CNRS Nantes University UFIP UFIP
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***  GCCflexi  ***

elNémo ID: 22020715384768006

Job options:

ID        	=	 22020715384768006
JOBID     	=	 GCCflexi
USERID    	=	 callun.bain.uk
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER GCCflexi

HEADER    LIGASE                                  17-MAR-20   6YBQ              
TITLE     ENGINEERED GLYCOLYL-COA CARBOXYLASE (QUINTUPLE MUTANT) WITH BOUND COA 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROPIONYL-COA CARBOXYLASE BETA CHAIN;                      
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 EC: 6.4.1.3;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PROPIONYL-COA CARBOXYLASE ALPHA SUBUNIT;                   
COMPND   9 CHAIN: G, H, I, J, K, L;                                             
COMPND  10 EC: 6.4.1.3;                                                         
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: METHYLORUBRUM EXTORQUENS (STRAIN ATCC 14718 /   
SOURCE   3 DSM 1338 / JCM 2805 / NCIMB 9133 / AM1);                             
SOURCE   4 ORGANISM_TAXID: 272630;                                              
SOURCE   5 GENE: PCCB, MEXAM1_META1P0172;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: METHYLORUBRUM EXTORQUENS (STRAIN ATCC 14718 /   
SOURCE  10 DSM 1338 / JCM 2805 / NCIMB 9133 / AM1);                             
SOURCE  11 ORGANISM_TAXID: 272630;                                              
SOURCE  12 GENE: PCCA, MEXAM1_META1P3203;                                       
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    BIOTIN DEPENDENT, ATP DEPENDENT, GLYCOLYL-COA, HETERODODECAMER,       
KEYWDS   2 ENZYME ENGINEERING, CO2 FIXATION, LIGASE                             
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    J.M.SCHULLER,S.K.SCHULLER,J.ZARZYCKI,M.SCHEFFEN,D.M.MARCHAL,T.J.ERB   
REVDAT   2   12-MAY-21 6YBQ    1       JRNL                                     
REVDAT   1   28-OCT-20 6YBQ    0                                                
JRNL        AUTH   M.SCHEFFEN,D.G.MARCHAL,T.BENEYTON,S.K.SCHULLER,M.KLOSE,      
JRNL        AUTH 2 C.DIEHL,J.LEHMANN,P.PFISTER,M.CARRILLO,H.HE,S.ASLAN,         
JRNL        AUTH 3 N.S.CORTINA,P.CLAUS,D.BOLLSCHWEILER,J.C.BARET,J.M.SCHULLER,  
JRNL        AUTH 4 J.ZARZYCKI,A.BAR-EVEN,T.J.ERB                                
JRNL        TITL   A NEW-TO-NATURE CARBOXYLATION MODULE TO IMPROVE NATURAL AND  
JRNL        TITL 2 SYNTHETIC CO2 FIXATION                                       
JRNL        REF    NAT CATAL                                  2021              
JRNL        REFN                   ESSN 2520-1158                               
JRNL        DOI    10.1038/S41929-020-00557-Y                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.96 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : UCSF CHIMERA, PHENIX                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 3N6R                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : RIGID BODY FIT                      
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 1.960                          
REMARK   3   NUMBER OF PARTICLES               : 218131                         
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 6YBQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-MAR-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292107087.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : ENGINEERED GLYCOLYL-COA           
REMARK 245                                    CARBOXYLASE WITH BOUND COA        
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.80                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K3 BIOQUANTUM (6K X      
REMARK 245                                       4K)                            
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 5500.00                        
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     MET C     1                                                      
REMARK 465     LYS C     2                                                      
REMARK 465     ASP C     3                                                      
REMARK 465     ILE C     4                                                      
REMARK 465     MET D     1                                                      
REMARK 465     LYS D     2                                                      
REMARK 465     ASP D     3                                                      
REMARK 465     ILE D     4                                                      
REMARK 465     MET E     1                                                      
REMARK 465     LYS E     2                                                      
REMARK 465     ASP E     3                                                      
REMARK 465     ILE E     4                                                      
REMARK 465     MET F     1                                                      
REMARK 465     LYS F     2                                                      
REMARK 465     ASP F     3                                                      
REMARK 465     ILE F     4                                                      
REMARK 465     MET G     1                                                      
REMARK 465     PHE G     2                                                      
REMARK 465     ASP G     3                                                      
REMARK 465     LYS G     4                                                      
REMARK 465     ILE G     5                                                      
REMARK 465     LEU G     6                                                      
REMARK 465     ILE G     7                                                      
REMARK 465     ALA G     8                                                      
REMARK 465     ASN G     9                                                      
REMARK 465     ARG G    10                                                      
REMARK 465     GLY G    11                                                      
REMARK 465     GLU G    12                                                      
REMARK 465     ILE G    13                                                      
REMARK 465     ALA G    14                                                      
REMARK 465     CYS G    15                                                      
REMARK 465     ARG G    16                                                      
REMARK 465     ILE G    17                                                      
REMARK 465     ILE G    18                                                      
REMARK 465     LYS G    19                                                      
REMARK 465     THR G    20                                                      
REMARK 465     ALA G    21                                                      
REMARK 465     GLN G    22                                                      
REMARK 465     LYS G    23                                                      
REMARK 465     MET G    24                                                      
REMARK 465     GLY G    25                                                      
REMARK 465     ILE G    26                                                      
REMARK 465     LYS G    27                                                      
REMARK 465     THR G    28                                                      
REMARK 465     VAL G    29                                                      
REMARK 465     ALA G    30                                                      
REMARK 465     VAL G    31                                                      
REMARK 465     TYR G    32                                                      
REMARK 465     SER G    33                                                      
REMARK 465     ASP G    34                                                      
REMARK 465     ALA G    35                                                      
REMARK 465     ASP G    36                                                      
REMARK 465     ARG G    37                                                      
REMARK 465     ASP G    38                                                      
REMARK 465     ALA G    39                                                      
REMARK 465     VAL G    40                                                      
REMARK 465     HIS G    41                                                      
REMARK 465     VAL G    42                                                      
REMARK 465     ALA G    43                                                      
REMARK 465     MET G    44                                                      
REMARK 465     ALA G    45                                                      
REMARK 465     ASP G    46                                                      
REMARK 465     GLU G    47                                                      
REMARK 465     ALA G    48                                                      
REMARK 465     VAL G    49                                                      
REMARK 465     HIS G    50                                                      
REMARK 465     ILE G    51                                                      
REMARK 465     GLY G    52                                                      
REMARK 465     PRO G    53                                                      
REMARK 465     ALA G    54                                                      
REMARK 465     PRO G    55                                                      
REMARK 465     ALA G    56                                                      
REMARK 465     ALA G    57                                                      
REMARK 465     GLN G    58                                                      
REMARK 465     SER G    59                                                      
REMARK 465     TYR G    60                                                      
REMARK 465     LEU G    61                                                      
REMARK 465     LEU G    62                                                      
REMARK 465     ILE G    63                                                      
REMARK 465     GLU G    64                                                      
REMARK 465     LYS G    65                                                      
REMARK 465     ILE G    66                                                      
REMARK 465     ILE G    67                                                      
REMARK 465     ASP G    68                                                      
REMARK 465     ALA G    69                                                      
REMARK 465     CYS G    70                                                      
REMARK 465     LYS G    71                                                      
REMARK 465     GLN G    72                                                      
REMARK 465     THR G    73                                                      
REMARK 465     GLY G    74                                                      
REMARK 465     ALA G    75                                                      
REMARK 465     GLN G    76                                                      
REMARK 465     ALA G    77                                                      
REMARK 465     VAL G    78                                                      
REMARK 465     HIS G    79                                                      
REMARK 465     PRO G    80                                                      
REMARK 465     GLY G    81                                                      
REMARK 465     TYR G    82                                                      
REMARK 465     GLY G    83                                                      
REMARK 465     PHE G    84                                                      
REMARK 465     LEU G    85                                                      
REMARK 465     SER G    86                                                      
REMARK 465     GLU G    87                                                      
REMARK 465     ARG G    88                                                      
REMARK 465     GLU G    89                                                      
REMARK 465     SER G    90                                                      
REMARK 465     PHE G    91                                                      
REMARK 465     PRO G    92                                                      
REMARK 465     LYS G    93                                                      
REMARK 465     ALA G    94                                                      
REMARK 465     LEU G    95                                                      
REMARK 465     ALA G    96                                                      
REMARK 465     GLU G    97                                                      
REMARK 465     ALA G    98                                                      
REMARK 465     GLY G    99                                                      
REMARK 465     ILE G   100                                                      
REMARK 465     VAL G   101                                                      
REMARK 465     PHE G   102                                                      
REMARK 465     ILE G   103                                                      
REMARK 465     GLY G   104                                                      
REMARK 465     PRO G   105                                                      
REMARK 465     ASN G   106                                                      
REMARK 465     PRO G   107                                                      
REMARK 465     GLY G   108                                                      
REMARK 465     ALA G   109                                                      
REMARK 465     ILE G   110                                                      
REMARK 465     ALA G   111                                                      
REMARK 465     ALA G   112                                                      
REMARK 465     MET G   113                                                      
REMARK 465     GLY G   114                                                      
REMARK 465     ASP G   115                                                      
REMARK 465     LYS G   116                                                      
REMARK 465     ILE G   117                                                      
REMARK 465     GLU G   118                                                      
REMARK 465     SER G   119                                                      
REMARK 465     LYS G   120                                                      
REMARK 465     LYS G   121                                                      
REMARK 465     ALA G   122                                                      
REMARK 465     ALA G   123                                                      
REMARK 465     ALA G   124                                                      
REMARK 465     ALA G   125                                                      
REMARK 465     ALA G   126                                                      
REMARK 465     GLU G   127                                                      
REMARK 465     VAL G   128                                                      
REMARK 465     SER G   129                                                      
REMARK 465     THR G   130                                                      
REMARK 465     VAL G   131                                                      
REMARK 465     PRO G   132                                                      
REMARK 465     GLY G   133                                                      
REMARK 465     PHE G   134                                                      
REMARK 465     LEU G   135                                                      
REMARK 465     GLY G   136                                                      
REMARK 465     VAL G   137                                                      
REMARK 465     ILE G   138                                                      
REMARK 465     GLU G   139                                                      
REMARK 465     SER G   140                                                      
REMARK 465     PRO G   141                                                      
REMARK 465     GLU G   142                                                      
REMARK 465     HIS G   143                                                      
REMARK 465     ALA G   144                                                      
REMARK 465     VAL G   145                                                      
REMARK 465     THR G   146                                                      
REMARK 465     ILE G   147                                                      
REMARK 465     ALA G   148                                                      
REMARK 465     ASP G   149                                                      
REMARK 465     GLU G   150                                                      
REMARK 465     ILE G   151                                                      
REMARK 465     GLY G   152                                                      
REMARK 465     TYR G   153                                                      
REMARK 465     PRO G   154                                                      
REMARK 465     VAL G   155                                                      
REMARK 465     MET G   156                                                      
REMARK 465     ILE G   157                                                      
REMARK 465     LYS G   158                                                      
REMARK 465     ALA G   159                                                      
REMARK 465     SER G   160                                                      
REMARK 465     ALA G   161                                                      
REMARK 465     GLY G   162                                                      
REMARK 465     GLY G   163                                                      
REMARK 465     GLY G   164                                                      
REMARK 465     GLY G   165                                                      
REMARK 465     LYS G   166                                                      
REMARK 465     GLY G   167                                                      
REMARK 465     MET G   168                                                      
REMARK 465     ARG G   169                                                      
REMARK 465     ILE G   170                                                      
REMARK 465     ALA G   171                                                      
REMARK 465     GLU G   172                                                      
REMARK 465     SER G   173                                                      
REMARK 465     ALA G   174                                                      
REMARK 465     ASP G   175                                                      
REMARK 465     GLU G   176                                                      
REMARK 465     VAL G   177                                                      
REMARK 465     ALA G   178                                                      
REMARK 465     GLU G   179                                                      
REMARK 465     GLY G   180                                                      
REMARK 465     PHE G   181                                                      
REMARK 465     ALA G   182                                                      
REMARK 465     ARG G   183                                                      
REMARK 465     ALA G   184                                                      
REMARK 465     LYS G   185                                                      
REMARK 465     SER G   186                                                      
REMARK 465     GLU G   187                                                      
REMARK 465     ALA G   188                                                      
REMARK 465     SER G   189                                                      
REMARK 465     SER G   190                                                      
REMARK 465     SER G   191                                                      
REMARK 465     PHE G   192                                                      
REMARK 465     GLY G   193                                                      
REMARK 465     ASP G   194                                                      
REMARK 465     ASP G   195                                                      
REMARK 465     ARG G   196                                                      
REMARK 465     VAL G   197                                                      
REMARK 465     PHE G   198                                                      
REMARK 465     VAL G   199                                                      
REMARK 465     GLU G   200                                                      
REMARK 465     LYS G   201                                                      
REMARK 465     PHE G   202                                                      
REMARK 465     ILE G   203                                                      
REMARK 465     THR G   204                                                      
REMARK 465     ASP G   205                                                      
REMARK 465     PRO G   206                                                      
REMARK 465     ARG G   207                                                      
REMARK 465     HIS G   208                                                      
REMARK 465     ILE G   209                                                      
REMARK 465     GLU G   210                                                      
REMARK 465     ILE G   211                                                      
REMARK 465     GLN G   212                                                      
REMARK 465     VAL G   213                                                      
REMARK 465     ILE G   214                                                      
REMARK 465     GLY G   215                                                      
REMARK 465     ASP G   216                                                      
REMARK 465     LYS G   217                                                      
REMARK 465     HIS G   218                                                      
REMARK 465     GLY G   219                                                      
REMARK 465     ASN G   220                                                      
REMARK 465     VAL G   221                                                      
REMARK 465     ILE G   222                                                      
REMARK 465     TYR G   223                                                      
REMARK 465     LEU G   224                                                      
REMARK 465     GLY G   225                                                      
REMARK 465     GLU G   226                                                      
REMARK 465     ARG G   227                                                      
REMARK 465     GLU G   228                                                      
REMARK 465     CYS G   229                                                      
REMARK 465     SER G   230                                                      
REMARK 465     ILE G   231                                                      
REMARK 465     GLN G   232                                                      
REMARK 465     ARG G   233                                                      
REMARK 465     ARG G   234                                                      
REMARK 465     ASN G   235                                                      
REMARK 465     GLN G   236                                                      
REMARK 465     LYS G   237                                                      
REMARK 465     VAL G   238                                                      
REMARK 465     ILE G   239                                                      
REMARK 465     GLU G   240                                                      
REMARK 465     GLU G   241                                                      
REMARK 465     ALA G   242                                                      
REMARK 465     PRO G   243                                                      
REMARK 465     SER G   244                                                      
REMARK 465     PRO G   245                                                      
REMARK 465     LEU G   246                                                      
REMARK 465     LEU G   247                                                      
REMARK 465     ASP G   248                                                      
REMARK 465     GLU G   249                                                      
REMARK 465     GLU G   250                                                      
REMARK 465     THR G   251                                                      
REMARK 465     ARG G   252                                                      
REMARK 465     ARG G   253                                                      
REMARK 465     LYS G   254                                                      
REMARK 465     MET G   255                                                      
REMARK 465     GLY G   256                                                      
REMARK 465     GLU G   257                                                      
REMARK 465     GLN G   258                                                      
REMARK 465     ALA G   259                                                      
REMARK 465     VAL G   260                                                      
REMARK 465     ALA G   261                                                      
REMARK 465     LEU G   262                                                      
REMARK 465     ALA G   263                                                      
REMARK 465     LYS G   264                                                      
REMARK 465     ALA G   265                                                      
REMARK 465     VAL G   266                                                      
REMARK 465     ASN G   267                                                      
REMARK 465     TYR G   268                                                      
REMARK 465     ASP G   269                                                      
REMARK 465     SER G   270                                                      
REMARK 465     ALA G   271                                                      
REMARK 465     GLY G   272                                                      
REMARK 465     THR G   273                                                      
REMARK 465     VAL G   274                                                      
REMARK 465     GLU G   275                                                      
REMARK 465     PHE G   276                                                      
REMARK 465     VAL G   277                                                      
REMARK 465     ALA G   278                                                      
REMARK 465     GLY G   279                                                      
REMARK 465     GLN G   280                                                      
REMARK 465     ASP G   281                                                      
REMARK 465     LYS G   282                                                      
REMARK 465     SER G   283                                                      
REMARK 465     PHE G   284                                                      
REMARK 465     TYR G   285                                                      
REMARK 465     PHE G   286                                                      
REMARK 465     LEU G   287                                                      
REMARK 465     GLU G   288                                                      
REMARK 465     MET G   289                                                      
REMARK 465     ASN G   290                                                      
REMARK 465     THR G   291                                                      
REMARK 465     ARG G   292                                                      
REMARK 465     LEU G   293                                                      
REMARK 465     GLN G   294                                                      
REMARK 465     VAL G   295                                                      
REMARK 465     GLU G   296                                                      
REMARK 465     HIS G   297                                                      
REMARK 465     PRO G   298                                                      
REMARK 465     VAL G   299                                                      
REMARK 465     THR G   300                                                      
REMARK 465     GLU G   301                                                      
REMARK 465     MET G   302                                                      
REMARK 465     ILE G   303                                                      
REMARK 465     THR G   304                                                      
REMARK 465     GLY G   305                                                      
REMARK 465     LEU G   306                                                      
REMARK 465     ASP G   307                                                      
REMARK 465     LEU G   308                                                      
REMARK 465     VAL G   309                                                      
REMARK 465     GLU G   310                                                      
REMARK 465     LEU G   311                                                      
REMARK 465     MET G   312                                                      
REMARK 465     ILE G   313                                                      
REMARK 465     ARG G   314                                                      
REMARK 465     VAL G   315                                                      
REMARK 465     ALA G   316                                                      
REMARK 465     ALA G   317                                                      
REMARK 465     GLY G   318                                                      
REMARK 465     GLU G   319                                                      
REMARK 465     LYS G   320                                                      
REMARK 465     LEU G   321                                                      
REMARK 465     PRO G   322                                                      
REMARK 465     LEU G   323                                                      
REMARK 465     SER G   324                                                      
REMARK 465     GLN G   325                                                      
REMARK 465     ASP G   326                                                      
REMARK 465     GLN G   327                                                      
REMARK 465     VAL G   328                                                      
REMARK 465     LYS G   329                                                      
REMARK 465     LEU G   330                                                      
REMARK 465     ASP G   331                                                      
REMARK 465     GLY G   332                                                      
REMARK 465     TRP G   333                                                      
REMARK 465     ALA G   334                                                      
REMARK 465     VAL G   335                                                      
REMARK 465     GLU G   336                                                      
REMARK 465     SER G   337                                                      
REMARK 465     ARG G   338                                                      
REMARK 465     VAL G   339                                                      
REMARK 465     TYR G   340                                                      
REMARK 465     ALA G   341                                                      
REMARK 465     GLU G   342                                                      
REMARK 465     ASP G   343                                                      
REMARK 465     PRO G   344                                                      
REMARK 465     THR G   345                                                      
REMARK 465     ARG G   346                                                      
REMARK 465     ASN G   347                                                      
REMARK 465     PHE G   348                                                      
REMARK 465     LEU G   349                                                      
REMARK 465     PRO G   350                                                      
REMARK 465     SER G   351                                                      
REMARK 465     ILE G   352                                                      
REMARK 465     GLY G   353                                                      
REMARK 465     ARG G   354                                                      
REMARK 465     LEU G   355                                                      
REMARK 465     THR G   356                                                      
REMARK 465     THR G   357                                                      
REMARK 465     TYR G   358                                                      
REMARK 465     GLN G   359                                                      
REMARK 465     PRO G   360                                                      
REMARK 465     PRO G   361                                                      
REMARK 465     GLU G   362                                                      
REMARK 465     GLU G   363                                                      
REMARK 465     GLY G   364                                                      
REMARK 465     PRO G   365                                                      
REMARK 465     LEU G   366                                                      
REMARK 465     GLY G   367                                                      
REMARK 465     GLY G   368                                                      
REMARK 465     ALA G   369                                                      
REMARK 465     ILE G   370                                                      
REMARK 465     VAL G   371                                                      
REMARK 465     ARG G   372                                                      
REMARK 465     ASN G   373                                                      
REMARK 465     ASP G   374                                                      
REMARK 465     THR G   375                                                      
REMARK 465     GLY G   376                                                      
REMARK 465     VAL G   377                                                      
REMARK 465     GLU G   378                                                      
REMARK 465     GLU G   379                                                      
REMARK 465     GLY G   380                                                      
REMARK 465     GLY G   381                                                      
REMARK 465     GLU G   382                                                      
REMARK 465     ILE G   383                                                      
REMARK 465     ALA G   384                                                      
REMARK 465     ILE G   385                                                      
REMARK 465     HIS G   386                                                      
REMARK 465     TYR G   387                                                      
REMARK 465     ASP G   388                                                      
REMARK 465     PRO G   389                                                      
REMARK 465     MET G   390                                                      
REMARK 465     ILE G   391                                                      
REMARK 465     ALA G   392                                                      
REMARK 465     LYS G   393                                                      
REMARK 465     LEU G   394                                                      
REMARK 465     VAL G   395                                                      
REMARK 465     THR G   396                                                      
REMARK 465     TRP G   397                                                      
REMARK 465     ALA G   398                                                      
REMARK 465     PRO G   399                                                      
REMARK 465     THR G   400                                                      
REMARK 465     ARG G   401                                                      
REMARK 465     LEU G   402                                                      
REMARK 465     GLU G   403                                                      
REMARK 465     ALA G   404                                                      
REMARK 465     ILE G   405                                                      
REMARK 465     GLU G   406                                                      
REMARK 465     ALA G   407                                                      
REMARK 465     GLN G   408                                                      
REMARK 465     ALA G   409                                                      
REMARK 465     THR G   410                                                      
REMARK 465     ALA G   411                                                      
REMARK 465     LEU G   412                                                      
REMARK 465     ASP G   413                                                      
REMARK 465     ALA G   414                                                      
REMARK 465     PHE G   415                                                      
REMARK 465     ALA G   416                                                      
REMARK 465     ILE G   417                                                      
REMARK 465     GLU G   418                                                      
REMARK 465     GLY G   419                                                      
REMARK 465     ILE G   420                                                      
REMARK 465     ARG G   421                                                      
REMARK 465     HIS G   422                                                      
REMARK 465     ASN G   423                                                      
REMARK 465     ILE G   424                                                      
REMARK 465     PRO G   425                                                      
REMARK 465     PHE G   426                                                      
REMARK 465     LEU G   427                                                      
REMARK 465     ALA G   428                                                      
REMARK 465     THR G   429                                                      
REMARK 465     LEU G   430                                                      
REMARK 465     MET G   431                                                      
REMARK 465     ALA G   432                                                      
REMARK 465     HIS G   433                                                      
REMARK 465     PRO G   434                                                      
REMARK 465     ARG G   435                                                      
REMARK 465     TRP G   436                                                      
REMARK 465     ARG G   437                                                      
REMARK 465     ASP G   438                                                      
REMARK 465     GLY G   439                                                      
REMARK 465     ARG G   440                                                      
REMARK 465     LEU G   441                                                      
REMARK 465     SER G   442                                                      
REMARK 465     THR G   443                                                      
REMARK 465     GLY G   444                                                      
REMARK 465     PHE G   445                                                      
REMARK 465     ILE G   446                                                      
REMARK 465     LYS G   447                                                      
REMARK 465     GLU G   448                                                      
REMARK 465     GLU G   449                                                      
REMARK 465     PHE G   450                                                      
REMARK 465     PRO G   451                                                      
REMARK 465     GLU G   452                                                      
REMARK 465     GLY G   453                                                      
REMARK 465     PHE G   454                                                      
REMARK 465     ILE G   455                                                      
REMARK 465     ALA G   456                                                      
REMARK 465     PRO G   457                                                      
REMARK 465     GLU G   458                                                      
REMARK 465     ALA G   667                                                      
REMARK 465     MET H     1                                                      
REMARK 465     PHE H     2                                                      
REMARK 465     ASP H     3                                                      
REMARK 465     LYS H     4                                                      
REMARK 465     ILE H     5                                                      
REMARK 465     LEU H     6                                                      
REMARK 465     ILE H     7                                                      
REMARK 465     ALA H     8                                                      
REMARK 465     ASN H     9                                                      
REMARK 465     ARG H    10                                                      
REMARK 465     GLY H    11                                                      
REMARK 465     GLU H    12                                                      
REMARK 465     ILE H    13                                                      
REMARK 465     ALA H    14                                                      
REMARK 465     CYS H    15                                                      
REMARK 465     ARG H    16                                                      
REMARK 465     ILE H    17                                                      
REMARK 465     ILE H    18                                                      
REMARK 465     LYS H    19                                                      
REMARK 465     THR H    20                                                      
REMARK 465     ALA H    21                                                      
REMARK 465     GLN H    22                                                      
REMARK 465     LYS H    23                                                      
REMARK 465     MET H    24                                                      
REMARK 465     GLY H    25                                                      
REMARK 465     ILE H    26                                                      
REMARK 465     LYS H    27                                                      
REMARK 465     THR H    28                                                      
REMARK 465     VAL H    29                                                      
REMARK 465     ALA H    30                                                      
REMARK 465     VAL H    31                                                      
REMARK 465     TYR H    32                                                      
REMARK 465     SER H    33                                                      
REMARK 465     ASP H    34                                                      
REMARK 465     ALA H    35                                                      
REMARK 465     ASP H    36                                                      
REMARK 465     ARG H    37                                                      
REMARK 465     ASP H    38                                                      
REMARK 465     ALA H    39                                                      
REMARK 465     VAL H    40                                                      
REMARK 465     HIS H    41                                                      
REMARK 465     VAL H    42                                                      
REMARK 465     ALA H    43                                                      
REMARK 465     MET H    44                                                      
REMARK 465     ALA H    45                                                      
REMARK 465     ASP H    46                                                      
REMARK 465     GLU H    47                                                      
REMARK 465     ALA H    48                                                      
REMARK 465     VAL H    49                                                      
REMARK 465     HIS H    50                                                      
REMARK 465     ILE H    51                                                      
REMARK 465     GLY H    52                                                      
REMARK 465     PRO H    53                                                      
REMARK 465     ALA H    54                                                      
REMARK 465     PRO H    55                                                      
REMARK 465     ALA H    56                                                      
REMARK 465     ALA H    57                                                      
REMARK 465     GLN H    58                                                      
REMARK 465     SER H    59                                                      
REMARK 465     TYR H    60                                                      
REMARK 465     LEU H    61                                                      
REMARK 465     LEU H    62                                                      
REMARK 465     ILE H    63                                                      
REMARK 465     GLU H    64                                                      
REMARK 465     LYS H    65                                                      
REMARK 465     ILE H    66                                                      
REMARK 465     ILE H    67                                                      
REMARK 465     ASP H    68                                                      
REMARK 465     ALA H    69                                                      
REMARK 465     CYS H    70                                                      
REMARK 465     LYS H    71                                                      
REMARK 465     GLN H    72                                                      
REMARK 465     THR H    73                                                      
REMARK 465     GLY H    74                                                      
REMARK 465     ALA H    75                                                      
REMARK 465     GLN H    76                                                      
REMARK 465     ALA H    77                                                      
REMARK 465     VAL H    78                                                      
REMARK 465     HIS H    79                                                      
REMARK 465     PRO H    80                                                      
REMARK 465     GLY H    81                                                      
REMARK 465     TYR H    82                                                      
REMARK 465     GLY H    83                                                      
REMARK 465     PHE H    84                                                      
REMARK 465     LEU H    85                                                      
REMARK 465     SER H    86                                                      
REMARK 465     GLU H    87                                                      
REMARK 465     ARG H    88                                                      
REMARK 465     GLU H    89                                                      
REMARK 465     SER H    90                                                      
REMARK 465     PHE H    91                                                      
REMARK 465     PRO H    92                                                      
REMARK 465     LYS H    93                                                      
REMARK 465     ALA H    94                                                      
REMARK 465     LEU H    95                                                      
REMARK 465     ALA H    96                                                      
REMARK 465     GLU H    97                                                      
REMARK 465     ALA H    98                                                      
REMARK 465     GLY H    99                                                      
REMARK 465     ILE H   100                                                      
REMARK 465     VAL H   101                                                      
REMARK 465     PHE H   102                                                      
REMARK 465     ILE H   103                                                      
REMARK 465     GLY H   104                                                      
REMARK 465     PRO H   105                                                      
REMARK 465     ASN H   106                                                      
REMARK 465     PRO H   107                                                      
REMARK 465     GLY H   108                                                      
REMARK 465     ALA H   109                                                      
REMARK 465     ILE H   110                                                      
REMARK 465     ALA H   111                                                      
REMARK 465     ALA H   112                                                      
REMARK 465     MET H   113                                                      
REMARK 465     GLY H   114                                                      
REMARK 465     ASP H   115                                                      
REMARK 465     LYS H   116                                                      
REMARK 465     ILE H   117                                                      
REMARK 465     GLU H   118                                                      
REMARK 465     SER H   119                                                      
REMARK 465     LYS H   120                                                      
REMARK 465     LYS H   121                                                      
REMARK 465     ALA H   122                                                      
REMARK 465     ALA H   123                                                      
REMARK 465     ALA H   124                                                      
REMARK 465     ALA H   125                                                      
REMARK 465     ALA H   126                                                      
REMARK 465     GLU H   127                                                      
REMARK 465     VAL H   128                                                      
REMARK 465     SER H   129                                                      
REMARK 465     THR H   130                                                      
REMARK 465     VAL H   131                                                      
REMARK 465     PRO H   132                                                      
REMARK 465     GLY H   133                                                      
REMARK 465     PHE H   134                                                      
REMARK 465     LEU H   135                                                      
REMARK 465     GLY H   136                                                      
REMARK 465     VAL H   137                                                      
REMARK 465     ILE H   138                                                      
REMARK 465     GLU H   139                                                      
REMARK 465     SER H   140                                                      
REMARK 465     PRO H   141                                                      
REMARK 465     GLU H   142                                                      
REMARK 465     HIS H   143                                                      
REMARK 465     ALA H   144                                                      
REMARK 465     VAL H   145                                                      
REMARK 465     THR H   146                                                      
REMARK 465     ILE H   147                                                      
REMARK 465     ALA H   148                                                      
REMARK 465     ASP H   149                                                      
REMARK 465     GLU H   150                                                      
REMARK 465     ILE H   151                                                      
REMARK 465     GLY H   152                                                      
REMARK 465     TYR H   153                                                      
REMARK 465     PRO H   154                                                      
REMARK 465     VAL H   155                                                      
REMARK 465     MET H   156                                                      
REMARK 465     ILE H   157                                                      
REMARK 465     LYS H   158                                                      
REMARK 465     ALA H   159                                                      
REMARK 465     SER H   160                                                      
REMARK 465     ALA H   161                                                      
REMARK 465     GLY H   162                                                      
REMARK 465     GLY H   163                                                      
REMARK 465     GLY H   164                                                      
REMARK 465     GLY H   165                                                      
REMARK 465     LYS H   166                                                      
REMARK 465     GLY H   167                                                      
REMARK 465     MET H   168                                                      
REMARK 465     ARG H   169                                                      
REMARK 465     ILE H   170                                                      
REMARK 465     ALA H   171                                                      
REMARK 465     GLU H   172                                                      
REMARK 465     SER H   173                                                      
REMARK 465     ALA H   174                                                      
REMARK 465     ASP H   175                                                      
REMARK 465     GLU H   176                                                      
REMARK 465     VAL H   177                                                      
REMARK 465     ALA H   178                                                      
REMARK 465     GLU H   179                                                      
REMARK 465     GLY H   180                                                      
REMARK 465     PHE H   181                                                      
REMARK 465     ALA H   182                                                      
REMARK 465     ARG H   183                                                      
REMARK 465     ALA H   184                                                      
REMARK 465     LYS H   185                                                      
REMARK 465     SER H   186                                                      
REMARK 465     GLU H   187                                                      
REMARK 465     ALA H   188                                                      
REMARK 465     SER H   189                                                      
REMARK 465     SER H   190                                                      
REMARK 465     SER H   191                                                      
REMARK 465     PHE H   192                                                      
REMARK 465     GLY H   193                                                      
REMARK 465     ASP H   194                                                      
REMARK 465     ASP H   195                                                      
REMARK 465     ARG H   196                                                      
REMARK 465     VAL H   197                                                      
REMARK 465     PHE H   198                                                      
REMARK 465     VAL H   199                                                      
REMARK 465     GLU H   200                                                      
REMARK 465     LYS H   201                                                      
REMARK 465     PHE H   202                                                      
REMARK 465     ILE H   203                                                      
REMARK 465     THR H   204                                                      
REMARK 465     ASP H   205                                                      
REMARK 465     PRO H   206                                                      
REMARK 465     ARG H   207                                                      
REMARK 465     HIS H   208                                                      
REMARK 465     ILE H   209                                                      
REMARK 465     GLU H   210                                                      
REMARK 465     ILE H   211                                                      
REMARK 465     GLN H   212                                                      
REMARK 465     VAL H   213                                                      
REMARK 465     ILE H   214                                                      
REMARK 465     GLY H   215                                                      
REMARK 465     ASP H   216                                                      
REMARK 465     LYS H   217                                                      
REMARK 465     HIS H   218                                                      
REMARK 465     GLY H   219                                                      
REMARK 465     ASN H   220                                                      
REMARK 465     VAL H   221                                                      
REMARK 465     ILE H   222                                                      
REMARK 465     TYR H   223                                                      
REMARK 465     LEU H   224                                                      
REMARK 465     GLY H   225                                                      
REMARK 465     GLU H   226                                                      
REMARK 465     ARG H   227                                                      
REMARK 465     GLU H   228                                                      
REMARK 465     CYS H   229                                                      
REMARK 465     SER H   230                                                      
REMARK 465     ILE H   231                                                      
REMARK 465     GLN H   232                                                      
REMARK 465     ARG H   233                                                      
REMARK 465     ARG H   234                                                      
REMARK 465     ASN H   235                                                      
REMARK 465     GLN H   236                                                      
REMARK 465     LYS H   237                                                      
REMARK 465     VAL H   238                                                      
REMARK 465     ILE H   239                                                      
REMARK 465     GLU H   240                                                      
REMARK 465     GLU H   241                                                      
REMARK 465     ALA H   242                                                      
REMARK 465     PRO H   243                                                      
REMARK 465     SER H   244                                                      
REMARK 465     PRO H   245                                                      
REMARK 465     LEU H   246                                                      
REMARK 465     LEU H   247                                                      
REMARK 465     ASP H   248                                                      
REMARK 465     GLU H   249                                                      
REMARK 465     GLU H   250                                                      
REMARK 465     THR H   251                                                      
REMARK 465     ARG H   252                                                      
REMARK 465     ARG H   253                                                      
REMARK 465     LYS H   254                                                      
REMARK 465     MET H   255                                                      
REMARK 465     GLY H   256                                                      
REMARK 465     GLU H   257                                                      
REMARK 465     GLN H   258                                                      
REMARK 465     ALA H   259                                                      
REMARK 465     VAL H   260                                                      
REMARK 465     ALA H   261                                                      
REMARK 465     LEU H   262                                                      
REMARK 465     ALA H   263                                                      
REMARK 465     LYS H   264                                                      
REMARK 465     ALA H   265                                                      
REMARK 465     VAL H   266                                                      
REMARK 465     ASN H   267                                                      
REMARK 465     TYR H   268                                                      
REMARK 465     ASP H   269                                                      
REMARK 465     SER H   270                                                      
REMARK 465     ALA H   271                                                      
REMARK 465     GLY H   272                                                      
REMARK 465     THR H   273                                                      
REMARK 465     VAL H   274                                                      
REMARK 465     GLU H   275                                                      
REMARK 465     PHE H   276                                                      
REMARK 465     VAL H   277                                                      
REMARK 465     ALA H   278                                                      
REMARK 465     GLY H   279                                                      
REMARK 465     GLN H   280                                                      
REMARK 465     ASP H   281                                                      
REMARK 465     LYS H   282                                                      
REMARK 465     SER H   283                                                      
REMARK 465     PHE H   284                                                      
REMARK 465     TYR H   285                                                      
REMARK 465     PHE H   286                                                      
REMARK 465     LEU H   287                                                      
REMARK 465     GLU H   288                                                      
REMARK 465     MET H   289                                                      
REMARK 465     ASN H   290                                                      
REMARK 465     THR H   291                                                      
REMARK 465     ARG H   292                                                      
REMARK 465     LEU H   293                                                      
REMARK 465     GLN H   294                                                      
REMARK 465     VAL H   295                                                      
REMARK 465     GLU H   296                                                      
REMARK 465     HIS H   297                                                      
REMARK 465     PRO H   298                                                      
REMARK 465     VAL H   299                                                      
REMARK 465     THR H   300                                                      
REMARK 465     GLU H   301                                                      
REMARK 465     MET H   302                                                      
REMARK 465     ILE H   303                                                      
REMARK 465     THR H   304                                                      
REMARK 465     GLY H   305                                                      
REMARK 465     LEU H   306                                                      
REMARK 465     ASP H   307                                                      
REMARK 465     LEU H   308                                                      
REMARK 465     VAL H   309                                                      
REMARK 465     GLU H   310                                                      
REMARK 465     LEU H   311                                                      
REMARK 465     MET H   312                                                      
REMARK 465     ILE H   313                                                      
REMARK 465     ARG H   314                                                      
REMARK 465     VAL H   315                                                      
REMARK 465     ALA H   316                                                      
REMARK 465     ALA H   317                                                      
REMARK 465     GLY H   318                                                      
REMARK 465     GLU H   319                                                      
REMARK 465     LYS H   320                                                      
REMARK 465     LEU H   321                                                      
REMARK 465     PRO H   322                                                      
REMARK 465     LEU H   323                                                      
REMARK 465     SER H   324                                                      
REMARK 465     GLN H   325                                                      
REMARK 465     ASP H   326                                                      
REMARK 465     GLN H   327                                                      
REMARK 465     VAL H   328                                                      
REMARK 465     LYS H   329                                                      
REMARK 465     LEU H   330                                                      
REMARK 465     ASP H   331                                                      
REMARK 465     GLY H   332                                                      
REMARK 465     TRP H   333                                                      
REMARK 465     ALA H   334                                                      
REMARK 465     VAL H   335                                                      
REMARK 465     GLU H   336                                                      
REMARK 465     SER H   337                                                      
REMARK 465     ARG H   338                                                      
REMARK 465     VAL H   339                                                      
REMARK 465     TYR H   340                                                      
REMARK 465     ALA H   341                                                      
REMARK 465     GLU H   342                                                      
REMARK 465     ASP H   343                                                      
REMARK 465     PRO H   344                                                      
REMARK 465     THR H   345                                                      
REMARK 465     ARG H   346                                                      
REMARK 465     ASN H   347                                                      
REMARK 465     PHE H   348                                                      
REMARK 465     LEU H   349                                                      
REMARK 465     PRO H   350                                                      
REMARK 465     SER H   351                                                      
REMARK 465     ILE H   352                                                      
REMARK 465     GLY H   353                                                      
REMARK 465     ARG H   354                                                      
REMARK 465     LEU H   355                                                      
REMARK 465     THR H   356                                                      
REMARK 465     THR H   357                                                      
REMARK 465     TYR H   358                                                      
REMARK 465     GLN H   359                                                      
REMARK 465     PRO H   360                                                      
REMARK 465     PRO H   361                                                      
REMARK 465     GLU H   362                                                      
REMARK 465     GLU H   363                                                      
REMARK 465     GLY H   364                                                      
REMARK 465     PRO H   365                                                      
REMARK 465     LEU H   366                                                      
REMARK 465     GLY H   367                                                      
REMARK 465     GLY H   368                                                      
REMARK 465     ALA H   369                                                      
REMARK 465     ILE H   370                                                      
REMARK 465     VAL H   371                                                      
REMARK 465     ARG H   372                                                      
REMARK 465     ASN H   373                                                      
REMARK 465     ASP H   374                                                      
REMARK 465     THR H   375                                                      
REMARK 465     GLY H   376                                                      
REMARK 465     VAL H   377                                                      
REMARK 465     GLU H   378                                                      
REMARK 465     GLU H   379                                                      
REMARK 465     GLY H   380                                                      
REMARK 465     GLY H   381                                                      
REMARK 465     GLU H   382                                                      
REMARK 465     ILE H   383                                                      
REMARK 465     ALA H   384                                                      
REMARK 465     ILE H   385                                                      
REMARK 465     HIS H   386                                                      
REMARK 465     TYR H   387                                                      
REMARK 465     ASP H   388                                                      
REMARK 465     PRO H   389                                                      
REMARK 465     MET H   390                                                      
REMARK 465     ILE H   391                                                      
REMARK 465     ALA H   392                                                      
REMARK 465     LYS H   393                                                      
REMARK 465     LEU H   394                                                      
REMARK 465     VAL H   395                                                      
REMARK 465     THR H   396                                                      
REMARK 465     TRP H   397                                                      
REMARK 465     ALA H   398                                                      
REMARK 465     PRO H   399                                                      
REMARK 465     THR H   400                                                      
REMARK 465     ARG H   401                                                      
REMARK 465     LEU H   402                                                      
REMARK 465     GLU H   403                                                      
REMARK 465     ALA H   404                                                      
REMARK 465     ILE H   405                                                      
REMARK 465     GLU H   406                                                      
REMARK 465     ALA H   407                                                      
REMARK 465     GLN H   408                                                      
REMARK 465     ALA H   409                                                      
REMARK 465     THR H   410                                                      
REMARK 465     ALA H   411                                                      
REMARK 465     LEU H   412                                                      
REMARK 465     ASP H   413                                                      
REMARK 465     ALA H   414                                                      
REMARK 465     PHE H   415                                                      
REMARK 465     ALA H   416                                                      
REMARK 465     ILE H   417                                                      
REMARK 465     GLU H   418                                                      
REMARK 465     GLY H   419                                                      
REMARK 465     ILE H   420                                                      
REMARK 465     ARG H   421                                                      
REMARK 465     HIS H   422                                                      
REMARK 465     ASN H   423                                                      
REMARK 465     ILE H   424                                                      
REMARK 465     PRO H   425                                                      
REMARK 465     PHE H   426                                                      
REMARK 465     LEU H   427                                                      
REMARK 465     ALA H   428                                                      
REMARK 465     THR H   429                                                      
REMARK 465     LEU H   430                                                      
REMARK 465     MET H   431                                                      
REMARK 465     ALA H   432                                                      
REMARK 465     HIS H   433                                                      
REMARK 465     PRO H   434                                                      
REMARK 465     ARG H   435                                                      
REMARK 465     TRP H   436                                                      
REMARK 465     ARG H   437                                                      
REMARK 465     ASP H   438                                                      
REMARK 465     GLY H   439                                                      
REMARK 465     ARG H   440                                                      
REMARK 465     LEU H   441                                                      
REMARK 465     SER H   442                                                      
REMARK 465     THR H   443                                                      
REMARK 465     GLY H   444                                                      
REMARK 465     PHE H   445                                                      
REMARK 465     ILE H   446                                                      
REMARK 465     LYS H   447                                                      
REMARK 465     GLU H   448                                                      
REMARK 465     GLU H   449                                                      
REMARK 465     PHE H   450                                                      
REMARK 465     PRO H   451                                                      
REMARK 465     GLU H   452                                                      
REMARK 465     GLY H   453                                                      
REMARK 465     PHE H   454                                                      
REMARK 465     ILE H   455                                                      
REMARK 465     ALA H   456                                                      
REMARK 465     ALA H   667                                                      
REMARK 465     MET I     1                                                      
REMARK 465     PHE I     2                                                      
REMARK 465     ASP I     3                                                      
REMARK 465     LYS I     4                                                      
REMARK 465     ILE I     5                                                      
REMARK 465     LEU I     6                                                      
REMARK 465     ILE I     7                                                      
REMARK 465     ALA I     8                                                      
REMARK 465     ASN I     9                                                      
REMARK 465     ARG I    10                                                      
REMARK 465     GLY I    11                                                      
REMARK 465     GLU I    12                                                      
REMARK 465     ILE I    13                                                      
REMARK 465     ALA I    14                                                      
REMARK 465     CYS I    15                                                      
REMARK 465     ARG I    16                                                      
REMARK 465     ILE I    17                                                      
REMARK 465     ILE I    18                                                      
REMARK 465     LYS I    19                                                      
REMARK 465     THR I    20                                                      
REMARK 465     ALA I    21                                                      
REMARK 465     GLN I    22                                                      
REMARK 465     LYS I    23                                                      
REMARK 465     MET I    24                                                      
REMARK 465     GLY I    25                                                      
REMARK 465     ILE I    26                                                      
REMARK 465     LYS I    27                                                      
REMARK 465     THR I    28                                                      
REMARK 465     VAL I    29                                                      
REMARK 465     ALA I    30                                                      
REMARK 465     VAL I    31                                                      
REMARK 465     TYR I    32                                                      
REMARK 465     SER I    33                                                      
REMARK 465     ASP I    34                                                      
REMARK 465     ALA I    35                                                      
REMARK 465     ASP I    36                                                      
REMARK 465     ARG I    37                                                      
REMARK 465     ASP I    38                                                      
REMARK 465     ALA I    39                                                      
REMARK 465     VAL I    40                                                      
REMARK 465     HIS I    41                                                      
REMARK 465     VAL I    42                                                      
REMARK 465     ALA I    43                                                      
REMARK 465     MET I    44                                                      
REMARK 465     ALA I    45                                                      
REMARK 465     ASP I    46                                                      
REMARK 465     GLU I    47                                                      
REMARK 465     ALA I    48                                                      
REMARK 465     VAL I    49                                                      
REMARK 465     HIS I    50                                                      
REMARK 465     ILE I    51                                                      
REMARK 465     GLY I    52                                                      
REMARK 465     PRO I    53                                                      
REMARK 465     ALA I    54                                                      
REMARK 465     PRO I    55                                                      
REMARK 465     ALA I    56                                                      
REMARK 465     ALA I    57                                                      
REMARK 465     GLN I    58                                                      
REMARK 465     SER I    59                                                      
REMARK 465     TYR I    60                                                      
REMARK 465     LEU I    61                                                      
REMARK 465     LEU I    62                                                      
REMARK 465     ILE I    63                                                      
REMARK 465     GLU I    64                                                      
REMARK 465     LYS I    65                                                      
REMARK 465     ILE I    66                                                      
REMARK 465     ILE I    67                                                      
REMARK 465     ASP I    68                                                      
REMARK 465     ALA I    69                                                      
REMARK 465     CYS I    70                                                      
REMARK 465     LYS I    71                                                      
REMARK 465     GLN I    72                                                      
REMARK 465     THR I    73                                                      
REMARK 465     GLY I    74                                                      
REMARK 465     ALA I    75                                                      
REMARK 465     GLN I    76                                                      
REMARK 465     ALA I    77                                                      
REMARK 465     VAL I    78                                                      
REMARK 465     HIS I    79                                                      
REMARK 465     PRO I    80                                                      
REMARK 465     GLY I    81                                                      
REMARK 465     TYR I    82                                                      
REMARK 465     GLY I    83                                                      
REMARK 465     PHE I    84                                                      
REMARK 465     LEU I    85                                                      
REMARK 465     SER I    86                                                      
REMARK 465     GLU I    87                                                      
REMARK 465     ARG I    88                                                      
REMARK 465     GLU I    89                                                      
REMARK 465     SER I    90                                                      
REMARK 465     PHE I    91                                                      
REMARK 465     PRO I    92                                                      
REMARK 465     LYS I    93                                                      
REMARK 465     ALA I    94                                                      
REMARK 465     LEU I    95                                                      
REMARK 465     ALA I    96                                                      
REMARK 465     GLU I    97                                                      
REMARK 465     ALA I    98                                                      
REMARK 465     GLY I    99                                                      
REMARK 465     ILE I   100                                                      
REMARK 465     VAL I   101                                                      
REMARK 465     PHE I   102                                                      
REMARK 465     ILE I   103                                                      
REMARK 465     GLY I   104                                                      
REMARK 465     PRO I   105                                                      
REMARK 465     ASN I   106                                                      
REMARK 465     PRO I   107                                                      
REMARK 465     GLY I   108                                                      
REMARK 465     ALA I   109                                                      
REMARK 465     ILE I   110                                                      
REMARK 465     ALA I   111                                                      
REMARK 465     ALA I   112                                                      
REMARK 465     MET I   113                                                      
REMARK 465     GLY I   114                                                      
REMARK 465     ASP I   115                                                      
REMARK 465     LYS I   116                                                      
REMARK 465     ILE I   117                                                      
REMARK 465     GLU I   118                                                      
REMARK 465     SER I   119                                                      
REMARK 465     LYS I   120                                                      
REMARK 465     LYS I   121                                                      
REMARK 465     ALA I   122                                                      
REMARK 465     ALA I   123                                                      
REMARK 465     ALA I   124                                                      
REMARK 465     ALA I   125                                                      
REMARK 465     ALA I   126                                                      
REMARK 465     GLU I   127                                                      
REMARK 465     VAL I   128                                                      
REMARK 465     SER I   129                                                      
REMARK 465     THR I   130                                                      
REMARK 465     VAL I   131                                                      
REMARK 465     PRO I   132                                                      
REMARK 465     GLY I   133                                                      
REMARK 465     PHE I   134                                                      
REMARK 465     LEU I   135                                                      
REMARK 465     GLY I   136                                                      
REMARK 465     VAL I   137                                                      
REMARK 465     ILE I   138                                                      
REMARK 465     GLU I   139                                                      
REMARK 465     SER I   140                                                      
REMARK 465     PRO I   141                                                      
REMARK 465     GLU I   142                                                      
REMARK 465     HIS I   143                                                      
REMARK 465     ALA I   144                                                      
REMARK 465     VAL I   145                                                      
REMARK 465     THR I   146                                                      
REMARK 465     ILE I   147                                                      
REMARK 465     ALA I   148                                                      
REMARK 465     ASP I   149                                                      
REMARK 465     GLU I   150                                                      
REMARK 465     ILE I   151                                                      
REMARK 465     GLY I   152                                                      
REMARK 465     TYR I   153                                                      
REMARK 465     PRO I   154                                                      
REMARK 465     VAL I   155                                                      
REMARK 465     MET I   156                                                      
REMARK 465     ILE I   157                                                      
REMARK 465     LYS I   158                                                      
REMARK 465     ALA I   159                                                      
REMARK 465     SER I   160                                                      
REMARK 465     ALA I   161                                                      
REMARK 465     GLY I   162                                                      
REMARK 465     GLY I   163                                                      
REMARK 465     GLY I   164                                                      
REMARK 465     GLY I   165                                                      
REMARK 465     LYS I   166                                                      
REMARK 465     GLY I   167                                                      
REMARK 465     MET I   168                                                      
REMARK 465     ARG I   169                                                      
REMARK 465     ILE I   170                                                      
REMARK 465     ALA I   171                                                      
REMARK 465     GLU I   172                                                      
REMARK 465     SER I   173                                                      
REMARK 465     ALA I   174                                                      
REMARK 465     ASP I   175                                                      
REMARK 465     GLU I   176                                                      
REMARK 465     VAL I   177                                                      
REMARK 465     ALA I   178                                                      
REMARK 465     GLU I   179                                                      
REMARK 465     GLY I   180                                                      
REMARK 465     PHE I   181                                                      
REMARK 465     ALA I   182                                                      
REMARK 465     ARG I   183                                                      
REMARK 465     ALA I   184                                                      
REMARK 465     LYS I   185                                                      
REMARK 465     SER I   186                                                      
REMARK 465     GLU I   187                                                      
REMARK 465     ALA I   188                                                      
REMARK 465     SER I   189                                                      
REMARK 465     SER I   190                                                      
REMARK 465     SER I   191                                                      
REMARK 465     PHE I   192                                                      
REMARK 465     GLY I   193                                                      
REMARK 465     ASP I   194                                                      
REMARK 465     ASP I   195                                                      
REMARK 465     ARG I   196                                                      
REMARK 465     VAL I   197                                                      
REMARK 465     PHE I   198                                                      
REMARK 465     VAL I   199                                                      
REMARK 465     GLU I   200                                                      
REMARK 465     LYS I   201                                                      
REMARK 465     PHE I   202                                                      
REMARK 465     ILE I   203                                                      
REMARK 465     THR I   204                                                      
REMARK 465     ASP I   205                                                      
REMARK 465     PRO I   206                                                      
REMARK 465     ARG I   207                                                      
REMARK 465     HIS I   208                                                      
REMARK 465     ILE I   209                                                      
REMARK 465     GLU I   210                                                      
REMARK 465     ILE I   211                                                      
REMARK 465     GLN I   212                                                      
REMARK 465     VAL I   213                                                      
REMARK 465     ILE I   214                                                      
REMARK 465     GLY I   215                                                      
REMARK 465     ASP I   216                                                      
REMARK 465     LYS I   217                                                      
REMARK 465     HIS I   218                                                      
REMARK 465     GLY I   219                                                      
REMARK 465     ASN I   220                                                      
REMARK 465     VAL I   221                                                      
REMARK 465     ILE I   222                                                      
REMARK 465     TYR I   223                                                      
REMARK 465     LEU I   224                                                      
REMARK 465     GLY I   225                                                      
REMARK 465     GLU I   226                                                      
REMARK 465     ARG I   227                                                      
REMARK 465     GLU I   228                                                      
REMARK 465     CYS I   229                                                      
REMARK 465     SER I   230                                                      
REMARK 465     ILE I   231                                                      
REMARK 465     GLN I   232                                                      
REMARK 465     ARG I   233                                                      
REMARK 465     ARG I   234                                                      
REMARK 465     ASN I   235                                                      
REMARK 465     GLN I   236                                                      
REMARK 465     LYS I   237                                                      
REMARK 465     VAL I   238                                                      
REMARK 465     ILE I   239                                                      
REMARK 465     GLU I   240                                                      
REMARK 465     GLU I   241                                                      
REMARK 465     ALA I   242                                                      
REMARK 465     PRO I   243                                                      
REMARK 465     SER I   244                                                      
REMARK 465     PRO I   245                                                      
REMARK 465     LEU I   246                                                      
REMARK 465     LEU I   247                                                      
REMARK 465     ASP I   248                                                      
REMARK 465     GLU I   249                                                      
REMARK 465     GLU I   250                                                      
REMARK 465     THR I   251                                                      
REMARK 465     ARG I   252                                                      
REMARK 465     ARG I   253                                                      
REMARK 465     LYS I   254                                                      
REMARK 465     MET I   255                                                      
REMARK 465     GLY I   256                                                      
REMARK 465     GLU I   257                                                      
REMARK 465     GLN I   258                                                      
REMARK 465     ALA I   259                                                      
REMARK 465     VAL I   260                                                      
REMARK 465     ALA I   261                                                      
REMARK 465     LEU I   262                                                      
REMARK 465     ALA I   263                                                      
REMARK 465     LYS I   264                                                      
REMARK 465     ALA I   265                                                      
REMARK 465     VAL I   266                                                      
REMARK 465     ASN I   267                                                      
REMARK 465     TYR I   268                                                      
REMARK 465     ASP I   269                                                      
REMARK 465     SER I   270                                                      
REMARK 465     ALA I   271                                                      
REMARK 465     GLY I   272                                                      
REMARK 465     THR I   273                                                      
REMARK 465     VAL I   274                                                      
REMARK 465     GLU I   275                                                      
REMARK 465     PHE I   276                                                      
REMARK 465     VAL I   277                                                      
REMARK 465     ALA I   278                                                      
REMARK 465     GLY I   279                                                      
REMARK 465     GLN I   280                                                      
REMARK 465     ASP I   281                                                      
REMARK 465     LYS I   282                                                      
REMARK 465     SER I   283                                                      
REMARK 465     PHE I   284                                                      
REMARK 465     TYR I   285                                                      
REMARK 465     PHE I   286                                                      
REMARK 465     LEU I   287                                                      
REMARK 465     GLU I   288                                                      
REMARK 465     MET I   289                                                      
REMARK 465     ASN I   290                                                      
REMARK 465     THR I   291                                                      
REMARK 465     ARG I   292                                                      
REMARK 465     LEU I   293                                                      
REMARK 465     GLN I   294                                                      
REMARK 465     VAL I   295                                                      
REMARK 465     GLU I   296                                                      
REMARK 465     HIS I   297                                                      
REMARK 465     PRO I   298                                                      
REMARK 465     VAL I   299                                                      
REMARK 465     THR I   300                                                      
REMARK 465     GLU I   301                                                      
REMARK 465     MET I   302                                                      
REMARK 465     ILE I   303                                                      
REMARK 465     THR I   304                                                      
REMARK 465     GLY I   305                                                      
REMARK 465     LEU I   306                                                      
REMARK 465     ASP I   307                                                      
REMARK 465     LEU I   308                                                      
REMARK 465     VAL I   309                                                      
REMARK 465     GLU I   310                                                      
REMARK 465     LEU I   311                                                      
REMARK 465     MET I   312                                                      
REMARK 465     ILE I   313                                                      
REMARK 465     ARG I   314                                                      
REMARK 465     VAL I   315                                                      
REMARK 465     ALA I   316                                                      
REMARK 465     ALA I   317                                                      
REMARK 465     GLY I   318                                                      
REMARK 465     GLU I   319                                                      
REMARK 465     LYS I   320                                                      
REMARK 465     LEU I   321                                                      
REMARK 465     PRO I   322                                                      
REMARK 465     LEU I   323                                                      
REMARK 465     SER I   324                                                      
REMARK 465     GLN I   325                                                      
REMARK 465     ASP I   326                                                      
REMARK 465     GLN I   327                                                      
REMARK 465     VAL I   328                                                      
REMARK 465     LYS I   329                                                      
REMARK 465     LEU I   330                                                      
REMARK 465     ASP I   331                                                      
REMARK 465     GLY I   332                                                      
REMARK 465     TRP I   333                                                      
REMARK 465     ALA I   334                                                      
REMARK 465     VAL I   335                                                      
REMARK 465     GLU I   336                                                      
REMARK 465     SER I   337                                                      
REMARK 465     ARG I   338                                                      
REMARK 465     VAL I   339                                                      
REMARK 465     TYR I   340                                                      
REMARK 465     ALA I   341                                                      
REMARK 465     GLU I   342                                                      
REMARK 465     ASP I   343                                                      
REMARK 465     PRO I   344                                                      
REMARK 465     THR I   345                                                      
REMARK 465     ARG I   346                                                      
REMARK 465     ASN I   347                                                      
REMARK 465     PHE I   348                                                      
REMARK 465     LEU I   349                                                      
REMARK 465     PRO I   350                                                      
REMARK 465     SER I   351                                                      
REMARK 465     ILE I   352                                                      
REMARK 465     GLY I   353                                                      
REMARK 465     ARG I   354                                                      
REMARK 465     LEU I   355                                                      
REMARK 465     THR I   356                                                      
REMARK 465     THR I   357                                                      
REMARK 465     TYR I   358                                                      
REMARK 465     GLN I   359                                                      
REMARK 465     PRO I   360                                                      
REMARK 465     PRO I   361                                                      
REMARK 465     GLU I   362                                                      
REMARK 465     GLU I   363                                                      
REMARK 465     GLY I   364                                                      
REMARK 465     PRO I   365                                                      
REMARK 465     LEU I   366                                                      
REMARK 465     GLY I   367                                                      
REMARK 465     GLY I   368                                                      
REMARK 465     ALA I   369                                                      
REMARK 465     ILE I   370                                                      
REMARK 465     VAL I   371                                                      
REMARK 465     ARG I   372                                                      
REMARK 465     ASN I   373                                                      
REMARK 465     ASP I   374                                                      
REMARK 465     THR I   375                                                      
REMARK 465     GLY I   376                                                      
REMARK 465     VAL I   377                                                      
REMARK 465     GLU I   378                                                      
REMARK 465     GLU I   379                                                      
REMARK 465     GLY I   380                                                      
REMARK 465     GLY I   381                                                      
REMARK 465     GLU I   382                                                      
REMARK 465     ILE I   383                                                      
REMARK 465     ALA I   384                                                      
REMARK 465     ILE I   385                                                      
REMARK 465     HIS I   386                                                      
REMARK 465     TYR I   387                                                      
REMARK 465     ASP I   388                                                      
REMARK 465     PRO I   389                                                      
REMARK 465     MET I   390                                                      
REMARK 465     ILE I   391                                                      
REMARK 465     ALA I   392                                                      
REMARK 465     LYS I   393                                                      
REMARK 465     LEU I   394                                                      
REMARK 465     VAL I   395                                                      
REMARK 465     THR I   396                                                      
REMARK 465     TRP I   397                                                      
REMARK 465     ALA I   398                                                      
REMARK 465     PRO I   399                                                      
REMARK 465     THR I   400                                                      
REMARK 465     ARG I   401                                                      
REMARK 465     LEU I   402                                                      
REMARK 465     GLU I   403                                                      
REMARK 465     ALA I   404                                                      
REMARK 465     ILE I   405                                                      
REMARK 465     GLU I   406                                                      
REMARK 465     ALA I   407                                                      
REMARK 465     GLN I   408                                                      
REMARK 465     ALA I   409                                                      
REMARK 465     THR I   410                                                      
REMARK 465     ALA I   411                                                      
REMARK 465     LEU I   412                                                      
REMARK 465     ASP I   413                                                      
REMARK 465     ALA I   414                                                      
REMARK 465     PHE I   415                                                      
REMARK 465     ALA I   416                                                      
REMARK 465     ILE I   417                                                      
REMARK 465     GLU I   418                                                      
REMARK 465     GLY I   419                                                      
REMARK 465     ILE I   420                                                      
REMARK 465     ARG I   421                                                      
REMARK 465     HIS I   422                                                      
REMARK 465     ASN I   423                                                      
REMARK 465     ILE I   424                                                      
REMARK 465     PRO I   425                                                      
REMARK 465     PHE I   426                                                      
REMARK 465     LEU I   427                                                      
REMARK 465     ALA I   428                                                      
REMARK 465     THR I   429                                                      
REMARK 465     LEU I   430                                                      
REMARK 465     MET I   431                                                      
REMARK 465     ALA I   432                                                      
REMARK 465     HIS I   433                                                      
REMARK 465     PRO I   434                                                      
REMARK 465     ARG I   435                                                      
REMARK 465     TRP I   436                                                      
REMARK 465     ARG I   437                                                      
REMARK 465     ASP I   438                                                      
REMARK 465     GLY I   439                                                      
REMARK 465     ARG I   440                                                      
REMARK 465     LEU I   441                                                      
REMARK 465     SER I   442                                                      
REMARK 465     THR I   443                                                      
REMARK 465     GLY I   444                                                      
REMARK 465     PHE I   445                                                      
REMARK 465     ILE I   446                                                      
REMARK 465     LYS I   447                                                      
REMARK 465     GLU I   448                                                      
REMARK 465     GLU I   449                                                      
REMARK 465     PHE I   450                                                      
REMARK 465     PRO I   451                                                      
REMARK 465     GLU I   452                                                      
REMARK 465     GLY I   453                                                      
REMARK 465     PHE I   454                                                      
REMARK 465     ILE I   455                                                      
REMARK 465     ALA I   456                                                      
REMARK 465     PRO I   457                                                      
REMARK 465     GLU I   458                                                      
REMARK 465     PRO I   459                                                      
REMARK 465     GLU I   460                                                      
REMARK 465     ALA I   667                                                      
REMARK 465     MET J     1                                                      
REMARK 465     PHE J     2                                                      
REMARK 465     ASP J     3                                                      
REMARK 465     LYS J     4                                                      
REMARK 465     ILE J     5                                                      
REMARK 465     LEU J     6                                                      
REMARK 465     ILE J     7                                                      
REMARK 465     ALA J     8                                                      
REMARK 465     ASN J     9                                                      
REMARK 465     ARG J    10                                                      
REMARK 465     GLY J    11                                                      
REMARK 465     GLU J    12                                                      
REMARK 465     ILE J    13                                                      
REMARK 465     ALA J    14                                                      
REMARK 465     CYS J    15                                                      
REMARK 465     ARG J    16                                                      
REMARK 465     ILE J    17                                                      
REMARK 465     ILE J    18                                                      
REMARK 465     LYS J    19                                                      
REMARK 465     THR J    20                                                      
REMARK 465     ALA J    21                                                      
REMARK 465     GLN J    22                                                      
REMARK 465     LYS J    23                                                      
REMARK 465     MET J    24                                                      
REMARK 465     GLY J    25                                                      
REMARK 465     ILE J    26                                                      
REMARK 465     LYS J    27                                                      
REMARK 465     THR J    28                                                      
REMARK 465     VAL J    29                                                      
REMARK 465     ALA J    30                                                      
REMARK 465     VAL J    31                                                      
REMARK 465     TYR J    32                                                      
REMARK 465     SER J    33                                                      
REMARK 465     ASP J    34                                                      
REMARK 465     ALA J    35                                                      
REMARK 465     ASP J    36                                                      
REMARK 465     ARG J    37                                                      
REMARK 465     ASP J    38                                                      
REMARK 465     ALA J    39                                                      
REMARK 465     VAL J    40                                                      
REMARK 465     HIS J    41                                                      
REMARK 465     VAL J    42                                                      
REMARK 465     ALA J    43                                                      
REMARK 465     MET J    44                                                      
REMARK 465     ALA J    45                                                      
REMARK 465     ASP J    46                                                      
REMARK 465     GLU J    47                                                      
REMARK 465     ALA J    48                                                      
REMARK 465     VAL J    49                                                      
REMARK 465     HIS J    50                                                      
REMARK 465     ILE J    51                                                      
REMARK 465     GLY J    52                                                      
REMARK 465     PRO J    53                                                      
REMARK 465     ALA J    54                                                      
REMARK 465     PRO J    55                                                      
REMARK 465     ALA J    56                                                      
REMARK 465     ALA J    57                                                      
REMARK 465     GLN J    58                                                      
REMARK 465     SER J    59                                                      
REMARK 465     TYR J    60                                                      
REMARK 465     LEU J    61                                                      
REMARK 465     LEU J    62                                                      
REMARK 465     ILE J    63                                                      
REMARK 465     GLU J    64                                                      
REMARK 465     LYS J    65                                                      
REMARK 465     ILE J    66                                                      
REMARK 465     ILE J    67                                                      
REMARK 465     ASP J    68                                                      
REMARK 465     ALA J    69                                                      
REMARK 465     CYS J    70                                                      
REMARK 465     LYS J    71                                                      
REMARK 465     GLN J    72                                                      
REMARK 465     THR J    73                                                      
REMARK 465     GLY J    74                                                      
REMARK 465     ALA J    75                                                      
REMARK 465     GLN J    76                                                      
REMARK 465     ALA J    77                                                      
REMARK 465     VAL J    78                                                      
REMARK 465     HIS J    79                                                      
REMARK 465     PRO J    80                                                      
REMARK 465     GLY J    81                                                      
REMARK 465     TYR J    82                                                      
REMARK 465     GLY J    83                                                      
REMARK 465     PHE J    84                                                      
REMARK 465     LEU J    85                                                      
REMARK 465     SER J    86                                                      
REMARK 465     GLU J    87                                                      
REMARK 465     ARG J    88                                                      
REMARK 465     GLU J    89                                                      
REMARK 465     SER J    90                                                      
REMARK 465     PHE J    91                                                      
REMARK 465     PRO J    92                                                      
REMARK 465     LYS J    93                                                      
REMARK 465     ALA J    94                                                      
REMARK 465     LEU J    95                                                      
REMARK 465     ALA J    96                                                      
REMARK 465     GLU J    97                                                      
REMARK 465     ALA J    98                                                      
REMARK 465     GLY J    99                                                      
REMARK 465     ILE J   100                                                      
REMARK 465     VAL J   101                                                      
REMARK 465     PHE J   102                                                      
REMARK 465     ILE J   103                                                      
REMARK 465     GLY J   104                                                      
REMARK 465     PRO J   105                                                      
REMARK 465     ASN J   106                                                      
REMARK 465     PRO J   107                                                      
REMARK 465     GLY J   108                                                      
REMARK 465     ALA J   109                                                      
REMARK 465     ILE J   110                                                      
REMARK 465     ALA J   111                                                      
REMARK 465     ALA J   112                                                      
REMARK 465     MET J   113                                                      
REMARK 465     GLY J   114                                                      
REMARK 465     ASP J   115                                                      
REMARK 465     LYS J   116                                                      
