.423   5.240  -6.513  1.00107.55           C  
HETATM 1869  C46 DPG A 263      33.839   5.095  -4.997  1.00 99.85           C  
HETATM 1870  C47 DPG A 263      32.671   5.207  -3.972  1.00100.50           C  
HETATM 1871  C48 DPG A 263      32.934   5.002  -2.466  1.00110.83           C  
HETATM 1872  C49 DPG A 263      33.963   6.022  -1.937  1.00117.28           C  
HETATM 1873  C50 DPG A 263      33.416   3.568  -2.237  1.00113.44           C  
HETATM 1874  C51 DPG A 263      33.146   3.023  -0.832  1.00135.79           C  
HETATM 1875  C52 DPG A 263      33.118   1.492  -0.787  1.00136.69           C  
HETATM 1876  C53 DPG A 263      32.365   0.830   0.443  1.00166.06           C  
HETATM 1877  C54 DPG A 263      31.637  -0.560   0.238  1.00160.52           C  
HETATM 1878  C55 DPG A 263      33.323   0.784   1.689  1.00205.46           C  
HETATM 1879  C56 DPG A 263      32.611   0.669   3.059  1.00260.73           C  
HETATM 1880  C57 DPG A 263      33.525   0.355   4.241  1.00319.07           C  
HETATM 1881  C58 DPG A 263      32.728   0.714   5.508  1.00393.18           C  
HETATM 1882  C59 DPG A 263      33.610   1.274   6.641  1.00470.11           C  
HETATM 1883  C60 DPG A 263      31.734  -0.355   6.006  1.00425.72           C  
HETATM 1884  O1  DPG A 263      32.698   1.280 -11.703  1.00198.04           O  
HETATM 1885  O2  DPG A 263      33.299   3.669 -11.012  1.00181.25           O  
HETATM 1886  O3  DPG A 263      35.142   5.239 -12.015  1.00206.02           O  
HETATM 1887  O4  DPG A 263      37.522   5.756 -12.351  1.00214.86           O  
HETATM 1888  O5  DPG A 263      35.991   7.749 -12.161  1.00209.82           O  
HETATM 1889  O6  DPG A 263      35.814   6.145 -14.245  1.00269.06           O  
HETATM 1890  O7  DPG A 263      36.622   7.207 -17.921  1.00389.11           O  
HETATM 1891  O8  DPG A 263      34.278   4.894 -16.201  1.00331.18           O  
HETATM 1892  O9  DPG A 263      34.131   2.341 -16.515  1.00341.57           O  
HETATM 1893  O10 DPG A 263      32.224   3.574 -15.413  1.00305.55           O  
HETATM 1894  O11 DPG A 263      32.625   3.869 -17.816  1.00385.52           O  
HETATM 1895  P1  DPG A 263      36.190   6.326 -12.634  1.00222.50           P  
HETATM 1896  P2  DPG A 263      33.293   3.617 -16.488  1.00340.68           P  
HETATM 1897  C1  DPG A 264      36.765  -8.741 -12.172  1.00249.55           C  
HETATM 1898  C2  DPG A 264      38.073  -9.531 -12.276  1.00249.76           C  
HETATM 1899  C3  DPG A 264      37.811 -10.981 -12.672  1.00249.99           C  
HETATM 1900  C4  DPG A 264      42.445 -12.444 -13.760  1.00245.76           C  
HETATM 1901  C5  DPG A 264      43.633 -11.616 -13.108  1.00249.19           C  
HETATM 1902  C6  DPG A 264      44.764 -11.444 -14.162  1.00242.22           C  
HETATM 1903  C11 DPG A 264      37.048  -6.489 -13.000  1.00249.49           C  
HETATM 1904  C12 DPG A 264      35.800  -5.736 -12.514  1.00250.00           C  
HETATM 1905  C13 DPG A 264      36.176  -4.762 -11.428  1.00246.43           C  
HETATM 1906  C14 DPG A 264      35.762  -3.422 -11.950  1.00248.91           C  
HETATM 1907  C15 DPG A 264      35.473  -5.091 -10.137  1.00234.97           C  
HETATM 1908  C16 DPG A 264      36.173  -4.703  -8.822  1.00217.10           C  
HETATM 1909  C17 DPG A 264      35.714  -5.327  -7.485  1.00194.55           C  
HETATM 1910  C18 DPG A 264      36.728  -5.756  -6.371  1.00173.88           C  
HETATM 1911  C19 DPG A 264      38.042  -6.296  -6.928  1.00184.35           C  
HETATM 1912  C20 DPG A 264      36.161  -6.766  -5.354  1.00154.62           C  
HETATM 1913  C21 DPG A 264      37.038  -6.784  -4.109  1.00131.91           C  
HETATM 1914  C22 DPG A 264      36.828  -8.079  -3.282  1.00118.12           C  
HETATM 1915  C23 DPG A 264      37.919  -8.835  -2.385  1.00105.00           C  
HETATM 1916  C24 DPG A 264      39.307  -8.657  -3.019  1.00114.05           C  
HETATM 1917  C25 DPG A 264      38.021  -8.256  -0.933  1.00 89.40           C  
HETATM 1918  C26 DPG A 264      38.481  -9.126   0.216  1.00 83.52           C  
HETATM 1919  C27 DPG A 264      37.958  -8.457   1.444  1.00 85.16           C  
HETATM 1920  C28 DPG A 264      38.048  -9.379   2.610  1.00 95.75           C  
HETATM 1921  C29 DPG A 264      36.659  -9.574   3.186  1.00104.65           C  
HETATM 1922  C30 DPG A 264      39.038  -8.897   3.680  1.00114.40           C  
HETATM 1923  C41 DPG A 264      38.339 -10.531 -10.079  1.00234.30           C  
HETATM 1924  C42 DPG A 264      39.315 -10.368  -8.886  1.00218.09           C  
HETATM 1925  C43 DPG A 264      38.916 -10.421  -7.385  1.00192.74           C  
HETATM 1926  C44 DPG A 264      37.535  -9.700  -7.243  1.00190.16           C  
HETATM 1927  C45 DPG A 264      39.012 -11.899  -6.801  1.00181.98           C  
HETATM 1928  C46 DPG A 264      38.470 -12.196  -5.348  1.00154.51           C  
HETATM 1929  C47 DPG A 264      38.982 -13.484  -4.639  1.00141.36           C  
HETATM 1930  C48 DPG A 264      38.127 -14.135  -3.528  1.00122.07           C  
HETATM 1931  C49 DPG A 264      36.723 -14.503  -4.053  1.00130.93           C  
HETATM 1932  C50 DPG A 264      38.059 -13.155  -2.354  1.00104.59           C  
HETATM 1933  C51 DPG A 264      37.351 -13.701  -1.118  1.00 90.93           C  
HETATM 1934  C52 DPG A 264      37.764 -13.024   0.188  1.00 83.58           C  
HETATM 1935  C53 DPG A 264      36.747 -13.117   1.402  1.00 84.95           C  
HETATM 1936  C54 DPG A 264      35.440 -12.227   1.363  1.00 84.77           C  
HETATM 1937  C55 DPG A 264      36.414 -14.626   1.687  1.00 86.59           C  
HETATM 1938  C56 DPG A 264      35.462 -14.900   2.872  1.00 99.48           C  
HETATM 1939  C57 DPG A 264      34.723 -16.237   2.835  1.00 98.92           C  
HETATM 1940  C58 DPG A 264      33.444 -16.055   3.674  1.00114.27           C  
HETATM 1941  C59 DPG A 264      33.372 -16.985   4.899  1.00147.49           C  
HETATM 1942  C60 DPG A 264      32.124 -15.991   2.884  1.00 99.66           C  
HETATM 1943  O1  DPG A 264      36.647  -7.851 -13.312  1.00248.41           O  
HETATM 1944  O2  DPG A 264      38.754  -9.521 -11.026  1.00243.62           O  
HETATM 1945  O3  DPG A 264      38.667 -11.304 -13.787  1.00245.56           O  
HETATM 1946  O4  DPG A 264      39.379 -13.368 -14.907  1.00232.58           O  
HETATM 1947  O5  DPG A 264      39.497 -13.409 -12.388  1.00249.91           O  
HETATM 1948  O6  DPG A 264      41.104 -11.831 -13.759  1.00245.77           O  
HETATM 1949  O7  DPG A 264      44.224 -12.195 -11.905  1.00248.75           O  
HETATM 1950  O8  DPG A 264      44.378 -10.469 -15.161  1.00228.32           O  
HETATM 1951  O9  DPG A 264      44.690  -8.374 -16.625  1.00193.25           O  
HETATM 1952  O10 DPG A 264      45.559  -8.379 -14.255  1.00241.24           O  
HETATM 1953  O11 DPG A 264      46.671  -9.760 -15.952  1.00211.68           O  
HETATM 1954  P1  DPG A 264      39.637 -12.612 -13.665  1.00246.43           P  
HETATM 1955  P2  DPG A 264      45.343  -9.193 -15.516  1.00221.49           P  
HETATM 1956  C1  DPG A 265      31.307 -11.964 -11.106  1.00210.37           C  
HETATM 1957  C2  DPG A 265      32.491 -11.058 -11.465  1.00212.57           C  
HETATM 1958  C3  DPG A 265      32.911 -11.263 -12.914  1.00219.54           C  
HETATM 1959  C4  DPG A 265      31.652 -11.578 -15.000  1.00223.17           C  
HETATM 1960  C5  DPG A 265      30.268 -12.351 -14.914  1.00223.19           C  
HETATM 1961  C6  DPG A 265      30.537 -13.826 -14.504  1.00223.08           C  
HETATM 1962  C11 DPG A 265      30.209 -12.611  -9.056  1.00194.87           C  
HETATM 1963  C12 DPG A 265      29.977 -12.043  -7.646  1.00182.00           C  
HETATM 1964  C13 DPG A 265      30.065 -13.134  -6.617  1.00171.86           C  
HETATM 1965  C14 DPG A 265      31.489 -13.139  -6.161  1.00167.24           C  
HETATM 1966  C15 DPG A 265      29.104 -12.825  -5.498  1.00160.44           C  
HETATM 1967  C16 DPG A 265      29.147 -13.661  -4.215  1.00147.21           C  
HETATM 1968  C17 DPG A 265      28.646 -13.031  -2.888  1.00133.84           C  
HETATM 1969  C18 DPG A 265      29.208 -13.566  -1.525  1.00120.95           C  
HETATM 1970  C19 DPG A 265      28.775 -14.999  -1.224  1.00118.28           C  
HETATM 1971  C20 DPG A 265      28.907 -12.689  -0.293  1.00110.50           C  
HETATM 1972  C21 DPG A 265      30.027 -12.899   0.721  1.00103.04           C  
HETATM 1973  C22 DPG A 265      29.746 -12.115   2.037  1.00 95.28           C  
HETATM 1974  C23 DPG A 265      30.605 -12.345   3.372  1.00 90.10           C  
HETATM 1975  C24 DPG A 265      32.094 -12.421   3.000  1.00 91.24           C  
HETATM 1976  C25 DPG A 265      30.472 -11.146   4.372  1.00 88.31           C  
HETATM 1977  C26 DPG A 265      31.064 -11.240   5.758  1.00 89.21           C  
HETATM 1978  C27 DPG A 265      31.367  -9.835   6.164  1.00 90.29           C  
HETATM 1979  C28 DPG A 265      32.375  -9.820   7.262  1.00 95.24           C  
HETATM 1980  C29 DPG A 265      32.146  -8.583   8.110  1.00101.23           C  
HETATM 1981  C30 DPG A 265      33.821  -9.899   6.752  1.00 92.56           C  
HETATM 1982  C41 DPG A 265      34.100 -10.238  -9.868  1.00201.55           C  
HETATM 1983  C42 DPG A 265      33.510 -10.472  -8.445  1.00189.47           C  
HETATM 1984  C43 DPG A 265      34.045  -9.670  -7.225  1.00177.91           C  
HETATM 1985  C44 DPG A 265      33.721  -8.165  -7.510  1.00180.69           C  
HETATM 1986  C45 DPG A 265      33.511 -10.261  -5.848  1.00164.04           C  
HETATM 1987  C46 DPG A 265      34.155  -9.845  -4.472  1.00149.85           C  
HETATM 1988  C47 DPG A 265      33.222  -9.795  -3.225  1.00137.18           C  
HETATM 1989  C48 DPG A 265      33.843  -9.698  -1.810  1.00123.55           C  
HETATM 1990  C49 DPG A 265      33.216 -10.773  -0.894  1.00115.43           C  
HETATM 1991  C50 DPG A 265      33.625  -8.276  -1.310  1.00119.04           C  
HETATM 1992  C51 DPG A 265      33.705  -8.045   0.197  1.00106.75           C  
HETATM 1993  C52 DPG A 265      33.853  -6.578   0.584  1.00103.97           C  
HETATM 1994  C53 DPG A 265      33.136  -6.044   1.893  1.00 96.01           C  
HETATM 1995  C54 DPG A 265      31.572  -6.240   2.044  1.00 95.24           C  
HETATM 1996  C55 DPG A 265      33.882  -6.554   3.183  1.00 90.65           C  
HETATM 1997  C56 DPG A 265      33.651  -5.706   4.456  1.00 88.25           C  
HETATM 1998  C57 DPG A 265      33.783  -6.443   5.786  1.00 89.27           C  
HETATM 1999  C58 DPG A 265      33.878  -5.389   6.889  1.00 93.22           C  
HETATM 2000  C59 DPG A 265      32.642  -4.498   7.072  1.00 94.17           C  
HETATM 2001  C60 DPG A 265      35.214  -4.659   7.079  1.00 94.20           C  
HETATM 2002  O1  DPG A 265      30.754 -11.516  -9.841  1.00201.34           O  
