HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   05-OCT-06   2IN1              
OBSLTE     21-OCT-08 2IN1      3EVX                                             
TITLE     CRYSTAL STRUCTURE OF THE HUMAN UBIQUITIN FOLD CONJUGATING             
TITLE    2 ENZYME 1 (UFC1), NORTHEAST STRUCTURAL GENOMICS TARGET HR41           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UFM1-CONJUGATING ENZYME 1;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: UBIQUITIN-FOLD MODIFIER-CONJUGATING ENZYME 1,               
COMPND   5 HSPC155;                                                             
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 GENE: RP11-297K8.1;                                                  
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;                           
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET21 JM109                               
KEYWDS    ALPHA-BETA PROTEIN, UFM1-CONJUGATING ENZYME 1, UFC1, CGI-             
KEYWDS   2 126, HSPC155, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE          
KEYWDS   3 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG,          
KEYWDS   4 UNKNOWN FUNCTION                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.FOROUHAR,M.ABASHIDZE,J.SEETHARAMAN,C.K.HO,H.JANJUA,                 
AUTHOR   2 K.CUNNINGHAM,L.C.MA,R.XIAO,J.LIU,M.C.BARAN,T.B.ACTON,B.ROST,         
AUTHOR   3 G.T.MONTELIONE,L.TONG,J.F.HUNT,NORTHEAST STRUCTURAL                  
AUTHOR   4 GENOMICS CONSORTIUM (NESG)                                           
REVDAT   3   21-OCT-08 2IN1    1       OBSLTE                                   
REVDAT   2   20-MAR-07 2IN1    1       TITLE                                    
REVDAT   1   24-OCT-06 2IN1    0                                                
JRNL        AUTH   F.FOROUHAR,M.ABASHIDZE,J.SEETHARAMAN,C.K.HO,                 
JRNL        AUTH 2 H.JANJUA,K.CUNNINGHAM,L.C.MA,R.XIAO,J.LIU,                   
JRNL        AUTH 3 M.C.BARAN,T.B.ACTON,B.ROST,G.T.MONTELIONE,L.TONG,            
JRNL        AUTH 4 J.F.HUNT                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN UBIQUITIN FOLD                
JRNL        TITL 2 CONJUGATING ENZYME 1 (UFC1), NORTHEAST STRUCTURAL            
JRNL        TITL 3 GENOMICS TARGET HR41.                                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.70 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.25                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 78899.460                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 17190                          
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) : 0.266                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1603                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2356                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2710                       
REMARK   3   BIN FREE R VALUE                    : 0.3240                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.70                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 281                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2674                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 142                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 10.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 20.12000                                             
REMARK   3    B22 (A**2) : -11.93000                                            
REMARK   3    B33 (A**2) : -8.19000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.73000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.37                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.26                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.43                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.34                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.10                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.93                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : OVERALL                                   
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 55.54                                                
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: XTALVIEW SOFTWARE HAS ALSO BEEN USED      
REMARK   3  IN THE REFINEMENT. THE FRIEDEL PAIRS WERE USED FOR PHASING          
REMARK   4                                                                      
REMARK   4 2IN1 COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007                        
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.                               
REMARK 100 THE RCSB ID CODE IS RCSB039769.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-SEP-2006                        
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97898                            
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19199                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.250                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : 0.07200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.16900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXD, SOLVE/RESOLVE                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THE STRUCTURE FACTOR FILE CONTAINS FRIEDEL PAIRS             
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM ACETATE, 18% PEG8000,       
REMARK 280  100MM (NH4)SCN, 50MM LISCN, AND 5MM DTT, VAPOR DIFFUSION,           
REMARK 280  HANGING DROP, TEMPERATURE 291K, PH 5.0                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,1/2+Y,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       33.24050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 300                                                                      
REMARK 300 REMARK: MONOMER                                                      
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                 
REMARK 465                                                                      
REMARK 465   M RES C  SSEQI                                                     
REMARK 465     MSE A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     CYS A   165                                                      
REMARK 465     ASN A   166                                                      
REMARK 465     GLN A   167                                                      
REMARK 465     LEU A   168                                                      
REMARK 465     GLU A   169                                                      
REMARK 465     HIS A   170                                                      
REMARK 465     HIS A   171                                                      
REMARK 465     HIS A   172                                                      
REMARK 465     HIS A   173                                                      
REMARK 465     HIS A   174                                                      
REMARK 465     HIS A   175                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     CYS B   165                                                      
REMARK 465     ASN B   166                                                      
REMARK 465     GLN B   167                                                      
REMARK 465     LEU B   168                                                      
REMARK 465     GLU B   169                                                      
REMARK 465     HIS B   170                                                      
REMARK 465     HIS B   171                                                      
REMARK 465     HIS B   172                                                      
REMARK 465     HIS B   173                                                      
REMARK 465     HIS B   174                                                      
REMARK 465     HIS B   175                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  17       38.79   -143.16                                   
REMARK 500    PRO A  22       31.12    -70.78                                   
REMARK 500    ASP A  24       44.48    -87.96                                   
REMARK 500    ARG A  25      -83.26      5.41                                   
REMARK 500    LEU A  75      -25.31     74.63                                   
REMARK 500    TYR A  90      -62.33    -26.33                                   
REMARK 500    THR A  93     -141.96    -88.51                                   
REMARK 500    ALA A  94      140.71   -172.78                                   
REMARK 500    LYS A 105       -6.17   -153.35                                   
REMARK 500    GLN A 160       44.73   -162.77                                   
REMARK 500    LYS B  17       39.13   -143.81                                   
REMARK 500    PRO B  22       31.65    -70.83                                   
REMARK 500    ASP B  24       44.18    -88.77                                   
REMARK 500    ARG B  25      -83.07      5.61                                   
REMARK 500    LEU B  75      -25.62     74.59                                   
REMARK 500    TYR B  90      -62.15    -26.48                                   
REMARK 500    THR B  93     -141.61    -88.63                                   
REMARK 500    ALA B  94      140.17   -173.38                                   
REMARK 500    LYS B 105       -6.41   -153.18                                   
REMARK 500    GLN B 160       44.73   -163.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: HR41   RELATED DB: TARGETDB                              
REMARK 900 RELATED ID: 1YWZ   RELATED DB: PDB                                   
REMARK 900 SOLUTION (NMR) STRUCTURE OF THIS PROTEIN                             
DBREF  2IN1 A    1   167  UNP    Q5VTX1   Q5VTX1_HUMAN     1    167             
DBREF  2IN1 B    1   167  UNP    Q5VTX1   Q5VTX1_HUMAN     1    167             
SEQADV 2IN1 MSE A    1  UNP  Q5VTX1    MET     1 MODIFIED RESIDUE               
SEQADV 2IN1 MSE A  109  UNP  Q5VTX1    MET   109 MODIFIED RESIDUE               
SEQADV 2IN1 MSE A  138  UNP  Q5VTX1    MET   138 MODIFIED RESIDUE               
SEQADV 2IN1 LEU A  168  UNP  Q5VTX1              CLONING ARTIFACT               
SEQADV 2IN1 GLU A  169  UNP  Q5VTX1              CLONING ARTIFACT               
SEQADV 2IN1 HIS A  170  UNP  Q5VTX1              CLONING ARTIFACT               
SEQADV 2IN1 HIS A  171  UNP  Q5VTX1              CLONING ARTIFACT               
SEQADV 2IN1 HIS A  172  UNP  Q5VTX1              CLONING ARTIFACT               
SEQADV 2IN1 HIS A  173  UNP  Q5VTX1              CLONING ARTIFACT               
SEQADV 2IN1 HIS A  174  UNP  Q5VTX1              CLONING ARTIFACT               
SEQADV 2IN1 HIS A  175  UNP  Q5VTX1              CLONING ARTIFACT               
SEQADV 2IN1 MSE B    1  UNP  Q5VTX1    MET     1 MODIFIED RESIDUE               
SEQADV 2IN1 MSE B  109  UNP  Q5VTX1    MET   109 MODIFIED RESIDUE               
SEQADV 2IN1 MSE B  138  UNP  Q5VTX1    MET   138 MODIFIED RESIDUE               
SEQADV 2IN1 LEU B  168  UNP  Q5VTX1              CLONING ARTIFACT               
SEQADV 2IN1 GLU B  169  UNP  Q5VTX1              CLONING ARTIFACT               
SEQADV 2IN1 HIS B  170  UNP  Q5VTX1              CLONING ARTIFACT               
SEQADV 2IN1 HIS B  171  UNP  Q5VTX1              CLONING ARTIFACT               
SEQADV 2IN1 HIS B  172  UNP  Q5VTX1              CLONING ARTIFACT               
SEQADV 2IN1 HIS B  173  UNP  Q5VTX1              CLONING ARTIFACT               
SEQADV 2IN1 HIS B  174  UNP  Q5VTX1              CLONING ARTIFACT               
SEQADV 2IN1 HIS B  175  UNP  Q5VTX1              CLONING ARTIFACT               
SEQRES   1 A  175  MSE ALA ASP GLU ALA THR ARG ARG VAL VAL SER GLU ILE          
SEQRES   2 A  175  PRO VAL LEU LYS THR ASN ALA GLY PRO ARG ASP ARG GLU          
SEQRES   3 A  175  LEU TRP VAL GLN ARG LEU LYS GLU GLU TYR GLN SER LEU          
SEQRES   4 A  175  ILE ARG TYR VAL GLU ASN ASN LYS ASN ALA ASP ASN ASP          
SEQRES   5 A  175  TRP PHE ARG LEU GLU SER ASN LYS GLU GLY THR ARG TRP          
SEQRES   6 A  175  PHE GLY LYS CYS TRP TYR ILE HIS ASP LEU LEU LYS TYR          
SEQRES   7 A  175  GLU PHE ASP ILE GLU PHE ASP ILE PRO ILE THR TYR PRO          
SEQRES   8 A  175  THR THR ALA PRO GLU ILE ALA VAL PRO GLU LEU ASP GLY          
SEQRES   9 A  175  LYS THR ALA LYS MSE TYR ARG GLY GLY LYS ILE CYS LEU          
SEQRES  10 A  175  THR ASP HIS PHE LYS PRO LEU TRP ALA ARG ASN VAL PRO          
SEQRES  11 A  175  LYS PHE GLY LEU ALA HIS LEU MSE ALA LEU GLY LEU GLY          
SEQRES  12 A  175  PRO TRP LEU ALA VAL GLU ILE PRO ASP LEU ILE GLN LYS          
SEQRES  13 A  175  GLY VAL ILE GLN HIS LYS GLU LYS CYS ASN GLN LEU GLU          
SEQRES  14 A  175  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 B  175  MSE ALA ASP GLU ALA THR ARG ARG VAL VAL SER GLU ILE          
SEQRES   2 B  175  PRO VAL LEU LYS THR ASN ALA GLY PRO ARG ASP ARG GLU          
SEQRES   3 B  175  LEU TRP VAL GLN ARG LEU LYS GLU GLU TYR GLN SER LEU          
SEQRES   4 B  175  ILE ARG TYR VAL GLU ASN ASN LYS ASN ALA ASP ASN ASP          
SEQRES   5 B  175  TRP PHE ARG LEU GLU SER ASN LYS GLU GLY THR ARG TRP          
SEQRES   6 B  175  PHE GLY LYS CYS TRP TYR ILE HIS ASP LEU LEU LYS TYR          
SEQRES   7 B  175  GLU PHE ASP ILE GLU PHE ASP ILE PRO ILE THR TYR PRO          
SEQRES   8 B  175  THR THR ALA PRO GLU ILE ALA VAL PRO GLU LEU ASP GLY          
SEQRES   9 B  175  LYS THR ALA LYS MSE TYR ARG GLY GLY LYS ILE CYS LEU          
SEQRES  10 B  175  THR ASP HIS PHE LYS PRO LEU TRP ALA ARG ASN VAL PRO          
SEQRES  11 B  175  LYS PHE GLY LEU ALA HIS LEU MSE ALA LEU GLY LEU GLY          
SEQRES  12 B  175  PRO TRP LEU ALA VAL GLU ILE PRO ASP LEU ILE GLN LYS          
SEQRES  13 B  175  GLY VAL ILE GLN HIS LYS GLU LYS CYS ASN GLN LEU GLU          
SEQRES  14 B  175  HIS HIS HIS HIS HIS HIS                                      
MODRES 2IN1 MSE A  109  MET  SELENOMETHIONINE                                   
MODRES 2IN1 MSE A  138  MET  SELENOMETHIONINE                                   
MODRES 2IN1 MSE B  109  MET  SELENOMETHIONINE                                   
MODRES 2IN1 MSE B  138  MET  SELENOMETHIONINE                                   
HET    MSE  A 109       8                                                       
HET    MSE  A 138       8                                                       
HET    MSE  B 109       8                                                       
HET    MSE  B 138       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    4(C5 H11 N O2 SE)                                            
FORMUL   3  HOH   *128(H2 O)                                                    
HELIX    1   1 GLU A    4  VAL A   10  1                                   7    
HELIX    2   2 ASP A   24  ALA A   49  1                                  26    
HELIX    3   3 VAL A   99  ASP A  103  5                                   5    
HELIX    4   4 TYR A  110  LYS A  114  5                                   5    
HELIX    5   5 PHE A  121  ARG A  127  1                                   7    
HELIX    6   6 GLY A  133  GLY A  141  1                                   9    
HELIX    7   7 GLY A  141  LYS A  156  1                                  16    
HELIX    8   8 GLU B    4  VAL B   10  1                                   7    
HELIX    9   9 ASP B   24  ALA B   49  1                                  26    
HELIX   10  10 VAL B   99  ASP B  103  5                                   5    
HELIX   11  11 TYR B  110  LYS B  114  5                                   5    
HELIX   12  12 PHE B  121  ARG B  127  1                                   7    
HELIX   13  13 GLY B  133  GLY B  141  1                                   9    
HELIX   14  14 GLY B  141  LYS B  156  1                                  16    
SHEET    1   A 3 PHE A  54  SER A  58  0                                        
SHEET    2   A 3 ARG A  64  HIS A  73 -1  O  PHE A  66   N  GLU A  57           
SHEET    3   A 3 LEU A  76  ASP A  85 -1  O  PHE A  80   N  CYS A  69           
SHEET    1   B 3 PHE B  54  SER B  58  0                                        
SHEET    2   B 3 ARG B  64  HIS B  73 -1  O  PHE B  66   N  GLU B  57           
SHEET    3   B 3 LEU B  76  ASP B  85 -1  O  PHE B  80   N  CYS B  69           
LINK         C   LYS A 108                 N   MSE A 109   1555   1555    1.33  
LINK         C   MSE A 109                 N   TYR A 110   1555   1555    1.33  
LINK         C   LEU A 137                 N   MSE A 138   1555   1555    1.33  
LINK         C   MSE A 138                 N   ALA A 139   1555   1555    1.33  
LINK         C   LYS B 108                 N   MSE B 109   1555   1555    1.33  
LINK         C   MSE B 109                 N   TYR B 110   1555   1555    1.33  
LINK         C   LEU B 137                 N   MSE B 138   1555   1555    1.33  
LINK         C   MSE B 138                 N   ALA B 139   1555   1555    1.33  
CISPEP   1 VAL A  129    PRO A  130          0        -0.30                     
CISPEP   2 VAL B  129    PRO B  130          0        -0.26                     
CRYST1   41.393   66.481   64.584  90.00 105.16  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.024159  0.000000  0.006546        0.00000                         
SCALE2      0.000000  0.015042  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016042        0.00000                         
ATOM      1  N   ASP A   3      29.338  36.081  17.972  1.00 73.31           N  
ATOM      2  CA  ASP A   3      29.965  37.431  18.088  1.00 73.33           C  
ATOM      3  C   ASP A   3      30.793  37.561  19.363  1.00 72.80           C  
ATOM      4  O   ASP A   3      31.188  36.559  19.958  1.00 73.20           O  
ATOM      5  CB  ASP A   3      28.883  38.516  18.052  1.00 73.96           C  
ATOM      6  CG  ASP A   3      27.737  38.231  19.003  1.00 73.59           C  
ATOM      7  OD1 ASP A   3      27.980  38.132  20.224  1.00 73.72           O  
ATOM      8  OD2 ASP A   3      26.590  38.108  18.527  1.00 73.41           O  
ATOM      9  N   GLU A   4      31.057  38.796  19.779  1.00 72.14           N  
ATOM     10  CA  GLU A   4      31.848  39.027  20.984  1.00 71.58           C  
ATOM     11  C   GLU A   4      30.983  39.354  22.199  1.00 70.84           C  
ATOM     12  O   GLU A   4      31.483  39.434  23.323  1.00 70.43           O  
ATOM     13  CB  GLU A   4      32.861  40.152  20.752  1.00 71.74           C  
ATOM     14  CG  GLU A   4      33.940  40.215  21.822  1.00 71.69           C  
ATOM     15  CD  GLU A   4      34.623  38.869  22.027  1.00 71.55           C  
ATOM     16  OE1 GLU A   4      35.177  38.324  21.049  1.00 71.21           O  
ATOM     17  OE2 GLU A   4      34.601  38.354  23.164  1.00 71.32           O  
ATOM     18  N   ALA A   5      29.688  39.546  21.963  1.00 70.14           N  
ATOM     19  CA  ALA A   5      28.738  39.846  23.031  1.00 68.93           C  
ATOM     20  C   ALA A   5      28.328  38.540  23.707  1.00 68.38           C  
ATOM     21  O   ALA A   5      28.132  38.489  24.922  1.00 68.44           O  
ATOM     22  CB  ALA A   5      27.514  40.545  22.461  1.00 69.14           C  
ATOM     23  N   THR A   6      28.201  37.488  22.902  1.00 67.06           N  
ATOM     24  CA  THR A   6      27.830  36.169  23.400  1.00 65.95           C  
ATOM     25  C   THR A   6      29.029  35.551  24.113  1.00 65.42           C  
ATOM     26  O   THR A   6      28.875  34.794  25.073  1.00 65.10           O  
ATOM     27  CB  THR A   6      27.392  35.234  22.246  1.00 65.70           C  
ATOM     28  OG1 THR A   6      26.269  35.805  21.564  1.00 65.02           O  
ATOM     29  CG2 THR A   6      27.003  33.865  22.783  1.00 65.60           C  
ATOM     30  N   ARG A   7      30.225  35.885  23.635  1.00 64.93           N  
ATOM     31  CA  ARG A   7      31.471  35.388  24.217  1.00 64.45           C  
ATOM     32  C   ARG A   7      31.472  35.709  25.708  1.00 63.29           C  
ATOM     33  O   ARG A   7      31.986  34.946  26.526  1.00 62.66           O  
ATOM     34  CB  ARG A   7      32.664  36.071  23.542  1.00 65.41           C  
ATOM     35  CG  ARG A   7      34.033  35.552  23.961  1.00 67.00           C  
ATOM     36  CD  ARG A   7      34.349  34.206  23.324  1.00 67.94           C  
ATOM     37  NE  ARG A   7      35.743  33.824  23.538  1.00 69.60           N  
ATOM     38  CZ  ARG A   7      36.316  32.738  23.024  1.00 70.63           C  
ATOM     39  NH1 ARG A   7      35.617  31.911  22.259  1.00 70.65           N  
ATOM     40  NH2 ARG A   7      37.594  32.482  23.274  1.00 71.58           N  
ATOM     41  N   ARG A   8      30.885  36.855  26.039  1.00 62.03           N  
ATOM     42  CA  ARG A   8      30.786  37.327  27.413  1.00 60.31           C  
ATOM     43  C   ARG A   8      29.698  36.579  28.177  1.00 58.74           C  
ATOM     44  O   ARG A   8      29.865  36.248  29.352  1.00 59.01           O  
ATOM     45  CB  ARG A   8      30.478  38.826  27.423  1.00 60.85           C  
ATOM     46  CG  ARG A   8      31.571  39.698  26.827  1.00 61.29           C  
ATOM     47  CD  ARG A   8      32.857  39.585  27.633  1.00 61.70           C  
ATOM     48  NE  ARG A   8      33.613  38.373  27.323  1.00 61.65           N  
ATOM     49  CZ  ARG A   8      34.505  37.819  28.139  1.00 61.27           C  
ATOM     50  NH1 ARG A   8      35.152  36.721  27.772  1.00 61.90           N  
ATOM     51  NH2 ARG A   8      34.735  38.349  29.331  1.00 60.71           N  
ATOM     52  N   VAL A   9      28.581  36.324  27.500  1.00 56.36           N  
ATOM     53  CA  VAL A   9      27.450  35.620  28.096  1.00 53.48           C  
ATOM     54  C   VAL A   9      27.860  34.221  28.539  1.00 51.41           C  
ATOM     55  O   VAL A   9      27.393  33.722  29.562  1.00 52.10           O  
ATOM     56  CB  VAL A   9      26.277  35.504  27.092  1.00 53.20           C  
ATOM     57  CG1 VAL A   9      25.080  34.842  27.759  1.00 52.82           C  
ATOM     58  CG2 VAL A   9      25.904  36.880  26.567  1.00 53.40           C  
ATOM     59  N   VAL A  10      28.743  33.599  27.765  1.00 48.32           N  
ATOM     60  CA  VAL A  10      29.217  32.255  28.068  1.00 46.01           C  
ATOM     61  C   VAL A  10      30.187  32.280  29.246  1.00 44.56           C  
ATOM     62  O   VAL A  10      30.482  31.248  29.854  1.00 43.60           O  
ATOM     63  CB  VAL A  10      29.924  31.639  26.844  1.00 45.83           C  
ATOM     64  CG1 VAL A  10      30.283  30.192  27.119  1.00 45.78           C  
ATOM     65  CG2 VAL A  10      29.029  31.744  25.627  1.00 45.99           C  
ATOM     66  N   SER A  11      30.673  33.474  29.561  1.00 43.35           N  
ATOM     67  CA  SER A  11      31.605  33.668  30.664  1.00 42.78           C  
ATOM     68  C   SER A  11      30.897  33.492  32.006  1.00 42.73           C  
ATOM     69  O   SER A  11      31.402  32.811  32.900  1.00 43.12           O  
ATOM     70  CB  SER A  11      32.215  35.070  30.592  1.00 41.42           C  
ATOM     71  OG  SER A  11      32.824  35.296  29.331  1.00 43.38           O  
ATOM     72  N   GLU A  12      29.724  34.106  32.130  1.00 42.16           N  
ATOM     73  CA  GLU A  12      28.934  34.049  33.354  1.00 41.22           C  
ATOM     74  C   GLU A  12      28.205  32.718  33.536  1.00 38.91           C  
ATOM     75  O   GLU A  12      27.400  32.566  34.456  1.00 37.54           O  
ATOM     76  CB  GLU A  12      27.918  35.198  33.376  1.00 43.82           C  
ATOM     77  CG  GLU A  12      28.539  36.593  33.368  1.00 47.68           C  
ATOM     78  CD  GLU A  12      27.498  37.709  33.326  1.00 50.74           C  
ATOM     79  OE1 GLU A  12      27.890  38.899  33.328  1.00 52.56           O  
ATOM     80  OE2 GLU A  12      26.285  37.400  33.289  1.00 51.83           O  
ATOM     81  N   ILE A  13      28.490  31.755  32.665  1.00 36.74           N  
ATOM     82  CA  ILE A  13      27.856  30.442  32.745  1.00 34.36           C  
ATOM     83  C   ILE A  13      28.792  29.436  33.409  1.00 32.81           C  
ATOM     84  O   ILE A  13      29.850  29.115  32.870  1.00 34.04           O  
ATOM     85  CB  ILE A  13      27.487  29.921  31.342  1.00 33.37           C  
ATOM     86  CG1 ILE A  13      26.538  30.911  30.665  1.00 32.10           C  
ATOM     87  CG2 ILE A  13      26.860  28.540  31.446  1.00 32.10           C  
ATOM     88  CD1 ILE A  13      26.036  30.452  29.315  1.00 31.27           C  
ATOM     89  N   PRO A  14      28.409  28.916  34.587  1.00 31.03           N  
ATOM     90  CA  PRO A  14      29.258  27.945  35.286  1.00 29.43           C  
ATOM     91  C   PRO A  14      29.592  26.708  34.455  1.00 28.44           C  
ATOM     92  O   PRO A  14      28.698  26.021  33.967  1.00 27.49           O  
ATOM     93  CB  PRO A  14      28.440  27.609  36.531  1.00 29.57           C  
ATOM     94  CG  PRO A  14      27.026  27.792  36.067  1.00 29.76           C  
ATOM     95  CD  PRO A  14      27.115  29.071  35.276  1.00 29.95           C  
ATOM     96  N   VAL A  15      30.880  26.421  34.304  1.00 28.87           N  
ATOM     97  CA  VAL A  15      31.291  25.264  33.521  1.00 29.41           C  
ATOM     98  C   VAL A  15      31.022  23.952  34.255  1.00 28.95           C  
ATOM     99  O   VAL A  15      30.859  23.933  35.471  1.00 27.68           O  
ATOM    100  CB  VAL A  15      32.792  25.331  33.148  1.00 29.83           C  
ATOM    101  CG1 VAL A  15      33.079  26.610  32.382  1.00 28.92           C  
ATOM    102  CG2 VAL A  15      33.648  25.245  34.399  1.00 31.04           C  
ATOM    103  N   LEU A  16      30.970  22.862  33.498  1.00 29.04           N  
ATOM    104  CA  LEU A  16      30.731  21.541  34.054  1.00 28.52           C  
ATOM    105  C   LEU A  16      32.076  20.920  34.413  1.00 28.68           C  
ATOM    106  O   LEU A  16      33.121  21.402  33.973  1.00 28.84           O  
ATOM    107  CB  LEU A  16      30.018  20.657  33.027  1.00 27.61           C  
ATOM    108  CG  LEU A  16      28.608  21.029  32.549  1.00 26.83           C  
ATOM    109  CD1 LEU A  16      27.670  21.034  33.734  1.00 27.34           C  
ATOM    110  CD2 LEU A  16      28.602  22.380  31.859  1.00 28.74           C  
ATOM    111  N   LYS A  17      32.052  19.858  35.212  1.00 28.39           N  
ATOM    112  CA  LYS A  17      33.279  19.178  35.599  1.00 28.53           C  
ATOM    113  C   LYS A  17      33.089  17.669  35.687  1.00 29.31           C  
ATOM    114  O   LYS A  17      33.629  17.020  36.581  1.00 31.70           O  
ATOM    115  CB  LYS A  17      33.796  19.714  36.937  1.00 29.33           C  
ATOM    116  CG  LYS A  17      34.302  21.155  36.874  1.00 31.23           C  
ATOM    117  CD  LYS A  17      35.725  21.317  37.433  1.00 33.34           C  
ATOM    118  CE  LYS A  17      36.786  20.560  36.614  1.00 34.84           C  
ATOM    119  NZ  LYS A  17      36.716  19.072  36.714  1.00 36.87           N  
ATOM    120  N   THR A  18      32.317  17.109  34.762  1.00 27.90           N  
ATOM    121  CA  THR A  18      32.085  15.670  34.748  1.00 26.03           C  
ATOM    122  C   THR A  18      31.861  15.168  33.328  1.00 26.57           C  
ATOM    123  O   THR A  18      30.828  15.441  32.718  1.00 25.55           O  
ATOM    124  CB  THR A  18      30.861  15.269  35.615  1.00 25.61           C  
ATOM    125  OG1 THR A  18      31.066  15.695  36.965  1.00 24.00           O  
ATOM    126  CG2 THR A  18      30.667  13.751  35.605  1.00 25.24           C  
ATOM    127  N   ASN A  19      32.843  14.442  32.801  1.00 26.48           N  
ATOM    128  CA  ASN A  19      32.734  13.889  31.459  1.00 24.86           C  
ATOM    129  C   ASN A  19      32.014  12.557  31.557  1.00 24.49           C  
ATOM    130  O   ASN A  19      32.637  11.497  31.619  1.00 22.71           O  
ATOM    131  CB  ASN A  19      34.117  13.699  30.837  1.00 27.46           C  
ATOM    132  CG  ASN A  19      34.076  12.850  29.583  1.00 28.51           C  
ATOM    133  OD1 ASN A  19      33.311  13.119  28.655  1.00 27.42           O  
ATOM    134  ND2 ASN A  19      34.900  11.808  29.553  1.00 30.70           N  
ATOM    135  N   ALA A  20      30.688  12.630  31.591  1.00 23.99           N  
ATOM    136  CA  ALA A  20      29.849  11.445  31.681  1.00 23.35           C  
ATOM    137  C   ALA A  20      28.664  11.564  30.731  1.00 22.54           C  
ATOM    138  O   ALA A  20      28.132  12.655  30.501  1.00 21.86           O  
ATOM    139  CB  ALA A  20      29.363  11.263  33.110  1.00 22.82           C  
ATOM    140  N   GLY A  21      28.259  10.424  30.186  1.00 22.55           N  
ATOM    141  CA  GLY A  21      27.146  10.390  29.262  1.00 25.12           C  
ATOM    142  C   GLY A  21      25.910   9.746  29.854  1.00 27.44           C  
ATOM    143  O   GLY A  21      25.916   9.292  31.001  1.00 27.60           O  
ATOM    144  N   PRO A  22      24.819   9.686  29.087  1.00 28.63           N  
ATOM    145  CA  PRO A  22      23.608   9.073  29.629  1.00 30.59           C  
ATOM    146  C   PRO A  22      23.638   7.553  29.819  1.00 32.56           C  
ATOM    147  O   PRO A  22      22.605   6.902  29.705  1.00 33.22           O  
ATOM    148  CB  PRO A  22      22.528   9.520  28.642  1.00 31.30           C  
ATOM    149  CG  PRO A  22      23.282   9.651  27.351  1.00 29.52           C  
ATOM    150  CD  PRO A  22      24.562  10.316  27.780  1.00 28.75           C  
ATOM    151  N   ARG A  23      24.802   6.978  30.105  1.00 33.75           N  
ATOM    152  CA  ARG A  23      24.865   5.532  30.311  1.00 35.89           C  
ATOM    153  C   ARG A  23      25.662   5.165  31.551  1.00 35.90           C  
ATOM    154  O   ARG A  23      25.551   4.047  32.056  1.00 35.02           O  
ATOM    155  CB  ARG A  23      25.475   4.813  29.099  1.00 37.18           C  
ATOM    156  CG  ARG A  23      24.630   4.819  27.829  1.00 39.15           C  
ATOM    157  CD  ARG A  23      24.902   3.577  26.974  1.00 42.59           C  
ATOM    158  NE  ARG A  23      24.291   2.360  27.524  1.00 46.84           N  
ATOM    159  CZ  ARG A  23      24.835   1.573  28.455  1.00 47.77           C  
ATOM    160  NH1 ARG A  23      24.181   0.496  28.879  1.00 47.34           N  
ATOM    161  NH2 ARG A  23      26.033   1.844  28.954  1.00 48.55           N  
ATOM    162  N   ASP A  24      26.475   6.102  32.034  1.00 36.68           N  
ATOM    163  CA  ASP A  24      27.289   5.866  33.224  1.00 36.32           C  
ATOM    164  C   ASP A  24      26.502   6.229  34.467  1.00 36.36           C  
ATOM    165  O   ASP A  24      27.006   6.878  35.387  1.00 35.97           O  