REMARK 465     ILE J   117                                                      
REMARK 465     GLU J   118                                                      
REMARK 465     SER J   119                                                      
REMARK 465     LYS J   120                                                      
REMARK 465     LYS J   121                                                      
REMARK 465     ALA J   122                                                      
REMARK 465     ALA J   123                                                      
REMARK 465     ALA J   124                                                      
REMARK 465     ALA J   125                                                      
REMARK 465     ALA J   126                                                      
REMARK 465     GLU J   127                                                      
REMARK 465     VAL J   128                                                      
REMARK 465     SER J   129                                                      
REMARK 465     THR J   130                                                      
REMARK 465     VAL J   131                                                      
REMARK 465     PRO J   132                                                      
REMARK 465     GLY J   133                                                      
REMARK 465     PHE J   134                                                      
REMARK 465     LEU J   135                                                      
REMARK 465     GLY J   136                                                      
REMARK 465     VAL J   137                                                      
REMARK 465     ILE J   138                                                      
REMARK 465     GLU J   139                                                      
REMARK 465     SER J   140                                                      
REMARK 465     PRO J   141                                                      
REMARK 465     GLU J   142                                                      
REMARK 465     HIS J   143                                                      
REMARK 465     ALA J   144                                                      
REMARK 465     VAL J   145                                                      
REMARK 465     THR J   146                                                      
REMARK 465     ILE J   147                                                      
REMARK 465     ALA J   148                                                      
REMARK 465     ASP J   149                                                      
REMARK 465     GLU J   150                                                      
REMARK 465     ILE J   151                                                      
REMARK 465     GLY J   152                                                      
REMARK 465     TYR J   153                                                      
REMARK 465     PRO J   154                                                      
REMARK 465     VAL J   155                                                      
REMARK 465     MET J   156                                                      
REMARK 465     ILE J   157                                                      
REMARK 465     LYS J   158                                                      
REMARK 465     ALA J   159                                                      
REMARK 465     SER J   160                                                      
REMARK 465     ALA J   161                                                      
REMARK 465     GLY J   162                                                      
REMARK 465     GLY J   163                                                      
REMARK 465     GLY J   164                                                      
REMARK 465     GLY J   165                                                      
REMARK 465     LYS J   166                                                      
REMARK 465     GLY J   167                                                      
REMARK 465     MET J   168                                                      
REMARK 465     ARG J   169                                                      
REMARK 465     ILE J   170                                                      
REMARK 465     ALA J   171                                                      
REMARK 465     GLU J   172                                                      
REMARK 465     SER J   173                                                      
REMARK 465     ALA J   174                                                      
REMARK 465     ASP J   175                                                      
REMARK 465     GLU J   176                                                      
REMARK 465     VAL J   177                                                      
REMARK 465     ALA J   178                                                      
REMARK 465     GLU J   179                                                      
REMARK 465     GLY J   180                                                      
REMARK 465     PHE J   181                                                      
REMARK 465     ALA J   182                                                      
REMARK 465     ARG J   183                                                      
REMARK 465     ALA J   184                                                      
REMARK 465     LYS J   185                                                      
REMARK 465     SER J   186                                                      
REMARK 465     GLU J   187                                                      
REMARK 465     ALA J   188                                                      
REMARK 465     SER J   189                                                      
REMARK 465     SER J   190                                                      
REMARK 465     SER J   191                                                      
REMARK 465     PHE J   192                                                      
REMARK 465     GLY J   193                                                      
REMARK 465     ASP J   194                                                      
REMARK 465     ASP J   195                                                      
REMARK 465     ARG J   196                                                      
REMARK 465     VAL J   197                                                      
REMARK 465     PHE J   198                                                      
REMARK 465     VAL J   199                                                      
REMARK 465     GLU J   200                                                      
REMARK 465     LYS J   201                                                      
REMARK 465     PHE J   202                                                      
REMARK 465     ILE J   203                                                      
REMARK 465     THR J   204                                                      
REMARK 465     ASP J   205                                                      
REMARK 465     PRO J   206                                                      
REMARK 465     ARG J   207                                                      
REMARK 465     HIS J   208                                                      
REMARK 465     ILE J   209                                                      
REMARK 465     GLU J   210                                                      
REMARK 465     ILE J   211                                                      
REMARK 465     GLN J   212                                                      
REMARK 465     VAL J   213                                                      
REMARK 465     ILE J   214                                                      
REMARK 465     GLY J   215                                                      
REMARK 465     ASP J   216                                                      
REMARK 465     LYS J   217                                                      
REMARK 465     HIS J   218                                                      
REMARK 465     GLY J   219                                                      
REMARK 465     ASN J   220                                                      
REMARK 465     VAL J   221                                                      
REMARK 465     ILE J   222                                                      
REMARK 465     TYR J   223                                                      
REMARK 465     LEU J   224                                                      
REMARK 465     GLY J   225                                                      
REMARK 465     GLU J   226                                                      
REMARK 465     ARG J   227                                                      
REMARK 465     GLU J   228                                                      
REMARK 465     CYS J   229                                                      
REMARK 465     SER J   230                                                      
REMARK 465     ILE J   231                                                      
REMARK 465     GLN J   232                                                      
REMARK 465     ARG J   233                                                      
REMARK 465     ARG J   234                                                      
REMARK 465     ASN J   235                                                      
REMARK 465     GLN J   236                                                      
REMARK 465     LYS J   237                                                      
REMARK 465     VAL J   238                                                      
REMARK 465     ILE J   239                                                      
REMARK 465     GLU J   240                                                      
REMARK 465     GLU J   241                                                      
REMARK 465     ALA J   242                                                      
REMARK 465     PRO J   243                                                      
REMARK 465     SER J   244                                                      
REMARK 465     PRO J   245                                                      
REMARK 465     LEU J   246                                                      
REMARK 465     LEU J   247                                                      
REMARK 465     ASP J   248                                                      
REMARK 465     GLU J   249                                                      
REMARK 465     GLU J   250                                                      
REMARK 465     THR J   251                                                      
REMARK 465     ARG J   252                                                      
REMARK 465     ARG J   253                                                      
REMARK 465     LYS J   254                                                      
REMARK 465     MET J   255                                                      
REMARK 465     GLY J   256                                                      
REMARK 465     GLU J   257                                                      
REMARK 465     GLN J   258                                                      
REMARK 465     ALA J   259                                                      
REMARK 465     VAL J   260                                                      
REMARK 465     ALA J   261                                                      
REMARK 465     LEU J   262                                                      
REMARK 465     ALA J   263                                                      
REMARK 465     LYS J   264                                                      
REMARK 465     ALA J   265                                                      
REMARK 465     VAL J   266                                                      
REMARK 465     ASN J   267                                                      
REMARK 465     TYR J   268                                                      
REMARK 465     ASP J   269                                                      
REMARK 465     SER J   270                                                      
REMARK 465     ALA J   271                                                      
REMARK 465     GLY J   272                                                      
REMARK 465     THR J   273                                                      
REMARK 465     VAL J   274                                                      
REMARK 465     GLU J   275                                                      
REMARK 465     PHE J   276                                                      
REMARK 465     VAL J   277                                                      
REMARK 465     ALA J   278                                                      
REMARK 465     GLY J   279                                                      
REMARK 465     GLN J   280                                                      
REMARK 465     ASP J   281                                                      
REMARK 465     LYS J   282                                                      
REMARK 465     SER J   283                                                      
REMARK 465     PHE J   284                                                      
REMARK 465     TYR J   285                                                      
REMARK 465     PHE J   286                                                      
REMARK 465     LEU J   287                                                      
REMARK 465     GLU J   288                                                      
REMARK 465     MET J   289                                                      
REMARK 465     ASN J   290                                                      
REMARK 465     THR J   291                                                      
REMARK 465     ARG J   292                                                      
REMARK 465     LEU J   293                                                      
REMARK 465     GLN J   294                                                      
REMARK 465     VAL J   295                                                      
REMARK 465     GLU J   296                                                      
REMARK 465     HIS J   297                                                      
REMARK 465     PRO J   298                                                      
REMARK 465     VAL J   299                                                      
REMARK 465     THR J   300                                                      
REMARK 465     GLU J   301                                                      
REMARK 465     MET J   302                                                      
REMARK 465     ILE J   303                                                      
REMARK 465     THR J   304                                                      
REMARK 465     GLY J   305                                                      
REMARK 465     LEU J   306                                                      
REMARK 465     ASP J   307                                                      
REMARK 465     LEU J   308                                                      
REMARK 465     VAL J   309                                                      
REMARK 465     GLU J   310                                                      
REMARK 465     LEU J   311                                                      
REMARK 465     MET J   312                                                      
REMARK 465     ILE J   313                                                      
REMARK 465     ARG J   314                                                      
REMARK 465     VAL J   315                                                      
REMARK 465     ALA J   316                                                      
REMARK 465     ALA J   317                                                      
REMARK 465     GLY J   318                                                      
REMARK 465     GLU J   319                                                      
REMARK 465     LYS J   320                                                      
REMARK 465     LEU J   321                                                      
REMARK 465     PRO J   322                                                      
REMARK 465     LEU J   323                                                      
REMARK 465     SER J   324                                                      
REMARK 465     GLN J   325                                                      
REMARK 465     ASP J   326                                                      
REMARK 465     GLN J   327                                                      
REMARK 465     VAL J   328                                                      
REMARK 465     LYS J   329                                                      
REMARK 465     LEU J   330                                                      
REMARK 465     ASP J   331                                                      
REMARK 465     GLY J   332                                                      
REMARK 465     TRP J   333                                                      
REMARK 465     ALA J   334                                                      
REMARK 465     VAL J   335                                                      
REMARK 465     GLU J   336                                                      
REMARK 465     SER J   337                                                      
REMARK 465     ARG J   338                                                      
REMARK 465     VAL J   339                                                      
REMARK 465     TYR J   340                                                      
REMARK 465     ALA J   341                                                      
REMARK 465     GLU J   342                                                      
REMARK 465     ASP J   343                                                      
REMARK 465     PRO J   344                                                      
REMARK 465     THR J   345                                                      
REMARK 465     ARG J   346                                                      
REMARK 465     ASN J   347                                                      
REMARK 465     PHE J   348                                                      
REMARK 465     LEU J   349                                                      
REMARK 465     PRO J   350                                                      
REMARK 465     SER J   351                                                      
REMARK 465     ILE J   352                                                      
REMARK 465     GLY J   353                                                      
REMARK 465     ARG J   354                                                      
REMARK 465     LEU J   355                                                      
REMARK 465     THR J   356                                                      
REMARK 465     THR J   357                                                      
REMARK 465     TYR J   358                                                      
REMARK 465     GLN J   359                                                      
REMARK 465     PRO J   360                                                      
REMARK 465     PRO J   361                                                      
REMARK 465     GLU J   362                                                      
REMARK 465     GLU J   363                                                      
REMARK 465     GLY J   364                                                      
REMARK 465     PRO J   365                                                      
REMARK 465     LEU J   366                                                      
REMARK 465     GLY J   367                                                      
REMARK 465     GLY J   368                                                      
REMARK 465     ALA J   369                                                      
REMARK 465     ILE J   370                                                      
REMARK 465     VAL J   371                                                      
REMARK 465     ARG J   372                                                      
REMARK 465     ASN J   373                                                      
REMARK 465     ASP J   374                                                      
REMARK 465     THR J   375                                                      
REMARK 465     GLY J   376                                                      
REMARK 465     VAL J   377                                                      
REMARK 465     GLU J   378                                                      
REMARK 465     GLU J   379                                                      
REMARK 465     GLY J   380                                                      
REMARK 465     GLY J   381                                                      
REMARK 465     GLU J   382                                                      
REMARK 465     ILE J   383                                                      
REMARK 465     ALA J   384                                                      
REMARK 465     ILE J   385                                                      
REMARK 465     HIS J   386                                                      
REMARK 465     TYR J   387                                                      
REMARK 465     ASP J   388                                                      
REMARK 465     PRO J   389                                                      
REMARK 465     MET J   390                                                      
REMARK 465     ILE J   391                                                      
REMARK 465     ALA J   392                                                      
REMARK 465     LYS J   393                                                      
REMARK 465     LEU J   394                                                      
REMARK 465     VAL J   395                                                      
REMARK 465     THR J   396                                                      
REMARK 465     TRP J   397                                                      
REMARK 465     ALA J   398                                                      
REMARK 465     PRO J   399                                                      
REMARK 465     THR J   400                                                      
REMARK 465     ARG J   401                                                      
REMARK 465     LEU J   402                                                      
REMARK 465     GLU J   403                                                      
REMARK 465     ALA J   404                                                      
REMARK 465     ILE J   405                                                      
REMARK 465     GLU J   406                                                      
REMARK 465     ALA J   407                                                      
REMARK 465     GLN J   408                                                      
REMARK 465     ALA J   409                                                      
REMARK 465     THR J   410                                                      
REMARK 465     ALA J   411                                                      
REMARK 465     LEU J   412                                                      
REMARK 465     ASP J   413                                                      
REMARK 465     ALA J   414                                                      
REMARK 465     PHE J   415                                                      
REMARK 465     ALA J   416                                                      
REMARK 465     ILE J   417                                                      
REMARK 465     GLU J   418                                                      
REMARK 465     GLY J   419                                                      
REMARK 465     ILE J   420                                                      
REMARK 465     ARG J   421                                                      
REMARK 465     HIS J   422                                                      
REMARK 465     ASN J   423                                                      
REMARK 465     ILE J   424                                                      
REMARK 465     PRO J   425                                                      
REMARK 465     PHE J   426                                                      
REMARK 465     LEU J   427                                                      
REMARK 465     ALA J   428                                                      
REMARK 465     THR J   429                                                      
REMARK 465     LEU J   430                                                      
REMARK 465     MET J   431                                                      
REMARK 465     ALA J   432                                                      
REMARK 465     HIS J   433                                                      
REMARK 465     PRO J   434                                                      
REMARK 465     ARG J   435                                                      
REMARK 465     TRP J   436                                                      
REMARK 465     ARG J   437                                                      
REMARK 465     ASP J   438                                                      
REMARK 465     GLY J   439                                                      
REMARK 465     ARG J   440                                                      
REMARK 465     LEU J   441                                                      
REMARK 465     SER J   442                                                      
REMARK 465     THR J   443                                                      
REMARK 465     GLY J   444                                                      
REMARK 465     PHE J   445                                                      
REMARK 465     ILE J   446                                                      
REMARK 465     LYS J   447                                                      
REMARK 465     GLU J   448                                                      
REMARK 465     GLU J   449                                                      
REMARK 465     PHE J   450                                                      
REMARK 465     PRO J   451                                                      
REMARK 465     GLU J   452                                                      
REMARK 465     GLY J   453                                                      
REMARK 465     PHE J   454                                                      
REMARK 465     ILE J   455                                                      
REMARK 465     ALA J   456                                                      
REMARK 465     ALA J   667                                                      
REMARK 465     MET K     1                                                      
REMARK 465     PHE K     2                                                      
REMARK 465     ASP K     3                                                      
REMARK 465     LYS K     4                                                      
REMARK 465     ILE K     5                                                      
REMARK 465     LEU K     6                                                      
REMARK 465     ILE K     7                                                      
REMARK 465     ALA K     8                                                      
REMARK 465     ASN K     9                                                      
REMARK 465     ARG K    10                                                      
REMARK 465     GLY K    11                                                      
REMARK 465     GLU K    12                                                      
REMARK 465     ILE K    13                                                      
REMARK 465     ALA K    14                                                      
REMARK 465     CYS K    15                                                      
REMARK 465     ARG K    16                                                      
REMARK 465     ILE K    17                                                      
REMARK 465     ILE K    18                                                      
REMARK 465     LYS K    19                                                      
REMARK 465     THR K    20                                                      
REMARK 465     ALA K    21                                                      
REMARK 465     GLN K    22                                                      
REMARK 465     LYS K    23                                                      
REMARK 465     MET K    24                                                      
REMARK 465     GLY K    25                                                      
REMARK 465     ILE K    26                                                      
REMARK 465     LYS K    27                                                      
REMARK 465     THR K    28                                                      
REMARK 465     VAL K    29                                                      
REMARK 465     ALA K    30                                                      
REMARK 465     VAL K    31                                                      
REMARK 465     TYR K    32                                                      
REMARK 465     SER K    33                                                      
REMARK 465     ASP K    34                                                      
REMARK 465     ALA K    35                                                      
REMARK 465     ASP K    36                                                      
REMARK 465     ARG K    37                                                      
REMARK 465     ASP K    38                                                      
REMARK 465     ALA K    39                                                      
REMARK 465     VAL K    40                                                      
REMARK 465     HIS K    41                                                      
REMARK 465     VAL K    42                                                      
REMARK 465     ALA K    43                                                      
REMARK 465     MET K    44                                                      
REMARK 465     ALA K    45                                                      
REMARK 465     ASP K    46                                                      
REMARK 465     GLU K    47                                                      
REMARK 465     ALA K    48                                                      
REMARK 465     VAL K    49                                                      
REMARK 465     HIS K    50                                                      
REMARK 465     ILE K    51                                                      
REMARK 465     GLY K    52                                                      
REMARK 465     PRO K    53                                                      
REMARK 465     ALA K    54                                                      
REMARK 465     PRO K    55                                                      
REMARK 465     ALA K    56                                                      
REMARK 465     ALA K    57                                                      
REMARK 465     GLN K    58                                                      
REMARK 465     SER K    59                                                      
REMARK 465     TYR K    60                                                      
REMARK 465     LEU K    61                                                      
REMARK 465     LEU K    62                                                      
REMARK 465     ILE K    63                                                      
REMARK 465     GLU K    64                                                      
REMARK 465     LYS K    65                                                      
REMARK 465     ILE K    66                                                      
REMARK 465     ILE K    67                                                      
REMARK 465     ASP K    68                                                      
REMARK 465     ALA K    69                                                      
REMARK 465     CYS K    70                                                      
REMARK 465     LYS K    71                                                      
REMARK 465     GLN K    72                                                      
REMARK 465     THR K    73                                                      
REMARK 465     GLY K    74                                                      
REMARK 465     ALA K    75                                                      
REMARK 465     GLN K    76                                                      
REMARK 465     ALA K    77                                                      
REMARK 465     VAL K    78                                                      
REMARK 465     HIS K    79                                                      
REMARK 465     PRO K    80                                                      
REMARK 465     GLY K    81                                                      
REMARK 465     TYR K    82                                                      
REMARK 465     GLY K    83                                                      
REMARK 465     PHE K    84                                                      
REMARK 465     LEU K    85                                                      
REMARK 465     SER K    86                                                      
REMARK 465     GLU K    87                                                      
REMARK 465     ARG K    88                                                      
REMARK 465     GLU K    89                                                      
REMARK 465     SER K    90                                                      
REMARK 465     PHE K    91                                                      
REMARK 465     PRO K    92                                                      
REMARK 465     LYS K    93                                                      
REMARK 465     ALA K    94                                                      
REMARK 465     LEU K    95                                                      
REMARK 465     ALA K    96                                                      
REMARK 465     GLU K    97                                                      
REMARK 465     ALA K    98                                                      
REMARK 465     GLY K    99                                                      
REMARK 465     ILE K   100                                                      
REMARK 465     VAL K   101                                                      
REMARK 465     PHE K   102                                                      
REMARK 465     ILE K   103                                                      
REMARK 465     GLY K   104                                                      
REMARK 465     PRO K   105                                                      
REMARK 465     ASN K   106                                                      
REMARK 465     PRO K   107                                                      
REMARK 465     GLY K   108                                                      
REMARK 465     ALA K   109                                                      
REMARK 465     ILE K   110                                                      
REMARK 465     ALA K   111                                                      
REMARK 465     ALA K   112                                                      
REMARK 465     MET K   113                                                      
REMARK 465     GLY K   114                                                      
REMARK 465     ASP K   115                                                      
REMARK 465     LYS K   116                                                      
REMARK 465     ILE K   117                                                      
REMARK 465     GLU K   118                                                      
REMARK 465     SER K   119                                                      
REMARK 465     LYS K   120                                                      
REMARK 465     LYS K   121                                                      
REMARK 465     ALA K   122                                                      
REMARK 465     ALA K   123                                                      
REMARK 465     ALA K   124                                                      
REMARK 465     ALA K   125                                                      
REMARK 465     ALA K   126                                                      
REMARK 465     GLU K   127                                                      
REMARK 465     VAL K   128                                                      
REMARK 465     SER K   129                                                      
REMARK 465     THR K   130                                                      
REMARK 465     VAL K   131                                                      
REMARK 465     PRO K   132                                                      
REMARK 465     GLY K   133                                                      
REMARK 465     PHE K   134                                                      
REMARK 465     LEU K   135                                                      
REMARK 465     GLY K   136                                                      
REMARK 465     VAL K   137                                                      
REMARK 465     ILE K   138                                                      
REMARK 465     GLU K   139                                                      
REMARK 465     SER K   140                                                      
REMARK 465     PRO K   141                                                      
REMARK 465     GLU K   142                                                      
REMARK 465     HIS K   143                                                      
REMARK 465     ALA K   144                                                      
REMARK 465     VAL K   145                                                      
REMARK 465     THR K   146                                                      
REMARK 465     ILE K   147                                                      
REMARK 465     ALA K   148                                                      
REMARK 465     ASP K   149                                                      
REMARK 465     GLU K   150                                                      
REMARK 465     ILE K   151                                                      
REMARK 465     GLY K   152                                                      
REMARK 465     TYR K   153                                                      
REMARK 465     PRO K   154                                                      
REMARK 465     VAL K   155                                                      
REMARK 465     MET K   156                                                      
REMARK 465     ILE K   157                                                      
REMARK 465     LYS K   158                                                      
REMARK 465     ALA K   159                                                      
REMARK 465     SER K   160                                                      
REMARK 465     ALA K   161                                                      
REMARK 465     GLY K   162                                                      
REMARK 465     GLY K   163                                                      
REMARK 465     GLY K   164                                                      
REMARK 465     GLY K   165                                                      
REMARK 465     LYS K   166                                                      
REMARK 465     GLY K   167                                                      
REMARK 465     MET K   168                                                      
REMARK 465     ARG K   169                                                      
REMARK 465     ILE K   170                                                      
REMARK 465     ALA K   171                                                      
REMARK 465     GLU K   172                                                      
REMARK 465     SER K   173                                                      
REMARK 465     ALA K   174                                                      
REMARK 465     ASP K   175                                                      
REMARK 465     GLU K   176                                                      
REMARK 465     VAL K   177                                                      
REMARK 465     ALA K   178                                                      
REMARK 465     GLU K   179                                                      
REMARK 465     GLY K   180                                                      
REMARK 465     PHE K   181                                                      
REMARK 465     ALA K   182                                                      
REMARK 465     ARG K   183                                                      
REMARK 465     ALA K   184                                                      
REMARK 465     LYS K   185                                                      
REMARK 465     SER K   186                                                      
REMARK 465     GLU K   187                                                      
REMARK 465     ALA K   188                                                      
REMARK 465     SER K   189                                                      
REMARK 465     SER K   190                                                      
REMARK 465     SER K   191                                                      
REMARK 465     PHE K   192                                                      
REMARK 465     GLY K   193                                                      
REMARK 465     ASP K   194                                                      
REMARK 465     ASP K   195                                                      
REMARK 465     ARG K   196                                                      
REMARK 465     VAL K   197                                                      
REMARK 465     PHE K   198                                                      
REMARK 465     VAL K   199                                                      
REMARK 465     GLU K   200                                                      
REMARK 465     LYS K   201                                                      
REMARK 465     PHE K   202                                                      
REMARK 465     ILE K   203                                                      
REMARK 465     THR K   204                                                      
REMARK 465     ASP K   205                                                      
REMARK 465     PRO K   206                                                      
REMARK 465     ARG K   207                                                      
REMARK 465     HIS K   208                                                      
REMARK 465     ILE K   209                                                      
REMARK 465     GLU K   210                                                      
REMARK 465     ILE K   211                                                      
REMARK 465     GLN K   212                                                      
REMARK 465     VAL K   213                                                      
REMARK 465     ILE K   214                                                      
REMARK 465     GLY K   215                                                      
REMARK 465     ASP K   216                                                      
REMARK 465     LYS K   217                                                      
REMARK 465     HIS K   218                                                      
REMARK 465     GLY K   219                                                      
REMARK 465     ASN K   220                                                      
REMARK 465     VAL K   221                                                      
REMARK 465     ILE K   222                                                      
REMARK 465     TYR K   223                                                      
REMARK 465     LEU K   224                                                      
REMARK 465     GLY K   225                                                      
REMARK 465     GLU K   226                                                      
REMARK 465     ARG K   227                                                      
REMARK 465     GLU K   228                                                      
REMARK 465     CYS K   229                                                      
REMARK 465     SER K   230                                                      
REMARK 465     ILE K   231                                                      
REMARK 465     GLN K   232                                                      
REMARK 465     ARG K   233                                                      
REMARK 465     ARG K   234                                                      
REMARK 465     ASN K   235                                                      
REMARK 465     GLN K   236                                                      
REMARK 465     LYS K   237                                                      
REMARK 465     VAL K   238                                                      
REMARK 465     ILE K   239                                                      
REMARK 465     GLU K   240                                                      
REMARK 465     GLU K   241                                                      
REMARK 465     ALA K   242                                                      
REMARK 465     PRO K   243                                                      
REMARK 465     SER K   244                                                      
REMARK 465     PRO K   245                                                      
REMARK 465     LEU K   246                                                      
REMARK 465     LEU K   247                                                      
REMARK 465     ASP K   248                                                      
REMARK 465     GLU K   249                                                      
REMARK 465     GLU K   250                                                      
REMARK 465     THR K   251                                                      
REMARK 465     ARG K   252                                                      
REMARK 465     ARG K   253                                                      
REMARK 465     LYS K   254                                                      
REMARK 465     MET K   255                                                      
REMARK 465     GLY K   256                                                      
REMARK 465     GLU K   257                                                      
REMARK 465     GLN K   258                                                      
REMARK 465     ALA K   259                                                      
REMARK 465     VAL K   260                                                      
REMARK 465     ALA K   261                                                      
REMARK 465     LEU K   262                                                      
REMARK 465     ALA K   263                                                      
REMARK 465     LYS K   264                                                      
REMARK 465     ALA K   265                                                      
REMARK 465     VAL K   266                                                      
REMARK 465     ASN K   267                                                      
REMARK 465     TYR K   268                                                      
REMARK 465     ASP K   269                                                      
REMARK 465     SER K   270                                                      
REMARK 465     ALA K   271                                                      
REMARK 465     GLY K   272                                                      
REMARK 465     THR K   273                                                      
REMARK 465     VAL K   274                                                      
REMARK 465     GLU K   275                                                      
REMARK 465     PHE K   276                                                      
REMARK 465     VAL K   277                                                      
REMARK 465     ALA K   278                                                      
REMARK 465     GLY K   279                                                      
REMARK 465     GLN K   280                                                      
REMARK 465     ASP K   281                                                      
REMARK 465     LYS K   282                                                      
REMARK 465     SER K   283                                                      
REMARK 465     PHE K   284                                                      
REMARK 465     TYR K   285                                                      
REMARK 465     PHE K   286                                                      
REMARK 465     LEU K   287                                                      
REMARK 465     GLU K   288                                                      
REMARK 465     MET K   289                                                      
REMARK 465     ASN K   290                                                      
REMARK 465     THR K   291                                                      
REMARK 465     ARG K   292                                                      
REMARK 465     LEU K   293                                                      
REMARK 465     GLN K   294                                                      
REMARK 465     VAL K   295                                                      
REMARK 465     GLU K   296                                                      
REMARK 465     HIS K   297                                                      
REMARK 465     PRO K   298                                                      
REMARK 465     VAL K   299                                                      
REMARK 465     THR K   300                                                      
REMARK 465     GLU K   301                                                      
REMARK 465     MET K   302                                                      
REMARK 465     ILE K   303                                                      
REMARK 465     THR K   304                                                      
REMARK 465     GLY K   305                                                      
REMARK 465     LEU K   306                                                      
REMARK 465     ASP K   307                                                      
REMARK 465     LEU K   308                                                      
REMARK 465     VAL K   309                                                      
REMARK 465     GLU K   310                                                      
REMARK 465     LEU K   311                                                      
REMARK 465     MET K   312                                                      
REMARK 465     ILE K   313                                                      
REMARK 465     ARG K   314                                                      
REMARK 465     VAL K   315                                                      
REMARK 465     ALA K   316                                                      
REMARK 465     ALA K   317                                                      
REMARK 465     GLY K   318                                                      
REMARK 465     GLU K   319                                                      
REMARK 465     LYS K   320                                                      
REMARK 465     LEU K   321                                                      
REMARK 465     PRO K   322                                                      
REMARK 465     LEU K   323                                                      
REMARK 465     SER K   324                                                      
REMARK 465     GLN K   325                                                      
REMARK 465     ASP K   326                                                      
REMARK 465     GLN K   327                                                      
REMARK 465     VAL K   328                                                      
REMARK 465     LYS K   329                                                      
REMARK 465     LEU K   330                                                      
REMARK 465     ASP K   331                                                      
REMARK 465     GLY K   332                                                      
REMARK 465     TRP K   333                                                      
REMARK 465     ALA K   334                                                      
REMARK 465     VAL K   335                                                      
REMARK 465     GLU K   336                                                      
REMARK 465     SER K   337                                                      
REMARK 465     ARG K   338                                                      
REMARK 465     VAL K   339                                                      
REMARK 465     TYR K   340                                                      
REMARK 465     ALA K   341                                                      
REMARK 465     GLU K   342                                                      
REMARK 465     ASP K   343                                                      
REMARK 465     PRO K   344                                                      
REMARK 465     THR K   345                                                      
REMARK 465     ARG K   346                                                      
REMARK 465     ASN K   347                                                      
REMARK 465     PHE K   348                                                      
REMARK 465     LEU K   349                                                      
REMARK 465     PRO K   350                                                      
REMARK 465     SER K   351                                                      
REMARK 465     ILE K   352                                                      
REMARK 465     GLY K   353                                                      
REMARK 465     ARG K   354                                                      
REMARK 465     LEU K   355                                                      
REMARK 465     THR K   356                                                      
REMARK 465     THR K   357                                                      
REMARK 465     TYR K   358                                                      
REMARK 465     GLN K   359                                                      
REMARK 465     PRO K   360                                                      
REMARK 465     PRO K   361                                                      
REMARK 465     GLU K   362                                                      
REMARK 465     GLU K   363                                                      
REMARK 465     GLY K   364                                                      
REMARK 465     PRO K   365                                                      
REMARK 465     LEU K   366                                                      
REMARK 465     GLY K   367                                                      
REMARK 465     GLY K   368                                                      
REMARK 465     ALA K   369                                                      
REMARK 465     ILE K   370                                                      
REMARK 465     VAL K   371                                                      
REMARK 465     ARG K   372                                                      
REMARK 465     ASN K   373                                                      
REMARK 465     ASP K   374                                                      
REMARK 465     THR K   375                                                      
REMARK 465     GLY K   376                                                      
REMARK 465     VAL K   377                                                      
REMARK 465     GLU K   378                                                      
REMARK 465     GLU K   379                                                      
REMARK 465     GLY K   380                                                      
REMARK 465     GLY K   381                                                      
REMARK 465     GLU K   382                                                      
REMARK 465     ILE K   383                                                      
REMARK 465     ALA K   384                                                      
REMARK 465     ILE K   385                                                      
REMARK 465     HIS K   386                                                      
REMARK 465     TYR K   387                                                      
REMARK 465     ASP K   388                                                      
REMARK 465     PRO K   389                                                      
REMARK 465     MET K   390                                                      
REMARK 465     ILE K   391                                                      
REMARK 465     ALA K   392                                                      
REMARK 465     LYS K   393                                                      
REMARK 465     LEU K   394                                                      
REMARK 465     VAL K   395                                                      
REMARK 465     THR K   396                                                      
REMARK 465     TRP K   397                                                      
REMARK 465     ALA K   398                                                      
REMARK 465     PRO K   399                                                      
REMARK 465     THR K   400                                                      
REMARK 465     ARG K   401                                                      
REMARK 465     LEU K   402                                                      
REMARK 465     GLU K   403                                                      
REMARK 465     ALA K   404                                                      
REMARK 465     ILE K   405                                                      
REMARK 465     GLU K   406                                                      
REMARK 465     ALA K   407                                                      
REMARK 465     GLN K   408                                                      
REMARK 465     ALA K   409                                                      
REMARK 465     THR K   410                                                      
REMARK 465     ALA K   411                                                      
REMARK 465     LEU K   412                                                      
REMARK 465     ASP K   413                                                      
REMARK 465     ALA K   414                                                      
REMARK 465     PHE K   415                                                      
REMARK 465     ALA K   416                                                      
REMARK 465     ILE K   417                                                      
REMARK 465     GLU K   418                                                      
REMARK 465     GLY K   419                                                      
REMARK 465     ILE K   420                                                      
REMARK 465     ARG K   421                                                      
REMARK 465     HIS K   422                                                      
REMARK 465     ASN K   423                                                      
REMARK 465     ILE K   424                                                      
REMARK 465     PRO K   425                                                      
REMARK 465     PHE K   426                                                      
REMARK 465     LEU K   427                                                      
REMARK 465     ALA K   428                                                      
REMARK 465     THR K   429                                                      
REMARK 465     LEU K   430                                                      
REMARK 465     MET K   431                                                      
REMARK 465     ALA K   432                                                      
REMARK 465     HIS K   433                                                      
REMARK 465     PRO K   434                                                      
REMARK 465     ARG K   435                                                      
REMARK 465     TRP K   436                                                      
REMARK 465     ARG K   437                                                      
REMARK 465     ASP K   438                                                      
REMARK 465     GLY K   439                                                      
REMARK 465     ARG K   440                                                      
REMARK 465     LEU K   441                                                      
REMARK 465     SER K   442                                                      
REMARK 465     THR K   443                                                      
REMARK 465     GLY K   444                                                      
REMARK 465     PHE K   445                                                      
REMARK 465     ILE K   446                                                      
REMARK 465     LYS K   447                                                      
REMARK 465     GLU K   448                                                      
REMARK 465     GLU K   449                                                      
REMARK 465     PHE K   450                                                      
REMARK 465     PRO K   451                                                      
REMARK 465     GLU K   452                                                      
REMARK 465     GLY K   453                                                      
REMARK 465     PHE K   454                                                      
REMARK 465     ILE K   455                                                      
REMARK 465     ALA K   456                                                      
REMARK 465     PRO K   457                                                      
REMARK 465     ALA K   667                                                      
REMARK 465     MET L     1                                                      
REMARK 465     PHE L     2                                                      
REMARK 465     ASP L     3                                                      
REMARK 465     LYS L     4                                                      
REMARK 465     ILE L     5                                                      
REMARK 465     LEU L     6                                                      
REMARK 465     ILE L     7                                                      
REMARK 465     ALA L     8                                                      
REMARK 465     ASN L     9                                                      
REMARK 465     ARG L    10                                                      
REMARK 465     GLY L    11                                                      
REMARK 465     GLU L    12                                                      
REMARK 465     ILE L    13                                                      
REMARK 465     ALA L    14                                                      
REMARK 465     CYS L    15                                                      
REMARK 465     ARG L    16                                                      
REMARK 465     ILE L    17                                                      
REMARK 465     ILE L    18                                                      
REMARK 465     LYS L    19                                                      
REMARK 465     THR L    20                                                      
REMARK 465     ALA L    21                                                      
REMARK 465     GLN L    22                                                      
REMARK 465     LYS L    23                                                      
REMARK 465     MET L    24                                                      
REMARK 465     GLY L    25                                                      
REMARK 465     ILE L    26                                                      
REMARK 465     LYS L    27                                                      
REMARK 465     THR L    28                                                      
REMARK 465     VAL L    29                                                      
REMARK 465     ALA L    30                                                      
REMARK 465     VAL L    31                                                      
REMARK 465     TYR L    32                                                      
REMARK 465     SER L    33                                                      
REMARK 465     ASP L    34                                                      
REMARK 465     ALA L    35                                                      
REMARK 465     ASP L    36                                                      
REMARK 465     ARG L    37                                                      
REMARK 465     ASP L    38                                                      
REMARK 465     ALA L    39                                                      
REMARK 465     VAL L    40                                                      
REMARK 465     HIS L    41                                                      
REMARK 465     VAL L    42                                                      
REMARK 465     ALA L    43                                                      
REMARK 465     MET L    44                                                      
REMARK 465     ALA L    45                                                      
REMARK 465     ASP L    46                                                      
REMARK 465     GLU L    47                                                      
REMARK 465     ALA L    48                                                      
REMARK 465     VAL L    49                                                      
REMARK 465     HIS L    50                                                      
REMARK 465     ILE L    51                                                      
REMARK 465     GLY L    52                                                      
REMARK 465     PRO L    53                                                      
REMARK 465     ALA L    54                                                      
REMARK 465     PRO L    55                                                      
REMARK 465     ALA L    56                                                      
REMARK 465     ALA L    57                                                      
REMARK 465     GLN L    58                                                      
REMARK 465     SER L    59                                                      
REMARK 465     TYR L    60                                                      
REMARK 465     LEU L    61                                                      
REMARK 465     LEU L    62                                                      
REMARK 465     ILE L    63                                                      
REMARK 465     GLU L    64                                                      
REMARK 465     LYS L    65                                                      
REMARK 465     ILE L    66                                                      
REMARK 465     ILE L    67                                                      
REMARK 465     ASP L    68                                                      
REMARK 465     ALA L    69                                                      
REMARK 465     CYS L    70                                                      
REMARK 465     LYS L    71                                                      
REMARK 465     GLN L    72                                                      
REMARK 465     THR L    73                                                      
REMARK 465     GLY L    74                                                      
REMARK 465     ALA L    75                                                      
REMARK 465     GLN L    76                                                      
REMARK 465     ALA L    77                                                      
REMARK 465     VAL L    78                                                      
REMARK 465     HIS L    79                                                      
REMARK 465     PRO L    80                                                      
REMARK 465     GLY L    81                                                      
REMARK 465     TYR L    82                                                      
REMARK 465     GLY L    83                                                      
REMARK 465     PHE L    84                                                      
REMARK 465     LEU L    85                                                      
REMARK 465     SER L    86                                                      
REMARK 465     GLU L    87                                                      
REMARK 465     ARG L    88                                                      
REMARK 465     GLU L    89                                                      
REMARK 465     SER L    90                                                      
REMARK 465     PHE L    91                                                      
REMARK 465     PRO L    92                                                      
REMARK 465     LYS L    93                                                      
REMARK 465     ALA L    94                                                      
REMARK 465     LEU L    95                                                      
REMARK 465     ALA L    96                                                      
REMARK 465     GLU L    97                                                      
REMARK 465     ALA L    98                                                      
REMARK 465     GLY L    99                                                      
REMARK 465     ILE L   100                                                      
REMARK 465     VAL L   101                                                      
REMARK 465     PHE L   102                                                      
REMARK 465     ILE L   103                                                      
REMARK 465     GLY L   104                                                      
REMARK 465     PRO L   105                                                      
REMARK 465     ASN L   106                                                      
REMARK 465     PRO L   107                                                      
REMARK 465     GLY L   108                                                      
REMARK 465     ALA L   109                                                      
REMARK 465     ILE L   110                                                      
REMARK 465     ALA L   111                                                      
REMARK 465     ALA L   112                                                      
REMARK 465     MET L   113                                                      
REMARK 465     GLY L   114                                                      
REMARK 465     ASP L   115                                                      
REMARK 465     LYS L   116                                                      
REMARK 465     ILE L   117                                                      
REMARK 465     GLU L   118                                                      
REMARK 465     SER L   119                                                      
REMARK 465     LYS L   120                                                      
REMARK 465     LYS L   121                                                      
REMARK 465     ALA L   122                                                      
REMARK 465     ALA L   123                                                      
REMARK 465     ALA L   124                                                      
REMARK 465     ALA L   125                                                      
REMARK 465     ALA L   126                                                      
REMARK 465     GLU L   127                                                      
REMARK 465     VAL L   128                                                      
REMARK 465     SER L   129                                                      
REMARK 465     THR L   130                                                      
REMARK 465     VAL L   131                                                      
REMARK 465     PRO L   132                                                      
REMARK 465     GLY L   133                                                      
REMARK 465     PHE L   134                                                      
REMARK 465     LEU L   135                                                      
REMARK 465     GLY L   136                                                      
REMARK 465     VAL L   137                                                      
REMARK 465     ILE L   138                                                      
REMARK 465     GLU L   139                                                      
REMARK 465     SER L   140                                                      
REMARK 465     PRO L   141                                                      
REMARK 465     GLU L   142                                                      
REMARK 465     HIS L   143                                                      
REMARK 465     ALA L   144                                                      
REMARK 465     VAL L   145                                                      
REMARK 465     THR L   146                                                      
REMARK 465     ILE L   147                                                      
REMARK 465     ALA L   148                                                      
REMARK 465     ASP L   149                                                      
REMARK 465     GLU L   150                                                      
REMARK 465     ILE L   151                                                      
REMARK 465     GLY L   152                                                      
REMARK 465     TYR L   153                                                      
REMARK 465     PRO L   154                                                      
REMARK 465     VAL L   155                                                      
REMARK 465     MET L   156                                                      
REMARK 465     ILE L   157                                                      
REMARK 465     LYS L   158                                                      
REMARK 465     ALA L   159                                                      
REMARK 465     SER L   160                                                      
REMARK 465     ALA L   161                                                      
REMARK 465     GLY L   162                                                      
REMARK 465     GLY L   163                                                      
REMARK 465     GLY L   164                                                      
REMARK 465     GLY L   165                                                      
REMARK 465     LYS L   166                                                      
REMARK 465     GLY L   167                                                      
REMARK 465     MET L   168                                                      
REMARK 465     ARG L   169                                                      
REMARK 465     ILE L   170                                                      
REMARK 465     ALA L   171                                                      
REMARK 465     GLU L   172                                                      
REMARK 465     SER L   173                                                      
REMARK 465     ALA L   174                                                      
REMARK 465     ASP L   175                                                      
REMARK 465     GLU L   176                                                      
REMARK 465     VAL L   177                                                      
REMARK 465     ALA L   178                                                      
REMARK 465     GLU L   179                                                      
REMARK 465     GLY L   180                                                      
REMARK 465     PHE L   181                                                      
REMARK 465     ALA L   182                                                      
REMARK 465     ARG L   183                                                      
REMARK 465     ALA L   184                                                      
REMARK 465     LYS L   185                                                      
REMARK 465     SER L   186                                                      
REMARK 465     GLU L   187                                                      
REMARK 465     ALA L   188                                                      
REMARK 465     SER L   189                                                      
REMARK 465     SER L   190                                                      
REMARK 465     SER L   191                                                      
REMARK 465     PHE L   192                                                      
REMARK 465     GLY L   193                                                      
REMARK 465     ASP L   194                                                      
REMARK 465     ASP L   195                                                      
REMARK 465     ARG L   196                                                      
REMARK 465     VAL L   197                                                      
REMARK 465     PHE L   198                                                      
REMARK 465     VAL L   199                                                      
REMARK 465     GLU L   200                                                      
REMARK 465     LYS L   201                                                      
REMARK 465     PHE L   202                                                      
REMARK 465     ILE L   203                                                      
REMARK 465     THR L   204                                                      
REMARK 465     ASP L   205                                                      
REMARK 465     PRO L   206                                                      
REMARK 465     ARG L   207                                                      
REMARK 465     HIS L   208                                                      
REMARK 465     ILE L   209                                                      
REMARK 465     GLU L   210                                                      
REMARK 465     ILE L   211                                                      
REMARK 465     GLN L   212                                                      
REMARK 465     VAL L   213                                                      
REMARK 465     ILE L   214                                                      
REMARK 465     GLY L   215                                                      
REMARK 465     ASP L   216                                                      
REMARK 465     LYS L   217                                                      
REMARK 465     HIS L   218                                                      
REMARK 465     GLY L   219                                                      
REMARK 465     ASN L   220                                                      
REMARK 465     VAL L   221                                                      
REMARK 465     ILE L   222                                                      
REMARK 465     TYR L   223                                                      
REMARK 465     LEU L   224                                                      
REMARK 465     GLY L   225                                                      
REMARK 465     GLU L   226                                                      
REMARK 465     ARG L   227                                                      
REMARK 465     GLU L   228                                                      
REMARK 465     CYS L   229                                                      
REMARK 465     SER L   230                                                      
REMARK 465     ILE L   231                                                      
REMARK 465     GLN L   232                                                      
REMARK 465     ARG L   233                                                      
REMARK 465     ARG L   234                                                      
REMARK 465     ASN L   235                                                      
REMARK 465     GLN L   236                                                      
REMARK 465     LYS L   237                                                      
REMARK 465     VAL L   238                                                      
REMARK 465     ILE L   239                                                      
REMARK 465     GLU L   240                                                      
REMARK 465     GLU L   241                                                      
REMARK 465     ALA L   242                                                      
REMARK 465     PRO L   243                                                      
REMARK 465     SER L   244                                                      
REMARK 465     PRO L   245                                                      
REMARK 465     LEU L   246                                                      
REMARK 465     LEU L   247                                                      
REMARK 465     ASP L   248                                                      
REMARK 465     GLU L   249                                                      
REMARK 465     GLU L   250                                                      
REMARK 465     THR L   251                                                      
REMARK 465     ARG L   252                                                      
REMARK 465     ARG L   253                                                      
REMARK 465     LYS L   254                                                      
REMARK 465     MET L   255                                                      
REMARK 465     GLY L   256                                                      
REMARK 465     GLU L   257                                                      
REMARK 465     GLN L   258                                                      
REMARK 465     ALA L   259                                                      
REMARK 465     VAL L   260                                                      
REMARK 465     ALA L   261                                                      
REMARK 465     LEU L   262                                                      
REMARK 465     ALA L   263                                                      
REMARK 465     LYS L   264                                                      
REMARK 465     ALA L   265                                                      
REMARK 465     VAL L   266                                                      
REMARK 465     ASN L   267                                                      
REMARK 465     TYR L   268                                                      
REMARK 465     ASP L   269                                                      
REMARK 465     SER L   270                                                      
REMARK 465     ALA L   271                                                      
REMARK 465     GLY L   272                                                      
REMARK 465     THR L   273                                                      
REMARK 465     VAL L   274                                                      
REMARK 465     GLU L   275                                                      
REMARK 465     PHE L   276                                                      
REMARK 465     VAL L   277                                                      
REMARK 465     ALA L   278                                                      
REMARK 465     GLY L   279                                                      
REMARK 465     GLN L   280                                                      
REMARK 465     ASP L   281                                                      
REMARK 465     LYS L   282                                                      
REMARK 465     SER L   283                                                      
REMARK 465     PHE L   284                                                      
REMARK 465     TYR L   285                                                      
REMARK 465     PHE L   286                                                      
REMARK 465     LEU L   287                                                      
REMARK 465     GLU L   288                                                      
REMARK 465     MET L   289                                                      
REMARK 465     ASN L   290                                                      
REMARK 465     THR L   291                                                      
REMARK 465     ARG L   292                                                      
REMARK 465     LEU L   293                                                      
REMARK 465     GLN L   294                                                      
REMARK 465     VAL L   295                                                      
REMARK 465     GLU L   296                                                      
REMARK 465     HIS L   297                                                      
REMARK 465     PRO L   298                                                      
REMARK 465     VAL L   299                                                      
REMARK 465     THR L   300                                                      
REMARK 465     GLU L   301                                                      
REMARK 465     MET L   302                                                      
REMARK 465     ILE L   303                                                      
REMARK 465     THR L   304                                                      
REMARK 465     GLY L   305                                                      
REMARK 465     LEU L   306                                                      
REMARK 465     ASP L   307                                                      
REMARK 465     LEU L   308                                                      
REMARK 465     VAL L   309                                                      
REMARK 465     GLU L   310                                                      
REMARK 465     LEU L   311                                                      
REMARK 465     MET L   312                                                      
REMARK 465     ILE L   313                                                      
REMARK 465     ARG L   314                                                      
REMARK 465     VAL L   315                                                      
REMARK 465     ALA L   316                                                      
REMARK 465     ALA L   317                                                      
REMARK 465     GLY L   318                                                      
REMARK 465     GLU L   319                                                      
REMARK 465     LYS L   320                                                      
REMARK 465     LEU L   321                                                      
REMARK 465     PRO L   322                                                      
REMARK 465     LEU L   323                                                      
REMARK 465     SER L   324                                                      
REMARK 465     GLN L   325                                                      
REMARK 465     ASP L   326                                                      
REMARK 465     GLN L   327                                                      
REMARK 465     VAL L   328                                                      
REMARK 465     LYS L   329                                                      
REMARK 465     LEU L   330                                                      
REMARK 465     ASP L   331                                                      
REMARK 465     GLY L   332                                                      
REMARK 465     TRP L   333                                                      
REMARK 465     ALA L   334                                                      
REMARK 465     VAL L   335                                                      
REMARK 465     GLU L   336                                                      
REMARK 465     SER L   337                                                      
REMARK 465     ARG L   338                                                      
REMARK 465     VAL L   339                                                      
REMARK 465     TYR L   340                                                      
REMARK 465     ALA L   341                                                      
REMARK 465     GLU L   342                                                      
REMARK 465     ASP L   343                                                      
REMARK 465     PRO L   344                                                      
REMARK 465     THR L   345                                                      
REMARK 465     ARG L   346                                                      
REMARK 465     ASN L   347                                                      
REMARK 465     PHE L   348                                                      
REMARK 465     LEU L   349                                                      
REMARK 465     PRO L   350                                                      
REMARK 465     SER L   351                                                      
REMARK 465     ILE L   352                                                      
REMARK 465     GLY L   353                                                      
REMARK 465     ARG L   354                                                      
REMARK 465     LEU L   355                                                      
REMARK 465     THR L   356                                                      
REMARK 465     THR L   357                                                      
REMARK 465     TYR L   358                                                      
REMARK 465     GLN L   359                                                      
REMARK 465     PRO L   360                                                      
REMARK 465     PRO L   361                                                      
REMARK 465     GLU L   362                                                      
REMARK 465     GLU L   363                                                      
REMARK 465     GLY L   364                                                      
REMARK 465     PRO L   365                                                      
REMARK 465     LEU L   366                                                      
REMARK 465     GLY L   367                                                      
REMARK 465     GLY L   368                                                      
REMARK 465     ALA L   369                                                      
REMARK 465     ILE L   370                                                      
REMARK 465     VAL L   371                                                      
REMARK 465     ARG L   372                                                      
REMARK 465     ASN L   373                                                      
REMARK 465     ASP L   374                                                      
REMARK 465     THR L   375                                                      
REMARK 465     GLY L   376                                                      
REMARK 465     VAL L   377                                                      
REMARK 465     GLU L   378                                                      
REMARK 465     GLU L   379                                                      
REMARK 465     GLY L   380                                                      
REMARK 465     GLY L   381                                                      
REMARK 465     GLU L   382                                                      
REMARK 465     ILE L   383                                                      
REMARK 465     ALA L   384                                                      
REMARK 465     ILE L   385                                                      
REMARK 465     HIS L   386                                                      
REMARK 465     TYR L   387                                                      
REMARK 465     ASP L   388                                                      
REMARK 465     PRO L   389                                                      
REMARK 465     MET L   390                                                      
REMARK 465     ILE L   391                                                      
REMARK 465     ALA L   392                                                      
REMARK 465     LYS L   393                                                      
REMARK 465     LEU L   394                                                      
REMARK 465     VAL L   395                                                      
REMARK 465     THR L   396                                                      
REMARK 465     TRP L   397                                                      
REMARK 465     ALA L   398                                                      
REMARK 465     PRO L   399                                                      
REMARK 465     THR L   400                                                      
REMARK 465     ARG L   401                                                      
REMARK 465     LEU L   402                                                      
REMARK 465     GLU L   403                                                      
REMARK 465     ALA L   404                                                      
REMARK 465     ILE L   405                                                      
REMARK 465     GLU L   406                                                      
REMARK 465     ALA L   407                                                      
REMARK 465     GLN L   408                                                      
REMARK 465     ALA L   409                                                      
REMARK 465     THR L   410                                                      
REMARK 465     ALA L   411                                                      
REMARK 465     LEU L   412                                                      
REMARK 465     ASP L   413                                                      
REMARK 465     ALA L   414                                                      
REMARK 465     PHE L   415                                                      
REMARK 465     ALA L   416                                                      
REMARK 465     ILE L   417                                                      
REMARK 465     GLU L   418                                                      
REMARK 465     GLY L   419                                                      
REMARK 465     ILE L   420                                                      
REMARK 465     ARG L   421                                                      
REMARK 465     HIS L   422                                                      
REMARK 465     ASN L   423                                                      
REMARK 465     ILE L   424                                                      
REMARK 465     PRO L   425                                                      
REMARK 465     PHE L   426                                                      
REMARK 465     LEU L   427                                                      
REMARK 465     ALA L   428                                                      
REMARK 465     THR L   429                                                      
REMARK 465     LEU L   430                                                      
REMARK 465     MET L   431                                                      
REMARK 465     ALA L   432                                                      
REMARK 465     HIS L   433                                                      
REMARK 465     PRO L   434                                                      
REMARK 465     ARG L   435                                                      
REMARK 465     TRP L   436                                                      
REMARK 465     ARG L   437                                                      
REMARK 465     ASP L   438                                                      
REMARK 465     GLY L   439                                                      
REMARK 465     ARG L   440                                                      
REMARK 465     LEU L   441                                                      
REMARK 465     SER L   442                                                      
REMARK 465     THR L   443                                                      
REMARK 465     GLY L   444                                                      
REMARK 465     PHE L   445                                                      
REMARK 465     ILE L   446                                                      
REMARK 465     LYS L   447                                                      
REMARK 465     GLU L   448                                                      
REMARK 465     GLU L   449                                                      
REMARK 465     PHE L   450                                                      
REMARK 465     PRO L   451                                                      
REMARK 465     GLU L   452                                                      
REMARK 465     GLY L   453                                                      
REMARK 465     PHE L   454                                                      
REMARK 465     ILE L   455                                                      
REMARK 465     ALA L   456                                                      
REMARK 465     ALA L   667                                                      
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    ASP A 186       -7.65     76.33                                   
REMARK 500    SER A 222        7.64     81.97                                   
REMARK 500    ALA A 330       15.01     57.11                                   
REMARK 500    ARG A 399      -67.12   -121.80                                   
REMARK 500    GLU A 443       50.21   -119.36                                   
REMARK 500    ASP B 186       -8.98     76.97                                   
REMARK 500    SER B 222        5.32     80.55                                   
REMARK 500    GLU B 293       16.45     57.17                                   
REMARK 500    ALA B 330       14.89     57.49                                   
REMARK 500    ARG B 399     -153.08   -151.27                                   
REMARK 500    LYS B 503      148.76   -171.41                                   
REMARK 500    ASP C 186       -3.53     77.07                                   
REMARK 500    SER C 222       11.36     81.17                                   
REMARK 500    ALA C 330       18.39     57.75                                   
REMARK 500    ARG C 399      -65.73   -123.66                                   
REMARK 500    ALA C 442       45.66    -89.44                                   
REMARK 500    ASP D 186       -7.97     75.81                                   
REMARK 500    SER D 222        5.51     81.81                                   
REMARK 500    ARG D 399      -65.10   -123.57                                   
REMARK 500    ASP E 186       -7.43     75.78                                   
REMARK 500    SER E 222       11.95     81.65                                   
REMARK 500    ALA E 330       16.84     56.63                                   
REMARK 500    ARG E 399     -153.28   -152.75                                   
REMARK 500    LYS E 400      137.92    -32.70                                   
REMARK 500    MET E 430     -179.49   -171.32                                   
REMARK 500    ASP F 186       -6.40     77.20                                   
REMARK 500    SER F 222        0.16     81.02                                   
REMARK 500    ARG F 399     -150.55   -151.79                                   
REMARK 500    LEU G 494       57.84    -90.49                                   
REMARK 500    GLN G 551      148.56   -172.00                                   
REMARK 500    LYS H 599       -8.42     76.35                                   
REMARK 500    ASP I 550       -0.13     81.12                                   
REMARK 500    LYS I 599       -5.19     72.67                                   
REMARK 500    LEU J 494       34.92    -98.05                                   
REMARK 500    SER J 506       58.11     39.68                                   
REMARK 500    ASP J 527       48.55    -83.77                                   
REMARK 500    GLN K 508      116.59   -160.87                                   
REMARK 500    LYS K 599       -7.95     74.99                                   
REMARK 500    LEU L 494       54.17    -92.76                                   
REMARK 500    SER L 506       57.50     39.06                                   
REMARK 500    ASP L 520     -159.83   -123.52                                   
REMARK 500    SER L 597     -168.97   -127.34                                   
REMARK 500    LYS L 599       -4.75     72.03                                   
REMARK 500    ALA L 651      146.19   -174.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue COA A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue COA B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue COA C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue COA D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue COA E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue COA F 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BTI G 701 and LYS G    
REMARK 800  633                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BTI H 701 and LYS H    
REMARK 800  633                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BTI I 701 and LYS I    
REMARK 800  633                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BTI J 701 and LYS J    
REMARK 800  633                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BTI K 701 and LYS K    
REMARK 800  633                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BTI L 701 and LYS L    
REMARK 800  633                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-10771   RELATED DB: EMDB                             
REMARK 900 ENGINEERED GLYCOLYL-COA CARBOXYLASE (QUINTUPLE MUTANT) WITH BOUND    
REMARK 900 COA                                                                  
DBREF  6YBQ A    1   510  UNP    C5AP75   C5AP75_METEA     1    510             
DBREF  6YBQ B    1   510  UNP    C5AP75   C5AP75_METEA     1    510             
DBREF  6YBQ C    1   510  UNP    C5AP75   C5AP75_METEA     1    510             
DBREF  6YBQ D    1   510  UNP    C5AP75   C5AP75_METEA     1    510             
DBREF  6YBQ E    1   510  UNP    C5AP75   C5AP75_METEA     1    510             
DBREF  6YBQ F    1   510  UNP    C5AP75   C5AP75_METEA     1    510             
DBREF  6YBQ G    1   667  UNP    C5AWU5   C5AWU5_METEA     1    667             
DBREF  6YBQ H    1   667  UNP    C5AWU5   C5AWU5_METEA     1    667             
DBREF  6YBQ I    1   667  UNP    C5AWU5   C5AWU5_METEA     1    667             
DBREF  6YBQ J    1   667  UNP    C5AWU5   C5AWU5_METEA     1    667             
DBREF  6YBQ K    1   667  UNP    C5AWU5   C5AWU5_METEA     1    667             
DBREF  6YBQ L    1   667  UNP    C5AWU5   C5AWU5_METEA     1    667             
SEQADV 6YBQ SER A  100  UNP  C5AP75    LEU   100 ENGINEERED MUTATION            
SEQADV 6YBQ HIS A  143  UNP  C5AP75    TYR   143 ENGINEERED MUTATION            
SEQADV 6YBQ ILE A  407  UNP  C5AP75    ASP   407 ENGINEERED MUTATION            
SEQADV 6YBQ VAL A  450  UNP  C5AP75    ILE   450 ENGINEERED MUTATION            
SEQADV 6YBQ ARG A  502  UNP  C5AP75    TRP   502 ENGINEERED MUTATION            
SEQADV 6YBQ SER B  100  UNP  C5AP75    LEU   100 ENGINEERED MUTATION            
SEQADV 6YBQ HIS B  143  UNP  C5AP75    TYR   143 ENGINEERED MUTATION            
SEQADV 6YBQ ILE B  407  UNP  C5AP75    ASP   407 ENGINEERED MUTATION            
SEQADV 6YBQ VAL B  450  UNP  C5AP75    ILE   450 ENGINEERED MUTATION            
SEQADV 6YBQ ARG B  502  UNP  C5AP75    TRP   502 ENGINEERED MUTATION            
SEQADV 6YBQ SER C  100  UNP  C5AP75    LEU   100 ENGINEERED MUTATION            
SEQADV 6YBQ HIS C  143  UNP  C5AP75    TYR   143 ENGINEERED MUTATION            
SEQADV 6YBQ ILE C  407  UNP  C5AP75    ASP   407 ENGINEERED MUTATION            
SEQADV 6YBQ VAL C  450  UNP  C5AP75    ILE   450 ENGINEERED MUTATION            
SEQADV 6YBQ ARG C  502  UNP  C5AP75    TRP   502 ENGINEERED MUTATION            
SEQADV 6YBQ SER D  100  UNP  C5AP75    LEU   100 ENGINEERED MUTATION            
SEQADV 6YBQ HIS D  143  UNP  C5AP75    TYR   143 ENGINEERED MUTATION            
SEQADV 6YBQ ILE D  407  UNP  C5AP75    ASP   407 ENGINEERED MUTATION            
SEQADV 6YBQ VAL D  450  UNP  C5AP75    ILE   450 ENGINEERED MUTATION            
SEQADV 6YBQ ARG D  502  UNP  C5AP75    TRP   502 ENGINEERED MUTATION            
SEQADV 6YBQ SER E  100  UNP  C5AP75    LEU   100 ENGINEERED MUTATION            
SEQADV 6YBQ HIS E  143  UNP  C5AP75    TYR   143 ENGINEERED MUTATION            
SEQADV 6YBQ ILE E  407  UNP  C5AP75    ASP   407 ENGINEERED MUTATION            
SEQADV 6YBQ VAL E  450  UNP  C5AP75    ILE   450 ENGINEERED MUTATION            
SEQADV 6YBQ ARG E  502  UNP  C5AP75    TRP   502 ENGINEERED MUTATION            
SEQADV 6YBQ SER F  100  UNP  C5AP75    LEU   100 ENGINEERED MUTATION            
SEQADV 6YBQ HIS F  143  UNP  C5AP75    TYR   143 ENGINEERED MUTATION            
SEQADV 6YBQ ILE F  407  UNP  C5AP75    ASP   407 ENGINEERED MUTATION            
SEQADV 6YBQ VAL F  450  UNP  C5AP75    ILE   450 ENGINEERED MUTATION            
SEQADV 6YBQ ARG F  502  UNP  C5AP75    TRP   502 ENGINEERED MUTATION            
SEQRES   1 A  510  MET LYS ASP ILE LEU GLU LYS LEU GLU GLU ARG ARG ALA          
SEQRES   2 A  510  GLN ALA ARG LEU GLY GLY GLY GLU LYS ARG LEU GLU ALA          
SEQRES   3 A  510  GLN HIS LYS ARG GLY LYS LEU THR ALA ARG GLU ARG ILE          
SEQRES   4 A  510  GLU LEU LEU LEU ASP HIS GLY SER PHE GLU GLU PHE ASP          
SEQRES   5 A  510  MET PHE VAL GLN HIS ARG SER THR ASP PHE GLY MET GLU          
SEQRES   6 A  510  LYS GLN LYS ILE PRO GLY ASP GLY VAL VAL THR GLY TRP          
SEQRES   7 A  510  GLY THR VAL ASN GLY ARG THR VAL PHE LEU PHE SER LYS          
SEQRES   8 A  510  ASP PHE THR VAL PHE GLY GLY SER SER SER GLU ALA HIS          
SEQRES   9 A  510  ALA ALA LYS ILE VAL LYS VAL GLN ASP MET ALA LEU LYS          
SEQRES  10 A  510  MET ARG ALA PRO ILE ILE GLY ILE PHE ASP ALA GLY GLY          
SEQRES  11 A  510  ALA ARG ILE GLN GLU GLY VAL ALA ALA LEU GLY GLY HIS          
SEQRES  12 A  510  GLY GLU VAL PHE ARG ARG ASN VAL ALA ALA SER GLY VAL          
SEQRES  13 A  510  ILE PRO GLN ILE SER VAL ILE MET GLY PRO CYS ALA GLY          
SEQRES  14 A  510  GLY ASP VAL TYR SER PRO ALA MET THR ASP PHE ILE PHE          
SEQRES  15 A  510  MET VAL ARG ASP THR SER TYR MET PHE VAL THR GLY PRO          
SEQRES  16 A  510  ASP VAL VAL LYS THR VAL THR ASN GLU VAL VAL THR ALA          
SEQRES  17 A  510  GLU GLU LEU GLY GLY ALA LYS VAL HIS THR SER LYS SER          
SEQRES  18 A  510  SER ILE ALA ASP GLY SER PHE GLU ASN ASP VAL GLU ALA          
SEQRES  19 A  510  ILE LEU GLN ILE ARG ARG LEU LEU ASP PHE LEU PRO ALA          
SEQRES  20 A  510  ASN ASN ILE GLU GLY VAL PRO GLU ILE GLU SER PHE ASP          
SEQRES  21 A  510  ASP VAL ASN ARG LEU ASP LYS SER LEU ASP THR LEU ILE          
SEQRES  22 A  510  PRO ASP ASN PRO ASN LYS PRO TYR ASP MET GLY GLU LEU          
SEQRES  23 A  510  ILE ARG ARG VAL VAL ASP GLU GLY ASP PHE PHE GLU ILE          
SEQRES  24 A  510  GLN ALA ALA TYR ALA ARG ASN ILE ILE THR GLY PHE GLY          
SEQRES  25 A  510  ARG VAL GLU GLY ARG THR VAL GLY PHE VAL ALA ASN GLN          
SEQRES  26 A  510  PRO LEU VAL LEU ALA GLY VAL LEU ASP SER ASP ALA SER          
SEQRES  27 A  510  ARG LYS ALA ALA ARG PHE VAL ARG PHE CYS ASN ALA PHE          
SEQRES  28 A  510  SER ILE PRO ILE VAL THR PHE VAL ASP VAL PRO GLY PHE          
SEQRES  29 A  510  LEU PRO GLY THR ALA GLN GLU TYR GLY GLY LEU ILE LYS          
SEQRES  30 A  510  HIS GLY ALA LYS LEU LEU PHE ALA TYR SER GLN ALA THR          
SEQRES  31 A  510  VAL PRO LEU VAL THR ILE ILE THR ARG LYS ALA PHE GLY          
SEQRES  32 A  510  GLY ALA TYR ILE VAL MET ALA SER LYS HIS VAL GLY ALA          
SEQRES  33 A  510  ASP LEU ASN TYR ALA TRP PRO THR ALA GLN ILE ALA VAL          
SEQRES  34 A  510  MET GLY ALA LYS GLY ALA VAL GLU ILE ILE PHE ARG ALA          
SEQRES  35 A  510  GLU ILE GLY ASP ALA ASP LYS VAL ALA GLU ARG THR LYS          
SEQRES  36 A  510  GLU TYR GLU ASP ARG PHE LEU SER PRO PHE VAL ALA ALA          
SEQRES  37 A  510  GLU ARG GLY TYR ILE ASP GLU VAL ILE MET PRO HIS SER          
SEQRES  38 A  510  THR ARG LYS ARG ILE ALA ARG ALA LEU GLY MET LEU ARG          
SEQRES  39 A  510  THR LYS GLU MET GLU GLN PRO ARG LYS LYS HIS ASP ASN          
SEQRES  40 A  510  ILE PRO LEU                                                  
SEQRES   1 B  510  MET LYS ASP ILE LEU GLU LYS LEU GLU GLU ARG ARG ALA          
SEQRES   2 B  510  GLN ALA ARG LEU GLY GLY GLY GLU LYS ARG LEU GLU ALA          
SEQRES   3 B  510  GLN HIS LYS ARG GLY LYS LEU THR ALA ARG GLU ARG ILE          
SEQRES   4 B  510  GLU LEU LEU LEU ASP HIS GLY SER PHE GLU GLU PHE ASP          
SEQRES   5 B  510  MET PHE VAL GLN HIS ARG SER THR ASP PHE GLY MET GLU          
SEQRES   6 B  510  LYS GLN LYS ILE PRO GLY ASP GLY VAL VAL THR GLY TRP          
SEQRES   7 B  510  GLY THR VAL ASN GLY ARG THR VAL PHE LEU PHE SER LYS          
SEQRES   8 B  510  ASP PHE THR VAL PHE GLY GLY SER SER SER GLU ALA HIS          
SEQRES   9 B  510  ALA ALA LYS ILE VAL LYS VAL GLN ASP MET ALA LEU LYS          
SEQRES  10 B  510  MET ARG ALA PRO ILE ILE GLY ILE PHE ASP ALA GLY GLY          
SEQRES  11 B  510  ALA ARG ILE GLN GLU GLY VAL ALA ALA LEU GLY GLY HIS          
SEQRES  12 B  510  GLY GLU VAL PHE ARG ARG ASN VAL ALA ALA SER GLY VAL          
SEQRES  13 B  510  ILE PRO GLN ILE SER VAL ILE MET GLY PRO CYS ALA GLY          
SEQRES  14 B  510  GLY ASP VAL TYR SER PRO ALA MET THR ASP PHE ILE PHE          
SEQRES  15 B  510  MET VAL ARG ASP THR SER TYR MET PHE VAL THR GLY PRO          
SEQRES  16 B  510  ASP VAL VAL LYS THR VAL THR ASN GLU VAL VAL THR ALA          
SEQRES  17 B  510  GLU GLU LEU GLY GLY ALA LYS VAL HIS THR SER LYS SER          
SEQRES  18 B  510  SER ILE ALA ASP GLY SER PHE GLU ASN ASP VAL GLU ALA          
SEQRES  19 B  510  ILE LEU GLN ILE ARG ARG LEU LEU ASP PHE LEU PRO ALA          
SEQRES  20 B  510  ASN ASN ILE GLU GLY VAL PRO GLU ILE GLU SER PHE ASP          
SEQRES  21 B  510  ASP VAL ASN ARG LEU ASP LYS SER LEU ASP THR LEU ILE          
SEQRES  22 B  510  PRO ASP ASN PRO ASN LYS PRO TYR ASP MET GLY GLU LEU          
SEQRES  23 B  510  ILE ARG ARG VAL VAL ASP GLU GLY ASP PHE PHE GLU ILE          
SEQRES  24 B  510  GLN ALA ALA TYR ALA ARG ASN ILE ILE THR GLY PHE GLY          
SEQRES  25 B  510  ARG VAL GLU GLY ARG THR VAL GLY PHE VAL ALA ASN GLN          
SEQRES  26 B  510  PRO LEU VAL LEU ALA GLY VAL LEU ASP SER ASP ALA SER          
SEQRES  27 B  510  ARG LYS ALA ALA ARG PHE VAL ARG PHE CYS ASN ALA PHE          
SEQRES  28 B  510  SER ILE PRO ILE VAL THR PHE VAL ASP VAL PRO GLY PHE          
SEQRES  29 B  510  LEU PRO GLY THR ALA GLN GLU TYR GLY GLY LEU ILE LYS          
SEQRES  30 B  510  HIS GLY ALA LYS LEU LEU PHE ALA TYR SER GLN ALA THR          
SEQRES  31 B  510  VAL PRO LEU VAL THR ILE ILE THR ARG LYS ALA PHE GLY          
SEQRES  32 B  510  GLY ALA TYR ILE VAL MET ALA SER LYS HIS VAL GLY ALA          
SEQRES  33 B  510  ASP LEU ASN TYR ALA TRP PRO THR ALA GLN ILE ALA VAL          
SEQRES  34 B  510  MET GLY ALA LYS GLY ALA VAL GLU ILE ILE PHE ARG ALA          
SEQRES  35 B  510  GLU ILE GLY ASP ALA ASP LYS VAL ALA GLU ARG THR LYS          
SEQRES  36 B  510  GLU TYR GLU ASP ARG PHE LEU SER PRO PHE VAL ALA ALA          
SEQRES  37 B  510  GLU ARG GLY TYR ILE ASP GLU VAL ILE MET PRO HIS SER          
SEQRES  38 B  510  THR ARG LYS ARG ILE ALA ARG ALA LEU GLY MET LEU ARG          
SEQRES  39 B  510  THR LYS GLU MET GLU GLN PRO ARG LYS LYS HIS ASP ASN          
SEQRES  40 B  510  ILE PRO LEU                                                  
SEQRES   1 C  510  MET LYS ASP ILE LEU GLU LYS LEU GLU GLU ARG ARG ALA          
SEQRES   2 C  510  GLN ALA ARG LEU GLY GLY GLY GLU LYS ARG LEU GLU ALA          
SEQRES   3 C  510  GLN HIS LYS ARG GLY LYS LEU THR ALA ARG GLU ARG ILE          
SEQRES   4 C  510  GLU LEU LEU LEU ASP HIS GLY SER PHE GLU GLU PHE ASP          
SEQRES   5 C  510  MET PHE VAL GLN HIS ARG SER THR ASP PHE GLY MET GLU          
SEQRES   6 C  510  LYS GLN LYS ILE PRO GLY ASP GLY VAL VAL THR GLY TRP          
SEQRES   7 C  510  GLY THR VAL ASN GLY ARG THR VAL PHE LEU PHE SER LYS          
SEQRES   8 C  510  ASP PHE THR VAL PHE GLY GLY SER SER SER GLU ALA HIS          
SEQRES   9 C  510  ALA ALA LYS ILE VAL LYS VAL GLN ASP MET ALA LEU LYS          
SEQRES  10 C  510  MET ARG ALA PRO ILE ILE GLY ILE PHE ASP ALA GLY GLY          
SEQRES  11 C  510  ALA ARG ILE GLN GLU GLY VAL ALA ALA LEU GLY GLY HIS          
SEQRES  12 C  510  GLY GLU VAL PHE ARG ARG ASN VAL ALA ALA SER GLY VAL          
SEQRES  13 C  510  ILE PRO GLN ILE SER VAL ILE MET GLY PRO CYS ALA GLY          
SEQRES  14 C  510  GLY ASP VAL TYR SER PRO ALA MET THR ASP PHE ILE PHE          
SEQRES  15 C  510  MET VAL ARG ASP THR SER TYR MET PHE VAL THR GLY PRO          
SEQRES  16 C  510  ASP VAL VAL LYS THR VAL THR ASN GLU VAL VAL THR ALA          
SEQRES  17 C  510  GLU GLU LEU GLY GLY ALA LYS VAL HIS THR SER LYS SER          
SEQRES  18 C  510  SER ILE ALA ASP GLY SER PHE GLU ASN ASP VAL GLU ALA          
SEQRES  19 C  510  ILE LEU GLN ILE ARG ARG LEU LEU ASP PHE LEU PRO ALA          
SEQRES  20 C  510  ASN ASN ILE GLU GLY VAL PRO GLU ILE GLU SER PHE ASP          
SEQRES  21 C  510  ASP VAL ASN ARG LEU ASP LYS SER LEU ASP THR LEU ILE          
SEQRES  22 C  510  PRO ASP ASN PRO ASN LYS PRO TYR ASP MET GLY GLU LEU          
SEQRES  23 C  510  ILE ARG ARG VAL VAL ASP GLU GLY ASP PHE PHE GLU ILE          
SEQRES  24 C  510  GLN ALA ALA TYR ALA ARG ASN ILE ILE THR GLY PHE GLY          
SEQRES  25 C  510  ARG VAL GLU GLY ARG THR VAL GLY PHE VAL ALA ASN GLN          
SEQRES  26 C  510  PRO LEU VAL LEU ALA GLY VAL LEU ASP SER ASP ALA SER          
SEQRES  27 C  510  ARG LYS ALA ALA ARG PHE VAL ARG PHE CYS ASN ALA PHE          
SEQRES  28 C  510  SER ILE PRO ILE VAL THR PHE VAL ASP VAL PRO GLY PHE          
SEQRES  29 C  510  LEU PRO GLY THR ALA GLN GLU TYR GLY GLY LEU ILE LYS          
SEQRES  30 C  510  HIS GLY ALA LYS LEU LEU PHE ALA TYR SER GLN ALA THR          
SEQRES  31 C  510  VAL PRO LEU VAL THR ILE ILE THR ARG LYS ALA PHE GLY          
SEQRES  32 C  510  GLY ALA TYR ILE VAL MET ALA SER LYS HIS VAL GLY ALA          
SEQRES  33 C  510  ASP LEU ASN TYR ALA TRP PRO THR ALA GLN ILE ALA VAL          
SEQRES  34 C  510  MET GLY ALA LYS GLY ALA VAL GLU ILE ILE PHE ARG ALA          
SEQRES  35 C  510  GLU ILE GLY ASP ALA ASP LYS VAL ALA GLU ARG THR LYS          
SEQRES  36 C  510  GLU TYR GLU ASP ARG PHE LEU SER PRO PHE VAL ALA ALA          
SEQRES  37 C  510  GLU ARG GLY TYR ILE ASP GLU VAL ILE MET PRO HIS SER          
SEQRES  38 C  510  THR ARG LYS ARG ILE ALA ARG ALA LEU GLY MET LEU ARG          
SEQRES  39 C  510  THR LYS GLU MET GLU GLN PRO ARG LYS LYS HIS ASP ASN          
SEQRES  40 C  510  ILE PRO LEU                                                  
SEQRES   1 D  510  MET LYS ASP ILE LEU GLU LYS LEU GLU GLU ARG ARG ALA          
SEQRES   2 D  510  GLN ALA ARG LEU GLY GLY GLY GLU LYS ARG LEU GLU ALA          
SEQRES   3 D  510  GLN HIS LYS ARG GLY LYS LEU THR ALA ARG GLU ARG ILE          
SEQRES   4 D  510  GLU LEU LEU LEU ASP HIS GLY SER PHE GLU GLU PHE ASP          
SEQRES   5 D  510  MET PHE VAL GLN HIS ARG SER THR ASP PHE GLY MET GLU          
SEQRES   6 D  510  LYS GLN LYS ILE PRO GLY ASP GLY VAL VAL THR GLY TRP          
SEQRES   7 D  510  GLY THR VAL ASN GLY ARG THR VAL PHE LEU PHE SER LYS          
SEQRES   8 D  510  ASP PHE THR VAL PHE GLY GLY SER SER SER GLU ALA HIS          
SEQRES   9 D  510  ALA ALA LYS ILE VAL LYS VAL GLN ASP MET ALA LEU LYS          
SEQRES  10 D  510  MET ARG ALA PRO ILE ILE GLY ILE PHE ASP ALA GLY GLY          
SEQRES  11 D  510  ALA ARG ILE GLN GLU GLY VAL ALA ALA LEU GLY GLY HIS          
SEQRES  12 D  510  GLY GLU VAL PHE ARG ARG ASN VAL ALA ALA SER GLY VAL          
SEQRES  13 D  510  ILE PRO GLN ILE SER VAL ILE MET GLY PRO CYS ALA GLY          
SEQRES  14 D  510  GLY ASP VAL TYR SER PRO ALA MET THR ASP PHE ILE PHE          
SEQRES  15 D  510  MET VAL ARG ASP THR SER TYR MET PHE VAL THR GLY PRO          
SEQRES  16 D  510  ASP VAL VAL LYS THR VAL THR ASN GLU VAL VAL THR ALA          
SEQRES  17 D  510  GLU GLU LEU GLY GLY ALA LYS VAL HIS THR SER LYS SER          
SEQRES  18 D  510  SER ILE ALA ASP GLY SER PHE GLU ASN ASP VAL GLU ALA          
SEQRES  19 D  510  ILE LEU GLN ILE ARG ARG LEU LEU ASP PHE LEU PRO ALA          
SEQRES  20 D  510  ASN ASN ILE GLU GLY VAL PRO GLU ILE GLU SER PHE ASP          
SEQRES  21 D  510  ASP VAL ASN ARG LEU ASP LYS SER LEU ASP THR LEU ILE          
SEQRES  22 D  510  PRO ASP ASN PRO ASN LYS PRO TYR ASP MET GLY GLU LEU          
SEQRES  23 D  510  ILE ARG ARG VAL VAL ASP GLU GLY ASP PHE PHE GLU ILE          
SEQRES  24 D  510  GLN ALA ALA TYR ALA ARG ASN ILE ILE THR GLY PHE GLY          
SEQRES  25 D  510  ARG VAL GLU GLY ARG THR VAL GLY PHE VAL ALA ASN GLN          
SEQRES  26 D  510  PRO LEU VAL LEU ALA GLY VAL LEU ASP SER ASP ALA SER          
SEQRES  27 D  510  ARG LYS ALA ALA ARG PHE VAL ARG PHE CYS ASN ALA PHE          
SEQRES  28 D  510  SER ILE PRO ILE VAL THR PHE VAL ASP VAL PRO GLY PHE          
SEQRES  29 D  510  LEU PRO GLY THR ALA GLN GLU TYR GLY GLY LEU ILE LYS          
SEQRES  30 D  510  HIS GLY ALA LYS LEU LEU PHE ALA TYR SER GLN ALA THR          
SEQRES  31 D  510  VAL PRO LEU VAL THR ILE ILE THR ARG LYS ALA PHE GLY          
SEQRES  32 D  510  GLY ALA TYR ILE VAL MET ALA SER LYS HIS VAL GLY ALA          
SEQRES  33 D  510  ASP LEU ASN TYR ALA TRP PRO THR ALA GLN ILE ALA VAL          
SEQRES  34 D  510  MET GLY ALA LYS GLY ALA VAL GLU ILE ILE PHE ARG ALA          
SEQRES  35 D  510  GLU ILE GLY ASP ALA ASP LYS VAL ALA GLU ARG THR LYS          
SEQRES  36 D  510  GLU TYR GLU ASP ARG PHE LEU SER PRO PHE VAL ALA ALA          
SEQRES  37 D  510  GLU ARG GLY TYR ILE ASP GLU VAL ILE MET PRO HIS SER          
SEQRES  38 D  510  THR ARG LYS ARG ILE ALA ARG ALA LEU GLY MET LEU ARG          
SEQRES  39 D  510  THR LYS GLU MET GLU GLN PRO ARG LYS LYS HIS ASP ASN          
SEQRES  40 D  510  ILE PRO LEU                                                  
SEQRES   1 E  510  MET LYS ASP ILE LEU GLU LYS LEU GLU GLU ARG ARG ALA          
SEQRES   2 E  510  GLN ALA ARG LEU GLY GLY GLY GLU LYS ARG LEU GLU ALA          
SEQRES   3 E  510  GLN HIS LYS ARG GLY LYS LEU THR ALA ARG GLU ARG ILE          
SEQRES   4 E  510  GLU LEU LEU LEU ASP HIS GLY SER PHE GLU GLU PHE ASP          
SEQRES   5 E  510  MET PHE VAL GLN HIS ARG SER THR ASP PHE GLY MET GLU          
SEQRES   6 E  510  LYS GLN LYS ILE PRO GLY ASP GLY VAL VAL THR GLY TRP          
SEQRES   7 E  510  GLY THR VAL ASN GLY ARG THR VAL PHE LEU PHE SER LYS          
SEQRES   8 E  510  ASP PHE THR VAL PHE GLY GLY SER SER SER GLU ALA HIS          
SEQRES   9 E  510  ALA ALA LYS ILE VAL LYS VAL GLN ASP MET ALA LEU LYS          
SEQRES  10 E  510  MET ARG ALA PRO ILE ILE GLY ILE PHE ASP ALA GLY GLY          
SEQRES  11 E  510  ALA ARG ILE GLN GLU GLY VAL ALA ALA LEU GLY GLY HIS          
SEQRES  12 E  510  GLY GLU VAL PHE ARG ARG ASN VAL ALA ALA SER GLY VAL          
SEQRES  13 E  510  ILE PRO GLN ILE SER VAL ILE MET GLY PRO CYS ALA GLY          
SEQRES  14 E  510  GLY ASP VAL TYR SER PRO ALA MET THR ASP PHE ILE PHE          
SEQRES  15 E  510  MET VAL ARG ASP THR SER TYR MET PHE VAL THR GLY PRO          
SEQRES  16 E  510  ASP VAL VAL LYS THR VAL THR ASN GLU VAL VAL THR ALA          
SEQRES  17 E  510  GLU GLU LEU GLY GLY ALA LYS VAL HIS THR SER LYS SER          
SEQRES  18 E  510  SER ILE ALA ASP GLY SER PHE GLU ASN ASP VAL GLU ALA          
SEQRES  19 E  510  ILE LEU GLN ILE ARG ARG LEU LEU ASP PHE LEU PRO ALA          
SEQRES  20 E  510  ASN ASN ILE GLU GLY VAL PRO GLU ILE GLU SER PHE ASP          
SEQRES  21 E  510  ASP VAL ASN ARG LEU ASP LYS SER LEU ASP THR LEU ILE          
SEQRES  22 E  510  PRO ASP ASN PRO ASN LYS PRO TYR ASP MET GLY GLU LEU          
SEQRES  23 E  510  ILE ARG ARG VAL VAL ASP GLU GLY ASP PHE PHE GLU ILE          
SEQRES  24 E  510  GLN ALA ALA TYR ALA ARG ASN ILE ILE THR GLY PHE GLY          
SEQRES  25 E  510  ARG VAL GLU GLY ARG THR VAL GLY PHE VAL ALA ASN GLN          
SEQRES  26 E  510  PRO LEU VAL LEU ALA GLY VAL LEU ASP SER ASP ALA SER          
SEQRES  27 E  510  ARG LYS ALA ALA ARG PHE VAL ARG PHE CYS ASN ALA PHE          
SEQRES  28 E  510  SER ILE PRO ILE VAL THR PHE VAL ASP VAL PRO GLY PHE          
SEQRES  29 E  510  LEU PRO GLY THR ALA GLN GLU TYR GLY GLY LEU ILE LYS          
SEQRES  30 E  510  HIS GLY ALA LYS LEU LEU PHE ALA TYR SER GLN ALA THR          
SEQRES  31 E  510  VAL PRO LEU VAL THR ILE ILE THR ARG LYS ALA PHE GLY          
SEQRES  32 E  510  GLY ALA TYR ILE VAL MET ALA SER LYS HIS VAL GLY ALA          
SEQRES  33 E  510  ASP LEU ASN TYR ALA TRP PRO THR ALA GLN ILE ALA VAL          
SEQRES  34 E  510  MET GLY ALA LYS GLY ALA VAL GLU ILE ILE PHE ARG ALA          
SEQRES  35 E  510  GLU ILE GLY ASP ALA ASP LYS VAL ALA GLU ARG THR LYS          
SEQRES  36 E  510  GLU TYR GLU ASP ARG PHE LEU SER PRO PHE VAL ALA ALA          
SEQRES  37 E  510  GLU ARG GLY TYR ILE ASP GLU VAL ILE MET PRO HIS SER          
SEQRES  38 E  510  THR ARG LYS ARG ILE ALA ARG ALA LEU GLY MET LEU ARG          
SEQRES  39 E  510  THR LYS GLU MET GLU GLN PRO ARG LYS LYS HIS ASP ASN          
SEQRES  40 E  510  ILE PRO LEU                                                  
