HEADER    PHOTORECEPTOR                           17-DEC-98   2AT9              
TITLE     STRUCTURE OF BACTERIORHODOPSIN AT 3.0 ANGSTROM BY ELECTRON            
TITLE    2 CRYSTALLOGRAPHY                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BACTERIORHODOPSIN;                                         
COMPND   3 CHAIN: A                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HALOBACTERIUM SALINARUM;                        
SOURCE   3 ORGANISM_TAXID: 2242;                                                
SOURCE   4 STRAIN: JW5                                                          
KEYWDS    PROTON PUMP, MEMBRANE PROTEIN, RETINAL PROTEIN, TWO-DIMENSIONAL       
KEYWDS   2 CRYSTAL, PHOTORECEPTOR                                               
EXPDTA    ELECTRON CRYSTALLOGRAPHY                                              
AUTHOR    K.MITSUOKA,T.HIRAI,K.MURATA,A.MIYAZAWA,A.KIDERA,Y.KIMURA,Y.FUJIYOSHI  
REVDAT   3   13-JUL-11 2AT9    1       VERSN                                    
REVDAT   2   24-FEB-09 2AT9    1       VERSN                                    
REVDAT   1   27-APR-99 2AT9    0                                                
JRNL        AUTH   K.MITSUOKA,T.HIRAI,K.MURATA,A.MIYAZAWA,A.KIDERA,Y.KIMURA,    
JRNL        AUTH 2 Y.FUJIYOSHI                                                  
JRNL        TITL   THE STRUCTURE OF BACTERIORHODOPSIN AT 3.0 A RESOLUTION BASED 
JRNL        TITL 2 ON ELECTRON CRYSTALLOGRAPHY: IMPLICATION OF THE CHARGE       
JRNL        TITL 3 DISTRIBUTION.                                                
JRNL        REF    J.MOL.BIOL.                   V. 286   861 1999              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   10024456                                                     
JRNL        DOI    10.1006/JMBI.1998.2529                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   H.LUECKE,H.T.RICHTER,J.K.LANYI                               
REMARK   1  TITL   PROTON TRANSFER PATHWAYS IN BACTERIORHODOPSIN AT 2.3         
REMARK   1  TITL 2 ANGSTROM RESOLUTION                                          
REMARK   1  REF    SCIENCE                       V. 280  1934 1998              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Y.KIMURA,D.G.VASSYLYEV,A.MIYAZAWA,A.KIDERA,M.MATSUSHIMA,     
REMARK   1  AUTH 2 K.MITSUOKA,K.MURATA,T.HIRAI,Y.FUJIYOSHI                      
REMARK   1  TITL   SURFACE OF BACTERIORHODOPSIN REVEALED BY HIGH-RESOLUTION     
REMARK   1  TITL 2 ELECTRON CRYSTALLOGRAPHY                                     
REMARK   1  REF    NATURE                        V. 389   206 1997              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   N.GRIGORIEFF,T.A.CESKA,K.H.DOWNING,J.M.BALDWIN,R.HENDERSON   
REMARK   1  TITL   ELECTRON-CRYSTALLOGRAPHIC REFINEMENT OF THE STRUCTURE OF     
REMARK   1  TITL 2 BACTERIORHODOPSIN                                            
REMARK   1  REF    J.MOL.BIOL.                   V. 259   393 1996              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 4                                                          
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   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 73.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 6107                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.330                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 358                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.13                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 39.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 219                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2930                       
REMARK   3   BIN FREE R VALUE                    : 0.3690                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 1.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 14                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1721                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 500                                     
REMARK   3   SOLVENT ATOMS            : 2                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.20                          
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) : 0.40                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.40                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 8.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.54                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.53                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.00                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 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  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2AT9 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          : NULL                              
REMARK 240   SAMPLE TYPE                    : NULL                              
REMARK 240   SPECIMEN TYPE                  : NULL                              
REMARK 240 DATA ACQUISITION                                                     
REMARK 240   DATE OF DATA COLLECTION        : NULL                              
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   : NULL                              
REMARK 240   RESOLUTION RANGE HIGH      (A) : NULL                              
REMARK 240   RESOLUTION RANGE LOW       (A) : NULL                              
REMARK 240   DATA SCALING SOFTWARE          : NULL                              
REMARK 240   COMPLETENESS FOR RANGE     (%) : NULL                              
REMARK 240   DATA REDUNDANCY                : NULL                              
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                  : X-PLOR 3.851                      
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: 27520 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -247.0 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     ALA A   228                                                      
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ALA A    98     O    VAL A   101              2.17            
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    LEU A  25       -9.29    -48.80                                   
REMARK 500    PRO A  37       41.99    -66.65                                   
REMARK 500    PHE A  42      -70.75    -68.35                                   
REMARK 500    TYR A  43      -25.10    -36.63                                   
REMARK 500    ALA A  44      -74.18    -76.04                                   
REMARK 500    ILE A  45      -65.03    -29.44                                   
REMARK 500    GLU A  74     -165.39   -163.36                                   
REMARK 500    TYR A  79       81.18    -62.09                                   
REMARK 500    LEU A  97      -73.36    -70.35                                   
REMARK 500    LEU A  99      -81.65    -56.04                                   
REMARK 500    LEU A 100      -61.40    -24.51                                   
REMARK 500    ASP A 102      105.59    -34.07                                   
REMARK 500    ASP A 104      136.49    -31.42                                   
REMARK 500    ILE A 108      -72.47    -69.83                                   
REMARK 500    ASP A 115      -73.21    -66.35                                   
REMARK 500    LEU A 127      -11.70   -144.95                                   
REMARK 500    ARG A 134      -97.06    -57.67                                   
REMARK 500    PHE A 135      -38.57     -9.53                                   
REMARK 500    ALA A 143      -51.71    -26.51                                   
REMARK 500    LEU A 146      -15.11    -49.89                                   
REMARK 500    PHE A 153      -99.80    -88.01                                   
REMARK 500    PHE A 156        6.35    -59.06                                   
REMARK 500    SER A 158     -141.09    -47.16                                   
REMARK 500    ALA A 160       85.83    -52.95                                   
REMARK 500    ARG A 164      105.29    -49.85                                   
REMARK 500    PRO A 165       18.36    -65.16                                   
REMARK 500    ALA A 168      -86.23    -10.58                                   
REMARK 500    SER A 169      -70.32    -41.51                                   
REMARK 500    THR A 170      -32.88    -38.26                                   
REMARK 500    SER A 183       -1.42    -52.69                                   
REMARK 500    ILE A 198      -91.04    -78.50                                   
REMARK 500    ASP A 212      -71.20    -71.88                                   
REMARK 500    SER A 214       -8.59    -51.13                                   
REMARK 500    LYS A 216      -83.63   -111.26                                   
REMARK 500    PHE A 219      -85.18    -36.68                                   
REMARK 500    ILE A 222      -11.06    -39.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 147         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL A  34        24.6      L          L   OUTSIDE RANGE           
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 2DP A 261                 
DBREF  2AT9 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    RET  A 249A     20                                                       
HET    2DP  A 261      60                                                       
HET    2DP  A 262      60                                                       
HET    2DP  A 263      60                                                       
HET    2DP  A 264      60                                                       
HET    2DP  A 265      60                                                       
HET    2DP  A 267      60                                                       
HET    2DP  A 268      60                                                       
HET    2DP  A 269      60                                                       
HETNAM     RET RETINAL                                                          
HETNAM     2DP 3-[[3-METHYLPHOSPHONO-GLYCEROLYL]PHOSPHONYL]-[1,2-DI[2,          
HETNAM   2 2DP  6,10,14-TETRAMETHYL-HEXADECAN-16-YL]GLYCEROL                    
FORMUL   2  RET    C20 H28 O                                                    
FORMUL   3  2DP    8(C47 H98 O11 P2)                                            
FORMUL  11  HOH   *2(H2 O)                                                      
HELIX    1   A PRO A    8  LYS A   30  1                                  23    
HELIX    2   B PRO A   37  LEU A   62  1                                  26    
HELIX    3   C TRP A   80  ASP A  102  1                                  23    
HELIX    4   D GLN A  105  LEU A  127  1                                  23    
HELIX    5   E TYR A  131  PHE A  156  1                                  26    
HELIX    6   F PRO A  165  ALA A  196  1                                  32    
HELIX    7   G LEU A  201  ARG A  225  1                                  25    
SHEET    1   A 2 THR A  67  VAL A  69  0                                        
SHEET    2   A 2 ASN A  76  ILE A  78 -1  N  ILE A  78   O  THR A  67           
LINK         C15 RET A 249A                NZ  LYS A 216     1555   1555  1.34  
SITE     1 AC1  5 LEU A  48  ILE A  52  TYR A  64  TRP A  80                    
SITE     2 AC1  5 PHE A  88                                                     
CRYST1   62.450   62.450  100.000  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  0.010000        0.00000                         
ATOM      1  N   GLY A   6      22.472  -4.457 -24.245  1.00 15.37           N  
ATOM      2  CA  GLY A   6      23.361  -5.050 -23.192  1.00 14.16           C  
ATOM      3  C   GLY A   6      23.216  -4.317 -21.874  1.00 13.63           C  
ATOM      4  O   GLY A   6      23.180  -3.088 -21.849  1.00 13.82           O  
ATOM      5  N   ARG A   7      23.130  -5.063 -20.776  1.00 12.52           N  
ATOM      6  CA  ARG A   7      22.966  -4.448 -19.459  1.00 10.85           C  
ATOM      7  C   ARG A   7      24.176  -4.631 -18.576  1.00  8.51           C  
ATOM      8  O   ARG A   7      24.330  -5.644 -17.902  1.00  7.75           O  
ATOM      9  CB  ARG A   7      21.717  -5.002 -18.747  1.00 10.40           C  
ATOM     10  CG  ARG A   7      20.992  -3.986 -17.879  1.00  7.49           C  
ATOM     11  CD  ARG A   7      19.533  -4.280 -17.784  1.00  4.28           C  
ATOM     12  NE  ARG A   7      19.145  -4.606 -16.423  1.00  5.46           N  
ATOM     13  CZ  ARG A   7      18.617  -5.770 -16.070  1.00  6.05           C  
ATOM     14  NH1 ARG A   7      18.420  -6.698 -16.993  1.00  4.07           N  
ATOM     15  NH2 ARG A   7      18.295  -6.013 -14.802  1.00  5.80           N  
ATOM     16  N   PRO A   8      25.057  -3.633 -18.575  1.00  9.24           N  
ATOM     17  CA  PRO A   8      26.267  -3.680 -17.770  1.00 10.09           C  
ATOM     18  C   PRO A   8      26.085  -3.192 -16.331  1.00 12.71           C  
ATOM     19  O   PRO A   8      27.067  -2.966 -15.629  1.00 13.73           O  
ATOM     20  CB  PRO A   8      27.249  -2.826 -18.560  1.00  8.91           C  
ATOM     21  CG  PRO A   8      26.398  -1.921 -19.408  1.00  9.08           C  
ATOM     22  CD  PRO A   8      24.976  -2.394 -19.363  1.00  9.37           C  
ATOM     23  N   GLU A   9      24.851  -3.013 -15.882  1.00 14.28           N  
ATOM     24  CA  GLU A   9      24.650  -2.582 -14.503  1.00 18.61           C  
ATOM     25  C   GLU A   9      24.483  -3.891 -13.756  1.00 19.72           C  
ATOM     26  O   GLU A   9      24.487  -3.950 -12.514  1.00 18.95           O  
ATOM     27  CB  GLU A   9      23.379  -1.740 -14.354  1.00 20.31           C  
ATOM     28  CG  GLU A   9      23.173  -0.705 -15.455  1.00 22.92           C  
ATOM     29  CD  GLU A   9      22.539  -1.300 -16.703  1.00 22.75           C  
ATOM     30  OE1 GLU A   9      23.071  -2.312 -17.209  1.00 22.27           O  
ATOM     31  OE2 GLU A   9      21.509  -0.758 -17.170  1.00 25.13           O  
ATOM     32  N   TRP A  10      24.347  -4.942 -14.555  1.00 17.85           N  
ATOM     33  CA  TRP A  10      24.165  -6.285 -14.049  1.00 18.25           C  
ATOM     34  C   TRP A  10      25.072  -6.639 -12.861  1.00 17.69           C  
ATOM     35  O   TRP A  10      24.592  -7.179 -11.864  1.00 18.64           O  
ATOM     36  CB  TRP A  10      24.371  -7.306 -15.185  1.00 18.21           C  
ATOM     37  CG  TRP A  10      25.756  -7.873 -15.228  1.00 16.22           C  
ATOM     38  CD1 TRP A  10      26.816  -7.377 -15.919  1.00 18.01           C  
ATOM     39  CD2 TRP A  10      26.251  -8.978 -14.474  1.00 15.42           C  
ATOM     40  NE1 TRP A  10      27.953  -8.101 -15.646  1.00 17.11           N  
ATOM     41  CE2 TRP A  10      27.635  -9.091 -14.759  1.00 16.02           C  
ATOM     42  CE3 TRP A  10      25.668  -9.886 -13.584  1.00 14.82           C  
ATOM     43  CZ2 TRP A  10      28.437 -10.071 -14.188  1.00 13.79           C  
ATOM     44  CZ3 TRP A  10      26.464 -10.856 -13.016  1.00 14.90           C  
ATOM     45  CH2 TRP A  10      27.838 -10.942 -13.320  1.00 14.61           C  
ATOM     46  N   ILE A  11      26.368  -6.335 -12.947  1.00 15.72           N  
ATOM     47  CA  ILE A  11      27.278  -6.695 -11.856  1.00 13.24           C  
ATOM     48  C   ILE A  11      27.088  -5.951 -10.524  1.00 13.27           C  
ATOM     49  O   ILE A  11      27.098  -6.577  -9.460  1.00 11.93           O  
ATOM     50  CB  ILE A  11      28.752  -6.601 -12.296  1.00  8.90           C  
ATOM     51  CG1 ILE A  11      29.622  -7.342 -11.287  1.00  9.13           C  
ATOM     52  CG2 ILE A  11      29.179  -5.186 -12.405  1.00  8.45           C  
ATOM     53  CD1 ILE A  11      29.567  -8.873 -11.426  1.00  6.35           C  
ATOM     54  N   TRP A  12      26.900  -4.633 -10.576  1.00 12.47           N  
ATOM     55  CA  TRP A  12      26.698  -3.857  -9.351  1.00 11.21           C  
ATOM     56  C   TRP A  12      25.342  -4.221  -8.755  1.00  8.02           C  
ATOM     57  O   TRP A  12      25.129  -4.083  -7.553  1.00  7.40           O  
ATOM     58  CB  TRP A  12      26.758  -2.336  -9.640  1.00 10.48           C  
ATOM     59  CG  TRP A  12      28.032  -1.910 -10.271  1.00  5.94           C  
ATOM     60  CD1 TRP A  12      28.187  -1.291 -11.472  1.00  5.10           C  
ATOM     61  CD2 TRP A  12      29.338  -2.232  -9.817  1.00  6.06           C  
ATOM     62  NE1 TRP A  12      29.512  -1.217 -11.801  1.00  4.47           N  
ATOM     63  CE2 TRP A  12      30.243  -1.796 -10.794  1.00  5.79           C  
ATOM     64  CE3 TRP A  12      29.830  -2.859  -8.667  1.00  5.65           C  
ATOM     65  CZ2 TRP A  12      31.617  -1.962 -10.665  1.00  6.24           C  
ATOM     66  CZ3 TRP A  12      31.199  -3.029  -8.540  1.00  6.45           C  
ATOM     67  CH2 TRP A  12      32.074  -2.584  -9.530  1.00  6.65           C  
ATOM     68  N   LEU A  13      24.437  -4.681  -9.616  1.00  6.84           N  
ATOM     69  CA  LEU A  13      23.092  -5.082  -9.211  1.00  5.30           C  
ATOM     70  C   LEU A  13      23.097  -6.580  -8.964  1.00  5.59           C  
ATOM     71  O   LEU A  13      22.136  -7.128  -8.433  1.00  5.60           O  
ATOM     72  CB  LEU A  13      22.079  -4.786 -10.322  1.00  6.24           C  
ATOM     73  CG  LEU A  13      21.183  -3.561 -10.288  1.00  2.07           C  
ATOM     74  CD1 LEU A  13      20.079  -3.697 -11.311  1.00  2.00           C  
ATOM     75  CD2 LEU A  13      20.643  -3.418  -8.897  1.00  3.36           C  
ATOM     76  N   ALA A  14      24.173  -7.239  -9.377  1.00  5.31           N  
ATOM     77  CA  ALA A  14      24.301  -8.676  -9.197  1.00  5.63           C  
ATOM     78  C   ALA A  14      24.979  -8.927  -7.865  1.00  5.57           C  
ATOM     79  O   ALA A  14      25.103 -10.063  -7.412  1.00  5.47           O  
ATOM     80  CB  ALA A  14      25.128  -9.272 -10.326  1.00  2.22           C  
ATOM     81  N   LEU A  15      25.398  -7.839  -7.235  1.00  5.90           N  
ATOM     82  CA  LEU A  15      26.104  -7.900  -5.970  1.00  5.77           C  
ATOM     83  C   LEU A  15      25.311  -7.391  -4.755  1.00  6.90           C  
ATOM     84  O   LEU A  15      25.730  -7.583  -3.614  1.00  6.91           O  
ATOM     85  CB  LEU A  15      27.411  -7.121  -6.119  1.00  4.47           C  
ATOM     86  CG  LEU A  15      28.293  -6.932  -4.894  1.00  4.47           C  
ATOM     87  CD1 LEU A  15      28.541  -8.254  -4.184  1.00  4.96           C  
ATOM     88  CD2 LEU A  15      29.596  -6.332  -5.347  1.00  4.42           C  
ATOM     89  N   GLY A  16      24.174  -6.741  -4.992  1.00  7.05           N  
ATOM     90  CA  GLY A  16      23.370  -6.239  -3.889  1.00  6.47           C  
ATOM     91  C   GLY A  16      22.408  -7.301  -3.366  1.00  8.66           C  
ATOM     92  O   GLY A  16      21.803  -7.141  -2.303  1.00  8.85           O  
ATOM     93  N   THR A  17      22.262  -8.388  -4.126  1.00  8.43           N  
ATOM     94  CA  THR A  17      21.387  -9.502  -3.759  1.00  7.89           C  
ATOM     95  C   THR A  17      22.137 -10.279  -2.706  1.00  7.86           C  
ATOM     96  O   THR A  17      21.624 -10.543  -1.620  1.00  7.81           O  
ATOM     97  CB  THR A  17      21.123 -10.460  -4.965  1.00  8.64           C  
ATOM     98  OG1 THR A  17      21.311  -9.760  -6.199  1.00  7.72           O  
ATOM     99  CG2 THR A  17      19.711 -10.998  -4.932  1.00  8.76           C  
ATOM    100  N   ALA A  18      23.368 -10.644  -3.061  1.00 10.07           N  
ATOM    101  CA  ALA A  18      24.268 -11.401  -2.192  1.00 11.01           C  
ATOM    102  C   ALA A  18      24.441 -10.714  -0.830  1.00 11.22           C  
ATOM    103  O   ALA A  18      24.087 -11.269   0.211  1.00 11.97           O  
ATOM    104  CB  ALA A  18      25.621 -11.563  -2.877  1.00  7.66           C  
ATOM    105  N   LEU A  19      24.983  -9.503  -0.854  1.00  9.54           N  
ATOM    106  CA  LEU A  19      25.212  -8.725   0.346  1.00  8.94           C  
ATOM    107  C   LEU A  19      23.990  -8.598   1.246  1.00 10.65           C  
ATOM    108  O   LEU A  19      24.037  -8.926   2.433  1.00 11.08           O  
ATOM    109  CB  LEU A  19      25.671  -7.334  -0.046  1.00  9.27           C  
ATOM    110  CG  LEU A  19      27.150  -7.254  -0.375  1.00 13.25           C  
ATOM    111  CD1 LEU A  19      27.658  -5.847  -0.079  1.00 11.80           C  
ATOM    112  CD2 LEU A  19      27.901  -8.312   0.432  1.00 10.82           C  
ATOM    113  N   MET A  20      22.897  -8.100   0.677  1.00  9.64           N  
ATOM    114  CA  MET A  20      21.667  -7.895   1.425  1.00  8.38           C  
ATOM    115  C   MET A  20      21.076  -9.215   1.854  1.00 11.50           C  
ATOM    116  O   MET A  20      20.602  -9.362   2.987  1.00 11.22           O  
ATOM    117  CB  MET A  20      20.654  -7.148   0.560  1.00  9.49           C  
ATOM    118  CG  MET A  20      20.907  -5.651   0.426  1.00  6.51           C  
ATOM    119  SD  MET A  20      20.194  -4.712   1.775  1.00 10.19           S  
ATOM    120  CE  MET A  20      21.188  -5.274   3.127  1.00  5.86           C  
ATOM    121  N   GLY A  21      21.121 -10.168   0.921  1.00 12.02           N  
ATOM    122  CA  GLY A  21      20.590 -11.502   1.137  1.00 11.25           C  
ATOM    123  C   GLY A  21      21.288 -12.302   2.213  1.00 10.50           C  
ATOM    124  O   GLY A  21      20.640 -12.960   3.027  1.00 11.84           O  
ATOM    125  N   LEU A  22      22.611 -12.253   2.217  1.00 10.90           N  
ATOM    126  CA  LEU A  22      23.385 -12.982   3.205  1.00 12.22           C  
ATOM    127  C   LEU A  22      23.319 -12.240   4.535  1.00 12.36           C  
ATOM    128  O   LEU A  22      23.519 -12.820   5.595  1.00 12.68           O  
ATOM    129  CB  LEU A  22      24.832 -13.115   2.722  1.00 12.30           C  
ATOM    130  CG  LEU A  22      25.757 -13.985   3.565  1.00 12.32           C  
ATOM    131  CD1 LEU A  22      25.065 -15.286   3.905  1.00 10.86           C  
ATOM    132  CD2 LEU A  22      27.053 -14.232   2.815  1.00 10.84           C  
ATOM    133  N   GLY A  23      23.020 -10.947   4.459  1.00 14.14           N  
ATOM    134  CA  GLY A  23      22.920 -10.122   5.651  1.00 14.85           C  
ATOM    135  C   GLY A  23      21.727 -10.544   6.468  1.00 14.62           C  
ATOM    136  O   GLY A  23      21.749 -10.481   7.696  1.00 13.95           O  
ATOM    137  N   THR A  24      20.679 -10.971   5.772  1.00 15.54           N  
ATOM    138  CA  THR A  24      19.467 -11.442   6.429  1.00 17.76           C  
ATOM    139  C   THR A  24      19.772 -12.802   7.026  1.00 18.33           C  
ATOM    140  O   THR A  24      19.644 -13.020   8.241  1.00 19.34           O  
ATOM    141  CB  THR A  24      18.325 -11.644   5.439  1.00 16.71           C  
ATOM    142  OG1 THR A  24      18.396 -10.636   4.428  1.00 19.56           O  
ATOM    143  CG2 THR A  24      16.985 -11.571   6.157  1.00 17.16           C  
ATOM    144  N   LEU A  25      20.179 -13.718   6.152  1.00 17.92           N  
ATOM    145  CA  LEU A  25      20.498 -15.074   6.560  1.00 17.74           C  
ATOM    146  C   LEU A  25      21.413 -15.021   7.755  1.00 18.83           C  
ATOM    147  O   LEU A  25      21.682 -16.045   8.380  1.00 20.09           O  
ATOM    148  CB  LEU A  25      21.187 -15.829   5.421  1.00 16.51           C  
ATOM    149  CG  LEU A  25      20.308 -16.743   4.567  1.00 14.82           C  
ATOM    150  CD1 LEU A  25      21.147 -17.341   3.468  1.00 13.67           C  
ATOM    151  CD2 LEU A  25      19.680 -17.835   5.434  1.00 13.71           C  
ATOM    152  N   TYR A  26      21.891 -13.823   8.070  1.00 18.46           N  
ATOM    153  CA  TYR A  26      22.788 -13.652   9.193  1.00 19.19           C  
ATOM    154  C   TYR A  26      22.129 -13.148  10.470  1.00 18.51           C  
ATOM    155  O   TYR A  26      22.643 -13.420  11.559  1.00 21.19           O  
ATOM    156  CB  TYR A  26      23.938 -12.710   8.823  1.00 20.83           C  
ATOM    157  CG  TYR A  26      24.949 -12.498   9.935  1.00 21.15           C  
ATOM    158  CD1 TYR A  26      24.651 -11.684  11.037  1.00 19.46           C  
ATOM    159  CD2 TYR A  26      26.205 -13.116   9.886  1.00 22.30           C  
ATOM    160  CE1 TYR A  26      25.578 -11.494  12.057  1.00 21.48           C  
ATOM    161  CE2 TYR A  26      27.148 -12.933  10.902  1.00 21.39           C  
ATOM    162  CZ  TYR A  26      26.828 -12.125  11.986  1.00 22.09           C  
ATOM    163  OH  TYR A  26      27.747 -11.946  12.997  1.00 22.61           O  
ATOM    164  N   PHE A  27      21.017 -12.429  10.382  1.00 14.86           N  
ATOM    165  CA  PHE A  27      20.449 -11.941  11.622  1.00 12.86           C  
ATOM    166  C   PHE A  27      19.531 -12.925  12.312  1.00 13.05           C  
ATOM    167  O   PHE A  27      19.413 -12.868  13.533  1.00 14.16           O  
ATOM    168  CB  PHE A  27      19.752 -10.588  11.430  1.00 12.58           C  
ATOM    169  CG  PHE A  27      20.701  -9.456  11.080  1.00 11.75           C  
ATOM    170  CD1 PHE A  27      21.822  -9.194  11.857  1.00 12.96           C  
ATOM    171  CD2 PHE A  27      20.486  -8.664   9.954  1.00 11.87           C  
ATOM    172  CE1 PHE A  27      22.713  -8.165  11.507  1.00 10.89           C  
ATOM    173  CE2 PHE A  27      21.373  -7.635   9.605  1.00  9.59           C  
ATOM    174  CZ  PHE A  27      22.479  -7.390  10.382  1.00  9.33           C  
ATOM    175  N   LEU A  28      18.888 -13.834  11.575  1.00 11.94           N  
ATOM    176  CA  LEU A  28      18.000 -14.810  12.239  1.00 12.67           C  
ATOM    177  C   LEU A  28      18.858 -15.707  13.111  1.00 11.85           C  
ATOM    178  O   LEU A  28      18.656 -15.837  14.318  1.00  9.42           O  
ATOM    179  CB  LEU A  28      17.265 -15.702  11.230  1.00 13.06           C  
ATOM    180  CG  LEU A  28      16.855 -15.171   9.861  1.00 13.52           C  
ATOM    181  CD1 LEU A  28      16.612 -16.317   8.878  1.00 11.40           C  
ATOM    182  CD2 LEU A  28      15.599 -14.353  10.038  1.00 15.36           C  
ATOM    183  N   VAL A  29      19.812 -16.333  12.433  1.00 13.38           N  
ATOM    184  CA  VAL A  29      20.789 -17.237  13.007  1.00 13.24           C  
ATOM    185  C   VAL A  29      21.255 -16.686  14.346  1.00 14.81           C  
ATOM    186  O   VAL A  29      21.192 -17.360  15.372  1.00 15.54           O  
ATOM    187  CB  VAL A  29      21.989 -17.365  12.053  1.00  9.79           C  
ATOM    188  CG1 VAL A  29      23.271 -17.542  12.837  1.00  7.99           C  
ATOM    189  CG2 VAL A  29      21.751 -18.516  11.085  1.00  6.57           C  
ATOM    190  N   LYS A  30      21.717 -15.447  14.317  1.00 16.18           N  
ATOM    191  CA  LYS A  30      22.193 -14.779  15.508  1.00 19.33           C  
ATOM    192  C   LYS A  30      21.019 -14.269  16.345  1.00 21.66           C  
ATOM    193  O   LYS A  30      21.160 -14.040  17.548  1.00 22.36           O  
ATOM    194  CB  LYS A  30      23.091 -13.603  15.104  1.00 19.37           C  
ATOM    195  CG  LYS A  30      23.869 -12.951  16.243  1.00 21.20           C  
ATOM    196  CD  LYS A  30      23.637 -11.424  16.279  1.00 24.76           C  
ATOM    197  CE  LYS A  30      24.896 -10.571  15.875  1.00 23.48           C  
ATOM    198  NZ  LYS A  30      25.953 -11.294  15.098  1.00 22.62           N  
ATOM    199  N   GLY A  31      19.859 -14.116  15.707  1.00 22.65           N  
ATOM    200  CA  GLY A  31      18.687 -13.577  16.385  1.00 24.10           C  
ATOM    201  C   GLY A  31      17.980 -14.398  17.439  1.00 23.27           C  
ATOM    202  O   GLY A  31      17.441 -15.452  17.120  1.00 22.15           O  
ATOM    203  N   MET A  32      17.961 -13.891  18.681  1.00 23.38           N  
ATOM    204  CA  MET A  32      17.304 -14.550  19.832  1.00 25.21           C  
ATOM    205  C   MET A  32      17.087 -13.546  20.970  1.00 25.99           C  
ATOM    206  O   MET A  32      17.651 -12.453  20.940  1.00 25.03           O  
ATOM    207  CB  MET A  32      18.160 -15.712  20.361  1.00 27.45           C  
ATOM    208  CG  MET A  32      18.860 -16.559  19.291  1.00 27.71           C  
ATOM    209  SD  MET A  32      17.649 -17.526  18.359  1.00 27.97           S  
ATOM    210  CE  MET A  32      16.894 -18.495  19.692  1.00 28.39           C  