ATOM    166  CB  ASP A  24      28.599   6.658  33.153  1.00 36.45           C  
ATOM    167  CG  ASP A  24      28.443   7.989  32.457  1.00 37.79           C  
ATOM    168  OD1 ASP A  24      27.729   8.870  32.995  1.00 38.78           O  
ATOM    169  OD2 ASP A  24      29.046   8.152  31.368  1.00 36.49           O  
ATOM    170  N   ARG A  25      25.249   5.779  34.448  1.00 36.18           N  
ATOM    171  CA  ARG A  25      24.265   5.961  35.508  1.00 35.79           C  
ATOM    172  C   ARG A  25      24.710   6.847  36.667  1.00 34.51           C  
ATOM    173  O   ARG A  25      24.396   8.035  36.708  1.00 34.91           O  
ATOM    174  CB  ARG A  25      23.820   4.576  36.013  1.00 37.98           C  
ATOM    175  CG  ARG A  25      24.679   3.403  35.509  1.00 39.16           C  
ATOM    176  CD  ARG A  25      25.766   3.001  36.504  1.00 41.12           C  
ATOM    177  NE  ARG A  25      25.227   2.200  37.602  1.00 43.05           N  
ATOM    178  CZ  ARG A  25      25.950   1.694  38.599  1.00 44.20           C  
ATOM    179  NH1 ARG A  25      25.360   0.976  39.546  1.00 44.47           N  
ATOM    180  NH2 ARG A  25      27.260   1.900  38.657  1.00 45.56           N  
ATOM    181  N   GLU A  26      25.432   6.258  37.609  1.00 34.51           N  
ATOM    182  CA  GLU A  26      25.938   6.982  38.763  1.00 33.41           C  
ATOM    183  C   GLU A  26      26.529   8.335  38.341  1.00 31.33           C  
ATOM    184  O   GLU A  26      26.072   9.388  38.779  1.00 31.29           O  
ATOM    185  CB  GLU A  26      27.007   6.128  39.448  1.00 36.60           C  
ATOM    186  CG  GLU A  26      27.691   6.781  40.626  1.00 40.18           C  
ATOM    187  CD  GLU A  26      26.801   6.843  41.836  1.00 41.73           C  
ATOM    188  OE1 GLU A  26      25.647   7.296  41.694  1.00 43.03           O  
ATOM    189  OE2 GLU A  26      27.256   6.442  42.929  1.00 43.68           O  
ATOM    190  N   LEU A  27      27.538   8.300  37.477  1.00 27.43           N  
ATOM    191  CA  LEU A  27      28.173   9.528  37.027  1.00 26.43           C  
ATOM    192  C   LEU A  27      27.231  10.436  36.241  1.00 25.31           C  
ATOM    193  O   LEU A  27      27.294  11.660  36.371  1.00 24.07           O  
ATOM    194  CB  LEU A  27      29.424   9.221  36.193  1.00 28.25           C  
ATOM    195  CG  LEU A  27      30.660   8.707  36.941  1.00 27.38           C  
ATOM    196  CD1 LEU A  27      30.908   9.588  38.158  1.00 25.88           C  
ATOM    197  CD2 LEU A  27      30.461   7.260  37.368  1.00 28.15           C  
ATOM    198  N   TRP A  28      26.357   9.849  35.429  1.00 24.63           N  
ATOM    199  CA  TRP A  28      25.421  10.656  34.661  1.00 24.74           C  
ATOM    200  C   TRP A  28      24.620  11.534  35.610  1.00 24.49           C  
ATOM    201  O   TRP A  28      24.273  12.663  35.269  1.00 23.94           O  
ATOM    202  CB  TRP A  28      24.461   9.787  33.845  1.00 24.29           C  
ATOM    203  CG  TRP A  28      23.417  10.599  33.138  1.00 26.17           C  
ATOM    204  CD1 TRP A  28      22.062  10.474  33.255  1.00 27.94           C  
ATOM    205  CD2 TRP A  28      23.641  11.682  32.221  1.00 27.79           C  
ATOM    206  NE1 TRP A  28      21.427  11.412  32.469  1.00 29.46           N  
ATOM    207  CE2 TRP A  28      22.373  12.164  31.824  1.00 27.75           C  
ATOM    208  CE3 TRP A  28      24.790  12.291  31.697  1.00 28.42           C  
ATOM    209  CZ2 TRP A  28      22.222  13.227  30.928  1.00 27.15           C  
ATOM    210  CZ3 TRP A  28      24.639  13.354  30.801  1.00 27.81           C  
ATOM    211  CH2 TRP A  28      23.362  13.808  30.427  1.00 26.38           C  
ATOM    212  N   VAL A  29      24.328  11.014  36.801  1.00 24.48           N  
ATOM    213  CA  VAL A  29      23.574  11.760  37.809  1.00 24.58           C  
ATOM    214  C   VAL A  29      24.370  12.989  38.211  1.00 24.92           C  
ATOM    215  O   VAL A  29      23.866  14.109  38.150  1.00 23.75           O  
ATOM    216  CB  VAL A  29      23.321  10.914  39.082  1.00 25.44           C  
ATOM    217  CG1 VAL A  29      22.572  11.737  40.120  1.00 24.85           C  
ATOM    218  CG2 VAL A  29      22.533   9.671  38.732  1.00 24.99           C  
ATOM    219  N   GLN A  30      25.615  12.767  38.626  1.00 25.93           N  
ATOM    220  CA  GLN A  30      26.496  13.856  39.042  1.00 27.12           C  
ATOM    221  C   GLN A  30      26.520  14.935  37.966  1.00 26.88           C  
ATOM    222  O   GLN A  30      26.390  16.122  38.266  1.00 27.91           O  
ATOM    223  CB  GLN A  30      27.919  13.330  39.282  1.00 30.30           C  
ATOM    224  CG  GLN A  30      28.912  14.383  39.784  1.00 33.77           C  
ATOM    225  CD  GLN A  30      30.316  13.821  39.985  1.00 36.38           C  
ATOM    226  OE1 GLN A  30      30.497  12.790  40.640  1.00 37.96           O  
ATOM    227  NE2 GLN A  30      31.316  14.507  39.436  1.00 37.00           N  
ATOM    228  N   ARG A  31      26.685  14.510  36.714  1.00 26.25           N  
ATOM    229  CA  ARG A  31      26.724  15.430  35.579  1.00 24.98           C  
ATOM    230  C   ARG A  31      25.376  16.124  35.447  1.00 22.79           C  
ATOM    231  O   ARG A  31      25.299  17.333  35.237  1.00 22.77           O  
ATOM    232  CB  ARG A  31      27.042  14.669  34.285  1.00 24.65           C  
ATOM    233  CG  ARG A  31      26.836  15.481  33.002  1.00 25.88           C  
ATOM    234  CD  ARG A  31      27.911  16.536  32.781  1.00 24.59           C  
ATOM    235  NE  ARG A  31      27.561  17.436  31.683  1.00 25.63           N  
ATOM    236  CZ  ARG A  31      28.440  18.152  30.984  1.00 27.20           C  
ATOM    237  NH1 ARG A  31      29.735  18.077  31.257  1.00 27.42           N  
ATOM    238  NH2 ARG A  31      28.022  18.954  30.013  1.00 27.13           N  
ATOM    239  N   LEU A  32      24.316  15.341  35.579  1.00 21.86           N  
ATOM    240  CA  LEU A  32      22.969  15.860  35.477  1.00 20.80           C  
ATOM    241  C   LEU A  32      22.762  17.008  36.464  1.00 21.51           C  
ATOM    242  O   LEU A  32      22.228  18.054  36.093  1.00 21.36           O  
ATOM    243  CB  LEU A  32      21.978  14.733  35.737  1.00 20.89           C  
ATOM    244  CG  LEU A  32      20.598  14.839  35.102  1.00 19.50           C  
ATOM    245  CD1 LEU A  32      20.718  15.182  33.620  1.00 20.33           C  
ATOM    246  CD2 LEU A  32      19.880  13.516  35.295  1.00 20.25           C  
ATOM    247  N   LYS A  33      23.189  16.821  37.714  1.00 20.49           N  
ATOM    248  CA  LYS A  33      23.049  17.872  38.733  1.00 19.81           C  
ATOM    249  C   LYS A  33      23.787  19.130  38.277  1.00 19.17           C  
ATOM    250  O   LYS A  33      23.303  20.249  38.447  1.00 18.31           O  
ATOM    251  CB  LYS A  33      23.625  17.418  40.085  1.00 20.35           C  
ATOM    252  CG  LYS A  33      22.832  16.320  40.787  1.00 22.52           C  
ATOM    253  CD  LYS A  33      23.353  16.061  42.209  1.00 24.18           C  
ATOM    254  CE  LYS A  33      24.820  15.612  42.207  1.00 23.94           C  
ATOM    255  NZ  LYS A  33      25.356  15.326  43.575  1.00 25.03           N  
ATOM    256  N   GLU A  34      24.963  18.923  37.698  1.00 17.97           N  
ATOM    257  CA  GLU A  34      25.798  19.999  37.200  1.00 17.05           C  
ATOM    258  C   GLU A  34      25.084  20.720  36.081  1.00 17.14           C  
ATOM    259  O   GLU A  34      25.207  21.933  35.923  1.00 14.51           O  
ATOM    260  CB  GLU A  34      27.099  19.424  36.661  1.00 19.73           C  
ATOM    261  CG  GLU A  34      28.144  19.154  37.710  1.00 20.40           C  
ATOM    262  CD  GLU A  34      29.258  18.287  37.191  1.00 21.02           C  
ATOM    263  OE1 GLU A  34      29.659  18.474  36.017  1.00 20.30           O  
ATOM    264  OE2 GLU A  34      29.732  17.420  37.965  1.00 23.51           O  
ATOM    265  N   GLU A  35      24.333  19.951  35.305  1.00 16.78           N  
ATOM    266  CA  GLU A  35      23.600  20.483  34.172  1.00 17.56           C  
ATOM    267  C   GLU A  35      22.454  21.394  34.640  1.00 17.55           C  
ATOM    268  O   GLU A  35      22.327  22.534  34.190  1.00 18.66           O  
ATOM    269  CB  GLU A  35      23.077  19.315  33.327  1.00 16.60           C  
ATOM    270  CG  GLU A  35      22.860  19.636  31.864  1.00 21.11           C  
ATOM    271  CD  GLU A  35      24.158  19.804  31.081  1.00 21.51           C  
ATOM    272  OE1 GLU A  35      24.850  18.790  30.821  1.00 18.47           O  
ATOM    273  OE2 GLU A  35      24.482  20.960  30.726  1.00 21.66           O  
ATOM    274  N   TYR A  36      21.635  20.904  35.562  1.00 16.39           N  
ATOM    275  CA  TYR A  36      20.518  21.695  36.070  1.00 15.07           C  
ATOM    276  C   TYR A  36      20.997  22.977  36.733  1.00 15.73           C  
ATOM    277  O   TYR A  36      20.432  24.055  36.524  1.00 16.95           O  
ATOM    278  CB  TYR A  36      19.724  20.879  37.076  1.00 14.78           C  
ATOM    279  CG  TYR A  36      19.104  19.652  36.478  1.00 14.51           C  
ATOM    280  CD1 TYR A  36      18.104  19.756  35.526  1.00 16.23           C  
ATOM    281  CD2 TYR A  36      19.501  18.389  36.882  1.00 15.58           C  
ATOM    282  CE1 TYR A  36      17.506  18.631  34.993  1.00 17.52           C  
ATOM    283  CE2 TYR A  36      18.915  17.255  36.360  1.00 15.68           C  
ATOM    284  CZ  TYR A  36      17.913  17.379  35.418  1.00 16.45           C  
ATOM    285  OH  TYR A  36      17.290  16.253  34.927  1.00 18.91           O  
ATOM    286  N   GLN A  37      22.044  22.839  37.541  1.00 15.84           N  
ATOM    287  CA  GLN A  37      22.638  23.952  38.267  1.00 13.81           C  
ATOM    288  C   GLN A  37      23.128  25.043  37.328  1.00 14.15           C  
ATOM    289  O   GLN A  37      22.846  26.222  37.532  1.00 13.97           O  
ATOM    290  CB  GLN A  37      23.792  23.436  39.140  1.00 12.40           C  
ATOM    291  CG  GLN A  37      23.349  22.885  40.498  1.00 10.47           C  
ATOM    292  CD  GLN A  37      24.460  22.144  41.246  1.00 10.88           C  
ATOM    293  OE1 GLN A  37      25.587  22.637  41.374  1.00 10.88           O  
ATOM    294  NE2 GLN A  37      24.135  20.959  41.758  1.00  8.28           N  
ATOM    295  N   SER A  38      23.859  24.649  36.295  1.00 16.07           N  
ATOM    296  CA  SER A  38      24.376  25.612  35.337  1.00 16.05           C  
ATOM    297  C   SER A  38      23.213  26.279  34.579  1.00 16.15           C  
ATOM    298  O   SER A  38      23.258  27.475  34.284  1.00 17.10           O  
ATOM    299  CB  SER A  38      25.338  24.899  34.380  1.00 17.96           C  
ATOM    300  OG  SER A  38      26.054  25.816  33.571  1.00 22.77           O  
ATOM    301  N   LEU A  39      22.162  25.513  34.290  1.00 15.15           N  
ATOM    302  CA  LEU A  39      20.990  26.037  33.584  1.00 15.28           C  
ATOM    303  C   LEU A  39      20.197  27.071  34.374  1.00 15.43           C  
ATOM    304  O   LEU A  39      19.747  28.072  33.811  1.00 15.69           O  
ATOM    305  CB  LEU A  39      20.040  24.904  33.207  1.00 15.64           C  
ATOM    306  CG  LEU A  39      20.514  23.959  32.108  1.00 16.36           C  
ATOM    307  CD1 LEU A  39      19.615  22.719  32.075  1.00 17.00           C  
ATOM    308  CD2 LEU A  39      20.493  24.694  30.770  1.00 16.83           C  
ATOM    309  N   ILE A  40      19.996  26.820  35.666  1.00 15.14           N  
ATOM    310  CA  ILE A  40      19.239  27.757  36.488  1.00 17.86           C  
ATOM    311  C   ILE A  40      20.049  29.021  36.715  1.00 17.40           C  
ATOM    312  O   ILE A  40      19.493  30.105  36.902  1.00 18.19           O  
ATOM    313  CB  ILE A  40      18.832  27.151  37.883  1.00 20.25           C  
ATOM    314  CG1 ILE A  40      20.029  27.126  38.841  1.00 21.11           C  
ATOM    315  CG2 ILE A  40      18.272  25.753  37.709  1.00 20.76           C  
ATOM    316  CD1 ILE A  40      20.214  28.411  39.651  1.00 22.15           C  
ATOM    317  N   ARG A  41      21.369  28.879  36.694  1.00 16.34           N  
ATOM    318  CA  ARG A  41      22.255  30.022  36.899  1.00 18.72           C  
ATOM    319  C   ARG A  41      22.200  30.905  35.651  1.00 17.68           C  
ATOM    320  O   ARG A  41      22.104  32.134  35.740  1.00 17.17           O  
ATOM    321  CB  ARG A  41      23.687  29.529  37.149  1.00 22.22           C  
ATOM    322  CG  ARG A  41      24.445  30.281  38.244  1.00 25.08           C  
ATOM    323  CD  ARG A  41      24.824  31.692  37.832  1.00 30.43           C  
ATOM    324  NE  ARG A  41      24.130  32.700  38.630  1.00 36.24           N  
ATOM    325  CZ  ARG A  41      24.477  33.984  38.689  1.00 39.28           C  
ATOM    326  NH1 ARG A  41      25.519  34.425  37.995  1.00 41.01           N  
ATOM    327  NH2 ARG A  41      23.786  34.831  39.444  1.00 40.64           N  
ATOM    328  N   TYR A  42      22.259  30.252  34.491  1.00 16.07           N  
ATOM    329  CA  TYR A  42      22.191  30.924  33.199  1.00 15.22           C  
ATOM    330  C   TYR A  42      20.869  31.695  33.117  1.00 15.31           C  
ATOM    331  O   TYR A  42      20.840  32.872  32.748  1.00 14.01           O  
ATOM    332  CB  TYR A  42      22.264  29.887  32.066  1.00 12.42           C  
ATOM    333  CG  TYR A  42      22.158  30.448  30.655  1.00  9.20           C  
ATOM    334  CD1 TYR A  42      21.682  29.652  29.607  1.00  8.99           C  
ATOM    335  CD2 TYR A  42      22.525  31.763  30.366  1.00  8.18           C  
ATOM    336  CE1 TYR A  42      21.569  30.153  28.307  1.00  7.72           C  
ATOM    337  CE2 TYR A  42      22.418  32.274  29.072  1.00  7.41           C  
ATOM    338  CZ  TYR A  42      21.939  31.467  28.052  1.00  8.02           C  
ATOM    339  OH  TYR A  42      21.815  31.983  26.781  1.00  8.47           O  
ATOM    340  N   VAL A  43      19.778  31.027  33.476  1.00 14.09           N  
ATOM    341  CA  VAL A  43      18.454  31.640  33.438  1.00 15.34           C  
ATOM    342  C   VAL A  43      18.415  32.898  34.295  1.00 16.12           C  
ATOM    343  O   VAL A  43      17.859  33.923  33.891  1.00 17.98           O  
ATOM    344  CB  VAL A  43      17.372  30.656  33.949  1.00 15.32           C  
ATOM    345  CG1 VAL A  43      16.018  31.336  33.977  1.00 12.63           C  
ATOM    346  CG2 VAL A  43      17.330  29.421  33.058  1.00 17.71           C  
ATOM    347  N   GLU A  44      19.006  32.802  35.485  1.00 16.18           N  
ATOM    348  CA  GLU A  44      19.066  33.917  36.423  1.00 14.52           C  
ATOM    349  C   GLU A  44      19.875  35.086  35.864  1.00 13.62           C  
ATOM    350  O   GLU A  44      19.498  36.246  36.038  1.00 11.19           O  
ATOM    351  CB  GLU A  44      19.656  33.445  37.761  1.00 13.78           C  
ATOM    352  CG  GLU A  44      18.766  32.459  38.505  1.00 16.41           C  
ATOM    353  CD  GLU A  44      17.411  33.055  38.871  1.00 17.57           C  
ATOM    354  OE1 GLU A  44      17.374  34.001  39.689  1.00 16.81           O  
ATOM    355  OE2 GLU A  44      16.386  32.585  38.329  1.00 18.86           O  
ATOM    356  N   ASN A  45      20.985  34.791  35.192  1.00 14.30           N  
ATOM    357  CA  ASN A  45      21.797  35.864  34.613  1.00 14.39           C  
ATOM    358  C   ASN A  45      21.042  36.551  33.488  1.00 14.08           C  
ATOM    359  O   ASN A  45      21.174  37.763  33.301  1.00 15.55           O  
ATOM    360  CB  ASN A  45      23.125  35.340  34.066  1.00 15.39           C  
ATOM    361  CG  ASN A  45      24.014  34.777  35.149  1.00 16.10           C  
ATOM    362  OD1 ASN A  45      24.182  35.385  36.210  1.00 17.93           O  
ATOM    363  ND2 ASN A  45      24.601  33.621  34.886  1.00 17.85           N  
ATOM    364  N   ASN A  46      20.264  35.782  32.727  1.00 15.19           N  
ATOM    365  CA  ASN A  46      19.490  36.366  31.632  1.00 16.50           C  
ATOM    366  C   ASN A  46      18.448  37.300  32.229  1.00 15.26           C  
ATOM    367  O   ASN A  46      18.210  38.401  31.721  1.00 17.51           O  
ATOM    368  CB  ASN A  46      18.778  35.296  30.801  1.00 15.42           C  
ATOM    369  CG  ASN A  46      19.730  34.472  29.964  1.00 18.17           C  
ATOM    370  OD1 ASN A  46      20.704  34.988  29.403  1.00 19.90           O  
ATOM    371  ND2 ASN A  46      19.441  33.181  29.853  1.00 20.17           N  
ATOM    372  N   LYS A  47      17.822  36.856  33.311  1.00 13.86           N  
ATOM    373  CA  LYS A  47      16.819  37.675  33.962  1.00 15.91           C  
ATOM    374  C   LYS A  47      17.420  39.012  34.366  1.00 14.59           C  
ATOM    375  O   LYS A  47      16.855  40.063  34.069  1.00 13.33           O  
ATOM    376  CB  LYS A  47      16.239  36.946  35.174  1.00 16.58           C  
ATOM    377  CG  LYS A  47      15.159  35.937  34.807  1.00 19.69           C  
ATOM    378  CD  LYS A  47      14.407  35.501  36.040  1.00 22.54           C  
ATOM    379  CE  LYS A  47      13.150  34.734  35.710  1.00 25.00           C  
ATOM    380  NZ  LYS A  47      12.389  34.429  36.965  1.00 26.09           N  
ATOM    381  N   ASN A  48      18.566  38.977  35.033  1.00 14.22           N  
ATOM    382  CA  ASN A  48      19.231  40.208  35.446  1.00 14.88           C  
ATOM    383  C   ASN A  48      19.527  41.081  34.244  1.00 14.17           C  
ATOM    384  O   ASN A  48      19.460  42.298  34.327  1.00 12.72           O  
ATOM    385  CB  ASN A  48      20.546  39.896  36.146  1.00 16.66           C  
ATOM    386  CG  ASN A  48      20.345  39.111  37.403  1.00 19.52           C  
ATOM    387  OD1 ASN A  48      19.574  39.514  38.278  1.00 20.01           O  
ATOM    388  ND2 ASN A  48      21.029  37.981  37.512  1.00 21.85           N  
ATOM    389  N   ALA A  49      19.862  40.449  33.126  1.00 13.64           N  
ATOM    390  CA  ALA A  49      20.188  41.184  31.917  1.00 13.13           C  
ATOM    391  C   ALA A  49      18.942  41.516  31.104  1.00 13.09           C  
ATOM    392  O   ALA A  49      19.033  42.082  30.012  1.00 12.85           O  
ATOM    393  CB  ALA A  49      21.159  40.383  31.076  1.00 11.99           C  
ATOM    394  N   ASP A  50      17.782  41.173  31.654  1.00 14.45           N  
ATOM    395  CA  ASP A  50      16.506  41.403  30.989  1.00 16.18           C  
ATOM    396  C   ASP A  50      16.542  40.783  29.599  1.00 15.75           C  
ATOM    397  O   ASP A  50      16.195  41.410  28.591  1.00 15.10           O  
ATOM    398  CB  ASP A  50      16.200  42.896  30.892  1.00 17.59           C  
ATOM    399  CG  ASP A  50      14.849  43.166  30.269  1.00 19.40           C  
ATOM    400  OD1 ASP A  50      13.918  42.360  30.522  1.00 20.68           O  
ATOM    401  OD2 ASP A  50      14.719  44.185  29.544  1.00 20.95           O  
ATOM    402  N   ASN A  51      17.000  39.540  29.567  1.00 15.47           N  
ATOM    403  CA  ASN A  51      17.083  38.788  28.335  1.00 16.48           C  
ATOM    404  C   ASN A  51      16.554  37.380  28.558  1.00 16.63           C  
ATOM    405  O   ASN A  51      16.900  36.461  27.822  1.00 18.27           O  
ATOM    406  CB  ASN A  51      18.525  38.730  27.833  1.00 18.25           C  
ATOM    407  CG  ASN A  51      18.622  38.115  26.456  1.00 19.32           C  
ATOM    408  OD1 ASN A  51      17.912  38.520  25.540  1.00 23.39           O  
ATOM    409  ND2 ASN A  51      19.497  37.137  26.299  1.00 21.79           N  
ATOM    410  N   ASP A  52      15.722  37.217  29.585  1.00 14.11           N  
ATOM    411  CA  ASP A  52      15.128  35.919  29.907  1.00 12.79           C  
ATOM    412  C   ASP A  52      14.433  35.417  28.645  1.00 12.30           C  
ATOM    413  O   ASP A  52      13.411  35.968  28.234  1.00 10.76           O  
ATOM    414  CB  ASP A  52      14.114  36.086  31.037  1.00 11.89           C  
ATOM    415  CG  ASP A  52      13.798  34.784  31.729  1.00 11.88           C  
ATOM    416  OD1 ASP A  52      14.287  33.726  31.275  1.00 10.94           O  
ATOM    417  OD2 ASP A  52      13.058  34.825  32.732  1.00 14.01           O  
ATOM    418  N   TRP A  53      14.963  34.368  28.029  1.00 11.80           N  
ATOM    419  CA  TRP A  53      14.364  33.900  26.785  1.00 12.28           C  
ATOM    420  C   TRP A  53      13.973  32.428  26.668  1.00 13.26           C  
ATOM    421  O   TRP A  53      13.430  32.017  25.637  1.00 14.68           O  
ATOM    422  CB  TRP A  53      15.294  34.259  25.627  1.00 11.45           C  
ATOM    423  CG  TRP A  53      16.647  33.625  25.718  1.00 12.02           C  
ATOM    424  CD1 TRP A  53      17.708  34.031  26.484  1.00 13.03           C  
ATOM    425  CD2 TRP A  53      17.081  32.455  25.025  1.00 11.57           C  
ATOM    426  NE1 TRP A  53      18.778  33.182  26.307  1.00 11.00           N  
ATOM    427  CE2 TRP A  53      18.416  32.205  25.416  1.00 11.89           C  
ATOM    428  CE3 TRP A  53      16.470  31.590  24.111  1.00 10.10           C  
ATOM    429  CZ2 TRP A  53      19.146  31.128  24.922  1.00 12.43           C  
ATOM    430  CZ3 TRP A  53      17.192  30.520  23.619  1.00 11.40           C  
ATOM    431  CH2 TRP A  53      18.519  30.297  24.025  1.00 12.97           C  
ATOM    432  N   PHE A  54      14.228  31.632  27.704  1.00 12.77           N  
ATOM    433  CA  PHE A  54      13.890  30.216  27.627  1.00 13.15           C  
ATOM    434  C   PHE A  54      13.669  29.509  28.960  1.00 13.48           C  
ATOM    435  O   PHE A  54      13.948  30.045  30.033  1.00 14.06           O  
ATOM    436  CB  PHE A  54      14.986  29.470  26.882  1.00 11.34           C  
ATOM    437  CG  PHE A  54      16.146  29.098  27.745  1.00 11.79           C  
ATOM    438  CD1 PHE A  54      16.318  27.783  28.165  1.00 11.22           C  
ATOM    439  CD2 PHE A  54      17.061  30.065  28.153  1.00 11.79           C  
ATOM    440  CE1 PHE A  54      17.388  27.431  28.980  1.00 11.19           C  
ATOM    441  CE2 PHE A  54      18.142  29.726  28.973  1.00 12.27           C  
ATOM    442  CZ  PHE A  54      18.307  28.403  29.389  1.00 11.32           C  
ATOM    443  N   ARG A  55      13.157  28.288  28.862  1.00 14.52           N  
ATOM    444  CA  ARG A  55      12.906  27.420  30.008  1.00 14.64           C  
ATOM    445  C   ARG A  55      13.144  26.023  29.472  1.00 14.10           C  
ATOM    446  O   ARG A  55      12.496  25.591  28.521  1.00 13.56           O  
ATOM    447  CB  ARG A  55      11.466  27.558  30.511  1.00 13.73           C  
ATOM    448  CG  ARG A  55      11.151  28.896  31.175  1.00 15.20           C  
ATOM    449  CD  ARG A  55      11.780  29.025  32.560  1.00 14.19           C  
ATOM    450  NE  ARG A  55      11.385  30.259  33.237  1.00 15.49           N  
ATOM    451  CZ  ARG A  55      11.875  31.469  32.968  1.00 16.78           C  
ATOM    452  NH1 ARG A  55      12.796  31.623  32.024  1.00 14.81           N  
ATOM    453  NH2 ARG A  55      11.443  32.527  33.652  1.00 15.15           N  
ATOM    454  N   LEU A  56      14.091  25.327  30.079  1.00 16.23           N  
ATOM    455  CA  LEU A  56      14.428  23.985  29.645  1.00 17.23           C  
ATOM    456  C   LEU A  56      14.269  22.992  30.785  1.00 18.57           C  
ATOM    457  O   LEU A  56      14.705  23.240  31.913  1.00 19.79           O  
ATOM    458  CB  LEU A  56      15.873  23.952  29.141  1.00 17.49           C  
ATOM    459  CG  LEU A  56      16.333  22.691  28.417  1.00 18.03           C  
ATOM    460  CD1 LEU A  56      15.652  22.620  27.056  1.00 18.38           C  
ATOM    461  CD2 LEU A  56      17.847  22.711  28.252  1.00 19.87           C  
ATOM    462  N   GLU A  57      13.638  21.864  30.482  1.00 18.94           N  
ATOM    463  CA  GLU A  57      13.452  20.811  31.467  1.00 18.95           C  
ATOM    464  C   GLU A  57      13.688  19.453  30.801  1.00 18.36           C  
ATOM    465  O   GLU A  57      13.708  19.357  29.574  1.00 17.77           O  
ATOM    466  CB  GLU A  57      12.046  20.885  32.073  1.00 20.02           C  
ATOM    467  CG  GLU A  57      12.053  20.795  33.599  1.00 22.28           C  
ATOM    468  CD  GLU A  57      12.749  21.985  34.257  1.00 22.47           C  
ATOM    469  OE1 GLU A  57      13.185  21.859  35.424  1.00 20.59           O  
ATOM    470  OE2 GLU A  57      12.848  23.044  33.606  1.00 22.15           O  
ATOM    471  N   SER A  58      13.881  18.417  31.615  1.00 19.18           N  
ATOM    472  CA  SER A  58      14.132  17.066  31.111  1.00 18.46           C  
ATOM    473  C   SER A  58      13.158  16.012  31.666  1.00 19.53           C  
ATOM    474  O   SER A  58      12.176  16.345  32.332  1.00 19.73           O  
ATOM    475  CB  SER A  58      15.586  16.649  31.427  1.00 18.45           C  
ATOM    476  OG  SER A  58      15.772  16.237  32.776  1.00 14.29           O  
ATOM    477  N   ASN A  59      13.437  14.742  31.382  1.00 20.58           N  
ATOM    478  CA  ASN A  59      12.608  13.637  31.863  1.00 20.37           C  
ATOM    479  C   ASN A  59      13.325  13.027  33.057  1.00 20.99           C  
ATOM    480  O   ASN A  59      14.486  13.338  33.305  1.00 21.01           O  
ATOM    481  CB  ASN A  59      12.428  12.578  30.772  1.00 17.66           C  
ATOM    482  CG  ASN A  59      13.744  11.987  30.320  1.00 16.46           C  
ATOM    483  OD1 ASN A  59      14.805  12.536  30.605  1.00 18.41           O  
ATOM    484  ND2 ASN A  59      13.684  10.871  29.598  1.00 17.39           N  
ATOM    485  N   LYS A  60      12.641  12.155  33.785  1.00 21.73           N  
ATOM    486  CA  LYS A  60      13.210  11.522  34.966  1.00 21.67           C  
ATOM    487  C   LYS A  60      14.673  11.113  34.815  1.00 21.79           C  
ATOM    488  O   LYS A  60      15.479  11.317  35.721  1.00 22.31           O  
ATOM    489  CB  LYS A  60      12.347  10.313  35.346  1.00 21.06           C  
ATOM    490  CG  LYS A  60      10.853  10.662  35.421  1.00 21.96           C  
ATOM    491  CD  LYS A  60       9.936   9.465  35.710  1.00 21.86           C  
ATOM    492  CE  LYS A  60      10.031   9.005  37.166  1.00 22.52           C  
ATOM    493  NZ  LYS A  60       8.968   8.018  37.529  1.00 22.34           N  
ATOM    494  N   GLU A  61      15.019  10.569  33.656  1.00 23.28           N  
ATOM    495  CA  GLU A  61      16.379  10.097  33.395  1.00 23.50           C  
ATOM    496  C   GLU A  61      17.329  11.129  32.759  1.00 23.06           C  
ATOM    497  O   GLU A  61      18.540  10.897  32.648  1.00 23.30           O  
ATOM    498  CB  GLU A  61      16.281   8.835  32.539  1.00 24.82           C  
ATOM    499  CG  GLU A  61      14.914   8.677  31.879  1.00 28.89           C  
ATOM    500  CD  GLU A  61      14.812   7.426  31.037  1.00 31.91           C  
ATOM    501  OE1 GLU A  61      15.060   6.331  31.590  1.00 33.60           O  
ATOM    502  OE2 GLU A  61      14.480   7.539  29.829  1.00 31.38           O  
ATOM    503  N   GLY A  62      16.772  12.265  32.351  1.00 21.81           N  
ATOM    504  CA  GLY A  62      17.571  13.324  31.762  1.00 19.22           C  
ATOM    505  C   GLY A  62      18.195  13.032  30.410  1.00 18.27           C  
ATOM    506  O   GLY A  62      19.221  13.618  30.068  1.00 17.62           O  
ATOM    507  N   THR A  63      17.589  12.129  29.641  1.00 18.46           N  
ATOM    508  CA  THR A  63      18.100  11.780  28.312  1.00 18.64           C  
ATOM    509  C   THR A  63      17.276  12.480  27.229  1.00 18.69           C  
ATOM    510  O   THR A  63      17.711  12.612  26.086  1.00 18.14           O  
ATOM    511  CB  THR A  63      18.056  10.250  28.060  1.00 18.36           C  
ATOM    512  OG1 THR A  63      16.698   9.790  28.072  1.00 18.05           O  
ATOM    513  CG2 THR A  63      18.855   9.516  29.127  1.00 18.93           C  
ATOM    514  N   ARG A  64      16.074  12.908  27.598  1.00 19.90           N  
ATOM    515  CA  ARG A  64      15.202  13.614  26.677  1.00 20.45           C  
ATOM    516  C   ARG A  64      14.831  14.949  27.312  1.00 20.19           C  
ATOM    517  O   ARG A  64      14.430  15.008  28.475  1.00 18.06           O  
ATOM    518  CB  ARG A  64      13.944  12.794  26.366  1.00 21.88           C  
ATOM    519  CG  ARG A  64      14.166  11.589  25.436  1.00 26.25           C  
ATOM    520  CD  ARG A  64      14.825  10.409  26.150  1.00 28.51           C  
ATOM    521  NE  ARG A  64      15.006   9.247  25.275  1.00 31.62           N  
ATOM    522  CZ  ARG A  64      15.851   9.202  24.249  1.00 30.76           C  
ATOM    523  NH1 ARG A  64      16.605  10.253  23.959  1.00 32.05           N  
ATOM    524  NH2 ARG A  64      15.945   8.105  23.514  1.00 28.80           N  
ATOM    525  N   TRP A  65      14.986  16.015  26.533  1.00 20.51           N  
ATOM    526  CA  TRP A  65      14.705  17.364  26.990  1.00 20.59           C  
ATOM    527  C   TRP A  65      13.641  18.037  26.142  1.00 22.18           C  
ATOM    528  O   TRP A  65      13.517  17.779  24.944  1.00 23.16           O  
ATOM    529  CB  TRP A  65      15.985  18.194  26.957  1.00 20.38           C  
ATOM    530  CG  TRP A  65      17.047  17.656  27.847  1.00 20.31           C  
ATOM    531  CD1 TRP A  65      17.819  16.549  27.635  1.00 19.11           C  
ATOM    532  CD2 TRP A  65      17.414  18.165  29.129  1.00 21.43           C  
ATOM    533  NE1 TRP A  65      18.643  16.334  28.711  1.00 19.31           N  
ATOM    534  CE2 TRP A  65      18.417  17.312  29.646  1.00 21.21           C  
ATOM    535  CE3 TRP A  65      16.991  19.260  29.898  1.00 21.03           C  
ATOM    536  CZ2 TRP A  65      19.005  17.521  30.901  1.00 21.98           C  
ATOM    537  CZ3 TRP A  65      17.575  19.467  31.145  1.00 21.07           C  
ATOM    538  CH2 TRP A  65      18.572  18.599  31.632  1.00 21.32           C  
ATOM    539  N   PHE A  66      12.877  18.910  26.778  1.00 21.82           N  
ATOM    540  CA  PHE A  66      11.817  19.624  26.101  1.00 22.93           C  
ATOM    541  C   PHE A  66      11.582  20.921  26.840  1.00 23.41           C  
ATOM    542  O   PHE A  66      11.919  21.052  28.020  1.00 22.31           O  
ATOM    543  CB  PHE A  66      10.533  18.804  26.117  1.00 24.06           C  
ATOM    544  CG  PHE A  66      10.166  18.295  27.477  1.00 24.57           C  
ATOM    545  CD1 PHE A  66      10.705  17.105  27.951  1.00 24.77           C  
ATOM    546  CD2 PHE A  66       9.314  19.026  28.304  1.00 27.35           C  
ATOM    547  CE1 PHE A  66      10.406  16.648  29.233  1.00 24.68           C  
ATOM    548  CE2 PHE A  66       9.007  18.580  29.593  1.00 25.65           C  