SEQRES   1 F  510  MET LYS ASP ILE LEU GLU LYS LEU GLU GLU ARG ARG ALA          
SEQRES   2 F  510  GLN ALA ARG LEU GLY GLY GLY GLU LYS ARG LEU GLU ALA          
SEQRES   3 F  510  GLN HIS LYS ARG GLY LYS LEU THR ALA ARG GLU ARG ILE          
SEQRES   4 F  510  GLU LEU LEU LEU ASP HIS GLY SER PHE GLU GLU PHE ASP          
SEQRES   5 F  510  MET PHE VAL GLN HIS ARG SER THR ASP PHE GLY MET GLU          
SEQRES   6 F  510  LYS GLN LYS ILE PRO GLY ASP GLY VAL VAL THR GLY TRP          
SEQRES   7 F  510  GLY THR VAL ASN GLY ARG THR VAL PHE LEU PHE SER LYS          
SEQRES   8 F  510  ASP PHE THR VAL PHE GLY GLY SER SER SER GLU ALA HIS          
SEQRES   9 F  510  ALA ALA LYS ILE VAL LYS VAL GLN ASP MET ALA LEU LYS          
SEQRES  10 F  510  MET ARG ALA PRO ILE ILE GLY ILE PHE ASP ALA GLY GLY          
SEQRES  11 F  510  ALA ARG ILE GLN GLU GLY VAL ALA ALA LEU GLY GLY HIS          
SEQRES  12 F  510  GLY GLU VAL PHE ARG ARG ASN VAL ALA ALA SER GLY VAL          
SEQRES  13 F  510  ILE PRO GLN ILE SER VAL ILE MET GLY PRO CYS ALA GLY          
SEQRES  14 F  510  GLY ASP VAL TYR SER PRO ALA MET THR ASP PHE ILE PHE          
SEQRES  15 F  510  MET VAL ARG ASP THR SER TYR MET PHE VAL THR GLY PRO          
SEQRES  16 F  510  ASP VAL VAL LYS THR VAL THR ASN GLU VAL VAL THR ALA          
SEQRES  17 F  510  GLU GLU LEU GLY GLY ALA LYS VAL HIS THR SER LYS SER          
SEQRES  18 F  510  SER ILE ALA ASP GLY SER PHE GLU ASN ASP VAL GLU ALA          
SEQRES  19 F  510  ILE LEU GLN ILE ARG ARG LEU LEU ASP PHE LEU PRO ALA          
SEQRES  20 F  510  ASN ASN ILE GLU GLY VAL PRO GLU ILE GLU SER PHE ASP          
SEQRES  21 F  510  ASP VAL ASN ARG LEU ASP LYS SER LEU ASP THR LEU ILE          
SEQRES  22 F  510  PRO ASP ASN PRO ASN LYS PRO TYR ASP MET GLY GLU LEU          
SEQRES  23 F  510  ILE ARG ARG VAL VAL ASP GLU GLY ASP PHE PHE GLU ILE          
SEQRES  24 F  510  GLN ALA ALA TYR ALA ARG ASN ILE ILE THR GLY PHE GLY          
SEQRES  25 F  510  ARG VAL GLU GLY ARG THR VAL GLY PHE VAL ALA ASN GLN          
SEQRES  26 F  510  PRO LEU VAL LEU ALA GLY VAL LEU ASP SER ASP ALA SER          
SEQRES  27 F  510  ARG LYS ALA ALA ARG PHE VAL ARG PHE CYS ASN ALA PHE          
SEQRES  28 F  510  SER ILE PRO ILE VAL THR PHE VAL ASP VAL PRO GLY PHE          
SEQRES  29 F  510  LEU PRO GLY THR ALA GLN GLU TYR GLY GLY LEU ILE LYS          
SEQRES  30 F  510  HIS GLY ALA LYS LEU LEU PHE ALA TYR SER GLN ALA THR          
SEQRES  31 F  510  VAL PRO LEU VAL THR ILE ILE THR ARG LYS ALA PHE GLY          
SEQRES  32 F  510  GLY ALA TYR ILE VAL MET ALA SER LYS HIS VAL GLY ALA          
SEQRES  33 F  510  ASP LEU ASN TYR ALA TRP PRO THR ALA GLN ILE ALA VAL          
SEQRES  34 F  510  MET GLY ALA LYS GLY ALA VAL GLU ILE ILE PHE ARG ALA          
SEQRES  35 F  510  GLU ILE GLY ASP ALA ASP LYS VAL ALA GLU ARG THR LYS          
SEQRES  36 F  510  GLU TYR GLU ASP ARG PHE LEU SER PRO PHE VAL ALA ALA          
SEQRES  37 F  510  GLU ARG GLY TYR ILE ASP GLU VAL ILE MET PRO HIS SER          
SEQRES  38 F  510  THR ARG LYS ARG ILE ALA ARG ALA LEU GLY MET LEU ARG          
SEQRES  39 F  510  THR LYS GLU MET GLU GLN PRO ARG LYS LYS HIS ASP ASN          
SEQRES  40 F  510  ILE PRO LEU                                                  
SEQRES   1 G  667  MET PHE ASP LYS ILE LEU ILE ALA ASN ARG GLY GLU ILE          
SEQRES   2 G  667  ALA CYS ARG ILE ILE LYS THR ALA GLN LYS MET GLY ILE          
SEQRES   3 G  667  LYS THR VAL ALA VAL TYR SER ASP ALA ASP ARG ASP ALA          
SEQRES   4 G  667  VAL HIS VAL ALA MET ALA ASP GLU ALA VAL HIS ILE GLY          
SEQRES   5 G  667  PRO ALA PRO ALA ALA GLN SER TYR LEU LEU ILE GLU LYS          
SEQRES   6 G  667  ILE ILE ASP ALA CYS LYS GLN THR GLY ALA GLN ALA VAL          
SEQRES   7 G  667  HIS PRO GLY TYR GLY PHE LEU SER GLU ARG GLU SER PHE          
SEQRES   8 G  667  PRO LYS ALA LEU ALA GLU ALA GLY ILE VAL PHE ILE GLY          
SEQRES   9 G  667  PRO ASN PRO GLY ALA ILE ALA ALA MET GLY ASP LYS ILE          
SEQRES  10 G  667  GLU SER LYS LYS ALA ALA ALA ALA ALA GLU VAL SER THR          
SEQRES  11 G  667  VAL PRO GLY PHE LEU GLY VAL ILE GLU SER PRO GLU HIS          
SEQRES  12 G  667  ALA VAL THR ILE ALA ASP GLU ILE GLY TYR PRO VAL MET          
SEQRES  13 G  667  ILE LYS ALA SER ALA GLY GLY GLY GLY LYS GLY MET ARG          
SEQRES  14 G  667  ILE ALA GLU SER ALA ASP GLU VAL ALA GLU GLY PHE ALA          
SEQRES  15 G  667  ARG ALA LYS SER GLU ALA SER SER SER PHE GLY ASP ASP          
SEQRES  16 G  667  ARG VAL PHE VAL GLU LYS PHE ILE THR ASP PRO ARG HIS          
SEQRES  17 G  667  ILE GLU ILE GLN VAL ILE GLY ASP LYS HIS GLY ASN VAL          
SEQRES  18 G  667  ILE TYR LEU GLY GLU ARG GLU CYS SER ILE GLN ARG ARG          
SEQRES  19 G  667  ASN GLN LYS VAL ILE GLU GLU ALA PRO SER PRO LEU LEU          
SEQRES  20 G  667  ASP GLU GLU THR ARG ARG LYS MET GLY GLU GLN ALA VAL          
SEQRES  21 G  667  ALA LEU ALA LYS ALA VAL ASN TYR ASP SER ALA GLY THR          
SEQRES  22 G  667  VAL GLU PHE VAL ALA GLY GLN ASP LYS SER PHE TYR PHE          
SEQRES  23 G  667  LEU GLU MET ASN THR ARG LEU GLN VAL GLU HIS PRO VAL          
SEQRES  24 G  667  THR GLU MET ILE THR GLY LEU ASP LEU VAL GLU LEU MET          
SEQRES  25 G  667  ILE ARG VAL ALA ALA GLY GLU LYS LEU PRO LEU SER GLN          
SEQRES  26 G  667  ASP GLN VAL LYS LEU ASP GLY TRP ALA VAL GLU SER ARG          
SEQRES  27 G  667  VAL TYR ALA GLU ASP PRO THR ARG ASN PHE LEU PRO SER          
SEQRES  28 G  667  ILE GLY ARG LEU THR THR TYR GLN PRO PRO GLU GLU GLY          
SEQRES  29 G  667  PRO LEU GLY GLY ALA ILE VAL ARG ASN ASP THR GLY VAL          
SEQRES  30 G  667  GLU GLU GLY GLY GLU ILE ALA ILE HIS TYR ASP PRO MET          
SEQRES  31 G  667  ILE ALA LYS LEU VAL THR TRP ALA PRO THR ARG LEU GLU          
SEQRES  32 G  667  ALA ILE GLU ALA GLN ALA THR ALA LEU ASP ALA PHE ALA          
SEQRES  33 G  667  ILE GLU GLY ILE ARG HIS ASN ILE PRO PHE LEU ALA THR          
SEQRES  34 G  667  LEU MET ALA HIS PRO ARG TRP ARG ASP GLY ARG LEU SER          
SEQRES  35 G  667  THR GLY PHE ILE LYS GLU GLU PHE PRO GLU GLY PHE ILE          
SEQRES  36 G  667  ALA PRO GLU PRO GLU GLY PRO VAL ALA HIS ARG LEU ALA          
SEQRES  37 G  667  ALA VAL ALA ALA ALA ILE ASP HIS LYS LEU ASN ILE ARG          
SEQRES  38 G  667  LYS ARG GLY ILE SER GLY GLN MET ARG ASP PRO SER LEU          
SEQRES  39 G  667  LEU THR PHE GLN ARG GLU ARG VAL VAL VAL LEU SER GLY          
SEQRES  40 G  667  GLN ARG PHE ASN VAL THR VAL ASP PRO ASP GLY ASP ASP          
SEQRES  41 G  667  LEU LEU VAL THR PHE ASP ASP GLY THR THR ALA PRO VAL          
SEQRES  42 G  667  ARG SER ALA TRP ARG PRO GLY ALA PRO VAL TRP SER GLY          
SEQRES  43 G  667  THR VAL GLY ASP GLN SER VAL ALA ILE GLN VAL ARG PRO          
SEQRES  44 G  667  LEU LEU ASN GLY VAL PHE LEU GLN HIS ALA GLY ALA ALA          
SEQRES  45 G  667  ALA GLU ALA ARG VAL PHE THR ARG ARG GLU ALA GLU LEU          
SEQRES  46 G  667  ALA ASP LEU MET PRO VAL LYS GLU ASN ALA GLY SER GLY          
SEQRES  47 G  667  LYS GLN LEU LEU CYS PRO MET PRO GLY LEU VAL LYS GLN          
SEQRES  48 G  667  ILE MET VAL SER GLU GLY GLN GLU VAL LYS ASN GLY GLU          
SEQRES  49 G  667  PRO LEU ALA ILE VAL GLU ALA MET LYS MET GLU ASN VAL          
SEQRES  50 G  667  LEU ARG ALA GLU ARG ASP GLY THR ILE SER LYS ILE ALA          
SEQRES  51 G  667  ALA LYS GLU GLY ASP SER LEU ALA VAL ASP ALA VAL ILE          
SEQRES  52 G  667  LEU GLU PHE ALA                                              
SEQRES   1 H  667  MET PHE ASP LYS ILE LEU ILE ALA ASN ARG GLY GLU ILE          
SEQRES   2 H  667  ALA CYS ARG ILE ILE LYS THR ALA GLN LYS MET GLY ILE          
SEQRES   3 H  667  LYS THR VAL ALA VAL TYR SER ASP ALA ASP ARG ASP ALA          
SEQRES   4 H  667  VAL HIS VAL ALA MET ALA ASP GLU ALA VAL HIS ILE GLY          
SEQRES   5 H  667  PRO ALA PRO ALA ALA GLN SER TYR LEU LEU ILE GLU LYS          
SEQRES   6 H  667  ILE ILE ASP ALA CYS LYS GLN THR GLY ALA GLN ALA VAL          
SEQRES   7 H  667  HIS PRO GLY TYR GLY PHE LEU SER GLU ARG GLU SER PHE          
SEQRES   8 H  667  PRO LYS ALA LEU ALA GLU ALA GLY ILE VAL PHE ILE GLY          
SEQRES   9 H  667  PRO ASN PRO GLY ALA ILE ALA ALA MET GLY ASP LYS ILE          
SEQRES  10 H  667  GLU SER LYS LYS ALA ALA ALA ALA ALA GLU VAL SER THR          
SEQRES  11 H  667  VAL PRO GLY PHE LEU GLY VAL ILE GLU SER PRO GLU HIS          
SEQRES  12 H  667  ALA VAL THR ILE ALA ASP GLU ILE GLY TYR PRO VAL MET          
SEQRES  13 H  667  ILE LYS ALA SER ALA GLY GLY GLY GLY LYS GLY MET ARG          
SEQRES  14 H  667  ILE ALA GLU SER ALA ASP GLU VAL ALA GLU GLY PHE ALA          
SEQRES  15 H  667  ARG ALA LYS SER GLU ALA SER SER SER PHE GLY ASP ASP          
SEQRES  16 H  667  ARG VAL PHE VAL GLU LYS PHE ILE THR ASP PRO ARG HIS          
SEQRES  17 H  667  ILE GLU ILE GLN VAL ILE GLY ASP LYS HIS GLY ASN VAL          
SEQRES  18 H  667  ILE TYR LEU GLY GLU ARG GLU CYS SER ILE GLN ARG ARG          
SEQRES  19 H  667  ASN GLN LYS VAL ILE GLU GLU ALA PRO SER PRO LEU LEU          
SEQRES  20 H  667  ASP GLU GLU THR ARG ARG LYS MET GLY GLU GLN ALA VAL          
SEQRES  21 H  667  ALA LEU ALA LYS ALA VAL ASN TYR ASP SER ALA GLY THR          
SEQRES  22 H  667  VAL GLU PHE VAL ALA GLY GLN ASP LYS SER PHE TYR PHE          
SEQRES  23 H  667  LEU GLU MET ASN THR ARG LEU GLN VAL GLU HIS PRO VAL          
SEQRES  24 H  667  THR GLU MET ILE THR GLY LEU ASP LEU VAL GLU LEU MET          
SEQRES  25 H  667  ILE ARG VAL ALA ALA GLY GLU LYS LEU PRO LEU SER GLN          
SEQRES  26 H  667  ASP GLN VAL LYS LEU ASP GLY TRP ALA VAL GLU SER ARG          
SEQRES  27 H  667  VAL TYR ALA GLU ASP PRO THR ARG ASN PHE LEU PRO SER          
SEQRES  28 H  667  ILE GLY ARG LEU THR THR TYR GLN PRO PRO GLU GLU GLY          
SEQRES  29 H  667  PRO LEU GLY GLY ALA ILE VAL ARG ASN ASP THR GLY VAL          
SEQRES  30 H  667  GLU GLU GLY GLY GLU ILE ALA ILE HIS TYR ASP PRO MET          
SEQRES  31 H  667  ILE ALA LYS LEU VAL THR TRP ALA PRO THR ARG LEU GLU          
SEQRES  32 H  667  ALA ILE GLU ALA GLN ALA THR ALA LEU ASP ALA PHE ALA          
SEQRES  33 H  667  ILE GLU GLY ILE ARG HIS ASN ILE PRO PHE LEU ALA THR          
SEQRES  34 H  667  LEU MET ALA HIS PRO ARG TRP ARG ASP GLY ARG LEU SER          
SEQRES  35 H  667  THR GLY PHE ILE LYS GLU GLU PHE PRO GLU GLY PHE ILE          
SEQRES  36 H  667  ALA PRO GLU PRO GLU GLY PRO VAL ALA HIS ARG LEU ALA          
SEQRES  37 H  667  ALA VAL ALA ALA ALA ILE ASP HIS LYS LEU ASN ILE ARG          
SEQRES  38 H  667  LYS ARG GLY ILE SER GLY GLN MET ARG ASP PRO SER LEU          
SEQRES  39 H  667  LEU THR PHE GLN ARG GLU ARG VAL VAL VAL LEU SER GLY          
SEQRES  40 H  667  GLN ARG PHE ASN VAL THR VAL ASP PRO ASP GLY ASP ASP          
SEQRES  41 H  667  LEU LEU VAL THR PHE ASP ASP GLY THR THR ALA PRO VAL          
SEQRES  42 H  667  ARG SER ALA TRP ARG PRO GLY ALA PRO VAL TRP SER GLY          
SEQRES  43 H  667  THR VAL GLY ASP GLN SER VAL ALA ILE GLN VAL ARG PRO          
SEQRES  44 H  667  LEU LEU ASN GLY VAL PHE LEU GLN HIS ALA GLY ALA ALA          
SEQRES  45 H  667  ALA GLU ALA ARG VAL PHE THR ARG ARG GLU ALA GLU LEU          
SEQRES  46 H  667  ALA ASP LEU MET PRO VAL LYS GLU ASN ALA GLY SER GLY          
SEQRES  47 H  667  LYS GLN LEU LEU CYS PRO MET PRO GLY LEU VAL LYS GLN          
SEQRES  48 H  667  ILE MET VAL SER GLU GLY GLN GLU VAL LYS ASN GLY GLU          
SEQRES  49 H  667  PRO LEU ALA ILE VAL GLU ALA MET LYS MET GLU ASN VAL          
SEQRES  50 H  667  LEU ARG ALA GLU ARG ASP GLY THR ILE SER LYS ILE ALA          
SEQRES  51 H  667  ALA LYS GLU GLY ASP SER LEU ALA VAL ASP ALA VAL ILE          
SEQRES  52 H  667  LEU GLU PHE ALA                                              
SEQRES   1 I  667  MET PHE ASP LYS ILE LEU ILE ALA ASN ARG GLY GLU ILE          
SEQRES   2 I  667  ALA CYS ARG ILE ILE LYS THR ALA GLN LYS MET GLY ILE          
SEQRES   3 I  667  LYS THR VAL ALA VAL TYR SER ASP ALA ASP ARG ASP ALA          
SEQRES   4 I  667  VAL HIS VAL ALA MET ALA ASP GLU ALA VAL HIS ILE GLY          
SEQRES   5 I  667  PRO ALA PRO ALA ALA GLN SER TYR LEU LEU ILE GLU LYS          
SEQRES   6 I  667  ILE ILE ASP ALA CYS LYS GLN THR GLY ALA GLN ALA VAL          
SEQRES   7 I  667  HIS PRO GLY TYR GLY PHE LEU SER GLU ARG GLU SER PHE          
SEQRES   8 I  667  PRO LYS ALA LEU ALA GLU ALA GLY ILE VAL PHE ILE GLY          
SEQRES   9 I  667  PRO ASN PRO GLY ALA ILE ALA ALA MET GLY ASP LYS ILE          
SEQRES  10 I  667  GLU SER LYS LYS ALA ALA ALA ALA ALA GLU VAL SER THR          
SEQRES  11 I  667  VAL PRO GLY PHE LEU GLY VAL ILE GLU SER PRO GLU HIS          
SEQRES  12 I  667  ALA VAL THR ILE ALA ASP GLU ILE GLY TYR PRO VAL MET          
SEQRES  13 I  667  ILE LYS ALA SER ALA GLY GLY GLY GLY LYS GLY MET ARG          
SEQRES  14 I  667  ILE ALA GLU SER ALA ASP GLU VAL ALA GLU GLY PHE ALA          
SEQRES  15 I  667  ARG ALA LYS SER GLU ALA SER SER SER PHE GLY ASP ASP          
SEQRES  16 I  667  ARG VAL PHE VAL GLU LYS PHE ILE THR ASP PRO ARG HIS          
SEQRES  17 I  667  ILE GLU ILE GLN VAL ILE GLY ASP LYS HIS GLY ASN VAL          
SEQRES  18 I  667  ILE TYR LEU GLY GLU ARG GLU CYS SER ILE GLN ARG ARG          
SEQRES  19 I  667  ASN GLN LYS VAL ILE GLU GLU ALA PRO SER PRO LEU LEU          
SEQRES  20 I  667  ASP GLU GLU THR ARG ARG LYS MET GLY GLU GLN ALA VAL          
SEQRES  21 I  667  ALA LEU ALA LYS ALA VAL ASN TYR ASP SER ALA GLY THR          
SEQRES  22 I  667  VAL GLU PHE VAL ALA GLY GLN ASP LYS SER PHE TYR PHE          
SEQRES  23 I  667  LEU GLU MET ASN THR ARG LEU GLN VAL GLU HIS PRO VAL          
SEQRES  24 I  667  THR GLU MET ILE THR GLY LEU ASP LEU VAL GLU LEU MET          
SEQRES  25 I  667  ILE ARG VAL ALA ALA GLY GLU LYS LEU PRO LEU SER GLN          
SEQRES  26 I  667  ASP GLN VAL LYS LEU ASP GLY TRP ALA VAL GLU SER ARG          
SEQRES  27 I  667  VAL TYR ALA GLU ASP PRO THR ARG ASN PHE LEU PRO SER          
SEQRES  28 I  667  ILE GLY ARG LEU THR THR TYR GLN PRO PRO GLU GLU GLY          
SEQRES  29 I  667  PRO LEU GLY GLY ALA ILE VAL ARG ASN ASP THR GLY VAL          
SEQRES  30 I  667  GLU GLU GLY GLY GLU ILE ALA ILE HIS TYR ASP PRO MET          
SEQRES  31 I  667  ILE ALA LYS LEU VAL THR TRP ALA PRO THR ARG LEU GLU          
SEQRES  32 I  667  ALA ILE GLU ALA GLN ALA THR ALA LEU ASP ALA PHE ALA          
SEQRES  33 I  667  ILE GLU GLY ILE ARG HIS ASN ILE PRO PHE LEU ALA THR          
SEQRES  34 I  667  LEU MET ALA HIS PRO ARG TRP ARG ASP GLY ARG LEU SER          
SEQRES  35 I  667  THR GLY PHE ILE LYS GLU GLU PHE PRO GLU GLY PHE ILE          
SEQRES  36 I  667  ALA PRO GLU PRO GLU GLY PRO VAL ALA HIS ARG LEU ALA          
SEQRES  37 I  667  ALA VAL ALA ALA ALA ILE ASP HIS LYS LEU ASN ILE ARG          
SEQRES  38 I  667  LYS ARG GLY ILE SER GLY GLN MET ARG ASP PRO SER LEU          
SEQRES  39 I  667  LEU THR PHE GLN ARG GLU ARG VAL VAL VAL LEU SER GLY          
SEQRES  40 I  667  GLN ARG PHE ASN VAL THR VAL ASP PRO ASP GLY ASP ASP          
SEQRES  41 I  667  LEU LEU VAL THR PHE ASP ASP GLY THR THR ALA PRO VAL          
SEQRES  42 I  667  ARG SER ALA TRP ARG PRO GLY ALA PRO VAL TRP SER GLY          
SEQRES  43 I  667  THR VAL GLY ASP GLN SER VAL ALA ILE GLN VAL ARG PRO          
SEQRES  44 I  667  LEU LEU ASN GLY VAL PHE LEU GLN HIS ALA GLY ALA ALA          
SEQRES  45 I  667  ALA GLU ALA ARG VAL PHE THR ARG ARG GLU ALA GLU LEU          
SEQRES  46 I  667  ALA ASP LEU MET PRO VAL LYS GLU ASN ALA GLY SER GLY          
SEQRES  47 I  667  LYS GLN LEU LEU CYS PRO MET PRO GLY LEU VAL LYS GLN          
SEQRES  48 I  667  ILE MET VAL SER GLU GLY GLN GLU VAL LYS ASN GLY GLU          
SEQRES  49 I  667  PRO LEU ALA ILE VAL GLU ALA MET LYS MET GLU ASN VAL          
SEQRES  50 I  667  LEU ARG ALA GLU ARG ASP GLY THR ILE SER LYS ILE ALA          
SEQRES  51 I  667  ALA LYS GLU GLY ASP SER LEU ALA VAL ASP ALA VAL ILE          
SEQRES  52 I  667  LEU GLU PHE ALA                                              
SEQRES   1 J  667  MET PHE ASP LYS ILE LEU ILE ALA ASN ARG GLY GLU ILE          
SEQRES   2 J  667  ALA CYS ARG ILE ILE LYS THR ALA GLN LYS MET GLY ILE          
SEQRES   3 J  667  LYS THR VAL ALA VAL TYR SER ASP ALA ASP ARG ASP ALA          
SEQRES   4 J  667  VAL HIS VAL ALA MET ALA ASP GLU ALA VAL HIS ILE GLY          
SEQRES   5 J  667  PRO ALA PRO ALA ALA GLN SER TYR LEU LEU ILE GLU LYS          
SEQRES   6 J  667  ILE ILE ASP ALA CYS LYS GLN THR GLY ALA GLN ALA VAL          
SEQRES   7 J  667  HIS PRO GLY TYR GLY PHE LEU SER GLU ARG GLU SER PHE          
SEQRES   8 J  667  PRO LYS ALA LEU ALA GLU ALA GLY ILE VAL PHE ILE GLY          
SEQRES   9 J  667  PRO ASN PRO GLY ALA ILE ALA ALA MET GLY ASP LYS ILE          
SEQRES  10 J  667  GLU SER LYS LYS ALA ALA ALA ALA ALA GLU VAL SER THR          
SEQRES  11 J  667  VAL PRO GLY PHE LEU GLY VAL ILE GLU SER PRO GLU HIS          
SEQRES  12 J  667  ALA VAL THR ILE ALA ASP GLU ILE GLY TYR PRO VAL MET          
SEQRES  13 J  667  ILE LYS ALA SER ALA GLY GLY GLY GLY LYS GLY MET ARG          
SEQRES  14 J  667  ILE ALA GLU SER ALA ASP GLU VAL ALA GLU GLY PHE ALA          
SEQRES  15 J  667  ARG ALA LYS SER GLU ALA SER SER SER PHE GLY ASP ASP          
SEQRES  16 J  667  ARG VAL PHE VAL GLU LYS PHE ILE THR ASP PRO ARG HIS          
SEQRES  17 J  667  ILE GLU ILE GLN VAL ILE GLY ASP LYS HIS GLY ASN VAL          
SEQRES  18 J  667  ILE TYR LEU GLY GLU ARG GLU CYS SER ILE GLN ARG ARG          
SEQRES  19 J  667  ASN GLN LYS VAL ILE GLU GLU ALA PRO SER PRO LEU LEU          
SEQRES  20 J  667  ASP GLU GLU THR ARG ARG LYS MET GLY GLU GLN ALA VAL          
SEQRES  21 J  667  ALA LEU ALA LYS ALA VAL ASN TYR ASP SER ALA GLY THR          
SEQRES  22 J  667  VAL GLU PHE VAL ALA GLY GLN ASP LYS SER PHE TYR PHE          
SEQRES  23 J  667  LEU GLU MET ASN THR ARG LEU GLN VAL GLU HIS PRO VAL          
SEQRES  24 J  667  THR GLU MET ILE THR GLY LEU ASP LEU VAL GLU LEU MET          
SEQRES  25 J  667  ILE ARG VAL ALA ALA GLY GLU LYS LEU PRO LEU SER GLN          
SEQRES  26 J  667  ASP GLN VAL LYS LEU ASP GLY TRP ALA VAL GLU SER ARG          
SEQRES  27 J  667  VAL TYR ALA GLU ASP PRO THR ARG ASN PHE LEU PRO SER          
SEQRES  28 J  667  ILE GLY ARG LEU THR THR TYR GLN PRO PRO GLU GLU GLY          
SEQRES  29 J  667  PRO LEU GLY GLY ALA ILE VAL ARG ASN ASP THR GLY VAL          
SEQRES  30 J  667  GLU GLU GLY GLY GLU ILE ALA ILE HIS TYR ASP PRO MET          
SEQRES  31 J  667  ILE ALA LYS LEU VAL THR TRP ALA PRO THR ARG LEU GLU          
SEQRES  32 J  667  ALA ILE GLU ALA GLN ALA THR ALA LEU ASP ALA PHE ALA          
SEQRES  33 J  667  ILE GLU GLY ILE ARG HIS ASN ILE PRO PHE LEU ALA THR          
SEQRES  34 J  667  LEU MET ALA HIS PRO ARG TRP ARG ASP GLY ARG LEU SER          
SEQRES  35 J  667  THR GLY PHE ILE LYS GLU GLU PHE PRO GLU GLY PHE ILE          
SEQRES  36 J  667  ALA PRO GLU PRO GLU GLY PRO VAL ALA HIS ARG LEU ALA          
SEQRES  37 J  667  ALA VAL ALA ALA ALA ILE ASP HIS LYS LEU ASN ILE ARG          
SEQRES  38 J  667  LYS ARG GLY ILE SER GLY GLN MET ARG ASP PRO SER LEU          
SEQRES  39 J  667  LEU THR PHE GLN ARG GLU ARG VAL VAL VAL LEU SER GLY          
SEQRES  40 J  667  GLN ARG PHE ASN VAL THR VAL ASP PRO ASP GLY ASP ASP          
SEQRES  41 J  667  LEU LEU VAL THR PHE ASP ASP GLY THR THR ALA PRO VAL          
SEQRES  42 J  667  ARG SER ALA TRP ARG PRO GLY ALA PRO VAL TRP SER GLY          
SEQRES  43 J  667  THR VAL GLY ASP GLN SER VAL ALA ILE GLN VAL ARG PRO          
SEQRES  44 J  667  LEU LEU ASN GLY VAL PHE LEU GLN HIS ALA GLY ALA ALA          
SEQRES  45 J  667  ALA GLU ALA ARG VAL PHE THR ARG ARG GLU ALA GLU LEU          
SEQRES  46 J  667  ALA ASP LEU MET PRO VAL LYS GLU ASN ALA GLY SER GLY          
SEQRES  47 J  667  LYS GLN LEU LEU CYS PRO MET PRO GLY LEU VAL LYS GLN          
SEQRES  48 J  667  ILE MET VAL SER GLU GLY GLN GLU VAL LYS ASN GLY GLU          
SEQRES  49 J  667  PRO LEU ALA ILE VAL GLU ALA MET LYS MET GLU ASN VAL          
SEQRES  50 J  667  LEU ARG ALA GLU ARG ASP GLY THR ILE SER LYS ILE ALA          
SEQRES  51 J  667  ALA LYS GLU GLY ASP SER LEU ALA VAL ASP ALA VAL ILE          
SEQRES  52 J  667  LEU GLU PHE ALA                                              
SEQRES   1 K  667  MET PHE ASP LYS ILE LEU ILE ALA ASN ARG GLY GLU ILE          
SEQRES   2 K  667  ALA CYS ARG ILE ILE LYS THR ALA GLN LYS MET GLY ILE          
SEQRES   3 K  667  LYS THR VAL ALA VAL TYR SER ASP ALA ASP ARG ASP ALA          
SEQRES   4 K  667  VAL HIS VAL ALA MET ALA ASP GLU ALA VAL HIS ILE GLY          
SEQRES   5 K  667  PRO ALA PRO ALA ALA GLN SER TYR LEU LEU ILE GLU LYS          
SEQRES   6 K  667  ILE ILE ASP ALA CYS LYS GLN THR GLY ALA GLN ALA VAL          
SEQRES   7 K  667  HIS PRO GLY TYR GLY PHE LEU SER GLU ARG GLU SER PHE          
SEQRES   8 K  667  PRO LYS ALA LEU ALA GLU ALA GLY ILE VAL PHE ILE GLY          
SEQRES   9 K  667  PRO ASN PRO GLY ALA ILE ALA ALA MET GLY ASP LYS ILE          
SEQRES  10 K  667  GLU SER LYS LYS ALA ALA ALA ALA ALA GLU VAL SER THR          
SEQRES  11 K  667  VAL PRO GLY PHE LEU GLY VAL ILE GLU SER PRO GLU HIS          
SEQRES  12 K  667  ALA VAL THR ILE ALA ASP GLU ILE GLY TYR PRO VAL MET          
SEQRES  13 K  667  ILE LYS ALA SER ALA GLY GLY GLY GLY LYS GLY MET ARG          
SEQRES  14 K  667  ILE ALA GLU SER ALA ASP GLU VAL ALA GLU GLY PHE ALA          
SEQRES  15 K  667  ARG ALA LYS SER GLU ALA SER SER SER PHE GLY ASP ASP          
SEQRES  16 K  667  ARG VAL PHE VAL GLU LYS PHE ILE THR ASP PRO ARG HIS          
SEQRES  17 K  667  ILE GLU ILE GLN VAL ILE GLY ASP LYS HIS GLY ASN VAL          
SEQRES  18 K  667  ILE TYR LEU GLY GLU ARG GLU CYS SER ILE GLN ARG ARG          
SEQRES  19 K  667  ASN GLN LYS VAL ILE GLU GLU ALA PRO SER PRO LEU LEU          
SEQRES  20 K  667  ASP GLU GLU THR ARG ARG LYS MET GLY GLU GLN ALA VAL          
SEQRES  21 K  667  ALA LEU ALA LYS ALA VAL ASN TYR ASP SER ALA GLY THR          
SEQRES  22 K  667  VAL GLU PHE VAL ALA GLY GLN ASP LYS SER PHE TYR PHE          
SEQRES  23 K  667  LEU GLU MET ASN THR ARG LEU GLN VAL GLU HIS PRO VAL          
SEQRES  24 K  667  THR GLU MET ILE THR GLY LEU ASP LEU VAL GLU LEU MET          
SEQRES  25 K  667  ILE ARG VAL ALA ALA GLY GLU LYS LEU PRO LEU SER GLN          
SEQRES  26 K  667  ASP GLN VAL LYS LEU ASP GLY TRP ALA VAL GLU SER ARG          
SEQRES  27 K  667  VAL TYR ALA GLU ASP PRO THR ARG ASN PHE LEU PRO SER          
SEQRES  28 K  667  ILE GLY ARG LEU THR THR TYR GLN PRO PRO GLU GLU GLY          
SEQRES  29 K  667  PRO LEU GLY GLY ALA ILE VAL ARG ASN ASP THR GLY VAL          
SEQRES  30 K  667  GLU GLU GLY GLY GLU ILE ALA ILE HIS TYR ASP PRO MET          
SEQRES  31 K  667  ILE ALA LYS LEU VAL THR TRP ALA PRO THR ARG LEU GLU          
SEQRES  32 K  667  ALA ILE GLU ALA GLN ALA THR ALA LEU ASP ALA PHE ALA          
SEQRES  33 K  667  ILE GLU GLY ILE ARG HIS ASN ILE PRO PHE LEU ALA THR          
SEQRES  34 K  667  LEU MET ALA HIS PRO ARG TRP ARG ASP GLY ARG LEU SER          
SEQRES  35 K  667  THR GLY PHE ILE LYS GLU GLU PHE PRO GLU GLY PHE ILE          
SEQRES  36 K  667  ALA PRO GLU PRO GLU GLY PRO VAL ALA HIS ARG LEU ALA          
SEQRES  37 K  667  ALA VAL ALA ALA ALA ILE ASP HIS LYS LEU ASN ILE ARG          
SEQRES  38 K  667  LYS ARG GLY ILE SER GLY GLN MET ARG ASP PRO SER LEU          
SEQRES  39 K  667  LEU THR PHE GLN ARG GLU ARG VAL VAL VAL LEU SER GLY          
SEQRES  40 K  667  GLN ARG PHE ASN VAL THR VAL ASP PRO ASP GLY ASP ASP          
SEQRES  41 K  667  LEU LEU VAL THR PHE ASP ASP GLY THR THR ALA PRO VAL          
SEQRES  42 K  667  ARG SER ALA TRP ARG PRO GLY ALA PRO VAL TRP SER GLY          
SEQRES  43 K  667  THR VAL GLY ASP GLN SER VAL ALA ILE GLN VAL ARG PRO          
SEQRES  44 K  667  LEU LEU ASN GLY VAL PHE LEU GLN HIS ALA GLY ALA ALA          
SEQRES  45 K  667  ALA GLU ALA ARG VAL PHE THR ARG ARG GLU ALA GLU LEU          
SEQRES  46 K  667  ALA ASP LEU MET PRO VAL LYS GLU ASN ALA GLY SER GLY          
SEQRES  47 K  667  LYS GLN LEU LEU CYS PRO MET PRO GLY LEU VAL LYS GLN          
SEQRES  48 K  667  ILE MET VAL SER GLU GLY GLN GLU VAL LYS ASN GLY GLU          
SEQRES  49 K  667  PRO LEU ALA ILE VAL GLU ALA MET LYS MET GLU ASN VAL          
SEQRES  50 K  667  LEU ARG ALA GLU ARG ASP GLY THR ILE SER LYS ILE ALA          
SEQRES  51 K  667  ALA LYS GLU GLY ASP SER LEU ALA VAL ASP ALA VAL ILE          
SEQRES  52 K  667  LEU GLU PHE ALA                                              
SEQRES   1 L  667  MET PHE ASP LYS ILE LEU ILE ALA ASN ARG GLY GLU ILE          
SEQRES   2 L  667  ALA CYS ARG ILE ILE LYS THR ALA GLN LYS MET GLY ILE          
SEQRES   3 L  667  LYS THR VAL ALA VAL TYR SER ASP ALA ASP ARG ASP ALA          
SEQRES   4 L  667  VAL HIS VAL ALA MET ALA ASP GLU ALA VAL HIS ILE GLY          
SEQRES   5 L  667  PRO ALA PRO ALA ALA GLN SER TYR LEU LEU ILE GLU LYS          
SEQRES   6 L  667  ILE ILE ASP ALA CYS LYS GLN THR GLY ALA GLN ALA VAL          
SEQRES   7 L  667  HIS PRO GLY TYR GLY PHE LEU SER GLU ARG GLU SER PHE          
SEQRES   8 L  667  PRO LYS ALA LEU ALA GLU ALA GLY ILE VAL PHE ILE GLY          
SEQRES   9 L  667  PRO ASN PRO GLY ALA ILE ALA ALA MET GLY ASP LYS ILE          
SEQRES  10 L  667  GLU SER LYS LYS ALA ALA ALA ALA ALA GLU VAL SER THR          
SEQRES  11 L  667  VAL PRO GLY PHE LEU GLY VAL ILE GLU SER PRO GLU HIS          
SEQRES  12 L  667  ALA VAL THR ILE ALA ASP GLU ILE GLY TYR PRO VAL MET          
SEQRES  13 L  667  ILE LYS ALA SER ALA GLY GLY GLY GLY LYS GLY MET ARG          
SEQRES  14 L  667  ILE ALA GLU SER ALA ASP GLU VAL ALA GLU GLY PHE ALA          
SEQRES  15 L  667  ARG ALA LYS SER GLU ALA SER SER SER PHE GLY ASP ASP          
SEQRES  16 L  667  ARG VAL PHE VAL GLU LYS PHE ILE THR ASP PRO ARG HIS          
SEQRES  17 L  667  ILE GLU ILE GLN VAL ILE GLY ASP LYS HIS GLY ASN VAL          
SEQRES  18 L  667  ILE TYR LEU GLY GLU ARG GLU CYS SER ILE GLN ARG ARG          
SEQRES  19 L  667  ASN GLN LYS VAL ILE GLU GLU ALA PRO SER PRO LEU LEU          
SEQRES  20 L  667  ASP GLU GLU THR ARG ARG LYS MET GLY GLU GLN ALA VAL          
SEQRES  21 L  667  ALA LEU ALA LYS ALA VAL ASN TYR ASP SER ALA GLY THR          
SEQRES  22 L  667  VAL GLU PHE VAL ALA GLY GLN ASP LYS SER PHE TYR PHE          
SEQRES  23 L  667  LEU GLU MET ASN THR ARG LEU GLN VAL GLU HIS PRO VAL          
SEQRES  24 L  667  THR GLU MET ILE THR GLY LEU ASP LEU VAL GLU LEU MET          
SEQRES  25 L  667  ILE ARG VAL ALA ALA GLY GLU LYS LEU PRO LEU SER GLN          
SEQRES  26 L  667  ASP GLN VAL LYS LEU ASP GLY TRP ALA VAL GLU SER ARG          
SEQRES  27 L  667  VAL TYR ALA GLU ASP PRO THR ARG ASN PHE LEU PRO SER          
SEQRES  28 L  667  ILE GLY ARG LEU THR THR TYR GLN PRO PRO GLU GLU GLY          
SEQRES  29 L  667  PRO LEU GLY GLY ALA ILE VAL ARG ASN ASP THR GLY VAL          
SEQRES  30 L  667  GLU GLU GLY GLY GLU ILE ALA ILE HIS TYR ASP PRO MET          
SEQRES  31 L  667  ILE ALA LYS LEU VAL THR TRP ALA PRO THR ARG LEU GLU          
SEQRES  32 L  667  ALA ILE GLU ALA GLN ALA THR ALA LEU ASP ALA PHE ALA          
SEQRES  33 L  667  ILE GLU GLY ILE ARG HIS ASN ILE PRO PHE LEU ALA THR          
SEQRES  34 L  667  LEU MET ALA HIS PRO ARG TRP ARG ASP GLY ARG LEU SER          
SEQRES  35 L  667  THR GLY PHE ILE LYS GLU GLU PHE PRO GLU GLY PHE ILE          
SEQRES  36 L  667  ALA PRO GLU PRO GLU GLY PRO VAL ALA HIS ARG LEU ALA          
SEQRES  37 L  667  ALA VAL ALA ALA ALA ILE ASP HIS LYS LEU ASN ILE ARG          
SEQRES  38 L  667  LYS ARG GLY ILE SER GLY GLN MET ARG ASP PRO SER LEU          
SEQRES  39 L  667  LEU THR PHE GLN ARG GLU ARG VAL VAL VAL LEU SER GLY          
SEQRES  40 L  667  GLN ARG PHE ASN VAL THR VAL ASP PRO ASP GLY ASP ASP          
SEQRES  41 L  667  LEU LEU VAL THR PHE ASP ASP GLY THR THR ALA PRO VAL          
SEQRES  42 L  667  ARG SER ALA TRP ARG PRO GLY ALA PRO VAL TRP SER GLY          
SEQRES  43 L  667  THR VAL GLY ASP GLN SER VAL ALA ILE GLN VAL ARG PRO          
SEQRES  44 L  667  LEU LEU ASN GLY VAL PHE LEU GLN HIS ALA GLY ALA ALA          
SEQRES  45 L  667  ALA GLU ALA ARG VAL PHE THR ARG ARG GLU ALA GLU LEU          
SEQRES  46 L  667  ALA ASP LEU MET PRO VAL LYS GLU ASN ALA GLY SER GLY          
SEQRES  47 L  667  LYS GLN LEU LEU CYS PRO MET PRO GLY LEU VAL LYS GLN          
SEQRES  48 L  667  ILE MET VAL SER GLU GLY GLN GLU VAL LYS ASN GLY GLU          
SEQRES  49 L  667  PRO LEU ALA ILE VAL GLU ALA MET LYS MET GLU ASN VAL          
SEQRES  50 L  667  LEU ARG ALA GLU ARG ASP GLY THR ILE SER LYS ILE ALA          
SEQRES  51 L  667  ALA LYS GLU GLY ASP SER LEU ALA VAL ASP ALA VAL ILE          
SEQRES  52 L  667  LEU GLU PHE ALA                                              
HET    COA  A 601      48                                                       
HET    COA  B 601      48                                                       
HET    COA  C 601      48                                                       
HET    COA  D 601      48                                                       
HET    COA  E 601      48                                                       
HET    COA  F 601      48                                                       
HET    BTI  G 701      15                                                       
HET    BTI  H 701      15                                                       
HET    BTI  I 701      15                                                       
HET    BTI  J 701      15                                                       
HET    BTI  K 701      15                                                       
HET    BTI  L 701      15                                                       
HETNAM     COA COENZYME A                                                       
HETNAM     BTI 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)                
HETNAM   2 BTI  PENTANAL                                                        
FORMUL  13  COA    6(C21 H36 N7 O16 P3 S)                                       
FORMUL  19  BTI    6(C10 H16 N2 O2 S)                                           
FORMUL  25  HOH   *871(H2 O)                                                    
HELIX    1 AA1 LEU A    5  ARG A   16  1                                  12    
HELIX    2 AA2 GLY A   20  ARG A   30  1                                  11    
HELIX    3 AA3 THR A   34  LEU A   43  1                                  10    
HELIX    4 AA4 GLY A   63  GLN A   67  5                                   5    
HELIX    5 AA5 VAL A   95  SER A   99  5                                   5    
HELIX    6 AA6 SER A  101  ARG A  119  1                                  19    
HELIX    7 AA7 ARG A  132  GLU A  135  5                                   4    
HELIX    8 AA8 GLY A  136  SER A  154  1                                  19    
HELIX    9 AA9 VAL A  172  MET A  177  1                                   6    
HELIX   10 AB1 GLY A  194  ASN A  203  1                                  10    
HELIX   11 AB2 THR A  207  GLY A  213  1                                   7    
HELIX   12 AB3 GLY A  213  LYS A  220  1                                   8    
HELIX   13 AB4 ASN A  230  LEU A  245  1                                  16    
HELIX   14 AB5 ASP A  266  LEU A  272  5                                   7    
HELIX   15 AB6 ASP A  282  VAL A  291  1                                  10    
HELIX   16 AB7 ASP A  292  ASP A  295  5                                   4    
HELIX   17 AB8 VAL A  328  VAL A  332  5                                   5    
HELIX   18 AB9 ASP A  334  PHE A  351  1                                  18    
HELIX   19 AC1 GLY A  367  GLY A  373  1                                   7    
HELIX   20 AC2 GLY A  374  ALA A  389  1                                  16    
HELIX   21 AC3 GLY A  403  MET A  409  1                                   7    
HELIX   22 AC4 SER A  411  GLY A  415  5                                   5    
HELIX   23 AC5 GLY A  431  PHE A  440  1                                  10    
HELIX   24 AC6 ARG A  441  ILE A  444  5                                   4    
HELIX   25 AC7 ASP A  446  LEU A  462  1                                  17    
HELIX   26 AC8 PRO A  464  ARG A  470  1                                   7    
HELIX   27 AC9 MET A  478  HIS A  480  5                                   3    
HELIX   28 AD1 SER A  481  ARG A  494  1                                  14    
HELIX   29 AD2 GLU B    6  ARG B   16  1                                  11    
HELIX   30 AD3 GLY B   20  ARG B   30  1                                  11    
HELIX   31 AD4 THR B   34  LEU B   43  1                                  10    
HELIX   32 AD5 GLY B   63  GLN B   67  5                                   5    
HELIX   33 AD6 VAL B   95  SER B   99  5                                   5    
HELIX   34 AD7 SER B  101  ARG B  119  1                                  19    
HELIX   35 AD8 ARG B  132  GLU B  135  5                                   4    
HELIX   36 AD9 GLY B  136  SER B  154  1                                  19    
HELIX   37 AE1 VAL B  172  MET B  177  1                                   6    
HELIX   38 AE2 GLY B  194  ASN B  203  1                                  10    
HELIX   39 AE3 THR B  207  GLY B  213  1                                   7    
HELIX   40 AE4 GLY B  213  LYS B  220  1                                   8    
HELIX   41 AE5 ASN B  230  ASP B  243  1                                  14    
HELIX   42 AE6 ASP B  266  LEU B  272  5                                   7    
HELIX   43 AE7 ASP B  282  VAL B  291  1                                  10    
HELIX   44 AE8 ASP B  292  ASP B  295  5                                   4    
HELIX   45 AE9 VAL B  328  VAL B  332  5                                   5    
HELIX   46 AF1 ASP B  334  PHE B  351  1                                  18    
HELIX   47 AF2 GLY B  367  GLY B  373  1                                   7    
HELIX   48 AF3 GLY B  374  ALA B  389  1                                  16    
HELIX   49 AF4 GLY B  403  MET B  409  1                                   7    
HELIX   50 AF5 SER B  411  GLY B  415  5                                   5    
HELIX   51 AF6 GLY B  431  PHE B  440  1                                  10    
HELIX   52 AF7 ALA B  447  LEU B  462  1                                  16    
HELIX   53 AF8 PRO B  464  ARG B  470  1                                   7    
HELIX   54 AF9 MET B  478  HIS B  480  5                                   3    
HELIX   55 AG1 SER B  481  ARG B  494  1                                  14    
HELIX   56 AG2 GLU C    6  ARG C   16  1                                  11    
HELIX   57 AG3 GLY C   20  ARG C   30  1                                  11    
HELIX   58 AG4 THR C   34  LEU C   43  1                                  10    
HELIX   59 AG5 GLY C   63  GLN C   67  5                                   5    
HELIX   60 AG6 VAL C   95  SER C   99  5                                   5    
HELIX   61 AG7 SER C  101  ARG C  119  1                                  19    
HELIX   62 AG8 ARG C  132  GLU C  135  5                                   4    
HELIX   63 AG9 GLY C  136  SER C  154  1                                  19    
HELIX   64 AH1 VAL C  172  MET C  177  1                                   6    
HELIX   65 AH2 GLY C  194  ASN C  203  1                                  10    
HELIX   66 AH3 THR C  207  GLY C  213  1                                   7    
HELIX   67 AH4 GLY C  213  LYS C  220  1                                   8    
HELIX   68 AH5 ASN C  230  ASP C  243  1                                  14    
HELIX   69 AH6 ASP C  266  LEU C  272  5                                   7    
HELIX   70 AH7 ASP C  282  VAL C  291  1                                  10    
HELIX   71 AH8 ASP C  292  ASP C  295  5                                   4    
HELIX   72 AH9 VAL C  328  VAL C  332  5                                   5    
HELIX   73 AI1 ASP C  334  PHE C  351  1                                  18    
HELIX   74 AI2 GLY C  367  GLY C  374  1                                   8    
HELIX   75 AI3 GLY C  374  ALA C  389  1                                  16    
HELIX   76 AI4 GLY C  403  MET C  409  1                                   7    
HELIX   77 AI5 SER C  411  GLY C  415  5                                   5    
HELIX   78 AI6 GLY C  431  PHE C  440  1                                  10    
HELIX   79 AI7 ARG C  441  ILE C  444  5                                   4    
HELIX   80 AI8 ALA C  447  LEU C  462  1                                  16    
HELIX   81 AI9 PRO C  464  ARG C  470  1                                   7    
HELIX   82 AJ1 MET C  478  HIS C  480  5                                   3    
HELIX   83 AJ2 SER C  481  ARG C  494  1                                  14    
HELIX   84 AJ3 GLU D    6  ARG D   16  1                                  11    
HELIX   85 AJ4 GLY D   20  ARG D   30  1                                  11    
HELIX   86 AJ5 THR D   34  LEU D   43  1                                  10    
HELIX   87 AJ6 THR D   60  GLN D   67  5                                   8    
HELIX   88 AJ7 VAL D   95  SER D   99  5                                   5    
HELIX   89 AJ8 SER D  101  ARG D  119  1                                  19    
HELIX   90 AJ9 ARG D  132  GLU D  135  5                                   4    
HELIX   91 AK1 GLY D  136  SER D  154  1                                  19    
HELIX   92 AK2 VAL D  172  MET D  177  1                                   6    
HELIX   93 AK3 GLY D  194  ASN D  203  1                                  10    
HELIX   94 AK4 THR D  207  GLY D  213  1                                   7    
HELIX   95 AK5 GLY D  213  LYS D  220  1                                   8    
HELIX   96 AK6 ASN D  230  LEU D  245  1                                  16    
HELIX   97 AK7 ASP D  266  LEU D  272  5                                   7    
HELIX   98 AK8 ASP D  282  VAL D  291  1                                  10    
HELIX   99 AK9 ASP D  292  ASP D  295  5                                   4    
HELIX  100 AL1 VAL D  328  VAL D  332  5                                   5    
HELIX  101 AL2 ASP D  334  PHE D  351  1                                  18    
HELIX  102 AL3 GLY D  367  GLY D  373  1                                   7    
HELIX  103 AL4 GLY D  374  ALA D  389  1                                  16    
HELIX  104 AL5 GLY D  403  MET D  409  1                                   7    
HELIX  105 AL6 SER D  411  GLY D  415  5                                   5    
HELIX  106 AL7 GLY D  431  PHE D  440  1                                  10    
HELIX  107 AL8 ARG D  441  ILE D  444  5                                   4    
HELIX  108 AL9 ALA D  447  LEU D  462  1                                  16    
HELIX  109 AM1 PRO D  464  ARG D  470  1                                   7    
HELIX  110 AM2 MET D  478  HIS D  480  5                                   3    
HELIX  111 AM3 SER D  481  ARG D  494  1                                  14    
HELIX  112 AM4 GLU E    6  ARG E   16  1                                  11    
HELIX  113 AM5 GLY E   20  ARG E   30  1                                  11    
HELIX  114 AM6 THR E   34  LEU E   43  1                                  10    
HELIX  115 AM7 VAL E   95  SER E   99  5                                   5    
HELIX  116 AM8 SER E  101  ARG E  119  1                                  19    
HELIX  117 AM9 ARG E  132  GLU E  135  5                                   4    
HELIX  118 AN1 GLY E  136  SER E  154  1                                  19    
HELIX  119 AN2 VAL E  172  MET E  177  1                                   6    
HELIX  120 AN3 GLY E  194  ASN E  203  1                                  10    
HELIX  121 AN4 THR E  207  GLY E  213  1                                   7    
HELIX  122 AN5 GLY E  213  LYS E  220  1                                   8    
HELIX  123 AN6 ASN E  230  LEU E  245  1                                  16    
HELIX  124 AN7 ASP E  266  LEU E  272  5                                   7    
HELIX  125 AN8 ASP E  282  VAL E  291  1                                  10    
HELIX  126 AN9 ASP E  292  ASP E  295  5                                   4    
HELIX  127 AO1 VAL E  328  VAL E  332  5                                   5    
HELIX  128 AO2 ASP E  334  PHE E  351  1                                  18    
HELIX  129 AO3 GLY E  367  GLY E  373  1                                   7    
HELIX  130 AO4 GLY E  374  ALA E  389  1                                  16    
HELIX  131 AO5 GLY E  403  MET E  409  1                                   7    
HELIX  132 AO6 SER E  411  GLY E  415  5                                   5    
HELIX  133 AO7 GLY E  431  PHE E  440  1                                  10    
HELIX  134 AO8 ALA E  447  LEU E  462  1                                  16    
HELIX  135 AO9 PRO E  464  ARG E  470  1                                   7    
HELIX  136 AP1 MET E  478  HIS E  480  5                                   3    
HELIX  137 AP2 SER E  481  ARG E  494  1                                  14    
HELIX  138 AP3 GLU F    6  ARG F   16  1                                  11    
HELIX  139 AP4 GLY F   20  ARG F   30  1                                  11    
HELIX  140 AP5 THR F   34  LEU F   43  1                                  10    
HELIX  141 AP6 GLY F   63  GLN F   67  5                                   5    
HELIX  142 AP7 VAL F   95  SER F   99  5                                   5    
HELIX  143 AP8 SER F  101  ARG F  119  1                                  19    
HELIX  144 AP9 ARG F  132  GLN F  134  5                                   3    
HELIX  145 AQ1 GLU F  135  SER F  154  1                                  20    
HELIX  146 AQ2 VAL F  172  MET F  177  1                                   6    
HELIX  147 AQ3 GLY F  194  ASN F  203  1                                  10    
HELIX  148 AQ4 THR F  207  GLY F  213  1                                   7    
HELIX  149 AQ5 GLY F  213  LYS F  220  1                                   8    
HELIX  150 AQ6 ASN F  230  ASP F  243  1                                  14    
HELIX  151 AQ7 ASP F  266  LEU F  272  5                                   7    
HELIX  152 AQ8 ASP F  282  VAL F  291  1                                  10    
HELIX  153 AQ9 ASP F  292  ASP F  295  5                                   4    
HELIX  154 AR1 VAL F  328  VAL F  332  5                                   5    
HELIX  155 AR2 ASP F  334  PHE F  351  1                                  18    
HELIX  156 AR3 GLY F  367  GLY F  373  1                                   7    
HELIX  157 AR4 GLY F  374  ALA F  389  1                                  16    
HELIX  158 AR5 GLY F  403  MET F  409  1                                   7    
HELIX  159 AR6 SER F  411  GLY F  415  5                                   5    
HELIX  160 AR7 GLY F  431  PHE F  440  1                                  10    
HELIX  161 AR8 ARG F  441  ILE F  444  5                                   4    
HELIX  162 AR9 ALA F  447  LEU F  462  1                                  16    
HELIX  163 AS1 PRO F  464  ARG F  470  1                                   7    
HELIX  164 AS2 MET F  478  HIS F  480  5                                   3    
HELIX  165 AS3 SER F  481  ARG F  494  1                                  14    
HELIX  166 AS4 GLY G  461  ARG G  483  1                                  23    
HELIX  167 AS5 THR G  579  LEU G  588  1                                  10    
HELIX  168 AS6 GLY H  461  ARG H  483  1                                  23    
HELIX  169 AS7 ASP H  491  LEU H  495  5                                   5    
HELIX  170 AS8 THR H  579  ASP H  587  1                                   9    
HELIX  171 AS9 PRO I  462  ARG I  483  1                                  22    
HELIX  172 AT1 ASP I  491  LEU I  495  5                                   5    
HELIX  173 AT2 THR I  579  ASP I  587  1                                   9    
HELIX  174 AT3 GLY J  461  ARG J  483  1                                  23    
HELIX  175 AT4 ASP J  491  LEU J  495  5                                   5    
HELIX  176 AT5 THR J  579  ASP J  587  1                                   9    
HELIX  177 AT6 GLY K  461  ARG K  483  1                                  23    
HELIX  178 AT7 ASP K  491  LEU K  495  5                                   5    
HELIX  179 AT8 THR K  579  ASP K  587  1                                   9    
HELIX  180 AT9 GLY L  461  ARG L  483  1                                  23    
HELIX  181 AU1 THR L  579  ASP L  587  1                                   9    
SHEET    1 AA1 7 GLU A  49  PHE A  51  0                                        
SHEET    2 AA1 7 VAL A  74  VAL A  81 -1  O  TRP A  78   N  GLU A  49           
SHEET    3 AA1 7 ARG A  84  LYS A  91 -1  O  LEU A  88   N  GLY A  77           
SHEET    4 AA1 7 ILE A 122  PHE A 126  1  O  ILE A 123   N  PHE A  87           
SHEET    5 AA1 7 GLN A 159  ILE A 163  1  O  VAL A 162   N  PHE A 126           
SHEET    6 AA1 7 PHE A 180  VAL A 184  1  O  PHE A 182   N  ILE A 163           
SHEET    7 AA1 7 GLY A 226  PHE A 228  1  O  GLY A 226   N  MET A 183           
SHEET    1 AA2 2 PRO A 166  ALA A 168  0                                        
SHEET    2 AA2 2 TYR A 189  PHE A 191  1  O  PHE A 191   N  CYS A 167           
SHEET    1 AA3 6 PHE A 297  ILE A 299  0                                        
SHEET    2 AA3 6 ILE A 307  VAL A 314 -1  O  PHE A 311   N  PHE A 297           
SHEET    3 AA3 6 ARG A 317  ASN A 324 -1  O  ALA A 323   N  ILE A 308           
SHEET    4 AA3 6 ILE A 355  VAL A 361  1  O  VAL A 356   N  GLY A 320           
SHEET    5 AA3 6 LEU A 393  PHE A 402  1  O  ILE A 396   N  THR A 357           
SHEET    6 AA3 6 GLN A 426  ALA A 428  1  O  GLN A 426   N  ARG A 399           
SHEET    1 AA4 7 PHE A 297  ILE A 299  0                                        
SHEET    2 AA4 7 ILE A 307  VAL A 314 -1  O  PHE A 311   N  PHE A 297           
SHEET    3 AA4 7 ARG A 317  ASN A 324 -1  O  ALA A 323   N  ILE A 308           
SHEET    4 AA4 7 ILE A 355  VAL A 361  1  O  VAL A 356   N  GLY A 320           
SHEET    5 AA4 7 LEU A 393  PHE A 402  1  O  ILE A 396   N  THR A 357           
SHEET    6 AA4 7 LEU A 418  ALA A 421  1  O  TYR A 420   N  THR A 395           
SHEET    7 AA4 7 GLU A 475  VAL A 476  1  O  GLU A 475   N  ALA A 421           
SHEET    1 AA5 7 GLU B  49  PHE B  51  0                                        
SHEET    2 AA5 7 VAL B  74  VAL B  81 -1  O  TRP B  78   N  GLU B  49           
SHEET    3 AA5 7 ARG B  84  LYS B  91 -1  O  SER B  90   N  VAL B  75           
SHEET    4 AA5 7 ILE B 122  PHE B 126  1  O  ILE B 125   N  PHE B  89           
SHEET    5 AA5 7 GLN B 159  ILE B 163  1  O  VAL B 162   N  PHE B 126           
SHEET    6 AA5 7 PHE B 180  VAL B 184  1  O  PHE B 182   N  ILE B 163           
SHEET    7 AA5 7 GLY B 226  PHE B 228  1  O  GLY B 226   N  MET B 183           
SHEET    1 AA6 2 PRO B 166  ALA B 168  0                                        
SHEET    2 AA6 2 TYR B 189  PHE B 191  1  O  PHE B 191   N  CYS B 167           
SHEET    1 AA7 6 PHE B 297  GLU B 298  0                                        
SHEET    2 AA7 6 ILE B 307  VAL B 314 -1  O  PHE B 311   N  PHE B 297           
SHEET    3 AA7 6 ARG B 317  ASN B 324 -1  O  VAL B 319   N  GLY B 312           
SHEET    4 AA7 6 ILE B 355  VAL B 361  1  O  VAL B 356   N  GLY B 320           
SHEET    5 AA7 6 LEU B 393  PHE B 402  1  O  ILE B 396   N  VAL B 359           
SHEET    6 AA7 6 ILE B 427  ALA B 428  1  O  ALA B 428   N  ALA B 401           
SHEET    1 AA8 7 PHE B 297  GLU B 298  0                                        
SHEET    2 AA8 7 ILE B 307  VAL B 314 -1  O  PHE B 311   N  PHE B 297           
SHEET    3 AA8 7 ARG B 317  ASN B 324 -1  O  VAL B 319   N  GLY B 312           
SHEET    4 AA8 7 ILE B 355  VAL B 361  1  O  VAL B 356   N  GLY B 320           
SHEET    5 AA8 7 LEU B 393  PHE B 402  1  O  ILE B 396   N  VAL B 359           
SHEET    6 AA8 7 LEU B 418  ALA B 421  1  O  TYR B 420   N  THR B 395           
SHEET    7 AA8 7 GLU B 475  VAL B 476  1  O  GLU B 475   N  ALA B 421           
SHEET    1 AA9 7 GLU C  49  PHE C  51  0                                        
SHEET    2 AA9 7 VAL C  74  VAL C  81 -1  O  TRP C  78   N  GLU C  49           
SHEET    3 AA9 7 ARG C  84  LYS C  91 -1  O  VAL C  86   N  GLY C  79           
SHEET    4 AA9 7 ILE C 122  PHE C 126  1  O  ILE C 125   N  LYS C  91           
SHEET    5 AA9 7 GLN C 159  ILE C 163  1  O  VAL C 162   N  PHE C 126           
SHEET    6 AA9 7 PHE C 180  VAL C 184  1  O  PHE C 182   N  ILE C 163           
SHEET    7 AA9 7 GLY C 226  PHE C 228  1  O  GLY C 226   N  MET C 183           
SHEET    1 AB1 2 PRO C 166  ALA C 168  0                                        
SHEET    2 AB1 2 TYR C 189  PHE C 191  1  O  PHE C 191   N  CYS C 167           
SHEET    1 AB2 6 PHE C 297  ILE C 299  0                                        
SHEET    2 AB2 6 ILE C 307  VAL C 314 -1  O  PHE C 311   N  PHE C 297           
SHEET    3 AB2 6 ARG C 317  ASN C 324 -1  O  VAL C 319   N  GLY C 312           
SHEET    4 AB2 6 ILE C 355  VAL C 361  1  O  VAL C 356   N  GLY C 320           
SHEET    5 AB2 6 LEU C 393  PHE C 402  1  O  ILE C 396   N  VAL C 359           
SHEET    6 AB2 6 GLN C 426  ALA C 428  1  O  GLN C 426   N  ARG C 399           
SHEET    1 AB3 7 PHE C 297  ILE C 299  0                                        
SHEET    2 AB3 7 ILE C 307  VAL C 314 -1  O  PHE C 311   N  PHE C 297           
SHEET    3 AB3 7 ARG C 317  ASN C 324 -1  O  VAL C 319   N  GLY C 312           
SHEET    4 AB3 7 ILE C 355  VAL C 361  1  O  VAL C 356   N  GLY C 320           
SHEET    5 AB3 7 LEU C 393  PHE C 402  1  O  ILE C 396   N  VAL C 359           
SHEET    6 AB3 7 LEU C 418  ALA C 421  1  O  TYR C 420   N  THR C 395           
SHEET    7 AB3 7 GLU C 475  VAL C 476  1  O  GLU C 475   N  ALA C 421           
SHEET    1 AB4 7 GLU D  49  PHE D  51  0                                        
SHEET    2 AB4 7 VAL D  74  VAL D  81 -1  O  TRP D  78   N  GLU D  49           
SHEET    3 AB4 7 ARG D  84  LYS D  91 -1  O  SER D  90   N  VAL D  75           
SHEET    4 AB4 7 ILE D 122  PHE D 126  1  O  ILE D 125   N  PHE D  89           
SHEET    5 AB4 7 GLN D 159  ILE D 163  1  O  VAL D 162   N  PHE D 126           
SHEET    6 AB4 7 PHE D 180  VAL D 184  1  O  PHE D 182   N  ILE D 163           
SHEET    7 AB4 7 GLY D 226  PHE D 228  1  O  GLY D 226   N  MET D 183           
SHEET    1 AB5 2 PRO D 166  ALA D 168  0                                        
SHEET    2 AB5 2 TYR D 189  PHE D 191  1  O  PHE D 191   N  CYS D 167           
SHEET    1 AB6 6 PHE D 297  GLU D 298  0                                        
SHEET    2 AB6 6 ILE D 307  VAL D 314 -1  O  PHE D 311   N  PHE D 297           
SHEET    3 AB6 6 ARG D 317  ASN D 324 -1  O  VAL D 319   N  GLY D 312           
SHEET    4 AB6 6 ILE D 355  VAL D 361  1  O  VAL D 356   N  GLY D 320           
SHEET    5 AB6 6 LEU D 393  PHE D 402  1  O  THR D 398   N  VAL D 359           
SHEET    6 AB6 6 GLN D 426  ALA D 428  1  O  GLN D 426   N  ALA D 401           
SHEET    1 AB7 7 PHE D 297  GLU D 298  0                                        
SHEET    2 AB7 7 ILE D 307  VAL D 314 -1  O  PHE D 311   N  PHE D 297           
SHEET    3 AB7 7 ARG D 317  ASN D 324 -1  O  VAL D 319   N  GLY D 312           
SHEET    4 AB7 7 ILE D 355  VAL D 361  1  O  VAL D 356   N  GLY D 320           
SHEET    5 AB7 7 LEU D 393  PHE D 402  1  O  THR D 398   N  VAL D 359           
SHEET    6 AB7 7 LEU D 418  ALA D 421  1  O  TYR D 420   N  THR D 395           
SHEET    7 AB7 7 GLU D 475  VAL D 476  1  O  GLU D 475   N  ALA D 421           
SHEET    1 AB8 7 GLU E  49  PHE E  51  0                                        
SHEET    2 AB8 7 VAL E  74  VAL E  81 -1  O  TRP E  78   N  GLU E  49           
SHEET    3 AB8 7 ARG E  84  LYS E  91 -1  O  SER E  90   N  VAL E  75           
SHEET    4 AB8 7 ILE E 122  PHE E 126  1  O  ILE E 125   N  LYS E  91           
SHEET    5 AB8 7 GLN E 159  ILE E 163  1  O  ILE E 160   N  GLY E 124           
SHEET    6 AB8 7 PHE E 180  VAL E 184  1  O  PHE E 182   N  ILE E 163           
SHEET    7 AB8 7 GLY E 226  PHE E 228  1  O  GLY E 226   N  MET E 183           
SHEET    1 AB9 2 PRO E 166  ALA E 168  0                                        
SHEET    2 AB9 2 TYR E 189  PHE E 191  1  O  PHE E 191   N  CYS E 167           
SHEET    1 AC1 6 PHE E 297  ILE E 299  0                                        
SHEET    2 AC1 6 ILE E 307  VAL E 314 -1  O  PHE E 311   N  PHE E 297           
SHEET    3 AC1 6 ARG E 317  ASN E 324 -1  O  VAL E 319   N  GLY E 312           
SHEET    4 AC1 6 ILE E 355  VAL E 361  1  O  VAL E 356   N  GLY E 320           
SHEET    5 AC1 6 LEU E 393  PHE E 402  1  O  ILE E 396   N  VAL E 359           
SHEET    6 AC1 6 ILE E 427  ALA E 428  1  O  ALA E 428   N  ALA E 401           
SHEET    1 AC2 7 PHE E 297  ILE E 299  0                                        
SHEET    2 AC2 7 ILE E 307  VAL E 314 -1  O  PHE E 311   N  PHE E 297           
SHEET    3 AC2 7 ARG E 317  ASN E 324 -1  O  VAL E 319   N  GLY E 312           
SHEET    4 AC2 7 ILE E 355  VAL E 361  1  O  VAL E 356   N  GLY E 320           
SHEET    5 AC2 7 LEU E 393  PHE E 402  1  O  ILE E 396   N  VAL E 359           
SHEET    6 AC2 7 LEU E 418  ALA E 421  1  O  TYR E 420   N  THR E 395           
SHEET    7 AC2 7 GLU E 475  VAL E 476  1  O  GLU E 475   N  ALA E 421           
SHEET    1 AC3 6 GLU F  49  PHE F  51  0                                        
SHEET    2 AC3 6 VAL F  74  VAL F  81 -1  O  TRP F  78   N  GLU F  49           
SHEET    3 AC3 6 ARG F  84  LYS F  91 -1  O  VAL F  86   N  GLY F  79           
SHEET    4 AC3 6 ILE F 122  ALA F 128  1  O  ILE F 123   N  PHE F  87           
SHEET    5 AC3 6 GLN F 159  ALA F 168  1  O  PRO F 166   N  ALA F 128           
SHEET    6 AC3 6 TYR F 189  PHE F 191  1  O  TYR F 189   N  CYS F 167           
SHEET    1 AC4 7 GLU F  49  PHE F  51  0                                        
SHEET    2 AC4 7 VAL F  74  VAL F  81 -1  O  TRP F  78   N  GLU F  49           
SHEET    3 AC4 7 ARG F  84  LYS F  91 -1  O  VAL F  86   N  GLY F  79           
SHEET    4 AC4 7 ILE F 122  ALA F 128  1  O  ILE F 123   N  PHE F  87           
SHEET    5 AC4 7 GLN F 159  ALA F 168  1  O  PRO F 166   N  ALA F 128           
SHEET    6 AC4 7 PHE F 180  VAL F 184  1  O  PHE F 182   N  ILE F 163           
SHEET    7 AC4 7 GLY F 226  PHE F 228  1  O  GLY F 226   N  MET F 183           
SHEET    1 AC5 6 PHE F 297  ILE F 299  0                                        
SHEET    2 AC5 6 ILE F 307  VAL F 314 -1  O  PHE F 311   N  PHE F 297           
SHEET    3 AC5 6 ARG F 317  ASN F 324 -1  O  ALA F 323   N  ILE F 308           
SHEET    4 AC5 6 ILE F 355  VAL F 361  1  O  VAL F 356   N  GLY F 320           
SHEET    5 AC5 6 LEU F 393  PHE F 402  1  O  ILE F 396   N  VAL F 359           
SHEET    6 AC5 6 GLN F 426  ALA F 428  1  O  GLN F 426   N  ALA F 401           
SHEET    1 AC6 7 PHE F 297  ILE F 299  0                                        
SHEET    2 AC6 7 ILE F 307  VAL F 314 -1  O  PHE F 311   N  PHE F 297           
SHEET    3 AC6 7 ARG F 317  ASN F 324 -1  O  ALA F 323   N  ILE F 308           
SHEET    4 AC6 7 ILE F 355  VAL F 361  1  O  VAL F 356   N  GLY F 320           
SHEET    5 AC6 7 LEU F 393  PHE F 402  1  O  ILE F 396   N  VAL F 359           
SHEET    6 AC6 7 LEU F 418  ALA F 421  1  O  TYR F 420   N  THR F 395           
SHEET    7 AC6 7 GLU F 475  VAL F 476  1  O  GLU F 475   N  ALA F 421           
SHEET    1 AC7 9 GLU G 500  LEU G 505  0                                        
SHEET    2 AC7 9 ARG G 509  ASP G 517 -1  O  PHE G 510   N  VAL G 503           
SHEET    3 AC7 9 ASP G 520  THR G 524 -1  O  THR G 524   N  THR G 513           
SHEET    4 AC7 9 THR G 530  SER G 535 -1  O  VAL G 533   N  LEU G 521           
SHEET    5 AC7 9 VAL G 543  VAL G 548 -1  O  THR G 547   N  ARG G 534           
SHEET    6 AC7 9 SER G 552  LEU G 560 -1  O  ILE G 555   N  TRP G 544           
SHEET    7 AC7 9 GLY G 563  HIS G 568 -1  O  GLY G 563   N  LEU G 560           
SHEET    8 AC7 9 ALA G 571  PHE G 578 -1  O  ALA G 575   N  VAL G 564           
SHEET    9 AC7 9 GLU G 500  LEU G 505 -1  N  VAL G 504   O  ARG G 576           
SHEET    1 AC8 3 GLN G 600  LEU G 602  0                                        
SHEET    2 AC8 3 VAL G 662  GLU G 665 -1  O  LEU G 664   N  LEU G 601           
SHEET    3 AC8 3 LYS G 648  ILE G 649 -1  N  LYS G 648   O  GLU G 665           
SHEET    1 AC9 4 VAL G 637  ARG G 639  0                                        
SHEET    2 AC9 4 PRO G 625  GLU G 630 -1  N  LEU G 626   O  LEU G 638           
SHEET    3 AC9 4 GLY G 607  ILE G 612 -1  N  LEU G 608   O  GLU G 630           
SHEET    4 AC9 4 SER G 656  LEU G 657 -1  O  LEU G 657   N  GLY G 607           
SHEET    1 AD1 2 GLU G 619  VAL G 620  0                                        
SHEET    2 AD1 2 GLY G 644  THR G 645 -1  O  GLY G 644   N  VAL G 620           
SHEET    1 AD2 9 GLU H 500  LEU H 505  0                                        
SHEET    2 AD2 9 ARG H 509  ASP H 517 -1  O  VAL H 512   N  ARG H 501           
SHEET    3 AD2 9 ASP H 520  THR H 524 -1  O  ASP H 520   N  ASP H 517           
SHEET    4 AD2 9 THR H 530  SER H 535 -1  O  ALA H 531   N  VAL H 523           
SHEET    5 AD2 9 VAL H 543  VAL H 548 -1  O  THR H 547   N  ARG H 534           
SHEET    6 AD2 9 SER H 552  LEU H 560 -1  O  ILE H 555   N  TRP H 544           
SHEET    7 AD2 9 GLY H 563  HIS H 568 -1  O  PHE H 565   N  ARG H 558           
SHEET    8 AD2 9 ALA H 571  PHE H 578 -1  O  ALA H 573   N  LEU H 566           
SHEET    9 AD2 9 GLU H 500  LEU H 505 -1  N  VAL H 504   O  ARG H 576           
SHEET    1 AD3 2 GLN H 600  LEU H 602  0                                        
SHEET    2 AD3 2 VAL H 662  GLU H 665 -1  O  LEU H 664   N  LEU H 601           
SHEET    1 AD4 4 VAL H 637  ARG H 639  0                                        
SHEET    2 AD4 4 PRO H 625  GLU H 630 -1  N  ALA H 627   O  LEU H 638           
SHEET    3 AD4 4 GLY H 607  ILE H 612 -1  N  LYS H 610   O  ILE H 628           
SHEET    4 AD4 4 SER H 656  LEU H 657 -1  O  LEU H 657   N  GLY H 607           
SHEET    1 AD5 2 GLU H 619  VAL H 620  0                                        
SHEET    2 AD5 2 GLY H 644  THR H 645 -1  O  GLY H 644   N  VAL H 620           
SHEET    1 AD6 9 GLU I 500  LEU I 505  0                                        
SHEET    2 AD6 9 ARG I 509  ASP I 517 -1  O  PHE I 510   N  VAL I 503           
SHEET    3 AD6 9 ASP I 520  PHE I 525 -1  O  ASP I 520   N  ASP I 517           
SHEET    4 AD6 9 THR I 530  SER I 535 -1  O  VAL I 533   N  LEU I 521           
SHEET    5 AD6 9 VAL I 543  VAL I 548 -1  O  THR I 547   N  ARG I 534           
SHEET    6 AD6 9 SER I 552  LEU I 560 -1  O  ILE I 555   N  TRP I 544           
SHEET    7 AD6 9 GLY I 563  HIS I 568 -1  O  GLY I 563   N  LEU I 560           
SHEET    8 AD6 9 ALA I 571  PHE I 578 -1  O  ALA I 573   N  LEU I 566           
SHEET    9 AD6 9 GLU I 500  LEU I 505 -1  N  VAL I 504   O  ARG I 576           
SHEET    1 AD7 3 GLN I 600  LEU I 602  0                                        
SHEET    2 AD7 3 VAL I 662  GLU I 665 -1  O  ILE I 663   N  LEU I 601           
SHEET    3 AD7 3 LYS I 648  ILE I 649 -1  N  LYS I 648   O  GLU I 665           
SHEET    1 AD8 4 GLU I 635  ARG I 639  0                                        
SHEET    2 AD8 4 PRO I 625  GLU I 630 -1  N  LEU I 626   O  LEU I 638           
SHEET    3 AD8 4 GLY I 607  ILE I 612 -1  N  LYS I 610   O  ILE I 628           
SHEET    4 AD8 4 SER I 656  LEU I 657 -1  O  LEU I 657   N  GLY I 607           
SHEET    1 AD9 2 GLU I 619  VAL I 620  0                                        
SHEET    2 AD9 2 GLY I 644  THR I 645 -1  O  GLY I 644   N  VAL I 620           
SHEET    1 AE1 9 GLU J 500  LEU J 505  0                                        
SHEET    2 AE1 9 ARG J 509  ASP J 517 -1  O  PHE J 510   N  VAL J 503           
SHEET    3 AE1 9 ASP J 520  THR J 524 -1  O  THR J 524   N  THR J 513           
SHEET    4 AE1 9 THR J 530  SER J 535 -1  O  ALA J 531   N  VAL J 523           
SHEET    5 AE1 9 VAL J 543  VAL J 548 -1  O  THR J 547   N  ARG J 534           
SHEET    6 AE1 9 GLN J 551  LEU J 560 -1  O  ILE J 555   N  TRP J 544           
SHEET    7 AE1 9 GLY J 563  HIS J 568 -1  O  PHE J 565   N  ARG J 558           
SHEET    8 AE1 9 ALA J 571  PHE J 578 -1  O  ALA J 573   N  LEU J 566           
SHEET    9 AE1 9 GLU J 500  LEU J 505 -1  N  VAL J 504   O  ARG J 576           
SHEET    1 AE2 3 GLN J 600  LEU J 602  0                                        
SHEET    2 AE2 3 VAL J 662  GLU J 665 -1  O  LEU J 664   N  LEU J 601           
SHEET    3 AE2 3 LYS J 648  ILE J 649 -1  N  LYS J 648   O  GLU J 665           
SHEET    1 AE3 4 GLU J 635  ARG J 639  0                                        
SHEET    2 AE3 4 PRO J 625  GLU J 630 -1  N  ALA J 627   O  LEU J 638           
SHEET    3 AE3 4 GLY J 607  ILE J 612 -1  N  LYS J 610   O  ILE J 628           
SHEET    4 AE3 4 SER J 656  LEU J 657 -1  O  LEU J 657   N  GLY J 607           
SHEET    1 AE4 2 GLU J 619  VAL J 620  0                                        
SHEET    2 AE4 2 GLY J 644  THR J 645 -1  O  GLY J 644   N  VAL J 620           
SHEET    1 AE5 9 GLU K 500  LEU K 505  0                                        
SHEET    2 AE5 9 ARG K 509  ASP K 517 -1  O  VAL K 512   N  ARG K 501           
SHEET    3 AE5 9 ASP K 520  PHE K 525 -1  O  THR K 524   N  THR K 513           
SHEET    4 AE5 9 THR K 530  SER K 535 -1  O  VAL K 533   N  LEU K 521           
SHEET    5 AE5 9 VAL K 543  VAL K 548 -1  O  THR K 547   N  ARG K 534           
SHEET    6 AE5 9 SER K 552  LEU K 560 -1  O  ILE K 555   N  TRP K 544           
SHEET    7 AE5 9 GLY K 563  HIS K 568 -1  O  GLY K 563   N  LEU K 560           
SHEET    8 AE5 9 ALA K 571  PHE K 578 -1  O  ALA K 575   N  VAL K 564           
SHEET    9 AE5 9 GLU K 500  LEU K 505 -1  N  VAL K 504   O  ARG K 576           
SHEET    1 AE6 3 LEU K 601  CYS K 603  0                                        
SHEET    2 AE6 3 ALA K 661  GLU K 665 -1  O  ALA K 661   N  CYS K 603           
SHEET    3 AE6 3 LYS K 648  ILE K 649 -1  N  LYS K 648   O  GLU K 665           
SHEET    1 AE7 4 GLU K 635  ARG K 639  0                                        
SHEET    2 AE7 4 PRO K 625  GLU K 630 -1  N  LEU K 626   O  LEU K 638           
SHEET    3 AE7 4 GLY K 607  ILE K 612 -1  N  LEU K 608   O  GLU K 630           
SHEET    4 AE7 4 SER K 656  LEU K 657 -1  O  LEU K 657   N  GLY K 607           
SHEET    1 AE8 2 GLU K 619  VAL K 620  0                                        
SHEET    2 AE8 2 GLY K 644  THR K 645 -1  O  GLY K 644   N  VAL K 620           
SHEET    1 AE9 9 GLU L 500  LEU L 505  0                                        
SHEET    2 AE9 9 GLN L 508  PRO L 516 -1  O  GLN L 508   N  LEU L 505           
SHEET    3 AE9 9 LEU L 521  THR L 524 -1  O  THR L 524   N  THR L 513           
SHEET    4 AE9 9 THR L 530  SER L 535 -1  O  ALA L 531   N  VAL L 523           
SHEET    5 AE9 9 VAL L 543  VAL L 548 -1  O  THR L 547   N  ARG L 534           
SHEET    6 AE9 9 SER L 552  LEU L 560 -1  O  ILE L 555   N  TRP L 544           
SHEET    7 AE9 9 GLY L 563  HIS L 568 -1  O  PHE L 565   N  ARG L 558           
SHEET    8 AE9 9 ALA L 571  PHE L 578 -1  O  ALA L 575   N  VAL L 564           
SHEET    9 AE9 9 GLU L 500  LEU L 505 -1  N  VAL L 504   O  ARG L 576           
SHEET    1 AF1 2 GLN L 600  CYS L 603  0                                        
SHEET    2 AF1 2 ALA L 661  GLU L 665 -1  O  ILE L 663   N  LEU L 601           
SHEET    1 AF2 3 LEU L 608  ILE L 612  0                                        
SHEET    2 AF2 3 PRO L 625  ALA L 631 -1  O  GLU L 630   N  LEU L 608           
SHEET    3 AF2 3 MET L 634  ARG L 639 -1  O  LEU L 638   N  ALA L 627           
SHEET    1 AF3 2 GLU L 619  VAL L 620  0                                        
SHEET    2 AF3 2 GLY L 644  THR L 645 -1  O  GLY L 644   N  VAL L 620           
LINK         NZ  LYS G 633                 C11 BTI G 701     1555   1555  1.52  
LINK         NZ  LYS H 633                 C11 BTI H 701     1555   1555  1.47  
LINK         NZ  LYS I 633                 C11 BTI I 701     1555   1555  1.53  
LINK         NZ  LYS J 633                 C11 BTI J 701     1555   1555  1.51  
LINK         NZ  LYS K 633                 C11 BTI K 701     1555   1555  1.53  
LINK         NZ  LYS L 633                 C11 BTI L 701     1555   1555  1.50  
SITE     1 AC1  9 ARG A  23  GLY A  97  GLY A 129  ALA A 131                    
SITE     2 AC1  9 ARG A 132  ILE A 133  GLN A 134  TYR A 189                    
SITE     3 AC1  9 ARG B 441                                                     
SITE     1 AC2 11 ILE A 438  ARG A 441  ARG B  23  PHE B  93                    
SITE     2 AC2 11 PHE B  96  GLY B  97  GLY B 129  ALA B 131                    
SITE     3 AC2 11 ARG B 132  ILE B 133  GLN B 134                               
SITE     1 AC3  7 ARG C  23  GLY C  97  GLY C 129  ALA C 131                    
SITE     2 AC3  7 ARG C 132  ILE C 133  ARG D 441                               
SITE     1 AC4  8 ARG C 441  ARG D  23  GLY D  97  GLY D 129                    
SITE     2 AC4  8 ALA D 131  ARG D 132  ILE D 133  GLN D 134                    
SITE     1 AC5 10 ARG E  23  GLY E  97  GLY E 129  ALA E 131                    
SITE     2 AC5 10 ARG E 132  ILE E 133  GLN E 134  TYR E 189                    
SITE     3 AC5 10 ASP E 196  ARG F 441                                          
SITE     1 AC6  8 ARG E 441  ARG F  23  GLY F  97  GLY F 129                    
SITE     2 AC6  8 ALA F 131  ARG F 132  ILE F 133  ASP F 196                    
SITE     1 AC7  9 ASN A 278  PRO A 362  GLY A 363  PHE A 364                    
SITE     2 AC7  9 HOH A 731  GLU G 630  ALA G 631  MET G 632                    
SITE     3 AC7  9 MET G 634                                                     
SITE     1 AC8  5 ASN C 278  PHE C 364  ALA H 631  MET H 632                    
SITE     2 AC8  5 MET H 634                                                     
SITE     1 AC9  7 ASN E 278  VAL E 332  PHE E 364  ALA I 631                    
SITE     2 AC9  7 MET I 632  MET I 634  HOH I 807                               
SITE     1 AD1  7 ASN B 278  VAL B 332  PHE B 364  GLU J 630                    
SITE     2 AD1  7 ALA J 631  MET J 632  MET J 634                               
SITE     1 AD2  7 ASN F 278  PHE F 364  GLU K 630  ALA K 631                    
SITE     2 AD2  7 MET K 632  MET K 634  HOH K 804                               
SITE     1 AD3  6 ASN D 278  PHE D 364  GLU L 630  ALA L 631                    
SITE     2 AD3  6 MET L 632  MET L 634                                          
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1                      
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
ATOM      1  N   LEU A   5     118.573 170.380  99.040  1.00 49.26           N  
ATOM      2  CA  LEU A   5     117.594 169.609  98.284  1.00 49.26           C  
ATOM      3  C   LEU A   5     116.234 169.677  98.982  1.00 49.26           C  
ATOM      4  O   LEU A   5     116.109 169.360 100.165  1.00 49.26           O  
ATOM      5  CB  LEU A   5     118.073 168.165  98.121  1.00 49.26           C  
ATOM      6  CG  LEU A   5     117.221 167.211  97.280  1.00 49.26           C  
ATOM      7  CD1 LEU A   5     118.044 166.393  96.288  1.00 49.26           C  
ATOM      8  CD2 LEU A   5     116.470 166.283  98.195  1.00 49.26           C  
ATOM      9  N   GLU A   6     115.218 170.101  98.227  1.00 54.87           N  
ATOM     10  CA  GLU A   6     113.930 170.446  98.820  1.00 54.87           C  
ATOM     11  C   GLU A   6     113.208 169.218  99.365  1.00 54.87           C  
ATOM     12  O   GLU A   6     112.453 169.318 100.340  1.00 54.87           O  
ATOM     13  CB  GLU A   6     113.060 171.157  97.782  1.00 54.87           C  
ATOM     14  CG  GLU A   6     113.732 172.344  97.110  1.00 54.87           C  
ATOM     15  CD  GLU A   6     113.013 172.783  95.851  1.00 54.87           C  
ATOM     16  OE1 GLU A   6     111.773 172.643  95.792  1.00 54.87           O  
ATOM     17  OE2 GLU A   6     113.689 173.266  94.918  1.00 54.87           O  
ATOM     18  N   LYS A   7     113.409 168.058  98.739  1.00 49.97           N  
ATOM     19  CA  LYS A   7     112.673 166.861  99.133  1.00 49.97           C  
ATOM     20  C   LYS A   7     112.984 166.462 100.573  1.00 49.97           C  
ATOM     21  O   LYS A   7     112.097 166.016 101.309  1.00 49.97           O  
ATOM     22  CB  LYS A   7     112.991 165.729  98.153  1.00 49.97           C  
ATOM     23  CG  LYS A   7     112.775 164.322  98.675  1.00 49.97           C  
ATOM     24  CD  LYS A   7     111.313 164.048  98.936  1.00 49.97           C  
ATOM     25  CE  LYS A   7     111.134 162.775  99.730  1.00 49.97           C  
ATOM     26  NZ  LYS A   7     111.580 162.969 101.129  1.00 49.97           N  
ATOM     27  N   LEU A   8     114.240 166.612 100.996  1.00 45.04           N  
ATOM     28  CA  LEU A   8     114.592 166.290 102.376  1.00 45.04           C  
ATOM     29  C   LEU A   8     113.927 167.255 103.353  1.00 45.04           C  
ATOM     30  O   LEU A   8     113.460 166.844 104.422  1.00 45.04           O  
ATOM     31  CB  LEU A   8     116.110 166.312 102.549  1.00 45.04           C  
ATOM     32  CG  LEU A   8     116.628 166.025 103.960  1.00 45.04           C  
ATOM     33  CD1 LEU A   8     116.430 164.556 104.317  1.00 45.04           C  
ATOM     34  CD2 LEU A   8     118.086 166.425 104.095  1.00 45.04           C  
ATOM     35  N   GLU A   9     113.896 168.544 103.013  1.00 48.24           N  
ATOM     36  CA  GLU A   9     113.169 169.505 103.835  1.00 48.24           C  
ATOM     37  C   GLU A   9     111.696 169.131 103.936  1.00 48.24           C  
ATOM     38  O   GLU A   9     111.078 169.280 104.996  1.00 48.24           O  
ATOM     39  CB  GLU A   9     113.326 170.910 103.256  1.00 48.24           C  
ATOM     40  CG  GLU A   9     112.712 172.010 104.106  1.00 48.24           C  
ATOM     41  CD  GLU A   9     113.079 171.895 105.576  1.00 48.24           C  
ATOM     42  OE1 GLU A   9     114.283 171.964 105.898  1.00 48.24           O  
ATOM     43  OE2 GLU A   9     112.162 171.729 106.409  1.00 48.24           O  
ATOM     44  N   GLU A  10     111.117 168.646 102.836  1.00 45.80           N  
ATOM     45  CA  GLU A  10     109.734 168.183 102.868  1.00 45.80           C  
ATOM     46  C   GLU A  10     109.574 166.995 103.809  1.00 45.80           C  
ATOM     47  O   GLU A  10     108.610 166.931 104.577  1.00 45.80           O  
ATOM     48  CB  GLU A  10     109.269 167.822 101.455  1.00 45.80           C  
ATOM     49  CG  GLU A  10     107.890 167.167 101.367  1.00 45.80           C  
ATOM     50  CD  GLU A  10     107.927 165.663 101.614  1.00 45.80           C  
ATOM     51  OE1 GLU A  10     109.033 165.112 101.794  1.00 45.80           O  
ATOM     52  OE2 GLU A  10     106.850 165.031 101.624  1.00 45.80           O  
ATOM     53  N   ARG A  11     110.493 166.031 103.740  1.00 35.82           N  
ATOM     54  CA  ARG A  11     110.438 164.884 104.648  1.00 35.82           C  
ATOM     55  C   ARG A  11     110.496 165.334 106.103  1.00 35.82           C  
ATOM     56  O   ARG A  11     109.758 164.825 106.957  1.00 35.82           O  
ATOM     57  CB  ARG A  11     111.587 163.923 104.346  1.00 35.82           C  
ATOM     58  CG  ARG A  11     111.345 162.493 104.811  1.00 35.82           C  
ATOM     59  CD  ARG A  11     112.294 161.514 104.134  1.00 35.82           C  
ATOM     60  NE  ARG A  11     111.732 160.167 104.056  1.00 35.82           N  
ATOM     61  CZ  ARG A  11     112.075 159.259 103.148  1.00 35.82           C  
ATOM     62  NH1 ARG A  11     112.976 159.543 102.220  1.00 35.82           N  
ATOM     63  NH2 ARG A  11     111.505 158.063 103.164  1.00 35.82           N  
ATOM     64  N   ARG A  12     111.375 166.289 106.400  1.00 35.19           N  
ATOM     65  CA  ARG A  12     111.464 166.827 107.752  1.00 35.19           C  
ATOM     66  C   ARG A  12     110.143 167.465 108.175  1.00 35.19           C  
ATOM     67  O   ARG A  12     109.603 167.158 109.248  1.00 35.19           O  
ATOM     68  CB  ARG A  12     112.603 167.842 107.823  1.00 35.19           C  
ATOM     69  CG  ARG A  12     114.000 167.234 107.867  1.00 35.19           C  
ATOM     70  CD  ARG A  12     115.055 168.273 107.522  1.00 35.19           C  
ATOM     71  NE  ARG A  12     116.413 167.834 107.830  1.00 35.19           N  
ATOM     72  CZ  ARG A  12     117.478 168.631 107.812  1.00 35.19           C  
ATOM     73  NH1 ARG A  12     117.351 169.915 107.504  1.00 35.19           N  
ATOM     74  NH2 ARG A  12     118.676 168.147 108.102  1.00 35.19           N  
ATOM     75  N   ALA A  13     109.616 168.367 107.343  1.00 38.75           N  
ATOM     76  CA  ALA A  13     108.363 169.036 107.671  1.00 38.75           C  
ATOM     77  C   ALA A  13     107.241 168.028 107.880  1.00 38.75           C  
ATOM     78  O   ALA A  13     106.376 168.219 108.741  1.00 38.75           O  
ATOM     79  CB  ALA A  13     107.996 170.030 106.570  1.00 38.75           C  
ATOM     80  N   GLN A  14     107.245 166.942 107.107  1.00 37.44           N  
ATOM     81  CA  GLN A  14     106.227 165.912 107.275  1.00 37.44           C  
ATOM     82  C   GLN A  14     106.392 165.192 108.605  1.00 37.44           C  
ATOM     83  O   GLN A  14     105.402 164.886 109.277  1.00 37.44           O  
ATOM     84  CB  GLN A  14     106.285 164.918 106.112  1.00 37.44           C  
ATOM     85  CG  GLN A  14     105.139 163.907 106.079  1.00 37.44           C  
ATOM     86  CD  GLN A  14     105.306 162.775 107.073  1.00 37.44           C  
ATOM     87  OE1 GLN A  14     106.399 162.531 107.579  1.00 37.44           O  
ATOM     88  NE2 GLN A  14     104.216 162.077 107.357  1.00 37.44           N  
ATOM     89  N   ALA A  15     107.634 164.908 109.000  1.00 33.86           N  
ATOM     90  CA  ALA A  15     107.849 164.251 110.285  1.00 33.86           C  
ATOM     91  C   ALA A  15     107.434 165.150 111.443  1.00 33.86           C  
ATOM     92  O   ALA A  15     107.061 164.656 112.512  1.00 33.86           O  
ATOM     93  CB  ALA A  15     109.313 163.841 110.435  1.00 33.86           C  
ATOM     94  N   ARG A  16     107.501 166.467 111.251  1.00 33.51           N  
ATOM     95  CA  ARG A  16     107.174 167.403 112.326  1.00 33.51           C  
ATOM     96  C   ARG A  16     105.683 167.482 112.647  1.00 33.51           C  
ATOM     97  O   ARG A  16     105.328 168.166 113.612  1.00 33.51           O  
ATOM     98  CB  ARG A  16     107.684 168.799 111.978  1.00 33.51           C  
ATOM     99  CG  ARG A  16     109.184 168.903 111.950  1.00 33.51           C  
ATOM    100  CD  ARG A  16     109.644 170.323 111.744  1.00 33.51           C  
ATOM    101  NE  ARG A  16     111.095 170.395 111.583  1.00 33.51           N  
ATOM    102  CZ  ARG A  16     111.724 170.849 110.501  1.00 33.51           C  
ATOM    103  NH1 ARG A  16     113.048 170.863 110.476  1.00 33.51           N  
ATOM    104  NH2 ARG A  16     111.051 171.292 109.448  1.00 33.51           N  
ATOM    105  N   LEU A  17     104.808 166.817 111.893  1.00 35.42           N  
ATOM    106  CA  LEU A  17     103.370 166.928 112.107  1.00 35.42           C  
ATOM    107  C   LEU A  17     102.807 165.874 113.051  1.00 35.42           C  
ATOM    108  O   LEU A  17     101.631 165.963 113.418  1.00 35.42           O  
ATOM    109  CB  LEU A  17     102.626 166.837 110.774  1.00 35.42           C  
ATOM    110  CG  LEU A  17     102.821 168.005 109.811  1.00 35.42           C  
ATOM    111  CD1 LEU A  17     102.277 167.645 108.443  1.00 35.42           C  
ATOM    112  CD2 LEU A  17     102.150 169.254 110.343  1.00 35.42           C  
ATOM    113  N   GLY A  18     103.596 164.887 113.441  1.00 33.02           N  
ATOM    114  CA  GLY A  18     103.119 163.899 114.392  1.00 33.02           C  
ATOM    115  C   GLY A  18     101.955 163.104 113.835  1.00 33.02           C  
ATOM    116  O   GLY A  18     102.039 162.506 112.757  1.00 33.02           O  
ATOM    117  N   GLY A  19     100.849 163.091 114.572  1.00 32.69           N  
ATOM    118  CA  GLY A  19      99.669 162.336 114.219  1.00 32.69           C  
ATOM    119  C   GLY A  19      98.609 163.100 113.457  1.00 32.69           C  
ATOM    120  O   GLY A  19      97.491 162.596 113.311  1.00 32.69           O  
ATOM    121  N   GLY A  20      98.915 164.302 112.973  1.00 37.50           N  
ATOM    122  CA  GLY A  20      97.982 165.050 112.153  1.00 37.50           C  
ATOM    123  C   GLY A  20      97.565 166.388 112.728  1.00 37.50           C  
ATOM    124  O   GLY A  20      97.725 166.643 113.925  1.00 37.50           O  
ATOM    125  N   GLU A  21      97.016 167.252 111.870  1.00 43.19           N  
ATOM    126  CA  GLU A  21      96.649 168.599 112.296  1.00 43.19           C  
ATOM    127  C   GLU A  21      95.442 168.586 113.224  1.00 43.19           C  
ATOM    128  O   GLU A  21      95.355 169.404 114.147  1.00 43.19           O  
ATOM    129  CB  GLU A  21      96.370 169.477 111.076  1.00 43.19           C  
ATOM    130  CG  GLU A  21      97.534 169.595 110.116  1.00 43.19           C  
ATOM    131  CD  GLU A  21      98.430 170.779 110.424  1.00 43.19           C  
ATOM    132  OE1 GLU A  21      98.337 171.325 111.543  1.00 43.19           O  
ATOM    133  OE2 GLU A  21      99.229 171.164 109.545  1.00 43.19           O  
ATOM    134  N   LYS A  22      94.494 167.678 112.991  1.00 40.29           N  
ATOM    135  CA  LYS A  22      93.315 167.609 113.847  1.00 40.29           C  
ATOM    136  C   LYS A  22      93.700 167.246 115.276  1.00 40.29           C  
ATOM    137  O   LYS A  22      93.268 167.898 116.235  1.00 40.29           O  
ATOM    138  CB  LYS A  22      92.317 166.597 113.278  1.00 40.29           C  
ATOM    139  CG  LYS A  22      91.237 166.166 114.262  1.00 40.29           C  
ATOM    140  CD  LYS A  22      90.115 165.400 113.577  1.00 40.29           C  
ATOM    141  CE  LYS A  22      90.387 163.903 113.538  1.00 40.29           C  
ATOM    142  NZ  LYS A  22      89.152 163.135 113.220  1.00 40.29           N  
ATOM    143  N   ARG A  23      94.517 166.203 115.436  1.00 34.55           N  
ATOM    144  CA  ARG A  23      94.934 165.784 116.769  1.00 34.55           C  
ATOM    145  C   ARG A  23      95.744 166.869 117.469  1.00 34.55           C  
ATOM    146  O   ARG A  23      95.633 167.036 118.688  1.00 34.55           O  
ATOM    147  CB  ARG A  23      95.734 164.486 116.675  1.00 34.55           C  
ATOM    148  CG  ARG A  23      94.933 163.294 116.171  1.00 34.55           C  
ATOM    149  CD  ARG A  23      95.722 162.006 116.294  1.00 34.55           C  
ATOM    150  NE  ARG A  23      94.988 160.839 115.811  1.00 34.55           N  
ATOM    151  CZ  ARG A  23      94.196 160.079 116.561  1.00 34.55           C  
ATOM    152  NH1 ARG A  23      94.011 160.353 117.844  1.00 34.55           N  
ATOM    153  NH2 ARG A  23      93.580 159.039 116.021  1.00 34.55           N  
ATOM    154  N   LEU A  24      96.527 167.643 116.717  1.00 32.74           N  
ATOM    155  CA  LEU A  24      97.341 168.687 117.333  1.00 32.74           C  
ATOM    156  C   LEU A  24      96.487 169.881 117.744  1.00 32.74           C  
ATOM    157  O   LEU A  24      96.713 170.483 118.803  1.00 32.74           O  
ATOM    158  CB  LEU A  24      98.449 169.117 116.370  1.00 32.74           C  
ATOM    159  CG  LEU A  24      99.574 168.110 116.088  1.00 32.74           C  
ATOM    160  CD1 LEU A  24     100.513 168.653 115.023  1.00 32.74           C  
ATOM    161  CD2 LEU A  24     100.364 167.759 117.338  1.00 32.74           C  
ATOM    162  N   GLU A  25      95.500 170.240 116.922  1.00 33.87           N  
ATOM    163  CA  GLU A  25      94.550 171.269 117.322  1.00 33.87           C  
ATOM    164  C   GLU A  25      93.757 170.831 118.542  1.00 33.87           C  
ATOM    165  O   GLU A  25      93.427 171.658 119.397  1.00 33.87           O  
ATOM    166  CB  GLU A  25      93.616 171.599 116.156  1.00 33.87           C  
ATOM    167  CG  GLU A  25      92.376 172.381 116.535  1.00 33.87           C  
ATOM    168  CD  GLU A  25      92.696 173.643 117.315  1.00 33.87           C  
ATOM    169  OE1 GLU A  25      93.750 174.258 117.049  1.00 33.87           O  
ATOM    170  OE2 GLU A  25      91.894 174.021 118.193  1.00 33.87           O  
ATOM    171  N   ALA A  26      93.457 169.536 118.650  1.00 29.58           N  
ATOM    172  CA  ALA A  26      92.769 169.034 119.834  1.00 29.58           C  
ATOM    173  C   ALA A  26      93.676 169.027 121.059  1.00 29.58           C  
ATOM    174  O   ALA A  26      93.195 169.189 122.186  1.00 29.58           O  
ATOM    175  CB  ALA A  26      92.230 167.633 119.570  1.00 29.58           C  
ATOM    176  N   GLN A  27      94.980 168.831 120.863  1.00 24.85           N  
ATOM    177  CA  GLN A  27      95.926 168.984 121.964  1.00 24.85           C  
ATOM    178  C   GLN A  27      95.938 170.426 122.455  1.00 24.85           C  
ATOM    179  O   GLN A  27      95.844 170.688 123.659  1.00 24.85           O  
ATOM    180  CB  GLN A  27      97.323 168.540 121.519  1.00 24.85           C  
ATOM    181  CG  GLN A  27      98.414 168.654 122.575  1.00 24.85           C  
ATOM    182  CD  GLN A  27      98.525 167.422 123.448  1.00 24.85           C  
ATOM    183  OE1 GLN A  27      97.665 166.546 123.419  1.00 24.85           O  
ATOM    184  NE2 GLN A  27      99.592 167.348 124.231  1.00 24.85           N  
ATOM    185  N   HIS A  28      96.046 171.377 121.527  1.00 25.53           N  
ATOM    186  CA  HIS A  28      95.946 172.788 121.891  1.00 25.53           C  
ATOM    187  C   HIS A  28      94.613 173.112 122.556  1.00 25.53           C  
ATOM    188  O   HIS A  28      94.547 174.001 123.412  1.00 25.53           O  
ATOM    189  CB  HIS A  28      96.122 173.670 120.658  1.00 25.53           C  
ATOM    190  CG  HIS A  28      97.547 173.948 120.298  1.00 25.53           C  
ATOM    191  ND1 HIS A  28      97.894 174.796 119.270  1.00 25.53           N  
ATOM    192  CD2 HIS A  28      98.710 173.503 120.827  1.00 25.53           C  
ATOM    193  CE1 HIS A  28      99.209 174.860 119.179  1.00 25.53           C  
ATOM    194  NE2 HIS A  28      99.728 174.083 120.111  1.00 25.53           N  
ATOM    195  N   LYS A  29      93.544 172.413 122.175  1.00 30.26           N  
ATOM    196  CA  LYS A  29      92.214 172.758 122.667  1.00 30.26           C  
ATOM    197  C   LYS A  29      92.043 172.381 124.132  1.00 30.26           C  
ATOM    198  O   LYS A  29      91.264 173.020 124.848  1.00 30.26           O  
ATOM    199  CB  LYS A  29      91.152 172.075 121.803  1.00 30.26           C  
ATOM    200  CG  LYS A  29      89.718 172.419 122.153  1.00 30.26           C  
ATOM    201  CD  LYS A  29      89.383 173.870 121.854  1.00 30.26           C  
ATOM    202  CE  LYS A  29      89.460 174.182 120.367  1.00 30.26           C  
ATOM    203  NZ  LYS A  29      88.875 175.513 120.046  1.00 30.26           N  
ATOM    204  N   ARG A  30      92.757 171.359 124.594  1.00 28.21           N  
ATOM    205  CA  ARG A  30      92.751 170.982 125.999  1.00 28.21           C  
ATOM    206  C   ARG A  30      93.633 171.880 126.858  1.00 28.21           C  
ATOM    207  O   ARG A  30      93.670 171.695 128.078  1.00 28.21           O  
ATOM    208  CB  ARG A  30      93.205 169.530 126.152  1.00 28.21           C  
ATOM    209  CG  ARG A  30      92.290 168.512 125.507  1.00 28.21           C  
ATOM    210  CD  ARG A  30      92.921 167.133 125.515  1.00 28.21           C  
ATOM    211  NE  ARG A  30      92.354 166.257 124.491  1.00 28.21           N  
ATOM    212  CZ  ARG A  30      93.000 165.823 123.411  1.00 28.21           C  
ATOM    213  NH1 ARG A  30      92.376 165.029 122.552  1.00 28.21           N  
ATOM    214  NH2 ARG A  30      94.261 166.170 123.175  1.00 28.21           N  
ATOM    215  N   GLY A  31      94.334 172.839 126.261  1.00 24.02           N  
ATOM    216  CA  GLY A  31      95.266 173.670 126.991  1.00 24.02           C  
ATOM    217  C   GLY A  31      96.663 173.107 127.104  1.00 24.02           C  
ATOM    218  O   GLY A  31      97.433 173.569 127.953  1.00 24.02           O  
ATOM    219  N   LYS A  32      97.016 172.134 126.274  1.00 19.44           N  
ATOM    220  CA  LYS A  32      98.311 171.479 126.318  1.00 19.44           C  
ATOM    221  C   LYS A  32      99.190 171.958 125.170  1.00 19.44           C  
ATOM    222  O   LYS A  32      98.708 172.268 124.079  1.00 19.44           O  
ATOM    223  CB  LYS A  32      98.159 169.958 126.238  1.00 19.44           C  
ATOM    224  CG  LYS A  32      97.588 169.302 127.480  1.00 19.44           C  
ATOM    225  CD  LYS A  32      97.963 167.831 127.540  1.00 19.44           C  
ATOM    226  CE  LYS A  32      97.016 166.991 126.731  1.00 19.44           C  
ATOM    227  NZ  LYS A  32      97.449 165.568 126.737  1.00 19.44           N  
ATOM    228  N   LEU A  33     100.488 172.021 125.432  1.00 14.27           N  
ATOM    229  CA  LEU A  33     101.472 172.249 124.390  1.00 14.27           C  
ATOM    230  C   LEU A  33     101.852 170.926 123.733  1.00 14.27           C  
ATOM    231  O   LEU A  33     101.604 169.843 124.267  1.00 14.27           O  
ATOM    232  CB  LEU A  33     102.720 172.923 124.956  1.00 14.27           C  
ATOM    233  CG  LEU A  33     102.613 174.347 125.504  1.00 14.27           C  
ATOM    234  CD1 LEU A  33     103.939 174.746 126.089  1.00 14.27           C  
ATOM    235  CD2 LEU A  33     102.172 175.348 124.447  1.00 14.27           C  
ATOM    236  N   THR A  34     102.458 171.028 122.556  1.00 12.80           N  
ATOM    237  CA  THR A  34     102.965 169.863 121.850  1.00 12.80           C  
ATOM    238  C   THR A  34     104.358 169.495 122.367  1.00 12.80           C  
ATOM    239  O   THR A  34     105.046 170.296 123.003  1.00 12.80           O  
ATOM    240  CB  THR A  34     103.005 170.117 120.340  1.00 12.80           C  
ATOM    241  OG1 THR A  34     103.912 171.183 120.044  1.00 12.80           O  
ATOM    242  CG2 THR A  34     101.630 170.477 119.812  1.00 12.80           C  
ATOM    243  N   ALA A  35     104.768 168.257 122.086  1.00 12.96           N  
ATOM    244  CA  ALA A  35     106.060 167.768 122.563  1.00 12.96           C  
ATOM    245  C   ALA A  35     107.209 168.631 122.046  1.00 12.96           C  
ATOM    246  O   ALA A  35     108.123 168.992 122.802  1.00 12.96           O  
ATOM    247  CB  ALA A  35     106.242 166.312 122.140  1.00 12.96           C  
ATOM    248  N   ARG A  36     107.165 168.989 120.762  1.00 12.59           N  
ATOM    249  CA  ARG A  36     108.217 169.813 120.177  1.00 12.59           C  
ATOM    250  C   ARG A  36     108.209 171.219 120.767  1.00 12.59           C  
ATOM    251  O   ARG A  36     109.272 171.801 121.011  1.00 12.59           O  
ATOM    252  CB  ARG A  36     108.060 169.849 118.655  1.00 12.59           C  
ATOM    253  CG  ARG A  36     108.265 168.484 118.014  1.00 12.59           C  
ATOM    254  CD  ARG A  36     108.235 168.503 116.491  1.00 12.59           C  
ATOM    255  NE  ARG A  36     108.497 167.169 115.956  1.00 12.59           N  
ATOM    256  CZ  ARG A  36     109.706 166.678 115.709  1.00 12.59           C  
ATOM    257  NH1 ARG A  36     110.782 167.410 115.925  1.00 12.59           N  
ATOM    258  NH2 ARG A  36     109.841 165.450 115.234  1.00 12.59           N  
ATOM    259  N   GLU A  37     107.022 171.772 121.023  1.00 13.48           N  
ATOM    260  CA  GLU A  37     106.929 173.071 121.681  1.00 13.48           C  
ATOM    261  C   GLU A  37     107.509 173.022 123.091  1.00 13.48           C  
ATOM    262  O   GLU A  37     108.173 173.968 123.533  1.00 13.48           O  
ATOM    263  CB  GLU A  37     105.473 173.530 121.722  1.00 13.48           C  
ATOM    264  CG  GLU A  37     104.914 173.982 120.385  1.00 13.48           C  
ATOM    265  CD  GLU A  37     103.403 174.140 120.396  1.00 13.48           C  
ATOM    266  OE1 GLU A  37     102.750 173.645 121.340  1.00 13.48           O  
ATOM    267  OE2 GLU A  37     102.865 174.758 119.456  1.00 13.48           O  
ATOM    268  N   ARG A  38     107.269 171.925 123.811  1.00 10.47           N  
ATOM    269  CA  ARG A  38     107.829 171.777 125.150  1.00 10.47           C  
ATOM    270  C   ARG A  38     109.352 171.765 125.097  1.00 10.47           C  
ATOM    271  O   ARG A  38     110.024 172.476 125.860  1.00 10.47           O  
ATOM    272  CB  ARG A  38     107.285 170.501 125.798  1.00 10.47           C  
ATOM    273  CG  ARG A  38     105.825 170.603 126.210  1.00 10.47           C  
ATOM    274  CD  ARG A  38     105.172 169.255 126.415  1.00 10.47           C  
ATOM    275  NE  ARG A  38     103.769 169.387 126.794  1.00 10.47           N  
ATOM    276  CZ  ARG A  38     102.912 168.379 126.881  1.00 10.47           C  
ATOM    277  NH1 ARG A  38     103.299 167.144 126.629  1.00 10.47           N  
ATOM    278  NH2 ARG A  38     101.657 168.610 127.230  1.00 10.47           N  
ATOM    279  N   ILE A  39     109.914 170.974 124.178  1.00 10.80           N  
ATOM    280  CA  ILE A  39     111.363 170.970 123.991  1.00 10.80           C  
ATOM    281  C   ILE A  39     111.858 172.379 123.688  1.00 10.80           C  
ATOM    282  O   ILE A  39     112.865 172.832 124.244  1.00 10.80           O  
ATOM    283  CB  ILE A  39     111.759 169.975 122.880  1.00 10.80           C  
ATOM    284  CG1 ILE A  39     111.629 168.538 123.381  1.00 10.80           C  
ATOM    285  CG2 ILE A  39     113.184 170.241 122.391  1.00 10.80           C  
ATOM    286  CD1 ILE A  39     111.659 167.495 122.281  1.00 10.80           C  
ATOM    287  N   GLU A  40     111.148 173.098 122.817  1.00 16.07           N  
ATOM    288  CA  GLU A  40     111.577 174.435 122.423  1.00 16.07           C  
ATOM    289  C   GLU A  40     111.614 175.378 123.617  1.00 16.07           C  
ATOM    290  O   GLU A  40     112.523 176.206 123.738  1.00 16.07           O  
ATOM    291  CB  GLU A  40     110.643 174.976 121.343  1.00 16.07           C  
ATOM    292  CG  GLU A  40     110.993 176.350 120.838  1.00 16.07           C  
ATOM    293  CD  GLU A  40     110.045 176.831 119.754  1.00 16.07           C  
ATOM    294  OE1 GLU A  40     109.088 176.100 119.427  1.00 16.07           O  
ATOM    295  OE2 GLU A  40     110.257 177.943 119.228  1.00 16.07           O  
ATOM    296  N   LEU A  41     110.628 175.270 124.504  1.00 11.95           N  
ATOM    297  CA  LEU A  41     110.581 176.144 125.671  1.00 11.95           C  
ATOM    298  C   LEU A  41     111.644 175.773 126.702  1.00 11.95           C  
ATOM    299  O   LEU A  41     112.117 176.644 127.439  1.00 11.95           O  
ATOM    300  CB  LEU A  41     109.186 176.097 126.295  1.00 11.95           C  
ATOM    301  CG  LEU A  41     108.803 177.107 127.376  1.00 11.95           C  
ATOM    302  CD1 LEU A  41     108.959 178.540 126.912  1.00 11.95           C  
ATOM    303  CD2 LEU A  41     107.373 176.848 127.806  1.00 11.95           C  
ATOM    304  N   LEU A  42     112.041 174.499 126.765  1.00  8.49           N  
ATOM    305  CA  LEU A  42     112.999 174.085 127.791  1.00  8.49           C  
ATOM    306  C   LEU A  42     114.419 174.555 127.478  1.00  8.49           C  
ATOM    307  O   LEU A  42     115.131 175.018 128.375  1.00  8.49           O  
ATOM    308  CB  LEU A  42     112.962 172.568 127.964  1.00  8.49           C  
ATOM    309  CG  LEU A  42     113.985 171.912 128.898  1.00  8.49           C  
ATOM    310  CD1 LEU A  42     113.924 172.502 130.280  1.00  8.49           C  
ATOM    311  CD2 LEU A  42     113.724 170.430 128.970  1.00  8.49           C  
ATOM    312  N   LEU A  43     114.842 174.466 126.221  1.00  8.11           N  
ATOM    313  CA  LEU A  43     116.244 174.625 125.856  1.00  8.11           C  
ATOM    314  C   LEU A  43     116.564 176.059 125.439  1.00  8.11           C  
ATOM    315  O   LEU A  43     115.684 176.842 125.079  1.00  8.11           O  
ATOM    316  CB  LEU A  43     116.614 173.672 124.717  1.00  8.11           C  
ATOM    317  CG  LEU A  43     116.543 172.167 124.953  1.00  8.11           C  
ATOM    318  CD1 LEU A  43     116.876 171.422 123.666  1.00  8.11           C  
ATOM    319  CD2 LEU A  43     117.466 171.750 126.070  1.00  8.11           C  
ATOM    320  N   ASP A  44     117.853 176.394 125.493  1.00 10.41           N  
ATOM    321  CA  ASP A  44     118.313 177.687 125.007  1.00 10.41           C  
ATOM    322  C   ASP A  44     118.088 177.795 123.501  1.00 10.41           C  
ATOM    323  O   ASP A  44     118.204 176.818 122.758  1.00 10.41           O  
ATOM    324  CB  ASP A  44     119.795 177.901 125.328  1.00 10.41           C  
ATOM    325  CG  ASP A  44     120.120 177.726 126.804  1.00 10.41           C  
ATOM    326  OD1 ASP A  44     119.226 177.910 127.657  1.00 10.41           O  
ATOM    327  OD2 ASP A  44     121.287 177.409 127.108  1.00 10.41           O  
ATOM    328  N   HIS A  45     117.760 179.004 123.059  1.00 13.93           N  
ATOM    329  CA  HIS A  45     117.411 179.246 121.665  1.00 13.93           C  
ATOM    330  C   HIS A  45     118.472 178.707 120.714  1.00 13.93           C  
ATOM    331  O   HIS A  45     119.658 179.020 120.838  1.00 13.93           O  
ATOM    332  CB  HIS A  45     117.209 180.743 121.439  1.00 13.93           C  
ATOM    333  CG  HIS A  45     116.838 181.095 120.034  1.00 13.93           C  
ATOM    334  ND1 HIS A  45     117.702 181.741 119.178  1.00 13.93           N  
ATOM    335  CD2 HIS A  45     115.701 180.883 119.333  1.00 13.93           C  
ATOM    336  CE1 HIS A  45     117.110 181.917 118.010  1.00 13.93           C  
ATOM    337  NE2 HIS A  45     115.895 181.405 118.078  1.00 13.93           N  
ATOM    338  N   GLY A  46     118.027 177.893 119.758  1.00 11.89           N  
ATOM    339  CA  GLY A  46     118.874 177.342 118.717  1.00 11.89           C  
ATOM    340  C   GLY A  46     119.782 176.199 119.115  1.00 11.89           C  
ATOM    341  O   GLY A  46     120.642 175.816 118.315  1.00 11.89           O  
ATOM    342  N   SER A  47     119.624 175.630 120.309  1.00  9.54           N  
ATOM    343  CA  SER A  47     120.558 174.629 120.813  1.00  9.54           C  
ATOM    344  C   SER A  47     120.137 173.180 120.581  1.00  9.54           C  
ATOM    345  O   SER A  47     120.929 172.278 120.868  1.00  9.54           O  
ATOM    346  CB  SER A  47     120.782 174.837 122.313  1.00  9.54           C  
ATOM    347  OG  SER A  47     119.704 174.326 123.063  1.00  9.54           O  
ATOM    348  N   PHE A  48     118.927 172.919 120.096  1.00  7.61           N  
ATOM    349  CA  PHE A  48     118.409 171.552 120.053  1.00  7.61           C  
ATOM    350  C   PHE A  48     119.014 170.771 118.887  1.00  7.61           C  
ATOM    351  O   PHE A  48     118.928 171.201 117.734  1.00  7.61           O  
ATOM    352  CB  PHE A  48     116.884 171.556 119.955  1.00  7.61           C  
ATOM    353  CG  PHE A  48     116.274 170.183 119.959  1.00  7.61           C  
ATOM    354  CD1 PHE A  48     116.678 169.228 120.870  1.00  7.61           C  
ATOM    355  CD2 PHE A  48     115.292 169.845 119.050  1.00  7.61           C  
ATOM    356  CE1 PHE A  48     116.121 167.974 120.869  1.00  7.61           C  
ATOM    357  CE2 PHE A  48     114.739 168.587 119.054  1.00  7.61           C  
ATOM    358  CZ  PHE A  48     115.154 167.658 119.964  1.00  7.61           C  
ATOM    359  N   GLU A  49     119.625 169.625 119.191  1.00 10.50           N  
ATOM    360  CA  GLU A  49     119.995 168.617 118.202  1.00 10.50           C  
ATOM    361  C   GLU A  49     119.147 167.368 118.431  1.00 10.50           C  
ATOM    362  O   GLU A  49     119.182 166.782 119.520  1.00 10.50           O  
ATOM    363  CB  GLU A  49     121.484 168.273 118.274  1.00 10.50           C  
ATOM    364  CG  GLU A  49     121.880 167.146 117.327  1.00 10.50           C  
ATOM    365  CD  GLU A  49     123.317 167.237 116.851  1.00 10.50           C  
ATOM    366  OE1 GLU A  49     124.225 166.808 117.594  1.00 10.50           O  
ATOM    367  OE2 GLU A  49     123.535 167.735 115.729  1.00 10.50           O  
ATOM    368  N   GLU A  50     118.378 166.982 117.411  1.00 10.73           N  
ATOM    369  CA  GLU A  50     117.480 165.832 117.465  1.00 10.73           C  
ATOM    370  C   GLU A  50     118.171 164.556 116.991  1.00 10.73           C  
ATOM    371  O   GLU A  50     118.978 164.582 116.058  1.00 10.73           O  
ATOM    372  CB  GLU A  50     116.240 166.080 116.599  1.00 10.73           C  
ATOM    373  CG  GLU A  50     115.093 165.113 116.859  1.00 10.73           C  
ATOM    374  CD  GLU A  50     113.837 165.437 116.069  1.00 10.73           C  
ATOM    375  OE1 GLU A  50     113.606 166.623 115.763  1.00 10.73           O  
ATOM    376  OE2 GLU A  50     113.075 164.499 115.763  1.00 10.73           O  
ATOM    377  N   PHE A  51     117.839 163.439 117.634  1.00 10.70           N  
ATOM    378  CA  PHE A  51     118.222 162.110 117.176  1.00 10.70           C  
ATOM    379  C   PHE A  51     117.004 161.363 116.634  1.00 10.70           C  
ATOM    380  O   PHE A  51     115.888 161.512 117.138  1.00 10.70           O  
ATOM    381  CB  PHE A  51     118.841 161.263 118.301  1.00 10.70           C  
ATOM    382  CG  PHE A  51     120.078 161.844 118.933  1.00 10.70           C  
ATOM    383  CD1 PHE A  51     120.924 162.692 118.244  1.00 10.70           C  
ATOM    384  CD2 PHE A  51     120.408 161.501 120.232  1.00 10.70           C  
ATOM    385  CE1 PHE A  51     122.060 163.196 118.848  1.00 10.70           C  
ATOM    386  CE2 PHE A  51     121.534 162.001 120.832  1.00 10.70           C  
ATOM    387  CZ  PHE A  51     122.362 162.846 120.142  1.00 10.70           C  
ATOM    388  N   ASP A  52     117.234 160.552 115.599  1.00 11.22           N  
ATOM    389  CA  ASP A  52     116.305 159.490 115.184  1.00 11.22           C  
ATOM    390  C   ASP A  52     114.954 160.036 114.709  1.00 11.22           C  
ATOM    391  O   ASP A  52     113.894 159.506 115.041  1.00 11.22           O  
ATOM    392  CB  ASP A  52     116.106 158.480 116.315  1.00 11.22           C  
ATOM    393  CG  ASP A  52     117.349 157.653 116.595  1.00 11.22           C  
ATOM    394  OD1 ASP A  52     118.175 157.473 115.678  1.00 11.22           O  
ATOM    395  OD2 ASP A  52     117.495 157.177 117.738  1.00 11.22           O  
ATOM    396  N   MET A  53     115.001 161.083 113.888  1.00 17.04           N  
ATOM    397  CA  MET A  53     113.772 161.718 113.415  1.00 17.04           C  
ATOM    398  C   MET A  53     112.919 160.763 112.578  1.00 17.04           C  
ATOM    399  O   MET A  53     111.688 160.783 112.670  1.00 17.04           O  
ATOM    400  CB  MET A  53     114.122 162.969 112.618  1.00 17.04           C  
ATOM    401  CG  MET A  53     112.966 163.871 112.286  1.00 17.04           C  
ATOM    402  SD  MET A  53     113.593 165.366 111.507  1.00 17.04           S  
ATOM    403  CE  MET A  53     112.098 166.308 111.326  1.00 17.04           C  
ATOM    404  N   PHE A  54     113.552 159.928 111.751  1.00 15.82           N  
ATOM    405  CA  PHE A  54     112.854 159.099 110.773  1.00 15.82           C  
ATOM    406  C   PHE A  54     112.683 157.636 111.200  1.00 15.82           C  
ATOM    407  O   PHE A  54     112.383 156.789 110.353  1.00 15.82           O  
ATOM    408  CB  PHE A  54     113.589 159.167 109.435  1.00 15.82           C  
ATOM    409  CG  PHE A  54     113.674 160.548 108.852  1.00 15.82           C  
ATOM    410  CD1 PHE A  54     112.603 161.415 108.926  1.00 15.82           C  
ATOM    411  CD2 PHE A  54     114.824 160.974 108.217  1.00 15.82           C  
ATOM    412  CE1 PHE A  54     112.681 162.678 108.383  1.00 15.82           C  
ATOM    413  CE2 PHE A  54     114.902 162.238 107.674  1.00 15.82           C  
ATOM    414  CZ  PHE A  54     113.830 163.087 107.759  1.00 15.82           C  
ATOM    415  N   VAL A  55     112.834 157.322 112.486  1.00 14.09           N  
ATOM    416  CA  VAL A  55     112.676 155.944 112.946  1.00 14.09           C  
ATOM    417  C   VAL A  55     111.217 155.506 112.834  1.00 14.09           C  
ATOM    418  O   VAL A  55     110.292 156.278 113.117  1.00 14.09           O  
ATOM    419  CB  VAL A  55     113.200 155.804 114.386  1.00 14.09           C  
ATOM    420  CG1 VAL A  55     112.714 154.521 115.021  1.00 14.09           C  
ATOM    421  CG2 VAL A  55     114.723 155.828 114.404  1.00 14.09           C  
ATOM    422  N   GLN A  56     111.010 154.249 112.425  1.00 19.14           N  
ATOM    423  CA  GLN A  56     109.689 153.656 112.239  1.00 19.14           C  
ATOM    424  C   GLN A  56     109.596 152.312 112.951  1.00 19.14           C  
ATOM    425  O   GLN A  56     110.601 151.642 113.198  1.00 19.14           O  
ATOM    426  CB  GLN A  56     109.366 153.446 110.753  1.00 19.14           C  
ATOM    427  CG  GLN A  56     109.488 154.689 109.918  1.00 19.14           C  
ATOM    428  CD  GLN A  56     108.873 154.524 108.547  1.00 19.14           C  
ATOM    429  OE1 GLN A  56     109.004 153.478 107.916  1.00 19.14           O  
ATOM    430  NE2 GLN A  56     108.187 155.557 108.083  1.00 19.14           N  
ATOM    431  N   HIS A  57     108.363 151.919 113.267  1.00 22.82           N  
ATOM    432  CA  HIS A  57     108.099 150.612 113.846  1.00 22.82           C  
ATOM    433  C   HIS A  57     108.102 149.533 112.765  1.00 22.82           C  
ATOM    434  O   HIS A  57     108.020 149.812 111.567  1.00 22.82           O  
ATOM    435  CB  HIS A  57     106.769 150.620 114.610  1.00 22.82           C  
ATOM    436  CG  HIS A  57     105.558 150.418 113.754  1.00 22.82           C  
ATOM    437  ND1 HIS A  57     104.726 151.451 113.386  1.00 22.82           N  
ATOM    438  CD2 HIS A  57     105.015 149.295 113.228  1.00 22.82           C  
ATOM    439  CE1 HIS A  57     103.737 150.976 112.653  1.00 22.82           C  
ATOM    440  NE2 HIS A  57     103.889 149.671 112.542  1.00 22.82           N  
ATOM    441  N   ARG A  58     108.204 148.280 113.215  1.00 25.56           N  
ATOM    442  CA  ARG A  58     108.358 147.131 112.329  1.00 25.56           C  
ATOM    443  C   ARG A  58     107.327 146.033 112.583  1.00 25.56           C  
ATOM    444  O   ARG A  58     107.478 144.927 112.052  1.00 25.56           O  
ATOM    445  CB  ARG A  58     109.772 146.548 112.465  1.00 25.56           C  
ATOM    446  CG  ARG A  58     110.873 147.451 111.919  1.00 25.56           C  
ATOM    447  CD  ARG A  58     112.269 146.882 112.151  1.00 25.56           C  
ATOM    448  NE  ARG A  58     112.715 147.032 113.531  1.00 25.56           N  
ATOM    449  CZ  ARG A  58     113.049 148.189 114.098  1.00 25.56           C  
ATOM    450  NH1 ARG A  58     112.992 149.328 113.415  1.00 25.56           N  
ATOM    451  NH2 ARG A  58     113.442 148.207 115.361  1.00 25.56           N  
ATOM    452  N   SER A  59     106.292 146.303 113.371  1.00 31.37           N  
ATOM    453  CA  SER A  59     105.248 145.319 113.622  1.00 31.37           C  
ATOM    454  C   SER A  59     104.358 145.122 112.400  1.00 31.37           C  
ATOM    455  O   SER A  59     104.157 146.029 111.589  1.00 31.37           O  
ATOM    456  CB  SER A  59     104.390 145.746 114.813  1.00 31.37           C  
ATOM    457  OG  SER A  59     103.245 144.922 114.931  1.00 31.37           O  
ATOM    458  N   THR A  60     103.813 143.909 112.285  1.00 37.60           N  
ATOM    459  CA  THR A  60     102.891 143.555 111.214  1.00 37.60           C  
ATOM    460  C   THR A  60     101.602 142.931 111.740  1.00 37.60           C  
ATOM    461  O   THR A  60     100.839 142.361 110.951  1.00 37.60           O  
ATOM    462  CB  THR A  60     103.560 142.591 110.226  1.00 37.60           C  
ATOM    463  OG1 THR A  60     104.239 141.557 110.948  1.00 37.60           O  
ATOM    464  CG2 THR A  60     104.550 143.327 109.334  1.00 37.60           C  
ATOM    465  N   ASP A  61     101.340 143.019 113.040  1.00 38.11           N  
ATOM    466  CA  ASP A  61     100.141 142.445 113.633  1.00 38.11           C  
ATOM    467  C   ASP A  61      99.023 143.478 113.714  1.00 38.11           C  
ATOM    468  O   ASP A  61      99.254 144.638 114.061  1.00 38.11           O  
ATOM    469  CB  ASP A  61     100.441 141.903 115.031  1.00 38.11           C  
ATOM    470  CG  ASP A  61     101.192 140.587 115.001  1.00 38.11           C  
ATOM    471  OD1 ASP A  61     100.800 139.692 114.224  1.00 38.11           O  
ATOM    472  OD2 ASP A  61     102.174 140.448 115.759  1.00 38.11           O  
ATOM    473  N   PHE A  62      97.807 143.040 113.389  1.00 37.14           N  
ATOM    474  CA  PHE A  62      96.590 143.831 113.590  1.00 37.14           C  
ATOM    475  C   PHE A  62      96.595 145.117 112.765  1.00 37.14           C  
ATOM    476  O   PHE A  62      96.197 146.181 113.241  1.00 37.14           O  
ATOM    477  CB  PHE A  62      96.383 144.149 115.072  1.00 37.14           C  
ATOM    478  CG  PHE A  62      96.314 142.935 115.949  1.00 37.14           C  
ATOM    479  CD1 PHE A  62      95.262 142.045 115.843  1.00 37.14           C  
ATOM    480  CD2 PHE A  62      97.299 142.685 116.884  1.00 37.14           C  
ATOM    481  CE1 PHE A  62      95.199 140.932 116.650  1.00 37.14           C  
ATOM    482  CE2 PHE A  62      97.238 141.576 117.689  1.00 37.14           C  
ATOM    483  CZ  PHE A  62      96.188 140.698 117.573  1.00 37.14           C  
ATOM    484  N   GLY A  63      97.030 145.020 111.511  1.00 40.53           N  
ATOM    485  CA  GLY A  63      96.959 146.143 110.600  1.00 40.53           C  
ATOM    486  C   GLY A  63      97.949 147.258 110.849  1.00 40.53           C  
ATOM    487  O   GLY A  63      97.887 148.279 110.155  1.00 40.53           O  
ATOM    488  N   MET A  64      98.860 147.103 111.810  1.00 39.36           N  
ATOM    489  CA  MET A  64      99.812 148.171 112.100  1.00 39.36           C  
ATOM    490  C   MET A  64     100.695 148.489 110.901  1.00 39.36           C  
ATOM    491  O   MET A  64     101.120 149.638 110.734  1.00 39.36           O  
ATOM    492  CB  MET A  64     100.671 147.789 113.302  1.00 39.36           C  
ATOM    493  CG  MET A  64      99.886 147.601 114.585  1.00 39.36           C  
ATOM    494  SD  MET A  64      99.036 149.096 115.119  1.00 39.36           S  
ATOM    495  CE  MET A  64     100.432 150.162 115.452  1.00 39.36           C  
ATOM    496  N   GLU A  65     100.987 147.494 110.061  1.00 42.56           N  
ATOM    497  CA  GLU A  65     101.845 147.719 108.903  1.00 42.56           C  
ATOM    498  C   GLU A  65     101.339 148.841 108.005  1.00 42.56           C  
ATOM    499  O   GLU A  65     102.116 149.379 107.211  1.00 42.56           O  
ATOM    500  CB  GLU A  65     101.985 146.429 108.088  1.00 42.56           C  
ATOM    501  CG  GLU A  65     100.678 145.857 107.553  1.00 42.56           C  
ATOM    502  CD  GLU A  65      99.989 144.932 108.536  1.00 42.56           C  
ATOM    503  OE1 GLU A  65      99.763 145.344 109.693  1.00 42.56           O  
ATOM    504  OE2 GLU A  65      99.674 143.788 108.150  1.00 42.56           O  
ATOM    505  N   LYS A  66     100.063 149.205 108.108  1.00 45.05           N  
ATOM    506  CA  LYS A  66      99.492 150.255 107.277  1.00 45.05           C  
ATOM    507  C   LYS A  66      99.585 151.643 107.898  1.00 45.05           C  
ATOM    508  O   LYS A  66      99.222 152.620 107.236  1.00 45.05           O  
ATOM    509  CB  LYS A  66      98.023 149.943 106.975  1.00 45.05           C  
ATOM    510  CG  LYS A  66      97.802 148.596 106.317  1.00 45.05           C  
ATOM    511  CD  LYS A  66      96.430 148.501 105.676  1.00 45.05           C  
ATOM    512  CE  LYS A  66      95.319 148.468 106.710  1.00 45.05           C  
ATOM    513  NZ  LYS A  66      95.245 147.154 107.399  1.00 45.05           N  
ATOM    514  N   GLN A  67     100.057 151.762 109.142  1.00 41.11           N  
ATOM    515  CA  GLN A  67     100.160 153.051 109.835  1.00 41.11           C  
ATOM    516  C   GLN A  67     101.591 153.217 110.338  1.00 41.11           C  
ATOM    517  O   GLN A  67     101.882 152.946 111.503  1.00 41.11           O  
ATOM    518  CB  GLN A  67      99.156 153.141 110.984  1.00 41.11           C  
ATOM    519  CG  GLN A  67      97.783 152.575 110.687  1.00 41.11           C  
ATOM    520  CD  GLN A  67      96.857 152.653 111.881  1.00 41.11           C  
ATOM    521  OE1 GLN A  67      96.204 151.672 112.240  1.00 41.11           O  
ATOM    522  NE2 GLN A  67      96.798 153.821 112.509  1.00 41.11           N  
ATOM    523  N   LYS A  68     102.472 153.704 109.473  1.00 31.62           N  
ATOM    524  CA  LYS A  68     103.869 153.930 109.818  1.00 31.62           C  
ATOM    525  C   LYS A  68     104.107 155.430 109.901  1.00 31.62           C  
ATOM    526  O   LYS A  68     103.967 156.142 108.902  1.00 31.62           O  
ATOM    527  CB  LYS A  68     104.801 153.276 108.799  1.00 31.62           C  
ATOM    528  CG  LYS A  68     104.926 151.775 108.989  1.00 31.62           C  
ATOM    529  CD  LYS A  68     105.832 151.135 107.963  1.00 31.62           C  
ATOM    530  CE  LYS A  68     105.829 149.621 108.096  1.00 31.62           C  
ATOM    531  NZ  LYS A  68     106.249 149.151 109.447  1.00 31.62           N  
ATOM    532  N   ILE A  69     104.462 155.900 111.090  1.00 23.00           N  
ATOM    533  CA  ILE A  69     104.558 157.319 111.397  1.00 23.00           C  
ATOM    534  C   ILE A  69     105.999 157.622 111.795  1.00 23.00           C  
ATOM    535  O   ILE A  69     106.503 157.049 112.765  1.00 23.00           O  
ATOM    536  CB  ILE A  69     103.581 157.725 112.512  1.00 23.00           C  
ATOM    537  CG1 ILE A  69     102.147 157.381 112.094  1.00 23.00           C  
ATOM    538  CG2 ILE A  69     103.701 159.205 112.823  1.00 23.00           C  
ATOM    539  CD1 ILE A  69     101.121 157.560 113.174  1.00 23.00           C  
ATOM    540  N   PRO A  70     106.704 158.504 111.085  1.00 19.64           N  
ATOM    541  CA  PRO A  70     108.093 158.804 111.455  1.00 19.64           C  
ATOM    542  C   PRO A  70     108.213 159.339 112.874  1.00 19.64           C  
ATOM    543  O   PRO A  70     107.448 160.205 113.303  1.00 19.64           O  
ATOM    544  CB  PRO A  70     108.516 159.848 110.417  1.00 19.64           C  
ATOM    545  CG  PRO A  70     107.261 160.430 109.917  1.00 19.64           C  
ATOM    546  CD  PRO A  70     106.254 159.332 109.956  1.00 19.64           C  
ATOM    547  N   GLY A  71     109.202 158.812 113.599  1.00 14.99           N  
ATOM    548  CA  GLY A  71     109.500 159.189 114.962  1.00 14.99           C  
ATOM    549  C   GLY A  71     108.953 158.233 116.006  1.00 14.99           C  
ATOM    550  O   GLY A  71     109.543 158.099 117.084  1.00 14.99           O  
ATOM    551  N   ASP A  72     107.830 157.581 115.709  1.00 16.73           N  
ATOM    552  CA  ASP A  72     107.257 156.507 116.522  1.00 16.73           C  
ATOM    553  C   ASP A  72     106.858 156.963 117.925  1.00 16.73           C  
ATOM    554  O   ASP A  72     106.909 156.181 118.877  1.00 16.73           O  
ATOM    555  CB  ASP A  72     108.206 155.311 116.615  1.00 16.73           C  
ATOM    556  CG  ASP A  72     107.477 154.015 116.913  1.00 16.73           C  
ATOM    557  OD1 ASP A  72     106.271 153.927 116.610  1.00 16.73           O  
ATOM    558  OD2 ASP A  72     108.103 153.088 117.466  1.00 16.73           O  
ATOM    559  N   GLY A  73     106.434 158.214 118.068  1.00 12.79           N  
ATOM    560  CA  GLY A  73     105.802 158.663 119.289  1.00 12.79           C  
ATOM    561  C   GLY A  73     106.704 159.272 120.342  1.00 12.79           C  
ATOM    562  O   GLY A  73     106.253 159.451 121.477  1.00 12.79           O  
ATOM    563  N   VAL A  74     107.955 159.590 120.019  1.00  9.70           N  
ATOM    564  CA  VAL A  74     108.845 160.260 120.966  1.00  9.70           C  
ATOM    565  C   VAL A  74     109.849 161.110 120.200  1.00  9.70           C  
ATOM    566  O   VAL A  74     110.324 160.721 119.130  1.00  9.70           O  
ATOM    567  CB  VAL A  74     109.563 159.252 121.895  1.00  9.70           C  
ATOM    568  CG1 VAL A  74     110.499 158.342 121.113  1.00  9.70           C  
ATOM    569  CG2 VAL A  74     110.315 159.992 122.992  1.00  9.70           C  
ATOM    570  N   VAL A  75     110.170 162.274 120.761  1.00  7.42           N  
ATOM    571  CA  VAL A  75     111.195 163.169 120.238  1.00  7.42           C  
ATOM    572  C   VAL A  75     112.357 163.155 121.227  1.00  7.42           C  
ATOM    573  O   VAL A  75     112.165 163.426 122.419  1.00  7.42           O  
ATOM    574  CB  VAL A  75     110.657 164.595 120.038  1.00  7.42           C  
ATOM    575  CG1 VAL A  75     111.694 165.469 119.347  1.00  7.42           C  
ATOM    576  CG2 VAL A  75     109.317 164.583 119.301  1.00  7.42           C  
ATOM    577  N   THR A  76     113.553 162.839 120.737  1.00  6.35           N  
ATOM    578  CA  THR A  76     114.743 162.639 121.555  1.00  6.35           C  
ATOM    579  C   THR A  76     115.888 163.522 121.069  1.00  6.35           C  
ATOM    580  O   THR A  76     116.002 163.809 119.874  1.00  6.35           O  
ATOM    581  CB  THR A  76     115.173 161.165 121.518  1.00  6.35           C  
ATOM    582  OG1 THR A  76     115.291 160.737 120.158  1.00  6.35           O  
ATOM    583  CG2 THR A  76     114.158 160.301 122.211  1.00  6.35           C  
ATOM    584  N   GLY A  77     116.760 163.930 121.991  1.00  6.59           N  
ATOM    585  CA  GLY A  77     117.909 164.731 121.596  1.00  6.59           C  
ATOM    586  C   GLY A  77     118.631 165.374 122.771  1.00  6.59           C  
ATOM    587  O   GLY A  77     118.502 164.940 123.917  1.00  6.59           O  
ATOM    588  N   TRP A  78     119.396 166.423 122.450  1.00  6.14           N  
ATOM    589  CA  TRP A  78     120.232 167.113 123.430  1.00  6.14           C  
ATOM    590  C   TRP A  78     120.325 168.603 123.112  1.00  6.14           C  
ATOM    591  O   TRP A  78     120.020 169.046 122.003  1.00  6.14           O  
ATOM    592  CB  TRP A  78     121.638 166.493 123.507  1.00  6.14           C  
ATOM    593  CG  TRP A  78     122.575 166.869 122.409  1.00  6.14           C  
ATOM    594  CD1 TRP A  78     122.729 166.244 121.209  1.00  6.14           C  
ATOM    595  CD2 TRP A  78     123.512 167.948 122.420  1.00  6.14           C  
ATOM    596  NE1 TRP A  78     123.697 166.872 120.468  1.00  6.14           N  
ATOM    597  CE2 TRP A  78     124.193 167.922 121.191  1.00  6.14           C  
ATOM    598  CE3 TRP A  78     123.839 168.936 123.348  1.00  6.14           C  
ATOM    599  CZ2 TRP A  78     125.177 168.845 120.870  1.00  6.14           C  
ATOM    600  CZ3 TRP A  78     124.812 169.847 123.027  1.00  6.14           C  
ATOM    601  CH2 TRP A  78     125.470 169.798 121.801  1.00  6.14           C  
ATOM    602  N   GLY A  79     120.739 169.368 124.116  1.00  6.78           N  
ATOM    603  CA  GLY A  79     120.899 170.801 123.978  1.00  6.78           C  
ATOM    604  C   GLY A  79     121.598 171.402 125.182  1.00  6.78           C  
ATOM    605  O   GLY A  79     122.325 170.718 125.903  1.00  6.78           O  
ATOM    606  N   THR A  80     121.355 172.697 125.404  1.00  9.34           N  
ATOM    607  CA  THR A  80     121.943 173.433 126.518  1.00  9.34           C  
ATOM    608  C   THR A  80     120.878 174.216 127.281  1.00  9.34           C  
ATOM    609  O   THR A  80     119.925 174.731 126.693  1.00  9.34           O  
ATOM    610  CB  THR A  80     123.047 174.405 126.040  1.00  9.34           C  
ATOM    611  OG1 THR A  80     122.523 175.290 125.047  1.00  9.34           O  
ATOM    612  CG2 THR A  80     124.249 173.644 125.473  1.00  9.34           C  
ATOM    613  N   VAL A  81     121.054 174.287 128.598  1.00  8.24           N  
ATOM    614  CA  VAL A  81     120.261 175.125 129.494  1.00  8.24           C  
ATOM    615  C   VAL A  81     121.229 176.042 130.231  1.00  8.24           C  
ATOM    616  O   VAL A  81     122.126 175.568 130.941  1.00  8.24           O  
ATOM    617  CB  VAL A  81     119.426 174.293 130.482  1.00  8.24           C  
ATOM    618  CG1 VAL A  81     118.729 175.185 131.504  1.00  8.24           C  
ATOM    619  CG2 VAL A  81     118.408 173.448 129.744  1.00  8.24           C  
ATOM    620  N   ASN A  82     121.035 177.348 130.070  1.00 11.61           N  
ATOM    621  CA  ASN A  82     121.980 178.363 130.519  1.00 11.61           C  
ATOM    622  C   ASN A  82     123.419 177.963 130.205  1.00 11.61           C  
ATOM    623  O   ASN A  82     124.318 178.178 131.021  1.00 11.61           O  
ATOM    624  CB  ASN A  82     121.813 178.635 132.018  1.00 11.61           C  
ATOM    625  CG  ASN A  82     122.405 179.964 132.438  1.00 11.61           C  
ATOM    626  OD1 ASN A  82     122.704 180.815 131.603  1.00 11.61           O  
ATOM    627  ND2 ASN A  82     122.571 180.151 133.738  1.00 11.61           N  
ATOM    628  N   GLY A  83     123.643 177.393 129.021  1.00 11.07           N  
ATOM    629  CA  GLY A  83     124.968 177.050 128.544  1.00 11.07           C  
ATOM    630  C   GLY A  83     125.498 175.703 128.983  1.00 11.07           C  
ATOM    631  O   GLY A  83     126.588 175.319 128.546  1.00 11.07           O  
ATOM    632  N   ARG A  84     124.771 174.978 129.825  1.00  8.31           N  
ATOM    633  CA  ARG A  84     125.200 173.681 130.331  1.00  8.31           C  
ATOM    634  C   ARG A  84     124.467 172.555 129.600  1.00  8.31           C  
ATOM    635  O   ARG A  84     123.258 172.632 129.382  1.00  8.31           O  
ATOM    636  CB  ARG A  84     124.958 173.601 131.840  1.00  8.31           C  
ATOM    637  CG  ARG A  84     125.698 174.672 132.652  1.00  8.31           C  
ATOM    638  CD  ARG A  84     125.126 174.850 134.042  1.00  8.31           C  
ATOM    639  NE  ARG A  84     125.582 173.811 134.959  1.00  8.31           N  
ATOM    640  CZ  ARG A  84     124.879 173.349 135.987  1.00  8.31           C  
ATOM    641  NH1 ARG A  84     123.673 173.827 136.242  1.00  8.31           N  
ATOM    642  NH2 ARG A  84     125.382 172.404 136.764  1.00  8.31           N  
ATOM    643  N   THR A  85     125.209 171.505 129.242  1.00  6.65           N  
ATOM    644  CA  THR A  85     124.689 170.419 128.411  1.00  6.65           C  
ATOM    645  C   THR A  85     123.623 169.598 129.136  1.00  6.65           C  
ATOM    646  O   THR A  85     123.777 169.248 130.307  1.00  6.65           O  
ATOM    647  CB  THR A  85     125.839 169.501 127.972  1.00  6.65           C  
ATOM    648  OG1 THR A  85     126.774 170.240 127.179  1.00  6.65           O  
ATOM    649  CG2 THR A  85     125.331 168.304 127.175  1.00  6.65           C  
ATOM    650  N   VAL A  86     122.534 169.289 128.422  1.00  7.85           N  
ATOM    651  CA  VAL A  86     121.474 168.414 128.919  1.00  7.85           C  
ATOM    652  C   VAL A  86     120.932 167.539 127.788  1.00  7.85           C  
ATOM    653  O   VAL A  86     120.908 167.937 126.621  1.00  7.85           O  
ATOM    654  CB  VAL A  86     120.308 169.199 129.574  1.00  7.85           C  
ATOM    655  CG1 VAL A  86     120.813 170.171 130.636  1.00  7.85           C  
ATOM    656  CG2 VAL A  86     119.466 169.909 128.533  1.00  7.85           C  
ATOM    657  N   PHE A  87     120.515 166.326 128.148  1.00 12.77           N  
ATOM    658  CA  PHE A  87     119.827 165.385 127.270  1.00 12.77           C  
ATOM    659  C   PHE A  87     118.346 165.308 127.642  1.00 12.77           C  
ATOM    660  O   PHE A  87     117.981 165.507 128.803  1.00 12.77           O  
ATOM    661  CB  PHE A  87     120.466 163.996 127.363  1.00 12.77           C  
ATOM    662  CG  PHE A  87     121.846 163.927 126.780  1.00 12.77           C  
ATOM    663  CD1 PHE A  87     122.949 164.288 127.528  1.00 12.77           C  
ATOM    664  CD2 PHE A  87     122.041 163.509 125.482  1.00 12.77           C  
ATOM    665  CE1 PHE A  87     124.213 164.233 126.986  1.00 12.77           C  
ATOM    666  CE2 PHE A  87     123.301 163.453 124.943  1.00 12.77           C  
ATOM    667  CZ  PHE A  87     124.385 163.814 125.698  1.00 12.77           C  
ATOM    668  N   LEU A  88     117.486 165.016 126.660  1.00  6.69           N  
ATOM    669  CA  LEU A  88     116.046 165.021 126.907  1.00  6.69           C  
ATOM    670  C   LEU A  88     115.292 164.147 125.904  1.00  6.69           C  
ATOM    671  O   LEU A  88     115.758 163.904 124.784  1.00  6.69           O  
ATOM    672  CB  LEU A  88     115.486 166.449 126.876  1.00  6.69           C  
ATOM    673  CG  LEU A  88     115.279 167.193 125.559  1.00  6.69           C  
ATOM    674  CD1 LEU A  88     114.502 168.474 125.832  1.00  6.69           C  
ATOM    675  CD2 LEU A  88     116.585 167.500 124.887  1.00  6.69           C  
ATOM    676  N   PHE A  89     114.131 163.653 126.355  1.00  5.55           N  
ATOM    677  CA  PHE A  89     113.110 163.040 125.511  1.00  5.55           C  
ATOM    678  C   PHE A  89     111.724 163.532 125.925  1.00  5.55           C  
ATOM    679  O   PHE A  89     111.507 163.964 127.058  1.00  5.55           O  
ATOM    680  CB  PHE A  89     113.159 161.509 125.558  1.00  5.55           C  
ATOM    681  CG  PHE A  89     112.910 160.918 126.918  1.00  5.55           C  
ATOM    682  CD1 PHE A  89     111.633 160.586 127.323  1.00  5.55           C  
ATOM    683  CD2 PHE A  89     113.954 160.667 127.780  1.00  5.55           C  
ATOM    684  CE1 PHE A  89     111.409 160.032 128.558  1.00  5.55           C  
ATOM    685  CE2 PHE A  89     113.727 160.110 129.012  1.00  5.55           C  
ATOM    686  CZ  PHE A  89     112.457 159.796 129.400  1.00  5.55           C  
ATOM    687  N   SER A  90     110.784 163.454 124.978  1.00  6.40           N  
ATOM    688  CA  SER A  90     109.440 164.012 125.135  1.00  6.40           C  
ATOM    689  C   SER A  90     108.462 163.187 124.309  1.00  6.40           C  
ATOM    690  O   SER A  90     108.631 163.061 123.094  1.00  6.40           O  
ATOM    691  CB  SER A  90     109.404 165.476 124.702  1.00  6.40           C  
ATOM    692  OG  SER A  90     108.083 165.979 124.687  1.00  6.40           O  
ATOM    693  N   LYS A  91     107.451 162.623 124.964  1.00 11.54           N  
ATOM    694  CA  LYS A  91     106.494 161.745 124.305  1.00 11.54           C  
ATOM    695  C   LYS A  91     105.409 162.542 123.585  1.00 11.54           C  
ATOM    696  O   LYS A  91     104.983 163.607 124.037  1.00 11.54           O  
ATOM    697  CB  LYS A  91     105.870 160.796 125.325  1.00 11.54           C  
ATOM    698  CG  LYS A  91     106.888 159.880 125.977  1.00 11.54           C  
ATOM    699  CD  LYS A  91     106.263 158.811 126.827  1.00 11.54           C  
ATOM    700  CE  LYS A  91     107.324 157.993 127.529  1.00 11.54           C  
ATOM    701  NZ  LYS A  91     107.484 156.649 126.938  1.00 11.54           N  
ATOM    702  N   ASP A  92     104.956 161.996 122.453  1.00 17.43           N  
ATOM    703  CA  ASP A  92     104.014 162.651 121.543  1.00 17.43           C  
ATOM    704  C   ASP A  92     102.665 161.940 121.634  1.00 17.43           C  
ATOM    705  O   ASP A  92     102.468 160.877 121.041  1.00 17.43           O  
ATOM    706  CB  ASP A  92     104.553 162.642 120.116  1.00 17.43           C  
ATOM    707  CG  ASP A  92     103.674 163.422 119.154  1.00 17.43           C  
ATOM    708  OD1 ASP A  92     102.630 163.951 119.584  1.00 17.43           O  
ATOM    709  OD2 ASP A  92     104.035 163.504 117.964  1.00 17.43           O  
ATOM    710  N   PHE A  93     101.730 162.556 122.359  1.00 20.52           N  
ATOM    711  CA  PHE A  93     100.433 161.941 122.624  1.00 20.52           C  
ATOM    712  C   PHE A  93      99.612 161.711 121.358  1.00 20.52           C  
ATOM    713  O   PHE A  93      98.736 160.841 121.355  1.00 20.52           O  
ATOM    714  CB  PHE A  93      99.648 162.813 123.608  1.00 20.52           C  
ATOM    715  CG  PHE A  93      98.405 162.163 124.143  1.00 20.52           C  
ATOM    716  CD1 PHE A  93      98.485 161.099 125.019  1.00 20.52           C  
ATOM    717  CD2 PHE A  93      97.157 162.623 123.777  1.00 20.52           C  
ATOM    718  CE1 PHE A  93      97.348 160.505 125.509  1.00 20.52           C  
ATOM    719  CE2 PHE A  93      96.017 162.029 124.270  1.00 20.52           C  
ATOM    720  CZ  PHE A  93      96.114 160.972 125.136  1.00 20.52           C  
ATOM    721  N   THR A  94      99.872 162.458 120.289  1.00 23.79           N  
ATOM    722  CA  THR A  94      99.106 162.311 119.056  1.00 23.79           C  
ATOM    723  C   THR A  94      99.477 161.071 118.249  1.00 23.79           C  
ATOM    724  O   THR A  94      98.805 160.786 117.253  1.00 23.79           O  
ATOM    725  CB  THR A  94      99.286 163.544 118.173  1.00 23.79           C  
ATOM    726  OG1 THR A  94     100.624 163.581 117.665  1.00 23.79           O  
ATOM    727  CG2 THR A  94      98.993 164.813 118.956  1.00 23.79           C  
ATOM    728  N   VAL A  95     100.509 160.331 118.644  1.00 23.21           N  
ATOM    729  CA  VAL A  95     101.016 159.193 117.882  1.00 23.21           C  
ATOM    730  C   VAL A  95     100.790 157.950 118.736  1.00 23.21           C  