HETATM 2003  O2  DPG A 265      33.599 -11.363 -10.619  1.00207.11           O  
HETATM 2004  O3  DPG A 265      33.473 -10.036 -13.416  1.00221.16           O  
HETATM 2005  O4  DPG A 265      33.464  -8.311 -15.161  1.00223.09           O  
HETATM 2006  O5  DPG A 265      31.673  -8.079 -13.407  1.00221.13           O  
HETATM 2007  O6  DPG A 265      31.614 -10.108 -15.091  1.00223.13           O  
HETATM 2008  O7  DPG A 265      29.473 -12.362 -16.140  1.00221.34           O  
HETATM 2009  O8  DPG A 265      29.335 -14.445 -13.988  1.00222.45           O  
HETATM 2010  O9  DPG A 265      29.673 -16.068 -12.018  1.00215.61           O  
HETATM 2011  O10 DPG A 265      27.944 -16.591 -13.781  1.00222.05           O  
HETATM 2012  O11 DPG A 265      30.327 -16.745 -14.344  1.00222.94           O  
HETATM 2013  P1  DPG A 265      32.527  -9.001 -14.249  1.00222.83           P  
HETATM 2014  P2  DPG A 265      29.316 -16.009 -13.501  1.00221.39           P  
HETATM 2015  C1  DPG A 266       1.914   1.771  26.124  1.00290.45           C  
HETATM 2016  C2  DPG A 266       2.426   3.188  25.864  1.00293.21           C  
HETATM 2017  C3  DPG A 266       1.276   4.189  25.798  1.00293.80           C  
HETATM 2018  C4  DPG A 266      -1.289   5.226  25.982  1.00292.04           C  
HETATM 2019  C5  DPG A 266      -2.802   5.460  25.566  1.00295.54           C  
HETATM 2020  C6  DPG A 266      -3.683   4.352  26.212  1.00289.36           C  
HETATM 2021  C11 DPG A 266       2.550   0.215  24.397  1.00296.88           C  
HETATM 2022  C12 DPG A 266       2.259  -0.078  22.919  1.00283.44           C  
HETATM 2023  C13 DPG A 266       3.532  -0.112  22.120  1.00270.62           C  
HETATM 2024  C14 DPG A 266       4.078  -1.495  22.281  1.00273.46           C  
HETATM 2025  C15 DPG A 266       3.238   0.203  20.674  1.00240.32           C  
HETATM 2026  C16 DPG A 266       4.406   0.101  19.682  1.00216.09           C  
HETATM 2027  C17 DPG A 266       4.309   0.748  18.284  1.00180.20           C  
HETATM 2028  C18 DPG A 266       4.879   0.074  16.994  1.00148.26           C  
HETATM 2029  C19 DPG A 266       5.835  -1.085  17.257  1.00154.53           C  
HETATM 2030  C20 DPG A 266       5.530   1.046  15.982  1.00126.03           C  
HETATM 2031  C21 DPG A 266       5.513   0.418  14.599  1.00102.51           C  
HETATM 2032  C22 DPG A 266       5.134   1.376  13.425  1.00 91.30           C  
HETATM 2033  C23 DPG A 266       4.189   0.861  12.227  1.00 90.63           C  
HETATM 2034  C24 DPG A 266       2.742   1.269  12.548  1.00 89.61           C  
HETATM 2035  C25 DPG A 266       4.520   1.505  10.837  1.00106.69           C  
HETATM 2036  C26 DPG A 266       4.189   0.749   9.568  1.00140.18           C  
HETATM 2037  C27 DPG A 266       3.716   1.756   8.573  1.00180.95           C  
HETATM 2038  C28 DPG A 266       2.895   1.075   7.529  1.00239.10           C  
HETATM 2039  C29 DPG A 266       3.558   1.318   6.187  1.00339.49           C  
HETATM 2040  C30 DPG A 266       1.427   1.520   7.535  1.00238.72           C  
HETATM 2041  C41 DPG A 266       2.406   3.636  23.479  1.00290.27           C  
HETATM 2042  C42 DPG A 266       3.351   4.510  22.620  1.00279.04           C  
HETATM 2043  C43 DPG A 266       3.542   4.348  21.084  1.00249.65           C  
HETATM 2044  C44 DPG A 266       4.766   3.386  20.906  1.00245.66           C  
HETATM 2045  C45 DPG A 266       2.197   3.939  20.345  1.00232.50           C  
HETATM 2046  C46 DPG A 266       2.218   3.616  18.800  1.00193.48           C  
HETATM 2047  C47 DPG A 266       0.836   3.525  18.090  1.00175.25           C  
HETATM 2048  C48 DPG A 266       0.735   2.939  16.667  1.00140.72           C  
HETATM 2049  C49 DPG A 266       1.371   1.535  16.581  1.00138.79           C  
HETATM 2050  C50 DPG A 266       1.407   3.905  15.688  1.00120.27           C  
HETATM 2051  C51 DPG A 266       0.904   3.759  14.247  1.00 98.19           C  
HETATM 2052  C52 DPG A 266       1.486   4.811  13.305  1.00 90.70           C  
HETATM 2053  C53 DPG A 266       0.601   5.209  12.039  1.00 91.67           C  
HETATM 2054  C54 DPG A 266      -0.687   6.090  12.302  1.00 90.31           C  
HETATM 2055  C55 DPG A 266       1.528   5.779  10.916  1.00105.23           C  
HETATM 2056  C56 DPG A 266       0.945   6.823   9.940  1.00128.32           C  
HETATM 2057  C57 DPG A 266       1.737   7.096   8.671  1.00176.33           C  
HETATM 2058  C58 DPG A 266       1.543   8.574   8.286  1.00195.30           C  
HETATM 2059  C59 DPG A 266       0.094   8.961   7.937  1.00214.40           C  
HETATM 2060  C60 DPG A 266       2.543   9.137   7.255  1.00257.16           C  
HETATM 2061  O1  DPG A 266       1.525   1.120  24.890  1.00297.76           O  
HETATM 2062  O2  DPG A 266       3.161   3.257  24.647  1.00297.57           O  
HETATM 2063  O3  DPG A 266       1.767   5.465  26.257  1.00288.77           O  
HETATM 2064  O4  DPG A 266       1.541   7.625  27.407  1.00266.17           O  
HETATM 2065  O5  DPG A 266       0.766   5.620  28.718  1.00220.73           O  
HETATM 2066  O6  DPG A 266      -0.541   6.361  26.551  1.00284.40           O  
HETATM 2067  O7  DPG A 266      -3.074   5.463  24.131  1.00295.60           O  
HETATM 2068  O8  DPG A 266      -5.055   4.801  26.331  1.00287.76           O  
HETATM 2069  O9  DPG A 266      -4.280   6.958  27.505  1.00263.53           O  
HETATM 2070  O10 DPG A 266      -6.700   6.707  26.831  1.00279.36           O  
HETATM 2071  O11 DPG A 266      -5.813   5.356  28.679  1.00222.41           O  
HETATM 2072  P1  DPG A 266       0.908   6.292  27.371  1.00267.11           P  
HETATM 2073  P2  DPG A 266      -5.465   6.006  27.363  1.00267.32           P  
HETATM 2074  C1  DPG A 267      30.225  15.323  20.613  1.00185.15           C  
HETATM 2075  C2  DPG A 267      30.803  13.960  21.006  1.00188.35           C  
HETATM 2076  C3  DPG A 267      32.216  14.103  21.561  1.00193.09           C  
HETATM 2077  C4  DPG A 267      30.138  13.488  25.424  1.00233.72           C  
HETATM 2078  C5  DPG A 267      29.043  14.290  26.248  1.00244.38           C  
HETATM 2079  C6  DPG A 267      29.025  13.766  27.712  1.00265.30           C  
HETATM 2080  C11 DPG A 267      28.177  16.207  19.722  1.00178.29           C  
HETATM 2081  C12 DPG A 267      28.036  15.525  18.355  1.00168.80           C  
HETATM 2082  C13 DPG A 267      28.513  16.408  17.235  1.00161.83           C  
HETATM 2083  C14 DPG A 267      29.985  16.162  17.138  1.00161.25           C  
HETATM 2084  C15 DPG A 267      27.799  16.038  15.959  1.00154.63           C  
HETATM 2085  C16 DPG A 267      28.202  16.787  14.683  1.00148.06           C  
HETATM 2086  C17 DPG A 267      27.562  16.381  13.336  1.00141.66           C  
HETATM 2087  C18 DPG A 267      28.292  16.660  11.979  1.00135.56           C  
HETATM 2088  C19 DPG A 267      29.133  17.935  11.974  1.00135.54           C  
HETATM 2089  C20 DPG A 267      27.380  16.694  10.734  1.00130.12           C  
HETATM 2090  C21 DPG A 267      28.180  16.196   9.531  1.00124.87           C  
HETATM 2091  C22 DPG A 267      27.262  15.695   8.376  1.00119.70           C  
HETATM 2092  C23 DPG A 267      27.624  14.430   7.454  1.00115.40           C  
HETATM 2093  C24 DPG A 267      26.746  13.255   7.897  1.00117.49           C  
HETATM 2094  C25 DPG A 267      27.307  14.652   5.935  1.00107.84           C  
HETATM 2095  C26 DPG A 267      27.977  13.736   4.935  1.00102.42           C  
HETATM 2096  C27 DPG A 267      27.237  13.915   3.652  1.00 94.81           C  
HETATM 2097  C28 DPG A 267      27.769  12.927   2.669  1.00 88.39           C  
HETATM 2098  C29 DPG A 267      26.619  12.333   1.886  1.00 82.86           C  
HETATM 2099  C30 DPG A 267      28.867  13.490   1.762  1.00 81.95           C  
HETATM 2100  C41 DPG A 267      31.910  13.234  18.944  1.00172.74           C  
HETATM 2101  C42 DPG A 267      31.272  12.960  17.555  1.00163.75           C  
HETATM 2102  C43 DPG A 267      31.925  12.071  16.450  1.00157.31           C  
HETATM 2103  C44 DPG A 267      31.288  10.648  16.612  1.00158.22           C  
HETATM 2104  C45 DPG A 267      31.846  12.738  15.011  1.00149.70           C  
HETATM 2105  C46 DPG A 267      31.659  11.926  13.670  1.00143.21           C  
HETATM 2106  C47 DPG A 267      32.444  12.362  12.403  1.00137.44           C  
HETATM 2107  C48 DPG A 267      31.821  12.429  10.994  1.00131.25           C  
HETATM 2108  C49 DPG A 267      30.440  13.121  11.018  1.00131.36           C  
HETATM 2109  C50 DPG A 267      31.726  11.013  10.418  1.00128.75           C  
HETATM 2110  C51 DPG A 267      31.513  10.999   8.901  1.00122.07           C  
HETATM 2111  C52 DPG A 267      31.042   9.663   8.334  1.00119.50           C  
HETATM 2112  C53 DPG A 267      30.029   9.673   7.110  1.00113.75           C  
HETATM 2113  C54 DPG A 267      29.307  11.033   6.746  1.00111.96           C  
HETATM 2114  C55 DPG A 267      30.693   8.990   5.861  1.00107.45           C  
HETATM 2115  C56 DPG A 267      30.114   9.313   4.470  1.00 99.75           C  
HETATM 2116  C57 DPG A 267      30.121   8.205   3.423  1.00 93.36           C  
HETATM 2117  C58 DPG A 267      30.100   8.888   2.045  1.00 84.01           C  
HETATM 2118  C59 DPG A 267      28.720   9.428   1.626  1.00 80.93           C  
HETATM 2119  C60 DPG A 267      30.805   8.124   0.904  1.00 75.34           C  
HETATM 2120  O1  DPG A 267      28.774  15.254  20.648  1.00185.43           O  
HETATM 2121  O2  DPG A 267      30.825  13.090  19.883  1.00179.49           O  
HETATM 2122  O3  DPG A 267      32.225  15.172  22.528  1.00201.95           O  
HETATM 2123  O4  DPG A 267      32.291  16.126  24.788  1.00226.01           O  
HETATM 2124  O5  DPG A 267      33.317  13.836  24.555  1.00223.30           O  
HETATM 2125  O6  DPG A 267      30.720  14.155  24.243  1.00219.75           O  
HETATM 2126  O7  DPG A 267      27.682  14.216  25.724  1.00237.51           O  
HETATM 2127  O8  DPG A 267      28.404  12.460  27.781  1.00266.35           O  
HETATM 2128  O9  DPG A 267      27.481  12.048  30.151  1.00306.35           O  
HETATM 2129  O10 DPG A 267      26.103  13.349  28.484  1.00277.42           O  
HETATM 2130  O11 DPG A 267      26.424  10.936  28.165  1.00272.31           O  
HETATM 2131  P1  DPG A 267      32.246  14.810  24.118  1.00218.35           P  
HETATM 2132  P2  DPG A 267      27.067  12.196  28.690  1.00280.78           P  
HETATM 2133  C1  DPG A 268      34.248   8.633  22.157  1.00216.74           C  
HETATM 2134  C2  DPG A 268      33.316   7.475  22.525  1.00219.83           C  
HETATM 2135  C3  DPG A 268      34.076   6.370  23.252  1.00226.06           C  
HETATM 2136  C4  DPG A 268      31.934   4.236  27.330  1.00263.16           C  