ATOM    211  N   GLY A  33      16.288 -13.919  21.971  1.00 27.65           N  
ATOM    212  CA  GLY A  33      16.020 -13.020  23.097  1.00 29.70           C  
ATOM    213  C   GLY A  33      16.294 -13.657  24.458  1.00 31.52           C  
ATOM    214  O   GLY A  33      15.644 -14.653  24.805  1.00 32.03           O  
ATOM    215  N   VAL A  34      17.215 -13.069  25.241  1.00 33.32           N  
ATOM    216  CA  VAL A  34      17.638 -13.635  26.549  1.00 34.83           C  
ATOM    217  C   VAL A  34      16.873 -13.352  27.877  1.00 34.65           C  
ATOM    218  O   VAL A  34      16.570 -14.296  28.623  1.00 34.54           O  
ATOM    219  CB  VAL A  34      19.197 -13.372  26.804  1.00 34.39           C  
ATOM    220  CG1 VAL A  34      19.968 -14.708  26.794  1.00 33.64           C  
ATOM    221  CG2 VAL A  34      19.786 -12.435  25.729  1.00 34.41           C  
ATOM    222  N   SER A  35      16.577 -12.093  28.201  1.00 33.48           N  
ATOM    223  CA  SER A  35      15.849 -11.814  29.451  1.00 33.22           C  
ATOM    224  C   SER A  35      14.732 -10.814  29.259  1.00 32.82           C  
ATOM    225  O   SER A  35      13.776 -10.777  30.034  1.00 32.43           O  
ATOM    226  CB  SER A  35      16.781 -11.266  30.542  1.00 33.52           C  
ATOM    227  OG  SER A  35      16.076 -10.376  31.410  1.00 30.80           O  
ATOM    228  N   ASP A  36      14.870  -9.988  28.234  1.00 32.52           N  
ATOM    229  CA  ASP A  36      13.872  -8.972  27.960  1.00 31.84           C  
ATOM    230  C   ASP A  36      13.469  -9.011  26.492  1.00 30.27           C  
ATOM    231  O   ASP A  36      14.281  -8.703  25.607  1.00 29.89           O  
ATOM    232  CB  ASP A  36      14.426  -7.578  28.300  1.00 32.46           C  
ATOM    233  CG  ASP A  36      14.855  -7.448  29.763  1.00 31.00           C  
ATOM    234  OD1 ASP A  36      13.996  -7.692  30.642  1.00 29.30           O  
ATOM    235  OD2 ASP A  36      16.038  -7.099  30.021  1.00 28.55           O  
ATOM    236  N   PRO A  37      12.212  -9.405  26.214  1.00 28.53           N  
ATOM    237  CA  PRO A  37      11.705  -9.471  24.839  1.00 26.20           C  
ATOM    238  C   PRO A  37      11.636  -8.048  24.297  1.00 25.33           C  
ATOM    239  O   PRO A  37      10.670  -7.652  23.641  1.00 24.51           O  
ATOM    240  CB  PRO A  37      10.328 -10.100  24.988  1.00 26.07           C  
ATOM    241  CG  PRO A  37       9.935  -9.798  26.391  1.00 26.52           C  
ATOM    242  CD  PRO A  37      11.197  -9.815  27.196  1.00 27.14           C  
ATOM    243  N   ASP A  38      12.684  -7.293  24.610  1.00 22.91           N  
ATOM    244  CA  ASP A  38      12.836  -5.919  24.189  1.00 20.67           C  
ATOM    245  C   ASP A  38      13.652  -5.960  22.919  1.00 18.74           C  
ATOM    246  O   ASP A  38      13.260  -5.399  21.894  1.00 18.10           O  
ATOM    247  CB  ASP A  38      13.583  -5.131  25.257  1.00 22.17           C  
ATOM    248  CG  ASP A  38      14.621  -4.194  24.671  1.00 23.29           C  
ATOM    249  OD1 ASP A  38      14.229  -3.082  24.245  1.00 22.10           O  
ATOM    250  OD2 ASP A  38      15.818  -4.572  24.635  1.00 24.22           O  
ATOM    251  N   ALA A  39      14.800  -6.621  22.995  1.00 17.41           N  
ATOM    252  CA  ALA A  39      15.654  -6.753  21.827  1.00 18.54           C  
ATOM    253  C   ALA A  39      14.847  -7.551  20.806  1.00 18.38           C  
ATOM    254  O   ALA A  39      15.102  -7.513  19.595  1.00 16.18           O  
ATOM    255  CB  ALA A  39      16.923  -7.495  22.186  1.00 17.58           C  
ATOM    256  N   LYS A  40      13.857  -8.266  21.331  1.00 18.99           N  
ATOM    257  CA  LYS A  40      12.987  -9.086  20.523  1.00 20.37           C  
ATOM    258  C   LYS A  40      12.315  -8.257  19.450  1.00 20.33           C  
ATOM    259  O   LYS A  40      12.330  -8.633  18.277  1.00 20.22           O  
ATOM    260  CB  LYS A  40      11.952  -9.748  21.411  1.00 22.59           C  
ATOM    261  CG  LYS A  40      12.436 -11.054  22.040  1.00 25.58           C  
ATOM    262  CD  LYS A  40      11.423 -12.195  21.802  1.00 27.38           C  
ATOM    263  CE  LYS A  40      11.182 -13.027  23.067  1.00 28.06           C  
ATOM    264  NZ  LYS A  40       9.965 -12.613  23.813  1.00 26.93           N  
ATOM    265  N   LYS A  41      11.728  -7.131  19.849  1.00 21.20           N  
ATOM    266  CA  LYS A  41      11.068  -6.228  18.897  1.00 23.07           C  
ATOM    267  C   LYS A  41      12.110  -5.813  17.863  1.00 23.42           C  
ATOM    268  O   LYS A  41      11.832  -5.696  16.661  1.00 21.86           O  
ATOM    269  CB  LYS A  41      10.562  -4.964  19.600  1.00 22.98           C  
ATOM    270  CG  LYS A  41       9.615  -5.226  20.763  1.00 26.31           C  
ATOM    271  CD  LYS A  41      10.133  -4.604  22.057  1.00 28.53           C  
ATOM    272  CE  LYS A  41       9.010  -4.380  23.075  1.00 29.08           C  
ATOM    273  NZ  LYS A  41       9.066  -3.005  23.691  1.00 29.32           N  
ATOM    274  N   PHE A  42      13.322  -5.598  18.368  1.00 22.84           N  
ATOM    275  CA  PHE A  42      14.447  -5.182  17.559  1.00 21.97           C  
ATOM    276  C   PHE A  42      14.914  -6.248  16.605  1.00 21.84           C  
ATOM    277  O   PHE A  42      14.753  -6.123  15.386  1.00 21.59           O  
ATOM    278  CB  PHE A  42      15.617  -4.816  18.452  1.00 21.55           C  
ATOM    279  CG  PHE A  42      15.515  -3.471  19.030  1.00 19.59           C  
ATOM    280  CD1 PHE A  42      15.145  -2.401  18.234  1.00 20.55           C  
ATOM    281  CD2 PHE A  42      15.770  -3.272  20.378  1.00 18.71           C  
ATOM    282  CE1 PHE A  42      15.026  -1.144  18.778  1.00 22.91           C  
ATOM    283  CE2 PHE A  42      15.660  -2.032  20.942  1.00 19.48           C  
ATOM    284  CZ  PHE A  42      15.287  -0.955  20.153  1.00 23.00           C  
ATOM    285  N   TYR A  43      15.521  -7.286  17.176  1.00 20.17           N  
ATOM    286  CA  TYR A  43      16.065  -8.368  16.393  1.00 19.50           C  
ATOM    287  C   TYR A  43      15.181  -8.654  15.203  1.00 18.80           C  
ATOM    288  O   TYR A  43      15.640  -9.166  14.184  1.00 18.26           O  
ATOM    289  CB  TYR A  43      16.215  -9.601  17.260  1.00 21.15           C  
ATOM    290  CG  TYR A  43      17.590  -9.732  17.887  1.00 24.18           C  
ATOM    291  CD1 TYR A  43      18.737  -9.872  17.098  1.00 24.25           C  
ATOM    292  CD2 TYR A  43      17.745  -9.727  19.277  1.00 26.02           C  
ATOM    293  CE1 TYR A  43      20.006 -10.008  17.687  1.00 26.89           C  
ATOM    294  CE2 TYR A  43      19.000  -9.862  19.870  1.00 25.97           C  
ATOM    295  CZ  TYR A  43      20.122 -10.005  19.078  1.00 26.93           C  
ATOM    296  OH  TYR A  43      21.347 -10.181  19.679  1.00 26.92           O  
ATOM    297  N   ALA A  44      13.903  -8.305  15.334  1.00 19.70           N  
ATOM    298  CA  ALA A  44      12.943  -8.520  14.255  1.00 20.16           C  
ATOM    299  C   ALA A  44      13.124  -7.482  13.149  1.00 19.37           C  
ATOM    300  O   ALA A  44      13.652  -7.785  12.070  1.00 18.65           O  
ATOM    301  CB  ALA A  44      11.516  -8.472  14.800  1.00 17.31           C  
ATOM    302  N   ILE A  45      12.684  -6.262  13.436  1.00 18.25           N  
ATOM    303  CA  ILE A  45      12.768  -5.157  12.498  1.00 18.38           C  
ATOM    304  C   ILE A  45      13.962  -5.311  11.560  1.00 18.80           C  
ATOM    305  O   ILE A  45      13.826  -5.511  10.351  1.00 17.49           O  
ATOM    306  CB  ILE A  45      12.856  -3.799  13.290  1.00 19.07           C  
ATOM    307  CG1 ILE A  45      11.606  -2.948  13.007  1.00 17.92           C  
ATOM    308  CG2 ILE A  45      14.154  -3.019  12.939  1.00 17.41           C  
ATOM    309  CD1 ILE A  45      10.601  -2.931  14.135  1.00 17.93           C  
ATOM    310  N   THR A  46      15.136  -5.250  12.165  1.00 21.41           N  
ATOM    311  CA  THR A  46      16.398  -5.321  11.467  1.00 21.61           C  
ATOM    312  C   THR A  46      16.630  -6.481  10.528  1.00 20.54           C  
ATOM    313  O   THR A  46      17.521  -6.406   9.682  1.00 21.52           O  
ATOM    314  CB  THR A  46      17.515  -5.274  12.457  1.00 22.65           C  
ATOM    315  OG1 THR A  46      17.245  -4.236  13.412  1.00 24.92           O  
ATOM    316  CG2 THR A  46      18.798  -4.974  11.742  1.00 26.49           C  
ATOM    317  N   THR A  47      15.866  -7.558  10.675  1.00 18.71           N  
ATOM    318  CA  THR A  47      16.018  -8.683   9.758  1.00 16.50           C  
ATOM    319  C   THR A  47      15.203  -8.313   8.529  1.00 18.20           C  
ATOM    320  O   THR A  47      15.610  -8.542   7.391  1.00 18.84           O  
ATOM    321  CB  THR A  47      15.398  -9.953  10.281  1.00 13.65           C  
ATOM    322  OG1 THR A  47      15.804 -10.181  11.634  1.00 14.90           O  
ATOM    323  CG2 THR A  47      15.810 -11.098   9.399  1.00 12.62           C  
ATOM    324  N   LEU A  48      14.031  -7.744   8.793  1.00 17.01           N  
ATOM    325  CA  LEU A  48      13.110  -7.329   7.757  1.00 15.81           C  
ATOM    326  C   LEU A  48      13.797  -6.399   6.760  1.00 14.59           C  
ATOM    327  O   LEU A  48      13.709  -6.600   5.545  1.00 14.27           O  
ATOM    328  CB  LEU A  48      11.929  -6.582   8.390  1.00 17.54           C  
ATOM    329  CG  LEU A  48      10.526  -7.176   8.554  1.00 15.62           C  
ATOM    330  CD1 LEU A  48       9.715  -6.240   9.445  1.00 16.83           C  
ATOM    331  CD2 LEU A  48       9.845  -7.323   7.221  1.00 15.13           C  
ATOM    332  N   VAL A  49      14.464  -5.373   7.285  1.00 10.94           N  
ATOM    333  CA  VAL A  49      15.141  -4.364   6.467  1.00  8.25           C  
ATOM    334  C   VAL A  49      16.004  -4.914   5.322  1.00  7.88           C  
ATOM    335  O   VAL A  49      15.819  -4.528   4.170  1.00  7.55           O  
ATOM    336  CB  VAL A  49      15.980  -3.428   7.359  1.00  6.68           C  
ATOM    337  CG1 VAL A  49      16.740  -2.429   6.515  1.00  5.63           C  
ATOM    338  CG2 VAL A  49      15.078  -2.730   8.334  1.00  2.70           C  
ATOM    339  N   PRO A  50      16.979  -5.789   5.623  1.00  6.39           N  
ATOM    340  CA  PRO A  50      17.797  -6.328   4.543  1.00  6.80           C  
ATOM    341  C   PRO A  50      17.034  -7.369   3.703  1.00  9.39           C  
ATOM    342  O   PRO A  50      17.259  -7.483   2.499  1.00 11.28           O  
ATOM    343  CB  PRO A  50      18.988  -6.935   5.275  1.00  6.51           C  
ATOM    344  CG  PRO A  50      18.881  -6.446   6.699  1.00  3.35           C  
ATOM    345  CD  PRO A  50      17.440  -6.284   6.924  1.00  4.41           C  
ATOM    346  N   ALA A  51      16.131  -8.122   4.335  1.00 11.01           N  
ATOM    347  CA  ALA A  51      15.327  -9.159   3.652  1.00 12.09           C  
ATOM    348  C   ALA A  51      14.422  -8.576   2.563  1.00 13.73           C  
ATOM    349  O   ALA A  51      14.430  -9.048   1.420  1.00 13.83           O  
ATOM    350  CB  ALA A  51      14.475  -9.914   4.672  1.00 12.11           C  
ATOM    351  N   ILE A  52      13.629  -7.570   2.937  1.00 11.73           N  
ATOM    352  CA  ILE A  52      12.734  -6.895   2.006  1.00  9.28           C  
ATOM    353  C   ILE A  52      13.584  -6.413   0.839  1.00 10.86           C  
ATOM    354  O   ILE A  52      13.295  -6.690  -0.322  1.00 10.08           O  
ATOM    355  CB  ILE A  52      12.075  -5.675   2.670  1.00  8.22           C  
ATOM    356  CG1 ILE A  52      10.702  -6.057   3.198  1.00  8.05           C  
ATOM    357  CG2 ILE A  52      11.947  -4.518   1.679  1.00  7.22           C  
ATOM    358  CD1 ILE A  52      10.731  -7.252   4.059  1.00  7.56           C  
ATOM    359  N   ALA A  53      14.642  -5.685   1.165  1.00 12.72           N  
ATOM    360  CA  ALA A  53      15.551  -5.160   0.158  1.00 14.73           C  
ATOM    361  C   ALA A  53      15.962  -6.246  -0.823  1.00 13.81           C  
ATOM    362  O   ALA A  53      15.895  -6.035  -2.035  1.00 13.66           O  
ATOM    363  CB  ALA A  53      16.807  -4.564   0.834  1.00 13.71           C  
ATOM    364  N   PHE A  54      16.382  -7.398  -0.276  1.00 12.29           N  
ATOM    365  CA  PHE A  54      16.855  -8.555  -1.047  1.00 10.12           C  
ATOM    366  C   PHE A  54      15.954  -8.912  -2.226  1.00  7.26           C  
ATOM    367  O   PHE A  54      16.451  -9.155  -3.326  1.00  6.99           O  
ATOM    368  CB  PHE A  54      17.048  -9.767  -0.117  1.00 13.23           C  
ATOM    369  CG  PHE A  54      17.283 -11.098  -0.848  1.00 15.93           C  
ATOM    370  CD1 PHE A  54      18.398 -11.285  -1.671  1.00 14.28           C  
ATOM    371  CD2 PHE A  54      16.374 -12.152  -0.717  1.00 12.76           C  
ATOM    372  CE1 PHE A  54      18.590 -12.488  -2.348  1.00 14.89           C  
ATOM    373  CE2 PHE A  54      16.564 -13.344  -1.386  1.00 12.88           C  
ATOM    374  CZ  PHE A  54      17.668 -13.516  -2.204  1.00 15.73           C  
ATOM    375  N   THR A  55      14.641  -8.930  -2.024  1.00  3.82           N  
ATOM    376  CA  THR A  55      13.744  -9.242  -3.131  1.00  2.35           C  
ATOM    377  C   THR A  55      13.835  -8.158  -4.189  1.00  2.27           C  
ATOM    378  O   THR A  55      13.673  -8.414  -5.380  1.00  2.00           O  
ATOM    379  CB  THR A  55      12.288  -9.352  -2.673  1.00  2.00           C  
ATOM    380  OG1 THR A  55      11.653  -8.081  -2.795  1.00  2.00           O  
ATOM    381  CG2 THR A  55      12.221  -9.817  -1.237  1.00  2.42           C  
ATOM    382  N   MET A  56      14.121  -6.944  -3.739  1.00  3.39           N  
ATOM    383  CA  MET A  56      14.237  -5.784  -4.613  1.00  2.96           C  
ATOM    384  C   MET A  56      15.505  -5.759  -5.456  1.00  3.42           C  
ATOM    385  O   MET A  56      15.450  -5.513  -6.653  1.00  2.52           O  
ATOM    386  CB  MET A  56      14.136  -4.535  -3.765  1.00  2.15           C  
ATOM    387  CG  MET A  56      12.784  -4.396  -3.086  1.00  4.72           C  
ATOM    388  SD  MET A  56      11.436  -4.596  -4.242  1.00  2.00           S  
ATOM    389  CE  MET A  56      11.929  -3.498  -5.517  1.00  2.03           C  
ATOM    390  N   TYR A  57      16.654  -6.003  -4.842  1.00  5.99           N  
ATOM    391  CA  TYR A  57      17.897  -6.045  -5.600  1.00  8.29           C  
ATOM    392  C   TYR A  57      17.767  -7.200  -6.598  1.00 10.53           C  
ATOM    393  O   TYR A  57      18.248  -7.127  -7.729  1.00 10.68           O  
ATOM    394  CB  TYR A  57      19.060  -6.309  -4.667  1.00 10.40           C  
ATOM    395  CG  TYR A  57      19.675  -5.059  -4.120  1.00 11.90           C  
ATOM    396  CD1 TYR A  57      19.957  -3.983  -4.957  1.00 13.30           C  
ATOM    397  CD2 TYR A  57      19.977  -4.947  -2.764  1.00 11.55           C  
ATOM    398  CE1 TYR A  57      20.529  -2.812  -4.460  1.00 11.76           C  
ATOM    399  CE2 TYR A  57      20.544  -3.791  -2.252  1.00 11.90           C  
ATOM    400  CZ  TYR A  57      20.820  -2.722  -3.107  1.00 13.06           C  
ATOM    401  OH  TYR A  57      21.401  -1.573  -2.615  1.00 12.71           O  
ATOM    402  N   LEU A  58      17.111  -8.272  -6.163  1.00  8.95           N  
ATOM    403  CA  LEU A  58      16.877  -9.425  -7.015  1.00  7.57           C  
ATOM    404  C   LEU A  58      15.886  -9.021  -8.097  1.00  8.75           C  
ATOM    405  O   LEU A  58      16.028  -9.455  -9.240  1.00  9.05           O  
ATOM    406  CB  LEU A  58      16.309 -10.577  -6.188  1.00  7.43           C  
ATOM    407  CG  LEU A  58      15.931 -11.945  -6.775  1.00  4.83           C  
ATOM    408  CD1 LEU A  58      16.699 -12.227  -8.036  1.00  2.00           C  
ATOM    409  CD2 LEU A  58      16.184 -13.024  -5.712  1.00  3.94           C  
ATOM    410  N   SER A  59      14.896  -8.185  -7.739  1.00  6.94           N  
ATOM    411  CA  SER A  59      13.867  -7.697  -8.677  1.00  5.02           C  
ATOM    412  C   SER A  59      14.406  -6.740  -9.737  1.00  6.90           C  
ATOM    413  O   SER A  59      13.847  -6.654 -10.836  1.00  6.14           O  
ATOM    414  CB  SER A  59      12.730  -7.002  -7.934  1.00  3.69           C  
ATOM    415  OG  SER A  59      11.774  -6.499  -8.849  1.00  2.00           O  
ATOM    416  N   MET A  60      15.475  -6.010  -9.402  1.00  6.20           N  
ATOM    417  CA  MET A  60      16.130  -5.082 -10.340  1.00  5.71           C  
ATOM    418  C   MET A  60      17.002  -5.987 -11.170  1.00  8.61           C  
ATOM    419  O   MET A  60      16.946  -6.015 -12.400  1.00  8.16           O  
ATOM    420  CB  MET A  60      17.062  -4.130  -9.610  1.00  2.00           C  
ATOM    421  CG  MET A  60      16.575  -2.744  -9.406  1.00  2.00           C  
ATOM    422  SD  MET A  60      17.458  -2.099  -8.013  1.00  2.00           S  
ATOM    423  CE  MET A  60      16.335  -2.466  -6.750  1.00  2.00           C  
ATOM    424  N   LEU A  61      17.813  -6.733 -10.431  1.00  9.88           N  
ATOM    425  CA  LEU A  61      18.759  -7.693 -10.958  1.00 10.65           C  
ATOM    426  C   LEU A  61      18.228  -8.559 -12.101  1.00 10.83           C  
ATOM    427  O   LEU A  61      18.964  -8.869 -13.043  1.00 12.27           O  
ATOM    428  CB  LEU A  61      19.239  -8.604  -9.820  1.00  9.69           C  
ATOM    429  CG  LEU A  61      20.063  -9.833 -10.223  1.00  8.92           C  
ATOM    430  CD1 LEU A  61      21.249  -9.382 -11.022  1.00  8.28           C  
ATOM    431  CD2 LEU A  61      20.502 -10.593  -8.981  1.00  8.16           C  
ATOM    432  N   LEU A  62      16.966  -8.965 -12.025  1.00  8.78           N  
ATOM    433  CA  LEU A  62      16.431  -9.820 -13.068  1.00  8.66           C  
ATOM    434  C   LEU A  62      15.903  -9.117 -14.301  1.00  7.84           C  
ATOM    435  O   LEU A  62      15.589  -9.765 -15.287  1.00  7.70           O  
ATOM    436  CB  LEU A  62      15.365 -10.731 -12.484  1.00  5.56           C  
ATOM    437  CG  LEU A  62      16.035 -12.044 -12.124  1.00  3.92           C  
ATOM    438  CD1 LEU A  62      15.282 -12.778 -11.043  1.00  2.00           C  
ATOM    439  CD2 LEU A  62      16.139 -12.842 -13.389  1.00  2.00           C  
ATOM    440  N   GLY A  63      15.816  -7.792 -14.252  1.00 10.38           N  
ATOM    441  CA  GLY A  63      15.319  -7.040 -15.394  1.00 11.71           C  
ATOM    442  C   GLY A  63      13.812  -6.834 -15.387  1.00 10.77           C  
ATOM    443  O   GLY A  63      13.196  -6.596 -16.431  1.00  8.88           O  
ATOM    444  N   TYR A  64      13.216  -6.919 -14.207  1.00  9.90           N  
ATOM    445  CA  TYR A  64      11.784  -6.750 -14.097  1.00 11.61           C  
ATOM    446  C   TYR A  64      11.416  -5.349 -13.628  1.00 13.44           C  
ATOM    447  O   TYR A  64      10.297  -4.881 -13.867  1.00 14.44           O  
ATOM    448  CB  TYR A  64      11.207  -7.799 -13.136  1.00 12.14           C  
ATOM    449  CG  TYR A  64       9.751  -7.594 -12.763  1.00 10.16           C  
ATOM    450  CD1 TYR A  64       8.726  -7.794 -13.690  1.00  8.75           C  
ATOM    451  CD2 TYR A  64       9.402  -7.196 -11.478  1.00  9.95           C  
ATOM    452  CE1 TYR A  64       7.394  -7.600 -13.335  1.00  7.72           C  
ATOM    453  CE2 TYR A  64       8.074  -7.002 -11.119  1.00  8.35           C  
ATOM    454  CZ  TYR A  64       7.081  -7.203 -12.044  1.00  6.71           C  
ATOM    455  OH  TYR A  64       5.781  -7.011 -11.651  1.00  6.99           O  
ATOM    456  N   GLY A  65      12.354  -4.675 -12.967  1.00 12.09           N  
ATOM    457  CA  GLY A  65      12.073  -3.346 -12.468  1.00  9.06           C  
ATOM    458  C   GLY A  65      12.728  -2.282 -13.300  1.00  8.07           C  
ATOM    459  O   GLY A  65      13.301  -1.350 -12.746  1.00  9.98           O  
ATOM    460  N   LEU A  66      12.651  -2.400 -14.622  1.00  6.40           N  
ATOM    461  CA  LEU A  66      13.259  -1.394 -15.496  1.00  7.76           C  
ATOM    462  C   LEU A  66      12.356  -0.838 -16.616  1.00  9.48           C  
ATOM    463  O   LEU A  66      12.200  -1.464 -17.661  1.00  9.09           O  
ATOM    464  CB  LEU A  66      14.537  -1.953 -16.114  1.00  5.21           C  
ATOM    465  CG  LEU A  66      15.221  -0.960 -17.037  1.00  2.42           C  
ATOM    466  CD1 LEU A  66      16.617  -0.781 -16.535  1.00  2.00           C  
ATOM    467  CD2 LEU A  66      15.181  -1.427 -18.484  1.00  2.00           C  
ATOM    468  N   THR A  67      11.790   0.347 -16.396  1.00 11.06           N  
ATOM    469  CA  THR A  67      10.905   1.001 -17.372  1.00 13.60           C  
ATOM    470  C   THR A  67      11.694   1.847 -18.370  1.00 15.58           C  
ATOM    471  O   THR A  67      12.913   1.961 -18.262  1.00 17.07           O  
ATOM    472  CB  THR A  67       9.879   1.948 -16.664  1.00 14.07           C  
ATOM    473  OG1 THR A  67      10.048   3.291 -17.139  1.00 11.59           O  
ATOM    474  CG2 THR A  67      10.075   1.935 -15.155  1.00 12.42           C  
ATOM    475  N   MET A  68      11.003   2.460 -19.327  1.00 17.47           N  
ATOM    476  CA  MET A  68      11.673   3.316 -20.302  1.00 18.49           C  
ATOM    477  C   MET A  68      10.923   4.616 -20.528  1.00 18.10           C  
ATOM    478  O   MET A  68      10.373   4.844 -21.609  1.00 19.10           O  
ATOM    479  CB  MET A  68      11.822   2.596 -21.620  1.00 22.64           C  
ATOM    480  CG  MET A  68      12.592   1.306 -21.492  1.00 29.27           C  
ATOM    481  SD  MET A  68      14.323   1.611 -21.087  1.00 35.19           S  
ATOM    482  CE  MET A  68      15.191   0.889 -22.558  1.00 35.58           C  
ATOM    483  N   VAL A  69      10.912   5.468 -19.503  1.00 15.83           N  
ATOM    484  CA  VAL A  69      10.239   6.763 -19.559  1.00 11.16           C  
ATOM    485  C   VAL A  69      10.987   7.758 -20.444  1.00 11.77           C  
ATOM    486  O   VAL A  69      12.222   7.736 -20.499  1.00 11.78           O  
ATOM    487  CB  VAL A  69      10.109   7.365 -18.163  1.00  8.95           C  
ATOM    488  CG1 VAL A  69       8.772   7.022 -17.596  1.00  9.89           C  
ATOM    489  CG2 VAL A  69      11.187   6.834 -17.262  1.00  7.40           C  
ATOM    490  N   PRO A  70      10.245   8.600 -21.198  1.00 11.01           N  
ATOM    491  CA  PRO A  70      10.759   9.634 -22.103  1.00 12.49           C  
ATOM    492  C   PRO A  70      10.816  11.092 -21.583  1.00 11.68           C  
ATOM    493  O   PRO A  70       9.798  11.667 -21.213  1.00 12.62           O  
ATOM    494  CB  PRO A  70       9.843   9.506 -23.332  1.00  9.25           C  
ATOM    495  CG  PRO A  70       8.604   8.745 -22.842  1.00 10.06           C  
ATOM    496  CD  PRO A  70       8.791   8.483 -21.357  1.00 11.40           C  
ATOM    497  N   PHE A  71      12.015  11.672 -21.560  1.00 13.17           N  
ATOM    498  CA  PHE A  71      12.204  13.063 -21.148  1.00 15.95           C  
ATOM    499  C   PHE A  71      12.467  13.898 -22.411  1.00 19.28           C  
ATOM    500  O   PHE A  71      13.630  14.190 -22.749  1.00 18.12           O  
ATOM    501  CB  PHE A  71      13.425  13.245 -20.248  1.00 16.87           C  
ATOM    502  CG  PHE A  71      13.364  12.502 -18.959  1.00 15.58           C  
ATOM    503  CD1 PHE A  71      12.195  12.422 -18.237  1.00 13.54           C  
ATOM    504  CD2 PHE A  71      14.505  11.875 -18.462  1.00 16.56           C  
ATOM    505  CE1 PHE A  71      12.164  11.721 -17.045  1.00 13.57           C  
ATOM    506  CE2 PHE A  71      14.467  11.172 -17.265  1.00 15.74           C  
ATOM    507  CZ  PHE A  71      13.304  11.098 -16.565  1.00 12.38           C  
ATOM    508  N   GLY A  72      11.388  14.273 -23.102  1.00 22.70           N  
ATOM    509  CA  GLY A  72      11.494  15.074 -24.322  1.00 23.75           C  
ATOM    510  C   GLY A  72      12.884  15.204 -24.938  1.00 22.40           C  
ATOM    511  O   GLY A  72      13.448  16.298 -24.969  1.00 22.32           O  
ATOM    512  N   GLY A  73      13.438  14.101 -25.425  1.00 21.96           N  
ATOM    513  CA  GLY A  73      14.748  14.173 -26.034  1.00 21.77           C  
ATOM    514  C   GLY A  73      15.489  12.860 -26.030  1.00 21.93           C  
ATOM    515  O   GLY A  73      16.548  12.725 -26.651  1.00 22.46           O  
ATOM    516  N   GLU A  74      14.927  11.892 -25.316  1.00 21.55           N  
ATOM    517  CA  GLU A  74      15.519  10.565 -25.205  1.00 20.24           C  
ATOM    518  C   GLU A  74      14.446   9.613 -24.687  1.00 20.54           C  
ATOM    519  O   GLU A  74      13.258   9.938 -24.699  1.00 21.09           O  
ATOM    520  CB  GLU A  74      16.718  10.585 -24.233  1.00 19.39           C  
ATOM    521  CG  GLU A  74      16.834  11.871 -23.373  1.00 18.86           C  
ATOM    522  CD  GLU A  74      18.148  12.637 -23.590  1.00 17.96           C  
ATOM    523  OE1 GLU A  74      19.139  12.317 -22.892  1.00 15.13           O  
ATOM    524  OE2 GLU A  74      18.183  13.551 -24.452  1.00 14.89           O  
ATOM    525  N   GLN A  75      14.882   8.439 -24.242  1.00 20.11           N  
ATOM    526  CA  GLN A  75      14.012   7.405 -23.691  1.00 18.50           C  
ATOM    527  C   GLN A  75      14.930   6.728 -22.689  1.00 17.79           C  
ATOM    528  O   GLN A  75      15.680   5.825 -23.067  1.00 17.68           O  
ATOM    529  CB  GLN A  75      13.646   6.402 -24.778  1.00 22.35           C  
ATOM    530  CG  GLN A  75      12.517   6.805 -25.695  1.00 22.81           C  
ATOM    531  CD  GLN A  75      11.621   5.629 -26.036  1.00 23.98           C  
ATOM    532  OE1 GLN A  75      11.854   4.508 -25.581  1.00 25.46           O  
ATOM    533  NE2 GLN A  75      10.589   5.878 -26.837  1.00 25.49           N  
ATOM    534  N   ASN A  76      14.906   7.144 -21.425  1.00 16.69           N  
ATOM    535  CA  ASN A  76      15.835   6.533 -20.469  1.00 14.62           C  
ATOM    536  C   ASN A  76      15.253   5.590 -19.448  1.00 10.92           C  
ATOM    537  O   ASN A  76      14.044   5.567 -19.214  1.00 11.51           O  
ATOM    538  CB  ASN A  76      16.672   7.597 -19.754  1.00 16.52           C  
ATOM    539  CG  ASN A  76      15.831   8.677 -19.106  1.00 19.73           C  
ATOM    540  OD1 ASN A  76      14.834   9.130 -19.671  1.00 19.17           O  
ATOM    541  ND2 ASN A  76      16.239   9.107 -17.913  1.00 20.66           N  
ATOM    542  N   PRO A  77      16.123   4.788 -18.826  1.00  7.47           N  
ATOM    543  CA  PRO A  77      15.810   3.783 -17.810  1.00  6.33           C  
ATOM    544  C   PRO A  77      15.595   4.319 -16.418  1.00  4.89           C  
ATOM    545  O   PRO A  77      16.325   5.173 -15.952  1.00  5.60           O  
ATOM    546  CB  PRO A  77      17.011   2.856 -17.863  1.00  7.81           C  
ATOM    547  CG  PRO A  77      18.141   3.777 -18.224  1.00  5.14           C  
ATOM    548  CD  PRO A  77      17.564   4.833 -19.123  1.00  4.16           C  
ATOM    549  N   ILE A  78      14.597   3.787 -15.740  1.00  5.23           N  
ATOM    550  CA  ILE A  78      14.304   4.225 -14.390  1.00  7.28           C  
ATOM    551  C   ILE A  78      13.860   3.027 -13.549  1.00  8.51           C  
ATOM    552  O   ILE A  78      12.697   2.624 -13.567  1.00  9.13           O  
ATOM    553  CB  ILE A  78      13.209   5.310 -14.404  1.00  6.53           C  
ATOM    554  CG1 ILE A  78      13.750   6.573 -15.060  1.00  6.00           C  
ATOM    555  CG2 ILE A  78      12.763   5.640 -12.994  1.00  7.63           C  
ATOM    556  CD1 ILE A  78      14.655   7.359 -14.167  1.00  8.04           C  
ATOM    557  N   TYR A  79      14.801   2.456 -12.813  1.00  9.76           N  
ATOM    558  CA  TYR A  79      14.492   1.300 -11.999  1.00 10.96           C  
ATOM    559  C   TYR A  79      13.452   1.637 -10.941  1.00  9.95           C  
ATOM    560  O   TYR A  79      13.774   1.878  -9.777  1.00  8.50           O  
ATOM    561  CB  TYR A  79      15.766   0.759 -11.335  1.00 15.82           C  
ATOM    562  CG  TYR A  79      16.826   0.183 -12.279  1.00 16.04           C  
ATOM    563  CD1 TYR A  79      17.636   1.024 -13.057  1.00 15.47           C  
ATOM    564  CD2 TYR A  79      17.076  -1.188 -12.322  1.00 14.84           C  
ATOM    565  CE1 TYR A  79      18.659   0.519 -13.838  1.00 14.96           C  
ATOM    566  CE2 TYR A  79      18.102  -1.700 -13.105  1.00 17.20           C  