ATOM    731  O   VAL A  95     101.556 157.673 119.666  1.00 23.21           O  
ATOM    732  CB  VAL A  95     102.493 159.361 117.507  1.00 23.21           C  
ATOM    733  CG1 VAL A  95     103.031 158.102 116.856  1.00 23.21           C  
ATOM    734  CG2 VAL A  95     102.675 160.553 116.584  1.00 23.21           C  
ATOM    735  N   PHE A  96      99.732 157.203 118.423  1.00 26.13           N  
ATOM    736  CA  PHE A  96      99.364 155.993 119.158  1.00 26.13           C  
ATOM    737  C   PHE A  96      99.229 156.267 120.655  1.00 26.13           C  
ATOM    738  O   PHE A  96      99.549 155.424 121.494  1.00 26.13           O  
ATOM    739  CB  PHE A  96     100.368 154.867 118.906  1.00 26.13           C  
ATOM    740  CG  PHE A  96     100.494 154.473 117.465  1.00 26.13           C  
ATOM    741  CD1 PHE A  96      99.476 153.785 116.831  1.00 26.13           C  
ATOM    742  CD2 PHE A  96     101.635 154.781 116.746  1.00 26.13           C  
ATOM    743  CE1 PHE A  96      99.592 153.420 115.510  1.00 26.13           C  
ATOM    744  CE2 PHE A  96     101.756 154.414 115.424  1.00 26.13           C  
ATOM    745  CZ  PHE A  96     100.733 153.733 114.807  1.00 26.13           C  
ATOM    746  N   GLY A  97      98.741 157.457 120.993  1.00 25.89           N  
ATOM    747  CA  GLY A  97      98.585 157.822 122.390  1.00 25.89           C  
ATOM    748  C   GLY A  97      99.882 157.850 123.165  1.00 25.89           C  
ATOM    749  O   GLY A  97      99.882 157.578 124.370  1.00 25.89           O  
ATOM    750  N   GLY A  98     100.992 158.173 122.505  1.00 22.10           N  
ATOM    751  CA  GLY A  98     102.282 158.180 123.166  1.00 22.10           C  
ATOM    752  C   GLY A  98     102.723 156.834 123.693  1.00 22.10           C  
ATOM    753  O   GLY A  98     103.597 156.776 124.558  1.00 22.10           O  
ATOM    754  N   SER A  99     102.149 155.746 123.190  1.00 21.71           N  
ATOM    755  CA  SER A  99     102.431 154.428 123.731  1.00 21.71           C  
ATOM    756  C   SER A  99     103.847 153.982 123.374  1.00 21.71           C  
ATOM    757  O   SER A  99     104.457 154.448 122.410  1.00 21.71           O  
ATOM    758  CB  SER A  99     101.409 153.412 123.223  1.00 21.71           C  
ATOM    759  OG  SER A  99     101.451 153.304 121.817  1.00 21.71           O  
ATOM    760  N   SER A 100     104.364 153.060 124.182  1.00 18.76           N  
ATOM    761  CA  SER A 100     105.741 152.590 124.089  1.00 18.76           C  
ATOM    762  C   SER A 100     105.822 151.330 123.237  1.00 18.76           C  
ATOM    763  O   SER A 100     105.112 150.352 123.490  1.00 18.76           O  
ATOM    764  CB  SER A 100     106.310 152.313 125.481  1.00 18.76           C  
ATOM    765  OG  SER A 100     107.632 151.813 125.399  1.00 18.76           O  
ATOM    766  N   SER A 101     106.695 151.359 122.242  1.00 17.46           N  
ATOM    767  CA  SER A 101     106.981 150.235 121.364  1.00 17.46           C  
ATOM    768  C   SER A 101     108.487 149.974 121.344  1.00 17.46           C  
ATOM    769  O   SER A 101     109.270 150.660 122.003  1.00 17.46           O  
ATOM    770  CB  SER A 101     106.442 150.505 119.957  1.00 17.46           C  
ATOM    771  OG  SER A 101     107.232 151.461 119.273  1.00 17.46           O  
ATOM    772  N   GLU A 102     108.886 148.971 120.560  1.00 17.47           N  
ATOM    773  CA  GLU A 102     110.278 148.526 120.552  1.00 17.47           C  
ATOM    774  C   GLU A 102     111.217 149.635 120.077  1.00 17.47           C  
ATOM    775  O   GLU A 102     112.198 149.970 120.755  1.00 17.47           O  
ATOM    776  CB  GLU A 102     110.399 147.274 119.679  1.00 17.47           C  
ATOM    777  CG  GLU A 102     111.794 146.695 119.573  1.00 17.47           C  
ATOM    778  CD  GLU A 102     111.808 145.315 118.944  1.00 17.47           C  
ATOM    779  OE1 GLU A 102     110.718 144.770 118.671  1.00 17.47           O  
ATOM    780  OE2 GLU A 102     112.911 144.773 118.724  1.00 17.47           O  
ATOM    781  N   ALA A 103     110.923 150.226 118.916  1.00 12.12           N  
ATOM    782  CA  ALA A 103     111.771 151.283 118.368  1.00 12.12           C  
ATOM    783  C   ALA A 103     111.741 152.537 119.240  1.00 12.12           C  
ATOM    784  O   ALA A 103     112.761 153.216 119.408  1.00 12.12           O  
ATOM    785  CB  ALA A 103     111.327 151.602 116.942  1.00 12.12           C  
ATOM    786  N   HIS A 104     110.573 152.852 119.796  1.00 10.81           N  
ATOM    787  CA  HIS A 104     110.416 153.954 120.745  1.00 10.81           C  
ATOM    788  C   HIS A 104     111.343 153.777 121.952  1.00 10.81           C  
ATOM    789  O   HIS A 104     112.123 154.679 122.311  1.00 10.81           O  
ATOM    790  CB  HIS A 104     108.934 153.981 121.142  1.00 10.81           C  
ATOM    791  CG  HIS A 104     108.556 154.976 122.191  1.00 10.81           C  
ATOM    792  ND1 HIS A 104     107.485 155.827 122.036  1.00 10.81           N  
ATOM    793  CD2 HIS A 104     109.042 155.209 123.432  1.00 10.81           C  
ATOM    794  CE1 HIS A 104     107.352 156.568 123.119  1.00 10.81           C  
ATOM    795  NE2 HIS A 104     108.287 156.215 123.980  1.00 10.81           N  
ATOM    796  N   ALA A 105     111.267 152.607 122.587  1.00  8.87           N  
ATOM    797  CA  ALA A 105     112.132 152.299 123.720  1.00  8.87           C  
ATOM    798  C   ALA A 105     113.604 152.385 123.334  1.00  8.87           C  
ATOM    799  O   ALA A 105     114.427 152.882 124.112  1.00  8.87           O  
ATOM    800  CB  ALA A 105     111.796 150.912 124.268  1.00  8.87           C  
ATOM    801  N   ALA A 106     113.957 151.896 122.143  1.00  7.80           N  
ATOM    802  CA  ALA A 106     115.342 151.992 121.690  1.00  7.80           C  
ATOM    803  C   ALA A 106     115.792 153.446 121.577  1.00  7.80           C  
ATOM    804  O   ALA A 106     116.933 153.785 121.923  1.00  7.80           O  
ATOM    805  CB  ALA A 106     115.506 151.270 120.355  1.00  7.80           C  
ATOM    806  N   LYS A 107     114.912 154.318 121.079  1.00  6.52           N  
ATOM    807  CA  LYS A 107     115.232 155.742 121.026  1.00  6.52           C  
ATOM    808  C   LYS A 107     115.554 156.281 122.417  1.00  6.52           C  
ATOM    809  O   LYS A 107     116.538 157.005 122.597  1.00  6.52           O  
ATOM    810  CB  LYS A 107     114.079 156.530 120.392  1.00  6.52           C  
ATOM    811  CG  LYS A 107     114.072 156.499 118.865  1.00  6.52           C  
ATOM    812  CD  LYS A 107     112.985 157.363 118.225  1.00  6.52           C  
ATOM    813  CE  LYS A 107     113.186 158.844 118.437  1.00  6.52           C  
ATOM    814  NZ  LYS A 107     112.391 159.673 117.487  1.00  6.52           N  
ATOM    815  N   ILE A 108     114.733 155.937 123.415  1.00  7.62           N  
ATOM    816  CA  ILE A 108     114.987 156.420 124.780  1.00  7.62           C  
ATOM    817  C   ILE A 108     116.316 155.870 125.309  1.00  7.62           C  
ATOM    818  O   ILE A 108     117.080 156.575 125.989  1.00  7.62           O  
ATOM    819  CB  ILE A 108     113.800 156.061 125.700  1.00  7.62           C  
ATOM    820  CG1 ILE A 108     112.521 156.744 125.191  1.00  7.62           C  
ATOM    821  CG2 ILE A 108     114.065 156.456 127.158  1.00  7.62           C  
ATOM    822  CD1 ILE A 108     111.267 156.447 125.982  1.00  7.62           C  
ATOM    823  N   VAL A 109     116.604 154.602 125.010  1.00  5.33           N  
ATOM    824  CA  VAL A 109     117.828 153.956 125.485  1.00  5.33           C  
ATOM    825  C   VAL A 109     119.062 154.655 124.917  1.00  5.33           C  
ATOM    826  O   VAL A 109     120.068 154.836 125.618  1.00  5.33           O  
ATOM    827  CB  VAL A 109     117.786 152.451 125.137  1.00  5.33           C  
ATOM    828  CG1 VAL A 109     119.133 151.758 125.338  1.00  5.33           C  
ATOM    829  CG2 VAL A 109     116.716 151.743 125.978  1.00  5.33           C  
ATOM    830  N   LYS A 110     119.008 155.051 123.642  1.00  5.73           N  
ATOM    831  CA  LYS A 110     120.119 155.787 123.036  1.00  5.73           C  
ATOM    832  C   LYS A 110     120.534 156.973 123.906  1.00  5.73           C  
ATOM    833  O   LYS A 110     121.710 157.122 124.275  1.00  5.73           O  
ATOM    834  CB  LYS A 110     119.730 156.259 121.626  1.00  5.73           C  
ATOM    835  CG  LYS A 110     120.855 156.945 120.854  1.00  5.73           C  
ATOM    836  CD  LYS A 110     120.511 157.235 119.385  1.00  5.73           C  
ATOM    837  CE  LYS A 110     120.870 156.081 118.467  1.00  5.73           C  
ATOM    838  NZ  LYS A 110     120.652 156.406 117.028  1.00  5.73           N  
ATOM    839  N   VAL A 111     119.566 157.810 124.275  1.00  5.33           N  
ATOM    840  CA  VAL A 111     119.886 159.054 124.966  1.00  5.33           C  
ATOM    841  C   VAL A 111     120.218 158.805 126.436  1.00  5.33           C  
ATOM    842  O   VAL A 111     121.052 159.514 127.004  1.00  5.33           O  
ATOM    843  CB  VAL A 111     118.748 160.081 124.796  1.00  5.33           C  
ATOM    844  CG1 VAL A 111     117.429 159.555 125.306  1.00  5.33           C  
ATOM    845  CG2 VAL A 111     119.084 161.376 125.486  1.00  5.33           C  
ATOM    846  N   GLN A 112     119.620 157.792 127.072  1.00  5.88           N  
ATOM    847  CA  GLN A 112     120.046 157.435 128.427  1.00  5.88           C  
ATOM    848  C   GLN A 112     121.519 157.025 128.446  1.00  5.88           C  
ATOM    849  O   GLN A 112     122.300 157.477 129.300  1.00  5.88           O  
ATOM    850  CB  GLN A 112     119.168 156.310 128.980  1.00  5.88           C  
ATOM    851  CG  GLN A 112     117.755 156.719 129.385  1.00  5.88           C  
ATOM    852  CD  GLN A 112     116.969 155.573 129.989  1.00  5.88           C  
ATOM    853  OE1 GLN A 112     116.616 155.592 131.168  1.00  5.88           O  
ATOM    854  NE2 GLN A 112     116.695 154.568 129.184  1.00  5.88           N  
ATOM    855  N   ASP A 113     121.915 156.168 127.502  1.00  7.01           N  
ATOM    856  CA  ASP A 113     123.307 155.739 127.420  1.00  7.01           C  
ATOM    857  C   ASP A 113     124.236 156.923 127.183  1.00  7.01           C  
ATOM    858  O   ASP A 113     125.285 157.041 127.830  1.00  7.01           O  
ATOM    859  CB  ASP A 113     123.468 154.699 126.310  1.00  7.01           C  
ATOM    860  CG  ASP A 113     122.876 153.354 126.679  1.00  7.01           C  
ATOM    861  OD1 ASP A 113     122.572 153.139 127.870  1.00  7.01           O  
ATOM    862  OD2 ASP A 113     122.712 152.511 125.775  1.00  7.01           O  
ATOM    863  N   MET A 114     123.859 157.820 126.269  1.00 10.81           N  
ATOM    864  CA  MET A 114     124.710 158.974 125.993  1.00 10.81           C  
ATOM    865  C   MET A 114     124.829 159.882 127.212  1.00 10.81           C  
ATOM    866  O   MET A 114     125.905 160.420 127.485  1.00 10.81           O  
ATOM    867  CB  MET A 114     124.185 159.753 124.790  1.00 10.81           C  
ATOM    868  CG  MET A 114     124.470 159.090 123.455  1.00 10.81           C  
ATOM    869  SD  MET A 114     123.890 160.047 122.052  1.00 10.81           S  
ATOM    870  CE  MET A 114     125.245 161.202 121.898  1.00 10.81           C  
ATOM    871  N   ALA A 115     123.739 160.067 127.958  1.00  5.74           N  
ATOM    872  CA  ALA A 115     123.799 160.928 129.134  1.00  5.74           C  
ATOM    873  C   ALA A 115     124.693 160.336 130.214  1.00  5.74           C  
ATOM    874  O   ALA A 115     125.427 161.067 130.885  1.00  5.74           O  
ATOM    875  CB  ALA A 115     122.401 161.178 129.689  1.00  5.74           C  
ATOM    876  N   LEU A 116     124.647 159.018 130.404  1.00  6.52           N  
ATOM    877  CA  LEU A 116     125.535 158.426 131.401  1.00  6.52           C  
ATOM    878  C   LEU A 116     126.989 158.508 130.946  1.00  6.52           C  
ATOM    879  O   LEU A 116     127.889 158.722 131.764  1.00  6.52           O  
ATOM    880  CB  LEU A 116     125.140 156.982 131.694  1.00  6.52           C  
ATOM    881  CG  LEU A 116     125.975 156.297 132.788  1.00  6.52           C  
ATOM    882  CD1 LEU A 116     125.879 157.014 134.136  1.00  6.52           C  
ATOM    883  CD2 LEU A 116     125.559 154.860 132.932  1.00  6.52           C  
ATOM    884  N   LYS A 117     127.232 158.371 129.641  1.00  8.35           N  
ATOM    885  CA  LYS A 117     128.595 158.439 129.115  1.00  8.35           C  
ATOM    886  C   LYS A 117     129.173 159.855 129.192  1.00  8.35           C  
ATOM    887  O   LYS A 117     130.349 160.025 129.528  1.00  8.35           O  
ATOM    888  CB  LYS A 117     128.604 157.910 127.682  1.00  8.35           C  
ATOM    889  CG  LYS A 117     129.943 157.838 127.006  1.00  8.35           C  
ATOM    890  CD  LYS A 117     129.814 157.080 125.679  1.00  8.35           C  
ATOM    891  CE  LYS A 117     129.036 157.895 124.656  1.00  8.35           C  
ATOM    892  NZ  LYS A 117     128.968 157.270 123.304  1.00  8.35           N  
ATOM    893  N   MET A 118     128.381 160.878 128.852  1.00  9.97           N  
ATOM    894  CA  MET A 118     128.808 162.273 128.955  1.00  9.97           C  
ATOM    895  C   MET A 118     128.825 162.800 130.383  1.00  9.97           C  
ATOM    896  O   MET A 118     129.386 163.874 130.619  1.00  9.97           O  
ATOM    897  CB  MET A 118     127.892 163.193 128.143  1.00  9.97           C  
ATOM    898  CG  MET A 118     127.819 162.924 126.677  1.00  9.97           C  
ATOM    899  SD  MET A 118     129.382 163.329 125.914  1.00  9.97           S  
ATOM    900  CE  MET A 118     129.988 161.687 125.672  1.00  9.97           C  
ATOM    901  N   ARG A 119     128.216 162.091 131.325  1.00  7.84           N  
ATOM    902  CA  ARG A 119     128.007 162.576 132.686  1.00  7.84           C  
ATOM    903  C   ARG A 119     127.311 163.942 132.681  1.00  7.84           C  
ATOM    904  O   ARG A 119     127.856 164.957 133.111  1.00  7.84           O  
ATOM    905  CB  ARG A 119     129.333 162.617 133.457  1.00  7.84           C  
ATOM    906  CG  ARG A 119     130.066 161.287 133.526  1.00  7.84           C  
ATOM    907  CD  ARG A 119     129.299 160.260 134.328  1.00  7.84           C  
ATOM    908  NE  ARG A 119     130.187 159.287 134.954  1.00  7.84           N  
ATOM    909  CZ  ARG A 119     130.505 158.103 134.439  1.00  7.84           C  
ATOM    910  NH1 ARG A 119     131.325 157.305 135.099  1.00  7.84           N  
ATOM    911  NH2 ARG A 119     130.013 157.707 133.275  1.00  7.84           N  
ATOM    912  N   ALA A 120     126.077 163.949 132.162  1.00  5.66           N  
ATOM    913  CA  ALA A 120     125.224 165.133 132.173  1.00  5.66           C  
ATOM    914  C   ALA A 120     123.788 164.791 132.574  1.00  5.66           C  
ATOM    915  O   ALA A 120     123.420 163.612 132.600  1.00  5.66           O  
ATOM    916  CB  ALA A 120     125.246 165.808 130.805  1.00  5.66           C  
ATOM    917  N   PRO A 121     122.957 165.785 132.890  1.00  7.04           N  
ATOM    918  CA  PRO A 121     121.583 165.502 133.332  1.00  7.04           C  
ATOM    919  C   PRO A 121     120.674 165.030 132.201  1.00  7.04           C  
ATOM    920  O   PRO A 121     120.933 165.254 131.019  1.00  7.04           O  
ATOM    921  CB  PRO A 121     121.098 166.845 133.888  1.00  7.04           C  
ATOM    922  CG  PRO A 121     122.284 167.687 134.043  1.00  7.04           C  
ATOM    923  CD  PRO A 121     123.346 167.182 133.143  1.00  7.04           C  
ATOM    924  N   ILE A 122     119.573 164.377 132.591  1.00 12.77           N  
ATOM    925  CA  ILE A 122     118.559 163.886 131.660  1.00 12.77           C  
ATOM    926  C   ILE A 122     117.164 164.248 132.175  1.00 12.77           C  
ATOM    927  O   ILE A 122     116.826 163.985 133.340  1.00 12.77           O  
ATOM    928  CB  ILE A 122     118.691 162.366 131.414  1.00 12.77           C  
ATOM    929  CG1 ILE A 122     117.716 161.894 130.319  1.00 12.77           C  
ATOM    930  CG2 ILE A 122     118.516 161.579 132.695  1.00 12.77           C  
ATOM    931  CD1 ILE A 122     118.155 160.627 129.629  1.00 12.77           C  
ATOM    932  N   ILE A 123     116.369 164.864 131.300  1.00  6.21           N  
ATOM    933  CA  ILE A 123     115.000 165.285 131.581  1.00  6.21           C  
ATOM    934  C   ILE A 123     114.046 164.439 130.743  1.00  6.21           C  
ATOM    935  O   ILE A 123     114.243 164.283 129.532  1.00  6.21           O  
ATOM    936  CB  ILE A 123     114.791 166.782 131.280  1.00  6.21           C  
ATOM    937  CG1 ILE A 123     115.897 167.655 131.900  1.00  6.21           C  
ATOM    938  CG2 ILE A 123     113.402 167.232 131.741  1.00  6.21           C  
ATOM    939  CD1 ILE A 123     116.016 167.567 133.378  1.00  6.21           C  
ATOM    940  N   GLY A 124     113.016 163.908 131.382  1.00  5.70           N  
ATOM    941  CA  GLY A 124     111.957 163.179 130.695  1.00  5.70           C  
ATOM    942  C   GLY A 124     110.623 163.887 130.846  1.00  5.70           C  
ATOM    943  O   GLY A 124     110.306 164.394 131.920  1.00  5.70           O  
ATOM    944  N   ILE A 125     109.843 163.911 129.765  1.00  6.41           N  
ATOM    945  CA  ILE A 125     108.552 164.600 129.712  1.00  6.41           C  
ATOM    946  C   ILE A 125     107.497 163.596 129.251  1.00  6.41           C  
ATOM    947  O   ILE A 125     107.585 163.066 128.137  1.00  6.41           O  
ATOM    948  CB  ILE A 125     108.603 165.827 128.787  1.00  6.41           C  
ATOM    949  CG1 ILE A 125     109.803 166.717 129.143  1.00  6.41           C  
ATOM    950  CG2 ILE A 125     107.317 166.626 128.875  1.00  6.41           C  
ATOM    951  CD1 ILE A 125     109.942 167.931 128.280  1.00  6.41           C  
ATOM    952  N   PHE A 126     106.496 163.345 130.097  1.00  8.89           N  
ATOM    953  CA  PHE A 126     105.579 162.221 129.928  1.00  8.89           C  
ATOM    954  C   PHE A 126     104.167 162.679 129.577  1.00  8.89           C  
ATOM    955  O   PHE A 126     103.580 163.508 130.279  1.00  8.89           O  
ATOM    956  CB  PHE A 126     105.556 161.363 131.191  1.00  8.89           C  
ATOM    957  CG  PHE A 126     106.849 160.654 131.450  1.00  8.89           C  
ATOM    958  CD1 PHE A 126     107.912 161.314 132.027  1.00  8.89           C  
ATOM    959  CD2 PHE A 126     107.008 159.332 131.095  1.00  8.89           C  
ATOM    960  CE1 PHE A 126     109.097 160.668 132.256  1.00  8.89           C  
ATOM    961  CE2 PHE A 126     108.195 158.684 131.322  1.00  8.89           C  
ATOM    962  CZ  PHE A 126     109.240 159.356 131.902  1.00  8.89           C  
ATOM    963  N   ASP A 127     103.643 162.139 128.473  1.00 15.85           N  
ATOM    964  CA  ASP A 127     102.254 162.302 128.035  1.00 15.85           C  
ATOM    965  C   ASP A 127     101.937 161.067 127.185  1.00 15.85           C  
ATOM    966  O   ASP A 127     102.167 161.064 125.975  1.00 15.85           O  
ATOM    967  CB  ASP A 127     102.097 163.598 127.254  1.00 15.85           C  
ATOM    968  CG  ASP A 127     100.654 163.949 126.953  1.00 15.85           C  
ATOM    969  OD1 ASP A 127      99.743 163.205 127.364  1.00 15.85           O  
ATOM    970  OD2 ASP A 127     100.440 164.989 126.301  1.00 15.85           O  
ATOM    971  N   ALA A 128     101.388 160.033 127.818  1.00 22.12           N  
ATOM    972  CA  ALA A 128     101.458 158.697 127.229  1.00 22.12           C  
ATOM    973  C   ALA A 128     100.309 157.830 127.735  1.00 22.12           C  
ATOM    974  O   ALA A 128      99.397 158.306 128.419  1.00 22.12           O  
ATOM    975  CB  ALA A 128     102.813 158.056 127.537  1.00 22.12           C  
ATOM    976  N   GLY A 129     100.351 156.546 127.366  1.00 32.64           N  
ATOM    977  CA  GLY A 129      99.372 155.563 127.789  1.00 32.64           C  
ATOM    978  C   GLY A 129      99.950 154.185 128.061  1.00 32.64           C  
ATOM    979  O   GLY A 129      99.196 153.232 128.278  1.00 32.64           O  
ATOM    980  N   GLY A 130     101.276 154.055 128.047  1.00 28.09           N  
ATOM    981  CA  GLY A 130     101.918 152.810 128.432  1.00 28.09           C  
ATOM    982  C   GLY A 130     102.407 151.956 127.278  1.00 28.09           C  
ATOM    983  O   GLY A 130     102.700 152.464 126.193  1.00 28.09           O  
ATOM    984  N   ALA A 131     102.511 150.650 127.515  1.00 25.95           N  
ATOM    985  CA  ALA A 131     102.929 149.719 126.474  1.00 25.95           C  
ATOM    986  C   ALA A 131     101.903 149.669 125.348  1.00 25.95           C  
ATOM    987  O   ALA A 131     100.694 149.751 125.580  1.00 25.95           O  
ATOM    988  CB  ALA A 131     103.125 148.324 127.065  1.00 25.95           C  
ATOM    989  N   ARG A 132     102.395 149.527 124.119  1.00 21.86           N  
ATOM    990  CA  ARG A 132     101.536 149.459 122.939  1.00 21.86           C  
ATOM    991  C   ARG A 132     101.034 148.029 122.775  1.00 21.86           C  
ATOM    992  O   ARG A 132     101.816 147.113 122.503  1.00 21.86           O  
ATOM    993  CB  ARG A 132     102.291 149.931 121.700  1.00 21.86           C  
ATOM    994  CG  ARG A 132     101.407 150.117 120.486  1.00 21.86           C  
ATOM    995  CD  ARG A 132     102.170 150.663 119.292  1.00 21.86           C  
ATOM    996  NE  ARG A 132     102.772 151.964 119.555  1.00 21.86           N  
ATOM    997  CZ  ARG A 132     103.724 152.516 118.813  1.00 21.86           C  
ATOM    998  NH1 ARG A 132     104.193 151.891 117.744  1.00 21.86           N  
ATOM    999  NH2 ARG A 132     104.207 153.702 119.140  1.00 21.86           N  
ATOM   1000  N   ILE A 133      99.724 147.841 122.928  1.00 24.08           N  
ATOM   1001  CA  ILE A 133      99.160 146.498 123.049  1.00 24.08           C  
ATOM   1002  C   ILE A 133      99.374 145.695 121.768  1.00 24.08           C  
ATOM   1003  O   ILE A 133      99.708 144.505 121.814  1.00 24.08           O  
ATOM   1004  CB  ILE A 133      97.669 146.590 123.423  1.00 24.08           C  
ATOM   1005  CG1 ILE A 133      97.496 147.276 124.784  1.00 24.08           C  
ATOM   1006  CG2 ILE A 133      97.034 145.221 123.429  1.00 24.08           C  
ATOM   1007  CD1 ILE A 133      97.961 146.457 125.976  1.00 24.08           C  
ATOM   1008  N   GLN A 134      99.195 146.331 120.609  1.00 26.74           N  
ATOM   1009  CA  GLN A 134      99.282 145.608 119.341  1.00 26.74           C  
ATOM   1010  C   GLN A 134     100.627 144.913 119.168  1.00 26.74           C  
ATOM   1011  O   GLN A 134     100.713 143.903 118.461  1.00 26.74           O  
ATOM   1012  CB  GLN A 134      99.032 146.559 118.170  1.00 26.74           C  
ATOM   1013  CG  GLN A 134      97.632 147.133 118.111  1.00 26.74           C  
ATOM   1014  CD  GLN A 134      97.439 148.311 119.034  1.00 26.74           C  
ATOM   1015  OE1 GLN A 134      98.194 148.502 119.986  1.00 26.74           O  
ATOM   1016  NE2 GLN A 134      96.426 149.116 118.755  1.00 26.74           N  
ATOM   1017  N   GLU A 135     101.680 145.428 119.796  1.00 21.78           N  
ATOM   1018  CA  GLU A 135     103.013 144.861 119.656  1.00 21.78           C  
ATOM   1019  C   GLU A 135     103.302 143.744 120.649  1.00 21.78           C  
ATOM   1020  O   GLU A 135     104.271 143.002 120.456  1.00 21.78           O  
ATOM   1021  CB  GLU A 135     104.066 145.964 119.799  1.00 21.78           C  
ATOM   1022  CG  GLU A 135     104.136 146.892 118.596  1.00 21.78           C  
ATOM   1023  CD  GLU A 135     105.524 147.457 118.356  1.00 21.78           C  
ATOM   1024  OE1 GLU A 135     106.427 147.216 119.184  1.00 21.78           O  
ATOM   1025  OE2 GLU A 135     105.713 148.148 117.333  1.00 21.78           O  
ATOM   1026  N   GLY A 136     102.494 143.602 121.695  1.00 15.87           N  
ATOM   1027  CA  GLY A 136     102.657 142.474 122.583  1.00 15.87           C  
ATOM   1028  C   GLY A 136     103.916 142.534 123.436  1.00 15.87           C  
ATOM   1029  O   GLY A 136     104.436 143.604 123.773  1.00 15.87           O  
ATOM   1030  N   VAL A 137     104.422 141.344 123.770  1.00 13.55           N  
ATOM   1031  CA  VAL A 137     105.472 141.219 124.778  1.00 13.55           C  
ATOM   1032  C   VAL A 137     106.723 141.994 124.387  1.00 13.55           C  
ATOM   1033  O   VAL A 137     107.455 142.475 125.259  1.00 13.55           O  
ATOM   1034  CB  VAL A 137     105.778 139.730 125.042  1.00 13.55           C  
ATOM   1035  CG1 VAL A 137     106.299 139.035 123.795  1.00 13.55           C  
ATOM   1036  CG2 VAL A 137     106.775 139.591 126.170  1.00 13.55           C  
ATOM   1037  N   ALA A 138     106.987 142.144 123.087  1.00 14.19           N  
ATOM   1038  CA  ALA A 138     108.131 142.941 122.659  1.00 14.19           C  
ATOM   1039  C   ALA A 138     108.149 144.284 123.378  1.00 14.19           C  
ATOM   1040  O   ALA A 138     109.169 144.685 123.950  1.00 14.19           O  
ATOM   1041  CB  ALA A 138     108.102 143.135 121.144  1.00 14.19           C  
ATOM   1042  N   ALA A 139     107.004 144.968 123.402  1.00 13.34           N  
ATOM   1043  CA  ALA A 139     106.944 146.280 124.033  1.00 13.34           C  
ATOM   1044  C   ALA A 139     107.408 146.214 125.482  1.00 13.34           C  
ATOM   1045  O   ALA A 139     108.192 147.061 125.931  1.00 13.34           O  
ATOM   1046  CB  ALA A 139     105.526 146.838 123.945  1.00 13.34           C  
ATOM   1047  N   LEU A 140     106.958 145.200 126.222  1.00 11.51           N  
ATOM   1048  CA  LEU A 140     107.387 145.047 127.608  1.00 11.51           C  
ATOM   1049  C   LEU A 140     108.905 145.008 127.701  1.00 11.51           C  
ATOM   1050  O   LEU A 140     109.509 145.708 128.524  1.00 11.51           O  
ATOM   1051  CB  LEU A 140     106.776 143.784 128.215  1.00 11.51           C  
ATOM   1052  CG  LEU A 140     105.257 143.642 128.141  1.00 11.51           C  
ATOM   1053  CD1 LEU A 140     104.834 142.292 128.696  1.00 11.51           C  
ATOM   1054  CD2 LEU A 140     104.553 144.766 128.872  1.00 11.51           C  
ATOM   1055  N   GLY A 141     109.541 144.211 126.842  1.00 11.50           N  
ATOM   1056  CA  GLY A 141     110.993 144.180 126.829  1.00 11.50           C  
ATOM   1057  C   GLY A 141     111.581 145.572 126.790  1.00 11.50           C  
ATOM   1058  O   GLY A 141     112.453 145.918 127.592  1.00 11.50           O  
ATOM   1059  N   GLY A 142     111.067 146.409 125.890  1.00 12.23           N  
ATOM   1060  CA  GLY A 142     111.559 147.769 125.801  1.00 12.23           C  
ATOM   1061  C   GLY A 142     111.557 148.465 127.146  1.00 12.23           C  
ATOM   1062  O   GLY A 142     112.594 148.959 127.601  1.00 12.23           O  
ATOM   1063  N   HIS A 143     110.424 148.473 127.766  1.00 12.00           N  
ATOM   1064  CA  HIS A 143     110.298 149.074 129.111  1.00 12.00           C  
ATOM   1065  C   HIS A 143     111.438 148.587 130.053  1.00 12.00           C  
ATOM   1066  O   HIS A 143     112.215 149.391 130.610  1.00 12.00           O  
ATOM   1067  CB  HIS A 143     108.929 148.753 129.638  1.00 12.00           C  
ATOM   1068  CG  HIS A 143     107.921 149.793 129.366  1.00 12.00           C  
ATOM   1069  ND1 HIS A 143     106.641 149.502 129.125  1.00 12.00           N  
ATOM   1070  CD2 HIS A 143     107.977 151.112 129.333  1.00 12.00           C  
ATOM   1071  CE1 HIS A 143     105.945 150.584 128.980  1.00 12.00           C  
ATOM   1072  NE2 HIS A 143     106.735 151.567 129.095  1.00 12.00           N  
ATOM   1073  N   GLY A 144     111.672 147.264 130.098  1.00  9.08           N  
ATOM   1074  CA  GLY A 144     112.715 146.724 130.946  1.00  9.08           C  
ATOM   1075  C   GLY A 144     114.056 147.373 130.683  1.00  9.08           C  
ATOM   1076  O   GLY A 144     114.717 147.851 131.609  1.00  9.08           O  
ATOM   1077  N   GLU A 145     114.448 147.456 129.410  1.00  9.53           N  
ATOM   1078  CA  GLU A 145     115.723 148.084 129.092  1.00  9.53           C  
ATOM   1079  C   GLU A 145     115.777 149.489 129.670  1.00  9.53           C  
ATOM   1080  O   GLU A 145     116.681 149.812 130.449  1.00  9.53           O  
ATOM   1081  CB  GLU A 145     115.941 148.097 127.580  1.00  9.53           C  
ATOM   1082  CG  GLU A 145     116.140 146.714 126.956  1.00  9.53           C  
ATOM   1083  CD  GLU A 145     117.261 145.919 127.598  1.00  9.53           C  
ATOM   1084  OE1 GLU A 145     117.008 144.776 128.029  1.00  9.53           O  
ATOM   1085  OE2 GLU A 145     118.394 146.434 127.672  1.00  9.53           O  
ATOM   1086  N   VAL A 146     114.760 150.303 129.387  1.00  6.29           N  
ATOM   1087  CA  VAL A 146     114.725 151.648 129.948  1.00  6.29           C  
ATOM   1088  C   VAL A 146     114.914 151.573 131.457  1.00  6.29           C  
ATOM   1089  O   VAL A 146     115.802 152.224 132.025  1.00  6.29           O  
ATOM   1090  CB  VAL A 146     113.414 152.360 129.560  1.00  6.29           C  
ATOM   1091  CG1 VAL A 146     113.243 153.654 130.339  1.00  6.29           C  
ATOM   1092  CG2 VAL A 146     113.376 152.627 128.048  1.00  6.29           C  
ATOM   1093  N   PHE A 147     114.139 150.709 132.115  1.00  6.67           N  
ATOM   1094  CA  PHE A 147     114.223 150.596 133.565  1.00  6.67           C  
ATOM   1095  C   PHE A 147     115.663 150.362 134.011  1.00  6.67           C  
ATOM   1096  O   PHE A 147     116.184 151.105 134.852  1.00  6.67           O  
ATOM   1097  CB  PHE A 147     113.300 149.480 134.069  1.00  6.67           C  
ATOM   1098  CG  PHE A 147     111.828 149.743 133.863  1.00  6.67           C  
ATOM   1099  CD1 PHE A 147     111.343 151.016 133.638  1.00  6.67           C  
ATOM   1100  CD2 PHE A 147     110.924 148.699 133.902  1.00  6.67           C  
ATOM   1101  CE1 PHE A 147     109.998 151.233 133.457  1.00  6.67           C  
ATOM   1102  CE2 PHE A 147     109.583 148.919 133.716  1.00  6.67           C  
ATOM   1103  CZ  PHE A 147     109.121 150.180 133.498  1.00  6.67           C  
ATOM   1104  N   ARG A 148     116.350 149.378 133.413  1.00  9.67           N  
ATOM   1105  CA  ARG A 148     117.678 149.048 133.924  1.00  9.67           C  
ATOM   1106  C   ARG A 148     118.551 150.294 133.937  1.00  9.67           C  
ATOM   1107  O   ARG A 148     119.250 150.569 134.921  1.00  9.67           O  
ATOM   1108  CB  ARG A 148     118.351 147.924 133.110  1.00  9.67           C  
ATOM   1109  CG  ARG A 148     118.976 148.322 131.769  1.00  9.67           C  
ATOM   1110  CD  ARG A 148     119.990 147.285 131.226  1.00  9.67           C  
ATOM   1111  NE  ARG A 148     119.430 146.015 130.767  1.00  9.67           N  
ATOM   1112  CZ  ARG A 148     119.652 144.826 131.328  1.00  9.67           C  
ATOM   1113  NH1 ARG A 148     119.092 143.748 130.798  1.00  9.67           N  
ATOM   1114  NH2 ARG A 148     120.427 144.689 132.399  1.00  9.67           N  
ATOM   1115  N   ARG A 149     118.452 151.107 132.889  1.00  7.13           N  
ATOM   1116  CA  ARG A 149     119.370 152.226 132.760  1.00  7.13           C  
ATOM   1117  C   ARG A 149     119.078 153.289 133.810  1.00  7.13           C  
ATOM   1118  O   ARG A 149     120.011 153.856 134.395  1.00  7.13           O  
ATOM   1119  CB  ARG A 149     119.314 152.762 131.333  1.00  7.13           C  
ATOM   1120  CG  ARG A 149     120.177 151.899 130.408  1.00  7.13           C  
ATOM   1121  CD  ARG A 149     119.853 152.006 128.952  1.00  7.13           C  
ATOM   1122  NE  ARG A 149     120.666 151.076 128.168  1.00  7.13           N  
ATOM   1123  CZ  ARG A 149     120.387 149.788 127.999  1.00  7.13           C  
ATOM   1124  NH1 ARG A 149     119.324 149.243 128.567  1.00  7.13           N  
ATOM   1125  NH2 ARG A 149     121.184 149.035 127.263  1.00  7.13           N  
ATOM   1126  N   ASN A 150     117.797 153.517 134.121  1.00  5.97           N  
ATOM   1127  CA  ASN A 150     117.465 154.372 135.255  1.00  5.97           C  
ATOM   1128  C   ASN A 150     118.304 153.973 136.467  1.00  5.97           C  
ATOM   1129  O   ASN A 150     119.027 154.796 137.044  1.00  5.97           O  
ATOM   1130  CB  ASN A 150     115.967 154.285 135.579  1.00  5.97           C  
ATOM   1131  CG  ASN A 150     115.084 154.982 134.554  1.00  5.97           C  
ATOM   1132  OD1 ASN A 150     114.120 154.404 134.059  1.00  5.97           O  
ATOM   1133  ND2 ASN A 150     115.384 156.237 134.265  1.00  5.97           N  
ATOM   1134  N   VAL A 151     118.291 152.679 136.800  1.00  6.35           N  
ATOM   1135  CA  VAL A 151     118.921 152.223 138.033  1.00  6.35           C  
ATOM   1136  C   VAL A 151     120.427 152.395 137.945  1.00  6.35           C  
ATOM   1137  O   VAL A 151     121.087 152.651 138.957  1.00  6.35           O  
ATOM   1138  CB  VAL A 151     118.518 150.765 138.336  1.00  6.35           C  
ATOM   1139  CG1 VAL A 151     119.218 150.247 139.595  1.00  6.35           C  
ATOM   1140  CG2 VAL A 151     116.998 150.654 138.479  1.00  6.35           C  
ATOM   1141  N   ALA A 152     120.993 152.300 136.742  1.00  5.51           N  
ATOM   1142  CA  ALA A 152     122.433 152.469 136.611  1.00  5.51           C  
ATOM   1143  C   ALA A 152     122.834 153.923 136.809  1.00  5.51           C  
ATOM   1144  O   ALA A 152     123.925 154.199 137.316  1.00  5.51           O  
ATOM   1145  CB  ALA A 152     122.904 151.963 135.251  1.00  5.51           C  
ATOM   1146  N   ALA A 153     121.962 154.858 136.431  1.00  5.16           N  
ATOM   1147  CA  ALA A 153     122.269 156.278 136.509  1.00  5.16           C  
ATOM   1148  C   ALA A 153     122.020 156.876 137.891  1.00  5.16           C  
ATOM   1149  O   ALA A 153     122.430 158.015 138.132  1.00  5.16           O  
ATOM   1150  CB  ALA A 153     121.451 157.027 135.461  1.00  5.16           C  
ATOM   1151  N   SER A 154     121.384 156.136 138.797  1.00  5.33           N  
ATOM   1152  CA  SER A 154     120.969 156.675 140.087  1.00  5.33           C  
ATOM   1153  C   SER A 154     122.189 157.002 140.946  1.00  5.33           C  
ATOM   1154  O   SER A 154     122.976 156.115 141.288  1.00  5.33           O  
ATOM   1155  CB  SER A 154     120.055 155.680 140.801  1.00  5.33           C  
ATOM   1156  OG  SER A 154     119.807 156.074 142.134  1.00  5.33           O  
ATOM   1157  N   GLY A 155     122.328 158.274 141.308  1.00  6.50           N  
ATOM   1158  CA  GLY A 155     123.454 158.769 142.072  1.00  6.50           C  
ATOM   1159  C   GLY A 155     124.671 159.164 141.258  1.00  6.50           C  
ATOM   1160  O   GLY A 155     125.682 159.561 141.848  1.00  6.50           O  
ATOM   1161  N   VAL A 156     124.615 159.054 139.932  1.00 12.77           N  
ATOM   1162  CA  VAL A 156     125.698 159.466 139.044  1.00 12.77           C  
ATOM   1163  C   VAL A 156     125.357 160.768 138.316  1.00 12.77           C  
ATOM   1164  O   VAL A 156     126.160 161.700 138.287  1.00 12.77           O  
ATOM   1165  CB  VAL A 156     126.051 158.342 138.039  1.00 12.77           C  
ATOM   1166  CG1 VAL A 156     127.327 158.677 137.268  1.00 12.77           C  
ATOM   1167  CG2 VAL A 156     126.195 157.002 138.747  1.00 12.77           C  
ATOM   1168  N   ILE A 157     124.172 160.842 137.716  1.00 12.77           N  
ATOM   1169  CA  ILE A 157     123.677 162.049 137.050  1.00 12.77           C  
ATOM   1170  C   ILE A 157     122.273 162.341 137.571  1.00 12.77           C  
ATOM   1171  O   ILE A 157     121.536 161.401 137.893  1.00 12.77           O  
ATOM   1172  CB  ILE A 157     123.693 161.913 135.513  1.00 12.77           C  
ATOM   1173  CG1 ILE A 157     122.822 160.740 135.034  1.00 12.77           C  
ATOM   1174  CG2 ILE A 157     125.120 161.807 135.012  1.00 12.77           C  
ATOM   1175  CD1 ILE A 157     122.654 160.605 133.517  1.00 12.77           C  
ATOM   1176  N   PRO A 158     121.858 163.603 137.691  1.00 12.77           N  
ATOM   1177  CA  PRO A 158     120.477 163.873 138.103  1.00 12.77           C  
ATOM   1178  C   PRO A 158     119.490 163.545 136.992  1.00 12.77           C  
ATOM   1179  O   PRO A 158     119.729 163.834 135.818  1.00 12.77           O  
ATOM   1180  CB  PRO A 158     120.480 165.370 138.430  1.00 12.77           C  
ATOM   1181  CG  PRO A 158     121.639 165.927 137.765  1.00 12.77           C  
ATOM   1182  CD  PRO A 158     122.607 164.845 137.440  1.00 12.77           C  
ATOM   1183  N   GLN A 159     118.379 162.928 137.379  1.00  7.11           N  
ATOM   1184  CA  GLN A 159     117.295 162.562 136.474  1.00  7.11           C  
ATOM   1185  C   GLN A 159     116.027 163.277 136.922  1.00  7.11           C  
ATOM   1186  O   GLN A 159     115.607 163.124 138.073  1.00  7.11           O  
ATOM   1187  CB  GLN A 159     117.080 161.048 136.467  1.00  7.11           C  
ATOM   1188  CG  GLN A 159     118.339 160.223 136.239  1.00  7.11           C  
ATOM   1189  CD  GLN A 159     118.093 158.737 136.372  1.00  7.11           C  
ATOM   1190  OE1 GLN A 159     117.598 158.091 135.453  1.00  7.11           O  
ATOM   1191  NE2 GLN A 159     118.432 158.192 137.527  1.00  7.11           N  
ATOM   1192  N   ILE A 160     115.419 164.058 136.027  1.00  5.08           N  
ATOM   1193  CA  ILE A 160     114.182 164.776 136.337  1.00  5.08           C  
ATOM   1194  C   ILE A 160     113.053 164.285 135.432  1.00  5.08           C  
ATOM   1195  O   ILE A 160     113.276 163.980 134.257  1.00  5.08           O  
ATOM   1196  CB  ILE A 160     114.363 166.303 136.208  1.00  5.08           C  
ATOM   1197  CG1 ILE A 160     115.365 166.823 137.245  1.00  5.08           C  
ATOM   1198  CG2 ILE A 160     113.042 167.032 136.388  1.00  5.08           C  
ATOM   1199  CD1 ILE A 160     115.953 168.167 136.914  1.00  5.08           C  
ATOM   1200  N   SER A 161     111.836 164.221 135.986  1.00  5.99           N  
ATOM   1201  CA  SER A 161     110.637 163.784 135.274  1.00  5.99           C  
ATOM   1202  C   SER A 161     109.529 164.821 135.415  1.00  5.99           C  
ATOM   1203  O   SER A 161     109.252 165.289 136.523  1.00  5.99           O  
ATOM   1204  CB  SER A 161     110.141 162.442 135.804  1.00  5.99           C  
ATOM   1205  OG  SER A 161     111.161 161.469 135.772  1.00  5.99           O  
ATOM   1206  N   VAL A 162     108.879 165.154 134.302  1.00  6.16           N  
ATOM   1207  CA  VAL A 162     107.793 166.131 134.265  1.00  6.16           C  
ATOM   1208  C   VAL A 162     106.567 165.456 133.650  1.00  6.16           C  
ATOM   1209  O   VAL A 162     106.605 165.025 132.490  1.00  6.16           O  
ATOM   1210  CB  VAL A 162     108.176 167.388 133.469  1.00  6.16           C  
ATOM   1211  CG1 VAL A 162     107.132 168.476 133.662  1.00  6.16           C  
ATOM   1212  CG2 VAL A 162     109.577 167.869 133.841  1.00  6.16           C  
ATOM   1213  N   ILE A 163     105.480 165.396 134.414  1.00  7.38           N  
ATOM   1214  CA  ILE A 163     104.243 164.741 134.001  1.00  7.38           C  
ATOM   1215  C   ILE A 163     103.278 165.820 133.519  1.00  7.38           C  
ATOM   1216  O   ILE A 163     102.762 166.613 134.312  1.00  7.38           O  
ATOM   1217  CB  ILE A 163     103.631 163.908 135.134  1.00  7.38           C  
ATOM   1218  CG1 ILE A 163     104.706 163.080 135.851  1.00  7.38           C  
ATOM   1219  CG2 ILE A 163     102.532 163.008 134.607  1.00  7.38           C  
ATOM   1220  CD1 ILE A 163     105.422 162.094 134.981  1.00  7.38           C  
ATOM   1221  N   MET A 164     103.035 165.835 132.211  1.00 11.61           N  
ATOM   1222  CA  MET A 164     102.218 166.843 131.547  1.00 11.61           C  
ATOM   1223  C   MET A 164     101.025 166.219 130.832  1.00 11.61           C  
ATOM   1224  O   MET A 164     100.442 166.836 129.938  1.00 11.61           O  
ATOM   1225  CB  MET A 164     103.091 167.648 130.582  1.00 11.61           C  
ATOM   1226  CG  MET A 164     104.309 168.262 131.273  1.00 11.61           C  
ATOM   1227  SD  MET A 164     105.417 169.215 130.224  1.00 11.61           S  
ATOM   1228  CE  MET A 164     104.728 170.846 130.434  1.00 11.61           C  
ATOM   1229  N   GLY A 165     100.655 165.004 131.216  1.00 12.09           N  
ATOM   1230  CA  GLY A 165      99.483 164.346 130.701  1.00 12.09           C  
ATOM   1231  C   GLY A 165      99.229 163.041 131.424  1.00 12.09           C  
ATOM   1232  O   GLY A 165      99.684 162.832 132.552  1.00 12.09           O  
ATOM   1233  N   PRO A 166      98.489 162.135 130.794  1.00 15.57           N  
ATOM   1234  CA  PRO A 166      98.304 160.809 131.387  1.00 15.57           C  
ATOM   1235  C   PRO A 166      99.609 160.036 131.459  1.00 15.57           C  
ATOM   1236  O   PRO A 166     100.504 160.198 130.628  1.00 15.57           O  
ATOM   1237  CB  PRO A 166      97.317 160.126 130.436  1.00 15.57           C  
ATOM   1238  CG  PRO A 166      96.654 161.213 129.713  1.00 15.57           C  
ATOM   1239  CD  PRO A 166      97.634 162.331 129.613  1.00 15.57           C  
ATOM   1240  N   CYS A 167      99.702 159.173 132.468  1.00 15.43           N  
ATOM   1241  CA  CYS A 167     100.834 158.258 132.601  1.00 15.43           C  
ATOM   1242  C   CYS A 167     100.329 157.031 133.354  1.00 15.43           C  
ATOM   1243  O   CYS A 167     100.179 157.071 134.577  1.00 15.43           O  
ATOM   1244  CB  CYS A 167     102.004 158.916 133.314  1.00 15.43           C  
ATOM   1245  SG  CYS A 167     103.399 157.811 133.571  1.00 15.43           S  
ATOM   1246  N   ALA A 168     100.074 155.953 132.618  1.00 19.07           N  
ATOM   1247  CA  ALA A 168      99.402 154.781 133.153  1.00 19.07           C  
ATOM   1248  C   ALA A 168     100.204 153.525 132.848  1.00 19.07           C  
ATOM   1249  O   ALA A 168     100.917 153.438 131.846  1.00 19.07           O  
ATOM   1250  CB  ALA A 168      97.986 154.646 132.585  1.00 19.07           C  
ATOM   1251  N   GLY A 169     100.065 152.545 133.734  1.00 18.66           N  
ATOM   1252  CA  GLY A 169     100.720 151.266 133.540  1.00 18.66           C  
ATOM   1253  C   GLY A 169     102.222 151.359 133.713  1.00 18.66           C  
ATOM   1254  O   GLY A 169     102.740 152.171 134.490  1.00 18.66           O  
ATOM   1255  N   GLY A 170     102.932 150.537 132.939  1.00 16.80           N  
ATOM   1256  CA  GLY A 170     104.357 150.358 133.161  1.00 16.80           C  
ATOM   1257  C   GLY A 170     105.146 151.647 133.058  1.00 16.80           C  
ATOM   1258  O   GLY A 170     106.253 151.748 133.591  1.00 16.80           O  
ATOM   1259  N   ASP A 171     104.600 152.642 132.358  1.00 18.67           N  
ATOM   1260  CA  ASP A 171     105.290 153.922 132.267  1.00 18.67           C  
ATOM   1261  C   ASP A 171     105.633 154.468 133.646  1.00 18.67           C  
ATOM   1262  O   ASP A 171     106.765 154.919 133.871  1.00 18.67           O  
ATOM   1263  CB  ASP A 171     104.431 154.930 131.503  1.00 18.67           C  
ATOM   1264  CG  ASP A 171     104.630 154.857 130.001  1.00 18.67           C  
ATOM   1265  OD1 ASP A 171     105.481 154.067 129.539  1.00 18.67           O  
ATOM   1266  OD2 ASP A 171     103.928 155.594 129.281  1.00 18.67           O  
ATOM   1267  N   VAL A 172     104.696 154.376 134.596  1.00 13.87           N  
ATOM   1268  CA  VAL A 172     104.842 155.087 135.861  1.00 13.87           C  
ATOM   1269  C   VAL A 172     106.096 154.665 136.609  1.00 13.87           C  
ATOM   1270  O   VAL A 172     106.611 155.436 137.424  1.00 13.87           O  
ATOM   1271  CB  VAL A 172     103.612 154.889 136.773  1.00 13.87           C  
ATOM   1272  CG1 VAL A 172     102.343 155.431 136.124  1.00 13.87           C  
ATOM   1273  CG2 VAL A 172     103.447 153.439 137.165  1.00 13.87           C  
ATOM   1274  N   TYR A 173     106.613 153.467 136.352  1.00 12.88           N  
ATOM   1275  CA  TYR A 173     107.735 152.973 137.137  1.00 12.88           C  
ATOM   1276  C   TYR A 173     109.056 153.606 136.728  1.00 12.88           C  
ATOM   1277  O   TYR A 173     110.004 153.574 137.517  1.00 12.88           O  
ATOM   1278  CB  TYR A 173     107.816 151.449 137.043  1.00 12.88           C  
ATOM   1279  CG  TYR A 173     106.738 150.740 137.842  1.00 12.88           C  
ATOM   1280  CD1 TYR A 173     106.513 151.049 139.179  1.00 12.88           C  
ATOM   1281  CD2 TYR A 173     105.938 149.776 137.255  1.00 12.88           C  
ATOM   1282  CE1 TYR A 173     105.532 150.415 139.902  1.00 12.88           C  
ATOM   1283  CE2 TYR A 173     104.952 149.132 137.977  1.00 12.88           C  
ATOM   1284  CZ  TYR A 173     104.754 149.456 139.298  1.00 12.88           C  
ATOM   1285  OH  TYR A 173     103.773 148.821 140.020  1.00 12.88           O  
ATOM   1286  N   SER A 174     109.148 154.191 135.526  1.00  9.92           N  
ATOM   1287  CA  SER A 174     110.366 154.929 135.193  1.00  9.92           C  
ATOM   1288  C   SER A 174     110.479 156.226 135.986  1.00  9.92           C  
ATOM   1289  O   SER A 174     111.507 156.428 136.654  1.00  9.92           O  
ATOM   1290  CB  SER A 174     110.444 155.172 133.684  1.00  9.92           C  
ATOM   1291  OG  SER A 174     111.476 156.085 133.386  1.00  9.92           O  
ATOM   1292  N   PRO A 175     109.496 157.134 135.967  1.00  9.11           N  
ATOM   1293  CA  PRO A 175     109.595 158.327 136.825  1.00  9.11           C  
ATOM   1294  C   PRO A 175     109.780 158.009 138.295  1.00  9.11           C  
ATOM   1295  O   PRO A 175     110.414 158.789 139.015  1.00  9.11           O  
ATOM   1296  CB  PRO A 175     108.262 159.049 136.581  1.00  9.11           C  
ATOM   1297  CG  PRO A 175     107.770 158.553 135.308  1.00  9.11           C  
ATOM   1298  CD  PRO A 175     108.320 157.190 135.086  1.00  9.11           C  
ATOM   1299  N   ALA A 176     109.241 156.881 138.759  1.00  9.92           N  
ATOM   1300  CA  ALA A 176     109.286 156.555 140.179  1.00  9.92           C  
ATOM   1301  C   ALA A 176     110.712 156.378 140.678  1.00  9.92           C  
ATOM   1302  O   ALA A 176     110.993 156.630 141.854  1.00  9.92           O  
ATOM   1303  CB  ALA A 176     108.479 155.286 140.448  1.00  9.92           C  
ATOM   1304  N   MET A 177     111.618 155.936 139.812  1.00 11.44           N  
ATOM   1305  CA  MET A 177     113.005 155.686 140.173  1.00 11.44           C  
ATOM   1306  C   MET A 177     113.904 156.897 139.974  1.00 11.44           C  
ATOM   1307  O   MET A 177     115.096 156.820 140.284  1.00 11.44           O  
ATOM   1308  CB  MET A 177     113.546 154.521 139.352  1.00 11.44           C  
ATOM   1309  CG  MET A 177     112.796 153.227 139.551  1.00 11.44           C  
ATOM   1310  SD  MET A 177     113.206 152.025 138.288  1.00 11.44           S  
ATOM   1311  CE  MET A 177     113.592 150.666 139.354  1.00 11.44           C  
ATOM   1312  N   THR A 178     113.369 157.999 139.466  1.00  7.49           N  
ATOM   1313  CA  THR A 178     114.131 159.213 139.231  1.00  7.49           C  
ATOM   1314  C   THR A 178     114.114 160.096 140.483  1.00  7.49           C  
ATOM   1315  O   THR A 178     113.430 159.812 141.466  1.00  7.49           O  
ATOM   1316  CB  THR A 178     113.579 159.959 138.012  1.00  7.49           C  
ATOM   1317  OG1 THR A 178     112.232 160.362 138.262  1.00  7.49           O  
ATOM   1318  CG2 THR A 178     113.638 159.083 136.745  1.00  7.49           C  
ATOM   1319  N   ASP A 179     114.885 161.185 140.435  1.00  7.36           N  
ATOM   1320  CA  ASP A 179     115.156 161.978 141.632  1.00  7.36           C  
ATOM   1321  C   ASP A 179     114.029 162.948 141.984  1.00  7.36           C  
ATOM   1322  O   ASP A 179     113.845 163.259 143.164  1.00  7.36           O  
ATOM   1323  CB  ASP A 179     116.467 162.750 141.460  1.00  7.36           C  
ATOM   1324  CG  ASP A 179     117.667 161.835 141.275  1.00  7.36           C  
ATOM   1325  OD1 ASP A 179     117.821 160.873 142.054  1.00  7.36           O  
ATOM   1326  OD2 ASP A 179     118.459 162.080 140.345  1.00  7.36           O  
ATOM   1327  N   PHE A 180     113.277 163.437 140.999  1.00  7.83           N  
ATOM   1328  CA  PHE A 180     112.215 164.409 141.235  1.00  7.83           C  
ATOM   1329  C   PHE A 180     111.112 164.225 140.196  1.00  7.83           C  
ATOM   1330  O   PHE A 180     111.399 164.033 139.013  1.00  7.83           O  
ATOM   1331  CB  PHE A 180     112.742 165.848 141.172  1.00  7.83           C  
ATOM   1332  CG  PHE A 180     113.879 166.136 142.115  1.00  7.83           C  
ATOM   1333  CD1 PHE A 180     113.658 166.311 143.469  1.00  7.83           C  
ATOM   1334  CD2 PHE A 180     115.169 166.261 141.638  1.00  7.83           C  
ATOM   1335  CE1 PHE A 180     114.704 166.586 144.323  1.00  7.83           C  
ATOM   1336  CE2 PHE A 180     116.210 166.539 142.487  1.00  7.83           C  
ATOM   1337  CZ  PHE A 180     115.979 166.702 143.826  1.00  7.83           C  
ATOM   1338  N   ILE A 181     109.856 164.283 140.646  1.00  6.23           N  
ATOM   1339  CA  ILE A 181     108.674 164.194 139.785  1.00  6.23           C  
ATOM   1340  C   ILE A 181     107.811 165.435 140.012  1.00  6.23           C  
ATOM   1341  O   ILE A 181     107.394 165.707 141.143  1.00  6.23           O  
ATOM   1342  CB  ILE A 181     107.854 162.915 140.053  1.00  6.23           C  
ATOM   1343  CG1 ILE A 181     108.715 161.655 139.965  1.00  6.23           C  
ATOM   1344  CG2 ILE A 181     106.685 162.804 139.078  1.00  6.23           C  
ATOM   1345  CD1 ILE A 181     108.007 160.399 140.449  1.00  6.23           C  
ATOM   1346  N   PHE A 182     107.528 166.171 138.936  1.00  6.80           N  
ATOM   1347  CA  PHE A 182     106.646 167.336 138.963  1.00  6.80           C  
ATOM   1348  C   PHE A 182     105.452 167.133 138.027  1.00  6.80           C  
ATOM   1349  O   PHE A 182     105.548 166.432 137.018  1.00  6.80           O  
ATOM   1350  CB  PHE A 182     107.404 168.615 138.575  1.00  6.80           C  
ATOM   1351  CG  PHE A 182     108.567 168.936 139.470  1.00  6.80           C  
ATOM   1352  CD1 PHE A 182     108.388 169.651 140.641  1.00  6.80           C  
ATOM   1353  CD2 PHE A 182     109.843 168.538 139.135  1.00  6.80           C  
ATOM   1354  CE1 PHE A 182     109.456 169.945 141.455  1.00  6.80           C  
ATOM   1355  CE2 PHE A 182     110.910 168.834 139.948  1.00  6.80           C  
ATOM   1356  CZ  PHE A 182     110.713 169.536 141.108  1.00  6.80           C  
ATOM   1357  N   MET A 183     104.325 167.779 138.356  1.00  9.69           N  
ATOM   1358  CA  MET A 183     103.039 167.548 137.701  1.00  9.69           C  
ATOM   1359  C   MET A 183     102.363 168.870 137.338  1.00  9.69           C  
ATOM   1360  O   MET A 183     102.637 169.917 137.927  1.00  9.69           O  
ATOM   1361  CB  MET A 183     102.098 166.720 138.599  1.00  9.69           C  
ATOM   1362  CG  MET A 183     102.568 165.305 138.885  1.00  9.69           C  
ATOM   1363  SD  MET A 183     101.375 164.282 139.784  1.00  9.69           S  
ATOM   1364  CE  MET A 183     100.085 164.025 138.565  1.00  9.69           C  
ATOM   1365  N   VAL A 184     101.468 168.810 136.349  1.00  9.78           N  
ATOM   1366  CA  VAL A 184     100.649 169.946 135.928  1.00  9.78           C  
ATOM   1367  C   VAL A 184      99.225 169.711 136.410  1.00  9.78           C  
ATOM   1368  O   VAL A 184      98.658 168.634 136.192  1.00  9.78           O  
ATOM   1369  CB  VAL A 184     100.683 170.145 134.402  1.00  9.78           C  
ATOM   1370  CG1 VAL A 184      99.855 171.362 133.992  1.00  9.78           C  
ATOM   1371  CG2 VAL A 184     102.112 170.286 133.915  1.00  9.78           C  
ATOM   1372  N   ARG A 185      98.647 170.721 137.052  1.00 14.15           N  
ATOM   1373  CA  ARG A 185      97.314 170.592 137.628  1.00 14.15           C  
ATOM   1374  C   ARG A 185      96.240 170.545 136.542  1.00 14.15           C  
ATOM   1375  O   ARG A 185      96.286 171.290 135.562  1.00 14.15           O  
ATOM   1376  CB  ARG A 185      97.035 171.749 138.591  1.00 14.15           C  
ATOM   1377  CG  ARG A 185      97.906 171.754 139.847  1.00 14.15           C  
ATOM   1378  CD  ARG A 185      97.373 172.680 140.927  1.00 14.15           C  
ATOM   1379  NE  ARG A 185      97.636 174.086 140.646  1.00 14.15           N  
ATOM   1380  CZ  ARG A 185      98.761 174.716 140.965  1.00 14.15           C  
ATOM   1381  NH1 ARG A 185      98.906 175.996 140.670  1.00 14.15           N  
ATOM   1382  NH2 ARG A 185      99.747 174.073 141.572  1.00 14.15           N  
ATOM   1383  N   ASP A 186      95.270 169.654 136.732  1.00 17.93           N  
ATOM   1384  CA  ASP A 186      94.036 169.476 135.975  1.00 17.93           C  
ATOM   1385  C   ASP A 186      94.229 168.782 134.622  1.00 17.93           C  
ATOM   1386  O   ASP A 186      93.231 168.439 133.990  1.00 17.93           O  
ATOM   1387  CB  ASP A 186      93.293 170.803 135.725  1.00 17.93           C  
ATOM   1388  CG  ASP A 186      93.293 171.709 136.935  1.00 17.93           C  
ATOM   1389  OD1 ASP A 186      92.775 171.291 137.990  1.00 17.93           O  
ATOM   1390  OD2 ASP A 186      93.816 172.837 136.833  1.00 17.93           O  
ATOM   1391  N   THR A 187      95.456 168.538 134.165  1.00 15.04           N  
ATOM   1392  CA  THR A 187      95.683 167.859 132.896  1.00 15.04           C  
ATOM   1393  C   THR A 187      96.529 166.596 133.001  1.00 15.04           C  
ATOM   1394  O   THR A 187      96.632 165.865 132.011  1.00 15.04           O  
ATOM   1395  CB  THR A 187      96.349 168.808 131.885  1.00 15.04           C  
ATOM   1396  OG1 THR A 187      97.423 169.515 132.512  1.00 15.04           O  
ATOM   1397  CG2 THR A 187      95.346 169.799 131.325  1.00 15.04           C  
ATOM   1398  N   SER A 188      97.134 166.316 134.153  1.00 11.82           N  
ATOM   1399  CA  SER A 188      98.040 165.188 134.317  1.00 11.82           C  
ATOM   1400  C   SER A 188      97.534 164.240 135.397  1.00 11.82           C  
ATOM   1401  O   SER A 188      96.830 164.652 136.323  1.00 11.82           O  
ATOM   1402  CB  SER A 188      99.450 165.676 134.672  1.00 11.82           C  
ATOM   1403  OG  SER A 188      99.582 165.932 136.055  1.00 11.82           O  
ATOM   1404  N   TYR A 189      97.888 162.959 135.268  1.00 13.17           N  
ATOM   1405  CA  TYR A 189      97.612 161.987 136.320  1.00 13.17           C  
ATOM   1406  C   TYR A 189      98.506 160.761 136.165  1.00 13.17           C  
ATOM   1407  O   TYR A 189      99.080 160.515 135.102  1.00 13.17           O  
ATOM   1408  CB  TYR A 189      96.136 161.574 136.338  1.00 13.17           C  
ATOM   1409  CG  TYR A 189      95.546 161.166 135.006  1.00 13.17           C  
ATOM   1410  CD1 TYR A 189      95.725 159.886 134.507  1.00 13.17           C  
ATOM   1411  CD2 TYR A 189      94.784 162.054 134.263  1.00 13.17           C  
ATOM   1412  CE1 TYR A 189      95.177 159.508 133.303  1.00 13.17           C  
ATOM   1413  CE2 TYR A 189      94.235 161.684 133.056  1.00 13.17           C  
ATOM   1414  CZ  TYR A 189      94.434 160.411 132.580  1.00 13.17           C  
ATOM   1415  OH  TYR A 189      93.883 160.040 131.379  1.00 13.17           O  
ATOM   1416  N   MET A 190      98.605 159.993 137.257  1.00 11.61           N  
ATOM   1417  CA  MET A 190      99.394 158.768 137.338  1.00 11.61           C  
ATOM   1418  C   MET A 190      98.621 157.691 138.089  1.00 11.61           C  
ATOM   1419  O   MET A 190      97.933 157.986 139.069  1.00 11.61           O  
ATOM   1420  CB  MET A 190     100.726 158.984 138.069  1.00 11.61           C  
ATOM   1421  CG  MET A 190     101.503 160.218 137.699  1.00 11.61           C  
ATOM   1422  SD  MET A 190     102.972 160.415 138.737  1.00 11.61           S  
ATOM   1423  CE  MET A 190     104.112 159.287 137.957  1.00 11.61           C  
ATOM   1424  N   PHE A 191      98.739 156.448 137.627  1.00 12.88           N  
ATOM   1425  CA  PHE A 191      98.309 155.274 138.383  1.00 12.88           C  
ATOM   1426  C   PHE A 191      98.741 154.017 137.642  1.00 12.88           C  
ATOM   1427  O   PHE A 191      98.939 154.029 136.426  1.00 12.88           O  
ATOM   1428  CB  PHE A 191      96.795 155.252 138.616  1.00 12.88           C  
ATOM   1429  CG  PHE A 191      95.993 155.719 137.447  1.00 12.88           C  
ATOM   1430  CD1 PHE A 191      95.897 154.948 136.305  1.00 12.88           C  
ATOM   1431  CD2 PHE A 191      95.324 156.926 137.489  1.00 12.88           C  
ATOM   1432  CE1 PHE A 191      95.156 155.381 135.229  1.00 12.88           C  
ATOM   1433  CE2 PHE A 191      94.582 157.357 136.415  1.00 12.88           C  
ATOM   1434  CZ  PHE A 191      94.499 156.583 135.287  1.00 12.88           C  
ATOM   1435  N   VAL A 192      98.887 152.931 138.403  1.00 14.74           N  
ATOM   1436  CA  VAL A 192      99.248 151.637 137.824  1.00 14.74           C  
ATOM   1437  C   VAL A 192      98.042 151.006 137.138  1.00 14.74           C  
ATOM   1438  O   VAL A 192      98.083 150.674 135.948  1.00 14.74           O  
ATOM   1439  CB  VAL A 192      99.826 150.700 138.905  1.00 14.74           C  
ATOM   1440  CG1 VAL A 192     100.301 149.395 138.291  1.00 14.74           C  
ATOM   1441  CG2 VAL A 192     100.956 151.370 139.675  1.00 14.74           C  
ATOM   1442  N   THR A 193      96.959 150.817 137.886  1.00 19.15           N  
ATOM   1443  CA  THR A 193      95.718 150.247 137.382  1.00 19.15           C  
ATOM   1444  C   THR A 193      94.668 151.345 137.242  1.00 19.15           C  
ATOM   1445  O   THR A 193      94.619 152.276 138.051  1.00 19.15           O  
ATOM   1446  CB  THR A 193      95.217 149.144 138.319  1.00 19.15           C  
ATOM   1447  OG1 THR A 193      96.308 148.283 138.673  1.00 19.15           O  
ATOM   1448  CG2 THR A 193      94.144 148.321 137.649  1.00 19.15           C  
ATOM   1449  N   GLY A 194      93.825 151.232 136.218  1.00 25.32           N  
ATOM   1450  CA  GLY A 194      92.936 152.306 135.839  1.00 25.32           C  
ATOM   1451  C   GLY A 194      91.526 152.193 136.390  1.00 25.32           C  
ATOM   1452  O   GLY A 194      91.159 151.213 137.043  1.00 25.32           O  
ATOM   1453  N   PRO A 195      90.701 153.214 136.125  1.00 29.18           N  
ATOM   1454  CA  PRO A 195      89.344 153.231 136.703  1.00 29.18           C  
ATOM   1455  C   PRO A 195      88.463 152.059 136.301  1.00 29.18           C  
ATOM   1456  O   PRO A 195      87.683 151.579 137.129  1.00 29.18           O  
ATOM   1457  CB  PRO A 195      88.771 154.558 136.192  1.00 29.18           C  
ATOM   1458  CG  PRO A 195      89.942 155.414 135.954  1.00 29.18           C  
ATOM   1459  CD  PRO A 195      91.072 154.520 135.556  1.00 29.18           C  
ATOM   1460  N   ASP A 196      88.529 151.603 135.049  1.00 34.64           N  
ATOM   1461  CA  ASP A 196      87.655 150.516 134.616  1.00 34.64           C  
ATOM   1462  C   ASP A 196      87.912 149.245 135.421  1.00 34.64           C  
ATOM   1463  O   ASP A 196      86.973 148.589 135.894  1.00 34.64           O  
ATOM   1464  CB  ASP A 196      87.841 150.266 133.118  1.00 34.64           C  
ATOM   1465  CG  ASP A 196      89.243 149.814 132.768  1.00 34.64           C  
ATOM   1466  OD1 ASP A 196      90.212 150.383 133.316  1.00 34.64           O  
ATOM   1467  OD2 ASP A 196      89.377 148.891 131.937  1.00 34.64           O  
ATOM   1468  N   VAL A 197      89.184 148.892 135.604  1.00 33.70           N  
ATOM   1469  CA  VAL A 197      89.525 147.705 136.382  1.00 33.70           C  
ATOM   1470  C   VAL A 197      89.184 147.914 137.851  1.00 33.70           C  
ATOM   1471  O   VAL A 197      88.756 146.981 138.542  1.00 33.70           O  
ATOM   1472  CB  VAL A 197      91.012 147.356 136.185  1.00 33.70           C  
ATOM   1473  CG1 VAL A 197      91.427 146.217 137.098  1.00 33.70           C  
ATOM   1474  CG2 VAL A 197      91.285 146.998 134.740  1.00 33.70           C  
ATOM   1475  N   VAL A 198      89.376 149.133 138.356  1.00 32.37           N  
ATOM   1476  CA  VAL A 198      89.024 149.427 139.741  1.00 32.37           C  
ATOM   1477  C   VAL A 198      87.533 149.215 139.961  1.00 32.37           C  
ATOM   1478  O   VAL A 198      87.110 148.679 140.989  1.00 32.37           O  
ATOM   1479  CB  VAL A 198      89.456 150.859 140.106  1.00 32.37           C  
ATOM   1480  CG1 VAL A 198      88.827 151.292 141.414  1.00 32.37           C  
ATOM   1481  CG2 VAL A 198      90.969 150.960 140.184  1.00 32.37           C  
ATOM   1482  N   LYS A 199      86.714 149.622 138.993  1.00 36.80           N  
ATOM   1483  CA  LYS A 199      85.278 149.387 139.083  1.00 36.80           C  
ATOM   1484  C   LYS A 199      84.974 147.898 139.047  1.00 36.80           C  
ATOM   1485  O   LYS A 199      84.232 147.379 139.889  1.00 36.80           O  
ATOM   1486  CB  LYS A 199      84.566 150.112 137.940  1.00 36.80           C  
ATOM   1487  CG  LYS A 199      83.096 149.767 137.761  1.00 36.80           C  
ATOM   1488  CD  LYS A 199      82.303 149.939 139.042  1.00 36.80           C  
ATOM   1489  CE  LYS A 199      80.833 149.593 138.845  1.00 36.80           C  
ATOM   1490  NZ  LYS A 199      80.253 150.210 137.622  1.00 36.80           N  
ATOM   1491  N   THR A 200      85.548 147.191 138.074  1.00 38.63           N  
ATOM   1492  CA  THR A 200      85.265 145.768 137.929  1.00 38.63           C  
ATOM   1493  C   THR A 200      85.620 144.986 139.191  1.00 38.63           C  
ATOM   1494  O   THR A 200      84.874 144.089 139.599  1.00 38.63           O  
ATOM   1495  CB  THR A 200      86.021 145.209 136.726  1.00 38.63           C  
ATOM   1496  OG1 THR A 200      85.476 145.755 135.520  1.00 38.63           O  
ATOM   1497  CG2 THR A 200      85.913 143.703 136.686  1.00 38.63           C  
ATOM   1498  N   VAL A 201      86.747 145.306 139.823  1.00 37.71           N  
ATOM   1499  CA  VAL A 201      87.260 144.471 140.909  1.00 37.71           C  
ATOM   1500  C   VAL A 201      86.790 144.955 142.277  1.00 37.71           C  
ATOM   1501  O   VAL A 201      86.526 144.142 143.165  1.00 37.71           O  
ATOM   1502  CB  VAL A 201      88.800 144.404 140.837  1.00 37.71           C  
ATOM   1503  CG1 VAL A 201      89.363 143.656 142.034  1.00 37.71           C  
ATOM   1504  CG2 VAL A 201      89.240 143.735 139.549  1.00 37.71           C  
ATOM   1505  N   THR A 202      86.679 146.267 142.483  1.00 38.55           N  
ATOM   1506  CA  THR A 202      86.325 146.822 143.781  1.00 38.55           C  
ATOM   1507  C   THR A 202      84.929 147.429 143.833  1.00 38.55           C  
ATOM   1508  O   THR A 202      84.473 147.786 144.924  1.00 38.55           O  
ATOM   1509  CB  THR A 202      87.339 147.901 144.192  1.00 38.55           C  
ATOM   1510  OG1 THR A 202      87.418 148.902 143.173  1.00 38.55           O  
ATOM   1511  CG2 THR A 202      88.716 147.299 144.404  1.00 38.55           C  
ATOM   1512  N   ASN A 203      84.246 147.560 142.699  1.00 41.07           N  
ATOM   1513  CA  ASN A 203      82.937 148.200 142.599  1.00 41.07           C  
ATOM   1514  C   ASN A 203      82.974 149.679 142.966  1.00 41.07           C  
ATOM   1515  O   ASN A 203      81.916 150.300 143.119  1.00 41.07           O  
ATOM   1516  CB  ASN A 203      81.898 147.484 143.468  1.00 41.07           C  
ATOM   1517  CG  ASN A 203      81.768 146.017 143.130  1.00 41.07           C  
ATOM   1518  OD1 ASN A 203      81.679 145.640 141.961  1.00 41.07           O  
ATOM   1519  ND2 ASN A 203      81.761 145.177 144.155  1.00 41.07           N  
ATOM   1520  N   GLU A 204      84.160 150.262 143.109  1.00 36.21           N  
ATOM   1521  CA  GLU A 204      84.300 151.665 143.469  1.00 36.21           C  
ATOM   1522  C   GLU A 204      84.339 152.511 142.203  1.00 36.21           C  
ATOM   1523  O   GLU A 204      85.078 152.202 141.263  1.00 36.21           O  
ATOM   1524  CB  GLU A 204      85.563 151.878 144.304  1.00 36.21           C  
ATOM   1525  CG  GLU A 204      85.849 153.324 144.666  1.00 36.21           C  
ATOM   1526  CD  GLU A 204      87.068 153.470 145.557  1.00 36.21           C  
ATOM   1527  OE1 GLU A 204      87.174 154.497 146.259  1.00 36.21           O  
ATOM   1528  OE2 GLU A 204      87.919 152.554 145.557  1.00 36.21           O  
ATOM   1529  N   VAL A 205      83.537 153.571 142.181  1.00 32.95           N  
ATOM   1530  CA  VAL A 205      83.423 154.460 141.030  1.00 32.95           C  
ATOM   1531  C   VAL A 205      84.319 155.667 141.269  1.00 32.95           C  
ATOM   1532  O   VAL A 205      84.137 156.401 142.248  1.00 32.95           O  
ATOM   1533  CB  VAL A 205      81.965 154.888 140.798  1.00 32.95           C  
ATOM   1534  CG1 VAL A 205      81.877 155.935 139.705  1.00 32.95           C  
ATOM   1535  CG2 VAL A 205      81.110 153.690 140.444  1.00 32.95           C  
ATOM   1536  N   VAL A 206      85.285 155.879 140.376  1.00 26.15           N  
ATOM   1537  CA  VAL A 206      86.224 156.988 140.488  1.00 26.15           C  
ATOM   1538  C   VAL A 206      86.597 157.509 139.109  1.00 26.15           C  
ATOM   1539  O   VAL A 206      86.597 156.774 138.118  1.00 26.15           O  
ATOM   1540  CB  VAL A 206      87.506 156.593 141.256  1.00 26.15           C  
ATOM   1541  CG1 VAL A 206      87.199 156.325 142.705  1.00 26.15           C  
ATOM   1542  CG2 VAL A 206      88.152 155.374 140.618  1.00 26.15           C  
ATOM   1543  N   THR A 207      86.920 158.796 139.064  1.00 19.92           N  
ATOM   1544  CA  THR A 207      87.488 159.442 137.894  1.00 19.92           C  
ATOM   1545  C   THR A 207      89.013 159.383 137.945  1.00 19.92           C  
ATOM   1546  O   THR A 207      89.615 159.110 138.984  1.00 19.92           O  
ATOM   1547  CB  THR A 207      87.042 160.902 137.805  1.00 19.92           C  
ATOM   1548  OG1 THR A 207      87.520 161.622 138.948  1.00 19.92           O  
ATOM   1549  CG2 THR A 207      85.529 161.007 137.730  1.00 19.92           C  
ATOM   1550  N   ALA A 208      89.632 159.657 136.796  1.00 17.34           N  
ATOM   1551  CA  ALA A 208      91.090 159.698 136.724  1.00 17.34           C  
ATOM   1552  C   ALA A 208      91.667 160.723 137.694  1.00 17.34           C  
ATOM   1553  O   ALA A 208      92.690 160.469 138.337  1.00 17.34           O  
ATOM   1554  CB  ALA A 208      91.533 160.004 135.295  1.00 17.34           C  
ATOM   1555  N   GLU A 209      91.031 161.889 137.805  1.00 18.58           N  
ATOM   1556  CA  GLU A 209      91.514 162.926 138.714  1.00 18.58           C  
ATOM   1557  C   GLU A 209      91.424 162.466 140.163  1.00 18.58           C  
ATOM   1558  O   GLU A 209      92.366 162.644 140.944  1.00 18.58           O  
ATOM   1559  CB  GLU A 209      90.718 164.216 138.497  1.00 18.58           C  
ATOM   1560  CG  GLU A 209      91.119 165.392 139.383  1.00 18.58           C  
ATOM   1561  CD  GLU A 209      92.465 165.984 139.012  1.00 18.58           C  
ATOM   1562  OE1 GLU A 209      92.861 165.875 137.834  1.00 18.58           O  
ATOM   1563  OE2 GLU A 209      93.127 166.562 139.900  1.00 18.58           O  
ATOM   1564  N   GLU A 210      90.295 161.860 140.537  1.00 19.20           N  
ATOM   1565  CA  GLU A 210      90.125 161.372 141.902  1.00 19.20           C  
ATOM   1566  C   GLU A 210      91.095 160.243 142.224  1.00 19.20           C  
ATOM   1567  O   GLU A 210      91.488 160.074 143.383  1.00 19.20           O  
ATOM   1568  CB  GLU A 210      88.687 160.901 142.112  1.00 19.20           C  
ATOM   1569  CG  GLU A 210      87.662 162.014 142.150  1.00 19.20           C  
ATOM   1570  CD  GLU A 210      86.269 161.527 141.808  1.00 19.20           C  
ATOM   1571  OE1 GLU A 210      85.833 161.727 140.656  1.00 19.20           O  
ATOM   1572  OE2 GLU A 210      85.613 160.933 142.688  1.00 19.20           O  
ATOM   1573  N   LEU A 211      91.483 159.458 141.220  1.00 13.72           N  
ATOM   1574  CA  LEU A 211      92.354 158.311 141.446  1.00 13.72           C  
ATOM   1575  C   LEU A 211      93.826 158.716 141.494  1.00 13.72           C  
ATOM   1576  O   LEU A 211      94.563 158.280 142.383  1.00 13.72           O  
ATOM   1577  CB  LEU A 211      92.106 157.264 140.356  1.00 13.72           C  
ATOM   1578  CG  LEU A 211      92.963 155.999 140.321  1.00 13.72           C  
ATOM   1579  CD1 LEU A 211      92.779 155.204 141.588  1.00 13.72           C  
ATOM   1580  CD2 LEU A 211      92.647 155.141 139.099  1.00 13.72           C  
ATOM   1581  N   GLY A 212      94.272 159.543 140.549  1.00  9.84           N  
ATOM   1582  CA  GLY A 212      95.685 159.828 140.386  1.00  9.84           C  
ATOM   1583  C   GLY A 212      96.073 161.246 140.008  1.00  9.84           C  
ATOM   1584  O   GLY A 212      97.121 161.447 139.392  1.00  9.84           O  
ATOM   1585  N   GLY A 213      95.259 162.234 140.357  1.00 10.19           N  
ATOM   1586  CA  GLY A 213      95.528 163.605 139.974  1.00 10.19           C  
ATOM   1587  C   GLY A 213      96.622 164.254 140.810  1.00 10.19           C  
ATOM   1588  O   GLY A 213      97.187 163.668 141.733  1.00 10.19           O  
ATOM   1589  N   ALA A 214      96.925 165.509 140.461  1.00 11.28           N  
ATOM   1590  CA  ALA A 214      98.042 166.212 141.088  1.00 11.28           C  
ATOM   1591  C   ALA A 214      97.857 166.347 142.597  1.00 11.28           C  
ATOM   1592  O   ALA A 214      98.806 166.145 143.362  1.00 11.28           O  
ATOM   1593  CB  ALA A 214      98.226 167.587 140.448  1.00 11.28           C  
ATOM   1594  N   LYS A 215      96.652 166.706 143.047  1.00 12.44           N  
ATOM   1595  CA  LYS A 215      96.427 166.896 144.478  1.00 12.44           C  
ATOM   1596  C   LYS A 215      96.752 165.625 145.255  1.00 12.44           C  
ATOM   1597  O   LYS A 215      97.433 165.669 146.289  1.00 12.44           O  
ATOM   1598  CB  LYS A 215      94.983 167.332 144.734  1.00 12.44           C  
ATOM   1599  CG  LYS A 215      94.700 167.754 146.167  1.00 12.44           C  
ATOM   1600  CD  LYS A 215      93.331 168.385 146.313  1.00 12.44           C  
ATOM   1601  CE  LYS A 215      93.206 169.147 147.619  1.00 12.44           C  
ATOM   1602  NZ  LYS A 215      94.030 170.390 147.624  1.00 12.44           N  
ATOM   1603  N   VAL A 216      96.280 164.479 144.758  1.00  9.27           N  
ATOM   1604  CA  VAL A 216      96.541 163.199 145.412  1.00  9.27           C  
ATOM   1605  C   VAL A 216      98.039 162.974 145.568  1.00  9.27           C  
ATOM   1606  O   VAL A 216      98.518 162.583 146.638  1.00  9.27           O  
ATOM   1607  CB  VAL A 216      95.883 162.051 144.620  1.00  9.27           C  
ATOM   1608  CG1 VAL A 216      96.345 160.699 145.121  1.00  9.27           C  
ATOM   1609  CG2 VAL A 216      94.374 162.142 144.696  1.00  9.27           C  
ATOM   1610  N   HIS A 217      98.799 163.197 144.499  1.00  8.48           N  
ATOM   1611  CA  HIS A 217     100.213 162.850 144.482  1.00  8.48           C  
ATOM   1612  C   HIS A 217     101.105 163.906 145.119  1.00  8.48           C  
ATOM   1613  O   HIS A 217     102.280 163.623 145.373  1.00  8.48           O  
ATOM   1614  CB  HIS A 217     100.656 162.580 143.044  1.00  8.48           C  
ATOM   1615  CG  HIS A 217     100.102 161.310 142.486  1.00  8.48           C  
ATOM   1616  ND1 HIS A 217     100.164 160.113 143.163  1.00  8.48           N  
ATOM   1617  CD2 HIS A 217      99.459 161.053 141.325  1.00  8.48           C  
ATOM   1618  CE1 HIS A 217      99.590 159.172 142.439  1.00  8.48           C  
ATOM   1619  NE2 HIS A 217      99.154 159.716 141.318  1.00  8.48           N  
ATOM   1620  N   THR A 218     100.578 165.093 145.402  1.00  8.73           N  
ATOM   1621  CA  THR A 218     101.342 166.131 146.077  1.00  8.73           C  
ATOM   1622  C   THR A 218     101.004 166.268 147.553  1.00  8.73           C  
ATOM   1623  O   THR A 218     101.806 166.836 148.300  1.00  8.73           O  
ATOM   1624  CB  THR A 218     101.121 167.488 145.400  1.00  8.73           C  
ATOM   1625  OG1 THR A 218      99.718 167.720 145.242  1.00  8.73           O  
ATOM   1626  CG2 THR A 218     101.819 167.543 144.046  1.00  8.73           C  
ATOM   1627  N   SER A 219      99.847 165.769 147.993  1.00 10.23           N  
ATOM   1628  CA  SER A 219      99.424 165.938 149.374  1.00 10.23           C  
ATOM   1629  C   SER A 219      99.178 164.645 150.139  1.00 10.23           C  
ATOM   1630  O   SER A 219      99.149 164.688 151.373  1.00 10.23           O  
ATOM   1631  CB  SER A 219      98.144 166.782 149.434  1.00 10.23           C  
ATOM   1632  OG  SER A 219      97.036 166.048 148.959  1.00 10.23           O  
ATOM   1633  N   LYS A 220      98.999 163.517 149.470  1.00 11.19           N  
ATOM   1634  CA  LYS A 220      98.561 162.298 150.147  1.00 11.19           C  
ATOM   1635  C   LYS A 220      99.480 161.099 149.947  1.00 11.19           C  
ATOM   1636  O   LYS A 220      99.727 160.365 150.904  1.00 11.19           O  
ATOM   1637  CB  LYS A 220      97.138 161.953 149.674  1.00 11.19           C  
ATOM   1638  CG  LYS A 220      96.463 160.821 150.427  1.00 11.19           C  
ATOM   1639  CD  LYS A 220      95.029 160.534 149.945  1.00 11.19           C  
ATOM   1640  CE  LYS A 220      94.214 161.789 149.654  1.00 11.19           C  
ATOM   1641  NZ  LYS A 220      92.891 161.458 149.060  1.00 11.19           N  
ATOM   1642  N   SER A 221      99.987 160.876 148.735  1.00  8.85           N  
ATOM   1643  CA  SER A 221     100.637 159.613 148.404  1.00  8.85           C  
ATOM   1644  C   SER A 221     102.157 159.632 148.521  1.00  8.85           C  
ATOM   1645  O   SER A 221     102.759 158.555 148.581  1.00  8.85           O  
ATOM   1646  CB  SER A 221     100.254 159.177 146.986  1.00  8.85           C  
ATOM   1647  OG  SER A 221     100.596 160.157 146.036  1.00  8.85           O  
ATOM   1648  N   SER A 222     102.787 160.805 148.569  1.00  8.67           N  
ATOM   1649  CA  SER A 222     104.242 160.986 148.665  1.00  8.67           C  
ATOM   1650  C   SER A 222     104.969 160.877 147.328  1.00  8.67           C  
ATOM   1651  O   SER A 222     106.206 160.877 147.314  1.00  8.67           O  
ATOM   1652  CB  SER A 222     104.870 159.976 149.632  1.00  8.67           C  
ATOM   1653  OG  SER A 222     104.782 158.655 149.135  1.00  8.67           O  
ATOM   1654  N   ILE A 223     104.253 160.791 146.208  1.00  7.99           N  
ATOM   1655  CA  ILE A 223     104.888 160.499 144.924  1.00  7.99           C  
ATOM   1656  C   ILE A 223     105.520 161.751 144.312  1.00  7.99           C  
ATOM   1657  O   ILE A 223     106.666 161.715 143.853  1.00  7.99           O  
ATOM   1658  CB  ILE A 223     103.865 159.846 143.972  1.00  7.99           C  
ATOM   1659  CG1 ILE A 223     103.325 158.531 144.561  1.00  7.99           C  
ATOM   1660  CG2 ILE A 223     104.473 159.585 142.611  1.00  7.99           C  
ATOM   1661  CD1 ILE A 223     104.368 157.485 144.916  1.00  7.99           C  
ATOM   1662  N   ALA A 224     104.800 162.871 144.293  1.00  7.86           N  
ATOM   1663  CA  ALA A 224     105.214 164.058 143.549  1.00  7.86           C  
ATOM   1664  C   ALA A 224     105.911 165.075 144.447  1.00  7.86           C  
ATOM   1665  O   ALA A 224     105.549 165.240 145.614  1.00  7.86           O  
ATOM   1666  CB  ALA A 224     104.015 164.711 142.863  1.00  7.86           C  
ATOM   1667  N   ASP A 225     106.921 165.750 143.888  1.00  8.85           N  
ATOM   1668  CA  ASP A 225     107.685 166.779 144.582  1.00  8.85           C  
ATOM   1669  C   ASP A 225     107.161 168.191 144.346  1.00  8.85           C  
ATOM   1670  O   ASP A 225     107.657 169.129 144.977  1.00  8.85           O  
ATOM   1671  CB  ASP A 225     109.159 166.714 144.163  1.00  8.85           C  
ATOM   1672  CG  ASP A 225     109.804 165.375 144.491  1.00  8.85           C  
ATOM   1673  OD1 ASP A 225     109.638 164.416 143.707  1.00  8.85           O  
ATOM   1674  OD2 ASP A 225     110.475 165.276 145.540  1.00  8.85           O  
ATOM   1675  N   GLY A 226     106.184 168.367 143.468  1.00  8.68           N  
ATOM   1676  CA  GLY A 226     105.623 169.683 143.229  1.00  8.68           C  
ATOM   1677  C   GLY A 226     104.625 169.648 142.089  1.00  8.68           C  
ATOM   1678  O   GLY A 226     104.583 168.700 141.299  1.00  8.68           O  
ATOM   1679  N   SER A 227     103.817 170.707 142.025  1.00 10.98           N  
ATOM   1680  CA  SER A 227     102.854 170.900 140.946  1.00 10.98           C  
ATOM   1681  C   SER A 227     102.819 172.367 140.531  1.00 10.98           C  
ATOM   1682  O   SER A 227     103.258 173.253 141.266  1.00 10.98           O  
ATOM   1683  CB  SER A 227     101.444 170.445 141.340  1.00 10.98           C  
ATOM   1684  OG  SER A 227     100.974 171.132 142.478  1.00 10.98           O  
ATOM   1685  N   PHE A 228     102.256 172.610 139.347  1.00 11.53           N  
ATOM   1686  CA  PHE A 228     102.260 173.925 138.721  1.00 11.53           C  
ATOM   1687  C   PHE A 228     100.957 174.142 137.956  1.00 11.53           C  
ATOM   1688  O   PHE A 228     100.248 173.196 137.612  1.00 11.53           O  
ATOM   1689  CB  PHE A 228     103.456 174.089 137.777  1.00 11.53           C  
ATOM   1690  CG  PHE A 228     104.787 173.897 138.435  1.00 11.53           C  
ATOM   1691  CD1 PHE A 228     105.290 174.832 139.318  1.00 11.53           C  
ATOM   1692  CD2 PHE A 228     105.543 172.779 138.158  1.00 11.53           C  
ATOM   1693  CE1 PHE A 228     106.515 174.643 139.915  1.00 11.53           C  
ATOM   1694  CE2 PHE A 228     106.765 172.591 138.750  1.00 11.53           C  
ATOM   1695  CZ  PHE A 228     107.251 173.523 139.625  1.00 11.53           C  
ATOM   1696  N   GLU A 229     100.658 175.415 137.686  1.00 18.31           N  
ATOM   1697  CA  GLU A 229      99.368 175.786 137.105  1.00 18.31           C  
ATOM   1698  C   GLU A 229      99.239 175.349 135.646  1.00 18.31           C  
ATOM   1699  O   GLU A 229      98.157 174.931 135.221  1.00 18.31           O  
ATOM   1700  CB  GLU A 229      99.160 177.296 137.231  1.00 18.31           C  
ATOM   1701  CG  GLU A 229      97.762 177.790 136.883  1.00 18.31           C  
ATOM   1702  CD  GLU A 229      96.754 177.544 137.989  1.00 18.31           C  
ATOM   1703  OE1 GLU A 229      97.087 176.840 138.965  1.00 18.31           O  
ATOM   1704  OE2 GLU A 229      95.622 178.062 137.884  1.00 18.31           O  
ATOM   1705  N   ASN A 230     100.309 175.452 134.858  1.00 14.95           N  
ATOM   1706  CA  ASN A 230     100.240 175.093 133.444  1.00 14.95           C  
ATOM   1707  C   ASN A 230     101.626 174.707 132.935  1.00 14.95           C  
ATOM   1708  O   ASN A 230     102.629 174.821 133.641  1.00 14.95           O  
ATOM   1709  CB  ASN A 230      99.642 176.228 132.598  1.00 14.95           C  
ATOM   1710  CG  ASN A 230     100.334 177.556 132.814  1.00 14.95           C  
ATOM   1711  OD1 ASN A 230     101.514 177.714 132.515  1.00 14.95           O  
ATOM   1712  ND2 ASN A 230      99.591 178.525 133.319  1.00 14.95           N  
ATOM   1713  N   ASP A 231     101.655 174.238 131.684  1.00 13.48           N  
ATOM   1714  CA  ASP A 231     102.882 173.716 131.084  1.00 13.48           C  
ATOM   1715  C   ASP A 231     104.015 174.744 131.111  1.00 13.48           C  
ATOM   1716  O   ASP A 231     105.163 174.411 131.440  1.00 13.48           O  
ATOM   1717  CB  ASP A 231     102.594 173.267 129.645  1.00 13.48           C  
ATOM   1718  CG  ASP A 231     101.689 172.040 129.574  1.00 13.48           C  
ATOM   1719  OD1 ASP A 231     101.088 171.673 130.601  1.00 13.48           O  
ATOM   1720  OD2 ASP A 231     101.584 171.435 128.488  1.00 13.48           O  
ATOM   1721  N   VAL A 232     103.708 176.000 130.783  1.00 12.43           N  
ATOM   1722  CA  VAL A 232     104.740 177.026 130.627  1.00 12.43           C  
ATOM   1723  C   VAL A 232     105.434 177.302 131.961  1.00 12.43           C  
ATOM   1724  O   VAL A 232     106.672 177.278 132.057  1.00 12.43           O  
ATOM   1725  CB  VAL A 232     104.119 178.302 130.020  1.00 12.43           C  
ATOM   1726  CG1 VAL A 232     105.100 179.459 130.012  1.00 12.43           C  
ATOM   1727  CG2 VAL A 232     103.619 178.036 128.605  1.00 12.43           C  
ATOM   1728  N   GLU A 233     104.644 177.605 133.000  1.00 14.90           N  
ATOM   1729  CA  GLU A 233     105.185 177.776 134.348  1.00 14.90           C  
ATOM   1730  C   GLU A 233     106.062 176.595 134.740  1.00 14.90           C  
ATOM   1731  O   GLU A 233     107.156 176.773 135.293  1.00 14.90           O  
ATOM   1732  CB  GLU A 233     104.039 177.948 135.355  1.00 14.90           C  
ATOM   1733  CG  GLU A 233     104.461 177.920 136.826  1.00 14.90           C  
ATOM   1734  CD  GLU A 233     103.305 178.170 137.779  1.00 14.90           C  
ATOM   1735  OE1 GLU A 233     102.790 179.306 137.813  1.00 14.90           O  
ATOM   1736  OE2 GLU A 233     102.914 177.227 138.497  1.00 14.90           O  
ATOM   1737  N   ALA A 234     105.591 175.380 134.458  1.00  9.99           N  
ATOM   1738  CA  ALA A 234     106.326 174.174 134.825  1.00  9.99           C  
ATOM   1739  C   ALA A 234     107.712 174.157 134.193  1.00  9.99           C  
ATOM   1740  O   ALA A 234     108.720 173.949 134.879  1.00  9.99           O  
ATOM   1741  CB  ALA A 234     105.532 172.934 134.411  1.00  9.99           C  
ATOM   1742  N   ILE A 235     107.781 174.369 132.878  1.00  9.40           N  
ATOM   1743  CA  ILE A 235     109.059 174.248 132.183  1.00  9.40           C  
ATOM   1744  C   ILE A 235     110.025 175.341 132.641  1.00  9.40           C  
ATOM   1745  O   ILE A 235     111.234 175.102 132.806  1.00  9.40           O  
ATOM   1746  CB  ILE A 235     108.826 174.267 130.661  1.00  9.40           C  
ATOM   1747  CG1 ILE A 235     108.171 172.955 130.218  1.00  9.40           C  
ATOM   1748  CG2 ILE A 235     110.121 174.492 129.912  1.00  9.40           C  
ATOM   1749  CD1 ILE A 235     107.361 173.070 128.961  1.00  9.40           C  
ATOM   1750  N   LEU A 236     109.511 176.550 132.874  1.00  9.75           N  
ATOM   1751  CA  LEU A 236     110.383 177.622 133.351  1.00  9.75           C  
ATOM   1752  C   LEU A 236     110.923 177.310 134.750  1.00  9.75           C  
ATOM   1753  O   LEU A 236     112.100 177.575 135.050  1.00  9.75           O  
ATOM   1754  CB  LEU A 236     109.625 178.951 133.302  1.00  9.75           C  
ATOM   1755  CG  LEU A 236     109.366 179.505 131.888  1.00  9.75           C  
ATOM   1756  CD1 LEU A 236     108.532 180.773 131.932  1.00  9.75           C  
ATOM   1757  CD2 LEU A 236     110.650 179.773 131.101  1.00  9.75           C  
ATOM   1758  N   GLN A 237     110.105 176.688 135.605  1.00  8.54           N  
ATOM   1759  CA  GLN A 237     110.615 176.293 136.915  1.00  8.54           C  
ATOM   1760  C   GLN A 237     111.626 175.156 136.808  1.00  8.54           C  
ATOM   1761  O   GLN A 237     112.513 175.040 137.660  1.00  8.54           O  
ATOM   1762  CB  GLN A 237     109.469 175.901 137.846  1.00  8.54           C  
ATOM   1763  CG  GLN A 237     108.675 177.084 138.367  1.00  8.54           C  
ATOM   1764  CD  GLN A 237     109.448 177.901 139.381  1.00  8.54           C  
ATOM   1765  OE1 GLN A 237     109.805 177.411 140.448  1.00  8.54           O  
ATOM   1766  NE2 GLN A 237     109.715 179.151 139.048  1.00  8.54           N  
ATOM   1767  N   ILE A 238     111.514 174.312 135.781  1.00  6.13           N  
ATOM   1768  CA  ILE A 238     112.543 173.295 135.557  1.00  6.13           C  
ATOM   1769  C   ILE A 238     113.878 173.953 135.221  1.00  6.13           C  
ATOM   1770  O   ILE A 238     114.934 173.541 135.721  1.00  6.13           O  
ATOM   1771  CB  ILE A 238     112.113 172.299 134.460  1.00  6.13           C  
ATOM   1772  CG1 ILE A 238     110.816 171.579 134.834  1.00  6.13           C  
ATOM   1773  CG2 ILE A 238     113.212 171.284 134.197  1.00  6.13           C  
ATOM   1774  CD1 ILE A 238     110.838 170.861 136.156  1.00  6.13           C  
ATOM   1775  N   ARG A 239     113.859 174.977 134.363  1.00  6.97           N  
ATOM   1776  CA  ARG A 239     115.089 175.732 134.108  1.00  6.97           C  
ATOM   1777  C   ARG A 239     115.673 176.257 135.423  1.00  6.97           C  
ATOM   1778  O   ARG A 239     116.878 176.106 135.704  1.00  6.97           O  
ATOM   1779  CB  ARG A 239     114.827 176.888 133.130  1.00  6.97           C  
ATOM   1780  CG  ARG A 239     114.418 176.474 131.709  1.00  6.97           C  
ATOM   1781  CD  ARG A 239     114.291 177.661 130.747  1.00  6.97           C  
ATOM   1782  NE  ARG A 239     115.527 178.416 130.584  1.00  6.97           N  
ATOM   1783  CZ  ARG A 239     116.454 178.174 129.661  1.00  6.97           C  
ATOM   1784  NH1 ARG A 239     116.317 177.184 128.791  1.00  6.97           N  
ATOM   1785  NH2 ARG A 239     117.533 178.936 129.611  1.00  6.97           N  
ATOM   1786  N   ARG A 240     114.815 176.861 136.252  1.00  6.99           N  
ATOM   1787  CA  ARG A 240     115.255 177.367 137.551  1.00  6.99           C  
ATOM   1788  C   ARG A 240     115.941 176.276 138.370  1.00  6.99           C  
ATOM   1789  O   ARG A 240     117.066 176.456 138.846  1.00  6.99           O  
ATOM   1790  CB  ARG A 240     114.064 177.948 138.315  1.00  6.99           C  
ATOM   1791  CG  ARG A 240     114.416 178.716 139.585  1.00  6.99           C  
ATOM   1792  CD  ARG A 240     113.160 179.130 140.329  1.00  6.99           C  
ATOM   1793  NE  ARG A 240     113.433 179.686 141.651  1.00  6.99           N  
ATOM   1794  CZ  ARG A 240     112.602 179.613 142.685  1.00  6.99           C  
ATOM   1795  NH1 ARG A 240     111.436 179.003 142.573  1.00  6.99           N  
ATOM   1796  NH2 ARG A 240     112.941 180.154 143.842  1.00  6.99           N  
ATOM   1797  N   LEU A 241     115.276 175.132 138.540  1.00  5.35           N  
ATOM   1798  CA  LEU A 241     115.850 174.056 139.343  1.00  5.35           C  
ATOM   1799  C   LEU A 241     117.201 173.621 138.795  1.00  5.35           C  
ATOM   1800  O   LEU A 241     118.151 173.412 139.561  1.00  5.35           O  
ATOM   1801  CB  LEU A 241     114.897 172.861 139.408  1.00  5.35           C  
ATOM   1802  CG  LEU A 241     115.342 171.637 140.223  1.00  5.35           C  
ATOM   1803  CD1 LEU A 241     115.763 172.005 141.637  1.00  5.35           C  
ATOM   1804  CD2 LEU A 241     114.249 170.578 140.251  1.00  5.35           C  
ATOM   1805  N   LEU A 242     117.312 173.483 137.471  1.00  7.35           N  
ATOM   1806  CA  LEU A 242     118.573 173.035 136.890  1.00  7.35           C  
ATOM   1807  C   LEU A 242     119.703 174.003 137.216  1.00  7.35           C  
ATOM   1808  O   LEU A 242     120.857 173.582 137.348  1.00  7.35           O  
ATOM   1809  CB  LEU A 242     118.437 172.856 135.376  1.00  7.35           C  
ATOM   1810  CG  LEU A 242     117.772 171.570 134.867  1.00  7.35           C  
ATOM   1811  CD1 LEU A 242     117.305 171.736 133.420  1.00  7.35           C  
ATOM   1812  CD2 LEU A 242     118.702 170.374 135.004  1.00  7.35           C  
ATOM   1813  N   ASP A 243     119.397 175.295 137.368  1.00  9.76           N  
ATOM   1814  CA  ASP A 243     120.457 176.228 137.762  1.00  9.76           C  
ATOM   1815  C   ASP A 243     121.009 175.960 139.168  1.00  9.76           C  
ATOM   1816  O   ASP A 243     122.096 176.446 139.489  1.00  9.76           O  
ATOM   1817  CB  ASP A 243     119.978 177.678 137.681  1.00  9.76           C  
ATOM   1818  CG  ASP A 243     119.931 178.203 136.261  1.00  9.76           C  
ATOM   1819  OD1 ASP A 243     120.525 177.571 135.363  1.00  9.76           O  
ATOM   1820  OD2 ASP A 243     119.305 179.263 136.044  1.00  9.76           O  
ATOM   1821  N   PHE A 244     120.299 175.211 140.015  1.00  6.01           N  
ATOM   1822  CA  PHE A 244     120.813 174.879 141.342  1.00  6.01           C  
ATOM   1823  C   PHE A 244     121.704 173.640 141.353  1.00  6.01           C  
ATOM   1824  O   PHE A 244     122.623 173.562 142.174  1.00  6.01           O  
ATOM   1825  CB  PHE A 244     119.665 174.641 142.334  1.00  6.01           C  
ATOM   1826  CG  PHE A 244     119.028 175.892 142.865  1.00  6.01           C  
ATOM   1827  CD1 PHE A 244     119.542 176.533 143.979  1.00  6.01           C  
ATOM   1828  CD2 PHE A 244     117.895 176.414 142.273  1.00  6.01           C  
ATOM   1829  CE1 PHE A 244     118.953 177.667 144.471  1.00  6.01           C  
ATOM   1830  CE2 PHE A 244     117.307 177.551 142.766  1.00  6.01           C  
ATOM   1831  CZ  PHE A 244     117.836 178.177 143.866  1.00  6.01           C  
ATOM   1832  N   LEU A 245     121.450 172.640 140.449  1.00  5.49           N  
ATOM   1833  CA  LEU A 245     121.956 171.287 140.648  1.00  5.49           C  
ATOM   1834  C   LEU A 245     123.335 171.078 140.022  1.00  5.49           C  
ATOM   1835  O   LEU A 245     123.648 171.664 138.982  1.00  5.49           O  
ATOM   1836  CB  LEU A 245     120.989 170.267 140.056  1.00  5.49           C  
ATOM   1837  CG  LEU A 245     119.625 170.127 140.736  1.00  5.49           C  
ATOM   1838  CD1 LEU A 245     118.712 169.253 139.905  1.00  5.49           C  
ATOM   1839  CD2 LEU A 245     119.774 169.588 142.143  1.00  5.49           C  
ATOM   1840  N   PRO A 246     124.166 170.230 140.640  1.00  5.85           N  
ATOM   1841  CA  PRO A 246     125.382 169.763 139.965  1.00  5.85           C  
ATOM   1842  C   PRO A 246     125.061 168.956 138.714  1.00  5.85           C  
ATOM   1843  O   PRO A 246     124.028 168.293 138.622  1.00  5.85           O  
ATOM   1844  CB  PRO A 246     126.071 168.888 141.020  1.00  5.85           C  
ATOM   1845  CG  PRO A 246     125.401 169.149 142.295  1.00  5.85           C  
ATOM   1846  CD  PRO A 246     124.066 169.724 142.021  1.00  5.85           C  
ATOM   1847  N   ALA A 247     125.977 169.018 137.745  1.00  5.40           N  
ATOM   1848  CA  ALA A 247     125.833 168.248 136.512  1.00  5.40           C  
ATOM   1849  C   ALA A 247     125.989 166.748 136.750  1.00  5.40           C  
ATOM   1850  O   ALA A 247     125.341 165.948 136.069  1.00  5.40           O  
ATOM   1851  CB  ALA A 247     126.853 168.715 135.473  1.00  5.40           C  
ATOM   1852  N   ASN A 248     126.845 166.352 137.688  1.00 10.40           N  
ATOM   1853  CA  ASN A 248     127.109 164.949 137.991  1.00 10.40           C  
ATOM   1854  C   ASN A 248     127.679 164.855 139.406  1.00 10.40           C  
ATOM   1855  O   ASN A 248     127.744 165.849 140.136  1.00 10.40           O  
ATOM   1856  CB  ASN A 248     128.057 164.322 136.962  1.00 10.40           C  
ATOM   1857  CG  ASN A 248     129.364 165.072 136.837  1.00 10.40           C  
ATOM   1858  OD1 ASN A 248     130.156 165.132 137.776  1.00 10.40           O  
ATOM   1859  ND2 ASN A 248     129.605 165.632 135.662  1.00 10.40           N  
ATOM   1860  N   ASN A 249     128.105 163.653 139.785  1.00  7.15           N  
ATOM   1861  CA  ASN A 249     128.585 163.356 141.128  1.00  7.15           C  
ATOM   1862  C   ASN A 249     130.079 163.626 141.313  1.00  7.15           C  
ATOM   1863  O   ASN A 249     130.638 163.227 142.338  1.00  7.15           O  
ATOM   1864  CB  ASN A 249     128.253 161.900 141.486  1.00  7.15           C  
ATOM   1865  CG  ASN A 249     129.086 160.883 140.723  1.00  7.15           C  
ATOM   1866  OD1 ASN A 249     129.754 161.203 139.747  1.00  7.15           O  
ATOM   1867  ND2 ASN A 249     129.029 159.639 141.170  1.00  7.15           N  
ATOM   1868  N   ILE A 250     130.732 164.285 140.356  1.00  8.59           N  
ATOM   1869  CA  ILE A 250     132.138 164.658 140.469  1.00  8.59           C  
ATOM   1870  C   ILE A 250     132.334 166.174 140.503  1.00  8.59           C  
ATOM   1871  O   ILE A 250     133.191 166.665 141.239  1.00  8.59           O  
ATOM   1872  CB  ILE A 250     132.977 164.024 139.334  1.00  8.59           C  
ATOM   1873  CG1 ILE A 250     132.890 162.498 139.371  1.00  8.59           C  
ATOM   1874  CG2 ILE A 250     134.437 164.447 139.435  1.00  8.59           C  
ATOM   1875  CD1 ILE A 250     133.160 161.879 140.733  1.00  8.59           C  
ATOM   1876  N   GLU A 251     131.561 166.942 139.726  1.00 13.17           N  
ATOM   1877  CA  GLU A 251     131.942 168.330 139.463  1.00 13.17           C  
ATOM   1878  C   GLU A 251     131.679 169.275 140.634  1.00 13.17           C  
ATOM   1879  O   GLU A 251     132.316 170.330 140.709  1.00 13.17           O  
ATOM   1880  CB  GLU A 251     131.216 168.884 138.232  1.00 13.17           C  
ATOM   1881  CG  GLU A 251     129.778 169.300 138.472  1.00 13.17           C  
ATOM   1882  CD  GLU A 251     129.158 169.992 137.272  1.00 13.17           C  
ATOM   1883  OE1 GLU A 251     129.805 170.051 136.203  1.00 13.17           O  
ATOM   1884  OE2 GLU A 251     128.035 170.519 137.414  1.00 13.17           O  
ATOM   1885  N   GLY A 252     130.751 168.945 141.527  1.00  9.53           N  
ATOM   1886  CA  GLY A 252     130.361 169.847 142.595  1.00  9.53           C  
ATOM   1887  C   GLY A 252     129.248 170.795 142.188  1.00  9.53           C  
ATOM   1888  O   GLY A 252     128.714 170.754 141.078  1.00  9.53           O  
ATOM   1889  N   VAL A 253     128.888 171.680 143.114  1.00  8.19           N  
ATOM   1890  CA  VAL A 253     127.735 172.556 142.921  1.00  8.19           C  
ATOM   1891  C   VAL A 253     128.115 173.711 142.004  1.00  8.19           C  
ATOM   1892  O   VAL A 253     129.272 174.151 142.012  1.00  8.19           O  
ATOM   1893  CB  VAL A 253     127.189 173.095 144.255  1.00  8.19           C  
ATOM   1894  CG1 VAL A 253     126.767 171.957 145.176  1.00  8.19           C  
ATOM   1895  CG2 VAL A 253     128.182 174.032 144.947  1.00  8.19           C  
ATOM   1896  N   PRO A 254     127.184 174.236 141.212  1.00  9.37           N  
ATOM   1897  CA  PRO A 254     127.479 175.431 140.418  1.00  9.37           C  
ATOM   1898  C   PRO A 254     127.681 176.653 141.299  1.00  9.37           C  
ATOM   1899  O   PRO A 254     127.247 176.705 142.450  1.00  9.37           O  
ATOM   1900  CB  PRO A 254     126.242 175.589 139.531  1.00  9.37           C  
ATOM   1901  CG  PRO A 254     125.190 174.785 140.166  1.00  9.37           C  
ATOM   1902  CD  PRO A 254     125.852 173.688 140.904  1.00  9.37           C  
ATOM   1903  N   GLU A 255     128.354 177.649 140.730  1.00 13.74           N  
ATOM   1904  CA  GLU A 255     128.686 178.885 141.425  1.00 13.74           C  
ATOM   1905  C   GLU A 255     128.266 180.081 140.581  1.00 13.74           C  
ATOM   1906  O   GLU A 255     128.615 180.163 139.400  1.00 13.74           O  
ATOM   1907  CB  GLU A 255     130.185 178.950 141.734  1.00 13.74           C  
ATOM   1908  CG  GLU A 255     130.713 177.767 142.530  1.00 13.74           C  
ATOM   1909  CD  GLU A 255     132.195 177.878 142.829  1.00 13.74           C  
ATOM   1910  OE1 GLU A 255     132.688 179.013 143.001  1.00 13.74           O  
ATOM   1911  OE2 GLU A 255     132.868 176.829 142.891  1.00 13.74           O  
ATOM   1912  N   ILE A 256     127.514 180.999 141.186  1.00 12.60           N  
ATOM   1913  CA  ILE A 256     127.149 182.265 140.563  1.00 12.60           C  
ATOM   1914  C   ILE A 256     127.632 183.405 141.458  1.00 12.60           C  
ATOM   1915  O   ILE A 256     128.003 183.207 142.614  1.00 12.60           O  
ATOM   1916  CB  ILE A 256     125.632 182.389 140.297  1.00 12.60           C  
ATOM   1917  CG1 ILE A 256     124.845 182.488 141.609  1.00 12.60           C  
ATOM   1918  CG2 ILE A 256     125.127 181.244 139.422  1.00 12.60           C  
ATOM   1919  CD1 ILE A 256     123.357 182.592 141.418  1.00 12.60           C  
ATOM   1920  N   GLU A 257     127.613 184.612 140.901  1.00 19.99           N  
ATOM   1921  CA  GLU A 257     127.978 185.811 141.646  1.00 19.99           C  
ATOM   1922  C   GLU A 257     126.763 186.323 142.416  1.00 19.99           C  
ATOM   1923  O   GLU A 257     125.700 186.557 141.833  1.00 19.99           O  
ATOM   1924  CB  GLU A 257     128.541 186.875 140.704  1.00 19.99           C  
ATOM   1925  CG  GLU A 257     127.586 187.452 139.674  1.00 19.99           C  
ATOM   1926  CD  GLU A 257     127.465 186.597 138.419  1.00 19.99           C  
ATOM   1927  OE1 GLU A 257     127.787 185.390 138.473  1.00 19.99           O  
ATOM   1928  OE2 GLU A 257     127.063 187.141 137.370  1.00 19.99           O  
ATOM   1929  N   SER A 258     126.914 186.465 143.728  1.00 19.11           N  
ATOM   1930  CA  SER A 258     125.830 186.886 144.603  1.00 19.11           C  
ATOM   1931  C   SER A 258     125.813 188.400 144.764  1.00 19.11           C  
ATOM   1932  O   SER A 258     126.853 189.060 144.726  1.00 19.11           O  
ATOM   1933  CB  SER A 258     125.962 186.230 145.977  1.00 19.11           C  
ATOM   1934  OG  SER A 258     124.816 186.483 146.768  1.00 19.11           O  
ATOM   1935  N   PHE A 259     124.610 188.946 144.947  1.00 23.62           N  
ATOM   1936  CA  PHE A 259     124.431 190.350 145.293  1.00 23.62           C  
ATOM   1937  C   PHE A 259     124.320 190.586 146.794  1.00 23.62           C  
ATOM   1938  O   PHE A 259     124.275 191.744 147.219  1.00 23.62           O  
ATOM   1939  CB  PHE A 259     123.176 190.918 144.619  1.00 23.62           C  
ATOM   1940  CG  PHE A 259     123.241 190.940 143.122  1.00 23.62           C  
ATOM   1941  CD1 PHE A 259     124.090 191.807 142.461  1.00 23.62           C  
ATOM   1942  CD2 PHE A 259     122.435 190.106 142.376  1.00 23.62           C  
ATOM   1943  CE1 PHE A 259     124.140 191.828 141.085  1.00 23.62           C  
ATOM   1944  CE2 PHE A 259     122.482 190.125 141.005  1.00 23.62           C  
ATOM   1945  CZ  PHE A 259     123.334 190.987 140.358  1.00 23.62           C  
ATOM   1946  N   ASP A 260     124.275 189.530 147.602  1.00 20.42           N  
ATOM   1947  CA  ASP A 260     124.113 189.665 149.040  1.00 20.42           C  
ATOM   1948  C   ASP A 260     125.476 189.798 149.721  1.00 20.42           C  
ATOM   1949  O   ASP A 260     126.525 189.826 149.074  1.00 20.42           O  
ATOM   1950  CB  ASP A 260     123.328 188.478 149.595  1.00 20.42           C  
ATOM   1951  CG  ASP A 260     122.539 188.829 150.841  1.00 20.42           C  
ATOM   1952  OD1 ASP A 260     122.892 189.819 151.513  1.00 20.42           O  
ATOM   1953  OD2 ASP A 260     121.567 188.116 151.151  1.00 20.42           O  
ATOM   1954  N   ASP A 261     125.459 189.871 151.051  1.00 20.24           N  
ATOM   1955  CA  ASP A 261     126.652 190.093 151.860  1.00 20.24           C  
ATOM   1956  C   ASP A 261     126.707 189.065 152.979  1.00 20.24           C  
ATOM   1957  O   ASP A 261     125.702 188.825 153.654  1.00 20.24           O  
ATOM   1958  CB  ASP A 261     126.656 191.510 152.440  1.00 20.24           C  
ATOM   1959  CG  ASP A 261     127.853 191.777 153.322  1.00 20.24           C  
ATOM   1960  OD1 ASP A 261     128.986 191.464 152.903  1.00 20.24           O  
ATOM   1961  OD2 ASP A 261     127.661 192.308 154.434  1.00 20.24           O  
ATOM   1962  N   VAL A 262     127.888 188.471 153.185  1.00 17.30           N  
ATOM   1963  CA  VAL A 262     128.036 187.376 154.141  1.00 17.30           C  
ATOM   1964  C   VAL A 262     128.326 187.854 155.558  1.00 17.30           C  
ATOM   1965  O   VAL A 262     128.466 187.018 156.462  1.00 17.30           O  
ATOM   1966  CB  VAL A 262     129.145 186.389 153.713  1.00 17.30           C  
ATOM   1967  CG1 VAL A 262     128.699 185.565 152.514  1.00 17.30           C  
ATOM   1968  CG2 VAL A 262     130.452 187.113 153.424  1.00 17.30           C  
ATOM   1969  N   ASN A 263     128.420 189.164 155.788  1.00 20.73           N  
ATOM   1970  CA  ASN A 263     128.665 189.699 157.123  1.00 20.73           C  
ATOM   1971  C   ASN A 263     127.505 190.528 157.664  1.00 20.73           C  
ATOM   1972  O   ASN A 263     127.680 191.231 158.664  1.00 20.73           O  
ATOM   1973  CB  ASN A 263     129.941 190.545 157.133  1.00 20.73           C  
ATOM   1974  CG  ASN A 263     131.175 189.746 156.776  1.00 20.73           C  
ATOM   1975  OD1 ASN A 263     131.407 188.662 157.310  1.00 20.73           O  
ATOM   1976  ND2 ASN A 263     131.978 190.281 155.870  1.00 20.73           N  
ATOM   1977  N   ARG A 264     126.331 190.470 157.043  1.00 18.34           N  
ATOM   1978  CA  ARG A 264     125.185 191.219 157.538  1.00 18.34           C  
ATOM   1979  C   ARG A 264     124.547 190.518 158.731  1.00 18.34           C  
ATOM   1980  O   ARG A 264     124.460 189.288 158.778  1.00 18.34           O  
ATOM   1981  CB  ARG A 264     124.147 191.418 156.431  1.00 18.34           C  
ATOM   1982  CG  ARG A 264     123.368 190.174 156.041  1.00 18.34           C  
ATOM   1983  CD  ARG A 264     122.319 190.483 154.977  1.00 18.34           C  
ATOM   1984  NE  ARG A 264     121.894 189.290 154.246  1.00 18.34           N  
ATOM   1985  CZ  ARG A 264     120.855 188.527 154.576  1.00 18.34           C  
ATOM   1986  NH1 ARG A 264     120.114 188.811 155.637  1.00 18.34           N  
ATOM   1987  NH2 ARG A 264     120.554 187.465 153.844  1.00 18.34           N  
ATOM   1988  N   LEU A 265     124.107 191.316 159.698  1.00 18.99           N  
ATOM   1989  CA  LEU A 265     123.392 190.842 160.873  1.00 18.99           C  
ATOM   1990  C   LEU A 265     121.903 191.133 160.731  1.00 18.99           C  
ATOM   1991  O   LEU A 265     121.499 192.064 160.031  1.00 18.99           O  
ATOM   1992  CB  LEU A 265     123.934 191.506 162.141  1.00 18.99           C  
ATOM   1993  CG  LEU A 265     125.437 191.374 162.410  1.00 18.99           C  
ATOM   1994  CD1 LEU A 265     125.818 192.160 163.644  1.00 18.99           C  
ATOM   1995  CD2 LEU A 265     125.867 189.922 162.562  1.00 18.99           C  
ATOM   1996  N   ASP A 266     121.088 190.323 161.404  1.00 20.61           N  
ATOM   1997  CA  ASP A 266     119.629 190.422 161.338  1.00 20.61           C  
ATOM   1998  C   ASP A 266     119.083 190.508 162.761  1.00 20.61           C  
ATOM   1999  O   ASP A 266     118.918 189.487 163.433  1.00 20.61           O  
ATOM   2000  CB  ASP A 266     119.041 189.234 160.586  1.00 20.61           C  
ATOM   2001  CG  ASP A 266     117.580 189.427 160.235  1.00 20.61           C  
ATOM   2002  OD1 ASP A 266     116.843 190.037 161.038  1.00 20.61           O  
ATOM   2003  OD2 ASP A 266     117.167 188.967 159.152  1.00 20.61           O  
ATOM   2004  N   LYS A 267     118.782 191.729 163.210  1.00 21.39           N  
ATOM   2005  CA  LYS A 267     118.332 191.930 164.584  1.00 21.39           C  
ATOM   2006  C   LYS A 267     116.948 191.341 164.825  1.00 21.39           C  
ATOM   2007  O   LYS A 267     116.660 190.880 165.936  1.00 21.39           O  
ATOM   2008  CB  LYS A 267     118.331 193.420 164.923  1.00 21.39           C  
ATOM   2009  CG  LYS A 267     119.711 194.042 165.048  1.00 21.39           C  
ATOM   2010  CD  LYS A 267     120.569 193.356 166.102  1.00 21.39           C  
ATOM   2011  CE  LYS A 267     121.834 194.147 166.381  1.00 21.39           C  
ATOM   2012  NZ  LYS A 267     122.543 193.650 167.583  1.00 21.39           N  
ATOM   2013  N   SER A 268     116.084 191.348 163.809  1.00 19.57           N  
ATOM   2014  CA  SER A 268     114.736 190.813 163.968  1.00 19.57           C  
ATOM   2015  C   SER A 268     114.746 189.409 164.561  1.00 19.57           C  
ATOM   2016  O   SER A 268     113.854 189.048 165.337  1.00 19.57           O  
ATOM   2017  CB  SER A 268     114.021 190.811 162.619  1.00 19.57           C  
ATOM   2018  OG  SER A 268     114.635 189.909 161.720  1.00 19.57           O  
ATOM   2019  N   LEU A 269     115.750 188.603 164.212  1.00 14.87           N  
ATOM   2020  CA  LEU A 269     115.775 187.220 164.676  1.00 14.87           C  
ATOM   2021  C   LEU A 269     115.769 187.134 166.197  1.00 14.87           C  
ATOM   2022  O   LEU A 269     115.297 186.141 166.760  1.00 14.87           O  
ATOM   2023  CB  LEU A 269     116.995 186.493 164.103  1.00 14.87           C  
ATOM   2024  CG  LEU A 269     117.077 186.377 162.578  1.00 14.87           C  
ATOM   2025  CD1 LEU A 269     118.201 185.448 162.146  1.00 14.87           C  
ATOM   2026  CD2 LEU A 269     115.760 185.920 161.996  1.00 14.87           C  
ATOM   2027  N   ASP A 270     116.275 188.160 166.882  1.00 17.78           N  
ATOM   2028  CA  ASP A 270     116.300 188.151 168.339  1.00 17.78           C  
ATOM   2029  C   ASP A 270     114.909 188.202 168.965  1.00 17.78           C  
ATOM   2030  O   ASP A 270     114.807 188.095 170.190  1.00 17.78           O  
ATOM   2031  CB  ASP A 270     117.139 189.325 168.854  1.00 17.78           C  
ATOM   2032  CG  ASP A 270     118.603 189.216 168.469  1.00 17.78           C  
ATOM   2033  OD1 ASP A 270     119.020 188.153 167.964  1.00 17.78           O  
ATOM   2034  OD2 ASP A 270     119.344 190.198 168.671  1.00 17.78           O  
ATOM   2035  N   THR A 271     113.847 188.371 168.173  1.00 18.01           N  
ATOM   2036  CA  THR A 271     112.480 188.372 168.687  1.00 18.01           C  
ATOM   2037  C   THR A 271     111.592 187.314 168.040  1.00 18.01           C  
ATOM   2038  O   THR A 271     110.391 187.271 168.328  1.00 18.01           O  
ATOM   2039  CB  THR A 271     111.845 189.754 168.503  1.00 18.01           C  
ATOM   2040  OG1 THR A 271     111.885 190.123 167.121  1.00 18.01           O  
ATOM   2041  CG2 THR A 271     112.576 190.791 169.330  1.00 18.01           C  
ATOM   2042  N   LEU A 272     112.146 186.457 167.182  1.00 15.64           N  
ATOM   2043  CA  LEU A 272     111.328 185.461 166.500  1.00 15.64           C  
ATOM   2044  C   LEU A 272     110.670 184.500 167.486  1.00 15.64           C  
ATOM   2045  O   LEU A 272     109.481 184.192 167.359  1.00 15.64           O  
ATOM   2046  CB  LEU A 272     112.182 184.695 165.492  1.00 15.64           C  
ATOM   2047  CG  LEU A 272     111.452 183.694 164.598  1.00 15.64           C  
ATOM   2048  CD1 LEU A 272     110.446 184.402 163.709  1.00 15.64           C  
ATOM   2049  CD2 LEU A 272     112.447 182.904 163.773  1.00 15.64           C  
ATOM   2050  N   ILE A 273     111.421 184.015 168.469  1.00 16.12           N  
ATOM   2051  CA  ILE A 273     110.920 182.995 169.389  1.00 16.12           C  
ATOM   2052  C   ILE A 273     110.012 183.651 170.425  1.00 16.12           C  
ATOM   2053  O   ILE A 273     110.451 184.562 171.140  1.00 16.12           O  
ATOM   2054  CB  ILE A 273     112.067 182.236 170.072  1.00 16.12           C  
ATOM   2055  CG1 ILE A 273     113.048 181.670 169.037  1.00 16.12           C  
ATOM   2056  CG2 ILE A 273     111.516 181.113 170.939  1.00 16.12           C  
ATOM   2057  CD1 ILE A 273     112.457 180.666 168.082  1.00 16.12           C  
ATOM   2058  N   PRO A 274     108.754 183.232 170.545  1.00 22.59           N  
ATOM   2059  CA  PRO A 274     107.884 183.806 171.576  1.00 22.59           C  
ATOM   2060  C   PRO A 274     108.293 183.377 172.977  1.00 22.59           C  
ATOM   2061  O   PRO A 274     108.882 182.314 173.185  1.00 22.59           O  
ATOM   2062  CB  PRO A 274     106.498 183.260 171.214  1.00 22.59           C  
ATOM   2063  CG  PRO A 274     106.595 182.870 169.798  1.00 22.59           C  
ATOM   2064  CD  PRO A 274     107.988 182.407 169.597  1.00 22.59           C  
ATOM   2065  N   ASP A 275     107.964 184.230 173.950  1.00 34.98           N  
ATOM   2066  CA  ASP A 275     108.234 183.906 175.346  1.00 34.98           C  
ATOM   2067  C   ASP A 275     107.313 182.806 175.857  1.00 34.98           C  
ATOM   2068  O   ASP A 275     107.698 182.040 176.747  1.00 34.98           O  
ATOM   2069  CB  ASP A 275     108.092 185.158 176.210  1.00 34.98           C  
ATOM   2070  CG  ASP A 275     109.100 186.233 175.852  1.00 34.98           C  
ATOM   2071  OD1 ASP A 275     110.202 185.887 175.376  1.00 34.98           O  
ATOM   2072  OD2 ASP A 275     108.791 187.427 176.049  1.00 34.98           O  
ATOM   2073  N   ASN A 276     106.106 182.714 175.316  1.00 32.62           N  
ATOM   2074  CA  ASN A 276     105.167 181.677 175.720  1.00 32.62           C  
ATOM   2075  C   ASN A 276     105.546 180.358 175.056  1.00 32.62           C  
ATOM   2076  O   ASN A 276     105.593 180.291 173.823  1.00 32.62           O  
ATOM   2077  CB  ASN A 276     103.749 182.076 175.336  1.00 32.62           C  
ATOM   2078  CG  ASN A 276     102.711 181.060 175.772  1.00 32.62           C  
ATOM   2079  OD1 ASN A 276     102.987 179.865 175.871  1.00 32.62           O  
ATOM   2080  ND2 ASN A 276     101.503 181.535 176.030  1.00 32.62           N  
ATOM   2081  N   PRO A 277     105.811 179.292 175.819  1.00 32.48           N  
ATOM   2082  CA  PRO A 277     106.199 178.017 175.193  1.00 32.48           C  
ATOM   2083  C   PRO A 277     105.102 177.375 174.360  1.00 32.48           C  
ATOM   2084  O   PRO A 277     105.398 176.436 173.611  1.00 32.48           O  
ATOM   2085  CB  PRO A 277     106.572 177.136 176.391  1.00 32.48           C  
ATOM   2086  CG  PRO A 277     105.869 177.725 177.539  1.00 32.48           C  
ATOM   2087  CD  PRO A 277     105.756 179.188 177.287  1.00 32.48           C  
ATOM   2088  N   ASN A 278     103.858 177.840 174.462  1.00 35.11           N  
ATOM   2089  CA  ASN A 278     102.745 177.276 173.709  1.00 35.11           C  
ATOM   2090  C   ASN A 278     102.440 178.030 172.420  1.00 35.11           C  
ATOM   2091  O   ASN A 278     101.515 177.643 171.701  1.00 35.11           O  
ATOM   2092  CB  ASN A 278     101.487 177.237 174.584  1.00 35.11           C  
ATOM   2093  CG  ASN A 278     101.755 176.680 175.964  1.00 35.11           C  
ATOM   2094  OD1 ASN A 278     101.483 177.330 176.972  1.00 35.11           O  
ATOM   2095  ND2 ASN A 278     102.287 175.467 176.018  1.00 35.11           N  
ATOM   2096  N   LYS A 279     103.184 179.087 172.108  1.00 29.46           N  
ATOM   2097  CA  LYS A 279     102.949 179.821 170.873  1.00 29.46           C  
ATOM   2098  C   LYS A 279     103.924 179.376 169.787  1.00 29.46           C  
ATOM   2099  O   LYS A 279     105.111 179.176 170.065  1.00 29.46           O  
ATOM   2100  CB  LYS A 279     103.099 181.325 171.098  1.00 29.46           C  
ATOM   2101  CG  LYS A 279     102.090 181.920 172.057  1.00 29.46           C  
ATOM   2102  CD  LYS A 279     100.779 182.220 171.366  1.00 29.46           C  
ATOM   2103  CE  LYS A 279      99.799 182.902 172.305  1.00 29.46           C  
ATOM   2104  NZ  LYS A 279      98.513 183.215 171.634  1.00 29.46           N  
ATOM   2105  N   PRO A 280     103.464 179.206 168.540  1.00 22.41           N  
ATOM   2106  CA  PRO A 280     104.379 178.810 167.462  1.00 22.41           C  
ATOM   2107  C   PRO A 280     104.969 179.987 166.700  1.00 22.41           C  
ATOM   2108  O   PRO A 280     104.610 181.144 166.934  1.00 22.41           O  
ATOM   2109  CB  PRO A 280     103.484 177.965 166.553  1.00 22.41           C  
ATOM   2110  CG  PRO A 280     102.142 178.562 166.716  1.00 22.41           C  
ATOM   2111  CD  PRO A 280     102.063 179.184 168.086  1.00 22.41           C  
ATOM   2112  N   TYR A 281     105.883 179.686 165.781  1.00 13.89           N  
ATOM   2113  CA  TYR A 281     106.432 180.667 164.858  1.00 13.89           C  
ATOM   2114  C   TYR A 281     106.709 179.975 163.527  1.00 13.89           C  
ATOM   2115  O   TYR A 281     106.694 178.747 163.429  1.00 13.89           O  
ATOM   2116  CB  TYR A 281     107.706 181.307 165.414  1.00 13.89           C  
ATOM   2117  CG  TYR A 281     108.834 180.322 165.575  1.00 13.89           C  
ATOM   2118  CD1 TYR A 281     108.902 179.507 166.684  1.00 13.89           C  
ATOM   2119  CD2 TYR A 281     109.816 180.189 164.608  1.00 13.89           C  
ATOM   2120  CE1 TYR A 281     109.909 178.602 166.834  1.00 13.89           C  
ATOM   2121  CE2 TYR A 281     110.833 179.282 164.756  1.00 13.89           C  
ATOM   2122  CZ  TYR A 281     110.875 178.491 165.873  1.00 13.89           C  
ATOM   2123  OH  TYR A 281     111.878 177.575 166.039  1.00 13.89           O  
ATOM   2124  N   ASP A 282     106.985 180.782 162.504  1.00 13.53           N  
ATOM   2125  CA  ASP A 282     107.165 180.298 161.137  1.00 13.53           C  
ATOM   2126  C   ASP A 282     108.655 180.098 160.870  1.00 13.53           C  
ATOM   2127  O   ASP A 282     109.409 181.069 160.755  1.00 13.53           O  
ATOM   2128  CB  ASP A 282     106.546 181.275 160.138  1.00 13.53           C  
ATOM   2129  CG  ASP A 282     106.485 180.714 158.727  1.00 13.53           C  
ATOM   2130  OD1 ASP A 282     106.862 179.542 158.523  1.00 13.53           O  
ATOM   2131  OD2 ASP A 282     106.057 181.451 157.817  1.00 13.53           O  
ATOM   2132  N   MET A 283     109.075 178.834 160.766  1.00 12.58           N  
ATOM   2133  CA  MET A 283     110.473 178.517 160.477  1.00 12.58           C  
ATOM   2134  C   MET A 283     110.866 178.909 159.054  1.00 12.58           C  
ATOM   2135  O   MET A 283     112.038 179.223 158.793  1.00 12.58           O  
ATOM   2136  CB  MET A 283     110.715 177.023 160.702  1.00 12.58           C  
ATOM   2137  CG  MET A 283     112.161 176.591 160.594  1.00 12.58           C  
ATOM   2138  SD  MET A 283     113.209 177.278 161.878  1.00 12.58           S  
ATOM   2139  CE  MET A 283     113.078 176.021 163.137  1.00 12.58           C  
ATOM   2140  N   GLY A 284     109.908 178.899 158.125  1.00 12.90           N  
ATOM   2141  CA  GLY A 284     110.204 179.287 156.757  1.00 12.90           C  
ATOM   2142  C   GLY A 284     110.677 180.720 156.629  1.00 12.90           C  
ATOM   2143  O   GLY A 284     111.506 181.031 155.770  1.00 12.90           O  
ATOM   2144  N   GLU A 285     110.166 181.611 157.478  1.00 16.69           N  
ATOM   2145  CA  GLU A 285     110.647 182.988 157.464  1.00 16.69           C  
ATOM   2146  C   GLU A 285     112.116 183.054 157.862  1.00 16.69           C  
ATOM   2147  O   GLU A 285     112.884 183.845 157.303  1.00 16.69           O  
ATOM   2148  CB  GLU A 285     109.790 183.860 158.384  1.00 16.69           C  
ATOM   2149  CG  GLU A 285     108.319 183.926 157.993  1.00 16.69           C  
ATOM   2150  CD  GLU A 285     108.105 184.188 156.512  1.00 16.69           C  
ATOM   2151  OE1 GLU A 285     108.000 183.211 155.740  1.00 16.69           O  
ATOM   2152  OE2 GLU A 285     108.045 185.372 156.121  1.00 16.69           O  
ATOM   2153  N   LEU A 286     112.537 182.204 158.800  1.00 12.30           N  
ATOM   2154  CA  LEU A 286     113.949 182.155 159.157  1.00 12.30           C  
ATOM   2155  C   LEU A 286     114.786 181.618 158.002  1.00 12.30           C  
ATOM   2156  O   LEU A 286     115.839 182.185 157.675  1.00 12.30           O  
ATOM   2157  CB  LEU A 286     114.140 181.306 160.415  1.00 12.30           C  
ATOM   2158  CG  LEU A 286     115.564 180.923 160.836  1.00 12.30           C  
ATOM   2159  CD1 LEU A 286     116.388 182.130 161.226  1.00 12.30           C  
ATOM   2160  CD2 LEU A 286     115.527 179.937 161.981  1.00 12.30           C  
ATOM   2161  N   ILE A 287     114.330 180.538 157.358  1.00  9.69           N  
ATOM   2162  CA  ILE A 287     115.052 180.034 156.189  1.00  9.69           C  
ATOM   2163  C   ILE A 287     115.222 181.144 155.159  1.00  9.69           C  
ATOM   2164  O   ILE A 287     116.314 181.354 154.619  1.00  9.69           O  
ATOM   2165  CB  ILE A 287     114.339 178.811 155.580  1.00  9.69           C  
ATOM   2166  CG1 ILE A 287     114.416 177.604 156.524  1.00  9.69           C  
ATOM   2167  CG2 ILE A 287     114.962 178.452 154.227  1.00  9.69           C  
ATOM   2168  CD1 ILE A 287     113.657 176.390 156.045  1.00  9.69           C  
ATOM   2169  N   ARG A 288     114.142 181.876 154.877  1.00 12.90           N  
ATOM   2170  CA  ARG A 288     114.173 182.885 153.824  1.00 12.90           C  
ATOM   2171  C   ARG A 288     114.959 184.124 154.232  1.00 12.90           C  
ATOM   2172  O   ARG A 288     115.418 184.866 153.360  1.00 12.90           O  
ATOM   2173  CB  ARG A 288     112.743 183.252 153.422  1.00 12.90           C  
ATOM   2174  CG  ARG A 288     112.041 182.149 152.637  1.00 12.90           C  
ATOM   2175  CD  ARG A 288     110.583 182.447 152.350  1.00 12.90           C  
ATOM   2176  NE  ARG A 288     110.003 181.453 151.451  1.00 12.90           N  
ATOM   2177  CZ  ARG A 288     109.681 180.214 151.811  1.00 12.90           C  
ATOM   2178  NH1 ARG A 288     109.159 179.378 150.927  1.00 12.90           N  
ATOM   2179  NH2 ARG A 288     109.880 179.804 153.054  1.00 12.90           N  
ATOM   2180  N   ARG A 289     115.131 184.360 155.531  1.00 15.93           N  
ATOM   2181  CA  ARG A 289     116.040 185.401 155.989  1.00 15.93           C  
ATOM   2182  C   ARG A 289     117.500 184.965 155.963  1.00 15.93           C  
ATOM   2183  O   ARG A 289     118.383 185.826 155.947  1.00 15.93           O  
ATOM   2184  CB  ARG A 289     115.672 185.843 157.407  1.00 15.93           C  
ATOM   2185  CG  ARG A 289     114.481 186.777 157.481  1.00 15.93           C  
ATOM   2186  CD  ARG A 289     114.060 187.020 158.912  1.00 15.93           C  
ATOM   2187  NE  ARG A 289     112.898 187.895 159.007  1.00 15.93           N  
ATOM   2188  CZ  ARG A 289     112.928 189.200 158.766  1.00 15.93           C  
ATOM   2189  NH1 ARG A 289     111.824 189.920 158.882  1.00 15.93           N  
ATOM   2190  NH2 ARG A 289     114.059 189.787 158.404  1.00 15.93           N  
ATOM   2191  N   VAL A 290     117.779 183.662 155.956  1.00 10.86           N  
ATOM   2192  CA  VAL A 290     119.168 183.212 156.003  1.00 10.86           C  
ATOM   2193  C   VAL A 290     119.776 183.007 154.611  1.00 10.86           C  
ATOM   2194  O   VAL A 290     120.986 183.182 154.440  1.00 10.86           O  
ATOM   2195  CB  VAL A 290     119.280 181.932 156.853  1.00 10.86           C  
ATOM   2196  CG1 VAL A 290     120.621 181.256 156.636  1.00 10.86           C  
ATOM   2197  CG2 VAL A 290     119.087 182.261 158.323  1.00 10.86           C  
ATOM   2198  N   VAL A 291     118.972 182.639 153.610  1.00  8.99           N  
ATOM   2199  CA  VAL A 291     119.512 182.383 152.273  1.00  8.99           C  
ATOM   2200  C   VAL A 291     119.871 183.697 151.576  1.00  8.99           C  
ATOM   2201  O   VAL A 291     119.444 184.787 151.970  1.00  8.99           O  
ATOM   2202  CB  VAL A 291     118.521 181.567 151.426  1.00  8.99           C  
ATOM   2203  CG1 VAL A 291     118.323 180.170 152.001  1.00  8.99           C  
ATOM   2204  CG2 VAL A 291     117.192 182.302 151.288  1.00  8.99           C  
ATOM   2205  N   ASP A 292     120.668 183.582 150.514  1.00 11.48           N  
ATOM   2206  CA  ASP A 292     120.991 184.732 149.677  1.00 11.48           C  
ATOM   2207  C   ASP A 292     119.744 185.246 148.960  1.00 11.48           C  
ATOM   2208  O   ASP A 292     119.016 184.477 148.330  1.00 11.48           O  
ATOM   2209  CB  ASP A 292     122.056 184.374 148.636  1.00 11.48           C  
ATOM   2210  CG  ASP A 292     123.364 183.907 149.246  1.00 11.48           C  
ATOM   2211  OD1 ASP A 292     123.553 184.045 150.471  1.00 11.48           O  
ATOM   2212  OD2 ASP A 292     124.215 183.413 148.481  1.00 11.48           O  
ATOM   2213  N   GLU A 293     119.510 186.551 149.051  1.00 16.72           N  
ATOM   2214  CA  GLU A 293     118.494 187.275 148.287  1.00 16.72           C  
ATOM   2215  C   GLU A 293     117.068 186.832 148.602  1.00 16.72           C  
ATOM   2216  O   GLU A 293     116.132 187.261 147.922  1.00 16.72           O  
ATOM   2217  CB  GLU A 293     118.751 187.155 146.779  1.00 16.72           C  
ATOM   2218  CG  GLU A 293     120.108 187.682 146.352  1.00 16.72           C  
ATOM   2219  CD  GLU A 293     120.491 187.290 144.938  1.00 16.72           C  
ATOM   2220  OE1 GLU A 293     119.590 187.010 144.122  1.00 16.72           O  
ATOM   2221  OE2 GLU A 293     121.703 187.265 144.647  1.00 16.72           O  
ATOM   2222  N   GLY A 294     116.872 186.009 149.627  1.00 13.22           N  
ATOM   2223  CA  GLY A 294     115.551 185.503 149.942  1.00 13.22           C  
ATOM   2224  C   GLY A 294     114.990 184.500 148.960  1.00 13.22           C  
ATOM   2225  O   GLY A 294     113.778 184.274 148.954  1.00 13.22           O  
ATOM   2226  N   ASP A 295     115.833 183.878 148.138  1.00 11.63           N  
ATOM   2227  CA  ASP A 295     115.396 182.956 147.096  1.00 11.63           C  
ATOM   2228  C   ASP A 295     115.532 181.523 147.599  1.00 11.63           C  
ATOM   2229  O   ASP A 295     116.619 181.109 148.013  1.00 11.63           O  
ATOM   2230  CB  ASP A 295     116.207 183.166 145.817  1.00 11.63           C  
ATOM   2231  CG  ASP A 295     115.805 182.223 144.704  1.00 11.63           C  
ATOM   2232  OD1 ASP A 295     114.595 181.979 144.537  1.00 11.63           O  
ATOM   2233  OD2 ASP A 295     116.703 181.732 143.993  1.00 11.63           O  
ATOM   2234  N   PHE A 296     114.429 180.778 147.563  1.00  6.99           N  
ATOM   2235  CA  PHE A 296     114.366 179.436 148.133  1.00  6.99           C  
ATOM   2236  C   PHE A 296     113.440 178.562 147.293  1.00  6.99           C  
ATOM   2237  O   PHE A 296     112.282 178.921 147.072  1.00  6.99           O  
ATOM   2238  CB  PHE A 296     113.882 179.507 149.589  1.00  6.99           C  
ATOM   2239  CG  PHE A 296     113.820 178.183 150.280  1.00  6.99           C  
ATOM   2240  CD1 PHE A 296     114.970 177.480 150.566  1.00  6.99           C  
ATOM   2241  CD2 PHE A 296     112.607 177.650 150.662  1.00  6.99           C  
ATOM   2242  CE1 PHE A 296     114.911 176.271 151.203  1.00  6.99           C  
ATOM   2243  CE2 PHE A 296     112.545 176.443 151.298  1.00  6.99           C  
ATOM   2244  CZ  PHE A 296     113.701 175.750 151.567  1.00  6.99           C  
ATOM   2245  N   PHE A 297     113.952 177.414 146.839  1.00  8.40           N  
ATOM   2246  CA  PHE A 297     113.207 176.462 146.011  1.00  8.40           C  
ATOM   2247  C   PHE A 297     112.782 175.296 146.903  1.00  8.40           C  
ATOM   2248  O   PHE A 297     113.600 174.446 147.257  1.00  8.40           O  
ATOM   2249  CB  PHE A 297     114.061 175.987 144.836  1.00  8.40           C  
ATOM   2250  CG  PHE A 297     113.277 175.348 143.716  1.00  8.40           C  
ATOM   2251  CD1 PHE A 297     112.646 174.129 143.890  1.00  8.40           C  
ATOM   2252  CD2 PHE A 297     113.188 175.960 142.478  1.00  8.40           C  
ATOM   2253  CE1 PHE A 297     111.938 173.550 142.863  1.00  8.40           C  
ATOM   2254  CE2 PHE A 297     112.482 175.377 141.454  1.00  8.40           C  
ATOM   2255  CZ  PHE A 297     111.858 174.177 141.649  1.00  8.40           C  
ATOM   2256  N   GLU A 298     111.507 175.267 147.278  1.00  6.53           N  
ATOM   2257  CA  GLU A 298     111.004 174.253 148.196  1.00  6.53           C  
ATOM   2258  C   GLU A 298     110.649 172.960 147.462  1.00  6.53           C  
ATOM   2259  O   GLU A 298     110.193 172.971 146.317  1.00  6.53           O  
ATOM   2260  CB  GLU A 298     109.784 174.776 148.960  1.00  6.53           C  
ATOM   2261  CG  GLU A 298     109.325 173.865 150.091  1.00  6.53           C  
ATOM   2262  CD  GLU A 298     108.397 174.552 151.078  1.00  6.53           C  
ATOM   2263  OE1 GLU A 298     107.982 173.898 152.055  1.00  6.53           O  
ATOM   2264  OE2 GLU A 298     108.085 175.742 150.879  1.00  6.53           O  
ATOM   2265  N   ILE A 299     110.870 171.840 148.144  1.00  6.21           N  
ATOM   2266  CA  ILE A 299     110.591 170.502 147.637  1.00  6.21           C  
ATOM   2267  C   ILE A 299     109.552 169.845 148.540  1.00  6.21           C  
ATOM   2268  O   ILE A 299     109.658 169.900 149.769  1.00  6.21           O  
ATOM   2269  CB  ILE A 299     111.883 169.657 147.562  1.00  6.21           C  
ATOM   2270  CG1 ILE A 299     112.888 170.275 146.578  1.00  6.21           C  
ATOM   2271  CG2 ILE A 299     111.581 168.197 147.227  1.00  6.21           C  
ATOM   2272  CD1 ILE A 299     112.485 170.236 145.129  1.00  6.21           C  
ATOM   2273  N   GLN A 300     108.555 169.215 147.918  1.00  8.00           N  
ATOM   2274  CA  GLN A 300     107.433 168.565 148.604  1.00  8.00           C  
ATOM   2275  C   GLN A 300     106.757 169.505 149.605  1.00  8.00           C  
ATOM   2276  O   GLN A 300     106.514 169.157 150.760  1.00  8.00           O  
ATOM   2277  CB  GLN A 300     107.884 167.264 149.282  1.00  8.00           C  
ATOM   2278  CG  GLN A 300     108.103 166.101 148.336  1.00  8.00           C  
ATOM   2279  CD  GLN A 300     107.693 164.776 148.930  1.00  8.00           C  
ATOM   2280  OE1 GLN A 300     106.513 164.429 148.952  1.00  8.00           O  
ATOM   2281  NE2 GLN A 300     108.663 164.026 149.411  1.00  8.00           N  
ATOM   2282  N   ALA A 301     106.417 170.708 149.135  1.00  7.32           N  
ATOM   2283  CA  ALA A 301     105.851 171.726 150.015  1.00  7.32           C  
ATOM   2284  C   ALA A 301     104.474 171.344 150.548  1.00  7.32           C  
ATOM   2285  O   ALA A 301     104.131 171.709 151.676  1.00  7.32           O  
ATOM   2286  CB  ALA A 301     105.767 173.062 149.285  1.00  7.32           C  
ATOM   2287  N   ALA A 302     103.666 170.639 149.760  1.00  7.11           N  
ATOM   2288  CA  ALA A 302     102.300 170.315 150.154  1.00  7.11           C  