ATOM    549  CZ  PHE A  66       9.555  17.388  30.059  1.00 25.06           C  
ATOM    550  N   GLY A  67      10.992  21.877  26.139  1.00 23.66           N  
ATOM    551  CA  GLY A  67      10.708  23.161  26.741  1.00 24.48           C  
ATOM    552  C   GLY A  67      10.205  24.159  25.723  1.00 24.18           C  
ATOM    553  O   GLY A  67       9.473  23.818  24.787  1.00 23.17           O  
ATOM    554  N   LYS A  68      10.603  25.408  25.912  1.00 23.22           N  
ATOM    555  CA  LYS A  68      10.197  26.466  25.012  1.00 22.00           C  
ATOM    556  C   LYS A  68      11.101  27.675  25.160  1.00 21.43           C  
ATOM    557  O   LYS A  68      11.735  27.874  26.197  1.00 22.12           O  
ATOM    558  CB  LYS A  68       8.741  26.856  25.272  1.00 21.97           C  
ATOM    559  CG  LYS A  68       8.458  27.389  26.669  1.00 23.83           C  
ATOM    560  CD  LYS A  68       6.952  27.585  26.894  1.00 22.77           C  
ATOM    561  CE  LYS A  68       6.187  26.244  26.988  1.00 22.45           C  
ATOM    562  NZ  LYS A  68       6.306  25.348  25.785  1.00 22.24           N  
ATOM    563  N   CYS A  69      11.155  28.470  24.097  1.00 21.26           N  
ATOM    564  CA  CYS A  69      11.979  29.673  24.033  1.00 20.68           C  
ATOM    565  C   CYS A  69      11.139  30.773  23.421  1.00 20.17           C  
ATOM    566  O   CYS A  69      10.146  30.502  22.746  1.00 21.09           O  
ATOM    567  CB  CYS A  69      13.179  29.429  23.124  1.00 20.52           C  
ATOM    568  SG  CYS A  69      12.679  29.163  21.399  1.00 21.91           S  
ATOM    569  N   TRP A  70      11.544  32.016  23.637  1.00 19.87           N  
ATOM    570  CA  TRP A  70      10.806  33.130  23.071  1.00 20.09           C  
ATOM    571  C   TRP A  70      11.714  34.271  22.623  1.00 19.91           C  
ATOM    572  O   TRP A  70      12.877  34.372  23.029  1.00 18.76           O  
ATOM    573  CB  TRP A  70       9.746  33.626  24.067  1.00 21.60           C  
ATOM    574  CG  TRP A  70      10.255  33.893  25.451  1.00 25.71           C  
ATOM    575  CD1 TRP A  70      10.710  35.085  25.949  1.00 26.35           C  
ATOM    576  CD2 TRP A  70      10.369  32.943  26.519  1.00 27.52           C  
ATOM    577  NE1 TRP A  70      11.098  34.936  27.262  1.00 28.44           N  
ATOM    578  CE2 TRP A  70      10.900  33.632  27.637  1.00 27.79           C  
ATOM    579  CE3 TRP A  70      10.074  31.576  26.641  1.00 27.90           C  
ATOM    580  CZ2 TRP A  70      11.144  32.999  28.864  1.00 27.91           C  
ATOM    581  CZ3 TRP A  70      10.316  30.943  27.864  1.00 30.15           C  
ATOM    582  CH2 TRP A  70      10.847  31.659  28.960  1.00 28.29           C  
ATOM    583  N   TYR A  71      11.165  35.110  21.755  1.00 18.35           N  
ATOM    584  CA  TYR A  71      11.872  36.257  21.210  1.00 18.56           C  
ATOM    585  C   TYR A  71      10.893  37.412  21.069  1.00 19.09           C  
ATOM    586  O   TYR A  71       9.890  37.295  20.362  1.00 20.12           O  
ATOM    587  CB  TYR A  71      12.437  35.924  19.835  1.00 19.50           C  
ATOM    588  CG  TYR A  71      13.239  37.033  19.205  1.00 19.47           C  
ATOM    589  CD1 TYR A  71      14.619  37.075  19.344  1.00 19.44           C  
ATOM    590  CD2 TYR A  71      12.622  38.006  18.419  1.00 20.26           C  
ATOM    591  CE1 TYR A  71      15.374  38.045  18.709  1.00 21.71           C  
ATOM    592  CE2 TYR A  71      13.365  38.989  17.778  1.00 20.98           C  
ATOM    593  CZ  TYR A  71      14.745  38.999  17.921  1.00 22.18           C  
ATOM    594  OH  TYR A  71      15.495  39.935  17.239  1.00 22.47           O  
ATOM    595  N   ILE A  72      11.194  38.523  21.738  1.00 17.90           N  
ATOM    596  CA  ILE A  72      10.348  39.708  21.701  1.00 15.82           C  
ATOM    597  C   ILE A  72      10.701  40.633  20.543  1.00 15.80           C  
ATOM    598  O   ILE A  72      11.789  41.207  20.490  1.00 15.49           O  
ATOM    599  CB  ILE A  72      10.447  40.506  23.018  1.00 15.34           C  
ATOM    600  CG1 ILE A  72       9.892  39.671  24.172  1.00 14.42           C  
ATOM    601  CG2 ILE A  72       9.675  41.816  22.899  1.00 14.67           C  
ATOM    602  CD1 ILE A  72       9.921  40.389  25.515  1.00 14.63           C  
ATOM    603  N   HIS A  73       9.759  40.773  19.619  1.00 16.98           N  
ATOM    604  CA  HIS A  73       9.930  41.618  18.448  1.00 16.03           C  
ATOM    605  C   HIS A  73       8.881  42.731  18.498  1.00 16.19           C  
ATOM    606  O   HIS A  73       7.677  42.465  18.440  1.00 17.33           O  
ATOM    607  CB  HIS A  73       9.776  40.766  17.186  1.00 18.02           C  
ATOM    608  CG  HIS A  73      10.068  41.508  15.924  1.00 19.38           C  
ATOM    609  ND1 HIS A  73       9.204  42.442  15.395  1.00 19.47           N  
ATOM    610  CD2 HIS A  73      11.155  41.502  15.117  1.00 20.27           C  
ATOM    611  CE1 HIS A  73       9.745  42.981  14.319  1.00 19.61           C  
ATOM    612  NE2 HIS A  73      10.930  42.429  14.128  1.00 21.41           N  
ATOM    613  N   ASP A  74       9.343  43.976  18.622  1.00 15.93           N  
ATOM    614  CA  ASP A  74       8.450  45.134  18.716  1.00 14.81           C  
ATOM    615  C   ASP A  74       7.397  44.942  19.811  1.00 15.40           C  
ATOM    616  O   ASP A  74       6.202  45.078  19.552  1.00 12.20           O  
ATOM    617  CB  ASP A  74       7.733  45.375  17.387  1.00 15.05           C  
ATOM    618  CG  ASP A  74       8.666  45.829  16.292  1.00 15.90           C  
ATOM    619  OD1 ASP A  74       9.843  46.104  16.597  1.00 17.51           O  
ATOM    620  OD2 ASP A  74       8.219  45.926  15.124  1.00 16.57           O  
ATOM    621  N   LEU A  75       7.846  44.624  21.025  1.00 17.88           N  
ATOM    622  CA  LEU A  75       6.947  44.408  22.161  1.00 18.60           C  
ATOM    623  C   LEU A  75       6.184  43.078  22.126  1.00 20.07           C  
ATOM    624  O   LEU A  75       5.782  42.572  23.169  1.00 19.84           O  
ATOM    625  CB  LEU A  75       5.959  45.578  22.285  1.00 19.54           C  
ATOM    626  CG  LEU A  75       6.430  46.778  23.121  1.00 20.46           C  
ATOM    627  CD1 LEU A  75       7.889  47.085  22.815  1.00 18.36           C  
ATOM    628  CD2 LEU A  75       5.544  47.992  22.842  1.00 18.89           C  
ATOM    629  N   LEU A  76       5.974  42.507  20.945  1.00 20.05           N  
ATOM    630  CA  LEU A  76       5.275  41.230  20.890  1.00 20.66           C  
ATOM    631  C   LEU A  76       6.230  40.088  21.262  1.00 20.63           C  
ATOM    632  O   LEU A  76       7.413  40.115  20.917  1.00 20.30           O  
ATOM    633  CB  LEU A  76       4.662  40.992  19.502  1.00 20.02           C  
ATOM    634  CG  LEU A  76       3.385  41.788  19.213  1.00 21.95           C  
ATOM    635  CD1 LEU A  76       2.918  41.535  17.786  1.00 22.53           C  
ATOM    636  CD2 LEU A  76       2.300  41.397  20.207  1.00 20.35           C  
ATOM    637  N   LYS A  77       5.707  39.099  21.983  1.00 19.26           N  
ATOM    638  CA  LYS A  77       6.491  37.952  22.417  1.00 19.26           C  
ATOM    639  C   LYS A  77       6.099  36.728  21.597  1.00 19.70           C  
ATOM    640  O   LYS A  77       4.928  36.351  21.543  1.00 19.67           O  
ATOM    641  CB  LYS A  77       6.244  37.685  23.910  1.00 20.01           C  
ATOM    642  CG  LYS A  77       7.219  36.705  24.564  1.00 21.36           C  
ATOM    643  CD  LYS A  77       6.890  36.463  26.037  1.00 22.63           C  
ATOM    644  CE  LYS A  77       6.867  37.761  26.840  1.00 23.78           C  
ATOM    645  NZ  LYS A  77       6.639  37.536  28.309  1.00 24.69           N  
ATOM    646  N   TYR A  78       7.084  36.119  20.951  1.00 20.14           N  
ATOM    647  CA  TYR A  78       6.855  34.934  20.136  1.00 20.48           C  
ATOM    648  C   TYR A  78       7.486  33.728  20.805  1.00 20.31           C  
ATOM    649  O   TYR A  78       8.700  33.688  21.000  1.00 19.81           O  
ATOM    650  CB  TYR A  78       7.470  35.131  18.762  1.00 19.67           C  
ATOM    651  CG  TYR A  78       6.785  36.194  17.942  1.00 20.47           C  
ATOM    652  CD1 TYR A  78       6.045  35.851  16.811  1.00 21.62           C  
ATOM    653  CD2 TYR A  78       6.907  37.546  18.269  1.00 20.88           C  
ATOM    654  CE1 TYR A  78       5.452  36.825  16.020  1.00 20.96           C  
ATOM    655  CE2 TYR A  78       6.314  38.530  17.482  1.00 20.64           C  
ATOM    656  CZ  TYR A  78       5.594  38.156  16.359  1.00 19.97           C  
ATOM    657  OH  TYR A  78       5.046  39.111  15.547  1.00 23.01           O  
ATOM    658  N   GLU A  79       6.661  32.738  21.132  1.00 19.71           N  
ATOM    659  CA  GLU A  79       7.122  31.530  21.814  1.00 19.71           C  
ATOM    660  C   GLU A  79       7.179  30.318  20.889  1.00 18.24           C  
ATOM    661  O   GLU A  79       6.295  30.116  20.053  1.00 16.71           O  
ATOM    662  CB  GLU A  79       6.181  31.228  22.987  1.00 22.41           C  
ATOM    663  CG  GLU A  79       6.862  30.839  24.297  1.00 27.41           C  
ATOM    664  CD  GLU A  79       5.867  30.588  25.438  1.00 30.04           C  
ATOM    665  OE1 GLU A  79       6.283  30.638  26.618  1.00 31.55           O  
ATOM    666  OE2 GLU A  79       4.674  30.326  25.161  1.00 29.52           O  
ATOM    667  N   PHE A  80       8.227  29.516  21.047  1.00 18.20           N  
ATOM    668  CA  PHE A  80       8.393  28.305  20.250  1.00 17.35           C  
ATOM    669  C   PHE A  80       8.832  27.133  21.125  1.00 17.01           C  
ATOM    670  O   PHE A  80       9.674  27.282  22.012  1.00 15.66           O  
ATOM    671  CB  PHE A  80       9.404  28.537  19.125  1.00 17.26           C  
ATOM    672  CG  PHE A  80       9.059  29.703  18.251  1.00 15.88           C  
ATOM    673  CD1 PHE A  80       9.348  31.001  18.661  1.00 15.07           C  
ATOM    674  CD2 PHE A  80       8.382  29.515  17.056  1.00 13.00           C  
ATOM    675  CE1 PHE A  80       8.965  32.091  17.898  1.00 14.10           C  
ATOM    676  CE2 PHE A  80       7.995  30.604  16.287  1.00 14.63           C  
ATOM    677  CZ  PHE A  80       8.287  31.895  16.711  1.00 14.64           C  
ATOM    678  N   ASP A  81       8.246  25.966  20.875  1.00 17.73           N  
ATOM    679  CA  ASP A  81       8.563  24.763  21.632  1.00 18.76           C  
ATOM    680  C   ASP A  81       9.867  24.149  21.147  1.00 19.01           C  
ATOM    681  O   ASP A  81      10.088  24.031  19.942  1.00 18.73           O  
ATOM    682  CB  ASP A  81       7.422  23.752  21.503  1.00 20.15           C  
ATOM    683  CG  ASP A  81       6.175  24.201  22.226  1.00 22.99           C  
ATOM    684  OD1 ASP A  81       5.712  25.336  21.966  1.00 24.87           O  
ATOM    685  OD2 ASP A  81       5.653  23.428  23.061  1.00 24.58           O  
ATOM    686  N   ILE A  82      10.727  23.769  22.092  1.00 19.89           N  
ATOM    687  CA  ILE A  82      12.022  23.169  21.771  1.00 20.83           C  
ATOM    688  C   ILE A  82      12.177  21.769  22.367  1.00 19.61           C  
ATOM    689  O   ILE A  82      11.568  21.440  23.384  1.00 18.49           O  
ATOM    690  CB  ILE A  82      13.200  24.059  22.259  1.00 21.04           C  
ATOM    691  CG1 ILE A  82      13.014  24.426  23.729  1.00 20.34           C  
ATOM    692  CG2 ILE A  82      13.297  25.317  21.410  1.00 19.94           C  
ATOM    693  CD1 ILE A  82      14.165  25.260  24.291  1.00 22.50           C  
ATOM    694  N   GLU A  83      13.004  20.950  21.726  1.00 20.31           N  
ATOM    695  CA  GLU A  83      13.218  19.577  22.178  1.00 20.68           C  
ATOM    696  C   GLU A  83      14.448  18.923  21.560  1.00 18.09           C  
ATOM    697  O   GLU A  83      14.852  19.258  20.449  1.00 18.48           O  
ATOM    698  CB  GLU A  83      11.980  18.749  21.842  1.00 21.78           C  
ATOM    699  CG  GLU A  83      11.470  19.013  20.438  1.00 25.05           C  
ATOM    700  CD  GLU A  83      10.029  18.602  20.238  1.00 27.13           C  
ATOM    701  OE1 GLU A  83       9.771  17.377  20.133  1.00 28.20           O  
ATOM    702  OE2 GLU A  83       9.159  19.511  20.193  1.00 26.04           O  
ATOM    703  N   PHE A  84      15.041  17.991  22.295  1.00 18.07           N  
ATOM    704  CA  PHE A  84      16.219  17.263  21.825  1.00 18.52           C  
ATOM    705  C   PHE A  84      16.544  16.114  22.759  1.00 18.56           C  
ATOM    706  O   PHE A  84      16.212  16.140  23.947  1.00 18.53           O  
ATOM    707  CB  PHE A  84      17.450  18.181  21.720  1.00 17.93           C  
ATOM    708  CG  PHE A  84      17.781  18.903  22.995  1.00 17.01           C  
ATOM    709  CD1 PHE A  84      17.116  20.081  23.336  1.00 18.17           C  
ATOM    710  CD2 PHE A  84      18.736  18.392  23.868  1.00 15.59           C  
ATOM    711  CE1 PHE A  84      17.397  20.743  24.535  1.00 17.58           C  
ATOM    712  CE2 PHE A  84      19.026  19.041  25.066  1.00 16.89           C  
ATOM    713  CZ  PHE A  84      18.355  20.222  25.404  1.00 19.09           C  
ATOM    714  N   ASP A  85      17.206  15.104  22.215  1.00 19.81           N  
ATOM    715  CA  ASP A  85      17.579  13.951  23.010  1.00 20.67           C  
ATOM    716  C   ASP A  85      19.076  13.924  23.202  1.00 21.36           C  
ATOM    717  O   ASP A  85      19.840  14.181  22.271  1.00 21.25           O  
ATOM    718  CB  ASP A  85      17.153  12.654  22.326  1.00 22.04           C  
ATOM    719  CG  ASP A  85      15.719  12.681  21.871  1.00 22.41           C  
ATOM    720  OD1 ASP A  85      14.892  13.338  22.548  1.00 27.23           O  
ATOM    721  OD2 ASP A  85      15.419  12.030  20.843  1.00 24.32           O  
ATOM    722  N   ILE A  86      19.491  13.606  24.418  1.00 22.34           N  
ATOM    723  CA  ILE A  86      20.900  13.520  24.733  1.00 22.57           C  
ATOM    724  C   ILE A  86      21.478  12.308  24.009  1.00 22.54           C  
ATOM    725  O   ILE A  86      21.031  11.183  24.228  1.00 25.04           O  
ATOM    726  CB  ILE A  86      21.099  13.350  26.251  1.00 22.56           C  
ATOM    727  CG1 ILE A  86      20.598  14.601  26.982  1.00 23.54           C  
ATOM    728  CG2 ILE A  86      22.555  13.062  26.560  1.00 22.64           C  
ATOM    729  CD1 ILE A  86      21.244  15.898  26.520  1.00 22.93           C  
ATOM    730  N   PRO A  87      22.446  12.526  23.099  1.00 22.77           N  
ATOM    731  CA  PRO A  87      23.053  11.402  22.374  1.00 23.08           C  
ATOM    732  C   PRO A  87      23.881  10.536  23.328  1.00 24.17           C  
ATOM    733  O   PRO A  87      24.348  11.020  24.365  1.00 24.22           O  
ATOM    734  CB  PRO A  87      23.904  12.090  21.301  1.00 21.30           C  
ATOM    735  CG  PRO A  87      24.210  13.428  21.905  1.00 22.50           C  
ATOM    736  CD  PRO A  87      22.906  13.813  22.552  1.00 22.36           C  
ATOM    737  N   ILE A  88      24.058   9.262  22.978  1.00 24.80           N  
ATOM    738  CA  ILE A  88      24.807   8.324  23.822  1.00 23.93           C  
ATOM    739  C   ILE A  88      26.234   8.788  24.114  1.00 24.36           C  
ATOM    740  O   ILE A  88      26.900   8.249  24.995  1.00 25.05           O  
ATOM    741  CB  ILE A  88      24.883   6.913  23.190  1.00 25.14           C  
ATOM    742  CG1 ILE A  88      25.185   5.877  24.278  1.00 26.22           C  
ATOM    743  CG2 ILE A  88      25.979   6.881  22.114  1.00 26.56           C  
ATOM    744  CD1 ILE A  88      25.129   4.430  23.806  1.00 25.87           C  
ATOM    745  N   THR A  89      26.705   9.787  23.381  1.00 23.61           N  
ATOM    746  CA  THR A  89      28.051  10.291  23.605  1.00 25.88           C  
ATOM    747  C   THR A  89      28.025  11.782  23.932  1.00 26.88           C  
ATOM    748  O   THR A  89      29.047  12.454  23.850  1.00 24.03           O  
ATOM    749  CB  THR A  89      28.948  10.033  22.362  1.00 25.15           C  
ATOM    750  OG1 THR A  89      28.240  10.394  21.171  1.00 22.06           O  
ATOM    751  CG2 THR A  89      29.332   8.564  22.277  1.00 23.58           C  
ATOM    752  N   TYR A  90      26.852  12.270  24.339  1.00 29.66           N  
ATOM    753  CA  TYR A  90      26.619  13.686  24.650  1.00 31.21           C  
ATOM    754  C   TYR A  90      27.786  14.562  25.102  1.00 33.23           C  
ATOM    755  O   TYR A  90      28.121  15.546  24.426  1.00 34.64           O  
ATOM    756  CB  TYR A  90      25.496  13.844  25.682  1.00 32.07           C  
ATOM    757  CG  TYR A  90      25.519  15.188  26.400  1.00 31.50           C  
ATOM    758  CD1 TYR A  90      25.803  15.263  27.770  1.00 29.96           C  
ATOM    759  CD2 TYR A  90      25.296  16.387  25.705  1.00 31.48           C  
ATOM    760  CE1 TYR A  90      25.867  16.495  28.433  1.00 28.89           C  
ATOM    761  CE2 TYR A  90      25.361  17.627  26.363  1.00 30.00           C  
ATOM    762  CZ  TYR A  90      25.648  17.667  27.727  1.00 29.81           C  
ATOM    763  OH  TYR A  90      25.724  18.876  28.377  1.00 30.12           O  
ATOM    764  N   PRO A  91      28.407  14.234  26.251  1.00 32.48           N  
ATOM    765  CA  PRO A  91      29.526  15.050  26.739  1.00 31.61           C  
ATOM    766  C   PRO A  91      30.476  15.460  25.616  1.00 31.22           C  
ATOM    767  O   PRO A  91      30.678  16.649  25.369  1.00 32.30           O  
ATOM    768  CB  PRO A  91      30.172  14.160  27.799  1.00 30.25           C  
ATOM    769  CG  PRO A  91      29.820  12.774  27.350  1.00 32.74           C  
ATOM    770  CD  PRO A  91      28.394  12.910  26.894  1.00 31.86           C  
ATOM    771  N   THR A  92      31.033  14.477  24.917  1.00 29.86           N  
ATOM    772  CA  THR A  92      31.956  14.745  23.825  1.00 29.90           C  
ATOM    773  C   THR A  92      31.246  15.230  22.562  1.00 29.48           C  
ATOM    774  O   THR A  92      31.792  16.034  21.806  1.00 28.44           O  
ATOM    775  CB  THR A  92      32.787  13.489  23.498  1.00 29.54           C  
ATOM    776  OG1 THR A  92      33.622  13.753  22.365  1.00 30.81           O  
ATOM    777  CG2 THR A  92      31.882  12.308  23.205  1.00 29.17           C  
ATOM    778  N   THR A  93      30.030  14.743  22.339  1.00 29.81           N  
ATOM    779  CA  THR A  93      29.229  15.133  21.177  1.00 29.63           C  
ATOM    780  C   THR A  93      28.419  16.373  21.550  1.00 30.46           C  
ATOM    781  O   THR A  93      28.903  17.237  22.271  1.00 32.34           O  
ATOM    782  CB  THR A  93      28.233  14.019  20.784  1.00 29.98           C  
ATOM    783  OG1 THR A  93      28.861  12.743  20.944  1.00 30.48           O  
ATOM    784  CG2 THR A  93      27.794  14.176  19.336  1.00 28.93           C  
ATOM    785  N   ALA A  94      27.179  16.445  21.073  1.00 29.56           N  
ATOM    786  CA  ALA A  94      26.290  17.572  21.358  1.00 27.67           C  
ATOM    787  C   ALA A  94      24.908  17.249  20.814  1.00 26.38           C  
ATOM    788  O   ALA A  94      24.777  16.653  19.746  1.00 28.74           O  
ATOM    789  CB  ALA A  94      26.818  18.846  20.710  1.00 27.64           C  
ATOM    790  N   PRO A  95      23.852  17.619  21.554  1.00 24.52           N  
ATOM    791  CA  PRO A  95      22.484  17.346  21.097  1.00 23.19           C  
ATOM    792  C   PRO A  95      22.032  18.210  19.918  1.00 21.95           C  
ATOM    793  O   PRO A  95      22.643  19.237  19.615  1.00 20.79           O  
ATOM    794  CB  PRO A  95      21.647  17.588  22.351  1.00 22.56           C  
ATOM    795  CG  PRO A  95      22.461  18.582  23.120  1.00 23.42           C  
ATOM    796  CD  PRO A  95      23.855  18.060  22.960  1.00 22.93           C  
ATOM    797  N   GLU A  96      20.969  17.775  19.246  1.00 22.16           N  
ATOM    798  CA  GLU A  96      20.446  18.514  18.107  1.00 21.91           C  
ATOM    799  C   GLU A  96      19.173  19.240  18.493  1.00 20.46           C  
ATOM    800  O   GLU A  96      18.083  18.684  18.421  1.00 19.82           O  
ATOM    801  CB  GLU A  96      20.162  17.582  16.923  1.00 21.27           C  
ATOM    802  CG  GLU A  96      21.381  16.833  16.397  1.00 24.28           C  
ATOM    803  CD  GLU A  96      21.058  15.929  15.218  1.00 26.36           C  
ATOM    804  OE1 GLU A  96      20.783  16.455  14.115  1.00 28.62           O  
ATOM    805  OE2 GLU A  96      21.066  14.692  15.393  1.00 24.91           O  
ATOM    806  N   ILE A  97      19.325  20.489  18.914  1.00 20.10           N  
ATOM    807  CA  ILE A  97      18.190  21.304  19.303  1.00 21.08           C  
ATOM    808  C   ILE A  97      17.158  21.288  18.182  1.00 20.42           C  
ATOM    809  O   ILE A  97      17.509  21.351  17.002  1.00 19.01           O  
ATOM    810  CB  ILE A  97      18.621  22.740  19.539  1.00 21.38           C  
ATOM    811  CG1 ILE A  97      19.840  22.756  20.463  1.00 22.73           C  
ATOM    812  CG2 ILE A  97      17.463  23.522  20.126  1.00 20.69           C  
ATOM    813  CD1 ILE A  97      20.513  24.115  20.560  1.00 25.47           C  
ATOM    814  N   ALA A  98      15.885  21.207  18.548  1.00 18.63           N  
ATOM    815  CA  ALA A  98      14.826  21.188  17.556  1.00 15.97           C  
ATOM    816  C   ALA A  98      13.655  22.073  17.915  1.00 16.91           C  
ATOM    817  O   ALA A  98      13.157  22.053  19.045  1.00 15.94           O  
ATOM    818  CB  ALA A  98      14.336  19.761  17.336  1.00 14.75           C  
ATOM    819  N   VAL A  99      13.243  22.876  16.943  1.00 15.75           N  
ATOM    820  CA  VAL A  99      12.086  23.742  17.096  1.00 17.09           C  
ATOM    821  C   VAL A  99      11.136  23.314  15.969  1.00 18.96           C  
ATOM    822  O   VAL A  99      11.203  23.813  14.834  1.00 18.45           O  
ATOM    823  CB  VAL A  99      12.459  25.266  17.016  1.00 16.71           C  
ATOM    824  CG1 VAL A  99      13.287  25.576  15.772  1.00 20.25           C  
ATOM    825  CG2 VAL A  99      11.182  26.105  17.038  1.00 17.62           C  
ATOM    826  N   PRO A 100      10.268  22.327  16.271  1.00 19.82           N  
ATOM    827  CA  PRO A 100       9.261  21.727  15.389  1.00 21.28           C  
ATOM    828  C   PRO A 100       8.299  22.693  14.714  1.00 23.07           C  
ATOM    829  O   PRO A 100       8.018  22.555  13.523  1.00 23.98           O  
ATOM    830  CB  PRO A 100       8.541  20.732  16.307  1.00 21.75           C  
ATOM    831  CG  PRO A 100       8.835  21.250  17.696  1.00 21.15           C  
ATOM    832  CD  PRO A 100      10.263  21.649  17.575  1.00 20.15           C  
ATOM    833  N   GLU A 101       7.794  23.661  15.474  1.00 24.70           N  
ATOM    834  CA  GLU A 101       6.858  24.646  14.943  1.00 25.50           C  
ATOM    835  C   GLU A 101       7.348  25.262  13.644  1.00 26.50           C  
ATOM    836  O   GLU A 101       6.594  25.394  12.679  1.00 27.66           O  
ATOM    837  CB  GLU A 101       6.612  25.755  15.974  1.00 26.35           C  
ATOM    838  CG  GLU A 101       5.586  25.375  17.039  1.00 28.88           C  
ATOM    839  CD  GLU A 101       5.367  26.450  18.099  1.00 31.37           C  
ATOM    840  OE1 GLU A 101       5.159  27.634  17.734  1.00 31.34           O  
ATOM    841  OE2 GLU A 101       5.386  26.099  19.303  1.00 30.33           O  
ATOM    842  N   LEU A 102       8.625  25.622  13.624  1.00 27.93           N  
ATOM    843  CA  LEU A 102       9.224  26.247  12.461  1.00 28.88           C  
ATOM    844  C   LEU A 102       9.628  25.285  11.348  1.00 29.07           C  
ATOM    845  O   LEU A 102       9.919  25.724  10.236  1.00 29.86           O  
ATOM    846  CB  LEU A 102      10.435  27.074  12.895  1.00 28.35           C  
ATOM    847  CG  LEU A 102      10.122  28.186  13.900  1.00 28.86           C  
ATOM    848  CD1 LEU A 102      11.396  28.924  14.299  1.00 28.87           C  
ATOM    849  CD2 LEU A 102       9.120  29.141  13.289  1.00 28.53           C  
ATOM    850  N   ASP A 103       9.635  23.984  11.629  1.00 30.19           N  
ATOM    851  CA  ASP A 103      10.022  23.000  10.618  1.00 31.20           C  
ATOM    852  C   ASP A 103       9.393  23.348   9.269  1.00 32.50           C  
ATOM    853  O   ASP A 103       8.202  23.652   9.183  1.00 33.52           O  
ATOM    854  CB  ASP A 103       9.625  21.581  11.068  1.00 30.25           C  
ATOM    855  CG  ASP A 103      10.134  20.486  10.120  1.00 30.70           C  
ATOM    856  OD1 ASP A 103      11.251  20.622   9.570  1.00 31.09           O  
ATOM    857  OD2 ASP A 103       9.420  19.472   9.940  1.00 29.91           O  
ATOM    858  N   GLY A 104      10.219  23.333   8.226  1.00 34.25           N  
ATOM    859  CA  GLY A 104       9.747  23.651   6.889  1.00 36.48           C  
ATOM    860  C   GLY A 104       9.311  25.097   6.730  1.00 38.55           C  
ATOM    861  O   GLY A 104       8.194  25.364   6.283  1.00 40.43           O  
ATOM    862  N   LYS A 105      10.195  26.027   7.088  1.00 39.10           N  
ATOM    863  CA  LYS A 105       9.917  27.464   7.005  1.00 38.81           C  
ATOM    864  C   LYS A 105      11.198  28.276   6.832  1.00 38.36           C  
ATOM    865  O   LYS A 105      11.154  29.489   6.627  1.00 37.71           O  
ATOM    866  CB  LYS A 105       9.190  27.934   8.270  1.00 40.11           C  
ATOM    867  CG  LYS A 105       7.693  27.647   8.274  1.00 41.52           C  
ATOM    868  CD  LYS A 105       7.032  28.106   9.568  1.00 42.36           C  
ATOM    869  CE  LYS A 105       5.529  28.269   9.397  1.00 41.69           C  
ATOM    870  NZ  LYS A 105       5.189  29.414   8.501  1.00 42.51           N  
ATOM    871  N   THR A 106      12.334  27.591   6.913  1.00 37.94           N  
ATOM    872  CA  THR A 106      13.635  28.231   6.781  1.00 37.34           C  
ATOM    873  C   THR A 106      14.666  27.246   6.260  1.00 37.69           C  
ATOM    874  O   THR A 106      14.875  26.186   6.849  1.00 38.20           O  
ATOM    875  CB  THR A 106      14.143  28.739   8.131  1.00 37.86           C  
ATOM    876  OG1 THR A 106      13.133  29.545   8.746  1.00 37.85           O  
ATOM    877  CG2 THR A 106      15.418  29.557   7.945  1.00 37.99           C  
ATOM    878  N   ALA A 107      15.317  27.616   5.165  1.00 38.53           N  
ATOM    879  CA  ALA A 107      16.340  26.788   4.551  1.00 38.96           C  
ATOM    880  C   ALA A 107      17.422  26.441   5.567  1.00 39.89           C  
ATOM    881  O   ALA A 107      17.990  25.346   5.538  1.00 40.38           O  
ATOM    882  CB  ALA A 107      16.950  27.523   3.375  1.00 37.60           C  
ATOM    883  N   LYS A 108      17.690  27.382   6.471  1.00 39.72           N  
ATOM    884  CA  LYS A 108      18.706  27.222   7.512  1.00 39.93           C  
ATOM    885  C   LYS A 108      18.181  26.383   8.674  1.00 40.12           C  
ATOM    886  O   LYS A 108      17.999  26.890   9.778  1.00 39.65           O  
ATOM    887  CB  LYS A 108      19.140  28.607   8.016  1.00 39.26           C  
ATOM    888  CG  LYS A 108      19.606  29.538   6.900  1.00 39.18           C  
ATOM    889  CD  LYS A 108      19.626  30.995   7.336  1.00 39.08           C  
ATOM    890  CE  LYS A 108      19.618  31.925   6.131  1.00 37.09           C  
ATOM    891  NZ  LYS A 108      18.453  31.652   5.233  1.00 37.07           N  
HETATM  892  N   MSE A 109      17.954  25.096   8.422  1.00 41.05           N  
HETATM  893  CA  MSE A 109      17.432  24.190   9.444  1.00 43.69           C  
HETATM  894  C   MSE A 109      17.291  22.779   8.857  1.00 44.27           C  
HETATM  895  O   MSE A 109      16.909  22.619   7.696  1.00 44.64           O  
HETATM  896  CB  MSE A 109      16.078  24.721   9.933  1.00 44.21           C  
HETATM  897  CG  MSE A 109      15.447  23.991  11.106  1.00 44.51           C  
HETATM  898 SE   MSE A 109      14.011  25.068  11.894  1.00 48.46          SE  
HETATM  899  CE  MSE A 109      12.915  25.244  10.297  1.00 46.32           C  
ATOM    900  N   TYR A 110      17.610  21.763   9.657  1.00 44.82           N  
ATOM    901  CA  TYR A 110      17.528  20.375   9.207  1.00 46.05           C  
ATOM    902  C   TYR A 110      16.114  19.812   9.188  1.00 46.56           C  
ATOM    903  O   TYR A 110      15.145  20.509   9.484  1.00 46.54           O  
ATOM    904  CB  TYR A 110      18.409  19.465  10.074  1.00 46.79           C  
ATOM    905  CG  TYR A 110      19.874  19.541   9.741  1.00 46.96           C  
ATOM    906  CD1 TYR A 110      20.740  20.338  10.487  1.00 47.59           C  
ATOM    907  CD2 TYR A 110      20.386  18.858   8.642  1.00 47.50           C  
ATOM    908  CE1 TYR A 110      22.085  20.459  10.142  1.00 49.41           C  
ATOM    909  CE2 TYR A 110      21.725  18.970   8.284  1.00 49.20           C  
ATOM    910  CZ  TYR A 110      22.570  19.774   9.034  1.00 49.48           C  
ATOM    911  OH  TYR A 110      23.890  19.919   8.660  1.00 51.19           O  
ATOM    912  N   ARG A 111      16.013  18.534   8.840  1.00 46.91           N  
ATOM    913  CA  ARG A 111      14.731  17.850   8.771  1.00 47.42           C  
ATOM    914  C   ARG A 111      14.158  17.679  10.180  1.00 46.57           C  
ATOM    915  O   ARG A 111      14.901  17.464  11.139  1.00 45.62           O  
ATOM    916  CB  ARG A 111      14.919  16.484   8.098  1.00 49.97           C  
ATOM    917  CG  ARG A 111      13.834  16.107   7.084  1.00 52.90           C  
ATOM    918  CD  ARG A 111      13.674  17.184   6.006  1.00 55.44           C  
ATOM    919  NE  ARG A 111      12.863  16.734   4.871  1.00 56.75           N  
ATOM    920  CZ  ARG A 111      13.271  15.852   3.963  1.00 57.89           C  
ATOM    921  NH1 ARG A 111      12.471  15.500   2.967  1.00 57.93           N  
ATOM    922  NH2 ARG A 111      14.485  15.326   4.047  1.00 58.83           N  
ATOM    923  N   GLY A 112      12.838  17.792  10.300  1.00 45.51           N  
ATOM    924  CA  GLY A 112      12.200  17.649  11.596  1.00 43.49           C  
ATOM    925  C   GLY A 112      12.299  18.890  12.467  1.00 42.29           C  
ATOM    926  O   GLY A 112      11.795  18.912  13.592  1.00 42.28           O  
ATOM    927  N   GLY A 113      12.960  19.923  11.955  1.00 40.35           N  
ATOM    928  CA  GLY A 113      13.094  21.160  12.704  1.00 38.33           C  
ATOM    929  C   GLY A 113      14.413  21.319  13.434  1.00 36.23           C  
ATOM    930  O   GLY A 113      14.606  22.283  14.177  1.00 33.52           O  
ATOM    931  N   LYS A 114      15.324  20.373  13.230  1.00 36.78           N  