ATOM    567  CZ  TYR A  79      18.891  -0.839 -13.854  1.00 16.94           C  
ATOM    568  OH  TYR A  79      19.928  -1.342 -14.601  1.00 17.99           O  
ATOM    569  N   TRP A  80      12.195   1.636 -11.361  1.00 11.21           N  
ATOM    570  CA  TRP A  80      11.092   1.937 -10.465  1.00 12.68           C  
ATOM    571  C   TRP A  80      11.117   1.072  -9.200  1.00 13.07           C  
ATOM    572  O   TRP A  80      10.626   1.490  -8.154  1.00 13.98           O  
ATOM    573  CB  TRP A  80       9.743   1.769 -11.197  1.00 10.91           C  
ATOM    574  CG  TRP A  80       9.424   0.367 -11.647  1.00 12.40           C  
ATOM    575  CD1 TRP A  80       9.457  -0.111 -12.924  1.00 12.72           C  
ATOM    576  CD2 TRP A  80       9.017  -0.732 -10.820  1.00 12.93           C  
ATOM    577  NE1 TRP A  80       9.103  -1.441 -12.948  1.00 13.60           N  
ATOM    578  CE2 TRP A  80       8.827  -1.847 -11.671  1.00 13.15           C  
ATOM    579  CE3 TRP A  80       8.800  -0.888  -9.446  1.00 13.22           C  
ATOM    580  CZ2 TRP A  80       8.428  -3.102 -11.185  1.00 13.63           C  
ATOM    581  CZ3 TRP A  80       8.399  -2.139  -8.964  1.00 12.83           C  
ATOM    582  CH2 TRP A  80       8.220  -3.226  -9.833  1.00 11.39           C  
ATOM    583  N   ALA A  81      11.688  -0.127  -9.295  1.00 11.01           N  
ATOM    584  CA  ALA A  81      11.759  -1.040  -8.153  1.00  9.05           C  
ATOM    585  C   ALA A  81      12.755  -0.559  -7.098  1.00  6.88           C  
ATOM    586  O   ALA A  81      13.153  -1.314  -6.219  1.00  4.50           O  
ATOM    587  CB  ALA A  81      12.140  -2.448  -8.640  1.00  8.89           C  
ATOM    588  N   ARG A  82      13.148   0.704  -7.199  1.00  5.44           N  
ATOM    589  CA  ARG A  82      14.103   1.288  -6.275  1.00  6.30           C  
ATOM    590  C   ARG A  82      13.393   1.920  -5.087  1.00  5.81           C  
ATOM    591  O   ARG A  82      13.767   1.721  -3.933  1.00  3.14           O  
ATOM    592  CB  ARG A  82      14.930   2.350  -7.009  1.00  9.22           C  
ATOM    593  CG  ARG A  82      16.435   2.359  -6.700  1.00  9.83           C  
ATOM    594  CD  ARG A  82      17.243   2.705  -7.946  1.00 10.89           C  
ATOM    595  NE  ARG A  82      18.444   1.889  -8.084  1.00 11.99           N  
ATOM    596  CZ  ARG A  82      19.222   1.886  -9.162  1.00 13.39           C  
ATOM    597  NH1 ARG A  82      18.930   2.661 -10.199  1.00 15.24           N  
ATOM    598  NH2 ARG A  82      20.291   1.107  -9.212  1.00 12.74           N  
ATOM    599  N   TYR A  83      12.360   2.693  -5.397  1.00  6.72           N  
ATOM    600  CA  TYR A  83      11.565   3.399  -4.410  1.00  5.79           C  
ATOM    601  C   TYR A  83      10.719   2.415  -3.651  1.00  6.82           C  
ATOM    602  O   TYR A  83      10.292   2.688  -2.536  1.00  7.49           O  
ATOM    603  CB  TYR A  83      10.705   4.436  -5.120  1.00  6.42           C  
ATOM    604  CG  TYR A  83      11.458   5.105  -6.266  1.00  9.00           C  
ATOM    605  CD1 TYR A  83      11.701   4.421  -7.454  1.00  8.37           C  
ATOM    606  CD2 TYR A  83      12.011   6.387  -6.122  1.00 10.23           C  
ATOM    607  CE1 TYR A  83      12.479   4.973  -8.454  1.00  9.21           C  
ATOM    608  CE2 TYR A  83      12.795   6.955  -7.120  1.00  8.55           C  
ATOM    609  CZ  TYR A  83      13.030   6.237  -8.286  1.00 10.63           C  
ATOM    610  OH  TYR A  83      13.851   6.748  -9.274  1.00  9.73           O  
ATOM    611  N   ALA A  84      10.500   1.249  -4.249  1.00  8.15           N  
ATOM    612  CA  ALA A  84       9.710   0.198  -3.610  1.00  9.70           C  
ATOM    613  C   ALA A  84      10.423  -0.360  -2.358  1.00 10.76           C  
ATOM    614  O   ALA A  84       9.840  -0.408  -1.272  1.00 10.60           O  
ATOM    615  CB  ALA A  84       9.419  -0.922  -4.614  1.00  8.11           C  
ATOM    616  N   ASP A  85      11.677  -0.773  -2.517  1.00 10.88           N  
ATOM    617  CA  ASP A  85      12.477  -1.293  -1.414  1.00 11.40           C  
ATOM    618  C   ASP A  85      12.661  -0.197  -0.356  1.00 11.91           C  
ATOM    619  O   ASP A  85      12.582  -0.463   0.846  1.00 11.39           O  
ATOM    620  CB  ASP A  85      13.834  -1.769  -1.977  1.00 13.37           C  
ATOM    621  CG  ASP A  85      15.042  -1.457  -1.068  1.00 14.20           C  
ATOM    622  OD1 ASP A  85      14.941  -1.612   0.170  1.00 12.88           O  
ATOM    623  OD2 ASP A  85      16.107  -1.080  -1.620  1.00 11.59           O  
ATOM    624  N   TRP A  86      12.896   1.033  -0.816  1.00 11.61           N  
ATOM    625  CA  TRP A  86      13.086   2.187   0.063  1.00 11.96           C  
ATOM    626  C   TRP A  86      11.765   2.597   0.711  1.00 10.90           C  
ATOM    627  O   TRP A  86      11.734   3.393   1.650  1.00 10.57           O  
ATOM    628  CB  TRP A  86      13.592   3.383  -0.725  1.00 12.58           C  
ATOM    629  CG  TRP A  86      14.957   3.283  -1.279  1.00 13.87           C  
ATOM    630  CD1 TRP A  86      15.962   2.449  -0.886  1.00 13.76           C  
ATOM    631  CD2 TRP A  86      15.497   4.102  -2.302  1.00 13.88           C  
ATOM    632  NE1 TRP A  86      17.105   2.704  -1.605  1.00 11.87           N  
ATOM    633  CE2 TRP A  86      16.838   3.722  -2.485  1.00 15.93           C  
ATOM    634  CE3 TRP A  86      14.976   5.129  -3.088  1.00 13.53           C  
ATOM    635  CZ2 TRP A  86      17.661   4.337  -3.426  1.00 17.95           C  
ATOM    636  CZ3 TRP A  86      15.790   5.733  -4.014  1.00 14.18           C  
ATOM    637  CH2 TRP A  86      17.115   5.341  -4.179  1.00 13.41           C  
ATOM    638  N   LEU A  87      10.672   2.061   0.201  1.00  9.38           N  
ATOM    639  CA  LEU A  87       9.389   2.401   0.748  1.00 10.17           C  
ATOM    640  C   LEU A  87       9.103   1.730   2.082  1.00 12.83           C  
ATOM    641  O   LEU A  87       8.439   2.326   2.928  1.00 13.20           O  
ATOM    642  CB  LEU A  87       8.302   2.045  -0.258  1.00 10.82           C  
ATOM    643  CG  LEU A  87       7.290   3.175  -0.454  1.00 12.63           C  
ATOM    644  CD1 LEU A  87       6.304   2.863  -1.591  1.00 10.26           C  
ATOM    645  CD2 LEU A  87       6.588   3.384   0.877  1.00 10.79           C  
ATOM    646  N   PHE A  88       9.614   0.507   2.278  1.00 12.70           N  
ATOM    647  CA  PHE A  88       9.382  -0.274   3.511  1.00 12.17           C  
ATOM    648  C   PHE A  88      10.538  -0.417   4.467  1.00 12.82           C  
ATOM    649  O   PHE A  88      10.353  -0.899   5.589  1.00 12.50           O  
ATOM    650  CB  PHE A  88       8.945  -1.695   3.174  1.00 13.04           C  
ATOM    651  CG  PHE A  88       7.674  -1.759   2.420  1.00 15.95           C  
ATOM    652  CD1 PHE A  88       6.502  -1.261   2.984  1.00 15.68           C  
ATOM    653  CD2 PHE A  88       7.656  -2.253   1.118  1.00 16.66           C  
ATOM    654  CE1 PHE A  88       5.343  -1.239   2.269  1.00 17.94           C  
ATOM    655  CE2 PHE A  88       6.500  -2.242   0.382  1.00 17.40           C  
ATOM    656  CZ  PHE A  88       5.334  -1.733   0.953  1.00 19.83           C  
ATOM    657  N   THR A  89      11.734  -0.058   4.012  1.00 10.62           N  
ATOM    658  CA  THR A  89      12.914  -0.166   4.849  1.00  8.56           C  
ATOM    659  C   THR A  89      13.074   1.063   5.718  1.00  8.96           C  
ATOM    660  O   THR A  89      13.371   0.963   6.909  1.00  7.56           O  
ATOM    661  CB  THR A  89      14.146  -0.308   4.005  1.00  5.99           C  
ATOM    662  OG1 THR A  89      14.138   0.694   2.986  1.00  6.35           O  
ATOM    663  CG2 THR A  89      14.165  -1.655   3.366  1.00  7.95           C  
ATOM    664  N   THR A  90      12.848   2.224   5.113  1.00  8.47           N  
ATOM    665  CA  THR A  90      13.003   3.485   5.812  1.00  6.66           C  
ATOM    666  C   THR A  90      12.123   3.644   7.032  1.00  5.80           C  
ATOM    667  O   THR A  90      12.591   4.083   8.078  1.00  8.84           O  
ATOM    668  CB  THR A  90      12.799   4.652   4.860  1.00  5.91           C  
ATOM    669  OG1 THR A  90      11.671   4.395   4.016  1.00  7.13           O  
ATOM    670  CG2 THR A  90      14.029   4.810   3.989  1.00  6.47           C  
ATOM    671  N   PRO A  91      10.850   3.271   6.938  1.00  3.40           N  
ATOM    672  CA  PRO A  91      10.048   3.442   8.136  1.00  2.27           C  
ATOM    673  C   PRO A  91      10.406   2.398   9.161  1.00  5.35           C  
ATOM    674  O   PRO A  91       9.999   2.492  10.311  1.00  6.24           O  
ATOM    675  CB  PRO A  91       8.626   3.285   7.638  1.00  4.41           C  
ATOM    676  CG  PRO A  91       8.716   3.283   6.148  1.00  5.97           C  
ATOM    677  CD  PRO A  91      10.049   2.716   5.848  1.00  4.78           C  
ATOM    678  N   LEU A  92      11.176   1.397   8.754  1.00  7.45           N  
ATOM    679  CA  LEU A  92      11.577   0.353   9.694  1.00 10.88           C  
ATOM    680  C   LEU A  92      12.801   0.799  10.490  1.00 13.02           C  
ATOM    681  O   LEU A  92      12.915   0.515  11.686  1.00 14.30           O  
ATOM    682  CB  LEU A  92      11.885  -0.951   8.957  1.00 11.16           C  
ATOM    683  CG  LEU A  92      10.780  -2.007   8.888  1.00 11.45           C  
ATOM    684  CD1 LEU A  92      11.316  -3.323   9.421  1.00 13.36           C  
ATOM    685  CD2 LEU A  92       9.568  -1.572   9.684  1.00 12.04           C  
ATOM    686  N   LEU A  93      13.710   1.502   9.819  1.00 12.96           N  
ATOM    687  CA  LEU A  93      14.925   1.997  10.453  1.00 13.79           C  
ATOM    688  C   LEU A  93      14.549   3.080  11.454  1.00 14.87           C  
ATOM    689  O   LEU A  93      14.971   3.059  12.614  1.00 15.20           O  
ATOM    690  CB  LEU A  93      15.865   2.568   9.397  1.00 11.04           C  
ATOM    691  CG  LEU A  93      16.606   1.500   8.609  1.00 10.74           C  
ATOM    692  CD1 LEU A  93      17.600   2.159   7.691  1.00 10.92           C  
ATOM    693  CD2 LEU A  93      17.287   0.543   9.568  1.00 11.60           C  
ATOM    694  N   LEU A  94      13.753   4.029  10.984  1.00 14.44           N  
ATOM    695  CA  LEU A  94      13.280   5.117  11.819  1.00 14.17           C  
ATOM    696  C   LEU A  94      12.660   4.543  13.080  1.00 14.97           C  
ATOM    697  O   LEU A  94      12.506   5.245  14.081  1.00 14.89           O  
ATOM    698  CB  LEU A  94      12.204   5.910  11.087  1.00 16.04           C  
ATOM    699  CG  LEU A  94      12.581   6.870   9.963  1.00 17.86           C  
ATOM    700  CD1 LEU A  94      11.593   8.000  10.063  1.00 18.91           C  
ATOM    701  CD2 LEU A  94      14.043   7.365  10.058  1.00 19.17           C  
ATOM    702  N   LEU A  95      12.273   3.270  13.016  1.00 12.72           N  
ATOM    703  CA  LEU A  95      11.664   2.599  14.153  1.00  9.28           C  
ATOM    704  C   LEU A  95      12.722   2.014  15.054  1.00  9.03           C  
ATOM    705  O   LEU A  95      12.582   2.028  16.268  1.00  8.93           O  
ATOM    706  CB  LEU A  95      10.742   1.513  13.671  1.00  5.46           C  
ATOM    707  CG  LEU A  95       9.496   2.168  13.129  1.00  5.63           C  
ATOM    708  CD1 LEU A  95       8.647   1.111  12.434  1.00  6.27           C  
ATOM    709  CD2 LEU A  95       8.761   2.855  14.266  1.00  4.52           C  
ATOM    710  N   ASP A  96      13.781   1.496  14.456  1.00  8.08           N  
ATOM    711  CA  ASP A  96      14.872   0.953  15.239  1.00  9.79           C  
ATOM    712  C   ASP A  96      15.350   2.151  16.067  1.00  7.70           C  
ATOM    713  O   ASP A  96      15.763   2.014  17.218  1.00  7.75           O  
ATOM    714  CB  ASP A  96      16.020   0.477  14.311  1.00 13.76           C  
ATOM    715  CG  ASP A  96      16.183  -1.061  14.265  1.00 14.68           C  
ATOM    716  OD1 ASP A  96      15.671  -1.747  15.182  1.00 14.42           O  
ATOM    717  OD2 ASP A  96      16.828  -1.571  13.311  1.00 11.90           O  
ATOM    718  N   LEU A  97      15.266   3.328  15.461  1.00  6.54           N  
ATOM    719  CA  LEU A  97      15.715   4.563  16.089  1.00  8.29           C  
ATOM    720  C   LEU A  97      14.878   5.065  17.243  1.00  8.65           C  
ATOM    721  O   LEU A  97      15.296   5.000  18.404  1.00  8.29           O  
ATOM    722  CB  LEU A  97      15.808   5.669  15.044  1.00 10.16           C  
ATOM    723  CG  LEU A  97      17.206   5.988  14.514  1.00 11.00           C  
ATOM    724  CD1 LEU A  97      17.122   7.147  13.539  1.00 12.23           C  
ATOM    725  CD2 LEU A  97      18.127   6.318  15.669  1.00 11.74           C  
ATOM    726  N   ALA A  98      13.705   5.593  16.908  1.00  9.62           N  
ATOM    727  CA  ALA A  98      12.775   6.131  17.895  1.00 10.80           C  
ATOM    728  C   ALA A  98      12.537   5.109  19.000  1.00 12.35           C  
ATOM    729  O   ALA A  98      12.359   5.470  20.158  1.00 11.44           O  
ATOM    730  CB  ALA A  98      11.481   6.495  17.226  1.00 11.87           C  
ATOM    731  N   LEU A  99      12.507   3.831  18.645  1.00 13.30           N  
ATOM    732  CA  LEU A  99      12.333   2.813  19.660  1.00 15.65           C  
ATOM    733  C   LEU A  99      13.458   3.047  20.656  1.00 17.20           C  
ATOM    734  O   LEU A  99      13.256   3.684  21.697  1.00 17.43           O  
ATOM    735  CB  LEU A  99      12.479   1.427  19.063  1.00 16.10           C  
ATOM    736  CG  LEU A  99      11.251   0.883  18.356  1.00 20.69           C  
ATOM    737  CD1 LEU A  99      11.137  -0.611  18.657  1.00 22.83           C  
ATOM    738  CD2 LEU A  99      10.008   1.632  18.801  1.00 22.19           C  
ATOM    739  N   LEU A 100      14.640   2.533  20.317  1.00 17.72           N  
ATOM    740  CA  LEU A 100      15.834   2.681  21.143  1.00 18.24           C  
ATOM    741  C   LEU A 100      15.667   3.929  22.004  1.00 18.33           C  
ATOM    742  O   LEU A 100      15.647   3.845  23.233  1.00 17.85           O  
ATOM    743  CB  LEU A 100      17.071   2.825  20.241  1.00 21.41           C  
ATOM    744  CG  LEU A 100      18.458   2.338  20.689  1.00 20.81           C  
ATOM    745  CD1 LEU A 100      18.312   1.106  21.560  1.00 20.63           C  
ATOM    746  CD2 LEU A 100      19.303   2.029  19.454  1.00 20.97           C  
ATOM    747  N   VAL A 101      15.538   5.079  21.343  1.00 15.88           N  
ATOM    748  CA  VAL A 101      15.340   6.351  22.032  1.00 15.31           C  
ATOM    749  C   VAL A 101      13.834   6.485  22.209  1.00 17.65           C  
ATOM    750  O   VAL A 101      13.180   7.082  21.363  1.00 18.00           O  
ATOM    751  CB  VAL A 101      15.864   7.549  21.177  1.00 11.72           C  
ATOM    752  CG1 VAL A 101      15.182   8.836  21.555  1.00 11.93           C  
ATOM    753  CG2 VAL A 101      17.329   7.722  21.385  1.00 13.31           C  
ATOM    754  N   ASP A 102      13.274   5.918  23.278  1.00 19.41           N  
ATOM    755  CA  ASP A 102      11.831   6.019  23.492  1.00 23.19           C  
ATOM    756  C   ASP A 102      11.418   7.375  22.963  1.00 23.56           C  
ATOM    757  O   ASP A 102      11.708   8.396  23.580  1.00 23.63           O  
ATOM    758  CB  ASP A 102      11.490   5.911  24.986  1.00 27.31           C  
ATOM    759  CG  ASP A 102      11.997   4.609  25.599  1.00 31.13           C  
ATOM    760  OD1 ASP A 102      12.899   3.999  24.973  1.00 33.24           O  
ATOM    761  OD2 ASP A 102      11.511   4.192  26.682  1.00 31.84           O  
ATOM    762  N   ALA A 103      10.767   7.393  21.804  1.00 23.51           N  
ATOM    763  CA  ALA A 103      10.361   8.657  21.193  1.00 23.83           C  
ATOM    764  C   ALA A 103       8.862   8.776  21.091  1.00 23.48           C  
ATOM    765  O   ALA A 103       8.220   8.024  20.361  1.00 23.55           O  
ATOM    766  CB  ALA A 103      10.978   8.790  19.821  1.00 22.09           C  
ATOM    767  N   ASP A 104       8.311   9.728  21.832  1.00 26.04           N  
ATOM    768  CA  ASP A 104       6.869   9.964  21.846  1.00 28.19           C  
ATOM    769  C   ASP A 104       6.251   9.622  20.487  1.00 27.85           C  
ATOM    770  O   ASP A 104       6.798   9.961  19.431  1.00 27.62           O  
ATOM    771  CB  ASP A 104       6.574  11.438  22.206  1.00 30.90           C  
ATOM    772  CG  ASP A 104       7.122  11.837  23.581  1.00 30.73           C  
ATOM    773  OD1 ASP A 104       7.419  10.934  24.400  1.00 31.33           O  
ATOM    774  OD2 ASP A 104       7.256  13.056  23.835  1.00 30.08           O  
ATOM    775  N   GLN A 105       5.113   8.943  20.524  1.00 27.23           N  
ATOM    776  CA  GLN A 105       4.423   8.558  19.301  1.00 27.15           C  
ATOM    777  C   GLN A 105       4.212   9.761  18.380  1.00 26.71           C  
ATOM    778  O   GLN A 105       4.061   9.616  17.161  1.00 26.00           O  
ATOM    779  CB  GLN A 105       3.090   7.942  19.666  1.00 26.15           C  
ATOM    780  CG  GLN A 105       3.185   7.103  20.894  1.00 24.87           C  
ATOM    781  CD  GLN A 105       2.204   5.980  20.849  1.00 26.68           C  
ATOM    782  OE1 GLN A 105       0.986   6.207  20.859  1.00 25.46           O  
ATOM    783  NE2 GLN A 105       2.713   4.748  20.784  1.00 26.82           N  
ATOM    784  N   GLY A 106       4.194  10.947  18.981  1.00 26.63           N  
ATOM    785  CA  GLY A 106       4.018  12.157  18.206  1.00 25.63           C  
ATOM    786  C   GLY A 106       5.098  12.224  17.150  1.00 23.54           C  
ATOM    787  O   GLY A 106       4.817  12.142  15.951  1.00 23.79           O  
ATOM    788  N   THR A 107       6.342  12.370  17.591  1.00 21.29           N  
ATOM    789  CA  THR A 107       7.442  12.419  16.642  1.00 20.48           C  
ATOM    790  C   THR A 107       7.426  11.112  15.842  1.00 16.28           C  
ATOM    791  O   THR A 107       7.915  11.069  14.716  1.00 15.45           O  
ATOM    792  CB  THR A 107       8.812  12.616  17.365  1.00 21.64           C  
ATOM    793  OG1 THR A 107       9.486  11.358  17.506  1.00 21.62           O  
ATOM    794  CG2 THR A 107       8.587  13.235  18.743  1.00 23.72           C  
ATOM    795  N   ILE A 108       6.845  10.054  16.408  1.00 13.19           N  
ATOM    796  CA  ILE A 108       6.793   8.802  15.679  1.00 10.03           C  
ATOM    797  C   ILE A 108       5.844   8.874  14.492  1.00 12.11           C  
ATOM    798  O   ILE A 108       6.329   8.924  13.360  1.00 12.30           O  
ATOM    799  CB  ILE A 108       6.397   7.605  16.549  1.00  7.81           C  
ATOM    800  CG1 ILE A 108       7.300   7.537  17.780  1.00  6.55           C  
ATOM    801  CG2 ILE A 108       6.538   6.319  15.738  1.00  4.67           C  
ATOM    802  CD1 ILE A 108       8.041   6.227  17.951  1.00  2.30           C  
ATOM    803  N   LEU A 109       4.518   8.897  14.697  1.00 10.60           N  
ATOM    804  CA  LEU A 109       3.640   8.940  13.520  1.00  9.07           C  
ATOM    805  C   LEU A 109       4.181   9.970  12.556  1.00 10.95           C  
ATOM    806  O   LEU A 109       4.216   9.742  11.351  1.00 11.64           O  
ATOM    807  CB  LEU A 109       2.189   9.296  13.826  1.00  6.16           C  
ATOM    808  CG  LEU A 109       1.471   9.658  12.503  1.00  3.63           C  
ATOM    809  CD1 LEU A 109       1.487   8.479  11.560  1.00  2.00           C  
ATOM    810  CD2 LEU A 109       0.044  10.072  12.753  1.00  2.57           C  
ATOM    811  N   ALA A 110       4.623  11.099  13.090  1.00 10.87           N  
ATOM    812  CA  ALA A 110       5.174  12.143  12.248  1.00 11.04           C  
ATOM    813  C   ALA A 110       6.392  11.612  11.494  1.00 10.77           C  
ATOM    814  O   ALA A 110       6.415  11.583  10.262  1.00  9.95           O  
ATOM    815  CB  ALA A 110       5.552  13.327  13.098  1.00 10.99           C  
ATOM    816  N   LEU A 111       7.399  11.190  12.248  1.00 10.42           N  
ATOM    817  CA  LEU A 111       8.627  10.658  11.672  1.00 11.59           C  
ATOM    818  C   LEU A 111       8.373   9.926  10.364  1.00 11.37           C  
ATOM    819  O   LEU A 111       8.932  10.266   9.322  1.00 12.01           O  
ATOM    820  CB  LEU A 111       9.288   9.682  12.648  1.00 10.27           C  
ATOM    821  CG  LEU A 111      10.488  10.182  13.444  1.00  9.30           C  
ATOM    822  CD1 LEU A 111      11.755   9.631  12.836  1.00  7.65           C  
ATOM    823  CD2 LEU A 111      10.503  11.701  13.460  1.00 10.18           C  
ATOM    824  N   VAL A 112       7.513   8.921  10.435  1.00  9.13           N  
ATOM    825  CA  VAL A 112       7.200   8.099   9.289  1.00  7.12           C  
ATOM    826  C   VAL A 112       6.521   8.825   8.142  1.00  7.56           C  
ATOM    827  O   VAL A 112       7.006   8.797   7.015  1.00  7.72           O  
ATOM    828  CB  VAL A 112       6.351   6.905   9.729  1.00  7.32           C  
ATOM    829  CG1 VAL A 112       6.133   6.990  11.209  1.00  4.93           C  
ATOM    830  CG2 VAL A 112       5.020   6.872   8.989  1.00  6.81           C  
ATOM    831  N   GLY A 113       5.396   9.466   8.417  1.00  6.92           N  
ATOM    832  CA  GLY A 113       4.687  10.157   7.360  1.00  4.88           C  
ATOM    833  C   GLY A 113       5.622  11.109   6.675  1.00  5.46           C  
ATOM    834  O   GLY A 113       5.570  11.247   5.455  1.00  4.58           O  
ATOM    835  N   ALA A 114       6.475  11.765   7.467  1.00  5.42           N  
ATOM    836  CA  ALA A 114       7.452  12.708   6.934  1.00  7.06           C  
ATOM    837  C   ALA A 114       8.315  11.916   5.953  1.00  9.35           C  
ATOM    838  O   ALA A 114       8.687  12.429   4.896  1.00  8.36           O  
ATOM    839  CB  ALA A 114       8.291  13.284   8.049  1.00  5.50           C  
ATOM    840  N   ASP A 115       8.605  10.658   6.309  1.00  8.94           N  
ATOM    841  CA  ASP A 115       9.371   9.728   5.463  1.00  9.16           C  
ATOM    842  C   ASP A 115       8.530   9.427   4.223  1.00  9.26           C  
ATOM    843  O   ASP A 115       8.831   9.873   3.108  1.00  5.53           O  
ATOM    844  CB  ASP A 115       9.570   8.366   6.143  1.00  9.12           C  
ATOM    845  CG  ASP A 115      10.629   8.375   7.189  1.00 10.87           C  
ATOM    846  OD1 ASP A 115      10.803   9.427   7.833  1.00 11.52           O  
ATOM    847  OD2 ASP A 115      11.280   7.326   7.371  1.00 11.13           O  
ATOM    848  N   GLY A 116       7.489   8.625   4.466  1.00  6.47           N  
ATOM    849  CA  GLY A 116       6.570   8.194   3.438  1.00  4.28           C  
ATOM    850  C   GLY A 116       6.473   9.157   2.285  1.00  6.75           C  
ATOM    851  O   GLY A 116       6.856   8.818   1.159  1.00  6.91           O  
ATOM    852  N   ILE A 117       5.973  10.360   2.575  1.00  7.10           N  
ATOM    853  CA  ILE A 117       5.776  11.411   1.578  1.00  7.45           C  
ATOM    854  C   ILE A 117       7.025  11.812   0.818  1.00  7.35           C  
ATOM    855  O   ILE A 117       6.948  12.404  -0.262  1.00  6.61           O  
ATOM    856  CB  ILE A 117       5.219  12.660   2.211  1.00  9.43           C  
ATOM    857  CG1 ILE A 117       4.395  13.418   1.182  1.00 10.41           C  
ATOM    858  CG2 ILE A 117       6.366  13.533   2.728  1.00 10.46           C  
ATOM    859  CD1 ILE A 117       3.615  14.528   1.785  1.00 15.57           C  
ATOM    860  N   MET A 118       8.174  11.508   1.406  1.00  6.21           N  
ATOM    861  CA  MET A 118       9.443  11.805   0.777  1.00  5.01           C  
ATOM    862  C   MET A 118       9.688  10.821  -0.377  1.00  6.78           C  
ATOM    863  O   MET A 118      10.046  11.230  -1.486  1.00  5.52           O  
ATOM    864  CB  MET A 118      10.565  11.683   1.790  1.00  2.86           C  
ATOM    865  CG  MET A 118      11.915  11.608   1.144  1.00  4.76           C  
ATOM    866  SD  MET A 118      13.104  10.857   2.197  1.00  4.37           S  
ATOM    867  CE  MET A 118      14.407  11.750   1.792  1.00  2.00           C  
ATOM    868  N   ILE A 119       9.483   9.525  -0.119  1.00  6.16           N  
ATOM    869  CA  ILE A 119       9.703   8.509  -1.148  1.00  4.58           C  
ATOM    870  C   ILE A 119       8.625   8.533  -2.190  1.00  3.08           C  
ATOM    871  O   ILE A 119       8.905   8.514  -3.385  1.00  2.17           O  
ATOM    872  CB  ILE A 119       9.793   7.092  -0.565  1.00  3.29           C  
ATOM    873  CG1 ILE A 119       9.536   7.125   0.944  1.00  5.73           C  
ATOM    874  CG2 ILE A 119      11.159   6.514  -0.888  1.00  2.00           C  
ATOM    875  CD1 ILE A 119      10.496   6.266   1.812  1.00  8.07           C  
ATOM    876  N   GLY A 120       7.385   8.568  -1.737  1.00  2.17           N  
ATOM    877  CA  GLY A 120       6.299   8.633  -2.684  1.00  3.23           C  
ATOM    878  C   GLY A 120       6.628   9.676  -3.736  1.00  4.84           C  
ATOM    879  O   GLY A 120       6.906   9.307  -4.871  1.00  4.74           O  
ATOM    880  N   THR A 121       6.612  10.963  -3.367  1.00  5.97           N  
ATOM    881  CA  THR A 121       6.918  12.057  -4.300  1.00  6.60           C  
ATOM    882  C   THR A 121       8.185  11.753  -5.079  1.00  9.26           C  
ATOM    883  O   THR A 121       8.306  12.133  -6.245  1.00  9.44           O  
ATOM    884  CB  THR A 121       7.144  13.364  -3.573  1.00  6.89           C  
ATOM    885  OG1 THR A 121       8.169  13.177  -2.598  1.00  7.20           O  
ATOM    886  CG2 THR A 121       5.896  13.798  -2.872  1.00  7.25           C  
ATOM    887  N   GLY A 122       9.135  11.078  -4.424  1.00 12.35           N  
ATOM    888  CA  GLY A 122      10.372  10.700  -5.092  1.00 14.70           C  
ATOM    889  C   GLY A 122       9.919   9.964  -6.335  1.00 15.32           C  
ATOM    890  O   GLY A 122      10.244  10.334  -7.470  1.00 16.45           O  
ATOM    891  N   LEU A 123       9.119   8.931  -6.093  1.00 14.39           N  
ATOM    892  CA  LEU A 123       8.531   8.103  -7.139  1.00 12.63           C  
ATOM    893  C   LEU A 123       7.881   8.943  -8.265  1.00 12.18           C  
ATOM    894  O   LEU A 123       8.223   8.773  -9.438  1.00 12.25           O  
ATOM    895  CB  LEU A 123       7.494   7.181  -6.500  1.00  9.40           C  
ATOM    896  CG  LEU A 123       7.133   5.897  -7.221  1.00  6.41           C  
ATOM    897  CD1 LEU A 123       8.252   4.929  -7.067  1.00  6.44           C  
ATOM    898  CD2 LEU A 123       5.852   5.333  -6.642  1.00  4.19           C  
ATOM    899  N   VAL A 124       6.953   9.841  -7.907  1.00 11.17           N  
ATOM    900  CA  VAL A 124       6.258  10.698  -8.888  1.00  8.47           C  
ATOM    901  C   VAL A 124       7.246  11.405  -9.803  1.00  7.13           C  
ATOM    902  O   VAL A 124       7.161  11.321 -11.030  1.00  6.81           O  
ATOM    903  CB  VAL A 124       5.402  11.807  -8.212  1.00  8.15           C  
ATOM    904  CG1 VAL A 124       4.553  12.524  -9.260  1.00  4.65           C  
ATOM    905  CG2 VAL A 124       4.508  11.216  -7.140  1.00 11.39           C  
ATOM    906  N   GLY A 125       8.176  12.115  -9.183  1.00  6.07           N  
ATOM    907  CA  GLY A 125       9.170  12.833  -9.940  1.00  4.35           C  
ATOM    908  C   GLY A 125      10.185  11.859 -10.462  1.00  5.40           C  
ATOM    909  O   GLY A 125      11.173  12.243 -11.083  1.00  4.51           O  
ATOM    910  N   ALA A 126       9.925  10.584 -10.213  1.00  6.70           N  
ATOM    911  CA  ALA A 126      10.819   9.527 -10.653  1.00  8.70           C  
ATOM    912  C   ALA A 126      10.291   8.763 -11.874  1.00  7.25           C  
ATOM    913  O   ALA A 126      10.883   7.777 -12.301  1.00  6.73           O  
ATOM    914  CB  ALA A 126      11.068   8.579  -9.503  1.00  9.86           C  
ATOM    915  N   LEU A 127       9.189   9.232 -12.443  1.00  6.48           N  
ATOM    916  CA  LEU A 127       8.609   8.569 -13.596  1.00  7.42           C  
ATOM    917  C   LEU A 127       7.970   9.553 -14.606  1.00  6.93           C  
ATOM    918  O   LEU A 127       7.650   9.169 -15.730  1.00  5.74           O  
ATOM    919  CB  LEU A 127       7.588   7.520 -13.102  1.00  7.55           C  
ATOM    920  CG  LEU A 127       8.091   6.527 -12.029  1.00  9.87           C  
ATOM    921  CD1 LEU A 127       6.952   5.729 -11.423  1.00  6.58           C  