ATOM   2289  C   ALA A 302     102.191 169.014 150.941  1.00  7.11           C  
ATOM   2290  O   ALA A 302     101.103 168.696 151.427  1.00  7.11           O  
ATOM   2291  CB  ALA A 302     101.396 170.241 148.916  1.00  7.11           C  
ATOM   2292  N   TYR A 303     103.282 168.270 151.087  1.00  6.89           N  
ATOM   2293  CA  TYR A 303     103.289 166.980 151.762  1.00  6.89           C  
ATOM   2294  C   TYR A 303     104.109 167.053 153.045  1.00  6.89           C  
ATOM   2295  O   TYR A 303     105.168 167.686 153.083  1.00  6.89           O  
ATOM   2296  CB  TYR A 303     103.848 165.899 150.834  1.00  6.89           C  
ATOM   2297  CG  TYR A 303     104.004 164.527 151.444  1.00  6.89           C  
ATOM   2298  CD1 TYR A 303     102.906 163.728 151.698  1.00  6.89           C  
ATOM   2299  CD2 TYR A 303     105.256 164.016 151.729  1.00  6.89           C  
ATOM   2300  CE1 TYR A 303     103.050 162.472 152.242  1.00  6.89           C  
ATOM   2301  CE2 TYR A 303     105.408 162.765 152.270  1.00  6.89           C  
ATOM   2302  CZ  TYR A 303     104.304 161.994 152.521  1.00  6.89           C  
ATOM   2303  OH  TYR A 303     104.460 160.743 153.064  1.00  6.89           O  
ATOM   2304  N   ALA A 304     103.608 166.406 154.094  1.00  6.57           N  
ATOM   2305  CA  ALA A 304     104.283 166.329 155.388  1.00  6.57           C  
ATOM   2306  C   ALA A 304     104.793 167.707 155.814  1.00  6.57           C  
ATOM   2307  O   ALA A 304     105.992 167.951 155.943  1.00  6.57           O  
ATOM   2308  CB  ALA A 304     105.414 165.298 155.348  1.00  6.57           C  
ATOM   2309  N   ARG A 305     103.840 168.615 156.033  1.00  7.69           N  
ATOM   2310  CA  ARG A 305     104.136 170.027 156.244  1.00  7.69           C  
ATOM   2311  C   ARG A 305     104.718 170.318 157.624  1.00  7.69           C  
ATOM   2312  O   ARG A 305     105.091 171.464 157.888  1.00  7.69           O  
ATOM   2313  CB  ARG A 305     102.868 170.853 156.005  1.00  7.69           C  
ATOM   2314  CG  ARG A 305     102.444 170.873 154.532  1.00  7.69           C  
ATOM   2315  CD  ARG A 305     101.327 171.850 154.224  1.00  7.69           C  
ATOM   2316  NE  ARG A 305     100.277 171.827 155.235  1.00  7.69           N  
ATOM   2317  CZ  ARG A 305      99.910 172.869 155.975  1.00  7.69           C  
ATOM   2318  NH1 ARG A 305      98.946 172.723 156.871  1.00  7.69           N  
ATOM   2319  NH2 ARG A 305     100.481 174.056 155.819  1.00  7.69           N  
ATOM   2320  N   ASN A 306     104.816 169.317 158.500  1.00  6.10           N  
ATOM   2321  CA  ASN A 306     105.549 169.442 159.758  1.00  6.10           C  
ATOM   2322  C   ASN A 306     107.068 169.399 159.578  1.00  6.10           C  
ATOM   2323  O   ASN A 306     107.788 169.399 160.583  1.00  6.10           O  
ATOM   2324  CB  ASN A 306     105.106 168.350 160.737  1.00  6.10           C  
ATOM   2325  CG  ASN A 306     105.091 166.970 160.115  1.00  6.10           C  
ATOM   2326  OD1 ASN A 306     104.698 166.803 158.964  1.00  6.10           O  
ATOM   2327  ND2 ASN A 306     105.518 165.973 160.877  1.00  6.10           N  
ATOM   2328  N   ILE A 307     107.568 169.369 158.345  1.00  6.59           N  
ATOM   2329  CA  ILE A 307     108.999 169.474 158.070  1.00  6.59           C  
ATOM   2330  C   ILE A 307     109.186 170.172 156.726  1.00  6.59           C  
ATOM   2331  O   ILE A 307     108.378 170.007 155.808  1.00  6.59           O  
ATOM   2332  CB  ILE A 307     109.690 168.091 158.103  1.00  6.59           C  
ATOM   2333  CG1 ILE A 307     111.194 168.234 158.324  1.00  6.59           C  
ATOM   2334  CG2 ILE A 307     109.434 167.301 156.833  1.00  6.59           C  
ATOM   2335  CD1 ILE A 307     111.828 167.003 158.897  1.00  6.59           C  
ATOM   2336  N   ILE A 308     110.249 170.965 156.627  1.00  5.11           N  
ATOM   2337  CA  ILE A 308     110.593 171.724 155.431  1.00  5.11           C  
ATOM   2338  C   ILE A 308     111.895 171.182 154.857  1.00  5.11           C  
ATOM   2339  O   ILE A 308     112.848 170.910 155.600  1.00  5.11           O  
ATOM   2340  CB  ILE A 308     110.728 173.229 155.733  1.00  5.11           C  
ATOM   2341  CG1 ILE A 308     109.401 173.799 156.227  1.00  5.11           C  
ATOM   2342  CG2 ILE A 308     111.215 173.979 154.501  1.00  5.11           C  
ATOM   2343  CD1 ILE A 308     109.527 175.138 156.883  1.00  5.11           C  
ATOM   2344  N   THR A 309     111.935 171.066 153.527  1.00  5.93           N  
ATOM   2345  CA  THR A 309     113.097 170.635 152.756  1.00  5.93           C  
ATOM   2346  C   THR A 309     113.212 171.489 151.498  1.00  5.93           C  
ATOM   2347  O   THR A 309     112.217 171.673 150.790  1.00  5.93           O  
ATOM   2348  CB  THR A 309     112.979 169.159 152.360  1.00  5.93           C  
ATOM   2349  OG1 THR A 309     111.706 168.932 151.742  1.00  5.93           O  
ATOM   2350  CG2 THR A 309     113.119 168.254 153.565  1.00  5.93           C  
ATOM   2351  N   GLY A 310     114.407 171.989 151.200  1.00  7.46           N  
ATOM   2352  CA  GLY A 310     114.571 172.724 149.953  1.00  7.46           C  
ATOM   2353  C   GLY A 310     115.995 173.163 149.678  1.00  7.46           C  
ATOM   2354  O   GLY A 310     116.930 172.805 150.391  1.00  7.46           O  
ATOM   2355  N   PHE A 311     116.134 173.939 148.599  1.00 12.77           N  
ATOM   2356  CA  PHE A 311     117.410 174.442 148.101  1.00 12.77           C  
ATOM   2357  C   PHE A 311     117.494 175.957 148.230  1.00 12.77           C  
ATOM   2358  O   PHE A 311     116.526 176.669 147.954  1.00 12.77           O  
ATOM   2359  CB  PHE A 311     117.622 174.084 146.626  1.00 12.77           C  
ATOM   2360  CG  PHE A 311     117.746 172.620 146.356  1.00 12.77           C  
ATOM   2361  CD1 PHE A 311     118.834 171.912 146.812  1.00 12.77           C  
ATOM   2362  CD2 PHE A 311     116.796 171.958 145.608  1.00 12.77           C  
ATOM   2363  CE1 PHE A 311     118.952 170.574 146.553  1.00 12.77           C  
ATOM   2364  CE2 PHE A 311     116.912 170.625 145.352  1.00 12.77           C  
ATOM   2365  CZ  PHE A 311     117.993 169.932 145.821  1.00 12.77           C  
ATOM   2366  N   GLY A 312     118.664 176.443 148.635  1.00  6.84           N  
ATOM   2367  CA  GLY A 312     118.985 177.855 148.580  1.00  6.84           C  
ATOM   2368  C   GLY A 312     120.432 178.072 148.185  1.00  6.84           C  
ATOM   2369  O   GLY A 312     121.117 177.114 147.825  1.00  6.84           O  
ATOM   2370  N   ARG A 313     120.913 179.313 148.242  1.00  6.41           N  
ATOM   2371  CA  ARG A 313     122.326 179.608 148.053  1.00  6.41           C  
ATOM   2372  C   ARG A 313     122.879 180.420 149.219  1.00  6.41           C  
ATOM   2373  O   ARG A 313     122.190 181.255 149.811  1.00  6.41           O  
ATOM   2374  CB  ARG A 313     122.586 180.368 146.738  1.00  6.41           C  
ATOM   2375  CG  ARG A 313     122.219 179.603 145.486  1.00  6.41           C  
ATOM   2376  CD  ARG A 313     122.573 180.387 144.218  1.00  6.41           C  
ATOM   2377  NE  ARG A 313     122.388 179.605 143.001  1.00  6.41           N  
ATOM   2378  CZ  ARG A 313     121.270 179.569 142.282  1.00  6.41           C  
ATOM   2379  NH1 ARG A 313     120.203 180.259 142.647  1.00  6.41           N  
ATOM   2380  NH2 ARG A 313     121.218 178.823 141.190  1.00  6.41           N  
ATOM   2381  N   VAL A 314     124.141 180.144 149.542  1.00  8.31           N  
ATOM   2382  CA  VAL A 314     124.942 180.928 150.475  1.00  8.31           C  
ATOM   2383  C   VAL A 314     126.246 181.278 149.771  1.00  8.31           C  
ATOM   2384  O   VAL A 314     126.914 180.397 149.219  1.00  8.31           O  
ATOM   2385  CB  VAL A 314     125.211 180.168 151.789  1.00  8.31           C  
ATOM   2386  CG1 VAL A 314     126.005 181.029 152.772  1.00  8.31           C  
ATOM   2387  CG2 VAL A 314     123.907 179.712 152.421  1.00  8.31           C  
ATOM   2388  N   GLU A 315     126.580 182.564 149.754  1.00 13.54           N  
ATOM   2389  CA  GLU A 315     127.757 183.063 149.043  1.00 13.54           C  
ATOM   2390  C   GLU A 315     127.823 182.509 147.621  1.00 13.54           C  
ATOM   2391  O   GLU A 315     128.886 182.144 147.121  1.00 13.54           O  
ATOM   2392  CB  GLU A 315     129.036 182.748 149.823  1.00 13.54           C  
ATOM   2393  CG  GLU A 315     130.235 183.584 149.419  1.00 13.54           C  
ATOM   2394  CD  GLU A 315     131.322 183.595 150.478  1.00 13.54           C  
ATOM   2395  OE1 GLU A 315     131.111 183.007 151.560  1.00 13.54           O  
ATOM   2396  OE2 GLU A 315     132.392 184.188 150.227  1.00 13.54           O  
ATOM   2397  N   GLY A 316     126.669 182.459 146.962  1.00 10.19           N  
ATOM   2398  CA  GLY A 316     126.575 182.032 145.583  1.00 10.19           C  
ATOM   2399  C   GLY A 316     126.721 180.549 145.327  1.00 10.19           C  
ATOM   2400  O   GLY A 316     126.828 180.155 144.164  1.00 10.19           O  
ATOM   2401  N   ARG A 317     126.720 179.714 146.363  1.00  9.85           N  
ATOM   2402  CA  ARG A 317     126.828 178.270 146.207  1.00  9.85           C  
ATOM   2403  C   ARG A 317     125.608 177.575 146.804  1.00  9.85           C  
ATOM   2404  O   ARG A 317     125.096 177.986 147.847  1.00  9.85           O  
ATOM   2405  CB  ARG A 317     128.116 177.756 146.854  1.00  9.85           C  
ATOM   2406  CG  ARG A 317     129.381 178.433 146.346  1.00  9.85           C  
ATOM   2407  CD  ARG A 317     130.620 177.836 146.971  1.00  9.85           C  
ATOM   2408  NE  ARG A 317     131.826 178.557 146.566  1.00  9.85           N  
ATOM   2409  CZ  ARG A 317     132.849 178.024 145.903  1.00  9.85           C  
ATOM   2410  NH1 ARG A 317     132.847 176.744 145.556  1.00  9.85           N  
ATOM   2411  NH2 ARG A 317     133.890 178.783 145.587  1.00  9.85           N  
ATOM   2412  N   THR A 318     125.161 176.513 146.134  1.00  5.74           N  
ATOM   2413  CA  THR A 318     123.942 175.806 146.513  1.00  5.74           C  
ATOM   2414  C   THR A 318     124.105 175.102 147.857  1.00  5.74           C  
ATOM   2415  O   THR A 318     125.139 174.496 148.135  1.00  5.74           O  
ATOM   2416  CB  THR A 318     123.569 174.781 145.438  1.00  5.74           C  
ATOM   2417  OG1 THR A 318     123.395 175.444 144.182  1.00  5.74           O  
ATOM   2418  CG2 THR A 318     122.284 174.035 145.798  1.00  5.74           C  
ATOM   2419  N   VAL A 319     123.062 175.178 148.680  1.00  5.60           N  
ATOM   2420  CA  VAL A 319     122.993 174.495 149.967  1.00  5.60           C  
ATOM   2421  C   VAL A 319     121.580 173.949 150.160  1.00  5.60           C  
ATOM   2422  O   VAL A 319     120.593 174.613 149.830  1.00  5.60           O  
ATOM   2423  CB  VAL A 319     123.376 175.439 151.131  1.00  5.60           C  
ATOM   2424  CG1 VAL A 319     123.276 174.728 152.477  1.00  5.60           C  
ATOM   2425  CG2 VAL A 319     124.766 176.039 150.916  1.00  5.60           C  
ATOM   2426  N   GLY A 320     121.488 172.731 150.685  1.00  7.18           N  
ATOM   2427  CA  GLY A 320     120.209 172.156 151.073  1.00  7.18           C  
ATOM   2428  C   GLY A 320     119.840 172.458 152.519  1.00  7.18           C  
ATOM   2429  O   GLY A 320     120.702 172.570 153.389  1.00  7.18           O  
ATOM   2430  N   PHE A 321     118.533 172.583 152.764  1.00 12.77           N  
ATOM   2431  CA  PHE A 321     117.996 172.939 154.071  1.00 12.77           C  
ATOM   2432  C   PHE A 321     116.913 171.959 154.508  1.00 12.77           C  
ATOM   2433  O   PHE A 321     116.020 171.620 153.720  1.00 12.77           O  
ATOM   2434  CB  PHE A 321     117.426 174.363 154.067  1.00 12.77           C  
ATOM   2435  CG  PHE A 321     118.456 175.429 153.854  1.00 12.77           C  
ATOM   2436  CD1 PHE A 321     118.916 175.718 152.586  1.00 12.77           C  
ATOM   2437  CD2 PHE A 321     118.966 176.147 154.920  1.00 12.77           C  
ATOM   2438  CE1 PHE A 321     119.859 176.694 152.385  1.00 12.77           C  
ATOM   2439  CE2 PHE A 321     119.912 177.123 154.716  1.00 12.77           C  
ATOM   2440  CZ  PHE A 321     120.356 177.395 153.449  1.00 12.77           C  
ATOM   2441  N   VAL A 322     117.000 171.538 155.778  1.00  6.99           N  
ATOM   2442  CA  VAL A 322     115.999 170.722 156.467  1.00  6.99           C  
ATOM   2443  C   VAL A 322     115.628 171.424 157.771  1.00  6.99           C  
ATOM   2444  O   VAL A 322     116.506 171.943 158.469  1.00  6.99           O  
ATOM   2445  CB  VAL A 322     116.523 169.297 156.761  1.00  6.99           C  
ATOM   2446  CG1 VAL A 322     115.462 168.460 157.469  1.00  6.99           C  
ATOM   2447  CG2 VAL A 322     117.003 168.601 155.488  1.00  6.99           C  
ATOM   2448  N   ALA A 323     114.338 171.444 158.113  1.00 12.77           N  
ATOM   2449  CA  ALA A 323     113.931 172.181 159.309  1.00 12.77           C  
ATOM   2450  C   ALA A 323     112.580 171.719 159.844  1.00 12.77           C  
ATOM   2451  O   ALA A 323     111.672 171.409 159.074  1.00 12.77           O  
ATOM   2452  CB  ALA A 323     113.867 173.682 159.031  1.00 12.77           C  
ATOM   2453  N   ASN A 324     112.448 171.709 161.171  1.00  7.79           N  
ATOM   2454  CA  ASN A 324     111.145 171.450 161.782  1.00  7.79           C  
ATOM   2455  C   ASN A 324     110.254 172.690 161.703  1.00  7.79           C  
ATOM   2456  O   ASN A 324     110.731 173.825 161.730  1.00  7.79           O  
ATOM   2457  CB  ASN A 324     111.287 171.010 163.238  1.00  7.79           C  
ATOM   2458  CG  ASN A 324     112.348 169.949 163.430  1.00  7.79           C  
ATOM   2459  OD1 ASN A 324     113.451 170.241 163.873  1.00  7.79           O  
ATOM   2460  ND2 ASN A 324     112.016 168.708 163.103  1.00  7.79           N  
ATOM   2461  N   GLN A 325     108.945 172.463 161.608  1.00  7.25           N  
ATOM   2462  CA  GLN A 325     107.960 173.531 161.408  1.00  7.25           C  
ATOM   2463  C   GLN A 325     106.944 173.536 162.544  1.00  7.25           C  
ATOM   2464  O   GLN A 325     106.003 172.724 162.543  1.00  7.25           O  
ATOM   2465  CB  GLN A 325     107.258 173.373 160.059  1.00  7.25           C  
ATOM   2466  CG  GLN A 325     106.053 174.275 159.855  1.00  7.25           C  
ATOM   2467  CD  GLN A 325     106.383 175.740 160.026  1.00  7.25           C  
ATOM   2468  OE1 GLN A 325     106.614 176.209 161.135  1.00  7.25           O  
ATOM   2469  NE2 GLN A 325     106.400 176.472 158.927  1.00  7.25           N  
ATOM   2470  N   PRO A 326     107.083 174.424 163.531  1.00  9.61           N  
ATOM   2471  CA  PRO A 326     106.140 174.424 164.662  1.00  9.61           C  
ATOM   2472  C   PRO A 326     104.689 174.671 164.279  1.00  9.61           C  
ATOM   2473  O   PRO A 326     103.799 174.362 165.079  1.00  9.61           O  
ATOM   2474  CB  PRO A 326     106.667 175.551 165.557  1.00  9.61           C  
ATOM   2475  CG  PRO A 326     108.073 175.721 165.192  1.00  9.61           C  
ATOM   2476  CD  PRO A 326     108.205 175.348 163.754  1.00  9.61           C  
ATOM   2477  N   LEU A 327     104.418 175.244 163.106  1.00 10.08           N  
ATOM   2478  CA  LEU A 327     103.045 175.564 162.725  1.00 10.08           C  
ATOM   2479  C   LEU A 327     102.187 174.327 162.459  1.00 10.08           C  
ATOM   2480  O   LEU A 327     100.960 174.452 162.418  1.00 10.08           O  
ATOM   2481  CB  LEU A 327     103.035 176.471 161.486  1.00 10.08           C  
ATOM   2482  CG  LEU A 327     103.454 177.937 161.648  1.00 10.08           C  
ATOM   2483  CD1 LEU A 327     103.394 178.670 160.314  1.00 10.08           C  
ATOM   2484  CD2 LEU A 327     102.604 178.656 162.675  1.00 10.08           C  
ATOM   2485  N   VAL A 328     102.785 173.145 162.291  1.00  9.11           N  
ATOM   2486  CA  VAL A 328     102.069 171.948 161.847  1.00  9.11           C  
ATOM   2487  C   VAL A 328     102.448 170.775 162.744  1.00  9.11           C  
ATOM   2488  O   VAL A 328     103.610 170.353 162.768  1.00  9.11           O  
ATOM   2489  CB  VAL A 328     102.357 171.613 160.372  1.00  9.11           C  
ATOM   2490  CG1 VAL A 328     101.598 170.363 159.946  1.00  9.11           C  
ATOM   2491  CG2 VAL A 328     101.990 172.782 159.483  1.00  9.11           C  
ATOM   2492  N   LEU A 329     101.460 170.242 163.462  1.00 10.20           N  
ATOM   2493  CA  LEU A 329     101.637 169.110 164.377  1.00 10.20           C  
ATOM   2494  C   LEU A 329     102.734 169.385 165.407  1.00 10.20           C  
ATOM   2495  O   LEU A 329     103.483 168.490 165.798  1.00 10.20           O  
ATOM   2496  CB  LEU A 329     101.921 167.810 163.615  1.00 10.20           C  
ATOM   2497  CG  LEU A 329     100.852 167.273 162.658  1.00 10.20           C  
ATOM   2498  CD1 LEU A 329     101.359 166.041 161.922  1.00 10.20           C  
ATOM   2499  CD2 LEU A 329      99.566 166.952 163.390  1.00 10.20           C  
ATOM   2500  N   ALA A 330     102.824 170.634 165.857  1.00 10.32           N  
ATOM   2501  CA  ALA A 330     103.775 171.081 166.871  1.00 10.32           C  
ATOM   2502  C   ALA A 330     105.225 170.802 166.488  1.00 10.32           C  
ATOM   2503  O   ALA A 330     106.111 170.877 167.345  1.00 10.32           O  
ATOM   2504  CB  ALA A 330     103.473 170.450 168.237  1.00 10.32           C  
ATOM   2505  N   GLY A 331     105.492 170.495 165.222  1.00  8.72           N  
ATOM   2506  CA  GLY A 331     106.832 170.171 164.782  1.00  8.72           C  
ATOM   2507  C   GLY A 331     107.303 168.781 165.133  1.00  8.72           C  
ATOM   2508  O   GLY A 331     108.511 168.536 165.133  1.00  8.72           O  
ATOM   2509  N   VAL A 332     106.387 167.854 165.413  1.00 10.37           N  
ATOM   2510  CA  VAL A 332     106.787 166.491 165.740  1.00 10.37           C  
ATOM   2511  C   VAL A 332     107.295 165.787 164.487  1.00 10.37           C  
ATOM   2512  O   VAL A 332     107.007 166.179 163.352  1.00 10.37           O  
ATOM   2513  CB  VAL A 332     105.631 165.700 166.376  1.00 10.37           C  
ATOM   2514  CG1 VAL A 332     105.130 166.373 167.643  1.00 10.37           C  
ATOM   2515  CG2 VAL A 332     104.509 165.491 165.371  1.00 10.37           C  
ATOM   2516  N   LEU A 333     108.063 164.726 164.704  1.00 10.29           N  
ATOM   2517  CA  LEU A 333     108.455 163.821 163.636  1.00 10.29           C  
ATOM   2518  C   LEU A 333     107.447 162.683 163.525  1.00 10.29           C  
ATOM   2519  O   LEU A 333     107.017 162.115 164.532  1.00 10.29           O  
ATOM   2520  CB  LEU A 333     109.849 163.246 163.880  1.00 10.29           C  
ATOM   2521  CG  LEU A 333     111.075 164.100 163.549  1.00 10.29           C  
ATOM   2522  CD1 LEU A 333     112.351 163.392 163.984  1.00 10.29           C  
ATOM   2523  CD2 LEU A 333     111.130 164.439 162.062  1.00 10.29           C  
ATOM   2524  N   ASP A 334     107.075 162.359 162.292  1.00 10.26           N  
ATOM   2525  CA  ASP A 334     106.183 161.248 161.998  1.00 10.26           C  
ATOM   2526  C   ASP A 334     106.721 160.502 160.782  1.00 10.26           C  
ATOM   2527  O   ASP A 334     107.732 160.888 160.188  1.00 10.26           O  
ATOM   2528  CB  ASP A 334     104.744 161.742 161.795  1.00 10.26           C  
ATOM   2529  CG  ASP A 334     104.553 162.486 160.488  1.00 10.26           C  
ATOM   2530  OD1 ASP A 334     105.548 162.989 159.930  1.00 10.26           O  
ATOM   2531  OD2 ASP A 334     103.397 162.577 160.026  1.00 10.26           O  
ATOM   2532  N   SER A 335     106.037 159.418 160.411  1.00  9.05           N  
ATOM   2533  CA  SER A 335     106.538 158.545 159.352  1.00  9.05           C  
ATOM   2534  C   SER A 335     106.710 159.309 158.038  1.00  9.05           C  
ATOM   2535  O   SER A 335     107.764 159.233 157.388  1.00  9.05           O  
ATOM   2536  CB  SER A 335     105.591 157.353 159.177  1.00  9.05           C  
ATOM   2537  OG  SER A 335     105.549 156.558 160.347  1.00  9.05           O  
ATOM   2538  N   ASP A 336     105.683 160.069 157.649  1.00  9.48           N  
ATOM   2539  CA  ASP A 336     105.716 160.808 156.389  1.00  9.48           C  
ATOM   2540  C   ASP A 336     106.877 161.800 156.356  1.00  9.48           C  
ATOM   2541  O   ASP A 336     107.645 161.844 155.387  1.00  9.48           O  
ATOM   2542  CB  ASP A 336     104.379 161.520 156.175  1.00  9.48           C  
ATOM   2543  CG  ASP A 336     103.254 160.561 155.828  1.00  9.48           C  
ATOM   2544  OD1 ASP A 336     103.503 159.340 155.769  1.00  9.48           O  
ATOM   2545  OD2 ASP A 336     102.116 161.026 155.622  1.00  9.48           O  
ATOM   2546  N   ALA A 337     107.014 162.611 157.410  1.00  7.23           N  
ATOM   2547  CA  ALA A 337     108.087 163.599 157.462  1.00  7.23           C  
ATOM   2548  C   ALA A 337     109.456 162.933 157.440  1.00  7.23           C  
ATOM   2549  O   ALA A 337     110.390 163.430 156.799  1.00  7.23           O  
ATOM   2550  CB  ALA A 337     107.940 164.470 158.707  1.00  7.23           C  
ATOM   2551  N   SER A 338     109.590 161.804 158.135  1.00  8.26           N  
ATOM   2552  CA  SER A 338     110.857 161.084 158.148  1.00  8.26           C  
ATOM   2553  C   SER A 338     111.252 160.645 156.743  1.00  8.26           C  
ATOM   2554  O   SER A 338     112.394 160.848 156.320  1.00  8.26           O  
ATOM   2555  CB  SER A 338     110.771 159.890 159.097  1.00  8.26           C  
ATOM   2556  OG  SER A 338     110.656 160.325 160.437  1.00  8.26           O  
ATOM   2557  N   ARG A 339     110.317 160.050 155.999  1.00  9.66           N  
ATOM   2558  CA  ARG A 339     110.622 159.636 154.629  1.00  9.66           C  
ATOM   2559  C   ARG A 339     110.978 160.844 153.758  1.00  9.66           C  
ATOM   2560  O   ARG A 339     111.978 160.830 153.014  1.00  9.66           O  
ATOM   2561  CB  ARG A 339     109.433 158.853 154.058  1.00  9.66           C  
ATOM   2562  CG  ARG A 339     109.283 157.446 154.645  1.00  9.66           C  
ATOM   2563  CD  ARG A 339     108.088 156.675 154.096  1.00  9.66           C  
ATOM   2564  NE  ARG A 339     107.974 156.798 152.649  1.00  9.66           N  
ATOM   2565  CZ  ARG A 339     106.828 156.798 151.978  1.00  9.66           C  
ATOM   2566  NH1 ARG A 339     105.669 156.678 152.609  1.00  9.66           N  
ATOM   2567  NH2 ARG A 339     106.844 156.918 150.662  1.00  9.66           N  
ATOM   2568  N   LYS A 340     110.171 161.909 153.859  1.00 12.77           N  
ATOM   2569  CA  LYS A 340     110.418 163.136 153.104  1.00 12.77           C  
ATOM   2570  C   LYS A 340     111.840 163.638 153.320  1.00 12.77           C  
ATOM   2571  O   LYS A 340     112.546 163.970 152.364  1.00 12.77           O  
ATOM   2572  CB  LYS A 340     109.389 164.211 153.498  1.00 12.77           C  
ATOM   2573  CG  LYS A 340     109.658 165.623 152.972  1.00 12.77           C  
ATOM   2574  CD  LYS A 340     108.477 166.578 153.216  1.00 12.77           C  
ATOM   2575  CE  LYS A 340     108.783 168.025 152.838  1.00 12.77           C  
ATOM   2576  NZ  LYS A 340     107.683 168.950 153.218  1.00 12.77           N  
ATOM   2577  N   ALA A 341     112.280 163.692 154.578  1.00  7.00           N  
ATOM   2578  CA  ALA A 341     113.605 164.228 154.879  1.00  7.00           C  
ATOM   2579  C   ALA A 341     114.712 163.255 154.472  1.00  7.00           C  
ATOM   2580  O   ALA A 341     115.776 163.677 153.998  1.00  7.00           O  
ATOM   2581  CB  ALA A 341     113.698 164.573 156.365  1.00  7.00           C  
ATOM   2582  N   ALA A 342     114.481 161.953 154.649  1.00  6.77           N  
ATOM   2583  CA  ALA A 342     115.522 160.961 154.390  1.00  6.77           C  
ATOM   2584  C   ALA A 342     115.923 160.948 152.918  1.00  6.77           C  
ATOM   2585  O   ALA A 342     117.118 160.924 152.588  1.00  6.77           O  
ATOM   2586  CB  ALA A 342     115.055 159.575 154.839  1.00  6.77           C  
ATOM   2587  N   ARG A 343     114.941 160.974 152.010  1.00 16.24           N  
ATOM   2588  CA  ARG A 343     115.311 160.939 150.590  1.00 16.24           C  
ATOM   2589  C   ARG A 343     116.061 162.207 150.166  1.00 16.24           C  
ATOM   2590  O   ARG A 343     117.013 162.139 149.377  1.00 16.24           O  
ATOM   2591  CB  ARG A 343     114.089 160.718 149.698  1.00 16.24           C  
ATOM   2592  CG  ARG A 343     114.466 160.421 148.234  1.00 16.24           C  
ATOM   2593  CD  ARG A 343     113.686 159.271 147.639  1.00 16.24           C  
ATOM   2594  NE  ARG A 343     114.284 158.765 146.403  1.00 16.24           N  
ATOM   2595  CZ  ARG A 343     113.829 159.013 145.180  1.00 16.24           C  
ATOM   2596  NH1 ARG A 343     112.769 159.780 144.993  1.00 16.24           N  
ATOM   2597  NH2 ARG A 343     114.446 158.491 144.134  1.00 16.24           N  
ATOM   2598  N   PHE A 344     115.648 163.369 150.676  1.00 12.77           N  
ATOM   2599  CA  PHE A 344     116.337 164.620 150.366  1.00 12.77           C  
ATOM   2600  C   PHE A 344     117.783 164.597 150.855  1.00 12.77           C  
ATOM   2601  O   PHE A 344     118.699 165.017 150.134  1.00 12.77           O  
ATOM   2602  CB  PHE A 344     115.570 165.796 150.979  1.00 12.77           C  
ATOM   2603  CG  PHE A 344     116.123 167.147 150.624  1.00 12.77           C  
ATOM   2604  CD1 PHE A 344     115.834 167.734 149.407  1.00 12.77           C  
ATOM   2605  CD2 PHE A 344     116.918 167.841 151.514  1.00 12.77           C  
ATOM   2606  CE1 PHE A 344     116.339 168.976 149.089  1.00 12.77           C  
ATOM   2607  CE2 PHE A 344     117.418 169.080 151.193  1.00 12.77           C  
ATOM   2608  CZ  PHE A 344     117.127 169.644 149.982  1.00 12.77           C  
ATOM   2609  N   VAL A 345     118.009 164.116 152.080  1.00 12.77           N  
ATOM   2610  CA  VAL A 345     119.373 164.028 152.598  1.00 12.77           C  
ATOM   2611  C   VAL A 345     120.210 163.090 151.738  1.00 12.77           C  
ATOM   2612  O   VAL A 345     121.375 163.379 151.433  1.00 12.77           O  
ATOM   2613  CB  VAL A 345     119.366 163.587 154.075  1.00 12.77           C  
ATOM   2614  CG1 VAL A 345     120.763 163.164 154.522  1.00 12.77           C  
ATOM   2615  CG2 VAL A 345     118.828 164.697 154.972  1.00 12.77           C  
ATOM   2616  N   ARG A 346     119.635 161.955 151.336  1.00 12.77           N  
ATOM   2617  CA  ARG A 346     120.371 161.019 150.492  1.00 12.77           C  
ATOM   2618  C   ARG A 346     120.764 161.668 149.167  1.00 12.77           C  
ATOM   2619  O   ARG A 346     121.904 161.518 148.709  1.00 12.77           O  
ATOM   2620  CB  ARG A 346     119.539 159.756 150.266  1.00 12.77           C  
ATOM   2621  CG  ARG A 346     119.326 158.902 151.522  1.00 12.77           C  
ATOM   2622  CD  ARG A 346     120.288 157.749 151.612  1.00 12.77           C  
ATOM   2623  NE  ARG A 346     120.023 156.745 150.588  1.00 12.77           N  
ATOM   2624  CZ  ARG A 346     120.618 155.561 150.526  1.00 12.77           C  
ATOM   2625  NH1 ARG A 346     121.510 155.208 151.433  1.00 12.77           N  
ATOM   2626  NH2 ARG A 346     120.312 154.724 149.551  1.00 12.77           N  
ATOM   2627  N   PHE A 347     119.848 162.421 148.552  1.00 12.77           N  
ATOM   2628  CA  PHE A 347     120.176 163.072 147.283  1.00 12.77           C  
ATOM   2629  C   PHE A 347     121.281 164.106 147.466  1.00 12.77           C  
ATOM   2630  O   PHE A 347     122.213 164.178 146.657  1.00 12.77           O  
ATOM   2631  CB  PHE A 347     118.940 163.720 146.656  1.00 12.77           C  
ATOM   2632  CG  PHE A 347     119.245 164.523 145.416  1.00 12.77           C  
ATOM   2633  CD1 PHE A 347     119.655 165.837 145.507  1.00 12.77           C  
ATOM   2634  CD2 PHE A 347     119.143 163.954 144.161  1.00 12.77           C  
ATOM   2635  CE1 PHE A 347     119.942 166.566 144.373  1.00 12.77           C  
ATOM   2636  CE2 PHE A 347     119.426 164.681 143.030  1.00 12.77           C  
ATOM   2637  CZ  PHE A 347     119.829 165.984 143.137  1.00 12.77           C  
ATOM   2638  N   CYS A 348     121.188 164.927 148.514  1.00 12.77           N  
ATOM   2639  CA  CYS A 348     122.236 165.911 148.766  1.00 12.77           C  
ATOM   2640  C   CYS A 348     123.591 165.240 148.960  1.00 12.77           C  
ATOM   2641  O   CYS A 348     124.605 165.712 148.434  1.00 12.77           O  
ATOM   2642  CB  CYS A 348     121.879 166.766 149.982  1.00 12.77           C  
ATOM   2643  SG  CYS A 348     120.353 167.687 149.811  1.00 12.77           S  
ATOM   2644  N   ASN A 349     123.629 164.132 149.698  1.00 12.77           N  
ATOM   2645  CA  ASN A 349     124.902 163.460 149.944  1.00 12.77           C  
ATOM   2646  C   ASN A 349     125.474 162.858 148.662  1.00 12.77           C  
ATOM   2647  O   ASN A 349     126.682 162.942 148.420  1.00 12.77           O  
ATOM   2648  CB  ASN A 349     124.731 162.386 151.017  1.00 12.77           C  
ATOM   2649  CG  ASN A 349     126.058 161.826 151.500  1.00 12.77           C  
ATOM   2650  OD1 ASN A 349     126.969 162.571 151.848  1.00 12.77           O  
ATOM   2651  ND2 ASN A 349     126.170 160.510 151.513  1.00 12.77           N  
ATOM   2652  N   ALA A 350     124.625 162.257 147.826  1.00 12.77           N  
ATOM   2653  CA  ALA A 350     125.116 161.603 146.611  1.00 12.77           C  
ATOM   2654  C   ALA A 350     125.840 162.582 145.685  1.00 12.77           C  
ATOM   2655  O   ALA A 350     126.842 162.222 145.060  1.00 12.77           O  
ATOM   2656  CB  ALA A 350     123.964 160.924 145.870  1.00 12.77           C  
ATOM   2657  N   PHE A 351     125.348 163.817 145.580  1.00 12.77           N  
ATOM   2658  CA  PHE A 351     125.863 164.801 144.634  1.00 12.77           C  
ATOM   2659  C   PHE A 351     126.666 165.920 145.306  1.00 12.77           C  
ATOM   2660  O   PHE A 351     126.870 166.977 144.704  1.00 12.77           O  
ATOM   2661  CB  PHE A 351     124.704 165.374 143.813  1.00 12.77           C  
ATOM   2662  CG  PHE A 351     124.123 164.395 142.818  1.00 12.77           C  
ATOM   2663  CD1 PHE A 351     124.739 164.171 141.602  1.00 12.77           C  
ATOM   2664  CD2 PHE A 351     122.968 163.695 143.098  1.00 12.77           C  
ATOM   2665  CE1 PHE A 351     124.220 163.279 140.703  1.00 12.77           C  
ATOM   2666  CE2 PHE A 351     122.451 162.800 142.193  1.00 12.77           C  
ATOM   2667  CZ  PHE A 351     123.077 162.594 140.999  1.00 12.77           C  
ATOM   2668  N   SER A 352     127.126 165.708 146.540  1.00  8.88           N  
ATOM   2669  CA  SER A 352     128.067 166.605 147.224  1.00  8.88           C  
ATOM   2670  C   SER A 352     127.476 167.998 147.473  1.00  8.88           C  
ATOM   2671  O   SER A 352     128.122 169.019 147.240  1.00  8.88           O  
ATOM   2672  CB  SER A 352     129.387 166.707 146.448  1.00  8.88           C  
ATOM   2673  OG  SER A 352     130.229 165.609 146.722  1.00  8.88           O  
ATOM   2674  N   ILE A 353     126.251 168.034 147.980  1.00 12.77           N  
ATOM   2675  CA  ILE A 353     125.561 169.265 148.360  1.00 12.77           C  
ATOM   2676  C   ILE A 353     125.569 169.353 149.886  1.00 12.77           C  
ATOM   2677  O   ILE A 353     125.089 168.427 150.552  1.00 12.77           O  
ATOM   2678  CB  ILE A 353     124.124 169.312 147.806  1.00 12.77           C  
ATOM   2679  CG1 ILE A 353     124.120 169.152 146.278  1.00 12.77           C  
ATOM   2680  CG2 ILE A 353     123.423 170.618 148.191  1.00 12.77           C  
ATOM   2681  CD1 ILE A 353     122.741 169.051 145.663  1.00 12.77           C  
ATOM   2682  N   PRO A 354     126.106 170.417 150.484  1.00  7.92           N  
ATOM   2683  CA  PRO A 354     126.089 170.529 151.950  1.00  7.92           C  
ATOM   2684  C   PRO A 354     124.678 170.719 152.490  1.00  7.92           C  
ATOM   2685  O   PRO A 354     123.771 171.171 151.791  1.00  7.92           O  
ATOM   2686  CB  PRO A 354     126.962 171.755 152.233  1.00  7.92           C  
ATOM   2687  CG  PRO A 354     127.033 172.497 150.975  1.00  7.92           C  
ATOM   2688  CD  PRO A 354     126.813 171.544 149.854  1.00  7.92           C  
ATOM   2689  N   ILE A 355     124.508 170.373 153.767  1.00 12.77           N  
ATOM   2690  CA  ILE A 355     123.203 170.350 154.425  1.00 12.77           C  
ATOM   2691  C   ILE A 355     123.234 171.196 155.702  1.00 12.77           C  
ATOM   2692  O   ILE A 355     124.140 171.055 156.538  1.00 12.77           O  
ATOM   2693  CB  ILE A 355     122.744 168.913 154.747  1.00 12.77           C  
ATOM   2694  CG1 ILE A 355     122.630 168.054 153.475  1.00 12.77           C  
ATOM   2695  CG2 ILE A 355     121.402 168.940 155.464  1.00 12.77           C  
ATOM   2696  CD1 ILE A 355     122.612 166.574 153.746  1.00 12.77           C  
ATOM   2697  N   VAL A 356     122.228 172.064 155.848  1.00 12.77           N  
ATOM   2698  CA  VAL A 356     121.976 172.840 157.063  1.00 12.77           C  
ATOM   2699  C   VAL A 356     120.627 172.418 157.651  1.00 12.77           C  
ATOM   2700  O   VAL A 356     119.624 172.344 156.928  1.00 12.77           O  
ATOM   2701  CB  VAL A 356     122.000 174.357 156.786  1.00 12.77           C  
ATOM   2702  CG1 VAL A 356     121.599 175.153 158.028  1.00 12.77           C  
ATOM   2703  CG2 VAL A 356     123.369 174.795 156.292  1.00 12.77           C  
ATOM   2704  N   THR A 357     120.608 172.141 158.960  1.00  7.88           N  
ATOM   2705  CA  THR A 357     119.420 171.671 159.675  1.00  7.88           C  
ATOM   2706  C   THR A 357     119.048 172.617 160.818  1.00  7.88           C  
ATOM   2707  O   THR A 357     119.910 172.999 161.617  1.00  7.88           O  
ATOM   2708  CB  THR A 357     119.636 170.248 160.217  1.00  7.88           C  
ATOM   2709  OG1 THR A 357     120.019 169.377 159.147  1.00  7.88           O  
ATOM   2710  CG2 THR A 357     118.372 169.713 160.877  1.00  7.88           C  
ATOM   2711  N   PHE A 358     117.764 172.997 160.879  1.00  6.22           N  
ATOM   2712  CA  PHE A 358     117.188 173.797 161.965  1.00  6.22           C  
ATOM   2713  C   PHE A 358     116.221 172.945 162.795  1.00  6.22           C  
ATOM   2714  O   PHE A 358     115.237 172.402 162.263  1.00  6.22           O  
ATOM   2715  CB  PHE A 358     116.468 175.040 161.431  1.00  6.22           C  
ATOM   2716  CG  PHE A 358     117.379 176.068 160.806  1.00  6.22           C  
ATOM   2717  CD1 PHE A 358     118.137 176.920 161.587  1.00  6.22           C  
ATOM   2718  CD2 PHE A 358     117.452 176.199 159.435  1.00  6.22           C  
ATOM   2719  CE1 PHE A 358     118.958 177.859 161.007  1.00  6.22           C  
ATOM   2720  CE2 PHE A 358     118.270 177.138 158.859  1.00  6.22           C  
ATOM   2721  CZ  PHE A 358     119.022 177.964 159.640  1.00  6.22           C  
ATOM   2722  N   VAL A 359     116.474 172.883 164.105  1.00  5.80           N  
ATOM   2723  CA  VAL A 359     115.840 171.920 165.004  1.00  5.80           C  
ATOM   2724  C   VAL A 359     114.907 172.639 165.974  1.00  5.80           C  
ATOM   2725  O   VAL A 359     115.326 173.542 166.709  1.00  5.80           O  
ATOM   2726  CB  VAL A 359     116.887 171.095 165.767  1.00  5.80           C  
ATOM   2727  CG1 VAL A 359     116.222 170.005 166.582  1.00  5.80           C  
ATOM   2728  CG2 VAL A 359     117.893 170.507 164.798  1.00  5.80           C  
ATOM   2729  N   ASP A 360     113.637 172.223 165.972  1.00 10.10           N  
ATOM   2730  CA  ASP A 360     112.658 172.558 167.011  1.00 10.10           C  
ATOM   2731  C   ASP A 360     111.683 171.378 167.082  1.00 10.10           C  
ATOM   2732  O   ASP A 360     110.671 171.356 166.379  1.00 10.10           O  
ATOM   2733  CB  ASP A 360     111.944 173.863 166.695  1.00 10.10           C  
ATOM   2734  CG  ASP A 360     111.087 174.366 167.847  1.00 10.10           C  
ATOM   2735  OD1 ASP A 360     110.819 173.595 168.790  1.00 10.10           O  
ATOM   2736  OD2 ASP A 360     110.671 175.539 167.801  1.00 10.10           O  
ATOM   2737  N   VAL A 361     111.979 170.420 167.957  1.00  7.79           N  
ATOM   2738  CA  VAL A 361     111.290 169.131 167.922  1.00  7.79           C  
ATOM   2739  C   VAL A 361     110.969 168.634 169.330  1.00  7.79           C  
ATOM   2740  O   VAL A 361     111.880 168.441 170.145  1.00  7.79           O  
ATOM   2741  CB  VAL A 361     112.112 168.096 167.134  1.00  7.79           C  
ATOM   2742  CG1 VAL A 361     113.444 167.786 167.813  1.00  7.79           C  
ATOM   2743  CG2 VAL A 361     111.306 166.832 166.930  1.00  7.79           C  
ATOM   2744  N   PRO A 362     109.693 168.430 169.660  1.00 10.60           N  
ATOM   2745  CA  PRO A 362     109.316 167.936 170.991  1.00 10.60           C  
ATOM   2746  C   PRO A 362     109.259 166.423 171.137  1.00 10.60           C  
ATOM   2747  O   PRO A 362     109.021 165.945 172.250  1.00 10.60           O  
ATOM   2748  CB  PRO A 362     107.918 168.538 171.167  1.00 10.60           C  
ATOM   2749  CG  PRO A 362     107.366 168.574 169.814  1.00 10.60           C  
ATOM   2750  CD  PRO A 362     108.507 168.816 168.877  1.00 10.60           C  
ATOM   2751  N   GLY A 363     109.460 165.665 170.067  1.00 10.21           N  
ATOM   2752  CA  GLY A 363     109.398 164.221 170.113  1.00 10.21           C  
ATOM   2753  C   GLY A 363     108.769 163.652 168.852  1.00 10.21           C  
ATOM   2754  O   GLY A 363     108.782 164.283 167.798  1.00 10.21           O  
ATOM   2755  N   PHE A 364     108.228 162.438 168.974  1.00 10.65           N  
ATOM   2756  CA  PHE A 364     107.543 161.729 167.900  1.00 10.65           C  
ATOM   2757  C   PHE A 364     106.032 161.756 168.116  1.00 10.65           C  
ATOM   2758  O   PHE A 364     105.547 161.990 169.224  1.00 10.65           O  
ATOM   2759  CB  PHE A 364     108.018 160.272 167.808  1.00 10.65           C  
ATOM   2760  CG  PHE A 364     109.499 160.125 167.635  1.00 10.65           C  
ATOM   2761  CD1 PHE A 364     110.330 160.056 168.733  1.00 10.65           C  
ATOM   2762  CD2 PHE A 364     110.060 160.053 166.377  1.00 10.65           C  
ATOM   2763  CE1 PHE A 364     111.688 159.928 168.581  1.00 10.65           C  
ATOM   2764  CE2 PHE A 364     111.419 159.927 166.221  1.00 10.65           C  
ATOM   2765  CZ  PHE A 364     112.232 159.864 167.325  1.00 10.65           C  
ATOM   2766  N   LEU A 365     105.292 161.504 167.036  1.00 11.60           N  
ATOM   2767  CA  LEU A 365     103.830 161.508 167.086  1.00 11.60           C  
ATOM   2768  C   LEU A 365     103.324 160.198 167.687  1.00 11.60           C  
ATOM   2769  O   LEU A 365     103.627 159.128 167.149  1.00 11.60           O  
ATOM   2770  CB  LEU A 365     103.247 161.703 165.687  1.00 11.60           C  
ATOM   2771  CG  LEU A 365     101.722 161.805 165.565  1.00 11.60           C  
ATOM   2772  CD1 LEU A 365     101.182 163.040 166.255  1.00 11.60           C  
ATOM   2773  CD2 LEU A 365     101.290 161.787 164.111  1.00 11.60           C  
ATOM   2774  N   PRO A 366     102.563 160.229 168.781  1.00 15.16           N  
ATOM   2775  CA  PRO A 366     102.088 158.987 169.398  1.00 15.16           C  
ATOM   2776  C   PRO A 366     100.797 158.462 168.783  1.00 15.16           C  
ATOM   2777  O   PRO A 366     100.023 159.189 168.160  1.00 15.16           O  
ATOM   2778  CB  PRO A 366     101.854 159.385 170.862  1.00 15.16           C  
ATOM   2779  CG  PRO A 366     101.762 160.846 170.886  1.00 15.16           C  
ATOM   2780  CD  PRO A 366     102.225 161.412 169.589  1.00 15.16           C  
ATOM   2781  N   GLY A 367     100.579 157.163 168.985  1.00 13.58           N  
ATOM   2782  CA  GLY A 367      99.321 156.529 168.639  1.00 13.58           C  
ATOM   2783  C   GLY A 367      99.439 155.207 167.905  1.00 13.58           C  
ATOM   2784  O   GLY A 367     100.455 154.920 167.267  1.00 13.58           O  
ATOM   2785  N   THR A 368      98.387 154.391 167.998  1.00 13.16           N  
ATOM   2786  CA  THR A 368      98.352 153.123 167.279  1.00 13.16           C  
ATOM   2787  C   THR A 368      98.530 153.321 165.780  1.00 13.16           C  
ATOM   2788  O   THR A 368      99.146 152.488 165.110  1.00 13.16           O  
ATOM   2789  CB  THR A 368      97.039 152.394 167.554  1.00 13.16           C  
ATOM   2790  OG1 THR A 368      95.940 153.245 167.216  1.00 13.16           O  
ATOM   2791  CG2 THR A 368      96.945 151.985 169.011  1.00 13.16           C  
ATOM   2792  N   ALA A 369      97.962 154.394 165.228  1.00 10.97           N  
ATOM   2793  CA  ALA A 369      98.110 154.657 163.800  1.00 10.97           C  
ATOM   2794  C   ALA A 369      99.578 154.665 163.392  1.00 10.97           C  
ATOM   2795  O   ALA A 369      99.966 154.022 162.412  1.00 10.97           O  
ATOM   2796  CB  ALA A 369      97.445 155.984 163.432  1.00 10.97           C  
ATOM   2797  N   GLN A 370     100.411 155.384 164.144  1.00 10.88           N  
ATOM   2798  CA  GLN A 370     101.820 155.493 163.787  1.00 10.88           C  
ATOM   2799  C   GLN A 370     102.546 154.163 163.969  1.00 10.88           C  
ATOM   2800  O   GLN A 370     103.340 153.765 163.112  1.00 10.88           O  
ATOM   2801  CB  GLN A 370     102.485 156.595 164.615  1.00 10.88           C  
ATOM   2802  CG  GLN A 370     102.265 158.005 164.097  1.00 10.88           C  
ATOM   2803  CD  GLN A 370     102.900 158.242 162.742  1.00 10.88           C  
ATOM   2804  OE1 GLN A 370     104.118 158.177 162.592  1.00 10.88           O  
ATOM   2805  NE2 GLN A 370     102.074 158.514 161.749  1.00 10.88           N  
ATOM   2806  N   GLU A 371     102.286 153.459 165.073  1.00 12.95           N  
ATOM   2807  CA  GLU A 371     102.995 152.209 165.340  1.00 12.95           C  
ATOM   2808  C   GLU A 371     102.620 151.133 164.326  1.00 12.95           C  
ATOM   2809  O   GLU A 371     103.495 150.476 163.753  1.00 12.95           O  
ATOM   2810  CB  GLU A 371     102.706 151.722 166.761  1.00 12.95           C  
ATOM   2811  CG  GLU A 371     103.201 152.629 167.877  1.00 12.95           C  
ATOM   2812  CD  GLU A 371     104.701 152.885 167.840  1.00 12.95           C  
ATOM   2813  OE1 GLU A 371     105.431 152.126 167.173  1.00 12.95           O  
ATOM   2814  OE2 GLU A 371     105.151 153.849 168.494  1.00 12.95           O  
ATOM   2815  N   TYR A 372     101.320 150.938 164.097  1.00 12.99           N  
ATOM   2816  CA  TYR A 372     100.855 149.923 163.160  1.00 12.99           C  
ATOM   2817  C   TYR A 372     101.298 150.216 161.733  1.00 12.99           C  
ATOM   2818  O   TYR A 372     101.377 149.290 160.920  1.00 12.99           O  
ATOM   2819  CB  TYR A 372      99.326 149.813 163.203  1.00 12.99           C  
ATOM   2820  CG  TYR A 372      98.725 149.332 164.511  1.00 12.99           C  
ATOM   2821  CD1 TYR A 372      99.513 148.845 165.544  1.00 12.99           C  
ATOM   2822  CD2 TYR A 372      97.352 149.362 164.704  1.00 12.99           C  
ATOM   2823  CE1 TYR A 372      98.950 148.410 166.724  1.00 12.99           C  
ATOM   2824  CE2 TYR A 372      96.786 148.931 165.877  1.00 12.99           C  
ATOM   2825  CZ  TYR A 372      97.585 148.455 166.884  1.00 12.99           C  
ATOM   2826  OH  TYR A 372      97.007 148.027 168.053  1.00 12.99           O  
ATOM   2827  N   GLY A 373     101.575 151.476 161.413  1.00 12.31           N  
ATOM   2828  CA  GLY A 373     102.098 151.873 160.125  1.00 12.31           C  
ATOM   2829  C   GLY A 373     103.601 151.808 159.967  1.00 12.31           C  
ATOM   2830  O   GLY A 373     104.102 152.121 158.885  1.00 12.31           O  
ATOM   2831  N   GLY A 374     104.338 151.429 161.008  1.00 10.08           N  
ATOM   2832  CA  GLY A 374     105.761 151.187 160.877  1.00 10.08           C  
ATOM   2833  C   GLY A 374     106.679 152.335 161.236  1.00 10.08           C  
ATOM   2834  O   GLY A 374     107.764 152.444 160.656  1.00 10.08           O  
ATOM   2835  N   LEU A 375     106.292 153.185 162.192  1.00  9.34           N  
ATOM   2836  CA  LEU A 375     107.106 154.348 162.542  1.00  9.34           C  
ATOM   2837  C   LEU A 375     108.531 153.972 162.930  1.00  9.34           C  
ATOM   2838  O   LEU A 375     109.451 154.760 162.717  1.00  9.34           O  
ATOM   2839  CB  LEU A 375     106.446 155.126 163.679  1.00  9.34           C  
ATOM   2840  CG  LEU A 375     107.251 156.272 164.296  1.00  9.34           C  
ATOM   2841  CD1 LEU A 375     107.634 157.302 163.243  1.00  9.34           C  
ATOM   2842  CD2 LEU A 375     106.481 156.918 165.438  1.00  9.34           C  
ATOM   2843  N   ILE A 376     108.734 152.797 163.522  1.00  9.67           N  
ATOM   2844  CA  ILE A 376     110.079 152.386 163.935  1.00  9.67           C  
ATOM   2845  C   ILE A 376     111.043 152.471 162.747  1.00  9.67           C  
ATOM   2846  O   ILE A 376     112.015 153.243 162.754  1.00  9.67           O  
ATOM   2847  CB  ILE A 376     110.031 150.979 164.563  1.00  9.67           C  
ATOM   2848  CG1 ILE A 376     109.325 151.033 165.929  1.00  9.67           C  
ATOM   2849  CG2 ILE A 376     111.420 150.373 164.716  1.00  9.67           C  
ATOM   2850  CD1 ILE A 376     108.918 149.694 166.479  1.00  9.67           C  
ATOM   2851  N   LYS A 377     110.736 151.740 161.672  1.00 10.13           N  
ATOM   2852  CA  LYS A 377     111.614 151.718 160.500  1.00 10.13           C  
ATOM   2853  C   LYS A 377     111.618 153.062 159.764  1.00 10.13           C  
ATOM   2854  O   LYS A 377     112.681 153.547 159.336  1.00 10.13           O  
ATOM   2855  CB  LYS A 377     111.187 150.583 159.561  1.00 10.13           C  
ATOM   2856  CG  LYS A 377     111.766 149.202 159.910  1.00 10.13           C  
ATOM   2857  CD  LYS A 377     111.505 148.158 158.813  1.00 10.13           C  
ATOM   2858  CE  LYS A 377     111.802 146.744 159.297  1.00 10.13           C  
ATOM   2859  NZ  LYS A 377     111.294 145.670 158.396  1.00 10.13           N  
ATOM   2860  N   HIS A 378     110.444 153.677 159.598  1.00  9.20           N  
ATOM   2861  CA  HIS A 378     110.367 154.943 158.873  1.00  9.20           C  
ATOM   2862  C   HIS A 378     111.205 156.017 159.554  1.00  9.20           C  
ATOM   2863  O   HIS A 378     111.940 156.757 158.892  1.00  9.20           O  
ATOM   2864  CB  HIS A 378     108.910 155.395 158.745  1.00  9.20           C  
ATOM   2865  CG  HIS A 378     108.060 154.478 157.923  1.00  9.20           C  
ATOM   2866  ND1 HIS A 378     108.423 154.060 156.663  1.00  9.20           N  
ATOM   2867  CD2 HIS A 378     106.862 153.902 158.179  1.00  9.20           C  
ATOM   2868  CE1 HIS A 378     107.489 153.262 156.179  1.00  9.20           C  
ATOM   2869  NE2 HIS A 378     106.530 153.152 157.079  1.00  9.20           N  
ATOM   2870  N   GLY A 379     111.108 156.114 160.878  1.00  9.42           N  
ATOM   2871  CA  GLY A 379     111.955 157.029 161.618  1.00  9.42           C  
ATOM   2872  C   GLY A 379     113.424 156.685 161.489  1.00  9.42           C  
ATOM   2873  O   GLY A 379     114.268 157.572 161.344  1.00  9.42           O  
ATOM   2874  N   ALA A 380     113.752 155.392 161.532  1.00  8.60           N  
ATOM   2875  CA  ALA A 380     115.143 154.986 161.366  1.00  8.60           C  
ATOM   2876  C   ALA A 380     115.730 155.436 160.031  1.00  8.60           C  
ATOM   2877  O   ALA A 380     116.950 155.592 159.920  1.00  8.60           O  
ATOM   2878  CB  ALA A 380     115.254 153.473 161.503  1.00  8.60           C  
ATOM   2879  N   LYS A 381     114.894 155.611 159.003  1.00  8.91           N  
ATOM   2880  CA  LYS A 381     115.423 155.994 157.688  1.00  8.91           C  
ATOM   2881  C   LYS A 381     116.197 157.319 157.741  1.00  8.91           C  
ATOM   2882  O   LYS A 381     117.274 157.443 157.143  1.00  8.91           O  
ATOM   2883  CB  LYS A 381     114.291 156.063 156.655  1.00  8.91           C  
ATOM   2884  CG  LYS A 381     113.661 154.706 156.349  1.00  8.91           C  
ATOM   2885  CD  LYS A 381     112.567 154.773 155.300  1.00  8.91           C  
ATOM   2886  CE  LYS A 381     111.825 153.451 155.176  1.00  8.91           C  
ATOM   2887  NZ  LYS A 381     110.661 153.558 154.266  1.00  8.91           N  
ATOM   2888  N   LEU A 382     115.670 158.320 158.453  1.00 12.77           N  
ATOM   2889  CA  LEU A 382     116.360 159.604 158.575  1.00 12.77           C  
ATOM   2890  C   LEU A 382     117.640 159.483 159.399  1.00 12.77           C  
ATOM   2891  O   LEU A 382     118.678 160.057 159.037  1.00 12.77           O  
ATOM   2892  CB  LEU A 382     115.420 160.639 159.195  1.00 12.77           C  
ATOM   2893  CG  LEU A 382     115.844 162.108 159.212  1.00 12.77           C  
ATOM   2894  CD1 LEU A 382     116.262 162.616 157.841  1.00 12.77           C  
ATOM   2895  CD2 LEU A 382     114.720 162.963 159.780  1.00 12.77           C  
ATOM   2896  N   LEU A 383     117.573 158.778 160.533  1.00 12.77           N  
ATOM   2897  CA  LEU A 383     118.777 158.474 161.301  1.00 12.77           C  
ATOM   2898  C   LEU A 383     119.858 157.903 160.393  1.00 12.77           C  
ATOM   2899  O   LEU A 383     121.020 158.324 160.442  1.00 12.77           O  
ATOM   2900  CB  LEU A 383     118.425 157.488 162.423  1.00 12.77           C  
ATOM   2901  CG  LEU A 383     119.493 157.064 163.428  1.00 12.77           C  
ATOM   2902  CD1 LEU A 383     120.162 158.255 164.062  1.00 12.77           C  
ATOM   2903  CD2 LEU A 383     118.881 156.162 164.494  1.00 12.77           C  
ATOM   2904  N   PHE A 384     119.467 156.972 159.523  1.00 12.77           N  
ATOM   2905  CA  PHE A 384     120.400 156.318 158.614  1.00 12.77           C  
ATOM   2906  C   PHE A 384     121.001 157.320 157.635  1.00 12.77           C  
ATOM   2907  O   PHE A 384     122.227 157.394 157.472  1.00 12.77           O  
ATOM   2908  CB  PHE A 384     119.662 155.201 157.874  1.00 12.77           C  
ATOM   2909  CG  PHE A 384     120.536 154.068 157.421  1.00 12.77           C  
ATOM   2910  CD1 PHE A 384     121.357 154.207 156.327  1.00 12.77           C  
ATOM   2911  CD2 PHE A 384     120.509 152.852 158.074  1.00 12.77           C  
ATOM   2912  CE1 PHE A 384     122.145 153.165 155.905  1.00 12.77           C  
ATOM   2913  CE2 PHE A 384     121.294 151.811 157.651  1.00 12.77           C  
ATOM   2914  CZ  PHE A 384     122.110 151.969 156.568  1.00 12.77           C  
ATOM   2915  N   ALA A 385     120.145 158.110 156.981  1.00 12.77           N  
ATOM   2916  CA  ALA A 385     120.626 159.051 155.977  1.00 12.77           C  
ATOM   2917  C   ALA A 385     121.630 160.026 156.575  1.00 12.77           C  
ATOM   2918  O   ALA A 385     122.661 160.316 155.960  1.00 12.77           O  
ATOM   2919  CB  ALA A 385     119.453 159.802 155.351  1.00 12.77           C  
ATOM   2920  N   TYR A 386     121.353 160.543 157.775  1.00 12.77           N  
ATOM   2921  CA  TYR A 386     122.294 161.481 158.379  1.00 12.77           C  
ATOM   2922  C   TYR A 386     123.580 160.779 158.800  1.00 12.77           C  
ATOM   2923  O   TYR A 386     124.675 161.292 158.552  1.00 12.77           O  
ATOM   2924  CB  TYR A 386     121.668 162.195 159.575  1.00 12.77           C  
ATOM   2925  CG  TYR A 386     120.916 163.477 159.257  1.00 12.77           C  
ATOM   2926  CD1 TYR A 386     121.530 164.530 158.596  1.00 12.77           C  
ATOM   2927  CD2 TYR A 386     119.603 163.647 159.656  1.00 12.77           C  
ATOM   2928  CE1 TYR A 386     120.847 165.698 158.323  1.00 12.77           C  
ATOM   2929  CE2 TYR A 386     118.920 164.809 159.390  1.00 12.77           C  
ATOM   2930  CZ  TYR A 386     119.545 165.835 158.728  1.00 12.77           C  
ATOM   2931  OH  TYR A 386     118.868 166.996 158.460  1.00 12.77           O  
ATOM   2932  N   SER A 387     123.478 159.598 159.418  1.00  8.62           N  
ATOM   2933  CA  SER A 387     124.673 158.926 159.917  1.00  8.62           C  
ATOM   2934  C   SER A 387     125.598 158.473 158.795  1.00  8.62           C  
ATOM   2935  O   SER A 387     126.801 158.324 159.022  1.00  8.62           O  
ATOM   2936  CB  SER A 387     124.283 157.730 160.781  1.00  8.62           C  
ATOM   2937  OG  SER A 387     123.424 158.124 161.828  1.00  8.62           O  
ATOM   2938  N   GLN A 388     125.056 158.255 157.601  1.00  8.81           N  
ATOM   2939  CA  GLN A 388     125.825 157.832 156.436  1.00  8.81           C  
ATOM   2940  C   GLN A 388     126.551 158.976 155.735  1.00  8.81           C  
ATOM   2941  O   GLN A 388     127.503 158.723 154.991  1.00  8.81           O  
ATOM   2942  CB  GLN A 388     124.865 157.152 155.461  1.00  8.81           C  
ATOM   2943  CG  GLN A 388     125.417 156.680 154.176  1.00  8.81           C  
ATOM   2944  CD  GLN A 388     124.377 155.889 153.419  1.00  8.81           C  
ATOM   2945  OE1 GLN A 388     123.257 156.354 153.213  1.00  8.81           O  
ATOM   2946  NE2 GLN A 388     124.731 154.686 153.020  1.00  8.81           N  
ATOM   2947  N   ALA A 389     126.118 160.213 155.949  1.00  8.97           N  
ATOM   2948  CA  ALA A 389     126.547 161.333 155.121  1.00  8.97           C  
ATOM   2949  C   ALA A 389     127.994 161.728 155.399  1.00  8.97           C  
ATOM   2950  O   ALA A 389     128.448 161.727 156.545  1.00  8.97           O  
ATOM   2951  CB  ALA A 389     125.633 162.535 155.352  1.00  8.97           C  
ATOM   2952  N   THR A 390     128.725 162.056 154.331  1.00  8.13           N  
ATOM   2953  CA  THR A 390     130.078 162.589 154.430  1.00  8.13           C  
ATOM   2954  C   THR A 390     130.219 164.030 153.941  1.00  8.13           C  
ATOM   2955  O   THR A 390     131.315 164.587 154.037  1.00  8.13           O  
ATOM   2956  CB  THR A 390     131.057 161.694 153.659  1.00  8.13           C  
ATOM   2957  OG1 THR A 390     130.694 161.659 152.278  1.00  8.13           O  
ATOM   2958  CG2 THR A 390     131.055 160.286 154.220  1.00  8.13           C  
ATOM   2959  N   VAL A 391     129.158 164.646 153.424  1.00  5.63           N  
ATOM   2960  CA  VAL A 391     129.157 166.071 153.087  1.00  5.63           C  
ATOM   2961  C   VAL A 391     129.215 166.904 154.364  1.00  5.63           C  
ATOM   2962  O   VAL A 391     129.054 166.357 155.464  1.00  5.63           O  
ATOM   2963  CB  VAL A 391     127.921 166.463 152.253  1.00  5.63           C  
ATOM   2964  CG1 VAL A 391     128.000 165.883 150.849  1.00  5.63           C  
ATOM   2965  CG2 VAL A 391     126.634 166.071 152.960  1.00  5.63           C  
ATOM   2966  N   PRO A 392     129.440 168.216 154.276  1.00  6.41           N  
ATOM   2967  CA  PRO A 392     129.365 169.058 155.480  1.00  6.41           C  
ATOM   2968  C   PRO A 392     127.947 169.134 156.034  1.00  6.41           C  
ATOM   2969  O   PRO A 392     126.986 169.347 155.291  1.00  6.41           O  
ATOM   2970  CB  PRO A 392     129.847 170.426 154.988  1.00  6.41           C  
ATOM   2971  CG  PRO A 392     130.662 170.142 153.802  1.00  6.41           C  
ATOM   2972  CD  PRO A 392     130.029 168.954 153.145  1.00  6.41           C  
ATOM   2973  N   LEU A 393     127.832 168.958 157.349  1.00  5.84           N  
ATOM   2974  CA  LEU A 393     126.581 169.108 158.086  1.00  5.84           C  
ATOM   2975  C   LEU A 393     126.726 170.224 159.110  1.00  5.84           C  
ATOM   2976  O   LEU A 393     127.633 170.185 159.949  1.00  5.84           O  
ATOM   2977  CB  LEU A 393     126.193 167.806 158.792  1.00  5.84           C  
ATOM   2978  CG  LEU A 393     126.054 166.543 157.949  1.00  5.84           C  
ATOM   2979  CD1 LEU A 393     125.795 165.333 158.831  1.00  5.84           C  
ATOM   2980  CD2 LEU A 393     124.944 166.715 156.940  1.00  5.84           C  
ATOM   2981  N   VAL A 394     125.831 171.209 159.053  1.00  6.84           N  
ATOM   2982  CA  VAL A 394     125.754 172.258 160.068  1.00  6.84           C  
ATOM   2983  C   VAL A 394     124.348 172.248 160.668  1.00  6.84           C  
ATOM   2984  O   VAL A 394     123.357 172.214 159.932  1.00  6.84           O  
ATOM   2985  CB  VAL A 394     126.115 173.642 159.493  1.00  6.84           C  
ATOM   2986  CG1 VAL A 394     125.976 174.713 160.558  1.00  6.84           C  
ATOM   2987  CG2 VAL A 394     127.546 173.645 158.916  1.00  6.84           C  
ATOM   2988  N   THR A 395     124.267 172.269 162.002  1.00  7.28           N  
ATOM   2989  CA  THR A 395     123.011 172.148 162.739  1.00  7.28           C  
ATOM   2990  C   THR A 395     122.846 173.305 163.721  1.00  7.28           C  
ATOM   2991  O   THR A 395     123.804 173.702 164.388  1.00  7.28           O  
ATOM   2992  CB  THR A 395     122.960 170.812 163.496  1.00  7.28           C  
ATOM   2993  OG1 THR A 395     123.185 169.736 162.579  1.00  7.28           O  
ATOM   2994  CG2 THR A 395     121.616 170.600 164.206  1.00  7.28           C  
ATOM   2995  N   ILE A 396     121.622 173.829 163.817  1.00  7.26           N  
ATOM   2996  CA  ILE A 396     121.275 174.909 164.739  1.00  7.26           C  
ATOM   2997  C   ILE A 396     119.984 174.549 165.479  1.00  7.26           C  
ATOM   2998  O   ILE A 396     118.936 174.350 164.852  1.00  7.26           O  
ATOM   2999  CB  ILE A 396     121.119 176.260 164.018  1.00  7.26           C  
ATOM   3000  CG1 ILE A 396     122.358 176.590 163.172  1.00  7.26           C  
ATOM   3001  CG2 ILE A 396     120.853 177.367 165.026  1.00  7.26           C  
ATOM   3002  CD1 ILE A 396     122.286 176.103 161.753  1.00  7.26           C  
ATOM   3003  N   ILE A 397     120.063 174.482 166.807  1.00  5.87           N  
ATOM   3004  CA  ILE A 397     118.904 174.258 167.670  1.00  5.87           C  
ATOM   3005  C   ILE A 397     118.317 175.611 168.060  1.00  5.87           C  
ATOM   3006  O   ILE A 397     118.996 176.434 168.682  1.00  5.87           O  
ATOM   3007  CB  ILE A 397     119.280 173.445 168.920  1.00  5.87           C  
ATOM   3008  CG1 ILE A 397     119.884 172.078 168.541  1.00  5.87           C  
ATOM   3009  CG2 ILE A 397     118.062 173.279 169.822  1.00  5.87           C  
ATOM   3010  CD1 ILE A 397     120.373 171.265 169.706  1.00  5.87           C  
ATOM   3011  N   THR A 398     117.051 175.838 167.708  1.00  8.52           N  
ATOM   3012  CA  THR A 398     116.375 177.096 168.018  1.00  8.52           C  
ATOM   3013  C   THR A 398     115.660 177.065 169.375  1.00  8.52           C  
ATOM   3014  O   THR A 398     115.948 177.901 170.235  1.00  8.52           O  
ATOM   3015  CB  THR A 398     115.413 177.468 166.879  1.00  8.52           C  
ATOM   3016  OG1 THR A 398     114.530 176.379 166.606  1.00  8.52           O  
ATOM   3017  CG2 THR A 398     116.192 177.836 165.619  1.00  8.52           C  
ATOM   3018  N   ARG A 399     114.702 176.150 169.581  1.00 15.52           N  
ATOM   3019  CA  ARG A 399     114.033 176.056 170.883  1.00 15.52           C  
ATOM   3020  C   ARG A 399     114.151 174.692 171.554  1.00 15.52           C  
ATOM   3021  O   ARG A 399     114.816 174.584 172.585  1.00 15.52           O  
ATOM   3022  CB  ARG A 399     112.556 176.419 170.746  1.00 15.52           C  
ATOM   3023  CG  ARG A 399     112.241 177.643 169.975  1.00 15.52           C  
ATOM   3024  CD  ARG A 399     110.734 177.865 170.006  1.00 15.52           C  
ATOM   3025  NE  ARG A 399     110.279 178.291 171.323  1.00 15.52           N  
ATOM   3026  CZ  ARG A 399     109.004 178.495 171.637  1.00 15.52           C  
ATOM   3027  NH1 ARG A 399     108.046 178.269 170.751  1.00 15.52           N  
ATOM   3028  NH2 ARG A 399     108.684 178.910 172.852  1.00 15.52           N  
ATOM   3029  N   LYS A 400     113.544 173.645 171.005  1.00 12.58           N  
ATOM   3030  CA  LYS A 400     113.356 172.387 171.719  1.00 12.58           C  
ATOM   3031  C   LYS A 400     114.098 171.257 171.027  1.00 12.58           C  
ATOM   3032  O   LYS A 400     114.088 171.153 169.797  1.00 12.58           O  
ATOM   3033  CB  LYS A 400     111.871 172.011 171.840  1.00 12.58           C  
ATOM   3034  CG  LYS A 400     111.062 172.919 172.734  1.00 12.58           C  
ATOM   3035  CD  LYS A 400     109.690 172.359 173.054  1.00 12.58           C  
ATOM   3036  CE  LYS A 400     108.734 172.427 171.880  1.00 12.58           C  
ATOM   3037  NZ  LYS A 400     107.349 172.158 172.350  1.00 12.58           N  
ATOM   3038  N   ALA A 401     114.741 170.413 171.833  1.00  8.87           N  
ATOM   3039  CA  ALA A 401     115.363 169.187 171.343  1.00  8.87           C  
ATOM   3040  C   ALA A 401     115.283 168.164 172.473  1.00  8.87           C  
ATOM   3041  O   ALA A 401     116.152 168.130 173.348  1.00  8.87           O  
ATOM   3042  CB  ALA A 401     116.795 169.434 170.895  1.00  8.87           C  
ATOM   3043  N   PHE A 402     114.236 167.345 172.446  1.00  9.58           N  
ATOM   3044  CA  PHE A 402     113.982 166.340 173.467  1.00  9.58           C  
ATOM   3045  C   PHE A 402     114.192 164.931 172.922  1.00  9.58           C  
ATOM   3046  O   PHE A 402     113.734 164.601 171.824  1.00  9.58           O  
ATOM   3047  CB  PHE A 402     112.554 166.449 174.008  1.00  9.58           C  
ATOM   3048  CG  PHE A 402     112.243 167.744 174.710  1.00  9.58           C  
ATOM   3049  CD1 PHE A 402     113.237 168.546 175.239  1.00  9.58           C  
ATOM   3050  CD2 PHE A 402     110.931 168.145 174.859  1.00  9.58           C  
ATOM   3051  CE1 PHE A 402     112.919 169.725 175.887  1.00  9.58           C  
ATOM   3052  CE2 PHE A 402     110.617 169.316 175.505  1.00  9.58           C  
ATOM   3053  CZ  PHE A 402     111.613 170.104 176.019  1.00  9.58           C  
ATOM   3054  N   GLY A 403     114.885 164.106 173.706  1.00  9.55           N  
ATOM   3055  CA  GLY A 403     114.899 162.669 173.520  1.00  9.55           C  
ATOM   3056  C   GLY A 403     115.616 162.206 172.263  1.00  9.55           C  
ATOM   3057  O   GLY A 403     116.572 162.820 171.786  1.00  9.55           O  
ATOM   3058  N   GLY A 404     115.148 161.073 171.737  1.00  8.01           N  
ATOM   3059  CA  GLY A 404     115.733 160.516 170.531  1.00  8.01           C  
ATOM   3060  C   GLY A 404     115.581 161.418 169.324  1.00  8.01           C  
ATOM   3061  O   GLY A 404     116.396 161.368 168.398  1.00  8.01           O  
ATOM   3062  N   ALA A 405     114.529 162.238 169.307  1.00  8.20           N  
ATOM   3063  CA  ALA A 405     114.380 163.231 168.252  1.00  8.20           C  
ATOM   3064  C   ALA A 405     115.604 164.136 168.179  1.00  8.20           C  
ATOM   3065  O   ALA A 405     116.059 164.489 167.086  1.00  8.20           O  
ATOM   3066  CB  ALA A 405     113.112 164.051 168.480  1.00  8.20           C  
ATOM   3067  N   TYR A 406     116.148 164.519 169.336  1.00  6.38           N  
ATOM   3068  CA  TYR A 406     117.386 165.293 169.365  1.00  6.38           C  
ATOM   3069  C   TYR A 406     118.511 164.548 168.654  1.00  6.38           C  
ATOM   3070  O   TYR A 406     119.246 165.132 167.851  1.00  6.38           O  
ATOM   3071  CB  TYR A 406     117.768 165.614 170.813  1.00  6.38           C  
ATOM   3072  CG  TYR A 406     119.248 165.781 171.073  1.00  6.38           C  
ATOM   3073  CD1 TYR A 406     119.931 166.910 170.649  1.00  6.38           C  
ATOM   3074  CD2 TYR A 406     119.960 164.808 171.747  1.00  6.38           C  
ATOM   3075  CE1 TYR A 406     121.279 167.060 170.896  1.00  6.38           C  
ATOM   3076  CE2 TYR A 406     121.302 164.948 171.994  1.00  6.38           C  
ATOM   3077  CZ  TYR A 406     121.960 166.074 171.571  1.00  6.38           C  
ATOM   3078  OH  TYR A 406     123.302 166.201 171.821  1.00  6.38           O  
ATOM   3079  N   ILE A 407     118.652 163.250 168.936  1.00  6.83           N  
ATOM   3080  CA  ILE A 407     119.711 162.453 168.319  1.00  6.83           C  
ATOM   3081  C   ILE A 407     119.538 162.422 166.803  1.00  6.83           C  
ATOM   3082  O   ILE A 407     120.504 162.580 166.049  1.00  6.83           O  
ATOM   3083  CB  ILE A 407     119.734 161.028 168.915  1.00  6.83           C  
ATOM   3084  CG1 ILE A 407     119.867 161.065 170.449  1.00  6.83           C  
ATOM   3085  CG2 ILE A 407     120.864 160.209 168.296  1.00  6.83           C  
ATOM   3086  CD1 ILE A 407     119.842 159.703 171.135  1.00  6.83           C  
ATOM   3087  N   VAL A 408     118.304 162.220 166.336  1.00  6.68           N  
ATOM   3088  CA  VAL A 408     118.061 161.998 164.910  1.00  6.68           C  
ATOM   3089  C   VAL A 408     118.363 163.251 164.086  1.00  6.68           C  
ATOM   3090  O   VAL A 408     118.834 163.147 162.949  1.00  6.68           O  
ATOM   3091  CB  VAL A 408     116.613 161.509 164.693  1.00  6.68           C  
ATOM   3092  CG1 VAL A 408     116.250 161.429 163.197  1.00  6.68           C  
ATOM   3093  CG2 VAL A 408     116.393 160.147 165.358  1.00  6.68           C  
ATOM   3094  N   MET A 409     118.114 164.444 164.632  1.00  6.72           N  
ATOM   3095  CA  MET A 409     118.198 165.696 163.867  1.00  6.72           C  
ATOM   3096  C   MET A 409     119.638 166.224 163.831  1.00  6.72           C  
ATOM   3097  O   MET A 409     119.974 167.272 164.384  1.00  6.72           O  
ATOM   3098  CB  MET A 409     117.252 166.741 164.444  1.00  6.72           C  
ATOM   3099  CG  MET A 409     115.762 166.444 164.275  1.00  6.72           C  
ATOM   3100  SD  MET A 409     115.180 166.228 162.574  1.00  6.72           S  
ATOM   3101  CE  MET A 409     115.625 167.789 161.799  1.00  6.72           C  
ATOM   3102  N   ALA A 410     120.492 165.485 163.129  1.00  6.33           N  
ATOM   3103  CA  ALA A 410     121.863 165.910 162.840  1.00  6.33           C  
ATOM   3104  C   ALA A 410     122.612 166.333 164.109  1.00  6.33           C  
ATOM   3105  O   ALA A 410     123.226 167.398 164.176  1.00  6.33           O  
ATOM   3106  CB  ALA A 410     121.868 167.027 161.793  1.00  6.33           C  
ATOM   3107  N   SER A 411     122.571 165.471 165.122  1.00  4.69           N  
ATOM   3108  CA  SER A 411     123.337 165.670 166.343  1.00  4.69           C  
ATOM   3109  C   SER A 411     124.817 165.362 166.116  1.00  4.69           C  
ATOM   3110  O   SER A 411     125.200 164.691 165.156  1.00  4.69           O  
ATOM   3111  CB  SER A 411     122.786 164.796 167.469  1.00  4.69           C  
ATOM   3112  OG  SER A 411     122.760 163.436 167.100  1.00  4.69           O  
ATOM   3113  N   LYS A 412     125.652 165.887 167.019  1.00  8.73           N  
ATOM   3114  CA  LYS A 412     127.079 165.574 167.015  1.00  8.73           C  
ATOM   3115  C   LYS A 412     127.330 164.075 167.093  1.00  8.73           C  
ATOM   3116  O   LYS A 412     128.298 163.571 166.516  1.00  8.73           O  
ATOM   3117  CB  LYS A 412     127.765 166.277 168.191  1.00  8.73           C  
ATOM   3118  CG  LYS A 412     129.263 166.082 168.269  1.00  8.73           C  
ATOM   3119  CD  LYS A 412     129.956 166.915 167.234  1.00  8.73           C  
ATOM   3120  CE  LYS A 412     130.253 168.306 167.773  1.00  8.73           C  
ATOM   3121  NZ  LYS A 412     130.232 169.325 166.701  1.00  8.73           N  
ATOM   3122  N   HIS A 413     126.468 163.354 167.804  1.00  7.35           N  
ATOM   3123  CA  HIS A 413     126.701 161.944 168.096  1.00  7.35           C  
ATOM   3124  C   HIS A 413     126.631 161.079 166.846  1.00  7.35           C  
ATOM   3125  O   HIS A 413     127.259 160.018 166.798  1.00  7.35           O  
ATOM   3126  CB  HIS A 413     125.689 161.489 169.141  1.00  7.35           C  
ATOM   3127  CG  HIS A 413     125.510 162.476 170.249  1.00  7.35           C  
ATOM   3128  ND1 HIS A 413     126.526 162.791 171.121  1.00  7.35           N  
ATOM   3129  CD2 HIS A 413     124.462 163.259 170.594  1.00  7.35           C  
ATOM   3130  CE1 HIS A 413     126.103 163.704 171.975  1.00  7.35           C  
ATOM   3131  NE2 HIS A 413     124.855 164.007 171.676  1.00  7.35           N  
ATOM   3132  N   VAL A 414     125.876 161.509 165.834  1.00 12.77           N  
ATOM   3133  CA  VAL A 414     125.754 160.765 164.588  1.00 12.77           C  
ATOM   3134  C   VAL A 414     126.644 161.318 163.478  1.00 12.77           C  
ATOM   3135  O   VAL A 414     126.651 160.762 162.373  1.00 12.77           O  
ATOM   3136  CB  VAL A 414     124.282 160.693 164.128  1.00 12.77           C  
ATOM   3137  CG1 VAL A 414     123.424 160.015 165.191  1.00 12.77           C  
ATOM   3138  CG2 VAL A 414     123.729 162.065 163.807  1.00 12.77           C  
ATOM   3139  N   GLY A 415     127.397 162.388 163.734  1.00 11.32           N  
ATOM   3140  CA  GLY A 415     128.472 162.773 162.836  1.00 11.32           C  
ATOM   3141  C   GLY A 415     128.519 164.211 162.357  1.00 11.32           C  
ATOM   3142  O   GLY A 415     129.332 164.536 161.488  1.00 11.32           O  
ATOM   3143  N   ALA A 416     127.680 165.085 162.902  1.00 12.77           N  
ATOM   3144  CA  ALA A 416     127.665 166.471 162.462  1.00 12.77           C  
ATOM   3145  C   ALA A 416     128.981 167.168 162.798  1.00 12.77           C  
ATOM   3146  O   ALA A 416     129.611 166.900 163.823  1.00 12.77           O  
ATOM   3147  CB  ALA A 416     126.501 167.224 163.096  1.00 12.77           C  
ATOM   3148  N   ASP A 417     129.383 168.081 161.913  1.00  9.71           N  
ATOM   3149  CA  ASP A 417     130.642 168.805 162.060  1.00  9.71           C  
ATOM   3150  C   ASP A 417     130.526 169.961 163.048  1.00  9.71           C  
ATOM   3151  O   ASP A 417     131.394 170.137 163.909  1.00  9.71           O  
ATOM   3152  CB  ASP A 417     131.101 169.318 160.697  1.00  9.71           C  
ATOM   3153  CG  ASP A 417     131.317 168.202 159.699  1.00  9.71           C  
ATOM   3154  OD1 ASP A 417     132.255 167.406 159.898  1.00  9.71           O  
ATOM   3155  OD2 ASP A 417     130.546 168.110 158.723  1.00  9.71           O  
ATOM   3156  N   LEU A 418     129.475 170.768 162.927  1.00  9.00           N  
ATOM   3157  CA  LEU A 418     129.280 171.943 163.768  1.00  9.00           C  
ATOM   3158  C   LEU A 418     127.852 171.972 164.294  1.00  9.00           C  
ATOM   3159  O   LEU A 418     126.896 171.852 163.522  1.00  9.00           O  
ATOM   3160  CB  LEU A 418     129.588 173.229 163.000  1.00  9.00           C  
ATOM   3161  CG  LEU A 418     131.070 173.539 162.796  1.00  9.00           C  
ATOM   3162  CD1 LEU A 418     131.236 174.612 161.765  1.00  9.00           C  
ATOM   3163  CD2 LEU A 418     131.715 173.962 164.101  1.00  9.00           C  
ATOM   3164  N   ASN A 419     127.722 172.131 165.609  1.00  8.86           N  
ATOM   3165  CA  ASN A 419     126.439 172.173 166.303  1.00  8.86           C  
ATOM   3166  C   ASN A 419     126.368 173.444 167.147  1.00  8.86           C  
ATOM   3167  O   ASN A 419     127.136 173.603 168.100  1.00  8.86           O  
ATOM   3168  CB  ASN A 419     126.262 170.927 167.170  1.00  8.86           C  
ATOM   3169  CG  ASN A 419     126.317 169.642 166.366  1.00  8.86           C  
ATOM   3170  OD1 ASN A 419     127.392 169.137 166.053  1.00  8.86           O  
ATOM   3171  ND2 ASN A 419     125.152 169.106 166.031  1.00  8.86           N  
ATOM   3172  N   TYR A 420     125.452 174.344 166.797  1.00  7.61           N  
ATOM   3173  CA  TYR A 420     125.212 175.587 167.516  1.00  7.61           C  
ATOM   3174  C   TYR A 420     123.865 175.537 168.230  1.00  7.61           C  
ATOM   3175  O   TYR A 420     123.008 174.703 167.930  1.00  7.61           O  
ATOM   3176  CB  TYR A 420     125.234 176.793 166.568  1.00  7.61           C  
ATOM   3177  CG  TYR A 420     126.539 177.047 165.849  1.00  7.61           C  
ATOM   3178  CD1 TYR A 420     127.705 177.312 166.547  1.00  7.61           C  
ATOM   3179  CD2 TYR A 420     126.597 177.050 164.466  1.00  7.61           C  
ATOM   3180  CE1 TYR A 420     128.889 177.553 165.885  1.00  7.61           C  
ATOM   3181  CE2 TYR A 420     127.772 177.291 163.801  1.00  7.61           C  
ATOM   3182  CZ  TYR A 420     128.917 177.544 164.514  1.00  7.61           C  
ATOM   3183  OH  TYR A 420     130.096 177.786 163.857  1.00  7.61           O  
ATOM   3184  N   ALA A 421     123.684 176.459 169.176  1.00  6.61           N  
ATOM   3185  CA  ALA A 421     122.453 176.580 169.946  1.00  6.61           C  
ATOM   3186  C   ALA A 421     122.142 178.045 170.219  1.00  6.61           C  
ATOM   3187  O   ALA A 421     123.034 178.820 170.568  1.00  6.61           O  
ATOM   3188  CB  ALA A 421     122.547 175.830 171.275  1.00  6.61           C  
ATOM   3189  N   TRP A 422     120.872 178.416 170.058  1.00  6.54           N  
ATOM   3190  CA  TRP A 422     120.393 179.727 170.467  1.00  6.54           C  
ATOM   3191  C   TRP A 422     120.162 179.750 171.980  1.00  6.54           C  
ATOM   3192  O   TRP A 422     120.019 178.703 172.611  1.00  6.54           O  
ATOM   3193  CB  TRP A 422     119.097 180.086 169.737  1.00  6.54           C  
ATOM   3194  CG  TRP A 422     119.236 180.516 168.295  1.00  6.54           C  
ATOM   3195  CD1 TRP A 422     120.350 180.456 167.511  1.00  6.54           C  
ATOM   3196  CD2 TRP A 422     118.204 181.074 167.474  1.00  6.54           C  
ATOM   3197  NE1 TRP A 422     120.075 180.943 166.259  1.00  6.54           N  
ATOM   3198  CE2 TRP A 422     118.763 181.324 166.209  1.00  6.54           C  
ATOM   3199  CE3 TRP A 422     116.860 181.381 167.685  1.00  6.54           C  
ATOM   3200  CZ2 TRP A 422     118.026 181.871 165.166  1.00  6.54           C  
ATOM   3201  CZ3 TRP A 422     116.135 181.923 166.648  1.00  6.54           C  
ATOM   3202  CH2 TRP A 422     116.716 182.158 165.406  1.00  6.54           C  
ATOM   3203  N   PRO A 423     120.121 180.938 172.590  1.00  8.80           N  
ATOM   3204  CA  PRO A 423     119.953 181.005 174.053  1.00  8.80           C  
ATOM   3205  C   PRO A 423     118.628 180.450 174.544  1.00  8.80           C  
ATOM   3206  O   PRO A 423     118.498 180.168 175.740  1.00  8.80           O  
ATOM   3207  CB  PRO A 423     120.077 182.506 174.355  1.00  8.80           C  
ATOM   3208  CG  PRO A 423     120.715 183.095 173.156  1.00  8.80           C  
ATOM   3209  CD  PRO A 423     120.257 182.277 172.005  1.00  8.80           C  
ATOM   3210  N   THR A 424     117.647 180.284 173.664  1.00  9.85           N  
ATOM   3211  CA  THR A 424     116.352 179.713 173.999  1.00  9.85           C  
ATOM   3212  C   THR A 424     116.298 178.199 173.816  1.00  9.85           C  
ATOM   3213  O   THR A 424     115.207 177.625 173.860  1.00  9.85           O  
ATOM   3214  CB  THR A 424     115.265 180.378 173.150  1.00  9.85           C  
ATOM   3215  OG1 THR A 424     115.707 180.454 171.791  1.00  9.85           O  
ATOM   3216  CG2 THR A 424     114.970 181.768 173.673  1.00  9.85           C  
ATOM   3217  N   ALA A 425     117.439 177.543 173.628  1.00  9.37           N  
ATOM   3218  CA  ALA A 425     117.457 176.108 173.389  1.00  9.37           C  
ATOM   3219  C   ALA A 425     117.194 175.348 174.683  1.00  9.37           C  
ATOM   3220  O   ALA A 425     117.650 175.746 175.758  1.00  9.37           O  
ATOM   3221  CB  ALA A 425     118.796 175.673 172.795  1.00  9.37           C  
ATOM   3222  N   GLN A 426     116.457 174.247 174.571  1.00 11.26           N  
ATOM   3223  CA  GLN A 426     116.148 173.365 175.698  1.00 11.26           C  
ATOM   3224  C   GLN A 426     116.505 171.938 175.284  1.00 11.26           C  
ATOM   3225  O   GLN A 426     115.718 171.258 174.621  1.00 11.26           O  
ATOM   3226  CB  GLN A 426     114.685 173.476 176.112  1.00 11.26           C  
ATOM   3227  CG  GLN A 426     114.197 174.896 176.326  1.00 11.26           C  
ATOM   3228  CD  GLN A 426     112.741 174.968 176.722  1.00 11.26           C  
ATOM   3229  OE1 GLN A 426     111.901 174.244 176.193  1.00 11.26           O  
ATOM   3230  NE2 GLN A 426     112.433 175.849 177.658  1.00 11.26           N  
ATOM   3231  N   ILE A 427     117.691 171.493 175.676  1.00  7.69           N  
ATOM   3232  CA  ILE A 427     118.254 170.213 175.259  1.00  7.69           C  
ATOM   3233  C   ILE A 427     118.181 169.280 176.462  1.00  7.69           C  
ATOM   3234  O   ILE A 427     118.985 169.388 177.394  1.00  7.69           O  
ATOM   3235  CB  ILE A 427     119.688 170.370 174.736  1.00  7.69           C  
ATOM   3236  CG1 ILE A 427     119.743 171.452 173.651  1.00  7.69           C  
ATOM   3237  CG2 ILE A 427     120.219 169.055 174.191  1.00  7.69           C  
ATOM   3238  CD1 ILE A 427     121.134 171.832 173.207  1.00  7.69           C  
ATOM   3239  N   ALA A 428     117.220 168.355 176.445  1.00  9.72           N  
ATOM   3240  CA  ALA A 428     116.948 167.494 177.591  1.00  9.72           C  
ATOM   3241  C   ALA A 428     116.385 166.153 177.127  1.00  9.72           C  
ATOM   3242  O   ALA A 428     115.997 165.984 175.971  1.00  9.72           O  
ATOM   3243  CB  ALA A 428     115.974 168.165 178.562  1.00  9.72           C  
ATOM   3244  N   VAL A 429     116.332 165.198 178.064  1.00 14.12           N  
ATOM   3245  CA  VAL A 429     115.765 163.878 177.784  1.00 14.12           C  
ATOM   3246  C   VAL A 429     114.260 163.958 177.571  1.00 14.12           C  
ATOM   3247  O   VAL A 429     113.699 163.193 176.778  1.00 14.12           O  
ATOM   3248  CB  VAL A 429     116.105 162.884 178.913  1.00 14.12           C  
ATOM   3249  CG1 VAL A 429     117.587 162.622 178.959  1.00 14.12           C  
ATOM   3250  CG2 VAL A 429     115.602 163.375 180.266  1.00 14.12           C  
ATOM   3251  N   MET A 430     113.573 164.845 178.285  1.00 20.35           N  
ATOM   3252  CA  MET A 430     112.098 164.963 178.203  1.00 20.35           C  
ATOM   3253  C   MET A 430     111.730 166.234 178.967  1.00 20.35           C  
ATOM   3254  O   MET A 430     112.559 166.888 179.603  1.00 20.35           O  
ATOM   3255  CB  MET A 430     111.328 163.749 178.791  1.00 20.35           C  
ATOM   3256  CG  MET A 430     111.390 163.669 180.304  1.00 20.35           C  
ATOM   3257  SD  MET A 430     110.274 162.413 180.980  1.00 20.35           S  
ATOM   3258  CE  MET A 430     111.024 160.921 180.330  1.00 20.35           C  
ATOM   3259  N   GLY A 431     110.441 166.552 178.905  1.00 23.79           N  
ATOM   3260  CA  GLY A 431     109.920 167.665 179.672  1.00 23.79           C  
ATOM   3261  C   GLY A 431     110.057 167.445 181.166  1.00 23.79           C  
ATOM   3262  O   GLY A 431     110.164 166.322 181.657  1.00 23.79           O  
ATOM   3263  N   ALA A 432     110.040 168.558 181.902  1.00 30.01           N  
ATOM   3264  CA  ALA A 432     110.341 168.509 183.329  1.00 30.01           C  
ATOM   3265  C   ALA A 432     109.276 167.743 184.104  1.00 30.01           C  
ATOM   3266  O   ALA A 432     109.600 166.965 185.008  1.00 30.01           O  
ATOM   3267  CB  ALA A 432     110.486 169.925 183.881  1.00 30.01           C  
ATOM   3268  N   LYS A 433     108.003 167.962 183.778  1.00 35.81           N  
ATOM   3269  CA  LYS A 433     106.924 167.290 184.496  1.00 35.81           C  
ATOM   3270  C   LYS A 433     107.092 165.775 184.457  1.00 35.81           C  
ATOM   3271  O   LYS A 433     107.081 165.109 185.499  1.00 35.81           O  
ATOM   3272  CB  LYS A 433     105.577 167.698 183.904  1.00 35.81           C  
ATOM   3273  CG  LYS A 433     104.385 167.027 184.563  1.00 35.81           C  
ATOM   3274  CD  LYS A 433     103.084 167.746 184.239  1.00 35.81           C  
ATOM   3275  CE  LYS A 433     102.831 167.825 182.743  1.00 35.81           C  
ATOM   3276  NZ  LYS A 433     101.532 168.482 182.438  1.00 35.81           N  
ATOM   3277  N   GLY A 434     107.232 165.212 183.256  1.00 34.55           N  
ATOM   3278  CA  GLY A 434     107.358 163.769 183.140  1.00 34.55           C  
ATOM   3279  C   GLY A 434     108.606 163.236 183.814  1.00 34.55           C  
ATOM   3280  O   GLY A 434     108.571 162.209 184.501  1.00 34.55           O  
ATOM   3281  N   ALA A 435     109.735 163.919 183.614  1.00 33.10           N  
ATOM   3282  CA  ALA A 435     110.974 163.487 184.248  1.00 33.10           C  
ATOM   3283  C   ALA A 435     110.821 163.442 185.760  1.00 33.10           C  
ATOM   3284  O   ALA A 435     111.292 162.506 186.414  1.00 33.10           O  
ATOM   3285  CB  ALA A 435     112.122 164.415 183.857  1.00 33.10           C  
ATOM   3286  N   VAL A 436     110.158 164.447 186.331  1.00 37.61           N  
ATOM   3287  CA  VAL A 436     109.999 164.512 187.778  1.00 37.61           C  
ATOM   3288  C   VAL A 436     109.060 163.413 188.260  1.00 37.61           C  
ATOM   3289  O   VAL A 436     109.325 162.746 189.266  1.00 37.61           O  
ATOM   3290  CB  VAL A 436     109.506 165.909 188.194  1.00 37.61           C  
ATOM   3291  CG1 VAL A 436     108.877 165.875 189.570  1.00 37.61           C  
ATOM   3292  CG2 VAL A 436     110.653 166.907 188.156  1.00 37.61           C  
ATOM   3293  N   GLU A 437     107.949 163.204 187.551  1.00 41.59           N  
ATOM   3294  CA  GLU A 437     107.031 162.137 187.937  1.00 41.59           C  
ATOM   3295  C   GLU A 437     107.663 160.758 187.826  1.00 41.59           C  
ATOM   3296  O   GLU A 437     107.246 159.843 188.544  1.00 41.59           O  
ATOM   3297  CB  GLU A 437     105.758 162.192 187.094  1.00 41.59           C  
ATOM   3298  CG  GLU A 437     105.014 163.514 187.175  1.00 41.59           C  
ATOM   3299  CD  GLU A 437     103.988 163.680 186.072  1.00 41.59           C  
ATOM   3300  OE1 GLU A 437     104.101 162.985 185.041  1.00 41.59           O  
ATOM   3301  OE2 GLU A 437     103.065 164.505 186.238  1.00 41.59           O  
ATOM   3302  N   ILE A 438     108.658 160.585 186.960  1.00 39.95           N  
ATOM   3303  CA  ILE A 438     109.346 159.300 186.884  1.00 39.95           C  
ATOM   3304  C   ILE A 438     110.388 159.178 187.989  1.00 39.95           C  
ATOM   3305  O   ILE A 438     110.503 158.135 188.641  1.00 39.95           O  
ATOM   3306  CB  ILE A 438     109.972 159.107 185.491  1.00 39.95           C  
ATOM   3307  CG1 ILE A 438     108.878 158.909 184.442  1.00 39.95           C  
ATOM   3308  CG2 ILE A 438     110.902 157.916 185.495  1.00 39.95           C  
ATOM   3309  CD1 ILE A 438     109.334 159.155 183.023  1.00 39.95           C  
ATOM   3310  N   ILE A 439     111.160 160.241 188.220  1.00 40.34           N  
ATOM   3311  CA  ILE A 439     112.243 160.171 189.195  1.00 40.34           C  
ATOM   3312  C   ILE A 439     111.700 160.133 190.617  1.00 40.34           C  
ATOM   3313  O   ILE A 439     112.294 159.500 191.497  1.00 40.34           O  
ATOM   3314  CB  ILE A 439     113.205 161.357 188.998  1.00 40.34           C  
ATOM   3315  CG1 ILE A 439     113.918 161.259 187.652  1.00 40.34           C  
ATOM   3316  CG2 ILE A 439     114.233 161.413 190.108  1.00 40.34           C  
ATOM   3317  CD1 ILE A 439     114.451 162.572 187.165  1.00 40.34           C  
ATOM   3318  N   PHE A 440     110.581 160.804 190.870  1.00 47.19           N  
ATOM   3319  CA  PHE A 440     110.020 160.951 192.207  1.00 47.19           C  
ATOM   3320  C   PHE A 440     108.655 160.281 192.302  1.00 47.19           C  
ATOM   3321  O   PHE A 440     107.704 160.828 192.864  1.00 47.19           O  
ATOM   3322  CB  PHE A 440     109.936 162.427 192.584  1.00 47.19           C  
ATOM   3323  CG  PHE A 440     111.277 163.088 192.719  1.00 47.19           C  
ATOM   3324  CD1 PHE A 440     112.113 162.769 193.770  1.00 47.19           C  
ATOM   3325  CD2 PHE A 440     111.710 164.010 191.785  1.00 47.19           C  
ATOM   3326  CE1 PHE A 440     113.344 163.367 193.897  1.00 47.19           C  
ATOM   3327  CE2 PHE A 440     112.946 164.607 191.908  1.00 47.19           C  
ATOM   3328  CZ  PHE A 440     113.762 164.285 192.965  1.00 47.19           C  
ATOM   3329  N   ARG A 441     108.553 159.074 191.743  1.00 55.42           N  
ATOM   3330  CA  ARG A 441     107.290 158.344 191.723  1.00 55.42           C  
ATOM   3331  C   ARG A 441     106.781 158.010 193.120  1.00 55.42           C  
ATOM   3332  O   ARG A 441     105.581 157.764 193.284  1.00 55.42           O  
ATOM   3333  CB  ARG A 441     107.452 157.056 190.911  1.00 55.42           C  
ATOM   3334  CG  ARG A 441     108.615 156.172 191.357  1.00 55.42           C  
ATOM   3335  CD  ARG A 441     108.989 155.150 190.296  1.00 55.42           C  
ATOM   3336  NE  ARG A 441     110.135 154.337 190.700  1.00 55.42           N  
ATOM   3337  CZ  ARG A 441     111.407 154.639 190.451  1.00 55.42           C  
ATOM   3338  NH1 ARG A 441     111.727 155.747 189.793  1.00 55.42           N  
ATOM   3339  NH2 ARG A 441     112.370 153.828 190.865  1.00 55.42           N  
ATOM   3340  N   ALA A 442     107.656 157.994 194.127  1.00 61.57           N  
ATOM   3341  CA  ALA A 442     107.230 157.632 195.475  1.00 61.57           C  
ATOM   3342  C   ALA A 442     106.414 158.732 196.143  1.00 61.57           C  
ATOM   3343  O   ALA A 442     105.531 158.433 196.955  1.00 61.57           O  
ATOM   3344  CB  ALA A 442     108.447 157.299 196.336  1.00 61.57           C  
ATOM   3345  N   GLU A 443     106.688 159.996 195.821  1.00 59.24           N  
ATOM   3346  CA  GLU A 443     106.016 161.124 196.455  1.00 59.24           C  
ATOM   3347  C   GLU A 443     105.263 161.946 195.417  1.00 59.24           C  
ATOM   3348  O   GLU A 443     105.395 163.173 195.363  1.00 59.24           O  
ATOM   3349  CB  GLU A 443     107.027 161.991 197.210  1.00 59.24           C  
ATOM   3350  CG  GLU A 443     108.133 162.574 196.343  1.00 59.24           C  
ATOM   3351  CD  GLU A 443     108.901 163.680 197.040  1.00 59.24           C  
ATOM   3352  OE1 GLU A 443     108.533 164.037 198.179  1.00 59.24           O  
ATOM   3353  OE2 GLU A 443     109.875 164.191 196.450  1.00 59.24           O  
ATOM   3354  N   ILE A 444     104.462 161.269 194.599  1.00 59.80           N  
ATOM   3355  CA  ILE A 444     103.832 161.868 193.427  1.00 59.80           C  
ATOM   3356  C   ILE A 444     102.518 162.548 193.793  1.00 59.80           C  
ATOM   3357  O   ILE A 444     101.771 162.985 192.911  1.00 59.80           O  
ATOM   3358  CB  ILE A 444     103.610 160.796 192.344  1.00 59.80           C  
ATOM   3359  CG1 ILE A 444     103.254 161.439 191.003  1.00 59.80           C  
ATOM   3360  CG2 ILE A 444     102.519 159.822 192.773  1.00 59.80           C  
ATOM   3361  CD1 ILE A 444     103.644 160.593 189.811  1.00 59.80           C  
ATOM   3362  N   GLY A 445     102.227 162.656 195.088  1.00 57.18           N  
ATOM   3363  CA  GLY A 445     100.936 163.159 195.519  1.00 57.18           C  
ATOM   3364  C   GLY A 445     100.941 164.567 196.083  1.00 57.18           C  
ATOM   3365  O   GLY A 445      99.982 165.317 195.878  1.00 57.18           O  
ATOM   3366  N   ASP A 446     102.004 164.945 196.789  1.00 56.99           N  
ATOM   3367  CA  ASP A 446     102.047 166.234 197.472  1.00 56.99           C  
ATOM   3368  C   ASP A 446     102.284 167.343 196.451  1.00 56.99           C  
ATOM   3369  O   ASP A 446     103.327 167.374 195.788  1.00 56.99           O  
ATOM   3370  CB  ASP A 446     103.135 166.237 198.540  1.00 56.99           C  
ATOM   3371  CG  ASP A 446     103.120 167.498 199.381  1.00 56.99           C  
ATOM   3372  OD1 ASP A 446     102.076 168.183 199.400  1.00 56.99           O  
ATOM   3373  OD2 ASP A 446     104.148 167.806 200.019  1.00 56.99           O  
ATOM   3374  N   ALA A 447     101.319 168.256 196.332  1.00 56.05           N  
ATOM   3375  CA  ALA A 447     101.350 169.247 195.260  1.00 56.05           C  
ATOM   3376  C   ALA A 447     102.560 170.171 195.375  1.00 56.05           C  
ATOM   3377  O   ALA A 447     103.346 170.301 194.430  1.00 56.05           O  
ATOM   3378  CB  ALA A 447     100.054 170.055 195.268  1.00 56.05           C  
ATOM   3379  N   ASP A 448     102.702 170.851 196.514  1.00 55.93           N  
ATOM   3380  CA  ASP A 448     103.766 171.840 196.660  1.00 55.93           C  
ATOM   3381  C   ASP A 448     105.137 171.233 196.387  1.00 55.93           C  
ATOM   3382  O   ASP A 448     105.967 171.837 195.696  1.00 55.93           O  
ATOM   3383  CB  ASP A 448     103.718 172.448 198.060  1.00 55.93           C  
ATOM   3384  CG  ASP A 448     103.714 171.398 199.148  1.00 55.93           C  
ATOM   3385  OD1 ASP A 448     102.903 170.455 199.049  1.00 55.93           O  
ATOM   3386  OD2 ASP A 448     104.516 171.511 200.097  1.00 55.93           O  
ATOM   3387  N   LYS A 449     105.398 170.045 196.935  1.00 54.27           N  
ATOM   3388  CA  LYS A 449     106.683 169.390 196.713  1.00 54.27           C  
ATOM   3389  C   LYS A 449     106.903 169.124 195.230  1.00 54.27           C  
ATOM   3390  O   LYS A 449     107.991 169.368 194.694  1.00 54.27           O  
ATOM   3391  CB  LYS A 449     106.742 168.087 197.512  1.00 54.27           C  
ATOM   3392  CG  LYS A 449     107.966 167.227 197.240  1.00 54.27           C  
ATOM   3393  CD  LYS A 449     109.258 167.979 197.505  1.00 54.27           C  
ATOM   3394  CE  LYS A 449     109.320 168.489 198.928  1.00 54.27           C  
ATOM   3395  NZ  LYS A 449     110.714 168.777 199.354  1.00 54.27           N  
ATOM   3396  N   VAL A 450     105.874 168.609 194.556  1.00 50.96           N  
ATOM   3397  CA  VAL A 450     105.974 168.328 193.129  1.00 50.96           C  
ATOM   3398  C   VAL A 450     106.300 169.598 192.358  1.00 50.96           C  
ATOM   3399  O   VAL A 450     107.157 169.598 191.469  1.00 50.96           O  
ATOM   3400  CB  VAL A 450     104.669 167.682 192.629  1.00 50.96           C  
ATOM   3401  CG1 VAL A 450     104.519 167.845 191.129  1.00 50.96           C  
ATOM   3402  CG2 VAL A 450     104.628 166.221 193.016  1.00 50.96           C  
ATOM   3403  N   ALA A 451     105.619 170.697 192.679  1.00 49.62           N  
ATOM   3404  CA  ALA A 451     105.850 171.942 191.955  1.00 49.62           C  
ATOM   3405  C   ALA A 451     107.260 172.463 192.194  1.00 49.62           C  
ATOM   3406  O   ALA A 451     107.919 172.946 191.264  1.00 49.62           O  
ATOM   3407  CB  ALA A 451     104.812 172.983 192.369  1.00 49.62           C  
ATOM   3408  N   GLU A 452     107.747 172.359 193.432  1.00 48.76           N  
ATOM   3409  CA  GLU A 452     109.098 172.822 193.730  1.00 48.76           C  
ATOM   3410  C   GLU A 452     110.133 172.000 192.972  1.00 48.76           C  
ATOM   3411  O   GLU A 452     111.080 172.552 192.396  1.00 48.76           O  
ATOM   3412  CB  GLU A 452     109.351 172.757 195.236  1.00 48.76           C  
ATOM   3413  CG  GLU A 452     110.701 173.310 195.669  1.00 48.76           C  
ATOM   3414  CD  GLU A 452     110.846 174.790 195.367  1.00 48.76           C  
ATOM   3415  OE1 GLU A 452     109.812 175.486 195.288  1.00 48.76           O  
ATOM   3416  OE2 GLU A 452     111.993 175.258 195.208  1.00 48.76           O  
ATOM   3417  N   ARG A 453     109.960 170.677 192.948  1.00 46.18           N  
ATOM   3418  CA  ARG A 453     110.884 169.824 192.209  1.00 46.18           C  
ATOM   3419  C   ARG A 453     110.815 170.106 190.714  1.00 46.18           C  
ATOM   3420  O   ARG A 453     111.837 170.084 190.019  1.00 46.18           O  
ATOM   3421  CB  ARG A 453     110.576 168.357 192.491  1.00 46.18           C  
ATOM   3422  CG  ARG A 453     110.713 167.965 193.947  1.00 46.18           C  
ATOM   3423  CD  ARG A 453     110.730 166.465 194.100  1.00 46.18           C  
ATOM   3424  NE  ARG A 453     111.012 166.024 195.462  1.00 46.18           N  
ATOM   3425  CZ  ARG A 453     112.180 166.177 196.079  1.00 46.18           C  
ATOM   3426  NH1 ARG A 453     112.335 165.733 197.318  1.00 46.18           N  
ATOM   3427  NH2 ARG A 453     113.191 166.773 195.464  1.00 46.18           N  
ATOM   3428  N   THR A 454     109.612 170.363 190.202  1.00 41.90           N  
ATOM   3429  CA  THR A 454     109.451 170.700 188.793  1.00 41.90           C  
ATOM   3430  C   THR A 454     110.220 171.966 188.451  1.00 41.90           C  
ATOM   3431  O   THR A 454     110.917 172.029 187.433  1.00 41.90           O  
ATOM   3432  CB  THR A 454     107.966 170.868 188.472  1.00 41.90           C  
ATOM   3433  OG1 THR A 454     107.218 169.835 189.124  1.00 41.90           O  
ATOM   3434  CG2 THR A 454     107.724 170.791 186.985  1.00 41.90           C  
ATOM   3435  N   LYS A 455     110.108 172.989 189.300  1.00 40.68           N  
ATOM   3436  CA  LYS A 455     110.826 174.233 189.046  1.00 40.68           C  
ATOM   3437  C   LYS A 455     112.333 174.027 189.141  1.00 40.68           C  
ATOM   3438  O   LYS A 455     113.094 174.601 188.354  1.00 40.68           O  
ATOM   3439  CB  LYS A 455     110.365 175.314 190.021  1.00 40.68           C  
ATOM   3440  CG  LYS A 455     111.071 176.648 189.849  1.00 40.68           C  
ATOM   3441  CD  LYS A 455     110.306 177.783 190.508  1.00 40.68           C  
ATOM   3442  CE  LYS A 455     110.822 178.064 191.904  1.00 40.68           C  
ATOM   3443  NZ  LYS A 455     109.993 179.079 192.611  1.00 40.68           N  
ATOM   3444  N   GLU A 456     112.782 173.205 190.091  1.00 38.04           N  
ATOM   3445  CA  GLU A 456     114.210 172.931 190.210  1.00 38.04           C  
ATOM   3446  C   GLU A 456     114.740 172.241 188.956  1.00 38.04           C  
ATOM   3447  O   GLU A 456     115.792 172.615 188.423  1.00 38.04           O  
ATOM   3448  CB  GLU A 456     114.477 172.083 191.454  1.00 38.04           C  
ATOM   3449  CG  GLU A 456     114.371 172.847 192.763  1.00 38.04           C  
ATOM   3450  CD  GLU A 456     114.486 171.947 193.975  1.00 38.04           C  
ATOM   3451  OE1 GLU A 456     114.836 170.760 193.807  1.00 38.04           O  
ATOM   3452  OE2 GLU A 456     114.225 172.426 195.099  1.00 38.04           O  
ATOM   3453  N   TYR A 457     114.015 171.231 188.465  1.00 26.34           N  
ATOM   3454  CA  TYR A 457     114.414 170.560 187.231  1.00 26.34           C  
ATOM   3455  C   TYR A 457     114.418 171.528 186.056  1.00 26.34           C  
ATOM   3456  O   TYR A 457     115.347 171.523 185.240  1.00 26.34           O  
ATOM   3457  CB  TYR A 457     113.484 169.381 186.946  1.00 26.34           C  
ATOM   3458  CG  TYR A 457     114.049 168.374 185.972  1.00 26.34           C  
ATOM   3459  CD1 TYR A 457     113.861 168.515 184.608  1.00 26.34           C  
ATOM   3460  CD2 TYR A 457     114.769 167.279 186.418  1.00 26.34           C  
ATOM   3461  CE1 TYR A 457     114.373 167.599 183.723  1.00 26.34           C  
ATOM   3462  CE2 TYR A 457     115.282 166.359 185.538  1.00 26.34           C  
ATOM   3463  CZ  TYR A 457     115.083 166.522 184.191  1.00 26.34           C  
ATOM   3464  OH  TYR A 457     115.596 165.607 183.307  1.00 26.34           O  
ATOM   3465  N   GLU A 458     113.380 172.359 185.947  1.00 31.04           N  
ATOM   3466  CA  GLU A 458     113.329 173.351 184.879  1.00 31.04           C  
ATOM   3467  C   GLU A 458     114.556 174.251 184.909  1.00 31.04           C  
ATOM   3468  O   GLU A 458     115.170 174.512 183.869  1.00 31.04           O  
ATOM   3469  CB  GLU A 458     112.055 174.185 185.009  1.00 31.04           C  
ATOM   3470  CG  GLU A 458     111.871 175.238 183.935  1.00 31.04           C  
ATOM   3471  CD  GLU A 458     111.458 174.658 182.597  1.00 31.04           C  
ATOM   3472  OE1 GLU A 458     110.762 173.623 182.594  1.00 31.04           O  
ATOM   3473  OE2 GLU A 458     111.829 175.232 181.551  1.00 31.04           O  
ATOM   3474  N   ASP A 459     114.929 174.735 186.095  1.00 32.75           N  
ATOM   3475  CA  ASP A 459     116.051 175.662 186.193  1.00 32.75           C  
ATOM   3476  C   ASP A 459     117.373 174.965 185.903  1.00 32.75           C  
ATOM   3477  O   ASP A 459     118.284 175.568 185.323  1.00 32.75           O  
ATOM   3478  CB  ASP A 459     116.080 176.308 187.576  1.00 32.75           C  
ATOM   3479  CG  ASP A 459     114.837 177.123 187.867  1.00 32.75           C  
ATOM   3480  OD1 ASP A 459     114.321 177.778 186.937  1.00 32.75           O  
ATOM   3481  OD2 ASP A 459     114.376 177.110 189.027  1.00 32.75           O  
ATOM   3482  N   ARG A 460     117.501 173.698 186.294  1.00 26.93           N  
ATOM   3483  CA  ARG A 460     118.784 173.023 186.139  1.00 26.93           C  
ATOM   3484  C   ARG A 460     119.009 172.515 184.717  1.00 26.93           C  
ATOM   3485  O   ARG A 460     120.107 172.677 184.175  1.00 26.93           O  
ATOM   3486  CB  ARG A 460     118.900 171.872 187.139  1.00 26.93           C  
ATOM   3487  CG  ARG A 460     119.161 172.314 188.564  1.00 26.93           C  
ATOM   3488  CD  ARG A 460     119.183 171.142 189.531  1.00 26.93           C  
ATOM   3489  NE  ARG A 460     120.357 170.296 189.344  1.00 26.93           N  
ATOM   3490  CZ  ARG A 460     120.478 169.059 189.816  1.00 26.93           C  
ATOM   3491  NH1 ARG A 460     121.589 168.376 189.591  1.00 26.93           N  
ATOM   3492  NH2 ARG A 460     119.493 168.499 190.508  1.00 26.93           N  
ATOM   3493  N   PHE A 461     117.998 171.910 184.086  1.00 19.72           N  
ATOM   3494  CA  PHE A 461     118.239 171.092 182.903  1.00 19.72           C  
ATOM   3495  C   PHE A 461     117.611 171.582 181.602  1.00 19.72           C  
ATOM   3496  O   PHE A 461     118.091 171.185 180.535  1.00 19.72           O  
ATOM   3497  CB  PHE A 461     117.761 169.655 183.150  1.00 19.72           C  
ATOM   3498  CG  PHE A 461     118.449 168.984 184.300  1.00 19.72           C  
ATOM   3499  CD1 PHE A 461     119.761 168.574 184.190  1.00 19.72           C  
ATOM   3500  CD2 PHE A 461     117.788 168.766 185.488  1.00 19.72           C  
ATOM   3501  CE1 PHE A 461     120.399 167.960 185.240  1.00 19.72           C  
ATOM   3502  CE2 PHE A 461     118.424 168.149 186.544  1.00 19.72           C  
ATOM   3503  CZ  PHE A 461     119.731 167.747 186.417  1.00 19.72           C  
ATOM   3504  N   LEU A 462     116.565 172.408 181.638  1.00 17.67           N  
ATOM   3505  CA  LEU A 462     115.908 172.849 180.404  1.00 17.67           C  
ATOM   3506  C   LEU A 462     116.586 174.136 179.934  1.00 17.67           C  
ATOM   3507  O   LEU A 462     116.085 175.249 180.101  1.00 17.67           O  
ATOM   3508  CB  LEU A 462     114.406 173.018 180.608  1.00 17.67           C  
ATOM   3509  CG  LEU A 462     113.587 171.731 180.436  1.00 17.67           C  
ATOM   3510  CD1 LEU A 462     114.155 170.600 181.266  1.00 17.67           C  
ATOM   3511  CD2 LEU A 462     112.137 171.951 180.784  1.00 17.67           C  
ATOM   3512  N   SER A 463     117.765 173.957 179.332  1.00 13.19           N  
ATOM   3513  CA  SER A 463     118.633 175.034 178.872  1.00 13.19           C  
ATOM   3514  C   SER A 463     119.719 174.445 177.974  1.00 13.19           C  
ATOM   3515  O   SER A 463     119.789 173.220 177.823  1.00 13.19           O  
ATOM   3516  CB  SER A 463     119.249 175.763 180.066  1.00 13.19           C  
ATOM   3517  OG  SER A 463     120.180 174.936 180.730  1.00 13.19           O  
ATOM   3518  N   PRO A 464     120.576 175.260 177.360  1.00 10.57           N  
ATOM   3519  CA  PRO A 464     121.650 174.723 176.511  1.00 10.57           C  
ATOM   3520  C   PRO A 464     122.980 174.469 177.209  1.00 10.57           C  
ATOM   3521  O   PRO A 464     123.966 174.209 176.514  1.00 10.57           O  
ATOM   3522  CB  PRO A 464     121.808 175.826 175.455  1.00 10.57           C  
ATOM   3523  CG  PRO A 464     121.390 177.071 176.126  1.00 10.57           C  
ATOM   3524  CD  PRO A 464     120.509 176.729 177.282  1.00 10.57           C  
ATOM   3525  N   PHE A 465     123.048 174.508 178.540  1.00 14.57           N  
ATOM   3526  CA  PHE A 465     124.337 174.586 179.222  1.00 14.57           C  
ATOM   3527  C   PHE A 465     124.900 173.240 179.670  1.00 14.57           C  
ATOM   3528  O   PHE A 465     126.121 173.114 179.772  1.00 14.57           O  
ATOM   3529  CB  PHE A 465     124.236 175.539 180.416  1.00 14.57           C  
ATOM   3530  CG  PHE A 465     123.941 176.959 180.018  1.00 14.57           C  
ATOM   3531  CD1 PHE A 465     124.780 177.638 179.148  1.00 14.57           C  
ATOM   3532  CD2 PHE A 465     122.816 177.606 180.488  1.00 14.57           C  
ATOM   3533  CE1 PHE A 465     124.506 178.937 178.763  1.00 14.57           C  
ATOM   3534  CE2 PHE A 465     122.540 178.905 180.106  1.00 14.57           C  
ATOM   3535  CZ  PHE A 465     123.387 179.569 179.243  1.00 14.57           C  
ATOM   3536  N   VAL A 466     124.078 172.229 179.951  1.00 11.52           N  
ATOM   3537  CA  VAL A 466     124.632 170.900 180.218  1.00 11.52           C  
ATOM   3538  C   VAL A 466     125.249 170.323 178.946  1.00 11.52           C  
ATOM   3539  O   VAL A 466     126.381 169.820 178.951  1.00 11.52           O  
ATOM   3540  CB  VAL A 466     123.559 169.963 180.803  1.00 11.52           C  
ATOM   3541  CG1 VAL A 466     124.116 168.556 180.979  1.00 11.52           C  
ATOM   3542  CG2 VAL A 466     123.052 170.486 182.135  1.00 11.52           C  
ATOM   3543  N   ALA A 467     124.513 170.402 177.835  1.00  9.28           N  
ATOM   3544  CA  ALA A 467     125.061 170.003 176.544  1.00  9.28           C  
ATOM   3545  C   ALA A 467     126.357 170.746 176.238  1.00  9.28           C  
ATOM   3546  O   ALA A 467     127.301 170.163 175.695  1.00  9.28           O  
ATOM   3547  CB  ALA A 467     124.027 170.240 175.441  1.00  9.28           C  
ATOM   3548  N   ALA A 468     126.429 172.030 176.592  1.00  9.02           N  
ATOM   3549  CA  ALA A 468     127.654 172.790 176.362  1.00  9.02           C  
ATOM   3550  C   ALA A 468     128.776 172.316 177.282  1.00  9.02           C  
ATOM   3551  O   ALA A 468     129.923 172.168 176.849  1.00  9.02           O  
ATOM   3552  CB  ALA A 468     127.391 174.281 176.558  1.00  9.02           C  
ATOM   3553  N   GLU A 469     128.456 172.064 178.553  1.00 12.61           N  
ATOM   3554  CA  GLU A 469     129.450 171.596 179.514  1.00 12.61           C  
ATOM   3555  C   GLU A 469     130.046 170.258 179.100  1.00 12.61           C  
ATOM   3556  O   GLU A 469     131.203 169.971 179.424  1.00 12.61           O  
ATOM   3557  CB  GLU A 469     128.819 171.486 180.903  1.00 12.61           C  
ATOM   3558  CG  GLU A 469     128.747 172.789 181.674  1.00 12.61           C  
ATOM   3559  CD  GLU A 469     127.698 172.770 182.766  1.00 12.61           C  
ATOM   3560  OE1 GLU A 469     127.528 171.717 183.414  1.00 12.61           O  
ATOM   3561  OE2 GLU A 469     127.046 173.813 182.981  1.00 12.61           O  
ATOM   3562  N   ARG A 470     129.278 169.427 178.399  1.00 12.80           N  
ATOM   3563  CA  ARG A 470     129.776 168.146 177.915  1.00 12.80           C  
ATOM   3564  C   ARG A 470     130.436 168.234 176.543  1.00 12.80           C  
ATOM   3565  O   ARG A 470     131.007 167.239 176.086  1.00 12.80           O  
ATOM   3566  CB  ARG A 470     128.636 167.123 177.861  1.00 12.80           C  
ATOM   3567  CG  ARG A 470     128.011 166.795 179.207  1.00 12.80           C  
ATOM   3568  CD  ARG A 470     128.991 166.151 180.173  1.00 12.80           C  
ATOM   3569  NE  ARG A 470     129.653 164.982 179.600  1.00 12.80           N  
ATOM   3570  CZ  ARG A 470     129.487 163.727 180.016  1.00 12.80           C  
ATOM   3571  NH1 ARG A 470     128.676 163.434 181.024  1.00 12.80           N  
ATOM   3572  NH2 ARG A 470     130.146 162.751 179.414  1.00 12.80           N  
ATOM   3573  N   GLY A 471     130.389 169.388 175.888  1.00  9.91           N  
ATOM   3574  CA  GLY A 471     130.957 169.531 174.562  1.00  9.91           C  
ATOM   3575  C   GLY A 471     130.100 169.012 173.429  1.00  9.91           C  
ATOM   3576  O   GLY A 471     130.614 168.797 172.329  1.00  9.91           O  
ATOM   3577  N   TYR A 472     128.805 168.800 173.662  1.00 10.33           N  
ATOM   3578  CA  TYR A 472     127.913 168.358 172.596  1.00 10.33           C  
ATOM   3579  C   TYR A 472     127.485 169.510 171.691  1.00 10.33           C  
ATOM   3580  O   TYR A 472     127.139 169.281 170.529  1.00 10.33           O  
ATOM   3581  CB  TYR A 472     126.685 167.667 173.194  1.00 10.33           C  
ATOM   3582  CG  TYR A 472     126.986 166.464 174.066  1.00 10.33           C  
ATOM   3583  CD1 TYR A 472     128.204 165.804 173.993  1.00 10.33           C  
ATOM   3584  CD2 TYR A 472     126.046 165.984 174.961  1.00 10.33           C  
ATOM   3585  CE1 TYR A 472     128.471 164.712 174.783  1.00 10.33           C  
ATOM   3586  CE2 TYR A 472     126.305 164.899 175.752  1.00 10.33           C  
ATOM   3587  CZ  TYR A 472     127.518 164.264 175.662  1.00 10.33           C  
ATOM   3588  OH  TYR A 472     127.769 163.176 176.457  1.00 10.33           O  
ATOM   3589  N   ILE A 473     127.483 170.737 172.204  1.00  9.62           N  
ATOM   3590  CA  ILE A 473     127.287 171.944 171.407  1.00  9.62           C  
ATOM   3591  C   ILE A 473     128.619 172.674 171.338  1.00  9.62           C  
ATOM   3592  O   ILE A 473     129.326 172.794 172.345  1.00  9.62           O  
ATOM   3593  CB  ILE A 473     126.185 172.852 171.994  1.00  9.62           C  
ATOM   3594  CG1 ILE A 473     124.812 172.189 171.864  1.00  9.62           C  
ATOM   3595  CG2 ILE A 473     126.178 174.242 171.326  1.00  9.62           C  
ATOM   3596  CD1 ILE A 473     124.278 172.119 170.462  1.00  9.62           C  
ATOM   3597  N   ASP A 474     128.969 173.151 170.144  1.00 11.35           N  
ATOM   3598  CA  ASP A 474     130.246 173.830 169.967  1.00 11.35           C  
ATOM   3599  C   ASP A 474     130.208 175.264 170.492  1.00 11.35           C  
ATOM   3600  O   ASP A 474     131.182 175.725 171.092  1.00 11.35           O  
ATOM   3601  CB  ASP A 474     130.659 173.806 168.497  1.00 11.35           C  
ATOM   3602  CG  ASP A 474     130.913 172.399 167.984  1.00 11.35           C  
ATOM   3603  OD1 ASP A 474     131.825 171.728 168.510  1.00 11.35           O  
ATOM   3604  OD2 ASP A 474     130.194 171.959 167.063  1.00 11.35           O  
ATOM   3605  N   GLU A 475     129.107 175.983 170.277  1.00 12.89           N  
ATOM   3606  CA  GLU A 475     128.977 177.340 170.794  1.00 12.89           C  
ATOM   3607  C   GLU A 475     127.503 177.705 170.927  1.00 12.89           C  
ATOM   3608  O   GLU A 475     126.662 177.230 170.161  1.00 12.89           O  
ATOM   3609  CB  GLU A 475     129.695 178.348 169.888  1.00 12.89           C  
ATOM   3610  CG  GLU A 475     129.606 179.800 170.336  1.00 12.89           C  
ATOM   3611  CD  GLU A 475     130.147 180.023 171.733  1.00 12.89           C  
ATOM   3612  OE1 GLU A 475     129.486 179.604 172.706  1.00 12.89           O  
ATOM   3613  OE2 GLU A 475     131.238 180.617 171.858  1.00 12.89           O  
ATOM   3614  N   VAL A 476     127.204 178.541 171.919  1.00 10.07           N  
ATOM   3615  CA  VAL A 476     125.906 179.192 172.064  1.00 10.07           C  
ATOM   3616  C   VAL A 476     126.015 180.577 171.435  1.00 10.07           C  
ATOM   3617  O   VAL A 476     126.827 181.401 171.873  1.00 10.07           O  
ATOM   3618  CB  VAL A 476     125.480 179.277 173.541  1.00 10.07           C  
ATOM   3619  CG1 VAL A 476     124.096 179.892 173.685  1.00 10.07           C  
ATOM   3620  CG2 VAL A 476     125.512 177.902 174.205  1.00 10.07           C  
ATOM   3621  N   ILE A 477     125.200 180.838 170.414  1.00  9.67           N  
ATOM   3622  CA  ILE A 477     125.324 182.034 169.590  1.00  9.67           C  
ATOM   3623  C   ILE A 477     124.101 182.923 169.782  1.00  9.67           C  
ATOM   3624  O   ILE A 477     123.038 182.483 170.226  1.00  9.67           O  
ATOM   3625  CB  ILE A 477     125.520 181.695 168.092  1.00  9.67           C  
ATOM   3626  CG1 ILE A 477     124.283 181.000 167.506  1.00  9.67           C  
ATOM   3627  CG2 ILE A 477     126.776 180.853 167.893  1.00  9.67           C  
ATOM   3628  CD1 ILE A 477     124.274 180.890 165.994  1.00  9.67           C  
ATOM   3629  N   MET A 478     124.265 184.203 169.440  1.00 15.98           N  
ATOM   3630  CA  MET A 478     123.121 185.102 169.382  1.00 15.98           C  
ATOM   3631  C   MET A 478     122.387 184.915 168.052  1.00 15.98           C  
ATOM   3632  O   MET A 478     123.027 184.710 167.018  1.00 15.98           O  
ATOM   3633  CB  MET A 478     123.552 186.560 169.528  1.00 15.98           C  
ATOM   3634  CG  MET A 478     123.996 186.970 170.931  1.00 15.98           C  
ATOM   3635  SD  MET A 478     122.653 187.033 172.131  1.00 15.98           S  
ATOM   3636  CE  MET A 478     121.732 188.462 171.557  1.00 15.98           C  
ATOM   3637  N   PRO A 479     121.054 184.990 168.046  1.00 11.30           N  
ATOM   3638  CA  PRO A 479     120.316 184.736 166.796  1.00 11.30           C  
ATOM   3639  C   PRO A 479     120.751 185.602 165.620  1.00 11.30           C  
ATOM   3640  O   PRO A 479     120.895 185.088 164.504  1.00 11.30           O  
ATOM   3641  CB  PRO A 479     118.861 185.007 167.203  1.00 11.30           C  
ATOM   3642  CG  PRO A 479     118.829 184.759 168.662  1.00 11.30           C  
ATOM   3643  CD  PRO A 479     120.144 185.230 169.177  1.00 11.30           C  
ATOM   3644  N   HIS A 480     120.978 186.900 165.839  1.00 13.07           N  
ATOM   3645  CA  HIS A 480     121.261 187.806 164.729  1.00 13.07           C  
ATOM   3646  C   HIS A 480     122.538 187.450 163.972  1.00 13.07           C  
ATOM   3647  O   HIS A 480     122.717 187.921 162.844  1.00 13.07           O  
ATOM   3648  CB  HIS A 480     121.339 189.255 165.221  1.00 13.07           C  
ATOM   3649  CG  HIS A 480     122.393 189.504 166.253  1.00 13.07           C  
ATOM   3650  ND1 HIS A 480     122.089 189.818 167.558  1.00 13.07           N  
ATOM   3651  CD2 HIS A 480     123.745 189.513 166.171  1.00 13.07           C  
ATOM   3652  CE1 HIS A 480     123.205 189.994 168.240  1.00 13.07           C  
ATOM   3653  NE2 HIS A 480     124.224 189.817 167.421  1.00 13.07           N  
ATOM   3654  N   SER A 481     123.424 186.648 164.553  1.00 10.65           N  
ATOM   3655  CA  SER A 481     124.659 186.227 163.903  1.00 10.65           C  
ATOM   3656  C   SER A 481     124.506 184.962 163.059  1.00 10.65           C  
ATOM   3657  O   SER A 481     125.477 184.555 162.411  1.00 10.65           O  
ATOM   3658  CB  SER A 481     125.747 186.009 164.959  1.00 10.65           C  
ATOM   3659  OG  SER A 481     125.306 185.122 165.967  1.00 10.65           O  
ATOM   3660  N   THR A 482     123.312 184.365 163.010  1.00  8.65           N  
ATOM   3661  CA  THR A 482     123.151 183.034 162.425  1.00  8.65           C  
ATOM   3662  C   THR A 482     123.784 182.950 161.037  1.00  8.65           C  
ATOM   3663  O   THR A 482     124.737 182.192 160.822  1.00  8.65           O  
ATOM   3664  CB  THR A 482     121.665 182.658 162.374  1.00  8.65           C  
ATOM   3665  OG1 THR A 482     121.172 182.461 163.702  1.00  8.65           O  
ATOM   3666  CG2 THR A 482     121.444 181.376 161.579  1.00  8.65           C  
ATOM   3667  N   ARG A 483     123.278 183.741 160.088  1.00  9.60           N  
ATOM   3668  CA  ARG A 483     123.831 183.728 158.736  1.00  9.60           C  
ATOM   3669  C   ARG A 483     125.347 183.860 158.776  1.00  9.60           C  
ATOM   3670  O   ARG A 483     126.071 183.017 158.233  1.00  9.60           O  
ATOM   3671  CB  ARG A 483     123.201 184.846 157.897  1.00  9.60           C  
ATOM   3672  CG  ARG A 483     123.621 184.875 156.423  1.00  9.60           C  
ATOM   3673  CD  ARG A 483     122.869 185.934 155.623  1.00  9.60           C  
ATOM   3674  NE  ARG A 483     123.645 186.431 154.491  1.00  9.60           N  
ATOM   3675  CZ  ARG A 483     123.720 185.844 153.301  1.00  9.60           C  
ATOM   3676  NH1 ARG A 483     123.070 184.719 153.056  1.00  9.60           N  
ATOM   3677  NH2 ARG A 483     124.458 186.387 152.345  1.00  9.60           N  
ATOM   3678  N   LYS A 484     125.845 184.878 159.483  1.00 11.36           N  
ATOM   3679  CA  LYS A 484     127.281 185.135 159.510  1.00 11.36           C  
ATOM   3680  C   LYS A 484     128.052 183.901 159.957  1.00 11.36           C  
ATOM   3681  O   LYS A 484     129.109 183.587 159.400  1.00 11.36           O  
ATOM   3682  CB  LYS A 484     127.580 186.330 160.419  1.00 11.36           C  
ATOM   3683  CG  LYS A 484     129.051 186.539 160.732  1.00 11.36           C  
ATOM   3684  CD  LYS A 484     129.303 187.935 161.285  1.00 11.36           C  
ATOM   3685  CE  LYS A 484     130.770 188.169 161.590  1.00 11.36           C  
ATOM   3686  NZ  LYS A 484     131.092 189.620 161.615  1.00 11.36           N  
ATOM   3687  N   ARG A 485     127.527 183.170 160.939  1.00  9.03           N  
ATOM   3688  CA  ARG A 485     128.208 181.958 161.379  1.00  9.03           C  
ATOM   3689  C   ARG A 485     128.158 180.897 160.285  1.00  9.03           C  
ATOM   3690  O   ARG A 485     129.200 180.379 159.862  1.00  9.03           O  
ATOM   3691  CB  ARG A 485     127.593 181.447 162.686  1.00  9.03           C  
ATOM   3692  CG  ARG A 485     127.672 182.421 163.869  1.00  9.03           C  
ATOM   3693  CD  ARG A 485     129.083 182.822 164.248  1.00  9.03           C  
ATOM   3694  NE  ARG A 485     129.797 181.784 164.982  1.00  9.03           N  
ATOM   3695  CZ  ARG A 485     130.184 181.877 166.254  1.00  9.03           C  
ATOM   3696  NH1 ARG A 485     129.924 182.959 166.975  1.00  9.03           N  
ATOM   3697  NH2 ARG A 485     130.839 180.872 166.812  1.00  9.03           N  
ATOM   3698  N   ILE A 486     126.959 180.620 159.761  1.00  6.94           N  
ATOM   3699  CA  ILE A 486     126.806 179.566 158.758  1.00  6.94           C  
ATOM   3700  C   ILE A 486     127.769 179.802 157.600  1.00  6.94           C  
ATOM   3701  O   ILE A 486     128.607 178.950 157.280  1.00  6.94           O  
ATOM   3702  CB  ILE A 486     125.342 179.481 158.280  1.00  6.94           C  
ATOM   3703  CG1 ILE A 486     124.475 178.752 159.314  1.00  6.94           C  
ATOM   3704  CG2 ILE A 486     125.236 178.753 156.941  1.00  6.94           C  
ATOM   3705  CD1 ILE A 486     122.996 179.055 159.210  1.00  6.94           C  
ATOM   3706  N   ALA A 487     127.709 180.996 157.003  1.00  7.94           N  
ATOM   3707  CA  ALA A 487     128.554 181.305 155.853  1.00  7.94           C  
ATOM   3708  C   ALA A 487     130.021 181.010 156.140  1.00  7.94           C  
ATOM   3709  O   ALA A 487     130.727 180.455 155.292  1.00  7.94           O  
ATOM   3710  CB  ALA A 487     128.376 182.764 155.438  1.00  7.94           C  
ATOM   3711  N   ARG A 488     130.497 181.351 157.339  1.00 10.17           N  
ATOM   3712  CA  ARG A 488     131.895 181.081 157.651  1.00 10.17           C  
ATOM   3713  C   ARG A 488     132.141 179.579 157.718  1.00 10.17           C  
ATOM   3714  O   ARG A 488     133.008 179.048 157.012  1.00 10.17           O  
ATOM   3715  CB  ARG A 488     132.292 181.776 158.959  1.00 10.17           C  
ATOM   3716  CG  ARG A 488     133.785 181.915 159.166  1.00 10.17           C  
ATOM   3717  CD  ARG A 488     134.114 182.956 160.224  1.00 10.17           C  
ATOM   3718  NE  ARG A 488     133.596 182.595 161.539  1.00 10.17           N  
ATOM   3719  CZ  ARG A 488     133.919 183.222 162.665  1.00 10.17           C  
ATOM   3720  NH1 ARG A 488     134.759 184.247 162.640  1.00 10.17           N  
ATOM   3721  NH2 ARG A 488     133.402 182.820 163.816  1.00 10.17           N  
ATOM   3722  N   ALA A 489     131.325 178.869 158.498  1.00  7.75           N  
ATOM   3723  CA  ALA A 489     131.518 177.436 158.683  1.00  7.75           C  
ATOM   3724  C   ALA A 489     131.629 176.724 157.342  1.00  7.75           C  
ATOM   3725  O   ALA A 489     132.632 176.061 157.053  1.00  7.75           O  
ATOM   3726  CB  ALA A 489     130.371 176.859 159.508  1.00  7.75           C  
ATOM   3727  N   LEU A 490     130.615 176.896 156.492  1.00  6.88           N  
ATOM   3728  CA  LEU A 490     130.587 176.199 155.213  1.00  6.88           C  
ATOM   3729  C   LEU A 490     131.894 176.415 154.464  1.00  6.88           C  
ATOM   3730  O   LEU A 490     132.506 175.461 153.970  1.00  6.88           O  
ATOM   3731  CB  LEU A 490     129.382 176.666 154.386  1.00  6.88           C  
ATOM   3732  CG  LEU A 490     127.999 176.213 154.872  1.00  6.88           C  
ATOM   3733  CD1 LEU A 490     126.889 176.915 154.088  1.00  6.88           C  
ATOM   3734  CD2 LEU A 490     127.858 174.709 154.779  1.00  6.88           C  
ATOM   3735  N   GLY A 491     132.372 177.659 154.430  1.00  8.10           N  
ATOM   3736  CA  GLY A 491     133.635 177.948 153.786  1.00  8.10           C  
ATOM   3737  C   GLY A 491     134.717 176.992 154.240  1.00  8.10           C  
ATOM   3738  O   GLY A 491     135.244 176.199 153.449  1.00  8.10           O  
ATOM   3739  N   MET A 492     134.998 177.013 155.544  1.00  8.74           N  
ATOM   3740  CA  MET A 492     136.065 176.183 156.091  1.00  8.74           C  
ATOM   3741  C   MET A 492     135.841 174.711 155.788  1.00  8.74           C  
ATOM   3742  O   MET A 492     136.808 173.960 155.621  1.00  8.74           O  
ATOM   3743  CB  MET A 492     136.167 176.401 157.598  1.00  8.74           C  
ATOM   3744  CG  MET A 492     137.043 175.408 158.345  1.00  8.74           C  
ATOM   3745  SD  MET A 492     136.191 173.914 158.879  1.00  8.74           S  
ATOM   3746  CE  MET A 492     135.400 174.497 160.372  1.00  8.74           C  
ATOM   3747  N   LEU A 493     134.584 174.280 155.725  1.00  6.78           N  
ATOM   3748  CA  LEU A 493     134.284 172.866 155.576  1.00  6.78           C  
ATOM   3749  C   LEU A 493     134.389 172.381 154.134  1.00  6.78           C  
ATOM   3750  O   LEU A 493     134.274 171.174 153.904  1.00  6.78           O  
ATOM   3751  CB  LEU A 493     132.888 172.572 156.140  1.00  6.78           C  
ATOM   3752  CG  LEU A 493     132.738 172.669 157.667  1.00  6.78           C  
ATOM   3753  CD1 LEU A 493     131.275 172.600 158.108  1.00  6.78           C  
ATOM   3754  CD2 LEU A 493     133.555 171.595 158.390  1.00  6.78           C  
ATOM   3755  N   ARG A 494     134.616 173.275 153.165  1.00  9.86           N  
ATOM   3756  CA  ARG A 494     134.665 172.845 151.769  1.00  9.86           C  
ATOM   3757  C   ARG A 494     135.705 171.751 151.524  1.00  9.86           C  
ATOM   3758  O   ARG A 494     135.557 170.969 150.580  1.00  9.86           O  
ATOM   3759  CB  ARG A 494     134.933 174.043 150.859  1.00  9.86           C  
ATOM   3760  CG  ARG A 494     133.746 174.981 150.747  1.00  9.86           C  
ATOM   3761  CD  ARG A 494     133.991 176.127 149.794  1.00  9.86           C  
ATOM   3762  NE  ARG A 494     132.888 177.087 149.812  1.00  9.86           N  
ATOM   3763  CZ  ARG A 494     133.002 178.373 149.496  1.00  9.86           C  
ATOM   3764  NH1 ARG A 494     134.172 178.874 149.127  1.00  9.86           N  
ATOM   3765  NH2 ARG A 494     131.939 179.163 149.547  1.00  9.86           N  
ATOM   3766  N   THR A 495     136.752 171.671 152.347  1.00  7.69           N  
ATOM   3767  CA  THR A 495     137.836 170.717 152.141  1.00  7.69           C  
ATOM   3768  C   THR A 495     137.636 169.389 152.879  1.00  7.69           C  
ATOM   3769  O   THR A 495     138.560 168.573 152.910  1.00  7.69           O  
ATOM   3770  CB  THR A 495     139.170 171.349 152.559  1.00  7.69           C  
ATOM   3771  OG1 THR A 495     139.058 171.885 153.880  1.00  7.69           O  
ATOM   3772  CG2 THR A 495     139.581 172.455 151.594  1.00  7.69           C  
ATOM   3773  N   LYS A 496     136.458 169.151 153.455  1.00  7.61           N  
ATOM   3774  CA  LYS A 496     136.192 167.907 154.176  1.00  7.61           C  
ATOM   3775  C   LYS A 496     136.331 166.696 153.261  1.00  7.61           C  
ATOM   3776  O   LYS A 496     135.714 166.636 152.196  1.00  7.61           O  
ATOM   3777  CB  LYS A 496     134.783 167.941 154.782  1.00  7.61           C  
ATOM   3778  CG  LYS A 496     134.401 166.735 155.645  1.00  7.61           C  
ATOM   3779  CD  LYS A 496     132.957 166.813 156.141  1.00  7.61           C  
ATOM   3780  CE  LYS A 496     132.579 165.618 157.002  1.00  7.61           C  
ATOM   3781  NZ  LYS A 496     131.142 165.598 157.353  1.00  7.61           N  
ATOM   3782  N   GLU A 497     137.142 165.725 153.684  1.00 15.67           N  
ATOM   3783  CA  GLU A 497     137.212 164.421 153.034  1.00 15.67           C  
ATOM   3784  C   GLU A 497     137.039 163.326 154.075  1.00 15.67           C  
ATOM   3785  O   GLU A 497     137.671 163.358 155.134  1.00 15.67           O  
ATOM   3786  CB  GLU A 497     138.516 164.209 152.250  1.00 15.67           C  
ATOM   3787  CG  GLU A 497     139.800 164.662 152.878  1.00 15.67           C  
ATOM   3788  CD  GLU A 497     140.996 164.287 152.011  1.00 15.67           C  
ATOM   3789  OE1 GLU A 497     140.906 163.275 151.285  1.00 15.67           O  
ATOM   3790  OE2 GLU A 497     142.017 165.000 152.040  1.00 15.67           O  
ATOM   3791  N   MET A 498     136.191 162.356 153.748  1.00 20.25           N  
ATOM   3792  CA  MET A 498     135.730 161.305 154.644  1.00 20.25           C  
ATOM   3793  C   MET A 498     135.092 160.215 153.796  1.00 20.25           C  
ATOM   3794  O   MET A 498     134.465 160.502 152.773  1.00 20.25           O  
ATOM   3795  CB  MET A 498     134.726 161.846 155.670  1.00 20.25           C  
ATOM   3796  CG  MET A 498     134.127 160.810 156.588  1.00 20.25           C  
ATOM   3797  SD  MET A 498     132.839 161.521 157.628  1.00 20.25           S  
ATOM   3798  CE  MET A 498     132.628 160.203 158.815  1.00 20.25           C  
ATOM   3799  N   GLU A 499     135.250 158.968 154.236  1.00 24.61           N  
ATOM   3800  CA  GLU A 499     134.767 157.815 153.489  1.00 24.61           C  
ATOM   3801  C   GLU A 499     134.214 156.766 154.445  1.00 24.61           C  
ATOM   3802  O   GLU A 499     134.753 156.548 155.533  1.00 24.61           O  
ATOM   3803  CB  GLU A 499     135.885 157.219 152.619  1.00 24.61           C  
ATOM   3804  CG  GLU A 499     137.142 156.826 153.386  1.00 24.61           C  
ATOM   3805  CD  GLU A 499     137.092 155.410 153.924  1.00 24.61           C  
ATOM   3806  OE1 GLU A 499     136.310 154.596 153.393  1.00 24.61           O  
ATOM   3807  OE2 GLU A 499     137.836 155.109 154.881  1.00 24.61           O  
ATOM   3808  N   GLN A 500     133.128 156.125 154.022  1.00 17.10           N  
ATOM   3809  CA  GLN A 500     132.527 155.008 154.735  1.00 17.10           C  
ATOM   3810  C   GLN A 500     133.252 153.714 154.374  1.00 17.10           C  
ATOM   3811  O   GLN A 500     133.983 153.656 153.385  1.00 17.10           O  
ATOM   3812  CB  GLN A 500     131.041 154.919 154.384  1.00 17.10           C  
ATOM   3813  CG  GLN A 500     130.191 156.122 154.806  1.00 17.10           C  
ATOM   3814  CD  GLN A 500     129.634 155.989 156.208  1.00 17.10           C  
ATOM   3815  OE1 GLN A 500     129.180 154.919 156.613  1.00 17.10           O  
ATOM   3816  NE2 GLN A 500     129.657 157.083 156.953  1.00 17.10           N  
ATOM   3817  N   PRO A 501     133.068 152.645 155.154  1.00 14.73           N  
ATOM   3818  CA  PRO A 501     133.742 151.378 154.835  1.00 14.73           C  
ATOM   3819  C   PRO A 501     133.303 150.816 153.488  1.00 14.73           C  
ATOM   3820  O   PRO A 501     132.270 151.192 152.932  1.00 14.73           O  
ATOM   3821  CB  PRO A 501     133.339 150.448 155.991  1.00 14.73           C  
ATOM   3822  CG  PRO A 501     132.222 151.121 156.679  1.00 14.73           C  
ATOM   3823  CD  PRO A 501     132.379 152.579 156.453  1.00 14.73           C  
ATOM   3824  N   ARG A 502     134.108 149.887 152.969  1.00 16.14           N  
ATOM   3825  CA  ARG A 502     133.917 149.382 151.612  1.00 16.14           C  
ATOM   3826  C   ARG A 502     132.807 148.336 151.571  1.00 16.14           C  
ATOM   3827  O   ARG A 502     132.787 147.404 152.380  1.00 16.14           O  
ATOM   3828  CB  ARG A 502     135.218 148.790 151.077  1.00 16.14           C  
ATOM   3829  CG  ARG A 502     136.231 149.823 150.616  1.00 16.14           C  
ATOM   3830  CD  ARG A 502     137.415 149.172 149.926  1.00 16.14           C  
ATOM   3831  NE  ARG A 502     138.501 148.887 150.859  1.00 16.14           N  
ATOM   3832  CZ  ARG A 502     139.523 149.704 151.103  1.00 16.14           C  
ATOM   3833  NH1 ARG A 502     140.457 149.347 151.971  1.00 16.14           N  
ATOM   3834  NH2 ARG A 502     139.616 150.875 150.486  1.00 16.14           N  
ATOM   3835  N   LYS A 503     131.898 148.486 150.613  1.00  9.72           N  
ATOM   3836  CA  LYS A 503     130.750 147.601 150.472  1.00  9.72           C  
ATOM   3837  C   LYS A 503     130.130 147.809 149.095  1.00  9.72           C  
ATOM   3838  O   LYS A 503     130.282 148.867 148.482  1.00  9.72           O  
ATOM   3839  CB  LYS A 503     129.721 147.866 151.576  1.00  9.72           C  
ATOM   3840  CG  LYS A 503     129.104 149.251 151.514  1.00  9.72           C  
ATOM   3841  CD  LYS A 503     128.216 149.571 152.710  1.00  9.72           C  
ATOM   3842  CE  LYS A 503     129.011 150.176 153.853  1.00  9.72           C  
ATOM   3843  NZ  LYS A 503     128.214 150.447 155.081  1.00  9.72           N  
ATOM   3844  N   LYS A 504     129.419 146.782 148.618  1.00  7.77           N  
ATOM   3845  CA  LYS A 504     128.628 146.934 147.399  1.00  7.77           C  
ATOM   3846  C   LYS A 504     127.586 148.031 147.573  1.00  7.77           C  