ATOM    932  CA  LYS A 114      16.627  20.430  13.882  1.00 38.29           C  
ATOM    933  C   LYS A 114      17.348  21.707  13.475  1.00 39.02           C  
ATOM    934  O   LYS A 114      17.378  22.078  12.301  1.00 38.81           O  
ATOM    935  CB  LYS A 114      17.469  19.206  13.507  1.00 38.00           C  
ATOM    936  CG  LYS A 114      16.864  17.874  13.951  1.00 39.30           C  
ATOM    937  CD  LYS A 114      17.676  16.666  13.456  1.00 41.65           C  
ATOM    938  CE  LYS A 114      17.789  16.638  11.922  1.00 42.54           C  
ATOM    939  NZ  LYS A 114      18.527  15.448  11.380  1.00 43.32           N  
ATOM    940  N   ILE A 115      17.916  22.386  14.461  1.00 40.69           N  
ATOM    941  CA  ILE A 115      18.633  23.623  14.217  1.00 42.90           C  
ATOM    942  C   ILE A 115      20.012  23.304  13.666  1.00 45.76           C  
ATOM    943  O   ILE A 115      20.577  22.245  13.953  1.00 46.50           O  
ATOM    944  CB  ILE A 115      18.795  24.437  15.522  1.00 42.66           C  
ATOM    945  CG1 ILE A 115      17.417  24.844  16.062  1.00 42.60           C  
ATOM    946  CG2 ILE A 115      19.674  25.646  15.279  1.00 42.19           C  
ATOM    947  CD1 ILE A 115      16.598  25.702  15.115  1.00 42.25           C  
ATOM    948  N   CYS A 116      20.549  24.220  12.867  1.00 47.45           N  
ATOM    949  CA  CYS A 116      21.874  24.038  12.290  1.00 49.17           C  
ATOM    950  C   CYS A 116      22.740  25.273  12.510  1.00 48.66           C  
ATOM    951  O   CYS A 116      22.549  26.304  11.872  1.00 48.33           O  
ATOM    952  CB  CYS A 116      21.766  23.719  10.794  1.00 51.80           C  
ATOM    953  SG  CYS A 116      20.639  24.768   9.843  1.00 58.04           S  
ATOM    954  N   LEU A 117      23.696  25.156  13.424  1.00 48.31           N  
ATOM    955  CA  LEU A 117      24.585  26.261  13.738  1.00 47.52           C  
ATOM    956  C   LEU A 117      25.608  26.494  12.634  1.00 47.93           C  
ATOM    957  O   LEU A 117      25.573  25.837  11.588  1.00 46.89           O  
ATOM    958  CB  LEU A 117      25.313  25.998  15.060  1.00 46.96           C  
ATOM    959  CG  LEU A 117      24.476  25.699  16.307  1.00 46.51           C  
ATOM    960  CD1 LEU A 117      23.323  26.687  16.410  1.00 46.59           C  
ATOM    961  CD2 LEU A 117      23.954  24.283  16.235  1.00 46.17           C  
ATOM    962  N   THR A 118      26.507  27.445  12.884  1.00 48.68           N  
ATOM    963  CA  THR A 118      27.571  27.792  11.946  1.00 49.02           C  
ATOM    964  C   THR A 118      28.698  26.777  12.045  1.00 48.65           C  
ATOM    965  O   THR A 118      28.934  26.198  13.107  1.00 47.64           O  
ATOM    966  CB  THR A 118      28.170  29.201  12.230  1.00 48.86           C  
ATOM    967  OG1 THR A 118      28.010  29.528  13.616  1.00 49.26           O  
ATOM    968  CG2 THR A 118      27.503  30.264  11.367  1.00 48.44           C  
ATOM    969  N   ASP A 119      29.387  26.572  10.927  1.00 49.17           N  
ATOM    970  CA  ASP A 119      30.498  25.631  10.852  1.00 49.78           C  
ATOM    971  C   ASP A 119      31.561  25.982  11.892  1.00 49.37           C  
ATOM    972  O   ASP A 119      32.444  25.180  12.196  1.00 49.90           O  
ATOM    973  CB  ASP A 119      31.115  25.657   9.442  1.00 50.45           C  
ATOM    974  CG  ASP A 119      30.320  26.517   8.461  1.00 50.27           C  
ATOM    975  OD1 ASP A 119      30.239  27.745   8.675  1.00 50.63           O  
ATOM    976  OD2 ASP A 119      29.781  25.967   7.475  1.00 50.00           O  
ATOM    977  N   HIS A 120      31.459  27.185  12.443  1.00 48.53           N  
ATOM    978  CA  HIS A 120      32.411  27.660  13.441  1.00 46.91           C  
ATOM    979  C   HIS A 120      31.965  27.244  14.839  1.00 45.91           C  
ATOM    980  O   HIS A 120      32.558  27.662  15.833  1.00 46.69           O  
ATOM    981  CB  HIS A 120      32.517  29.184  13.347  1.00 47.17           C  
ATOM    982  CG  HIS A 120      32.690  29.686  11.944  1.00 46.67           C  
ATOM    983  ND1 HIS A 120      32.441  30.992  11.581  1.00 45.86           N  
ATOM    984  CD2 HIS A 120      33.064  29.046  10.810  1.00 45.56           C  
ATOM    985  CE1 HIS A 120      32.650  31.134  10.284  1.00 45.36           C  
ATOM    986  NE2 HIS A 120      33.029  29.968   9.793  1.00 45.95           N  
ATOM    987  N   PHE A 121      30.928  26.407  14.900  1.00 44.51           N  
ATOM    988  CA  PHE A 121      30.376  25.929  16.168  1.00 41.48           C  
ATOM    989  C   PHE A 121      31.073  24.689  16.720  1.00 40.60           C  
ATOM    990  O   PHE A 121      31.727  24.752  17.762  1.00 41.20           O  
ATOM    991  CB  PHE A 121      28.880  25.623  16.021  1.00 39.85           C  
ATOM    992  CG  PHE A 121      28.258  25.027  17.258  1.00 38.92           C  
ATOM    993  CD1 PHE A 121      27.944  25.828  18.353  1.00 39.72           C  
ATOM    994  CD2 PHE A 121      28.020  23.658  17.343  1.00 38.82           C  
ATOM    995  CE1 PHE A 121      27.399  25.275  19.522  1.00 38.78           C  
ATOM    996  CE2 PHE A 121      27.477  23.092  18.505  1.00 39.02           C  
ATOM    997  CZ  PHE A 121      27.168  23.905  19.597  1.00 38.45           C  
ATOM    998  N   LYS A 122      30.930  23.566  16.023  1.00 39.10           N  
ATOM    999  CA  LYS A 122      31.517  22.306  16.469  1.00 37.11           C  
ATOM   1000  C   LYS A 122      32.941  22.367  17.003  1.00 36.51           C  
ATOM   1001  O   LYS A 122      33.224  21.835  18.074  1.00 36.31           O  
ATOM   1002  CB  LYS A 122      31.441  21.256  15.358  1.00 37.28           C  
ATOM   1003  CG  LYS A 122      30.267  20.319  15.527  1.00 38.67           C  
ATOM   1004  CD  LYS A 122      30.328  19.634  16.890  1.00 38.50           C  
ATOM   1005  CE  LYS A 122      29.016  18.954  17.224  1.00 37.85           C  
ATOM   1006  NZ  LYS A 122      29.114  18.183  18.485  1.00 38.12           N  
ATOM   1007  N   PRO A 123      33.859  23.009  16.263  1.00 36.52           N  
ATOM   1008  CA  PRO A 123      35.242  23.086  16.747  1.00 36.18           C  
ATOM   1009  C   PRO A 123      35.300  23.630  18.179  1.00 35.60           C  
ATOM   1010  O   PRO A 123      35.937  23.043  19.058  1.00 35.13           O  
ATOM   1011  CB  PRO A 123      35.905  24.014  15.731  1.00 36.95           C  
ATOM   1012  CG  PRO A 123      35.144  23.726  14.466  1.00 36.78           C  
ATOM   1013  CD  PRO A 123      33.715  23.684  14.959  1.00 36.61           C  
ATOM   1014  N   LEU A 124      34.618  24.750  18.402  1.00 34.03           N  
ATOM   1015  CA  LEU A 124      34.569  25.381  19.716  1.00 32.67           C  
ATOM   1016  C   LEU A 124      34.115  24.395  20.797  1.00 32.73           C  
ATOM   1017  O   LEU A 124      34.764  24.251  21.836  1.00 32.54           O  
ATOM   1018  CB  LEU A 124      33.619  26.578  19.677  1.00 31.14           C  
ATOM   1019  CG  LEU A 124      33.247  27.195  21.022  1.00 29.63           C  
ATOM   1020  CD1 LEU A 124      34.484  27.745  21.708  1.00 31.37           C  
ATOM   1021  CD2 LEU A 124      32.227  28.289  20.799  1.00 30.08           C  
ATOM   1022  N   TRP A 125      32.995  23.725  20.543  1.00 30.39           N  
ATOM   1023  CA  TRP A 125      32.443  22.751  21.479  1.00 28.94           C  
ATOM   1024  C   TRP A 125      33.455  21.638  21.784  1.00 29.48           C  
ATOM   1025  O   TRP A 125      33.877  21.467  22.932  1.00 28.92           O  
ATOM   1026  CB  TRP A 125      31.142  22.161  20.905  1.00 26.51           C  
ATOM   1027  CG  TRP A 125      30.457  21.196  21.820  1.00 24.92           C  
ATOM   1028  CD1 TRP A 125      30.816  19.903  22.059  1.00 24.58           C  
ATOM   1029  CD2 TRP A 125      29.336  21.466  22.672  1.00 24.73           C  
ATOM   1030  NE1 TRP A 125      29.995  19.349  23.011  1.00 24.78           N  
ATOM   1031  CE2 TRP A 125      29.076  20.285  23.406  1.00 25.47           C  
ATOM   1032  CE3 TRP A 125      28.527  22.589  22.890  1.00 23.44           C  
ATOM   1033  CZ2 TRP A 125      28.042  20.196  24.345  1.00 23.54           C  
ATOM   1034  CZ3 TRP A 125      27.497  22.500  23.827  1.00 23.83           C  
ATOM   1035  CH2 TRP A 125      27.266  21.312  24.540  1.00 24.12           C  
ATOM   1036  N   ALA A 126      33.854  20.902  20.751  1.00 29.27           N  
ATOM   1037  CA  ALA A 126      34.809  19.805  20.892  1.00 28.62           C  
ATOM   1038  C   ALA A 126      36.048  20.140  21.728  1.00 29.26           C  
ATOM   1039  O   ALA A 126      36.454  19.353  22.582  1.00 29.63           O  
ATOM   1040  CB  ALA A 126      35.236  19.325  19.513  1.00 28.98           C  
ATOM   1041  N   ARG A 127      36.646  21.303  21.485  1.00 29.47           N  
ATOM   1042  CA  ARG A 127      37.850  21.705  22.208  1.00 30.08           C  
ATOM   1043  C   ARG A 127      37.574  22.231  23.609  1.00 30.28           C  
ATOM   1044  O   ARG A 127      38.479  22.712  24.291  1.00 31.10           O  
ATOM   1045  CB  ARG A 127      38.618  22.759  21.405  1.00 30.33           C  
ATOM   1046  CG  ARG A 127      37.887  24.075  21.240  1.00 31.19           C  
ATOM   1047  CD  ARG A 127      38.440  24.859  20.062  1.00 31.55           C  
ATOM   1048  NE  ARG A 127      37.707  26.107  19.865  1.00 31.51           N  
ATOM   1049  CZ  ARG A 127      37.724  26.825  18.746  1.00 29.20           C  
ATOM   1050  NH1 ARG A 127      38.443  26.421  17.704  1.00 26.86           N  
ATOM   1051  NH2 ARG A 127      37.015  27.946  18.672  1.00 28.75           N  
ATOM   1052  N   ASN A 128      36.324  22.140  24.040  1.00 30.13           N  
ATOM   1053  CA  ASN A 128      35.957  22.611  25.368  1.00 29.33           C  
ATOM   1054  C   ASN A 128      35.434  21.477  26.240  1.00 28.60           C  
ATOM   1055  O   ASN A 128      35.212  21.654  27.434  1.00 29.87           O  
ATOM   1056  CB  ASN A 128      34.910  23.716  25.248  1.00 30.34           C  
ATOM   1057  CG  ASN A 128      35.535  25.091  25.129  1.00 30.86           C  
ATOM   1058  OD1 ASN A 128      36.049  25.635  26.106  1.00 30.21           O  
ATOM   1059  ND2 ASN A 128      35.509  25.653  23.929  1.00 31.70           N  
ATOM   1060  N   VAL A 129      35.260  20.309  25.629  1.00 28.47           N  
ATOM   1061  CA  VAL A 129      34.758  19.128  26.319  1.00 26.50           C  
ATOM   1062  C   VAL A 129      35.574  18.806  27.569  1.00 26.50           C  
ATOM   1063  O   VAL A 129      36.806  18.820  27.544  1.00 27.90           O  
ATOM   1064  CB  VAL A 129      34.771  17.897  25.373  1.00 25.21           C  
ATOM   1065  CG1 VAL A 129      34.249  16.659  26.088  1.00 25.44           C  
ATOM   1066  CG2 VAL A 129      33.931  18.189  24.149  1.00 25.06           C  
ATOM   1067  N   PRO A 130      34.891  18.518  28.689  1.00 26.91           N  
ATOM   1068  CA  PRO A 130      33.430  18.485  28.844  1.00 26.14           C  
ATOM   1069  C   PRO A 130      32.899  19.669  29.665  1.00 24.82           C  
ATOM   1070  O   PRO A 130      31.860  19.566  30.321  1.00 24.39           O  
ATOM   1071  CB  PRO A 130      33.214  17.163  29.557  1.00 27.43           C  
ATOM   1072  CG  PRO A 130      34.351  17.171  30.547  1.00 27.80           C  
ATOM   1073  CD  PRO A 130      35.540  17.719  29.749  1.00 27.13           C  
ATOM   1074  N   LYS A 131      33.625  20.784  29.620  1.00 23.87           N  
ATOM   1075  CA  LYS A 131      33.267  21.992  30.362  1.00 23.61           C  
ATOM   1076  C   LYS A 131      31.957  22.644  29.925  1.00 21.51           C  
ATOM   1077  O   LYS A 131      31.266  23.263  30.731  1.00 20.44           O  
ATOM   1078  CB  LYS A 131      34.410  23.010  30.286  1.00 23.81           C  
ATOM   1079  CG  LYS A 131      35.634  22.572  31.070  1.00 25.42           C  
ATOM   1080  CD  LYS A 131      36.703  23.656  31.169  1.00 26.62           C  
ATOM   1081  CE  LYS A 131      37.292  24.014  29.814  1.00 27.59           C  
ATOM   1082  NZ  LYS A 131      38.465  24.925  29.961  1.00 26.48           N  
ATOM   1083  N   PHE A 132      31.619  22.510  28.651  1.00 19.82           N  
ATOM   1084  CA  PHE A 132      30.383  23.082  28.141  1.00 19.35           C  
ATOM   1085  C   PHE A 132      29.225  22.132  28.384  1.00 18.53           C  
ATOM   1086  O   PHE A 132      29.387  20.912  28.326  1.00 19.45           O  
ATOM   1087  CB  PHE A 132      30.505  23.368  26.645  1.00 18.27           C  
ATOM   1088  CG  PHE A 132      31.230  24.641  26.328  1.00 18.13           C  
ATOM   1089  CD1 PHE A 132      31.977  25.300  27.301  1.00 19.06           C  
ATOM   1090  CD2 PHE A 132      31.159  25.188  25.055  1.00 16.78           C  
ATOM   1091  CE1 PHE A 132      32.639  26.488  27.007  1.00 19.67           C  
ATOM   1092  CE2 PHE A 132      31.817  26.372  24.755  1.00 18.26           C  
ATOM   1093  CZ  PHE A 132      32.561  27.026  25.734  1.00 16.06           C  
ATOM   1094  N   GLY A 133      28.057  22.700  28.664  1.00 17.25           N  
ATOM   1095  CA  GLY A 133      26.870  21.897  28.901  1.00 14.38           C  
ATOM   1096  C   GLY A 133      25.683  22.386  28.087  1.00 11.86           C  
ATOM   1097  O   GLY A 133      25.843  23.195  27.176  1.00 11.41           O  
ATOM   1098  N   LEU A 134      24.488  21.910  28.415  1.00 11.70           N  
ATOM   1099  CA  LEU A 134      23.290  22.319  27.687  1.00  9.84           C  
ATOM   1100  C   LEU A 134      23.091  23.828  27.753  1.00 10.28           C  
ATOM   1101  O   LEU A 134      22.580  24.428  26.806  1.00 10.74           O  
ATOM   1102  CB  LEU A 134      22.062  21.600  28.248  1.00  5.62           C  
ATOM   1103  CG  LEU A 134      22.065  20.068  28.149  1.00  2.68           C  
ATOM   1104  CD1 LEU A 134      20.825  19.541  28.841  1.00  1.86           C  
ATOM   1105  CD2 LEU A 134      22.106  19.616  26.683  1.00  1.00           C  
ATOM   1106  N   ALA A 135      23.494  24.436  28.867  1.00 11.35           N  
ATOM   1107  CA  ALA A 135      23.377  25.885  29.043  1.00 11.96           C  
ATOM   1108  C   ALA A 135      24.244  26.579  27.992  1.00 12.41           C  
ATOM   1109  O   ALA A 135      23.800  27.529  27.349  1.00 12.18           O  
ATOM   1110  CB  ALA A 135      23.828  26.283  30.453  1.00 10.37           C  
ATOM   1111  N   HIS A 136      25.478  26.093  27.825  1.00 16.26           N  
ATOM   1112  CA  HIS A 136      26.412  26.651  26.841  1.00 19.28           C  
ATOM   1113  C   HIS A 136      25.864  26.437  25.438  1.00 18.76           C  
ATOM   1114  O   HIS A 136      26.022  27.286  24.563  1.00 19.84           O  
ATOM   1115  CB  HIS A 136      27.791  25.988  26.954  1.00 21.02           C  
ATOM   1116  CG  HIS A 136      28.464  26.232  28.267  1.00 22.01           C  
ATOM   1117  ND1 HIS A 136      28.165  25.507  29.400  1.00 22.96           N  
ATOM   1118  CD2 HIS A 136      29.360  27.174  28.650  1.00 22.80           C  
ATOM   1119  CE1 HIS A 136      28.842  25.994  30.426  1.00 24.54           C  
ATOM   1120  NE2 HIS A 136      29.575  27.007  29.997  1.00 24.67           N  
ATOM   1121  N   LEU A 137      25.228  25.287  25.238  1.00 19.45           N  
ATOM   1122  CA  LEU A 137      24.621  24.928  23.961  1.00 19.78           C  
ATOM   1123  C   LEU A 137      23.497  25.921  23.645  1.00 19.81           C  
ATOM   1124  O   LEU A 137      23.359  26.389  22.519  1.00 18.64           O  
ATOM   1125  CB  LEU A 137      24.034  23.518  24.051  1.00 20.64           C  
ATOM   1126  CG  LEU A 137      23.070  23.091  22.935  1.00 21.44           C  
ATOM   1127  CD1 LEU A 137      23.877  22.659  21.703  1.00 19.21           C  
ATOM   1128  CD2 LEU A 137      22.179  21.952  23.421  1.00 16.99           C  
HETATM 1129  N   MSE A 138      22.700  26.225  24.664  1.00 20.62           N  
HETATM 1130  CA  MSE A 138      21.581  27.140  24.546  1.00 20.41           C  
HETATM 1131  C   MSE A 138      22.074  28.550  24.224  1.00 21.08           C  
HETATM 1132  O   MSE A 138      21.447  29.285  23.451  1.00 22.63           O  
HETATM 1133  CB  MSE A 138      20.794  27.149  25.863  1.00 21.28           C  
HETATM 1134  CG  MSE A 138      19.275  27.305  25.727  1.00 25.98           C  
HETATM 1135 SE   MSE A 138      18.361  25.896  24.707  1.00 25.80          SE  
HETATM 1136  CE  MSE A 138      19.218  24.366  25.478  1.00 29.06           C  
ATOM   1137  N   ALA A 139      23.208  28.920  24.813  1.00 20.75           N  
ATOM   1138  CA  ALA A 139      23.783  30.251  24.620  1.00 18.92           C  
ATOM   1139  C   ALA A 139      24.512  30.405  23.297  1.00 17.24           C  
ATOM   1140  O   ALA A 139      24.407  31.440  22.629  1.00 17.70           O  
ATOM   1141  CB  ALA A 139      24.730  30.574  25.766  1.00 19.79           C  
ATOM   1142  N   LEU A 140      25.255  29.373  22.927  1.00 15.98           N  
ATOM   1143  CA  LEU A 140      26.005  29.390  21.682  1.00 17.59           C  
ATOM   1144  C   LEU A 140      25.236  28.748  20.534  1.00 18.01           C  
ATOM   1145  O   LEU A 140      25.616  28.884  19.372  1.00 17.82           O  
ATOM   1146  CB  LEU A 140      27.334  28.668  21.873  1.00 17.01           C  
ATOM   1147  CG  LEU A 140      28.287  29.358  22.842  1.00 18.71           C  
ATOM   1148  CD1 LEU A 140      29.482  28.459  23.079  1.00 18.85           C  
ATOM   1149  CD2 LEU A 140      28.720  30.714  22.287  1.00 17.21           C  
ATOM   1150  N   GLY A 141      24.155  28.050  20.862  1.00 17.17           N  
ATOM   1151  CA  GLY A 141      23.368  27.398  19.836  1.00 17.51           C  
ATOM   1152  C   GLY A 141      22.062  28.097  19.514  1.00 17.46           C  
ATOM   1153  O   GLY A 141      22.020  29.015  18.695  1.00 17.61           O  
ATOM   1154  N   LEU A 142      20.988  27.660  20.158  1.00 16.45           N  
ATOM   1155  CA  LEU A 142      19.679  28.245  19.916  1.00 16.81           C  
ATOM   1156  C   LEU A 142      19.690  29.773  19.983  1.00 18.14           C  
ATOM   1157  O   LEU A 142      19.196  30.444  19.075  1.00 18.18           O  
ATOM   1158  CB  LEU A 142      18.672  27.713  20.932  1.00 16.58           C  
ATOM   1159  CG  LEU A 142      17.441  26.985  20.386  1.00 15.78           C  
ATOM   1160  CD1 LEU A 142      16.479  26.729  21.547  1.00 14.67           C  
ATOM   1161  CD2 LEU A 142      16.768  27.818  19.305  1.00 14.98           C  
ATOM   1162  N   GLY A 143      20.259  30.302  21.067  1.00 18.10           N  
ATOM   1163  CA  GLY A 143      20.319  31.736  21.284  1.00 15.26           C  
ATOM   1164  C   GLY A 143      20.539  32.588  20.047  1.00 14.99           C  
ATOM   1165  O   GLY A 143      19.608  33.244  19.556  1.00 13.93           O  
ATOM   1166  N   PRO A 144      21.775  32.604  19.519  1.00 14.92           N  
ATOM   1167  CA  PRO A 144      22.101  33.395  18.326  1.00 12.32           C  
ATOM   1168  C   PRO A 144      21.269  32.971  17.111  1.00 13.22           C  
ATOM   1169  O   PRO A 144      20.933  33.798  16.263  1.00 13.90           O  
ATOM   1170  CB  PRO A 144      23.598  33.152  18.155  1.00 11.33           C  
ATOM   1171  CG  PRO A 144      23.789  31.779  18.744  1.00 13.78           C  
ATOM   1172  CD  PRO A 144      22.931  31.807  19.972  1.00 12.53           C  
ATOM   1173  N   TRP A 145      20.925  31.686  17.036  1.00 13.44           N  
ATOM   1174  CA  TRP A 145      20.121  31.187  15.923  1.00 14.66           C  
ATOM   1175  C   TRP A 145      18.777  31.931  15.880  1.00 15.53           C  
ATOM   1176  O   TRP A 145      18.350  32.419  14.830  1.00 15.05           O  
ATOM   1177  CB  TRP A 145      19.855  29.682  16.068  1.00 14.53           C  
ATOM   1178  CG  TRP A 145      19.272  29.082  14.818  1.00 13.99           C  
ATOM   1179  CD1 TRP A 145      19.962  28.577  13.737  1.00 11.30           C  
ATOM   1180  CD2 TRP A 145      17.889  29.035  14.461  1.00 12.15           C  
ATOM   1181  NE1 TRP A 145      19.090  28.232  12.737  1.00 10.62           N  
ATOM   1182  CE2 TRP A 145      17.811  28.501  13.152  1.00 12.63           C  
ATOM   1183  CE3 TRP A 145      16.705  29.398  15.117  1.00 13.20           C  
ATOM   1184  CZ2 TRP A 145      16.591  28.320  12.483  1.00 13.45           C  
ATOM   1185  CZ3 TRP A 145      15.489  29.220  14.456  1.00 14.07           C  
ATOM   1186  CH2 TRP A 145      15.443  28.684  13.146  1.00 14.01           C  
ATOM   1187  N   LEU A 146      18.125  32.005  17.037  1.00 15.57           N  
ATOM   1188  CA  LEU A 146      16.834  32.667  17.181  1.00 14.87           C  
ATOM   1189  C   LEU A 146      16.915  34.170  16.922  1.00 14.99           C  
ATOM   1190  O   LEU A 146      16.093  34.736  16.189  1.00 15.80           O  
ATOM   1191  CB  LEU A 146      16.278  32.427  18.590  1.00 14.34           C  
ATOM   1192  CG  LEU A 146      15.764  31.033  18.950  1.00 14.19           C  
ATOM   1193  CD1 LEU A 146      15.521  30.936  20.452  1.00 12.05           C  
ATOM   1194  CD2 LEU A 146      14.477  30.763  18.188  1.00 14.05           C  
ATOM   1195  N   ALA A 147      17.904  34.809  17.540  1.00 13.62           N  
ATOM   1196  CA  ALA A 147      18.113  36.247  17.404  1.00 12.13           C  
ATOM   1197  C   ALA A 147      18.152  36.653  15.946  1.00 12.88           C  
ATOM   1198  O   ALA A 147      17.691  37.735  15.570  1.00 12.84           O  
ATOM   1199  CB  ALA A 147      19.416  36.646  18.079  1.00 11.47           C  
ATOM   1200  N   VAL A 148      18.699  35.763  15.127  1.00 14.72           N  
ATOM   1201  CA  VAL A 148      18.836  36.004  13.698  1.00 16.10           C  
ATOM   1202  C   VAL A 148      17.635  35.619  12.850  1.00 16.54           C  
ATOM   1203  O   VAL A 148      17.042  36.456  12.171  1.00 17.02           O  
ATOM   1204  CB  VAL A 148      20.041  35.255  13.146  1.00 16.25           C  
ATOM   1205  CG1 VAL A 148      20.109  35.434  11.637  1.00 18.04           C  
ATOM   1206  CG2 VAL A 148      21.297  35.774  13.807  1.00 18.23           C  
ATOM   1207  N   GLU A 149      17.297  34.336  12.892  1.00 17.54           N  
ATOM   1208  CA  GLU A 149      16.191  33.795  12.118  1.00 16.96           C  
ATOM   1209  C   GLU A 149      14.817  34.365  12.468  1.00 17.87           C  
ATOM   1210  O   GLU A 149      14.048  34.725  11.577  1.00 16.55           O  
ATOM   1211  CB  GLU A 149      16.157  32.272  12.264  1.00 18.76           C  
ATOM   1212  CG  GLU A 149      17.439  31.577  11.840  1.00 21.55           C  
ATOM   1213  CD  GLU A 149      17.818  31.895  10.408  1.00 22.78           C  
ATOM   1214  OE1 GLU A 149      16.940  31.760   9.526  1.00 22.44           O  
ATOM   1215  OE2 GLU A 149      18.988  32.270  10.163  1.00 23.21           O  
ATOM   1216  N   ILE A 150      14.514  34.459  13.760  1.00 17.45           N  
ATOM   1217  CA  ILE A 150      13.211  34.944  14.196  1.00 15.95           C  
ATOM   1218  C   ILE A 150      12.789  36.290  13.613  1.00 15.18           C  
ATOM   1219  O   ILE A 150      11.731  36.395  12.988  1.00 14.80           O  
ATOM   1220  CB  ILE A 150      13.117  35.002  15.744  1.00 15.86           C  
ATOM   1221  CG1 ILE A 150      13.449  33.629  16.343  1.00 15.05           C  
ATOM   1222  CG2 ILE A 150      11.702  35.395  16.162  1.00 14.28           C  
ATOM   1223  CD1 ILE A 150      12.489  32.517  15.936  1.00 12.42           C  
ATOM   1224  N   PRO A 151      13.599  37.346  13.812  1.00 14.26           N  
ATOM   1225  CA  PRO A 151      13.209  38.647  13.256  1.00 13.67           C  
ATOM   1226  C   PRO A 151      13.161  38.633  11.720  1.00 13.78           C  
ATOM   1227  O   PRO A 151      12.404  39.379  11.107  1.00 14.23           O  
ATOM   1228  CB  PRO A 151      14.277  39.594  13.810  1.00 12.84           C  
ATOM   1229  CG  PRO A 151      15.478  38.702  13.947  1.00 13.04           C  
ATOM   1230  CD  PRO A 151      14.878  37.448  14.534  1.00 13.21           C  
ATOM   1231  N   ASP A 152      13.954  37.766  11.100  1.00 12.04           N  
ATOM   1232  CA  ASP A 152      13.964  37.684   9.647  1.00 11.47           C  
ATOM   1233  C   ASP A 152      12.666  37.040   9.103  1.00 11.18           C  
ATOM   1234  O   ASP A 152      12.068  37.536   8.144  1.00  9.83           O  
ATOM   1235  CB  ASP A 152      15.206  36.909   9.185  1.00 10.67           C  
ATOM   1236  CG  ASP A 152      15.337  36.852   7.675  1.00 10.03           C  
ATOM   1237  OD1 ASP A 152      15.481  37.923   7.029  1.00  8.38           O  
ATOM   1238  OD2 ASP A 152      15.304  35.724   7.142  1.00  7.91           O  
ATOM   1239  N   LEU A 153      12.236  35.950   9.737  1.00 12.48           N  
ATOM   1240  CA  LEU A 153      11.024  35.219   9.350  1.00 12.23           C  
ATOM   1241  C   LEU A 153       9.780  36.072   9.581  1.00 13.91           C  
ATOM   1242  O   LEU A 153       8.803  36.002   8.827  1.00 13.13           O  
ATOM   1243  CB  LEU A 153      10.916  33.921  10.163  1.00 11.61           C  
ATOM   1244  CG  LEU A 153      12.077  32.925   9.989  1.00 14.25           C  
ATOM   1245  CD1 LEU A 153      12.074  31.829  11.070  1.00  9.43           C  
ATOM   1246  CD2 LEU A 153      11.967  32.327   8.603  1.00 13.36           C  
ATOM   1247  N   ILE A 154       9.821  36.876  10.639  1.00 16.36           N  
ATOM   1248  CA  ILE A 154       8.706  37.751  10.965  1.00 15.08           C  
ATOM   1249  C   ILE A 154       8.560  38.883   9.941  1.00 16.22           C  
ATOM   1250  O   ILE A 154       7.445  39.219   9.546  1.00 15.15           O  
ATOM   1251  CB  ILE A 154       8.866  38.364  12.375  1.00 14.90           C  
ATOM   1252  CG1 ILE A 154       8.849  37.263  13.432  1.00 12.86           C  
ATOM   1253  CG2 ILE A 154       7.718  39.341  12.655  1.00 13.20           C  
ATOM   1254  CD1 ILE A 154       9.025  37.792  14.846  1.00 12.96           C  
ATOM   1255  N   GLN A 155       9.678  39.460   9.505  1.00 17.01           N  
ATOM   1256  CA  GLN A 155       9.621  40.547   8.539  1.00 17.67           C  
ATOM   1257  C   GLN A 155       9.292  40.069   7.129  1.00 19.59           C  
ATOM   1258  O   GLN A 155       8.809  40.844   6.299  1.00 20.53           O  
ATOM   1259  CB  GLN A 155      10.936  41.327   8.514  1.00 17.21           C  
ATOM   1260  CG  GLN A 155      12.070  40.693   7.713  1.00 14.87           C  
ATOM   1261  CD  GLN A 155      13.302  41.594   7.659  1.00 12.80           C  
ATOM   1262  OE1 GLN A 155      14.316  41.253   7.046  1.00 14.65           O  
ATOM   1263  NE2 GLN A 155      13.213  42.754   8.306  1.00 12.48           N  
ATOM   1264  N   LYS A 156       9.551  38.793   6.860  1.00 20.29           N  
ATOM   1265  CA  LYS A 156       9.283  38.210   5.547  1.00 21.09           C  
ATOM   1266  C   LYS A 156       7.884  37.612   5.461  1.00 22.66           C  
ATOM   1267  O   LYS A 156       7.465  37.152   4.399  1.00 24.13           O  
ATOM   1268  CB  LYS A 156      10.334  37.139   5.223  1.00 19.28           C  
ATOM   1269  CG  LYS A 156      11.739  37.706   5.093  1.00 18.52           C  
ATOM   1270  CD  LYS A 156      12.757  36.668   4.685  1.00 18.21           C  
ATOM   1271  CE  LYS A 156      14.113  37.327   4.503  1.00 20.30           C  
ATOM   1272  NZ  LYS A 156      15.151  36.381   4.025  1.00 17.79           N  
ATOM   1273  N   GLY A 157       7.168  37.627   6.583  1.00 23.95           N  
ATOM   1274  CA  GLY A 157       5.818  37.091   6.626  1.00 24.65           C  
ATOM   1275  C   GLY A 157       5.772  35.578   6.760  1.00 26.56           C  
ATOM   1276  O   GLY A 157       4.756  34.965   6.439  1.00 25.93           O  
ATOM   1277  N   VAL A 158       6.866  34.981   7.233  1.00 28.74           N  
ATOM   1278  CA  VAL A 158       6.956  33.530   7.405  1.00 31.76           C  
ATOM   1279  C   VAL A 158       6.214  33.083   8.653  1.00 34.14           C  
ATOM   1280  O   VAL A 158       5.440  32.120   8.629  1.00 34.08           O  
ATOM   1281  CB  VAL A 158       8.417  33.053   7.545  1.00 30.93           C  
ATOM   1282  CG1 VAL A 158       8.452  31.533   7.682  1.00 29.50           C  
ATOM   1283  CG2 VAL A 158       9.238  33.506   6.352  1.00 29.22           C  
ATOM   1284  N   ILE A 159       6.475  33.774   9.754  1.00 36.53           N  
ATOM   1285  CA  ILE A 159       5.824  33.452  11.012  1.00 40.52           C  
ATOM   1286  C   ILE A 159       5.023  34.687  11.412  1.00 42.63           C  
ATOM   1287  O   ILE A 159       5.337  35.802  10.995  1.00 42.78           O  
ATOM   1288  CB  ILE A 159       6.874  33.079  12.118  1.00 41.00           C  
ATOM   1289  CG1 ILE A 159       6.191  32.329  13.270  1.00 42.25           C  
ATOM   1290  CG2 ILE A 159       7.559  34.324  12.653  1.00 40.49           C  
ATOM   1291  CD1 ILE A 159       5.668  30.932  12.897  1.00 42.35           C  
ATOM   1292  N   GLN A 160       3.974  34.492  12.196  1.00 46.15           N  
ATOM   1293  CA  GLN A 160       3.150  35.616  12.608  1.00 50.21           C  
ATOM   1294  C   GLN A 160       2.287  35.255  13.806  1.00 52.97           C  
ATOM   1295  O   GLN A 160       1.096  35.570  13.845  1.00 54.33           O  
ATOM   1296  CB  GLN A 160       2.269  36.064  11.436  1.00 50.11           C  
ATOM   1297  CG  GLN A 160       1.396  34.962  10.849  1.00 51.74           C  
ATOM   1298  CD  GLN A 160       0.665  35.398   9.588  1.00 53.42           C  
ATOM   1299  OE1 GLN A 160      -0.103  34.631   9.005  1.00 54.47           O  
ATOM   1300  NE2 GLN A 160       0.903  36.635   9.159  1.00 53.01           N  
ATOM   1301  N   HIS A 161       2.895  34.592  14.785  1.00 55.64           N  
ATOM   1302  CA  HIS A 161       2.175  34.190  15.987  1.00 57.90           C  
ATOM   1303  C   HIS A 161       1.634  35.445  16.660  1.00 57.24           C  
ATOM   1304  O   HIS A 161       0.453  35.521  17.001  1.00 56.13           O  
ATOM   1305  CB  HIS A 161       3.105  33.439  16.948  1.00 59.49           C  
ATOM   1306  CG  HIS A 161       2.378  32.607  17.959  1.00 61.54           C  
ATOM   1307  ND1 HIS A 161       3.028  31.822  18.888  1.00 62.27           N  
ATOM   1308  CD2 HIS A 161       1.053  32.425  18.175  1.00 61.50           C  
ATOM   1309  CE1 HIS A 161       2.135  31.193  19.631  1.00 62.08           C  
ATOM   1310  NE2 HIS A 161       0.929  31.541  19.219  1.00 61.67           N  
ATOM   1311  N   LYS A 162       2.519  36.422  16.838  1.00 57.21           N  
ATOM   1312  CA  LYS A 162       2.179  37.705  17.444  1.00 57.35           C  
ATOM   1313  C   LYS A 162       1.248  37.529  18.643  1.00 56.74           C  
ATOM   1314  O   LYS A 162       0.272  38.265  18.802  1.00 55.68           O  