ATOM    922  CD2 LEU A 127       9.106   5.575 -12.654  1.00  9.09           C  
ATOM    923  N   THR A 128       7.811  10.816 -14.201  1.00  6.15           N  
ATOM    924  CA  THR A 128       7.213  11.881 -15.019  1.00  4.95           C  
ATOM    925  C   THR A 128       7.873  12.130 -16.394  1.00  8.80           C  
ATOM    926  O   THR A 128       9.093  12.142 -16.496  1.00  9.46           O  
ATOM    927  CB  THR A 128       7.218  13.169 -14.225  1.00  2.29           C  
ATOM    928  OG1 THR A 128       7.102  12.848 -12.837  1.00  2.00           O  
ATOM    929  CG2 THR A 128       6.065  14.050 -14.628  1.00  2.72           C  
ATOM    930  N   LYS A 129       7.066  12.336 -17.445  1.00 11.00           N  
ATOM    931  CA  LYS A 129       7.579  12.541 -18.818  1.00 11.33           C  
ATOM    932  C   LYS A 129       7.796  13.971 -19.278  1.00 12.96           C  
ATOM    933  O   LYS A 129       7.722  14.227 -20.483  1.00 13.70           O  
ATOM    934  CB  LYS A 129       6.678  11.888 -19.879  1.00 11.53           C  
ATOM    935  CG  LYS A 129       5.736  10.798 -19.410  1.00 11.94           C  
ATOM    936  CD  LYS A 129       5.258  10.017 -20.619  1.00 14.11           C  
ATOM    937  CE  LYS A 129       3.798   9.621 -20.505  1.00 15.97           C  
ATOM    938  NZ  LYS A 129       3.138   9.366 -21.829  1.00 16.10           N  
ATOM    939  N   VAL A 130       8.019  14.903 -18.350  1.00 12.62           N  
ATOM    940  CA  VAL A 130       8.292  16.304 -18.712  1.00 11.81           C  
ATOM    941  C   VAL A 130       9.655  16.576 -18.135  1.00 12.17           C  
ATOM    942  O   VAL A 130       9.833  16.590 -16.911  1.00 13.25           O  
ATOM    943  CB  VAL A 130       7.351  17.326 -18.059  1.00 12.09           C  
ATOM    944  CG1 VAL A 130       8.099  18.647 -17.854  1.00 10.81           C  
ATOM    945  CG2 VAL A 130       6.140  17.557 -18.931  1.00 13.31           C  
ATOM    946  N   TYR A 131      10.627  16.804 -18.997  1.00 11.53           N  
ATOM    947  CA  TYR A 131      11.949  17.032 -18.477  1.00 10.66           C  
ATOM    948  C   TYR A 131      12.008  18.172 -17.483  1.00  9.15           C  
ATOM    949  O   TYR A 131      13.015  18.343 -16.802  1.00  9.10           O  
ATOM    950  CB  TYR A 131      12.933  17.277 -19.604  1.00 11.05           C  
ATOM    951  CG  TYR A 131      14.327  17.311 -19.078  1.00 10.18           C  
ATOM    952  CD1 TYR A 131      14.992  16.137 -18.743  1.00 11.01           C  
ATOM    953  CD2 TYR A 131      14.965  18.512 -18.856  1.00 10.40           C  
ATOM    954  CE1 TYR A 131      16.266  16.167 -18.192  1.00 13.13           C  
ATOM    955  CE2 TYR A 131      16.219  18.551 -18.313  1.00 12.37           C  
ATOM    956  CZ  TYR A 131      16.875  17.386 -17.980  1.00 12.37           C  
ATOM    957  OH  TYR A 131      18.133  17.449 -17.421  1.00 12.76           O  
ATOM    958  N   SER A 132      10.933  18.943 -17.370  1.00  9.31           N  
ATOM    959  CA  SER A 132      10.960  20.056 -16.436  1.00 10.00           C  
ATOM    960  C   SER A 132      10.043  19.960 -15.213  1.00 10.94           C  
ATOM    961  O   SER A 132      10.041  20.862 -14.372  1.00  9.91           O  
ATOM    962  CB  SER A 132      10.703  21.362 -17.182  1.00 10.41           C  
ATOM    963  OG  SER A 132      11.000  21.223 -18.557  1.00 11.51           O  
ATOM    964  N   TYR A 133       9.285  18.873 -15.093  1.00 10.50           N  
ATOM    965  CA  TYR A 133       8.393  18.726 -13.943  1.00 11.30           C  
ATOM    966  C   TYR A 133       8.966  17.848 -12.837  1.00 11.24           C  
ATOM    967  O   TYR A 133       8.475  17.858 -11.710  1.00 10.70           O  
ATOM    968  CB  TYR A 133       7.023  18.215 -14.396  1.00 10.46           C  
ATOM    969  CG  TYR A 133       6.189  19.293 -15.073  1.00 12.33           C  
ATOM    970  CD1 TYR A 133       6.456  20.664 -14.859  1.00  9.41           C  
ATOM    971  CD2 TYR A 133       5.135  18.952 -15.930  1.00 11.47           C  
ATOM    972  CE1 TYR A 133       5.705  21.642 -15.473  1.00  6.64           C  
ATOM    973  CE2 TYR A 133       4.373  19.935 -16.552  1.00 10.27           C  
ATOM    974  CZ  TYR A 133       4.663  21.272 -16.317  1.00  9.88           C  
ATOM    975  OH  TYR A 133       3.890  22.228 -16.931  1.00 10.12           O  
ATOM    976  N   ARG A 134      10.001  17.082 -13.165  1.00 11.99           N  
ATOM    977  CA  ARG A 134      10.646  16.244 -12.166  1.00 11.90           C  
ATOM    978  C   ARG A 134      11.097  17.203 -11.063  1.00 14.16           C  
ATOM    979  O   ARG A 134      10.303  17.596 -10.204  1.00 14.09           O  
ATOM    980  CB  ARG A 134      11.871  15.531 -12.755  1.00  9.41           C  
ATOM    981  CG  ARG A 134      11.619  14.815 -14.055  1.00  8.96           C  
ATOM    982  CD  ARG A 134      12.515  13.595 -14.184  1.00  9.88           C  
ATOM    983  NE  ARG A 134      11.774  12.336 -14.111  1.00 11.54           N  
ATOM    984  CZ  ARG A 134      12.330  11.126 -14.008  1.00 12.62           C  
ATOM    985  NH1 ARG A 134      13.645  10.992 -13.962  1.00 11.96           N  
ATOM    986  NH2 ARG A 134      11.567  10.038 -13.992  1.00 12.67           N  
ATOM    987  N   PHE A 135      12.374  17.588 -11.138  1.00 13.43           N  
ATOM    988  CA  PHE A 135      13.050  18.488 -10.199  1.00 10.84           C  
ATOM    989  C   PHE A 135      12.186  19.208  -9.171  1.00 10.33           C  
ATOM    990  O   PHE A 135      12.616  19.372  -8.027  1.00  9.19           O  
ATOM    991  CB  PHE A 135      13.873  19.516 -10.971  1.00  7.80           C  
ATOM    992  CG  PHE A 135      14.783  18.920 -12.001  1.00  6.65           C  
ATOM    993  CD1 PHE A 135      15.883  18.162 -11.623  1.00  5.01           C  
ATOM    994  CD2 PHE A 135      14.554  19.143 -13.361  1.00  6.70           C  
ATOM    995  CE1 PHE A 135      16.744  17.635 -12.588  1.00  4.27           C  
ATOM    996  CE2 PHE A 135      15.406  18.622 -14.331  1.00  4.19           C  
ATOM    997  CZ  PHE A 135      16.501  17.869 -13.945  1.00  4.42           C  
ATOM    998  N   VAL A 136      10.989  19.651  -9.558  1.00  9.34           N  
ATOM    999  CA  VAL A 136      10.114  20.330  -8.600  1.00  9.82           C  
ATOM   1000  C   VAL A 136       9.756  19.325  -7.526  1.00  9.13           C  
ATOM   1001  O   VAL A 136       9.872  19.617  -6.335  1.00  8.74           O  
ATOM   1002  CB  VAL A 136       8.821  20.873  -9.268  1.00 12.55           C  
ATOM   1003  CG1 VAL A 136       8.744  20.383 -10.695  1.00 12.61           C  
ATOM   1004  CG2 VAL A 136       7.576  20.459  -8.473  1.00 12.64           C  
ATOM   1005  N   TRP A 137       9.334  18.137  -7.964  1.00  7.68           N  
ATOM   1006  CA  TRP A 137       8.983  17.039  -7.067  1.00  5.36           C  
ATOM   1007  C   TRP A 137      10.209  16.708  -6.216  1.00  6.34           C  
ATOM   1008  O   TRP A 137      10.098  16.353  -5.047  1.00  6.51           O  
ATOM   1009  CB  TRP A 137       8.556  15.819  -7.877  1.00  2.00           C  
ATOM   1010  CG  TRP A 137       7.100  15.817  -8.227  1.00  2.00           C  
ATOM   1011  CD1 TRP A 137       6.547  15.818  -9.473  1.00  2.00           C  
ATOM   1012  CD2 TRP A 137       6.009  15.796  -7.312  1.00  2.00           C  
ATOM   1013  NE1 TRP A 137       5.183  15.795  -9.388  1.00  2.00           N  
ATOM   1014  CE2 TRP A 137       4.831  15.782  -8.066  1.00  2.00           C  
ATOM   1015  CE3 TRP A 137       5.913  15.785  -5.915  1.00  3.58           C  
ATOM   1016  CZ2 TRP A 137       3.585  15.759  -7.474  1.00  2.00           C  
ATOM   1017  CZ3 TRP A 137       4.673  15.769  -5.335  1.00  2.00           C  
ATOM   1018  CH2 TRP A 137       3.529  15.755  -6.109  1.00  2.00           C  
ATOM   1019  N   TRP A 138      11.384  16.845  -6.809  1.00  7.28           N  
ATOM   1020  CA  TRP A 138      12.625  16.590  -6.104  1.00  8.11           C  
ATOM   1021  C   TRP A 138      12.733  17.525  -4.912  1.00  7.49           C  
ATOM   1022  O   TRP A 138      13.282  17.162  -3.874  1.00  9.16           O  
ATOM   1023  CB  TRP A 138      13.822  16.832  -7.032  1.00 12.32           C  
ATOM   1024  CG  TRP A 138      15.149  16.428  -6.440  1.00 11.09           C  
ATOM   1025  CD1 TRP A 138      15.631  15.177  -6.342  1.00  9.65           C  
ATOM   1026  CD2 TRP A 138      16.140  17.289  -5.871  1.00 11.95           C  
ATOM   1027  NE1 TRP A 138      16.857  15.187  -5.748  1.00 12.06           N  
ATOM   1028  CE2 TRP A 138      17.195  16.477  -5.447  1.00 13.33           C  
ATOM   1029  CE3 TRP A 138      16.233  18.668  -5.680  1.00 14.45           C  
ATOM   1030  CZ2 TRP A 138      18.350  16.995  -4.834  1.00 14.50           C  
ATOM   1031  CZ3 TRP A 138      17.384  19.190  -5.069  1.00 14.60           C  
ATOM   1032  CH2 TRP A 138      18.423  18.352  -4.654  1.00 14.67           C  
ATOM   1033  N   ALA A 139      12.228  18.742  -5.066  1.00  6.26           N  
ATOM   1034  CA  ALA A 139      12.293  19.712  -3.984  1.00  4.58           C  
ATOM   1035  C   ALA A 139      11.463  19.255  -2.807  1.00  2.98           C  
ATOM   1036  O   ALA A 139      11.974  19.071  -1.706  1.00  2.00           O  
ATOM   1037  CB  ALA A 139      11.803  21.037  -4.457  1.00  5.94           C  
ATOM   1038  N   ILE A 140      10.176  19.074  -3.054  1.00  2.42           N  
ATOM   1039  CA  ILE A 140       9.267  18.638  -2.019  1.00  2.50           C  
ATOM   1040  C   ILE A 140       9.796  17.410  -1.287  1.00  3.07           C  
ATOM   1041  O   ILE A 140       9.572  17.254  -0.088  1.00  2.44           O  
ATOM   1042  CB  ILE A 140       7.887  18.308  -2.595  1.00  2.00           C  
ATOM   1043  CG1 ILE A 140       7.619  19.150  -3.845  1.00  2.72           C  
ATOM   1044  CG2 ILE A 140       6.838  18.551  -1.542  1.00  2.00           C  
ATOM   1045  CD1 ILE A 140       6.132  19.196  -4.315  1.00  5.15           C  
ATOM   1046  N   SER A 141      10.505  16.538  -1.997  1.00  3.56           N  
ATOM   1047  CA  SER A 141      11.026  15.340  -1.349  1.00  6.89           C  
ATOM   1048  C   SER A 141      12.166  15.664  -0.405  1.00  9.02           C  
ATOM   1049  O   SER A 141      12.122  15.330   0.780  1.00  9.03           O  
ATOM   1050  CB  SER A 141      11.501  14.315  -2.367  1.00  4.64           C  
ATOM   1051  OG  SER A 141      11.998  13.169  -1.692  1.00  5.71           O  
ATOM   1052  N   THR A 142      13.199  16.295  -0.934  1.00  6.83           N  
ATOM   1053  CA  THR A 142      14.298  16.684  -0.098  1.00  7.24           C  
ATOM   1054  C   THR A 142      13.667  17.487   1.020  1.00  9.72           C  
ATOM   1055  O   THR A 142      13.709  17.097   2.190  1.00 11.00           O  
ATOM   1056  CB  THR A 142      15.206  17.612  -0.813  1.00  8.44           C  
ATOM   1057  OG1 THR A 142      15.669  16.989  -2.021  1.00  7.85           O  
ATOM   1058  CG2 THR A 142      16.365  18.003   0.118  1.00  8.92           C  
ATOM   1059  N   ALA A 143      13.078  18.617   0.635  1.00  8.45           N  
ATOM   1060  CA  ALA A 143      12.409  19.511   1.562  1.00  8.81           C  
ATOM   1061  C   ALA A 143      11.924  18.730   2.756  1.00  9.91           C  
ATOM   1062  O   ALA A 143      12.211  19.072   3.897  1.00  9.73           O  
ATOM   1063  CB  ALA A 143      11.258  20.153   0.883  1.00  8.39           C  
ATOM   1064  N   ALA A 144      11.202  17.654   2.482  1.00 11.95           N  
ATOM   1065  CA  ALA A 144      10.669  16.807   3.541  1.00 13.42           C  
ATOM   1066  C   ALA A 144      11.734  16.057   4.319  1.00 12.77           C  
ATOM   1067  O   ALA A 144      11.686  16.005   5.551  1.00 12.96           O  
ATOM   1068  CB  ALA A 144       9.693  15.829   2.971  1.00 16.87           C  
ATOM   1069  N   MET A 145      12.678  15.455   3.601  1.00 11.37           N  
ATOM   1070  CA  MET A 145      13.776  14.701   4.224  1.00 10.72           C  
ATOM   1071  C   MET A 145      14.319  15.521   5.389  1.00  8.08           C  
ATOM   1072  O   MET A 145      14.328  15.096   6.549  1.00  4.43           O  
ATOM   1073  CB  MET A 145      14.871  14.475   3.185  1.00  9.02           C  
ATOM   1074  CG  MET A 145      16.105  13.789   3.683  1.00  6.70           C  
ATOM   1075  SD  MET A 145      17.347  13.794   2.386  1.00  2.00           S  
ATOM   1076  CE  MET A 145      18.514  12.744   3.069  1.00  2.00           C  
ATOM   1077  N   LEU A 146      14.740  16.723   5.040  1.00  6.98           N  
ATOM   1078  CA  LEU A 146      15.288  17.655   5.984  1.00  7.86           C  
ATOM   1079  C   LEU A 146      14.404  17.825   7.210  1.00 10.42           C  
ATOM   1080  O   LEU A 146      14.842  18.377   8.224  1.00  8.96           O  
ATOM   1081  CB  LEU A 146      15.452  18.991   5.308  1.00  8.61           C  
ATOM   1082  CG  LEU A 146      16.706  19.140   4.492  1.00  8.92           C  
ATOM   1083  CD1 LEU A 146      16.362  19.498   3.066  1.00  9.08           C  
ATOM   1084  CD2 LEU A 146      17.517  20.223   5.130  1.00 10.08           C  
ATOM   1085  N   TYR A 147      13.155  17.377   7.136  1.00 11.94           N  
ATOM   1086  CA  TYR A 147      12.304  17.539   8.302  1.00 13.61           C  
ATOM   1087  C   TYR A 147      12.529  16.414   9.314  1.00 12.93           C  
ATOM   1088  O   TYR A 147      12.497  16.656  10.529  1.00 12.52           O  
ATOM   1089  CB  TYR A 147      10.816  17.634   7.926  1.00 15.29           C  
ATOM   1090  CG  TYR A 147       9.974  17.840   9.157  1.00 17.75           C  
ATOM   1091  CD1 TYR A 147       9.769  19.114   9.670  1.00 19.22           C  
ATOM   1092  CD2 TYR A 147       9.543  16.747   9.912  1.00 17.86           C  
ATOM   1093  CE1 TYR A 147       9.180  19.296  10.917  1.00 21.42           C  
ATOM   1094  CE2 TYR A 147       8.959  16.908  11.151  1.00 19.78           C  
ATOM   1095  CZ  TYR A 147       8.781  18.182  11.656  1.00 22.56           C  
ATOM   1096  OH  TYR A 147       8.243  18.334  12.918  1.00 24.05           O  
ATOM   1097  N   ILE A 148      12.753  15.191   8.838  1.00  9.95           N  
ATOM   1098  CA  ILE A 148      12.994  14.113   9.786  1.00 10.48           C  
ATOM   1099  C   ILE A 148      14.398  14.351  10.292  1.00 12.42           C  
ATOM   1100  O   ILE A 148      14.653  14.357  11.500  1.00 12.48           O  
ATOM   1101  CB  ILE A 148      12.920  12.701   9.153  1.00  9.47           C  
ATOM   1102  CG1 ILE A 148      12.916  12.804   7.620  1.00 12.24           C  
ATOM   1103  CG2 ILE A 148      11.695  11.972   9.697  1.00  7.63           C  
ATOM   1104  CD1 ILE A 148      12.609  11.507   6.883  1.00  7.76           C  
ATOM   1105  N   LEU A 149      15.310  14.567   9.353  1.00 13.25           N  
ATOM   1106  CA  LEU A 149      16.701  14.829   9.690  1.00 12.46           C  
ATOM   1107  C   LEU A 149      16.780  15.773  10.888  1.00 10.68           C  
ATOM   1108  O   LEU A 149      17.420  15.473  11.892  1.00  9.29           O  
ATOM   1109  CB  LEU A 149      17.412  15.443   8.483  1.00 13.94           C  
ATOM   1110  CG  LEU A 149      18.322  14.512   7.681  1.00 15.66           C  
ATOM   1111  CD1 LEU A 149      19.760  14.842   8.017  1.00 18.07           C  
ATOM   1112  CD2 LEU A 149      18.034  13.057   7.999  1.00 14.84           C  
ATOM   1113  N   TYR A 150      16.110  16.909  10.774  1.00 10.36           N  
ATOM   1114  CA  TYR A 150      16.088  17.889  11.844  1.00 12.08           C  
ATOM   1115  C   TYR A 150      15.605  17.296  13.182  1.00 12.84           C  
ATOM   1116  O   TYR A 150      16.320  17.299  14.195  1.00 12.22           O  
ATOM   1117  CB  TYR A 150      15.177  19.043  11.451  1.00 10.93           C  
ATOM   1118  CG  TYR A 150      14.964  20.028  12.566  1.00 10.69           C  
ATOM   1119  CD1 TYR A 150      13.952  19.840  13.501  1.00 10.53           C  
ATOM   1120  CD2 TYR A 150      15.819  21.117  12.722  1.00 12.30           C  
ATOM   1121  CE1 TYR A 150      13.799  20.709  14.569  1.00 14.88           C  
ATOM   1122  CE2 TYR A 150      15.679  22.000  13.790  1.00 14.34           C  
ATOM   1123  CZ  TYR A 150      14.673  21.786  14.714  1.00 15.29           C  
ATOM   1124  OH  TYR A 150      14.565  22.632  15.795  1.00 15.31           O  
ATOM   1125  N   VAL A 151      14.373  16.806  13.174  1.00 13.44           N  
ATOM   1126  CA  VAL A 151      13.781  16.224  14.360  1.00 15.69           C  
ATOM   1127  C   VAL A 151      14.693  15.134  14.903  1.00 15.84           C  
ATOM   1128  O   VAL A 151      14.620  14.767  16.074  1.00 14.75           O  
ATOM   1129  CB  VAL A 151      12.385  15.645  14.033  1.00 17.25           C  
ATOM   1130  CG1 VAL A 151      12.304  14.186  14.472  1.00 17.69           C  
ATOM   1131  CG2 VAL A 151      11.287  16.499  14.710  1.00 17.48           C  
ATOM   1132  N   LEU A 152      15.556  14.613  14.046  1.00 16.89           N  
ATOM   1133  CA  LEU A 152      16.467  13.567  14.480  1.00 16.74           C  
ATOM   1134  C   LEU A 152      17.564  14.138  15.386  1.00 18.72           C  
ATOM   1135  O   LEU A 152      18.052  13.443  16.280  1.00 18.86           O  
ATOM   1136  CB  LEU A 152      17.077  12.856  13.269  1.00 13.23           C  
ATOM   1137  CG  LEU A 152      16.499  11.464  13.044  1.00 10.84           C  
ATOM   1138  CD1 LEU A 152      17.129  10.827  11.818  1.00 13.58           C  
ATOM   1139  CD2 LEU A 152      16.743  10.616  14.268  1.00 11.35           C  
ATOM   1140  N   PHE A 153      17.935  15.403  15.170  1.00 20.29           N  
ATOM   1141  CA  PHE A 153      18.970  16.043  15.984  1.00 21.47           C  
ATOM   1142  C   PHE A 153      18.386  16.679  17.207  1.00 21.89           C  
ATOM   1143  O   PHE A 153      18.125  16.025  18.220  1.00 21.97           O  
ATOM   1144  CB  PHE A 153      19.672  17.153  15.228  1.00 23.36           C  
ATOM   1145  CG  PHE A 153      20.426  16.680  14.085  1.00 23.27           C  
ATOM   1146  CD1 PHE A 153      21.506  15.847  14.275  1.00 24.95           C  
ATOM   1147  CD2 PHE A 153      20.000  16.974  12.811  1.00 23.66           C  
ATOM   1148  CE1 PHE A 153      22.154  15.291  13.209  1.00 26.49           C  
ATOM   1149  CE2 PHE A 153      20.629  16.432  11.732  1.00 26.45           C  
ATOM   1150  CZ  PHE A 153      21.718  15.577  11.928  1.00 27.59           C  
ATOM   1151  N   PHE A 154      18.213  17.986  17.091  1.00 22.50           N  
ATOM   1152  CA  PHE A 154      17.665  18.788  18.147  1.00 24.28           C  
ATOM   1153  C   PHE A 154      16.519  18.003  18.712  1.00 23.41           C  
ATOM   1154  O   PHE A 154      16.181  18.121  19.896  1.00 23.25           O  
ATOM   1155  CB  PHE A 154      17.152  20.088  17.567  1.00 27.02           C  
ATOM   1156  CG  PHE A 154      17.995  20.613  16.448  1.00 29.90           C  
ATOM   1157  CD1 PHE A 154      17.764  20.211  15.137  1.00 29.68           C  
ATOM   1158  CD2 PHE A 154      19.020  21.523  16.703  1.00 33.31           C  
ATOM   1159  CE1 PHE A 154      18.550  20.715  14.076  1.00 30.63           C  
ATOM   1160  CE2 PHE A 154      19.810  22.030  15.659  1.00 34.62           C  
ATOM   1161  CZ  PHE A 154      19.570  21.624  14.334  1.00 33.01           C  
ATOM   1162  N   GLY A 155      15.938  17.176  17.850  1.00 23.33           N  
ATOM   1163  CA  GLY A 155      14.804  16.366  18.244  1.00 24.57           C  
ATOM   1164  C   GLY A 155      15.045  15.237  19.223  1.00 24.70           C  
ATOM   1165  O   GLY A 155      14.806  15.389  20.427  1.00 24.30           O  
ATOM   1166  N   PHE A 156      15.510  14.098  18.725  1.00 24.54           N  
ATOM   1167  CA  PHE A 156      15.708  12.972  19.616  1.00 25.45           C  
ATOM   1168  C   PHE A 156      16.679  13.235  20.768  1.00 27.14           C  
ATOM   1169  O   PHE A 156      17.010  12.304  21.508  1.00 28.69           O  
ATOM   1170  CB  PHE A 156      16.129  11.724  18.831  1.00 24.82           C  
ATOM   1171  CG  PHE A 156      14.981  11.022  18.149  1.00 25.18           C  
ATOM   1172  CD1 PHE A 156      13.694  11.050  18.696  1.00 24.14           C  
ATOM   1173  CD2 PHE A 156      15.170  10.376  16.923  1.00 25.89           C  
ATOM   1174  CE1 PHE A 156      12.615  10.444  18.018  1.00 24.30           C  
ATOM   1175  CE2 PHE A 156      14.092   9.768  16.241  1.00 24.75           C  
ATOM   1176  CZ  PHE A 156      12.817   9.804  16.786  1.00 22.73           C  
ATOM   1177  N   THR A 157      17.150  14.474  20.937  1.00 25.87           N  
ATOM   1178  CA  THR A 157      18.029  14.742  22.076  1.00 24.50           C  
ATOM   1179  C   THR A 157      17.160  14.799  23.328  1.00 23.78           C  
ATOM   1180  O   THR A 157      16.734  15.854  23.798  1.00 22.57           O  
ATOM   1181  CB  THR A 157      18.852  16.042  21.939  1.00 24.97           C  
ATOM   1182  OG1 THR A 157      18.055  17.090  21.364  1.00 22.05           O  
ATOM   1183  CG2 THR A 157      20.094  15.757  21.084  1.00 24.06           C  
ATOM   1184  N   SER A 158      16.899  13.596  23.814  1.00 24.89           N  
ATOM   1185  CA  SER A 158      16.117  13.284  24.994  1.00 25.82           C  
ATOM   1186  C   SER A 158      16.486  14.129  26.209  1.00 28.72           C  
ATOM   1187  O   SER A 158      16.764  15.336  26.122  1.00 29.01           O  
ATOM   1188  CB  SER A 158      16.377  11.814  25.339  1.00 23.49           C  
ATOM   1189  OG  SER A 158      17.774  11.566  25.518  1.00 18.03           O  
ATOM   1190  N   LYS A 159      16.472  13.434  27.346  1.00 31.48           N  
ATOM   1191  CA  LYS A 159      16.827  13.936  28.672  1.00 34.01           C  
ATOM   1192  C   LYS A 159      17.454  12.660  29.250  1.00 35.89           C  
ATOM   1193  O   LYS A 159      16.869  12.004  30.120  1.00 36.51           O  
ATOM   1194  CB  LYS A 159      15.565  14.335  29.465  1.00 33.79           C  
ATOM   1195  CG  LYS A 159      15.799  14.640  30.960  1.00 33.71           C  
ATOM   1196  CD  LYS A 159      14.983  15.858  31.438  1.00 33.40           C  
ATOM   1197  CE  LYS A 159      14.154  15.553  32.695  1.00 31.99           C  
ATOM   1198  NZ  LYS A 159      12.841  16.318  32.759  1.00 31.03           N  
ATOM   1199  N   ALA A 160      18.616  12.282  28.708  1.00 37.19           N  
ATOM   1200  CA  ALA A 160      19.334  11.076  29.144  1.00 38.35           C  
ATOM   1201  C   ALA A 160      19.511  11.146  30.664  1.00 38.95           C  
ATOM   1202  O   ALA A 160      20.541  11.617  31.151  1.00 39.90           O  
ATOM   1203  CB  ALA A 160      20.704  11.004  28.438  1.00 38.46           C  
ATOM   1204  N   GLU A 161      18.510  10.689  31.416  1.00 38.64           N  
ATOM   1205  CA  GLU A 161      18.570  10.772  32.880  1.00 38.10           C  
ATOM   1206  C   GLU A 161      18.512   9.432  33.600  1.00 39.21           C  
ATOM   1207  O   GLU A 161      19.448   9.058  34.324  1.00 38.72           O  
ATOM   1208  CB  GLU A 161      17.433  11.670  33.399  1.00 36.71           C  
ATOM   1209  CG  GLU A 161      17.618  12.184  34.842  1.00 35.09           C  
ATOM   1210  CD  GLU A 161      18.916  12.990  35.048  1.00 34.61           C  
ATOM   1211  OE1 GLU A 161      19.378  13.657  34.091  1.00 34.33           O  
ATOM   1212  OE2 GLU A 161      19.472  12.956  36.173  1.00 33.84           O  
ATOM   1213  N   SER A 162      17.407   8.719  33.407  1.00 39.27           N  
ATOM   1214  CA  SER A 162      17.205   7.427  34.063  1.00 39.44           C  
ATOM   1215  C   SER A 162      17.624   6.229  33.216  1.00 37.98           C  
ATOM   1216  O   SER A 162      17.315   5.074  33.572  1.00 37.68           O  
ATOM   1217  CB  SER A 162      15.717   7.268  34.446  1.00 41.14           C  
ATOM   1218  OG  SER A 162      15.001   6.475  33.502  1.00 41.04           O  
ATOM   1219  N   MET A 163      18.331   6.488  32.115  1.00 35.41           N  
ATOM   1220  CA  MET A 163      18.704   5.401  31.211  1.00 33.85           C  
ATOM   1221  C   MET A 163      20.154   4.911  31.122  1.00 32.76           C  
ATOM   1222  O   MET A 163      21.086   5.460  31.738  1.00 29.71           O  
ATOM   1223  CB  MET A 163      18.207   5.728  29.793  1.00 33.47           C  
ATOM   1224  CG  MET A 163      16.719   5.996  29.696  1.00 28.99           C  
ATOM   1225  SD  MET A 163      16.450   7.562  28.851  1.00 30.00           S  
ATOM   1226  CE  MET A 163      14.650   7.787  29.159  1.00 29.93           C  
ATOM   1227  N   ARG A 164      20.287   3.839  30.338  1.00 32.02           N  
ATOM   1228  CA  ARG A 164      21.554   3.183  30.068  1.00 32.17           C  
ATOM   1229  C   ARG A 164      22.547   4.244  29.653  1.00 32.35           C  
ATOM   1230  O   ARG A 164      22.522   4.760  28.523  1.00 33.19           O  
ATOM   1231  CB  ARG A 164      21.398   2.166  28.942  1.00 31.45           C  
ATOM   1232  CG  ARG A 164      22.660   1.383  28.664  1.00 31.02           C  
ATOM   1233  CD  ARG A 164      22.895   0.315  29.733  1.00 31.61           C  
ATOM   1234  NE  ARG A 164      21.746  -0.582  29.882  1.00 32.05           N  
ATOM   1235  CZ  ARG A 164      21.837  -1.860  30.248  1.00 32.77           C  
ATOM   1236  NH1 ARG A 164      23.026  -2.399  30.506  1.00 33.10           N  
ATOM   1237  NH2 ARG A 164      20.745  -2.604  30.353  1.00 32.75           N  
ATOM   1238  N   PRO A 165      23.459   4.574  30.559  1.00 31.67           N  
ATOM   1239  CA  PRO A 165      24.454   5.601  30.239  1.00 30.36           C  
ATOM   1240  C   PRO A 165      25.331   5.067  29.109  1.00 28.58           C  
ATOM   1241  O   PRO A 165      26.440   5.555  28.868  1.00 28.92           O  
ATOM   1242  CB  PRO A 165      25.209   5.789  31.553  1.00 32.46           C  
ATOM   1243  CG  PRO A 165      25.016   4.449  32.278  1.00 35.00           C  
ATOM   1244  CD  PRO A 165      23.654   3.958  31.881  1.00 31.84           C  
ATOM   1245  N   GLU A 166      24.815   4.050  28.426  1.00 25.34           N  
ATOM   1246  CA  GLU A 166      25.518   3.439  27.316  1.00 23.73           C  
ATOM   1247  C   GLU A 166      24.886   3.795  25.966  1.00 23.97           C  
ATOM   1248  O   GLU A 166      25.591   3.943  24.959  1.00 23.90           O  
ATOM   1249  CB  GLU A 166      25.538   1.918  27.482  1.00 23.18           C  
ATOM   1250  CG  GLU A 166      25.764   1.442  28.903  1.00 21.35           C  
ATOM   1251  CD  GLU A 166      26.616   0.190  28.959  1.00 19.78           C  
ATOM   1252  OE1 GLU A 166      27.774   0.251  28.500  1.00 17.40           O  
ATOM   1253  OE2 GLU A 166      26.130  -0.845  29.461  1.00 18.65           O  
ATOM   1254  N   VAL A 167      23.560   3.939  25.946  1.00 22.93           N  
ATOM   1255  CA  VAL A 167      22.852   4.254  24.702  1.00 21.13           C  
ATOM   1256  C   VAL A 167      23.545   5.336  23.898  1.00 20.13           C  
ATOM   1257  O   VAL A 167      24.005   5.092  22.778  1.00 19.22           O  
ATOM   1258  CB  VAL A 167      21.403   4.687  24.977  1.00 19.23           C  
ATOM   1259  CG1 VAL A 167      20.916   5.667  23.918  1.00 17.36           C  
ATOM   1260  CG2 VAL A 167      20.525   3.459  24.985  1.00 20.44           C  
ATOM   1261  N   ALA A 168      23.603   6.526  24.490  1.00 20.88           N  
ATOM   1262  CA  ALA A 168      24.235   7.685  23.877  1.00 21.84           C  
ATOM   1263  C   ALA A 168      25.016   7.272  22.637  1.00 21.95           C  
ATOM   1264  O   ALA A 168      24.489   7.308  21.526  1.00 22.22           O  
ATOM   1265  CB  ALA A 168      25.154   8.342  24.878  1.00 21.90           C  
ATOM   1266  N   SER A 169      26.264   6.863  22.834  1.00 23.04           N  
ATOM   1267  CA  SER A 169      27.105   6.432  21.721  1.00 24.29           C  
ATOM   1268  C   SER A 169      26.298   5.582  20.749  1.00 23.03           C  
ATOM   1269  O   SER A 169      25.992   6.019  19.637  1.00 22.06           O  
ATOM   1270  CB  SER A 169      28.309   5.616  22.221  1.00 24.74           C  
ATOM   1271  OG  SER A 169      28.870   4.820  21.184  1.00 24.08           O  
ATOM   1272  N   THR A 170      25.948   4.375  21.183  1.00 22.39           N  
ATOM   1273  CA  THR A 170      25.191   3.472  20.336  1.00 21.31           C  
ATOM   1274  C   THR A 170      24.184   4.280  19.562  1.00 22.07           C  
ATOM   1275  O   THR A 170      23.883   3.941  18.424  1.00 23.76           O  
ATOM   1276  CB  THR A 170      24.448   2.373  21.142  1.00 20.75           C  
ATOM   1277  OG1 THR A 170      25.256   1.190  21.182  1.00 19.61           O  