HETATM 2137  C5  DPG A 268      32.538   5.297  28.346  1.00272.74           C  
HETATM 2138  C6  DPG A 268      32.321   6.726  27.773  1.00267.33           C  
HETATM 2139  C11 DPG A 268      34.486  10.428  20.567  1.00203.93           C  
HETATM 2140  C12 DPG A 268      35.847  10.200  19.895  1.00198.81           C  
HETATM 2141  C13 DPG A 268      36.131  11.275  18.875  1.00191.42           C  
HETATM 2142  C14 DPG A 268      37.625  11.297  18.775  1.00190.72           C  
HETATM 2143  C15 DPG A 268      35.439  10.969  17.582  1.00182.77           C  
HETATM 2144  C16 DPG A 268      36.062  11.355  16.231  1.00174.71           C  
HETATM 2145  C17 DPG A 268      35.331  11.031  14.914  1.00167.91           C  
HETATM 2146  C18 DPG A 268      35.979  10.264  13.711  1.00162.72           C  
HETATM 2147  C19 DPG A 268      37.502  10.354  13.672  1.00162.57           C  
HETATM 2148  C20 DPG A 268      35.443  10.611  12.306  1.00157.99           C  
HETATM 2149  C21 DPG A 268      35.501   9.356  11.441  1.00155.84           C  
HETATM 2150  C22 DPG A 268      35.550   9.717   9.923  1.00153.61           C  
HETATM 2151  C23 DPG A 268      35.643   8.572   8.803  1.00153.28           C  
HETATM 2152  C24 DPG A 268      34.217   8.167   8.400  1.00153.46           C  
HETATM 2153  C25 DPG A 268      36.347   9.070   7.496  1.00154.43           C  
HETATM 2154  C26 DPG A 268      36.753   8.054   6.452  1.00156.59           C  
HETATM 2155  C27 DPG A 268      37.382   8.850   5.360  1.00160.10           C  
HETATM 2156  C28 DPG A 268      37.551   7.998   4.149  1.00165.55           C  
HETATM 2157  C29 DPG A 268      38.860   7.242   4.259  1.00164.99           C  
HETATM 2158  C30 DPG A 268      37.446   8.788   2.839  1.00173.40           C  
HETATM 2159  C41 DPG A 268      33.531   5.924  20.679  1.00204.80           C  
HETATM 2160  C42 DPG A 268      32.570   4.742  20.378  1.00202.47           C  
HETATM 2161  C43 DPG A 268      32.509   4.059  18.971  1.00192.09           C  
HETATM 2162  C44 DPG A 268      31.533   2.849  19.125  1.00193.18           C  
HETATM 2163  C45 DPG A 268      32.188   5.144  17.862  1.00184.57           C  
HETATM 2164  C46 DPG A 268      32.119   4.799  16.327  1.00175.25           C  
HETATM 2165  C47 DPG A 268      31.253   5.743  15.437  1.00170.48           C  
HETATM 2166  C48 DPG A 268      31.593   5.914  13.939  1.00163.63           C  
HETATM 2167  C49 DPG A 268      31.074   7.266  13.406  1.00161.57           C  
HETATM 2168  C50 DPG A 268      30.975   4.743  13.171  1.00160.72           C  
HETATM 2169  C51 DPG A 268      31.611   4.480  11.806  1.00156.68           C  
HETATM 2170  C52 DPG A 268      30.678   3.708  10.866  1.00154.76           C  
HETATM 2171  C53 DPG A 268      31.283   3.331   9.450  1.00153.33           C  
HETATM 2172  C54 DPG A 268      30.849   1.966   8.778  1.00153.29           C  
HETATM 2173  C55 DPG A 268      31.099   4.536   8.454  1.00153.43           C  
HETATM 2174  C56 DPG A 268      32.039   4.513   7.226  1.00154.88           C  
HETATM 2175  C57 DPG A 268      31.671   5.475   6.098  1.00157.59           C  
HETATM 2176  C58 DPG A 268      32.522   5.045   4.889  1.00162.02           C  
HETATM 2177  C59 DPG A 268      31.746   5.046   3.559  1.00168.83           C  
HETATM 2178  C60 DPG A 268      33.911   5.701   4.769  1.00162.55           C  
HETATM 2179  O1  DPG A 268      33.914   9.116  20.829  1.00205.98           O  
HETATM 2180  O2  DPG A 268      32.727   6.916  21.355  1.00210.16           O  
HETATM 2181  O3  DPG A 268      33.121   5.444  23.810  1.00230.94           O  
HETATM 2182  O4  DPG A 268      30.928   6.281  24.517  1.00237.23           O  
HETATM 2183  O5  DPG A 268      32.869   6.998  25.954  1.00250.33           O  
HETATM 2184  O6  DPG A 268      32.148   4.464  25.890  1.00249.74           O  
HETATM 2185  O7  DPG A 268      33.958   5.142  28.651  1.00275.63           O  
HETATM 2186  O8  DPG A 268      32.953   7.720  28.614  1.00275.28           O  
HETATM 2187  O9  DPG A 268      30.995   9.394  28.607  1.00275.21           O  
HETATM 2188  O10 DPG A 268      33.182  10.038  29.692  1.00285.49           O  
HETATM 2189  O11 DPG A 268      33.057   9.849  27.249  1.00262.40           O  
HETATM 2190  P1  DPG A 268      32.237   5.924  25.097  1.00242.47           P  
HETATM 2191  P2  DPG A 268      32.517   9.299  28.546  1.00274.64           P  
HETATM 2192  C1  DPG A 269      12.322 -21.195  23.900  1.00263.28           C  
HETATM 2193  C2  DPG A 269      11.529 -21.004  25.197  1.00286.81           C  
HETATM 2194  C3  DPG A 269      12.354 -20.258  26.241  1.00301.69           C  
HETATM 2195  C4  DPG A 269      12.212 -21.833  30.345  1.00306.11           C  
HETATM 2196  C5  DPG A 269      13.466 -22.755  30.654  1.00301.92           C  
HETATM 2197  C6  DPG A 269      14.718 -22.175  29.936  1.00310.54           C  
HETATM 2198  C11 DPG A 269      13.213 -19.241  22.793  1.00240.05           C  
HETATM 2199  C12 DPG A 269      12.225 -18.172  23.254  1.00250.00           C  
HETATM 2200  C13 DPG A 269      12.667 -16.752  23.107  1.00246.86           C  
HETATM 2201  C14 DPG A 269      13.792 -16.551  24.076  1.00266.74           C  
HETATM 2202  C15 DPG A 269      13.094 -16.436  21.693  1.00215.29           C  
HETATM 2203  C16 DPG A 269      13.145 -14.957  21.287  1.00205.96           C  
HETATM 2204  C17 DPG A 269      14.003 -14.534  20.070  1.00178.07           C  
HETATM 2205  C18 DPG A 269      13.743 -13.167  19.354  1.00162.19           C  
HETATM 2206  C19 DPG A 269      13.710 -11.977  20.310  1.00183.51           C  
HETATM 2207  C20 DPG A 269      12.486 -13.105  18.458  1.00143.44           C  
HETATM 2208  C21 DPG A 269      12.761 -12.177  17.278  1.00121.59           C  
HETATM 2209  C22 DPG A 269      12.030 -12.584  15.963  1.00102.61           C  
HETATM 2210  C23 DPG A 269      12.738 -12.496  14.524  1.00 90.50           C  
HETATM 2211  C24 DPG A 269      13.806 -13.600  14.459  1.00 90.20           C  
HETATM 2212  C25 DPG A 269      11.760 -12.790  13.334  1.00 89.04           C  
HETATM 2213  C26 DPG A 269      12.237 -12.564  11.919  1.00 99.47           C  
HETATM 2214  C27 DPG A 269      11.699 -13.659  11.061  1.00113.17           C  
HETATM 2215  C28 DPG A 269      12.662 -13.969   9.963  1.00139.83           C  
HETATM 2216  C29 DPG A 269      12.645 -15.461   9.699  1.00147.88           C  
HETATM 2217  C30 DPG A 269      12.409 -13.156   8.688  1.00185.02           C  
HETATM 2218  C41 DPG A 269      12.192 -22.910  26.521  1.00304.93           C  
HETATM 2219  C42 DPG A 269      12.549 -24.204  25.741  1.00295.09           C  
HETATM 2220  C43 DPG A 269      14.030 -24.656  25.516  1.00291.80           C  
HETATM 2221  C44 DPG A 269      14.436 -25.463  26.794  1.00307.75           C  
HETATM 2222  C45 DPG A 269      14.213 -25.376  24.113  1.00267.46           C  
HETATM 2223  C46 DPG A 269      15.604 -25.361  23.361  1.00252.25           C  
HETATM 2224  C47 DPG A 269      15.574 -25.585  21.818  1.00218.16           C  
HETATM 2225  C48 DPG A 269      16.696 -24.976  20.946  1.00198.10           C  
HETATM 2226  C49 DPG A 269      16.680 -23.435  21.017  1.00199.73           C  
HETATM 2227  C50 DPG A 269      16.482 -25.480  19.516  1.00165.73           C  
HETATM 2228  C51 DPG A 269      17.585 -25.072  18.538  1.00145.05           C  
HETATM 2229  C52 DPG A 269      17.119 -24.884  17.092  1.00118.52           C  
HETATM 2230  C53 DPG A 269      17.818 -23.715  16.272  1.00106.46           C  
HETATM 2231  C54 DPG A 269      19.351 -23.856  15.906  1.00101.94           C  
HETATM 2232  C55 DPG A 269      16.963 -23.355  14.999  1.00 93.35           C  
HETATM 2233  C56 DPG A 269      17.053 -21.888  14.519  1.00 90.47           C  
HETATM 2234  C57 DPG A 269      16.965 -21.654  13.011  1.00 90.18           C  
HETATM 2235  C58 DPG A 269      17.464 -20.214  12.784  1.00 91.41           C  
HETATM 2236  C59 DPG A 269      18.990 -20.109  12.600  1.00 92.66           C  
HETATM 2237  C60 DPG A 269      16.683 -19.405  11.727  1.00102.02           C  
HETATM 2238  O1  DPG A 269      13.390 -20.214  23.858  1.00262.44           O  
HETATM 2239  O2  DPG A 269      11.159 -22.270  25.738  1.00295.05           O  
HETATM 2240  O3  DPG A 269      11.444 -19.649  27.180  1.00311.14           O  
HETATM 2241  O4  DPG A 269      10.668 -19.086  29.440  1.00314.26           O  
HETATM 2242  O5  DPG A 269      13.121 -18.698  29.012  1.00316.10           O  
HETATM 2243  O6  DPG A 269      12.158 -21.153  29.039  1.00316.02           O  
HETATM 2244  O7  DPG A 269      13.329 -24.157  30.264  1.00307.09           O  
HETATM 2245  O8  DPG A 269      15.799 -21.969  30.877  1.00298.42           O  
HETATM 2246  O9  DPG A 269      18.153 -22.701  30.127  1.00308.63           O  
HETATM 2247  O10 DPG A 269      17.125 -20.616  29.145  1.00315.66           O  
HETATM 2248  O11 DPG A 269      17.847 -20.617  31.490  1.00286.68           O  
HETATM 2249  P1  DPG A 269      11.891 -19.536  28.746  1.00316.63           P  
HETATM 2250  P2  DPG A 269      17.282 -21.475  30.385  1.00305.61           P  
HETATM 2251  C1  DPG A 270      31.142 -26.374  24.654  1.00207.46           C  
HETATM 2252  C2  DPG A 270      31.778 -25.075  24.139  1.00193.51           C  
HETATM 2253  C3  DPG A 270      33.159 -24.871  24.752  1.00210.28           C  
HETATM 2254  C4  DPG A 270      37.741 -25.882  22.431  1.00156.74           C  
HETATM 2255  C5  DPG A 270      38.875 -26.383  23.424  1.00176.41           C  
HETATM 2256  C6  DPG A 270      40.250 -26.330  22.698  1.00161.59           C  
HETATM 2257  C11 DPG A 270      28.908 -27.241  24.272  1.00196.98           C  
HETATM 2258  C12 DPG A 270      28.045 -26.007  24.548  1.00204.48           C  
HETATM 2259  C13 DPG A 270      26.656 -26.138  23.969  1.00189.21           C  
HETATM 2260  C14 DPG A 270      25.842 -26.760  25.061  1.00219.51           C  
HETATM 2261  C15 DPG A 270      26.100 -24.800  23.568  1.00179.65           C  
HETATM 2262  C16 DPG A 270      25.296 -24.686  22.256  1.00153.73           C  
HETATM 2263  C17 DPG A 270      24.723 -23.317  21.832  1.00146.99           C  
HETATM 2264  C18 DPG A 270      24.838 -22.750  20.376  1.00129.16           C  
HETATM 2265  C19 DPG A 270      24.733 -21.225  20.333  1.00128.75           C  
HETATM 2266  C20 DPG A 270      23.861 -23.348  19.345  1.00120.93           C  
HETATM 2267  C21 DPG A 270      24.434 -23.137  17.947  1.00114.54           C  
HETATM 2268  C22 DPG A 270      23.343 -23.136  16.839  1.00112.57           C  
HETATM 2269  C23 DPG A 270      23.349 -22.203  15.537  1.00112.79           C  
HETATM 2270  C24 DPG A 270      23.944 -20.833  15.902  1.00112.51           C  