ATOM   1315  CB  LYS A 162       1.520  38.605  16.388  1.00 57.75           C  
ATOM   1316  CG  LYS A 162       1.813  38.179  14.941  1.00 57.55           C  
ATOM   1317  CD  LYS A 162       1.375  39.217  13.913  1.00 56.62           C  
ATOM   1318  CE  LYS A 162       2.358  40.375  13.837  1.00 55.71           C  
ATOM   1319  NZ  LYS A 162       3.691  39.943  13.318  1.00 55.76           N  
ATOM   1320  N   GLU A 163       1.566  36.552  19.487  1.00 56.64           N  
ATOM   1321  CA  GLU A 163       0.755  36.251  20.662  1.00 57.86           C  
ATOM   1322  C   GLU A 163      -0.689  35.959  20.233  1.00 58.26           C  
ATOM   1323  O   GLU A 163      -1.638  36.591  20.709  1.00 58.03           O  
ATOM   1324  CB  GLU A 163       0.793  37.425  21.655  1.00 57.16           C  
ATOM   1325  CG  GLU A 163       2.197  37.774  22.156  1.00 53.92           C  
ATOM   1326  CD  GLU A 163       2.198  38.876  23.198  1.00 51.25           C  
ATOM   1327  OE1 GLU A 163       1.675  39.970  22.911  1.00 50.69           O  
ATOM   1328  OE2 GLU A 163       2.730  38.646  24.299  1.00 50.50           O  
ATOM   1329  N   LYS A 164      -0.844  34.993  19.329  1.00 58.44           N  
ATOM   1330  CA  LYS A 164      -2.159  34.616  18.815  1.00 59.43           C  
ATOM   1331  C   LYS A 164      -2.974  33.822  19.825  1.00 59.36           C  
ATOM   1332  O   LYS A 164      -4.124  34.228  20.088  1.00 59.27           O  
ATOM   1333  CB  LYS A 164      -2.023  33.796  17.526  1.00 61.07           C  
ATOM   1334  CG  LYS A 164      -3.367  33.451  16.884  1.00 61.62           C  
ATOM   1335  CD  LYS A 164      -3.234  32.468  15.720  1.00 61.68           C  
ATOM   1336  CE  LYS A 164      -2.393  33.017  14.579  1.00 61.94           C  
ATOM   1337  NZ  LYS A 164      -2.307  32.019  13.475  1.00 62.50           N  
TER    1338      LYS A 164                                                      
ATOM   1339  N   ASP B   3      -4.337  20.920  42.397  1.00 72.01           N  
ATOM   1340  CA  ASP B   3      -4.938  19.572  42.186  1.00 72.59           C  
ATOM   1341  C   ASP B   3      -6.295  19.444  42.871  1.00 72.27           C  
ATOM   1342  O   ASP B   3      -6.936  20.448  43.184  1.00 72.54           O  
ATOM   1343  CB  ASP B   3      -3.988  18.487  42.703  1.00 73.42           C  
ATOM   1344  CG  ASP B   3      -3.477  18.773  44.105  1.00 73.22           C  
ATOM   1345  OD1 ASP B   3      -4.302  18.875  45.037  1.00 73.11           O  
ATOM   1346  OD2 ASP B   3      -2.244  18.897  44.272  1.00 73.55           O  
ATOM   1347  N   GLU B   4      -6.732  18.209  43.105  1.00 71.61           N  
ATOM   1348  CA  GLU B   4      -8.022  17.978  43.748  1.00 71.31           C  
ATOM   1349  C   GLU B   4      -7.889  17.654  45.232  1.00 70.68           C  
ATOM   1350  O   GLU B   4      -8.888  17.577  45.951  1.00 70.21           O  
ATOM   1351  CB  GLU B   4      -8.781  16.853  43.040  1.00 71.23           C  
ATOM   1352  CG  GLU B   4     -10.252  16.796  43.420  1.00 70.77           C  
ATOM   1353  CD  GLU B   4     -10.942  18.139  43.245  1.00 70.19           C  
ATOM   1354  OE1 GLU B   4     -10.937  18.672  42.114  1.00 69.11           O  
ATOM   1355  OE2 GLU B   4     -11.484  18.663  44.242  1.00 70.60           O  
ATOM   1356  N   ALA B   5      -6.651  17.462  45.682  1.00 70.27           N  
ATOM   1357  CA  ALA B   5      -6.368  17.164  47.082  1.00 68.68           C  
ATOM   1358  C   ALA B   5      -6.354  18.471  47.869  1.00 68.11           C  
ATOM   1359  O   ALA B   5      -6.801  18.525  49.017  1.00 68.24           O  
ATOM   1360  CB  ALA B   5      -5.022  16.464  47.206  1.00 68.98           C  
ATOM   1361  N   THR B   6      -5.838  19.522  47.237  1.00 66.99           N  
ATOM   1362  CA  THR B   6      -5.767  20.842  47.853  1.00 65.72           C  
ATOM   1363  C   THR B   6      -7.159  21.463  47.865  1.00 65.00           C  
ATOM   1364  O   THR B   6      -7.503  22.224  48.769  1.00 64.92           O  
ATOM   1365  CB  THR B   6      -4.808  21.775  47.076  1.00 65.98           C  
ATOM   1366  OG1 THR B   6      -3.493  21.202  47.049  1.00 64.96           O  
ATOM   1367  CG2 THR B   6      -4.739  23.142  47.740  1.00 65.85           C  
ATOM   1368  N   ARG B   7      -7.953  21.128  46.851  1.00 64.67           N  
ATOM   1369  CA  ARG B   7      -9.322  21.626  46.726  1.00 64.21           C  
ATOM   1370  C   ARG B   7     -10.077  21.308  48.015  1.00 62.82           C  
ATOM   1371  O   ARG B   7     -10.933  22.074  48.461  1.00 62.07           O  
ATOM   1372  CB  ARG B   7     -10.013  20.941  45.542  1.00 65.79           C  
ATOM   1373  CG  ARG B   7     -11.409  21.459  45.213  1.00 66.96           C  
ATOM   1374  CD  ARG B   7     -11.361  22.806  44.501  1.00 68.16           C  
ATOM   1375  NE  ARG B   7     -12.674  23.188  43.983  1.00 69.87           N  
ATOM   1376  CZ  ARG B   7     -12.908  24.271  43.246  1.00 70.71           C  
ATOM   1377  NH1 ARG B   7     -11.915  25.094  42.932  1.00 71.09           N  
ATOM   1378  NH2 ARG B   7     -14.138  24.529  42.819  1.00 71.26           N  
ATOM   1379  N   ARG B   8      -9.738  20.163  48.600  1.00 61.75           N  
ATOM   1380  CA  ARG B   8     -10.346  19.692  49.836  1.00 59.78           C  
ATOM   1381  C   ARG B   8      -9.789  20.438  51.045  1.00 58.36           C  
ATOM   1382  O   ARG B   8     -10.525  20.769  51.977  1.00 58.18           O  
ATOM   1383  CB  ARG B   8     -10.085  18.194  50.000  1.00 60.79           C  
ATOM   1384  CG  ARG B   8     -10.731  17.319  48.936  1.00 61.32           C  
ATOM   1385  CD  ARG B   8     -12.246  17.433  48.986  1.00 61.97           C  
ATOM   1386  NE  ARG B   8     -12.741  18.641  48.331  1.00 61.94           N  
ATOM   1387  CZ  ARG B   8     -13.915  19.207  48.596  1.00 61.98           C  
ATOM   1388  NH1 ARG B   8     -14.285  20.302  47.945  1.00 62.22           N  
ATOM   1389  NH2 ARG B   8     -14.708  18.691  49.527  1.00 62.07           N  
ATOM   1390  N   VAL B   9      -8.483  20.690  51.021  1.00 56.18           N  
ATOM   1391  CA  VAL B   9      -7.802  21.395  52.104  1.00 53.37           C  
ATOM   1392  C   VAL B   9      -8.379  22.799  52.279  1.00 51.60           C  
ATOM   1393  O   VAL B   9      -8.489  23.302  53.398  1.00 51.27           O  
ATOM   1394  CB  VAL B   9      -6.282  21.509  51.824  1.00 53.31           C  
ATOM   1395  CG1 VAL B   9      -5.577  22.171  53.001  1.00 53.54           C  
ATOM   1396  CG2 VAL B   9      -5.701  20.131  51.561  1.00 53.35           C  
ATOM   1397  N   VAL B  10      -8.755  23.418  51.164  1.00 48.97           N  
ATOM   1398  CA  VAL B  10      -9.316  24.762  51.182  1.00 46.75           C  
ATOM   1399  C   VAL B  10     -10.747  24.736  51.704  1.00 44.82           C  
ATOM   1400  O   VAL B  10     -11.315  25.771  52.062  1.00 44.42           O  
ATOM   1401  CB  VAL B  10      -9.309  25.378  49.772  1.00 46.71           C  
ATOM   1402  CG1 VAL B  10      -9.749  26.828  49.836  1.00 47.10           C  
ATOM   1403  CG2 VAL B  10      -7.922  25.267  49.168  1.00 45.99           C  
ATOM   1404  N   SER B  11     -11.320  23.540  51.746  1.00 43.10           N  
ATOM   1405  CA  SER B  11     -12.681  23.353  52.225  1.00 42.94           C  
ATOM   1406  C   SER B  11     -12.743  23.534  53.738  1.00 42.91           C  
ATOM   1407  O   SER B  11     -13.624  24.221  54.258  1.00 42.86           O  
ATOM   1408  CB  SER B  11     -13.174  21.952  51.854  1.00 41.20           C  
ATOM   1409  OG  SER B  11     -13.060  21.728  50.459  1.00 41.53           O  
ATOM   1410  N   GLU B  12     -11.793  22.916  54.434  1.00 42.22           N  
ATOM   1411  CA  GLU B  12     -11.723  22.976  55.890  1.00 41.98           C  
ATOM   1412  C   GLU B  12     -11.179  24.307  56.411  1.00 39.68           C  
ATOM   1413  O   GLU B  12     -10.938  24.459  57.608  1.00 39.52           O  
ATOM   1414  CB  GLU B  12     -10.858  21.824  56.419  1.00 44.71           C  
ATOM   1415  CG  GLU B  12     -11.395  20.431  56.102  1.00 48.15           C  
ATOM   1416  CD  GLU B  12     -10.478  19.316  56.593  1.00 51.38           C  
ATOM   1417  OE1 GLU B  12     -10.825  18.129  56.401  1.00 52.92           O  
ATOM   1418  OE2 GLU B  12      -9.411  19.624  57.168  1.00 52.04           O  
ATOM   1419  N   ILE B  13     -10.993  25.269  55.514  1.00 36.69           N  
ATOM   1420  CA  ILE B  13     -10.485  26.582  55.900  1.00 34.06           C  
ATOM   1421  C   ILE B  13     -11.626  27.592  56.005  1.00 33.09           C  
ATOM   1422  O   ILE B  13     -12.263  27.917  55.006  1.00 34.47           O  
ATOM   1423  CB  ILE B  13      -9.463  27.097  54.872  1.00 32.37           C  
ATOM   1424  CG1 ILE B  13      -8.308  26.104  54.765  1.00 30.97           C  
ATOM   1425  CG2 ILE B  13      -8.970  28.479  55.272  1.00 31.35           C  
ATOM   1426  CD1 ILE B  13      -7.190  26.558  53.852  1.00 28.86           C  
ATOM   1427  N   PRO B  14     -11.889  28.112  57.214  1.00 31.29           N  
ATOM   1428  CA  PRO B  14     -12.974  29.085  57.387  1.00 30.17           C  
ATOM   1429  C   PRO B  14     -12.841  30.319  56.498  1.00 29.37           C  
ATOM   1430  O   PRO B  14     -11.820  31.005  56.525  1.00 29.00           O  
ATOM   1431  CB  PRO B  14     -12.893  29.424  58.872  1.00 30.56           C  
ATOM   1432  CG  PRO B  14     -11.433  29.239  59.181  1.00 30.47           C  
ATOM   1433  CD  PRO B  14     -11.114  27.961  58.458  1.00 30.82           C  
ATOM   1434  N   VAL B  15     -13.878  30.605  55.717  1.00 28.50           N  
ATOM   1435  CA  VAL B  15     -13.842  31.765  54.833  1.00 28.72           C  
ATOM   1436  C   VAL B  15     -13.988  33.081  55.599  1.00 27.58           C  
ATOM   1437  O   VAL B  15     -14.474  33.110  56.727  1.00 27.52           O  
ATOM   1438  CB  VAL B  15     -14.948  31.697  53.748  1.00 29.19           C  
ATOM   1439  CG1 VAL B  15     -14.810  30.421  52.945  1.00 29.19           C  
ATOM   1440  CG2 VAL B  15     -16.322  31.791  54.389  1.00 31.30           C  
ATOM   1441  N   LEU B  16     -13.552  34.166  54.969  1.00 27.29           N  
ATOM   1442  CA  LEU B  16     -13.629  35.488  55.566  1.00 27.76           C  
ATOM   1443  C   LEU B  16     -14.976  36.108  55.202  1.00 27.78           C  
ATOM   1444  O   LEU B  16     -15.666  35.620  54.306  1.00 28.20           O  
ATOM   1445  CB  LEU B  16     -12.493  36.372  55.041  1.00 27.45           C  
ATOM   1446  CG  LEU B  16     -11.039  35.988  55.347  1.00 27.74           C  
ATOM   1447  CD1 LEU B  16     -10.836  35.988  56.845  1.00 27.59           C  
ATOM   1448  CD2 LEU B  16     -10.688  34.627  54.766  1.00 28.62           C  
ATOM   1449  N   LYS B  17     -15.352  37.176  55.899  1.00 26.70           N  
ATOM   1450  CA  LYS B  17     -16.608  37.854  55.620  1.00 26.89           C  
ATOM   1451  C   LYS B  17     -16.488  39.362  55.795  1.00 26.99           C  
ATOM   1452  O   LYS B  17     -17.402  40.007  56.304  1.00 27.84           O  
ATOM   1453  CB  LYS B  17     -17.723  37.318  56.520  1.00 28.44           C  
ATOM   1454  CG  LYS B  17     -18.119  35.876  56.215  1.00 30.32           C  
ATOM   1455  CD  LYS B  17     -19.629  35.706  55.976  1.00 31.18           C  
ATOM   1456  CE  LYS B  17     -20.131  36.464  54.736  1.00 31.85           C  
ATOM   1457  NZ  LYS B  17     -20.125  37.953  54.867  1.00 34.03           N  
ATOM   1458  N   THR B  18     -15.358  39.923  55.376  1.00 25.92           N  
ATOM   1459  CA  THR B  18     -15.145  41.361  55.482  1.00 23.55           C  
ATOM   1460  C   THR B  18     -14.235  41.857  54.371  1.00 23.90           C  
ATOM   1461  O   THR B  18     -13.038  41.577  54.362  1.00 23.05           O  
ATOM   1462  CB  THR B  18     -14.526  41.754  56.846  1.00 23.04           C  
ATOM   1463  OG1 THR B  18     -15.391  41.333  57.906  1.00 22.31           O  
ATOM   1464  CG2 THR B  18     -14.350  43.272  56.939  1.00 22.78           C  
ATOM   1465  N   ASN B  19     -14.817  42.582  53.421  1.00 25.30           N  
ATOM   1466  CA  ASN B  19     -14.048  43.133  52.316  1.00 24.04           C  
ATOM   1467  C   ASN B  19     -13.463  44.468  52.755  1.00 22.80           C  
ATOM   1468  O   ASN B  19     -14.017  45.533  52.480  1.00 21.95           O  
ATOM   1469  CB  ASN B  19     -14.931  43.323  51.086  1.00 26.36           C  
ATOM   1470  CG  ASN B  19     -14.264  44.168  50.021  1.00 28.24           C  
ATOM   1471  OD1 ASN B  19     -13.136  43.892  49.604  1.00 30.25           O  
ATOM   1472  ND2 ASN B  19     -14.957  45.215  49.578  1.00 29.54           N  
ATOM   1473  N   ALA B  20     -12.340  44.392  53.460  1.00 22.13           N  
ATOM   1474  CA  ALA B  20     -11.657  45.576  53.953  1.00 20.56           C  
ATOM   1475  C   ALA B  20     -10.158  45.455  53.725  1.00 20.24           C  
ATOM   1476  O   ALA B  20      -9.587  44.363  53.792  1.00 18.92           O  
ATOM   1477  CB  ALA B  20     -11.951  45.767  55.431  1.00 18.73           C  
ATOM   1478  N   GLY B  21      -9.535  46.594  53.452  1.00 21.26           N  
ATOM   1479  CA  GLY B  21      -8.106  46.631  53.215  1.00 23.73           C  
ATOM   1480  C   GLY B  21      -7.338  47.278  54.351  1.00 26.40           C  
ATOM   1481  O   GLY B  21      -7.928  47.739  55.336  1.00 26.07           O  
ATOM   1482  N   PRO B  22      -6.008  47.335  54.240  1.00 27.34           N  
ATOM   1483  CA  PRO B  22      -5.235  47.948  55.318  1.00 29.89           C  
ATOM   1484  C   PRO B  22      -5.353  49.469  55.463  1.00 31.57           C  
ATOM   1485  O   PRO B  22      -4.398  50.118  55.878  1.00 32.32           O  
ATOM   1486  CB  PRO B  22      -3.810  47.496  55.012  1.00 30.47           C  
ATOM   1487  CG  PRO B  22      -3.808  47.368  53.517  1.00 29.16           C  
ATOM   1488  CD  PRO B  22      -5.130  46.706  53.238  1.00 27.81           C  
ATOM   1489  N   ARG B  23      -6.505  50.044  55.130  1.00 32.15           N  
ATOM   1490  CA  ARG B  23      -6.664  51.488  55.270  1.00 33.71           C  
ATOM   1491  C   ARG B  23      -7.975  51.858  55.932  1.00 34.31           C  
ATOM   1492  O   ARG B  23      -8.140  52.983  56.406  1.00 34.56           O  
ATOM   1493  CB  ARG B  23      -6.578  52.203  53.915  1.00 35.65           C  
ATOM   1494  CG  ARG B  23      -5.209  52.196  53.248  1.00 38.07           C  
ATOM   1495  CD  ARG B  23      -5.018  53.439  52.370  1.00 41.55           C  
ATOM   1496  NE  ARG B  23      -4.762  54.657  53.151  1.00 44.99           N  
ATOM   1497  CZ  ARG B  23      -5.696  55.446  53.684  1.00 47.05           C  
ATOM   1498  NH1 ARG B  23      -5.337  56.520  54.378  1.00 46.75           N  
ATOM   1499  NH2 ARG B  23      -6.983  55.180  53.516  1.00 49.11           N  
ATOM   1500  N   ASP B  24      -8.914  50.915  55.955  1.00 35.68           N  
ATOM   1501  CA  ASP B  24     -10.215  51.154  56.571  1.00 35.81           C  
ATOM   1502  C   ASP B  24     -10.163  50.796  58.042  1.00 36.44           C  
ATOM   1503  O   ASP B  24     -11.067  50.155  58.585  1.00 36.91           O  
ATOM   1504  CB  ASP B  24     -11.311  50.364  55.850  1.00 36.77           C  
ATOM   1505  CG  ASP B  24     -10.826  49.033  55.329  1.00 38.96           C  
ATOM   1506  OD1 ASP B  24     -10.476  48.154  56.153  1.00 39.88           O  
ATOM   1507  OD2 ASP B  24     -10.798  48.869  54.084  1.00 38.00           O  
ATOM   1508  N   ARG B  25      -9.068  51.241  58.656  1.00 36.79           N  
ATOM   1509  CA  ARG B  25      -8.752  51.064  60.069  1.00 36.32           C  
ATOM   1510  C   ARG B  25      -9.725  50.184  60.848  1.00 34.23           C  
ATOM   1511  O   ARG B  25      -9.475  48.999  61.049  1.00 34.21           O  
ATOM   1512  CB  ARG B  25      -8.620  52.452  60.723  1.00 38.67           C  
ATOM   1513  CG  ARG B  25      -9.116  53.622  59.853  1.00 39.91           C  
ATOM   1514  CD  ARG B  25     -10.558  54.024  60.169  1.00 42.38           C  
ATOM   1515  NE  ARG B  25     -10.644  54.827  61.387  1.00 43.08           N  
ATOM   1516  CZ  ARG B  25     -11.768  55.341  61.880  1.00 44.64           C  
ATOM   1517  NH1 ARG B  25     -11.731  56.059  62.997  1.00 45.04           N  
ATOM   1518  NH2 ARG B  25     -12.927  55.141  61.265  1.00 46.41           N  
ATOM   1519  N   GLU B  26     -10.825  50.775  61.293  1.00 33.39           N  
ATOM   1520  CA  GLU B  26     -11.844  50.052  62.034  1.00 32.11           C  
ATOM   1521  C   GLU B  26     -12.140  48.698  61.374  1.00 30.16           C  
ATOM   1522  O   GLU B  26     -11.957  47.645  61.984  1.00 29.74           O  
ATOM   1523  CB  GLU B  26     -13.113  50.903  62.085  1.00 35.47           C  
ATOM   1524  CG  GLU B  26     -14.298  50.249  62.756  1.00 39.58           C  
ATOM   1525  CD  GLU B  26     -14.145  50.186  64.254  1.00 40.87           C  
ATOM   1526  OE1 GLU B  26     -13.072  49.743  64.710  1.00 41.94           O  
ATOM   1527  OE2 GLU B  26     -15.093  50.582  64.970  1.00 41.79           O  
ATOM   1528  N   LEU B  27     -12.583  48.729  60.121  1.00 26.64           N  
ATOM   1529  CA  LEU B  27     -12.904  47.500  59.412  1.00 24.81           C  
ATOM   1530  C   LEU B  27     -11.699  46.593  59.209  1.00 24.06           C  
ATOM   1531  O   LEU B  27     -11.824  45.368  59.285  1.00 22.54           O  
ATOM   1532  CB  LEU B  27     -13.560  47.807  58.064  1.00 25.95           C  
ATOM   1533  CG  LEU B  27     -15.006  48.325  58.092  1.00 25.44           C  
ATOM   1534  CD1 LEU B  27     -15.833  47.448  59.020  1.00 24.00           C  
ATOM   1535  CD2 LEU B  27     -15.051  49.774  58.554  1.00 26.62           C  
ATOM   1536  N   TRP B  28     -10.533  47.177  58.949  1.00 22.94           N  
ATOM   1537  CA  TRP B  28      -9.336  46.367  58.761  1.00 23.19           C  
ATOM   1538  C   TRP B  28      -9.115  45.492  59.987  1.00 23.21           C  
ATOM   1539  O   TRP B  28      -8.630  44.368  59.870  1.00 22.77           O  
ATOM   1540  CB  TRP B  28      -8.098  47.236  58.541  1.00 24.15           C  
ATOM   1541  CG  TRP B  28      -6.836  46.421  58.457  1.00 25.20           C  
ATOM   1542  CD1 TRP B  28      -5.721  46.555  59.232  1.00 27.48           C  
ATOM   1543  CD2 TRP B  28      -6.568  45.338  57.553  1.00 26.28           C  
ATOM   1544  NE1 TRP B  28      -4.772  45.625  58.869  1.00 27.66           N  
ATOM   1545  CE2 TRP B  28      -5.267  44.866  57.841  1.00 26.12           C  
ATOM   1546  CE3 TRP B  28      -7.300  44.721  56.528  1.00 25.54           C  
ATOM   1547  CZ2 TRP B  28      -4.681  43.804  57.140  1.00 24.54           C  
ATOM   1548  CZ3 TRP B  28      -6.715  43.662  55.829  1.00 24.62           C  
ATOM   1549  CH2 TRP B  28      -5.420  43.217  56.140  1.00 23.22           C  
ATOM   1550  N   VAL B  29      -9.463  46.017  61.161  1.00 22.56           N  
ATOM   1551  CA  VAL B  29      -9.319  45.274  62.412  1.00 23.01           C  
ATOM   1552  C   VAL B  29     -10.212  44.043  62.357  1.00 23.45           C  
ATOM   1553  O   VAL B  29      -9.745  42.923  62.553  1.00 21.91           O  
ATOM   1554  CB  VAL B  29      -9.742  46.122  63.635  1.00 23.35           C  
ATOM   1555  CG1 VAL B  29      -9.623  45.300  64.908  1.00 22.88           C  
ATOM   1556  CG2 VAL B  29      -8.879  47.361  63.731  1.00 23.04           C  
ATOM   1557  N   GLN B  30     -11.499  44.266  62.092  1.00 24.53           N  
ATOM   1558  CA  GLN B  30     -12.470  43.179  62.004  1.00 25.37           C  
ATOM   1559  C   GLN B  30     -11.944  42.100  61.060  1.00 25.97           C  
ATOM   1560  O   GLN B  30     -11.970  40.917  61.386  1.00 27.23           O  
ATOM   1561  CB  GLN B  30     -13.816  43.706  61.489  1.00 27.73           C  
ATOM   1562  CG  GLN B  30     -14.932  42.659  61.436  1.00 31.32           C  
ATOM   1563  CD  GLN B  30     -16.248  43.217  60.900  1.00 34.40           C  
ATOM   1564  OE1 GLN B  30     -16.738  44.250  61.369  1.00 35.78           O  
ATOM   1565  NE2 GLN B  30     -16.832  42.524  59.921  1.00 35.24           N  
ATOM   1566  N   ARG B  31     -11.467  42.523  59.892  1.00 24.79           N  
ATOM   1567  CA  ARG B  31     -10.928  41.603  58.898  1.00 25.02           C  
ATOM   1568  C   ARG B  31      -9.700  40.906  59.462  1.00 23.65           C  
ATOM   1569  O   ARG B  31      -9.532  39.692  59.326  1.00 23.10           O  
ATOM   1570  CB  ARG B  31     -10.547  42.363  57.623  1.00 25.80           C  
ATOM   1571  CG  ARG B  31      -9.729  41.556  56.612  1.00 26.87           C  
ATOM   1572  CD  ARG B  31     -10.549  40.492  55.892  1.00 25.07           C  
ATOM   1573  NE  ARG B  31      -9.691  39.593  55.119  1.00 25.22           N  
ATOM   1574  CZ  ARG B  31     -10.097  38.876  54.074  1.00 25.99           C  
ATOM   1575  NH1 ARG B  31     -11.356  38.950  53.658  1.00 26.90           N  
ATOM   1576  NH2 ARG B  31      -9.245  38.077  53.450  1.00 26.36           N  
ATOM   1577  N   LEU B  32      -8.838  41.689  60.095  1.00 22.88           N  
ATOM   1578  CA  LEU B  32      -7.622  41.168  60.696  1.00 20.47           C  
ATOM   1579  C   LEU B  32      -7.944  40.019  61.663  1.00 20.74           C  
ATOM   1580  O   LEU B  32      -7.293  38.976  61.619  1.00 19.36           O  
ATOM   1581  CB  LEU B  32      -6.905  42.302  61.424  1.00 20.25           C  
ATOM   1582  CG  LEU B  32      -5.393  42.203  61.571  1.00 18.80           C  
ATOM   1583  CD1 LEU B  32      -4.749  41.846  60.236  1.00 16.36           C  
ATOM   1584  CD2 LEU B  32      -4.878  43.534  62.090  1.00 16.95           C  
ATOM   1585  N   LYS B  33      -8.949  40.205  62.522  1.00 20.56           N  
ATOM   1586  CA  LYS B  33      -9.340  39.161  63.477  1.00 19.80           C  
ATOM   1587  C   LYS B  33      -9.746  37.903  62.717  1.00 19.07           C  
ATOM   1588  O   LYS B  33      -9.415  36.785  63.108  1.00 18.10           O  
ATOM   1589  CB  LYS B  33     -10.519  39.618  64.351  1.00 20.19           C  
ATOM   1590  CG  LYS B  33     -10.193  40.715  65.361  1.00 23.73           C  
ATOM   1591  CD  LYS B  33     -11.362  40.972  66.326  1.00 23.81           C  
ATOM   1592  CE  LYS B  33     -12.624  41.432  65.585  1.00 24.66           C  
ATOM   1593  NZ  LYS B  33     -13.778  41.716  66.497  1.00 25.95           N  
ATOM   1594  N   GLU B  34     -10.470  38.111  61.625  1.00 19.27           N  
ATOM   1595  CA  GLU B  34     -10.941  37.033  60.775  1.00 17.92           C  
ATOM   1596  C   GLU B  34      -9.763  36.310  60.165  1.00 16.57           C  
ATOM   1597  O   GLU B  34      -9.796  35.098  59.960  1.00 14.46           O  
ATOM   1598  CB  GLU B  34     -11.798  37.607  59.656  1.00 17.78           C  
ATOM   1599  CG  GLU B  34     -13.228  37.879  60.040  1.00 18.18           C  
ATOM   1600  CD  GLU B  34     -13.933  38.747  59.021  1.00 18.37           C  
ATOM   1601  OE1 GLU B  34     -13.685  38.563  57.807  1.00 20.09           O  
ATOM   1602  OE2 GLU B  34     -14.740  39.603  59.442  1.00 19.42           O  
ATOM   1603  N   GLU B  35      -8.722  37.076  59.874  1.00 16.48           N  
ATOM   1604  CA  GLU B  35      -7.520  36.540  59.263  1.00 17.46           C  
ATOM   1605  C   GLU B  35      -6.765  35.629  60.248  1.00 17.83           C  
ATOM   1606  O   GLU B  35      -6.429  34.486  59.924  1.00 17.86           O  
ATOM   1607  CB  GLU B  35      -6.641  37.705  58.797  1.00 16.14           C  
ATOM   1608  CG  GLU B  35      -5.712  37.383  57.645  1.00 20.59           C  
ATOM   1609  CD  GLU B  35      -6.442  37.217  56.312  1.00 20.65           C  
ATOM   1610  OE1 GLU B  35      -6.906  38.228  55.734  1.00 17.83           O  
ATOM   1611  OE2 GLU B  35      -6.551  36.063  55.849  1.00 22.27           O  
ATOM   1612  N   TYR B  36      -6.519  36.124  61.456  1.00 16.66           N  
ATOM   1613  CA  TYR B  36      -5.811  35.334  62.460  1.00 15.49           C  
ATOM   1614  C   TYR B  36      -6.567  34.052  62.789  1.00 16.18           C  
ATOM   1615  O   TYR B  36      -5.980  32.972  62.888  1.00 17.50           O  
ATOM   1616  CB  TYR B  36      -5.632  36.152  63.729  1.00 15.00           C  
ATOM   1617  CG  TYR B  36      -4.799  37.377  63.520  1.00 16.02           C  
ATOM   1618  CD1 TYR B  36      -3.451  37.272  63.199  1.00 16.69           C  
ATOM   1619  CD2 TYR B  36      -5.347  38.643  63.672  1.00 16.03           C  
ATOM   1620  CE1 TYR B  36      -2.667  38.397  63.044  1.00 17.61           C  
ATOM   1621  CE2 TYR B  36      -4.574  39.776  63.518  1.00 17.03           C  
ATOM   1622  CZ  TYR B  36      -3.231  39.650  63.210  1.00 17.97           C  
ATOM   1623  OH  TYR B  36      -2.441  40.777  63.108  1.00 20.36           O  
ATOM   1624  N   GLN B  37      -7.878  34.196  62.956  1.00 16.03           N  
ATOM   1625  CA  GLN B  37      -8.759  33.089  63.284  1.00 14.55           C  
ATOM   1626  C   GLN B  37      -8.708  31.994  62.226  1.00 14.66           C  
ATOM   1627  O   GLN B  37      -8.558  30.810  62.539  1.00 14.77           O  
ATOM   1628  CB  GLN B  37     -10.195  33.606  63.457  1.00 13.88           C  
ATOM   1629  CG  GLN B  37     -10.493  34.162  64.853  1.00 11.89           C  
ATOM   1630  CD  GLN B  37     -11.831  34.899  64.950  1.00 14.13           C  
ATOM   1631  OE1 GLN B  37     -12.870  34.408  64.491  1.00 13.51           O  
ATOM   1632  NE2 GLN B  37     -11.809  36.083  65.565  1.00 13.69           N  
ATOM   1633  N   SER B  38      -8.823  32.387  60.968  1.00 15.46           N  
ATOM   1634  CA  SER B  38      -8.779  31.420  59.883  1.00 15.46           C  
ATOM   1635  C   SER B  38      -7.391  30.753  59.812  1.00 14.31           C  
ATOM   1636  O   SER B  38      -7.278  29.558  59.522  1.00 14.35           O  
ATOM   1637  CB  SER B  38      -9.133  32.125  58.569  1.00 15.24           C  
ATOM   1638  OG  SER B  38      -9.349  31.198  57.517  1.00 21.84           O  
ATOM   1639  N   LEU B  39      -6.341  31.521  60.097  1.00 14.23           N  
ATOM   1640  CA  LEU B  39      -4.973  30.995  60.079  1.00 15.17           C  
ATOM   1641  C   LEU B  39      -4.689  29.964  61.161  1.00 15.50           C  
ATOM   1642  O   LEU B  39      -4.024  28.963  60.899  1.00 15.81           O  
ATOM   1643  CB  LEU B  39      -3.962  32.128  60.229  1.00 15.58           C  
ATOM   1644  CG  LEU B  39      -3.822  33.068  59.040  1.00 14.87           C  
ATOM   1645  CD1 LEU B  39      -3.033  34.305  59.457  1.00 15.49           C  
ATOM   1646  CD2 LEU B  39      -3.132  32.331  57.899  1.00 14.45           C  
ATOM   1647  N   ILE B  40      -5.161  30.217  62.380  1.00 15.00           N  
ATOM   1648  CA  ILE B  40      -4.921  29.279  63.472  1.00 18.00           C  
ATOM   1649  C   ILE B  40      -5.731  28.012  63.254  1.00 17.52           C  
ATOM   1650  O   ILE B  40      -5.331  26.928  63.682  1.00 17.10           O  
ATOM   1651  CB  ILE B  40      -5.279  29.879  64.881  1.00 19.69           C  
ATOM   1652  CG1 ILE B  40      -6.794  29.898  65.102  1.00 20.16           C  
ATOM   1653  CG2 ILE B  40      -4.701  31.286  65.016  1.00 20.17           C  
ATOM   1654  CD1 ILE B  40      -7.356  28.614  65.705  1.00 22.14           C  
ATOM   1655  N   ARG B  41      -6.871  28.151  62.584  1.00 17.05           N  
ATOM   1656  CA  ARG B  41      -7.743  27.010  62.313  1.00 18.18           C  
ATOM   1657  C   ARG B  41      -7.069  26.127  61.264  1.00 17.42           C  
ATOM   1658  O   ARG B  41      -7.039  24.898  61.392  1.00 16.03           O  
ATOM   1659  CB  ARG B  41      -9.102  27.503  61.804  1.00 22.13           C  
ATOM   1660  CG  ARG B  41     -10.312  26.755  62.366  1.00 26.78           C  
ATOM   1661  CD  ARG B  41     -10.433  25.341  61.825  1.00 31.58           C  
ATOM   1662  NE  ARG B  41     -10.244  24.336  62.870  1.00 38.12           N  
ATOM   1663  CZ  ARG B  41     -10.564  23.049  62.743  1.00 42.21           C  
ATOM   1664  NH1 ARG B  41     -11.096  22.600  61.612  1.00 43.31           N  
ATOM   1665  NH2 ARG B  41     -10.354  22.206  63.749  1.00 44.20           N  
ATOM   1666  N   TYR B  42      -6.530  26.774  60.231  1.00 15.71           N  
ATOM   1667  CA  TYR B  42      -5.824  26.097  59.148  1.00 14.42           C  
ATOM   1668  C   TYR B  42      -4.640  25.330  59.742  1.00 13.72           C  
ATOM   1669  O   TYR B  42      -4.422  24.155  59.435  1.00 13.12           O  
ATOM   1670  CB  TYR B  42      -5.321  27.134  58.128  1.00 12.73           C  
ATOM   1671  CG  TYR B  42      -4.515  26.578  56.964  1.00  9.91           C  
ATOM   1672  CD1 TYR B  42      -3.578  27.376  56.301  1.00  9.34           C  
ATOM   1673  CD2 TYR B  42      -4.684  25.261  56.528  1.00  9.56           C  
ATOM   1674  CE1 TYR B  42      -2.822  26.875  55.235  1.00  9.32           C  
ATOM   1675  CE2 TYR B  42      -3.938  24.750  55.462  1.00  8.26           C  
ATOM   1676  CZ  TYR B  42      -3.008  25.562  54.824  1.00  9.87           C  
ATOM   1677  OH  TYR B  42      -2.255  25.046  53.785  1.00 11.35           O  
ATOM   1678  N   VAL B  43      -3.880  26.002  60.600  1.00 13.72           N  
ATOM   1679  CA  VAL B  43      -2.718  25.388  61.237  1.00 14.15           C  
ATOM   1680  C   VAL B  43      -3.120  24.133  62.005  1.00 13.93           C  
ATOM   1681  O   VAL B  43      -2.437  23.109  61.943  1.00 14.63           O  
ATOM   1682  CB  VAL B  43      -2.034  26.374  62.219  1.00 14.74           C  
ATOM   1683  CG1 VAL B  43      -0.878  25.688  62.927  1.00 13.35           C  
ATOM   1684  CG2 VAL B  43      -1.538  27.600  61.461  1.00 15.12           C  
ATOM   1685  N   GLU B  44      -4.231  24.231  62.732  1.00 13.69           N  
ATOM   1686  CA  GLU B  44      -4.749  23.117  63.515  1.00 12.75           C  
ATOM   1687  C   GLU B  44      -5.160  21.950  62.622  1.00 13.19           C  
ATOM   1688  O   GLU B  44      -4.904  20.793  62.954  1.00 11.43           O  
ATOM   1689  CB  GLU B  44      -5.934  23.586  64.373  1.00 13.11           C  
ATOM   1690  CG  GLU B  44      -5.543  24.577  65.468  1.00 15.03           C  
ATOM   1691  CD  GLU B  44      -4.553  23.989  66.469  1.00 17.25           C  
ATOM   1692  OE1 GLU B  44      -4.932  23.054  67.212  1.00 18.37           O  
ATOM   1693  OE2 GLU B  44      -3.391  24.456  66.501  1.00 18.75           O  
ATOM   1694  N   ASN B  45      -5.794  22.240  61.487  1.00 14.61           N  
ATOM   1695  CA  ASN B  45      -6.202  21.164  60.575  1.00 13.71           C  
ATOM   1696  C   ASN B  45      -4.984  20.475  59.979  1.00 13.78           C  
ATOM   1697  O   ASN B  45      -5.013  19.266  59.735  1.00 12.55           O  