ATOM   1278  CG2 THR A 170      23.128   2.011  20.486  1.00 21.02           C  
ATOM   1279  N   PHE A 171      23.666   5.355  20.150  1.00 20.50           N  
ATOM   1280  CA  PHE A 171      22.690   6.149  19.423  1.00 18.90           C  
ATOM   1281  C   PHE A 171      23.343   7.063  18.386  1.00 19.74           C  
ATOM   1282  O   PHE A 171      23.157   6.900  17.176  1.00 19.55           O  
ATOM   1283  CB  PHE A 171      21.842   6.979  20.385  1.00 16.87           C  
ATOM   1284  CG  PHE A 171      20.846   7.872  19.691  1.00 14.27           C  
ATOM   1285  CD1 PHE A 171      19.681   7.339  19.138  1.00 12.81           C  
ATOM   1286  CD2 PHE A 171      21.076   9.247  19.579  1.00 12.21           C  
ATOM   1287  CE1 PHE A 171      18.758   8.158  18.486  1.00 10.63           C  
ATOM   1288  CE2 PHE A 171      20.155  10.073  18.928  1.00 10.35           C  
ATOM   1289  CZ  PHE A 171      18.993   9.521  18.381  1.00 10.19           C  
ATOM   1290  N   LYS A 172      24.121   8.017  18.871  1.00 20.93           N  
ATOM   1291  CA  LYS A 172      24.785   8.992  18.019  1.00 20.74           C  
ATOM   1292  C   LYS A 172      25.713   8.410  16.965  1.00 20.01           C  
ATOM   1293  O   LYS A 172      26.150   9.119  16.055  1.00 18.82           O  
ATOM   1294  CB  LYS A 172      25.539   9.972  18.904  1.00 22.23           C  
ATOM   1295  CG  LYS A 172      24.746  10.338  20.169  1.00 25.67           C  
ATOM   1296  CD  LYS A 172      25.369   9.751  21.437  1.00 24.77           C  
ATOM   1297  CE  LYS A 172      24.894  10.498  22.678  1.00 27.84           C  
ATOM   1298  NZ  LYS A 172      26.051  10.974  23.522  1.00 28.43           N  
ATOM   1299  N   VAL A 173      26.023   7.125  17.075  1.00 20.41           N  
ATOM   1300  CA  VAL A 173      26.903   6.523  16.081  1.00 20.20           C  
ATOM   1301  C   VAL A 173      26.078   6.101  14.865  1.00 17.67           C  
ATOM   1302  O   VAL A 173      26.588   6.035  13.747  1.00 17.27           O  
ATOM   1303  CB  VAL A 173      27.702   5.327  16.670  1.00 20.84           C  
ATOM   1304  CG1 VAL A 173      28.898   5.862  17.443  1.00 20.58           C  
ATOM   1305  CG2 VAL A 173      26.818   4.470  17.587  1.00 20.51           C  
ATOM   1306  N   LEU A 174      24.797   5.826  15.097  1.00 15.85           N  
ATOM   1307  CA  LEU A 174      23.897   5.474  14.008  1.00 14.29           C  
ATOM   1308  C   LEU A 174      23.280   6.801  13.569  1.00 14.49           C  
ATOM   1309  O   LEU A 174      23.060   7.047  12.382  1.00 12.32           O  
ATOM   1310  CB  LEU A 174      22.783   4.532  14.484  1.00 12.31           C  
ATOM   1311  CG  LEU A 174      22.917   3.886  15.854  1.00  8.83           C  
ATOM   1312  CD1 LEU A 174      21.570   3.404  16.375  1.00  5.86           C  
ATOM   1313  CD2 LEU A 174      23.884   2.748  15.726  1.00 11.47           C  
ATOM   1314  N   ARG A 175      23.017   7.648  14.557  1.00 13.87           N  
ATOM   1315  CA  ARG A 175      22.436   8.959  14.328  1.00 15.46           C  
ATOM   1316  C   ARG A 175      23.378   9.823  13.486  1.00 16.68           C  
ATOM   1317  O   ARG A 175      22.988  10.859  12.942  1.00 15.11           O  
ATOM   1318  CB  ARG A 175      22.169   9.636  15.673  1.00 16.87           C  
ATOM   1319  CG  ARG A 175      20.857  10.390  15.753  1.00 16.10           C  
ATOM   1320  CD  ARG A 175      21.110  11.883  15.915  1.00 17.42           C  
ATOM   1321  NE  ARG A 175      22.069  12.207  16.968  1.00 18.01           N  
ATOM   1322  CZ  ARG A 175      23.176  12.929  16.787  1.00 19.90           C  
ATOM   1323  NH1 ARG A 175      23.483  13.414  15.586  1.00 19.94           N  
ATOM   1324  NH2 ARG A 175      23.971  13.186  17.818  1.00 19.89           N  
ATOM   1325  N   ASN A 176      24.629   9.390  13.404  1.00 16.76           N  
ATOM   1326  CA  ASN A 176      25.620  10.097  12.623  1.00 17.65           C  
ATOM   1327  C   ASN A 176      25.767   9.352  11.308  1.00 18.39           C  
ATOM   1328  O   ASN A 176      26.232   9.916  10.320  1.00 19.13           O  
ATOM   1329  CB  ASN A 176      26.952  10.110  13.354  1.00 23.05           C  
ATOM   1330  CG  ASN A 176      27.135  11.334  14.238  1.00 26.46           C  
ATOM   1331  OD1 ASN A 176      26.624  12.421  13.933  1.00 26.92           O  
ATOM   1332  ND2 ASN A 176      27.875  11.163  15.351  1.00 26.44           N  
ATOM   1333  N   VAL A 177      25.379   8.074  11.307  1.00 17.58           N  
ATOM   1334  CA  VAL A 177      25.440   7.238  10.104  1.00 16.72           C  
ATOM   1335  C   VAL A 177      24.179   7.404   9.268  1.00 15.18           C  
ATOM   1336  O   VAL A 177      24.121   6.961   8.120  1.00 14.43           O  
ATOM   1337  CB  VAL A 177      25.608   5.741  10.430  1.00 18.18           C  
ATOM   1338  CG1 VAL A 177      24.927   4.877   9.352  1.00 17.88           C  
ATOM   1339  CG2 VAL A 177      27.080   5.402  10.491  1.00 17.27           C  
ATOM   1340  N   THR A 178      23.159   8.028   9.836  1.00 12.24           N  
ATOM   1341  CA  THR A 178      21.969   8.259   9.052  1.00 11.90           C  
ATOM   1342  C   THR A 178      22.094   9.610   8.385  1.00 12.95           C  
ATOM   1343  O   THR A 178      21.854   9.743   7.184  1.00 13.06           O  
ATOM   1344  CB  THR A 178      20.704   8.302   9.886  1.00 11.34           C  
ATOM   1345  OG1 THR A 178      21.050   8.290  11.274  1.00 12.79           O  
ATOM   1346  CG2 THR A 178      19.802   7.121   9.530  1.00 11.29           C  
ATOM   1347  N   VAL A 179      22.483  10.618   9.160  1.00 11.77           N  
ATOM   1348  CA  VAL A 179      22.583  11.968   8.621  1.00 11.55           C  
ATOM   1349  C   VAL A 179      23.534  12.082   7.446  1.00 13.27           C  
ATOM   1350  O   VAL A 179      23.323  12.893   6.543  1.00 11.90           O  
ATOM   1351  CB  VAL A 179      23.009  12.985   9.698  1.00  8.94           C  
ATOM   1352  CG1 VAL A 179      22.702  14.374   9.207  1.00  7.45           C  
ATOM   1353  CG2 VAL A 179      22.299  12.711  11.011  1.00  4.35           C  
ATOM   1354  N   VAL A 180      24.570  11.255   7.454  1.00 13.79           N  
ATOM   1355  CA  VAL A 180      25.564  11.291   6.397  1.00 17.34           C  
ATOM   1356  C   VAL A 180      25.220  10.428   5.214  1.00 17.52           C  
ATOM   1357  O   VAL A 180      25.244  10.873   4.068  1.00 16.65           O  
ATOM   1358  CB  VAL A 180      26.931  10.806   6.895  1.00 18.96           C  
ATOM   1359  CG1 VAL A 180      27.987  11.039   5.806  1.00 18.25           C  
ATOM   1360  CG2 VAL A 180      27.296  11.520   8.190  1.00 22.76           C  
ATOM   1361  N   LEU A 181      24.922   9.170   5.507  1.00 17.20           N  
ATOM   1362  CA  LEU A 181      24.618   8.204   4.471  1.00 14.02           C  
ATOM   1363  C   LEU A 181      23.366   8.523   3.703  1.00 14.30           C  
ATOM   1364  O   LEU A 181      23.345   8.417   2.482  1.00 14.88           O  
ATOM   1365  CB  LEU A 181      24.516   6.822   5.076  1.00 10.39           C  
ATOM   1366  CG  LEU A 181      24.892   5.720   4.091  1.00 10.34           C  
ATOM   1367  CD1 LEU A 181      26.070   6.123   3.225  1.00  7.01           C  
ATOM   1368  CD2 LEU A 181      25.180   4.458   4.896  1.00 11.22           C  
ATOM   1369  N   TRP A 182      22.331   8.932   4.421  1.00 14.31           N  
ATOM   1370  CA  TRP A 182      21.054   9.255   3.801  1.00 13.41           C  
ATOM   1371  C   TRP A 182      21.134  10.476   2.892  1.00 13.20           C  
ATOM   1372  O   TRP A 182      20.744  10.409   1.720  1.00 12.06           O  
ATOM   1373  CB  TRP A 182      19.986   9.485   4.878  1.00 11.94           C  
ATOM   1374  CG  TRP A 182      19.466   8.203   5.541  1.00 11.29           C  
ATOM   1375  CD1 TRP A 182      20.151   7.030   5.756  1.00 11.42           C  
ATOM   1376  CD2 TRP A 182      18.154   7.991   6.074  1.00  9.48           C  
ATOM   1377  NE1 TRP A 182      19.347   6.117   6.383  1.00  7.18           N  
ATOM   1378  CE2 TRP A 182      18.119   6.682   6.587  1.00  7.34           C  
ATOM   1379  CE3 TRP A 182      17.006   8.790   6.163  1.00  8.31           C  
ATOM   1380  CZ2 TRP A 182      16.984   6.155   7.177  1.00  8.63           C  
ATOM   1381  CZ3 TRP A 182      15.888   8.267   6.746  1.00  6.13           C  
ATOM   1382  CH2 TRP A 182      15.877   6.963   7.247  1.00  8.69           C  
ATOM   1383  N   SER A 183      21.646  11.584   3.431  1.00 12.01           N  
ATOM   1384  CA  SER A 183      21.747  12.843   2.685  1.00 10.61           C  
ATOM   1385  C   SER A 183      22.444  12.751   1.335  1.00 10.32           C  
ATOM   1386  O   SER A 183      22.552  13.746   0.631  1.00 11.49           O  
ATOM   1387  CB  SER A 183      22.459  13.903   3.529  1.00 10.52           C  
ATOM   1388  OG  SER A 183      21.648  14.359   4.594  1.00  9.59           O  
ATOM   1389  N   ALA A 184      22.917  11.566   0.971  1.00  8.37           N  
ATOM   1390  CA  ALA A 184      23.613  11.402  -0.296  1.00  6.43           C  
ATOM   1391  C   ALA A 184      22.688  11.128  -1.475  1.00  5.87           C  
ATOM   1392  O   ALA A 184      22.996  11.490  -2.606  1.00  5.20           O  
ATOM   1393  CB  ALA A 184      24.637  10.290  -0.168  1.00  5.05           C  
ATOM   1394  N   TYR A 185      21.545  10.501  -1.199  1.00  6.14           N  
ATOM   1395  CA  TYR A 185      20.572  10.122  -2.228  1.00  4.57           C  
ATOM   1396  C   TYR A 185      20.057  11.228  -3.125  1.00  4.18           C  
ATOM   1397  O   TYR A 185      20.094  11.103  -4.351  1.00  2.00           O  
ATOM   1398  CB  TYR A 185      19.406   9.417  -1.573  1.00  4.43           C  
ATOM   1399  CG  TYR A 185      19.796   8.098  -0.971  1.00  4.81           C  
ATOM   1400  CD1 TYR A 185      19.980   6.979  -1.775  1.00  3.48           C  
ATOM   1401  CD2 TYR A 185      19.947   7.954   0.405  1.00  5.88           C  
ATOM   1402  CE1 TYR A 185      20.290   5.739  -1.234  1.00  4.16           C  
ATOM   1403  CE2 TYR A 185      20.259   6.713   0.962  1.00  6.58           C  
ATOM   1404  CZ  TYR A 185      20.427   5.613   0.132  1.00  5.49           C  
ATOM   1405  OH  TYR A 185      20.707   4.391   0.678  1.00  4.67           O  
ATOM   1406  N   PRO A 186      19.532  12.317  -2.530  1.00  6.33           N  
ATOM   1407  CA  PRO A 186      19.039  13.396  -3.398  1.00  5.88           C  
ATOM   1408  C   PRO A 186      20.132  13.858  -4.364  1.00  4.78           C  
ATOM   1409  O   PRO A 186      19.862  14.174  -5.520  1.00  2.55           O  
ATOM   1410  CB  PRO A 186      18.615  14.504  -2.420  1.00  2.62           C  
ATOM   1411  CG  PRO A 186      18.973  14.045  -1.057  1.00  2.00           C  
ATOM   1412  CD  PRO A 186      19.328  12.598  -1.092  1.00  5.72           C  
ATOM   1413  N   VAL A 187      21.369  13.841  -3.857  1.00  7.02           N  
ATOM   1414  CA  VAL A 187      22.589  14.261  -4.562  1.00  8.44           C  
ATOM   1415  C   VAL A 187      23.028  13.465  -5.783  1.00 10.55           C  
ATOM   1416  O   VAL A 187      23.663  14.018  -6.687  1.00  9.04           O  
ATOM   1417  CB  VAL A 187      23.757  14.262  -3.616  1.00  6.80           C  
ATOM   1418  CG1 VAL A 187      24.814  15.194  -4.125  1.00  3.82           C  
ATOM   1419  CG2 VAL A 187      23.288  14.643  -2.236  1.00  8.22           C  
ATOM   1420  N   VAL A 188      22.720  12.162  -5.774  1.00 11.55           N  
ATOM   1421  CA  VAL A 188      23.031  11.227  -6.866  1.00 10.63           C  
ATOM   1422  C   VAL A 188      21.820  11.158  -7.785  1.00 10.11           C  
ATOM   1423  O   VAL A 188      21.942  11.250  -8.998  1.00  9.85           O  
ATOM   1424  CB  VAL A 188      23.249   9.802  -6.351  1.00 10.12           C  
ATOM   1425  CG1 VAL A 188      23.880   8.968  -7.418  1.00 11.31           C  
ATOM   1426  CG2 VAL A 188      24.071   9.820  -5.093  1.00  8.03           C  
ATOM   1427  N   TRP A 189      20.652  10.968  -7.175  1.00 10.03           N  
ATOM   1428  CA  TRP A 189      19.388  10.887  -7.890  1.00 10.31           C  
ATOM   1429  C   TRP A 189      19.323  12.163  -8.716  1.00 10.43           C  
ATOM   1430  O   TRP A 189      18.837  12.166  -9.849  1.00  9.14           O  
ATOM   1431  CB  TRP A 189      18.226  10.837  -6.868  1.00 12.54           C  
ATOM   1432  CG  TRP A 189      16.814  10.540  -7.416  1.00 12.53           C  
ATOM   1433  CD1 TRP A 189      16.151   9.353  -7.349  1.00 12.91           C  
ATOM   1434  CD2 TRP A 189      15.924  11.452  -8.096  1.00 13.58           C  
ATOM   1435  NE1 TRP A 189      14.913   9.460  -7.937  1.00 14.93           N  
ATOM   1436  CE2 TRP A 189      14.750  10.738  -8.405  1.00 13.61           C  
ATOM   1437  CE3 TRP A 189      16.014  12.807  -8.472  1.00 14.05           C  
ATOM   1438  CZ2 TRP A 189      13.671  11.318  -9.071  1.00 15.34           C  
ATOM   1439  CZ3 TRP A 189      14.939  13.390  -9.136  1.00 13.28           C  
ATOM   1440  CH2 TRP A 189      13.784  12.644  -9.427  1.00 18.06           C  
ATOM   1441  N   LEU A 190      19.837  13.237  -8.117  1.00  9.87           N  
ATOM   1442  CA  LEU A 190      19.880  14.574  -8.702  1.00  8.02           C  
ATOM   1443  C   LEU A 190      20.571  14.679 -10.063  1.00  8.52           C  
ATOM   1444  O   LEU A 190      20.057  15.341 -10.968  1.00  7.04           O  
ATOM   1445  CB  LEU A 190      20.573  15.506  -7.712  1.00  8.63           C  
ATOM   1446  CG  LEU A 190      20.754  17.003  -7.977  1.00  8.82           C  
ATOM   1447  CD1 LEU A 190      19.496  17.613  -8.544  1.00  7.71           C  
ATOM   1448  CD2 LEU A 190      21.120  17.670  -6.671  1.00  7.47           C  
ATOM   1449  N   ILE A 191      21.736  14.036 -10.190  1.00  8.78           N  
ATOM   1450  CA  ILE A 191      22.551  14.051 -11.413  1.00  9.31           C  
ATOM   1451  C   ILE A 191      22.703  12.680 -12.048  1.00 10.03           C  
ATOM   1452  O   ILE A 191      23.364  12.525 -13.079  1.00  8.96           O  
ATOM   1453  CB  ILE A 191      24.000  14.544 -11.134  1.00  7.99           C  
ATOM   1454  CG1 ILE A 191      24.388  14.236  -9.682  1.00  7.37           C  
ATOM   1455  CG2 ILE A 191      24.127  16.022 -11.464  1.00  6.55           C  
ATOM   1456  CD1 ILE A 191      24.714  12.768  -9.419  1.00  6.66           C  
ATOM   1457  N   GLY A 192      22.109  11.682 -11.414  1.00 12.61           N  
ATOM   1458  CA  GLY A 192      22.218  10.321 -11.901  1.00 15.07           C  
ATOM   1459  C   GLY A 192      21.769  10.084 -13.325  1.00 16.72           C  
ATOM   1460  O   GLY A 192      22.178  10.790 -14.247  1.00 18.19           O  
ATOM   1461  N   SER A 193      20.928   9.073 -13.499  1.00 16.74           N  
ATOM   1462  CA  SER A 193      20.431   8.716 -14.813  1.00 17.31           C  
ATOM   1463  C   SER A 193      19.128   9.419 -15.107  1.00 17.17           C  
ATOM   1464  O   SER A 193      18.620   9.357 -16.232  1.00 17.33           O  
ATOM   1465  CB  SER A 193      20.198   7.217 -14.900  1.00 15.57           C  
ATOM   1466  OG  SER A 193      19.225   6.939 -15.883  1.00 13.73           O  
ATOM   1467  N   GLU A 194      18.589  10.094 -14.098  1.00 15.59           N  
ATOM   1468  CA  GLU A 194      17.314  10.773 -14.265  1.00 14.73           C  
ATOM   1469  C   GLU A 194      17.350  12.238 -13.890  1.00 13.10           C  
ATOM   1470  O   GLU A 194      16.433  12.994 -14.172  1.00 13.29           O  
ATOM   1471  CB  GLU A 194      16.249  10.043 -13.452  1.00 14.78           C  
ATOM   1472  CG  GLU A 194      16.800   8.993 -12.518  1.00 14.30           C  
ATOM   1473  CD  GLU A 194      16.742   9.474 -11.105  1.00 15.97           C  
ATOM   1474  OE1 GLU A 194      15.996  10.456 -10.872  1.00 16.02           O  
ATOM   1475  OE2 GLU A 194      17.431   8.887 -10.239  1.00 15.61           O  
ATOM   1476  N   GLY A 195      18.422  12.642 -13.244  1.00 14.47           N  
ATOM   1477  CA  GLY A 195      18.528  14.029 -12.871  1.00 11.78           C  
ATOM   1478  C   GLY A 195      19.024  14.798 -14.060  1.00 10.51           C  
ATOM   1479  O   GLY A 195      18.239  15.195 -14.914  1.00 10.21           O  
ATOM   1480  N   ALA A 196      20.339  14.965 -14.130  1.00  9.28           N  
ATOM   1481  CA  ALA A 196      20.964  15.737 -15.195  1.00  9.76           C  
ATOM   1482  C   ALA A 196      21.528  14.925 -16.325  1.00  8.38           C  
ATOM   1483  O   ALA A 196      21.798  15.449 -17.402  1.00  8.52           O  
ATOM   1484  CB  ALA A 196      22.059  16.604 -14.617  1.00 10.20           C  
ATOM   1485  N   GLY A 197      21.725  13.646 -16.091  1.00  9.38           N  
ATOM   1486  CA  GLY A 197      22.291  12.844 -17.149  1.00 13.05           C  
ATOM   1487  C   GLY A 197      23.799  12.974 -17.146  1.00 14.44           C  
ATOM   1488  O   GLY A 197      24.476  12.765 -18.159  1.00 14.55           O  
ATOM   1489  N   ILE A 198      24.323  13.348 -15.991  1.00 14.29           N  
ATOM   1490  CA  ILE A 198      25.747  13.468 -15.838  1.00 14.92           C  
ATOM   1491  C   ILE A 198      26.189  12.008 -15.665  1.00 16.08           C  
ATOM   1492  O   ILE A 198      26.433  11.309 -16.656  1.00 15.66           O  
ATOM   1493  CB  ILE A 198      26.095  14.292 -14.589  1.00 14.74           C  
ATOM   1494  CG1 ILE A 198      25.030  15.352 -14.358  1.00 13.76           C  
ATOM   1495  CG2 ILE A 198      27.434  14.988 -14.768  1.00 15.21           C  
ATOM   1496  CD1 ILE A 198      25.131  16.512 -15.294  1.00 12.62           C  
ATOM   1497  N   VAL A 199      26.249  11.538 -14.420  1.00 14.65           N  
ATOM   1498  CA  VAL A 199      26.676  10.167 -14.139  1.00 13.22           C  
ATOM   1499  C   VAL A 199      25.672   9.126 -14.628  1.00 15.62           C  
ATOM   1500  O   VAL A 199      24.540   9.078 -14.148  1.00 15.94           O  
ATOM   1501  CB  VAL A 199      26.864   9.923 -12.620  1.00 11.11           C  
ATOM   1502  CG1 VAL A 199      28.177   9.224 -12.359  1.00 10.02           C  
ATOM   1503  CG2 VAL A 199      26.785  11.222 -11.863  1.00  8.62           C  
ATOM   1504  N   PRO A 200      26.049   8.306 -15.620  1.00 17.43           N  
ATOM   1505  CA  PRO A 200      25.128   7.275 -16.118  1.00 18.44           C  
ATOM   1506  C   PRO A 200      24.976   6.103 -15.144  1.00 19.22           C  
ATOM   1507  O   PRO A 200      25.826   5.880 -14.266  1.00 18.32           O  
ATOM   1508  CB  PRO A 200      25.742   6.845 -17.450  1.00 18.33           C  
ATOM   1509  CG  PRO A 200      26.758   7.919 -17.771  1.00 19.87           C  
ATOM   1510  CD  PRO A 200      27.276   8.349 -16.421  1.00 18.23           C  
ATOM   1511  N   LEU A 201      23.882   5.359 -15.324  1.00 19.13           N  
ATOM   1512  CA  LEU A 201      23.528   4.211 -14.479  1.00 17.56           C  
ATOM   1513  C   LEU A 201      24.676   3.403 -13.851  1.00 17.61           C  
ATOM   1514  O   LEU A 201      24.801   3.366 -12.624  1.00 16.03           O  
ATOM   1515  CB  LEU A 201      22.588   3.272 -15.249  1.00 15.73           C  
ATOM   1516  CG  LEU A 201      21.137   3.766 -15.355  1.00 14.51           C  
ATOM   1517  CD1 LEU A 201      20.304   2.795 -16.181  1.00 14.31           C  
ATOM   1518  CD2 LEU A 201      20.537   3.901 -13.959  1.00 16.74           C  
ATOM   1519  N   ASN A 202      25.505   2.773 -14.690  1.00 16.31           N  
ATOM   1520  CA  ASN A 202      26.626   1.946 -14.230  1.00 14.07           C  
ATOM   1521  C   ASN A 202      27.244   2.444 -12.923  1.00 14.24           C  
ATOM   1522  O   ASN A 202      27.194   1.761 -11.900  1.00 13.78           O  
ATOM   1523  CB  ASN A 202      27.714   1.855 -15.311  1.00 11.83           C  
ATOM   1524  CG  ASN A 202      27.171   2.062 -16.716  1.00 10.73           C  
ATOM   1525  OD1 ASN A 202      25.987   1.859 -16.978  1.00  9.20           O  
ATOM   1526  ND2 ASN A 202      28.043   2.469 -17.629  1.00  9.96           N  
ATOM   1527  N   ILE A 203      27.810   3.643 -12.957  1.00 14.52           N  
ATOM   1528  CA  ILE A 203      28.448   4.217 -11.778  1.00 14.66           C  
ATOM   1529  C   ILE A 203      27.432   4.598 -10.697  1.00 15.82           C  
ATOM   1530  O   ILE A 203      27.647   4.353  -9.504  1.00 14.19           O  
ATOM   1531  CB  ILE A 203      29.254   5.458 -12.170  1.00 12.62           C  
ATOM   1532  CG1 ILE A 203      29.444   5.500 -13.696  1.00 10.77           C  
ATOM   1533  CG2 ILE A 203      30.567   5.443 -11.471  1.00 12.73           C  
ATOM   1534  CD1 ILE A 203      30.622   4.681 -14.240  1.00  7.12           C  
ATOM   1535  N   GLU A 204      26.324   5.200 -11.134  1.00 16.04           N  
ATOM   1536  CA  GLU A 204      25.267   5.613 -10.227  1.00 14.29           C  
ATOM   1537  C   GLU A 204      24.852   4.401  -9.457  1.00 15.49           C  
ATOM   1538  O   GLU A 204      25.002   4.348  -8.240  1.00 16.37           O  
ATOM   1539  CB  GLU A 204      24.045   6.109 -10.979  1.00 14.23           C  
ATOM   1540  CG  GLU A 204      22.931   6.569 -10.046  1.00 12.85           C  
ATOM   1541  CD  GLU A 204      21.543   6.415 -10.630  1.00 13.27           C  
ATOM   1542  OE1 GLU A 204      21.403   6.446 -11.872  1.00 13.41           O  
ATOM   1543  OE2 GLU A 204      20.587   6.267  -9.836  1.00 12.78           O  
ATOM   1544  N   THR A 205      24.318   3.425 -10.185  1.00 14.94           N  
ATOM   1545  CA  THR A 205      23.857   2.176  -9.584  1.00 13.74           C  
ATOM   1546  C   THR A 205      24.820   1.661  -8.504  1.00 15.01           C  
ATOM   1547  O   THR A 205      24.365   1.079  -7.502  1.00 12.97           O  
ATOM   1548  CB  THR A 205      23.670   1.064 -10.647  1.00 12.71           C  
ATOM   1549  OG1 THR A 205      23.051   1.607 -11.820  1.00  8.29           O  
ATOM   1550  CG2 THR A 205      22.824  -0.068 -10.080  1.00  8.92           C  
ATOM   1551  N   LEU A 206      26.132   1.866  -8.702  1.00 13.33           N  
ATOM   1552  CA  LEU A 206      27.110   1.410  -7.714  1.00 11.78           C  
ATOM   1553  C   LEU A 206      27.155   2.396  -6.587  1.00 10.50           C  
ATOM   1554  O   LEU A 206      27.295   2.040  -5.419  1.00 10.06           O  
ATOM   1555  CB  LEU A 206      28.514   1.302  -8.281  1.00 13.56           C  
ATOM   1556  CG  LEU A 206      29.534   1.374  -7.131  1.00 13.89           C  
ATOM   1557  CD1 LEU A 206      29.607   0.049  -6.367  1.00 13.34           C  
ATOM   1558  CD2 LEU A 206      30.870   1.767  -7.698  1.00 15.51           C  
ATOM   1559  N   LEU A 207      27.073   3.656  -6.951  1.00 10.57           N  
ATOM   1560  CA  LEU A 207      27.077   4.683  -5.948  1.00 10.28           C  
ATOM   1561  C   LEU A 207      25.908   4.358  -5.049  1.00 10.37           C  
ATOM   1562  O   LEU A 207      25.958   4.559  -3.836  1.00 11.49           O  
ATOM   1563  CB  LEU A 207      26.867   6.031  -6.614  1.00  9.94           C  
ATOM   1564  CG  LEU A 207      28.217   6.603  -6.950  1.00  9.34           C  
ATOM   1565  CD1 LEU A 207      28.079   7.896  -7.710  1.00 11.02           C  
ATOM   1566  CD2 LEU A 207      28.945   6.786  -5.638  1.00  9.81           C  
ATOM   1567  N   PHE A 208      24.859   3.827  -5.666  1.00  9.98           N  
ATOM   1568  CA  PHE A 208      23.642   3.510  -4.958  1.00  8.63           C  
ATOM   1569  C   PHE A 208      23.673   2.295  -4.050  1.00  9.30           C  
ATOM   1570  O   PHE A 208      23.033   2.319  -3.008  1.00 11.34           O  
ATOM   1571  CB  PHE A 208      22.487   3.409  -5.958  1.00  9.62           C  
ATOM   1572  CG  PHE A 208      21.502   4.570  -5.878  1.00  9.45           C  
ATOM   1573  CD1 PHE A 208      21.012   5.008  -4.653  1.00  4.20           C  
ATOM   1574  CD2 PHE A 208      21.083   5.230  -7.034  1.00 10.57           C  
ATOM   1575  CE1 PHE A 208      20.148   6.063  -4.584  1.00  4.52           C  
ATOM   1576  CE2 PHE A 208      20.206   6.303  -6.959  1.00  9.95           C  
ATOM   1577  CZ  PHE A 208      19.740   6.713  -5.729  1.00  7.62           C  
ATOM   1578  N   MET A 209      24.406   1.240  -4.411  1.00 10.51           N  
ATOM   1579  CA  MET A 209      24.469   0.048  -3.549  1.00 10.12           C  
ATOM   1580  C   MET A 209      25.395   0.178  -2.331  1.00 10.05           C  
ATOM   1581  O   MET A 209      25.107  -0.400  -1.282  1.00  9.31           O  
ATOM   1582  CB  MET A 209      24.866  -1.188  -4.351  1.00  9.96           C  
ATOM   1583  CG  MET A 209      24.946  -2.474  -3.504  1.00  8.90           C  
ATOM   1584  SD  MET A 209      26.404  -2.596  -2.416  1.00  6.42           S  
ATOM   1585  CE  MET A 209      27.751  -2.381  -3.576  1.00  4.32           C  
ATOM   1586  N   VAL A 210      26.503   0.914  -2.469  1.00 12.02           N  
ATOM   1587  CA  VAL A 210      27.430   1.132  -1.343  1.00 13.01           C  
ATOM   1588  C   VAL A 210      26.711   2.010  -0.354  1.00 12.23           C  
ATOM   1589  O   VAL A 210      27.013   2.011   0.836  1.00 10.77           O  
ATOM   1590  CB  VAL A 210      28.721   1.904  -1.726  1.00 12.86           C  
ATOM   1591  CG1 VAL A 210      29.789   0.946  -2.174  1.00 14.88           C  
ATOM   1592  CG2 VAL A 210      28.419   2.933  -2.794  1.00 14.39           C  
ATOM   1593  N   LEU A 211      25.765   2.770  -0.890  1.00 11.81           N  
ATOM   1594  CA  LEU A 211      24.948   3.685  -0.124  1.00 13.66           C  
ATOM   1595  C   LEU A 211      23.912   2.892   0.651  1.00 11.20           C  
ATOM   1596  O   LEU A 211      23.592   3.208   1.793  1.00 11.13           O  
ATOM   1597  CB  LEU A 211      24.280   4.684  -1.083  1.00 15.97           C  
ATOM   1598  CG  LEU A 211      25.130   5.947  -1.316  1.00 18.15           C  
ATOM   1599  CD1 LEU A 211      24.450   6.920  -2.285  1.00 16.22           C  
ATOM   1600  CD2 LEU A 211      25.359   6.608   0.041  1.00 19.77           C  
ATOM   1601  N   ASP A 212      23.416   1.841   0.019  1.00  9.72           N  
ATOM   1602  CA  ASP A 212      22.419   0.985   0.626  1.00  9.36           C  
ATOM   1603  C   ASP A 212      23.055   0.150   1.734  1.00 10.61           C  
ATOM   1604  O   ASP A 212      22.800   0.389   2.909  1.00  9.32           O  
ATOM   1605  CB  ASP A 212      21.799   0.070  -0.441  1.00 12.19           C  
ATOM   1606  CG  ASP A 212      20.432   0.568  -0.939  1.00 15.17           C  
ATOM   1607  OD1 ASP A 212      19.550   0.820  -0.094  1.00 16.62           O  
ATOM   1608  OD2 ASP A 212      20.235   0.706  -2.172  1.00 14.65           O  
ATOM   1609  N   VAL A 213      23.885  -0.824   1.358  1.00 11.05           N  
ATOM   1610  CA  VAL A 213      24.548  -1.704   2.327  1.00 11.02           C  
ATOM   1611  C   VAL A 213      25.026  -0.959   3.555  1.00 12.14           C  
ATOM   1612  O   VAL A 213      24.565  -1.224   4.663  1.00 11.87           O  
ATOM   1613  CB  VAL A 213      25.759  -2.411   1.720  1.00 10.14           C  
ATOM   1614  CG1 VAL A 213      25.311  -3.495   0.775  1.00  9.64           C  
ATOM   1615  CG2 VAL A 213      26.605  -1.423   1.004  1.00  9.76           C  
ATOM   1616  N   SER A 214      25.952  -0.019   3.360  1.00 14.39           N  
ATOM   1617  CA  SER A 214      26.488   0.768   4.478  1.00 15.82           C  
ATOM   1618  C   SER A 214      25.340   1.347   5.279  1.00 15.76           C  
ATOM   1619  O   SER A 214      25.540   1.918   6.345  1.00 16.35           O  
ATOM   1620  CB  SER A 214      27.379   1.909   3.978  1.00 16.40           C  
ATOM   1621  OG  SER A 214      26.633   2.807   3.184  1.00 16.98           O  
ATOM   1622  N   ALA A 215      24.136   1.202   4.750  1.00 14.78           N  
ATOM   1623  CA  ALA A 215      22.976   1.706   5.428  1.00 15.77           C  
ATOM   1624  C   ALA A 215      22.216   0.568   6.143  1.00 17.20           C  
ATOM   1625  O   ALA A 215      21.629   0.797   7.197  1.00 18.54           O  
ATOM   1626  CB  ALA A 215      22.070   2.448   4.426  1.00 15.39           C  
ATOM   1627  N   LYS A 216      22.232  -0.648   5.595  1.00 15.38           N  
ATOM   1628  CA  LYS A 216      21.517  -1.785   6.207  1.00 14.17           C  
ATOM   1629  C   LYS A 216      22.436  -2.864   6.781  1.00 14.89           C  
ATOM   1630  O   LYS A 216      22.705  -2.867   7.989  1.00 16.64           O  
ATOM   1631  CB  LYS A 216      20.511  -2.403   5.237  1.00 13.40           C  
ATOM   1632  CG  LYS A 216      19.407  -1.445   4.809  1.00  9.68           C  
ATOM   1633  CD  LYS A 216      19.396  -1.249   3.317  1.00  3.51           C  