ATOM   3847  O   LYS A 504     127.497 148.960 146.764  1.00  7.77           O  
ATOM   3848  CB  LYS A 504     127.942 145.613 147.034  1.00  7.77           C  
ATOM   3849  CG  LYS A 504     128.807 144.553 146.408  1.00  7.77           C  
ATOM   3850  CD  LYS A 504     127.948 143.618 145.555  1.00  7.77           C  
ATOM   3851  CE  LYS A 504     128.395 142.192 145.667  1.00  7.77           C  
ATOM   3852  NZ  LYS A 504     127.405 141.266 145.063  1.00  7.77           N  
ATOM   3853  N   HIS A 505     126.786 147.925 148.628  1.00  8.16           N  
ATOM   3854  CA  HIS A 505     125.802 148.928 149.013  1.00  8.16           C  
ATOM   3855  C   HIS A 505     125.357 148.612 150.437  1.00  8.16           C  
ATOM   3856  O   HIS A 505     125.614 147.527 150.961  1.00  8.16           O  
ATOM   3857  CB  HIS A 505     124.608 148.973 148.052  1.00  8.16           C  
ATOM   3858  CG  HIS A 505     123.830 147.697 147.969  1.00  8.16           C  
ATOM   3859  ND1 HIS A 505     123.034 147.238 148.995  1.00  8.16           N  
ATOM   3860  CD2 HIS A 505     123.694 146.803 146.963  1.00  8.16           C  
ATOM   3861  CE1 HIS A 505     122.461 146.105 148.633  1.00  8.16           C  
ATOM   3862  NE2 HIS A 505     122.843 145.821 147.404  1.00  8.16           N  
ATOM   3863  N   ASP A 506     124.699 149.584 151.058  1.00  7.97           N  
ATOM   3864  CA  ASP A 506     124.161 149.432 152.400  1.00  7.97           C  
ATOM   3865  C   ASP A 506     122.860 148.628 152.370  1.00  7.97           C  
ATOM   3866  O   ASP A 506     122.368 148.230 151.314  1.00  7.97           O  
ATOM   3867  CB  ASP A 506     123.935 150.800 153.034  1.00  7.97           C  
ATOM   3868  CG  ASP A 506     122.929 151.637 152.267  1.00  7.97           C  
ATOM   3869  OD1 ASP A 506     121.721 151.351 152.365  1.00  7.97           O  
ATOM   3870  OD2 ASP A 506     123.346 152.581 151.561  1.00  7.97           O  
ATOM   3871  N   ASN A 507     122.303 148.371 153.555  1.00  8.30           N  
ATOM   3872  CA  ASN A 507     121.006 147.713 153.683  1.00  8.30           C  
ATOM   3873  C   ASN A 507     120.004 148.580 154.439  1.00  8.30           C  
ATOM   3874  O   ASN A 507     119.346 148.106 155.368  1.00  8.30           O  
ATOM   3875  CB  ASN A 507     121.125 146.359 154.382  1.00  8.30           C  
ATOM   3876  CG  ASN A 507     119.883 145.511 154.199  1.00  8.30           C  
ATOM   3877  OD1 ASN A 507     119.167 145.646 153.211  1.00  8.30           O  
ATOM   3878  ND2 ASN A 507     119.610 144.649 155.159  1.00  8.30           N  
ATOM   3879  N   ILE A 508     119.899 149.851 154.068  1.00  8.17           N  
ATOM   3880  CA  ILE A 508     118.926 150.776 154.649  1.00  8.17           C  
ATOM   3881  C   ILE A 508     117.550 150.116 154.703  1.00  8.17           C  
ATOM   3882  O   ILE A 508     117.158 149.442 153.741  1.00  8.17           O  
ATOM   3883  CB  ILE A 508     118.882 152.091 153.851  1.00  8.17           C  
ATOM   3884  CG1 ILE A 508     118.123 153.177 154.627  1.00  8.17           C  
ATOM   3885  CG2 ILE A 508     118.309 151.858 152.455  1.00  8.17           C  
ATOM   3886  CD1 ILE A 508     118.388 154.589 154.149  1.00  8.17           C  
ATOM   3887  N   PRO A 509     116.792 150.260 155.793  1.00 11.97           N  
ATOM   3888  CA  PRO A 509     115.425 149.727 155.805  1.00 11.97           C  
ATOM   3889  C   PRO A 509     114.550 150.427 154.778  1.00 11.97           C  
ATOM   3890  O   PRO A 509     114.747 151.600 154.459  1.00 11.97           O  
ATOM   3891  CB  PRO A 509     114.937 150.000 157.232  1.00 11.97           C  
ATOM   3892  CG  PRO A 509     115.893 150.919 157.829  1.00 11.97           C  
ATOM   3893  CD  PRO A 509     117.175 150.826 157.098  1.00 11.97           C  
ATOM   3894  N   LEU A 510     113.568 149.695 154.267  1.00 14.90           N  
ATOM   3895  CA  LEU A 510     112.669 150.232 153.253  1.00 14.90           C  
ATOM   3896  C   LEU A 510     111.215 150.189 153.718  1.00 14.90           C  
ATOM   3897  O   LEU A 510     110.852 149.414 154.601  1.00 14.90           O  
ATOM   3898  CB  LEU A 510     112.823 149.459 151.943  1.00 14.90           C  
ATOM   3899  CG  LEU A 510     114.246 149.352 151.404  1.00 14.90           C  
ATOM   3900  CD1 LEU A 510     114.318 148.412 150.213  1.00 14.90           C  
ATOM   3901  CD2 LEU A 510     114.786 150.720 151.053  1.00 14.90           C  
ATOM   3902  OXT LEU A 510     110.365 150.925 153.216  1.00 14.90           O  
TER    3903      LEU A 510                                                      
ATOM   3904  N   LEU B   5     144.084 135.385 193.923  1.00 46.40           N  
ATOM   3905  CA  LEU B   5     143.446 135.467 195.229  1.00 46.40           C  
ATOM   3906  C   LEU B   5     142.059 134.824 195.212  1.00 46.40           C  
ATOM   3907  O   LEU B   5     141.449 134.664 194.155  1.00 46.40           O  
ATOM   3908  CB  LEU B   5     143.328 136.926 195.684  1.00 46.40           C  
ATOM   3909  CG  LEU B   5     144.501 137.600 196.407  1.00 46.40           C  
ATOM   3910  CD1 LEU B   5     144.836 136.885 197.713  1.00 46.40           C  
ATOM   3911  CD2 LEU B   5     145.733 137.718 195.513  1.00 46.40           C  
ATOM   3912  N   GLU B   6     141.573 134.453 196.399  1.00 52.20           N  
ATOM   3913  CA  GLU B   6     140.180 134.043 196.541  1.00 52.20           C  
ATOM   3914  C   GLU B   6     139.248 135.244 196.462  1.00 52.20           C  
ATOM   3915  O   GLU B   6     138.105 135.124 196.002  1.00 52.20           O  
ATOM   3916  CB  GLU B   6     139.990 133.317 197.871  1.00 52.20           C  
ATOM   3917  CG  GLU B   6     141.053 132.275 198.164  1.00 52.20           C  
ATOM   3918  CD  GLU B   6     140.672 131.355 199.307  1.00 52.20           C  
ATOM   3919  OE1 GLU B   6     141.539 130.578 199.759  1.00 52.20           O  
ATOM   3920  OE2 GLU B   6     139.508 131.410 199.756  1.00 52.20           O  
ATOM   3921  N   LYS B   7     139.728 136.407 196.905  1.00 44.96           N  
ATOM   3922  CA  LYS B   7     138.940 137.631 196.844  1.00 44.96           C  
ATOM   3923  C   LYS B   7     138.533 137.950 195.409  1.00 44.96           C  
ATOM   3924  O   LYS B   7     137.452 138.498 195.167  1.00 44.96           O  
ATOM   3925  CB  LYS B   7     139.748 138.768 197.475  1.00 44.96           C  
ATOM   3926  CG  LYS B   7     139.441 140.182 196.992  1.00 44.96           C  
ATOM   3927  CD  LYS B   7     138.163 140.718 197.589  1.00 44.96           C  
ATOM   3928  CE  LYS B   7     137.702 141.948 196.846  1.00 44.96           C  
ATOM   3929  NZ  LYS B   7     137.193 141.588 195.506  1.00 44.96           N  
ATOM   3930  N   LEU B   8     139.381 137.606 194.440  1.00 38.52           N  
ATOM   3931  CA  LEU B   8     139.063 137.899 193.046  1.00 38.52           C  
ATOM   3932  C   LEU B   8     137.890 137.051 192.556  1.00 38.52           C  
ATOM   3933  O   LEU B   8     136.967 137.562 191.909  1.00 38.52           O  
ATOM   3934  CB  LEU B   8     140.300 137.678 192.174  1.00 38.52           C  
ATOM   3935  CG  LEU B   8     140.138 137.737 190.655  1.00 38.52           C  
ATOM   3936  CD1 LEU B   8     139.513 139.052 190.198  1.00 38.52           C  
ATOM   3937  CD2 LEU B   8     141.485 137.508 189.985  1.00 38.52           C  
ATOM   3938  N   GLU B   9     137.907 135.750 192.856  1.00 41.56           N  
ATOM   3939  CA  GLU B   9     136.766 134.906 192.516  1.00 41.56           C  
ATOM   3940  C   GLU B   9     135.514 135.335 193.271  1.00 41.56           C  
ATOM   3941  O   GLU B   9     134.401 135.215 192.745  1.00 41.56           O  
ATOM   3942  CB  GLU B   9     137.094 133.441 192.808  1.00 41.56           C  
ATOM   3943  CG  GLU B   9     135.985 132.461 192.464  1.00 41.56           C  
ATOM   3944  CD  GLU B   9     135.669 132.426 190.980  1.00 41.56           C  
ATOM   3945  OE1 GLU B   9     134.511 132.714 190.613  1.00 41.56           O  
ATOM   3946  OE2 GLU B   9     136.578 132.112 190.183  1.00 41.56           O  
ATOM   3947  N   GLU B  10     135.674 135.838 194.496  1.00 39.43           N  
ATOM   3948  CA  GLU B  10     134.534 136.398 195.215  1.00 39.43           C  
ATOM   3949  C   GLU B  10     133.949 137.586 194.460  1.00 39.43           C  
ATOM   3950  O   GLU B  10     132.728 137.704 194.306  1.00 39.43           O  
ATOM   3951  CB  GLU B  10     134.966 136.805 196.624  1.00 39.43           C  
ATOM   3952  CG  GLU B  10     133.831 136.931 197.622  1.00 39.43           C  
ATOM   3953  CD  GLU B  10     133.159 138.294 197.584  1.00 39.43           C  
ATOM   3954  OE1 GLU B  10     133.638 139.183 196.847  1.00 39.43           O  
ATOM   3955  OE2 GLU B  10     132.148 138.475 198.295  1.00 39.43           O  
ATOM   3956  N   ARG B  11     134.815 138.475 193.975  1.00 29.69           N  
ATOM   3957  CA  ARG B  11     134.359 139.632 193.208  1.00 29.69           C  
ATOM   3958  C   ARG B  11     133.640 139.195 191.936  1.00 29.69           C  
ATOM   3959  O   ARG B  11     132.630 139.793 191.540  1.00 29.69           O  
ATOM   3960  CB  ARG B  11     135.554 140.525 192.870  1.00 29.69           C  
ATOM   3961  CG  ARG B  11     135.205 141.974 192.521  1.00 29.69           C  
ATOM   3962  CD  ARG B  11     136.400 142.711 191.929  1.00 29.69           C  
ATOM   3963  NE  ARG B  11     137.223 143.382 192.933  1.00 29.69           N  
ATOM   3964  CZ  ARG B  11     137.101 144.658 193.287  1.00 29.69           C  
ATOM   3965  NH1 ARG B  11     136.176 145.433 192.739  1.00 29.69           N  
ATOM   3966  NH2 ARG B  11     137.909 145.162 194.205  1.00 29.69           N  
ATOM   3967  N   ARG B  12     134.141 138.141 191.290  1.00 29.12           N  
ATOM   3968  CA  ARG B  12     133.474 137.623 190.099  1.00 29.12           C  
ATOM   3969  C   ARG B  12     132.077 137.108 190.440  1.00 29.12           C  
ATOM   3970  O   ARG B  12     131.085 137.479 189.795  1.00 29.12           O  
ATOM   3971  CB  ARG B  12     134.311 136.513 189.460  1.00 29.12           C  
ATOM   3972  CG  ARG B  12     135.685 136.923 188.959  1.00 29.12           C  
ATOM   3973  CD  ARG B  12     136.277 135.809 188.116  1.00 29.12           C  
ATOM   3974  NE  ARG B  12     137.526 136.166 187.450  1.00 29.12           N  
ATOM   3975  CZ  ARG B  12     138.403 135.275 186.997  1.00 29.12           C  
ATOM   3976  NH1 ARG B  12     138.180 133.977 187.144  1.00 29.12           N  
ATOM   3977  NH2 ARG B  12     139.511 135.677 186.397  1.00 29.12           N  
ATOM   3978  N   ALA B  13     131.989 136.228 191.442  1.00 32.56           N  
ATOM   3979  CA  ALA B  13     130.696 135.704 191.867  1.00 32.56           C  
ATOM   3980  C   ALA B  13     129.732 136.822 192.239  1.00 32.56           C  
ATOM   3981  O   ALA B  13     128.523 136.699 192.017  1.00 32.56           O  
ATOM   3982  CB  ALA B  13     130.879 134.752 193.048  1.00 32.56           C  
ATOM   3983  N   GLN B  14     130.245 137.918 192.794  1.00 32.73           N  
ATOM   3984  CA  GLN B  14     129.379 139.019 193.192  1.00 32.73           C  
ATOM   3985  C   GLN B  14     128.951 139.864 192.002  1.00 32.73           C  
ATOM   3986  O   GLN B  14     127.900 140.512 192.056  1.00 32.73           O  
ATOM   3987  CB  GLN B  14     130.086 139.892 194.230  1.00 32.73           C  
ATOM   3988  CG  GLN B  14     129.151 140.711 195.103  1.00 32.73           C  
ATOM   3989  CD  GLN B  14     128.610 141.948 194.403  1.00 32.73           C  
ATOM   3990  OE1 GLN B  14     129.176 142.419 193.417  1.00 32.73           O  
ATOM   3991  NE2 GLN B  14     127.506 142.477 194.913  1.00 32.73           N  
ATOM   3992  N   ALA B  15     129.742 139.878 190.928  1.00 28.64           N  
ATOM   3993  CA  ALA B  15     129.302 140.571 189.724  1.00 28.64           C  
ATOM   3994  C   ALA B  15     128.296 139.747 188.934  1.00 28.64           C  
ATOM   3995  O   ALA B  15     127.469 140.313 188.212  1.00 28.64           O  
ATOM   3996  CB  ALA B  15     130.497 140.920 188.836  1.00 28.64           C  
ATOM   3997  N   ARG B  16     128.346 138.422 189.055  1.00 28.54           N  
ATOM   3998  CA  ARG B  16     127.420 137.590 188.289  1.00 28.54           C  
ATOM   3999  C   ARG B  16     125.977 137.664 188.785  1.00 28.54           C  
ATOM   4000  O   ARG B  16     125.107 137.064 188.146  1.00 28.54           O  
ATOM   4001  CB  ARG B  16     127.870 136.130 188.299  1.00 28.54           C  
ATOM   4002  CG  ARG B  16     129.244 135.888 187.731  1.00 28.54           C  
ATOM   4003  CD  ARG B  16     129.529 134.412 187.604  1.00 28.54           C  
ATOM   4004  NE  ARG B  16     130.869 134.162 187.085  1.00 28.54           N  
ATOM   4005  CZ  ARG B  16     131.925 133.849 187.830  1.00 28.54           C  
ATOM   4006  NH1 ARG B  16     133.096 133.642 187.251  1.00 28.54           N  
ATOM   4007  NH2 ARG B  16     131.823 133.744 189.147  1.00 28.54           N  
ATOM   4008  N   LEU B  17     125.686 138.366 189.881  1.00 30.31           N  
ATOM   4009  CA  LEU B  17     124.335 138.392 190.430  1.00 30.31           C  
ATOM   4010  C   LEU B  17     123.489 139.552 189.928  1.00 30.31           C  
ATOM   4011  O   LEU B  17     122.263 139.513 190.080  1.00 30.31           O  
ATOM   4012  CB  LEU B  17     124.380 138.457 191.958  1.00 30.31           C  
ATOM   4013  CG  LEU B  17     124.850 137.191 192.677  1.00 30.31           C  
ATOM   4014  CD1 LEU B  17     124.927 137.446 194.166  1.00 30.31           C  
ATOM   4015  CD2 LEU B  17     123.935 136.015 192.383  1.00 30.31           C  
ATOM   4016  N   GLY B  18     124.099 140.577 189.350  1.00 28.28           N  
ATOM   4017  CA  GLY B  18     123.313 141.690 188.848  1.00 28.28           C  
ATOM   4018  C   GLY B  18     122.574 142.393 189.967  1.00 28.28           C  
ATOM   4019  O   GLY B  18     123.155 142.768 190.991  1.00 28.28           O  
ATOM   4020  N   GLY B  19     121.272 142.583 189.770  1.00 27.66           N  
ATOM   4021  CA  GLY B  19     120.425 143.303 190.694  1.00 27.66           C  
ATOM   4022  C   GLY B  19     119.897 142.528 191.879  1.00 27.66           C  
ATOM   4023  O   GLY B  19     119.074 143.068 192.622  1.00 27.66           O  
ATOM   4024  N   GLY B  20     120.324 141.291 192.087  1.00 32.62           N  
ATOM   4025  CA  GLY B  20     120.018 140.566 193.304  1.00 32.62           C  
ATOM   4026  C   GLY B  20     119.223 139.295 193.054  1.00 32.62           C  
ATOM   4027  O   GLY B  20     118.704 139.043 191.968  1.00 32.62           O  
ATOM   4028  N   GLU B  21     119.143 138.494 194.121  1.00 38.19           N  
ATOM   4029  CA  GLU B  21     118.433 137.218 194.077  1.00 38.19           C  
ATOM   4030  C   GLU B  21     116.961 137.414 193.735  1.00 38.19           C  
ATOM   4031  O   GLU B  21     116.401 136.701 192.894  1.00 38.19           O  
ATOM   4032  CB  GLU B  21     118.556 136.515 195.430  1.00 38.19           C  
ATOM   4033  CG  GLU B  21     119.964 136.149 195.841  1.00 38.19           C  
ATOM   4034  CD  GLU B  21     120.564 135.065 194.976  1.00 38.19           C  
ATOM   4035  OE1 GLU B  21     119.803 134.199 194.496  1.00 38.19           O  
ATOM   4036  OE2 GLU B  21     121.796 135.076 194.781  1.00 38.19           O  
ATOM   4037  N   LYS B  22     116.315 138.370 194.403  1.00 35.22           N  
ATOM   4038  CA  LYS B  22     114.868 138.517 194.301  1.00 35.22           C  
ATOM   4039  C   LYS B  22     114.444 138.930 192.896  1.00 35.22           C  
ATOM   4040  O   LYS B  22     113.449 138.425 192.360  1.00 35.22           O  
ATOM   4041  CB  LYS B  22     114.394 139.530 195.338  1.00 35.22           C  
ATOM   4042  CG  LYS B  22     112.900 139.620 195.486  1.00 35.22           C  
ATOM   4043  CD  LYS B  22     112.360 140.926 194.924  1.00 35.22           C  
ATOM   4044  CE  LYS B  22     110.843 140.911 194.849  1.00 35.22           C  
ATOM   4045  NZ  LYS B  22     110.293 142.184 194.300  1.00 35.22           N  
ATOM   4046  N   ARG B  23     115.190 139.840 192.277  1.00 30.09           N  
ATOM   4047  CA  ARG B  23     114.848 140.256 190.923  1.00 30.09           C  
ATOM   4048  C   ARG B  23     115.069 139.119 189.932  1.00 30.09           C  
ATOM   4049  O   ARG B  23     114.299 138.958 188.978  1.00 30.09           O  
ATOM   4050  CB  ARG B  23     115.661 141.491 190.539  1.00 30.09           C  
ATOM   4051  CG  ARG B  23     115.321 142.728 191.361  1.00 30.09           C  
ATOM   4052  CD  ARG B  23     115.821 144.001 190.698  1.00 30.09           C  
ATOM   4053  NE  ARG B  23     115.644 145.189 191.532  1.00 30.09           N  
ATOM   4054  CZ  ARG B  23     114.633 146.049 191.429  1.00 30.09           C  
ATOM   4055  NH1 ARG B  23     113.676 145.875 190.528  1.00 30.09           N  
ATOM   4056  NH2 ARG B  23     114.579 147.094 192.239  1.00 30.09           N  
ATOM   4057  N   LEU B  24     116.097 138.300 190.158  1.00 28.01           N  
ATOM   4058  CA  LEU B  24     116.346 137.166 189.274  1.00 28.01           C  
ATOM   4059  C   LEU B  24     115.241 136.120 189.390  1.00 28.01           C  
ATOM   4060  O   LEU B  24     114.797 135.559 188.378  1.00 28.01           O  
ATOM   4061  CB  LEU B  24     117.710 136.552 189.586  1.00 28.01           C  
ATOM   4062  CG  LEU B  24     118.955 137.413 189.340  1.00 28.01           C  
ATOM   4063  CD1 LEU B  24     120.182 136.735 189.940  1.00 28.01           C  
ATOM   4064  CD2 LEU B  24     119.168 137.706 187.866  1.00 28.01           C  
ATOM   4065  N   GLU B  25     114.772 135.849 190.611  1.00 29.20           N  
ATOM   4066  CA  GLU B  25     113.675 134.897 190.756  1.00 29.20           C  
ATOM   4067  C   GLU B  25     112.379 135.455 190.183  1.00 29.20           C  
ATOM   4068  O   GLU B  25     111.555 134.691 189.667  1.00 29.20           O  
ATOM   4069  CB  GLU B  25     113.490 134.490 192.223  1.00 29.20           C  
ATOM   4070  CG  GLU B  25     113.193 135.610 193.189  1.00 29.20           C  
ATOM   4071  CD  GLU B  25     111.728 136.012 193.212  1.00 29.20           C  
ATOM   4072  OE1 GLU B  25     110.878 135.218 192.753  1.00 29.20           O  
ATOM   4073  OE2 GLU B  25     111.425 137.122 193.697  1.00 29.20           O  
ATOM   4074  N   ALA B  26     112.183 136.772 190.248  1.00 23.86           N  
ATOM   4075  CA  ALA B  26     111.036 137.371 189.574  1.00 23.86           C  
ATOM   4076  C   ALA B  26     111.133 137.208 188.061  1.00 23.86           C  
ATOM   4077  O   ALA B  26     110.134 136.904 187.400  1.00 23.86           O  
ATOM   4078  CB  ALA B  26     110.923 138.845 189.943  1.00 23.86           C  
ATOM   4079  N   GLN B  27     112.322 137.419 187.493  1.00 19.24           N  
ATOM   4080  CA  GLN B  27     112.509 137.192 186.062  1.00 19.24           C  
ATOM   4081  C   GLN B  27     112.162 135.756 185.695  1.00 19.24           C  
ATOM   4082  O   GLN B  27     111.460 135.510 184.708  1.00 19.24           O  
ATOM   4083  CB  GLN B  27     113.947 137.527 185.663  1.00 19.24           C  
ATOM   4084  CG  GLN B  27     114.266 137.372 184.185  1.00 19.24           C  
ATOM   4085  CD  GLN B  27     114.061 138.643 183.397  1.00 19.24           C  
ATOM   4086  OE1 GLN B  27     113.298 139.523 183.793  1.00 19.24           O  
ATOM   4087  NE2 GLN B  27     114.750 138.749 182.269  1.00 19.24           N  
ATOM   4088  N   HIS B  28     112.630 134.794 186.489  1.00 20.38           N  
ATOM   4089  CA  HIS B  28     112.276 133.402 186.228  1.00 20.38           C  
ATOM   4090  C   HIS B  28     110.772 133.180 186.351  1.00 20.38           C  
ATOM   4091  O   HIS B  28     110.191 132.393 185.595  1.00 20.38           O  
ATOM   4092  CB  HIS B  28     113.037 132.476 187.175  1.00 20.38           C  
ATOM   4093  CG  HIS B  28     114.414 132.130 186.704  1.00 20.38           C  
ATOM   4094  ND1 HIS B  28     115.198 131.190 187.334  1.00 20.38           N  
ATOM   4095  CD2 HIS B  28     115.146 132.597 185.667  1.00 20.38           C  
ATOM   4096  CE1 HIS B  28     116.355 131.093 186.706  1.00 20.38           C  
ATOM   4097  NE2 HIS B  28     116.349 131.936 185.691  1.00 20.38           N  
ATOM   4098  N   LYS B  29     110.123 133.872 187.289  1.00 24.06           N  
ATOM   4099  CA  LYS B  29     108.690 133.686 187.495  1.00 24.06           C  
ATOM   4100  C   LYS B  29     107.883 134.091 186.266  1.00 24.06           C  
ATOM   4101  O   LYS B  29     106.800 133.546 186.032  1.00 24.06           O  
ATOM   4102  CB  LYS B  29     108.236 134.487 188.716  1.00 24.06           C  
ATOM   4103  CG  LYS B  29     106.771 134.328 189.089  1.00 24.06           C  
ATOM   4104  CD  LYS B  29     106.411 132.903 189.484  1.00 24.06           C  
ATOM   4105  CE  LYS B  29     107.118 132.464 190.759  1.00 24.06           C  
ATOM   4106  NZ  LYS B  29     106.660 133.245 191.939  1.00 24.06           N  
ATOM   4107  N   ARG B  30     108.384 135.038 185.476  1.00 22.00           N  
ATOM   4108  CA  ARG B  30     107.700 135.471 184.264  1.00 22.00           C  
ATOM   4109  C   ARG B  30     107.922 134.527 183.088  1.00 22.00           C  
ATOM   4110  O   ARG B  30     107.326 134.740 182.028  1.00 22.00           O  
ATOM   4111  CB  ARG B  30     108.151 136.883 183.868  1.00 22.00           C  
ATOM   4112  CG  ARG B  30     108.101 137.911 184.978  1.00 22.00           C  
ATOM   4113  CD  ARG B  30     108.461 139.298 184.466  1.00 22.00           C  
ATOM   4114  NE  ARG B  30     108.579 140.280 185.545  1.00 22.00           N  
ATOM   4115  CZ  ARG B  30     109.723 140.796 185.991  1.00 22.00           C  
ATOM   4116  NH1 ARG B  30     109.698 141.682 186.977  1.00 22.00           N  
ATOM   4117  NH2 ARG B  30     110.891 140.443 185.466  1.00 22.00           N  
ATOM   4118  N   GLY B  31     108.742 133.494 183.248  1.00 18.36           N  
ATOM   4119  CA  GLY B  31     109.101 132.630 182.144  1.00 18.36           C  
ATOM   4120  C   GLY B  31     110.258 133.124 181.307  1.00 18.36           C  
ATOM   4121  O   GLY B  31     110.371 132.730 180.142  1.00 18.36           O  
ATOM   4122  N   LYS B  32     111.118 133.972 181.862  1.00 15.24           N  
ATOM   4123  CA  LYS B  32     112.232 134.581 181.151  1.00 15.24           C  
ATOM   4124  C   LYS B  32     113.557 134.041 181.676  1.00 15.24           C  
ATOM   4125  O   LYS B  32     113.740 133.892 182.888  1.00 15.24           O  
ATOM   4126  CB  LYS B  32     112.208 136.105 181.306  1.00 15.24           C  
ATOM   4127  CG  LYS B  32     111.065 136.812 180.582  1.00 15.24           C  
ATOM   4128  CD  LYS B  32     110.830 138.220 181.119  1.00 15.24           C  
ATOM   4129  CE  LYS B  32     111.586 139.272 180.316  1.00 15.24           C  
ATOM   4130  NZ  LYS B  32     111.878 140.487 181.112  1.00 15.24           N  
ATOM   4131  N   LEU B  33     114.480 133.748 180.762  1.00 12.02           N  
ATOM   4132  CA  LEU B  33     115.853 133.464 181.146  1.00 12.02           C  
ATOM   4133  C   LEU B  33     116.570 134.755 181.543  1.00 12.02           C  
ATOM   4134  O   LEU B  33     116.091 135.867 181.306  1.00 12.02           O  
ATOM   4135  CB  LEU B  33     116.614 132.787 180.005  1.00 12.02           C  
ATOM   4136  CG  LEU B  33     116.156 131.418 179.499  1.00 12.02           C  
ATOM   4137  CD1 LEU B  33     117.077 130.928 178.405  1.00 12.02           C  
ATOM   4138  CD2 LEU B  33     116.094 130.400 180.620  1.00 12.02           C  
ATOM   4139  N   THR B  34     117.738 134.594 182.156  1.00 11.87           N  
ATOM   4140  CA  THR B  34     118.621 135.705 182.477  1.00 11.87           C  
ATOM   4141  C   THR B  34     119.580 135.966 181.314  1.00 11.87           C  
ATOM   4142  O   THR B  34     119.794 135.114 180.451  1.00 11.87           O  
ATOM   4143  CB  THR B  34     119.414 135.424 183.760  1.00 11.87           C  
ATOM   4144  OG1 THR B  34     120.307 134.328 183.546  1.00 11.87           O  
ATOM   4145  CG2 THR B  34     118.489 135.102 184.925  1.00 11.87           C  
ATOM   4146  N   ALA B  35     120.159 137.169 181.301  1.00 11.31           N  
ATOM   4147  CA  ALA B  35     121.092 137.540 180.236  1.00 11.31           C  
ATOM   4148  C   ALA B  35     122.232 136.533 180.108  1.00 11.31           C  
ATOM   4149  O   ALA B  35     122.572 136.091 178.999  1.00 11.31           O  
ATOM   4150  CB  ALA B  35     121.637 138.944 180.499  1.00 11.31           C  
ATOM   4151  N   ARG B  36     122.819 136.142 181.237  1.00 10.21           N  
ATOM   4152  CA  ARG B  36     123.956 135.230 181.216  1.00 10.21           C  
ATOM   4153  C   ARG B  36     123.540 133.828 180.773  1.00 10.21           C  
ATOM   4154  O   ARG B  36     124.276 133.165 180.032  1.00 10.21           O  
ATOM   4155  CB  ARG B  36     124.621 135.220 182.596  1.00 10.21           C  
ATOM   4156  CG  ARG B  36     125.514 136.434 182.844  1.00 10.21           C  
ATOM   4157  CD  ARG B  36     126.013 136.558 184.274  1.00 10.21           C  
ATOM   4158  NE  ARG B  36     126.679 137.841 184.471  1.00 10.21           N  
ATOM   4159  CZ  ARG B  36     127.878 138.144 183.990  1.00 10.21           C  
ATOM   4160  NH1 ARG B  36     128.568 137.254 183.297  1.00 10.21           N  
ATOM   4161  NH2 ARG B  36     128.392 139.340 184.211  1.00 10.21           N  
ATOM   4162  N   GLU B  37     122.354 133.376 181.184  1.00 12.97           N  
ATOM   4163  CA  GLU B  37     121.837 132.095 180.707  1.00 12.97           C  
ATOM   4164  C   GLU B  37     121.612 132.120 179.195  1.00 12.97           C  
ATOM   4165  O   GLU B  37     121.900 131.139 178.495  1.00 12.97           O  
ATOM   4166  CB  GLU B  37     120.543 131.753 181.450  1.00 12.97           C  
ATOM   4167  CG  GLU B  37     120.738 131.325 182.904  1.00 12.97           C  
ATOM   4168  CD  GLU B  37     119.453 131.361 183.722  1.00 12.97           C  
ATOM   4169  OE1 GLU B  37     118.450 131.937 183.254  1.00 12.97           O  
ATOM   4170  OE2 GLU B  37     119.450 130.815 184.843  1.00 12.97           O  
ATOM   4171  N   ARG B  38     121.102 133.239 178.673  1.00  9.07           N  
ATOM   4172  CA  ARG B  38     120.909 133.373 177.232  1.00  9.07           C  
ATOM   4173  C   ARG B  38     122.243 133.266 176.493  1.00  9.07           C  
ATOM   4174  O   ARG B  38     122.353 132.555 175.479  1.00  9.07           O  
ATOM   4175  CB  ARG B  38     120.197 134.700 176.931  1.00  9.07           C  
ATOM   4176  CG  ARG B  38     118.750 134.774 177.458  1.00  9.07           C  
ATOM   4177  CD  ARG B  38     118.163 136.189 177.472  1.00  9.07           C  
ATOM   4178  NE  ARG B  38     116.740 136.181 177.813  1.00  9.07           N  
ATOM   4179  CZ  ARG B  38     116.043 137.242 178.209  1.00  9.07           C  
ATOM   4180  NH1 ARG B  38     116.615 138.429 178.322  1.00  9.07           N  
ATOM   4181  NH2 ARG B  38     114.756 137.115 178.499  1.00  9.07           N  
ATOM   4182  N   ILE B  39     123.282 133.931 177.008  1.00  8.66           N  
ATOM   4183  CA  ILE B  39     124.608 133.813 176.401  1.00  8.66           C  
ATOM   4184  C   ILE B  39     125.077 132.364 176.427  1.00  8.66           C  
ATOM   4185  O   ILE B  39     125.581 131.837 175.429  1.00  8.66           O  
ATOM   4186  CB  ILE B  39     125.610 134.744 177.109  1.00  8.66           C  
ATOM   4187  CG1 ILE B  39     125.253 136.195 176.800  1.00  8.66           C  
ATOM   4188  CG2 ILE B  39     127.044 134.432 176.681  1.00  8.66           C  
ATOM   4189  CD1 ILE B  39     125.995 137.225 177.602  1.00  8.66           C  
ATOM   4190  N   GLU B  40     124.905 131.698 177.567  1.00 12.18           N  
ATOM   4191  CA  GLU B  40     125.345 130.313 177.700  1.00 12.18           C  
ATOM   4192  C   GLU B  40     124.650 129.402 176.694  1.00 12.18           C  
ATOM   4193  O   GLU B  40     125.255 128.443 176.203  1.00 12.18           O  
ATOM   4194  CB  GLU B  40     125.093 129.837 179.129  1.00 12.18           C  
ATOM   4195  CG  GLU B  40     125.360 128.370 179.381  1.00 12.18           C  
ATOM   4196  CD  GLU B  40     125.147 127.990 180.832  1.00 12.18           C  
ATOM   4197  OE1 GLU B  40     124.281 128.605 181.487  1.00 12.18           O  
ATOM   4198  OE2 GLU B  40     125.849 127.080 181.318  1.00 12.18           O  
ATOM   4199  N   LEU B  41     123.390 129.686 176.372  1.00 10.47           N  
ATOM   4200  CA  LEU B  41     122.667 128.853 175.414  1.00 10.47           C  
ATOM   4201  C   LEU B  41     123.093 129.140 173.977  1.00 10.47           C  
ATOM   4202  O   LEU B  41     123.143 128.221 173.154  1.00 10.47           O  
ATOM   4203  CB  LEU B  41     121.160 129.056 175.577  1.00 10.47           C  
ATOM   4204  CG  LEU B  41     120.219 128.086 174.864  1.00 10.47           C  
ATOM   4205  CD1 LEU B  41     120.472 126.667 175.332  1.00 10.47           C  
ATOM   4206  CD2 LEU B  41     118.785 128.484 175.123  1.00 10.47           C  
ATOM   4207  N   LEU B  42     123.403 130.397 173.651  1.00  7.46           N  
ATOM   4208  CA  LEU B  42     123.720 130.724 172.261  1.00  7.46           C  
ATOM   4209  C   LEU B  42     125.081 130.175 171.837  1.00  7.46           C  
ATOM   4210  O   LEU B  42     125.221 129.662 170.721  1.00  7.46           O  
ATOM   4211  CB  LEU B  42     123.661 132.235 172.045  1.00  7.46           C  
ATOM   4212  CG  LEU B  42     124.110 132.788 170.689  1.00  7.46           C  
ATOM   4213  CD1 LEU B  42     123.233 132.286 169.562  1.00  7.46           C  
ATOM   4214  CD2 LEU B  42     124.103 134.297 170.732  1.00  7.46           C  
ATOM   4215  N   LEU B  43     126.087 130.258 172.704  1.00  7.49           N  
ATOM   4216  CA  LEU B  43     127.467 129.978 172.325  1.00  7.49           C  
ATOM   4217  C   LEU B  43     127.834 128.517 172.584  1.00  7.49           C  
ATOM   4218  O   LEU B  43     127.203 127.818 173.380  1.00  7.49           O  
ATOM   4219  CB  LEU B  43     128.446 130.891 173.076  1.00  7.49           C  
ATOM   4220  CG  LEU B  43     128.357 132.406 172.888  1.00  7.49           C  
ATOM   4221  CD1 LEU B  43     129.388 133.110 173.758  1.00  7.49           C  
ATOM   4222  CD2 LEU B  43     128.529 132.788 171.427  1.00  7.49           C  
ATOM   4223  N   ASP B  44     128.878 128.064 171.891  1.00  9.51           N  
ATOM   4224  CA  ASP B  44     129.415 126.728 172.114  1.00  9.51           C  
ATOM   4225  C   ASP B  44     129.963 126.607 173.534  1.00  9.51           C  
ATOM   4226  O   ASP B  44     130.391 127.587 174.146  1.00  9.51           O  
ATOM   4227  CB  ASP B  44     130.517 126.408 171.098  1.00  9.51           C  
ATOM   4228  CG  ASP B  44     130.038 126.476 169.654  1.00  9.51           C  
ATOM   4229  OD1 ASP B  44     128.858 126.167 169.389  1.00  9.51           O  
ATOM   4230  OD2 ASP B  44     130.857 126.829 168.780  1.00  9.51           O  
ATOM   4231  N   HIS B  45     129.940 125.382 174.056  1.00 13.63           N  
ATOM   4232  CA  HIS B  45     130.337 125.127 175.435  1.00 13.63           C  
ATOM   4233  C   HIS B  45     131.782 125.542 175.681  1.00 13.63           C  
ATOM   4234  O   HIS B  45     132.697 125.079 174.996  1.00 13.63           O  
ATOM   4235  CB  HIS B  45     130.150 123.647 175.769  1.00 13.63           C  
ATOM   4236  CG  HIS B  45     130.443 123.311 177.196  1.00 13.63           C  
ATOM   4237  ND1 HIS B  45     131.665 122.830 177.613  1.00 13.63           N  
ATOM   4238  CD2 HIS B  45     129.672 123.388 178.305  1.00 13.63           C  
ATOM   4239  CE1 HIS B  45     131.633 122.622 178.917  1.00 13.63           C  
ATOM   4240  NE2 HIS B  45     130.434 122.953 179.361  1.00 13.63           N  
ATOM   4241  N   GLY B  46     131.981 126.411 176.668  1.00 11.07           N  
ATOM   4242  CA  GLY B  46     133.311 126.800 177.085  1.00 11.07           C  
ATOM   4243  C   GLY B  46     133.990 127.862 176.250  1.00 11.07           C  
ATOM   4244  O   GLY B  46     135.200 128.055 176.392  1.00 11.07           O  
ATOM   4245  N   SER B  47     133.254 128.573 175.396  1.00  7.39           N  
ATOM   4246  CA  SER B  47     133.862 129.501 174.450  1.00  7.39           C  
ATOM   4247  C   SER B  47     133.738 130.973 174.833  1.00  7.39           C  
ATOM   4248  O   SER B  47     134.451 131.798 174.256  1.00  7.39           O  
ATOM   4249  CB  SER B  47     133.247 129.304 173.061  1.00  7.39           C  
ATOM   4250  OG  SER B  47     131.865 129.574 173.078  1.00  7.39           O  
ATOM   4251  N   PHE B  48     132.874 131.325 175.780  1.00  6.53           N  
ATOM   4252  CA  PHE B  48     132.587 132.728 176.060  1.00  6.53           C  
ATOM   4253  C   PHE B  48     133.763 133.398 176.766  1.00  6.53           C  
ATOM   4254  O   PHE B  48     134.221 132.923 177.810  1.00  6.53           O  
ATOM   4255  CB  PHE B  48     131.323 132.854 176.909  1.00  6.53           C  
ATOM   4256  CG  PHE B  48     130.927 134.273 177.203  1.00  6.53           C  
ATOM   4257  CD1 PHE B  48     130.872 135.225 176.199  1.00  6.53           C  
ATOM   4258  CD2 PHE B  48     130.600 134.657 178.488  1.00  6.53           C  
ATOM   4259  CE1 PHE B  48     130.504 136.522 176.478  1.00  6.53           C  
ATOM   4260  CE2 PHE B  48     130.235 135.949 178.761  1.00  6.53           C  
ATOM   4261  CZ  PHE B  48     130.190 136.880 177.755  1.00  6.53           C  
ATOM   4262  N   GLU B  49     134.256 134.490 176.185  1.00  8.75           N  
ATOM   4263  CA  GLU B  49     135.170 135.420 176.841  1.00  8.75           C  
ATOM   4264  C   GLU B  49     134.450 136.745 177.058  1.00  8.75           C  
ATOM   4265  O   GLU B  49     133.997 137.375 176.093  1.00  8.75           O  
ATOM   4266  CB  GLU B  49     136.444 135.648 176.029  1.00  8.75           C  
ATOM   4267  CG  GLU B  49     137.387 136.619 176.724  1.00  8.75           C  
ATOM   4268  CD  GLU B  49     138.803 136.607 176.179  1.00  8.75           C  
ATOM   4269  OE1 GLU B  49     138.999 136.936 174.990  1.00  8.75           O  
ATOM   4270  OE2 GLU B  49     139.723 136.279 176.953  1.00  8.75           O  
ATOM   4271  N   GLU B  50     134.345 137.152 178.322  1.00  7.78           N  
ATOM   4272  CA  GLU B  50     133.622 138.354 178.721  1.00  7.78           C  
ATOM   4273  C   GLU B  50     134.533 139.578 178.758  1.00  7.78           C  
ATOM   4274  O   GLU B  50     135.690 139.495 179.177  1.00  7.78           O  
ATOM   4275  CB  GLU B  50     132.980 138.157 180.097  1.00  7.78           C  
ATOM   4276  CG  GLU B  50     131.965 139.226 180.455  1.00  7.78           C  
ATOM   4277  CD  GLU B  50     131.266 138.971 181.773  1.00  7.78           C  
ATOM   4278  OE1 GLU B  50     131.358 137.841 182.291  1.00  7.78           O  
ATOM   4279  OE2 GLU B  50     130.620 139.904 182.290  1.00  7.78           O  
ATOM   4280  N   PHE B  51     133.998 140.715 178.321  1.00  7.29           N  
ATOM   4281  CA  PHE B  51     134.642 142.016 178.455  1.00  7.29           C  
ATOM   4282  C   PHE B  51     133.958 142.854 179.531  1.00  7.29           C  
ATOM   4283  O   PHE B  51     132.729 142.863 179.637  1.00  7.29           O  
ATOM   4284  CB  PHE B  51     134.602 142.810 177.143  1.00  7.29           C  
ATOM   4285  CG  PHE B  51     135.341 142.183 176.001  1.00  7.29           C  
ATOM   4286  CD1 PHE B  51     136.344 141.262 176.205  1.00  7.29           C  
ATOM   4287  CD2 PHE B  51     135.040 142.550 174.705  1.00  7.29           C  
ATOM   4288  CE1 PHE B  51     137.018 140.710 175.142  1.00  7.29           C  
ATOM   4289  CE2 PHE B  51     135.706 141.999 173.644  1.00  7.29           C  
ATOM   4290  CZ  PHE B  51     136.696 141.083 173.858  1.00  7.29           C  
ATOM   4291  N   ASP B  52     134.763 143.575 180.312  1.00  8.32           N  
ATOM   4292  CA  ASP B  52     134.294 144.702 181.121  1.00  8.32           C  
ATOM   4293  C   ASP B  52     133.270 144.276 182.178  1.00  8.32           C  
ATOM   4294  O   ASP B  52     132.188 144.849 182.291  1.00  8.32           O  
ATOM   4295  CB  ASP B  52     133.728 145.804 180.218  1.00  8.32           C  
ATOM   4296  CG  ASP B  52     134.787 146.441 179.335  1.00  8.32           C  
ATOM   4297  OD1 ASP B  52     135.976 146.410 179.708  1.00  8.32           O  
ATOM   4298  OD2 ASP B  52     134.430 146.984 178.268  1.00  8.32           O  
ATOM   4299  N   MET B  53     133.638 143.275 182.983  1.00 11.53           N  
ATOM   4300  CA  MET B  53     132.748 142.792 184.038  1.00 11.53           C  
ATOM   4301  C   MET B  53     132.607 143.801 185.178  1.00 11.53           C  
ATOM   4302  O   MET B  53     131.557 143.850 185.825  1.00 11.53           O  
ATOM   4303  CB  MET B  53     133.258 141.447 184.564  1.00 11.53           C  
ATOM   4304  CG  MET B  53     132.443 140.811 185.683  1.00 11.53           C  
ATOM   4305  SD  MET B  53     133.252 139.365 186.386  1.00 11.53           S  
ATOM   4306  CE  MET B  53     132.352 138.062 185.560  1.00 11.53           C  
ATOM   4307  N   PHE B  54     133.629 144.620 185.424  1.00  9.98           N  
ATOM   4308  CA  PHE B  54     133.696 145.472 186.607  1.00  9.98           C  
ATOM   4309  C   PHE B  54     133.410 146.946 186.317  1.00  9.98           C  
ATOM   4310  O   PHE B  54     133.638 147.791 187.189  1.00  9.98           O  
ATOM   4311  CB  PHE B  54     135.072 145.328 187.264  1.00  9.98           C  
ATOM   4312  CG  PHE B  54     135.381 143.942 187.755  1.00  9.98           C  
ATOM   4313  CD1 PHE B  54     134.418 143.160 188.362  1.00  9.98           C  
ATOM   4314  CD2 PHE B  54     136.652 143.428 187.621  1.00  9.98           C  
ATOM   4315  CE1 PHE B  54     134.721 141.893 188.815  1.00  9.98           C  
ATOM   4316  CE2 PHE B  54     136.956 142.166 188.073  1.00  9.98           C  
ATOM   4317  CZ  PHE B  54     135.988 141.399 188.668  1.00  9.98           C  
ATOM   4318  N   VAL B  55     132.899 147.273 185.129  1.00  9.44           N  
ATOM   4319  CA  VAL B  55     132.611 148.660 184.773  1.00  9.44           C  
ATOM   4320  C   VAL B  55     131.453 149.196 185.610  1.00  9.44           C  
ATOM   4321  O   VAL B  55     130.448 148.508 185.830  1.00  9.44           O  
ATOM   4322  CB  VAL B  55     132.319 148.775 183.266  1.00  9.44           C  
ATOM   4323  CG1 VAL B  55     131.651 150.096 182.931  1.00  9.44           C  
ATOM   4324  CG2 VAL B  55     133.609 148.637 182.461  1.00  9.44           C  
ATOM   4325  N   GLN B  56     131.597 150.436 186.085  1.00 14.20           N  
ATOM   4326  CA  GLN B  56     130.600 151.120 186.902  1.00 14.20           C  
ATOM   4327  C   GLN B  56     130.274 152.487 186.310  1.00 14.20           C  
ATOM   4328  O   GLN B  56     131.064 153.066 185.560  1.00 14.20           O  
ATOM   4329  CB  GLN B  56     131.084 151.312 188.347  1.00 14.20           C  
ATOM   4330  CG  GLN B  56     131.520 150.058 189.034  1.00 14.20           C  
ATOM   4331  CD  GLN B  56     131.925 150.302 190.469  1.00 14.20           C  
ATOM   4332  OE1 GLN B  56     132.531 151.322 190.793  1.00 14.20           O  
ATOM   4333  NE2 GLN B  56     131.583 149.368 191.339  1.00 14.20           N  
ATOM   4334  N   HIS B  57     129.105 153.017 186.676  1.00 15.61           N  
ATOM   4335  CA  HIS B  57     128.715 154.353 186.245  1.00 15.61           C  
ATOM   4336  C   HIS B  57     129.353 155.409 187.145  1.00 15.61           C  
ATOM   4337  O   HIS B  57     129.844 155.122 188.238  1.00 15.61           O  
ATOM   4338  CB  HIS B  57     127.197 154.523 186.243  1.00 15.61           C  
ATOM   4339  CG  HIS B  57     126.582 154.500 187.603  1.00 15.61           C  
ATOM   4340  ND1 HIS B  57     126.165 153.337 188.207  1.00 15.61           N  
ATOM   4341  CD2 HIS B  57     126.337 155.494 188.488  1.00 15.61           C  
ATOM   4342  CE1 HIS B  57     125.671 153.617 189.398  1.00 15.61           C  
ATOM   4343  NE2 HIS B  57     125.766 154.918 189.594  1.00 15.61           N  
ATOM   4344  N   ARG B  58     129.328 156.656 186.666  1.00 18.98           N  
ATOM   4345  CA  ARG B  58     129.968 157.775 187.349  1.00 18.98           C  
ATOM   4346  C   ARG B  58     128.999 158.926 187.618  1.00 18.98           C  
ATOM   4347  O   ARG B  58     129.438 160.063 187.807  1.00 18.98           O  
ATOM   4348  CB  ARG B  58     131.169 158.264 186.533  1.00 18.98           C  
ATOM   4349  CG  ARG B  58     132.374 157.342 186.626  1.00 18.98           C  
ATOM   4350  CD  ARG B  58     133.495 157.714 185.669  1.00 18.98           C  
ATOM   4351  NE  ARG B  58     133.117 157.533 184.275  1.00 18.98           N  
ATOM   4352  CZ  ARG B  58     133.039 156.354 183.664  1.00 18.98           C  
ATOM   4353  NH1 ARG B  58     133.310 155.228 184.316  1.00 18.98           N  
ATOM   4354  NH2 ARG B  58     132.684 156.299 182.391  1.00 18.98           N  
ATOM   4355  N   SER B  59     127.696 158.661 187.642  1.00 24.48           N  
ATOM   4356  CA  SER B  59     126.724 159.700 187.951  1.00 24.48           C  
ATOM   4357  C   SER B  59     126.681 159.983 189.449  1.00 24.48           C  
ATOM   4358  O   SER B  59     126.856 159.092 190.282  1.00 24.48           O  
ATOM   4359  CB  SER B  59     125.332 159.298 187.462  1.00 24.48           C  
ATOM   4360  OG  SER B  59     124.403 160.348 187.659  1.00 24.48           O  
ATOM   4361  N   THR B  60     126.428 161.250 189.784  1.00 32.02           N  
ATOM   4362  CA  THR B  60     126.298 161.690 191.168  1.00 32.02           C  
ATOM   4363  C   THR B  60     125.008 162.474 191.387  1.00 32.02           C  
ATOM   4364  O   THR B  60     124.907 163.233 192.356  1.00 32.02           O  
ATOM   4365  CB  THR B  60     127.505 162.535 191.582  1.00 32.02           C  
ATOM   4366  OG1 THR B  60     127.775 163.512 190.569  1.00 32.02           O  
ATOM   4367  CG2 THR B  60     128.735 161.654 191.791  1.00 32.02           C  
ATOM   4368  N   ASP B  61     124.022 162.299 190.516  1.00 33.22           N  
ATOM   4369  CA  ASP B  61     122.757 163.010 190.600  1.00 33.22           C  
ATOM   4370  C   ASP B  61     121.666 162.103 191.154  1.00 33.22           C  
ATOM   4371  O   ASP B  61     121.717 160.879 191.017  1.00 33.22           O  
ATOM   4372  CB  ASP B  61     122.336 163.535 189.227  1.00 33.22           C  
ATOM   4373  CG  ASP B  61     122.918 164.900 188.916  1.00 33.22           C  
ATOM   4374  OD1 ASP B  61     122.942 165.762 189.819  1.00 33.22           O  
ATOM   4375  OD2 ASP B  61     123.345 165.114 187.762  1.00 33.22           O  
ATOM   4376  N   PHE B  62     120.678 162.729 191.790  1.00 31.64           N  
ATOM   4377  CA  PHE B  62     119.474 162.048 192.262  1.00 31.64           C  
ATOM   4378  C   PHE B  62     119.811 160.789 193.060  1.00 31.64           C  
ATOM   4379  O   PHE B  62     119.141 159.761 192.953  1.00 31.64           O  
ATOM   4380  CB  PHE B  62     118.552 161.728 191.087  1.00 31.64           C  
ATOM   4381  CG  PHE B  62     118.104 162.943 190.326  1.00 31.64           C  
ATOM   4382  CD1 PHE B  62     117.315 163.901 190.928  1.00 31.64           C  
ATOM   4383  CD2 PHE B  62     118.481 163.132 189.009  1.00 31.64           C  
ATOM   4384  CE1 PHE B  62     116.908 165.016 190.235  1.00 31.64           C  
ATOM   4385  CE2 PHE B  62     118.074 164.248 188.315  1.00 31.64           C  
ATOM   4386  CZ  PHE B  62     117.288 165.189 188.930  1.00 31.64           C  
ATOM   4387  N   GLY B  63     120.858 160.874 193.876  1.00 35.18           N  
ATOM   4388  CA  GLY B  63     121.223 159.765 194.734  1.00 35.18           C  
ATOM   4389  C   GLY B  63     121.748 158.538 194.026  1.00 35.18           C  
ATOM   4390  O   GLY B  63     121.725 157.449 194.603  1.00 35.18           O  
ATOM   4391  N   MET B  64     122.236 158.678 192.792  1.00 33.34           N  
ATOM   4392  CA  MET B  64     122.722 157.521 192.050  1.00 33.34           C  
ATOM   4393  C   MET B  64     124.061 157.018 192.572  1.00 33.34           C  
ATOM   4394  O   MET B  64     124.387 155.845 192.371  1.00 33.34           O  
ATOM   4395  CB  MET B  64     122.854 157.861 190.566  1.00 33.34           C  
ATOM   4396  CG  MET B  64     121.534 158.034 189.832  1.00 33.34           C  
ATOM   4397  SD  MET B  64     120.506 156.556 189.818  1.00 33.34           S  
ATOM   4398  CE  MET B  64     121.578 155.412 188.966  1.00 33.34           C  
ATOM   4399  N   GLU B  65     124.839 157.871 193.237  1.00 36.84           N  
ATOM   4400  CA  GLU B  65     126.145 157.468 193.743  1.00 36.84           C  
ATOM   4401  C   GLU B  65     126.058 156.435 194.858  1.00 36.84           C  
ATOM   4402  O   GLU B  65     127.081 155.831 195.195  1.00 36.84           O  
ATOM   4403  CB  GLU B  65     126.923 158.695 194.226  1.00 36.84           C  
ATOM   4404  CG  GLU B  65     126.387 159.361 195.489  1.00 36.84           C  
ATOM   4405  CD  GLU B  65     125.182 160.246 195.234  1.00 36.84           C  
ATOM   4406  OE1 GLU B  65     124.727 160.320 194.074  1.00 36.84           O  
ATOM   4407  OE2 GLU B  65     124.691 160.871 196.196  1.00 36.84           O  
ATOM   4408  N   LYS B  66     124.878 156.213 195.429  1.00 38.44           N  
ATOM   4409  CA  LYS B  66     124.708 155.233 196.492  1.00 38.44           C  
ATOM   4410  C   LYS B  66     124.394 153.834 195.978  1.00 38.44           C  
ATOM   4411  O   LYS B  66     124.271 152.911 196.789  1.00 38.44           O  
ATOM   4412  CB  LYS B  66     123.593 155.676 197.445  1.00 38.44           C  
ATOM   4413  CG  LYS B  66     123.853 156.997 198.150  1.00 38.44           C  
ATOM   4414  CD  LYS B  66     122.761 157.320 199.160  1.00 38.44           C  
ATOM   4415  CE  LYS B  66     121.452 157.711 198.491  1.00 38.44           C  
ATOM   4416  NZ  LYS B  66     121.312 159.187 198.357  1.00 38.44           N  
ATOM   4417  N   GLN B  67     124.253 153.650 194.663  1.00 31.93           N  
ATOM   4418  CA  GLN B  67     123.937 152.341 194.083  1.00 31.93           C  
ATOM   4419  C   GLN B  67     124.771 152.146 192.816  1.00 31.93           C  
ATOM   4420  O   GLN B  67     124.332 152.487 191.717  1.00 31.93           O  
ATOM   4421  CB  GLN B  67     122.444 152.213 193.800  1.00 31.93           C  
ATOM   4422  CG  GLN B  67     121.774 153.460 193.245  1.00 31.93           C  
ATOM   4423  CD  GLN B  67     120.264 153.390 193.349  1.00 31.93           C  
ATOM   4424  OE1 GLN B  67     119.667 152.328 193.177  1.00 31.93           O  
ATOM   4425  NE2 GLN B  67     119.640 154.520 193.652  1.00 31.93           N  
ATOM   4426  N   LYS B  68     125.957 151.563 192.981  1.00 24.08           N  
ATOM   4427  CA  LYS B  68     126.874 151.260 191.885  1.00 24.08           C  
ATOM   4428  C   LYS B  68     126.967 149.745 191.746  1.00 24.08           C  
ATOM   4429  O   LYS B  68     127.555 149.074 192.599  1.00 24.08           O  
ATOM   4430  CB  LYS B  68     128.247 151.877 192.139  1.00 24.08           C  
ATOM   4431  CG  LYS B  68     128.269 153.393 192.042  1.00 24.08           C  
ATOM   4432  CD  LYS B  68     129.647 153.966 192.300  1.00 24.08           C  
ATOM   4433  CE  LYS B  68     129.632 155.487 192.248  1.00 24.08           C  
ATOM   4434  NZ  LYS B  68     129.151 156.015 190.938  1.00 24.08           N  
ATOM   4435  N   ILE B  69     126.394 149.211 190.677  1.00 16.16           N  
ATOM   4436  CA  ILE B  69     126.346 147.770 190.440  1.00 16.16           C  
ATOM   4437  C   ILE B  69     127.365 147.421 189.358  1.00 16.16           C  
ATOM   4438  O   ILE B  69     127.385 148.084 188.312  1.00 16.16           O  
ATOM   4439  CB  ILE B  69     124.936 147.304 190.036  1.00 16.16           C  
ATOM   4440  CG1 ILE B  69     123.945 147.560 191.173  1.00 16.16           C  
ATOM   4441  CG2 ILE B  69     124.935 145.832 189.686  1.00 16.16           C  
ATOM   4442  CD1 ILE B  69     123.272 148.887 191.079  1.00 16.16           C  
ATOM   4443  N   PRO B  70     128.214 146.414 189.566  1.00 14.09           N  
ATOM   4444  CA  PRO B  70     129.223 146.072 188.551  1.00 14.09           C  
ATOM   4445  C   PRO B  70     128.584 145.567 187.264  1.00 14.09           C  
ATOM   4446  O   PRO B  70     127.693 144.717 187.286  1.00 14.09           O  
ATOM   4447  CB  PRO B  70     130.068 144.983 189.226  1.00 14.09           C  
ATOM   4448  CG  PRO B  70     129.573 144.836 190.596  1.00 14.09           C  
ATOM   4449  CD  PRO B  70     128.466 145.770 190.862  1.00 14.09           C  
ATOM   4450  N   GLY B  71     129.062 146.097 186.135  1.00 12.74           N  
ATOM   4451  CA  GLY B  71     128.589 145.745 184.812  1.00 12.74           C  
ATOM   4452  C   GLY B  71     127.717 146.809 184.169  1.00 12.74           C  
ATOM   4453  O   GLY B  71     127.680 146.904 182.937  1.00 12.74           O  
ATOM   4454  N   ASP B  72     127.020 147.603 184.979  1.00 12.76           N  
ATOM   4455  CA  ASP B  72     126.180 148.716 184.535  1.00 12.76           C  
ATOM   4456  C   ASP B  72     125.049 148.267 183.614  1.00 12.76           C  
ATOM   4457  O   ASP B  72     124.534 149.063 182.828  1.00 12.76           O  
ATOM   4458  CB  ASP B  72     127.012 149.812 183.859  1.00 12.76           C  
ATOM   4459  CG  ASP B  72     126.346 151.180 183.924  1.00 12.76           C  
ATOM   4460  OD1 ASP B  72     125.601 151.447 184.888  1.00 12.76           O  
ATOM   4461  OD2 ASP B  72     126.568 151.997 183.008  1.00 12.76           O  
ATOM   4462  N   GLY B  73     124.636 147.009 183.713  1.00 10.95           N  
ATOM   4463  CA  GLY B  73     123.417 146.548 183.085  1.00 10.95           C  
ATOM   4464  C   GLY B  73     123.534 145.851 181.743  1.00 10.95           C  
ATOM   4465  O   GLY B  73     122.503 145.635 181.100  1.00 10.95           O  
ATOM   4466  N   VAL B  74     124.735 145.476 181.308  1.00  8.25           N  
ATOM   4467  CA  VAL B  74     124.915 144.766 180.042  1.00  8.25           C  
ATOM   4468  C   VAL B  74     126.103 143.818 180.166  1.00  8.25           C  
ATOM   4469  O   VAL B  74     127.127 144.161 180.762  1.00  8.25           O  
ATOM   4470  CB  VAL B  74     125.095 145.746 178.858  1.00  8.25           C  
ATOM   4471  CG1 VAL B  74     126.414 146.497 178.952  1.00  8.25           C  
ATOM   4472  CG2 VAL B  74     124.972 145.022 177.528  1.00  8.25           C  
ATOM   4473  N   VAL B  75     125.954 142.619 179.602  1.00  5.97           N  
ATOM   4474  CA  VAL B  75     127.007 141.610 179.526  1.00  5.97           C  
ATOM   4475  C   VAL B  75     127.489 141.529 178.080  1.00  5.97           C  
ATOM   4476  O   VAL B  75     126.685 141.338 177.163  1.00  5.97           O  
ATOM   4477  CB  VAL B  75     126.506 140.239 180.014  1.00  5.97           C  
ATOM   4478  CG1 VAL B  75     127.630 139.215 180.011  1.00  5.97           C  
ATOM   4479  CG2 VAL B  75     125.869 140.350 181.394  1.00  5.97           C  
ATOM   4480  N   THR B  76     128.799 141.648 177.878  1.00  9.37           N  
ATOM   4481  CA  THR B  76     129.386 141.780 176.550  1.00  9.37           C  
ATOM   4482  C   THR B  76     130.564 140.826 176.386  1.00  9.37           C  
ATOM   4483  O   THR B  76     131.261 140.508 177.352  1.00  9.37           O  
ATOM   4484  CB  THR B  76     129.852 143.232 176.296  1.00  9.37           C  
ATOM   4485  OG1 THR B  76     130.671 143.681 177.381  1.00  9.37           O  
ATOM   4486  CG2 THR B  76     128.663 144.166 176.154  1.00  9.37           C  
ATOM   4487  N   GLY B  77     130.791 140.373 175.155  1.00  7.26           N  
ATOM   4488  CA  GLY B  77     131.968 139.561 174.888  1.00  7.26           C  
ATOM   4489  C   GLY B  77     131.908 138.863 173.542  1.00  7.26           C  
ATOM   4490  O   GLY B  77     131.214 139.309 172.623  1.00  7.26           O  
ATOM   4491  N   TRP B  78     132.653 137.757 173.447  1.00 12.77           N  
ATOM   4492  CA  TRP B  78     132.758 136.999 172.202  1.00 12.77           C  
ATOM   4493  C   TRP B  78     132.849 135.502 172.478  1.00 12.77           C  
ATOM   4494  O   TRP B  78     133.035 135.061 173.614  1.00 12.77           O  
ATOM   4495  CB  TRP B  78     133.954 137.458 171.349  1.00 12.77           C  
ATOM   4496  CG  TRP B  78     135.309 137.002 171.815  1.00 12.77           C  
ATOM   4497  CD1 TRP B  78     136.107 137.610 172.734  1.00 12.77           C  
ATOM   4498  CD2 TRP B  78     136.030 135.852 171.360  1.00 12.77           C  
ATOM   4499  NE1 TRP B  78     137.272 136.907 172.890  1.00 12.77           N  
ATOM   4500  CE2 TRP B  78     137.250 135.823 172.056  1.00 12.77           C  
ATOM   4501  CE3 TRP B  78     135.759 134.844 170.436  1.00 12.77           C  
ATOM   4502  CZ2 TRP B  78     138.194 134.823 171.858  1.00 12.77           C  
ATOM   4503  CZ3 TRP B  78     136.695 133.856 170.241  1.00 12.77           C  
ATOM   4504  CH2 TRP B  78     137.897 133.852 170.951  1.00 12.77           C  
ATOM   4505  N   GLY B  79     132.718 134.732 171.403  1.00  7.84           N  
ATOM   4506  CA  GLY B  79     132.711 133.284 171.493  1.00  7.84           C  
ATOM   4507  C   GLY B  79     132.601 132.669 170.114  1.00  7.84           C  
ATOM   4508  O   GLY B  79     132.883 133.322 169.109  1.00  7.84           O  
ATOM   4509  N   THR B  80     132.162 131.410 170.067  1.00  7.12           N  
ATOM   4510  CA  THR B  80     132.010 130.684 168.812  1.00  7.12           C  
ATOM   4511  C   THR B  80     130.645 130.015 168.717  1.00  7.12           C  
ATOM   4512  O   THR B  80     130.104 129.533 169.714  1.00  7.12           O  
ATOM   4513  CB  THR B  80     133.098 129.611 168.629  1.00  7.12           C  
ATOM   4514  OG1 THR B  80     133.054 128.679 169.713  1.00  7.12           O  
ATOM   4515  CG2 THR B  80     134.486 130.234 168.537  1.00  7.12           C  
ATOM   4516  N   VAL B  81     130.112 129.983 167.498  1.00  7.36           N  
ATOM   4517  CA  VAL B  81     128.913 129.234 167.140  1.00  7.36           C  
ATOM   4518  C   VAL B  81     129.309 128.250 166.044  1.00  7.36           C  
ATOM   4519  O   VAL B  81     129.742 128.658 164.960  1.00  7.36           O  
ATOM   4520  CB  VAL B  81     127.773 130.159 166.680  1.00  7.36           C  
ATOM   4521  CG1 VAL B  81     126.585 129.354 166.167  1.00  7.36           C  
ATOM   4522  CG2 VAL B  81     127.348 131.077 167.810  1.00  7.36           C  
ATOM   4523  N   ASN B  82     129.174 126.959 166.335  1.00 11.04           N  
ATOM   4524  CA  ASN B  82     129.617 125.888 165.440  1.00 11.04           C  
ATOM   4525  C   ASN B  82     131.032 126.150 164.925  1.00 11.04           C  
ATOM   4526  O   ASN B  82     131.330 125.977 163.744  1.00 11.04           O  
ATOM   4527  CB  ASN B  82     128.630 125.699 164.282  1.00 11.04           C  
ATOM   4528  CG  ASN B  82     128.793 124.365 163.580  1.00 11.04           C  
ATOM   4529  OD1 ASN B  82     129.382 123.430 164.120  1.00 11.04           O  
ATOM   4530  ND2 ASN B  82     128.256 124.268 162.373  1.00 11.04           N  
ATOM   4531  N   GLY B  83     131.912 126.582 165.831  1.00 10.02           N  
ATOM   4532  CA  GLY B  83     133.303 126.828 165.523  1.00 10.02           C  
ATOM   4533  C   GLY B  83     133.624 128.166 164.893  1.00 10.02           C  
ATOM   4534  O   GLY B  83     134.808 128.494 164.759  1.00 10.02           O  
ATOM   4535  N   ARG B  84     132.625 128.950 164.504  1.00  8.40           N  
ATOM   4536  CA  ARG B  84     132.841 130.224 163.833  1.00  8.40           C  
ATOM   4537  C   ARG B  84     132.703 131.389 164.815  1.00  8.40           C  
ATOM   4538  O   ARG B  84     131.806 131.398 165.660  1.00  8.40           O  
ATOM   4539  CB  ARG B  84     131.860 130.375 162.668  1.00  8.40           C  
ATOM   4540  CG  ARG B  84     131.936 129.252 161.637  1.00  8.40           C  
ATOM   4541  CD  ARG B  84     130.730 129.229 160.729  1.00  8.40           C  
ATOM   4542  NE  ARG B  84     130.813 130.249 159.695  1.00  8.40           N  
ATOM   4543  CZ  ARG B  84     129.766 130.859 159.152  1.00  8.40           C  
ATOM   4544  NH1 ARG B  84     128.538 130.564 159.538  1.00  8.40           N  
ATOM   4545  NH2 ARG B  84     129.948 131.773 158.217  1.00  8.40           N  
ATOM   4546  N   THR B  85     133.597 132.370 164.689  1.00 12.77           N  
ATOM   4547  CA  THR B  85     133.680 133.486 165.630  1.00 12.77           C  
ATOM   4548  C   THR B  85     132.434 134.368 165.582  1.00 12.77           C  
ATOM   4549  O   THR B  85     131.936 134.705 164.507  1.00 12.77           O  
ATOM   4550  CB  THR B  85     134.921 134.332 165.327  1.00 12.77           C  
ATOM   4551  OG1 THR B  85     136.084 133.499 165.339  1.00 12.77           O  
ATOM   4552  CG2 THR B  85     135.100 135.471 166.338  1.00 12.77           C  
ATOM   4553  N   VAL B  86     131.934 134.743 166.763  1.00 12.77           N  
ATOM   4554  CA  VAL B  86     130.847 135.707 166.893  1.00 12.77           C  
ATOM   4555  C   VAL B  86     131.084 136.607 168.106  1.00 12.77           C  
ATOM   4556  O   VAL B  86     131.724 136.212 169.086  1.00 12.77           O  
ATOM   4557  CB  VAL B  86     129.458 135.019 166.994  1.00 12.77           C  
ATOM   4558  CG1 VAL B  86     129.236 134.050 165.838  1.00 12.77           C  
ATOM   4559  CG2 VAL B  86     129.281 134.297 168.312  1.00 12.77           C  
ATOM   4560  N   PHE B  87     130.570 137.835 168.018  1.00 12.77           N  
ATOM   4561  CA  PHE B  87     130.531 138.813 169.102  1.00 12.77           C  
ATOM   4562  C   PHE B  87     129.085 139.025 169.544  1.00 12.77           C  
ATOM   4563  O   PHE B  87     128.156 138.821 168.758  1.00 12.77           O  
ATOM   4564  CB  PHE B  87     131.145 140.146 168.656  1.00 12.77           C  
ATOM   4565  CG  PHE B  87     132.622 140.075 168.403  1.00 12.77           C  
ATOM   4566  CD1 PHE B  87     133.110 139.646 167.187  1.00 12.77           C  
ATOM   4567  CD2 PHE B  87     133.525 140.424 169.389  1.00 12.77           C  
ATOM   4568  CE1 PHE B  87     134.461 139.573 166.962  1.00 12.77           C  
ATOM   4569  CE2 PHE B  87     134.870 140.346 169.165  1.00 12.77           C  
ATOM   4570  CZ  PHE B  87     135.341 139.919 167.955  1.00 12.77           C  
ATOM   4571  N   LEU B  88     128.887 139.439 170.800  1.00 12.77           N  
ATOM   4572  CA  LEU B  88     127.526 139.583 171.312  1.00 12.77           C  
ATOM   4573  C   LEU B  88     127.469 140.457 172.562  1.00 12.77           C  
ATOM   4574  O   LEU B  88     128.464 140.644 173.277  1.00 12.77           O  
ATOM   4575  CB  LEU B  88     126.895 138.214 171.600  1.00 12.77           C  
ATOM   4576  CG  LEU B  88     127.388 137.396 172.795  1.00 12.77           C  
ATOM   4577  CD1 LEU B  88     126.480 136.193 172.997  1.00 12.77           C  
ATOM   4578  CD2 LEU B  88     128.816 136.979 172.607  1.00 12.77           C  
ATOM   4579  N   PHE B  89     126.269 141.010 172.787  1.00 12.77           N  
ATOM   4580  CA  PHE B  89     125.899 141.720 174.003  1.00 12.77           C  
ATOM   4581  C   PHE B  89     124.465 141.376 174.408  1.00 12.77           C  
ATOM   4582  O   PHE B  89     123.601 141.140 173.562  1.00 12.77           O  
ATOM   4583  CB  PHE B  89     126.057 143.238 173.841  1.00 12.77           C  
ATOM   4584  CG  PHE B  89     125.078 143.875 172.892  1.00 12.77           C  
ATOM   4585  CD1 PHE B  89     123.854 144.325 173.340  1.00 12.77           C  
ATOM   4586  CD2 PHE B  89     125.402 144.077 171.566  1.00 12.77           C  
ATOM   4587  CE1 PHE B  89     122.968 144.928 172.483  1.00 12.77           C  
ATOM   4588  CE2 PHE B  89     124.512 144.686 170.709  1.00 12.77           C  
ATOM   4589  CZ  PHE B  89     123.297 145.110 171.172  1.00 12.77           C  
ATOM   4590  N   SER B  90     124.224 141.375 175.721  1.00  7.63           N  
ATOM   4591  CA  SER B  90     122.947 140.988 176.317  1.00  7.63           C  
ATOM   4592  C   SER B  90     122.607 141.933 177.464  1.00  7.63           C  
ATOM   4593  O   SER B  90     123.400 142.090 178.396  1.00  7.63           O  
ATOM   4594  CB  SER B  90     123.003 139.546 176.823  1.00  7.63           C  
ATOM   4595  OG  SER B  90     121.778 139.160 177.406  1.00  7.63           O  
ATOM   4596  N   LYS B  91     121.429 142.545 177.406  1.00  9.69           N  
ATOM   4597  CA  LYS B  91     120.990 143.513 178.406  1.00  9.69           C  
ATOM   4598  C   LYS B  91     120.339 142.812 179.598  1.00  9.69           C  
ATOM   4599  O   LYS B  91     119.651 141.802 179.440  1.00  9.69           O  
ATOM   4600  CB  LYS B  91     120.025 144.516 177.771  1.00  9.69           C  
ATOM   4601  CG  LYS B  91     120.705 145.413 176.730  1.00  9.69           C  
ATOM   4602  CD  LYS B  91     119.878 146.591 176.305  1.00  9.69           C  
ATOM   4603  CE  LYS B  91     120.556 147.357 175.183  1.00  9.69           C  
ATOM   4604  NZ  LYS B  91     120.870 148.753 175.555  1.00  9.69           N  
ATOM   4605  N   ASP B  92     120.571 143.357 180.797  1.00 13.46           N  
ATOM   4606  CA  ASP B  92     120.128 142.773 182.063  1.00 13.46           C  
ATOM   4607  C   ASP B  92     119.018 143.646 182.642  1.00 13.46           C  
ATOM   4608  O   ASP B  92     119.265 144.778 183.067  1.00 13.46           O  
ATOM   4609  CB  ASP B  92     121.297 142.636 183.038  1.00 13.46           C  
ATOM   4610  CG  ASP B  92     120.930 141.865 184.301  1.00 13.46           C  
ATOM   4611  OD1 ASP B  92     119.738 141.812 184.663  1.00 13.46           O  
ATOM   4612  OD2 ASP B  92     121.844 141.300 184.932  1.00 13.46           O  
ATOM   4613  N   PHE B  93     117.800 143.104 182.666  1.00 15.44           N  
ATOM   4614  CA  PHE B  93     116.618 143.860 183.069  1.00 15.44           C  
ATOM   4615  C   PHE B  93     116.585 144.159 184.564  1.00 15.44           C  
ATOM   4616  O   PHE B  93     115.825 145.034 184.986  1.00 15.44           O  
ATOM   4617  CB  PHE B  93     115.367 143.082 182.650  1.00 15.44           C  
ATOM   4618  CG  PHE B  93     114.076 143.817 182.873  1.00 15.44           C  
ATOM   4619  CD1 PHE B  93     113.684 144.831 182.022  1.00 15.44           C  
ATOM   4620  CD2 PHE B  93     113.242 143.472 183.917  1.00 15.44           C  
ATOM   4621  CE1 PHE B  93     112.499 145.495 182.217  1.00 15.44           C  
ATOM   4622  CE2 PHE B  93     112.054 144.132 184.116  1.00 15.44           C  
ATOM   4623  CZ  PHE B  93     111.681 145.144 183.264  1.00 15.44           C  
ATOM   4624  N   THR B  94     117.384 143.462 185.369  1.00 17.84           N  
ATOM   4625  CA  THR B  94     117.409 143.667 186.813  1.00 17.84           C  
ATOM   4626  C   THR B  94     118.304 144.824 187.252  1.00 17.84           C  
ATOM   4627  O   THR B  94     118.424 145.061 188.458  1.00 17.84           O  
ATOM   4628  CB  THR B  94     117.864 142.385 187.516  1.00 17.84           C  
ATOM   4629  OG1 THR B  94     119.255 142.161 187.264  1.00 17.84           O  
ATOM   4630  CG2 THR B  94     117.059 141.183 187.045  1.00 17.84           C  
ATOM   4631  N   VAL B  95     118.921 145.550 186.322  1.00 16.36           N  
ATOM   4632  CA  VAL B  95     119.829 146.655 186.629  1.00 16.36           C  
ATOM   4633  C   VAL B  95     119.242 147.902 185.981  1.00 16.36           C  
ATOM   4634  O   VAL B  95     119.378 148.110 184.770  1.00 16.36           O  
ATOM   4635  CB  VAL B  95     121.256 146.380 186.142  1.00 16.36           C  
ATOM   4636  CG1 VAL B  95     122.198 147.498 186.540  1.00 16.36           C  
ATOM   4637  CG2 VAL B  95     121.744 145.054 186.685  1.00 16.36           C  
ATOM   4638  N   PHE B  96     118.575 148.731 186.787  1.00 18.82           N  
ATOM   4639  CA  PHE B  96     117.945 149.963 186.313  1.00 18.82           C  
ATOM   4640  C   PHE B  96     117.031 149.696 185.122  1.00 18.82           C  
ATOM   4641  O   PHE B  96     116.892 150.530 184.225  1.00 18.82           O  
ATOM   4642  CB  PHE B  96     118.997 151.020 185.966  1.00 18.82           C  
ATOM   4643  CG  PHE B  96     120.051 151.190 187.020  1.00 18.82           C  
ATOM   4644  CD1 PHE B  96     119.750 151.798 188.223  1.00 18.82           C  
ATOM   4645  CD2 PHE B  96     121.338 150.735 186.811  1.00 18.82           C  
ATOM   4646  CE1 PHE B  96     120.715 151.953 189.195  1.00 18.82           C  
ATOM   4647  CE2 PHE B  96     122.309 150.886 187.780  1.00 18.82           C  
ATOM   4648  CZ  PHE B  96     121.997 151.495 188.971  1.00 18.82           C  
ATOM   4649  N   GLY B  97     116.401 148.525 185.108  1.00 18.08           N  
ATOM   4650  CA  GLY B  97     115.529 148.161 184.009  1.00 18.08           C  
ATOM   4651  C   GLY B  97     116.252 148.003 182.693  1.00 18.08           C  
ATOM   4652  O   GLY B  97     115.686 148.311 181.643  1.00 18.08           O  
ATOM   4653  N   GLY B  98     117.493 147.527 182.725  1.00 14.71           N  
ATOM   4654  CA  GLY B  98     118.316 147.427 181.536  1.00 14.71           C  
ATOM   4655  C   GLY B  98     118.473 148.733 180.785  1.00 14.71           C  
ATOM   4656  O   GLY B  98     118.746 148.731 179.583  1.00 14.71           O  
ATOM   4657  N   SER B  99     118.326 149.853 181.486  1.00 14.60           N  
ATOM   4658  CA  SER B  99     118.398 151.160 180.847  1.00 14.60           C  
ATOM   4659  C   SER B  99     119.828 151.497 180.440  1.00 14.60           C  
ATOM   4660  O   SER B  99     120.799 151.057 181.059  1.00 14.60           O  
ATOM   4661  CB  SER B  99     117.859 152.247 181.776  1.00 14.60           C  
ATOM   4662  OG  SER B  99     118.675 152.399 182.919  1.00 14.60           O  
ATOM   4663  N   SER B 100     119.944 152.299 179.384  1.00 14.05           N  
ATOM   4664  CA  SER B 100     121.232 152.647 178.802  1.00 14.05           C  
ATOM   4665  C   SER B 100     121.802 153.896 179.460  1.00 14.05           C  
ATOM   4666  O   SER B 100     121.109 154.908 179.601  1.00 14.05           O  
ATOM   4667  CB  SER B 100     121.101 152.871 177.298  1.00 14.05           C  
ATOM   4668  OG  SER B 100     122.346 153.230 176.740  1.00 14.05           O  
ATOM   4669  N   SER B 101     123.071 153.818 179.841  1.00 14.63           N  
ATOM   4670  CA  SER B 101     123.837 154.920 180.400  1.00 14.63           C  
ATOM   4671  C   SER B 101     125.129 155.083 179.603  1.00 14.63           C  
ATOM   4672  O   SER B 101     125.372 154.374 178.624  1.00 14.63           O  
ATOM   4673  CB  SER B 101     124.127 154.687 181.887  1.00 14.63           C  
ATOM   4674  OG  SER B 101     124.528 153.353 182.136  1.00 14.63           O  
ATOM   4675  N   GLU B 102     125.961 156.032 180.035  1.00 15.04           N  
ATOM   4676  CA  GLU B 102     127.212 156.332 179.343  1.00 15.04           C  
ATOM   4677  C   GLU B 102     128.122 155.104 179.262  1.00 15.04           C  
ATOM   4678  O   GLU B 102     128.550 154.701 178.174  1.00 15.04           O  
ATOM   4679  CB  GLU B 102     127.910 157.500 180.049  1.00 15.04           C  
ATOM   4680  CG  GLU B 102     129.120 158.058 179.325  1.00 15.04           C  
ATOM   4681  CD  GLU B 102     129.554 159.413 179.859  1.00 15.04           C  
ATOM   4682  OE1 GLU B 102     128.948 159.896 180.839  1.00 15.04           O  
ATOM   4683  OE2 GLU B 102     130.503 159.997 179.296  1.00 15.04           O  
ATOM   4684  N   ALA B 103     128.432 154.497 180.412  1.00 10.85           N  
ATOM   4685  CA  ALA B 103     129.348 153.355 180.442  1.00 10.85           C  
ATOM   4686  C   ALA B 103     128.744 152.124 179.764  1.00 10.85           C  
ATOM   4687  O   ALA B 103     129.446 151.374 179.072  1.00 10.85           O  
ATOM   4688  CB  ALA B 103     129.727 153.044 181.890  1.00 10.85           C  
ATOM   4689  N   HIS B 104     127.457 151.878 180.004  1.00  9.26           N  
ATOM   4690  CA  HIS B 104     126.685 150.880 179.266  1.00  9.26           C  
ATOM   4691  C   HIS B 104     126.959 150.977 177.764  1.00  9.26           C  
ATOM   4692  O   HIS B 104     127.408 150.016 177.106  1.00  9.26           O  
ATOM   4693  CB  HIS B 104     125.210 151.165 179.563  1.00  9.26           C  
ATOM   4694  CG  HIS B 104     124.238 150.160 179.036  1.00  9.26           C  
ATOM   4695  ND1 HIS B 104     123.558 149.279 179.848  1.00  9.26           N  
ATOM   4696  CD2 HIS B 104     123.863 149.868 177.770  1.00  9.26           C  
ATOM   4697  CE1 HIS B 104     122.766 148.526 179.109  1.00  9.26           C  
ATOM   4698  NE2 HIS B 104     122.942 148.855 177.844  1.00  9.26           N  
ATOM   4699  N   ALA B 105     126.698 152.164 177.214  1.00  7.29           N  
ATOM   4700  CA  ALA B 105     126.880 152.412 175.791  1.00  7.29           C  
ATOM   4701  C   ALA B 105     128.330 152.217 175.372  1.00  7.29           C  
ATOM   4702  O   ALA B 105     128.598 151.732 174.269  1.00  7.29           O  
ATOM   4703  CB  ALA B 105     126.402 153.823 175.450  1.00  7.29           C  
ATOM   4704  N   ALA B 106     129.279 152.607 176.227  1.00  7.81           N  
ATOM   4705  CA  ALA B 106     130.691 152.405 175.910  1.00  7.81           C  
ATOM   4706  C   ALA B 106     131.029 150.923 175.752  1.00  7.81           C  
ATOM   4707  O   ALA B 106     131.781 150.542 174.846  1.00  7.81           O  
ATOM   4708  CB  ALA B 106     131.563 153.051 176.986  1.00  7.81           C  
ATOM   4709  N   LYS B 107     130.479 150.071 176.622  1.00  7.56           N  
ATOM   4710  CA  LYS B 107     130.697 148.627 176.495  1.00  7.56           C  
ATOM   4711  C   LYS B 107     130.166 148.110 175.155  1.00  7.56           C  
ATOM   4712  O   LYS B 107     130.861 147.375 174.419  1.00  7.56           O  
ATOM   4713  CB  LYS B 107     130.044 147.889 177.678  1.00  7.56           C  
ATOM   4714  CG  LYS B 107     130.731 148.109 179.028  1.00  7.56           C  
ATOM   4715  CD  LYS B 107     130.087 147.355 180.214  1.00  7.56           C  
ATOM   4716  CE  LYS B 107     129.949 145.864 179.991  1.00  7.56           C  
ATOM   4717  NZ  LYS B 107     129.683 145.095 181.244  1.00  7.56           N  
ATOM   4718  N   ILE B 108     128.940 148.517 174.804  1.00 12.77           N  
ATOM   4719  CA  ILE B 108     128.366 148.072 173.529  1.00 12.77           C  
ATOM   4720  C   ILE B 108     129.221 148.562 172.356  1.00 12.77           C  
ATOM   4721  O   ILE B 108     129.468 147.821 171.393  1.00 12.77           O  
ATOM   4722  CB  ILE B 108     126.892 148.521 173.398  1.00 12.77           C  
ATOM   4723  CG1 ILE B 108     126.024 147.881 174.495  1.00 12.77           C  
ATOM   4724  CG2 ILE B 108     126.328 148.146 172.023  1.00 12.77           C  
ATOM   4725  CD1 ILE B 108     124.583 148.291 174.495  1.00 12.77           C  
ATOM   4726  N   VAL B 109     129.669 149.819 172.410  1.00  6.18           N  
ATOM   4727  CA  VAL B 109     130.506 150.384 171.351  1.00  6.18           C  
ATOM   4728  C   VAL B 109     131.801 149.591 171.201  1.00  6.18           C  
ATOM   4729  O   VAL B 109     132.278 149.364 170.081  1.00  6.18           O  
ATOM   4730  CB  VAL B 109     130.779 151.878 171.623  1.00  6.18           C  
ATOM   4731  CG1 VAL B 109     131.954 152.374 170.811  1.00  6.18           C  
ATOM   4732  CG2 VAL B 109     129.538 152.730 171.327  1.00  6.18           C  
ATOM   4733  N   LYS B 110     132.394 149.161 172.319  1.00  5.62           N  
ATOM   4734  CA  LYS B 110     133.625 148.378 172.238  1.00  5.62           C  
ATOM   4735  C   LYS B 110     133.393 147.109 171.428  1.00  5.62           C  
ATOM   4736  O   LYS B 110     134.159 146.794 170.501  1.00  5.62           O  
ATOM   4737  CB  LYS B 110     134.150 148.048 173.644  1.00  5.62           C  
ATOM   4738  CG  LYS B 110     135.335 147.069 173.679  1.00  5.62           C  
ATOM   4739  CD  LYS B 110     135.837 146.738 175.098  1.00  5.62           C  
ATOM   4740  CE  LYS B 110     136.282 147.968 175.872  1.00  5.62           C  
ATOM   4741  NZ  LYS B 110     137.042 147.641 177.117  1.00  5.62           N  
ATOM   4742  N   VAL B 111     132.323 146.373 171.749  1.00  6.86           N  
ATOM   4743  CA  VAL B 111     132.124 145.123 171.010  1.00  6.86           C  
ATOM   4744  C   VAL B 111     131.760 145.392 169.543  1.00  6.86           C  
ATOM   4745  O   VAL B 111     132.182 144.644 168.648  1.00  6.86           O  
ATOM   4746  CB  VAL B 111     131.102 144.201 171.709  1.00  6.86           C  
ATOM   4747  CG1 VAL B 111     129.745 144.827 171.811  1.00  6.86           C  
ATOM   4748  CG2 VAL B 111     131.001 142.883 170.978  1.00  6.86           C  
ATOM   4749  N   GLN B 112     131.024 146.470 169.256  1.00  5.64           N  
ATOM   4750  CA  GLN B 112     130.712 146.797 167.861  1.00  5.64           C  
ATOM   4751  C   GLN B 112     131.986 147.060 167.059  1.00  5.64           C  
ATOM   4752  O   GLN B 112     132.172 146.523 165.953  1.00  5.64           O  
ATOM   4753  CB  GLN B 112     129.784 148.012 167.797  1.00  5.64           C  
ATOM   4754  CG  GLN B 112     128.314 147.715 168.046  1.00  5.64           C  
ATOM   4755  CD  GLN B 112     127.433 148.928 167.840  1.00  5.64           C  
ATOM   4756  OE1 GLN B 112     126.547 148.937 166.990  1.00  5.64           O  
ATOM   4757  NE2 GLN B 112     127.679 149.962 168.617  1.00  5.64           N  
ATOM   4758  N   ASP B 113     132.881 147.883 167.614  1.00  5.98           N  
ATOM   4759  CA  ASP B 113     134.140 148.194 166.944  1.00  5.98           C  
ATOM   4760  C   ASP B 113     134.946 146.927 166.681  1.00  5.98           C  
ATOM   4761  O   ASP B 113     135.477 146.732 165.580  1.00  5.98           O  
ATOM   4762  CB  ASP B 113     134.958 149.182 167.780  1.00  5.98           C  
ATOM   4763  CG  ASP B 113     134.389 150.588 167.754  1.00  5.98           C  
ATOM   4764  OD1 ASP B 113     133.636 150.918 166.817  1.00  5.98           O  
ATOM   4765  OD2 ASP B 113     134.700 151.369 168.674  1.00  5.98           O  
ATOM   4766  N   MET B 114     135.053 146.056 167.687  1.00  7.59           N  
ATOM   4767  CA  MET B 114     135.828 144.830 167.499  1.00  7.59           C  
ATOM   4768  C   MET B 114     135.229 143.958 166.397  1.00  7.59           C  
ATOM   4769  O   MET B 114     135.963 143.401 165.567  1.00  7.59           O  
ATOM   4770  CB  MET B 114     135.930 144.056 168.811  1.00  7.59           C  
ATOM   4771  CG  MET B 114     136.774 144.739 169.873  1.00  7.59           C  
ATOM   4772  SD  MET B 114     137.253 143.605 171.180  1.00  7.59           S  
ATOM   4773  CE  MET B 114     138.476 142.645 170.304  1.00  7.59           C  
ATOM   4774  N   ALA B 115     133.897 143.853 166.352  1.00  5.37           N  
ATOM   4775  CA  ALA B 115     133.265 143.007 165.345  1.00  5.37           C  
ATOM   4776  C   ALA B 115     133.517 143.539 163.943  1.00  5.37           C  
ATOM   4777  O   ALA B 115     133.689 142.759 163.001  1.00  5.37           O  
ATOM   4778  CB  ALA B 115     131.766 142.891 165.607  1.00  5.37           C  
ATOM   4779  N   LEU B 116     133.531 144.862 163.776  1.00  4.88           N  
ATOM   4780  CA  LEU B 116     133.823 145.397 162.448  1.00  4.88           C  
ATOM   4781  C   LEU B 116     135.290 145.184 162.086  1.00  4.88           C  
ATOM   4782  O   LEU B 116     135.608 144.839 160.943  1.00  4.88           O  
ATOM   4783  CB  LEU B 116     133.460 146.878 162.356  1.00  4.88           C  
ATOM   4784  CG  LEU B 116     133.638 147.500 160.964  1.00  4.88           C  
ATOM   4785  CD1 LEU B 116     132.671 146.904 159.955  1.00  4.88           C  
ATOM   4786  CD2 LEU B 116     133.471 148.994 161.015  1.00  4.88           C  
ATOM   4787  N   LYS B 117     136.192 145.362 163.058  1.00  8.24           N  
ATOM   4788  CA  LYS B 117     137.621 145.219 162.797  1.00  8.24           C  
ATOM   4789  C   LYS B 117     137.980 143.797 162.385  1.00  8.24           C  
ATOM   4790  O   LYS B 117     138.803 143.600 161.485  1.00  8.24           O  
ATOM   4791  CB  LYS B 117     138.414 145.642 164.035  1.00  8.24           C  
ATOM   4792  CG  LYS B 117     139.920 145.539 163.920  1.00  8.24           C  
ATOM   4793  CD  LYS B 117     140.600 145.697 165.279  1.00  8.24           C  
ATOM   4794  CE  LYS B 117     140.083 146.895 166.047  1.00  8.24           C  
ATOM   4795  NZ  LYS B 117     140.078 148.121 165.219  1.00  8.24           N  
ATOM   4796  N   MET B 118     137.385 142.795 163.024  1.00  6.60           N  
ATOM   4797  CA  MET B 118     137.712 141.408 162.709  1.00  6.60           C  
ATOM   4798  C   MET B 118     136.775 140.786 161.675  1.00  6.60           C  
ATOM   4799  O   MET B 118     136.956 139.616 161.328  1.00  6.60           O  
ATOM   4800  CB  MET B 118     137.719 140.562 163.986  1.00  6.60           C  
ATOM   4801  CG  MET B 118     139.099 140.375 164.605  1.00  6.60           C  
ATOM   4802  SD  MET B 118     139.925 141.898 165.083  1.00  6.60           S  
ATOM   4803  CE  MET B 118     139.072 142.301 166.600  1.00  6.60           C  
ATOM   4804  N   ARG B 119     135.814 141.546 161.157  1.00  7.79           N  
ATOM   4805  CA  ARG B 119     134.866 141.101 160.135  1.00  7.79           C  
ATOM   4806  C   ARG B 119     134.184 139.785 160.534  1.00  7.79           C  
ATOM   4807  O   ARG B 119     134.343 138.747 159.893  1.00  7.79           O  
ATOM   4808  CB  ARG B 119     135.555 140.995 158.767  1.00  7.79           C  
ATOM   4809  CG  ARG B 119     136.274 142.271 158.324  1.00  7.79           C  
ATOM   4810  CD  ARG B 119     135.301 143.354 157.898  1.00  7.79           C  
ATOM   4811  NE  ARG B 119     135.880 144.336 156.988  1.00  7.79           N  
ATOM   4812  CZ  ARG B 119     136.493 145.451 157.372  1.00  7.79           C  
ATOM   4813  NH1 ARG B 119     136.979 146.277 156.460  1.00  7.79           N  
ATOM   4814  NH2 ARG B 119     136.636 145.742 158.656  1.00  7.79           N  
ATOM   4815  N   ALA B 120     133.428 139.848 161.625  1.00  4.56           N  
ATOM   4816  CA  ALA B 120     132.586 138.766 162.115  1.00  4.56           C  
ATOM   4817  C   ALA B 120     131.195 139.262 162.493  1.00  4.56           C  
ATOM   4818  O   ALA B 120     130.997 140.459 162.721  1.00  4.56           O  
ATOM   4819  CB  ALA B 120     133.231 138.079 163.329  1.00  4.56           C  
ATOM   4820  N   PRO B 121     130.209 138.360 162.579  1.00  6.56           N  
ATOM   4821  CA  PRO B 121     128.834 138.773 162.907  1.00  6.56           C  
ATOM   4822  C   PRO B 121     128.673 139.216 164.358  1.00  6.56           C  
ATOM   4823  O   PRO B 121     129.459 138.861 165.237  1.00  6.56           O  
ATOM   4824  CB  PRO B 121     128.008 137.510 162.632  1.00  6.56           C  
ATOM   4825  CG  PRO B 121     128.861 136.657 161.786  1.00  6.56           C  
ATOM   4826  CD  PRO B 121     130.256 136.934 162.219  1.00  6.56           C  
ATOM   4827  N   ILE B 122     127.604 139.983 164.604  1.00 12.77           N  
ATOM   4828  CA  ILE B 122     127.275 140.508 165.930  1.00 12.77           C  
ATOM   4829  C   ILE B 122     125.785 140.302 166.222  1.00 12.77           C  
ATOM   4830  O   ILE B 122     124.923 140.567 165.369  1.00 12.77           O  
ATOM   4831  CB  ILE B 122     127.680 141.993 166.078  1.00 12.77           C  
ATOM   4832  CG1 ILE B 122     127.461 142.492 167.517  1.00 12.77           C  
ATOM   4833  CG2 ILE B 122     126.969 142.878 165.080  1.00 12.77           C  
ATOM   4834  CD1 ILE B 122     128.210 143.761 167.846  1.00 12.77           C  
ATOM   4835  N   ILE B 123     125.501 139.812 167.432  1.00  6.94           N  
ATOM   4836  CA  ILE B 123     124.163 139.475 167.912  1.00  6.94           C  
ATOM   4837  C   ILE B 123     123.838 140.348 169.125  1.00  6.94           C  
ATOM   4838  O   ILE B 123     124.593 140.362 170.102  1.00  6.94           O  
ATOM   4839  CB  ILE B 123     124.056 137.984 168.296  1.00  6.94           C  
ATOM   4840  CG1 ILE B 123     124.571 137.046 167.191  1.00  6.94           C  
ATOM   4841  CG2 ILE B 123     122.629 137.632 168.679  1.00  6.94           C  
ATOM   4842  CD1 ILE B 123     123.941 137.217 165.865  1.00  6.94           C  
ATOM   4843  N   GLY B 124     122.709 141.051 169.071  1.00  6.98           N  
ATOM   4844  CA  GLY B 124     122.221 141.857 170.185  1.00  6.98           C  
ATOM   4845  C   GLY B 124     120.921 141.299 170.745  1.00  6.98           C  
ATOM   4846  O   GLY B 124     119.983 141.027 169.998  1.00  6.98           O  
ATOM   4847  N   ILE B 125     120.880 141.151 172.068  1.00  6.67           N  
ATOM   4848  CA  ILE B 125     119.731 140.618 172.795  1.00  6.67           C  
ATOM   4849  C   ILE B 125     119.179 141.726 173.688  1.00  6.67           C  
ATOM   4850  O   ILE B 125     119.925 142.326 174.470  1.00  6.67           O  
ATOM   4851  CB  ILE B 125     120.115 139.373 173.617  1.00  6.67           C  
ATOM   4852  CG1 ILE B 125     120.823 138.340 172.733  1.00  6.67           C  
ATOM   4853  CG2 ILE B 125     118.892 138.746 174.262  1.00  6.67           C  
ATOM   4854  CD1 ILE B 125     121.355 137.141 173.470  1.00  6.67           C  
ATOM   4855  N   PHE B 126     117.874 141.976 173.592  1.00  7.76           N  
ATOM   4856  CA  PHE B 126     117.263 143.205 174.090  1.00  7.76           C  
ATOM   4857  C   PHE B 126     116.205 142.900 175.143  1.00  7.76           C  
ATOM   4858  O   PHE B 126     115.258 142.151 174.883  1.00  7.76           O  
ATOM   4859  CB  PHE B 126     116.647 144.000 172.941  1.00  7.76           C  
ATOM   4860  CG  PHE B 126     117.655 144.636 172.038  1.00  7.76           C  
ATOM   4861  CD1 PHE B 126     118.249 143.918 171.021  1.00  7.76           C  
ATOM   4862  CD2 PHE B 126     118.012 145.954 172.209  1.00  7.76           C  
ATOM   4863  CE1 PHE B 126     119.172 144.508 170.195  1.00  7.76           C  
ATOM   4864  CE2 PHE B 126     118.935 146.543 171.386  1.00  7.76           C  
ATOM   4865  CZ  PHE B 126     119.516 145.821 170.381  1.00  7.76           C  
ATOM   4866  N   ASP B 127     116.379 143.483 176.331  1.00 12.97           N  
ATOM   4867  CA  ASP B 127     115.418 143.429 177.438  1.00 12.97           C  
ATOM   4868  C   ASP B 127     115.669 144.683 178.283  1.00 12.97           C  
ATOM   4869  O   ASP B 127     116.518 144.674 179.176  1.00 12.97           O  
ATOM   4870  CB  ASP B 127     115.607 142.147 178.236  1.00 12.97           C  
ATOM   4871  CG  ASP B 127     114.485 141.881 179.222  1.00 12.97           C  
ATOM   4872  OD1 ASP B 127     113.625 142.758 179.422  1.00 12.97           O  
ATOM   4873  OD2 ASP B 127     114.475 140.776 179.799  1.00 12.97           O  
ATOM   4874  N   ALA B 128     114.912 145.746 178.015  1.00 17.42           N  
ATOM   4875  CA  ALA B 128     115.356 147.074 178.437  1.00 17.42           C  
ATOM   4876  C   ALA B 128     114.257 148.113 178.248  1.00 17.42           C  
ATOM   4877  O   ALA B 128     113.253 147.877 177.572  1.00 17.42           O  
ATOM   4878  CB  ALA B 128     116.604 147.490 177.664  1.00 17.42           C  
ATOM   4879  N   GLY B 129     114.488 149.290 178.840  1.00 24.50           N  
ATOM   4880  CA  GLY B 129     113.522 150.371 178.853  1.00 24.50           C  
ATOM   4881  C   GLY B 129     114.041 151.717 178.376  1.00 24.50           C  
ATOM   4882  O   GLY B 129     113.406 152.743 178.629  1.00 24.50           O  
ATOM   4883  N   GLY B 130     115.186 151.742 177.697  1.00 19.33           N  
ATOM   4884  CA  GLY B 130     115.644 152.959 177.050  1.00 19.33           C  
ATOM   4885  C   GLY B 130     116.679 153.767 177.812  1.00 19.33           C  
ATOM   4886  O   GLY B 130     117.471 153.216 178.578  1.00 19.33           O  
ATOM   4887  N   ALA B 131     116.679 155.083 177.598  1.00 17.95           N  
ATOM   4888  CA  ALA B 131     117.678 155.963 178.191  1.00 17.95           C  
ATOM   4889  C   ALA B 131     117.412 156.172 179.678  1.00 17.95           C  
ATOM   4890  O   ALA B 131     116.298 156.519 180.078  1.00 17.95           O  
ATOM   4891  CB  ALA B 131     117.696 157.310 177.471  1.00 17.95           C  
ATOM   4892  N   ARG B 132     118.452 155.978 180.487  1.00 15.25           N  
ATOM   4893  CA  ARG B 132     118.353 156.142 181.934  1.00 15.25           C  
ATOM   4894  C   ARG B 132     118.101 157.608 182.272  1.00 15.25           C  
ATOM   4895  O   ARG B 132     118.958 158.464 182.035  1.00 15.25           O  
ATOM   4896  CB  ARG B 132     119.633 155.639 182.604  1.00 15.25           C  
ATOM   4897  CG  ARG B 132     119.512 155.398 184.106  1.00 15.25           C  
ATOM   4898  CD  ARG B 132     120.760 154.755 184.710  1.00 15.25           C  
ATOM   4899  NE  ARG B 132     121.050 153.434 184.162  1.00 15.25           N  
ATOM   4900  CZ  ARG B 132     122.162 152.747 184.403  1.00 15.25           C  
ATOM   4901  NH1 ARG B 132     123.107 153.242 185.187  1.00 15.25           N  
ATOM   4902  NH2 ARG B 132     122.333 151.554 183.859  1.00 15.25           N  
ATOM   4903  N   ILE B 133     116.931 157.892 182.849  1.00 17.82           N  
ATOM   4904  CA  ILE B 133     116.485 159.276 182.993  1.00 17.82           C  
ATOM   4905  C   ILE B 133     117.435 160.063 183.891  1.00 17.82           C  
ATOM   4906  O   ILE B 133     117.800 161.204 183.583  1.00 17.82           O  
ATOM   4907  CB  ILE B 133     115.040 159.325 183.528  1.00 17.82           C  
ATOM   4908  CG1 ILE B 133     114.085 158.495 182.662  1.00 17.82           C  
ATOM   4909  CG2 ILE B 133     114.557 160.760 183.602  1.00 17.82           C  
ATOM   4910  CD1 ILE B 133     114.130 158.805 181.190  1.00 17.82           C  
ATOM   4911  N   GLN B 134     117.847 159.468 185.012  1.00 18.67           N  
ATOM   4912  CA  GLN B 134     118.680 160.168 185.985  1.00 18.67           C  
ATOM   4913  C   GLN B 134     119.963 160.727 185.383  1.00 18.67           C  
ATOM   4914  O   GLN B 134     120.513 161.688 185.927  1.00 18.67           O  
ATOM   4915  CB  GLN B 134     119.036 159.236 187.145  1.00 18.67           C  
ATOM   4916  CG  GLN B 134     117.866 158.808 188.002  1.00 18.67           C  
ATOM   4917  CD  GLN B 134     117.153 157.582 187.475  1.00 18.67           C  
ATOM   4918  OE1 GLN B 134     117.465 157.076 186.399  1.00 18.67           O  
ATOM   4919  NE2 GLN B 134     116.188 157.095 188.238  1.00 18.67           N  
ATOM   4920  N   GLU B 135     120.458 160.149 184.290  1.00 16.84           N  
ATOM   4921  CA  GLU B 135     121.707 160.594 183.687  1.00 16.84           C  
ATOM   4922  C   GLU B 135     121.525 161.728 182.682  1.00 16.84           C  
ATOM   4923  O   GLU B 135     122.522 162.325 182.265  1.00 16.84           O  
ATOM   4924  CB  GLU B 135     122.415 159.415 183.008  1.00 16.84           C  
ATOM   4925  CG  GLU B 135     123.151 158.492 183.966  1.00 16.84           C  
ATOM   4926  CD  GLU B 135     124.293 157.739 183.303  1.00 16.84           C  
ATOM   4927  OE1 GLU B 135     124.363 157.719 182.057  1.00 16.84           O  
ATOM   4928  OE2 GLU B 135     125.126 157.167 184.033  1.00 16.84           O  
ATOM   4929  N   GLY B 136     120.292 162.045 182.287  1.00 11.68           N  
ATOM   4930  CA  GLY B 136     120.085 163.184 181.411  1.00 11.68           C  
ATOM   4931  C   GLY B 136     120.685 162.997 180.026  1.00 11.68           C  
ATOM   4932  O   GLY B 136     120.871 161.878 179.537  1.00 11.68           O  
ATOM   4933  N   VAL B 137     121.007 164.131 179.393  1.00  9.74           N  
ATOM   4934  CA  VAL B 137     121.401 164.143 177.985  1.00  9.74           C  
ATOM   4935  C   VAL B 137     122.606 163.249 177.731  1.00  9.74           C  
ATOM   4936  O   VAL B 137     122.763 162.713 176.628  1.00  9.74           O  
ATOM   4937  CB  VAL B 137     121.666 165.589 177.509  1.00  9.74           C  
ATOM   4938  CG1 VAL B 137     122.895 166.162 178.176  1.00  9.74           C  
ATOM   4939  CG2 VAL B 137     121.812 165.636 175.991  1.00  9.74           C  
ATOM   4940  N   ALA B 138     123.476 163.070 178.727  1.00 10.14           N  
ATOM   4941  CA  ALA B 138     124.624 162.189 178.538  1.00 10.14           C  
ATOM   4942  C   ALA B 138     124.181 160.829 178.018  1.00 10.14           C  
ATOM   4943  O   ALA B 138     124.754 160.303 177.055  1.00 10.14           O  
ATOM   4944  CB  ALA B 138     125.401 162.041 179.845  1.00 10.14           C  
ATOM   4945  N   ALA B 139     123.123 160.270 178.610  1.00 10.41           N  
ATOM   4946  CA  ALA B 139     122.616 158.982 178.154  1.00 10.41           C  
ATOM   4947  C   ALA B 139     122.290 159.019 176.669  1.00 10.41           C  
ATOM   4948  O   ALA B 139     122.674 158.114 175.919  1.00 10.41           O  
ATOM   4949  CB  ALA B 139     121.387 158.583 178.966  1.00 10.41           C  
ATOM   4950  N   LEU B 140     121.610 160.076 176.220  1.00  9.58           N  
ATOM   4951  CA  LEU B 140     121.277 160.196 174.807  1.00  9.58           C  
ATOM   4952  C   LEU B 140     122.534 160.102 173.956  1.00  9.58           C  
ATOM   4953  O   LEU B 140     122.573 159.371 172.958  1.00  9.58           O  
ATOM   4954  CB  LEU B 140     120.537 161.512 174.551  1.00  9.58           C  
ATOM   4955  CG  LEU B 140     119.227 161.728 175.323  1.00  9.58           C  
ATOM   4956  CD1 LEU B 140     118.642 163.093 175.011  1.00  9.58           C  
ATOM   4957  CD2 LEU B 140     118.225 160.635 175.006  1.00  9.58           C  
ATOM   4958  N   GLY B 141     123.593 160.796 174.373  1.00  9.81           N  
ATOM   4959  CA  GLY B 141     124.842 160.719 173.637  1.00  9.81           C  
ATOM   4960  C   GLY B 141     125.250 159.286 173.376  1.00  9.81           C  
ATOM   4961  O   GLY B 141     125.568 158.912 172.245  1.00  9.81           O  
ATOM   4962  N   GLY B 142     125.189 158.451 174.416  1.00 10.71           N  
ATOM   4963  CA  GLY B 142     125.529 157.050 174.242  1.00 10.71           C  
ATOM   4964  C   GLY B 142     124.760 156.414 173.103  1.00 10.71           C  
ATOM   4965  O   GLY B 142     125.353 155.862 172.171  1.00 10.71           O  
ATOM   4966  N   HIS B 143     123.459 156.417 173.187  1.00 10.74           N  
ATOM   4967  CA  HIS B 143     122.586 155.940 172.090  1.00 10.74           C  
ATOM   4968  C   HIS B 143     123.171 156.403 170.732  1.00 10.74           C  
ATOM   4969  O   HIS B 143     123.424 155.574 169.831  1.00 10.74           O  
ATOM   4970  CB  HIS B 143     121.160 156.460 172.360  1.00 10.74           C  
ATOM   4971  CG  HIS B 143     120.394 155.490 173.160  1.00 10.74           C  
ATOM   4972  ND1 HIS B 143     119.445 155.823 174.031  1.00 10.74           N  
ATOM   4973  CD2 HIS B 143     120.385 154.166 173.150  1.00 10.74           C  
ATOM   4974  CE1 HIS B 143     118.889 154.775 174.515  1.00 10.74           C  
ATOM   4975  NE2 HIS B 143     119.437 153.764 174.000  1.00 10.74           N  
ATOM   4976  N   GLY B 144     123.461 157.706 170.550  1.00  8.50           N  
ATOM   4977  CA  GLY B 144     123.948 158.189 169.274  1.00  8.50           C  
ATOM   4978  C   GLY B 144     125.137 157.392 168.783  1.00  8.50           C  
ATOM   4979  O   GLY B 144     125.126 156.861 167.670  1.00  8.50           O  
ATOM   4980  N   GLU B 145     126.144 157.228 169.642  1.00  9.75           N  
ATOM   4981  CA  GLU B 145     127.370 156.572 169.208  1.00  9.75           C  
ATOM   4982  C   GLU B 145     127.093 155.141 168.767  1.00  9.75           C  
ATOM   4983  O   GLU B 145     127.721 154.642 167.828  1.00  9.75           O  
ATOM   4984  CB  GLU B 145     128.415 156.614 170.324  1.00  9.75           C  
ATOM   4985  CG  GLU B 145     128.908 158.014 170.692  1.00  9.75           C  
ATOM   4986  CD  GLU B 145     129.599 158.726 169.541  1.00  9.75           C  
ATOM   4987  OE1 GLU B 145     130.097 158.043 168.622  1.00  9.75           O  
ATOM   4988  OE2 GLU B 145     129.646 159.972 169.551  1.00  9.75           O  
ATOM   4989  N   VAL B 146     126.134 154.476 169.412  1.00  6.39           N  
ATOM   4990  CA  VAL B 146     125.765 153.125 168.998  1.00  6.39           C  
ATOM   4991  C   VAL B 146     125.126 153.162 167.615  1.00  6.39           C  
ATOM   4992  O   VAL B 146     125.531 152.427 166.705  1.00  6.39           O  
ATOM   4993  CB  VAL B 146     124.841 152.476 170.048  1.00  6.39           C  
ATOM   4994  CG1 VAL B 146     124.275 151.155 169.543  1.00  6.39           C  
ATOM   4995  CG2 VAL B 146     125.595 152.266 171.351  1.00  6.39           C  
ATOM   4996  N   PHE B 147     124.164 154.069 167.422  1.00  5.87           N  
ATOM   4997  CA  PHE B 147     123.472 154.182 166.140  1.00  5.87           C  
ATOM   4998  C   PHE B 147     124.468 154.280 164.993  1.00  5.87           C  
ATOM   4999  O   PHE B 147     124.423 153.490 164.042  1.00  5.87           O  
ATOM   5000  CB  PHE B 147     122.555 155.410 166.141  1.00  5.87           C  
ATOM   5001  CG  PHE B 147     121.413 155.343 167.123  1.00  5.87           C  
ATOM   5002  CD1 PHE B 147     121.006 154.150 167.688  1.00  5.87           C  
ATOM   5003  CD2 PHE B 147     120.734 156.496 167.469  1.00  5.87           C  
ATOM   5004  CE1 PHE B 147     119.961 154.118 168.578  1.00  5.87           C  
ATOM   5005  CE2 PHE B 147     119.693 156.463 168.347  1.00  5.87           C  
ATOM   5006  CZ  PHE B 147     119.303 155.282 168.903  1.00  5.87           C  
ATOM   5007  N   ARG B 148     125.398 155.233 165.088  1.00  9.61           N  
ATOM   5008  CA  ARG B 148     126.354 155.455 164.011  1.00  9.61           C  
ATOM   5009  C   ARG B 148     127.048 154.156 163.627  1.00  9.61           C  
ATOM   5010  O   ARG B 148     127.142 153.821 162.440  1.00  9.61           O  
ATOM   5011  CB  ARG B 148     127.373 156.527 164.419  1.00  9.61           C  
ATOM   5012  CG  ARG B 148     128.588 156.629 163.505  1.00  9.61           C  
ATOM   5013  CD  ARG B 148     129.353 157.940 163.637  1.00  9.61           C  
ATOM   5014  NE  ARG B 148     129.407 158.485 164.986  1.00  9.61           N  
ATOM   5015  CZ  ARG B 148     130.026 159.623 165.286  1.00  9.61           C  
ATOM   5016  NH1 ARG B 148     130.035 160.072 166.532  1.00  9.61           N  
ATOM   5017  NH2 ARG B 148     130.650 160.311 164.338  1.00  9.61           N  
ATOM   5018  N   ARG B 149     127.481 153.376 164.621  1.00  6.10           N  
ATOM   5019  CA  ARG B 149     128.234 152.173 164.303  1.00  6.10           C  
ATOM   5020  C   ARG B 149     127.359 151.160 163.574  1.00  6.10           C  
ATOM   5021  O   ARG B 149     127.809 150.540 162.604  1.00  6.10           O  
ATOM   5022  CB  ARG B 149     128.866 151.600 165.574  1.00  6.10           C  
ATOM   5023  CG  ARG B 149     130.172 152.325 165.918  1.00  6.10           C  
ATOM   5024  CD  ARG B 149     130.556 152.313 167.366  1.00  6.10           C  
ATOM   5025  NE  ARG B 149     131.750 153.132 167.555  1.00  6.10           N  
ATOM   5026  CZ  ARG B 149     131.739 154.448 167.741  1.00  6.10           C  
ATOM   5027  NH1 ARG B 149     130.599 155.119 167.784  1.00  6.10           N  
ATOM   5028  NH2 ARG B 149     132.879 155.096 167.893  1.00  6.10           N  
ATOM   5029  N   ASN B 150     126.085 151.035 163.966  1.00  6.16           N  
ATOM   5030  CA  ASN B 150     125.179 150.182 163.203  1.00  6.16           C  
ATOM   5031  C   ASN B 150     125.273 150.532 161.723  1.00  6.16           C  
ATOM   5032  O   ASN B 150     125.534 149.668 160.877  1.00  6.16           O  
ATOM   5033  CB  ASN B 150     123.732 150.320 163.695  1.00  6.16           C  
ATOM   5034  CG  ASN B 150     123.502 149.694 165.053  1.00  6.16           C  
ATOM   5035  OD1 ASN B 150     123.176 150.379 166.017  1.00  6.16           O  
ATOM   5036  ND2 ASN B 150     123.653 148.384 165.133  1.00  6.16           N  
ATOM   5037  N   VAL B 151     125.170 151.824 161.411  1.00  5.10           N  
ATOM   5038  CA  VAL B 151     125.147 152.248 160.017  1.00  5.10           C  
ATOM   5039  C   VAL B 151     126.475 151.925 159.342  1.00  5.10           C  
ATOM   5040  O   VAL B 151     126.508 151.515 158.177  1.00  5.10           O  
ATOM   5041  CB  VAL B 151     124.795 153.746 159.923  1.00  5.10           C  
ATOM   5042  CG1 VAL B 151     124.937 154.252 158.500  1.00  5.10           C  
ATOM   5043  CG2 VAL B 151     123.384 153.994 160.443  1.00  5.10           C  
ATOM   5044  N   ALA B 152     127.590 152.087 160.060  1.00  5.16           N  
ATOM   5045  CA  ALA B 152     128.882 151.784 159.458  1.00  5.16           C  
ATOM   5046  C   ALA B 152     128.993 150.306 159.108  1.00  5.16           C  
ATOM   5047  O   ALA B 152     129.633 149.953 158.113  1.00  5.16           O  
ATOM   5048  CB  ALA B 152     130.021 152.205 160.385  1.00  5.16           C  
ATOM   5049  N   ALA B 153     128.361 149.435 159.890  1.00  4.59           N  
ATOM   5050  CA  ALA B 153     128.493 147.998 159.683  1.00  4.59           C  
ATOM   5051  C   ALA B 153     127.520 147.440 158.650  1.00  4.59           C  
ATOM   5052  O   ALA B 153     127.653 146.273 158.271  1.00  4.59           O  
ATOM   5053  CB  ALA B 153     128.296 147.257 161.005  1.00  4.59           C  
ATOM   5054  N   SER B 154     126.566 148.239 158.185  1.00  5.58           N  
ATOM   5055  CA  SER B 154     125.512 147.742 157.309  1.00  5.58           C  
ATOM   5056  C   SER B 154     126.082 147.340 155.953  1.00  5.58           C  
ATOM   5057  O   SER B 154     126.781 148.120 155.304  1.00  5.58           O  
ATOM   5058  CB  SER B 154     124.420 148.796 157.137  1.00  5.58           C  
ATOM   5059  OG  SER B 154     123.402 148.327 156.279  1.00  5.58           O  
ATOM   5060  N   GLY B 155     125.778 146.119 155.529  1.00  7.38           N  
ATOM   5061  CA  GLY B 155     126.337 145.555 154.320  1.00  7.38           C  
ATOM   5062  C   GLY B 155     127.766 145.069 154.423  1.00  7.38           C  
ATOM   5063  O   GLY B 155     128.350 144.705 153.397  1.00  7.38           O  
ATOM   5064  N   VAL B 156     128.347 145.041 155.622  1.00 12.77           N  
ATOM   5065  CA  VAL B 156     129.714 144.578 155.839  1.00 12.77           C  
ATOM   5066  C   VAL B 156     129.748 143.312 156.699  1.00 12.77           C  
ATOM   5067  O   VAL B 156     130.388 142.325 156.335  1.00 12.77           O  
ATOM   5068  CB  VAL B 156     130.586 145.695 156.461  1.00 12.77           C  
ATOM   5069  CG1 VAL B 156     132.004 145.210 156.658  1.00 12.77           C  
ATOM   5070  CG2 VAL B 156     130.575 146.953 155.594  1.00 12.77           C  
ATOM   5071  N   ILE B 157     129.079 143.331 157.850  1.00 12.77           N  
ATOM   5072  CA  ILE B 157     128.915 142.151 158.703  1.00 12.77           C  
ATOM   5073  C   ILE B 157     127.433 141.950 159.004  1.00 12.77           C  
ATOM   5074  O   ILE B 157     126.703 142.938 159.162  1.00 12.77           O  
ATOM   5075  CB  ILE B 157     129.716 142.265 160.013  1.00 12.77           C  
ATOM   5076  CG1 ILE B 157     129.367 143.552 160.777  1.00 12.77           C  
ATOM   5077  CG2 ILE B 157     131.206 142.151 159.743  1.00 12.77           C  
ATOM   5078  CD1 ILE B 157     129.875 143.595 162.193  1.00 12.77           C  
ATOM   5079  N   PRO B 158     126.944 140.712 159.104  1.00 12.77           N  
ATOM   5080  CA  PRO B 158     125.531 140.513 159.447  1.00 12.77           C  
ATOM   5081  C   PRO B 158     125.258 140.858 160.902  1.00 12.77           C  
ATOM   5082  O   PRO B 158     126.016 140.488 161.800  1.00 12.77           O  
ATOM   5083  CB  PRO B 158     125.294 139.025 159.174  1.00 12.77           C  
ATOM   5084  CG  PRO B 158     126.610 138.396 159.174  1.00 12.77           C  
ATOM   5085  CD  PRO B 158     127.658 139.438 158.935  1.00 12.77           C  
ATOM   5086  N   GLN B 159     124.150 141.556 161.123  1.00 12.77           N  
ATOM   5087  CA  GLN B 159     123.728 142.028 162.438  1.00 12.77           C  
ATOM   5088  C   GLN B 159     122.362 141.429 162.750  1.00 12.77           C  
ATOM   5089  O   GLN B 159     121.408 141.649 161.998  1.00 12.77           O  
ATOM   5090  CB  GLN B 159     123.668 143.559 162.467  1.00 12.77           C  
ATOM   5091  CG  GLN B 159     124.942 144.251 161.991  1.00 12.77           C  
ATOM   5092  CD  GLN B 159     124.830 145.765 161.984  1.00 12.77           C  
ATOM   5093  OE1 GLN B 159     125.126 146.424 162.975  1.00 12.77           O  
ATOM   5094  NE2 GLN B 159     124.404 146.322 160.861  1.00 12.77           N  
ATOM   5095  N   ILE B 160     122.263 140.668 163.845  1.00  7.09           N  
ATOM   5096  CA  ILE B 160     121.000 140.033 164.230  1.00  7.09           C  
ATOM   5097  C   ILE B 160     120.566 140.532 165.603  1.00  7.09           C  
ATOM   5098  O   ILE B 160     121.388 140.665 166.515  1.00  7.09           O  
ATOM   5099  CB  ILE B 160     121.085 138.491 164.227  1.00  7.09           C  
ATOM   5100  CG1 ILE B 160     121.335 137.946 162.818  1.00  7.09           C  
ATOM   5101  CG2 ILE B 160     119.811 137.876 164.791  1.00  7.09           C  
ATOM   5102  CD1 ILE B 160     121.852 136.532 162.813  1.00  7.09           C  
ATOM   5103  N   SER B 161     119.265 140.795 165.744  1.00  6.06           N  
ATOM   5104  CA  SER B 161     118.667 141.310 166.969  1.00  6.06           C  
ATOM   5105  C   SER B 161     117.539 140.400 167.448  1.00  6.06           C  
ATOM   5106  O   SER B 161     116.695 139.968 166.657  1.00  6.06           O  
ATOM   5107  CB  SER B 161     118.136 142.730 166.765  1.00  6.06           C  
ATOM   5108  OG  SER B 161     119.089 143.546 166.116  1.00  6.06           O  
ATOM   5109  N   VAL B 162     117.533 140.119 168.749  1.00  6.75           N  
ATOM   5110  CA  VAL B 162     116.539 139.268 169.397  1.00  6.75           C  
ATOM   5111  C   VAL B 162     115.887 140.070 170.522  1.00  6.75           C  
ATOM   5112  O   VAL B 162     116.559 140.441 171.493  1.00  6.75           O  
ATOM   5113  CB  VAL B 162     117.160 137.971 169.949  1.00  6.75           C  
ATOM   5114  CG1 VAL B 162     116.073 136.994 170.346  1.00  6.75           C  
ATOM   5115  CG2 VAL B 162     118.115 137.329 168.950  1.00  6.75           C  
ATOM   5116  N   ILE B 163     114.583 140.314 170.403  1.00 12.77           N  
ATOM   5117  CA  ILE B 163     113.809 141.026 171.418  1.00 12.77           C  
ATOM   5118  C   ILE B 163     113.189 139.986 172.343  1.00 12.77           C  
ATOM   5119  O   ILE B 163     112.297 139.235 171.942  1.00 12.77           O  
ATOM   5120  CB  ILE B 163     112.725 141.923 170.805  1.00 12.77           C  
ATOM   5121  CG1 ILE B 163     113.233 142.654 169.558  1.00 12.77           C  
ATOM   5122  CG2 ILE B 163     112.187 142.907 171.854  1.00 12.77           C  
ATOM   5123  CD1 ILE B 163     114.543 143.348 169.718  1.00 12.77           C  
ATOM   5124  N   MET B 164     113.649 139.953 173.589  1.00 10.85           N  
ATOM   5125  CA  MET B 164     113.214 138.956 174.561  1.00 10.85           C  
ATOM   5126  C   MET B 164     112.595 139.598 175.800  1.00 10.85           C  
ATOM   5127  O   MET B 164     112.465 138.945 176.841  1.00 10.85           O  
ATOM   5128  CB  MET B 164     114.394 138.051 174.923  1.00 10.85           C  
ATOM   5129  CG  MET B 164     115.175 137.573 173.700  1.00 10.85           C  
ATOM   5130  SD  MET B 164     116.464 136.353 174.018  1.00 10.85           S  
ATOM   5131  CE  MET B 164     115.482 134.887 174.261  1.00 10.85           C  
ATOM   5132  N   GLY B 165     112.200 140.863 175.696  1.00 10.73           N  
ATOM   5133  CA  GLY B 165     111.461 141.554 176.726  1.00 10.73           C  
ATOM   5134  C   GLY B 165     110.952 142.888 176.213  1.00 10.73           C  
ATOM   5135  O   GLY B 165     110.706 143.054 175.016  1.00 10.73           O  
ATOM   5136  N   PRO B 166     110.764 143.860 177.104  1.00 12.76           N  
ATOM   5137  CA  PRO B 166     110.425 145.211 176.649  1.00 12.76           C  
ATOM   5138  C   PRO B 166     111.565 145.861 175.885  1.00 12.76           C  
ATOM   5139  O   PRO B 166     112.744 145.580 176.116  1.00 12.76           O  
ATOM   5140  CB  PRO B 166     110.137 145.963 177.951  1.00 12.76           C  
ATOM   5141  CG  PRO B 166     109.817 144.917 178.930  1.00 12.76           C  
ATOM   5142  CD  PRO B 166     110.676 143.757 178.567  1.00 12.76           C  
ATOM   5143  N   CYS B 167     111.189 146.748 174.964  1.00 12.96           N  
ATOM   5144  CA  CYS B 167     112.142 147.560 174.210  1.00 12.96           C  
ATOM   5145  C   CYS B 167     111.413 148.834 173.789  1.00 12.96           C  
ATOM   5146  O   CYS B 167     110.667 148.828 172.807  1.00 12.96           O  
ATOM   5147  CB  CYS B 167     112.691 146.803 173.012  1.00 12.96           C  
ATOM   5148  SG  CYS B 167     113.883 147.741 172.049  1.00 12.96           S  
ATOM   5149  N   ALA B 168     111.594 149.906 174.583  1.00 15.24           N  
ATOM   5150  CA  ALA B 168     110.864 151.166 174.293  1.00 15.24           C  
ATOM   5151  C   ALA B 168     111.777 152.390 174.113  1.00 15.24           C  
ATOM   5152  O   ALA B 168     112.962 152.341 174.497  1.00 15.24           O  
ATOM   5153  CB  ALA B 168     109.830 151.410 175.367  1.00 15.24           C  
ATOM   5154  N   GLY B 169     111.182 153.445 173.540  1.00 14.60           N  
ATOM   5155  CA  GLY B 169     111.716 154.783 173.251  1.00 14.60           C  
ATOM   5156  C   GLY B 169     112.933 154.664 172.352  1.00 14.60           C  
ATOM   5157  O   GLY B 169     112.867 153.952 171.329  1.00 14.60           O  
ATOM   5158  N   GLY B 170     113.987 155.340 172.747  1.00 13.80           N  
ATOM   5159  CA  GLY B 170     115.281 155.302 172.041  1.00 13.80           C  
ATOM   5160  C   GLY B 170     115.825 153.895 171.807  1.00 13.80           C  
ATOM   5161  O   GLY B 170     116.556 153.741 170.809  1.00 13.80           O  
ATOM   5162  N   ASP B 171     115.526 152.897 172.659  1.00 15.57           N  
ATOM   5163  CA  ASP B 171     116.111 151.568 172.361  1.00 15.57           C  
ATOM   5164  C   ASP B 171     115.727 150.993 170.975  1.00 15.57           C  
ATOM   5165  O   ASP B 171     116.539 150.197 170.460  1.00 15.57           O  
ATOM   5166  CB  ASP B 171     115.704 150.573 173.450  1.00 15.57           C  
ATOM   5167  CG  ASP B 171     116.617 150.324 174.594  1.00 15.57           C  
ATOM   5168  OD1 ASP B 171     117.793 150.727 174.501  1.00 15.57           O  
ATOM   5169  OD2 ASP B 171     116.160 149.725 175.587  1.00 15.57           O  
ATOM   5170  N   VAL B 172     114.565 151.294 170.402  1.00 11.68           N  
ATOM   5171  CA  VAL B 172     114.075 150.577 169.176  1.00 11.68           C  
ATOM   5172  C   VAL B 172     114.816 150.840 167.871  1.00 11.68           C  
ATOM   5173  O   VAL B 172     114.849 149.976 166.987  1.00 11.68           O  
ATOM   5174  CB  VAL B 172     112.571 150.884 169.031  1.00 11.68           C  
ATOM   5175  CG1 VAL B 172     111.837 150.613 170.328  1.00 11.68           C  
ATOM   5176  CG2 VAL B 172     112.330 152.308 168.537  1.00 11.68           C  
ATOM   5177  N   TYR B 173     115.427 152.015 167.721  1.00 10.74           N  
ATOM   5178  CA  TYR B 173     116.012 152.365 166.436  1.00 10.74           C  
ATOM   5179  C   TYR B 173     117.301 151.604 166.146  1.00 10.74           C  
ATOM   5180  O   TYR B 173     117.708 151.546 164.986  1.00 10.74           O  
ATOM   5181  CB  TYR B 173     116.240 153.876 166.358  1.00 10.74           C  
ATOM   5182  CG  TYR B 173     114.953 154.668 166.258  1.00 10.74           C  
ATOM   5183  CD1 TYR B 173     114.030 154.407 165.255  1.00 10.74           C  
ATOM   5184  CD2 TYR B 173     114.657 155.668 167.167  1.00 10.74           C  
ATOM   5185  CE1 TYR B 173     112.858 155.118 165.158  1.00 10.74           C  
ATOM   5186  CE2 TYR B 173     113.483 156.387 167.078  1.00 10.74           C  
ATOM   5187  CZ  TYR B 173     112.586 156.108 166.073  1.00 10.74           C  
ATOM   5188  OH  TYR B 173     111.420 156.827 165.989  1.00 10.74           O  
ATOM   5189  N   SER B 174     117.940 150.993 167.144  1.00  7.95           N  
ATOM   5190  CA  SER B 174     119.121 150.199 166.823  1.00  7.95           C  
ATOM   5191  C   SER B 174     118.699 148.899 166.141  1.00  7.95           C  
ATOM   5192  O   SER B 174     119.175 148.616 165.036  1.00  7.95           O  
ATOM   5193  CB  SER B 174     119.982 149.924 168.061  1.00  7.95           C  
ATOM   5194  OG  SER B 174     121.240 149.400 167.686  1.00  7.95           O  
ATOM   5195  N   PRO B 175     117.811 148.091 166.735  1.00  7.19           N  
ATOM   5196  CA  PRO B 175     117.319 146.905 166.013  1.00  7.19           C  
ATOM   5197  C   PRO B 175     116.745 147.214 164.643  1.00  7.19           C  
ATOM   5198  O   PRO B 175     116.888 146.407 163.716  1.00  7.19           O  
ATOM   5199  CB  PRO B 175     116.237 146.340 166.942  1.00  7.19           C  
ATOM   5200  CG  PRO B 175     116.414 146.967 168.226  1.00  7.19           C  
ATOM   5201  CD  PRO B 175     117.314 148.137 168.120  1.00  7.19           C  
ATOM   5202  N   ALA B 176     116.086 148.362 164.495  1.00  8.84           N  
ATOM   5203  CA  ALA B 176     115.459 148.711 163.226  1.00  8.84           C  
ATOM   5204  C   ALA B 176     116.473 148.793 162.094  1.00  8.84           C  
ATOM   5205  O   ALA B 176     116.149 148.470 160.948  1.00  8.84           O  
ATOM   5206  CB  ALA B 176     114.714 150.036 163.369  1.00  8.84           C  
ATOM   5207  N   MET B 177     117.697 149.211 162.394  1.00 11.37           N  
ATOM   5208  CA  MET B 177     118.744 149.371 161.397  1.00 11.37           C  
ATOM   5209  C   MET B 177     119.561 148.104 161.169  1.00 11.37           C  
ATOM   5210  O   MET B 177     120.450 148.108 160.314  1.00 11.37           O  
ATOM   5211  CB  MET B 177     119.672 150.509 161.814  1.00 11.37           C  
ATOM   5212  CG  MET B 177     118.938 151.740 162.288  1.00 11.37           C  
ATOM   5213  SD  MET B 177     120.020 152.932 163.072  1.00 11.37           S  
ATOM   5214  CE  MET B 177     120.044 154.065 161.721  1.00 11.37           C  
ATOM   5215  N   THR B 178     119.295 147.037 161.917  1.00  7.25           N  
ATOM   5216  CA  THR B 178     119.960 145.756 161.727  1.00  7.25           C  
ATOM   5217  C   THR B 178     119.253 144.960 160.622  1.00  7.25           C  
ATOM   5218  O   THR B 178     118.272 145.413 160.029  1.00  7.25           O  
ATOM   5219  CB  THR B 178     120.010 144.990 163.048  1.00  7.25           C  
ATOM   5220  OG1 THR B 178     118.680 144.704 163.491  1.00  7.25           O  
ATOM   5221  CG2 THR B 178     120.750 145.799 164.123  1.00  7.25           C  
ATOM   5222  N   ASP B 179     119.769 143.764 160.321  1.00  7.95           N  
ATOM   5223  CA  ASP B 179     119.277 143.001 159.174  1.00  7.95           C  
ATOM   5224  C   ASP B 179     118.049 142.149 159.506  1.00  7.95           C  
ATOM   5225  O   ASP B 179     117.131 142.059 158.685  1.00  7.95           O  
ATOM   5226  CB  ASP B 179     120.393 142.123 158.605  1.00  7.95           C  
ATOM   5227  CG  ASP B 179     121.637 142.919 158.231  1.00  7.95           C  
ATOM   5228  OD1 ASP B 179     121.520 143.902 157.472  1.00  7.95           O  
ATOM   5229  OD2 ASP B 179     122.734 142.557 158.695  1.00  7.95           O  
ATOM   5230  N   PHE B 180     118.014 141.495 160.672  1.00  6.67           N  
ATOM   5231  CA  PHE B 180     116.869 140.688 161.087  1.00  6.67           C  
ATOM   5232  C   PHE B 180     116.497 140.971 162.542  1.00  6.67           C  
ATOM   5233  O   PHE B 180     117.371 141.059 163.410  1.00  6.67           O  
ATOM   5234  CB  PHE B 180     117.140 139.179 160.911  1.00  6.67           C  
ATOM   5235  CG  PHE B 180     117.617 138.797 159.539  1.00  6.67           C  
ATOM   5236  CD1 PHE B 180     116.744 138.748 158.470  1.00  6.67           C  
ATOM   5237  CD2 PHE B 180     118.942 138.487 159.322  1.00  6.67           C  
ATOM   5238  CE1 PHE B 180     117.189 138.401 157.213  1.00  6.67           C  
ATOM   5239  CE2 PHE B 180     119.387 138.134 158.072  1.00  6.67           C  
ATOM   5240  CZ  PHE B 180     118.511 138.091 157.017  1.00  6.67           C  
ATOM   5241  N   ILE B 181     115.194 141.115 162.794  1.00  5.45           N  
ATOM   5242  CA  ILE B 181     114.624 141.255 164.134  1.00  5.45           C  
ATOM   5243  C   ILE B 181     113.703 140.065 164.397  1.00  5.45           C  
ATOM   5244  O   ILE B 181     112.805 139.783 163.596  1.00  5.45           O  
ATOM   5245  CB  ILE B 181     113.847 142.578 164.298  1.00  5.45           C  
ATOM   5246  CG1 ILE B 181     114.708 143.793 163.934  1.00  5.45           C  
ATOM   5247  CG2 ILE B 181     113.319 142.720 165.732  1.00  5.45           C  
ATOM   5248  CD1 ILE B 181     113.907 145.064 163.741  1.00  5.45           C  
ATOM   5249  N   PHE B 182     113.921 139.377 165.518  1.00  6.50           N  
ATOM   5250  CA  PHE B 182     113.066 138.284 165.972  1.00  6.50           C  
ATOM   5251  C   PHE B 182     112.526 138.572 167.373  1.00  6.50           C  
ATOM   5252  O   PHE B 182     113.209 139.175 168.204  1.00  6.50           O  
ATOM   5253  CB  PHE B 182     113.823 136.948 165.968  1.00  6.50           C  
ATOM   5254  CG  PHE B 182     114.258 136.491 164.596  1.00  6.50           C  
ATOM   5255  CD1 PHE B 182     113.383 135.826 163.758  1.00  6.50           C  
ATOM   5256  CD2 PHE B 182     115.544 136.725 164.146  1.00  6.50           C  
ATOM   5257  CE1 PHE B 182     113.783 135.410 162.508  1.00  6.50           C  
ATOM   5258  CE2 PHE B 182     115.939 136.304 162.894  1.00  6.50           C  
ATOM   5259  CZ  PHE B 182     115.058 135.652 162.079  1.00  6.50           C  
ATOM   5260  N   MET B 183     111.295 138.119 167.636  1.00  7.63           N  
ATOM   5261  CA  MET B 183     110.577 138.401 168.875  1.00  7.63           C  
ATOM   5262  C   MET B 183     110.088 137.108 169.526  1.00  7.63           C  
ATOM   5263  O   MET B 183     109.912 136.083 168.866  1.00  7.63           O  
ATOM   5264  CB  MET B 183     109.369 139.329 168.634  1.00  7.63           C  
ATOM   5265  CG  MET B 183     109.688 140.650 167.943  1.00  7.63           C  
ATOM   5266  SD  MET B 183     108.258 141.745 167.734  1.00  7.63           S  
ATOM   5267  CE  MET B 183     107.749 142.045 169.428  1.00  7.63           C  
ATOM   5268  N   VAL B 184     109.854 137.174 170.837  1.00  7.99           N  
ATOM   5269  CA  VAL B 184     109.298 136.070 171.617  1.00  7.99           C  
ATOM   5270  C   VAL B 184     107.850 136.402 171.944  1.00  7.99           C  
ATOM   5271  O   VAL B 184     107.537 137.521 172.365  1.00  7.99           O  
ATOM   5272  CB  VAL B 184     110.092 135.790 172.911  1.00  7.99           C  
ATOM   5273  CG1 VAL B 184     109.504 134.599 173.659  1.00  7.99           C  
ATOM   5274  CG2 VAL B 184     111.551 135.529 172.606  1.00  7.99           C  
ATOM   5275  N   ARG B 185     106.973 135.423 171.763  1.00 12.29           N  
ATOM   5276  CA  ARG B 185     105.549 135.648 171.953  1.00 12.29           C  
ATOM   5277  C   ARG B 185     105.199 135.786 173.432  1.00 12.29           C  
ATOM   5278  O   ARG B 185     105.679 135.031 174.279  1.00 12.29           O  
ATOM   5279  CB  ARG B 185     104.740 134.507 171.327  1.00 12.29           C  
ATOM   5280  CG  ARG B 185     104.821 134.442 169.807  1.00 12.29           C  
ATOM   5281  CD  ARG B 185     103.745 133.555 169.198  1.00 12.29           C  
ATOM   5282  NE  ARG B 185     103.979 132.127 169.382  1.00 12.29           N  
ATOM   5283  CZ  ARG B 185     104.697 131.372 168.558  1.00 12.29           C  
ATOM   5284  NH1 ARG B 185     104.845 130.081 168.801  1.00 12.29           N  
ATOM   5285  NH2 ARG B 185     105.276 131.901 167.493  1.00 12.29           N  
ATOM   5286  N   ASP B 186     104.341 136.758 173.726  1.00 17.04           N  
ATOM   5287  CA  ASP B 186     103.644 137.015 174.981  1.00 17.04           C  
ATOM   5288  C   ASP B 186     104.512 137.661 176.066  1.00 17.04           C  
ATOM   5289  O   ASP B 186     103.963 138.085 177.083  1.00 17.04           O  
ATOM   5290  CB  ASP B 186     103.017 135.742 175.578  1.00 17.04           C  
ATOM   5291  CG  ASP B 186     102.336 134.878 174.535  1.00 17.04           C  
ATOM   5292  OD1 ASP B 186     101.607 135.429 173.685  1.00 17.04           O  
ATOM   5293  OD2 ASP B 186     102.537 133.647 174.561  1.00 17.04           O  
ATOM   5294  N   THR B 187     105.827 137.778 175.891  1.00 13.64           N  
ATOM   5295  CA  THR B 187     106.668 138.461 176.865  1.00 13.64           C  
ATOM   5296  C   THR B 187     107.460 139.633 176.304  1.00 13.64           C  
ATOM   5297  O   THR B 187     108.099 140.348 177.083  1.00 13.64           O  
ATOM   5298  CB  THR B 187     107.648 137.472 177.515  1.00 13.64           C  
ATOM   5299  OG1 THR B 187     108.381 136.776 176.501  1.00 13.64           O  
ATOM   5300  CG2 THR B 187     106.904 136.485 178.387  1.00 13.64           C  
ATOM   5301  N   SER B 188     107.442 139.855 174.996  1.00 10.03           N  
ATOM   5302  CA  SER B 188     108.200 140.924 174.363  1.00 10.03           C  
ATOM   5303  C   SER B 188     107.269 141.929 173.696  1.00 10.03           C  
ATOM   5304  O   SER B 188     106.147 141.594 173.309  1.00 10.03           O  
ATOM   5305  CB  SER B 188     109.169 140.364 173.323  1.00 10.03           C  
ATOM   5306  OG  SER B 188     108.485 139.599 172.356  1.00 10.03           O  
ATOM   5307  N   TYR B 189     107.750 143.166 173.562  1.00 11.13           N  
ATOM   5308  CA  TYR B 189     107.028 144.204 172.838  1.00 11.13           C  
ATOM   5309  C   TYR B 189     107.972 145.355 172.501  1.00 11.13           C  
ATOM   5310  O   TYR B 189     108.997 145.556 173.157  1.00 11.13           O  
ATOM   5311  CB  TYR B 189     105.812 144.704 173.627  1.00 11.13           C  
ATOM   5312  CG  TYR B 189     106.037 145.017 175.085  1.00 11.13           C  
ATOM   5313  CD1 TYR B 189     106.417 146.284 175.489  1.00 11.13           C  
ATOM   5314  CD2 TYR B 189     105.823 144.059 176.061  1.00 11.13           C  
ATOM   5315  CE1 TYR B 189     106.603 146.581 176.822  1.00 11.13           C  
ATOM   5316  CE2 TYR B 189     106.007 144.346 177.394  1.00 11.13           C  
ATOM   5317  CZ  TYR B 189     106.397 145.607 177.771  1.00 11.13           C  
ATOM   5318  OH  TYR B 189     106.578 145.893 179.101  1.00 11.13           O  
ATOM   5319  N   MET B 190     107.615 146.096 171.448  1.00 11.02           N  
ATOM   5320  CA  MET B 190     108.357 147.258 170.973  1.00 11.02           C  
ATOM   5321  C   MET B 190     107.409 148.419 170.709  1.00 11.02           C  
ATOM   5322  O   MET B 190     106.320 148.223 170.165  1.00 11.02           O  
ATOM   5323  CB  MET B 190     109.120 146.980 169.664  1.00 11.02           C  
ATOM   5324  CG  MET B 190     109.805 145.644 169.537  1.00 11.02           C  
ATOM   5325  SD  MET B 190     110.623 145.473 167.933  1.00 11.02           S  
ATOM   5326  CE  MET B 190     112.041 146.530 168.156  1.00 11.02           C  
ATOM   5327  N   PHE B 191     107.831 149.629 171.075  1.00 11.06           N  
ATOM   5328  CA  PHE B 191     107.168 150.836 170.598  1.00 11.06           C  
ATOM   5329  C   PHE B 191     108.031 152.060 170.876  1.00 11.06           C  
ATOM   5330  O   PHE B 191     108.867 152.060 171.784  1.00 11.06           O  
ATOM   5331  CB  PHE B 191     105.777 151.028 171.219  1.00 11.06           C  
ATOM   5332  CG  PHE B 191     105.686 150.642 172.662  1.00 11.06           C  
ATOM   5333  CD1 PHE B 191     106.269 151.418 173.643  1.00 11.06           C  
ATOM   5334  CD2 PHE B 191     105.000 149.508 173.038  1.00 11.06           C  
ATOM   5335  CE1 PHE B 191     106.174 151.062 174.968  1.00 11.06           C  
ATOM   5336  CE2 PHE B 191     104.904 149.151 174.360  1.00 11.06           C  
ATOM   5337  CZ  PHE B 191     105.492 149.930 175.325  1.00 11.06           C  
ATOM   5338  N   VAL B 192     107.806 153.103 170.073  1.00 13.03           N  
ATOM   5339  CA  VAL B 192     108.515 154.369 170.232  1.00 13.03           C  
ATOM   5340  C   VAL B 192     107.940 155.167 171.397  1.00 13.03           C  
ATOM   5341  O   VAL B 192     108.685 155.768 172.177  1.00 13.03           O  
ATOM   5342  CB  VAL B 192     108.461 155.169 168.915  1.00 13.03           C  
ATOM   5343  CG1 VAL B 192     108.953 156.588 169.126  1.00 13.03           C  
ATOM   5344  CG2 VAL B 192     109.276 154.487 167.821  1.00 13.03           C  
ATOM   5345  N   THR B 193     106.615 155.189 171.528  1.00 15.74           N  
ATOM   5346  CA  THR B 193     105.918 155.910 172.585  1.00 15.74           C  
ATOM   5347  C   THR B 193     104.925 154.972 173.261  1.00 15.74           C  
ATOM   5348  O   THR B 193     104.267 154.168 172.596  1.00 15.74           O  
ATOM   5349  CB  THR B 193     105.193 157.149 172.033  1.00 15.74           C  
ATOM   5350  OG1 THR B 193     106.152 158.089 171.533  1.00 15.74           O  
ATOM   5351  CG2 THR B 193     104.374 157.810 173.107  1.00 15.74           C  
ATOM   5352  N   GLY B 194     104.816 155.087 174.583  1.00 19.69           N  
ATOM   5353  CA  GLY B 194     104.121 154.112 175.391  1.00 19.69           C  
ATOM   5354  C   GLY B 194     102.666 154.425 175.686  1.00 19.69           C  
ATOM   5355  O   GLY B 194     102.144 155.489 175.347  1.00 19.69           O  
ATOM   5356  N   PRO B 195     101.989 153.484 176.356  1.00 24.37           N  
ATOM   5357  CA  PRO B 195     100.533 153.613 176.546  1.00 24.37           C  
ATOM   5358  C   PRO B 195     100.089 154.868 177.281  1.00 24.37           C  
ATOM   5359  O   PRO B 195      99.070 155.456 176.907  1.00 24.37           O  
ATOM   5360  CB  PRO B 195     100.179 152.347 177.339  1.00 24.37           C  
ATOM   5361  CG  PRO B 195     101.252 151.391 177.051  1.00 24.37           C  
ATOM   5362  CD  PRO B 195     102.492 152.178 176.810  1.00 24.37           C  
ATOM   5363  N   ASP B 196     100.791 155.279 178.337  1.00 30.50           N  
ATOM   5364  CA  ASP B 196     100.328 156.418 179.129  1.00 30.50           C  
ATOM   5365  C   ASP B 196     100.278 157.694 178.291  1.00 30.50           C  
ATOM   5366  O   ASP B 196      99.283 158.431 178.314  1.00 30.50           O  
ATOM   5367  CB  ASP B 196     101.232 156.599 180.348  1.00 30.50           C  
ATOM   5368  CG  ASP B 196     101.304 155.354 181.208  1.00 30.50           C  
ATOM   5369  OD1 ASP B 196     100.256 154.934 181.742  1.00 30.50           O  
ATOM   5370  OD2 ASP B 196     102.409 154.792 181.349  1.00 30.50           O  
ATOM   5371  N   VAL B 197     101.350 157.977 177.551  1.00 28.64           N  
ATOM   5372  CA  VAL B 197     101.358 159.137 176.664  1.00 28.64           C  
ATOM   5373  C   VAL B 197     100.273 159.004 175.603  1.00 28.64           C  
ATOM   5374  O   VAL B 197      99.608 159.986 175.241  1.00 28.64           O  
ATOM   5375  CB  VAL B 197     102.747 159.312 176.023  1.00 28.64           C  
ATOM   5376  CG1 VAL B 197     102.713 160.424 175.001  1.00 28.64           C  
ATOM   5377  CG2 VAL B 197     103.794 159.594 177.076  1.00 28.64           C  
ATOM   5378  N   VAL B 198     100.094 157.794 175.074  1.00 27.82           N  
ATOM   5379  CA  VAL B 198      99.073 157.565 174.057  1.00 27.82           C  
ATOM   5380  C   VAL B 198      97.699 157.930 174.602  1.00 27.82           C  
ATOM   5381  O   VAL B 198      96.879 158.540 173.908  1.00 27.82           O  
ATOM   5382  CB  VAL B 198      99.131 156.104 173.570  1.00 27.82           C  
ATOM   5383  CG1 VAL B 198      97.854 155.718 172.854  1.00 27.82           C  
ATOM   5384  CG2 VAL B 198     100.350 155.876 172.673  1.00 27.82           C  
ATOM   5385  N   LYS B 199      97.433 157.576 175.859  1.00 33.43           N  
ATOM   5386  CA  LYS B 199      96.182 157.966 176.501  1.00 33.43           C  
ATOM   5387  C   LYS B 199      96.087 159.480 176.625  1.00 33.43           C  
ATOM   5388  O   LYS B 199      95.088 160.088 176.226  1.00 33.43           O  
ATOM   5389  CB  LYS B 199      96.076 157.305 177.878  1.00 33.43           C  
ATOM   5390  CG  LYS B 199      94.908 157.779 178.741  1.00 33.43           C  
ATOM   5391  CD  LYS B 199      93.583 157.266 178.227  1.00 33.43           C  
ATOM   5392  CE  LYS B 199      92.457 157.543 179.213  1.00 33.43           C  
ATOM   5393  NZ  LYS B 199      92.742 156.994 180.565  1.00 33.43           N  
ATOM   5394  N   THR B 200      97.124 160.104 177.182  1.00 34.89           N  
ATOM   5395  CA  THR B 200      97.074 161.543 177.418  1.00 34.89           C  
ATOM   5396  C   THR B 200      96.820 162.326 176.137  1.00 34.89           C  
ATOM   5397  O   THR B 200      96.146 163.361 176.171  1.00 34.89           O  
ATOM   5398  CB  THR B 200      98.372 162.020 178.066  1.00 34.89           C  
ATOM   5399  OG1 THR B 200      99.486 161.649 177.246  1.00 34.89           O  
ATOM   5400  CG2 THR B 200      98.535 161.415 179.444  1.00 34.89           C  
ATOM   5401  N   VAL B 201      97.337 161.859 175.005  1.00 34.38           N  
ATOM   5402  CA  VAL B 201      97.311 162.635 173.770  1.00 34.38           C  
ATOM   5403  C   VAL B 201      96.135 162.255 172.877  1.00 34.38           C  
ATOM   5404  O   VAL B 201      95.506 163.129 172.280  1.00 34.38           O  