ATOM   1698  CB  ASN B  45      -7.075  21.687  59.435  1.00 13.87           C  
ATOM   1699  CG  ASN B  45      -8.383  22.258  59.922  1.00 14.78           C  
ATOM   1700  OD1 ASN B  45      -9.059  21.663  60.760  1.00 16.61           O  
ATOM   1701  ND2 ASN B  45      -8.755  23.412  59.392  1.00 16.86           N  
ATOM   1702  N   ASN B  46      -3.923  21.242  59.721  1.00 13.67           N  
ATOM   1703  CA  ASN B  46      -2.705  20.655  59.165  1.00 15.80           C  
ATOM   1704  C   ASN B  46      -2.108  19.723  60.202  1.00 16.02           C  
ATOM   1705  O   ASN B  46      -1.649  18.625  59.882  1.00 16.49           O  
ATOM   1706  CB  ASN B  46      -1.666  21.724  58.804  1.00 15.51           C  
ATOM   1707  CG  ASN B  46      -2.062  22.544  57.597  1.00 18.64           C  
ATOM   1708  OD1 ASN B  46      -2.616  22.023  56.623  1.00 19.62           O  
ATOM   1709  ND2 ASN B  46      -1.760  23.839  57.643  1.00 21.86           N  
ATOM   1710  N   LYS B  47      -2.116  20.167  61.452  1.00 15.65           N  
ATOM   1711  CA  LYS B  47      -1.575  19.354  62.521  1.00 17.10           C  
ATOM   1712  C   LYS B  47      -2.298  18.017  62.568  1.00 15.21           C  
ATOM   1713  O   LYS B  47      -1.664  16.962  62.578  1.00 14.20           O  
ATOM   1714  CB  LYS B  47      -1.682  20.088  63.859  1.00 17.49           C  
ATOM   1715  CG  LYS B  47      -0.557  21.100  64.087  1.00 19.70           C  
ATOM   1716  CD  LYS B  47      -0.523  21.523  65.536  1.00 22.93           C  
ATOM   1717  CE  LYS B  47       0.726  22.292  65.883  1.00 25.72           C  
ATOM   1718  NZ  LYS B  47       0.744  22.610  67.345  1.00 28.37           N  
ATOM   1719  N   ASN B  48      -3.624  18.056  62.580  1.00 14.70           N  
ATOM   1720  CA  ASN B  48      -4.405  16.825  62.598  1.00 14.91           C  
ATOM   1721  C   ASN B  48      -4.053  15.949  61.414  1.00 13.82           C  
ATOM   1722  O   ASN B  48      -4.035  14.730  61.527  1.00 15.19           O  
ATOM   1723  CB  ASN B  48      -5.895  17.137  62.539  1.00 16.78           C  
ATOM   1724  CG  ASN B  48      -6.355  17.930  63.722  1.00 18.88           C  
ATOM   1725  OD1 ASN B  48      -6.125  17.538  64.866  1.00 20.83           O  
ATOM   1726  ND2 ASN B  48      -7.004  19.060  63.465  1.00 21.61           N  
ATOM   1727  N   ALA B  49      -3.783  16.575  60.277  1.00 13.96           N  
ATOM   1728  CA  ALA B  49      -3.456  15.832  59.072  1.00 13.13           C  
ATOM   1729  C   ALA B  49      -1.974  15.505  58.995  1.00 12.43           C  
ATOM   1730  O   ALA B  49      -1.502  14.950  58.001  1.00 11.59           O  
ATOM   1731  CB  ALA B  49      -3.877  16.628  57.846  1.00 14.87           C  
ATOM   1732  N   ASP B  50      -1.247  15.849  60.052  1.00 15.11           N  
ATOM   1733  CA  ASP B  50       0.191  15.619  60.112  1.00 15.48           C  
ATOM   1734  C   ASP B  50       0.857  16.237  58.894  1.00 15.09           C  
ATOM   1735  O   ASP B  50       1.660  15.609  58.195  1.00 15.13           O  
ATOM   1736  CB  ASP B  50       0.506  14.127  60.182  1.00 17.46           C  
ATOM   1737  CG  ASP B  50       1.992  13.859  60.323  1.00 18.38           C  
ATOM   1738  OD1 ASP B  50       2.679  14.665  60.999  1.00 21.95           O  
ATOM   1739  OD2 ASP B  50       2.471  12.840  59.772  1.00 19.10           O  
ATOM   1740  N   ASN B  51       0.489  17.485  58.644  1.00 15.36           N  
ATOM   1741  CA  ASN B  51       1.034  18.230  57.533  1.00 16.45           C  
ATOM   1742  C   ASN B  51       1.387  19.639  57.988  1.00 15.99           C  
ATOM   1743  O   ASN B  51       1.471  20.558  57.177  1.00 16.93           O  
ATOM   1744  CB  ASN B  51       0.036  18.286  56.378  1.00 17.83           C  
ATOM   1745  CG  ASN B  51       0.642  18.893  55.134  1.00 20.31           C  
ATOM   1746  OD1 ASN B  51       1.712  18.478  54.699  1.00 24.36           O  
ATOM   1747  ND2 ASN B  51      -0.033  19.875  54.554  1.00 22.31           N  
ATOM   1748  N   ASP B  52       1.579  19.802  59.296  1.00 14.54           N  
ATOM   1749  CA  ASP B  52       1.930  21.100  59.871  1.00 12.23           C  
ATOM   1750  C   ASP B  52       3.170  21.602  59.135  1.00 11.94           C  
ATOM   1751  O   ASP B  52       4.259  21.056  59.309  1.00 12.02           O  
ATOM   1752  CB  ASP B  52       2.225  20.938  61.359  1.00 11.84           C  
ATOM   1753  CG  ASP B  52       2.163  22.244  62.108  1.00 12.32           C  
ATOM   1754  OD1 ASP B  52       1.980  23.300  61.463  1.00 14.77           O  
ATOM   1755  OD2 ASP B  52       2.297  22.214  63.347  1.00 13.95           O  
ATOM   1756  N   TRP B  53       3.024  22.645  58.326  1.00 10.95           N  
ATOM   1757  CA  TRP B  53       4.166  23.119  57.553  1.00 10.26           C  
ATOM   1758  C   TRP B  53       4.568  24.594  57.641  1.00 10.07           C  
ATOM   1759  O   TRP B  53       5.553  25.003  57.017  1.00 11.29           O  
ATOM   1760  CB  TRP B  53       3.947  22.753  56.085  1.00 10.86           C  
ATOM   1761  CG  TRP B  53       2.732  23.388  55.480  1.00 10.28           C  
ATOM   1762  CD1 TRP B  53       1.430  22.986  55.614  1.00 11.85           C  
ATOM   1763  CD2 TRP B  53       2.706  24.557  54.661  1.00  8.58           C  
ATOM   1764  NE1 TRP B  53       0.598  23.836  54.927  1.00  9.96           N  
ATOM   1765  CE2 TRP B  53       1.358  24.808  54.331  1.00 10.03           C  
ATOM   1766  CE3 TRP B  53       3.694  25.419  54.174  1.00  6.89           C  
ATOM   1767  CZ2 TRP B  53       0.976  25.885  53.533  1.00 11.79           C  
ATOM   1768  CZ3 TRP B  53       3.318  26.487  53.385  1.00  8.56           C  
ATOM   1769  CH2 TRP B  53       1.969  26.713  53.068  1.00 11.22           C  
ATOM   1770  N   PHE B  54       3.834  25.393  58.409  1.00  9.60           N  
ATOM   1771  CA  PHE B  54       4.166  26.810  58.504  1.00 10.22           C  
ATOM   1772  C   PHE B  54       3.675  27.514  59.766  1.00 10.65           C  
ATOM   1773  O   PHE B  54       2.875  26.984  60.536  1.00  9.79           O  
ATOM   1774  CB  PHE B  54       3.590  27.549  57.303  1.00  8.22           C  
ATOM   1775  CG  PHE B  54       2.150  27.922  57.467  1.00  9.50           C  
ATOM   1776  CD1 PHE B  54       1.787  29.236  57.749  1.00  8.91           C  
ATOM   1777  CD2 PHE B  54       1.155  26.957  57.366  1.00  9.75           C  
ATOM   1778  CE1 PHE B  54       0.454  29.585  57.926  1.00  7.31           C  
ATOM   1779  CE2 PHE B  54      -0.185  27.294  57.543  1.00 10.97           C  
ATOM   1780  CZ  PHE B  54      -0.536  28.614  57.824  1.00  9.42           C  
ATOM   1781  N   ARG B  55       4.171  28.732  59.945  1.00 11.16           N  
ATOM   1782  CA  ARG B  55       3.805  29.597  61.059  1.00 13.74           C  
ATOM   1783  C   ARG B  55       3.872  30.994  60.475  1.00 12.72           C  
ATOM   1784  O   ARG B  55       4.909  31.422  59.970  1.00 12.86           O  
ATOM   1785  CB  ARG B  55       4.791  29.466  62.225  1.00 13.28           C  
ATOM   1786  CG  ARG B  55       4.741  28.129  62.963  1.00 13.79           C  
ATOM   1787  CD  ARG B  55       3.499  28.002  63.835  1.00 16.44           C  
ATOM   1788  NE  ARG B  55       3.491  26.766  64.624  1.00 19.45           N  
ATOM   1789  CZ  ARG B  55       3.207  25.557  64.147  1.00 20.03           C  
ATOM   1790  NH1 ARG B  55       2.900  25.400  62.863  1.00 19.78           N  
ATOM   1791  NH2 ARG B  55       3.222  24.502  64.959  1.00 19.81           N  
ATOM   1792  N   LEU B  56       2.750  31.695  60.523  1.00 15.62           N  
ATOM   1793  CA  LEU B  56       2.680  33.035  59.976  1.00 17.38           C  
ATOM   1794  C   LEU B  56       2.248  34.031  61.039  1.00 17.64           C  
ATOM   1795  O   LEU B  56       1.304  33.783  61.794  1.00 17.45           O  
ATOM   1796  CB  LEU B  56       1.683  33.066  58.814  1.00 17.68           C  
ATOM   1797  CG  LEU B  56       1.647  34.331  57.957  1.00 17.31           C  
ATOM   1798  CD1 LEU B  56       2.922  34.403  57.119  1.00 18.18           C  
ATOM   1799  CD2 LEU B  56       0.420  34.313  57.053  1.00 16.94           C  
ATOM   1800  N   GLU B  57       2.945  35.160  61.092  1.00 18.00           N  
ATOM   1801  CA  GLU B  57       2.609  36.215  62.037  1.00 18.24           C  
ATOM   1802  C   GLU B  57       2.745  37.570  61.341  1.00 18.03           C  
ATOM   1803  O   GLU B  57       3.353  37.666  60.272  1.00 18.18           O  
ATOM   1804  CB  GLU B  57       3.517  36.142  63.270  1.00 18.20           C  
ATOM   1805  CG  GLU B  57       2.737  36.235  64.583  1.00 20.14           C  
ATOM   1806  CD  GLU B  57       1.802  35.043  64.806  1.00 19.91           C  
ATOM   1807  OE1 GLU B  57       0.836  35.171  65.591  1.00 19.29           O  
ATOM   1808  OE2 GLU B  57       2.047  33.980  64.200  1.00 20.08           O  
ATOM   1809  N   SER B  58       2.161  38.606  61.940  1.00 17.65           N  
ATOM   1810  CA  SER B  58       2.204  39.960  61.378  1.00 17.09           C  
ATOM   1811  C   SER B  58       2.763  41.016  62.350  1.00 17.80           C  
ATOM   1812  O   SER B  58       3.269  40.684  63.421  1.00 17.94           O  
ATOM   1813  CB  SER B  58       0.793  40.379  60.918  1.00 17.04           C  
ATOM   1814  OG  SER B  58      -0.044  40.805  61.987  1.00 10.80           O  
ATOM   1815  N   ASN B  59       2.672  42.286  61.960  1.00 19.60           N  
ATOM   1816  CA  ASN B  59       3.143  43.392  62.793  1.00 19.98           C  
ATOM   1817  C   ASN B  59       1.922  44.004  63.459  1.00 21.24           C  
ATOM   1818  O   ASN B  59       0.795  43.696  63.084  1.00 21.35           O  
ATOM   1819  CB  ASN B  59       3.856  44.448  61.941  1.00 18.38           C  
ATOM   1820  CG  ASN B  59       2.958  45.031  60.878  1.00 17.79           C  
ATOM   1821  OD1 ASN B  59       1.896  44.479  60.580  1.00 17.19           O  
ATOM   1822  ND2 ASN B  59       3.379  46.140  60.287  1.00 17.61           N  
ATOM   1823  N   LYS B  60       2.146  44.877  64.433  1.00 21.91           N  
ATOM   1824  CA  LYS B  60       1.057  45.508  65.170  1.00 23.00           C  
ATOM   1825  C   LYS B  60      -0.131  45.925  64.305  1.00 23.05           C  
ATOM   1826  O   LYS B  60      -1.283  45.735  64.689  1.00 23.25           O  
ATOM   1827  CB  LYS B  60       1.614  46.711  65.939  1.00 22.57           C  
ATOM   1828  CG  LYS B  60       2.867  46.357  66.755  1.00 22.39           C  
ATOM   1829  CD  LYS B  60       3.521  47.553  67.469  1.00 22.51           C  
ATOM   1830  CE  LYS B  60       2.703  48.026  68.677  1.00 23.55           C  
ATOM   1831  NZ  LYS B  60       3.429  49.032  69.510  1.00 21.75           N  
ATOM   1832  N   GLU B  61       0.154  46.462  63.126  1.00 24.86           N  
ATOM   1833  CA  GLU B  61      -0.888  46.935  62.215  1.00 24.65           C  
ATOM   1834  C   GLU B  61      -1.388  45.902  61.186  1.00 23.55           C  
ATOM   1835  O   GLU B  61      -2.376  46.131  60.474  1.00 23.48           O  
ATOM   1836  CB  GLU B  61      -0.371  48.194  61.526  1.00 25.99           C  
ATOM   1837  CG  GLU B  61       1.145  48.342  61.633  1.00 29.93           C  
ATOM   1838  CD  GLU B  61       1.664  49.598  60.962  1.00 33.17           C  
ATOM   1839  OE1 GLU B  61       1.178  50.693  61.324  1.00 35.57           O  
ATOM   1840  OE2 GLU B  61       2.557  49.491  60.083  1.00 31.23           O  
ATOM   1841  N   GLY B  62      -0.701  44.766  61.118  1.00 22.15           N  
ATOM   1842  CA  GLY B  62      -1.089  43.703  60.206  1.00 19.93           C  
ATOM   1843  C   GLY B  62      -0.950  43.993  58.721  1.00 18.67           C  
ATOM   1844  O   GLY B  62      -1.665  43.406  57.910  1.00 18.25           O  
ATOM   1845  N   THR B  63      -0.033  44.888  58.359  1.00 18.63           N  
ATOM   1846  CA  THR B  63       0.191  45.239  56.959  1.00 18.62           C  
ATOM   1847  C   THR B  63       1.442  44.540  56.436  1.00 18.96           C  
ATOM   1848  O   THR B  63       1.639  44.409  55.229  1.00 18.85           O  
ATOM   1849  CB  THR B  63       0.356  46.767  56.772  1.00 19.27           C  
ATOM   1850  OG1 THR B  63       1.518  47.220  57.476  1.00 19.76           O  
ATOM   1851  CG2 THR B  63      -0.873  47.499  57.292  1.00 19.70           C  
ATOM   1852  N   ARG B  64       2.295  44.109  57.358  1.00 20.83           N  
ATOM   1853  CA  ARG B  64       3.512  43.403  57.004  1.00 20.52           C  
ATOM   1854  C   ARG B  64       3.510  42.070  57.741  1.00 20.69           C  
ATOM   1855  O   ARG B  64       3.267  42.008  58.949  1.00 17.18           O  
ATOM   1856  CB  ARG B  64       4.755  44.223  57.372  1.00 23.23           C  
ATOM   1857  CG  ARG B  64       5.027  45.431  56.460  1.00 26.94           C  
ATOM   1858  CD  ARG B  64       4.100  46.614  56.744  1.00 29.35           C  
ATOM   1859  NE  ARG B  64       4.385  47.773  55.892  1.00 31.56           N  
ATOM   1860  CZ  ARG B  64       4.174  47.811  54.578  1.00 31.65           C  
ATOM   1861  NH1 ARG B  64       3.671  46.757  53.951  1.00 34.16           N  
ATOM   1862  NH2 ARG B  64       4.468  48.903  53.889  1.00 30.80           N  
ATOM   1863  N   TRP B  65       3.769  41.003  56.990  1.00 21.87           N  
ATOM   1864  CA  TRP B  65       3.782  39.655  57.529  1.00 21.25           C  
ATOM   1865  C   TRP B  65       5.132  38.982  57.338  1.00 22.21           C  
ATOM   1866  O   TRP B  65       5.848  39.244  56.371  1.00 22.90           O  
ATOM   1867  CB  TRP B  65       2.692  38.823  56.856  1.00 20.93           C  
ATOM   1868  CG  TRP B  65       1.325  39.364  57.095  1.00 20.04           C  
ATOM   1869  CD1 TRP B  65       0.767  40.474  56.526  1.00 17.20           C  
ATOM   1870  CD2 TRP B  65       0.361  38.856  58.018  1.00 20.90           C  
ATOM   1871  NE1 TRP B  65      -0.487  40.691  57.044  1.00 19.52           N  
ATOM   1872  CE2 TRP B  65      -0.764  39.713  57.963  1.00 20.90           C  
ATOM   1873  CE3 TRP B  65       0.338  37.758  58.892  1.00 20.32           C  
ATOM   1874  CZ2 TRP B  65      -1.904  39.506  58.753  1.00 19.56           C  
ATOM   1875  CZ3 TRP B  65      -0.793  37.553  59.676  1.00 19.91           C  
ATOM   1876  CH2 TRP B  65      -1.898  38.424  59.600  1.00 19.73           C  
ATOM   1877  N   PHE B  66       5.469  38.106  58.271  1.00 22.43           N  
ATOM   1878  CA  PHE B  66       6.725  37.392  58.226  1.00 22.25           C  
ATOM   1879  C   PHE B  66       6.550  36.095  58.986  1.00 21.90           C  
ATOM   1880  O   PHE B  66       5.659  35.965  59.827  1.00 21.30           O  
ATOM   1881  CB  PHE B  66       7.827  38.209  58.888  1.00 23.10           C  
ATOM   1882  CG  PHE B  66       7.460  38.721  60.245  1.00 25.20           C  
ATOM   1883  CD1 PHE B  66       6.758  39.913  60.381  1.00 26.23           C  
ATOM   1884  CD2 PHE B  66       7.778  37.992  61.389  1.00 27.12           C  
ATOM   1885  CE1 PHE B  66       6.373  40.373  61.638  1.00 27.86           C  
ATOM   1886  CE2 PHE B  66       7.397  38.442  62.657  1.00 26.90           C  
ATOM   1887  CZ  PHE B  66       6.692  39.635  62.783  1.00 27.98           C  
ATOM   1888  N   GLY B  67       7.416  35.137  58.689  1.00 22.59           N  
ATOM   1889  CA  GLY B  67       7.354  33.853  59.353  1.00 23.09           C  
ATOM   1890  C   GLY B  67       8.299  32.857  58.720  1.00 23.73           C  
ATOM   1891  O   GLY B  67       9.398  33.200  58.268  1.00 23.10           O  
ATOM   1892  N   LYS B  68       7.866  31.607  58.690  1.00 22.98           N  
ATOM   1893  CA  LYS B  68       8.671  30.550  58.107  1.00 22.34           C  
ATOM   1894  C   LYS B  68       7.810  29.345  57.771  1.00 21.52           C  
ATOM   1895  O   LYS B  68       6.728  29.151  58.334  1.00 20.99           O  
ATOM   1896  CB  LYS B  68       9.797  30.155  59.067  1.00 22.78           C  
ATOM   1897  CG  LYS B  68       9.337  29.628  60.421  1.00 25.05           C  
ATOM   1898  CD  LYS B  68      10.523  29.434  61.374  1.00 24.91           C  
ATOM   1899  CE  LYS B  68      11.144  30.770  61.832  1.00 25.07           C  
ATOM   1900  NZ  LYS B  68      11.643  31.655  60.729  1.00 26.14           N  
ATOM   1901  N   CYS B  69       8.305  28.547  56.833  1.00 21.49           N  
ATOM   1902  CA  CYS B  69       7.622  27.345  56.366  1.00 20.86           C  
ATOM   1903  C   CYS B  69       8.653  26.240  56.257  1.00 20.18           C  
ATOM   1904  O   CYS B  69       9.849  26.507  56.164  1.00 20.57           O  
ATOM   1905  CB  CYS B  69       7.028  27.587  54.982  1.00 19.64           C  
ATOM   1906  SG  CYS B  69       8.295  27.856  53.716  1.00 19.31           S  
ATOM   1907  N   TRP B  70       8.191  25.000  56.251  1.00 20.19           N  
ATOM   1908  CA  TRP B  70       9.107  23.884  56.134  1.00 20.24           C  
ATOM   1909  C   TRP B  70       8.548  22.739  55.294  1.00 19.20           C  
ATOM   1910  O   TRP B  70       7.339  22.634  55.069  1.00 15.96           O  
ATOM   1911  CB  TRP B  70       9.524  23.394  57.530  1.00 20.96           C  
ATOM   1912  CG  TRP B  70       8.382  23.129  58.465  1.00 24.44           C  
ATOM   1913  CD1 TRP B  70       7.731  21.935  58.663  1.00 25.81           C  
ATOM   1914  CD2 TRP B  70       7.750  24.077  59.332  1.00 26.26           C  
ATOM   1915  NE1 TRP B  70       6.737  22.085  59.600  1.00 25.94           N  
ATOM   1916  CE2 TRP B  70       6.724  23.389  60.027  1.00 25.97           C  
ATOM   1917  CE3 TRP B  70       7.948  25.442  59.591  1.00 27.27           C  
ATOM   1918  CZ2 TRP B  70       5.895  24.024  60.967  1.00 26.45           C  
ATOM   1919  CZ3 TRP B  70       7.123  26.076  60.529  1.00 28.46           C  
ATOM   1920  CH2 TRP B  70       6.109  25.363  61.203  1.00 26.82           C  
ATOM   1921  N   TYR B  71       9.461  21.902  54.812  1.00 19.01           N  
ATOM   1922  CA  TYR B  71       9.125  20.752  53.987  1.00 18.76           C  
ATOM   1923  C   TYR B  71      10.040  19.600  54.365  1.00 19.22           C  
ATOM   1924  O   TYR B  71      11.264  19.719  54.264  1.00 19.97           O  
ATOM   1925  CB  TYR B  71       9.338  21.080  52.515  1.00 19.87           C  
ATOM   1926  CG  TYR B  71       8.960  19.975  51.568  1.00 19.54           C  
ATOM   1927  CD1 TYR B  71       7.699  19.934  50.996  1.00 20.23           C  
ATOM   1928  CD2 TYR B  71       9.881  19.001  51.204  1.00 20.73           C  
ATOM   1929  CE1 TYR B  71       7.362  18.956  50.072  1.00 21.11           C  
ATOM   1930  CE2 TYR B  71       9.557  18.014  50.281  1.00 20.88           C  
ATOM   1931  CZ  TYR B  71       8.292  18.001  49.714  1.00 22.00           C  
ATOM   1932  OH  TYR B  71       7.973  17.054  48.760  1.00 23.53           O  
ATOM   1933  N   ILE B  72       9.441  18.487  54.786  1.00 17.79           N  
ATOM   1934  CA  ILE B  72      10.190  17.304  55.189  1.00 15.62           C  
ATOM   1935  C   ILE B  72      10.468  16.379  54.015  1.00 15.58           C  
ATOM   1936  O   ILE B  72       9.555  15.807  53.419  1.00 17.01           O  
ATOM   1937  CB  ILE B  72       9.443  16.506  56.279  1.00 15.36           C  
ATOM   1938  CG1 ILE B  72       9.340  17.348  57.557  1.00 12.88           C  
ATOM   1939  CG2 ILE B  72      10.175  15.198  56.567  1.00 14.20           C  
ATOM   1940  CD1 ILE B  72       8.662  16.639  58.702  1.00 12.28           C  
ATOM   1941  N   HIS B  73      11.748  16.235  53.693  1.00 16.81           N  
ATOM   1942  CA  HIS B  73      12.188  15.386  52.595  1.00 16.06           C  
ATOM   1943  C   HIS B  73      13.072  14.275  53.170  1.00 16.08           C  
ATOM   1944  O   HIS B  73      14.139  14.543  53.725  1.00 16.52           O  
ATOM   1945  CB  HIS B  73      12.953  16.237  51.580  1.00 17.24           C  
ATOM   1946  CG  HIS B  73      13.337  15.493  50.346  1.00 19.00           C  
ATOM   1947  ND1 HIS B  73      14.350  14.561  50.329  1.00 20.46           N  
ATOM   1948  CD2 HIS B  73      12.808  15.500  49.101  1.00 19.42           C  
ATOM   1949  CE1 HIS B  73      14.429  14.022  49.125  1.00 19.79           C  
ATOM   1950  NE2 HIS B  73      13.503  14.575  48.362  1.00 20.70           N  
ATOM   1951  N   ASP B  74      12.610  13.029  53.049  1.00 16.05           N  
ATOM   1952  CA  ASP B  74      13.333  11.870  53.581  1.00 15.47           C  
ATOM   1953  C   ASP B  74      13.693  12.067  55.055  1.00 15.35           C  
ATOM   1954  O   ASP B  74      14.856  11.943  55.436  1.00 14.10           O  
ATOM   1955  CB  ASP B  74      14.622  11.623  52.790  1.00 15.61           C  
ATOM   1956  CG  ASP B  74      14.365  11.162  51.375  1.00 15.70           C  
ATOM   1957  OD1 ASP B  74      13.195  10.893  51.043  1.00 15.83           O  
ATOM   1958  OD2 ASP B  74      15.339  11.057  50.594  1.00 15.24           O  
ATOM   1959  N   LEU B  75      12.693  12.382  55.874  1.00 16.11           N  
ATOM   1960  CA  LEU B  75      12.899  12.601  57.308  1.00 18.82           C  
ATOM   1961  C   LEU B  75      13.572  13.932  57.665  1.00 19.15           C  
ATOM   1962  O   LEU B  75      13.388  14.440  58.767  1.00 19.50           O  
ATOM   1963  CB  LEU B  75      13.689  11.431  57.918  1.00 18.13           C  
ATOM   1964  CG  LEU B  75      12.854  10.234  58.401  1.00 18.78           C  
ATOM   1965  CD1 LEU B  75      11.749   9.929  57.398  1.00 18.05           C  
ATOM   1966  CD2 LEU B  75      13.754   9.020  58.609  1.00 18.01           C  
ATOM   1967  N   LEU B  76      14.351  14.500  56.751  1.00 19.02           N  
ATOM   1968  CA  LEU B  76      14.982  15.778  57.050  1.00 20.63           C  
ATOM   1969  C   LEU B  76      13.974  16.919  56.886  1.00 21.69           C  
ATOM   1970  O   LEU B  76      13.133  16.895  55.985  1.00 21.81           O  
ATOM   1971  CB  LEU B  76      16.208  16.011  56.156  1.00 20.50           C  
ATOM   1972  CG  LEU B  76      17.458  15.214  56.551  1.00 23.13           C  
ATOM   1973  CD1 LEU B  76      18.577  15.463  55.548  1.00 23.89           C  
ATOM   1974  CD2 LEU B  76      17.897  15.611  57.955  1.00 22.10           C  
ATOM   1975  N   LYS B  77      14.061  17.906  57.775  1.00 19.76           N  
ATOM   1976  CA  LYS B  77      13.166  19.055  57.755  1.00 19.45           C  
ATOM   1977  C   LYS B  77      13.917  20.282  57.240  1.00 19.45           C  
ATOM   1978  O   LYS B  77      14.957  20.660  57.779  1.00 19.18           O  
ATOM   1979  CB  LYS B  77      12.629  19.326  59.168  1.00 20.07           C  
ATOM   1980  CG  LYS B  77      11.461  20.312  59.240  1.00 19.98           C  
ATOM   1981  CD  LYS B  77      11.005  20.557  60.678  1.00 20.76           C  
ATOM   1982  CE  LYS B  77      10.616  19.259  61.383  1.00 23.09           C  
ATOM   1983  NZ  LYS B  77      10.063  19.485  62.760  1.00 22.48           N  
ATOM   1984  N   TYR B  78      13.390  20.894  56.187  1.00 19.98           N  
ATOM   1985  CA  TYR B  78      14.004  22.072  55.598  1.00 19.15           C  
ATOM   1986  C   TYR B  78      13.121  23.273  55.860  1.00 18.63           C  
ATOM   1987  O   TYR B  78      11.967  23.300  55.434  1.00 17.17           O  
ATOM   1988  CB  TYR B  78      14.172  21.876  54.097  1.00 19.06           C  
ATOM   1989  CG  TYR B  78      15.173  20.812  53.731  1.00 19.16           C  
ATOM   1990  CD1 TYR B  78      16.384  21.152  53.131  1.00 19.08           C  
ATOM   1991  CD2 TYR B  78      14.898  19.457  53.949  1.00 20.53           C  
ATOM   1992  CE1 TYR B  78      17.291  20.177  52.749  1.00 17.99           C  
ATOM   1993  CE2 TYR B  78      15.805  18.471  53.569  1.00 19.88           C  
ATOM   1994  CZ  TYR B  78      16.994  18.845  52.966  1.00 18.27           C  
ATOM   1995  OH  TYR B  78      17.877  17.888  52.541  1.00 22.80           O  
ATOM   1996  N   GLU B  79      13.674  24.269  56.546  1.00 19.10           N  
ATOM   1997  CA  GLU B  79      12.932  25.478  56.905  1.00 19.35           C  
ATOM   1998  C   GLU B  79      13.351  26.689  56.075  1.00 17.83           C  
ATOM   1999  O   GLU B  79      14.538  26.893  55.812  1.00 15.33           O  
ATOM   2000  CB  GLU B  79      13.156  25.779  58.391  1.00 21.58           C  
ATOM   2001  CG  GLU B  79      11.911  26.169  59.178  1.00 27.04           C  
ATOM   2002  CD  GLU B  79      12.196  26.421  60.669  1.00 29.55           C  
ATOM   2003  OE1 GLU B  79      11.243  26.366  61.476  1.00 31.79           O  
ATOM   2004  OE2 GLU B  79      13.363  26.685  61.035  1.00 30.27           O  
ATOM   2005  N   PHE B  80      12.366  27.487  55.670  1.00 17.70           N  
ATOM   2006  CA  PHE B  80      12.623  28.699  54.898  1.00 16.93           C  
ATOM   2007  C   PHE B  80      11.807  29.872  55.439  1.00 16.31           C  
ATOM   2008  O   PHE B  80      10.641  29.718  55.797  1.00 15.71           O  
ATOM   2009  CB  PHE B  80      12.309  28.466  53.419  1.00 16.89           C  
ATOM   2010  CG  PHE B  80      13.043  27.298  52.839  1.00 16.07           C  
ATOM   2011  CD1 PHE B  80      12.580  26.003  53.040  1.00 15.33           C  
ATOM   2012  CD2 PHE B  80      14.241  27.482  52.157  1.00 14.52           C  
ATOM   2013  CE1 PHE B  80      13.299  24.910  52.578  1.00 15.92           C  
ATOM   2014  CE2 PHE B  80      14.967  26.391  51.691  1.00 16.50           C  
ATOM   2015  CZ  PHE B  80      14.495  25.102  51.903  1.00 15.17           C  
ATOM   2016  N   ASP B  81      12.439  31.039  55.510  1.00 16.66           N  
ATOM   2017  CA  ASP B  81      11.787  32.243  56.009  1.00 18.55           C  
ATOM   2018  C   ASP B  81      10.902  32.860  54.936  1.00 19.25           C  
ATOM   2019  O   ASP B  81      11.319  32.988  53.785  1.00 19.04           O  
ATOM   2020  CB  ASP B  81      12.842  33.254  56.468  1.00 20.97           C  
ATOM   2021  CG  ASP B  81      13.557  32.810  57.728  1.00 23.85           C  
ATOM   2022  OD1 ASP B  81      14.093  31.680  57.744  1.00 24.54           O  
ATOM   2023  OD2 ASP B  81      13.585  33.586  58.706  1.00 24.54           O  
ATOM   2024  N   ILE B  82       9.682  33.238  55.318  1.00 20.22           N  
ATOM   2025  CA  ILE B  82       8.728  33.842  54.387  1.00 20.87           C  
ATOM   2026  C   ILE B  82       8.289  35.241  54.823  1.00 20.02           C  
ATOM   2027  O   ILE B  82       8.289  35.565  56.011  1.00 18.30           O  
ATOM   2028  CB  ILE B  82       7.463  32.954  54.213  1.00 21.48           C  
ATOM   2029  CG1 ILE B  82       6.876  32.589  55.577  1.00 21.15           C  
ATOM   2030  CG2 ILE B  82       7.804  31.697  53.431  1.00 19.99           C  
ATOM   2031  CD1 ILE B  82       5.593  31.762  55.481  1.00 22.91           C  
ATOM   2032  N   GLU B  83       7.907  36.064  53.851  1.00 20.40           N  
ATOM   2033  CA  GLU B  83       7.490  37.435  54.134  1.00 21.49           C  
ATOM   2034  C   GLU B  83       6.734  38.085  52.975  1.00 19.99           C  
ATOM   2035  O   GLU B  83       6.938  37.742  51.813  1.00 21.15           O  
ATOM   2036  CB  GLU B  83       8.728  38.267  54.462  1.00 21.40           C  
ATOM   2037  CG  GLU B  83       9.878  37.996  53.503  1.00 23.33           C  
ATOM   2038  CD  GLU B  83      11.228  38.406  54.057  1.00 26.07           C  
ATOM   2039  OE1 GLU B  83      11.496  39.632  54.108  1.00 26.86           O  
ATOM   2040  OE2 GLU B  83      12.009  37.496  54.450  1.00 22.48           O  
ATOM   2041  N   PHE B  84       5.858  39.026  53.305  1.00 18.69           N  
ATOM   2042  CA  PHE B  84       5.075  39.744  52.304  1.00 18.98           C  
ATOM   2043  C   PHE B  84       4.320  40.894  52.946  1.00 18.53           C  
ATOM   2044  O   PHE B  84       4.003  40.871  54.141  1.00 19.96           O  
ATOM   2045  CB  PHE B  84       4.068  38.816  51.599  1.00 18.60           C  
ATOM   2046  CG  PHE B  84       3.136  38.104  52.536  1.00 16.88           C  
ATOM   2047  CD1 PHE B  84       3.533  36.926  53.162  1.00 17.09           C  
ATOM   2048  CD2 PHE B  84       1.874  38.624  52.815  1.00 14.17           C  
ATOM   2049  CE1 PHE B  84       2.687  36.270  54.055  1.00 18.04           C  
ATOM   2050  CE2 PHE B  84       1.017  37.980  53.706  1.00 16.38           C  
ATOM   2051  CZ  PHE B  84       1.425  36.798  54.329  1.00 18.02           C  
ATOM   2052  N   ASP B  85       4.029  41.907  52.142  1.00 19.38           N  
ATOM   2053  CA  ASP B  85       3.305  43.061  52.640  1.00 20.38           C  
ATOM   2054  C   ASP B  85       1.914  43.084  52.055  1.00 21.00           C  
ATOM   2055  O   ASP B  85       1.722  42.819  50.872  1.00 20.20           O  
ATOM   2056  CB  ASP B  85       4.018  44.357  52.257  1.00 20.82           C  
ATOM   2057  CG  ASP B  85       5.487  44.329  52.587  1.00 21.40           C  
ATOM   2058  OD1 ASP B  85       5.859  43.680  53.596  1.00 24.83           O  
ATOM   2059  OD2 ASP B  85       6.265  44.972  51.844  1.00 20.95           O  
ATOM   2060  N   ILE B  86       0.942  43.401  52.895  1.00 21.41           N  
ATOM   2061  CA  ILE B  86      -0.434  43.485  52.455  1.00 21.90           C  
ATOM   2062  C   ILE B  86      -0.566  44.703  51.541  1.00 21.94           C  
ATOM   2063  O   ILE B  86      -0.292  45.831  51.957  1.00 23.84           O  
ATOM   2064  CB  ILE B  86      -1.376  43.657  53.662  1.00 22.24           C  
ATOM   2065  CG1 ILE B  86      -1.309  42.410  54.554  1.00 23.70           C  
ATOM   2066  CG2 ILE B  86      -2.784  43.938  53.194  1.00 21.93           C  
ATOM   2067  CD1 ILE B  86      -1.641  41.115  53.844  1.00 24.45           C  
ATOM   2068  N   PRO B  87      -0.941  44.488  50.267  1.00 22.64           N  
ATOM   2069  CA  PRO B  87      -1.100  45.611  49.334  1.00 23.27           C  
ATOM   2070  C   PRO B  87      -2.297  46.476  49.740  1.00 24.31           C  
ATOM   2071  O   PRO B  87      -3.228  45.992  50.397  1.00 23.26           O  
ATOM   2072  CB  PRO B  87      -1.297  44.921  47.980  1.00 22.35           C  
ATOM   2073  CG  PRO B  87      -1.862  43.575  48.352  1.00 23.05           C  
ATOM   2074  CD  PRO B  87      -1.060  43.198  49.564  1.00 23.58           C  
ATOM   2075  N   ILE B  88      -2.270  47.751  49.347  1.00 24.13           N  
ATOM   2076  CA  ILE B  88      -3.340  48.692  49.693  1.00 24.08           C  
ATOM   2077  C   ILE B  88      -4.725  48.231  49.231  1.00 24.60           C  
ATOM   2078  O   ILE B  88      -5.745  48.775  49.654  1.00 23.78           O  
ATOM   2079  CB  ILE B  88      -3.092  50.099  49.105  1.00 25.03           C  
ATOM   2080  CG1 ILE B  88      -3.903  51.137  49.895  1.00 25.95           C  