ATOM   1634  CE  LYS A 216      17.958  -1.157   2.856  1.00  2.71           C  
ATOM   1635  NZ  LYS A 216      17.648   0.094   2.148  1.00  2.00           N  
ATOM   1636  N   VAL A 217      22.907  -3.785   5.938  1.00 13.18           N  
ATOM   1637  CA  VAL A 217      23.823  -4.830   6.419  1.00 13.49           C  
ATOM   1638  C   VAL A 217      24.655  -4.256   7.567  1.00 14.42           C  
ATOM   1639  O   VAL A 217      24.524  -4.672   8.714  1.00 13.02           O  
ATOM   1640  CB  VAL A 217      24.787  -5.299   5.308  1.00 11.92           C  
ATOM   1641  CG1 VAL A 217      24.177  -6.457   4.588  1.00 10.22           C  
ATOM   1642  CG2 VAL A 217      25.070  -4.167   4.334  1.00  7.35           C  
ATOM   1643  N   GLY A 218      25.484  -3.274   7.230  1.00 15.10           N  
ATOM   1644  CA  GLY A 218      26.301  -2.621   8.218  1.00 16.35           C  
ATOM   1645  C   GLY A 218      25.470  -2.049   9.357  1.00 18.81           C  
ATOM   1646  O   GLY A 218      25.686  -2.411  10.522  1.00 20.15           O  
ATOM   1647  N   PHE A 219      24.522  -1.165   9.048  1.00 18.68           N  
ATOM   1648  CA  PHE A 219      23.692  -0.571  10.095  1.00 18.47           C  
ATOM   1649  C   PHE A 219      23.380  -1.582  11.187  1.00 19.86           C  
ATOM   1650  O   PHE A 219      24.073  -1.637  12.206  1.00 20.27           O  
ATOM   1651  CB  PHE A 219      22.374  -0.062   9.535  1.00 15.86           C  
ATOM   1652  CG  PHE A 219      21.601   0.779  10.501  1.00 13.04           C  
ATOM   1653  CD1 PHE A 219      20.893   0.196  11.532  1.00 10.68           C  
ATOM   1654  CD2 PHE A 219      21.591   2.159  10.380  1.00 14.28           C  
ATOM   1655  CE1 PHE A 219      20.193   0.977  12.432  1.00 12.77           C  
ATOM   1656  CE2 PHE A 219      20.892   2.954  11.276  1.00 12.62           C  
ATOM   1657  CZ  PHE A 219      20.192   2.365  12.301  1.00 13.03           C  
ATOM   1658  N   GLY A 220      22.332  -2.371  10.965  1.00 19.57           N  
ATOM   1659  CA  GLY A 220      21.933  -3.382  11.929  1.00 19.68           C  
ATOM   1660  C   GLY A 220      23.084  -3.913  12.769  1.00 20.42           C  
ATOM   1661  O   GLY A 220      22.959  -4.011  13.994  1.00 20.85           O  
ATOM   1662  N   LEU A 221      24.204  -4.260  12.134  1.00 19.21           N  
ATOM   1663  CA  LEU A 221      25.344  -4.741  12.905  1.00 17.66           C  
ATOM   1664  C   LEU A 221      25.692  -3.645  13.901  1.00 15.82           C  
ATOM   1665  O   LEU A 221      25.578  -3.850  15.107  1.00 14.41           O  
ATOM   1666  CB  LEU A 221      26.575  -5.000  12.028  1.00 18.63           C  
ATOM   1667  CG  LEU A 221      26.493  -5.353  10.541  1.00 19.06           C  
ATOM   1668  CD1 LEU A 221      27.908  -5.462  10.023  1.00 20.06           C  
ATOM   1669  CD2 LEU A 221      25.750  -6.664  10.312  1.00 19.22           C  
ATOM   1670  N   ILE A 222      26.090  -2.481  13.380  1.00 13.62           N  
ATOM   1671  CA  ILE A 222      26.478  -1.329  14.194  1.00 13.08           C  
ATOM   1672  C   ILE A 222      25.587  -1.146  15.428  1.00 14.91           C  
ATOM   1673  O   ILE A 222      25.902  -0.361  16.331  1.00 14.97           O  
ATOM   1674  CB  ILE A 222      26.492  -0.004  13.332  1.00 11.20           C  
ATOM   1675  CG1 ILE A 222      27.836   0.133  12.610  1.00 11.61           C  
ATOM   1676  CG2 ILE A 222      26.329   1.237  14.208  1.00  7.76           C  
ATOM   1677  CD1 ILE A 222      28.027   1.462  11.884  1.00 12.24           C  
ATOM   1678  N   LEU A 223      24.480  -1.880  15.477  1.00 16.20           N  
ATOM   1679  CA  LEU A 223      23.560  -1.778  16.600  1.00 17.24           C  
ATOM   1680  C   LEU A 223      23.454  -3.058  17.453  1.00 19.30           C  
ATOM   1681  O   LEU A 223      23.821  -3.049  18.637  1.00 19.02           O  
ATOM   1682  CB  LEU A 223      22.173  -1.360  16.084  1.00 13.97           C  
ATOM   1683  CG  LEU A 223      20.894  -1.903  16.746  1.00 11.66           C  
ATOM   1684  CD1 LEU A 223      20.901  -1.639  18.256  1.00 11.47           C  
ATOM   1685  CD2 LEU A 223      19.687  -1.240  16.088  1.00 10.05           C  
ATOM   1686  N   LEU A 224      22.959  -4.149  16.863  1.00 20.13           N  
ATOM   1687  CA  LEU A 224      22.775  -5.407  17.606  1.00 21.59           C  
ATOM   1688  C   LEU A 224      24.042  -5.958  18.270  1.00 21.04           C  
ATOM   1689  O   LEU A 224      23.955  -6.772  19.191  1.00 20.69           O  
ATOM   1690  CB  LEU A 224      22.142  -6.469  16.705  1.00 21.44           C  
ATOM   1691  CG  LEU A 224      21.677  -5.887  15.374  1.00 19.48           C  
ATOM   1692  CD1 LEU A 224      22.209  -6.740  14.245  1.00 19.21           C  
ATOM   1693  CD2 LEU A 224      20.165  -5.797  15.348  1.00 19.85           C  
ATOM   1694  N   ARG A 225      25.211  -5.526  17.806  1.00 20.57           N  
ATOM   1695  CA  ARG A 225      26.451  -5.967  18.428  1.00 20.38           C  
ATOM   1696  C   ARG A 225      26.403  -5.290  19.792  1.00 20.39           C  
ATOM   1697  O   ARG A 225      26.734  -5.882  20.821  1.00 20.27           O  
ATOM   1698  CB  ARG A 225      27.666  -5.466  17.635  1.00 21.79           C  
ATOM   1699  CG  ARG A 225      29.055  -5.789  18.247  1.00 24.55           C  
ATOM   1700  CD  ARG A 225      30.039  -6.363  17.197  1.00 23.77           C  
ATOM   1701  NE  ARG A 225      31.327  -6.756  17.764  1.00 20.98           N  
ATOM   1702  CZ  ARG A 225      32.371  -5.939  17.879  1.00 22.21           C  
ATOM   1703  NH1 ARG A 225      32.275  -4.680  17.466  1.00 22.97           N  
ATOM   1704  NH2 ARG A 225      33.526  -6.382  18.375  1.00 21.28           N  
ATOM   1705  N   SER A 226      25.959  -4.040  19.785  1.00 18.43           N  
ATOM   1706  CA  SER A 226      25.863  -3.261  21.011  1.00 18.43           C  
ATOM   1707  C   SER A 226      24.651  -3.645  21.805  1.00 16.42           C  
ATOM   1708  O   SER A 226      23.758  -4.314  21.296  1.00 15.70           O  
ATOM   1709  CB  SER A 226      25.766  -1.764  20.694  1.00 20.78           C  
ATOM   1710  OG  SER A 226      24.526  -1.228  21.144  1.00 20.87           O  
ATOM   1711  N   ARG A 227      24.622  -3.195  23.055  1.00 16.85           N  
ATOM   1712  CA  ARG A 227      23.495  -3.456  23.933  1.00 15.77           C  
ATOM   1713  C   ARG A 227      22.425  -2.417  23.646  1.00 16.00           C  
ATOM   1714  O   ARG A 227      22.766  -1.347  23.085  1.00 14.27           O  
ATOM   1715  CB  ARG A 227      23.914  -3.370  25.404  1.00 17.47           C  
ATOM   1716  CG  ARG A 227      24.947  -4.402  25.805  1.00 16.63           C  
ATOM   1717  CD  ARG A 227      26.326  -3.882  25.491  1.00 17.29           C  
ATOM   1718  NE  ARG A 227      27.181  -3.920  26.673  1.00 20.13           N  
ATOM   1719  CZ  ARG A 227      27.827  -2.870  27.176  1.00 21.31           C  
ATOM   1720  NH1 ARG A 227      27.719  -1.679  26.595  1.00 21.64           N  
ATOM   1721  NH2 ARG A 227      28.589  -3.015  28.257  1.00 21.26           N  
TER    1722      ARG A 227                                                      
HETATM 1723  C1  RET A 249A     15.058   9.967  -3.477  1.00  5.21           C  
HETATM 1724  C2  RET A 249A     14.337  10.668  -4.621  1.00  5.79           C  
HETATM 1725  C3  RET A 249A     14.687  12.110  -4.825  1.00  4.59           C  
HETATM 1726  C4  RET A 249A     14.602  12.963  -3.578  1.00  2.00           C  
HETATM 1727  C5  RET A 249A     15.028  12.241  -2.321  1.00  5.82           C  
HETATM 1728  C6  RET A 249A     15.272  10.910  -2.258  1.00  3.53           C  
HETATM 1729  C7  RET A 249A     15.759  10.300  -1.010  1.00  2.00           C  
HETATM 1730  C8  RET A 249A     15.984   9.013  -0.728  1.00  2.00           C  
HETATM 1731  C9  RET A 249A     16.445   8.386   0.490  1.00  3.70           C  
HETATM 1732  C10 RET A 249A     16.550   7.051   0.453  1.00  5.00           C  
HETATM 1733  C11 RET A 249A     16.959   6.137   1.496  1.00  5.69           C  
HETATM 1734  C12 RET A 249A     17.038   4.800   1.365  1.00  3.96           C  
HETATM 1735  C13 RET A 249A     17.421   3.814   2.353  1.00  5.23           C  
HETATM 1736  C14 RET A 249A     17.403   2.520   1.958  1.00  6.72           C  
HETATM 1737  C15 RET A 249A     17.725   1.312   2.708  1.00  6.35           C  
HETATM 1738  C16 RET A 249A     14.193   8.763  -3.127  1.00  2.17           C  
HETATM 1739  C17 RET A 249A     16.406   9.490  -3.981  1.00  8.33           C  
HETATM 1740  C18 RET A 249A     15.170  13.209  -1.168  1.00  9.80           C  
HETATM 1741  C19 RET A 249A     16.760   9.238   1.697  1.00  2.88           C  
HETATM 1742  C20 RET A 249A     17.793   4.275   3.744  1.00  3.99           C  
HETATM 1743  C1  2DP A 261       2.349   5.989 -12.643  1.00 15.53           C  
HETATM 1744  C2  2DP A 261       1.578   5.408 -13.846  1.00 17.54           C  
HETATM 1745  C3  2DP A 261       1.256   6.460 -14.947  1.00 19.15           C  
HETATM 1746  C4  2DP A 261       2.681   4.585 -19.101  1.00 21.87           C  
HETATM 1747  C5  2DP A 261       3.843   5.347 -19.927  1.00 19.90           C  
HETATM 1748  C6  2DP A 261       3.204   6.074 -21.165  1.00 19.29           C  
HETATM 1749  C11 2DP A 261       2.300   5.020 -10.400  1.00 13.98           C  
HETATM 1750  C12 2DP A 261       1.659   5.285  -9.007  1.00 14.11           C  
HETATM 1751  C13 2DP A 261       2.534   6.072  -7.969  1.00 13.32           C  
HETATM 1752  C14 2DP A 261       2.809   7.448  -8.549  1.00 13.56           C  
HETATM 1753  C15 2DP A 261       1.822   6.300  -6.599  1.00 14.38           C  
HETATM 1754  C16 2DP A 261       2.576   5.779  -5.337  1.00 14.24           C  
HETATM 1755  C17 2DP A 261       2.896   6.809  -4.209  1.00  9.78           C  
HETATM 1756  C18 2DP A 261       1.773   7.620  -3.456  1.00  7.81           C  
HETATM 1757  C19 2DP A 261       0.374   7.060  -3.370  1.00  8.12           C  
HETATM 1758  C20 2DP A 261       2.061   9.008  -2.780  1.00  6.25           C  
HETATM 1759  C21 2DP A 261       1.633   9.316  -1.322  1.00  2.00           C  
HETATM 1760  C22 2DP A 261       1.922   8.227  -0.260  1.00  2.00           C  
HETATM 1761  C23 2DP A 261       1.906   8.562   1.246  1.00  2.00           C  
HETATM 1762  C24 2DP A 261       2.171   9.990   1.659  1.00  2.00           C  
HETATM 1763  C25 2DP A 261       1.627   7.472   2.331  1.00  4.06           C  
HETATM 1764  C26 2DP A 261       2.374   7.626   3.687  1.00  7.48           C  
HETATM 1765  C27 2DP A 261       1.423   8.256   4.681  1.00 13.99           C  
HETATM 1766  C28 2DP A 261       1.507   7.752   6.104  1.00 18.73           C  
HETATM 1767  C29 2DP A 261       1.009   6.315   6.300  1.00 17.74           C  
HETATM 1768  C30 2DP A 261       0.785   8.691   7.071  1.00 19.68           C  
HETATM 1769  C41 2DP A 261      -0.887   5.435 -13.022  1.00 14.49           C  
HETATM 1770  C42 2DP A 261      -1.826   4.343 -12.383  1.00 11.39           C  
HETATM 1771  C43 2DP A 261      -3.412   4.492 -12.359  1.00  8.02           C  
HETATM 1772  C44 2DP A 261      -4.034   4.344 -13.793  1.00  8.49           C  
HETATM 1773  C45 2DP A 261      -4.076   3.444 -11.367  1.00  6.16           C  
HETATM 1774  C46 2DP A 261      -4.557   3.871  -9.936  1.00  7.61           C  
HETATM 1775  C47 2DP A 261      -3.505   4.413  -8.884  1.00  7.15           C  
HETATM 1776  C48 2DP A 261      -2.932   3.535  -7.699  1.00  7.27           C  
HETATM 1777  C49 2DP A 261      -2.921   2.024  -8.018  1.00  8.52           C  
HETATM 1778  C50 2DP A 261      -3.754   3.801  -6.430  1.00  9.95           C  
HETATM 1779  C51 2DP A 261      -2.942   4.361  -5.249  1.00 13.55           C  
HETATM 1780  C52 2DP A 261      -2.091   3.331  -4.492  1.00 17.42           C  
HETATM 1781  C53 2DP A 261      -1.016   3.862  -3.459  1.00 18.83           C  
HETATM 1782  C54 2DP A 261      -1.384   3.608  -1.954  1.00 19.99           C  
HETATM 1783  C55 2DP A 261       0.399   3.258  -3.915  1.00 21.38           C  
HETATM 1784  C56 2DP A 261       1.203   2.350  -2.955  1.00 23.09           C  
HETATM 1785  C57 2DP A 261       2.468   2.971  -2.311  1.00 24.28           C  
HETATM 1786  C58 2DP A 261       2.245   4.171  -1.340  1.00 26.55           C  
HETATM 1787  C59 2DP A 261       1.605   3.802   0.034  1.00 25.78           C  
HETATM 1788  C60 2DP A 261       3.563   4.973  -1.124  1.00 28.36           C  
HETATM 1789  O1  2DP A 261       1.613   5.824 -11.398  1.00 13.98           O  
HETATM 1790  O2  2DP A 261       0.360   4.723 -13.384  1.00 15.75           O  
HETATM 1791  O3  2DP A 261       1.784   6.025 -16.267  1.00 22.31           O  
HETATM 1792  O4  2DP A 261       2.091   7.838 -18.176  1.00 23.96           O  
HETATM 1793  O5  2DP A 261      -0.244   7.056 -17.608  1.00 23.52           O  
HETATM 1794  O6  2DP A 261       1.414   5.337 -18.772  1.00 22.87           O  
HETATM 1795  O7  2DP A 261       4.891   4.456 -20.450  1.00 19.55           O  
HETATM 1796  O8  2DP A 261       4.150   6.295 -22.263  1.00 20.64           O  
HETATM 1797  O9  2DP A 261       2.678   4.642 -23.706  1.00 20.19           O  
HETATM 1798  O10 2DP A 261       3.668   6.764 -24.791  1.00 20.95           O  
HETATM 1799  O11 2DP A 261       5.122   4.814 -24.176  1.00 20.81           O  
HETATM 1800  P1  2DP A 261       1.224   6.672 -17.745  1.00 24.80           P  
HETATM 1801  P2  2DP A 261       3.894   5.605 -23.776  1.00 21.87           P  
HETATM 1802  CM  2DP A 261       5.160   3.840 -25.318  1.00 22.16           C  
HETATM 1803  C1  2DP A 262      31.407  12.833 -17.613  1.00 23.52           C  
HETATM 1804  C2  2DP A 262      32.515  11.846 -18.019  1.00 23.03           C  
HETATM 1805  C3  2DP A 262      33.024  12.088 -19.466  1.00 22.83           C  
HETATM 1806  C4  2DP A 262      30.565   8.930 -21.861  1.00 23.52           C  
HETATM 1807  C5  2DP A 262      29.797  10.355 -21.950  1.00 26.11           C  
HETATM 1808  C6  2DP A 262      28.580  10.226 -22.922  1.00 28.11           C  
HETATM 1809  C11 2DP A 262      31.331  13.537 -15.248  1.00 24.73           C  
HETATM 1810  C12 2DP A 262      31.699  14.782 -14.389  1.00 26.07           C  
HETATM 1811  C13 2DP A 262      31.548  14.633 -12.838  1.00 25.29           C  
HETATM 1812  C14 2DP A 262      32.967  14.482 -12.277  1.00 25.34           C  
HETATM 1813  C15 2DP A 262      30.878  15.887 -12.203  1.00 22.65           C  
HETATM 1814  C16 2DP A 262      30.973  16.032 -10.674  1.00 23.24           C  
HETATM 1815  C17 2DP A 262      30.323  14.932  -9.802  1.00 25.33           C  
HETATM 1816  C18 2DP A 262      30.953  14.574  -8.420  1.00 28.05           C  
HETATM 1817  C19 2DP A 262      32.472  14.355  -8.333  1.00 30.20           C  
HETATM 1818  C20 2DP A 262      30.072  14.426  -7.123  1.00 28.37           C  
HETATM 1819  C21 2DP A 262      30.713  14.483  -5.701  1.00 25.32           C  
HETATM 1820  C22 2DP A 262      29.845  14.912  -4.488  1.00 22.89           C  
HETATM 1821  C23 2DP A 262      29.314  16.368  -4.315  1.00 22.15           C  
HETATM 1822  C24 2DP A 262      28.435  16.954  -5.397  1.00 21.05           C  
HETATM 1823  C25 2DP A 262      29.666  17.238  -3.056  1.00 21.11           C  
HETATM 1824  C26 2DP A 262      28.809  16.987  -1.790  1.00 21.01           C  
HETATM 1825  C27 2DP A 262      27.840  18.136  -1.632  1.00 21.96           C  
HETATM 1826  C28 2DP A 262      26.503  17.996  -2.331  1.00 20.53           C  
HETATM 1827  C29 2DP A 262      26.208  19.131  -3.284  1.00 20.28           C  
HETATM 1828  C30 2DP A 262      25.353  17.844  -1.349  1.00 21.21           C  
HETATM 1829  C41 2DP A 262      32.597   9.660 -16.749  1.00 19.26           C  
HETATM 1830  C42 2DP A 262      31.753  10.056 -15.486  1.00 19.62           C  
HETATM 1831  C43 2DP A 262      32.307   9.981 -13.993  1.00 17.60           C  
HETATM 1832  C44 2DP A 262      33.648  10.772 -13.819  1.00 18.26           C  
HETATM 1833  C45 2DP A 262      31.217  10.522 -12.974  1.00 16.45           C  
HETATM 1834  C46 2DP A 262      31.589  11.000 -11.520  1.00 15.78           C  
HETATM 1835  C47 2DP A 262      31.992   9.945 -10.411  1.00 14.96           C  
HETATM 1836  C48 2DP A 262      31.542  10.094  -8.899  1.00 15.45           C  
HETATM 1837  C49 2DP A 262      30.318  11.015  -8.717  1.00 16.30           C  
HETATM 1838  C50 2DP A 262      32.703  10.625  -8.071  1.00 16.76           C  
HETATM 1839  C51 2DP A 262      32.997   9.766  -6.837  1.00 18.01           C  
HETATM 1840  C52 2DP A 262      32.703  10.415  -5.485  1.00 18.52           C  
HETATM 1841  C53 2DP A 262      32.916   9.539  -4.182  1.00 21.33           C  
HETATM 1842  C54 2DP A 262      34.252   9.827  -3.399  1.00 22.35           C  
HETATM 1843  C55 2DP A 262      31.583   9.683  -3.312  1.00 20.93           C  
HETATM 1844  C56 2DP A 262      31.594   9.303  -1.814  1.00 22.79           C  
HETATM 1845  C57 2DP A 262      30.726   8.073  -1.394  1.00 21.28           C  
HETATM 1846  C58 2DP A 262      29.543   8.355  -0.433  1.00 18.30           C  
HETATM 1847  C59 2DP A 262      28.444   7.297  -0.527  1.00 17.81           C  
HETATM 1848  C60 2DP A 262      29.990   8.520   1.041  1.00 15.86           C  
HETATM 1849  O1  2DP A 262      31.909  13.731 -16.577  1.00 24.63           O  
HETATM 1850  O2  2DP A 262      32.054  10.464 -17.846  1.00 21.00           O  
HETATM 1851  O3  2DP A 262      32.387  11.160 -20.406  1.00 23.98           O  
HETATM 1852  O4  2DP A 262      33.994   9.211 -19.714  1.00 23.28           O  
HETATM 1853  O5  2DP A 262      33.688   9.806 -22.177  1.00 22.56           O  
HETATM 1854  O6  2DP A 262      31.659   8.772 -20.871  1.00 22.57           O  
HETATM 1855  O7  2DP A 262      30.606  11.464 -22.481  1.00 25.42           O  
HETATM 1856  O8  2DP A 262      27.302  10.082 -22.219  1.00 30.05           O  
HETATM 1857  O9  2DP A 262      24.716   9.821 -22.447  1.00 29.27           O  
HETATM 1858  O10 2DP A 262      26.173   9.307 -24.462  1.00 31.72           O  
HETATM 1859  O11 2DP A 262      26.153   7.738 -22.503  1.00 27.67           O  
HETATM 1860  P1  2DP A 262      33.045   9.686 -20.804  1.00 22.16           P  
HETATM 1861  P2  2DP A 262      26.052   9.207 -22.919  1.00 28.81           P  
HETATM 1862  CM  2DP A 262      27.028   7.225 -21.392  1.00 23.68           C  
HETATM 1863  C1  2DP A 263      35.316   3.184 -18.802  1.00 28.60           C  
HETATM 1864  C2  2DP A 263      34.861   4.660 -18.946  1.00 29.95           C  
HETATM 1865  C3  2DP A 263      34.821   5.139 -20.410  1.00 32.63           C  
HETATM 1866  C4  2DP A 263      32.138   5.841 -23.339  1.00 32.52           C  
HETATM 1867  C5  2DP A 263      31.298   6.216 -24.676  1.00 29.36           C  
HETATM 1868  C6  2DP A 263      32.044   5.709 -25.979  1.00 26.56           C  
HETATM 1869  C11 2DP A 263      35.090   2.761 -16.366  1.00 25.69           C  
HETATM 1870  C12 2DP A 263      33.914   2.518 -15.361  1.00 23.33           C  
HETATM 1871  C13 2DP A 263      34.274   1.718 -14.066  1.00 21.19           C  
HETATM 1872  C14 2DP A 263      33.159   1.940 -13.061  1.00 22.93           C  
HETATM 1873  C15 2DP A 263      34.360   0.195 -14.294  1.00 18.12           C  
HETATM 1874  C16 2DP A 263      35.449  -0.503 -13.459  1.00 15.46           C  
HETATM 1875  C17 2DP A 263      34.971  -1.543 -12.415  1.00 10.68           C  
HETATM 1876  C18 2DP A 263      35.252  -1.355 -10.891  1.00  4.86           C  
HETATM 1877  C19 2DP A 263      36.025  -2.446 -10.148  1.00  3.11           C  
HETATM 1878  C20 2DP A 263      34.751  -0.102 -10.120  1.00  2.00           C  
HETATM 1879  C21 2DP A 263      35.686   0.608  -9.141  1.00  2.00           C  
HETATM 1880  C22 2DP A 263      35.203   0.804  -7.701  1.00  2.00           C  
HETATM 1881  C23 2DP A 263      34.927  -0.394  -6.782  1.00  2.00           C  
HETATM 1882  C24 2DP A 263      35.937  -1.524  -6.675  1.00  2.76           C  
HETATM 1883  C25 2DP A 263      33.630  -0.462  -5.971  1.00  4.26           C  
HETATM 1884  C26 2DP A 263      33.083  -1.882  -5.735  1.00  4.95           C  
HETATM 1885  C27 2DP A 263      32.401  -1.857  -4.396  1.00  8.59           C  
HETATM 1886  C28 2DP A 263      33.314  -1.987  -3.236  1.00  5.86           C  
HETATM 1887  C29 2DP A 263      33.133  -3.291  -2.487  1.00  8.33           C  
HETATM 1888  C30 2DP A 263      33.190  -0.793  -2.314  1.00  4.82           C  
HETATM 1889  C41 2DP A 263      35.219   6.806 -17.656  1.00 24.93           C  
HETATM 1890  C42 2DP A 263      34.411   6.438 -16.367  1.00 24.26           C  
HETATM 1891  C43 2DP A 263      35.088   6.469 -14.941  1.00 25.94           C  
HETATM 1892  C44 2DP A 263      35.542   7.920 -14.554  1.00 28.10           C  
HETATM 1893  C45 2DP A 263      34.134   5.880 -13.809  1.00 24.32           C  
HETATM 1894  C46 2DP A 263      34.749   5.162 -12.552  1.00 22.77           C  
HETATM 1895  C47 2DP A 263      34.422   5.680 -11.093  1.00 22.27           C  
HETATM 1896  C48 2DP A 263      34.330   4.655  -9.896  1.00 22.28           C  
HETATM 1897  C49 2DP A 263      33.011   3.854  -9.938  1.00 22.29           C  
HETATM 1898  C50 2DP A 263      34.451   5.386  -8.563  1.00 19.89           C  
HETATM 1899  C51 2DP A 263      34.754   4.428  -7.402  1.00 19.31           C  
HETATM 1900  C52 2DP A 263      33.614   4.217  -6.395  1.00 20.08           C  
HETATM 1901  C53 2DP A 263      33.540   5.203  -5.159  1.00 18.63           C  
HETATM 1902  C54 2DP A 263      32.718   6.473  -5.446  1.00 18.46           C  
HETATM 1903  C55 2DP A 263      32.997   4.365  -3.936  1.00 19.95           C  
HETATM 1904  C56 2DP A 263      32.983   4.997  -2.540  1.00 19.78           C  
HETATM 1905  C57 2DP A 263      32.504   4.050  -1.413  1.00 17.96           C  
HETATM 1906  C58 2DP A 263      33.620   3.501  -0.500  1.00 17.02           C  
HETATM 1907  C59 2DP A 263      33.200   3.323   0.969  1.00 15.33           C  
HETATM 1908  C60 2DP A 263      34.229   2.187  -1.055  1.00 14.20           C  
HETATM 1909  O1  2DP A 263      34.585   2.514 -17.726  1.00 25.70           O  
HETATM 1910  O2  2DP A 263      35.723   5.540 -18.171  1.00 27.51           O  
HETATM 1911  O3  2DP A 263      33.528   5.788 -20.681  1.00 35.10           O  
HETATM 1912  O4  2DP A 263      31.218   5.512 -19.483  1.00 35.85           O  
HETATM 1913  O5  2DP A 263      32.373   3.459 -20.413  1.00 34.64           O  
HETATM 1914  O6  2DP A 263      31.413   5.288 -22.130  1.00 34.57           O  
HETATM 1915  O7  2DP A 263      31.109   7.663 -24.870  1.00 29.20           O  
HETATM 1916  O8  2DP A 263      33.053   4.655 -25.760  1.00 23.30           O  
HETATM 1917  O9  2DP A 263      31.486   2.800 -26.779  1.00 20.45           O  
HETATM 1918  O10 2DP A 263      33.853   2.162 -26.070  1.00 19.17           O  
HETATM 1919  O11 2DP A 263      32.088   2.720 -24.356  1.00 19.47           O  
HETATM 1920  P1  2DP A 263      32.074   4.945 -20.593  1.00 36.20           P  
HETATM 1921  P2  2DP A 263      32.607   3.038 -25.740  1.00 20.55           P  
HETATM 1922  CM  2DP A 263      32.958   2.552 -23.150  1.00 17.95           C  
HETATM 1923  C1  2DP A 264      41.020 -11.813 -16.275  1.00 28.37           C  
HETATM 1924  C2  2DP A 264      42.566 -11.788 -16.109  1.00 27.31           C  
HETATM 1925  C3  2DP A 264      43.266 -12.512 -17.237  1.00 27.56           C  
HETATM 1926  C4  2DP A 264      44.472 -14.853 -20.032  1.00 22.51           C  
HETATM 1927  C5  2DP A 264      43.035 -15.505 -19.758  1.00 21.32           C  
HETATM 1928  C6  2DP A 264      42.902 -15.806 -18.226  1.00 23.30           C  
HETATM 1929  C11 2DP A 264      40.189 -10.201 -14.639  1.00 23.88           C  
HETATM 1930  C12 2DP A 264      39.033  -9.166 -14.472  1.00 22.73           C  
HETATM 1931  C13 2DP A 264      38.164  -9.317 -13.162  1.00 21.97           C  
HETATM 1932  C14 2DP A 264      37.056 -10.329 -13.470  1.00 24.58           C  
HETATM 1933  C15 2DP A 264      38.939  -9.875 -11.911  1.00 17.16           C  
HETATM 1934  C16 2DP A 264      39.810  -8.869 -11.147  1.00 12.66           C  
HETATM 1935  C17 2DP A 264      39.180  -7.500 -10.876  1.00 12.15           C  
HETATM 1936  C18 2DP A 264      38.470  -7.219  -9.531  1.00 13.68           C  
HETATM 1937  C19 2DP A 264      37.407  -6.115  -9.474  1.00 14.72           C  
HETATM 1938  C20 2DP A 264      38.829  -8.039  -8.238  1.00 16.74           C  
HETATM 1939  C21 2DP A 264      37.819  -8.220  -7.082  1.00 16.05           C  
HETATM 1940  C22 2DP A 264      38.217  -7.658  -5.708  1.00 16.77           C  
HETATM 1941  C23 2DP A 264      37.977  -6.157  -5.378  1.00 21.63           C  
HETATM 1942  C24 2DP A 264      38.828  -5.090  -6.093  1.00 23.30           C  
HETATM 1943  C25 2DP A 264      36.918  -5.699  -4.318  1.00 21.22           C  
HETATM 1944  C26 2DP A 264      37.534  -5.265  -2.958  1.00 18.11           C  
HETATM 1945  C27 2DP A 264      37.349  -3.763  -2.793  1.00 14.90           C  
HETATM 1946  C28 2DP A 264      37.669  -3.154  -1.427  1.00 13.40           C  
HETATM 1947  C29 2DP A 264      38.072  -4.134  -0.334  1.00 12.43           C  
HETATM 1948  C30 2DP A 264      36.538  -2.278  -0.913  1.00 12.40           C  
HETATM 1949  C41 2DP A 264      42.425 -13.599 -14.289  1.00 26.20           C  
HETATM 1950  C42 2DP A 264      41.537 -13.054 -13.145  1.00 27.51           C  
HETATM 1951  C43 2DP A 264      40.503 -13.917 -12.309  1.00 27.78           C  
HETATM 1952  C44 2DP A 264      40.366 -13.246 -10.891  1.00 24.46           C  
HETATM 1953  C45 2DP A 264      39.070 -14.032 -13.059  1.00 26.53           C  
HETATM 1954  C46 2DP A 264      37.669 -13.845 -12.316  1.00 24.05           C  
HETATM 1955  C47 2DP A 264      37.136 -14.925 -11.286  1.00 20.64           C  
HETATM 1956  C48 2DP A 264      37.552 -14.965  -9.744  1.00 19.76           C  
HETATM 1957  C49 2DP A 264      36.582 -15.826  -8.947  1.00 20.12           C  
HETATM 1958  C50 2DP A 264      37.575 -13.557  -9.112  1.00 19.96           C  
HETATM 1959  C51 2DP A 264      38.639 -13.389  -8.006  1.00 19.75           C  
HETATM 1960  C52 2DP A 264      38.686 -12.014  -7.314  1.00 18.30           C  
HETATM 1961  C53 2DP A 264      37.859 -11.830  -5.972  1.00 19.31           C  
HETATM 1962  C54 2DP A 264      36.875 -13.005  -5.608  1.00 18.93           C  
HETATM 1963  C55 2DP A 264      38.890 -11.508  -4.808  1.00 18.62           C  
HETATM 1964  C56 2DP A 264      38.342 -10.801  -3.542  1.00 19.32           C  
HETATM 1965  C57 2DP A 264      38.240 -11.683  -2.276  1.00 20.40           C  
HETATM 1966  C58 2DP A 264      37.446 -11.074  -1.099  1.00 19.90           C  
HETATM 1967  C59 2DP A 264      36.527 -12.075  -0.361  1.00 18.87           C  
HETATM 1968  C60 2DP A 264      38.383 -10.361  -0.093  1.00 21.26           C  
HETATM 1969  O1  2DP A 264      40.423 -10.495 -16.043  1.00 26.53           O  
HETATM 1970  O2  2DP A 264      43.014 -12.372 -14.842  1.00 26.61           O  
HETATM 1971  O3  2DP A 264      43.685 -11.554 -18.246  1.00 27.51           O  
HETATM 1972  O4  2DP A 264      45.726 -11.226 -19.860  1.00 27.41           O  
HETATM 1973  O5  2DP A 264      43.458 -11.971 -20.781  1.00 28.16           O  
HETATM 1974  O6  2DP A 264      44.844 -13.646 -19.261  1.00 24.55           O  
HETATM 1975  O7  2DP A 264      42.809 -16.786 -20.455  1.00 20.49           O  
HETATM 1976  O8  2DP A 264      41.508 -15.843 -17.761  1.00 25.36           O  
HETATM 1977  O9  2DP A 264      41.641 -18.441 -18.026  1.00 24.87           O  
HETATM 1978  O10 2DP A 264      39.855 -17.428 -16.506  1.00 27.23           O  
HETATM 1979  O11 2DP A 264      39.655 -17.261 -18.974  1.00 27.09           O  
HETATM 1980  P1  2DP A 264      44.461 -12.051 -19.634  1.00 27.42           P  
HETATM 1981  P2  2DP A 264      40.649 -17.282 -17.818  1.00 26.17           P  
HETATM 1982  CM  2DP A 264      38.893 -16.045 -19.421  1.00 28.60           C  
HETATM 1983  C1  2DP A 265      32.798 -12.118 -16.506  1.00 24.02           C  
HETATM 1984  C2  2DP A 265      31.999 -10.817 -16.264  1.00 25.34           C  
HETATM 1985  C3  2DP A 265      31.456 -10.195 -17.567  1.00 26.51           C  
HETATM 1986  C4  2DP A 265      29.943  -7.013 -18.776  1.00 28.96           C  
HETATM 1987  C5  2DP A 265      29.563  -8.072 -19.928  1.00 27.04           C  
HETATM 1988  C6  2DP A 265      28.450  -7.431 -20.805  1.00 30.27           C  