HETATM 2271  C25 DPG A 270      24.259 -22.747  14.379  1.00114.45           C  
HETATM 2272  C26 DPG A 270      23.972 -22.361  12.946  1.00117.25           C  
HETATM 2273  C27 DPG A 270      25.289 -22.216  12.260  1.00118.50           C  
HETATM 2274  C28 DPG A 270      25.154 -21.337  11.065  1.00119.92           C  
HETATM 2275  C29 DPG A 270      26.345 -21.568  10.156  1.00119.93           C  
HETATM 2276  C30 DPG A 270      24.981 -19.852  11.409  1.00119.64           C  
HETATM 2277  C41 DPG A 270      30.785 -22.974  23.455  1.00177.10           C  
HETATM 2278  C42 DPG A 270      29.501 -22.210  23.883  1.00187.10           C  
HETATM 2279  C43 DPG A 270      29.253 -20.716  23.520  1.00178.56           C  
HETATM 2280  C44 DPG A 270      30.292 -19.888  24.352  1.00199.11           C  
HETATM 2281  C45 DPG A 270      29.234 -20.468  21.952  1.00148.82           C  
HETATM 2282  C46 DPG A 270      28.427 -19.275  21.305  1.00139.61           C  
HETATM 2283  C47 DPG A 270      27.908 -19.460  19.846  1.00124.52           C  
HETATM 2284  C48 DPG A 270      27.720 -18.212  18.949  1.00118.61           C  
HETATM 2285  C49 DPG A 270      26.542 -17.346  19.446  1.00121.60           C  
HETATM 2286  C50 DPG A 270      27.488 -18.667  17.508  1.00113.48           C  
HETATM 2287  C51 DPG A 270      28.015 -17.700  16.442  1.00112.39           C  
HETATM 2288  C52 DPG A 270      27.368 -17.881  15.070  1.00113.34           C  
HETATM 2289  C53 DPG A 270      28.300 -17.676  13.791  1.00115.57           C  
HETATM 2290  C54 DPG A 270      29.339 -18.825  13.468  1.00116.21           C  
HETATM 2291  C55 DPG A 270      27.425 -17.264  12.561  1.00117.97           C  
HETATM 2292  C56 DPG A 270      27.843 -17.702  11.142  1.00119.87           C  
HETATM 2293  C57 DPG A 270      27.490 -16.769   9.991  1.00119.80           C  
HETATM 2294  C58 DPG A 270      27.231 -17.639   8.748  1.00117.19           C  
HETATM 2295  C59 DPG A 270      26.276 -16.979   7.735  1.00112.49           C  
HETATM 2296  C60 DPG A 270      28.465 -18.270   8.076  1.00114.37           C  
HETATM 2297  O1  DPG A 270      30.172 -26.837  23.681  1.00182.27           O  
HETATM 2298  O2  DPG A 270      30.957 -23.964  24.492  1.00202.92           O  
HETATM 2299  O3  DPG A 270      34.152 -24.910  23.708  1.00182.90           O  
HETATM 2300  O4  DPG A 270      34.752 -27.120  22.828  1.00164.06           O  
HETATM 2301  O5  DPG A 270      35.638 -26.594  25.134  1.00221.77           O  
HETATM 2302  O6  DPG A 270      36.535 -25.280  23.033  1.00168.12           O  
HETATM 2303  O7  DPG A 270      38.701 -27.732  23.955  1.00188.87           O  
HETATM 2304  O8  DPG A 270      41.332 -26.308  23.660  1.00181.78           O  
HETATM 2305  O9  DPG A 270      41.714 -28.851  23.771  1.00184.39           O  
HETATM 2306  O10 DPG A 270      42.907 -27.338  25.405  1.00230.41           O  
HETATM 2307  O11 DPG A 270      40.486 -27.669  25.613  1.00237.34           O  
HETATM 2308  P1  DPG A 270      35.274 -26.097  23.754  1.00183.99           P  
HETATM 2309  P2  DPG A 270      41.628 -27.594  24.631  1.00206.81           P  
HETATM 2310  C1  RET A 271      15.283   9.939   1.351  1.00 17.34           C  
HETATM 2311  C2  RET A 271      14.545  10.704   0.239  1.00 17.34           C  
HETATM 2312  C3  RET A 271      15.009  12.064   0.051  1.00 17.34           C  
HETATM 2313  C4  RET A 271      14.809  12.878   1.350  1.00 17.34           C  
HETATM 2314  C5  RET A 271      15.182  12.112   2.601  1.00 17.34           C  
HETATM 2315  C6  RET A 271      15.409  10.791   2.626  1.00 17.34           C  
HETATM 2316  C7  RET A 271      15.806  10.044   3.815  1.00 17.34           C  
HETATM 2317  C8  RET A 271      16.045   8.724   3.881  1.00 17.34           C  
HETATM 2318  C9  RET A 271      16.438   7.932   5.031  1.00 17.34           C  
HETATM 2319  C10 RET A 271      16.636   6.592   4.894  1.00 17.34           C  
HETATM 2320  C11 RET A 271      17.015   5.656   5.907  1.00 17.34           C  
HETATM 2321  C12 RET A 271      17.205   4.334   5.712  1.00 17.34           C  
HETATM 2322  C13 RET A 271      17.588   3.300   6.609  1.00 17.34           C  
HETATM 2323  C14 RET A 271      17.682   2.043   6.082  1.00 17.34           C  
HETATM 2324  C15 RET A 271      18.033   0.830   6.672  1.00 17.34           C  
HETATM 2325  C16 RET A 271      14.523   8.640   1.636  1.00 17.34           C  
HETATM 2326  C17 RET A 271      16.671   9.620   0.758  1.00 17.34           C  
HETATM 2327  C18 RET A 271      15.289  13.048   3.781  1.00 17.34           C  
HETATM 2328  C19 RET A 271      16.616   8.643   6.340  1.00 17.34           C  
HETATM 2329  C20 RET A 271      17.856   3.620   8.054  1.00 17.34           C  
CONECT 1631 2324                                                                
CONECT 1720 1721 1766                                                           
CONECT 1721 1720 1722 1767                                                      
CONECT 1722 1721 1768                                                           
CONECT 1723 1724 1771                                                           
CONECT 1724 1723 1725 1772                                                      
CONECT 1725 1724 1773                                                           
CONECT 1726 1727 1766                                                           
CONECT 1727 1726 1728                                                           
CONECT 1728 1727 1729 1730                                                      
CONECT 1729 1728                                                                
CONECT 1730 1728 1731                                                           
CONECT 1731 1730 1732                                                           
CONECT 1732 1731 1733                                                           
CONECT 1733 1732 1734 1735                                                      
CONECT 1734 1733                                                                
CONECT 1735 1733 1736                                                           
CONECT 1736 1735 1737                                                           
CONECT 1737 1736 1738                                                           
CONECT 1738 1737 1739 1740                                                      
CONECT 1739 1738                                                                
CONECT 1740 1738 1741                                                           
CONECT 1741 1740 1742                                                           
CONECT 1742 1741 1743                                                           
CONECT 1743 1742 1744 1745                                                      
CONECT 1744 1743                                                                
CONECT 1745 1743                                                                
CONECT 1746 1747 1767                                                           
CONECT 1747 1746 1748                                                           
CONECT 1748 1747 1749 1750                                                      
CONECT 1749 1748                                                                
CONECT 1750 1748 1751                                                           
CONECT 1751 1750 1752                                                           
CONECT 1752 1751 1753                                                           
CONECT 1753 1752 1754 1755                                                      
CONECT 1754 1753                                                                
CONECT 1755 1753 1756                                                           
CONECT 1756 1755 1757                                                           
CONECT 1757 1756 1758                                                           
CONECT 1758 1757 1759 1760                                                      
CONECT 1759 1758                                                                
CONECT 1760 1758 1761                                                           
CONECT 1761 1760 1762                                                           
CONECT 1762 1761 1763                                                           
CONECT 1763 1762 1764 1765                                                      
CONECT 1764 1763                                                                
CONECT 1765 1763                                                                
CONECT 1766 1720 1726                                                           
CONECT 1767 1721 1746                                                           
CONECT 1768 1722 1777                                                           
CONECT 1769 1777                                                                
CONECT 1770 1777                                                                
CONECT 1771 1723 1777                                                           
CONECT 1772 1724                                                                
CONECT 1773 1725 1778                                                           
CONECT 1774 1778                                                                
CONECT 1775 1778                                                                
CONECT 1776 1778                                                                
CONECT 1777 1768 1769 1770 1771                                                 
CONECT 1778 1773 1774 1775 1776                                                 
CONECT 1779 1780 1825                                                           
CONECT 1780 1779 1781 1826                                                      
CONECT 1781 1780 1827                                                           
CONECT 1782 1783 1830                                                           
CONECT 1783 1782 1784 1831                                                      
CONECT 1784 1783 1832                                                           
CONECT 1785 1786 1825                                                           
CONECT 1786 1785 1787                                                           
CONECT 1787 1786 1788 1789                                                      
CONECT 1788 1787                                                                
CONECT 1789 1787 1790                                                           
CONECT 1790 1789 1791                                                           
CONECT 1791 1790 1792                                                           
CONECT 1792 1791 1793 1794                                                      
CONECT 1793 1792                                                                
CONECT 1794 1792 1795                                                           