ATOM   2081  CG2 ILE B  88      -3.500  50.126  47.627  1.00 25.19           C  
ATOM   2082  CD1 ILE B  88      -3.623  52.583  49.512  1.00 27.45           C  
ATOM   2083  N   THR B  89      -4.767  47.225  48.368  1.00 25.72           N  
ATOM   2084  CA  THR B  89      -6.043  46.721  47.885  1.00 26.03           C  
ATOM   2085  C   THR B  89      -6.176  45.230  48.181  1.00 27.11           C  
ATOM   2086  O   THR B  89      -7.009  44.551  47.591  1.00 26.00           O  
ATOM   2087  CB  THR B  89      -6.190  46.974  46.355  1.00 26.24           C  
ATOM   2088  OG1 THR B  89      -4.977  46.608  45.680  1.00 22.47           O  
ATOM   2089  CG2 THR B  89      -6.481  48.446  46.086  1.00 24.33           C  
ATOM   2090  N   TYR B  90      -5.370  44.747  49.127  1.00 29.90           N  
ATOM   2091  CA  TYR B  90      -5.329  43.331  49.514  1.00 31.86           C  
ATOM   2092  C   TYR B  90      -6.562  42.456  49.318  1.00 33.16           C  
ATOM   2093  O   TYR B  90      -6.508  41.471  48.571  1.00 35.27           O  
ATOM   2094  CB  TYR B  90      -4.879  43.169  50.972  1.00 31.30           C  
ATOM   2095  CG  TYR B  90      -5.263  41.826  51.581  1.00 31.16           C  
ATOM   2096  CD1 TYR B  90      -6.199  41.750  52.620  1.00 28.89           C  
ATOM   2097  CD2 TYR B  90      -4.724  40.626  51.093  1.00 31.13           C  
ATOM   2098  CE1 TYR B  90      -6.590  40.517  53.156  1.00 27.74           C  
ATOM   2099  CE2 TYR B  90      -5.115  39.389  51.628  1.00 29.50           C  
ATOM   2100  CZ  TYR B  90      -6.048  39.349  52.658  1.00 28.40           C  
ATOM   2101  OH  TYR B  90      -6.437  38.141  53.182  1.00 27.91           O  
ATOM   2102  N   PRO B  91      -7.680  42.786  49.994  1.00 31.50           N  
ATOM   2103  CA  PRO B  91      -8.894  41.970  49.856  1.00 30.83           C  
ATOM   2104  C   PRO B  91      -9.155  41.554  48.406  1.00 30.72           C  
ATOM   2105  O   PRO B  91      -9.209  40.363  48.096  1.00 30.67           O  
ATOM   2106  CB  PRO B  91      -9.986  42.862  50.449  1.00 30.34           C  
ATOM   2107  CG  PRO B  91      -9.456  44.251  50.230  1.00 32.06           C  
ATOM   2108  CD  PRO B  91      -7.992  44.114  50.549  1.00 30.81           C  
ATOM   2109  N   THR B  92      -9.282  42.535  47.519  1.00 29.96           N  
ATOM   2110  CA  THR B  92      -9.530  42.267  46.114  1.00 29.64           C  
ATOM   2111  C   THR B  92      -8.279  41.781  45.380  1.00 29.81           C  
ATOM   2112  O   THR B  92      -8.367  40.971  44.456  1.00 30.90           O  
ATOM   2113  CB  THR B  92     -10.081  43.520  45.414  1.00 29.81           C  
ATOM   2114  OG1 THR B  92     -10.228  43.255  44.015  1.00 32.83           O  
ATOM   2115  CG2 THR B  92      -9.151  44.700  45.612  1.00 30.11           C  
ATOM   2116  N   THR B  93      -7.116  42.266  45.802  1.00 29.86           N  
ATOM   2117  CA  THR B  93      -5.840  41.877  45.199  1.00 29.18           C  
ATOM   2118  C   THR B  93      -5.329  40.636  45.926  1.00 29.46           C  
ATOM   2119  O   THR B  93      -6.112  39.773  46.295  1.00 30.85           O  
ATOM   2120  CB  THR B  93      -4.781  42.992  45.359  1.00 28.88           C  
ATOM   2121  OG1 THR B  93      -5.402  44.268  45.173  1.00 29.08           O  
ATOM   2122  CG2 THR B  93      -3.669  42.830  44.330  1.00 25.98           C  
ATOM   2123  N   ALA B  94      -4.019  40.563  46.145  1.00 27.77           N  
ATOM   2124  CA  ALA B  94      -3.396  39.434  46.836  1.00 26.64           C  
ATOM   2125  C   ALA B  94      -1.926  39.752  47.057  1.00 25.66           C  
ATOM   2126  O   ALA B  94      -1.275  40.333  46.187  1.00 27.73           O  
ATOM   2127  CB  ALA B  94      -3.535  38.161  46.015  1.00 27.01           C  
ATOM   2128  N   PRO B  95      -1.384  39.389  48.233  1.00 24.38           N  
ATOM   2129  CA  PRO B  95       0.030  39.659  48.527  1.00 22.98           C  
ATOM   2130  C   PRO B  95       1.011  38.796  47.735  1.00 22.02           C  
ATOM   2131  O   PRO B  95       0.634  37.770  47.165  1.00 23.04           O  
ATOM   2132  CB  PRO B  95       0.120  39.421  50.031  1.00 21.72           C  
ATOM   2133  CG  PRO B  95      -0.972  38.426  50.290  1.00 24.56           C  
ATOM   2134  CD  PRO B  95      -2.098  38.952  49.447  1.00 23.11           C  
ATOM   2135  N   GLU B  96       2.267  39.229  47.687  1.00 21.24           N  
ATOM   2136  CA  GLU B  96       3.289  38.485  46.966  1.00 22.17           C  
ATOM   2137  C   GLU B  96       4.192  37.761  47.946  1.00 21.14           C  
ATOM   2138  O   GLU B  96       5.168  38.322  48.441  1.00 20.96           O  
ATOM   2139  CB  GLU B  96       4.135  39.412  46.083  1.00 21.31           C  
ATOM   2140  CG  GLU B  96       3.347  40.167  45.024  1.00 24.44           C  
ATOM   2141  CD  GLU B  96       4.221  41.070  44.167  1.00 27.06           C  
ATOM   2142  OE1 GLU B  96       5.012  40.543  43.357  1.00 28.30           O  
ATOM   2143  OE2 GLU B  96       4.129  42.306  44.309  1.00 27.32           O  
ATOM   2144  N   ILE B  97       3.850  36.512  48.230  1.00 19.92           N  
ATOM   2145  CA  ILE B  97       4.635  35.701  49.143  1.00 20.68           C  
ATOM   2146  C   ILE B  97       6.091  35.714  48.696  1.00 20.44           C  
ATOM   2147  O   ILE B  97       6.382  35.650  47.500  1.00 19.81           O  
ATOM   2148  CB  ILE B  97       4.142  34.266  49.133  1.00 20.64           C  
ATOM   2149  CG1 ILE B  97       2.620  34.250  49.320  1.00 22.16           C  
ATOM   2150  CG2 ILE B  97       4.846  33.478  50.221  1.00 21.12           C  
ATOM   2151  CD1 ILE B  97       1.987  32.894  49.065  1.00 23.22           C  
ATOM   2152  N   ALA B  98       7.006  35.801  49.654  1.00 19.22           N  
ATOM   2153  CA  ALA B  98       8.421  35.820  49.326  1.00 17.50           C  
ATOM   2154  C   ALA B  98       9.251  34.931  50.227  1.00 18.54           C  
ATOM   2155  O   ALA B  98       9.110  34.949  51.455  1.00 19.18           O  
ATOM   2156  CB  ALA B  98       8.958  37.245  49.387  1.00 14.34           C  
ATOM   2157  N   VAL B  99      10.098  34.127  49.595  1.00 18.60           N  
ATOM   2158  CA  VAL B  99      11.021  33.258  50.310  1.00 18.23           C  
ATOM   2159  C   VAL B  99      12.411  33.682  49.823  1.00 19.89           C  
ATOM   2160  O   VAL B  99      12.934  33.166  48.826  1.00 18.09           O  
ATOM   2161  CB  VAL B  99      10.740  31.732  50.055  1.00 18.29           C  
ATOM   2162  CG1 VAL B  99      10.642  31.423  48.566  1.00 19.54           C  
ATOM   2163  CG2 VAL B  99      11.840  30.898  50.706  1.00 17.82           C  
ATOM   2164  N   PRO B 100      13.000  34.679  50.513  1.00 20.64           N  
ATOM   2165  CA  PRO B 100      14.317  35.275  50.260  1.00 21.58           C  
ATOM   2166  C   PRO B 100      15.488  34.311  50.168  1.00 21.85           C  
ATOM   2167  O   PRO B 100      16.333  34.451  49.282  1.00 24.49           O  
ATOM   2168  CB  PRO B 100      14.472  36.275  51.408  1.00 21.99           C  
ATOM   2169  CG  PRO B 100      13.522  35.760  52.461  1.00 21.94           C  
ATOM   2170  CD  PRO B 100      12.347  35.360  51.642  1.00 19.23           C  
ATOM   2171  N   GLU B 101      15.541  33.343  51.079  1.00 22.92           N  
ATOM   2172  CA  GLU B 101      16.618  32.360  51.092  1.00 24.63           C  
ATOM   2173  C   GLU B 101      16.852  31.741  49.726  1.00 25.63           C  
ATOM   2174  O   GLU B 101      17.992  31.604  49.277  1.00 26.09           O  
ATOM   2175  CB  GLU B 101      16.316  31.250  52.111  1.00 24.80           C  
ATOM   2176  CG  GLU B 101      16.663  31.631  53.546  1.00 26.78           C  
ATOM   2177  CD  GLU B 101      16.324  30.555  54.573  1.00 29.21           C  
ATOM   2178  OE1 GLU B 101      16.693  29.375  54.363  1.00 29.11           O  
ATOM   2179  OE2 GLU B 101      15.697  30.901  55.601  1.00 28.53           O  
ATOM   2180  N   LEU B 102      15.759  31.380  49.064  1.00 27.59           N  
ATOM   2181  CA  LEU B 102      15.825  30.749  47.755  1.00 28.24           C  
ATOM   2182  C   LEU B 102      16.034  31.709  46.587  1.00 28.73           C  
ATOM   2183  O   LEU B 102      16.338  31.268  45.484  1.00 30.13           O  
ATOM   2184  CB  LEU B 102      14.559  29.922  47.524  1.00 27.92           C  
ATOM   2185  CG  LEU B 102      14.319  28.813  48.554  1.00 27.54           C  
ATOM   2186  CD1 LEU B 102      13.022  28.079  48.250  1.00 28.22           C  
ATOM   2187  CD2 LEU B 102      15.491  27.860  48.539  1.00 27.10           C  
ATOM   2188  N   ASP B 103      15.885  33.010  46.822  1.00 30.52           N  
ATOM   2189  CA  ASP B 103      16.059  33.990  45.754  1.00 32.26           C  
ATOM   2190  C   ASP B 103      17.283  33.639  44.910  1.00 33.65           C  
ATOM   2191  O   ASP B 103      18.353  33.335  45.439  1.00 35.13           O  
ATOM   2192  CB  ASP B 103      16.176  35.406  46.342  1.00 31.46           C  
ATOM   2193  CG  ASP B 103      16.220  36.502  45.268  1.00 31.73           C  
ATOM   2194  OD1 ASP B 103      15.530  36.369  44.233  1.00 32.82           O  
ATOM   2195  OD2 ASP B 103      16.929  37.517  45.474  1.00 31.10           O  
ATOM   2196  N   GLY B 104      17.101  33.656  43.591  1.00 34.87           N  
ATOM   2197  CA  GLY B 104      18.182  33.335  42.675  1.00 36.90           C  
ATOM   2198  C   GLY B 104      18.636  31.887  42.758  1.00 38.71           C  
ATOM   2199  O   GLY B 104      19.827  31.617  42.928  1.00 40.62           O  
ATOM   2200  N   LYS B 105      17.691  30.957  42.626  1.00 39.35           N  
ATOM   2201  CA  LYS B 105      17.974  29.519  42.695  1.00 38.69           C  
ATOM   2202  C   LYS B 105      16.951  28.709  41.899  1.00 38.76           C  
ATOM   2203  O   LYS B 105      17.090  27.495  41.741  1.00 37.32           O  
ATOM   2204  CB  LYS B 105      17.961  29.052  44.154  1.00 40.12           C  
ATOM   2205  CG  LYS B 105      19.250  29.340  44.912  1.00 41.49           C  
ATOM   2206  CD  LYS B 105      19.171  28.884  46.363  1.00 41.86           C  
ATOM   2207  CE  LYS B 105      20.557  28.722  46.973  1.00 41.50           C  
ATOM   2208  NZ  LYS B 105      21.307  27.578  46.374  1.00 41.95           N  
ATOM   2209  N   THR B 106      15.927  29.394  41.402  1.00 38.36           N  
ATOM   2210  CA  THR B 106      14.870  28.756  40.633  1.00 37.42           C  
ATOM   2211  C   THR B 106      14.242  29.739  39.663  1.00 37.79           C  
ATOM   2212  O   THR B 106      13.770  30.802  40.068  1.00 37.56           O  
ATOM   2213  CB  THR B 106      13.750  28.250  41.541  1.00 38.14           C  
ATOM   2214  OG1 THR B 106      14.308  27.446  42.584  1.00 37.33           O  
ATOM   2215  CG2 THR B 106      12.744  27.431  40.738  1.00 38.04           C  
ATOM   2216  N   ALA B 107      14.229  29.369  38.388  1.00 38.95           N  
ATOM   2217  CA  ALA B 107      13.654  30.196  37.338  1.00 38.65           C  
ATOM   2218  C   ALA B 107      12.209  30.541  37.671  1.00 39.68           C  
ATOM   2219  O   ALA B 107      11.734  31.636  37.361  1.00 40.54           O  
ATOM   2220  CB  ALA B 107      13.720  29.457  36.016  1.00 37.44           C  
ATOM   2221  N   LYS B 108      11.522  29.601  38.316  1.00 39.67           N  
ATOM   2222  CA  LYS B 108      10.120  29.766  38.705  1.00 39.87           C  
ATOM   2223  C   LYS B 108       9.990  30.607  39.974  1.00 40.07           C  
ATOM   2224  O   LYS B 108       9.587  30.102  41.019  1.00 39.23           O  
ATOM   2225  CB  LYS B 108       9.488  28.385  38.923  1.00 38.86           C  
ATOM   2226  CG  LYS B 108       9.650  27.450  37.728  1.00 38.71           C  
ATOM   2227  CD  LYS B 108       9.407  25.994  38.097  1.00 39.52           C  
ATOM   2228  CE  LYS B 108      10.022  25.059  37.062  1.00 38.20           C  
ATOM   2229  NZ  LYS B 108      11.484  25.332  36.876  1.00 37.99           N  
HETATM 2230  N   MSE B 109      10.318  31.892  39.871  1.00 41.30           N  
HETATM 2231  CA  MSE B 109      10.255  32.799  41.015  1.00 43.77           C  
HETATM 2232  C   MSE B 109      10.673  34.208  40.576  1.00 44.49           C  
HETATM 2233  O   MSE B 109      11.588  34.366  39.764  1.00 44.79           O  
HETATM 2234  CB  MSE B 109      11.179  32.269  42.119  1.00 44.45           C  
HETATM 2235  CG  MSE B 109      11.127  32.998  43.447  1.00 45.57           C  
HETATM 2236 SE   MSE B 109      11.979  31.930  44.843  1.00 50.00          SE  
HETATM 2237  CE  MSE B 109      13.733  31.748  44.019  1.00 46.35           C  
ATOM   2238  N   TYR B 110       9.992  35.226  41.104  1.00 44.99           N  
ATOM   2239  CA  TYR B 110      10.291  36.615  40.756  1.00 46.24           C  
ATOM   2240  C   TYR B 110      11.524  37.179  41.452  1.00 46.86           C  
ATOM   2241  O   TYR B 110      12.215  36.485  42.196  1.00 47.42           O  
ATOM   2242  CB  TYR B 110       9.094  37.525  41.061  1.00 46.58           C  
ATOM   2243  CG  TYR B 110       7.995  37.449  40.034  1.00 46.82           C  
ATOM   2244  CD1 TYR B 110       6.871  36.654  40.243  1.00 47.09           C  
ATOM   2245  CD2 TYR B 110       8.107  38.130  38.826  1.00 47.13           C  
ATOM   2246  CE1 TYR B 110       5.883  36.534  39.269  1.00 48.58           C  
ATOM   2247  CE2 TYR B 110       7.131  38.018  37.844  1.00 48.60           C  
ATOM   2248  CZ  TYR B 110       6.022  37.216  38.068  1.00 49.02           C  
ATOM   2249  OH  TYR B 110       5.073  37.072  37.078  1.00 50.15           O  
ATOM   2250  N   ARG B 111      11.788  38.455  41.197  1.00 47.10           N  
ATOM   2251  CA  ARG B 111      12.930  39.138  41.782  1.00 47.48           C  
ATOM   2252  C   ARG B 111      12.717  39.310  43.288  1.00 46.55           C  
ATOM   2253  O   ARG B 111      11.593  39.527  43.745  1.00 45.40           O  
ATOM   2254  CB  ARG B 111      13.110  40.503  41.104  1.00 49.80           C  
ATOM   2255  CG  ARG B 111      14.556  40.880  40.771  1.00 52.91           C  
ATOM   2256  CD  ARG B 111      15.237  39.802  39.927  1.00 54.83           C  
ATOM   2257  NE  ARG B 111      16.507  40.249  39.354  1.00 56.61           N  
ATOM   2258  CZ  ARG B 111      16.611  41.129  38.361  1.00 57.82           C  
ATOM   2259  NH1 ARG B 111      17.805  41.479  37.902  1.00 58.49           N  
ATOM   2260  NH2 ARG B 111      15.521  41.656  37.822  1.00 58.08           N  
ATOM   2261  N   GLY B 112      13.798  39.198  44.055  1.00 45.83           N  
ATOM   2262  CA  GLY B 112      13.694  39.343  45.496  1.00 43.93           C  
ATOM   2263  C   GLY B 112      13.169  38.104  46.202  1.00 42.37           C  
ATOM   2264  O   GLY B 112      13.036  38.088  47.427  1.00 42.02           O  
ATOM   2265  N   GLY B 113      12.854  37.071  45.428  1.00 40.19           N  
ATOM   2266  CA  GLY B 113      12.363  35.836  46.009  1.00 38.43           C  
ATOM   2267  C   GLY B 113      10.859  35.680  45.976  1.00 36.56           C  
ATOM   2268  O   GLY B 113      10.320  34.719  46.524  1.00 34.63           O  
ATOM   2269  N   LYS B 114      10.176  36.625  45.339  1.00 36.69           N  
ATOM   2270  CA  LYS B 114       8.721  36.568  45.245  1.00 38.12           C  
ATOM   2271  C   LYS B 114       8.300  35.288  44.532  1.00 38.82           C  
ATOM   2272  O   LYS B 114       8.866  34.912  43.505  1.00 37.77           O  
ATOM   2273  CB  LYS B 114       8.180  37.792  44.496  1.00 37.91           C  
ATOM   2274  CG  LYS B 114       8.481  39.125  45.182  1.00 39.42           C  
ATOM   2275  CD  LYS B 114       8.029  40.329  44.344  1.00 41.75           C  
ATOM   2276  CE  LYS B 114       8.703  40.353  42.963  1.00 42.18           C  
ATOM   2277  NZ  LYS B 114       8.343  41.544  42.124  1.00 43.63           N  
ATOM   2278  N   ILE B 115       7.311  34.612  45.100  1.00 40.36           N  
ATOM   2279  CA  ILE B 115       6.811  33.374  44.531  1.00 43.02           C  
ATOM   2280  C   ILE B 115       5.896  33.694  43.361  1.00 45.31           C  
ATOM   2281  O   ILE B 115       5.268  34.755  43.324  1.00 45.55           O  
ATOM   2282  CB  ILE B 115       6.014  32.564  45.580  1.00 42.82           C  
ATOM   2283  CG1 ILE B 115       6.933  32.156  46.738  1.00 42.88           C  
ATOM   2284  CG2 ILE B 115       5.378  31.353  44.931  1.00 41.74           C  
ATOM   2285  CD1 ILE B 115       8.116  31.295  46.332  1.00 42.07           C  
ATOM   2286  N   CYS B 116       5.834  32.777  42.402  1.00 47.18           N  
ATOM   2287  CA  CYS B 116       4.981  32.955  41.234  1.00 48.90           C  
ATOM   2288  C   CYS B 116       4.123  31.721  40.990  1.00 48.48           C  
ATOM   2289  O   CYS B 116       4.609  30.691  40.534  1.00 47.76           O  
ATOM   2290  CB  CYS B 116       5.827  33.275  39.994  1.00 51.35           C  
ATOM   2291  SG  CYS B 116       7.272  32.220  39.727  1.00 57.25           S  
ATOM   2292  N   LEU B 117       2.837  31.839  41.301  1.00 48.36           N  
ATOM   2293  CA  LEU B 117       1.910  30.733  41.127  1.00 47.64           C  
ATOM   2294  C   LEU B 117       1.582  30.498  39.660  1.00 47.84           C  
ATOM   2295  O   LEU B 117       2.140  31.152  38.772  1.00 47.12           O  
ATOM   2296  CB  LEU B 117       0.614  30.997  41.901  1.00 47.19           C  
ATOM   2297  CG  LEU B 117       0.709  31.299  43.398  1.00 46.47           C  
ATOM   2298  CD1 LEU B 117       1.655  30.311  44.070  1.00 46.14           C  
ATOM   2299  CD2 LEU B 117       1.196  32.717  43.595  1.00 46.15           C  
ATOM   2300  N   THR B 118       0.677  29.549  39.423  1.00 48.90           N  
ATOM   2301  CA  THR B 118       0.231  29.200  38.076  1.00 48.85           C  
ATOM   2302  C   THR B 118      -0.791  30.216  37.592  1.00 48.37           C  
ATOM   2303  O   THR B 118      -1.528  30.799  38.387  1.00 47.79           O  
ATOM   2304  CB  THR B 118      -0.431  27.791  38.023  1.00 49.03           C  
ATOM   2305  OG1 THR B 118      -0.991  27.468  39.303  1.00 49.24           O  
ATOM   2306  CG2 THR B 118       0.581  26.725  37.613  1.00 48.57           C  
ATOM   2307  N   ASP B 119      -0.823  30.419  36.280  1.00 49.37           N  
ATOM   2308  CA  ASP B 119      -1.744  31.360  35.655  1.00 49.36           C  
ATOM   2309  C   ASP B 119      -3.187  31.010  36.017  1.00 48.96           C  
ATOM   2310  O   ASP B 119      -4.101  31.811  35.831  1.00 49.01           O  
ATOM   2311  CB  ASP B 119      -1.566  31.333  34.127  1.00 50.14           C  
ATOM   2312  CG  ASP B 119      -0.387  30.469  33.681  1.00 49.93           C  
ATOM   2313  OD1 ASP B 119      -0.422  29.239  33.908  1.00 50.27           O  
ATOM   2314  OD2 ASP B 119       0.574  31.019  33.100  1.00 49.63           O  
ATOM   2315  N   HIS B 120      -3.379  29.807  36.546  1.00 47.89           N  
ATOM   2316  CA  HIS B 120      -4.702  29.333  36.931  1.00 46.99           C  
ATOM   2317  C   HIS B 120      -5.021  29.752  38.364  1.00 46.26           C  
ATOM   2318  O   HIS B 120      -6.033  29.336  38.927  1.00 46.79           O  
ATOM   2319  CB  HIS B 120      -4.749  27.810  36.799  1.00 46.98           C  
ATOM   2320  CG  HIS B 120      -4.192  27.307  35.501  1.00 46.96           C  
ATOM   2321  ND1 HIS B 120      -3.791  26.001  35.315  1.00 46.19           N  
ATOM   2322  CD2 HIS B 120      -3.946  27.944  34.331  1.00 45.47           C  
ATOM   2323  CE1 HIS B 120      -3.319  25.857  34.090  1.00 44.63           C  
ATOM   2324  NE2 HIS B 120      -3.402  27.021  33.472  1.00 45.02           N  
ATOM   2325  N   PHE B 121      -4.155  30.586  38.939  1.00 44.94           N  
ATOM   2326  CA  PHE B 121      -4.315  31.069  40.312  1.00 41.65           C  
ATOM   2327  C   PHE B 121      -5.195  32.311  40.435  1.00 40.90           C  
ATOM   2328  O   PHE B 121      -6.285  32.252  41.008  1.00 42.20           O  
ATOM   2329  CB  PHE B 121      -2.949  31.376  40.937  1.00 40.48           C  
ATOM   2330  CG  PHE B 121      -3.035  31.975  42.316  1.00 39.57           C  
ATOM   2331  CD1 PHE B 121      -3.317  31.177  43.421  1.00 39.99           C  
ATOM   2332  CD2 PHE B 121      -2.867  33.343  42.507  1.00 39.05           C  
ATOM   2333  CE1 PHE B 121      -3.435  31.732  44.705  1.00 38.98           C  
ATOM   2334  CE2 PHE B 121      -2.984  33.911  43.783  1.00 39.12           C  
ATOM   2335  CZ  PHE B 121      -3.268  33.101  44.885  1.00 38.75           C  
ATOM   2336  N   LYS B 122      -4.719  33.433  39.901  1.00 39.93           N  
ATOM   2337  CA  LYS B 122      -5.452  34.693  39.987  1.00 37.83           C  
ATOM   2338  C   LYS B 122      -6.950  34.633  39.733  1.00 36.72           C  
ATOM   2339  O   LYS B 122      -7.733  35.166  40.515  1.00 36.85           O  
ATOM   2340  CB  LYS B 122      -4.825  35.741  39.062  1.00 37.30           C  
ATOM   2341  CG  LYS B 122      -3.896  36.679  39.799  1.00 38.24           C  
ATOM   2342  CD  LYS B 122      -4.633  37.366  40.946  1.00 38.13           C  
ATOM   2343  CE  LYS B 122      -3.668  38.049  41.894  1.00 37.38           C  
ATOM   2344  NZ  LYS B 122      -4.387  38.820  42.933  1.00 38.49           N  
ATOM   2345  N   PRO B 123      -7.372  33.991  38.634  1.00 36.38           N  
ATOM   2346  CA  PRO B 123      -8.810  33.915  38.356  1.00 35.25           C  
ATOM   2347  C   PRO B 123      -9.579  33.374  39.565  1.00 34.43           C  
ATOM   2348  O   PRO B 123     -10.570  33.960  40.002  1.00 33.98           O  
ATOM   2349  CB  PRO B 123      -8.874  32.985  37.146  1.00 36.34           C  
ATOM   2350  CG  PRO B 123      -7.578  33.273  36.436  1.00 36.38           C  
ATOM   2351  CD  PRO B 123      -6.591  33.314  37.580  1.00 36.35           C  
ATOM   2352  N   LEU B 124      -9.100  32.258  40.105  1.00 33.63           N  
ATOM   2353  CA  LEU B 124      -9.722  31.626  41.263  1.00 32.86           C  
ATOM   2354  C   LEU B 124      -9.872  32.610  42.423  1.00 32.26           C  
ATOM   2355  O   LEU B 124     -10.957  32.756  42.994  1.00 32.96           O  
ATOM   2356  CB  LEU B 124      -8.884  30.428  41.710  1.00 31.32           C  
ATOM   2357  CG  LEU B 124      -9.241  29.813  43.059  1.00 30.49           C  
ATOM   2358  CD1 LEU B 124     -10.657  29.260  43.028  1.00 31.89           C  
ATOM   2359  CD2 LEU B 124      -8.245  28.719  43.382  1.00 30.95           C  
ATOM   2360  N   TRP B 125      -8.776  33.279  42.767  1.00 29.43           N  
ATOM   2361  CA  TRP B 125      -8.772  34.255  43.852  1.00 27.79           C  
ATOM   2362  C   TRP B 125      -9.802  35.371  43.606  1.00 28.10           C  
ATOM   2363  O   TRP B 125     -10.742  35.546  44.387  1.00 26.10           O  
ATOM   2364  CB  TRP B 125      -7.359  34.843  44.009  1.00 26.08           C  
ATOM   2365  CG  TRP B 125      -7.225  35.813  45.144  1.00 25.00           C  
ATOM   2366  CD1 TRP B 125      -7.657  37.107  45.170  1.00 24.37           C  
ATOM   2367  CD2 TRP B 125      -6.684  35.546  46.444  1.00 25.29           C  
ATOM   2368  NE1 TRP B 125      -7.427  37.661  46.403  1.00 24.89           N  
ATOM   2369  CE2 TRP B 125      -6.830  36.726  47.207  1.00 25.55           C  
ATOM   2370  CE3 TRP B 125      -6.095  34.423  47.040  1.00 23.68           C  
ATOM   2371  CZ2 TRP B 125      -6.405  36.817  48.538  1.00 24.38           C  
ATOM   2372  CZ3 TRP B 125      -5.673  34.513  48.367  1.00 24.04           C  
ATOM   2373  CH2 TRP B 125      -5.832  35.703  49.098  1.00 24.66           C  
ATOM   2374  N   ALA B 126      -9.626  36.105  42.511  1.00 28.06           N  
ATOM   2375  CA  ALA B 126     -10.519  37.202  42.149  1.00 28.02           C  
ATOM   2376  C   ALA B 126     -12.010  36.869  42.246  1.00 29.04           C  
ATOM   2377  O   ALA B 126     -12.789  37.657  42.780  1.00 29.20           O  
ATOM   2378  CB  ALA B 126     -10.194  37.682  40.743  1.00 27.61           C  
ATOM   2379  N   ARG B 127     -12.407  35.706  41.736  1.00 29.89           N  
ATOM   2380  CA  ARG B 127     -13.814  35.304  41.754  1.00 29.62           C  
ATOM   2381  C   ARG B 127     -14.280  34.781  43.105  1.00 29.85           C  
ATOM   2382  O   ARG B 127     -15.407  34.305  43.242  1.00 30.52           O  
ATOM   2383  CB  ARG B 127     -14.071  34.247  40.677  1.00 29.61           C  
ATOM   2384  CG  ARG B 127     -13.355  32.934  40.906  1.00 30.55           C  
ATOM   2385  CD  ARG B 127     -13.248  32.145  39.610  1.00 31.46           C  
ATOM   2386  NE  ARG B 127     -12.516  30.896  39.811  1.00 30.88           N  
ATOM   2387  CZ  ARG B 127     -11.962  30.180  38.837  1.00 29.27           C  
ATOM   2388  NH1 ARG B 127     -12.052  30.586  37.575  1.00 26.87           N  
ATOM   2389  NH2 ARG B 127     -11.315  29.056  39.130  1.00 27.35           N  
ATOM   2390  N   ASN B 128     -13.415  34.869  44.107  1.00 29.98           N  
ATOM   2391  CA  ASN B 128     -13.766  34.403  45.443  1.00 28.76           C  
ATOM   2392  C   ASN B 128     -13.755  35.541  46.456  1.00 28.10           C  
ATOM   2393  O   ASN B 128     -14.170  35.364  47.599  1.00 27.79           O  
ATOM   2394  CB  ASN B 128     -12.802  33.296  45.869  1.00 29.07           C  
ATOM   2395  CG  ASN B 128     -13.283  31.922  45.455  1.00 29.12           C  
ATOM   2396  OD1 ASN B 128     -14.219  31.377  46.043  1.00 28.69           O  
ATOM   2397  ND2 ASN B 128     -12.660  31.359  44.430  1.00 29.31           N  
ATOM   2398  N   VAL B 129     -13.293  36.708  46.013  1.00 27.36           N  
ATOM   2399  CA  VAL B 129     -13.209  37.887  46.859  1.00 26.47           C  
ATOM   2400  C   VAL B 129     -14.541  38.211  47.527  1.00 26.68           C  
ATOM   2401  O   VAL B 129     -15.591  38.197  46.883  1.00 27.45           O  
ATOM   2402  CB  VAL B 129     -12.742  39.115  46.034  1.00 26.42           C  
ATOM   2403  CG1 VAL B 129     -12.656  40.356  46.913  1.00 26.21           C  
ATOM   2404  CG2 VAL B 129     -11.395  38.822  45.402  1.00 25.89           C  
ATOM   2405  N   PRO B 130     -14.517  38.503  48.840  1.00 26.83           N  
ATOM   2406  CA  PRO B 130     -13.335  38.539  49.711  1.00 26.53           C  
ATOM   2407  C   PRO B 130     -13.287  37.354  50.693  1.00 25.72           C  
ATOM   2408  O   PRO B 130     -12.716  37.460  51.782  1.00 25.66           O  
ATOM   2409  CB  PRO B 130     -13.510  39.864  50.430  1.00 26.41           C  
ATOM   2410  CG  PRO B 130     -14.978  39.850  50.716  1.00 27.08           C  
ATOM   2411  CD  PRO B 130     -15.609  39.302  49.430  1.00 26.24           C  
ATOM   2412  N   LYS B 131     -13.890  36.236  50.290  1.00 24.47           N  
ATOM   2413  CA  LYS B 131     -13.956  35.032  51.111  1.00 23.21           C  
ATOM   2414  C   LYS B 131     -12.609  34.379  51.392  1.00 21.61           C  
ATOM   2415  O   LYS B 131     -12.420  33.760  52.439  1.00 21.27           O  
ATOM   2416  CB  LYS B 131     -14.909  34.014  50.471  1.00 23.12           C  
ATOM   2417  CG  LYS B 131     -16.360  34.453  50.529  1.00 25.43           C  
ATOM   2418  CD  LYS B 131     -17.332  33.370  50.077  1.00 26.37           C  
ATOM   2419  CE  LYS B 131     -17.159  33.013  48.609  1.00 27.52           C  
ATOM   2420  NZ  LYS B 131     -18.247  32.102  48.150  1.00 26.42           N  
ATOM   2421  N   PHE B 132     -11.674  34.513  50.461  1.00 19.44           N  
ATOM   2422  CA  PHE B 132     -10.348  33.938  50.641  1.00 19.01           C  
ATOM   2423  C   PHE B 132      -9.468  34.889  51.430  1.00 17.80           C  
ATOM   2424  O   PHE B 132      -9.586  36.108  51.300  1.00 19.62           O  
ATOM   2425  CB  PHE B 132      -9.702  33.650  49.287  1.00 18.57           C  
ATOM   2426  CG  PHE B 132     -10.170  32.377  48.651  1.00 17.50           C  
ATOM   2427  CD1 PHE B 132     -11.308  31.721  49.114  1.00 17.26           C  
ATOM   2428  CD2 PHE B 132      -9.468  31.826  47.594  1.00 15.98           C  
ATOM   2429  CE1 PHE B 132     -11.735  30.534  48.531  1.00 17.70           C  
ATOM   2430  CE2 PHE B 132      -9.887  30.645  47.007  1.00 18.39           C  
ATOM   2431  CZ  PHE B 132     -11.024  29.994  47.476  1.00 15.52           C  
ATOM   2432  N   GLY B 133      -8.595  34.321  52.258  1.00 16.37           N  
ATOM   2433  CA  GLY B 133      -7.691  35.122  53.065  1.00 13.04           C  
ATOM   2434  C   GLY B 133      -6.257  34.633  52.963  1.00 10.48           C  
ATOM   2435  O   GLY B 133      -5.936  33.825  52.095  1.00  9.52           O  
ATOM   2436  N   LEU B 134      -5.389  35.107  53.847  1.00 10.67           N  
ATOM   2437  CA  LEU B 134      -3.989  34.698  53.821  1.00  7.90           C  
ATOM   2438  C   LEU B 134      -3.852  33.190  53.982  1.00  8.81           C  
ATOM   2439  O   LEU B 134      -2.930  32.589  53.426  1.00 10.39           O  
ATOM   2440  CB  LEU B 134      -3.208  35.418  54.921  1.00  4.26           C  
ATOM   2441  CG  LEU B 134      -3.157  36.951  54.833  1.00  3.93           C  
ATOM   2442  CD1 LEU B 134      -2.428  37.486  56.050  1.00  1.00           C  
ATOM   2443  CD2 LEU B 134      -2.455  37.396  53.544  1.00  2.29           C  
ATOM   2444  N   ALA B 135      -4.764  32.584  54.741  1.00  9.23           N  
ATOM   2445  CA  ALA B 135      -4.755  31.135  54.955  1.00 10.53           C  
ATOM   2446  C   ALA B 135      -4.976  30.439  53.616  1.00 11.54           C  
ATOM   2447  O   ALA B 135      -4.268  29.491  53.289  1.00 10.79           O  
ATOM   2448  CB  ALA B 135      -5.854  30.742  55.942  1.00  9.18           C  
ATOM   2449  N   HIS B 136      -5.958  30.924  52.848  1.00 15.62           N  
ATOM   2450  CA  HIS B 136      -6.268  30.365  51.525  1.00 19.25           C  
ATOM   2451  C   HIS B 136      -5.088  30.579  50.587  1.00 19.05           C  
ATOM   2452  O   HIS B 136      -4.785  29.728  49.754  1.00 19.65           O  
ATOM   2453  CB  HIS B 136      -7.515  31.024  50.929  1.00 21.40           C  
ATOM   2454  CG  HIS B 136      -8.754  30.780  51.728  1.00 22.68           C  
ATOM   2455  ND1 HIS B 136      -9.063  31.508  52.857  1.00 23.92           N  
ATOM   2456  CD2 HIS B 136      -9.722  29.841  51.609  1.00 22.87           C  
ATOM   2457  CE1 HIS B 136     -10.167  31.025  53.401  1.00 26.07           C  
ATOM   2458  NE2 HIS B 136     -10.587  30.012  52.664  1.00 25.14           N  
ATOM   2459  N   LEU B 137      -4.434  31.727  50.736  1.00 19.19           N  
ATOM   2460  CA  LEU B 137      -3.268  32.083  49.940  1.00 19.97           C  
ATOM   2461  C   LEU B 137      -2.143  31.092  50.234  1.00 20.60           C  
ATOM   2462  O   LEU B 137      -1.452  30.626  49.331  1.00 18.92           O  
ATOM   2463  CB  LEU B 137      -2.802  33.493  50.312  1.00 20.21           C  