HETATM 1989  C11 2DP A 265      31.414 -13.840 -15.428  1.00 19.30           C  
HETATM 1990  C12 2DP A 265      31.181 -14.502 -14.049  1.00 18.69           C  
HETATM 1991  C13 2DP A 265      30.070 -13.858 -13.161  1.00 18.51           C  
HETATM 1992  C14 2DP A 265      28.756 -14.534 -13.526  1.00 16.75           C  
HETATM 1993  C15 2DP A 265      30.306 -14.087 -11.641  1.00 19.23           C  
HETATM 1994  C16 2DP A 265      29.808 -12.965 -10.710  1.00 19.73           C  
HETATM 1995  C17 2DP A 265      29.993 -13.178  -9.179  1.00 20.75           C  
HETATM 1996  C18 2DP A 265      29.173 -12.354  -8.107  1.00 21.51           C  
HETATM 1997  C19 2DP A 265      28.499 -11.041  -8.516  1.00 18.61           C  
HETATM 1998  C20 2DP A 265      29.009 -12.878  -6.620  1.00 22.10           C  
HETATM 1999  C21 2DP A 265      29.597 -12.108  -5.395  1.00 20.79           C  
HETATM 2000  C22 2DP A 265      29.314 -12.692  -3.986  1.00 22.49           C  
HETATM 2001  C23 2DP A 265      30.472 -13.253  -3.081  1.00 22.78           C  
HETATM 2002  C24 2DP A 265      31.025 -14.646  -3.327  1.00 23.46           C  
HETATM 2003  C25 2DP A 265      31.062 -12.436  -1.904  1.00 22.81           C  
HETATM 2004  C26 2DP A 265      30.276 -12.588  -0.563  1.00 21.74           C  
HETATM 2005  C27 2DP A 265      31.131 -13.354   0.430  1.00 19.77           C  
HETATM 2006  C28 2DP A 265      32.448 -12.719   0.798  1.00 18.35           C  
HETATM 2007  C29 2DP A 265      33.501 -13.739   1.209  1.00 16.90           C  
HETATM 2008  C30 2DP A 265      32.280 -11.634   1.875  1.00 15.18           C  
HETATM 2009  C41 2DP A 265      32.396  -9.412 -14.154  1.00 24.22           C  
HETATM 2010  C42 2DP A 265      32.710 -10.585 -13.119  1.00 22.81           C  
HETATM 2011  C43 2DP A 265      33.697 -10.395 -11.863  1.00 22.98           C  
HETATM 2012  C44 2DP A 265      33.687  -8.906 -11.267  1.00 19.75           C  
HETATM 2013  C45 2DP A 265      33.380 -11.468 -10.705  1.00 19.66           C  
HETATM 2014  C46 2DP A 265      34.437 -11.811  -9.567  1.00 15.06           C  
HETATM 2015  C47 2DP A 265      34.520 -10.983  -8.197  1.00 14.18           C  
HETATM 2016  C48 2DP A 265      33.334 -10.895  -7.117  1.00 12.23           C  
HETATM 2017  C49 2DP A 265      33.391  -9.574  -6.327  1.00 10.95           C  
HETATM 2018  C50 2DP A 265      33.404 -12.070  -6.123  1.00 11.67           C  
HETATM 2019  C51 2DP A 265      32.739 -13.367  -6.629  1.00 14.69           C  
HETATM 2020  C52 2DP A 265      33.678 -14.562  -6.877  1.00 17.18           C  
HETATM 2021  C53 2DP A 265      33.151 -16.026  -6.545  1.00 17.34           C  
HETATM 2022  C54 2DP A 265      33.463 -17.094  -7.647  1.00 18.09           C  
HETATM 2023  C55 2DP A 265      33.682 -16.466  -5.086  1.00 17.89           C  
HETATM 2024  C56 2DP A 265      34.984 -15.885  -4.482  1.00 21.21           C  
HETATM 2025  C57 2DP A 265      34.800 -14.846  -3.325  1.00 25.93           C  
HETATM 2026  C58 2DP A 265      35.064 -15.312  -1.848  1.00 27.51           C  
HETATM 2027  C59 2DP A 265      34.103 -16.404  -1.320  1.00 28.87           C  
HETATM 2028  C60 2DP A 265      36.541 -15.750  -1.617  1.00 28.55           C  
HETATM 2029  O1  2DP A 265      32.624 -13.026 -15.371  1.00 21.10           O  
HETATM 2030  O2  2DP A 265      32.815  -9.856 -15.509  1.00 25.52           O  
HETATM 2031  O3  2DP A 265      32.505  -9.491 -18.314  1.00 29.44           O  
HETATM 2032  O4  2DP A 265      33.038  -7.311 -19.684  1.00 30.47           O  
HETATM 2033  O5  2DP A 265      33.678  -7.446 -17.232  1.00 31.08           O  
HETATM 2034  O6  2DP A 265      31.109  -7.314 -17.878  1.00 30.46           O  
HETATM 2035  O7  2DP A 265      29.016  -9.345 -19.447  1.00 23.37           O  
HETATM 2036  O8  2DP A 265      28.780  -7.448 -22.238  1.00 34.74           O  
HETATM 2037  O9  2DP A 265      26.180  -7.606 -22.722  1.00 36.19           O  
HETATM 2038  O10 2DP A 265      27.747  -6.626 -24.517  1.00 36.03           O  
HETATM 2039  O11 2DP A 265      27.753  -9.098 -23.998  1.00 37.59           O  
HETATM 2040  P1  2DP A 265      32.667  -7.813 -18.305  1.00 29.83           P  
HETATM 2041  P2  2DP A 265      27.577  -7.706 -23.397  1.00 36.40           P  
HETATM 2042  CM  2DP A 265      27.747 -10.380 -23.207  1.00 37.88           C  
HETATM 2043  C1  2DP A 267      29.026  14.949  14.711  1.00 25.27           C  
HETATM 2044  C2  2DP A 267      30.144  13.906  14.872  1.00 27.18           C  
HETATM 2045  C3  2DP A 267      31.245  14.289  15.882  1.00 30.62           C  
HETATM 2046  C4  2DP A 267      32.847   9.950  18.039  1.00 33.72           C  
HETATM 2047  C5  2DP A 267      34.346   9.655  18.604  1.00 31.61           C  
HETATM 2048  C6  2DP A 267      34.476   8.132  19.172  1.00 31.50           C  
HETATM 2049  C11 2DP A 267      28.053  15.079  12.449  1.00 22.64           C  
HETATM 2050  C12 2DP A 267      27.494  14.066  11.389  1.00 21.91           C  
HETATM 2051  C13 2DP A 267      26.857  14.674  10.074  1.00 21.80           C  
HETATM 2052  C14 2DP A 267      25.799  15.707  10.487  1.00 23.54           C  
HETATM 2053  C15 2DP A 267      27.889  15.398   9.148  1.00 22.01           C  
HETATM 2054  C16 2DP A 267      27.468  15.587   7.660  1.00 24.95           C  
HETATM 2055  C17 2DP A 267      27.986  14.561   6.575  1.00 26.93           C  
HETATM 2056  C18 2DP A 267      29.069  14.918   5.444  1.00 29.71           C  
HETATM 2057  C19 2DP A 267      30.037  16.090   5.665  1.00 29.12           C  
HETATM 2058  C20 2DP A 267      29.203  14.038   4.107  1.00 31.81           C  
HETATM 2059  C21 2DP A 267      29.628  14.625   2.705  1.00 30.11           C  
HETATM 2060  C22 2DP A 267      30.825  14.001   1.898  1.00 30.44           C  
HETATM 2061  C23 2DP A 267      30.827  12.565   1.218  1.00 29.80           C  
HETATM 2062  C24 2DP A 267      31.966  11.624   1.560  1.00 30.38           C  
HETATM 2063  C25 2DP A 267      29.718  12.044   0.201  1.00 29.14           C  
HETATM 2064  C26 2DP A 267      29.776  12.461  -1.335  1.00 25.98           C  
HETATM 2065  C27 2DP A 267      28.708  11.642  -2.121  1.00 22.45           C  
HETATM 2066  C28 2DP A 267      28.324  12.118  -3.531  1.00 19.35           C  
HETATM 2067  C29 2DP A 267      26.921  12.648  -3.643  1.00 17.62           C  
HETATM 2068  C30 2DP A 267      28.523  11.056  -4.618  1.00 15.64           C  
HETATM 2069  C41 2DP A 267      30.961  12.239  13.233  1.00 27.26           C  
HETATM 2070  C42 2DP A 267      31.862  12.256  11.954  1.00 25.98           C  
HETATM 2071  C43 2DP A 267      31.242  12.081  10.503  1.00 24.15           C  
HETATM 2072  C44 2DP A 267      29.901  11.224  10.504  1.00 22.35           C  
HETATM 2073  C45 2DP A 267      31.003  13.495   9.847  1.00 22.26           C  
HETATM 2074  C46 2DP A 267      31.277  13.726   8.330  1.00 20.48           C  
HETATM 2075  C47 2DP A 267      30.933  12.581   7.317  1.00 20.52           C  
HETATM 2076  C48 2DP A 267      32.038  11.617   6.704  1.00 23.92           C  
HETATM 2077  C49 2DP A 267      33.385  11.610   7.506  1.00 22.85           C  
HETATM 2078  C50 2DP A 267      32.276  11.970   5.197  1.00 24.19           C  
HETATM 2079  C51 2DP A 267      32.436  13.468   4.846  1.00 24.35           C  
HETATM 2080  C52 2DP A 267      33.786  14.149   5.144  1.00 25.66           C  
HETATM 2081  C53 2DP A 267      35.073  13.730   4.320  1.00 27.01           C  
HETATM 2082  C54 2DP A 267      35.797  12.407   4.809  1.00 26.47           C  
HETATM 2083  C55 2DP A 267      34.623  13.694   2.790  1.00 26.44           C  
HETATM 2084  C56 2DP A 267      34.896  14.928   1.938  1.00 24.37           C  
HETATM 2085  C57 2DP A 267      36.349  15.017   1.488  1.00 22.68           C  
HETATM 2086  C58 2DP A 267      36.684  16.154   0.536  1.00 20.98           C  
HETATM 2087  C59 2DP A 267      38.055  16.753   0.856  1.00 20.14           C  
HETATM 2088  C60 2DP A 267      36.623  15.703  -0.923  1.00 19.38           C  
HETATM 2089  O1  2DP A 267      28.008  14.462  13.779  1.00 23.00           O  
HETATM 2090  O2  2DP A 267      30.762  13.631  13.607  1.00 26.82           O  
HETATM 2091  O3  2DP A 267      31.649  13.073  16.613  1.00 35.86           O  
HETATM 2092  O4  2DP A 267      34.164  12.807  17.192  1.00 39.23           O  
HETATM 2093  O5  2DP A 267      33.435  12.386  14.826  1.00 38.82           O  
HETATM 2094  O6  2DP A 267      32.674  10.663  16.708  1.00 36.32           O  
HETATM 2095  O7  2DP A 267      34.771  10.589  19.677  1.00 27.97           O  
HETATM 2096  O8  2DP A 267      33.902   7.847  20.528  1.00 31.23           O  
HETATM 2097  O9  2DP A 267      35.161   6.736  22.601  1.00 29.86           O  
HETATM 2098  O10 2DP A 267      36.094   8.860  21.597  1.00 32.16           O  
HETATM 2099  O11 2DP A 267      33.990   8.909  22.952  1.00 29.07           O  
HETATM 2100  P1  2DP A 267      33.081  12.265  16.299  1.00 38.29           P  
HETATM 2101  P2  2DP A 267      34.805   8.083  21.955  1.00 31.13           P  
HETATM 2102  CM  2DP A 267      34.431  10.220  23.548  1.00 24.63           C  
HETATM 2103  C1  2DP A 268      32.059   3.295  14.460  1.00 15.80           C  
HETATM 2104  C2  2DP A 268      31.676   2.331  15.563  1.00 18.12           C  
HETATM 2105  C3  2DP A 268      32.714   2.316  16.696  1.00 20.35           C  
HETATM 2106  C4  2DP A 268      30.954   0.798  21.342  1.00 30.38           C  
HETATM 2107  C5  2DP A 268      31.965   1.439  22.408  1.00 30.14           C  
HETATM 2108  C6  2DP A 268      31.347   2.786  22.945  1.00 31.33           C  
HETATM 2109  C11 2DP A 268      31.709   3.427  12.104  1.00 19.96           C  
HETATM 2110  C12 2DP A 268      30.632   3.362  10.983  1.00 19.74           C  
HETATM 2111  C13 2DP A 268      31.120   2.780   9.601  1.00 20.26           C  
HETATM 2112  C14 2DP A 268      29.868   2.545   8.754  1.00 21.84           C  
HETATM 2113  C15 2DP A 268      32.051   3.750   8.789  1.00 17.94           C  
HETATM 2114  C16 2DP A 268      33.581   3.523   8.944  1.00 15.31           C  
HETATM 2115  C17 2DP A 268      34.528   4.616   8.366  1.00 12.25           C  
HETATM 2116  C18 2DP A 268      35.047   5.821   9.224  1.00 12.76           C  
HETATM 2117  C19 2DP A 268      34.549   5.990  10.665  1.00 11.07           C  
HETATM 2118  C20 2DP A 268      36.081   6.859   8.635  1.00 12.90           C  
HETATM 2119  C21 2DP A 268      35.635   8.243   8.082  1.00 17.41           C  
HETATM 2120  C22 2DP A 268      36.061   8.628   6.616  1.00 22.94           C  
HETATM 2121  C23 2DP A 268      35.163   8.298   5.336  1.00 24.12           C  
HETATM 2122  C24 2DP A 268      33.639   8.197   5.484  1.00 25.46           C  
HETATM 2123  C25 2DP A 268      35.799   8.037   3.908  1.00 23.58           C  
HETATM 2124  C26 2DP A 268      36.066   9.272   2.995  1.00 22.98           C  
HETATM 2125  C27 2DP A 268      36.631   8.765   1.668  1.00 19.93           C  
HETATM 2126  C28 2DP A 268      35.874   9.166   0.423  1.00 18.50           C  
HETATM 2127  C29 2DP A 268      34.989   8.058  -0.161  1.00 17.41           C  
HETATM 2128  C30 2DP A 268      36.822   9.702  -0.630  1.00 16.02           C  
HETATM 2129  C41 2DP A 268      32.476   0.210  14.278  1.00 18.51           C  
HETATM 2130  C42 2DP A 268      31.692  -0.967  13.553  1.00 21.91           C  
HETATM 2131  C43 2DP A 268      31.877  -1.308  11.987  1.00 23.07           C  
HETATM 2132  C44 2DP A 268      33.239  -2.063  11.730  1.00 20.96           C  
HETATM 2133  C45 2DP A 268      30.646  -2.162  11.391  1.00 22.42           C  
HETATM 2134  C46 2DP A 268      30.716  -2.864   9.966  1.00 21.86           C  
HETATM 2135  C47 2DP A 268      30.167  -2.111   8.679  1.00 24.82           C  
HETATM 2136  C48 2DP A 268      30.497  -2.579   7.172  1.00 24.11           C  
HETATM 2137  C49 2DP A 268      30.980  -1.379   6.325  1.00 22.06           C  
HETATM 2138  C50 2DP A 268      29.239  -3.228   6.485  1.00 22.05           C  
HETATM 2139  C51 2DP A 268      29.110  -4.769   6.638  1.00 19.18           C  
HETATM 2140  C52 2DP A 268      28.587  -5.535   5.419  1.00 16.48           C  
HETATM 2141  C53 2DP A 268      29.440  -5.475   4.080  1.00 14.94           C  
HETATM 2142  C54 2DP A 268      29.986  -6.855   3.578  1.00 12.68           C  
HETATM 2143  C55 2DP A 268      28.551  -4.715   2.992  1.00 13.13           C  
HETATM 2144  C56 2DP A 268      29.187  -3.549   2.195  1.00 12.41           C  
HETATM 2145  C57 2DP A 268      30.671  -3.730   1.734  1.00  7.96           C  
HETATM 2146  C58 2DP A 268      31.179  -2.822   0.586  1.00  4.39           C  
HETATM 2147  C59 2DP A 268      30.189  -2.623  -0.576  1.00  2.00           C  
HETATM 2148  C60 2DP A 268      31.688  -1.453   1.116  1.00  2.80           C  
HETATM 2149  O1  2DP A 268      31.086   3.268  13.402  1.00 16.95           O  
HETATM 2150  O2  2DP A 268      31.455   0.972  15.041  1.00 18.52           O  
HETATM 2151  O3  2DP A 268      32.388   1.249  17.643  1.00 24.53           O  
HETATM 2152  O4  2DP A 268      29.922   0.401  17.807  1.00 26.53           O  
HETATM 2153  O5  2DP A 268      30.538   2.703  18.721  1.00 26.96           O  
HETATM 2154  O6  2DP A 268      31.478   0.552  19.950  1.00 29.35           O  
HETATM 2155  O7  2DP A 268      33.292   1.752  21.838  1.00 31.90           O  
HETATM 2156  O8  2DP A 268      32.350   3.858  23.160  1.00 33.38           O  
HETATM 2157  O9  2DP A 268      34.074   4.798  21.455  1.00 33.99           O  
HETATM 2158  O10 2DP A 268      31.594   4.960  20.848  1.00 32.32           O  
HETATM 2159  O11 2DP A 268      32.567   6.435  22.624  1.00 33.25           O  
HETATM 2160  P1  2DP A 268      30.964   1.255  18.505  1.00 26.84           P  
HETATM 2161  P2  2DP A 268      32.656   5.054  21.990  1.00 34.74           P  
HETATM 2162  CM  2DP A 268      31.333   7.296  22.626  1.00 33.22           C  
HETATM 2163  C1  2DP A 269      11.600 -15.801  18.013  1.00 17.79           C  
HETATM 2164  C2  2DP A 269      11.145 -17.273  18.036  1.00 17.78           C  
HETATM 2165  C3  2DP A 269      10.466 -17.737  19.369  1.00 22.58           C  
HETATM 2166  C4  2DP A 269      10.615 -17.495  24.437  1.00 31.84           C  
HETATM 2167  C5  2DP A 269      10.025 -16.155  25.127  1.00 31.54           C  
HETATM 2168  C6  2DP A 269       8.685 -15.722  24.402  1.00 33.92           C  
HETATM 2169  C11 2DP A 269      11.262 -13.640  16.865  1.00 13.16           C  
HETATM 2170  C12 2DP A 269      11.980 -13.567  15.475  1.00 11.49           C  
HETATM 2171  C13 2DP A 269      13.127 -12.497  15.351  1.00  8.82           C  
HETATM 2172  C14 2DP A 269      14.413 -13.156  15.851  1.00 10.48           C  
HETATM 2173  C15 2DP A 269      13.429 -12.026  13.899  1.00  5.37           C  
HETATM 2174  C16 2DP A 269      12.275 -12.052  12.881  1.00  2.73           C  
HETATM 2175  C17 2DP A 269      12.679 -12.399  11.430  1.00  2.00           C  
HETATM 2176  C18 2DP A 269      11.841 -11.968  10.184  1.00  2.00           C  
HETATM 2177  C19 2DP A 269      11.138 -10.621  10.142  1.00  2.00           C  
HETATM 2178  C20 2DP A 269      11.736 -12.883   8.954  1.00  4.37           C  
HETATM 2179  C21 2DP A 269      12.584 -12.585   7.719  1.00  4.80           C  
HETATM 2180  C22 2DP A 269      11.911 -12.798   6.365  1.00  5.36           C  
HETATM 2181  C23 2DP A 269      12.489 -13.850   5.383  1.00  7.19           C  
HETATM 2182  C24 2DP A 269      11.893 -15.263   5.383  1.00  8.14           C  
HETATM 2183  C25 2DP A 269      13.648 -13.487   4.398  1.00  7.47           C  
HETATM 2184  C26 2DP A 269      14.853 -14.458   4.353  1.00  9.56           C  
HETATM 2185  C27 2DP A 269      15.934 -13.772   3.547  1.00 12.06           C  
HETATM 2186  C28 2DP A 269      17.141 -14.565   3.081  1.00 10.91           C  
HETATM 2187  C29 2DP A 269      17.451 -14.314   1.629  1.00  9.47           C  
HETATM 2188  C30 2DP A 269      17.038 -16.078   3.328  1.00 10.03           C  
HETATM 2189  C41 2DP A 269      12.474 -18.638  16.352  1.00 19.91           C  
HETATM 2190  C42 2DP A 269      13.993 -19.060  16.254  1.00 22.20           C  
HETATM 2191  C43 2DP A 269      14.645 -19.703  14.923  1.00 23.46           C  
HETATM 2192  C44 2DP A 269      14.161 -18.946  13.605  1.00 24.29           C  
HETATM 2193  C45 2DP A 269      16.274 -19.770  15.038  1.00 23.75           C  
HETATM 2194  C46 2DP A 269      17.297 -18.997  14.085  1.00 23.49           C  
HETATM 2195  C47 2DP A 269      18.004 -19.746  12.877  1.00 22.67           C  
HETATM 2196  C48 2DP A 269      17.301 -19.875  11.447  1.00 23.32           C  
HETATM 2197  C49 2DP A 269      16.096 -20.850  11.483  1.00 21.72           C  
HETATM 2198  C50 2DP A 269      18.318 -20.357  10.376  1.00 22.44           C  
HETATM 2199  C51 2DP A 269      17.811 -20.234   8.907  1.00 22.17           C  
HETATM 2200  C52 2DP A 269      18.118 -21.414   7.979  1.00 19.28           C  
HETATM 2201  C53 2DP A 269      19.635 -21.728   7.709  1.00 19.87           C  
HETATM 2202  C54 2DP A 269      20.054 -23.208   7.991  1.00 18.81           C  
HETATM 2203  C55 2DP A 269      19.961 -21.200   6.231  1.00 19.31           C  
HETATM 2204  C56 2DP A 269      20.042 -22.180   5.044  1.00 18.56           C  
HETATM 2205  C57 2DP A 269      19.365 -21.704   3.740  1.00 17.64           C  
HETATM 2206  C58 2DP A 269      17.903 -22.180   3.535  1.00 18.42           C  
HETATM 2207  C59 2DP A 269      16.848 -21.288   4.229  1.00 19.20           C  
HETATM 2208  C60 2DP A 269      17.548 -22.342   2.039  1.00 18.00           C  
HETATM 2209  O1  2DP A 269      10.764 -15.003  17.107  1.00 15.85           O  
HETATM 2210  O2  2DP A 269      12.274 -18.139  17.729  1.00 18.91           O  
HETATM 2211  O3  2DP A 269      10.605 -16.753  20.469  1.00 27.33           O  
HETATM 2212  O4  2DP A 269      12.246 -15.649  22.221  1.00 30.18           O  
HETATM 2213  O5  2DP A 269      12.720 -18.008  21.398  1.00 29.98           O  
HETATM 2214  O6  2DP A 269      10.572 -17.603  22.923  1.00 31.36           O  
HETATM 2215  O7  2DP A 269      10.933 -15.008  25.034  1.00 32.27           O  
HETATM 2216  O8  2DP A 269       7.603 -15.225  25.299  1.00 35.20           O  
HETATM 2217  O9  2DP A 269       5.280 -16.379  24.778  1.00 35.22           O  
HETATM 2218  O10 2DP A 269       5.285 -13.975  25.623  1.00 34.05           O  
HETATM 2219  O11 2DP A 269       6.033 -14.489  23.288  1.00 35.41           O  
HETATM 2220  P1  2DP A 269      11.655 -16.976  21.775  1.00 30.22           P  
HETATM 2221  P2  2DP A 269       6.010 -15.013  24.724  1.00 35.91           P  
HETATM 2222  CM  2DP A 269       6.222 -15.316  22.053  1.00 36.50           C  
HETATM 2223  O   HOH A 270      20.385   0.046  -5.523  1.00  6.66           O  
HETATM 2224  O   HOH A 271      16.551   5.843 -11.195  1.00 29.77           O  
CONECT 1635 1737                                                                
CONECT 1723 1724 1728 1738 1739                                                 
CONECT 1724 1723 1725                                                           
CONECT 1725 1724 1726                                                           
CONECT 1726 1725 1727                                                           
CONECT 1727 1726 1728 1740                                                      
CONECT 1728 1723 1727 1729                                                      
CONECT 1729 1728 1730                                                           
CONECT 1730 1729 1731                                                           
CONECT 1731 1730 1732 1741                                                      
CONECT 1732 1731 1733                                                           
CONECT 1733 1732 1734                                                           
CONECT 1734 1733 1735                                                           
CONECT 1735 1734 1736 1742                                                      
CONECT 1736 1735 1737                                                           
CONECT 1737 1635 1736                                                           
CONECT 1738 1723                                                                
CONECT 1739 1723                                                                
CONECT 1740 1727                                                                
CONECT 1741 1731                                                                
CONECT 1742 1735                                                                
CONECT 1743 1744 1789                                                           
CONECT 1744 1743 1745 1790                                                      
CONECT 1745 1744 1791                                                           
CONECT 1746 1747 1794                                                           
CONECT 1747 1746 1748 1795                                                      
CONECT 1748 1747 1796                                                           
CONECT 1749 1750 1789                                                           
CONECT 1750 1749 1751                                                           
CONECT 1751 1750 1752 1753                                                      
CONECT 1752 1751                                                                
CONECT 1753 1751 1754                                                           
CONECT 1754 1753 1755                                                           
CONECT 1755 1754 1756                                                           
CONECT 1756 1755 1757 1758                                                      
CONECT 1757 1756                                                                
CONECT 1758 1756 1759                                                           
CONECT 1759 1758 1760                                                           
CONECT 1760 1759 1761                                                           
CONECT 1761 1760 1762 1763                                                      
CONECT 1762 1761                                                                
CONECT 1763 1761 1764                                                           
CONECT 1764 1763 1765                                                           
CONECT 1765 1764 1766                                                           
CONECT 1766 1765 1767 1768                                                      
CONECT 1767 1766                                                                
CONECT 1768 1766                                                                
CONECT 1769 1770 1790                                                           
CONECT 1770 1769 1771                                                           
CONECT 1771 1770 1772 1773                                                      
CONECT 1772 1771                                                                
CONECT 1773 1771 1774                                                           
CONECT 1774 1773 1775                                                           
CONECT 1775 1774 1776                                                           
CONECT 1776 1775 1777 1778                                                      
CONECT 1777 1776                                                                
CONECT 1778 1776 1779                                                           
CONECT 1779 1778 1780                                                           
CONECT 1780 1779 1781                                                           
CONECT 1781 1780 1782 1783                                                      
CONECT 1782 1781                                                                
CONECT 1783 1781 1784                                                           
CONECT 1784 1783 1785                                                           
CONECT 1785 1784 1786                                                           
CONECT 1786 1785 1787 1788                                                      
CONECT 1787 1786                                                                
CONECT 1788 1786                                                                
CONECT 1789 1743 1749                                                           
CONECT 1790 1744 1769                                                           
CONECT 1791 1745 1800                                                           
CONECT 1792 1800                                                                
CONECT 1793 1800                                                                
CONECT 1794 1746 1800                                                           
CONECT 1795 1747                                                                
CONECT 1796 1748 1801                                                           
CONECT 1797 1801                                                                
CONECT 1798 1801                                                                
CONECT 1799 1801 1802                                                           
CONECT 1800 1791 1792 1793 1794                                                 
CONECT 1801 1796 1797 1798 1799                                                 
CONECT 1802 1799                                                                
CONECT 1803 1804 1849                                                           
CONECT 1804 1803 1805 1850                                                      
CONECT 1805 1804 1851                                                           
CONECT 1806 1807 1854                                                           
CONECT 1807 1806 1808 1855                                                      
CONECT 1808 1807 1856                                                           
CONECT 1809 1810 1849                                                           
CONECT 1810 1809 1811                                                           
CONECT 1811 1810 1812 1813                                                      
CONECT 1812 1811                                                                
CONECT 1813 1811 1814                                                           
CONECT 1814 1813 1815                                                           
CONECT 1815 1814 1816                                                           
CONECT 1816 1815 1817 1818                                                      
CONECT 1817 1816                                                                
CONECT 1818 1816 1819                                                           
CONECT 1819 1818 1820                                                           
CONECT 1820 1819 1821                                                           
CONECT 1821 1820 1822 1823                                                      
CONECT 1822 1821                                                                
CONECT 1823 1821 1824                                                           
CONECT 1824 1823 1825                                                           
CONECT 1825 1824 1826                                                           
CONECT 1826 1825 1827 1828                                                      
CONECT 1827 1826                                                                
CONECT 1828 1826                                                                
CONECT 1829 1830 1850                                                           
CONECT 1830 1829 1831                                                           
CONECT 1831 1830 1832 1833                                                      
CONECT 1832 1831                                                                
CONECT 1833 1831 1834                                                           
CONECT 1834 1833 1835                                                           
CONECT 1835 1834 1836                                                           
CONECT 1836 1835 1837 1838                                                      
CONECT 1837 1836                                                                
CONECT 1838 1836 1839                                                           
CONECT 1839 1838 1840                                                           
CONECT 1840 1839 1841                                                           
CONECT 1841 1840 1842 1843                                                      