ATOM   5405  CB  VAL B 201      98.649 162.483 173.017  1.00 34.38           C  
ATOM   5406  CG1 VAL B 201      98.599 163.235 171.702  1.00 34.38           C  
ATOM   5407  CG2 VAL B 201      99.792 162.994 173.868  1.00 34.38           C  
ATOM   5408  N   THR B 202      95.819 160.967 172.766  1.00 35.10           N  
ATOM   5409  CA  THR B 202      94.818 160.497 171.821  1.00 35.10           C  
ATOM   5410  C   THR B 202      93.545 159.984 172.479  1.00 35.10           C  
ATOM   5411  O   THR B 202      92.577 159.699 171.766  1.00 35.10           O  
ATOM   5412  CB  THR B 202      95.403 159.380 170.944  1.00 35.10           C  
ATOM   5413  OG1 THR B 202      95.633 158.213 171.739  1.00 35.10           O  
ATOM   5414  CG2 THR B 202      96.713 159.823 170.311  1.00 35.10           C  
ATOM   5415  N   ASN B 203      93.517 159.854 173.803  1.00 37.64           N  
ATOM   5416  CA  ASN B 203      92.387 159.331 174.565  1.00 37.64           C  
ATOM   5417  C   ASN B 203      92.143 157.848 174.323  1.00 37.64           C  
ATOM   5418  O   ASN B 203      91.080 157.337 174.692  1.00 37.64           O  
ATOM   5419  CB  ASN B 203      91.097 160.104 174.268  1.00 37.64           C  
ATOM   5420  CG  ASN B 203      91.244 161.591 174.499  1.00 37.64           C  
ATOM   5421  OD1 ASN B 203      91.094 162.393 173.578  1.00 37.64           O  
ATOM   5422  ND2 ASN B 203      91.537 161.970 175.736  1.00 37.64           N  
ATOM   5423  N   GLU B 204      93.092 157.139 173.719  1.00 32.22           N  
ATOM   5424  CA  GLU B 204      92.941 155.724 173.417  1.00 32.22           C  
ATOM   5425  C   GLU B 204      93.591 154.898 174.522  1.00 32.22           C  
ATOM   5426  O   GLU B 204      94.713 155.194 174.945  1.00 32.22           O  
ATOM   5427  CB  GLU B 204      93.557 155.396 172.054  1.00 32.22           C  
ATOM   5428  CG  GLU B 204      93.274 153.994 171.567  1.00 32.22           C  
ATOM   5429  CD  GLU B 204      93.789 153.740 170.160  1.00 32.22           C  
ATOM   5430  OE1 GLU B 204      94.396 154.657 169.566  1.00 32.22           O  
ATOM   5431  OE2 GLU B 204      93.580 152.622 169.646  1.00 32.22           O  
ATOM   5432  N   VAL B 205      92.875 153.883 174.997  1.00 27.73           N  
ATOM   5433  CA  VAL B 205      93.361 152.977 176.033  1.00 27.73           C  
ATOM   5434  C   VAL B 205      93.885 151.717 175.356  1.00 27.73           C  
ATOM   5435  O   VAL B 205      93.154 151.052 174.614  1.00 27.73           O  
ATOM   5436  CB  VAL B 205      92.257 152.639 177.049  1.00 27.73           C  
ATOM   5437  CG1 VAL B 205      92.778 151.689 178.117  1.00 27.73           C  
ATOM   5438  CG2 VAL B 205      91.719 153.902 177.680  1.00 27.73           C  
ATOM   5439  N   VAL B 206      95.148 151.390 175.616  1.00 21.86           N  
ATOM   5440  CA  VAL B 206      95.798 150.227 175.019  1.00 21.86           C  
ATOM   5441  C   VAL B 206      96.810 149.660 176.002  1.00 21.86           C  
ATOM   5442  O   VAL B 206      97.445 150.397 176.761  1.00 21.86           O  
ATOM   5443  CB  VAL B 206      96.482 150.578 173.680  1.00 21.86           C  
ATOM   5444  CG1 VAL B 206      95.458 150.864 172.615  1.00 21.86           C  
ATOM   5445  CG2 VAL B 206      97.398 151.770 173.855  1.00 21.86           C  
ATOM   5446  N   THR B 207      96.952 148.341 175.978  1.00 16.97           N  
ATOM   5447  CA  THR B 207      97.999 147.634 176.695  1.00 16.97           C  
ATOM   5448  C   THR B 207      99.235 147.490 175.811  1.00 16.97           C  
ATOM   5449  O   THR B 207      99.180 147.654 174.591  1.00 16.97           O  
ATOM   5450  CB  THR B 207      97.514 146.253 177.137  1.00 16.97           C  
ATOM   5451  OG1 THR B 207      97.267 145.444 175.984  1.00 16.97           O  
ATOM   5452  CG2 THR B 207      96.243 146.357 177.972  1.00 16.97           C  
ATOM   5453  N   ALA B 208     100.361 147.178 176.453  1.00 14.58           N  
ATOM   5454  CA  ALA B 208     101.619 147.039 175.728  1.00 14.58           C  
ATOM   5455  C   ALA B 208     101.532 145.955 174.659  1.00 14.58           C  
ATOM   5456  O   ALA B 208     102.075 146.116 173.562  1.00 14.58           O  
ATOM   5457  CB  ALA B 208     102.749 146.739 176.709  1.00 14.58           C  
ATOM   5458  N   GLU B 209     100.859 144.842 174.963  1.00 15.53           N  
ATOM   5459  CA  GLU B 209     100.716 143.762 173.989  1.00 15.53           C  
ATOM   5460  C   GLU B 209      99.893 144.211 172.788  1.00 15.53           C  
ATOM   5461  O   GLU B 209     100.233 143.898 171.642  1.00 15.53           O  
ATOM   5462  CB  GLU B 209     100.082 142.542 174.664  1.00 15.53           C  
ATOM   5463  CG  GLU B 209      99.887 141.318 173.774  1.00 15.53           C  
ATOM   5464  CD  GLU B 209     101.181 140.585 173.466  1.00 15.53           C  
ATOM   5465  OE1 GLU B 209     102.063 140.517 174.348  1.00 15.53           O  
ATOM   5466  OE2 GLU B 209     101.309 140.066 172.339  1.00 15.53           O  
ATOM   5467  N   GLU B 210      98.808 144.948 173.033  1.00 16.41           N  
ATOM   5468  CA  GLU B 210      97.989 145.460 171.938  1.00 16.41           C  
ATOM   5469  C   GLU B 210      98.739 146.506 171.122  1.00 16.41           C  
ATOM   5470  O   GLU B 210      98.582 146.575 169.899  1.00 16.41           O  
ATOM   5471  CB  GLU B 210      96.688 146.047 172.488  1.00 16.41           C  
ATOM   5472  CG  GLU B 210      95.807 145.049 173.220  1.00 16.41           C  
ATOM   5473  CD  GLU B 210      94.588 145.690 173.862  1.00 16.41           C  
ATOM   5474  OE1 GLU B 210      93.486 145.116 173.745  1.00 16.41           O  
ATOM   5475  OE2 GLU B 210      94.729 146.763 174.486  1.00 16.41           O  
ATOM   5476  N   LEU B 211      99.559 147.326 171.780  1.00 12.20           N  
ATOM   5477  CA  LEU B 211     100.243 148.416 171.090  1.00 12.20           C  
ATOM   5478  C   LEU B 211     101.430 147.919 170.268  1.00 12.20           C  
ATOM   5479  O   LEU B 211     101.610 148.336 169.120  1.00 12.20           O  
ATOM   5480  CB  LEU B 211     100.691 149.476 172.104  1.00 12.20           C  
ATOM   5481  CG  LEU B 211     101.363 150.745 171.564  1.00 12.20           C  
ATOM   5482  CD1 LEU B 211     100.487 151.454 170.550  1.00 12.20           C  
ATOM   5483  CD2 LEU B 211     101.739 151.699 172.688  1.00 12.20           C  
ATOM   5484  N   GLY B 212     102.260 147.044 170.840  1.00  9.41           N  
ATOM   5485  CA  GLY B 212     103.475 146.601 170.179  1.00  9.41           C  
ATOM   5486  C   GLY B 212     103.884 145.147 170.346  1.00  9.41           C  
ATOM   5487  O   GLY B 212     105.072 144.835 170.249  1.00  9.41           O  
ATOM   5488  N   GLY B 213     102.937 144.250 170.598  1.00  8.90           N  
ATOM   5489  CA  GLY B 213     103.251 142.847 170.772  1.00  8.90           C  
ATOM   5490  C   GLY B 213     103.755 142.184 169.496  1.00  8.90           C  
ATOM   5491  O   GLY B 213     103.845 142.785 168.425  1.00  8.90           O  
ATOM   5492  N   ALA B 214     104.084 140.896 169.630  1.00  9.29           N  
ATOM   5493  CA  ALA B 214     104.669 140.143 168.522  1.00  9.29           C  
ATOM   5494  C   ALA B 214     103.686 139.966 167.367  1.00  9.29           C  
ATOM   5495  O   ALA B 214     104.082 140.028 166.200  1.00  9.29           O  
ATOM   5496  CB  ALA B 214     105.160 138.785 169.017  1.00  9.29           C  
ATOM   5497  N   LYS B 215     102.407 139.725 167.665  1.00 10.56           N  
ATOM   5498  CA  LYS B 215     101.414 139.576 166.603  1.00 10.56           C  
ATOM   5499  C   LYS B 215     101.354 140.828 165.731  1.00 10.56           C  
ATOM   5500  O   LYS B 215     101.366 140.745 164.495  1.00 10.56           O  
ATOM   5501  CB  LYS B 215     100.045 139.264 167.213  1.00 10.56           C  
ATOM   5502  CG  LYS B 215      99.011 138.755 166.225  1.00 10.56           C  
ATOM   5503  CD  LYS B 215      97.772 138.233 166.938  1.00 10.56           C  
ATOM   5504  CE  LYS B 215      96.566 138.190 166.019  1.00 10.56           C  
ATOM   5505  NZ  LYS B 215      96.838 137.434 164.771  1.00 10.56           N  
ATOM   5506  N   VAL B 216     101.319 142.000 166.369  1.00  8.94           N  
ATOM   5507  CA  VAL B 216     101.292 143.271 165.651  1.00  8.94           C  
ATOM   5508  C   VAL B 216     102.480 143.385 164.700  1.00  8.94           C  
ATOM   5509  O   VAL B 216     102.316 143.671 163.510  1.00  8.94           O  
ATOM   5510  CB  VAL B 216     101.254 144.441 166.653  1.00  8.94           C  
ATOM   5511  CG1 VAL B 216     101.622 145.740 165.984  1.00  8.94           C  
ATOM   5512  CG2 VAL B 216      99.881 144.567 167.286  1.00  8.94           C  
ATOM   5513  N   HIS B 217     103.696 143.177 165.211  1.00  7.63           N  
ATOM   5514  CA  HIS B 217     104.897 143.444 164.429  1.00  7.63           C  
ATOM   5515  C   HIS B 217     105.267 142.317 163.474  1.00  7.63           C  
ATOM   5516  O   HIS B 217     106.127 142.522 162.612  1.00  7.63           O  
ATOM   5517  CB  HIS B 217     106.082 143.734 165.354  1.00  7.63           C  
ATOM   5518  CG  HIS B 217     105.961 145.018 166.108  1.00  7.63           C  
ATOM   5519  ND1 HIS B 217     105.680 146.222 165.499  1.00  7.63           N  
ATOM   5520  CD2 HIS B 217     106.095 145.288 167.426  1.00  7.63           C  
ATOM   5521  CE1 HIS B 217     105.640 147.175 166.410  1.00  7.63           C  
ATOM   5522  NE2 HIS B 217     105.888 146.635 167.588  1.00  7.63           N  
ATOM   5523  N   THR B 218     104.654 141.144 163.601  1.00  8.48           N  
ATOM   5524  CA  THR B 218     104.875 140.049 162.670  1.00  8.48           C  
ATOM   5525  C   THR B 218     103.770 139.898 161.632  1.00  8.48           C  
ATOM   5526  O   THR B 218     103.961 139.157 160.664  1.00  8.48           O  
ATOM   5527  CB  THR B 218     105.029 138.724 163.429  1.00  8.48           C  
ATOM   5528  OG1 THR B 218     103.915 138.534 164.307  1.00  8.48           O  
ATOM   5529  CG2 THR B 218     106.329 138.693 164.210  1.00  8.48           C  
ATOM   5530  N   SER B 219     102.627 140.568 161.796  1.00 10.41           N  
ATOM   5531  CA  SER B 219     101.545 140.444 160.830  1.00 10.41           C  
ATOM   5532  C   SER B 219     101.045 141.755 160.240  1.00 10.41           C  
ATOM   5533  O   SER B 219     100.423 141.720 159.174  1.00 10.41           O  
ATOM   5534  CB  SER B 219     100.350 139.716 161.461  1.00 10.41           C  
ATOM   5535  OG  SER B 219      99.574 140.601 162.240  1.00 10.41           O  
ATOM   5536  N   LYS B 220     101.294 142.898 160.877  1.00 11.30           N  
ATOM   5537  CA  LYS B 220     100.702 144.163 160.457  1.00 11.30           C  
ATOM   5538  C   LYS B 220     101.721 145.227 160.074  1.00 11.30           C  
ATOM   5539  O   LYS B 220     101.572 145.861 159.025  1.00 11.30           O  
ATOM   5540  CB  LYS B 220      99.791 144.696 161.574  1.00 11.30           C  
ATOM   5541  CG  LYS B 220      98.539 143.874 161.793  1.00 11.30           C  
ATOM   5542  CD  LYS B 220      97.985 144.056 163.197  1.00 11.30           C  
ATOM   5543  CE  LYS B 220      97.496 145.472 163.436  1.00 11.30           C  
ATOM   5544  NZ  LYS B 220      96.198 145.725 162.765  1.00 11.30           N  
ATOM   5545  N   SER B 221     102.751 145.450 160.889  1.00  9.21           N  
ATOM   5546  CA  SER B 221     103.552 146.665 160.792  1.00  9.21           C  
ATOM   5547  C   SER B 221     104.799 146.537 159.921  1.00  9.21           C  
ATOM   5548  O   SER B 221     105.415 147.563 159.614  1.00  9.21           O  
ATOM   5549  CB  SER B 221     103.969 147.128 162.191  1.00  9.21           C  
ATOM   5550  OG  SER B 221     104.788 146.171 162.822  1.00  9.21           O  
ATOM   5551  N   SER B 222     105.185 145.329 159.513  1.00  9.16           N  
ATOM   5552  CA  SER B 222     106.372 145.047 158.692  1.00  9.16           C  
ATOM   5553  C   SER B 222     107.681 145.006 159.476  1.00  9.16           C  
ATOM   5554  O   SER B 222     108.744 144.869 158.856  1.00  9.16           O  
ATOM   5555  CB  SER B 222     106.556 146.073 157.571  1.00  9.16           C  
ATOM   5556  OG  SER B 222     107.208 147.220 158.069  1.00  9.16           O  
ATOM   5557  N   ILE B 223     107.654 145.112 160.804  1.00  8.39           N  
ATOM   5558  CA  ILE B 223     108.883 145.350 161.560  1.00  8.39           C  
ATOM   5559  C   ILE B 223     109.683 144.062 161.753  1.00  8.39           C  
ATOM   5560  O   ILE B 223     110.889 144.028 161.486  1.00  8.39           O  
ATOM   5561  CB  ILE B 223     108.555 146.033 162.905  1.00  8.39           C  
ATOM   5562  CG1 ILE B 223     107.929 147.418 162.675  1.00  8.39           C  
ATOM   5563  CG2 ILE B 223     109.796 146.168 163.766  1.00  8.39           C  
ATOM   5564  CD1 ILE B 223     108.779 148.388 161.894  1.00  8.39           C  
ATOM   5565  N   ALA B 224     109.048 142.994 162.230  1.00  7.01           N  
ATOM   5566  CA  ALA B 224     109.760 141.798 162.667  1.00  7.01           C  
ATOM   5567  C   ALA B 224     109.774 140.693 161.611  1.00  7.01           C  
ATOM   5568  O   ALA B 224     108.851 140.558 160.807  1.00  7.01           O  
ATOM   5569  CB  ALA B 224     109.152 141.250 163.960  1.00  7.01           C  
ATOM   5570  N   ASP B 225     110.839 139.885 161.644  1.00  7.69           N  
ATOM   5571  CA  ASP B 225     111.052 138.796 160.696  1.00  7.69           C  
ATOM   5572  C   ASP B 225     110.496 137.458 161.166  1.00  7.69           C  
ATOM   5573  O   ASP B 225     110.356 136.545 160.346  1.00  7.69           O  
ATOM   5574  CB  ASP B 225     112.545 138.642 160.402  1.00  7.69           C  
ATOM   5575  CG  ASP B 225     113.129 139.861 159.723  1.00  7.69           C  
ATOM   5576  OD1 ASP B 225     113.447 140.844 160.423  1.00  7.69           O  
ATOM   5577  OD2 ASP B 225     113.255 139.841 158.482  1.00  7.69           O  
ATOM   5578  N   GLY B 226     110.200 137.313 162.451  1.00  7.21           N  
ATOM   5579  CA  GLY B 226     109.510 136.132 162.936  1.00  7.21           C  
ATOM   5580  C   GLY B 226     109.385 136.162 164.445  1.00  7.21           C  
ATOM   5581  O   GLY B 226     110.020 136.968 165.132  1.00  7.21           O  
ATOM   5582  N   SER B 227     108.538 135.265 164.950  1.00  7.97           N  
ATOM   5583  CA  SER B 227     108.317 135.087 166.379  1.00  7.97           C  
ATOM   5584  C   SER B 227     108.428 133.616 166.754  1.00  7.97           C  
ATOM   5585  O   SER B 227     108.185 132.728 165.934  1.00  7.97           O  
ATOM   5586  CB  SER B 227     106.948 135.618 166.818  1.00  7.97           C  
ATOM   5587  OG  SER B 227     105.909 135.101 166.013  1.00  7.97           O  
ATOM   5588  N   PHE B 228     108.788 133.372 168.013  1.00  8.45           N  
ATOM   5589  CA  PHE B 228     108.997 132.034 168.544  1.00  8.45           C  
ATOM   5590  C   PHE B 228     108.257 131.876 169.870  1.00  8.45           C  
ATOM   5591  O   PHE B 228     107.864 132.854 170.507  1.00  8.45           O  
ATOM   5592  CB  PHE B 228     110.490 131.747 168.722  1.00  8.45           C  
ATOM   5593  CG  PHE B 228     111.285 131.884 167.461  1.00  8.45           C  
ATOM   5594  CD1 PHE B 228     111.146 130.969 166.439  1.00  8.45           C  
ATOM   5595  CD2 PHE B 228     112.167 132.928 167.294  1.00  8.45           C  
ATOM   5596  CE1 PHE B 228     111.874 131.093 165.283  1.00  8.45           C  
ATOM   5597  CE2 PHE B 228     112.895 133.052 166.137  1.00  8.45           C  
ATOM   5598  CZ  PHE B 228     112.745 132.135 165.133  1.00  8.45           C  
ATOM   5599  N   GLU B 229     108.081 130.618 170.282  1.00 15.13           N  
ATOM   5600  CA  GLU B 229     107.208 130.314 171.416  1.00 15.13           C  
ATOM   5601  C   GLU B 229     107.841 130.705 172.750  1.00 15.13           C  
ATOM   5602  O   GLU B 229     107.136 131.142 173.665  1.00 15.13           O  
ATOM   5603  CB  GLU B 229     106.842 128.830 171.410  1.00 15.13           C  
ATOM   5604  CG  GLU B 229     105.815 128.421 172.456  1.00 15.13           C  
ATOM   5605  CD  GLU B 229     104.407 128.876 172.123  1.00 15.13           C  
ATOM   5606  OE1 GLU B 229     104.138 129.190 170.946  1.00 15.13           O  
ATOM   5607  OE2 GLU B 229     103.564 128.916 173.043  1.00 15.13           O  
ATOM   5608  N   ASN B 230     109.154 130.546 172.892  1.00 11.54           N  
ATOM   5609  CA  ASN B 230     109.829 130.899 174.137  1.00 11.54           C  
ATOM   5610  C   ASN B 230     111.308 131.157 173.856  1.00 11.54           C  
ATOM   5611  O   ASN B 230     111.767 131.085 172.714  1.00 11.54           O  
ATOM   5612  CB  ASN B 230     109.632 129.813 175.196  1.00 11.54           C  
ATOM   5613  CG  ASN B 230     110.222 128.486 174.793  1.00 11.54           C  
ATOM   5614  OD1 ASN B 230     111.387 128.392 174.421  1.00 11.54           O  
ATOM   5615  ND2 ASN B 230     109.413 127.446 174.870  1.00 11.54           N  
ATOM   5616  N   ASP B 231     112.051 131.458 174.927  1.00 12.15           N  
ATOM   5617  CA  ASP B 231     113.437 131.906 174.793  1.00 12.15           C  
ATOM   5618  C   ASP B 231     114.327 130.816 174.197  1.00 12.15           C  
ATOM   5619  O   ASP B 231     115.150 131.086 173.310  1.00 12.15           O  
ATOM   5620  CB  ASP B 231     113.969 132.346 176.163  1.00 12.15           C  
ATOM   5621  CG  ASP B 231     113.395 133.678 176.622  1.00 12.15           C  
ATOM   5622  OD1 ASP B 231     112.462 134.195 175.973  1.00 12.15           O  
ATOM   5623  OD2 ASP B 231     113.885 134.213 177.636  1.00 12.15           O  
ATOM   5624  N   VAL B 232     114.173 129.580 174.673  1.00 10.81           N  
ATOM   5625  CA  VAL B 232     115.051 128.483 174.264  1.00 10.81           C  
ATOM   5626  C   VAL B 232     114.883 128.183 172.774  1.00 10.81           C  
ATOM   5627  O   VAL B 232     115.867 128.074 172.025  1.00 10.81           O  
ATOM   5628  CB  VAL B 232     114.776 127.242 175.139  1.00 10.81           C  
ATOM   5629  CG1 VAL B 232     115.438 125.999 174.567  1.00 10.81           C  
ATOM   5630  CG2 VAL B 232     115.229 127.484 176.578  1.00 10.81           C  
ATOM   5631  N   GLU B 233     113.634 128.029 172.329  1.00 12.28           N  
ATOM   5632  CA  GLU B 233     113.351 127.809 170.912  1.00 12.28           C  
ATOM   5633  C   GLU B 233     113.988 128.899 170.056  1.00 12.28           C  
ATOM   5634  O   GLU B 233     114.643 128.617 169.042  1.00 12.28           O  
ATOM   5635  CB  GLU B 233     111.833 127.749 170.699  1.00 12.28           C  
ATOM   5636  CG  GLU B 233     111.379 127.628 169.247  1.00 12.28           C  
ATOM   5637  CD  GLU B 233     109.870 127.525 169.104  1.00 12.28           C  
ATOM   5638  OE1 GLU B 233     109.289 126.527 169.579  1.00 12.28           O  
ATOM   5639  OE2 GLU B 233     109.261 128.442 168.515  1.00 12.28           O  
ATOM   5640  N   ALA B 234     113.808 130.156 170.466  1.00  8.59           N  
ATOM   5641  CA  ALA B 234     114.348 131.286 169.717  1.00  8.59           C  
ATOM   5642  C   ALA B 234     115.863 131.193 169.576  1.00  8.59           C  
ATOM   5643  O   ALA B 234     116.406 131.348 168.476  1.00  8.59           O  
ATOM   5644  CB  ALA B 234     113.949 132.599 170.394  1.00  8.59           C  
ATOM   5645  N   ILE B 235     116.570 130.968 170.685  1.00  8.20           N  
ATOM   5646  CA  ILE B 235     118.030 130.973 170.628  1.00  8.20           C  
ATOM   5647  C   ILE B 235     118.542 129.819 169.763  1.00  8.20           C  
ATOM   5648  O   ILE B 235     119.495 129.977 168.977  1.00  8.20           O  
ATOM   5649  CB  ILE B 235     118.608 130.947 172.056  1.00  8.20           C  
ATOM   5650  CG1 ILE B 235     118.318 132.288 172.749  1.00  8.20           C  
ATOM   5651  CG2 ILE B 235     120.096 130.655 172.023  1.00  8.20           C  
ATOM   5652  CD1 ILE B 235     118.668 132.345 174.199  1.00  8.20           C  
ATOM   5653  N   LEU B 236     117.905 128.649 169.865  1.00  8.52           N  
ATOM   5654  CA  LEU B 236     118.308 127.531 169.015  1.00  8.52           C  
ATOM   5655  C   LEU B 236     118.108 127.872 167.535  1.00  8.52           C  
ATOM   5656  O   LEU B 236     118.972 127.581 166.691  1.00  8.52           O  
ATOM   5657  CB  LEU B 236     117.532 126.271 169.414  1.00  8.52           C  
ATOM   5658  CG  LEU B 236     117.830 125.688 170.808  1.00  8.52           C  
ATOM   5659  CD1 LEU B 236     117.011 124.433 171.093  1.00  8.52           C  
ATOM   5660  CD2 LEU B 236     119.311 125.405 170.999  1.00  8.52           C  
ATOM   5661  N   GLN B 237     116.993 128.532 167.205  1.00  8.93           N  
ATOM   5662  CA  GLN B 237     116.772 128.951 165.823  1.00  8.93           C  
ATOM   5663  C   GLN B 237     117.792 129.994 165.366  1.00  8.93           C  
ATOM   5664  O   GLN B 237     118.142 130.032 164.184  1.00  8.93           O  
ATOM   5665  CB  GLN B 237     115.347 129.476 165.647  1.00  8.93           C  
ATOM   5666  CG  GLN B 237     114.277 128.389 165.657  1.00  8.93           C  
ATOM   5667  CD  GLN B 237     114.351 127.483 164.446  1.00  8.93           C  
ATOM   5668  OE1 GLN B 237     114.061 127.895 163.328  1.00  8.93           O  
ATOM   5669  NE2 GLN B 237     114.750 126.245 164.665  1.00  8.93           N  
ATOM   5670  N   ILE B 238     118.280 130.846 166.270  1.00 12.77           N  
ATOM   5671  CA  ILE B 238     119.317 131.803 165.878  1.00 12.77           C  
ATOM   5672  C   ILE B 238     120.600 131.068 165.501  1.00 12.77           C  
ATOM   5673  O   ILE B 238     121.281 131.433 164.533  1.00 12.77           O  
ATOM   5674  CB  ILE B 238     119.563 132.839 166.991  1.00 12.77           C  
ATOM   5675  CG1 ILE B 238     118.310 133.678 167.268  1.00 12.77           C  
ATOM   5676  CG2 ILE B 238     120.735 133.741 166.632  1.00 12.77           C  
ATOM   5677  CD1 ILE B 238     117.784 134.489 166.103  1.00 12.77           C  
ATOM   5678  N   ARG B 239     120.947 130.020 166.250  1.00  8.11           N  
ATOM   5679  CA  ARG B 239     122.090 129.189 165.853  1.00  8.11           C  
ATOM   5680  C   ARG B 239     121.875 128.604 164.452  1.00  8.11           C  
ATOM   5681  O   ARG B 239     122.762 128.664 163.577  1.00  8.11           O  
ATOM   5682  CB  ARG B 239     122.317 128.069 166.876  1.00  8.11           C  
ATOM   5683  CG  ARG B 239     122.971 128.502 168.192  1.00  8.11           C  
ATOM   5684  CD  ARG B 239     123.098 127.364 169.208  1.00  8.11           C  
ATOM   5685  NE  ARG B 239     123.930 126.259 168.739  1.00  8.11           N  
ATOM   5686  CZ  ARG B 239     125.246 126.163 168.918  1.00  8.11           C  
ATOM   5687  NH1 ARG B 239     125.923 127.104 169.558  1.00  8.11           N  
ATOM   5688  NH2 ARG B 239     125.895 125.110 168.446  1.00  8.11           N  
ATOM   5689  N   ARG B 240     120.686 128.043 164.226  1.00 12.01           N  
ATOM   5690  CA  ARG B 240     120.348 127.507 162.908  1.00 12.01           C  
ATOM   5691  C   ARG B 240     120.539 128.558 161.816  1.00 12.01           C  
ATOM   5692  O   ARG B 240     121.109 128.275 160.758  1.00 12.01           O  
ATOM   5693  CB  ARG B 240     118.912 126.979 162.917  1.00 12.01           C  
ATOM   5694  CG  ARG B 240     118.468 126.243 161.659  1.00 12.01           C  
ATOM   5695  CD  ARG B 240     116.969 125.978 161.674  1.00 12.01           C  
ATOM   5696  NE  ARG B 240     116.472 125.487 160.392  1.00 12.01           N  
ATOM   5697  CZ  ARG B 240     115.213 125.591 159.978  1.00 12.01           C  
ATOM   5698  NH1 ARG B 240     114.292 126.164 160.737  1.00 12.01           N  
ATOM   5699  NH2 ARG B 240     114.874 125.115 158.789  1.00 12.01           N  
ATOM   5700  N   LEU B 241     120.076 129.784 162.064  1.00 12.77           N  
ATOM   5701  CA  LEU B 241     120.207 130.843 161.068  1.00 12.77           C  
ATOM   5702  C   LEU B 241     121.671 131.136 160.784  1.00 12.77           C  
ATOM   5703  O   LEU B 241     122.081 131.240 159.624  1.00 12.77           O  
ATOM   5704  CB  LEU B 241     119.494 132.114 161.534  1.00 12.77           C  
ATOM   5705  CG  LEU B 241     119.537 133.325 160.590  1.00 12.77           C  
ATOM   5706  CD1 LEU B 241     119.102 132.976 159.174  1.00 12.77           C  
ATOM   5707  CD2 LEU B 241     118.709 134.471 161.133  1.00 12.77           C  
ATOM   5708  N   LEU B 242     122.479 131.268 161.839  1.00  8.87           N  
ATOM   5709  CA  LEU B 242     123.873 131.638 161.634  1.00  8.87           C  
ATOM   5710  C   LEU B 242     124.589 130.597 160.791  1.00  8.87           C  
ATOM   5711  O   LEU B 242     125.537 130.930 160.072  1.00  8.87           O  
ATOM   5712  CB  LEU B 242     124.588 131.828 162.971  1.00  8.87           C  
ATOM   5713  CG  LEU B 242     124.437 133.187 163.665  1.00  8.87           C  
ATOM   5714  CD1 LEU B 242     124.820 133.048 165.131  1.00  8.87           C  
ATOM   5715  CD2 LEU B 242     125.257 134.290 163.002  1.00  8.87           C  
ATOM   5716  N   ASP B 243     124.134 129.343 160.837  1.00 12.15           N  
ATOM   5717  CA  ASP B 243     124.753 128.333 159.973  1.00 12.15           C  
ATOM   5718  C   ASP B 243     124.464 128.533 158.480  1.00 12.15           C  
ATOM   5719  O   ASP B 243     125.137 127.904 157.659  1.00 12.15           O  
ATOM   5720  CB  ASP B 243     124.319 126.925 160.392  1.00 12.15           C  
ATOM   5721  CG  ASP B 243     124.897 126.508 161.728  1.00 12.15           C  
ATOM   5722  OD1 ASP B 243     126.050 126.881 162.024  1.00 12.15           O  
ATOM   5723  OD2 ASP B 243     124.199 125.792 162.481  1.00 12.15           O  
ATOM   5724  N   PHE B 244     123.504 129.383 158.104  1.00 12.77           N  
ATOM   5725  CA  PHE B 244     123.260 129.701 156.696  1.00 12.77           C  
ATOM   5726  C   PHE B 244     124.091 130.873 156.177  1.00 12.77           C  
ATOM   5727  O   PHE B 244     124.413 130.911 154.985  1.00 12.77           O  
ATOM   5728  CB  PHE B 244     121.785 130.051 156.455  1.00 12.77           C  
ATOM   5729  CG  PHE B 244     120.864 128.866 156.374  1.00 12.77           C  
ATOM   5730  CD1 PHE B 244     120.715 128.168 155.190  1.00 12.77           C  
ATOM   5731  CD2 PHE B 244     120.112 128.477 157.464  1.00 12.77           C  
ATOM   5732  CE1 PHE B 244     119.861 127.097 155.108  1.00 12.77           C  
ATOM   5733  CE2 PHE B 244     119.258 127.402 157.381  1.00 12.77           C  
ATOM   5734  CZ  PHE B 244     119.136 126.714 156.198  1.00 12.77           C  
ATOM   5735  N   LEU B 245     124.416 131.838 157.028  1.00  7.80           N  
ATOM   5736  CA  LEU B 245     124.837 133.177 156.628  1.00  7.80           C  
ATOM   5737  C   LEU B 245     126.354 133.277 156.446  1.00  7.80           C  
ATOM   5738  O   LEU B 245     127.109 132.646 157.186  1.00  7.80           O  
ATOM   5739  CB  LEU B 245     124.399 134.197 157.668  1.00  7.80           C  
ATOM   5740  CG  LEU B 245     122.889 134.345 157.870  1.00  7.80           C  
ATOM   5741  CD1 LEU B 245     122.572 135.421 158.878  1.00  7.80           C  
ATOM   5742  CD2 LEU B 245     122.197 134.626 156.560  1.00  7.80           C  
ATOM   5743  N   PRO B 246     126.808 134.079 155.478  1.00  7.37           N  
ATOM   5744  CA  PRO B 246     128.233 134.424 155.411  1.00  7.37           C  
ATOM   5745  C   PRO B 246     128.682 135.206 156.639  1.00  7.37           C  
ATOM   5746  O   PRO B 246     127.898 135.908 157.279  1.00  7.37           O  
ATOM   5747  CB  PRO B 246     128.338 135.275 154.138  1.00  7.37           C  
ATOM   5748  CG  PRO B 246     127.141 134.953 153.342  1.00  7.37           C  
ATOM   5749  CD  PRO B 246     126.069 134.578 154.307  1.00  7.37           C  
ATOM   5750  N   ALA B 247     129.970 135.066 156.967  1.00  7.54           N  
ATOM   5751  CA  ALA B 247     130.546 135.779 158.104  1.00  7.54           C  
ATOM   5752  C   ALA B 247     130.777 137.254 157.796  1.00  7.54           C  
ATOM   5753  O   ALA B 247     130.795 138.079 158.714  1.00  7.54           O  
ATOM   5754  CB  ALA B 247     131.862 135.129 158.528  1.00  7.54           C  
ATOM   5755  N   ASN B 248     130.984 137.595 156.527  1.00 12.77           N  
ATOM   5756  CA  ASN B 248     131.165 138.971 156.084  1.00 12.77           C  
ATOM   5757  C   ASN B 248     130.918 139.025 154.579  1.00 12.77           C  
ATOM   5758  O   ASN B 248     130.577 138.020 153.951  1.00 12.77           O  
ATOM   5759  CB  ASN B 248     132.560 139.482 156.440  1.00 12.77           C  
ATOM   5760  CG  ASN B 248     133.645 138.624 155.850  1.00 12.77           C  
ATOM   5761  OD1 ASN B 248     133.707 138.433 154.640  1.00 12.77           O  
ATOM   5762  ND2 ASN B 248     134.500 138.089 156.701  1.00 12.77           N  
ATOM   5763  N   ASN B 249     131.098 140.214 154.007  1.00 10.93           N  
ATOM   5764  CA  ASN B 249     130.814 140.497 152.602  1.00 10.93           C  
ATOM   5765  C   ASN B 249     131.938 140.091 151.644  1.00 10.93           C  
ATOM   5766  O   ASN B 249     131.867 140.449 150.465  1.00 10.93           O  
ATOM   5767  CB  ASN B 249     130.509 141.989 152.423  1.00 10.93           C  
ATOM   5768  CG  ASN B 249     131.717 142.875 152.675  1.00 10.93           C  
ATOM   5769  OD1 ASN B 249     132.726 142.433 153.216  1.00 10.93           O  
ATOM   5770  ND2 ASN B 249     131.611 144.133 152.288  1.00 10.93           N  
ATOM   5771  N   ILE B 250     132.977 139.393 152.107  1.00 10.79           N  
ATOM   5772  CA  ILE B 250     134.068 138.943 151.251  1.00 10.79           C  
ATOM   5773  C   ILE B 250     134.165 137.422 151.179  1.00 10.79           C  
ATOM   5774  O   ILE B 250     134.489 136.872 150.122  1.00 10.79           O  
ATOM   5775  CB  ILE B 250     135.416 139.551 151.704  1.00 10.79           C  
ATOM   5776  CG1 ILE B 250     135.443 141.056 151.437  1.00 10.79           C  
ATOM   5777  CG2 ILE B 250     136.586 138.887 150.994  1.00 10.79           C  
ATOM   5778  CD1 ILE B 250     135.315 141.438 149.973  1.00 10.79           C  
ATOM   5779  N   GLU B 251     133.894 136.720 152.278  1.00 14.14           N  
ATOM   5780  CA  GLU B 251     134.255 135.309 152.386  1.00 14.14           C  
ATOM   5781  C   GLU B 251     133.285 134.357 151.685  1.00 14.14           C  
ATOM   5782  O   GLU B 251     133.638 133.191 151.488  1.00 14.14           O  
ATOM   5783  CB  GLU B 251     134.393 134.923 153.863  1.00 14.14           C  
ATOM   5784  CG  GLU B 251     133.122 134.984 154.687  1.00 14.14           C  
ATOM   5785  CD  GLU B 251     132.384 133.657 154.735  1.00 14.14           C  
ATOM   5786  OE1 GLU B 251     132.975 132.621 154.362  1.00 14.14           O  
ATOM   5787  OE2 GLU B 251     131.219 133.643 155.180  1.00 14.14           O  
ATOM   5788  N   GLY B 252     132.091 134.808 151.302  1.00 10.45           N  
ATOM   5789  CA  GLY B 252     131.126 133.958 150.629  1.00 10.45           C  
ATOM   5790  C   GLY B 252     130.341 133.056 151.569  1.00 10.45           C  
ATOM   5791  O   GLY B 252     130.525 133.044 152.784  1.00 10.45           O  
ATOM   5792  N   VAL B 253     129.446 132.272 150.977  1.00  7.31           N  
ATOM   5793  CA  VAL B 253     128.515 131.450 151.748  1.00  7.31           C  
ATOM   5794  C   VAL B 253     129.245 130.250 152.345  1.00  7.31           C  
ATOM   5795  O   VAL B 253     130.191 129.734 151.734  1.00  7.31           O  
ATOM   5796  CB  VAL B 253     127.321 130.992 150.892  1.00  7.31           C  
ATOM   5797  CG1 VAL B 253     126.571 132.183 150.286  1.00  7.31           C  
ATOM   5798  CG2 VAL B 253     127.759 130.020 149.797  1.00  7.31           C  
ATOM   5799  N   PRO B 254     128.839 129.771 153.522  1.00  8.05           N  
ATOM   5800  CA  PRO B 254     129.428 128.541 154.058  1.00  8.05           C  
ATOM   5801  C   PRO B 254     128.969 127.323 153.270  1.00  8.05           C  
ATOM   5802  O   PRO B 254     127.912 127.325 152.638  1.00  8.05           O  
ATOM   5803  CB  PRO B 254     128.916 128.503 155.502  1.00  8.05           C  
ATOM   5804  CG  PRO B 254     127.679 129.285 155.495  1.00  8.05           C  
ATOM   5805  CD  PRO B 254     127.732 130.257 154.361  1.00  8.05           C  
ATOM   5806  N   GLU B 255     129.788 126.275 153.311  1.00 13.32           N  
ATOM   5807  CA  GLU B 255     129.526 125.027 152.608  1.00 13.32           C  
ATOM   5808  C   GLU B 255     129.546 123.855 153.582  1.00 13.32           C  
ATOM   5809  O   GLU B 255     130.402 123.785 154.468  1.00 13.32           O  
ATOM   5810  CB  GLU B 255     130.554 124.805 151.492  1.00 13.32           C  
ATOM   5811  CG  GLU B 255     130.356 123.528 150.690  1.00 13.32           C  
ATOM   5812  CD  GLU B 255     130.832 123.660 149.253  1.00 13.32           C  
ATOM   5813  OE1 GLU B 255     131.893 124.279 149.028  1.00 13.32           O  
ATOM   5814  OE2 GLU B 255     130.143 123.148 148.346  1.00 13.32           O  
ATOM   5815  N   ILE B 256     128.586 122.944 153.418  1.00 11.44           N  
ATOM   5816  CA  ILE B 256     128.519 121.702 154.175  1.00 11.44           C  
ATOM   5817  C   ILE B 256     128.340 120.543 153.195  1.00 11.44           C  
ATOM   5818  O   ILE B 256     128.106 120.738 152.004  1.00 11.44           O  
ATOM   5819  CB  ILE B 256     127.385 121.708 155.223  1.00 11.44           C  
ATOM   5820  CG1 ILE B 256     126.012 121.779 154.547  1.00 11.44           C  
ATOM   5821  CG2 ILE B 256     127.576 122.857 156.207  1.00 11.44           C  
ATOM   5822  CD1 ILE B 256     124.852 121.723 155.507  1.00 11.44           C  
ATOM   5823  N   GLU B 257     128.459 119.326 153.722  1.00 17.52           N  
ATOM   5824  CA  GLU B 257     128.290 118.102 152.945  1.00 17.52           C  
ATOM   5825  C   GLU B 257     126.818 117.700 152.901  1.00 17.52           C  
ATOM   5826  O   GLU B 257     126.178 117.546 153.946  1.00 17.52           O  
ATOM   5827  CB  GLU B 257     129.133 116.977 153.549  1.00 17.52           C  
ATOM   5828  CG  GLU B 257     129.331 115.768 152.653  1.00 17.52           C  
ATOM   5829  CD  GLU B 257     128.095 114.902 152.550  1.00 17.52           C  
ATOM   5830  OE1 GLU B 257     127.929 114.225 151.513  1.00 17.52           O  
ATOM   5831  OE2 GLU B 257     127.289 114.898 153.503  1.00 17.52           O  
ATOM   5832  N   SER B 258     126.292 117.519 151.693  1.00 16.96           N  
ATOM   5833  CA  SER B 258     124.885 117.202 151.479  1.00 16.96           C  
ATOM   5834  C   SER B 258     124.644 115.698 151.437  1.00 16.96           C  
ATOM   5835  O   SER B 258     125.476 114.925 150.959  1.00 16.96           O  
ATOM   5836  CB  SER B 258     124.384 117.823 150.172  1.00 16.96           C  
ATOM   5837  OG  SER B 258     123.031 117.481 149.932  1.00 16.96           O  
ATOM   5838  N   PHE B 259     123.478 115.295 151.939  1.00 19.72           N  
ATOM   5839  CA  PHE B 259     122.986 113.929 151.832  1.00 19.72           C  
ATOM   5840  C   PHE B 259     122.064 113.726 150.632  1.00 19.72           C  
ATOM   5841  O   PHE B 259     121.464 112.655 150.505  1.00 19.72           O  
ATOM   5842  CB  PHE B 259     122.233 113.532 153.107  1.00 19.72           C  
ATOM   5843  CG  PHE B 259     123.096 113.444 154.333  1.00 19.72           C  
ATOM   5844  CD1 PHE B 259     124.110 112.508 154.423  1.00 19.72           C  
ATOM   5845  CD2 PHE B 259     122.873 114.282 155.410  1.00 19.72           C  
ATOM   5846  CE1 PHE B 259     124.892 112.424 155.556  1.00 19.72           C  
ATOM   5847  CE2 PHE B 259     123.649 114.198 156.544  1.00 19.72           C  
ATOM   5848  CZ  PHE B 259     124.659 113.268 156.617  1.00 19.72           C  
ATOM   5849  N   ASP B 260     121.935 114.720 149.759  1.00 18.70           N  
ATOM   5850  CA  ASP B 260     120.969 114.713 148.668  1.00 18.70           C  
ATOM   5851  C   ASP B 260     121.693 114.571 147.328  1.00 18.70           C  
ATOM   5852  O   ASP B 260     122.924 114.529 147.258  1.00 18.70           O  
ATOM   5853  CB  ASP B 260     120.111 115.979 148.721  1.00 18.70           C  
ATOM   5854  CG  ASP B 260     118.718 115.775 148.144  1.00 18.70           C  
ATOM   5855  OD1 ASP B 260     118.373 114.638 147.762  1.00 18.70           O  
ATOM   5856  OD2 ASP B 260     117.958 116.760 148.087  1.00 18.70           O  
ATOM   5857  N   ASP B 261     120.907 114.495 146.254  1.00 18.53           N  
ATOM   5858  CA  ASP B 261     121.404 114.190 144.916  1.00 18.53           C  
ATOM   5859  C   ASP B 261     120.987 115.288 143.947  1.00 18.53           C  
ATOM   5860  O   ASP B 261     119.804 115.633 143.868  1.00 18.53           O  
ATOM   5861  CB  ASP B 261     120.876 112.828 144.446  1.00 18.53           C  
ATOM   5862  CG  ASP B 261     121.318 112.475 143.038  1.00 18.53           C  
ATOM   5863  OD1 ASP B 261     122.138 113.213 142.455  1.00 18.53           O  
ATOM   5864  OD2 ASP B 261     120.840 111.449 142.512  1.00 18.53           O  
ATOM   5865  N   VAL B 262     121.961 115.830 143.205  1.00 16.72           N  
ATOM   5866  CA  VAL B 262     121.694 116.923 142.269  1.00 16.72           C  
ATOM   5867  C   VAL B 262     121.135 116.454 140.936  1.00 16.72           C  
ATOM   5868  O   VAL B 262     120.870 117.292 140.064  1.00 16.72           O  
ATOM   5869  CB  VAL B 262     122.954 117.760 141.962  1.00 16.72           C  
ATOM   5870  CG1 VAL B 262     123.431 118.501 143.199  1.00 16.72           C  
ATOM   5871  CG2 VAL B 262     124.070 116.896 141.378  1.00 16.72           C  
ATOM   5872  N   ASN B 263     120.955 115.148 140.741  1.00 18.91           N  
ATOM   5873  CA  ASN B 263     120.485 114.604 139.473  1.00 18.91           C  
ATOM   5874  C   ASN B 263     119.163 113.858 139.600  1.00 18.91           C  
ATOM   5875  O   ASN B 263     118.738 113.211 138.638  1.00 18.91           O  
ATOM   5876  CB  ASN B 263     121.549 113.680 138.875  1.00 18.91           C  
ATOM   5877  CG  ASN B 263     122.755 114.437 138.363  1.00 18.91           C  
ATOM   5878  OD1 ASN B 263     122.628 115.516 137.785  1.00 18.91           O  
ATOM   5879  ND2 ASN B 263     123.937 113.880 138.582  1.00 18.91           N  
ATOM   5880  N   ARG B 264     118.503 113.925 140.752  1.00 17.70           N  
ATOM   5881  CA  ARG B 264     117.210 113.275 140.904  1.00 17.70           C  
ATOM   5882  C   ARG B 264     116.123 114.060 140.179  1.00 17.70           C  
ATOM   5883  O   ARG B 264     116.153 115.291 140.108  1.00 17.70           O  
ATOM   5884  CB  ARG B 264     116.848 113.128 142.383  1.00 17.70           C  
ATOM   5885  CG  ARG B 264     116.614 114.436 143.122  1.00 17.70           C  
ATOM   5886  CD  ARG B 264     116.076 114.209 144.529  1.00 17.70           C  
ATOM   5887  NE  ARG B 264     116.193 115.402 145.368  1.00 17.70           N  
ATOM   5888  CZ  ARG B 264     115.203 116.253 145.632  1.00 17.70           C  
ATOM   5889  NH1 ARG B 264     113.992 116.068 145.129  1.00 17.70           N  
ATOM   5890  NH2 ARG B 264     115.427 117.303 146.407  1.00 17.70           N  
ATOM   5891  N   LEU B 265     115.160 113.326 139.632  1.00 18.49           N  
ATOM   5892  CA  LEU B 265     113.983 113.887 138.991  1.00 18.49           C  
ATOM   5893  C   LEU B 265     112.780 113.734 139.912  1.00 18.49           C  
ATOM   5894  O   LEU B 265     112.750 112.869 140.791  1.00 18.49           O  
ATOM   5895  CB  LEU B 265     113.712 113.202 137.649  1.00 18.49           C  
ATOM   5896  CG  LEU B 265     114.874 113.209 136.655  1.00 18.49           C  
ATOM   5897  CD1 LEU B 265     114.569 112.325 135.465  1.00 18.49           C  
ATOM   5898  CD2 LEU B 265     115.188 114.616 136.194  1.00 18.49           C  
ATOM   5899  N   ASP B 266     111.782 114.590 139.702  1.00 21.09           N  
ATOM   5900  CA  ASP B 266     110.590 114.639 140.547  1.00 21.09           C  
ATOM   5901  C   ASP B 266     109.349 114.590 139.656  1.00 21.09           C  
ATOM   5902  O   ASP B 266     108.954 115.601 139.071  1.00 21.09           O  
ATOM   5903  CB  ASP B 266     110.606 115.887 141.423  1.00 21.09           C  
ATOM   5904  CG  ASP B 266     109.435 115.945 142.374  1.00 21.09           C  
ATOM   5905  OD1 ASP B 266     108.668 114.963 142.446  1.00 21.09           O  
ATOM   5906  OD2 ASP B 266     109.290 116.975 143.061  1.00 21.09           O  
ATOM   5907  N   LYS B 267     108.727 113.411 139.582  1.00 21.10           N  
ATOM   5908  CA  LYS B 267     107.613 113.204 138.660  1.00 21.10           C  
ATOM   5909  C   LYS B 267     106.367 113.964 139.100  1.00 21.10           C  
ATOM   5910  O   LYS B 267     105.605 114.452 138.259  1.00 21.10           O  
ATOM   5911  CB  LYS B 267     107.299 111.713 138.540  1.00 21.10           C  
ATOM   5912  CG  LYS B 267     108.438 110.842 138.047  1.00 21.10           C  
ATOM   5913  CD  LYS B 267     108.723 111.018 136.564  1.00 21.10           C  
ATOM   5914  CE  LYS B 267     109.872 111.972 136.318  1.00 21.10           C  
ATOM   5915  NZ  LYS B 267     110.231 112.029 134.881  1.00 21.10           N  
ATOM   5916  N   SER B 268     106.133 114.061 140.412  1.00 19.44           N  
ATOM   5917  CA  SER B 268     104.905 114.682 140.898  1.00 19.44           C  
ATOM   5918  C   SER B 268     104.761 116.117 140.407  1.00 19.44           C  
ATOM   5919  O   SER B 268     103.639 116.587 140.186  1.00 19.44           O  
ATOM   5920  CB  SER B 268     104.860 114.629 142.427  1.00 19.44           C  
ATOM   5921  OG  SER B 268     106.088 115.037 143.002  1.00 19.44           O  
ATOM   5922  N   LEU B 269     105.877 116.819 140.201  1.00 16.13           N  
ATOM   5923  CA  LEU B 269     105.812 118.196 139.726  1.00 16.13           C  
ATOM   5924  C   LEU B 269     105.116 118.310 138.377  1.00 16.13           C  
ATOM   5925  O   LEU B 269     104.633 119.393 138.033  1.00 16.13           O  
ATOM   5926  CB  LEU B 269     107.221 118.791 139.629  1.00 16.13           C  
ATOM   5927  CG  LEU B 269     107.970 119.063 140.936  1.00 16.13           C  
ATOM   5928  CD1 LEU B 269     109.296 119.748 140.657  1.00 16.13           C  
ATOM   5929  CD2 LEU B 269     107.144 119.884 141.899  1.00 16.13           C  
ATOM   5930  N   ASP B 270     105.059 117.225 137.603  1.00 18.66           N  
ATOM   5931  CA  ASP B 270     104.377 117.265 136.317  1.00 18.66           C  
ATOM   5932  C   ASP B 270     102.872 117.452 136.461  1.00 18.66           C  
ATOM   5933  O   ASP B 270     102.215 117.820 135.483  1.00 18.66           O  
ATOM   5934  CB  ASP B 270     104.673 115.989 135.526  1.00 18.66           C  
ATOM   5935  CG  ASP B 270     106.123 115.891 135.095  1.00 18.66           C  
ATOM   5936  OD1 ASP B 270     106.755 116.943 134.866  1.00 18.66           O  
ATOM   5937  OD2 ASP B 270     106.633 114.758 134.986  1.00 18.66           O  
ATOM   5938  N   THR B 271     102.311 117.211 137.648  1.00 18.21           N  
ATOM   5939  CA  THR B 271     100.882 117.388 137.886  1.00 18.21           C  
ATOM   5940  C   THR B 271     100.599 118.413 138.982  1.00 18.21           C  
ATOM   5941  O   THR B 271      99.567 118.342 139.649  1.00 18.21           O  
ATOM   5942  CB  THR B 271     100.224 116.055 138.237  1.00 18.21           C  
ATOM   5943  OG1 THR B 271     100.831 115.509 139.413  1.00 18.21           O  
ATOM   5944  CG2 THR B 271     100.354 115.068 137.092  1.00 18.21           C  
ATOM   5945  N   LEU B 272     101.499 119.379 139.177  1.00 15.11           N  
ATOM   5946  CA  LEU B 272     101.284 120.400 140.198  1.00 15.11           C  
ATOM   5947  C   LEU B 272     100.289 121.463 139.734  1.00 15.11           C  
ATOM   5948  O   LEU B 272      99.374 121.827 140.478  1.00 15.11           O  
ATOM   5949  CB  LEU B 272     102.616 121.043 140.590  1.00 15.11           C  
ATOM   5950  CG  LEU B 272     102.566 122.080 141.716  1.00 15.11           C  
ATOM   5951  CD1 LEU B 272     101.978 121.482 142.987  1.00 15.11           C  
ATOM   5952  CD2 LEU B 272     103.943 122.651 141.989  1.00 15.11           C  
ATOM   5953  N   ILE B 273     100.450 121.969 138.515  1.00 15.52           N  
ATOM   5954  CA  ILE B 273      99.600 123.036 137.984  1.00 15.52           C  
ATOM   5955  C   ILE B 273      98.232 122.454 137.630  1.00 15.52           C  
ATOM   5956  O   ILE B 273      98.161 121.490 136.856  1.00 15.52           O  
ATOM   5957  CB  ILE B 273     100.251 123.709 136.762  1.00 15.52           C  
ATOM   5958  CG1 ILE B 273     101.639 124.274 137.099  1.00 15.52           C  
ATOM   5959  CG2 ILE B 273      99.361 124.821 136.213  1.00 15.52           C  
ATOM   5960  CD1 ILE B 273     101.721 125.123 138.351  1.00 15.52           C  
ATOM   5961  N   PRO B 274      97.128 122.990 138.153  1.00 22.96           N  
ATOM   5962  CA  PRO B 274      95.808 122.453 137.799  1.00 22.96           C  
ATOM   5963  C   PRO B 274      95.381 122.837 136.390  1.00 22.96           C  
ATOM   5964  O   PRO B 274      95.824 123.834 135.818  1.00 22.96           O  
ATOM   5965  CB  PRO B 274      94.876 123.081 138.843  1.00 22.96           C  
ATOM   5966  CG  PRO B 274      95.761 123.578 139.915  1.00 22.96           C  
ATOM   5967  CD  PRO B 274      97.015 123.989 139.227  1.00 22.96           C  
ATOM   5968  N   ASP B 275      94.496 122.009 135.829  1.00 34.57           N  
ATOM   5969  CA  ASP B 275      93.935 122.296 134.512  1.00 34.57           C  
ATOM   5970  C   ASP B 275      93.061 123.544 134.547  1.00 34.57           C  
ATOM   5971  O   ASP B 275      93.132 124.392 133.651  1.00 34.57           O  
ATOM   5972  CB  ASP B 275      93.134 121.093 134.012  1.00 34.57           C  
ATOM   5973  CG  ASP B 275      94.015 119.915 133.652  1.00 34.57           C  
ATOM   5974  OD1 ASP B 275      95.116 120.136 133.106  1.00 34.57           O  
ATOM   5975  OD2 ASP B 275      93.607 118.764 133.916  1.00 34.57           O  
ATOM   5976  N   ASN B 276      92.232 123.670 135.571  1.00 33.76           N  
ATOM   5977  CA  ASN B 276      91.360 124.831 135.700  1.00 33.76           C  
ATOM   5978  C   ASN B 276      92.184 126.053 136.086  1.00 33.76           C  
ATOM   5979  O   ASN B 276      92.864 126.025 137.120  1.00 33.76           O  
ATOM   5980  CB  ASN B 276      90.285 124.561 136.745  1.00 33.76           C  
ATOM   5981  CG  ASN B 276      89.284 125.694 136.865  1.00 33.76           C  
ATOM   5982  OD1 ASN B 276      89.479 126.778 136.319  1.00 33.76           O  
ATOM   5983  ND2 ASN B 276      88.202 125.444 137.586  1.00 33.76           N  
ATOM   5984  N   PRO B 277      92.160 127.139 135.306  1.00 33.48           N  
ATOM   5985  CA  PRO B 277      92.985 128.308 135.643  1.00 33.48           C  
ATOM   5986  C   PRO B 277      92.471 129.121 136.818  1.00 33.48           C  
ATOM   5987  O   PRO B 277      93.152 130.066 137.231  1.00 33.48           O  
ATOM   5988  CB  PRO B 277      92.956 129.138 134.351  1.00 33.48           C  
ATOM   5989  CG  PRO B 277      91.713 128.741 133.673  1.00 33.48           C  
ATOM   5990  CD  PRO B 277      91.468 127.311 134.017  1.00 33.48           C  
ATOM   5991  N   ASN B 278      91.302 128.800 137.368  1.00 36.85           N  
ATOM   5992  CA  ASN B 278      90.771 129.499 138.529  1.00 36.85           C  
ATOM   5993  C   ASN B 278      91.078 128.790 139.842  1.00 36.85           C  
ATOM   5994  O   ASN B 278      90.628 129.247 140.895  1.00 36.85           O  
ATOM   5995  CB  ASN B 278      89.257 129.683 138.384  1.00 36.85           C  
ATOM   5996  CG  ASN B 278      88.871 130.335 137.072  1.00 36.85           C  
ATOM   5997  OD1 ASN B 278      87.994 129.849 136.359  1.00 36.85           O  
ATOM   5998  ND2 ASN B 278      89.525 131.442 136.747  1.00 36.85           N  
ATOM   5999  N   LYS B 279      91.828 127.691 139.807  1.00 29.39           N  
ATOM   6000  CA  LYS B 279      92.217 126.978 141.013  1.00 29.39           C  
ATOM   6001  C   LYS B 279      93.657 127.310 141.385  1.00 29.39           C  
ATOM   6002  O   LYS B 279      94.525 127.358 140.509  1.00 29.39           O  
ATOM   6003  CB  LYS B 279      92.087 125.468 140.817  1.00 29.39           C  
ATOM   6004  CG  LYS B 279      90.696 124.999 140.455  1.00 29.39           C  
ATOM   6005  CD  LYS B 279      89.773 124.988 141.654  1.00 29.39           C  
ATOM   6006  CE  LYS B 279      88.970 123.702 141.723  1.00 29.39           C  
ATOM   6007  NZ  LYS B 279      88.242 123.423 140.456  1.00 29.39           N  
ATOM   6008  N   PRO B 280      93.963 127.551 142.665  1.00 21.86           N  
ATOM   6009  CA  PRO B 280      95.354 127.827 143.044  1.00 21.86           C  
ATOM   6010  C   PRO B 280      96.150 126.577 143.384  1.00 21.86           C  
ATOM   6011  O   PRO B 280      95.643 125.455 143.296  1.00 21.86           O  
ATOM   6012  CB  PRO B 280      95.200 128.737 144.264  1.00 21.86           C  
ATOM   6013  CG  PRO B 280      93.936 128.308 144.885  1.00 21.86           C  
ATOM   6014  CD  PRO B 280      93.051 127.731 143.807  1.00 21.86           C  
ATOM   6015  N   TYR B 281      97.406 126.779 143.773  1.00 13.09           N  
ATOM   6016  CA  TYR B 281      98.287 125.712 144.222  1.00 13.09           C  
ATOM   6017  C   TYR B 281      99.311 126.321 145.169  1.00 13.09           C  
ATOM   6018  O   TYR B 281      99.538 127.532 145.169  1.00 13.09           O  
ATOM   6019  CB  TYR B 281      98.977 125.013 143.047  1.00 13.09           C  
ATOM   6020  CG  TYR B 281      99.891 125.921 142.259  1.00 13.09           C  
ATOM   6021  CD1 TYR B 281      99.397 126.728 141.252  1.00 13.09           C  
ATOM   6022  CD2 TYR B 281     101.245 125.977 142.532  1.00 13.09           C  
ATOM   6023  CE1 TYR B 281     100.221 127.560 140.537  1.00 13.09           C  
ATOM   6024  CE2 TYR B 281     102.081 126.807 141.822  1.00 13.09           C  
ATOM   6025  CZ  TYR B 281     101.564 127.598 140.826  1.00 13.09           C  
ATOM   6026  OH  TYR B 281     102.399 128.427 140.119  1.00 13.09           O  
ATOM   6027  N   ASP B 282      99.931 125.469 145.979  1.00 13.21           N  
ATOM   6028  CA  ASP B 282     100.849 125.920 147.021  1.00 13.21           C  
ATOM   6029  C   ASP B 282     102.279 125.914 146.484  1.00 13.21           C  
ATOM   6030  O   ASP B 282     102.861 124.850 146.253  1.00 13.21           O  
ATOM   6031  CB  ASP B 282     100.721 125.042 148.262  1.00 13.21           C  
ATOM   6032  CG  ASP B 282     101.450 125.615 149.459  1.00 13.21           C  
ATOM   6033  OD1 ASP B 282     102.175 126.617 149.295  1.00 13.21           O  
ATOM   6034  OD2 ASP B 282     101.292 125.067 150.568  1.00 13.21           O  
ATOM   6035  N   MET B 283     102.853 127.107 146.315  1.00 13.47           N  
ATOM   6036  CA  MET B 283     104.215 127.231 145.797  1.00 13.47           C  
ATOM   6037  C   MET B 283     105.263 126.753 146.801  1.00 13.47           C  
ATOM   6038  O   MET B 283     106.355 126.314 146.405  1.00 13.47           O  
ATOM   6039  CB  MET B 283     104.481 128.684 145.412  1.00 13.47           C  
ATOM   6040  CG  MET B 283     105.721 128.895 144.575  1.00 13.47           C  
ATOM   6041  SD  MET B 283     105.549 128.358 142.874  1.00 13.47           S  
ATOM   6042  CE  MET B 283     105.156 129.909 142.080  1.00 13.47           C  
ATOM   6043  N   GLY B 284     104.959 126.833 148.096  1.00 13.57           N  
ATOM   6044  CA  GLY B 284     105.903 126.367 149.096  1.00 13.57           C  
ATOM   6045  C   GLY B 284     106.217 124.894 148.960  1.00 13.57           C  
ATOM   6046  O   GLY B 284     107.321 124.455 149.293  1.00 13.57           O  
ATOM   6047  N   GLU B 285     105.262 124.112 148.459  1.00 16.56           N  
ATOM   6048  CA  GLU B 285     105.532 122.711 148.169  1.00 16.56           C  
ATOM   6049  C   GLU B 285     106.626 122.581 147.116  1.00 16.56           C  
ATOM   6050  O   GLU B 285     107.526 121.744 147.238  1.00 16.56           O  
ATOM   6051  CB  GLU B 285     104.245 122.012 147.722  1.00 16.56           C  
ATOM   6052  CG  GLU B 285     104.459 120.744 146.919  1.00 16.56           C  
ATOM   6053  CD  GLU B 285     103.160 120.058 146.535  1.00 16.56           C  
ATOM   6054  OE1 GLU B 285     102.142 120.265 147.229  1.00 16.56           O  
ATOM   6055  OE2 GLU B 285     103.161 119.305 145.541  1.00 16.56           O  
ATOM   6056  N   LEU B 286     106.565 123.408 146.069  1.00 11.52           N  
ATOM   6057  CA  LEU B 286     107.631 123.423 145.072  1.00 11.52           C  
ATOM   6058  C   LEU B 286     108.967 123.788 145.712  1.00 11.52           C  
ATOM   6059  O   LEU B 286     109.978 123.098 145.509  1.00 11.52           O  
ATOM   6060  CB  LEU B 286     107.276 124.396 143.940  1.00 11.52           C  
ATOM   6061  CG  LEU B 286     108.228 124.529 142.744  1.00 11.52           C  
ATOM   6062  CD1 LEU B 286     108.581 123.165 142.150  1.00 11.52           C  
ATOM   6063  CD2 LEU B 286     107.637 125.446 141.672  1.00 11.52           C  
ATOM   6064  N   ILE B 287     108.987 124.856 146.516  1.00  9.57           N  
ATOM   6065  CA  ILE B 287     110.245 125.273 147.141  1.00  9.57           C  
ATOM   6066  C   ILE B 287     110.835 124.131 147.964  1.00  9.57           C  
ATOM   6067  O   ILE B 287     112.039 123.861 147.896  1.00  9.57           O  
ATOM   6068  CB  ILE B 287     110.051 126.544 147.993  1.00  9.57           C  
ATOM   6069  CG1 ILE B 287     109.743 127.753 147.094  1.00  9.57           C  
ATOM   6070  CG2 ILE B 287     111.312 126.825 148.833  1.00  9.57           C  
ATOM   6071  CD1 ILE B 287     109.380 129.028 147.837  1.00  9.57           C  
ATOM   6072  N   ARG B 288     110.003 123.433 148.739  1.00 13.51           N  
ATOM   6073  CA  ARG B 288     110.502 122.379 149.614  1.00 13.51           C  
ATOM   6074  C   ARG B 288     110.825 121.091 148.866  1.00 13.51           C  
ATOM   6075  O   ARG B 288     111.584 120.266 149.382  1.00 13.51           O  
ATOM   6076  CB  ARG B 288     109.493 122.108 150.732  1.00 13.51           C  
ATOM   6077  CG  ARG B 288     109.394 123.257 151.728  1.00 13.51           C  
ATOM   6078  CD  ARG B 288     108.107 123.266 152.522  1.00 13.51           C  
ATOM   6079  NE  ARG B 288     108.130 124.298 153.558  1.00 13.51           N  
ATOM   6080  CZ  ARG B 288     107.815 125.575 153.362  1.00 13.51           C  
ATOM   6081  NH1 ARG B 288     107.873 126.434 154.369  1.00 13.51           N  
ATOM   6082  NH2 ARG B 288     107.444 126.006 152.166  1.00 13.51           N  
ATOM   6083  N   ARG B 289     110.270 120.899 147.672  1.00 16.26           N  
ATOM   6084  CA  ARG B 289     110.695 119.801 146.816  1.00 16.26           C  
ATOM   6085  C   ARG B 289     111.992 120.101 146.076  1.00 16.26           C  
ATOM   6086  O   ARG B 289     112.633 119.168 145.581  1.00 16.26           O  
ATOM   6087  CB  ARG B 289     109.607 119.466 145.794  1.00 16.26           C  
ATOM   6088  CG  ARG B 289     108.311 118.948 146.382  1.00 16.26           C  
ATOM   6089  CD  ARG B 289     108.122 117.493 146.029  1.00 16.26           C  
ATOM   6090  NE  ARG B 289     106.797 116.990 146.363  1.00 16.26           N  
ATOM   6091  CZ  ARG B 289     106.427 115.726 146.190  1.00 16.26           C  
ATOM   6092  NH1 ARG B 289     105.201 115.341 146.516  1.00 16.26           N  
ATOM   6093  NH2 ARG B 289     107.284 114.847 145.686  1.00 16.26           N  
ATOM   6094  N   VAL B 290     112.390 121.367 145.980  1.00 10.03           N  
ATOM   6095  CA  VAL B 290     113.566 121.723 145.187  1.00 10.03           C  
ATOM   6096  C   VAL B 290     114.827 121.888 146.040  1.00 10.03           C  
ATOM   6097  O   VAL B 290     115.942 121.703 145.542  1.00 10.03           O  
ATOM   6098  CB  VAL B 290     113.283 122.992 144.359  1.00 10.03           C  
ATOM   6099  CG1 VAL B 290     114.566 123.615 143.853  1.00 10.03           C  
ATOM   6100  CG2 VAL B 290     112.366 122.662 143.187  1.00 10.03           C  
ATOM   6101  N   VAL B 291     114.679 122.229 147.321  1.00  9.11           N  
ATOM   6102  CA  VAL B 291     115.849 122.451 148.171  1.00  9.11           C  
ATOM   6103  C   VAL B 291     116.401 121.118 148.675  1.00  9.11           C  
ATOM   6104  O   VAL B 291     115.718 120.093 148.699  1.00  9.11           O  
ATOM   6105  CB  VAL B 291     115.530 123.394 149.348  1.00  9.11           C  
ATOM   6106  CG1 VAL B 291     115.166 124.785 148.855  1.00  9.11           C  
ATOM   6107  CG2 VAL B 291     114.453 122.816 150.245  1.00  9.11           C  
ATOM   6108  N   ASP B 292     117.673 121.141 149.075  1.00 11.15           N  
ATOM   6109  CA  ASP B 292     118.287 119.992 149.733  1.00 11.15           C  
ATOM   6110  C   ASP B 292     117.491 119.581 150.967  1.00 11.15           C  
ATOM   6111  O   ASP B 292     117.169 120.412 151.820  1.00 11.15           O  
ATOM   6112  CB  ASP B 292     119.728 120.308 150.141  1.00 11.15           C  
ATOM   6113  CG  ASP B 292     120.676 120.402 148.962  1.00 11.15           C  
ATOM   6114  OD1 ASP B 292     120.291 120.020 147.842  1.00 11.15           O  
ATOM   6115  OD2 ASP B 292     121.814 120.869 149.163  1.00 11.15           O  
ATOM   6116  N   GLU B 293     117.187 118.288 151.060  1.00 15.91           N  
ATOM   6117  CA  GLU B 293     116.649 117.648 152.261  1.00 15.91           C  
ATOM   6118  C   GLU B 293     115.347 118.284 152.754  1.00 15.91           C  
ATOM   6119  O   GLU B 293     114.934 118.044 153.891  1.00 15.91           O  
ATOM   6120  CB  GLU B 293     117.696 117.644 153.384  1.00 15.91           C  
ATOM   6121  CG  GLU B 293     119.004 116.958 153.014  1.00 15.91           C  
ATOM   6122  CD  GLU B 293     120.176 117.384 153.879  1.00 15.91           C  
ATOM   6123  OE1 GLU B 293     119.969 117.680 155.073  1.00 15.91           O  
ATOM   6124  OE2 GLU B 293     121.311 117.417 153.362  1.00 15.91           O  
ATOM   6125  N   GLY B 294     114.674 119.073 151.920  1.00 13.24           N  
ATOM   6126  CA  GLY B 294     113.423 119.691 152.318  1.00 13.24           C  
ATOM   6127  C   GLY B 294     113.533 120.738 153.405  1.00 13.24           C  
ATOM   6128  O   GLY B 294     112.533 121.045 154.056  1.00 13.24           O  
ATOM   6129  N   ASP B 295     114.718 121.305 153.613  1.00 13.50           N  
ATOM   6130  CA  ASP B 295     114.985 122.209 154.727  1.00 13.50           C  
ATOM   6131  C   ASP B 295     114.948 123.658 154.243  1.00 13.50           C  
ATOM   6132  O   ASP B 295     115.742 124.047 153.381  1.00 13.50           O  
ATOM   6133  CB  ASP B 295     116.336 121.876 155.359  1.00 13.50           C  
ATOM   6134  CG  ASP B 295     116.635 122.712 156.583  1.00 13.50           C  
ATOM   6135  OD1 ASP B 295     115.798 122.748 157.507  1.00 13.50           O  
ATOM   6136  OD2 ASP B 295     117.718 123.327 156.622  1.00 13.50           O  
ATOM   6137  N   PHE B 296     114.041 124.455 154.817  1.00 10.45           N  
ATOM   6138  CA  PHE B 296     113.788 125.831 154.394  1.00 10.45           C  
ATOM   6139  C   PHE B 296     113.536 126.716 155.613  1.00 10.45           C  
ATOM   6140  O   PHE B 296     112.680 126.398 156.442  1.00 10.45           O  
ATOM   6141  CB  PHE B 296     112.587 125.887 153.435  1.00 10.45           C  
ATOM   6142  CG  PHE B 296     112.387 127.220 152.773  1.00 10.45           C  
ATOM   6143  CD1 PHE B 296     113.360 127.757 151.958  1.00 10.45           C  
ATOM   6144  CD2 PHE B 296     111.216 127.930 152.950  1.00 10.45           C  
ATOM   6145  CE1 PHE B 296     113.178 128.974 151.353  1.00 10.45           C  
ATOM   6146  CE2 PHE B 296     111.037 129.149 152.339  1.00 10.45           C  
ATOM   6147  CZ  PHE B 296     112.015 129.663 151.539  1.00 10.45           C  
ATOM   6148  N   PHE B 297     114.278 127.827 155.709  1.00 12.77           N  
ATOM   6149  CA  PHE B 297     114.178 128.809 156.797  1.00 12.77           C  
ATOM   6150  C   PHE B 297     113.450 130.047 156.271  1.00 12.77           C  
ATOM   6151  O   PHE B 297     114.061 130.915 155.642  1.00 12.77           O  
ATOM   6152  CB  PHE B 297     115.564 129.170 157.334  1.00 12.77           C  
ATOM   6153  CG  PHE B 297     115.546 129.905 158.655  1.00 12.77           C  
ATOM   6154  CD1 PHE B 297     115.041 131.186 158.755  1.00 12.77           C  
ATOM   6155  CD2 PHE B 297     116.050 129.312 159.797  1.00 12.77           C  
ATOM   6156  CE1 PHE B 297     115.031 131.846 159.963  1.00 12.77           C  
ATOM   6157  CE2 PHE B 297     116.037 129.973 160.996  1.00 12.77           C  
ATOM   6158  CZ  PHE B 297     115.533 131.233 161.079  1.00 12.77           C  
ATOM   6159  N   GLU B 298     112.154 130.135 156.551  1.00  7.71           N  
ATOM   6160  CA  GLU B 298     111.321 131.197 156.002  1.00  7.71           C  
ATOM   6161  C   GLU B 298     111.507 132.502 156.766  1.00  7.71           C  
ATOM   6162  O   GLU B 298     111.668 132.511 157.989  1.00  7.71           O  
ATOM   6163  CB  GLU B 298     109.849 130.793 156.023  1.00  7.71           C  
ATOM   6164  CG  GLU B 298     108.954 131.735 155.228  1.00  7.71           C  
ATOM   6165  CD  GLU B 298     107.583 131.153 154.915  1.00  7.71           C  
ATOM   6166  OE1 GLU B 298     106.821 131.805 154.173  1.00  7.71           O  
ATOM   6167  OE2 GLU B 298     107.269 130.049 155.404  1.00  7.71           O  
ATOM   6168  N   ILE B 299     111.491 133.604 156.025  1.00  6.42           N  
ATOM   6169  CA  ILE B 299     111.638 134.953 156.559  1.00  6.42           C  
ATOM   6170  C   ILE B 299     110.333 135.711 156.326  1.00  6.42           C  
ATOM   6171  O   ILE B 299     109.775 135.673 155.225  1.00  6.42           O  
ATOM   6172  CB  ILE B 299     112.831 135.670 155.901  1.00  6.42           C  
ATOM   6173  CG1 ILE B 299     114.154 134.967 156.248  1.00  6.42           C  
ATOM   6174  CG2 ILE B 299     112.867 137.141 156.266  1.00  6.42           C  
ATOM   6175  CD1 ILE B 299     114.612 135.104 157.677  1.00  6.42           C  
ATOM   6176  N   GLN B 300     109.860 136.402 157.364  1.00  6.56           N  
ATOM   6177  CA  GLN B 300     108.606 137.161 157.343  1.00  6.56           C  
ATOM   6178  C   GLN B 300     107.438 136.312 156.829  1.00  6.56           C  
ATOM   6179  O   GLN B 300     106.700 136.706 155.925  1.00  6.56           O  
ATOM   6180  CB  GLN B 300     108.751 138.448 156.524  1.00  6.56           C  
ATOM   6181  CG  GLN B 300     109.709 139.485 157.093  1.00  6.56           C  
ATOM   6182  CD  GLN B 300     109.503 140.852 156.498  1.00  6.56           C  
ATOM   6183  OE1 GLN B 300     108.454 141.465 156.669  1.00  6.56           O  
ATOM   6184  NE2 GLN B 300     110.505 141.340 155.790  1.00  6.56           N  
ATOM   6185  N   ALA B 301     107.257 135.143 157.449  1.00  6.09           N  
ATOM   6186  CA  ALA B 301     106.247 134.191 156.991  1.00  6.09           C  
ATOM   6187  C   ALA B 301     104.828 134.718 157.192  1.00  6.09           C  
ATOM   6188  O   ALA B 301     103.941 134.447 156.376  1.00  6.09           O  
ATOM   6189  CB  ALA B 301     106.421 132.855 157.715  1.00  6.09           C  
ATOM   6190  N   ALA B 302     104.591 135.459 158.270  1.00  6.55           N  
ATOM   6191  CA  ALA B 302     103.254 135.919 158.629  1.00  6.55           C  
ATOM   6192  C   ALA B 302     102.896 137.284 158.052  1.00  6.55           C  
ATOM   6193  O   ALA B 302     101.780 137.759 158.281  1.00  6.55           O  
ATOM   6194  CB  ALA B 302     103.107 135.960 160.152  1.00  6.55           C  
ATOM   6195  N   TYR B 303     103.806 137.928 157.330  1.00  5.35           N  
ATOM   6196  CA  TYR B 303     103.569 139.224 156.707  1.00  5.35           C  
ATOM   6197  C   TYR B 303     103.574 139.089 155.188  1.00  5.35           C  
ATOM   6198  O   TYR B 303     104.442 138.426 154.618  1.00  5.35           O  
ATOM   6199  CB  TYR B 303     104.631 140.234 157.154  1.00  5.35           C  
ATOM   6200  CG  TYR B 303     104.493 141.618 156.571  1.00  5.35           C  
ATOM   6201  CD1 TYR B 303     103.458 142.454 156.946  1.00  5.35           C  
ATOM   6202  CD2 TYR B 303     105.419 142.101 155.669  1.00  5.35           C  
ATOM   6203  CE1 TYR B 303     103.341 143.719 156.423  1.00  5.35           C  
ATOM   6204  CE2 TYR B 303     105.311 143.363 155.142  1.00  5.35           C  
ATOM   6205  CZ  TYR B 303     104.271 144.167 155.518  1.00  5.35           C  
ATOM   6206  OH  TYR B 303     104.173 145.425 154.985  1.00  5.35           O  
ATOM   6207  N   ALA B 304     102.598 139.726 154.543  1.00  5.49           N  
ATOM   6208  CA  ALA B 304     102.483 139.780 153.084  1.00  5.49           C  
ATOM   6209  C   ALA B 304     102.622 138.384 152.472  1.00  5.49           C  
ATOM   6210  O   ALA B 304     103.559 138.076 151.736  1.00  5.49           O  
ATOM   6211  CB  ALA B 304     103.508 140.750 152.492  1.00  5.49           C  
ATOM   6212  N   ARG B 305     101.652 137.538 152.799  1.00  6.97           N  
ATOM   6213  CA  ARG B 305     101.688 136.120 152.464  1.00  6.97           C  
ATOM   6214  C   ARG B 305     101.371 135.839 151.000  1.00  6.97           C  
ATOM   6215  O   ARG B 305     101.358 134.670 150.604  1.00  6.97           O  
ATOM   6216  CB  ARG B 305     100.729 135.363 153.383  1.00  6.97           C  
ATOM   6217  CG  ARG B 305     101.073 135.570 154.852  1.00  6.97           C  
ATOM   6218  CD  ARG B 305     100.235 134.757 155.803  1.00  6.97           C  
ATOM   6219  NE  ARG B 305      98.812 134.796 155.489  1.00  6.97           N  
ATOM   6220  CZ  ARG B 305      98.110 133.766 155.027  1.00  6.97           C  
ATOM   6221  NH1 ARG B 305      96.820 133.918 154.782  1.00  6.97           N  
ATOM   6222  NH2 ARG B 305      98.683 132.588 154.815  1.00  6.97           N  
ATOM   6223  N   ASN B 306     101.122 136.872 150.195  1.00  6.32           N  
ATOM   6224  CA  ASN B 306     101.060 136.720 148.746  1.00  6.32           C  
ATOM   6225  C   ASN B 306     102.433 136.514 148.110  1.00  6.32           C  
ATOM   6226  O   ASN B 306     102.500 136.289 146.898  1.00  6.32           O  
ATOM   6227  CB  ASN B 306     100.355 137.927 148.109  1.00  6.32           C  
ATOM   6228  CG  ASN B 306     100.920 139.255 148.566  1.00  6.32           C  
ATOM   6229  OD1 ASN B 306     101.771 139.311 149.449  1.00  6.32           O  
ATOM   6230  ND2 ASN B 306     100.478 140.329 147.937  1.00  6.32           N  
ATOM   6231  N   ILE B 307     103.519 136.578 148.887  1.00  4.94           N  
ATOM   6232  CA  ILE B 307     104.868 136.334 148.389  1.00  4.94           C  
ATOM   6233  C   ILE B 307     105.668 135.602 149.466  1.00  4.94           C  
ATOM   6234  O   ILE B 307     105.429 135.775 150.664  1.00  4.94           O  
ATOM   6235  CB  ILE B 307     105.554 137.659 147.960  1.00  4.94           C  
ATOM   6236  CG1 ILE B 307     106.752 137.389 147.045  1.00  4.94           C  
ATOM   6237  CG2 ILE B 307     105.984 138.491 149.170  1.00  4.94           C  
ATOM   6238  CD1 ILE B 307     107.168 138.584 146.219  1.00  4.94           C  
ATOM   6239  N   ILE B 308     106.620 134.773 149.031  1.00  6.14           N  
ATOM   6240  CA  ILE B 308     107.450 133.947 149.906  1.00  6.14           C  
ATOM   6241  C   ILE B 308     108.916 134.321 149.720  1.00  6.14           C  
ATOM   6242  O   ILE B 308     109.372 134.516 148.588  1.00  6.14           O  
ATOM   6243  CB  ILE B 308     107.262 132.439 149.627  1.00  6.14           C  
ATOM   6244  CG1 ILE B 308     105.810 132.006 149.811  1.00  6.14           C  
ATOM   6245  CG2 ILE B 308     108.181 131.602 150.514  1.00  6.14           C  
ATOM   6246  CD1 ILE B 308     105.517 130.673 149.189  1.00  6.14           C  
ATOM   6247  N   THR B 309     109.656 134.364 150.837  1.00 12.77           N  
ATOM   6248  CA  THR B 309     111.088 134.644 150.885  1.00 12.77           C  
ATOM   6249  C   THR B 309     111.781 133.743 151.902  1.00 12.77           C  
ATOM   6250  O   THR B 309     111.264 133.539 153.002  1.00 12.77           O  
ATOM   6251  CB  THR B 309     111.362 136.096 151.283  1.00 12.77           C  
ATOM   6252  OG1 THR B 309     110.732 136.368 152.540  1.00 12.77           O  
ATOM   6253  CG2 THR B 309     110.842 137.051 150.244  1.00 12.77           C  
ATOM   6254  N   GLY B 310     112.973 133.255 151.562  1.00  8.30           N  
ATOM   6255  CA  GLY B 310     113.737 132.508 152.555  1.00  8.30           C  
ATOM   6256  C   GLY B 310     115.004 131.869 152.019  1.00  8.30           C  
ATOM   6257  O   GLY B 310     115.361 132.012 150.850  1.00  8.30           O  
ATOM   6258  N   PHE B 311     115.697 131.167 152.923  1.00 12.77           N  
ATOM   6259  CA  PHE B 311     116.982 130.523 152.662  1.00 12.77           C  
ATOM   6260  C   PHE B 311     116.844 129.008 152.588  1.00 12.77           C  
ATOM   6261  O   PHE B 311     116.185 128.394 153.430  1.00 12.77           O  
ATOM   6262  CB  PHE B 311     118.009 130.857 153.752  1.00 12.77           C  
ATOM   6263  CG  PHE B 311     118.317 132.315 153.878  1.00 12.77           C  
ATOM   6264  CD1 PHE B 311     118.969 132.987 152.869  1.00 12.77           C  
ATOM   6265  CD2 PHE B 311     117.962 133.017 155.011  1.00 12.77           C  
ATOM   6266  CE1 PHE B 311     119.248 134.323 152.988  1.00 12.77           C  
ATOM   6267  CE2 PHE B 311     118.245 134.348 155.126  1.00 12.77           C  
ATOM   6268  CZ  PHE B 311     118.890 134.999 154.117  1.00 12.77           C  
ATOM   6269  N   GLY B 312     117.487 128.413 151.583  1.00  7.89           N  
ATOM   6270  CA  GLY B 312     117.717 126.981 151.531  1.00  7.89           C  
ATOM   6271  C   GLY B 312     119.131 126.645 151.087  1.00  7.89           C  
ATOM   6272  O   GLY B 312     119.982 127.533 151.015  1.00  7.89           O  
ATOM   6273  N   ARG B 313     119.402 125.374 150.796  1.00  7.95           N  
ATOM   6274  CA  ARG B 313     120.701 124.936 150.299  1.00  7.95           C  
ATOM   6275  C   ARG B 313     120.527 124.129 149.019  1.00  7.95           C  
ATOM   6276  O   ARG B 313     119.583 123.346 148.891  1.00  7.95           O  
ATOM   6277  CB  ARG B 313     121.464 124.084 151.333  1.00  7.95           C  
ATOM   6278  CG  ARG B 313     121.946 124.851 152.560  1.00  7.95           C  
ATOM   6279  CD  ARG B 313     122.857 124.022 153.458  1.00  7.95           C  
ATOM   6280  NE  ARG B 313     123.342 124.800 154.591  1.00  7.95           N  
ATOM   6281  CZ  ARG B 313     122.734 124.877 155.768  1.00  7.95           C  
ATOM   6282  NH1 ARG B 313     121.607 124.221 155.992  1.00  7.95           N  
ATOM   6283  NH2 ARG B 313     123.258 125.616 156.730  1.00  7.95           N  
ATOM   6284  N   VAL B 314     121.445 124.337 148.077  1.00  7.63           N  
ATOM   6285  CA  VAL B 314     121.603 123.503 146.890  1.00  7.63           C  
ATOM   6286  C   VAL B 314     123.068 123.083 146.813  1.00  7.63           C  
ATOM   6287  O   VAL B 314     123.968 123.921 146.937  1.00  7.63           O  
ATOM   6288  CB  VAL B 314     121.167 124.222 145.594  1.00  7.63           C  
ATOM   6289  CG1 VAL B 314     121.287 123.283 144.396  1.00  7.63           C  
ATOM   6290  CG2 VAL B 314     119.736 124.731 145.692  1.00  7.63           C  
ATOM   6291  N   GLU B 315     123.299 121.785 146.636  1.00 12.92           N  
ATOM   6292  CA  GLU B 315     124.645 121.203 146.648  1.00 12.92           C  
ATOM   6293  C   GLU B 315     125.446 121.655 147.869  1.00 12.92           C  
ATOM   6294  O   GLU B 315     126.656 121.867 147.800  1.00 12.92           O  
ATOM   6295  CB  GLU B 315     125.397 121.534 145.358  1.00 12.92           C  
ATOM   6296  CG  GLU B 315     126.426 120.489 144.956  1.00 12.92           C  
ATOM   6297  CD  GLU B 315     126.838 120.597 143.497  1.00 12.92           C  
ATOM   6298  OE1 GLU B 315     126.318 121.485 142.790  1.00 12.92           O  
ATOM   6299  OE2 GLU B 315     127.682 119.791 143.055  1.00 12.92           O  
ATOM   6300  N   GLY B 316     124.766 121.788 149.003  1.00 10.34           N  
ATOM   6301  CA  GLY B 316     125.414 122.154 150.243  1.00 10.34           C  
ATOM   6302  C   GLY B 316     125.708 123.628 150.428  1.00 10.34           C  
ATOM   6303  O   GLY B 316     126.285 123.994 151.458  1.00 10.34           O  
ATOM   6304  N   ARG B 317     125.341 124.484 149.475  1.00 10.06           N  
ATOM   6305  CA  ARG B 317     125.622 125.911 149.541  1.00 10.06           C  
ATOM   6306  C   ARG B 317     124.321 126.710 149.635  1.00 10.06           C  
ATOM   6307  O   ARG B 317     123.303 126.331 149.052  1.00 10.06           O  
ATOM   6308  CB  ARG B 317     126.442 126.360 148.319  1.00 10.06           C  
ATOM   6309  CG  ARG B 317     127.768 125.632 148.110  1.00 10.06           C  
ATOM   6310  CD  ARG B 317     128.380 125.976 146.770  1.00 10.06           C  
ATOM   6311  NE  ARG B 317     129.575 125.182 146.490  1.00 10.06           N  
ATOM   6312  CZ  ARG B 317     130.824 125.615 146.637  1.00 10.06           C  
ATOM   6313  NH1 ARG B 317     131.070 126.843 147.073  1.00 10.06           N  
ATOM   6314  NH2 ARG B 317     131.835 124.809 146.349  1.00 10.06           N  
ATOM   6315  N   THR B 318     124.377 127.835 150.353  1.00  6.33           N  
ATOM   6316  CA  THR B 318     123.189 128.631 150.663  1.00  6.33           C  
ATOM   6317  C   THR B 318     122.666 129.382 149.440  1.00  6.33           C  
ATOM   6318  O   THR B 318     123.428 129.997 148.692  1.00  6.33           O  
ATOM   6319  CB  THR B 318     123.492 129.635 151.783  1.00  6.33           C  
ATOM   6320  OG1 THR B 318     123.748 128.934 153.000  1.00  6.33           O  
ATOM   6321  CG2 THR B 318     122.324 130.621 152.015  1.00  6.33           C  
ATOM   6322  N   VAL B 319     121.346 129.360 149.275  1.00  6.01           N  
ATOM   6323  CA  VAL B 319     120.647 130.023 148.180  1.00  6.01           C  
ATOM   6324  C   VAL B 319     119.395 130.699 148.731  1.00  6.01           C  
ATOM   6325  O   VAL B 319     118.680 130.130 149.562  1.00  6.01           O  
ATOM   6326  CB  VAL B 319     120.271 129.023 147.062  1.00  6.01           C  
ATOM   6327  CG1 VAL B 319     119.504 129.711 145.931  1.00  6.01           C  
ATOM   6328  CG2 VAL B 319     121.503 128.295 146.540  1.00  6.01           C  
ATOM   6329  N   GLY B 320     119.124 131.911 148.258  1.00  7.93           N  
ATOM   6330  CA  GLY B 320     117.882 132.590 148.578  1.00  7.93           C  
ATOM   6331  C   GLY B 320     116.786 132.303 147.561  1.00  7.93           C  
ATOM   6332  O   GLY B 320     117.051 132.073 146.388  1.00  7.93           O  
ATOM   6333  N   PHE B 321     115.540 132.319 148.036  1.00 12.77           N  
ATOM   6334  CA  PHE B 321     114.369 131.994 147.232  1.00 12.77           C  
ATOM   6335  C   PHE B 321     113.297 133.064 147.417  1.00 12.77           C  
ATOM   6336  O   PHE B 321     113.020 133.481 148.550  1.00 12.77           O  
ATOM   6337  CB  PHE B 321     113.803 130.617 147.602  1.00 12.77           C  
ATOM   6338  CG  PHE B 321     114.712 129.473 147.261  1.00 12.77           C  
ATOM   6339  CD1 PHE B 321     115.734 129.110 148.109  1.00 12.77           C  
ATOM   6340  CD2 PHE B 321     114.537 128.755 146.095  1.00 12.77           C  
ATOM   6341  CE1 PHE B 321     116.564 128.060 147.800  1.00 12.77           C  
ATOM   6342  CE2 PHE B 321     115.369 127.708 145.785  1.00 12.77           C  
ATOM   6343  CZ  PHE B 321     116.379 127.364 146.637  1.00 12.77           C  
ATOM   6344  N   VAL B 322     112.724 133.511 146.292  1.00 12.77           N  
ATOM   6345  CA  VAL B 322     111.567 134.409 146.239  1.00 12.77           C  
ATOM   6346  C   VAL B 322     110.522 133.800 145.300  1.00 12.77           C  
ATOM   6347  O   VAL B 322     110.857 133.391 144.185  1.00 12.77           O  
ATOM   6348  CB  VAL B 322     111.964 135.821 145.756  1.00 12.77           C  
ATOM   6349  CG1 VAL B 322     110.758 136.765 145.741  1.00 12.77           C  
ATOM   6350  CG2 VAL B 322     113.097 136.389 146.602  1.00 12.77           C  
ATOM   6351  N   ALA B 323     109.257 133.760 145.731  1.00  5.72           N  
ATOM   6352  CA  ALA B 323     108.220 133.114 144.924  1.00  5.72           C  
ATOM   6353  C   ALA B 323     106.835 133.720 145.134  1.00  5.72           C  
ATOM   6354  O   ALA B 323     106.452 134.038 146.260  1.00  5.72           O  
ATOM   6355  CB  ALA B 323     108.156 131.617 145.227  1.00  5.72           C  
ATOM   6356  N   ASN B 324     106.071 133.840 144.044  1.00  6.54           N  
ATOM   6357  CA  ASN B 324     104.668 134.239 144.173  1.00  6.54           C  
ATOM   6358  C   ASN B 324     103.846 133.107 144.788  1.00  6.54           C  
ATOM   6359  O   ASN B 324     104.101 131.929 144.534  1.00  6.54           O  
ATOM   6360  CB  ASN B 324     104.056 134.639 142.825  1.00  6.54           C  
ATOM   6361  CG  ASN B 324     104.860 135.690 142.099  1.00  6.54           C  
ATOM   6362  OD1 ASN B 324     105.580 135.390 141.156  1.00  6.54           O  
ATOM   6363  ND2 ASN B 324     104.727 136.934 142.525  1.00  6.54           N  
ATOM   6364  N   GLN B 325     102.850 133.471 145.598  1.00  7.89           N  
ATOM   6365  CA  GLN B 325     102.000 132.507 146.308  1.00  7.89           C  
ATOM   6366  C   GLN B 325     100.550 132.636 145.852  1.00  7.89           C  
ATOM   6367  O   GLN B 325      99.807 133.493 146.362  1.00  7.89           O  
ATOM   6368  CB  GLN B 325     102.099 132.689 147.823  1.00  7.89           C  
ATOM   6369  CG  GLN B 325     101.124 131.835 148.618  1.00  7.89           C  
ATOM   6370  CD  GLN B 325     101.232 130.360 148.298  1.00  7.89           C  
ATOM   6371  OE1 GLN B 325     100.770 129.904 147.257  1.00  7.89           O  
ATOM   6372  NE2 GLN B 325     101.836 129.606 149.198  1.00  7.89           N  
ATOM   6373  N   PRO B 326     100.098 131.806 144.907  1.00 10.34           N  
ATOM   6374  CA  PRO B 326      98.715 131.930 144.415  1.00 10.34           C  
ATOM   6375  C   PRO B 326      97.643 131.843 145.491  1.00 10.34           C  
ATOM   6376  O   PRO B 326      96.578 132.449 145.333  1.00 10.34           O  
ATOM   6377  CB  PRO B 326      98.598 130.767 143.423  1.00 10.34           C  
ATOM   6378  CG  PRO B 326      99.966 130.513 142.959  1.00 10.34           C  
ATOM   6379  CD  PRO B 326     100.902 130.904 144.068  1.00 10.34           C  
ATOM   6380  N   LEU B 327      97.875 131.099 146.573  1.00 11.29           N  
ATOM   6381  CA  LEU B 327      96.840 130.897 147.581  1.00 11.29           C  
ATOM   6382  C   LEU B 327      96.387 132.184 148.269  1.00 11.29           C  
ATOM   6383  O   LEU B 327      95.364 132.155 148.960  1.00 11.29           O  
ATOM   6384  CB  LEU B 327      97.328 129.913 148.646  1.00 11.29           C  
ATOM   6385  CG  LEU B 327      97.520 128.447 148.257  1.00 11.29           C  
ATOM   6386  CD1 LEU B 327      98.213 127.692 149.378  1.00 11.29           C  
ATOM   6387  CD2 LEU B 327      96.204 127.772 147.912  1.00 11.29           C  
ATOM   6388  N   VAL B 328      97.100 133.298 148.109  1.00  9.32           N  
ATOM   6389  CA  VAL B 328      96.832 134.527 148.852  1.00  9.32           C  
ATOM   6390  C   VAL B 328      96.746 135.692 147.870  1.00  9.32           C  
ATOM   6391  O   VAL B 328      97.743 136.046 147.231  1.00  9.32           O  
ATOM   6392  CB  VAL B 328      97.908 134.791 149.920  1.00  9.32           C  
ATOM   6393  CG1 VAL B 328      97.669 136.126 150.613  1.00  9.32           C  
ATOM   6394  CG2 VAL B 328      97.936 133.665 150.940  1.00  9.32           C  
ATOM   6395  N   LEU B 329      95.560 136.295 147.774  1.00  9.70           N  
ATOM   6396  CA  LEU B 329      95.292 137.425 146.877  1.00  9.70           C  
ATOM   6397  C   LEU B 329      95.687 137.111 145.435  1.00  9.70           C  
ATOM   6398  O   LEU B 329      96.187 137.966 144.704  1.00  9.70           O  
ATOM   6399  CB  LEU B 329      95.986 138.700 147.364  1.00  9.70           C  
ATOM   6400  CG  LEU B 329      95.627 139.202 148.765  1.00  9.70           C  
ATOM   6401  CD1 LEU B 329      96.492 140.380 149.155  1.00  9.70           C  
ATOM   6402  CD2 LEU B 329      94.153 139.587 148.846  1.00  9.70           C  
ATOM   6403  N   ALA B 330      95.452 135.869 145.019  1.00 10.47           N  
ATOM   6404  CA  ALA B 330      95.700 135.407 143.655  1.00 10.47           C  
ATOM   6405  C   ALA B 330      97.153 135.599 143.221  1.00 10.47           C  
ATOM   6406  O   ALA B 330      97.465 135.499 142.032  1.00 10.47           O  
ATOM   6407  CB  ALA B 330      94.761 136.101 142.661  1.00 10.47           C  
ATOM   6408  N   GLY B 331      98.058 135.852 144.164  1.00  9.21           N  
ATOM   6409  CA  GLY B 331      99.457 136.055 143.844  1.00  9.21           C  
ATOM   6410  C   GLY B 331      99.821 137.413 143.287  1.00  9.21           C  
ATOM   6411  O   GLY B 331     100.917 137.568 142.743  1.00  9.21           O  
ATOM   6412  N   VAL B 332      98.945 138.411 143.412  1.00 10.07           N  
ATOM   6413  CA  VAL B 332      99.239 139.734 142.875  1.00 10.07           C  
ATOM   6414  C   VAL B 332     100.305 140.421 143.725  1.00 10.07           C  
ATOM   6415  O   VAL B 332     100.442 140.163 144.926  1.00 10.07           O  
ATOM   6416  CB  VAL B 332      97.961 140.591 142.800  1.00 10.07           C  
ATOM   6417  CG1 VAL B 332      96.843 139.853 142.087  1.00 10.07           C  
ATOM   6418  CG2 VAL B 332      97.526 141.004 144.186  1.00 10.07           C  
ATOM   6419  N   LEU B 333     101.075 141.300 143.089  1.00  9.39           N  
ATOM   6420  CA  LEU B 333     102.017 142.149 143.802  1.00  9.39           C  
ATOM   6421  C   LEU B 333     101.293 143.344 144.415  1.00  9.39           C  
ATOM   6422  O   LEU B 333     100.406 143.935 143.796  1.00  9.39           O  
ATOM   6423  CB  LEU B 333     103.124 142.638 142.863  1.00  9.39           C  
ATOM   6424  CG  LEU B 333     104.290 141.696 142.536  1.00  9.39           C  
ATOM   6425  CD1 LEU B 333     105.183 142.287 141.437  1.00  9.39           C  
ATOM   6426  CD2 LEU B 333     105.108 141.391 143.786  1.00  9.39           C  
ATOM   6427  N   ASP B 334     101.664 143.683 145.646  1.00  9.93           N  
ATOM   6428  CA  ASP B 334     101.195 144.894 146.306  1.00  9.93           C  
ATOM   6429  C   ASP B 334     102.359 145.511 147.075  1.00  9.93           C  
ATOM   6430  O   ASP B 334     103.478 144.990 147.071  1.00  9.93           O  
ATOM   6431  CB  ASP B 334      99.988 144.605 147.205  1.00  9.93           C  
ATOM   6432  CG  ASP B 334     100.349 143.832 148.459  1.00  9.93           C  
ATOM   6433  OD1 ASP B 334     101.422 143.203 148.502  1.00  9.93           O  
ATOM   6434  OD2 ASP B 334      99.541 143.852 149.410  1.00  9.93           O  
ATOM   6435  N   SER B 335     102.087 146.632 147.746  1.00  9.02           N  
ATOM   6436  CA  SER B 335     103.151 147.404 148.383  1.00  9.02           C  
ATOM   6437  C   SER B 335     103.873 146.588 149.455  1.00  9.02           C  
ATOM   6438  O   SER B 335     105.109 146.543 149.491  1.00  9.02           O  
ATOM   6439  CB  SER B 335     102.570 148.688 148.972  1.00  9.02           C  
ATOM   6440  OG  SER B 335     102.139 149.560 147.950  1.00  9.02           O  
ATOM   6441  N   ASP B 336     103.114 145.937 150.338  1.00  8.24           N  
ATOM   6442  CA  ASP B 336     103.722 145.175 151.426  1.00  8.24           C  
ATOM   6443  C   ASP B 336     104.619 144.062 150.885  1.00  8.24           C  
ATOM   6444  O   ASP B 336     105.760 143.892 151.336  1.00  8.24           O  
ATOM   6445  CB  ASP B 336     102.625 144.610 152.333  1.00  8.24           C  
ATOM   6446  CG  ASP B 336     101.900 145.688 153.127  1.00  8.24           C  
ATOM   6447  OD1 ASP B 336     102.233 146.882 152.977  1.00  8.24           O  
ATOM   6448  OD2 ASP B 336     100.989 145.340 153.904  1.00  8.24           O  
ATOM   6449  N   ALA B 337     104.115 143.293 149.917  1.00  5.99           N  
ATOM   6450  CA  ALA B 337     104.916 142.243 149.295  1.00  5.99           C  
ATOM   6451  C   ALA B 337     106.157 142.817 148.619  1.00  5.99           C  
ATOM   6452  O   ALA B 337     107.247 142.236 148.705  1.00  5.99           O  
ATOM   6453  CB  ALA B 337     104.067 141.469 148.285  1.00  5.99           C  
ATOM   6454  N   SER B 338     106.004 143.954 147.935  1.00  6.77           N  
ATOM   6455  CA  SER B 338     107.129 144.575 147.242  1.00  6.77           C  
ATOM   6456  C   SER B 338     108.243 144.919 148.221  1.00  6.77           C  
ATOM   6457  O   SER B 338     109.414 144.609 147.985  1.00  6.77           O  
ATOM   6458  CB  SER B 338     106.663 145.828 146.490  1.00  6.77           C  
ATOM   6459  OG  SER B 338     105.568 145.552 145.640  1.00  6.77           O  
ATOM   6460  N   ARG B 339     107.888 145.543 149.344  1.00  7.46           N  
ATOM   6461  CA  ARG B 339     108.889 145.916 150.337  1.00  7.46           C  
ATOM   6462  C   ARG B 339     109.545 144.677 150.950  1.00  7.46           C  
ATOM   6463  O   ARG B 339     110.782 144.607 151.076  1.00  7.46           O  
ATOM   6464  CB  ARG B 339     108.232 146.794 151.406  1.00  7.46           C  
ATOM   6465  CG  ARG B 339     107.723 148.133 150.882  1.00  7.46           C  
ATOM   6466  CD  ARG B 339     106.896 148.862 151.919  1.00  7.46           C  
ATOM   6467  NE  ARG B 339     107.617 148.977 153.180  1.00  7.46           N  
ATOM   6468  CZ  ARG B 339     107.056 148.914 154.381  1.00  7.46           C  
ATOM   6469  NH1 ARG B 339     105.747 148.756 154.514  1.00  7.46           N  
ATOM   6470  NH2 ARG B 339     107.815 149.022 155.459  1.00  7.46           N  
ATOM   6471  N   LYS B 340     108.723 143.689 151.338  1.00  8.28           N  
ATOM   6472  CA  LYS B 340     109.229 142.433 151.894  1.00  8.28           C  
ATOM   6473  C   LYS B 340     110.280 141.808 150.986  1.00  8.28           C  
ATOM   6474  O   LYS B 340     111.361 141.419 151.442  1.00  8.28           O  
ATOM   6475  CB  LYS B 340     108.068 141.452 152.129  1.00  8.28           C  
ATOM   6476  CG  LYS B 340     108.470 140.020 152.508  1.00  8.28           C  
ATOM   6477  CD  LYS B 340     107.251 139.156 152.857  1.00  8.28           C  
ATOM   6478  CE  LYS B 340     107.563 137.677 152.985  1.00  8.28           C  
ATOM   6479  NZ  LYS B 340     106.335 136.871 153.216  1.00  8.28           N  
ATOM   6480  N   ALA B 341     109.971 141.692 149.694  1.00  4.63           N  
ATOM   6481  CA  ALA B 341     110.890 141.038 148.766  1.00  4.63           C  
ATOM   6482  C   ALA B 341     112.117 141.900 148.478  1.00  4.63           C  
ATOM   6483  O   ALA B 341     113.222 141.373 148.290  1.00  4.63           O  
ATOM   6484  CB  ALA B 341     110.159 140.692 147.472  1.00  4.63           C  
ATOM   6485  N   ALA B 342     111.944 143.223 148.430  1.00  6.78           N  
ATOM   6486  CA  ALA B 342     113.056 144.112 148.109  1.00  6.78           C  
ATOM   6487  C   ALA B 342     114.148 144.049 149.174  1.00  6.78           C  
ATOM   6488  O   ALA B 342     115.339 143.962 148.847  1.00  6.78           O  
ATOM   6489  CB  ALA B 342     112.550 145.542 147.933  1.00  6.78           C  
ATOM   6490  N   ARG B 343     113.769 144.117 150.455  1.00 12.77           N  
ATOM   6491  CA  ARG B 343     114.799 144.087 151.501  1.00 12.77           C  
ATOM   6492  C   ARG B 343     115.598 142.789 151.433  1.00 12.77           C  
ATOM   6493  O   ARG B 343     116.827 142.794 151.576  1.00 12.77           O  
ATOM   6494  CB  ARG B 343     114.182 144.272 152.891  1.00 12.77           C  
ATOM   6495  CG  ARG B 343     115.203 144.465 154.044  1.00 12.77           C  
ATOM   6496  CD  ARG B 343     115.313 145.922 154.467  1.00 12.77           C  
ATOM   6497  NE  ARG B 343     116.491 146.228 155.284  1.00 12.77           N  
ATOM   6498  CZ  ARG B 343     116.565 146.088 156.603  1.00 12.77           C  
ATOM   6499  NH1 ARG B 343     115.534 145.635 157.297  1.00 12.77           N  
ATOM   6500  NH2 ARG B 343     117.683 146.406 157.238  1.00 12.77           N  
ATOM   6501  N   PHE B 344     114.912 141.675 151.177  1.00 12.77           N  
ATOM   6502  CA  PHE B 344     115.566 140.376 151.060  1.00 12.77           C  
ATOM   6503  C   PHE B 344     116.537 140.339 149.882  1.00 12.77           C  
ATOM   6504  O   PHE B 344     117.664 139.839 150.005  1.00 12.77           O  
ATOM   6505  CB  PHE B 344     114.494 139.290 150.930  1.00 12.77           C  
ATOM   6506  CG  PHE B 344     115.021 137.895 151.030  1.00 12.77           C  
ATOM   6507  CD1 PHE B 344     115.341 137.346 152.257  1.00 12.77           C  
ATOM   6508  CD2 PHE B 344     115.187 137.125 149.898  1.00 12.77           C  
ATOM   6509  CE1 PHE B 344     115.821 136.064 152.342  1.00 12.77           C  
ATOM   6510  CE2 PHE B 344     115.667 135.849 149.984  1.00 12.77           C  
ATOM   6511  CZ  PHE B 344     115.983 135.319 151.207  1.00 12.77           C  
ATOM   6512  N   VAL B 345     116.111 140.845 148.722  1.00 12.77           N  
ATOM   6513  CA  VAL B 345     116.998 140.856 147.558  1.00 12.77           C  
ATOM   6514  C   VAL B 345     118.236 141.697 147.852  1.00 12.77           C  
ATOM   6515  O   VAL B 345     119.360 141.318 147.498  1.00 12.77           O  
ATOM   6516  CB  VAL B 345     116.249 141.347 146.301  1.00 12.77           C  
ATOM   6517  CG1 VAL B 345     117.220 141.716 145.183  1.00 12.77           C  
ATOM   6518  CG2 VAL B 345     115.278 140.283 145.804  1.00 12.77           C  
ATOM   6519  N   ARG B 346     118.053 142.833 148.533  1.00 12.77           N  
ATOM   6520  CA  ARG B 346     119.185 143.700 148.854  1.00 12.77           C  
ATOM   6521  C   ARG B 346     120.159 143.001 149.801  1.00 12.77           C  
ATOM   6522  O   ARG B 346     121.379 143.042 149.593  1.00 12.77           O  
ATOM   6523  CB  ARG B 346     118.687 145.016 149.456  1.00 12.77           C  
ATOM   6524  CG  ARG B 346     117.947 145.943 148.480  1.00 12.77           C  
ATOM   6525  CD  ARG B 346     118.817 147.050 147.939  1.00 12.77           C  
ATOM   6526  NE  ARG B 346     119.154 148.042 148.957  1.00 12.77           N  
ATOM   6527  CZ  ARG B 346     119.824 149.161 148.718  1.00 12.77           C  
ATOM   6528  NH1 ARG B 346     120.224 149.454 147.492  1.00 12.77           N  
ATOM   6529  NH2 ARG B 346     120.085 149.995 149.710  1.00 12.77           N  
ATOM   6530  N   PHE B 347     119.640 142.316 150.822  1.00 12.77           N  
ATOM   6531  CA  PHE B 347     120.518 141.593 151.740  1.00 12.77           C  
ATOM   6532  C   PHE B 347     121.312 140.527 150.998  1.00 12.77           C  
ATOM   6533  O   PHE B 347     122.537 140.447 151.128  1.00 12.77           O  
ATOM   6534  CB  PHE B 347     119.720 140.957 152.875  1.00 12.77           C  
ATOM   6535  CG  PHE B 347     120.574 140.157 153.827  1.00 12.77           C  
ATOM   6536  CD1 PHE B 347     121.184 140.759 154.909  1.00 12.77           C  
ATOM   6537  CD2 PHE B 347     120.797 138.812 153.616  1.00 12.77           C  
ATOM   6538  CE1 PHE B 347     121.975 140.031 155.770  1.00 12.77           C  
ATOM   6539  CE2 PHE B 347     121.586 138.085 154.475  1.00 12.77           C  
ATOM   6540  CZ  PHE B 347     122.174 138.696 155.548  1.00 12.77           C  
ATOM   6541  N   CYS B 348     120.624 139.694 150.217  1.00 12.77           N  
ATOM   6542  CA  CYS B 348     121.305 138.658 149.452  1.00 12.77           C  
ATOM   6543  C   CYS B 348     122.396 139.241 148.561  1.00 12.77           C  
ATOM   6544  O   CYS B 348     123.498 138.693 148.482  1.00 12.77           O  
ATOM   6545  CB  CYS B 348     120.288 137.880 148.621  1.00 12.77           C  
ATOM   6546  SG  CYS B 348     119.045 137.044 149.605  1.00 12.77           S  
ATOM   6547  N   ASN B 349     122.111 140.351 147.880  1.00 12.77           N  
ATOM   6548  CA  ASN B 349     123.107 140.907 146.969  1.00 12.77           C  
ATOM   6549  C   ASN B 349     124.313 141.445 147.729  1.00 12.77           C  
ATOM   6550  O   ASN B 349     125.450 141.299 147.270  1.00 12.77           O  
ATOM   6551  CB  ASN B 349     122.493 141.999 146.096  1.00 12.77           C  
ATOM   6552  CG  ASN B 349     123.433 142.472 145.005  1.00 12.77           C  
ATOM   6553  OD1 ASN B 349     123.911 141.687 144.191  1.00 12.77           O  
ATOM   6554  ND2 ASN B 349     123.692 143.764 144.979  1.00 12.77           N  
ATOM   6555  N   ALA B 350     124.087 142.069 148.889  1.00 12.77           N  
ATOM   6556  CA  ALA B 350     125.195 142.659 149.639  1.00 12.77           C  
ATOM   6557  C   ALA B 350     126.205 141.601 150.075  1.00 12.77           C  
ATOM   6558  O   ALA B 350     127.417 141.821 149.984  1.00 12.77           O  
ATOM   6559  CB  ALA B 350     124.667 143.436 150.846  1.00 12.77           C  
ATOM   6560  N   PHE B 351     125.730 140.448 150.551  1.00 12.77           N  
ATOM   6561  CA  PHE B 351     126.584 139.396 151.091  1.00 12.77           C  
ATOM   6562  C   PHE B 351     126.829 138.249 150.102  1.00 12.77           C  
ATOM   6563  O   PHE B 351     127.221 137.154 150.520  1.00 12.77           O  
ATOM   6564  CB  PHE B 351     125.985 138.877 152.400  1.00 12.77           C  
ATOM   6565  CG  PHE B 351     126.012 139.893 153.513  1.00 12.77           C  
ATOM   6566  CD1 PHE B 351     127.158 140.098 154.258  1.00 12.77           C  
ATOM   6567  CD2 PHE B 351     124.907 140.664 153.797  1.00 12.77           C  
ATOM   6568  CE1 PHE B 351     127.187 141.037 155.264  1.00 12.77           C  
ATOM   6569  CE2 PHE B 351     124.944 141.602 154.805  1.00 12.77           C  
ATOM   6570  CZ  PHE B 351     126.084 141.784 155.533  1.00 12.77           C  
ATOM   6571  N   SER B 352     126.612 138.484 148.807  1.00  8.32           N  
ATOM   6572  CA  SER B 352     126.954 137.542 147.734  1.00  8.32           C  
ATOM   6573  C   SER B 352     126.259 136.186 147.891  1.00  8.32           C  
ATOM   6574  O   SER B 352     126.886 135.131 147.810  1.00  8.32           O  
ATOM   6575  CB  SER B 352     128.470 137.369 147.628  1.00  8.32           C  
ATOM   6576  OG  SER B 352     129.090 138.593 147.286  1.00  8.32           O  
ATOM   6577  N   ILE B 353     124.949 136.216 148.082  1.00 12.77           N  
ATOM   6578  CA  ILE B 353     124.107 135.019 148.114  1.00 12.77           C  
ATOM   6579  C   ILE B 353     123.320 134.956 146.807  1.00 12.77           C  
ATOM   6580  O   ILE B 353     122.674 135.945 146.443  1.00 12.77           O  
ATOM   6581  CB  ILE B 353     123.151 135.019 149.329  1.00 12.77           C  
ATOM   6582  CG1 ILE B 353     123.926 135.140 150.653  1.00 12.77           C  
ATOM   6583  CG2 ILE B 353     122.281 133.760 149.331  1.00 12.77           C  
ATOM   6584  CD1 ILE B 353     123.053 135.375 151.871  1.00 12.77           C  
ATOM   6585  N   PRO B 354     123.343 133.839 146.074  1.00  8.28           N  
ATOM   6586  CA  PRO B 354     122.541 133.749 144.841  1.00  8.28           C  
ATOM   6587  C   PRO B 354     121.045 133.639 145.119  1.00  8.28           C  
ATOM   6588  O   PRO B 354     120.615 133.183 146.179  1.00  8.28           O  
ATOM   6589  CB  PRO B 354     123.069 132.489 144.147  1.00  8.28           C  
ATOM   6590  CG  PRO B 354     123.870 131.770 145.132  1.00  8.28           C  
ATOM   6591  CD  PRO B 354     124.200 132.656 146.273  1.00  8.28           C  
ATOM   6592  N   ILE B 355     120.248 134.062 144.130  1.00 12.77           N  
ATOM   6593  CA  ILE B 355     118.795 134.173 144.261  1.00 12.77           C  
ATOM   6594  C   ILE B 355     118.082 133.417 143.135  1.00 12.77           C  
ATOM   6595  O   ILE B 355     118.355 133.638 141.944  1.00 12.77           O  
ATOM   6596  CB  ILE B 355     118.326 135.643 144.285  1.00 12.77           C  
ATOM   6597  CG1 ILE B 355     119.017 136.453 145.397  1.00 12.77           C  
ATOM   6598  CG2 ILE B 355     116.820 135.702 144.452  1.00 12.77           C  
ATOM   6599  CD1 ILE B 355     119.011 137.944 145.150  1.00 12.77           C  
ATOM   6600  N   VAL B 356     117.146 132.547 143.528  1.00 12.77           N  
ATOM   6601  CA  VAL B 356     116.228 131.849 142.631  1.00 12.77           C  
ATOM   6602  C   VAL B 356     114.819 132.407 142.836  1.00 12.77           C  
ATOM   6603  O   VAL B 356     114.390 132.649 143.973  1.00 12.77           O  
ATOM   6604  CB  VAL B 356     116.252 130.324 142.866  1.00 12.77           C  
ATOM   6605  CG1 VAL B 356     115.203 129.620 142.014  1.00 12.77           C  
ATOM   6606  CG2 VAL B 356     117.634 129.737 142.590  1.00 12.77           C  
ATOM   6607  N   THR B 357     114.098 132.599 141.731  1.00  8.59           N  
ATOM   6608  CA  THR B 357     112.773 133.214 141.728  1.00  8.59           C  
ATOM   6609  C   THR B 357     111.771 132.337 140.980  1.00  8.59           C  
ATOM   6610  O   THR B 357     112.060 131.865 139.876  1.00  8.59           O  
ATOM   6611  CB  THR B 357     112.839 134.612 141.104  1.00  8.59           C  
ATOM   6612  OG1 THR B 357     113.851 135.378 141.768  1.00  8.59           O  
ATOM   6613  CG2 THR B 357     111.499 135.337 141.209  1.00  8.59           C  
ATOM   6614  N   PHE B 358     110.606 132.116 141.594  1.00  6.10           N  
ATOM   6615  CA  PHE B 358     109.485 131.394 140.993  1.00  6.10           C  
ATOM   6616  C   PHE B 358     108.319 132.354 140.755  1.00  6.10           C  
ATOM   6617  O   PHE B 358     107.801 132.968 141.702  1.00  6.10           O  
ATOM   6618  CB  PHE B 358     109.031 130.219 141.863  1.00  6.10           C  
ATOM   6619  CG  PHE B 358     110.040 129.112 141.976  1.00  6.10           C  
ATOM   6620  CD1 PHE B 358     110.154 128.156 140.984  1.00  6.10           C  
ATOM   6621  CD2 PHE B 358     110.852 129.007 143.083  1.00  6.10           C  
ATOM   6622  CE1 PHE B 358     111.070 127.136 141.091  1.00  6.10           C  
ATOM   6623  CE2 PHE B 358     111.769 127.986 143.189  1.00  6.10           C  
ATOM   6624  CZ  PHE B 358     111.878 127.056 142.195  1.00  6.10           C  
ATOM   6625  N   VAL B 359     107.886 132.449 139.497  1.00  5.69           N  
ATOM   6626  CA  VAL B 359     106.973 133.493 139.035  1.00  5.69           C  
ATOM   6627  C   VAL B 359     105.620 132.877 138.691  1.00  5.69           C  
ATOM   6628  O   VAL B 359     105.540 131.936 137.891  1.00  5.69           O  
ATOM   6629  CB  VAL B 359     107.543 134.246 137.824  1.00  5.69           C  
ATOM   6630  CG1 VAL B 359     106.596 135.357 137.383  1.00  5.69           C  
ATOM   6631  CG2 VAL B 359     108.922 134.804 138.125  1.00  5.69           C  
ATOM   6632  N   ASP B 360     104.561 133.410 139.307  1.00 10.00           N  
ATOM   6633  CA  ASP B 360     103.181 133.217 138.855  1.00 10.00           C  
ATOM   6634  C   ASP B 360     102.394 134.444 139.316  1.00 10.00           C  
ATOM   6635  O   ASP B 360     101.914 134.479 140.451  1.00 10.00           O  
ATOM   6636  CB  ASP B 360     102.596 131.926 139.411  1.00 10.00           C  
ATOM   6637  CG  ASP B 360     101.131 131.739 139.058  1.00 10.00           C  
ATOM   6638  OD1 ASP B 360     100.599 132.514 138.237  1.00 10.00           O  
ATOM   6639  OD2 ASP B 360     100.511 130.800 139.596  1.00 10.00           O  
ATOM   6640  N   VAL B 361     102.251 135.430 138.434  1.00  7.91           N  
ATOM   6641  CA  VAL B 361     101.730 136.742 138.816  1.00  7.91           C  
ATOM   6642  C   VAL B 361     100.781 137.280 137.747  1.00  7.91           C  
ATOM   6643  O   VAL B 361     101.187 137.433 136.587  1.00  7.91           O  
ATOM   6644  CB  VAL B 361     102.877 137.733 139.087  1.00  7.91           C  
ATOM   6645  CG1 VAL B 361     103.797 137.894 137.869  1.00  7.91           C  
ATOM   6646  CG2 VAL B 361     102.326 139.074 139.547  1.00  7.91           C  
ATOM   6647  N   PRO B 362      99.526 137.586 138.083  1.00 10.11           N  
ATOM   6648  CA  PRO B 362      98.595 138.166 137.106  1.00 10.11           C  
ATOM   6649  C   PRO B 362      98.610 139.683 137.002  1.00 10.11           C  
ATOM   6650  O   PRO B 362      97.903 140.223 136.145  1.00 10.11           O  
ATOM   6651  CB  PRO B 362      97.227 137.692 137.619  1.00 10.11           C  
ATOM   6652  CG  PRO B 362      97.409 137.335 139.023  1.00 10.11           C  
ATOM   6653  CD  PRO B 362      98.852 137.243 139.346  1.00 10.11           C  
ATOM   6654  N   GLY B 363      99.370 140.379 137.831  1.00  9.39           N  
ATOM   6655  CA  GLY B 363      99.382 141.822 137.835  1.00  9.39           C  
ATOM   6656  C   GLY B 363      99.489 142.360 139.245  1.00  9.39           C  
ATOM   6657  O   GLY B 363      99.885 141.654 140.168  1.00  9.39           O  
ATOM   6658  N   PHE B 364      99.121 143.629 139.388  1.00 11.26           N  
ATOM   6659  CA  PHE B 364      99.137 144.345 140.653  1.00 11.26           C  
ATOM   6660  C   PHE B 364      97.728 144.442 141.235  1.00 11.26           C  
ATOM   6661  O   PHE B 364      96.731 144.208 140.549  1.00 11.26           O  
ATOM   6662  CB  PHE B 364      99.734 145.741 140.459  1.00 11.26           C  
ATOM   6663  CG  PHE B 364     101.116 145.726 139.875  1.00 11.26           C  
ATOM   6664  CD1 PHE B 364     102.227 145.621 140.687  1.00 11.26           C  
ATOM   6665  CD2 PHE B 364     101.301 145.800 138.510  1.00 11.26           C  
ATOM   6666  CE1 PHE B 364     103.493 145.600 140.147  1.00 11.26           C  
ATOM   6667  CE2 PHE B 364     102.563 145.779 137.970  1.00 11.26           C  
ATOM   6668  CZ  PHE B 364     103.659 145.678 138.789  1.00 11.26           C  
ATOM   6669  N   LEU B 365      97.660 144.785 142.518  1.00 12.04           N  
ATOM   6670  CA  LEU B 365      96.381 144.873 143.220  1.00 12.04           C  
ATOM   6671  C   LEU B 365      95.712 146.215 142.931  1.00 12.04           C  
ATOM   6672  O   LEU B 365      96.310 147.260 143.203  1.00 12.04           O  
ATOM   6673  CB  LEU B 365      96.575 144.703 144.721  1.00 12.04           C  
ATOM   6674  CG  LEU B 365      95.295 144.631 145.559  1.00 12.04           C  
ATOM   6675  CD1 LEU B 365      94.515 143.354 145.309  1.00 12.04           C  
ATOM   6676  CD2 LEU B 365      95.626 144.764 147.029  1.00 12.04           C  
ATOM   6677  N   PRO B 366      94.495 146.239 142.390  1.00 16.23           N  
ATOM   6678  CA  PRO B 366      93.831 147.517 142.113  1.00 16.23           C  
ATOM   6679  C   PRO B 366      93.169 148.120 143.344  1.00 16.23           C  
ATOM   6680  O   PRO B 366      92.887 147.447 144.336  1.00 16.23           O  
ATOM   6681  CB  PRO B 366      92.771 147.158 141.063  1.00 16.23           C  
ATOM   6682  CG  PRO B 366      93.015 145.746 140.685  1.00 16.23           C  
ATOM   6683  CD  PRO B 366      93.747 145.113 141.812  1.00 16.23           C  
ATOM   6684  N   GLY B 367      92.910 149.419 143.249  1.00 15.73           N  
ATOM   6685  CA  GLY B 367      92.122 150.131 144.240  1.00 15.73           C  
ATOM   6686  C   GLY B 367      92.727 151.441 144.704  1.00 15.73           C  
ATOM   6687  O   GLY B 367      93.943 151.642 144.670  1.00 15.73           O  
ATOM   6688  N   THR B 368      91.856 152.348 145.151  1.00 15.54           N  
ATOM   6689  CA  THR B 368      92.305 153.628 145.686  1.00 15.54           C  
ATOM   6690  C   THR B 368      93.206 153.453 146.901  1.00 15.54           C  
ATOM   6691  O   THR B 368      94.085 154.286 147.143  1.00 15.54           O  
ATOM   6692  CB  THR B 368      91.100 154.495 146.056  1.00 15.54           C  
ATOM   6693  OG1 THR B 368      90.347 153.849 147.087  1.00 15.54           O  
ATOM   6694  CG2 THR B 368      90.214 154.726 144.845  1.00 15.54           C  
ATOM   6695  N   ALA B 369      92.998 152.395 147.684  1.00 12.87           N  
ATOM   6696  CA  ALA B 369      93.852 152.157 148.844  1.00 12.87           C  
ATOM   6697  C   ALA B 369      95.314 152.021 148.431  1.00 12.87           C  
ATOM   6698  O   ALA B 369      96.192 152.682 148.995  1.00 12.87           O  
ATOM   6699  CB  ALA B 369      93.378 150.916 149.597  1.00 12.87           C  
ATOM   6700  N   GLN B 370      95.593 151.171 147.439  1.00 11.40           N  
ATOM   6701  CA  GLN B 370      96.968 150.998 146.972  1.00 11.40           C  
ATOM   6702  C   GLN B 370      97.539 152.295 146.408  1.00 11.40           C  
ATOM   6703  O   GLN B 370      98.703 152.627 146.659  1.00 11.40           O  
ATOM   6704  CB  GLN B 370      97.036 149.894 145.914  1.00 11.40           C  
ATOM   6705  CG  GLN B 370      96.975 148.472 146.443  1.00 11.40           C  
ATOM   6706  CD  GLN B 370      98.122 148.117 147.375  1.00 11.40           C  
ATOM   6707  OE1 GLN B 370      99.286 148.110 146.980  1.00 11.40           O  
ATOM   6708  NE2 GLN B 370      97.789 147.810 148.617  1.00 11.40           N  
ATOM   6709  N   GLU B 371      96.746 153.036 145.630  1.00 13.59           N  
ATOM   6710  CA  GLU B 371      97.269 154.233 144.977  1.00 13.59           C  
ATOM   6711  C   GLU B 371      97.575 155.330 145.990  1.00 13.59           C  
ATOM   6712  O   GLU B 371      98.610 155.999 145.891  1.00 13.59           O  
ATOM   6713  CB  GLU B 371      96.285 154.737 143.918  1.00 13.59           C  
ATOM   6714  CG  GLU B 371      96.052 153.783 142.756  1.00 13.59           C  
ATOM   6715  CD  GLU B 371      97.304 153.494 141.939  1.00 13.59           C  
ATOM   6716  OE1 GLU B 371      98.317 154.204 142.109  1.00 13.59           O  
ATOM   6717  OE2 GLU B 371      97.268 152.558 141.116  1.00 13.59           O  
ATOM   6718  N   TYR B 372      96.692 155.530 146.972  1.00 13.28           N  
ATOM   6719  CA  TYR B 372      96.921 156.548 147.989  1.00 13.28           C  
ATOM   6720  C   TYR B 372      98.027 156.152 148.960  1.00 13.28           C  
ATOM   6721  O   TYR B 372      98.617 157.030 149.596  1.00 13.28           O  
ATOM   6722  CB  TYR B 372      95.627 156.827 148.764  1.00 13.28           C  
ATOM   6723  CG  TYR B 372      94.468 157.356 147.940  1.00 13.28           C  
ATOM   6724  CD1 TYR B 372      94.619 157.674 146.599  1.00 13.28           C  
ATOM   6725  CD2 TYR B 372      93.218 157.537 148.513  1.00 13.28           C  
ATOM   6726  CE1 TYR B 372      93.563 158.154 145.858  1.00 13.28           C  
ATOM   6727  CE2 TYR B 372      92.157 158.018 147.776  1.00 13.28           C  
ATOM   6728  CZ  TYR B 372      92.335 158.323 146.449  1.00 13.28           C  
ATOM   6729  OH  TYR B 372      91.288 158.803 145.703  1.00 13.28           O  
ATOM   6730  N   GLY B 373      98.322 154.861 149.086  1.00 12.11           N  
ATOM   6731  CA  GLY B 373      99.406 154.376 149.913  1.00 12.11           C  
ATOM   6732  C   GLY B 373     100.773 154.400 149.272  1.00 12.11           C  
ATOM   6733  O   GLY B 373     101.759 154.068 149.934  1.00 12.11           O  
ATOM   6734  N   GLY B 374     100.867 154.770 148.002  1.00  9.31           N  
ATOM   6735  CA  GLY B 374     102.137 154.950 147.340  1.00  9.31           C  
ATOM   6736  C   GLY B 374     102.650 153.772 146.542  1.00  9.31           C  
ATOM   6737  O   GLY B 374     103.869 153.598 146.453  1.00  9.31           O  
ATOM   6738  N   LEU B 375     101.768 152.965 145.949  1.00  8.41           N  
ATOM   6739  CA  LEU B 375     102.218 151.766 145.251  1.00  8.41           C  
ATOM   6740  C   LEU B 375     103.193 152.094 144.127  1.00  8.41           C  
ATOM   6741  O   LEU B 375     104.019 151.253 143.766  1.00  8.41           O  
ATOM   6742  CB  LEU B 375     101.020 150.989 144.703  1.00  8.41           C  
ATOM   6743  CG  LEU B 375     101.326 149.755 143.850  1.00  8.41           C  
ATOM   6744  CD1 LEU B 375     102.165 148.748 144.628  1.00  8.41           C  
ATOM   6745  CD2 LEU B 375     100.054 149.111 143.349  1.00  8.41           C  
ATOM   6746  N   ILE B 376     103.133 153.309 143.580  1.00  8.62           N  
ATOM   6747  CA  ILE B 376     104.019 153.675 142.475  1.00  8.62           C  
ATOM   6748  C   ILE B 376     105.484 153.547 142.892  1.00  8.62           C  
ATOM   6749  O   ILE B 376     106.331 153.119 142.101  1.00  8.62           O  
ATOM   6750  CB  ILE B 376     103.679 155.092 141.964  1.00  8.62           C  
ATOM   6751  CG1 ILE B 376     102.410 155.052 141.099  1.00  8.62           C  
ATOM   6752  CG2 ILE B 376     104.831 155.682 141.153  1.00  8.62           C  
ATOM   6753  CD1 ILE B 376     101.780 156.402 140.818  1.00  8.62           C  
ATOM   6754  N   LYS B 377     105.807 153.906 144.136  1.00 10.16           N  
ATOM   6755  CA  LYS B 377     107.191 153.873 144.607  1.00 10.16           C  
ATOM   6756  C   LYS B 377     107.538 152.566 145.329  1.00 10.16           C  
ATOM   6757  O   LYS B 377     108.627 152.000 145.119  1.00 10.16           O  
ATOM   6758  CB  LYS B 377     107.453 155.089 145.508  1.00 10.16           C  
ATOM   6759  CG  LYS B 377     107.855 156.342 144.722  1.00 10.16           C  
ATOM   6760  CD  LYS B 377     108.362 157.464 145.608  1.00 10.16           C  
ATOM   6761  CE  LYS B 377     108.451 158.780 144.851  1.00 10.16           C  
ATOM   6762  NZ  LYS B 377     108.738 159.921 145.753  1.00 10.16           N  
ATOM   6763  N   HIS B 378     106.629 152.073 146.173  1.00  9.65           N  
ATOM   6764  CA  HIS B 378     106.833 150.777 146.809  1.00  9.65           C  
ATOM   6765  C   HIS B 378     107.056 149.687 145.767  1.00  9.65           C  
ATOM   6766  O   HIS B 378     107.941 148.841 145.923  1.00  9.65           O  
ATOM   6767  CB  HIS B 378     105.640 150.440 147.705  1.00  9.65           C  
ATOM   6768  CG  HIS B 378     105.400 151.437 148.794  1.00  9.65           C  
ATOM   6769  ND1 HIS B 378     106.419 151.986 149.539  1.00  9.65           N  
ATOM   6770  CD2 HIS B 378     104.256 151.986 149.263  1.00  9.65           C  
ATOM   6771  CE1 HIS B 378     105.915 152.829 150.420  1.00  9.65           C  
ATOM   6772  NE2 HIS B 378     104.604 152.847 150.274  1.00  9.65           N  
ATOM   6773  N   GLY B 379     106.284 149.710 144.680  1.00 10.36           N  
ATOM   6774  CA  GLY B 379     106.477 148.729 143.628  1.00 10.36           C  
ATOM   6775  C   GLY B 379     107.822 148.867 142.942  1.00 10.36           C  
ATOM   6776  O   GLY B 379     108.434 147.873 142.547  1.00 10.36           O  
ATOM   6777  N   ALA B 380     108.301 150.101 142.792  1.00  8.20           N  
ATOM   6778  CA  ALA B 380     109.578 150.338 142.135  1.00  8.20           C  
ATOM   6779  C   ALA B 380     110.758 149.867 142.972  1.00  8.20           C  
ATOM   6780  O   ALA B 380     111.837 149.633 142.418  1.00  8.20           O  
ATOM   6781  CB  ALA B 380     109.744 151.820 141.822  1.00  8.20           C  
ATOM   6782  N   LYS B 381     110.593 149.777 144.291  1.00  8.09           N  
ATOM   6783  CA  LYS B 381     111.697 149.303 145.130  1.00  8.09           C  
ATOM   6784  C   LYS B 381     112.187 147.917 144.702  1.00  8.09           C  
ATOM   6785  O   LYS B 381     113.397 147.672 144.647  1.00  8.09           O  
ATOM   6786  CB  LYS B 381     111.279 149.292 146.598  1.00  8.09           C  
ATOM   6787  CG  LYS B 381     110.914 150.662 147.151  1.00  8.09           C  
ATOM   6788  CD  LYS B 381     110.280 150.574 148.515  1.00  8.09           C  
ATOM   6789  CE  LYS B 381     110.013 151.950 149.096  1.00  8.09           C  
ATOM   6790  NZ  LYS B 381     109.562 151.874 150.501  1.00  8.09           N  
ATOM   6791  N   LEU B 382     111.267 146.996 144.395  1.00 12.77           N  
ATOM   6792  CA  LEU B 382     111.660 145.643 143.984  1.00 12.77           C  
ATOM   6793  C   LEU B 382     112.355 145.645 142.624  1.00 12.77           C  
ATOM   6794  O   LEU B 382     113.359 144.944 142.426  1.00 12.77           O  
ATOM   6795  CB  LEU B 382     110.434 144.722 143.957  1.00 12.77           C  
ATOM   6796  CG  LEU B 382     110.651 143.222 143.729  1.00 12.77           C  
ATOM   6797  CD1 LEU B 382     111.698 142.658 144.674  1.00 12.77           C  
ATOM   6798  CD2 LEU B 382     109.337 142.455 143.851  1.00 12.77           C  
ATOM   6799  N   LEU B 383     111.813 146.404 141.670  1.00  8.04           N  
ATOM   6800  CA  LEU B 383     112.449 146.572 140.368  1.00  8.04           C  
ATOM   6801  C   LEU B 383     113.883 147.066 140.530  1.00  8.04           C  
ATOM   6802  O   LEU B 383     114.823 146.515 139.945  1.00  8.04           O  
ATOM   6803  CB  LEU B 383     111.616 147.550 139.531  1.00  8.04           C  
ATOM   6804  CG  LEU B 383     112.079 147.946 138.131  1.00  8.04           C  
ATOM   6805  CD1 LEU B 383     112.137 146.757 137.214  1.00  8.04           C  
ATOM   6806  CD2 LEU B 383     111.160 149.018 137.554  1.00  8.04           C  
ATOM   6807  N   PHE B 384     114.053 148.109 141.341  1.00  7.95           N  
ATOM   6808  CA  PHE B 384     115.367 148.665 141.649  1.00  7.95           C  
ATOM   6809  C   PHE B 384     116.296 147.600 142.229  1.00  7.95           C  
ATOM   6810  O   PHE B 384     117.434 147.431 141.770  1.00  7.95           O  
ATOM   6811  CB  PHE B 384     115.171 149.841 142.614  1.00  7.95           C  
ATOM   6812  CG  PHE B 384     116.313 150.817 142.662  1.00  7.95           C  
ATOM   6813  CD1 PHE B 384     117.505 150.477 143.250  1.00  7.95           C  
ATOM   6814  CD2 PHE B 384     116.174 152.092 142.149  1.00  7.95           C  
ATOM   6815  CE1 PHE B 384     118.541 151.375 143.308  1.00  7.95           C  
ATOM   6816  CE2 PHE B 384     117.211 152.992 142.204  1.00  7.95           C  
ATOM   6817  CZ  PHE B 384     118.389 152.633 142.785  1.00  7.95           C  
ATOM   6818  N   ALA B 385     115.813 146.850 143.225  1.00 12.77           N  
ATOM   6819  CA  ALA B 385     116.650 145.852 143.888  1.00 12.77           C  
ATOM   6820  C   ALA B 385     117.142 144.798 142.904  1.00 12.77           C  
ATOM   6821  O   ALA B 385     118.327 144.450 142.894  1.00 12.77           O  
ATOM   6822  CB  ALA B 385     115.887 145.193 145.038  1.00 12.77           C  
ATOM   6823  N   TYR B 386     116.242 144.271 142.070  1.00 12.77           N  
ATOM   6824  CA  TYR B 386     116.651 143.256 141.100  1.00 12.77           C  
ATOM   6825  C   TYR B 386     117.594 143.831 140.043  1.00 12.77           C  
ATOM   6826  O   TYR B 386     118.556 143.167 139.640  1.00 12.77           O  
ATOM   6827  CB  TYR B 386     115.432 142.636 140.423  1.00 12.77           C  
ATOM   6828  CG  TYR B 386     114.814 141.442 141.126  1.00 12.77           C  
ATOM   6829  CD1 TYR B 386     115.554 140.305 141.410  1.00 12.77           C  
ATOM   6830  CD2 TYR B 386     113.478 141.440 141.471  1.00 12.77           C  
ATOM   6831  CE1 TYR B 386     114.978 139.218 142.038  1.00 12.77           C  
ATOM   6832  CE2 TYR B 386     112.900 140.362 142.096  1.00 12.77           C  
ATOM   6833  CZ  TYR B 386     113.647 139.254 142.375  1.00 12.77           C  
ATOM   6834  OH  TYR B 386     113.051 138.184 143.001  1.00 12.77           O  
ATOM   6835  N   SER B 387     117.336 145.054 139.574  1.00  8.18           N  
ATOM   6836  CA  SER B 387     118.150 145.632 138.508  1.00  8.18           C  
ATOM   6837  C   SER B 387     119.538 146.032 138.986  1.00  8.18           C  
ATOM   6838  O   SER B 387     120.449 146.157 138.163  1.00  8.18           O  
ATOM   6839  CB  SER B 387     117.440 146.844 137.902  1.00  8.18           C  
ATOM   6840  OG  SER B 387     116.235 146.465 137.272  1.00  8.18           O  
ATOM   6841  N   GLN B 388     119.712 146.243 140.288  1.00  8.16           N  
ATOM   6842  CA  GLN B 388     121.010 146.580 140.857  1.00  8.16           C  
ATOM   6843  C   GLN B 388     121.866 145.355 141.171  1.00  8.16           C  
ATOM   6844  O   GLN B 388     123.085 145.492 141.307  1.00  8.16           O  
ATOM   6845  CB  GLN B 388     120.766 147.418 142.111  1.00  8.16           C  
ATOM   6846  CG  GLN B 388     121.890 147.641 143.045  1.00  8.16           C  
ATOM   6847  CD  GLN B 388     121.426 148.491 144.205  1.00  8.16           C  
ATOM   6848  OE1 GLN B 388     120.513 148.112 144.937  1.00  8.16           O  
ATOM   6849  NE2 GLN B 388     122.016 149.658 144.351  1.00  8.16           N  
ATOM   6850  N   ALA B 389     121.266 144.171 141.260  1.00  8.88           N  
ATOM   6851  CA  ALA B 389     121.968 142.987 141.737  1.00  8.88           C  
ATOM   6852  C   ALA B 389     123.049 142.523 140.764  1.00  8.88           C  
ATOM   6853  O   ALA B 389     122.885 142.589 139.544  1.00  8.88           O  
ATOM   6854  CB  ALA B 389     120.976 141.854 141.978  1.00  8.88           C  
ATOM   6855  N   THR B 390     124.161 142.044 141.324  1.00  9.61           N  
ATOM   6856  CA  THR B 390     125.254 141.448 140.567  1.00  9.61           C  
ATOM   6857  C   THR B 390     125.542 140.001 140.950  1.00  9.61           C  
ATOM   6858  O   THR B 390     126.464 139.401 140.389  1.00  9.61           O  
ATOM   6859  CB  THR B 390     126.530 142.280 140.743  1.00  9.61           C  
ATOM   6860  OG1 THR B 390     126.848 142.376 142.133  1.00  9.61           O  
ATOM   6861  CG2 THR B 390     126.348 143.673 140.168  1.00  9.61           C  
ATOM   6862  N   VAL B 391     124.796 139.429 141.889  1.00  6.11           N  
ATOM   6863  CA  VAL B 391     124.891 138.010 142.226  1.00  6.11           C  
ATOM   6864  C   VAL B 391     124.183 137.220 141.130  1.00  6.11           C  
ATOM   6865  O   VAL B 391     123.423 137.807 140.349  1.00  6.11           O  
ATOM   6866  CB  VAL B 391     124.281 137.710 143.609  1.00  6.11           C  
ATOM   6867  CG1 VAL B 391     125.126 138.310 144.724  1.00  6.11           C  
ATOM   6868  CG2 VAL B 391     122.832 138.189 143.686  1.00  6.11           C  
ATOM   6869  N   PRO B 392     124.394 135.908 141.026  1.00  6.02           N  
ATOM   6870  CA  PRO B 392     123.631 135.124 140.049  1.00  6.02           C  
ATOM   6871  C   PRO B 392     122.132 135.193 140.318  1.00  6.02           C  
ATOM   6872  O   PRO B 392     121.686 135.161 141.464  1.00  6.02           O  
ATOM   6873  CB  PRO B 392     124.176 133.705 140.235  1.00  6.02           C  
ATOM   6874  CG  PRO B 392     125.514 133.888 140.805  1.00  6.02           C  
ATOM   6875  CD  PRO B 392     125.416 135.085 141.690  1.00  6.02           C  
ATOM   6876  N   LEU B 393     121.362 135.295 139.236  1.00  4.97           N  
ATOM   6877  CA  LEU B 393     119.902 135.345 139.272  1.00  4.97           C  
ATOM   6878  C   LEU B 393     119.346 134.260 138.357  1.00  4.97           C  
ATOM   6879  O   LEU B 393     119.640 134.261 137.158  1.00  4.97           O  
ATOM   6880  CB  LEU B 393     119.388 136.719 138.825  1.00  4.97           C  
ATOM   6881  CG  LEU B 393     119.700 137.957 139.665  1.00  4.97           C  
ATOM   6882  CD1 LEU B 393     119.135 139.201 138.992  1.00  4.97           C  
ATOM   6883  CD2 LEU B 393     119.168 137.832 141.076  1.00  4.97           C  
ATOM   6884  N   VAL B 394     118.546 133.341 138.907  1.00  5.62           N  
ATOM   6885  CA  VAL B 394     117.889 132.299 138.112  1.00  5.62           C  
ATOM   6886  C   VAL B 394     116.380 132.390 138.330  1.00  5.62           C  
ATOM   6887  O   VAL B 394     115.917 132.443 139.474  1.00  5.62           O  
ATOM   6888  CB  VAL B 394     118.414 130.889 138.448  1.00  5.62           C  
ATOM   6889  CG1 VAL B 394     117.594 129.813 137.743  1.00  5.62           C  
ATOM   6890  CG2 VAL B 394     119.879 130.757 138.065  1.00  5.62           C  
ATOM   6891  N   THR B 395     115.618 132.399 137.232  1.00  4.96           N  
ATOM   6892  CA  THR B 395     114.182 132.657 137.250  1.00  4.96           C  
ATOM   6893  C   THR B 395     113.432 131.553 136.510  1.00  4.96           C  
ATOM   6894  O   THR B 395     113.879 131.084 135.459  1.00  4.96           O  
ATOM   6895  CB  THR B 395     113.875 134.028 136.622  1.00  4.96           C  
ATOM   6896  OG1 THR B 395     114.613 135.043 137.310  1.00  4.96           O  
ATOM   6897  CG2 THR B 395     112.392 134.360 136.684  1.00  4.96           C  
ATOM   6898  N   ILE B 396     112.286 131.147 137.061  1.00  4.47           N  
ATOM   6899  CA  ILE B 396     111.451 130.082 136.507  1.00  4.47           C  
ATOM   6900  C   ILE B 396     109.993 130.546 136.507  1.00  4.47           C  
ATOM   6901  O   ILE B 396     109.431 130.846 137.569  1.00  4.47           O  
ATOM   6902  CB  ILE B 396     111.594 128.764 137.291  1.00  4.47           C  
ATOM   6903  CG1 ILE B 396     113.070 128.335 137.416  1.00  4.47           C  
ATOM   6904  CG2 ILE B 396     110.750 127.660 136.652  1.00  4.47           C  
ATOM   6905  CD1 ILE B 396     113.772 128.864 138.660  1.00  4.47           C  
ATOM   6906  N   ILE B 397     109.388 130.603 135.320  1.00  5.89           N  
ATOM   6907  CA  ILE B 397     107.977 130.948 135.155  1.00  5.89           C  
ATOM   6908  C   ILE B 397     107.178 129.648 135.112  1.00  5.89           C  
ATOM   6909  O   ILE B 397     107.304 128.858 134.175  1.00  5.89           O  
ATOM   6910  CB  ILE B 397     107.731 131.785 133.891  1.00  5.89           C  
ATOM   6911  CG1 ILE B 397     108.522 133.098 133.933  1.00  5.89           C  
ATOM   6912  CG2 ILE B 397     106.242 132.066 133.730  1.00  5.89           C  
ATOM   6913  CD1 ILE B 397     108.460 133.924 132.667  1.00  5.89           C  
ATOM   6914  N   THR B 398     106.340 129.435 136.122  1.00  7.55           N  
ATOM   6915  CA  THR B 398     105.485 128.255 136.189  1.00  7.55           C  
ATOM   6916  C   THR B 398     104.128 128.469 135.534  1.00  7.55           C  
ATOM   6917  O   THR B 398     103.563 127.527 134.971  1.00  7.55           O  
ATOM   6918  CB  THR B 398     105.269 127.841 137.649  1.00  7.55           C  
ATOM   6919  OG1 THR B 398     104.698 128.931 138.380  1.00  7.55           O  
ATOM   6920  CG2 THR B 398     106.573 127.431 138.297  1.00  7.55           C  
ATOM   6921  N   ARG B 399     103.594 129.684 135.615  1.00 14.95           N  
ATOM   6922  CA  ARG B 399     102.250 130.014 135.163  1.00 14.95           C  
ATOM   6923  C   ARG B 399     102.246 131.480 134.745  1.00 14.95           C  
ATOM   6924  O   ARG B 399     103.272 132.002 134.299  1.00 14.95           O  
ATOM   6925  CB  ARG B 399     101.208 129.705 136.242  1.00 14.95           C  
ATOM   6926  CG  ARG B 399      99.831 129.380 135.692  1.00 14.95           C  
ATOM   6927  CD  ARG B 399      98.772 129.269 136.783  1.00 14.95           C  
ATOM   6928  NE  ARG B 399      97.833 128.193 136.501  1.00 14.95           N  
ATOM   6929  CZ  ARG B 399      96.849 127.822 137.313  1.00 14.95           C  
ATOM   6930  NH1 ARG B 399      96.668 128.432 138.474  1.00 14.95           N  
ATOM   6931  NH2 ARG B 399      96.043 126.831 136.962  1.00 14.95           N  
ATOM   6932  N   LYS B 400     101.093 132.130 134.826  1.00 12.18           N  
ATOM   6933  CA  LYS B 400     100.914 133.460 134.262  1.00 12.18           C  
ATOM   6934  C   LYS B 400     102.056 134.405 134.612  1.00 12.18           C  
ATOM   6935  O   LYS B 400     102.663 134.321 135.683  1.00 12.18           O  
ATOM   6936  CB  LYS B 400      99.599 134.052 134.761  1.00 12.18           C  
ATOM   6937  CG  LYS B 400      98.380 133.443 134.125  1.00 12.18           C  
ATOM   6938  CD  LYS B 400      97.416 132.979 135.182  1.00 12.18           C  
ATOM   6939  CE  LYS B 400      96.757 134.153 135.871  1.00 12.18           C  
ATOM   6940  NZ  LYS B 400      95.638 133.728 136.755  1.00 12.18           N  
ATOM   6941  N   ALA B 401     102.339 135.308 133.678  1.00  9.72           N  
ATOM   6942  CA  ALA B 401     103.247 136.429 133.895  1.00  9.72           C  
ATOM   6943  C   ALA B 401     102.791 137.542 132.954  1.00  9.72           C  
ATOM   6944  O   ALA B 401     103.134 137.531 131.770  1.00  9.72           O  
ATOM   6945  CB  ALA B 401     104.689 136.023 133.638  1.00  9.72           C  
ATOM   6946  N   PHE B 402     102.021 138.490 133.484  1.00 10.28           N  
ATOM   6947  CA  PHE B 402     101.392 139.533 132.687  1.00 10.28           C  
ATOM   6948  C   PHE B 402     102.045 140.885 132.950  1.00 10.28           C  
ATOM   6949  O   PHE B 402     102.144 141.322 134.100  1.00 10.28           O  
ATOM   6950  CB  PHE B 402      99.892 139.632 132.981  1.00 10.28           C  
ATOM   6951  CG  PHE B 402      99.088 138.423 132.569  1.00 10.28           C  
ATOM   6952  CD1 PHE B 402      99.590 137.478 131.694  1.00 10.28           C  
ATOM   6953  CD2 PHE B 402      97.812 138.241 133.064  1.00 10.28           C  
ATOM   6954  CE1 PHE B 402      98.830 136.375 131.328  1.00 10.28           C  
ATOM   6955  CE2 PHE B 402      97.056 137.143 132.700  1.00 10.28           C  
ATOM   6956  CZ  PHE B 402      97.569 136.213 131.833  1.00 10.28           C  
ATOM   6957  N   GLY B 403     102.472 141.536 131.873  1.00  9.67           N  
ATOM   6958  CA  GLY B 403     102.837 142.943 131.883  1.00  9.67           C  
ATOM   6959  C   GLY B 403     103.966 143.335 132.818  1.00  9.67           C  
ATOM   6960  O   GLY B 403     104.994 142.647 132.965  1.00  9.67           O  
ATOM   6961  N   GLY B 404     103.780 144.506 133.430  1.00  9.36           N  
ATOM   6962  CA  GLY B 404     104.803 145.062 134.292  1.00  9.36           C  