CONECT 1795 1794 1796                                                           
CONECT 1796 1795 1797                                                           
CONECT 1797 1796 1798 1799                                                      
CONECT 1798 1797                                                                
CONECT 1799 1797 1800                                                           
CONECT 1800 1799 1801                                                           
CONECT 1801 1800 1802                                                           
CONECT 1802 1801 1803 1804                                                      
CONECT 1803 1802                                                                
CONECT 1804 1802                                                                
CONECT 1805 1806 1826                                                           
CONECT 1806 1805 1807                                                           
CONECT 1807 1806 1808 1809                                                      
CONECT 1808 1807                                                                
CONECT 1809 1807 1810                                                           
CONECT 1810 1809 1811                                                           
CONECT 1811 1810 1812                                                           
CONECT 1812 1811 1813 1814                                                      
CONECT 1813 1812                                                                
CONECT 1814 1812 1815                                                           
CONECT 1815 1814 1816                                                           
CONECT 1816 1815 1817                                                           
CONECT 1817 1816 1818 1819                                                      
CONECT 1818 1817                                                                
CONECT 1819 1817 1820                                                           
CONECT 1820 1819 1821                                                           
CONECT 1821 1820 1822                                                           
CONECT 1822 1821 1823 1824                                                      
CONECT 1823 1822                                                                
CONECT 1824 1822                                                                
CONECT 1825 1779 1785                                                           
CONECT 1826 1780 1805                                                           
CONECT 1827 1781 1836                                                           
CONECT 1828 1836                                                                
CONECT 1829 1836                                                                
CONECT 1830 1782 1836                                                           
CONECT 1831 1783                                                                
CONECT 1832 1784 1837                                                           
CONECT 1833 1837                                                                
CONECT 1834 1837                                                                
CONECT 1835 1837                                                                
CONECT 1836 1827 1828 1829 1830                                                 
CONECT 1837 1832 1833 1834 1835                                                 
CONECT 1838 1839 1884                                                           
CONECT 1839 1838 1840 1885                                                      
CONECT 1840 1839 1886                                                           
CONECT 1841 1842 1889                                                           
CONECT 1842 1841 1843 1890                                                      
CONECT 1843 1842 1891                                                           
CONECT 1844 1845 1884                                                           
CONECT 1845 1844 1846                                                           
CONECT 1846 1845 1847 1848                                                      
CONECT 1847 1846                                                                
CONECT 1848 1846 1849                                                           
CONECT 1849 1848 1850                                                           
CONECT 1850 1849 1851                                                           
CONECT 1851 1850 1852 1853                                                      
CONECT 1852 1851                                                                
CONECT 1853 1851 1854                                                           
CONECT 1854 1853 1855                                                           
CONECT 1855 1854 1856                                                           
CONECT 1856 1855 1857 1858                                                      
CONECT 1857 1856                                                                
CONECT 1858 1856 1859                                                           
CONECT 1859 1858 1860                                                           
CONECT 1860 1859 1861                                                           
CONECT 1861 1860 1862 1863                                                      
CONECT 1862 1861                                                                
CONECT 1863 1861                                                                
CONECT 1864 1865 1885                                                           
CONECT 1865 1864 1866                                                           
CONECT 1866 1865 1867 1868                                                      
CONECT 1867 1866                                                                
CONECT 1868 1866 1869                                                           
CONECT 1869 1868 1870                                                           
CONECT 1870 1869 1871                                                           
CONECT 1871 1870 1872 1873                                                      
CONECT 1872 1871                                                                
CONECT 1873 1871 1874                                                           
CONECT 1874 1873 1875                                                           
CONECT 1875 1874 1876                                                           
CONECT 1876 1875 1877 1878                                                      
CONECT 1877 1876                                                                
CONECT 1878 1876 1879                                                           
CONECT 1879 1878 1880                                                           
CONECT 1880 1879 1881                                                           
CONECT 1881 1880 1882 1883                                                      
CONECT 1882 1881                                                                
CONECT 1883 1881                                                                
CONECT 1884 1838 1844                                                           
CONECT 1885 1839 1864                                                           
CONECT 1886 1840 1895                                                           
CONECT 1887 1895                                                                
CONECT 1888 1895                                                                
CONECT 1889 1841 1895                                                           
CONECT 1890 1842                                                                
CONECT 1891 1843 1896                                                           
CONECT 1892 1896                                                                
CONECT 1893 1896                                                                
CONECT 1894 1896                                                                
CONECT 1895 1886 1887 1888 1889                                                 
CONECT 1896 1891 1892 1893 1894                                                 
CONECT 1897 1898 1943                                                           
CONECT 1898 1897 1899 1944                                                      
CONECT 1899 1898 1945                                                           
CONECT 1900 1901 1948                                                           
CONECT 1901 1900 1902 1949                                                      
CONECT 1902 1901 1950                                                           
CONECT 1903 1904 1943                                                           
CONECT 1904 1903 1905                                                           
CONECT 1905 1904 1906 1907                                                      
CONECT 1906 1905                                                                
CONECT 1907 1905 1908                                                           
CONECT 1908 1907 1909                                                           
CONECT 1909 1908 1910                                                           
CONECT 1910 1909 1911 1912                                                      
CONECT 1911 1910                                                                
CONECT 1912 1910 1913                                                           
CONECT 1913 1912 1914                                                           
CONECT 1914 1913 1915                                                           
CONECT 1915 1914 1916 1917                                                      
CONECT 1916 1915                                                                
CONECT 1917 1915 1918                                                           
CONECT 1918 1917 1919                                                           
CONECT 1919 1918 1920                                                           
CONECT 1920 1919 1921 1922                                                      
CONECT 1921 1920                                                                
CONECT 1922 1920                                                                
CONECT 1923 1924 1944                                                           
CONECT 1924 1923 1925                                                           
CONECT 1925 1924 1926 1927                                                      
CONECT 1926 1925                                                                
CONECT 1927 1925 1928                                                           
CONECT 1928 1927 1929                                                           