CONECT 1842 1841                                                                
CONECT 1843 1841 1844                                                           
CONECT 1844 1843 1845                                                           
CONECT 1845 1844 1846                                                           
CONECT 1846 1845 1847 1848                                                      
CONECT 1847 1846                                                                
CONECT 1848 1846                                                                
CONECT 1849 1803 1809                                                           
CONECT 1850 1804 1829                                                           
CONECT 1851 1805 1860                                                           
CONECT 1852 1860                                                                
CONECT 1853 1860                                                                
CONECT 1854 1806 1860                                                           
CONECT 1855 1807                                                                
CONECT 1856 1808 1861                                                           
CONECT 1857 1861                                                                
CONECT 1858 1861                                                                
CONECT 1859 1861 1862                                                           
CONECT 1860 1851 1852 1853 1854                                                 
CONECT 1861 1856 1857 1858 1859                                                 
CONECT 1862 1859                                                                
CONECT 1863 1864 1909                                                           
CONECT 1864 1863 1865 1910                                                      
CONECT 1865 1864 1911                                                           
CONECT 1866 1867 1914                                                           
CONECT 1867 1866 1868 1915                                                      
CONECT 1868 1867 1916                                                           
CONECT 1869 1870 1909                                                           
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 1884                                                           
CONECT 1884 1883 1885                                                           
CONECT 1885 1884 1886                                                           
CONECT 1886 1885 1887 1888                                                      
CONECT 1887 1886                                                                
CONECT 1888 1886                                                                
CONECT 1889 1890 1910                                                           
CONECT 1890 1889 1891                                                           
CONECT 1891 1890 1892 1893                                                      
CONECT 1892 1891                                                                
CONECT 1893 1891 1894                                                           
CONECT 1894 1893 1895                                                           
CONECT 1895 1894 1896                                                           
CONECT 1896 1895 1897 1898                                                      
CONECT 1897 1896                                                                
CONECT 1898 1896 1899                                                           
CONECT 1899 1898 1900                                                           
CONECT 1900 1899 1901                                                           
CONECT 1901 1900 1902 1903                                                      
CONECT 1902 1901                                                                
CONECT 1903 1901 1904                                                           
CONECT 1904 1903 1905                                                           
CONECT 1905 1904 1906                                                           
CONECT 1906 1905 1907 1908                                                      
CONECT 1907 1906                                                                
CONECT 1908 1906                                                                
CONECT 1909 1863 1869                                                           
CONECT 1910 1864 1889                                                           
CONECT 1911 1865 1920                                                           
CONECT 1912 1920                                                                
CONECT 1913 1920                                                                
CONECT 1914 1866 1920                                                           
CONECT 1915 1867                                                                
CONECT 1916 1868 1921                                                           
CONECT 1917 1921                                                                
CONECT 1918 1921                                                                
CONECT 1919 1921 1922                                                           
CONECT 1920 1911 1912 1913 1914                                                 
CONECT 1921 1916 1917 1918 1919                                                 
CONECT 1922 1919                                                                
CONECT 1923 1924 1969                                                           
CONECT 1924 1923 1925 1970                                                      
CONECT 1925 1924 1971                                                           
CONECT 1926 1927 1974                                                           
CONECT 1927 1926 1928 1975                                                      
CONECT 1928 1927 1976                                                           
CONECT 1929 1930 1969                                                           
CONECT 1930 1929 1931                                                           
CONECT 1931 1930 1932 1933                                                      
CONECT 1932 1931                                                                
CONECT 1933 1931 1934                                                           
CONECT 1934 1933 1935                                                           
CONECT 1935 1934 1936                                                           
CONECT 1936 1935 1937 1938                                                      
CONECT 1937 1936                                                                
CONECT 1938 1936 1939                                                           
CONECT 1939 1938 1940                                                           
CONECT 1940 1939 1941                                                           
CONECT 1941 1940 1942 1943                                                      
CONECT 1942 1941                                                                
CONECT 1943 1941 1944                                                           
CONECT 1944 1943 1945                                                           
CONECT 1945 1944 1946                                                           
CONECT 1946 1945 1947 1948                                                      
CONECT 1947 1946                                                                
CONECT 1948 1946                                                                
CONECT 1949 1950 1970                                                           
CONECT 1950 1949 1951                                                           
CONECT 1951 1950 1952 1953                                                      
CONECT 1952 1951                                                                
CONECT 1953 1951 1954                                                           
CONECT 1954 1953 1955                                                           
CONECT 1955 1954 1956                                                           
CONECT 1956 1955 1957 1958                                                      
CONECT 1957 1956                                                                
CONECT 1958 1956 1959                                                           
CONECT 1959 1958 1960                                                           
CONECT 1960 1959 1961                                                           
CONECT 1961 1960 1962 1963                                                      
CONECT 1962 1961                                                                
CONECT 1963 1961 1964                                                           
CONECT 1964 1963 1965                                                           
CONECT 1965 1964 1966                                                           
CONECT 1966 1965 1967 1968                                                      
CONECT 1967 1966                                                                
CONECT 1968 1966                                                                
CONECT 1969 1923 1929                                                           
CONECT 1970 1924 1949                                                           
CONECT 1971 1925 1980                                                           
CONECT 1972 1980                                                                
CONECT 1973 1980                                                                
CONECT 1974 1926 1980                                                           
CONECT 1975 1927                                                                
CONECT 1976 1928 1981                                                           
CONECT 1977 1981                                                                
CONECT 1978 1981                                                                
CONECT 1979 1981 1982                                                           
CONECT 1980 1971 1972 1973 1974                                                 
CONECT 1981 1976 1977 1978 1979                                                 
CONECT 1982 1979                                                                
CONECT 1983 1984 2029                                                           
CONECT 1984 1983 1985 2030                                                      
CONECT 1985 1984 2031                                                           
CONECT 1986 1987 2034                                                           
CONECT 1987 1986 1988 2035                                                      
CONECT 1988 1987 2036                                                           
CONECT 1989 1990 2029                                                           
CONECT 1990 1989 1991                                                           
CONECT 1991 1990 1992 1993                                                      
CONECT 1992 1991                                                                
CONECT 1993 1991 1994                                                           
CONECT 1994 1993 1995                                                           
CONECT 1995 1994 1996                                                           
CONECT 1996 1995 1997 1998                                                      
CONECT 1997 1996                                                                
CONECT 1998 1996 1999                                                           
CONECT 1999 1998 2000                                                           
CONECT 2000 1999 2001                                                           
CONECT 2001 2000 2002 2003                                                      
CONECT 2002 2001                                                                
CONECT 2003 2001 2004                                                           
CONECT 2004 2003 2005                                                           
CONECT 2005 2004 2006                                                           
CONECT 2006 2005 2007 2008                                                      
CONECT 2007 2006                                                                
CONECT 2008 2006                                                                
CONECT 2009 2010 2030                                                           
CONECT 2010 2009 2011                                                           
CONECT 2011 2010 2012 2013                                                      
CONECT 2012 2011                                                                
CONECT 2013 2011 2014                                                           
CONECT 2014 2013 2015                                                           
CONECT 2015 2014 2016                                                           
CONECT 2016 2015 2017 2018                                                      
CONECT 2017 2016                                                                
CONECT 2018 2016 2019                                                           
CONECT 2019 2018 2020                                                           
CONECT 2020 2019 2021                                                           
CONECT 2021 2020 2022 2023                                                      
CONECT 2022 2021                                                                
CONECT 2023 2021 2024                                                           
CONECT 2024 2023 2025                                                           
CONECT 2025 2024 2026                                                           
CONECT 2026 2025 2027 2028                                                      
CONECT 2027 2026                                                                
CONECT 2028 2026                                                                
CONECT 2029 1983 1989                                                           
CONECT 2030 1984 2009                                                           
CONECT 2031 1985 2040                                                           
CONECT 2032 2040                                                                
CONECT 2033 2040                                                                
CONECT 2034 1986 2040                                                           
CONECT 2035 1987                                                                
CONECT 2036 1988 2041                                                           
CONECT 2037 2041                                                                
CONECT 2038 2041                                                                
CONECT 2039 2041 2042                                                           
CONECT 2040 2031 2032 2033 2034                                                 
CONECT 2041 2036 2037 2038 2039                                                 
CONECT 2042 2039                                                                
CONECT 2043 2044 2089                                                           
CONECT 2044 2043 2045 2090                                                      
CONECT 2045 2044 2091                                                           
CONECT 2046 2047 2094                                                           
CONECT 2047 2046 2048 2095                                                      
CONECT 2048 2047 2096                                                           
CONECT 2049 2050 2089                                                           
CONECT 2050 2049 2051                                                           
CONECT 2051 2050 2052 2053                                                      
CONECT 2052 2051                                                                
CONECT 2053 2051 2054                                                           
CONECT 2054 2053 2055                                                           
CONECT 2055 2054 2056                                                           
CONECT 2056 2055 2057 2058                                                      
CONECT 2057 2056                                                                
CONECT 2058 2056 2059                                                           
CONECT 2059 2058 2060                                                           
CONECT 2060 2059 2061                                                           
CONECT 2061 2060 2062 2063                                                      
CONECT 2062 2061                                                                
CONECT 2063 2061 2064                                                           
CONECT 2064 2063 2065                                                           
CONECT 2065 2064 2066                                                           
CONECT 2066 2065 2067 2068                                                      
CONECT 2067 2066                                                                
CONECT 2068 2066                                                                
CONECT 2069 2070 2090                                                           
CONECT 2070 2069 2071                                                           
CONECT 2071 2070 2072 2073                                                      
CONECT 2072 2071                                                                
CONECT 2073 2071 2074                                                           
CONECT 2074 2073 2075                                                           
CONECT 2075 2074 2076                                                           
CONECT 2076 2075 2077 2078                                                      
CONECT 2077 2076                                                                
CONECT 2078 2076 2079                                                           
CONECT 2079 2078 2080                                                           
CONECT 2080 2079 2081                                                           
CONECT 2081 2080 2082 2083                                                      
CONECT 2082 2081                                                                
CONECT 2083 2081 2084                                                           
CONECT 2084 2083 2085                                                           
CONECT 2085 2084 2086                                                           
CONECT 2086 2085 2087 2088                                                      
CONECT 2087 2086                                                                
CONECT 2088 2086                                                                
CONECT 2089 2043 2049                                                           
CONECT 2090 2044 2069                                                           
CONECT 2091 2045 2100                                                           
CONECT 2092 2100                                                                
CONECT 2093 2100                                                                
CONECT 2094 2046 2100                                                           
CONECT 2095 2047                                                                
CONECT 2096 2048 2101                                                           
CONECT 2097 2101                                                                
CONECT 2098 2101                                                                
CONECT 2099 2101 2102                                                           
CONECT 2100 2091 2092 2093 2094                                                 
CONECT 2101 2096 2097 2098 2099                                                 
CONECT 2102 2099                                                                
CONECT 2103 2104 2149                                                           
CONECT 2104 2103 2105 2150                                                      
CONECT 2105 2104 2151                                                           
CONECT 2106 2107 2154                                                           
CONECT 2107 2106 2108 2155                                                      
CONECT 2108 2107 2156                                                           
CONECT 2109 2110 2149                                                           
CONECT 2110 2109 2111                                                           
CONECT 2111 2110 2112 2113                                                      
CONECT 2112 2111                                                                
CONECT 2113 2111 2114                                                           
CONECT 2114 2113 2115                                                           
CONECT 2115 2114 2116                                                           
CONECT 2116 2115 2117 2118                                                      
CONECT 2117 2116                                                                
CONECT 2118 2116 2119                                                           
CONECT 2119 2118 2120                                                           
CONECT 2120 2119 2121                                                           
CONECT 2121 2120 2122 2123                                                      
CONECT 2122 2121                                                                
CONECT 2123 2121 2124                                                           
CONECT 2124 2123 2125                                                           
CONECT 2125 2124 2126                                                           
CONECT 2126 2125 2127 2128                                                      
CONECT 2127 2126                                                                
CONECT 2128 2126                                                                
CONECT 2129 2130 2150                                                           
CONECT 2130 2129 2131                                                           
CONECT 2131 2130 2132 2133                                                      
CONECT 2132 2131                                                                
CONECT 2133 2131 2134                                                           
CONECT 2134 2133 2135                                                           
CONECT 2135 2134 2136                                                           
CONECT 2136 2135 2137 2138                                                      
CONECT 2137 2136                                                                
CONECT 2138 2136 2139                                                           
CONECT 2139 2138 2140                                                           
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                                                                
CONECT 2149 2103 2109                                                           
CONECT 2150 2104 2129                                                           
CONECT 2151 2105 2160                                                           
CONECT 2152 2160                                                                
CONECT 2153 2160                                                                
CONECT 2154 2106 2160                                                           
CONECT 2155 2107                                                                
CONECT 2156 2108 2161                                                           
CONECT 2157 2161                                                                
CONECT 2158 2161                                                                
CONECT 2159 2161 2162                                                           
CONECT 2160 2151 2152 2153 2154                                                 
CONECT 2161 2156 2157 2158 2159                                                 
CONECT 2162 2159                                                                
CONECT 2163 2164 2209                                                           
CONECT 2164 2163 2165 2210                                                      
CONECT 2165 2164 2211                                                           
CONECT 2166 2167 2214                                                           
CONECT 2167 2166 2168 2215                                                      
CONECT 2168 2167 2216                                                           
CONECT 2169 2170 2209                                                           
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 2179                                                           
CONECT 2179 2178 2180                                                           
CONECT 2180 2179 2181                                                           
CONECT 2181 2180 2182 2183                                                      
CONECT 2182 2181                                                                
CONECT 2183 2181 2184                                                           
CONECT 2184 2183 2185                                                           
CONECT 2185 2184 2186                                                           
CONECT 2186 2185 2187 2188                                                      
CONECT 2187 2186                                                                
CONECT 2188 2186                                                                
CONECT 2189 2190 2210                                                           
CONECT 2190 2189 2191                                                           
CONECT 2191 2190 2192 2193                                                      
CONECT 2192 2191                                                                
CONECT 2193 2191 2194                                                           
CONECT 2194 2193 2195                                                           
CONECT 2195 2194 2196                                                           
CONECT 2196 2195 2197 2198                                                      
CONECT 2197 2196                                                                
CONECT 2198 2196 2199                                                           
CONECT 2199 2198 2200                                                           
CONECT 2200 2199 2201                                                           
CONECT 2201 2200 2202 2203                                                      
CONECT 2202 2201                                                                
CONECT 2203 2201 2204                                                           
CONECT 2204 2203 2205                                                           
CONECT 2205 2204 2206                                                           
CONECT 2206 2205 2207 2208                                                      
CONECT 2207 2206                                                                
CONECT 2208 2206                                                                
CONECT 2209 2163 2169                                                           
CONECT 2210 2164 2189                                                           
CONECT 2211 2165 2220                                                           
CONECT 2212 2220                                                                
CONECT 2213 2220                                                                
CONECT 2214 2166 2220                                                           
CONECT 2215 2167                                                                
CONECT 2216 2168 2221                                                           
CONECT 2217 2221                                                                
CONECT 2218 2221                                                                
CONECT 2219 2221 2222                                                           
CONECT 2220 2211 2212 2213 2214                                                 
CONECT 2221 2216 2217 2218 2219                                                 
CONECT 2222 2219                                                                
MASTER      343    0    9    7    2    0    2    6 2223    1  501   20          
END                                                                             