ATOM   2464  CG  LEU B 137      -1.408  33.917  49.831  1.00 20.49           C  
ATOM   2465  CD1 LEU B 137      -1.484  34.345  48.355  1.00 18.93           C  
ATOM   2466  CD2 LEU B 137      -0.887  35.060  50.702  1.00 16.23           C  
HETATM 2467  N   MSE B 138      -1.971  30.786  51.515  1.00 21.45           N  
HETATM 2468  CA  MSE B 138      -0.940  29.869  51.976  1.00 21.17           C  
HETATM 2469  C   MSE B 138      -1.202  28.458  51.449  1.00 21.43           C  
HETATM 2470  O   MSE B 138      -0.273  27.726  51.091  1.00 22.01           O  
HETATM 2471  CB  MSE B 138      -0.922  29.867  53.510  1.00 22.51           C  
HETATM 2472  CG  MSE B 138       0.461  29.708  54.155  1.00 26.75           C  
HETATM 2473 SE   MSE B 138       1.781  31.076  53.677  1.00 28.22          SE  
HETATM 2474  CE  MSE B 138       0.698  32.647  53.963  1.00 28.62           C  
ATOM   2475  N   ALA B 139      -2.478  28.087  51.393  1.00 20.60           N  
ATOM   2476  CA  ALA B 139      -2.879  26.759  50.935  1.00 19.45           C  
ATOM   2477  C   ALA B 139      -2.840  26.607  49.424  1.00 17.76           C  
ATOM   2478  O   ALA B 139      -2.415  25.573  48.900  1.00 17.38           O  
ATOM   2479  CB  ALA B 139      -4.275  26.434  51.450  1.00 18.66           C  
ATOM   2480  N   LEU B 140      -3.288  27.642  48.729  1.00 16.18           N  
ATOM   2481  CA  LEU B 140      -3.313  27.620  47.277  1.00 17.20           C  
ATOM   2482  C   LEU B 140      -2.075  28.256  46.671  1.00 17.08           C  
ATOM   2483  O   LEU B 140      -1.821  28.114  45.479  1.00 17.14           O  
ATOM   2484  CB  LEU B 140      -4.561  28.339  46.768  1.00 16.11           C  
ATOM   2485  CG  LEU B 140      -5.876  27.654  47.130  1.00 17.16           C  
ATOM   2486  CD1 LEU B 140      -7.029  28.552  46.741  1.00 17.21           C  
ATOM   2487  CD2 LEU B 140      -5.972  26.300  46.432  1.00 16.51           C  
ATOM   2488  N   GLY B 141      -1.305  28.952  47.500  1.00 18.14           N  
ATOM   2489  CA  GLY B 141      -0.110  29.611  47.012  1.00 16.51           C  
ATOM   2490  C   GLY B 141       1.178  28.912  47.386  1.00 16.79           C  
ATOM   2491  O   GLY B 141       1.621  27.995  46.696  1.00 16.64           O  
ATOM   2492  N   LEU B 142       1.785  29.347  48.484  1.00 15.91           N  
ATOM   2493  CA  LEU B 142       3.037  28.763  48.939  1.00 15.71           C  
ATOM   2494  C   LEU B 142       2.989  27.233  48.993  1.00 16.38           C  
ATOM   2495  O   LEU B 142       3.867  26.560  48.452  1.00 16.32           O  
ATOM   2496  CB  LEU B 142       3.392  29.299  50.323  1.00 15.69           C  
ATOM   2497  CG  LEU B 142       4.732  30.025  50.464  1.00 15.70           C  
ATOM   2498  CD1 LEU B 142       4.974  30.288  51.948  1.00 15.67           C  
ATOM   2499  CD2 LEU B 142       5.863  29.192  49.869  1.00 15.42           C  
ATOM   2500  N   GLY B 143       1.955  26.705  49.647  1.00 16.43           N  
ATOM   2501  CA  GLY B 143       1.791  25.273  49.802  1.00 15.39           C  
ATOM   2502  C   GLY B 143       2.225  24.417  48.624  1.00 14.15           C  
ATOM   2503  O   GLY B 143       3.276  23.759  48.670  1.00 12.15           O  
ATOM   2504  N   PRO B 144       1.423  24.400  47.546  1.00 14.74           N  
ATOM   2505  CA  PRO B 144       1.740  23.609  46.353  1.00 13.10           C  
ATOM   2506  C   PRO B 144       3.067  24.030  45.722  1.00 13.21           C  
ATOM   2507  O   PRO B 144       3.780  23.196  45.166  1.00 13.81           O  
ATOM   2508  CB  PRO B 144       0.533  23.849  45.452  1.00 12.28           C  
ATOM   2509  CG  PRO B 144       0.072  25.226  45.860  1.00 15.22           C  
ATOM   2510  CD  PRO B 144       0.196  25.198  47.355  1.00 14.86           C  
ATOM   2511  N   TRP B 145       3.404  25.315  45.823  1.00 12.52           N  
ATOM   2512  CA  TRP B 145       4.662  25.812  45.266  1.00 14.22           C  
ATOM   2513  C   TRP B 145       5.840  25.072  45.907  1.00 15.31           C  
ATOM   2514  O   TRP B 145       6.738  24.584  45.216  1.00 16.89           O  
ATOM   2515  CB  TRP B 145       4.821  27.319  45.519  1.00 13.87           C  
ATOM   2516  CG  TRP B 145       5.954  27.915  44.736  1.00 12.40           C  
ATOM   2517  CD1 TRP B 145       5.904  28.418  43.457  1.00 12.79           C  
ATOM   2518  CD2 TRP B 145       7.329  27.961  45.125  1.00 10.92           C  
ATOM   2519  NE1 TRP B 145       7.165  28.764  43.027  1.00 10.70           N  
ATOM   2520  CE2 TRP B 145       8.058  28.494  44.031  1.00 11.14           C  
ATOM   2521  CE3 TRP B 145       8.019  27.600  46.288  1.00 11.82           C  
ATOM   2522  CZ2 TRP B 145       9.445  28.671  44.069  1.00 12.67           C  
ATOM   2523  CZ3 TRP B 145       9.403  27.777  46.328  1.00 13.02           C  
ATOM   2524  CH2 TRP B 145      10.101  28.309  45.219  1.00 12.57           C  
ATOM   2525  N   LEU B 146       5.824  25.004  47.236  1.00 15.11           N  
ATOM   2526  CA  LEU B 146       6.870  24.340  48.012  1.00 14.87           C  
ATOM   2527  C   LEU B 146       6.928  22.835  47.749  1.00 14.66           C  
ATOM   2528  O   LEU B 146       8.005  22.269  47.529  1.00 14.95           O  
ATOM   2529  CB  LEU B 146       6.638  24.578  49.509  1.00 13.87           C  
ATOM   2530  CG  LEU B 146       6.899  25.975  50.076  1.00 15.52           C  
ATOM   2531  CD1 LEU B 146       6.353  26.072  51.498  1.00 12.75           C  
ATOM   2532  CD2 LEU B 146       8.396  26.247  50.059  1.00 14.95           C  
ATOM   2533  N   ALA B 147       5.762  22.194  47.791  1.00 14.33           N  
ATOM   2534  CA  ALA B 147       5.647  20.755  47.570  1.00 12.73           C  
ATOM   2535  C   ALA B 147       6.353  20.345  46.288  1.00 13.16           C  
ATOM   2536  O   ALA B 147       6.943  19.265  46.198  1.00 12.18           O  
ATOM   2537  CB  ALA B 147       4.177  20.359  47.498  1.00 11.67           C  
ATOM   2538  N   VAL B 148       6.294  21.235  45.304  1.00 14.98           N  
ATOM   2539  CA  VAL B 148       6.889  20.992  44.003  1.00 16.00           C  
ATOM   2540  C   VAL B 148       8.347  21.376  43.875  1.00 17.59           C  
ATOM   2541  O   VAL B 148       9.203  20.535  43.586  1.00 19.56           O  
ATOM   2542  CB  VAL B 148       6.124  21.740  42.915  1.00 17.52           C  
ATOM   2543  CG1 VAL B 148       6.826  21.557  41.575  1.00 19.20           C  
ATOM   2544  CG2 VAL B 148       4.704  21.224  42.858  1.00 17.95           C  
ATOM   2545  N   GLU B 149       8.619  22.659  44.077  1.00 18.38           N  
ATOM   2546  CA  GLU B 149       9.970  23.196  43.962  1.00 18.11           C  
ATOM   2547  C   GLU B 149      10.980  22.625  44.959  1.00 17.57           C  
ATOM   2548  O   GLU B 149      12.093  22.264  44.577  1.00 17.14           O  
ATOM   2549  CB  GLU B 149       9.925  24.721  44.104  1.00 19.03           C  
ATOM   2550  CG  GLU B 149       9.033  25.411  43.092  1.00 21.53           C  
ATOM   2551  CD  GLU B 149       9.429  25.096  41.664  1.00 22.91           C  
ATOM   2552  OE1 GLU B 149      10.634  25.230  41.346  1.00 22.41           O  
ATOM   2553  OE2 GLU B 149       8.541  24.723  40.863  1.00 22.44           O  
ATOM   2554  N   ILE B 150      10.588  22.535  46.228  1.00 15.92           N  
ATOM   2555  CA  ILE B 150      11.494  22.051  47.261  1.00 15.40           C  
ATOM   2556  C   ILE B 150      12.155  20.703  46.969  1.00 14.27           C  
ATOM   2557  O   ILE B 150      13.385  20.599  46.959  1.00 12.16           O  
ATOM   2558  CB  ILE B 150      10.798  21.996  48.645  1.00 14.62           C  
ATOM   2559  CG1 ILE B 150      10.208  23.369  48.995  1.00 15.05           C  
ATOM   2560  CG2 ILE B 150      11.812  21.606  49.720  1.00 12.11           C  
ATOM   2561  CD1 ILE B 150      11.250  24.484  49.129  1.00 12.05           C  
ATOM   2562  N   PRO B 151      11.356  19.649  46.734  1.00 14.22           N  
ATOM   2563  CA  PRO B 151      11.974  18.348  46.452  1.00 13.98           C  
ATOM   2564  C   PRO B 151      12.785  18.364  45.150  1.00 12.91           C  
ATOM   2565  O   PRO B 151      13.746  17.615  44.999  1.00 13.46           O  
ATOM   2566  CB  PRO B 151      10.775  17.404  46.395  1.00 13.77           C  
ATOM   2567  CG  PRO B 151       9.662  18.294  45.914  1.00 13.85           C  
ATOM   2568  CD  PRO B 151       9.887  19.550  46.720  1.00 12.54           C  
ATOM   2569  N   ASP B 152      12.414  19.232  44.217  1.00 11.13           N  
ATOM   2570  CA  ASP B 152      13.139  19.309  42.958  1.00 12.13           C  
ATOM   2571  C   ASP B 152      14.530  19.952  43.137  1.00 12.54           C  
ATOM   2572  O   ASP B 152      15.529  19.456  42.608  1.00 12.16           O  
ATOM   2573  CB  ASP B 152      12.298  20.077  41.927  1.00 11.96           C  
ATOM   2574  CG  ASP B 152      12.950  20.129  40.550  1.00 11.66           C  
ATOM   2575  OD1 ASP B 152      13.131  19.061  39.916  1.00 13.64           O  
ATOM   2576  OD2 ASP B 152      13.274  21.249  40.102  1.00  9.08           O  
ATOM   2577  N   LEU B 153      14.583  21.049  43.890  1.00 13.15           N  
ATOM   2578  CA  LEU B 153      15.831  21.775  44.168  1.00 12.75           C  
ATOM   2579  C   LEU B 153      16.785  20.915  44.997  1.00 14.35           C  
ATOM   2580  O   LEU B 153      18.004  20.976  44.833  1.00 15.12           O  
ATOM   2581  CB  LEU B 153      15.517  23.077  44.925  1.00 13.08           C  
ATOM   2582  CG  LEU B 153      14.598  24.069  44.189  1.00 14.78           C  
ATOM   2583  CD1 LEU B 153      14.051  25.165  45.115  1.00 10.11           C  
ATOM   2584  CD2 LEU B 153      15.391  24.665  43.047  1.00 14.78           C  
ATOM   2585  N   ILE B 154      16.218  20.114  45.893  1.00 14.93           N  
ATOM   2586  CA  ILE B 154      17.018  19.243  46.740  1.00 15.55           C  
ATOM   2587  C   ILE B 154      17.654  18.112  45.933  1.00 17.24           C  
ATOM   2588  O   ILE B 154      18.811  17.770  46.161  1.00 16.07           O  
ATOM   2589  CB  ILE B 154      16.175  18.626  47.885  1.00 14.42           C  
ATOM   2590  CG1 ILE B 154      15.649  19.724  48.806  1.00 12.49           C  
ATOM   2591  CG2 ILE B 154      17.027  17.656  48.694  1.00 13.03           C  
ATOM   2592  CD1 ILE B 154      14.793  19.198  49.933  1.00  8.59           C  
ATOM   2593  N   GLN B 155      16.908  17.536  44.990  1.00 18.83           N  
ATOM   2594  CA  GLN B 155      17.444  16.443  44.183  1.00 19.59           C  
ATOM   2595  C   GLN B 155      18.435  16.920  43.129  1.00 20.94           C  
ATOM   2596  O   GLN B 155      19.265  16.143  42.655  1.00 22.74           O  
ATOM   2597  CB  GLN B 155      16.321  15.659  43.500  1.00 19.21           C  
ATOM   2598  CG  GLN B 155      15.751  16.292  42.241  1.00 17.94           C  
ATOM   2599  CD  GLN B 155      14.708  15.397  41.578  1.00 15.84           C  
ATOM   2600  OE1 GLN B 155      14.145  15.739  40.536  1.00 15.90           O  
ATOM   2601  NE2 GLN B 155      14.450  14.241  42.184  1.00 15.35           N  
ATOM   2602  N   LYS B 156      18.351  18.196  42.771  1.00 22.42           N  
ATOM   2603  CA  LYS B 156      19.245  18.775  41.771  1.00 23.77           C  
ATOM   2604  C   LYS B 156      20.497  19.375  42.398  1.00 24.99           C  
ATOM   2605  O   LYS B 156      21.388  19.843  41.688  1.00 25.67           O  
ATOM   2606  CB  LYS B 156      18.503  19.845  40.962  1.00 22.43           C  
ATOM   2607  CG  LYS B 156      17.357  19.273  40.137  1.00 21.45           C  
ATOM   2608  CD  LYS B 156      16.683  20.310  39.269  1.00 20.25           C  
ATOM   2609  CE  LYS B 156      15.604  19.655  38.435  1.00 21.65           C  
ATOM   2610  NZ  LYS B 156      14.953  20.607  37.510  1.00 23.21           N  
ATOM   2611  N   GLY B 157      20.551  19.360  43.729  1.00 25.51           N  
ATOM   2612  CA  GLY B 157      21.692  19.897  44.450  1.00 24.87           C  
ATOM   2613  C   GLY B 157      21.668  21.408  44.582  1.00 26.78           C  
ATOM   2614  O   GLY B 157      22.709  22.023  44.807  1.00 26.36           O  
ATOM   2615  N   VAL B 158      20.485  22.006  44.438  1.00 29.03           N  
ATOM   2616  CA  VAL B 158      20.325  23.460  44.538  1.00 31.80           C  
ATOM   2617  C   VAL B 158      20.338  23.907  45.992  1.00 34.17           C  
ATOM   2618  O   VAL B 158      21.028  24.862  46.359  1.00 33.36           O  
ATOM   2619  CB  VAL B 158      18.993  23.940  43.921  1.00 31.13           C  
ATOM   2620  CG1 VAL B 158      18.895  25.460  44.017  1.00 30.24           C  
ATOM   2621  CG2 VAL B 158      18.886  23.489  42.479  1.00 29.43           C  
ATOM   2622  N   ILE B 159      19.550  23.225  46.814  1.00 36.03           N  
ATOM   2623  CA  ILE B 159      19.484  23.546  48.227  1.00 39.94           C  
ATOM   2624  C   ILE B 159      19.979  22.312  48.974  1.00 42.73           C  
ATOM   2625  O   ILE B 159      19.931  21.198  48.450  1.00 42.36           O  
ATOM   2626  CB  ILE B 159      18.026  23.917  48.655  1.00 40.27           C  
ATOM   2627  CG1 ILE B 159      18.042  24.666  49.995  1.00 42.48           C  
ATOM   2628  CG2 ILE B 159      17.164  22.672  48.772  1.00 40.25           C  
ATOM   2629  CD1 ILE B 159      18.679  26.067  49.935  1.00 41.71           C  
ATOM   2630  N   GLN B 160      20.485  22.506  50.183  1.00 46.30           N  
ATOM   2631  CA  GLN B 160      20.993  21.384  50.953  1.00 50.08           C  
ATOM   2632  C   GLN B 160      21.136  21.745  52.419  1.00 52.83           C  
ATOM   2633  O   GLN B 160      22.146  21.430  53.049  1.00 54.70           O  
ATOM   2634  CB  GLN B 160      22.344  20.935  50.382  1.00 50.65           C  
ATOM   2635  CG  GLN B 160      23.397  22.033  50.315  1.00 51.87           C  
ATOM   2636  CD  GLN B 160      24.661  21.591  49.596  1.00 52.15           C  
ATOM   2637  OE1 GLN B 160      25.617  22.357  49.472  1.00 52.49           O  
ATOM   2638  NE2 GLN B 160      24.669  20.351  49.117  1.00 52.23           N  
ATOM   2639  N   HIS B 161      20.116  22.406  52.960  1.00 55.54           N  
ATOM   2640  CA  HIS B 161      20.135  22.808  54.362  1.00 57.73           C  
ATOM   2641  C   HIS B 161      20.260  21.558  55.220  1.00 57.26           C  
ATOM   2642  O   HIS B 161      21.101  21.490  56.117  1.00 57.53           O  
ATOM   2643  CB  HIS B 161      18.849  23.559  54.725  1.00 60.01           C  
ATOM   2644  CG  HIS B 161      18.970  24.392  55.963  1.00 62.42           C  
ATOM   2645  ND1 HIS B 161      17.942  25.178  56.438  1.00 63.44           N  
ATOM   2646  CD2 HIS B 161      20.008  24.576  56.813  1.00 62.16           C  
ATOM   2647  CE1 HIS B 161      18.342  25.811  57.526  1.00 62.65           C  
ATOM   2648  NE2 HIS B 161      19.592  25.464  57.775  1.00 62.68           N  
ATOM   2649  N   LYS B 162      19.410  20.577  54.927  1.00 57.17           N  
ATOM   2650  CA  LYS B 162      19.396  19.297  55.625  1.00 57.45           C  
ATOM   2651  C   LYS B 162      19.597  19.476  57.129  1.00 57.23           C  
ATOM   2652  O   LYS B 162      20.364  18.743  57.759  1.00 56.74           O  
ATOM   2653  CB  LYS B 162      20.493  18.393  55.044  1.00 57.62           C  
ATOM   2654  CG  LYS B 162      20.968  18.820  53.649  1.00 57.08           C  
ATOM   2655  CD  LYS B 162      21.865  17.782  52.985  1.00 57.09           C  
ATOM   2656  CE  LYS B 162      21.051  16.622  52.426  1.00 56.45           C  
ATOM   2657  NZ  LYS B 162      20.165  17.055  51.299  1.00 55.61           N  
ATOM   2658  N   GLU B 163      18.896  20.454  57.697  1.00 56.74           N  
ATOM   2659  CA  GLU B 163      19.004  20.757  59.121  1.00 57.54           C  
ATOM   2660  C   GLU B 163      20.470  21.048  59.470  1.00 58.14           C  
ATOM   2661  O   GLU B 163      21.056  20.411  60.350  1.00 58.67           O  
ATOM   2662  CB  GLU B 163      18.474  19.584  59.960  1.00 56.61           C  
ATOM   2663  CG  GLU B 163      17.011  19.235  59.684  1.00 54.11           C  
ATOM   2664  CD  GLU B 163      16.477  18.139  60.589  1.00 51.36           C  
ATOM   2665  OE1 GLU B 163      17.065  17.042  60.601  1.00 51.07           O  
ATOM   2666  OE2 GLU B 163      15.468  18.373  61.280  1.00 49.65           O  
ATOM   2667  N   LYS B 164      21.055  22.015  58.765  1.00 58.29           N  
ATOM   2668  CA  LYS B 164      22.451  22.393  58.982  1.00 59.04           C  
ATOM   2669  C   LYS B 164      22.653  23.189  60.269  1.00 58.88           C  
ATOM   2670  O   LYS B 164      23.516  22.783  61.073  1.00 58.57           O  
ATOM   2671  CB  LYS B 164      22.983  23.214  57.800  1.00 59.91           C  
ATOM   2672  CG  LYS B 164      24.468  23.556  57.923  1.00 60.22           C  
ATOM   2673  CD  LYS B 164      24.944  24.535  56.852  1.00 61.25           C  
ATOM   2674  CE  LYS B 164      24.801  23.983  55.442  1.00 61.68           C  
ATOM   2675  NZ  LYS B 164      25.291  24.981  54.445  1.00 61.47           N  
TER    2676      LYS B 164                                                      
HETATM 2677  O   HOH A 176      23.531  12.496  43.394  1.00 37.97           O  
HETATM 2678  O   HOH A 177      11.695  16.503  18.298  1.00 16.52           O  
HETATM 2679  O   HOH A 178      23.329  33.966  23.534  1.00 22.09           O  
HETATM 2680  O   HOH A 179      14.633  26.433  33.513  1.00 19.57           O  
HETATM 2681  O   HOH A 180      16.670  39.496   4.325  1.00 34.29           O  
HETATM 2682  O   HOH A 181       6.198  21.648  18.473  1.00 22.92           O  
HETATM 2683  O   HOH A 182      41.228  27.934  16.948  1.00 22.76           O  
HETATM 2684  O   HOH A 183      28.658  22.961  37.602  1.00 61.77           O  
HETATM 2685  O   HOH A 184      26.648   5.222  44.751  1.00  5.00           O  
HETATM 2686  O   HOH A 185      31.358  25.344   5.228  1.00 58.76           O  
HETATM 2687  O   HOH A 186      22.341  34.363  26.593  1.00 12.02           O  
HETATM 2688  O   HOH A 187      14.099  42.275  16.780  1.00 29.68           O  
HETATM 2689  O   HOH A 188      11.570  36.883  33.214  1.00 20.70           O  
HETATM 2690  O   HOH A 189      14.524  17.396  34.364  1.00  7.78           O  
HETATM 2691  O   HOH A 190       6.588  22.761  25.481  1.00  7.90           O  
HETATM 2692  O   HOH A 191      14.843  35.736  22.499  1.00  4.15           O  
HETATM 2693  O   HOH A 192      14.432  41.191  21.217  1.00  7.00           O  
HETATM 2694  O   HOH A 193      15.921  33.186   7.446  1.00  8.16           O  
HETATM 2695  O   HOH A 194      15.657  31.543   5.539  1.00 17.11           O  
HETATM 2696  O   HOH A 195      23.368  33.192  12.961  1.00 23.94           O  
HETATM 2697  O   HOH A 196      25.694  29.025  15.655  1.00 21.41           O  
HETATM 2698  O   HOH A 197      17.938  38.644  11.559  1.00 21.62           O  
HETATM 2699  O   HOH A 198      16.175  40.698  11.564  1.00 14.28           O  
HETATM 2700  O   HOH A 199       5.033  38.336  10.472  1.00 20.93           O  
HETATM 2701  O   HOH A 200      12.141  37.829  37.241  1.00  8.05           O  
HETATM 2702  O   HOH A 201      21.262   3.294  31.758  1.00 11.41           O  
HETATM 2703  O   HOH A 202      33.117  30.791  34.472  1.00 40.81           O  
HETATM 2704  O   HOH A 203      16.578  32.835  29.638  1.00 22.28           O  
HETATM 2705  O   HOH A 204       4.807  28.204  21.328  1.00 29.50           O  
HETATM 2706  O   HOH A 205       7.977  24.540  18.241  1.00 34.19           O  
HETATM 2707  O   HOH A 206       9.335  15.609  17.544  1.00 27.65           O  
HETATM 2708  O   HOH A 207      18.238  12.220  18.935  1.00 28.60           O  
HETATM 2709  O   HOH A 208      20.318  14.935  19.649  1.00  6.20           O  
HETATM 2710  O   HOH A 209      30.256   9.109  25.339  1.00 45.11           O  
HETATM 2711  O   HOH A 210      13.667  23.603   7.451  1.00 23.62           O  
HETATM 2712  O   HOH A 211      33.080  31.095  23.886  1.00 16.43           O  
HETATM 2713  O   HOH A 212      33.203  16.920  19.725  1.00 35.80           O  
HETATM 2714  O   HOH A 213      18.049  40.287   8.529  1.00 44.88           O  
HETATM 2715  O   HOH A 214      24.164  16.911  46.702  1.00 15.69           O  
HETATM 2716  O   HOH A 215      18.291  36.867  23.563  1.00 54.58           O  
HETATM 2717  O   HOH A 216      29.451  34.630  14.534  1.00 11.56           O  
HETATM 2718  O   HOH A 217      36.643  31.051  26.940  1.00 42.31           O  
HETATM 2719  O   HOH A 218      34.229  12.506  38.932  1.00 14.68           O  
HETATM 2720  O   HOH A 219       3.241  39.883  26.624  1.00 13.04           O  
HETATM 2721  O   HOH A 220      22.191  26.611  40.970  1.00 11.76           O  
HETATM 2722  O   HOH A 221      17.308   5.796  30.521  1.00  8.08           O  
HETATM 2723  O   HOH A 222      15.648   3.994  30.760  1.00 17.26           O  
HETATM 2724  O   HOH A 223      16.141   6.875  27.413  1.00 28.31           O  
HETATM 2725  O   HOH A 224      25.979  20.922  15.731  1.00 18.32           O  
HETATM 2726  O   HOH A 225      23.050  29.530  13.968  1.00  7.11           O  
HETATM 2727  O   HOH B 176      21.622   8.078  54.662  1.00 21.86           O  
HETATM 2728  O   HOH B 177      12.236  26.634  63.696  1.00  6.00           O  
HETATM 2729  O   HOH B 178      -2.489  22.658  53.126  1.00 14.54           O  
HETATM 2730  O   HOH B 179       9.351  14.833  49.121  1.00 16.94           O  
HETATM 2731  O   HOH B 180       9.017  22.706  35.381  1.00 23.60           O  
HETATM 2732  O   HOH B 181      12.942  11.958  40.227  1.00  8.31           O  
HETATM 2733  O   HOH B 182      -5.519  49.409  62.435  1.00 17.94           O  
HETATM 2734  O   HOH B 183       5.020  34.402  67.652  1.00 14.89           O  
HETATM 2735  O   HOH B 184     -15.107  25.978  46.114  1.00 22.53           O  
HETATM 2736  O   HOH B 185     -14.567  26.296  58.952  1.00 14.90           O  
HETATM 2737  O   HOH B 186      16.541  23.271  58.776  1.00 32.15           O  
HETATM 2738  O   HOH B 187       0.296  39.047  63.970  1.00 40.32           O  
HETATM 2739  O   HOH B 188       0.284  48.115  52.986  1.00 39.19           O  
HETATM 2740  O   HOH B 189      -0.292  51.239  59.188  1.00 30.12           O  
HETATM 2741  O   HOH B 190      10.285  40.874  51.302  1.00 20.51           O  
HETATM 2742  O   HOH B 191      11.292  15.414  39.967  1.00 27.38           O  
HETATM 2743  O   HOH B 192       0.750  30.623  63.021  1.00  3.56           O  
HETATM 2744  O   HOH B 193     -12.949  33.963  59.569  1.00 25.44           O  
HETATM 2745  O   HOH B 194     -17.338  38.003  63.062  1.00 10.94           O  
HETATM 2746  O   HOH B 195       2.736  42.094  48.442  1.00  2.62           O  
HETATM 2747  O   HOH B 196      -2.200  23.374  50.695  1.00 32.39           O  
HETATM 2748  O   HOH B 197       7.195  25.940  66.026  1.00  8.00           O  
HETATM 2749  O   HOH B 198       6.798  15.939  52.798  1.00  3.00           O  
HETATM 2750  O   HOH B 199       4.916  17.426  48.110  1.00 21.08           O  
HETATM 2751  O   HOH B 200       5.718  21.530  53.478  1.00  4.73           O  
HETATM 2752  O   HOH B 201       8.540  11.917  54.921  1.00  3.00           O  
HETATM 2753  O   HOH B 202      13.955  32.491  53.263  1.00 23.29           O  
HETATM 2754  O   HOH B 203      15.758  35.161  54.269  1.00 31.16           O  
HETATM 2755  O   HOH B 204       0.302  37.064  43.224  1.00 10.33           O  
HETATM 2756  O   HOH B 205      21.301  28.299  42.536  1.00 14.74           O  
HETATM 2757  O   HOH B 206      12.092  23.675  39.918  1.00 15.23           O  
HETATM 2758  O   HOH B 207       3.583  26.269  33.594  1.00 22.34           O  
HETATM 2759  O   HOH B 208       2.817  24.129  41.700  1.00 38.89           O  
HETATM 2760  O   HOH B 209       2.738  27.540  41.048  1.00 22.60           O  
HETATM 2761  O   HOH B 210       5.654  25.118  40.667  1.00 11.09           O  
HETATM 2762  O   HOH B 211       9.147  21.976  38.437  1.00 30.13           O  
HETATM 2763  O   HOH B 212       7.604  19.524  38.536  1.00  3.13           O  
HETATM 2764  O   HOH B 213       9.211  18.251  42.407  1.00 25.61           O  
HETATM 2765  O   HOH B 214      20.641  14.128  45.424  1.00  7.87           O  
HETATM 2766  O   HOH B 215      19.637  14.959  47.578  1.00 30.44           O  
HETATM 2767  O   HOH B 216      20.590  18.434  48.138  1.00 16.76           O  
HETATM 2768  O   HOH B 217       8.727  25.137  32.943  1.00  4.00           O  
HETATM 2769  O   HOH B 218       8.782  20.796  33.484  1.00 25.46           O  
HETATM 2770  O   HOH B 219     -15.982  27.461  60.731  1.00 24.33           O  
HETATM 2771  O   HOH B 220     -17.597  31.562  58.585  1.00 12.86           O  
HETATM 2772  O   HOH B 221     -17.947  42.859  53.434  1.00 26.85           O  
HETATM 2773  O   HOH B 222      -8.554  51.470  48.957  1.00 14.75           O  
HETATM 2774  O   HOH B 223      -4.001  50.609  60.433  1.00 48.77           O  
HETATM 2775  O   HOH B 224       1.068  24.259  59.070  1.00  7.40           O  
HETATM 2776  O   HOH B 225       0.946  19.563  67.687  1.00  2.21           O  
HETATM 2777  O   HOH B 226       2.069  52.154  68.839  1.00 32.47           O  
HETATM 2778  O   HOH B 227       4.710  44.474  48.781  1.00 29.41           O  
HETATM 2779  O   HOH B 228      11.217  40.538  48.621  1.00 16.45           O  
HETATM 2780  O   HOH B 229       6.062  33.190  62.498  1.00  4.74           O  
HETATM 2781  O   HOH B 230      18.633   9.483  54.270  1.00 17.14           O  
HETATM 2782  O   HOH B 231      19.518   9.400  51.776  1.00 23.45           O  
HETATM 2783  O   HOH B 232       2.563  24.948  39.260  1.00 28.62           O  
HETATM 2784  O   HOH B 233      -0.534  35.408  41.126  1.00  8.39           O  
HETATM 2785  O   HOH B 234     -13.371  20.600  41.859  1.00 44.62           O  
HETATM 2786  O   HOH B 235     -15.541  36.272  63.571  1.00 42.23           O  
HETATM 2787  O   HOH B 236     -15.578  34.481  61.226  1.00 12.45           O  
HETATM 2788  O   HOH B 237       6.350  23.697  37.853  1.00 17.40           O  
HETATM 2789  O   HOH B 238       6.023  23.672  34.224  1.00 18.37           O  
HETATM 2790  O   HOH B 239       2.066  35.257  70.099  1.00 52.16           O  
HETATM 2791  O   HOH B 240     -10.392  25.972  45.746  1.00 36.07           O  
HETATM 2792  O   HOH B 241     -18.438  33.073  56.669  1.00 22.77           O  
HETATM 2793  O   HOH B 242      13.452  17.494  36.924  1.00  6.55           O  
HETATM 2794  O   HOH B 243     -20.336  30.677  51.590  1.00 29.53           O  
HETATM 2795  O   HOH B 244      -7.252  49.918  51.807  1.00 35.23           O  
HETATM 2796  O   HOH B 245      -6.427  20.743  67.223  1.00 27.02           O  
HETATM 2797  O   HOH B 246      -3.226  11.281  59.444  1.00 52.11           O  
HETATM 2798  O   HOH B 247       7.469  20.088  61.244  1.00  3.97           O  
HETATM 2799  O   HOH B 248       3.225  42.322  66.029  1.00 16.27           O  
HETATM 2800  O   HOH B 249       2.205  50.954  57.165  1.00 48.60           O  
HETATM 2801  O   HOH B 250      13.001  41.602  52.038  1.00 18.29           O  
HETATM 2802  O   HOH B 251      -9.159  26.847  39.057  1.00 21.14           O  
HETATM 2803  O   HOH B 252       1.099  20.732  44.426  1.00 10.57           O  
HETATM 2804  O   HOH B 253      22.009  28.469  56.214  1.00 34.42           O  
CONECT  885  892                                                                
CONECT  892  885  893                                                           
CONECT  893  892  894  896                                                      
CONECT  894  893  895  900                                                      
CONECT  895  894                                                                
CONECT  896  893  897                                                           
CONECT  897  896  898                                                           
CONECT  898  897  899                                                           
CONECT  899  898                                                                
CONECT  900  894                                                                
CONECT 1123 1129                                                                
CONECT 1129 1123 1130                                                           
CONECT 1130 1129 1131 1133                                                      
CONECT 1131 1130 1132 1137                                                      
CONECT 1132 1131                                                                
CONECT 1133 1130 1134                                                           
CONECT 1134 1133 1135                                                           
CONECT 1135 1134 1136                                                           
CONECT 1136 1135                                                                
CONECT 1137 1131                                                                
CONECT 2223 2230                                                                
CONECT 2230 2223 2231                                                           
CONECT 2231 2230 2232 2234                                                      
CONECT 2232 2231 2233 2238                                                      
CONECT 2233 2232                                                                
CONECT 2234 2231 2235                                                           
CONECT 2235 2234 2236                                                           
CONECT 2236 2235 2237                                                           
CONECT 2237 2236                                                                
CONECT 2238 2232                                                                
CONECT 2461 2467                                                                
CONECT 2467 2461 2468                                                           
CONECT 2468 2467 2469 2471                                                      
CONECT 2469 2468 2470 2475                                                      
CONECT 2470 2469                                                                
CONECT 2471 2468 2472                                                           
CONECT 2472 2471 2473                                                           
CONECT 2473 2472 2474                                                           
CONECT 2474 2473                                                                
CONECT 2475 2469                                                                
MASTER      287    0    4   14    6    0    0    6 2802    2   40   28          
END                                                                             