CONECT 1929 1928 1930                                                           
CONECT 1930 1929 1931 1932                                                      
CONECT 1931 1930                                                                
CONECT 1932 1930 1933                                                           
CONECT 1933 1932 1934                                                           
CONECT 1934 1933 1935                                                           
CONECT 1935 1934 1936 1937                                                      
CONECT 1936 1935                                                                
CONECT 1937 1935 1938                                                           
CONECT 1938 1937 1939                                                           
CONECT 1939 1938 1940                                                           
CONECT 1940 1939 1941 1942                                                      
CONECT 1941 1940                                                                
CONECT 1942 1940                                                                
CONECT 1943 1897 1903                                                           
CONECT 1944 1898 1923                                                           
CONECT 1945 1899 1954                                                           
CONECT 1946 1954                                                                
CONECT 1947 1954                                                                
CONECT 1948 1900 1954                                                           
CONECT 1949 1901                                                                
CONECT 1950 1902 1955                                                           
CONECT 1951 1955                                                                
CONECT 1952 1955                                                                
CONECT 1953 1955                                                                
CONECT 1954 1945 1946 1947 1948                                                 
CONECT 1955 1950 1951 1952 1953                                                 
CONECT 1956 1957 2002                                                           
CONECT 1957 1956 1958 2003                                                      
CONECT 1958 1957 2004                                                           
CONECT 1959 1960 2007                                                           
CONECT 1960 1959 1961 2008                                                      
CONECT 1961 1960 2009                                                           
CONECT 1962 1963 2002                                                           
CONECT 1963 1962 1964                                                           
CONECT 1964 1963 1965 1966                                                      
CONECT 1965 1964                                                                
CONECT 1966 1964 1967                                                           
CONECT 1967 1966 1968                                                           
CONECT 1968 1967 1969                                                           
CONECT 1969 1968 1970 1971                                                      
CONECT 1970 1969                                                                
CONECT 1971 1969 1972                                                           
CONECT 1972 1971 1973                                                           
CONECT 1973 1972 1974                                                           
CONECT 1974 1973 1975 1976                                                      
CONECT 1975 1974                                                                
CONECT 1976 1974 1977                                                           
CONECT 1977 1976 1978                                                           
CONECT 1978 1977 1979                                                           
CONECT 1979 1978 1980 1981                                                      
CONECT 1980 1979                                                                
CONECT 1981 1979                                                                
CONECT 1982 1983 2003                                                           
CONECT 1983 1982 1984                                                           
CONECT 1984 1983 1985 1986                                                      
CONECT 1985 1984                                                                
CONECT 1986 1984 1987                                                           
CONECT 1987 1986 1988                                                           
CONECT 1988 1987 1989                                                           
CONECT 1989 1988 1990 1991                                                      
CONECT 1990 1989                                                                
CONECT 1991 1989 1992                                                           
CONECT 1992 1991 1993                                                           
CONECT 1993 1992 1994                                                           
CONECT 1994 1993 1995 1996                                                      
CONECT 1995 1994                                                                
CONECT 1996 1994 1997                                                           
CONECT 1997 1996 1998                                                           
CONECT 1998 1997 1999                                                           
CONECT 1999 1998 2000 2001                                                      
CONECT 2000 1999                                                                
CONECT 2001 1999                                                                
CONECT 2002 1956 1962                                                           
CONECT 2003 1957 1982                                                           
CONECT 2004 1958 2013                                                           
CONECT 2005 2013                                                                
CONECT 2006 2013                                                                
CONECT 2007 1959 2013                                                           
CONECT 2008 1960                                                                
CONECT 2009 1961 2014                                                           
CONECT 2010 2014                                                                
CONECT 2011 2014                                                                
CONECT 2012 2014                                                                
CONECT 2013 2004 2005 2006 2007                                                 
CONECT 2014 2009 2010 2011 2012                                                 
CONECT 2015 2016 2061                                                           
CONECT 2016 2015 2017 2062                                                      
CONECT 2017 2016 2063                                                           
CONECT 2018 2019 2066                                                           
CONECT 2019 2018 2020 2067                                                      
CONECT 2020 2019 2068                                                           
CONECT 2021 2022 2061                                                           
CONECT 2022 2021 2023                                                           
CONECT 2023 2022 2024 2025                                                      
CONECT 2024 2023                                                                
CONECT 2025 2023 2026                                                           
CONECT 2026 2025 2027                                                           
CONECT 2027 2026 2028                                                           
CONECT 2028 2027 2029 2030                                                      
CONECT 2029 2028                                                                
CONECT 2030 2028 2031                                                           
CONECT 2031 2030 2032                                                           
CONECT 2032 2031 2033                                                           
CONECT 2033 2032 2034 2035                                                      
CONECT 2034 2033                                                                
CONECT 2035 2033 2036                                                           
CONECT 2036 2035 2037                                                           
CONECT 2037 2036 2038                                                           
CONECT 2038 2037 2039 2040                                                      
CONECT 2039 2038                                                                
CONECT 2040 2038                                                                
CONECT 2041 2042 2062                                                           
CONECT 2042 2041 2043                                                           
CONECT 2043 2042 2044 2045                                                      
CONECT 2044 2043                                                                
CONECT 2045 2043 2046                                                           
CONECT 2046 2045 2047                                                           
CONECT 2047 2046 2048                                                           
CONECT 2048 2047 2049 2050                                                      
CONECT 2049 2048                                                                
CONECT 2050 2048 2051                                                           
CONECT 2051 2050 2052                                                           
CONECT 2052 2051 2053                                                           
CONECT 2053 2052 2054 2055                                                      
CONECT 2054 2053                                                                
CONECT 2055 2053 2056                                                           
CONECT 2056 2055 2057                                                           
CONECT 2057 2056 2058                                                           
CONECT 2058 2057 2059 2060                                                      
CONECT 2059 2058                                                                
CONECT 2060 2058                                                                
CONECT 2061 2015 2021                                                           
CONECT 2062 2016 2041                                                           
CONECT 2063 2017 2072                                                           
CONECT 2064 2072                                                                
CONECT 2065 2072                                                                
CONECT 2066 2018 2072                                                           
CONECT 2067 2019                                                                
CONECT 2068 2020 2073                                                           
CONECT 2069 2073                                                                
CONECT 2070 2073                                                                
CONECT 2071 2073                                                                
CONECT 2072 2063 2064 2065 2066                                                 
CONECT 2073 2068 2069 2070 2071                                                 
CONECT 2074 2075 2120                                                           
CONECT 2075 2074 2076 2121                                                      
CONECT 2076 2075 2122                                                           
CONECT 2077 2078 2125                                                           
CONECT 2078 2077 2079 2126                                                      
CONECT 2079 2078 2127                                                           
CONECT 2080 2081 2120                                                           
CONECT 2081 2080 2082                                                           
CONECT 2082 2081 2083 2084                                                      
CONECT 2083 2082                                                                
CONECT 2084 2082 2085                                                           
CONECT 2085 2084 2086                                                           
CONECT 2086 2085 2087                                                           
CONECT 2087 2086 2088 2089                                                      
CONECT 2088 2087                                                                
CONECT 2089 2087 2090                                                           
CONECT 2090 2089 2091                                                           
CONECT 2091 2090 2092                                                           
CONECT 2092 2091 2093 2094                                                      
CONECT 2093 2092                                                                
CONECT 2094 2092 2095                                                           
CONECT 2095 2094 2096                                                           
CONECT 2096 2095 2097                                                           
CONECT 2097 2096 2098 2099                                                      
CONECT 2098 2097                                                                
CONECT 2099 2097                                                                
CONECT 2100 2101 2121                                                           
CONECT 2101 2100 2102                                                           
CONECT 2102 2101 2103 2104                                                      
CONECT 2103 2102                                                                
CONECT 2104 2102 2105                                                           
CONECT 2105 2104 2106                                                           
CONECT 2106 2105 2107                                                           
CONECT 2107 2106 2108 2109                                                      
CONECT 2108 2107                                                                
CONECT 2109 2107 2110                                                           
CONECT 2110 2109 2111                                                           
CONECT 2111 2110 2112                                                           
CONECT 2112 2111 2113 2114                                                      
CONECT 2113 2112                                                                
CONECT 2114 2112 2115                                                           
CONECT 2115 2114 2116                                                           
CONECT 2116 2115 2117                                                           
CONECT 2117 2116 2118 2119                                                      
CONECT 2118 2117                                                                
CONECT 2119 2117                                                                
CONECT 2120 2074 2080                                                           
CONECT 2121 2075 2100                                                           
CONECT 2122 2076 2131                                                           
CONECT 2123 2131                                                                
CONECT 2124 2131                                                                
CONECT 2125 2077 2131                                                           
CONECT 2126 2078                                                                
CONECT 2127 2079 2132                                                           
CONECT 2128 2132                                                                
CONECT 2129 2132                                                                
CONECT 2130 2132                                                                
CONECT 2131 2122 2123 2124 2125                                                 
CONECT 2132 2127 2128 2129 2130                                                 
CONECT 2133 2134 2179                                                           
CONECT 2134 2133 2135 2180                                                      
CONECT 2135 2134 2181                                                           
CONECT 2136 2137 2184                                                           
CONECT 2137 2136 2138 2185                                                      
CONECT 2138 2137 2186                                                           
CONECT 2139 2140 2179                                                           
CONECT 2140 2139 2141                                                           
CONECT 2141 2140 2142 2143                                                      
CONECT 2142 2141                                                                
CONECT 2143 2141 2144                                                           
CONECT 2144 2143 2145                                                           
CONECT 2145 2144 2146                                                           
CONECT 2146 2145 2147 2148                                                      
CONECT 2147 2146                                                                
CONECT 2148 2146 2149                                                           
CONECT 2149 2148 2150                                                           
CONECT 2150 2149 2151                                                           
CONECT 2151 2150 2152 2153                                                      
CONECT 2152 2151                                                                
CONECT 2153 2151 2154                                                           
CONECT 2154 2153 2155                                                           
CONECT 2155 2154 2156                                                           
CONECT 2156 2155 2157 2158                                                      
CONECT 2157 2156                                                                
CONECT 2158 2156                                                                
CONECT 2159 2160 2180                                                           
CONECT 2160 2159 2161                                                           
CONECT 2161 2160 2162 2163                                                      
CONECT 2162 2161                                                                
CONECT 2163 2161 2164                                                           
CONECT 2164 2163 2165                                                           
CONECT 2165 2164 2166                                                           
CONECT 2166 2165 2167 2168                                                      
CONECT 2167 2166                                                                
CONECT 2168 2166 2169                                                           
CONECT 2169 2168 2170                                                           
CONECT 2170 2169 2171                                                           
CONECT 2171 2170 2172 2173                                                      
CONECT 2172 2171                                                                
CONECT 2173 2171 2174                                                           
CONECT 2174 2173 2175                                                           
CONECT 2175 2174 2176                                                           
CONECT 2176 2175 2177 2178                                                      
CONECT 2177 2176                                                                
CONECT 2178 2176                                                                
CONECT 2179 2133 2139                                                           
CONECT 2180 2134 2159                                                           
CONECT 2181 2135 2190                                                           
CONECT 2182 2190                                                                
CONECT 2183 2190                                                                
CONECT 2184 2136 2190                                                           
CONECT 2185 2137                                                                
CONECT 2186 2138 2191                                                           
CONECT 2187 2191                                                                
CONECT 2188 2191                                                                
CONECT 2189 2191                                                                
CONECT 2190 2181 2182 2183 2184                                                 
CONECT 2191 2186 2187 2188 2189                                                 
CONECT 2192 2193 2238                                                           
CONECT 2193 2192 2194 2239                                                      
CONECT 2194 2193 2240                                                           
CONECT 2195 2196 2243                                                           
CONECT 2196 2195 2197 2244                                                      
CONECT 2197 2196 2245                                                           
CONECT 2198 2199 2238                                                           
CONECT 2199 2198 2200                                                           
CONECT 2200 2199 2201 2202                                                      
CONECT 2201 2200                                                                
CONECT 2202 2200 2203                                                           
CONECT 2203 2202 2204                                                           
CONECT 2204 2203 2205                                                           
CONECT 2205 2204 2206 2207                                                      
CONECT 2206 2205                                                                
CONECT 2207 2205 2208                                                           
CONECT 2208 2207 2209                                                           
CONECT 2209 2208 2210                                                           
CONECT 2210 2209 2211 2212                                                      
CONECT 2211 2210                                                                
CONECT 2212 2210 2213                                                           
CONECT 2213 2212 2214                                                           
CONECT 2214 2213 2215                                                           
CONECT 2215 2214 2216 2217                                                      
CONECT 2216 2215                                                                
CONECT 2217 2215                                                                
CONECT 2218 2219 2239                                                           
CONECT 2219 2218 2220                                                           
CONECT 2220 2219 2221 2222                                                      
CONECT 2221 2220                                                                
CONECT 2222 2220 2223                                                           
CONECT 2223 2222 2224                                                           
CONECT 2224 2223 2225                                                           
CONECT 2225 2224 2226 2227                                                      
CONECT 2226 2225                                                                
CONECT 2227 2225 2228                                                           
CONECT 2228 2227 2229                                                           
CONECT 2229 2228 2230                                                           
CONECT 2230 2229 2231 2232                                                      
CONECT 2231 2230                                                                
CONECT 2232 2230 2233                                                           
CONECT 2233 2232 2234                                                           
CONECT 2234 2233 2235                                                           
CONECT 2235 2234 2236 2237                                                      
CONECT 2236 2235                                                                
CONECT 2237 2235                                                                
CONECT 2238 2192 2198                                                           
CONECT 2239 2193 2218                                                           
CONECT 2240 2194 2249                                                           
CONECT 2241 2249                                                                
CONECT 2242 2249                                                                
CONECT 2243 2195 2249                                                           
CONECT 2244 2196                                                                
CONECT 2245 2197 2250                                                           
CONECT 2246 2250                                                                
CONECT 2247 2250                                                                
CONECT 2248 2250                                                                
CONECT 2249 2240 2241 2242 2243                                                 
CONECT 2250 2245 2246 2247 2248                                                 
CONECT 2251 2252 2297                                                           
CONECT 2252 2251 2253 2298                                                      
CONECT 2253 2252 2299                                                           
CONECT 2254 2255 2302                                                           
CONECT 2255 2254 2256 2303                                                      
CONECT 2256 2255 2304                                                           
CONECT 2257 2258 2297                                                           
CONECT 2258 2257 2259                                                           
CONECT 2259 2258 2260 2261                                                      
CONECT 2260 2259                                                                
CONECT 2261 2259 2262                                                           
CONECT 2262 2261 2263                                                           
CONECT 2263 2262 2264                                                           
CONECT 2264 2263 2265 2266                                                      
CONECT 2265 2264                                                                
CONECT 2266 2264 2267                                                           
CONECT 2267 2266 2268                                                           
CONECT 2268 2267 2269                                                           
CONECT 2269 2268 2270 2271                                                      
CONECT 2270 2269                                                                
CONECT 2271 2269 2272                                                           
CONECT 2272 2271 2273                                                           
CONECT 2273 2272 2274                                                           
CONECT 2274 2273 2275 2276                                                      
CONECT 2275 2274                                                                
CONECT 2276 2274                                                                
CONECT 2277 2278 2298                                                           
CONECT 2278 2277 2279                                                           
CONECT 2279 2278 2280 2281                                                      
CONECT 2280 2279                                                                
CONECT 2281 2279 2282                                                           
CONECT 2282 2281 2283                                                           
CONECT 2283 2282 2284                                                           
CONECT 2284 2283 2285 2286                                                      
CONECT 2285 2284                                                                
CONECT 2286 2284 2287                                                           
CONECT 2287 2286 2288                                                           
CONECT 2288 2287 2289                                                           
CONECT 2289 2288 2290 2291                                                      
CONECT 2290 2289                                                                
CONECT 2291 2289 2292                                                           
CONECT 2292 2291 2293                                                           
CONECT 2293 2292 2294                                                           
CONECT 2294 2293 2295 2296                                                      
CONECT 2295 2294                                                                
CONECT 2296 2294                                                                
CONECT 2297 2251 2257                                                           
CONECT 2298 2252 2277                                                           
CONECT 2299 2253 2308                                                           
CONECT 2300 2308                                                                
CONECT 2301 2308                                                                
CONECT 2302 2254 2308                                                           
CONECT 2303 2255                                                                
CONECT 2304 2256 2309                                                           
CONECT 2305 2309                                                                
CONECT 2306 2309                                                                
CONECT 2307 2309                                                                
CONECT 2308 2299 2300 2301 2302                                                 
CONECT 2309 2304 2305 2306 2307                                                 
CONECT 2310 2311 2315 2325 2326                                                 
CONECT 2311 2310 2312                                                           
CONECT 2312 2311 2313                                                           
CONECT 2313 2312 2314                                                           
CONECT 2314 2313 2315 2327                                                      
CONECT 2315 2310 2314 2316                                                      
CONECT 2316 2315 2317                                                           
CONECT 2317 2316 2318                                                           
CONECT 2318 2317 2319 2328                                                      
CONECT 2319 2318 2320                                                           
CONECT 2320 2319 2321                                                           
CONECT 2321 2320 2322                                                           
CONECT 2322 2321 2323 2329                                                      
CONECT 2323 2322 2324                                                           
CONECT 2324 1631 2323                                                           
CONECT 2325 2310                                                                
CONECT 2326 2310                                                                
CONECT 2327 2314                                                                
CONECT 2328 2318                                                                
CONECT 2329 2322                                                                
MASTER      333    0   11    7    0    0   33    6 2328    1  611   20          
END                                                                             