ATOM   6963  C   GLY B 404     105.236 144.103 135.378  1.00  9.36           C  
ATOM   6964  O   GLY B 404     106.406 144.071 135.761  1.00  9.36           O  
ATOM   6965  N   ALA B 405     104.298 143.311 135.896  1.00  8.38           N  
ATOM   6966  CA  ALA B 405     104.653 142.321 136.905  1.00  8.38           C  
ATOM   6967  C   ALA B 405     105.642 141.305 136.347  1.00  8.38           C  
ATOM   6968  O   ALA B 405     106.576 140.893 137.042  1.00  8.38           O  
ATOM   6969  CB  ALA B 405     103.398 141.630 137.433  1.00  8.38           C  
ATOM   6970  N   TYR B 406     105.455 140.894 135.091  1.00  7.16           N  
ATOM   6971  CA  TYR B 406     106.438 140.034 134.442  1.00  7.16           C  
ATOM   6972  C   TYR B 406     107.794 140.717 134.370  1.00  7.16           C  
ATOM   6973  O   TYR B 406     108.829 140.081 134.595  1.00  7.16           O  
ATOM   6974  CB  TYR B 406     105.966 139.638 133.040  1.00  7.16           C  
ATOM   6975  CG  TYR B 406     107.085 139.378 132.054  1.00  7.16           C  
ATOM   6976  CD1 TYR B 406     107.801 138.189 132.079  1.00  7.16           C  
ATOM   6977  CD2 TYR B 406     107.421 140.318 131.099  1.00  7.16           C  
ATOM   6978  CE1 TYR B 406     108.817 137.953 131.184  1.00  7.16           C  
ATOM   6979  CE2 TYR B 406     108.432 140.091 130.201  1.00  7.16           C  
ATOM   6980  CZ  TYR B 406     109.127 138.908 130.243  1.00  7.16           C  
ATOM   6981  OH  TYR B 406     110.136 138.705 129.341  1.00  7.16           O  
ATOM   6982  N   ILE B 407     107.815 142.009 134.038  1.00  7.03           N  
ATOM   6983  CA  ILE B 407     109.100 142.709 133.970  1.00  7.03           C  
ATOM   6984  C   ILE B 407     109.780 142.704 135.339  1.00  7.03           C  
ATOM   6985  O   ILE B 407     110.974 142.409 135.458  1.00  7.03           O  
ATOM   6986  CB  ILE B 407     108.925 144.142 133.434  1.00  7.03           C  
ATOM   6987  CG1 ILE B 407     108.300 144.138 132.037  1.00  7.03           C  
ATOM   6988  CG2 ILE B 407     110.272 144.856 133.373  1.00  7.03           C  
ATOM   6989  CD1 ILE B 407     107.893 145.508 131.558  1.00  7.03           C  
ATOM   6990  N   VAL B 408     109.017 143.008 136.392  1.00  7.18           N  
ATOM   6991  CA  VAL B 408     109.582 143.228 137.724  1.00  7.18           C  
ATOM   6992  C   VAL B 408     110.181 141.949 138.308  1.00  7.18           C  
ATOM   6993  O   VAL B 408     111.172 142.010 139.043  1.00  7.18           O  
ATOM   6994  CB  VAL B 408     108.504 143.829 138.655  1.00  7.18           C  
ATOM   6995  CG1 VAL B 408     108.953 143.841 140.112  1.00  7.18           C  
ATOM   6996  CG2 VAL B 408     108.116 145.244 138.200  1.00  7.18           C  
ATOM   6997  N   MET B 409     109.604 140.781 138.007  1.00  6.71           N  
ATOM   6998  CA  MET B 409     109.981 139.517 138.651  1.00  6.71           C  
ATOM   6999  C   MET B 409     111.198 138.889 137.957  1.00  6.71           C  
ATOM   7000  O   MET B 409     111.129 137.831 137.331  1.00  6.71           O  
ATOM   7001  CB  MET B 409     108.802 138.553 138.656  1.00  6.71           C  
ATOM   7002  CG  MET B 409     107.655 138.929 139.576  1.00  6.71           C  
ATOM   7003  SD  MET B 409     108.102 139.202 141.301  1.00  6.71           S  
ATOM   7004  CE  MET B 409     108.640 137.571 141.804  1.00  6.71           C  
ATOM   7005  N   ALA B 410     112.337 139.564 138.096  1.00  6.63           N  
ATOM   7006  CA  ALA B 410     113.641 139.021 137.707  1.00  6.63           C  
ATOM   7007  C   ALA B 410     113.654 138.546 136.250  1.00  6.63           C  
ATOM   7008  O   ALA B 410     114.061 137.426 135.938  1.00  6.63           O  
ATOM   7009  CB  ALA B 410     114.061 137.894 138.656  1.00  6.63           C  
ATOM   7010  N   SER B 411     113.217 139.420 135.347  1.00  6.37           N  
ATOM   7011  CA  SER B 411     113.219 139.136 133.919  1.00  6.37           C  
ATOM   7012  C   SER B 411     114.597 139.385 133.303  1.00  6.37           C  
ATOM   7013  O   SER B 411     115.423 140.131 133.833  1.00  6.37           O  
ATOM   7014  CB  SER B 411     112.180 139.995 133.206  1.00  6.37           C  
ATOM   7015  OG  SER B 411     112.359 141.361 133.504  1.00  6.37           O  
ATOM   7016  N   LYS B 412     114.828 138.742 132.154  1.00  7.99           N  
ATOM   7017  CA  LYS B 412     116.053 138.964 131.390  1.00  7.99           C  
ATOM   7018  C   LYS B 412     116.288 140.445 131.113  1.00  7.99           C  
ATOM   7019  O   LYS B 412     117.438 140.891 131.064  1.00  7.99           O  
ATOM   7020  CB  LYS B 412     116.002 138.179 130.071  1.00  7.99           C  
ATOM   7021  CG  LYS B 412     117.367 137.972 129.413  1.00  7.99           C  
ATOM   7022  CD  LYS B 412     117.376 136.868 128.361  1.00  7.99           C  
ATOM   7023  CE  LYS B 412     117.304 135.467 128.946  1.00  7.99           C  
ATOM   7024  NZ  LYS B 412     118.381 135.183 129.926  1.00  7.99           N  
ATOM   7025  N   HIS B 413     115.215 141.223 130.959  1.00  8.54           N  
ATOM   7026  CA  HIS B 413     115.357 142.624 130.575  1.00  8.54           C  
ATOM   7027  C   HIS B 413     115.979 143.460 131.686  1.00  8.54           C  
ATOM   7028  O   HIS B 413     116.604 144.488 131.402  1.00  8.54           O  
ATOM   7029  CB  HIS B 413     113.998 143.201 130.174  1.00  8.54           C  
ATOM   7030  CG  HIS B 413     113.130 142.237 129.430  1.00  8.54           C  
ATOM   7031  ND1 HIS B 413     113.354 141.896 128.115  1.00  8.54           N  
ATOM   7032  CD2 HIS B 413     112.057 141.515 129.826  1.00  8.54           C  
ATOM   7033  CE1 HIS B 413     112.447 141.018 127.730  1.00  8.54           C  
ATOM   7034  NE2 HIS B 413     111.651 140.767 128.751  1.00  8.54           N  
ATOM   7035  N   VAL B 414     115.825 143.053 132.947  1.00  8.34           N  
ATOM   7036  CA  VAL B 414     116.427 143.785 134.057  1.00  8.34           C  
ATOM   7037  C   VAL B 414     117.703 143.115 134.565  1.00  8.34           C  
ATOM   7038  O   VAL B 414     118.285 143.575 135.552  1.00  8.34           O  
ATOM   7039  CB  VAL B 414     115.421 144.008 135.199  1.00  8.34           C  
ATOM   7040  CG1 VAL B 414     114.178 144.722 134.691  1.00  8.34           C  
ATOM   7041  CG2 VAL B 414     115.030 142.715 135.855  1.00  8.34           C  
ATOM   7042  N   GLY B 415     118.153 142.043 133.914  1.00 10.64           N  
ATOM   7043  CA  GLY B 415     119.507 141.554 134.099  1.00 10.64           C  
ATOM   7044  C   GLY B 415     119.656 140.112 134.544  1.00 10.64           C  
ATOM   7045  O   GLY B 415     120.755 139.695 134.917  1.00 10.64           O  
ATOM   7046  N   ALA B 416     118.580 139.333 134.502  1.00  8.50           N  
ATOM   7047  CA  ALA B 416     118.658 137.944 134.929  1.00  8.50           C  
ATOM   7048  C   ALA B 416     119.552 137.139 133.990  1.00  8.50           C  
ATOM   7049  O   ALA B 416     119.553 137.348 132.775  1.00  8.50           O  
ATOM   7050  CB  ALA B 416     117.265 137.328 134.993  1.00  8.50           C  
ATOM   7051  N   ASP B 417     120.318 136.214 134.571  1.00  8.50           N  
ATOM   7052  CA  ASP B 417     121.279 135.417 133.813  1.00  8.50           C  
ATOM   7053  C   ASP B 417     120.598 134.307 133.023  1.00  8.50           C  
ATOM   7054  O   ASP B 417     120.865 134.131 131.830  1.00  8.50           O  
ATOM   7055  CB  ASP B 417     122.326 134.825 134.761  1.00  8.50           C  
ATOM   7056  CG  ASP B 417     123.190 135.888 135.410  1.00  8.50           C  
ATOM   7057  OD1 ASP B 417     124.065 136.446 134.719  1.00  8.50           O  
ATOM   7058  OD2 ASP B 417     122.982 136.177 136.604  1.00  8.50           O  
ATOM   7059  N   LEU B 418     119.737 133.538 133.678  1.00  7.85           N  
ATOM   7060  CA  LEU B 418     119.048 132.407 133.074  1.00  7.85           C  
ATOM   7061  C   LEU B 418     117.556 132.491 133.373  1.00  7.85           C  
ATOM   7062  O   LEU B 418     117.158 132.785 134.503  1.00  7.85           O  
ATOM   7063  CB  LEU B 418     119.627 131.082 133.589  1.00  7.85           C  
ATOM   7064  CG  LEU B 418     120.980 130.649 133.010  1.00  7.85           C  
ATOM   7065  CD1 LEU B 418     121.512 129.437 133.726  1.00  7.85           C  
ATOM   7066  CD2 LEU B 418     120.870 130.354 131.524  1.00  7.85           C  
ATOM   7067  N   ASN B 419     116.737 132.223 132.356  1.00  7.92           N  
ATOM   7068  CA  ASN B 419     115.283 132.354 132.441  1.00  7.92           C  
ATOM   7069  C   ASN B 419     114.654 131.137 131.774  1.00  7.92           C  
ATOM   7070  O   ASN B 419     114.711 131.001 130.549  1.00  7.92           O  
ATOM   7071  CB  ASN B 419     114.793 133.644 131.780  1.00  7.92           C  
ATOM   7072  CG  ASN B 419     115.366 134.896 132.413  1.00  7.92           C  
ATOM   7073  OD1 ASN B 419     116.438 135.360 132.036  1.00  7.92           O  
ATOM   7074  ND2 ASN B 419     114.635 135.467 133.362  1.00  7.92           N  
ATOM   7075  N   TYR B 420     114.060 130.262 132.577  1.00  7.54           N  
ATOM   7076  CA  TYR B 420     113.350 129.080 132.114  1.00  7.54           C  
ATOM   7077  C   TYR B 420     111.839 129.303 132.167  1.00  7.54           C  
ATOM   7078  O   TYR B 420     111.342 130.244 132.788  1.00  7.54           O  
ATOM   7079  CB  TYR B 420     113.722 127.862 132.961  1.00  7.54           C  
ATOM   7080  CG  TYR B 420     115.194 127.508 132.995  1.00  7.54           C  
ATOM   7081  CD1 TYR B 420     115.865 127.130 131.847  1.00  7.54           C  
ATOM   7082  CD2 TYR B 420     115.904 127.523 134.184  1.00  7.54           C  
ATOM   7083  CE1 TYR B 420     117.198 126.796 131.879  1.00  7.54           C  
ATOM   7084  CE2 TYR B 420     117.235 127.189 134.225  1.00  7.54           C  
ATOM   7085  CZ  TYR B 420     117.882 126.828 133.069  1.00  7.54           C  
ATOM   7086  OH  TYR B 420     119.210 126.493 133.107  1.00  7.54           O  
ATOM   7087  N   ALA B 421     111.107 128.405 131.507  1.00  7.05           N  
ATOM   7088  CA  ALA B 421     109.650 128.414 131.521  1.00  7.05           C  
ATOM   7089  C   ALA B 421     109.124 126.987 131.432  1.00  7.05           C  
ATOM   7090  O   ALA B 421     109.654 126.168 130.680  1.00  7.05           O  
ATOM   7091  CB  ALA B 421     109.083 129.250 130.369  1.00  7.05           C  
ATOM   7092  N   TRP B 422     108.091 126.696 132.218  1.00  7.45           N  
ATOM   7093  CA  TRP B 422     107.352 125.448 132.113  1.00  7.45           C  
ATOM   7094  C   TRP B 422     106.404 125.492 130.912  1.00  7.45           C  
ATOM   7095  O   TRP B 422     106.152 126.558 130.348  1.00  7.45           O  
ATOM   7096  CB  TRP B 422     106.573 125.190 133.404  1.00  7.45           C  
ATOM   7097  CG  TRP B 422     107.410 124.754 134.586  1.00  7.45           C  
ATOM   7098  CD1 TRP B 422     108.770 124.733 134.671  1.00  7.45           C  
ATOM   7099  CD2 TRP B 422     106.926 124.274 135.847  1.00  7.45           C  
ATOM   7100  NE1 TRP B 422     109.160 124.273 135.900  1.00  7.45           N  
ATOM   7101  CE2 TRP B 422     108.049 123.980 136.641  1.00  7.45           C  
ATOM   7102  CE3 TRP B 422     105.654 124.062 136.381  1.00  7.45           C  
ATOM   7103  CZ2 TRP B 422     107.936 123.488 137.937  1.00  7.45           C  
ATOM   7104  CZ3 TRP B 422     105.549 123.570 137.666  1.00  7.45           C  
ATOM   7105  CH2 TRP B 422     106.681 123.295 138.429  1.00  7.45           C  
ATOM   7106  N   PRO B 423     105.876 124.337 130.488  1.00  9.46           N  
ATOM   7107  CA  PRO B 423     104.967 124.335 129.327  1.00  9.46           C  
ATOM   7108  C   PRO B 423     103.688 125.121 129.555  1.00  9.46           C  
ATOM   7109  O   PRO B 423     103.113 125.652 128.596  1.00  9.46           O  
ATOM   7110  CB  PRO B 423     104.673 122.843 129.111  1.00  9.46           C  
ATOM   7111  CG  PRO B 423     105.717 122.114 129.854  1.00  9.46           C  
ATOM   7112  CD  PRO B 423     106.102 122.980 131.002  1.00  9.46           C  
ATOM   7113  N   THR B 424     103.220 125.198 130.797  1.00 10.73           N  
ATOM   7114  CA  THR B 424     101.999 125.906 131.160  1.00 10.73           C  
ATOM   7115  C   THR B 424     102.172 127.419 131.240  1.00 10.73           C  
ATOM   7116  O   THR B 424     101.211 128.110 131.589  1.00 10.73           O  
ATOM   7117  CB  THR B 424     101.486 125.386 132.506  1.00 10.73           C  
ATOM   7118  OG1 THR B 424     102.524 125.496 133.486  1.00 10.73           O  
ATOM   7119  CG2 THR B 424     101.019 123.944 132.397  1.00 10.73           C  
ATOM   7120  N   ALA B 425     103.354 127.945 130.938  1.00  9.41           N  
ATOM   7121  CA  ALA B 425     103.609 129.370 131.093  1.00  9.41           C  
ATOM   7122  C   ALA B 425     102.790 130.200 130.106  1.00  9.41           C  
ATOM   7123  O   ALA B 425     102.664 129.853 128.930  1.00  9.41           O  
ATOM   7124  CB  ALA B 425     105.096 129.661 130.905  1.00  9.41           C  
ATOM   7125  N   GLN B 426     102.237 131.305 130.600  1.00 11.64           N  
ATOM   7126  CA  GLN B 426     101.491 132.282 129.808  1.00 11.64           C  
ATOM   7127  C   GLN B 426     102.155 133.649 129.981  1.00 11.64           C  
ATOM   7128  O   GLN B 426     101.993 134.300 131.017  1.00 11.64           O  
ATOM   7129  CB  GLN B 426     100.028 132.313 130.234  1.00 11.64           C  
ATOM   7130  CG  GLN B 426      99.248 131.068 129.874  1.00 11.64           C  
ATOM   7131  CD  GLN B 426      97.837 131.091 130.413  1.00 11.64           C  
ATOM   7132  OE1 GLN B 426      97.488 131.938 131.231  1.00 11.64           O  
ATOM   7133  NE2 GLN B 426      97.015 130.160 129.957  1.00 11.64           N  
ATOM   7134  N   ILE B 427     102.900 134.080 128.967  1.00  9.76           N  
ATOM   7135  CA  ILE B 427     103.681 135.315 128.995  1.00  9.76           C  
ATOM   7136  C   ILE B 427     103.058 136.279 127.988  1.00  9.76           C  
ATOM   7137  O   ILE B 427     103.163 136.068 126.775  1.00  9.76           O  
ATOM   7138  CB  ILE B 427     105.161 135.043 128.680  1.00  9.76           C  
ATOM   7139  CG1 ILE B 427     105.677 133.877 129.533  1.00  9.76           C  
ATOM   7140  CG2 ILE B 427     105.997 136.288 128.904  1.00  9.76           C  
ATOM   7141  CD1 ILE B 427     107.097 133.456 129.243  1.00  9.76           C  
ATOM   7142  N   ALA B 428     102.427 137.348 128.479  1.00 10.99           N  
ATOM   7143  CA  ALA B 428     101.629 138.218 127.619  1.00 10.99           C  
ATOM   7144  C   ALA B 428     101.426 139.583 128.266  1.00 10.99           C  
ATOM   7145  O   ALA B 428     101.615 139.757 129.470  1.00 10.99           O  
ATOM   7146  CB  ALA B 428     100.275 137.577 127.305  1.00 10.99           C  
ATOM   7147  N   VAL B 429     101.031 140.553 127.433  1.00 14.80           N  
ATOM   7148  CA  VAL B 429     100.779 141.911 127.911  1.00 14.80           C  
ATOM   7149  C   VAL B 429      99.598 141.938 128.872  1.00 14.80           C  
ATOM   7150  O   VAL B 429      99.587 142.709 129.838  1.00 14.80           O  
ATOM   7151  CB  VAL B 429     100.561 142.874 126.728  1.00 14.80           C  
ATOM   7152  CG1 VAL B 429     101.828 143.002 125.921  1.00 14.80           C  
ATOM   7153  CG2 VAL B 429      99.400 142.421 125.846  1.00 14.80           C  
ATOM   7154  N   MET B 430      98.586 141.106 128.642  1.00 21.43           N  
ATOM   7155  CA  MET B 430      97.385 141.037 129.509  1.00 21.43           C  
ATOM   7156  C   MET B 430      96.577 139.844 129.031  1.00 21.43           C  
ATOM   7157  O   MET B 430      96.912 139.153 128.065  1.00 21.43           O  
ATOM   7158  CB  MET B 430      96.456 142.270 129.483  1.00 21.43           C  
ATOM   7159  CG  MET B 430      95.898 142.579 128.107  1.00 21.43           C  
ATOM   7160  SD  MET B 430      94.548 143.785 128.161  1.00 21.43           S  
ATOM   7161  CE  MET B 430      95.467 145.299 128.430  1.00 21.43           C  
ATOM   7162  N   GLY B 431      95.493 139.597 129.762  1.00 25.21           N  
ATOM   7163  CA  GLY B 431      94.593 138.518 129.410  1.00 25.21           C  
ATOM   7164  C   GLY B 431      93.884 138.766 128.092  1.00 25.21           C  
ATOM   7165  O   GLY B 431      93.708 139.898 127.643  1.00 25.21           O  
ATOM   7166  N   ALA B 432      93.453 137.663 127.477  1.00 33.64           N  
ATOM   7167  CA  ALA B 432      92.900 137.718 126.126  1.00 33.64           C  
ATOM   7168  C   ALA B 432      91.696 138.651 126.038  1.00 33.64           C  
ATOM   7169  O   ALA B 432      91.586 139.444 125.095  1.00 33.64           O  
ATOM   7170  CB  ALA B 432      92.518 136.311 125.667  1.00 33.64           C  
ATOM   7171  N   LYS B 433      90.777 138.559 127.000  1.00 38.88           N  
ATOM   7172  CA  LYS B 433      89.530 139.313 126.921  1.00 38.88           C  
ATOM   7173  C   LYS B 433      89.795 140.811 126.824  1.00 38.88           C  
ATOM   7174  O   LYS B 433      89.298 141.487 125.916  1.00 38.88           O  
ATOM   7175  CB  LYS B 433      88.653 138.997 128.132  1.00 38.88           C  
ATOM   7176  CG  LYS B 433      87.233 139.522 128.019  1.00 38.88           C  
ATOM   7177  CD  LYS B 433      86.549 139.637 129.375  1.00 38.88           C  
ATOM   7178  CE  LYS B 433      86.766 138.403 130.237  1.00 38.88           C  
ATOM   7179  NZ  LYS B 433      85.981 138.468 131.498  1.00 38.88           N  
ATOM   7180  N   GLY B 434      90.558 141.353 127.773  1.00 38.38           N  
ATOM   7181  CA  GLY B 434      90.860 142.774 127.738  1.00 38.38           C  
ATOM   7182  C   GLY B 434      91.629 143.177 126.496  1.00 38.38           C  
ATOM   7183  O   GLY B 434      91.403 144.254 125.933  1.00 38.38           O  
ATOM   7184  N   ALA B 435      92.554 142.322 126.057  1.00 37.30           N  
ATOM   7185  CA  ALA B 435      93.309 142.611 124.844  1.00 37.30           C  
ATOM   7186  C   ALA B 435      92.378 142.790 123.652  1.00 37.30           C  
ATOM   7187  O   ALA B 435      92.520 143.745 122.882  1.00 37.30           O  
ATOM   7188  CB  ALA B 435      94.325 141.501 124.577  1.00 37.30           C  
ATOM   7189  N   VAL B 436      91.413 141.883 123.485  1.00 42.39           N  
ATOM   7190  CA  VAL B 436      90.505 142.000 122.348  1.00 42.39           C  
ATOM   7191  C   VAL B 436      89.559 143.178 122.538  1.00 42.39           C  
ATOM   7192  O   VAL B 436      89.196 143.853 121.568  1.00 42.39           O  
ATOM   7193  CB  VAL B 436      89.738 140.681 122.119  1.00 42.39           C  
ATOM   7194  CG1 VAL B 436      90.706 139.562 121.813  1.00 42.39           C  
ATOM   7195  CG2 VAL B 436      88.880 140.311 123.314  1.00 42.39           C  
ATOM   7196  N   GLU B 437      89.156 143.458 123.779  1.00 45.27           N  
ATOM   7197  CA  GLU B 437      88.301 144.613 124.027  1.00 45.27           C  
ATOM   7198  C   GLU B 437      88.980 145.900 123.583  1.00 45.27           C  
ATOM   7199  O   GLU B 437      88.346 146.767 122.970  1.00 45.27           O  
ATOM   7200  CB  GLU B 437      87.936 144.691 125.507  1.00 45.27           C  
ATOM   7201  CG  GLU B 437      86.802 143.779 125.917  1.00 45.27           C  
ATOM   7202  CD  GLU B 437      86.671 143.653 127.420  1.00 45.27           C  
ATOM   7203  OE1 GLU B 437      85.985 142.717 127.882  1.00 45.27           O  
ATOM   7204  OE2 GLU B 437      87.256 144.488 128.142  1.00 45.27           O  
ATOM   7205  N   ILE B 438      90.271 146.044 123.881  1.00 45.43           N  
ATOM   7206  CA  ILE B 438      90.987 147.258 123.506  1.00 45.43           C  
ATOM   7207  C   ILE B 438      91.303 147.268 122.015  1.00 45.43           C  
ATOM   7208  O   ILE B 438      91.087 148.274 121.329  1.00 45.43           O  
ATOM   7209  CB  ILE B 438      92.263 147.416 124.355  1.00 45.43           C  
ATOM   7210  CG1 ILE B 438      91.914 147.444 125.845  1.00 45.43           C  
ATOM   7211  CG2 ILE B 438      92.996 148.678 123.963  1.00 45.43           C  
ATOM   7212  CD1 ILE B 438      93.102 147.268 126.764  1.00 45.43           C  
ATOM   7213  N   ILE B 439      91.815 146.156 121.486  1.00 46.61           N  
ATOM   7214  CA  ILE B 439      92.205 146.114 120.079  1.00 46.61           C  
ATOM   7215  C   ILE B 439      90.979 146.253 119.186  1.00 46.61           C  
ATOM   7216  O   ILE B 439      90.924 147.122 118.308  1.00 46.61           O  
ATOM   7217  CB  ILE B 439      92.982 144.819 119.772  1.00 46.61           C  
ATOM   7218  CG1 ILE B 439      94.303 144.792 120.544  1.00 46.61           C  
ATOM   7219  CG2 ILE B 439      93.261 144.705 118.279  1.00 46.61           C  
ATOM   7220  CD1 ILE B 439      95.021 143.456 120.506  1.00 46.61           C  
ATOM   7221  N   PHE B 440      89.980 145.397 119.394  1.00 51.89           N  
ATOM   7222  CA  PHE B 440      88.760 145.399 118.588  1.00 51.89           C  
ATOM   7223  C   PHE B 440      87.675 146.137 119.366  1.00 51.89           C  
ATOM   7224  O   PHE B 440      86.790 145.541 119.979  1.00 51.89           O  
ATOM   7225  CB  PHE B 440      88.346 143.972 118.245  1.00 51.89           C  
ATOM   7226  CG  PHE B 440      89.433 143.165 117.606  1.00 51.89           C  
ATOM   7227  CD1 PHE B 440      89.795 143.384 116.290  1.00 51.89           C  
ATOM   7228  CD2 PHE B 440      90.099 142.191 118.324  1.00 51.89           C  
ATOM   7229  CE1 PHE B 440      90.795 142.644 115.704  1.00 51.89           C  
ATOM   7230  CE2 PHE B 440      91.101 141.448 117.743  1.00 51.89           C  
ATOM   7231  CZ  PHE B 440      91.448 141.675 116.430  1.00 51.89           C  
ATOM   7232  N   ARG B 441      87.750 147.467 119.329  1.00 60.33           N  
ATOM   7233  CA  ARG B 441      86.811 148.299 120.070  1.00 60.33           C  
ATOM   7234  C   ARG B 441      85.623 148.733 119.225  1.00 60.33           C  
ATOM   7235  O   ARG B 441      84.536 148.960 119.770  1.00 60.33           O  
ATOM   7236  CB  ARG B 441      87.520 149.536 120.633  1.00 60.33           C  
ATOM   7237  CG  ARG B 441      88.338 150.334 119.624  1.00 60.33           C  
ATOM   7238  CD  ARG B 441      89.143 151.427 120.314  1.00 60.33           C  
ATOM   7239  NE  ARG B 441      90.022 152.145 119.394  1.00 60.33           N  
ATOM   7240  CZ  ARG B 441      91.269 151.782 119.099  1.00 60.33           C  
ATOM   7241  NH1 ARG B 441      91.807 150.698 119.645  1.00 60.33           N  
ATOM   7242  NH2 ARG B 441      91.983 152.507 118.250  1.00 60.33           N  
ATOM   7243  N   ALA B 442      85.801 148.855 117.910  1.00 64.99           N  
ATOM   7244  CA  ALA B 442      84.674 149.147 117.032  1.00 64.99           C  
ATOM   7245  C   ALA B 442      83.635 148.033 117.094  1.00 64.99           C  
ATOM   7246  O   ALA B 442      82.485 148.254 117.490  1.00 64.99           O  
ATOM   7247  CB  ALA B 442      85.169 149.346 115.599  1.00 64.99           C  
ATOM   7248  N   GLU B 443      84.031 146.819 116.710  1.00 63.04           N  
ATOM   7249  CA  GLU B 443      83.133 145.665 116.695  1.00 63.04           C  
ATOM   7250  C   GLU B 443      82.994 145.068 118.099  1.00 63.04           C  
ATOM   7251  O   GLU B 443      83.275 143.896 118.349  1.00 63.04           O  
ATOM   7252  CB  GLU B 443      83.634 144.628 115.698  1.00 63.04           C  
ATOM   7253  CG  GLU B 443      85.062 144.165 115.943  1.00 63.04           C  
ATOM   7254  CD  GLU B 443      85.442 142.966 115.098  1.00 63.04           C  
ATOM   7255  OE1 GLU B 443      85.261 143.022 113.864  1.00 63.04           O  
ATOM   7256  OE2 GLU B 443      85.918 141.964 115.670  1.00 63.04           O  
ATOM   7257  N   ILE B 444      82.537 145.910 119.025  1.00 62.50           N  
ATOM   7258  CA  ILE B 444      82.385 145.498 120.416  1.00 62.50           C  
ATOM   7259  C   ILE B 444      80.999 144.938 120.722  1.00 62.50           C  
ATOM   7260  O   ILE B 444      80.824 144.277 121.756  1.00 62.50           O  
ATOM   7261  CB  ILE B 444      82.684 146.685 121.352  1.00 62.50           C  
ATOM   7262  CG1 ILE B 444      82.911 146.209 122.790  1.00 62.50           C  
ATOM   7263  CG2 ILE B 444      81.549 147.696 121.311  1.00 62.50           C  
ATOM   7264  CD1 ILE B 444      84.201 145.448 122.990  1.00 62.50           C  
ATOM   7265  N   GLY B 445      80.017 145.169 119.856  1.00 58.32           N  
ATOM   7266  CA  GLY B 445      78.646 144.801 120.153  1.00 58.32           C  
ATOM   7267  C   GLY B 445      78.341 143.322 120.022  1.00 58.32           C  
ATOM   7268  O   GLY B 445      77.624 142.760 120.855  1.00 58.32           O  
ATOM   7269  N   ASP B 446      78.879 142.679 118.989  1.00 59.75           N  
ATOM   7270  CA  ASP B 446      78.551 141.288 118.723  1.00 59.75           C  
ATOM   7271  C   ASP B 446      79.058 140.392 119.853  1.00 59.75           C  
ATOM   7272  O   ASP B 446      79.727 140.836 120.790  1.00 59.75           O  
ATOM   7273  CB  ASP B 446      79.148 140.847 117.388  1.00 59.75           C  
ATOM   7274  CG  ASP B 446      78.355 139.734 116.734  1.00 59.75           C  
ATOM   7275  OD1 ASP B 446      77.672 138.983 117.460  1.00 59.75           O  
ATOM   7276  OD2 ASP B 446      78.416 139.611 115.493  1.00 59.75           O  
ATOM   7277  N   ALA B 447      78.721 139.106 119.755  1.00 59.55           N  
ATOM   7278  CA  ALA B 447      79.108 138.126 120.762  1.00 59.55           C  
ATOM   7279  C   ALA B 447      79.815 136.940 120.120  1.00 59.55           C  
ATOM   7280  O   ALA B 447      80.671 136.306 120.745  1.00 59.55           O  
ATOM   7281  CB  ALA B 447      77.881 137.654 121.542  1.00 59.55           C  
ATOM   7282  N   ASP B 448      79.458 136.631 118.873  1.00 61.11           N  
ATOM   7283  CA  ASP B 448      80.133 135.562 118.146  1.00 61.11           C  
ATOM   7284  C   ASP B 448      81.518 136.001 117.692  1.00 61.11           C  
ATOM   7285  O   ASP B 448      82.498 135.263 117.858  1.00 61.11           O  
ATOM   7286  CB  ASP B 448      79.294 135.145 116.937  1.00 61.11           C  
ATOM   7287  CG  ASP B 448      78.224 134.130 117.288  1.00 61.11           C  
ATOM   7288  OD1 ASP B 448      78.162 133.706 118.461  1.00 61.11           O  
ATOM   7289  OD2 ASP B 448      77.442 133.759 116.389  1.00 61.11           O  
ATOM   7290  N   LYS B 449      81.609 137.201 117.121  1.00 58.19           N  
ATOM   7291  CA  LYS B 449      82.897 137.730 116.695  1.00 58.19           C  
ATOM   7292  C   LYS B 449      83.839 137.890 117.880  1.00 58.19           C  
ATOM   7293  O   LYS B 449      85.031 137.578 117.784  1.00 58.19           O  
ATOM   7294  CB  LYS B 449      82.688 139.066 115.986  1.00 58.19           C  
ATOM   7295  CG  LYS B 449      83.842 139.496 115.107  1.00 58.19           C  
ATOM   7296  CD  LYS B 449      83.858 138.728 113.801  1.00 58.19           C  
ATOM   7297  CE  LYS B 449      85.126 138.998 113.015  1.00 58.19           C  
ATOM   7298  NZ  LYS B 449      85.077 138.374 111.667  1.00 58.19           N  
ATOM   7299  N   VAL B 450      83.320 138.376 119.009  1.00 55.50           N  
ATOM   7300  CA  VAL B 450      84.153 138.572 120.190  1.00 55.50           C  
ATOM   7301  C   VAL B 450      84.703 137.240 120.679  1.00 55.50           C  
ATOM   7302  O   VAL B 450      85.889 137.127 121.011  1.00 55.50           O  
ATOM   7303  CB  VAL B 450      83.352 139.296 121.288  1.00 55.50           C  
ATOM   7304  CG1 VAL B 450      84.052 139.189 122.631  1.00 55.50           C  
ATOM   7305  CG2 VAL B 450      83.147 140.747 120.913  1.00 55.50           C  
ATOM   7306  N   ALA B 451      83.855 136.211 120.737  1.00 54.79           N  
ATOM   7307  CA  ALA B 451      84.317 134.898 121.173  1.00 54.79           C  
ATOM   7308  C   ALA B 451      85.356 134.334 120.212  1.00 54.79           C  
ATOM   7309  O   ALA B 451      86.374 133.776 120.642  1.00 54.79           O  
ATOM   7310  CB  ALA B 451      83.133 133.942 121.303  1.00 54.79           C  
ATOM   7311  N   GLU B 452      85.115 134.468 118.907  1.00 54.89           N  
ATOM   7312  CA  GLU B 452      86.083 134.001 117.922  1.00 54.89           C  
ATOM   7313  C   GLU B 452      87.436 134.674 118.124  1.00 54.89           C  
ATOM   7314  O   GLU B 452      88.481 134.009 118.164  1.00 54.89           O  
ATOM   7315  CB  GLU B 452      85.548 134.268 116.514  1.00 54.89           C  
ATOM   7316  CG  GLU B 452      86.396 133.697 115.389  1.00 54.89           C  
ATOM   7317  CD  GLU B 452      87.531 134.620 114.979  1.00 54.89           C  
ATOM   7318  OE1 GLU B 452      87.375 135.853 115.103  1.00 54.89           O  
ATOM   7319  OE2 GLU B 452      88.582 134.110 114.537  1.00 54.89           O  
ATOM   7320  N   ARG B 453      87.431 135.999 118.270  1.00 52.08           N  
ATOM   7321  CA  ARG B 453      88.683 136.736 118.379  1.00 52.08           C  
ATOM   7322  C   ARG B 453      89.387 136.433 119.696  1.00 52.08           C  
ATOM   7323  O   ARG B 453      90.620 136.358 119.743  1.00 52.08           O  
ATOM   7324  CB  ARG B 453      88.409 138.230 118.225  1.00 52.08           C  
ATOM   7325  CG  ARG B 453      87.908 138.605 116.839  1.00 52.08           C  
ATOM   7326  CD  ARG B 453      87.984 140.093 116.597  1.00 52.08           C  
ATOM   7327  NE  ARG B 453      87.589 140.473 115.244  1.00 52.08           N  
ATOM   7328  CZ  ARG B 453      88.324 140.256 114.159  1.00 52.08           C  
ATOM   7329  NH1 ARG B 453      87.883 140.645 112.972  1.00 52.08           N  
ATOM   7330  NH2 ARG B 453      89.497 139.647 114.253  1.00 52.08           N  
ATOM   7331  N   THR B 454      88.625 136.244 120.774  1.00 47.66           N  
ATOM   7332  CA  THR B 454      89.221 135.860 122.047  1.00 47.66           C  
ATOM   7333  C   THR B 454      89.896 134.500 121.941  1.00 47.66           C  
ATOM   7334  O   THR B 454      91.022 134.312 122.418  1.00 47.66           O  
ATOM   7335  CB  THR B 454      88.153 135.852 123.139  1.00 47.66           C  
ATOM   7336  OG1 THR B 454      87.582 137.160 123.256  1.00 47.66           O  
ATOM   7337  CG2 THR B 454      88.744 135.448 124.476  1.00 47.66           C  
ATOM   7338  N   LYS B 455      89.213 133.529 121.330  1.00 46.78           N  
ATOM   7339  CA  LYS B 455      89.808 132.210 121.155  1.00 46.78           C  
ATOM   7340  C   LYS B 455      91.085 132.291 120.330  1.00 46.78           C  
ATOM   7341  O   LYS B 455      92.085 131.637 120.651  1.00 46.78           O  
ATOM   7342  CB  LYS B 455      88.802 131.267 120.499  1.00 46.78           C  
ATOM   7343  CG  LYS B 455      89.373 129.913 120.134  1.00 46.78           C  
ATOM   7344  CD  LYS B 455      88.281 128.869 119.976  1.00 46.78           C  
ATOM   7345  CE  LYS B 455      88.867 127.477 119.828  1.00 46.78           C  
ATOM   7346  NZ  LYS B 455      89.668 127.342 118.583  1.00 46.78           N  
ATOM   7347  N   GLU B 456      91.073 133.099 119.269  1.00 44.13           N  
ATOM   7348  CA  GLU B 456      92.264 133.241 118.437  1.00 44.13           C  
ATOM   7349  C   GLU B 456      93.416 133.861 119.224  1.00 44.13           C  
ATOM   7350  O   GLU B 456      94.554 133.376 119.170  1.00 44.13           O  
ATOM   7351  CB  GLU B 456      91.937 134.079 117.203  1.00 44.13           C  
ATOM   7352  CG  GLU B 456      93.018 134.068 116.143  1.00 44.13           C  
ATOM   7353  CD  GLU B 456      92.617 134.836 114.901  1.00 44.13           C  
ATOM   7354  OE1 GLU B 456      93.514 135.374 114.220  1.00 44.13           O  
ATOM   7355  OE2 GLU B 456      91.404 134.904 114.608  1.00 44.13           O  
ATOM   7356  N   TYR B 457      93.139 134.941 119.962  1.00 33.47           N  
ATOM   7357  CA  TYR B 457      94.181 135.571 120.766  1.00 33.47           C  
ATOM   7358  C   TYR B 457      94.752 134.593 121.785  1.00 33.47           C  
ATOM   7359  O   TYR B 457      95.970 134.542 121.991  1.00 33.47           O  
ATOM   7360  CB  TYR B 457      93.635 136.818 121.462  1.00 33.47           C  
ATOM   7361  CG  TYR B 457      94.705 137.797 121.898  1.00 33.47           C  
ATOM   7362  CD1 TYR B 457      95.331 137.672 123.126  1.00 33.47           C  
ATOM   7363  CD2 TYR B 457      95.090 138.844 121.078  1.00 33.47           C  
ATOM   7364  CE1 TYR B 457      96.306 138.559 123.521  1.00 33.47           C  
ATOM   7365  CE2 TYR B 457      96.060 139.733 121.464  1.00 33.47           C  
ATOM   7366  CZ  TYR B 457      96.666 139.590 122.686  1.00 33.47           C  
ATOM   7367  OH  TYR B 457      97.636 140.478 123.072  1.00 33.47           O  
ATOM   7368  N   GLU B 458      93.890 133.806 122.433  1.00 35.66           N  
ATOM   7369  CA  GLU B 458      94.365 132.828 123.406  1.00 35.66           C  
ATOM   7370  C   GLU B 458      95.263 131.794 122.743  1.00 35.66           C  
ATOM   7371  O   GLU B 458      96.347 131.479 123.248  1.00 35.66           O  
ATOM   7372  CB  GLU B 458      93.176 132.151 124.090  1.00 35.66           C  
ATOM   7373  CG  GLU B 458      93.544 131.096 125.127  1.00 35.66           C  
ATOM   7374  CD  GLU B 458      93.636 131.649 126.534  1.00 35.66           C  
ATOM   7375  OE1 GLU B 458      92.942 132.642 126.836  1.00 35.66           O  
ATOM   7376  OE2 GLU B 458      94.405 131.087 127.341  1.00 35.66           O  
ATOM   7377  N   ASP B 459      94.827 131.250 121.607  1.00 39.32           N  
ATOM   7378  CA  ASP B 459      95.605 130.214 120.942  1.00 39.32           C  
ATOM   7379  C   ASP B 459      96.897 130.756 120.352  1.00 39.32           C  
ATOM   7380  O   ASP B 459      97.805 129.974 120.056  1.00 39.32           O  
ATOM   7381  CB  ASP B 459      94.771 129.553 119.844  1.00 39.32           C  
ATOM   7382  CG  ASP B 459      93.627 128.729 120.399  1.00 39.32           C  
ATOM   7383  OD1 ASP B 459      93.843 128.000 121.389  1.00 39.32           O  
ATOM   7384  OD2 ASP B 459      92.512 128.810 119.845  1.00 39.32           O  
ATOM   7385  N   ARG B 460      97.002 132.070 120.179  1.00 32.14           N  
ATOM   7386  CA  ARG B 460      98.160 132.652 119.519  1.00 32.14           C  
ATOM   7387  C   ARG B 460      99.162 133.306 120.465  1.00 32.14           C  
ATOM   7388  O   ARG B 460     100.346 133.383 120.120  1.00 32.14           O  
ATOM   7389  CB  ARG B 460      97.690 133.683 118.492  1.00 32.14           C  
ATOM   7390  CG  ARG B 460      98.791 134.287 117.677  1.00 32.14           C  
ATOM   7391  CD  ARG B 460      98.234 134.935 116.428  1.00 32.14           C  
ATOM   7392  NE  ARG B 460      99.254 135.701 115.720  1.00 32.14           N  
ATOM   7393  CZ  ARG B 460      99.020 136.805 115.018  1.00 32.14           C  
ATOM   7394  NH1 ARG B 460     100.026 137.422 114.418  1.00 32.14           N  
ATOM   7395  NH2 ARG B 460      97.792 137.296 114.913  1.00 32.14           N  
ATOM   7396  N   PHE B 461      98.739 133.773 121.644  1.00 24.96           N  
ATOM   7397  CA  PHE B 461      99.590 134.616 122.483  1.00 24.96           C  
ATOM   7398  C   PHE B 461      99.694 134.202 123.948  1.00 24.96           C  
ATOM   7399  O   PHE B 461     100.613 134.677 124.623  1.00 24.96           O  
ATOM   7400  CB  PHE B 461      99.105 136.072 122.437  1.00 24.96           C  
ATOM   7401  CG  PHE B 461      99.173 136.697 121.072  1.00 24.96           C  
ATOM   7402  CD1 PHE B 461     100.383 136.845 120.418  1.00 24.96           C  
ATOM   7403  CD2 PHE B 461      98.028 137.150 120.446  1.00 24.96           C  
ATOM   7404  CE1 PHE B 461     100.442 137.423 119.171  1.00 24.96           C  
ATOM   7405  CE2 PHE B 461      98.089 137.728 119.196  1.00 24.96           C  
ATOM   7406  CZ  PHE B 461      99.295 137.865 118.562  1.00 24.96           C  
ATOM   7407  N   LEU B 462      98.807 133.355 124.469  1.00 19.62           N  
ATOM   7408  CA  LEU B 462      98.848 132.961 125.881  1.00 19.62           C  
ATOM   7409  C   LEU B 462      99.565 131.616 125.977  1.00 19.62           C  
ATOM   7410  O   LEU B 462      98.959 130.553 126.100  1.00 19.62           O  
ATOM   7411  CB  LEU B 462      97.442 132.928 126.475  1.00 19.62           C  
ATOM   7412  CG  LEU B 462      96.962 134.281 127.014  1.00 19.62           C  
ATOM   7413  CD1 LEU B 462      96.997 135.355 125.944  1.00 19.62           C  
ATOM   7414  CD2 LEU B 462      95.572 134.165 127.591  1.00 19.62           C  
ATOM   7415  N   SER B 463     100.895 131.688 125.924  1.00 14.17           N  
ATOM   7416  CA  SER B 463     101.784 130.535 125.835  1.00 14.17           C  
ATOM   7417  C   SER B 463     103.227 131.013 125.977  1.00 14.17           C  
ATOM   7418  O   SER B 463     103.474 132.225 125.976  1.00 14.17           O  
ATOM   7419  CB  SER B 463     101.577 129.799 124.511  1.00 14.17           C  
ATOM   7420  OG  SER B 463     101.765 130.668 123.414  1.00 14.17           O  
ATOM   7421  N   PRO B 464     104.203 130.115 126.113  1.00 12.46           N  
ATOM   7422  CA  PRO B 464     105.600 130.548 126.262  1.00 12.46           C  
ATOM   7423  C   PRO B 464     106.365 130.781 124.967  1.00 12.46           C  
ATOM   7424  O   PRO B 464     107.533 131.177 125.037  1.00 12.46           O  
ATOM   7425  CB  PRO B 464     106.226 129.381 127.040  1.00 12.46           C  
ATOM   7426  CG  PRO B 464     105.431 128.206 126.676  1.00 12.46           C  
ATOM   7427  CD  PRO B 464     104.047 128.672 126.375  1.00 12.46           C  
ATOM   7428  N   PHE B 465     105.757 130.568 123.802  1.00 16.13           N  
ATOM   7429  CA  PHE B 465     106.526 130.427 122.572  1.00 16.13           C  
ATOM   7430  C   PHE B 465     106.802 131.745 121.852  1.00 16.13           C  
ATOM   7431  O   PHE B 465     107.801 131.837 121.134  1.00 16.13           O  
ATOM   7432  CB  PHE B 465     105.820 129.448 121.633  1.00 16.13           C  
ATOM   7433  CG  PHE B 465     105.619 128.085 122.234  1.00 16.13           C  
ATOM   7434  CD1 PHE B 465     106.706 127.299 122.573  1.00 16.13           C  
ATOM   7435  CD2 PHE B 465     104.351 127.598 122.470  1.00 16.13           C  
ATOM   7436  CE1 PHE B 465     106.528 126.050 123.134  1.00 16.13           C  
ATOM   7437  CE2 PHE B 465     104.168 126.351 123.027  1.00 16.13           C  
ATOM   7438  CZ  PHE B 465     105.260 125.577 123.361  1.00 16.13           C  
ATOM   7439  N   VAL B 466     105.972 132.775 122.020  1.00 13.89           N  
ATOM   7440  CA  VAL B 466     106.331 134.075 121.461  1.00 13.89           C  
ATOM   7441  C   VAL B 466     107.542 134.646 122.188  1.00 13.89           C  
ATOM   7442  O   VAL B 466     108.456 135.198 121.564  1.00 13.89           O  
ATOM   7443  CB  VAL B 466     105.137 135.047 121.504  1.00 13.89           C  
ATOM   7444  CG1 VAL B 466     105.583 136.433 121.084  1.00 13.89           C  
ATOM   7445  CG2 VAL B 466     104.028 134.570 120.597  1.00 13.89           C  
ATOM   7446  N   ALA B 467     107.565 134.536 123.516  1.00 11.84           N  
ATOM   7447  CA  ALA B 467     108.744 134.949 124.270  1.00 11.84           C  
ATOM   7448  C   ALA B 467     109.971 134.144 123.856  1.00 11.84           C  
ATOM   7449  O   ALA B 467     111.069 134.695 123.724  1.00 11.84           O  
ATOM   7450  CB  ALA B 467     108.482 134.811 125.767  1.00 11.84           C  
ATOM   7451  N   ALA B 468     109.805 132.838 123.638  1.00 12.70           N  
ATOM   7452  CA  ALA B 468     110.926 132.012 123.205  1.00 12.70           C  
ATOM   7453  C   ALA B 468     111.429 132.434 121.827  1.00 12.70           C  
ATOM   7454  O   ALA B 468     112.642 132.480 121.591  1.00 12.70           O  
ATOM   7455  CB  ALA B 468     110.527 130.538 123.209  1.00 12.70           C  
ATOM   7456  N   GLU B 469     110.514 132.766 120.912  1.00 15.24           N  
ATOM   7457  CA  GLU B 469     110.914 133.141 119.559  1.00 15.24           C  
ATOM   7458  C   GLU B 469     111.791 134.386 119.557  1.00 15.24           C  
ATOM   7459  O   GLU B 469     112.689 134.509 118.718  1.00 15.24           O  
ATOM   7460  CB  GLU B 469     109.676 133.359 118.687  1.00 15.24           C  
ATOM   7461  CG  GLU B 469     108.978 132.082 118.251  1.00 15.24           C  
ATOM   7462  CD  GLU B 469     107.556 132.319 117.785  1.00 15.24           C  
ATOM   7463  OE1 GLU B 469     107.224 133.474 117.443  1.00 15.24           O  
ATOM   7464  OE2 GLU B 469     106.769 131.351 117.759  1.00 15.24           O  
ATOM   7465  N   ARG B 470     111.552 135.312 120.481  1.00 15.51           N  
ATOM   7466  CA  ARG B 470     112.361 136.513 120.630  1.00 15.51           C  
ATOM   7467  C   ARG B 470     113.585 136.307 121.514  1.00 15.51           C  
ATOM   7468  O   ARG B 470     114.347 137.255 121.722  1.00 15.51           O  
ATOM   7469  CB  ARG B 470     111.507 137.648 121.203  1.00 15.51           C  
ATOM   7470  CG  ARG B 470     110.364 138.104 120.304  1.00 15.51           C  
ATOM   7471  CD  ARG B 470     110.856 138.628 118.975  1.00 15.51           C  
ATOM   7472  NE  ARG B 470     111.764 139.761 119.137  1.00 15.51           N  
ATOM   7473  CZ  ARG B 470     111.447 141.030 118.898  1.00 15.51           C  
ATOM   7474  NH1 ARG B 470     110.238 141.366 118.471  1.00 15.51           N  
ATOM   7475  NH2 ARG B 470     112.357 141.972 119.082  1.00 15.51           N  
ATOM   7476  N   GLY B 471     113.799 135.100 122.026  1.00 12.11           N  
ATOM   7477  CA  GLY B 471     114.913 134.852 122.918  1.00 12.11           C  
ATOM   7478  C   GLY B 471     114.824 135.512 124.275  1.00 12.11           C  
ATOM   7479  O   GLY B 471     115.856 135.755 124.901  1.00 12.11           O  
ATOM   7480  N   TYR B 472     113.617 135.812 124.753  1.00 11.79           N  
ATOM   7481  CA  TYR B 472     113.440 136.301 126.116  1.00 11.79           C  
ATOM   7482  C   TYR B 472     113.474 135.176 127.143  1.00 11.79           C  
ATOM   7483  O   TYR B 472     113.782 135.429 128.312  1.00 11.79           O  
ATOM   7484  CB  TYR B 472     112.121 137.065 126.236  1.00 11.79           C  
ATOM   7485  CG  TYR B 472     112.011 138.288 125.355  1.00 11.79           C  
ATOM   7486  CD1 TYR B 472     113.135 138.892 124.812  1.00 11.79           C  
ATOM   7487  CD2 TYR B 472     110.776 138.843 125.072  1.00 11.79           C  
ATOM   7488  CE1 TYR B 472     113.028 140.001 124.016  1.00 11.79           C  
ATOM   7489  CE2 TYR B 472     110.662 139.949 124.276  1.00 11.79           C  
ATOM   7490  CZ  TYR B 472     111.790 140.527 123.751  1.00 11.79           C  
ATOM   7491  OH  TYR B 472     111.683 141.637 122.954  1.00 11.79           O  
ATOM   7492  N   ILE B 473     113.164 133.952 126.730  1.00 10.86           N  
ATOM   7493  CA  ILE B 473     113.260 132.757 127.561  1.00 10.86           C  
ATOM   7494  C   ILE B 473     114.356 131.876 126.979  1.00 10.86           C  
ATOM   7495  O   ILE B 473     114.419 131.680 125.760  1.00 10.86           O  
ATOM   7496  CB  ILE B 473     111.911 132.014 127.631  1.00 10.86           C  
ATOM   7497  CG1 ILE B 473     110.884 132.824 128.436  1.00 10.86           C  
ATOM   7498  CG2 ILE B 473     112.069 130.600 128.176  1.00 10.86           C  
ATOM   7499  CD1 ILE B 473     111.255 133.056 129.874  1.00 10.86           C  
ATOM   7500  N   ASP B 474     115.224 131.355 127.848  1.00 11.71           N  
ATOM   7501  CA  ASP B 474     116.372 130.583 127.385  1.00 11.71           C  
ATOM   7502  C   ASP B 474     115.995 129.157 126.999  1.00 11.71           C  
ATOM   7503  O   ASP B 474     116.613 128.586 126.095  1.00 11.71           O  
ATOM   7504  CB  ASP B 474     117.465 130.555 128.455  1.00 11.71           C  
ATOM   7505  CG  ASP B 474     118.091 131.919 128.691  1.00 11.71           C  
ATOM   7506  OD1 ASP B 474     118.695 132.474 127.751  1.00 11.71           O  
ATOM   7507  OD2 ASP B 474     117.974 132.437 129.819  1.00 11.71           O  
ATOM   7508  N   GLU B 475     115.007 128.567 127.668  1.00 13.31           N  
ATOM   7509  CA  GLU B 475     114.573 127.210 127.366  1.00 13.31           C  
ATOM   7510  C   GLU B 475     113.236 126.941 128.044  1.00 13.31           C  
ATOM   7511  O   GLU B 475     112.970 127.443 129.138  1.00 13.31           O  
ATOM   7512  CB  GLU B 475     115.612 126.172 127.818  1.00 13.31           C  
ATOM   7513  CG  GLU B 475     115.208 124.727 127.569  1.00 13.31           C  
ATOM   7514  CD  GLU B 475     114.954 124.428 126.107  1.00 13.31           C  
ATOM   7515  OE1 GLU B 475     115.777 123.717 125.495  1.00 13.31           O  
ATOM   7516  OE2 GLU B 475     113.934 124.905 125.566  1.00 13.31           O  
ATOM   7517  N   VAL B 476     112.404 126.149 127.372  1.00 11.00           N  
ATOM   7518  CA  VAL B 476     111.174 125.600 127.932  1.00 11.00           C  
ATOM   7519  C   VAL B 476     111.507 124.209 128.458  1.00 11.00           C  
ATOM   7520  O   VAL B 476     112.009 123.363 127.708  1.00 11.00           O  
ATOM   7521  CB  VAL B 476     110.050 125.549 126.881  1.00 11.00           C  
ATOM   7522  CG1 VAL B 476     108.765 125.015 127.478  1.00 11.00           C  
ATOM   7523  CG2 VAL B 476     109.804 126.924 126.260  1.00 11.00           C  
ATOM   7524  N   ILE B 477     111.240 123.965 129.740  1.00 10.33           N  
ATOM   7525  CA  ILE B 477     111.707 122.758 130.416  1.00 10.33           C  
ATOM   7526  C   ILE B 477     110.530 121.959 130.955  1.00 10.33           C  
ATOM   7527  O   ILE B 477     109.458 122.497 131.247  1.00 10.33           O  
ATOM   7528  CB  ILE B 477     112.698 123.076 131.561  1.00 10.33           C  
ATOM   7529  CG1 ILE B 477     111.997 123.794 132.719  1.00 10.33           C  
ATOM   7530  CG2 ILE B 477     113.878 123.873 131.038  1.00 10.33           C  
ATOM   7531  CD1 ILE B 477     112.897 124.079 133.888  1.00 10.33           C  
ATOM   7532  N   MET B 478     110.751 120.655 131.087  1.00 16.06           N  
ATOM   7533  CA  MET B 478     109.799 119.788 131.758  1.00 16.06           C  
ATOM   7534  C   MET B 478     109.861 120.025 133.266  1.00 16.06           C  
ATOM   7535  O   MET B 478     110.949 120.199 133.818  1.00 16.06           O  
ATOM   7536  CB  MET B 478     110.106 118.322 131.461  1.00 16.06           C  
ATOM   7537  CG  MET B 478     110.242 117.982 129.977  1.00 16.06           C  
ATOM   7538  SD  MET B 478     108.938 118.685 128.968  1.00 16.06           S  
ATOM   7539  CE  MET B 478     107.563 117.694 129.517  1.00 16.06           C  
ATOM   7540  N   PRO B 479     108.719 120.033 133.960  1.00 12.60           N  
ATOM   7541  CA  PRO B 479     108.753 120.311 135.408  1.00 12.60           C  
ATOM   7542  C   PRO B 479     109.683 119.395 136.191  1.00 12.60           C  
ATOM   7543  O   PRO B 479     110.451 119.878 137.035  1.00 12.60           O  
ATOM   7544  CB  PRO B 479     107.287 120.134 135.824  1.00 12.60           C  
ATOM   7545  CG  PRO B 479     106.514 120.401 134.595  1.00 12.60           C  
ATOM   7546  CD  PRO B 479     107.341 119.895 133.464  1.00 12.60           C  
ATOM   7547  N   HIS B 480     109.664 118.090 135.908  1.00 15.33           N  
ATOM   7548  CA  HIS B 480     110.469 117.139 136.667  1.00 15.33           C  
ATOM   7549  C   HIS B 480     111.965 117.421 136.578  1.00 15.33           C  
ATOM   7550  O   HIS B 480     112.731 116.819 137.335  1.00 15.33           O  
ATOM   7551  CB  HIS B 480     110.186 115.694 136.216  1.00 15.33           C  
ATOM   7552  CG  HIS B 480     110.530 115.407 134.789  1.00 15.33           C  
ATOM   7553  ND1 HIS B 480     109.624 115.552 133.762  1.00 15.33           N  
ATOM   7554  CD2 HIS B 480     111.682 114.988 134.216  1.00 15.33           C  
ATOM   7555  CE1 HIS B 480     110.199 115.223 132.620  1.00 15.33           C  
ATOM   7556  NE2 HIS B 480     111.449 114.884 132.866  1.00 15.33           N  
ATOM   7557  N   SER B 481     112.395 118.318 135.694  1.00 12.17           N  
ATOM   7558  CA  SER B 481     113.806 118.638 135.522  1.00 12.17           C  
ATOM   7559  C   SER B 481     114.271 119.799 136.398  1.00 12.17           C  
ATOM   7560  O   SER B 481     115.482 120.019 136.514  1.00 12.17           O  
ATOM   7561  CB  SER B 481     114.086 118.962 134.046  1.00 12.17           C  
ATOM   7562  OG  SER B 481     113.677 117.900 133.210  1.00 12.17           O  
ATOM   7563  N   THR B 482     113.346 120.494 137.067  1.00  9.16           N  
ATOM   7564  CA  THR B 482     113.638 121.814 137.621  1.00  9.16           C  
ATOM   7565  C   THR B 482     114.884 121.807 138.507  1.00  9.16           C  
ATOM   7566  O   THR B 482     115.851 122.530 138.240  1.00  9.16           O  
ATOM   7567  CB  THR B 482     112.414 122.331 138.383  1.00  9.16           C  
ATOM   7568  OG1 THR B 482     111.307 122.426 137.478  1.00  9.16           O  
ATOM   7569  CG2 THR B 482     112.685 123.703 138.988  1.00  9.16           C  
ATOM   7570  N   ARG B 483     114.889 120.983 139.557  1.00  9.50           N  
ATOM   7571  CA  ARG B 483     116.047 120.942 140.447  1.00  9.50           C  
ATOM   7572  C   ARG B 483     117.321 120.690 139.651  1.00  9.50           C  
ATOM   7573  O   ARG B 483     118.281 121.468 139.726  1.00  9.50           O  
ATOM   7574  CB  ARG B 483     115.852 119.880 141.535  1.00  9.50           C  
ATOM   7575  CG  ARG B 483     116.985 119.811 142.560  1.00  9.50           C  
ATOM   7576  CD  ARG B 483     116.704 118.847 143.701  1.00  9.50           C  
ATOM   7577  NE  ARG B 483     117.933 118.281 144.248  1.00  9.50           N  
ATOM   7578  CZ  ARG B 483     118.665 118.820 145.219  1.00  9.50           C  
ATOM   7579  NH1 ARG B 483     118.317 119.961 145.791  1.00  9.50           N  
ATOM   7580  NH2 ARG B 483     119.763 118.205 145.625  1.00  9.50           N  
ATOM   7581  N   LYS B 484     117.321 119.635 138.831  1.00  9.92           N  
ATOM   7582  CA  LYS B 484     118.513 119.294 138.065  1.00  9.92           C  
ATOM   7583  C   LYS B 484     119.013 120.479 137.256  1.00  9.92           C  
ATOM   7584  O   LYS B 484     120.225 120.663 137.109  1.00  9.92           O  
ATOM   7585  CB  LYS B 484     118.229 118.102 137.148  1.00  9.92           C  
ATOM   7586  CG  LYS B 484     119.383 117.708 136.241  1.00  9.92           C  
ATOM   7587  CD  LYS B 484     119.029 116.514 135.369  1.00  9.92           C  
ATOM   7588  CE  LYS B 484     120.233 115.997 134.602  1.00  9.92           C  
ATOM   7589  NZ  LYS B 484     120.786 116.988 133.638  1.00  9.92           N  
ATOM   7590  N   ARG B 485     118.104 121.309 136.745  1.00  8.73           N  
ATOM   7591  CA  ARG B 485     118.543 122.463 135.977  1.00  8.73           C  
ATOM   7592  C   ARG B 485     119.168 123.504 136.898  1.00  8.73           C  
ATOM   7593  O   ARG B 485     120.306 123.941 136.681  1.00  8.73           O  
ATOM   7594  CB  ARG B 485     117.369 123.054 135.189  1.00  8.73           C  
ATOM   7595  CG  ARG B 485     116.629 122.086 134.262  1.00  8.73           C  
ATOM   7596  CD  ARG B 485     117.533 121.310 133.340  1.00  8.73           C  
ATOM   7597  NE  ARG B 485     118.049 122.152 132.265  1.00  8.73           N  
ATOM   7598  CZ  ARG B 485     117.671 122.079 130.990  1.00  8.73           C  
ATOM   7599  NH1 ARG B 485     116.758 121.206 130.591  1.00  8.73           N  
ATOM   7600  NH2 ARG B 485     118.213 122.893 130.100  1.00  8.73           N  
ATOM   7601  N   ILE B 486     118.462 123.853 137.977  1.00  6.95           N  
ATOM   7602  CA  ILE B 486     118.942 124.896 138.881  1.00  6.95           C  
ATOM   7603  C   ILE B 486     120.343 124.555 139.368  1.00  6.95           C  
ATOM   7604  O   ILE B 486     121.287 125.336 139.202  1.00  6.95           O  
ATOM   7605  CB  ILE B 486     117.956 125.082 140.053  1.00  6.95           C  
ATOM   7606  CG1 ILE B 486     116.628 125.656 139.548  1.00  6.95           C  
ATOM   7607  CG2 ILE B 486     118.550 125.970 141.141  1.00  6.95           C  
ATOM   7608  CD1 ILE B 486     115.524 125.672 140.575  1.00  6.95           C  
ATOM   7609  N   ALA B 487     120.513 123.345 139.896  1.00  7.67           N  
ATOM   7610  CA  ALA B 487     121.799 122.957 140.459  1.00  7.67           C  
ATOM   7611  C   ALA B 487     122.906 123.068 139.421  1.00  7.67           C  
ATOM   7612  O   ALA B 487     124.020 123.497 139.739  1.00  7.67           O  
ATOM   7613  CB  ALA B 487     121.723 121.541 141.018  1.00  7.67           C  
ATOM   7614  N   ARG B 488     122.618 122.717 138.168  1.00  9.33           N  
ATOM   7615  CA  ARG B 488     123.641 122.869 137.143  1.00  9.33           C  
ATOM   7616  C   ARG B 488     123.930 124.345 136.916  1.00  9.33           C  
ATOM   7617  O   ARG B 488     125.078 124.794 137.042  1.00  9.33           O  
ATOM   7618  CB  ARG B 488     123.202 122.170 135.853  1.00  9.33           C  
ATOM   7619  CG  ARG B 488     124.294 121.988 134.819  1.00  9.33           C  
ATOM   7620  CD  ARG B 488     123.927 120.917 133.801  1.00  9.33           C  
ATOM   7621  NE  ARG B 488     122.882 121.344 132.874  1.00  9.33           N  
ATOM   7622  CZ  ARG B 488     122.557 120.696 131.760  1.00  9.33           C  
ATOM   7623  NH1 ARG B 488     123.192 119.580 131.419  1.00  9.33           N  
ATOM   7624  NH2 ARG B 488     121.593 121.170 130.983  1.00  9.33           N  
ATOM   7625  N   ALA B 489     122.877 125.130 136.689  1.00  6.79           N  
ATOM   7626  CA  ALA B 489     123.040 126.546 136.390  1.00  6.79           C  
ATOM   7627  C   ALA B 489     123.877 127.236 137.458  1.00  6.79           C  
ATOM   7628  O   ALA B 489     124.895 127.869 137.155  1.00  6.79           O  
ATOM   7629  CB  ALA B 489     121.670 127.204 136.268  1.00  6.79           C  
ATOM   7630  N   LEU B 490     123.472 127.099 138.722  1.00  6.63           N  
ATOM   7631  CA  LEU B 490     124.187 127.768 139.803  1.00  6.63           C  
ATOM   7632  C   LEU B 490     125.666 127.413 139.765  1.00  6.63           C  
ATOM   7633  O   LEU B 490     126.528 128.297 139.855  1.00  6.63           O  
ATOM   7634  CB  LEU B 490     123.564 127.403 141.156  1.00  6.63           C  
ATOM   7635  CG  LEU B 490     122.191 128.011 141.467  1.00  6.63           C  
ATOM   7636  CD1 LEU B 490     121.634 127.506 142.797  1.00  6.63           C  
ATOM   7637  CD2 LEU B 490     122.229 129.529 141.451  1.00  6.63           C  
ATOM   7638  N   GLY B 491     125.978 126.132 139.578  1.00  8.10           N  
ATOM   7639  CA  GLY B 491     127.370 125.723 139.522  1.00  8.10           C  
ATOM   7640  C   GLY B 491     128.169 126.494 138.492  1.00  8.10           C  
ATOM   7641  O   GLY B 491     129.306 126.892 138.747  1.00  8.10           O  
ATOM   7642  N   MET B 492     127.585 126.718 137.312  1.00  8.42           N  
ATOM   7643  CA  MET B 492     128.294 127.437 136.262  1.00  8.42           C  
ATOM   7644  C   MET B 492     128.457 128.913 136.599  1.00  8.42           C  
ATOM   7645  O   MET B 492     129.447 129.528 136.192  1.00  8.42           O  
ATOM   7646  CB  MET B 492     127.562 127.280 134.929  1.00  8.42           C  
ATOM   7647  CG  MET B 492     128.074 128.172 133.804  1.00  8.42           C  
ATOM   7648  SD  MET B 492     127.217 129.743 133.646  1.00  8.42           S  
ATOM   7649  CE  MET B 492     125.735 129.237 132.787  1.00  8.42           C  
ATOM   7650  N   LEU B 493     127.510 129.496 137.334  1.00  6.77           N  
ATOM   7651  CA  LEU B 493     127.465 130.939 137.528  1.00  6.77           C  
ATOM   7652  C   LEU B 493     128.341 131.431 138.680  1.00  6.77           C  
ATOM   7653  O   LEU B 493     128.488 132.645 138.845  1.00  6.77           O  
ATOM   7654  CB  LEU B 493     126.010 131.389 137.745  1.00  6.77           C  
ATOM   7655  CG  LEU B 493     125.051 131.173 136.565  1.00  6.77           C  
ATOM   7656  CD1 LEU B 493     123.594 131.333 136.975  1.00  6.77           C  
ATOM   7657  CD2 LEU B 493     125.375 132.112 135.414  1.00  6.77           C  
ATOM   7658  N   ARG B 494     128.933 130.527 139.465  1.00  9.69           N  
ATOM   7659  CA  ARG B 494     129.727 130.929 140.625  1.00  9.69           C  
ATOM   7660  C   ARG B 494     130.827 131.935 140.280  1.00  9.69           C  
ATOM   7661  O   ARG B 494     131.210 132.742 141.133  1.00  9.69           O  
ATOM   7662  CB  ARG B 494     130.328 129.686 141.292  1.00  9.69           C  
ATOM   7663  CG  ARG B 494     129.307 128.829 142.019  1.00  9.69           C  
ATOM   7664  CD  ARG B 494     129.892 127.545 142.577  1.00  9.69           C  
ATOM   7665  NE  ARG B 494     128.845 126.677 143.108  1.00  9.69           N  
ATOM   7666  CZ  ARG B 494     129.001 125.385 143.378  1.00  9.69           C  
ATOM   7667  NH1 ARG B 494     130.168 124.791 143.177  1.00  9.69           N  
ATOM   7668  NH2 ARG B 494     127.981 124.686 143.853  1.00  9.69           N  
ATOM   7669  N   THR B 495     131.342 131.910 139.051  1.00  7.82           N  
ATOM   7670  CA  THR B 495     132.434 132.786 138.631  1.00  7.82           C  
ATOM   7671  C   THR B 495     131.960 134.113 138.029  1.00  7.82           C  
ATOM   7672  O   THR B 495     132.774 134.838 137.451  1.00  7.82           O  
ATOM   7673  CB  THR B 495     133.334 132.059 137.624  1.00  7.82           C  
ATOM   7674  OG1 THR B 495     132.646 131.915 136.377  1.00  7.82           O  
ATOM   7675  CG2 THR B 495     133.749 130.686 138.155  1.00  7.82           C  
ATOM   7676  N   LYS B 496     130.678 134.444 138.165  1.00  7.22           N  
ATOM   7677  CA  LYS B 496     130.139 135.691 137.630  1.00  7.22           C  
ATOM   7678  C   LYS B 496     130.876 136.907 138.189  1.00  7.22           C  
ATOM   7679  O   LYS B 496     131.085 137.023 139.399  1.00  7.22           O  
ATOM   7680  CB  LYS B 496     128.642 135.781 137.947  1.00  7.22           C  
ATOM   7681  CG  LYS B 496     127.938 137.047 137.439  1.00  7.22           C  
ATOM   7682  CD  LYS B 496     126.423 137.025 137.667  1.00  7.22           C  
ATOM   7683  CE  LYS B 496     125.736 138.232 137.043  1.00  7.22           C  
ATOM   7684  NZ  LYS B 496     124.339 138.423 137.488  1.00  7.22           N  
ATOM   7685  N   GLU B 497     131.262 137.816 137.294  1.00 16.17           N  
ATOM   7686  CA  GLU B 497     131.938 139.063 137.642  1.00 16.17           C  
ATOM   7687  C   GLU B 497     131.209 140.222 136.974  1.00 16.17           C  
ATOM   7688  O   GLU B 497     131.084 140.253 135.746  1.00 16.17           O  
ATOM   7689  CB  GLU B 497     133.412 139.040 137.219  1.00 16.17           C  
ATOM   7690  CG  GLU B 497     134.246 137.980 137.914  1.00 16.17           C  
ATOM   7691  CD  GLU B 497     135.728 138.314 137.928  1.00 16.17           C  
ATOM   7692  OE1 GLU B 497     136.536 137.462 137.500  1.00 16.17           O  
ATOM   7693  OE2 GLU B 497     136.085 139.427 138.368  1.00 16.17           O  
ATOM   7694  N   MET B 498     130.769 141.186 137.743  1.00 22.35           N  
ATOM   7695  CA  MET B 498     129.920 142.285 137.266  1.00 22.35           C  
ATOM   7696  C   MET B 498     129.914 143.389 138.344  1.00 22.35           C  
ATOM   7697  O   MET B 498     129.983 143.109 139.550  1.00 22.35           O  
ATOM   7698  CB  MET B 498     128.502 141.794 137.004  1.00 22.35           C  
ATOM   7699  CG  MET B 498     127.654 142.760 136.396  1.00 22.35           C  
ATOM   7700  SD  MET B 498     126.020 142.059 136.225  1.00 22.35           S  
ATOM   7701  CE  MET B 498     125.171 143.503 135.632  1.00 22.35           C  
ATOM   7702  N   GLU B 499     130.034 144.655 137.898  1.00 25.74           N  
ATOM   7703  CA  GLU B 499     130.134 145.810 138.782  1.00 25.74           C  
ATOM   7704  C   GLU B 499     129.259 146.953 138.276  1.00 25.74           C  
ATOM   7705  O   GLU B 499     129.216 147.228 137.075  1.00 25.74           O  
ATOM   7706  CB  GLU B 499     131.594 146.275 138.905  1.00 25.74           C  
ATOM   7707  CG  GLU B 499     132.179 146.900 137.643  1.00 25.74           C  
ATOM   7708  CD  GLU B 499     132.577 145.872 136.604  1.00 25.74           C  
ATOM   7709  OE1 GLU B 499     132.108 144.718 136.694  1.00 25.74           O  
ATOM   7710  OE2 GLU B 499     133.361 146.218 135.696  1.00 25.74           O  
ATOM   7711  N   GLN B 500     128.559 147.608 139.204  1.00 16.66           N  
ATOM   7712  CA  GLN B 500     127.680 148.754 138.871  1.00 16.66           C  
ATOM   7713  C   GLN B 500     128.568 150.014 138.731  1.00 16.66           C  
ATOM   7714  O   GLN B 500     129.723 149.984 139.208  1.00 16.66           O  
ATOM   7715  CB  GLN B 500     126.720 149.043 140.026  1.00 16.66           C  
ATOM   7716  CG  GLN B 500     125.464 148.173 140.225  1.00 16.66           C  
ATOM   7717  CD  GLN B 500     124.481 148.085 139.088  1.00 16.66           C  
ATOM   7718  OE1 GLN B 500     124.444 147.074 138.445  1.00 16.66           O  
ATOM   7719  NE2 GLN B 500     123.669 149.084 138.820  1.00 16.66           N  
ATOM   7720  N   PRO B 501     128.143 151.147 138.096  1.00 13.54           N  
ATOM   7721  CA  PRO B 501     128.969 152.374 138.041  1.00 13.54           C  
ATOM   7722  C   PRO B 501     129.398 152.915 139.426  1.00 13.54           C  
ATOM   7723  O   PRO B 501     128.787 152.678 140.470  1.00 13.54           O  
ATOM   7724  CB  PRO B 501     128.205 153.412 137.159  1.00 13.54           C  
ATOM   7725  CG  PRO B 501     126.957 152.733 136.729  1.00 13.54           C  
ATOM   7726  CD  PRO B 501     126.937 151.326 137.298  1.00 13.54           C  
ATOM   7727  N   ARG B 502     130.483 153.692 139.378  1.00 15.83           N  
ATOM   7728  CA  ARG B 502     131.081 154.241 140.591  1.00 15.83           C  
ATOM   7729  C   ARG B 502     130.183 155.321 141.181  1.00 15.83           C  
ATOM   7730  O   ARG B 502     129.690 156.194 140.462  1.00 15.83           O  
ATOM   7731  CB  ARG B 502     132.466 154.822 140.299  1.00 15.83           C  
ATOM   7732  CG  ARG B 502     133.605 153.809 140.319  1.00 15.83           C  
ATOM   7733  CD  ARG B 502     134.968 154.491 140.397  1.00 15.83           C  
ATOM   7734  NE  ARG B 502     135.341 155.129 139.139  1.00 15.83           N  
ATOM   7735  CZ  ARG B 502     135.773 154.476 138.065  1.00 15.83           C  
ATOM   7736  NH1 ARG B 502     136.085 155.149 136.968  1.00 15.83           N  
ATOM   7737  NH2 ARG B 502     135.895 153.155 138.080  1.00 15.83           N  
ATOM   7738  N   LYS B 503     129.967 155.258 142.492  1.00  8.26           N  
ATOM   7739  CA  LYS B 503     129.071 156.190 143.162  1.00  8.26           C  
ATOM   7740  C   LYS B 503     129.182 156.019 144.671  1.00  8.26           C  
ATOM   7741  O   LYS B 503     129.439 154.919 145.166  1.00  8.26           O  
ATOM   7742  CB  LYS B 503     127.620 155.983 142.703  1.00  8.26           C  
ATOM   7743  CG  LYS B 503     126.961 154.684 143.166  1.00  8.26           C  
ATOM   7744  CD  LYS B 503     125.560 154.478 142.584  1.00  8.26           C  
ATOM   7745  CE  LYS B 503     125.572 153.990 141.136  1.00  8.26           C  
ATOM   7746  NZ  LYS B 503     124.216 153.700 140.597  1.00  8.26           N  
ATOM   7747  N   LYS B 504     128.978 157.127 145.391  1.00  7.67           N  
ATOM   7748  CA  LYS B 504     128.871 157.065 146.845  1.00  7.67           C  
ATOM   7749  C   LYS B 504     127.756 156.115 147.258  1.00  7.67           C  
ATOM   7750  O   LYS B 504     127.948 155.241 148.109  1.00  7.67           O  
ATOM   7751  CB  LYS B 504     128.636 158.467 147.416  1.00  7.67           C  
ATOM   7752  CG  LYS B 504     129.814 159.414 147.258  1.00  7.67           C  
ATOM   7753  CD  LYS B 504     129.506 160.842 147.711  1.00  7.67           C  
ATOM   7754  CE  LYS B 504     129.004 160.913 149.130  1.00  7.67           C  
ATOM   7755  NZ  LYS B 504     129.385 162.228 149.735  1.00  7.67           N  
ATOM   7756  N   HIS B 505     126.582 156.274 146.657  1.00  7.56           N  
ATOM   7757  CA  HIS B 505     125.477 155.344 146.818  1.00  7.56           C  
ATOM   7758  C   HIS B 505     124.345 155.758 145.886  1.00  7.56           C  
ATOM   7759  O   HIS B 505     124.296 156.890 145.402  1.00  7.56           O  
ATOM   7760  CB  HIS B 505     124.981 155.289 148.263  1.00  7.56           C  
ATOM   7761  CG  HIS B 505     124.486 156.600 148.788  1.00  7.56           C  
ATOM   7762  ND1 HIS B 505     123.278 157.142 148.411  1.00  7.56           N  
ATOM   7763  CD2 HIS B 505     125.028 157.469 149.672  1.00  7.56           C  
ATOM   7764  CE1 HIS B 505     123.099 158.290 149.038  1.00  7.56           C  
ATOM   7765  NE2 HIS B 505     124.146 158.510 149.809  1.00  7.56           N  
ATOM   7766  N   ASP B 506     123.429 154.823 145.666  1.00  7.35           N  
ATOM   7767  CA  ASP B 506     122.253 155.036 144.841  1.00  7.35           C  
ATOM   7768  C   ASP B 506     121.222 155.891 145.578  1.00  7.35           C  
ATOM   7769  O   ASP B 506     121.366 156.209 146.759  1.00  7.35           O  
ATOM   7770  CB  ASP B 506     121.640 153.698 144.451  1.00  7.35           C  
ATOM   7771  CG  ASP B 506     121.085 152.943 145.650  1.00  7.35           C  
ATOM   7772  OD1 ASP B 506     120.019 153.335 146.164  1.00  7.35           O  
ATOM   7773  OD2 ASP B 506     121.722 151.967 146.093  1.00  7.35           O  
ATOM   7774  N   ASN B 507     120.162 156.259 144.857  1.00  6.35           N  
ATOM   7775  CA  ASN B 507     119.071 157.050 145.419  1.00  6.35           C  
ATOM   7776  C   ASN B 507     117.759 156.278 145.326  1.00  6.35           C  
ATOM   7777  O   ASN B 507     116.741 156.812 144.874  1.00  6.35           O  
ATOM   7778  CB  ASN B 507     118.948 158.404 144.720  1.00  6.35           C  
ATOM   7779  CG  ASN B 507     117.984 159.335 145.431  1.00  6.35           C  
ATOM   7780  OD1 ASN B 507     117.707 159.175 146.618  1.00  6.35           O  
ATOM   7781  ND2 ASN B 507     117.466 160.310 144.705  1.00  6.35           N  
ATOM   7782  N   ILE B 508     117.788 155.011 145.726  1.00  7.83           N  
ATOM   7783  CA  ILE B 508     116.613 154.144 145.728  1.00  7.83           C  
ATOM   7784  C   ILE B 508     115.483 154.869 146.451  1.00  7.83           C  
ATOM   7785  O   ILE B 508     115.731 155.512 147.480  1.00  7.83           O  
ATOM   7786  CB  ILE B 508     116.924 152.788 146.387  1.00  7.83           C  
ATOM   7787  CG1 ILE B 508     115.788 151.789 146.138  1.00  7.83           C  
ATOM   7788  CG2 ILE B 508     117.202 152.962 147.872  1.00  7.83           C  
ATOM   7789  CD1 ILE B 508     116.026 150.408 146.704  1.00  7.83           C  
ATOM   7790  N   PRO B 509     114.245 154.812 145.964  1.00 11.57           N  
ATOM   7791  CA  PRO B 509     113.159 155.508 146.660  1.00 11.57           C  
ATOM   7792  C   PRO B 509     112.880 154.899 148.024  1.00 11.57           C  
ATOM   7793  O   PRO B 509     113.132 153.718 148.270  1.00 11.57           O  
ATOM   7794  CB  PRO B 509     111.962 155.346 145.717  1.00 11.57           C  
ATOM   7795  CG  PRO B 509     112.307 154.242 144.820  1.00 11.57           C  
ATOM   7796  CD  PRO B 509     113.784 154.202 144.705  1.00 11.57           C  
ATOM   7797  N   LEU B 510     112.358 155.732 148.919  1.00 15.87           N  
ATOM   7798  CA  LEU B 510     112.089 155.323 150.294  1.00 15.87           C  
ATOM   7799  C   LEU B 510     110.610 155.464 150.648  1.00 15.87           C  
ATOM   7800  O   LEU B 510     109.777 155.771 149.797  1.00 15.87           O  
ATOM   7801  CB  LEU B 510     112.933 156.145 151.269  1.00 15.87           C  
ATOM   7802  CG  LEU B 510     114.447 156.063 151.091  1.00 15.87           C  
ATOM   7803  CD1 LEU B 510     115.149 156.930 152.116  1.00 15.87           C  
ATOM   7804  CD2 LEU B 510     114.900 154.625 151.200  1.00 15.87           C  
ATOM   7805  OXT LEU B 510     110.211 155.270 151.796  1.00 15.87           O  
TER    7806      LEU B 510                                                      
ATOM   7807  N   LEU C   5     121.026 188.004 174.885  1.00 45.52           N  
ATOM   7808  CA  LEU C   5     120.813 188.156 176.316  1.00 45.52           C  
ATOM   7809  C   LEU C   5     122.069 188.701 176.995  1.00 45.52           C  
ATOM   7810  O   LEU C   5     123.178 188.232 176.738  1.00 45.52           O  
ATOM   7811  CB  LEU C   5     120.409 186.819 176.942  1.00 45.52           C  
ATOM   7812  CG  LEU C   5     119.701 186.861 178.293  1.00 45.52           C  
ATOM   7813  CD1 LEU C   5     118.243 187.248 178.124  1.00 45.52           C  
ATOM   7814  CD2 LEU C   5     119.820 185.516 178.993  1.00 45.52           C  
ATOM   7815  N   GLU C   6     121.882 189.703 177.857  1.00 49.24           N  
ATOM   7816  CA  GLU C   6     122.998 190.235 178.634  1.00 49.24           C  
ATOM   7817  C   GLU C   6     123.656 189.143 179.468  1.00 49.24           C  
ATOM   7818  O   GLU C   6     124.881 189.137 179.653  1.00 49.24           O  
ATOM   7819  CB  GLU C   6     122.506 191.366 179.539  1.00 49.24           C  
ATOM   7820  CG  GLU C   6     121.840 192.517 178.807  1.00 49.24           C  
ATOM   7821  CD  GLU C   6     122.833 193.409 178.091  1.00 49.24           C  
ATOM   7822  OE1 GLU C   6     122.397 194.383 177.442  1.00 49.24           O  
ATOM   7823  OE2 GLU C   6     124.049 193.139 178.180  1.00 49.24           O  
ATOM   7824  N   LYS C   7     122.856 188.206 179.979  1.00 43.11           N  
ATOM   7825  CA  LYS C   7     123.380 187.192 180.886  1.00 43.11           C  
ATOM   7826  C   LYS C   7     124.374 186.275 180.178  1.00 43.11           C  
ATOM   7827  O   LYS C   7     125.364 185.842 180.777  1.00 43.11           O  
ATOM   7828  CB  LYS C   7     122.217 186.402 181.488  1.00 43.11           C  
ATOM   7829  CG  LYS C   7     122.548 184.991 181.950  1.00 43.11           C  
ATOM   7830  CD  LYS C   7     123.502 185.003 183.124  1.00 43.11           C  
ATOM   7831  CE  LYS C   7     124.112 183.636 183.351  1.00 43.11           C  
ATOM   7832  NZ  LYS C   7     125.073 183.283 182.275  1.00 43.11           N  
ATOM   7833  N   LEU C   8     124.128 185.964 178.905  1.00 38.52           N  
ATOM   7834  CA  LEU C   8     125.089 185.163 178.149  1.00 38.52           C  
ATOM   7835  C   LEU C   8     126.385 185.935 177.928  1.00 38.52           C  
ATOM   7836  O   LEU C   8     127.482 185.361 177.988  1.00 38.52           O  
ATOM   7837  CB  LEU C   8     124.477 184.736 176.816  1.00 38.52           C  
ATOM   7838  CG  LEU C   8     125.417 184.206 175.731  1.00 38.52           C  
ATOM   7839  CD1 LEU C   8     126.171 182.973 176.206  1.00 38.52           C  
ATOM   7840  CD2 LEU C   8     124.640 183.893 174.478  1.00 38.52           C  
ATOM   7841  N   GLU C   9     126.278 187.240 177.672  1.00 41.50           N  
ATOM   7842  CA  GLU C   9     127.471 188.074 177.579  1.00 41.50           C  
ATOM   7843  C   GLU C   9     128.268 188.023 178.875  1.00 41.50           C  
ATOM   7844  O   GLU C   9     129.504 187.976 178.855  1.00 41.50           O  
ATOM   7845  CB  GLU C   9     127.077 189.512 177.244  1.00 41.50           C  
ATOM   7846  CG  GLU C   9     126.972 189.805 175.757  1.00 41.50           C  
ATOM   7847  CD  GLU C   9     128.304 189.715 175.039  1.00 41.50           C  
ATOM   7848  OE1 GLU C   9     129.346 189.615 175.720  1.00 41.50           O  
ATOM   7849  OE2 GLU C   9     128.309 189.746 173.791  1.00 41.50           O  
ATOM   7850  N   GLU C  10     127.573 188.007 180.015  1.00 38.71           N  
ATOM   7851  CA  GLU C  10     128.257 187.897 181.301  1.00 38.71           C  
ATOM   7852  C   GLU C  10     128.929 186.537 181.454  1.00 38.71           C  
ATOM   7853  O   GLU C  10     130.062 186.443 181.940  1.00 38.71           O  
ATOM   7854  CB  GLU C  10     127.264 188.148 182.437  1.00 38.71           C  
ATOM   7855  CG  GLU C  10     127.828 187.943 183.841  1.00 38.71           C  
ATOM   7856  CD  GLU C  10     127.789 186.490 184.296  1.00 38.71           C  
ATOM   7857  OE1 GLU C  10     127.276 185.637 183.544  1.00 38.71           O  
ATOM   7858  OE2 GLU C  10     128.273 186.202 185.411  1.00 38.71           O  
ATOM   7859  N   ARG C  11     128.221 185.466 181.093  1.00 29.99           N  
ATOM   7860  CA  ARG C  11     128.817 184.130 181.102  1.00 29.99           C  
ATOM   7861  C   ARG C  11     130.131 184.110 180.329  1.00 29.99           C  
ATOM   7862  O   ARG C  11     131.135 183.557 180.797  1.00 29.99           O  
ATOM   7863  CB  ARG C  11     127.839 183.119 180.502  1.00 29.99           C  
ATOM   7864  CG  ARG C  11     127.908 181.725 181.128  1.00 29.99           C  
ATOM   7865  CD  ARG C  11     126.965 180.753 180.438  1.00 29.99           C  
ATOM   7866  NE  ARG C  11     125.683 180.646 181.125  1.00 29.99           N  
ATOM   7867  CZ  ARG C  11     125.374 179.712 182.022  1.00 29.99           C  
ATOM   7868  NH1 ARG C  11     126.250 178.778 182.365  1.00 29.99           N  
ATOM   7869  NH2 ARG C  11     124.176 179.717 182.582  1.00 29.99           N  
ATOM   7870  N   ARG C  12     130.135 184.703 179.134  1.00 28.31           N  
ATOM   7871  CA  ARG C  12     131.349 184.739 178.324  1.00 28.31           C  
ATOM   7872  C   ARG C  12     132.438 185.571 178.998  1.00 28.31           C  
ATOM   7873  O   ARG C  12     133.606 185.157 179.061  1.00 28.31           O  
ATOM   7874  CB  ARG C  12     131.031 185.296 176.937  1.00 28.31           C  
ATOM   7875  CG  ARG C  12     130.030 184.490 176.130  1.00 28.31           C  
ATOM   7876  CD  ARG C  12     129.605 185.250 174.888  1.00 28.31           C  
ATOM   7877  NE  ARG C  12     129.059 184.390 173.844  1.00 28.31           N  
ATOM   7878  CZ  ARG C  12     128.698 184.819 172.637  1.00 28.31           C  
ATOM   7879  NH1 ARG C  12     128.823 186.100 172.317  1.00 28.31           N  
ATOM   7880  NH2 ARG C  12     128.211 183.969 171.745  1.00 28.31           N  
ATOM   7881  N   ALA C  13     132.078 186.767 179.478  1.00 32.33           N  
ATOM   7882  CA  ALA C  13     133.048 187.619 180.156  1.00 32.33           C  
ATOM   7883  C   ALA C  13     133.690 186.905 181.336  1.00 32.33           C  
ATOM   7884  O   ALA C  13     134.871 187.123 181.626  1.00 32.33           O  
ATOM   7885  CB  ALA C  13     132.376 188.912 180.620  1.00 32.33           C  
ATOM   7886  N   GLN C  14     132.938 186.040 182.017  1.00 31.49           N  
ATOM   7887  CA  GLN C  14     133.485 185.338 183.174  1.00 31.49           C  
ATOM   7888  C   GLN C  14     134.326 184.139 182.757  1.00 31.49           C  
ATOM   7889  O   GLN C  14     135.315 183.814 183.422  1.00 31.49           O  
ATOM   7890  CB  GLN C  14     132.361 184.894 184.108  1.00 31.49           C  
ATOM   7891  CG  GLN C  14     132.857 184.211 185.374  1.00 31.49           C  
ATOM   7892  CD  GLN C  14     132.646 182.712 185.363  1.00 31.49           C  
ATOM   7893  OE1 GLN C  14     131.515 182.230 185.301  1.00 31.49           O  
ATOM   7894  NE2 GLN C  14     133.740 181.966 185.418  1.00 31.49           N  
ATOM   7895  N   ALA C  15     133.948 183.462 181.671  1.00 28.42           N  
ATOM   7896  CA  ALA C  15     134.794 182.388 181.164  1.00 28.42           C  
ATOM   7897  C   ALA C  15     136.146 182.920 180.714  1.00 28.42           C  
ATOM   7898  O   ALA C  15     137.159 182.220 180.823  1.00 28.42           O  
ATOM   7899  CB  ALA C  15     134.110 181.664 180.006  1.00 28.42           C  
ATOM   7900  N   ARG C  16     136.180 184.152 180.210  1.00 28.51           N  
ATOM   7901  CA  ARG C  16     137.418 184.720 179.683  1.00 28.51           C  
ATOM   7902  C   ARG C  16     138.453 185.061 180.754  1.00 28.51           C  
ATOM   7903  O   ARG C  16     139.558 185.473 180.388  1.00 28.51           O  
ATOM   7904  CB  ARG C  16     137.111 185.978 178.873  1.00 28.51           C  
ATOM   7905  CG  ARG C  16     136.653 185.726 177.457  1.00 28.51           C  
ATOM   7906  CD  ARG C  16     136.443 187.032 176.726  1.00 28.51           C  
ATOM   7907  NE  ARG C  16     135.508 186.904 175.612  1.00 28.51           N  
ATOM   7908  CZ  ARG C  16     134.245 187.318 175.630  1.00 28.51           C  
ATOM   7909  NH1 ARG C  16     133.489 187.154 174.558  1.00 28.51           N  
ATOM   7910  NH2 ARG C  16     133.727 187.888 176.711  1.00 28.51           N  
ATOM   7911  N   LEU C  17     138.155 184.911 182.044  1.00 31.78           N  
ATOM   7912  CA  LEU C  17     139.085 185.304 183.096  1.00 31.78           C  
ATOM   7913  C   LEU C  17     139.873 184.139 183.679  1.00 31.78           C  
ATOM   7914  O   LEU C  17     140.729 184.361 184.540  1.00 31.78           O  
ATOM   7915  CB  LEU C  17     138.341 186.027 184.223  1.00 31.78           C  
ATOM   7916  CG  LEU C  17     137.758 187.405 183.893  1.00 31.78           C  
ATOM   7917  CD1 LEU C  17     137.249 188.071 185.154  1.00 31.78           C  
ATOM   7918  CD2 LEU C  17     138.781 188.296 183.205  1.00 31.78           C  
ATOM   7919  N   GLY C  18     139.614 182.918 183.240  1.00 29.76           N  
ATOM   7920  CA  GLY C  18     140.452 181.804 183.647  1.00 29.76           C  
ATOM   7921  C   GLY C  18     140.444 181.610 185.150  1.00 29.76           C  
ATOM   7922  O   GLY C  18     139.391 181.442 185.775  1.00 29.76           O  
ATOM   7923  N   GLY C  19     141.631 181.635 185.749  1.00 30.30           N  
ATOM   7924  CA  GLY C  19     141.811 181.360 187.157  1.00 30.30           C  
ATOM   7925  C   GLY C  19     141.907 182.568 188.066  1.00 30.30           C  
ATOM   7926  O   GLY C  19     142.302 182.411 189.227  1.00 30.30           O  
ATOM   7927  N   GLY C  20     141.561 183.762 187.588  1.00 35.37           N  
ATOM   7928  CA  GLY C  20     141.533 184.939 188.437  1.00 35.37           C  
ATOM   7929  C   GLY C  20     142.388 186.102 187.972  1.00 35.37           C  
ATOM   7930  O   GLY C  20     143.382 185.918 187.264  1.00 35.37           O  
ATOM   7931  N   GLU C  21     142.001 187.313 188.379  1.00 41.04           N  
ATOM   7932  CA  GLU C  21     142.758 188.507 188.015  1.00 41.04           C  
ATOM   7933  C   GLU C  21     144.175 188.457 188.574  1.00 41.04           C  
ATOM   7934  O   GLU C  21     145.132 188.873 187.909  1.00 41.04           O  
ATOM   7935  CB  GLU C  21     142.038 189.758 188.523  1.00 41.04           C  
ATOM   7936  CG  GLU C  21     140.626 189.926 188.001  1.00 41.04           C  
ATOM   7937  CD  GLU C  21     140.588 190.440 186.577  1.00 41.04           C  
ATOM   7938  OE1 GLU C  21     141.639 190.408 185.903  1.00 41.04           O  
ATOM   7939  OE2 GLU C  21     139.506 190.877 186.132  1.00 41.04           O  
ATOM   7940  N   LYS C  22     144.325 187.951 189.798  1.00 37.71           N  
ATOM   7941  CA  LYS C  22     145.630 187.933 190.450  1.00 37.71           C  
ATOM   7942  C   LYS C  22     146.606 187.028 189.707  1.00 37.71           C  
ATOM   7943  O   LYS C  22     147.763 187.397 189.473  1.00 37.71           O  
ATOM   7944  CB  LYS C  22     145.467 187.483 191.901  1.00 37.71           C  
ATOM   7945  CG  LYS C  22     146.724 187.582 192.734  1.00 37.71           C  
ATOM   7946  CD  LYS C  22     146.484 187.128 194.167  1.00 37.71           C  
ATOM   7947  CE  LYS C  22     145.498 188.031 194.897  1.00 37.71           C  
ATOM   7948  NZ  LYS C  22     145.865 189.472 194.814  1.00 37.71           N  
ATOM   7949  N   ARG C  23     146.159 185.825 189.343  1.00 31.09           N  
ATOM   7950  CA  ARG C  23     147.021 184.901 188.616  1.00 31.09           C  
ATOM   7951  C   ARG C  23     147.422 185.465 187.257  1.00 31.09           C  
ATOM   7952  O   ARG C  23     148.571 185.305 186.826  1.00 31.09           O  
ATOM   7953  CB  ARG C  23     146.322 183.550 188.463  1.00 31.09           C  
ATOM   7954  CG  ARG C  23     146.191 182.776 189.765  1.00 31.09           C  
ATOM   7955  CD  ARG C  23     145.805 181.331 189.524  1.00 31.09           C  
ATOM   7956  NE  ARG C  23     145.513 180.612 190.762  1.00 31.09           N  
ATOM   7957  CZ  ARG C  23     146.395 179.894 191.452  1.00 31.09           C  
ATOM   7958  NH1 ARG C  23     147.653 179.785 191.048  1.00 31.09           N  
ATOM   7959  NH2 ARG C  23     146.013 179.281 192.561  1.00 31.09           N  
ATOM   7960  N   LEU C  24     146.493 186.126 186.561  1.00 28.87           N  
ATOM   7961  CA  LEU C  24     146.834 186.705 185.266  1.00 28.87           C  
ATOM   7962  C   LEU C  24     147.838 187.843 185.428  1.00 28.87           C  
ATOM   7963  O   LEU C  24     148.770 187.981 184.625  1.00 28.87           O  
ATOM   7964  CB  LEU C  24     145.569 187.192 184.555  1.00 28.87           C  
ATOM   7965  CG  LEU C  24     144.504 186.150 184.189  1.00 28.87           C  
ATOM   7966  CD1 LEU C  24     143.210 186.838 183.791  1.00 28.87           C  
ATOM   7967  CD2 LEU C  24     144.962 185.211 183.078  1.00 28.87           C  
ATOM   7968  N   GLU C  25     147.680 188.652 186.479  1.00 30.98           N  
ATOM   7969  CA  GLU C  25     148.656 189.702 186.746  1.00 30.98           C  
ATOM   7970  C   GLU C  25     150.027 189.111 187.047  1.00 30.98           C  
ATOM   7971  O   GLU C  25     151.052 189.661 186.632  1.00 30.98           O  
ATOM   7972  CB  GLU C  25     148.189 190.578 187.908  1.00 30.98           C  
ATOM   7973  CG  GLU C  25     149.065 191.796 188.171  1.00 30.98           C  
ATOM   7974  CD  GLU C  25     149.387 192.580 186.912  1.00 30.98           C  
ATOM   7975  OE1 GLU C  25     150.544 192.512 186.446  1.00 30.98           O  
ATOM   7976  OE2 GLU C  25     148.483 193.262 186.387  1.00 30.98           O  
ATOM   7977  N   ALA C  26     150.064 187.994 187.774  1.00 26.13           N  
ATOM   7978  CA  ALA C  26     151.341 187.349 188.061  1.00 26.13           C  
ATOM   7979  C   ALA C  26     151.984 186.812 186.788  1.00 26.13           C  
ATOM   7980  O   ALA C  26     153.201 186.923 186.607  1.00 26.13           O  
ATOM   7981  CB  ALA C  26     151.145 186.231 189.081  1.00 26.13           C  
ATOM   7982  N   GLN C  27     151.182 186.227 185.897  1.00 20.49           N  
ATOM   7983  CA  GLN C  27     151.697 185.819 184.592  1.00 20.49           C  
ATOM   7984  C   GLN C  27     152.313 187.005 183.859  1.00 20.49           C  
ATOM   7985  O   GLN C  27     153.407 186.897 183.296  1.00 20.49           O  
ATOM   7986  CB  GLN C  27     150.575 185.189 183.764  1.00 20.49           C  
ATOM   7987  CG  GLN C  27     150.958 184.731 182.361  1.00 20.49           C  
ATOM   7988  CD  GLN C  27     151.426 183.290 182.309  1.00 20.49           C  
ATOM   7989  OE1 GLN C  27     151.925 182.749 183.293  1.00 20.49           O  
ATOM   7990  NE2 GLN C  27     151.258 182.659 181.155  1.00 20.49           N  
ATOM   7991  N   HIS C  28     151.626 188.147 183.863  1.00 21.85           N  
ATOM   7992  CA  HIS C  28     152.165 189.331 183.199  1.00 21.85           C  
ATOM   7993  C   HIS C  28     153.465 189.792 183.850  1.00 21.85           C  
ATOM   7994  O   HIS C  28     154.396 190.217 183.159  1.00 21.85           O  
ATOM   7995  CB  HIS C  28     151.133 190.458 183.212  1.00 21.85           C  
ATOM   7996  CG  HIS C  28     150.185 190.428 182.055  1.00 21.85           C  
ATOM   7997  ND1 HIS C  28     149.188 191.365 181.889  1.00 21.85           N  
ATOM   7998  CD2 HIS C  28     150.079 189.579 181.007  1.00 21.85           C  
ATOM   7999  CE1 HIS C  28     148.511 191.094 180.789  1.00 21.85           C  
ATOM   8000  NE2 HIS C  28     149.031 190.015 180.235  1.00 21.85           N  
ATOM   8001  N   LYS C  29     153.549 189.707 185.179  1.00 24.52           N  
ATOM   8002  CA  LYS C  29     154.750 190.153 185.879  1.00 24.52           C  
ATOM   8003  C   LYS C  29     155.958 189.288 185.541  1.00 24.52           C  
ATOM   8004  O   LYS C  29     157.092 189.776 185.561  1.00 24.52           O  
ATOM   8005  CB  LYS C  29     154.504 190.157 187.387  1.00 24.52           C  
ATOM   8006  CG  LYS C  29     155.638 190.740 188.201  1.00 24.52           C  
ATOM   8007  CD  LYS C  29     155.369 190.612 189.685  1.00 24.52           C  
ATOM   8008  CE  LYS C  29     156.544 191.096 190.510  1.00 24.52           C  
ATOM   8009  NZ  LYS C  29     156.386 190.744 191.947  1.00 24.52           N  
ATOM   8010  N   ARG C  30     155.742 188.009 185.233  1.00 24.07           N  
ATOM   8011  CA  ARG C  30     156.820 187.150 184.754  1.00 24.07           C  
ATOM   8012  C   ARG C  30     157.275 187.500 183.344  1.00 24.07           C  
ATOM   8013  O   ARG C  30     158.228 186.887 182.854  1.00 24.07           O  
ATOM   8014  CB  ARG C  30     156.388 185.684 184.774  1.00 24.07           C  
ATOM   8015  CG  ARG C  30     156.290 185.047 186.139  1.00 24.07           C  
ATOM   8016  CD  ARG C  30     155.035 184.194 186.221  1.00 24.07           C  
ATOM   8017  NE  ARG C  30     155.162 183.055 187.119  1.00 24.07           N  
ATOM   8018  CZ  ARG C  30     154.178 182.193 187.355  1.00 24.07           C  
ATOM   8019  NH1 ARG C  30     154.369 181.176 188.183  1.00 24.07           N  
ATOM   8020  NH2 ARG C  30     153.001 182.350 186.759  1.00 24.07           N  
ATOM   8021  N   GLY C  31     156.624 188.450 182.681  1.00 19.64           N  
ATOM   8022  CA  GLY C  31     156.944 188.746 181.301  1.00 19.64           C  
ATOM   8023  C   GLY C  31     156.363 187.768 180.310  1.00 19.64           C  
ATOM   8024  O   GLY C  31     156.962 187.536 179.257  1.00 19.64           O  
ATOM   8025  N   LYS C  32     155.207 187.187 180.616  1.00 16.87           N  
ATOM   8026  CA  LYS C  32     154.568 186.193 179.768  1.00 16.87           C  
ATOM   8027  C   LYS C  32     153.159 186.640 179.409  1.00 16.87           C  
ATOM   8028  O   LYS C  32     152.454 187.231 180.232  1.00 16.87           O  
ATOM   8029  CB  LYS C  32     154.516 184.826 180.454  1.00 16.87           C  
ATOM   8030  CG  LYS C  32     155.875 184.227 180.764  1.00 16.87           C  
ATOM   8031  CD  LYS C  32     155.813 182.732 180.897  1.00 16.87           C  
ATOM   8032  CE  LYS C  32     155.162 182.311 182.181  1.00 16.87           C  
ATOM   8033  NZ  LYS C  32     154.387 181.071 181.968  1.00 16.87           N  
ATOM   8034  N   LEU C  33     152.759 186.356 178.174  1.00 13.19           N  
ATOM   8035  CA  LEU C  33     151.409 186.614 177.708  1.00 13.19           C  
ATOM   8036  C   LEU C  33     150.447 185.551 178.237  1.00 13.19           C  
ATOM   8037  O   LEU C  33     150.848 184.502 178.744  1.00 13.19           O  
ATOM   8038  CB  LEU C  33     151.368 186.643 176.181  1.00 13.19           C  
ATOM   8039  CG  LEU C  33     152.078 187.794 175.462  1.00 13.19           C  
ATOM   8040  CD1 LEU C  33     151.894 187.684 173.959  1.00 13.19           C  
ATOM   8041  CD2 LEU C  33     151.571 189.124 175.964  1.00 13.19           C  
ATOM   8042  N   THR C  34     149.159 185.843 178.115  1.00 11.91           N  
ATOM   8043  CA  THR C  34     148.108 184.892 178.435  1.00 11.91           C  
ATOM   8044  C   THR C  34     147.759 184.059 177.203  1.00 11.91           C  
ATOM   8045  O   THR C  34     148.109 184.399 176.073  1.00 11.91           O  
ATOM   8046  CB  THR C  34     146.857 185.612 178.938  1.00 11.91           C  
ATOM   8047  OG1 THR C  34     146.344 186.456 177.904  1.00 11.91           O  
ATOM   8048  CG2 THR C  34     147.162 186.445 180.167  1.00 11.91           C  
ATOM   8049  N   ALA C  35     147.053 182.954 177.444  1.00 10.53           N  
ATOM   8050  CA  ALA C  35     146.636 182.068 176.359  1.00 10.53           C  
ATOM   8051  C   ALA C  35     145.876 182.827 175.275  1.00 10.53           C  
ATOM   8052  O   ALA C  35     146.205 182.742 174.081  1.00 10.53           O  
ATOM   8053  CB  ALA C  35     145.781 180.933 176.928  1.00 10.53           C  
ATOM   8054  N   ARG C  36     144.860 183.592 175.678  1.00 10.72           N  
ATOM   8055  CA  ARG C  36     144.001 184.252 174.705  1.00 10.72           C  
ATOM   8056  C   ARG C  36     144.745 185.361 173.968  1.00 10.72           C  
ATOM   8057  O   ARG C  36     144.528 185.560 172.769  1.00 10.72           O  
ATOM   8058  CB  ARG C  36     142.740 184.775 175.404  1.00 10.72           C  
ATOM   8059  CG  ARG C  36     141.789 183.654 175.832  1.00 10.72           C  
ATOM   8060  CD  ARG C  36     140.595 184.123 176.645  1.00 10.72           C  
ATOM   8061  NE  ARG C  36     139.777 182.990 177.063  1.00 10.72           N  
ATOM   8062  CZ  ARG C  36     138.917 182.356 176.276  1.00 10.72           C  
ATOM   8063  NH1 ARG C  36     138.746 182.739 175.023  1.00 10.72           N  
ATOM   8064  NH2 ARG C  36     138.228 181.333 176.746  1.00 10.72           N  
ATOM   8065  N   GLU C  37     145.656 186.058 174.647  1.00 12.52           N  
ATOM   8066  CA  GLU C  37     146.484 187.051 173.968  1.00 12.52           C  
ATOM   8067  C   GLU C  37     147.376 186.400 172.911  1.00 12.52           C  
ATOM   8068  O   GLU C  37     147.568 186.956 171.822  1.00 12.52           O  
ATOM   8069  CB  GLU C  37     147.326 187.819 174.990  1.00 12.52           C  
ATOM   8070  CG  GLU C  37     146.528 188.738 175.909  1.00 12.52           C  
ATOM   8071  CD  GLU C  37     147.341 189.284 177.071  1.00 12.52           C  
ATOM   8072  OE1 GLU C  37     148.141 188.529 177.662  1.00 12.52           O  
ATOM   8073  OE2 GLU C  37     147.176 190.476 177.399  1.00 12.52           O  
ATOM   8074  N   ARG C  38     147.941 185.229 173.220  1.00  8.65           N  
ATOM   8075  CA  ARG C  38     148.756 184.509 172.246  1.00  8.65           C  
ATOM   8076  C   ARG C  38     147.929 184.135 171.019  1.00  8.65           C  
ATOM   8077  O   ARG C  38     148.342 184.381 169.875  1.00  8.65           O  
ATOM   8078  CB  ARG C  38     149.379 183.269 172.904  1.00  8.65           C  
ATOM   8079  CG  ARG C  38     150.432 183.587 173.972  1.00  8.65           C  
ATOM   8080  CD  ARG C  38     150.781 182.408 174.886  1.00  8.65           C  
ATOM   8081  NE  ARG C  38     151.856 182.753 175.815  1.00  8.65           N  
ATOM   8082  CZ  ARG C  38     152.179 182.057 176.900  1.00  8.65           C  
ATOM   8083  NH1 ARG C  38     151.513 180.962 177.218  1.00  8.65           N  
ATOM   8084  NH2 ARG C  38     153.174 182.464 177.672  1.00  8.65           N  
ATOM   8085  N   ILE C  39     146.740 183.565 171.237  1.00  9.23           N  
ATOM   8086  CA  ILE C  39     145.867 183.253 170.108  1.00  9.23           C  
ATOM   8087  C   ILE C  39     145.575 184.518 169.305  1.00  9.23           C  
ATOM   8088  O   ILE C  39     145.554 184.496 168.071  1.00  9.23           O  
ATOM   8089  CB  ILE C  39     144.569 182.570 170.587  1.00  9.23           C  
ATOM   8090  CG1 ILE C  39     144.844 181.131 171.038  1.00  9.23           C  
ATOM   8091  CG2 ILE C  39     143.518 182.571 169.476  1.00  9.23           C  
ATOM   8092  CD1 ILE C  39     143.743 180.517 171.886  1.00  9.23           C  
ATOM   8093  N   GLU C  40     145.385 185.646 169.991  1.00 13.36           N  
ATOM   8094  CA  GLU C  40     145.057 186.890 169.299  1.00 13.36           C  
ATOM   8095  C   GLU C  40     146.209 187.357 168.420  1.00 13.36           C  
ATOM   8096  O   GLU C  40     145.990 187.862 167.315  1.00 13.36           O  
ATOM   8097  CB  GLU C  40     144.698 187.976 170.311  1.00 13.36           C  
ATOM   8098  CG  GLU C  40     144.138 189.238 169.694  1.00 13.36           C  
ATOM   8099  CD  GLU C  40     143.717 190.265 170.726  1.00 13.36           C  
ATOM   8100  OE1 GLU C  40     144.126 190.143 171.899  1.00 13.36           O  
ATOM   8101  OE2 GLU C  40     142.975 191.200 170.361  1.00 13.36           O  
ATOM   8102  N   LEU C  41     147.442 187.205 168.901  1.00 10.51           N  
ATOM   8103  CA  LEU C  41     148.597 187.673 168.141  1.00 10.51           C  
ATOM   8104  C   LEU C  41     148.919 186.746 166.974  1.00 10.51           C  
ATOM   8105  O   LEU C  41     149.504 187.188 165.982  1.00 10.51           O  
ATOM   8106  CB  LEU C  41     149.811 187.811 169.062  1.00 10.51           C  
ATOM   8107  CG  LEU C  41     151.082 188.475 168.525  1.00 10.51           C  
ATOM   8108  CD1 LEU C  41     150.773 189.825 167.912  1.00 10.51           C  
ATOM   8109  CD2 LEU C  41     152.101 188.629 169.636  1.00 10.51           C  
ATOM   8110  N   LEU C  42     148.546 185.467 167.068  1.00  7.55           N  
ATOM   8111  CA  LEU C  42     148.878 184.530 165.997  1.00  7.55           C  
ATOM   8112  C   LEU C  42     147.948 184.671 164.790  1.00  7.55           C  
ATOM   8113  O   LEU C  42     148.412 184.637 163.646  1.00  7.55           O  
ATOM   8114  CB  LEU C  42     148.851 183.096 166.530  1.00  7.55           C  
ATOM   8115  CG  LEU C  42     149.021 181.953 165.528  1.00  7.55           C  
ATOM   8116  CD1 LEU C  42     150.335 182.082 164.803  1.00  7.55           C  
ATOM   8117  CD2 LEU C  42     148.936 180.601 166.209  1.00  7.55           C  
ATOM   8118  N   LEU C  43     146.648 184.829 165.015  1.00  7.57           N  
ATOM   8119  CA  LEU C  43     145.656 184.763 163.948  1.00  7.57           C  
ATOM   8120  C   LEU C  43     145.367 186.141 163.353  1.00  7.57           C  
ATOM   8121  O   LEU C  43     145.611 187.180 163.969  1.00  7.57           O  
ATOM   8122  CB  LEU C  43     144.354 184.152 164.463  1.00  7.57           C  
ATOM   8123  CG  LEU C  43     144.376 182.719 164.999  1.00  7.57           C  
ATOM   8124  CD1 LEU C  43     143.009 182.340 165.521  1.00  7.57           C  
ATOM   8125  CD2 LEU C  43     144.851 181.732 163.942  1.00  7.57           C  
ATOM   8126  N   ASP C  44     144.818 186.129 162.136  1.00  9.34           N  
ATOM   8127  CA  ASP C  44     144.359 187.354 161.500  1.00  9.34           C  
ATOM   8128  C   ASP C  44     143.225 187.977 162.308  1.00  9.34           C  
ATOM   8129  O   ASP C  44     142.431 187.285 162.950  1.00  9.34           O  
ATOM   8130  CB  ASP C  44     143.886 187.085 160.064  1.00  9.34           C  
ATOM   8131  CG  ASP C  44     144.991 186.555 159.162  1.00  9.34           C  
ATOM   8132  OD1 ASP C  44     146.143 187.019 159.276  1.00  9.34           O  
ATOM   8133  OD2 ASP C  44     144.704 185.681 158.323  1.00  9.34           O  
ATOM   8134  N   HIS C  45     143.152 189.302 162.257  1.00 12.77           N  
ATOM   8135  CA  HIS C  45     142.215 190.057 163.079  1.00 12.77           C  
ATOM   8136  C   HIS C  45     140.770 189.694 162.758  1.00 12.77           C  
ATOM   8137  O   HIS C  45     140.332 189.807 161.611  1.00 12.77           O  
ATOM   8138  CB  HIS C  45     142.442 191.552 162.872  1.00 12.77           C  
ATOM   8139  CG  HIS C  45     141.468 192.414 163.609  1.00 12.77           C  
ATOM   8140  ND1 HIS C  45     140.412 193.041 162.986  1.00 12.77           N  
ATOM   8141  CD2 HIS C  45     141.382 192.744 164.918  1.00 12.77           C  
ATOM   8142  CE1 HIS C  45     139.721 193.726 163.878  1.00 12.77           C  
ATOM   8143  NE2 HIS C  45     140.289 193.562 165.059  1.00 12.77           N  
ATOM   8144  N   GLY C  46     140.031 189.265 163.781  1.00 10.57           N  
ATOM   8145  CA  GLY C  46     138.622 188.955 163.667  1.00 10.57           C  
ATOM   8146  C   GLY C  46     138.284 187.557 163.197  1.00 10.57           C  
ATOM   8147  O   GLY C  46     137.096 187.248 163.046  1.00 10.57           O  
ATOM   8148  N   SER C  47     139.274 186.702 162.972  1.00  8.17           N  
ATOM   8149  CA  SER C  47     139.053 185.404 162.353  1.00  8.17           C  
ATOM   8150  C   SER C  47     138.859 184.264 163.348  1.00  8.17           C  
ATOM   8151  O   SER C  47     138.520 183.155 162.925  1.00  8.17           O  
ATOM   8152  CB  SER C  47     140.231 185.064 161.443  1.00  8.17           C  
ATOM   8153  OG  SER C  47     141.355 184.709 162.214  1.00  8.17           O  
ATOM   8154  N   PHE C  48     139.078 184.492 164.639  1.00  6.36           N  
ATOM   8155  CA  PHE C  48     139.111 183.403 165.611  1.00  6.36           C  
ATOM   8156  C   PHE C  48     137.702 182.927 165.945  1.00  6.36           C  
ATOM   8157  O   PHE C  48     136.858 183.722 166.369  1.00  6.36           O  
ATOM   8158  CB  PHE C  48     139.832 183.840 166.884  1.00  6.36           C  
ATOM   8159  CG  PHE C  48     139.886 182.770 167.947  1.00  6.36           C  
ATOM   8160  CD1 PHE C  48     140.273 181.485 167.633  1.00  6.36           C  
ATOM   8161  CD2 PHE C  48     139.550 183.047 169.258  1.00  6.36           C  
ATOM   8162  CE1 PHE C  48     140.322 180.501 168.596  1.00  6.36           C  
ATOM   8163  CE2 PHE C  48     139.597 182.058 170.225  1.00  6.36           C  
ATOM   8164  CZ  PHE C  48     139.985 180.791 169.889  1.00  6.36           C  
ATOM   8165  N   GLU C  49     137.452 181.632 165.749  1.00  8.72           N  
ATOM   8166  CA  GLU C  49     136.239 180.964 166.208  1.00  8.72           C  
ATOM   8167  C   GLU C  49     136.627 179.917 167.242  1.00  8.72           C  
ATOM   8168  O   GLU C  49     137.386 178.986 166.939  1.00  8.72           O  
ATOM   8169  CB  GLU C  49     135.459 180.314 165.062  1.00  8.72           C  
ATOM   8170  CG  GLU C  49     134.205 179.584 165.541  1.00  8.72           C  
ATOM   8171  CD  GLU C  49     133.210 179.292 164.432  1.00  8.72           C  
ATOM   8172  OE1 GLU C  49     133.620 178.752 163.385  1.00  8.72           O  
ATOM   8173  OE2 GLU C  49     132.016 179.605 164.613  1.00  8.72           O  
ATOM   8174  N   GLU C  50     136.099 180.077 168.452  1.00  9.43           N  
ATOM   8175  CA  GLU C  50     136.424 179.243 169.598  1.00  9.43           C  
ATOM   8176  C   GLU C  50     135.432 178.095 169.752  1.00  9.43           C  
ATOM   8177  O   GLU C  50     134.239 178.237 169.477  1.00  9.43           O  
ATOM   8178  CB  GLU C  50     136.438 180.080 170.880  1.00  9.43           C  
ATOM   8179  CG  GLU C  50     136.861 179.308 172.112  1.00  9.43           C  
ATOM   8180  CD  GLU C  50     137.009 180.171 173.354  1.00  9.43           C  
ATOM   8181  OE1 GLU C  50     136.928 181.409 173.242  1.00  9.43           O  
ATOM   8182  OE2 GLU C  50     137.204 179.603 174.451  1.00  9.43           O  
ATOM   8183  N   PHE C  51     135.944 176.952 170.198  1.00  8.61           N  
ATOM   8184  CA  PHE C  51     135.137 175.786 170.524  1.00  8.61           C  
ATOM   8185  C   PHE C  51     135.139 175.535 172.026  1.00  8.61           C  
ATOM   8186  O   PHE C  51     136.176 175.642 172.687  1.00  8.61           O  
ATOM   8187  CB  PHE C  51     135.656 174.523 169.827  1.00  8.61           C  
ATOM   8188  CG  PHE C  51     135.561 174.548 168.329  1.00  8.61           C  
ATOM   8189  CD1 PHE C  51     134.631 175.331 167.676  1.00  8.61           C  
ATOM   8190  CD2 PHE C  51     136.407 173.761 167.573  1.00  8.61           C  
ATOM   8191  CE1 PHE C  51     134.557 175.332 166.302  1.00  8.61           C  
ATOM   8192  CE2 PHE C  51     136.333 173.763 166.200  1.00  8.61           C  
ATOM   8193  CZ  PHE C  51     135.408 174.548 165.568  1.00  8.61           C  
ATOM   8194  N   ASP C  52     133.970 175.184 172.554  1.00  9.30           N  
ATOM   8195  CA  ASP C  52     133.847 174.562 173.872  1.00  9.30           C  
ATOM   8196  C   ASP C  52     134.316 175.488 175.001  1.00  9.30           C  
ATOM   8197  O   ASP C  52     135.099 175.104 175.869  1.00  9.30           O  
ATOM   8198  CB  ASP C  52     134.606 173.232 173.893  1.00  9.30           C  
ATOM   8199  CG  ASP C  52     134.005 172.205 172.956  1.00  9.30           C  
ATOM   8200  OD1 ASP C  52     132.849 171.798 173.181  1.00  9.30           O  
ATOM   8201  OD2 ASP C  52     134.686 171.817 171.986  1.00  9.30           O  
ATOM   8202  N   MET C  53     133.801 176.721 174.994  1.00 13.09           N  
ATOM   8203  CA  MET C  53     134.172 177.706 176.008  1.00 13.09           C  
ATOM   8204  C   MET C  53     133.668 177.327 177.400  1.00 13.09           C  
ATOM   8205  O   MET C  53     134.274 177.729 178.398  1.00 13.09           O  
ATOM   8206  CB  MET C  53     133.639 179.083 175.599  1.00 13.09           C  
ATOM   8207  CG  MET C  53     133.890 180.207 176.596  1.00 13.09           C  
ATOM   8208  SD  MET C  53     132.956 181.695 176.203  1.00 13.09           S  
ATOM   8209  CE  MET C  53     134.245 182.727 175.526  1.00 13.09           C  
ATOM   8210  N   PHE C  54     132.578 176.565 177.492  1.00 11.85           N  
ATOM   8211  CA  PHE C  54     131.906 176.288 178.759  1.00 11.85           C  
ATOM   8212  C   PHE C  54     132.177 174.890 179.312  1.00 11.85           C  
ATOM   8213  O   PHE C  54     131.549 174.497 180.299  1.00 11.85           O  
ATOM   8214  CB  PHE C  54     130.398 176.483 178.600  1.00 11.85           C  
ATOM   8215  CG  PHE C  54     129.991 177.892 178.272  1.00 11.85           C  
ATOM   8216  CD1 PHE C  54     130.675 178.971 178.794  1.00 11.85           C  
ATOM   8217  CD2 PHE C  54     128.912 178.134 177.451  1.00 11.85           C  
ATOM   8218  CE1 PHE C  54     130.294 180.255 178.498  1.00 11.85           C  
ATOM   8219  CE2 PHE C  54     128.530 179.421 177.153  1.00 11.85           C  
ATOM   8220  CZ  PHE C  54     129.222 180.480 177.679  1.00 11.85           C  
ATOM   8221  N   VAL C  55     133.095 174.135 178.711  1.00 10.17           N  
ATOM   8222  CA  VAL C  55     133.362 172.776 179.171  1.00 10.17           C  
ATOM   8223  C   VAL C  55     133.941 172.805 180.586  1.00 10.17           C  
ATOM   8224  O   VAL C  55     134.788 173.644 180.918  1.00 10.17           O  
ATOM   8225  CB  VAL C  55     134.294 172.065 178.173  1.00 10.17           C  
ATOM   8226  CG1 VAL C  55     134.941 170.837 178.784  1.00 10.17           C  
ATOM   8227  CG2 VAL C  55     133.531 171.684 176.899  1.00 10.17           C  
ATOM   8228  N   GLN C  56     133.462 171.890 181.434  1.00 14.54           N  
ATOM   8229  CA  GLN C  56     133.881 171.761 182.828  1.00 14.54           C  
ATOM   8230  C   GLN C  56     134.283 170.320 183.131  1.00 14.54           C  
ATOM   8231  O   GLN C  56     133.854 169.382 182.456  1.00 14.54           O  
ATOM   8232  CB  GLN C  56     132.766 172.180 183.801  1.00 14.54           C  
ATOM   8233  CG  GLN C  56     132.429 173.649 183.805  1.00 14.54           C  
ATOM   8234  CD  GLN C  56     131.238 173.957 184.686  1.00 14.54           C  
ATOM   8235  OE1 GLN C  56     130.439 173.078 185.004  1.00 14.54           O  
ATOM   8236  NE2 GLN C  56     131.115 175.212 185.083  1.00 14.54           N  
ATOM   8237  N   HIS C  57     135.102 170.151 184.170  1.00 16.39           N  
ATOM   8238  CA  HIS C  57     135.521 168.827 184.615  1.00 16.39           C  
ATOM   8239  C   HIS C  57     134.429 168.160 185.451  1.00 16.39           C  
ATOM   8240  O   HIS C  57     133.525 168.811 185.976  1.00 16.39           O  
ATOM   8241  CB  HIS C  57     136.833 168.900 185.409  1.00 16.39           C  
ATOM   8242  CG  HIS C  57     136.680 169.381 186.818  1.00 16.39           C  
ATOM   8243  ND1 HIS C  57     137.100 170.627 187.225  1.00 16.39           N  
ATOM   8244  CD2 HIS C  57     136.192 168.772 187.923  1.00 16.39           C  
ATOM   8245  CE1 HIS C  57     136.857 170.772 188.515  1.00 16.39           C  
ATOM   8246  NE2 HIS C  57     136.302 169.662 188.961  1.00 16.39           N  
ATOM   8247  N   ARG C  58     134.529 166.834 185.566  1.00 19.75           N  
ATOM   8248  CA  ARG C  58     133.530 166.018 186.250  1.00 19.75           C  
ATOM   8249  C   ARG C  58     134.157 165.143 187.335  1.00 19.75           C  
ATOM   8250  O   ARG C  58     133.624 164.084 187.669  1.00 19.75           O  
ATOM   8251  CB  ARG C  58     132.765 165.162 185.243  1.00 19.75           C  
ATOM   8252  CG  ARG C  58     131.902 165.976 184.292  1.00 19.75           C  
ATOM   8253  CD  ARG C  58     131.230 165.118 183.239  1.00 19.75           C  
ATOM   8254  NE  ARG C  58     132.162 164.665 182.213  1.00 19.75           N  
ATOM   8255  CZ  ARG C  58     132.684 165.441 181.266  1.00 19.75           C  
ATOM   8256  NH1 ARG C  58     132.383 166.734 181.192  1.00 19.75           N  
ATOM   8257  NH2 ARG C  58     133.520 164.915 180.387  1.00 19.75           N  
ATOM   8258  N   SER C  59     135.283 165.573 187.896  1.00 24.68           N  
ATOM   8259  CA  SER C  59     135.926 164.851 188.986  1.00 24.68           C  
ATOM   8260  C   SER C  59     135.310 165.229 190.329  1.00 24.68           C  
ATOM   8261  O   SER C  59     134.936 166.382 190.556  1.00 24.68           O  
ATOM   8262  CB  SER C  59     137.426 165.143 189.003  1.00 24.68           C  
ATOM   8263  OG  SER C  59     138.116 164.222 189.828  1.00 24.68           O  
ATOM   8264  N   THR C  60     135.205 164.242 191.220  1.00 33.21           N  
ATOM   8265  CA  THR C  60     134.659 164.442 192.559  1.00 33.21           C  
ATOM   8266  C   THR C  60     135.624 164.027 193.664  1.00 33.21           C  
ATOM   8267  O   THR C  60     135.204 163.909 194.821  1.00 33.21           O  
ATOM   8268  CB  THR C  60     133.347 163.668 192.725  1.00 33.21           C  
ATOM   8269  OG1 THR C  60     133.540 162.302 192.339  1.00 33.21           O  
ATOM   8270  CG2 THR C  60     132.243 164.283 191.887  1.00 33.21           C  
ATOM   8271  N   ASP C  61     136.894 163.805 193.351  1.00 33.48           N  
ATOM   8272  CA  ASP C  61     137.864 163.345 194.332  1.00 33.48           C  
ATOM   8273  C   ASP C  61     138.705 164.506 194.850  1.00 33.48           C  
ATOM   8274  O   ASP C  61     139.004 165.458 194.125  1.00 33.48           O  
ATOM   8275  CB  ASP C  61     138.775 162.269 193.736  1.00 33.48           C  
ATOM   8276  CG  ASP C  61     138.089 160.921 193.611  1.00 33.48           C  
ATOM   8277  OD1 ASP C  61     137.090 160.688 194.323  1.00 33.48           O  
ATOM   8278  OD2 ASP C  61     138.553 160.089 192.804  1.00 33.48           O  
ATOM   8279  N   PHE C  62     139.070 164.417 196.128  1.00 31.21           N  
ATOM   8280  CA  PHE C  62     139.990 165.358 196.770  1.00 31.21           C  
ATOM   8281  C   PHE C  62     139.493 166.800 196.681  1.00 31.21           C  
ATOM   8282  O   PHE C  62     140.278 167.736 196.516  1.00 31.21           O  
ATOM   8283  CB  PHE C  62     141.395 165.231 196.181  1.00 31.21           C  
ATOM   8284  CG  PHE C  62     141.961 163.848 196.260  1.00 31.21           C  
ATOM   8285  CD1 PHE C  62     142.303 163.295 197.479  1.00 31.21           C  
ATOM   8286  CD2 PHE C  62     142.150 163.097 195.117  1.00 31.21           C  
ATOM   8287  CE1 PHE C  62     142.822 162.027 197.552  1.00 31.21           C  
ATOM   8288  CE2 PHE C  62     142.666 161.828 195.190  1.00 31.21           C  
ATOM   8289  CZ  PHE C  62     143.002 161.293 196.408  1.00 31.21           C  
ATOM   8290  N   GLY C  63     138.182 166.988 196.810  1.00 36.10           N  
ATOM   8291  CA  GLY C  63     137.615 168.319 196.895  1.00 36.10           C  
ATOM   8292  C   GLY C  63     137.523 169.073 195.589  1.00 36.10           C  
ATOM   8293  O   GLY C  63     137.269 170.283 195.610  1.00 36.10           O  
ATOM   8294  N   MET C  64     137.717 168.403 194.454  1.00 34.42           N  
ATOM   8295  CA  MET C  64     137.715 169.087 193.166  1.00 34.42           C  
ATOM   8296  C   MET C  64     136.332 169.578 192.758  1.00 34.42           C  
ATOM   8297  O   MET C  64     136.236 170.523 191.970  1.00 34.42           O  
ATOM   8298  CB  MET C  64     138.261 168.158 192.084  1.00 34.42           C  
ATOM   8299  CG  MET C  64     139.761 167.956 192.133  1.00 34.42           C  
ATOM   8300  SD  MET C  64     140.702 169.423 191.679  1.00 34.42           S  
ATOM   8301  CE  MET C  64     140.294 169.559 189.944  1.00 34.42           C  
ATOM   8302  N   GLU C  65     135.263 168.963 193.266  1.00 39.48           N  
ATOM   8303  CA  GLU C  65     133.919 169.359 192.861  1.00 39.48           C  
ATOM   8304  C   GLU C  65     133.585 170.789 193.264  1.00 39.48           C  
ATOM   8305  O   GLU C  65     132.662 171.380 192.695  1.00 39.48           O  
ATOM   8306  CB  GLU C  65     132.884 168.396 193.451  1.00 39.48           C  
ATOM   8307  CG  GLU C  65     132.726 168.455 194.968  1.00 39.48           C  
ATOM   8308  CD  GLU C  65     133.740 167.605 195.707  1.00 39.48           C  
ATOM   8309  OE1 GLU C  65     134.493 166.857 195.050  1.00 39.48           O  
ATOM   8310  OE2 GLU C  65     133.784 167.687 196.952  1.00 39.48           O  
ATOM   8311  N   LYS C  66     134.309 171.357 194.225  1.00 42.04           N  
ATOM   8312  CA  LYS C  66     134.009 172.696 194.712  1.00 42.04           C  
ATOM   8313  C   LYS C  66     134.620 173.798 193.860  1.00 42.04           C  
ATOM   8314  O   LYS C  66     134.301 174.971 194.078  1.00 42.04           O  
ATOM   8315  CB  LYS C  66     134.498 172.844 196.153  1.00 42.04           C  
ATOM   8316  CG  LYS C  66     133.690 172.055 197.162  1.00 42.04           C  
ATOM   8317  CD  LYS C  66     134.280 172.161 198.556  1.00 42.04           C  
ATOM   8318  CE  LYS C  66     135.558 171.354 198.679  1.00 42.04           C  
ATOM   8319  NZ  LYS C  66     136.050 171.297 200.079  1.00 42.04           N  
ATOM   8320  N   GLN C  67     135.482 173.461 192.903  1.00 36.65           N  
ATOM   8321  CA  GLN C  67     136.144 174.441 192.044  1.00 36.65           C  
ATOM   8322  C   GLN C  67     136.070 173.967 190.595  1.00 36.65           C  
ATOM   8323  O   GLN C  67     137.003 173.349 190.079  1.00 36.65           O  
ATOM   8324  CB  GLN C  67     137.583 174.666 192.513  1.00 36.65           C  
ATOM   8325  CG  GLN C  67     138.415 173.406 192.645  1.00 36.65           C  
ATOM   8326  CD  GLN C  67     139.780 173.679 193.244  1.00 36.65           C  
ATOM   8327  OE1 GLN C  67     140.148 174.830 193.476  1.00 36.65           O  
ATOM   8328  NE2 GLN C  67     140.530 172.617 193.517  1.00 36.65           N  
ATOM   8329  N   LYS C  68     134.965 174.296 189.932  1.00 27.48           N  
ATOM   8330  CA  LYS C  68     134.783 174.044 188.511  1.00 27.48           C  
ATOM   8331  C   LYS C  68     135.028 175.351 187.770  1.00 27.48           C  
ATOM   8332  O   LYS C  68     134.405 176.371 188.081  1.00 27.48           O  
ATOM   8333  CB  LYS C  68     133.383 173.509 188.216  1.00 27.48           C  
ATOM   8334  CG  LYS C  68     132.965 172.346 189.094  1.00 27.48           C  
ATOM   8335  CD  LYS C  68     132.057 171.379 188.363  1.00 27.48           C  
ATOM   8336  CE  LYS C  68     131.600 170.248 189.267  1.00 27.48           C  
ATOM   8337  NZ  LYS C  68     132.575 169.114 189.306  1.00 27.48           N  
ATOM   8338  N   ILE C  69     135.940 175.324 186.807  1.00 16.90           N  
ATOM   8339  CA  ILE C  69     136.369 176.509 186.079  1.00 16.90           C  
ATOM   8340  C   ILE C  69     136.030 176.312 184.604  1.00 16.90           C  
ATOM   8341  O   ILE C  69     136.491 175.348 183.989  1.00 16.90           O  
ATOM   8342  CB  ILE C  69     137.872 176.777 186.263  1.00 16.90           C  
ATOM   8343  CG1 ILE C  69     138.190 177.058 187.735  1.00 16.90           C  
ATOM   8344  CG2 ILE C  69     138.307 177.942 185.407  1.00 16.90           C  
ATOM   8345  CD1 ILE C  69     139.655 176.999 188.075  1.00 16.90           C  
ATOM   8346  N   PRO C  70     135.242 177.195 183.984  1.00 14.41           N  
ATOM   8347  CA  PRO C  70     134.898 177.001 182.569  1.00 14.41           C  
ATOM   8348  C   PRO C  70     136.123 177.009 181.665  1.00 14.41           C  
ATOM   8349  O   PRO C  70     137.055 177.794 181.849  1.00 14.41           O  
ATOM   8350  CB  PRO C  70     133.957 178.174 182.269  1.00 14.41           C  
ATOM   8351  CG  PRO C  70     134.214 179.162 183.314  1.00 14.41           C  
ATOM   8352  CD  PRO C  70     134.626 178.416 184.529  1.00 14.41           C  
ATOM   8353  N   GLY C  71     136.104 176.112 180.678  1.00 12.52           N  
ATOM   8354  CA  GLY C  71     137.196 175.896 179.758  1.00 12.52           C  
ATOM   8355  C   GLY C  71     138.132 174.767 180.151  1.00 12.52           C  
ATOM   8356  O   GLY C  71     138.745 174.149 179.276  1.00 12.52           O  
ATOM   8357  N   ASP C  72     138.254 174.491 181.449  1.00 13.72           N  
ATOM   8358  CA  ASP C  72     139.054 173.387 181.985  1.00 13.72           C  
ATOM   8359  C   ASP C  72     140.526 173.473 181.577  1.00 13.72           C  
ATOM   8360  O   ASP C  72     141.220 172.457 181.502  1.00 13.72           O  
ATOM   8361  CB  ASP C  72     138.473 172.028 181.586  1.00 13.72           C  
ATOM   8362  CG  ASP C  72     138.913 170.908 182.514  1.00 13.72           C  
ATOM   8363  OD1 ASP C  72     138.937 171.122 183.742  1.00 13.72           O  
ATOM   8364  OD2 ASP C  72     139.234 169.808 182.015  1.00 13.72           O  
ATOM   8365  N   GLY C  73     141.022 174.678 181.337  1.00 10.27           N  
ATOM   8366  CA  GLY C  73     142.444 174.907 181.217  1.00 10.27           C  
ATOM   8367  C   GLY C  73     143.038 174.865 179.824  1.00 10.27           C  
ATOM   8368  O   GLY C  73     144.254 174.695 179.706  1.00 10.27           O  
ATOM   8369  N   VAL C  74     142.237 175.022 178.774  1.00  7.78           N  
ATOM   8370  CA  VAL C  74     142.768 175.091 177.418  1.00  7.78           C  
ATOM   8371  C   VAL C  74     141.758 175.814 176.541  1.00  7.78           C  
ATOM   8372  O   VAL C  74     140.546 175.643 176.693  1.00  7.78           O  
ATOM   8373  CB  VAL C  74     143.111 173.684 176.868  1.00  7.78           C  
ATOM   8374  CG1 VAL C  74     141.876 172.794 176.792  1.00  7.78           C  
ATOM   8375  CG2 VAL C  74     143.797 173.792 175.512  1.00  7.78           C  
ATOM   8376  N   VAL C  75     142.273 176.633 175.626  1.00  5.73           N  
ATOM   8377  CA  VAL C  75     141.477 177.388 174.666  1.00  5.73           C  
ATOM   8378  C   VAL C  75     141.719 176.800 173.280  1.00  5.73           C  
ATOM   8379  O   VAL C  75     142.868 176.699 172.837  1.00  5.73           O  
ATOM   8380  CB  VAL C  75     141.831 178.885 174.699  1.00  5.73           C  
ATOM   8381  CG1 VAL C  75     140.843 179.689 173.867  1.00  5.73           C  
ATOM   8382  CG2 VAL C  75     141.904 179.408 176.141  1.00  5.73           C  
ATOM   8383  N   THR C  76     140.641 176.436 172.591  1.00  5.28           N  
ATOM   8384  CA  THR C  76     140.704 175.670 171.353  1.00  5.28           C  
ATOM   8385  C   THR C  76     139.855 176.330 170.272  1.00  5.28           C  
ATOM   8386  O   THR C  76     138.824 176.942 170.565  1.00  5.28           O  
ATOM   8387  CB  THR C  76     140.223 174.226 171.589  1.00  5.28           C  
ATOM   8388  OG1 THR C  76     138.953 174.241 172.248  1.00  5.28           O  
ATOM   8389  CG2 THR C  76     141.217 173.456 172.450  1.00  5.28           C  
ATOM   8390  N   GLY C  77     140.281 176.196 169.018  1.00  5.48           N  
ATOM   8391  CA  GLY C  77     139.465 176.683 167.917  1.00  5.48           C  
ATOM   8392  C   GLY C  77     140.234 176.767 166.611  1.00  5.48           C  
ATOM   8393  O   GLY C  77     141.214 176.049 166.401  1.00  5.48           O  
ATOM   8394  N   TRP C  78     139.755 177.650 165.731  1.00  5.70           N  
ATOM   8395  CA  TRP C  78     140.335 177.787 164.398  1.00  5.70           C  
ATOM   8396  C   TRP C  78     140.279 179.234 163.919  1.00  5.70           C  
ATOM   8397  O   TRP C  78     139.528 180.060 164.442  1.00  5.70           O  
ATOM   8398  CB  TRP C  78     139.636 176.869 163.383  1.00  5.70           C  
ATOM   8399  CG  TRP C  78     138.268 177.301 162.957  1.00  5.70           C  
ATOM   8400  CD1 TRP C  78     137.097 177.050 163.599  1.00  5.70           C  
ATOM   8401  CD2 TRP C  78     137.929 178.044 161.783  1.00  5.70           C  
ATOM   8402  NE1 TRP C  78     136.050 177.596 162.906  1.00  5.70           N  
ATOM   8403  CE2 TRP C  78     136.535 178.213 161.785  1.00  5.70           C  
ATOM   8404  CE3 TRP C  78     138.671 178.591 160.732  1.00  5.70           C  
ATOM   8405  CZ2 TRP C  78     135.869 178.900 160.780  1.00  5.70           C  
ATOM   8406  CZ3 TRP C  78     138.009 179.268 159.741  1.00  5.70           C  
ATOM   8407  CH2 TRP C  78     136.623 179.420 159.771  1.00  5.70           C  
ATOM   8408  N   GLY C  79     141.092 179.518 162.909  1.00  6.11           N  
ATOM   8409  CA  GLY C  79     141.111 180.822 162.280  1.00  6.11           C  
ATOM   8410  C   GLY C  79     141.925 180.811 161.003  1.00  6.11           C  
ATOM   8411  O   GLY C  79     142.112 179.766 160.379  1.00  6.11           O  
ATOM   8412  N   THR C  80     142.403 181.992 160.612  1.00  7.71           N  
ATOM   8413  CA  THR C  80     143.196 182.147 159.399  1.00  7.71           C  
ATOM   8414  C   THR C  80     144.522 182.850 159.680  1.00  7.71           C  
ATOM   8415  O   THR C  80     144.592 183.772 160.497  1.00  7.71           O  
ATOM   8416  CB  THR C  80     142.430 182.932 158.323  1.00  7.71           C  
ATOM   8417  OG1 THR C  80     142.037 184.204 158.843  1.00  7.71           O  
ATOM   8418  CG2 THR C  80     141.199 182.157 157.840  1.00  7.71           C  
ATOM   8419  N   VAL C  81     145.566 182.407 158.982  1.00  7.37           N  
ATOM   8420  CA  VAL C  81     146.870 183.062 158.946  1.00  7.37           C  
ATOM   8421  C   VAL C  81     147.141 183.434 157.492  1.00  7.37           C  
ATOM   8422  O   VAL C  81     147.218 182.558 156.621  1.00  7.37           O  
ATOM   8423  CB  VAL C  81     147.987 182.169 159.516  1.00  7.37           C  
ATOM   8424  CG1 VAL C  81     149.364 182.809 159.337  1.00  7.37           C  
ATOM   8425  CG2 VAL C  81     147.740 181.882 160.983  1.00  7.37           C  
ATOM   8426  N   ASN C  82     147.257 184.734 157.233  1.00 10.74           N  
ATOM   8427  CA  ASN C  82     147.411 185.271 155.881  1.00 10.74           C  
ATOM   8428  C   ASN C  82     146.376 184.684 154.920  1.00 10.74           C  
ATOM   8429  O   ASN C  82     146.666 184.391 153.760  1.00 10.74           O  
ATOM   8430  CB  ASN C  82     148.833 185.042 155.367  1.00 10.74           C  
ATOM   8431  CG  ASN C  82     149.181 185.935 154.198  1.00 10.74           C  
ATOM   8432  OD1 ASN C  82     148.636 187.027 154.055  1.00 10.74           O  
ATOM   8433  ND2 ASN C  82     150.103 185.480 153.363  1.00 10.74           N  
ATOM   8434  N   GLY C  83     145.146 184.521 155.408  1.00  9.61           N  
ATOM   8435  CA  GLY C  83     144.047 184.020 154.614  1.00  9.61           C  
ATOM   8436  C   GLY C  83     143.878 182.513 154.579  1.00  9.61           C  
ATOM   8437  O   GLY C  83     142.857 182.040 154.067  1.00  9.61           O  
ATOM   8438  N   ARG C  84     144.834 181.745 155.091  1.00  6.89           N  
ATOM   8439  CA  ARG C  84     144.789 180.288 155.019  1.00  6.89           C  
ATOM   8440  C   ARG C  84     144.357 179.684 156.356  1.00  6.89           C  
ATOM   8441  O   ARG C  84     144.785 180.135 157.419  1.00  6.89           O  
ATOM   8442  CB  ARG C  84     146.150 179.732 154.584  1.00  6.89           C  
ATOM   8443  CG  ARG C  84     146.748 180.420 153.344  1.00  6.89           C  
ATOM   8444  CD  ARG C  84     148.238 180.171 153.187  1.00  6.89           C  
ATOM   8445  NE  ARG C  84     148.528 178.808 152.760  1.00  6.89           N  
ATOM   8446  CZ  ARG C  84     149.641 178.143 153.051  1.00  6.89           C  
ATOM   8447  NH1 ARG C  84     150.590 178.704 153.776  1.00  6.89           N  
ATOM   8448  NH2 ARG C  84     149.811 176.912 152.604  1.00  6.89           N  
ATOM   8449  N   THR C  85     143.505 178.658 156.288  1.00  7.68           N  
ATOM   8450  CA  THR C  85     142.887 178.063 157.472  1.00  7.68           C  
ATOM   8451  C   THR C  85     143.909 177.338 158.345  1.00  7.68           C  
ATOM   8452  O   THR C  85     144.727 176.563 157.846  1.00  7.68           O  
ATOM   8453  CB  THR C  85     141.786 177.084 157.056  1.00  7.68           C  
ATOM   8454  OG1 THR C  85     140.763 177.780 156.338  1.00  7.68           O  
ATOM   8455  CG2 THR C  85     141.182 176.392 158.270  1.00  7.68           C  
ATOM   8456  N   VAL C  86     143.837 177.572 159.657  1.00 12.77           N  
ATOM   8457  CA  VAL C  86     144.653 176.872 160.644  1.00 12.77           C  
ATOM   8458  C   VAL C  86     143.818 176.595 161.893  1.00 12.77           C  
ATOM   8459  O   VAL C  86     143.001 177.421 162.309  1.00 12.77           O  
ATOM   8460  CB  VAL C  86     145.920 177.667 161.028  1.00 12.77           C  
ATOM   8461  CG1 VAL C  86     146.764 178.015 159.799  1.00 12.77           C  
ATOM   8462  CG2 VAL C  86     145.555 178.909 161.815  1.00 12.77           C  
ATOM   8463  N   PHE C  87     144.047 175.439 162.500  1.00 12.77           N  
ATOM   8464  CA  PHE C  87     143.481 175.061 163.786  1.00 12.77           C  
ATOM   8465  C   PHE C  87     144.521 175.255 164.883  1.00 12.77           C  
ATOM   8466  O   PHE C  87     145.725 175.274 164.620  1.00 12.77           O  
ATOM   8467  CB  PHE C  87     143.010 173.609 163.748  1.00 12.77           C  
ATOM   8468  CG  PHE C  87     141.821 173.384 162.862  1.00 12.77           C  
ATOM   8469  CD1 PHE C  87     141.979 173.129 161.516  1.00 12.77           C  
ATOM   8470  CD2 PHE C  87     140.546 173.437 163.375  1.00 12.77           C  
ATOM   8471  CE1 PHE C  87     140.882 172.930 160.706  1.00 12.77           C  
ATOM   8472  CE2 PHE C  87     139.455 173.236 162.569  1.00 12.77           C  
ATOM   8473  CZ  PHE C  87     139.623 172.986 161.235  1.00 12.77           C  
ATOM   8474  N   LEU C  88     144.055 175.391 166.125  1.00 12.77           N  
ATOM   8475  CA  LEU C  88     144.997 175.638 167.210  1.00 12.77           C  
ATOM   8476  C   LEU C  88     144.375 175.386 168.579  1.00 12.77           C  
ATOM   8477  O   LEU C  88     143.148 175.349 168.745  1.00 12.77           O  
ATOM   8478  CB  LEU C  88     145.551 177.067 167.141  1.00 12.77           C  
ATOM   8479  CG  LEU C  88     144.681 178.244 167.570  1.00 12.77           C  
ATOM   8480  CD1 LEU C  88     145.526 179.515 167.604  1.00 12.77           C  
ATOM   8481  CD2 LEU C  88     143.491 178.412 166.661  1.00 12.77           C  
ATOM   8482  N   PHE C  89     145.271 175.221 169.558  1.00 12.77           N  
ATOM   8483  CA  PHE C  89     144.946 175.146 170.976  1.00 12.77           C  
ATOM   8484  C   PHE C  89     146.068 175.780 171.797  1.00 12.77           C  
ATOM   8485  O   PHE C  89     147.227 175.806 171.377  1.00 12.77           O  
ATOM   8486  CB  PHE C  89     144.690 173.704 171.444  1.00 12.77           C  
ATOM   8487  CG  PHE C  89     145.884 172.791 171.365  1.00 12.77           C  
ATOM   8488  CD1 PHE C  89     146.792 172.727 172.402  1.00 12.77           C  
ATOM   8489  CD2 PHE C  89     146.066 171.949 170.286  1.00 12.77           C  
ATOM   8490  CE1 PHE C  89     147.865 171.880 172.342  1.00 12.77           C  
ATOM   8491  CE2 PHE C  89     147.142 171.097 170.234  1.00 12.77           C  
ATOM   8492  CZ  PHE C  89     148.039 171.065 171.259  1.00 12.77           C  
ATOM   8493  N   SER C  90     145.704 176.281 172.978  1.00  7.40           N  
ATOM   8494  CA  SER C  90     146.605 177.032 173.851  1.00  7.40           C  
ATOM   8495  C   SER C  90     146.277 176.727 175.308  1.00  7.40           C  
ATOM   8496  O   SER C  90     145.154 176.971 175.756  1.00  7.40           O  
ATOM   8497  CB  SER C  90     146.497 178.535 173.582  1.00  7.40           C  
ATOM   8498  OG  SER C  90     147.259 179.272 174.510  1.00  7.40           O  
ATOM   8499  N   LYS C  91     147.258 176.199 176.040  1.00  9.81           N  
ATOM   8500  CA  LYS C  91     147.075 175.811 177.435  1.00  9.81           C  
ATOM   8501  C   LYS C  91     147.178 177.030 178.347  1.00  9.81           C  
ATOM   8502  O   LYS C  91     147.987 177.930 178.114  1.00  9.81           O  
ATOM   8503  CB  LYS C  91     148.110 174.751 177.826  1.00  9.81           C  
ATOM   8504  CG  LYS C  91     147.942 173.442 177.049  1.00  9.81           C  
ATOM   8505  CD  LYS C  91     148.742 172.294 177.615  1.00  9.81           C  
ATOM   8506  CE  LYS C  91     148.604 171.042 176.771  1.00  9.81           C  
ATOM   8507  NZ  LYS C  91     147.891 169.949 177.471  1.00  9.81           N  
ATOM   8508  N   ASP C  92     146.336 177.058 179.384  1.00 13.73           N  
ATOM   8509  CA  ASP C  92     146.215 178.194 180.298  1.00 13.73           C  
ATOM   8510  C   ASP C  92     146.832 177.815 181.638  1.00 13.73           C  
ATOM   8511  O   ASP C  92     146.245 177.050 182.409  1.00 13.73           O  
ATOM   8512  CB  ASP C  92     144.757 178.615 180.461  1.00 13.73           C  
ATOM   8513  CG  ASP C  92     144.597 179.875 181.305  1.00 13.73           C  
ATOM   8514  OD1 ASP C  92     145.572 180.298 181.960  1.00 13.73           O  
ATOM   8515  OD2 ASP C  92     143.491 180.451 181.305  1.00 13.73           O  
ATOM   8516  N   PHE C  93     148.014 178.367 181.910  1.00 15.62           N  
ATOM   8517  CA  PHE C  93     148.755 178.058 183.126  1.00 15.62           C  
ATOM   8518  C   PHE C  93     147.991 178.440 184.389  1.00 15.62           C  
ATOM   8519  O   PHE C  93     148.280 177.900 185.461  1.00 15.62           O  
ATOM   8520  CB  PHE C  93     150.101 178.780 183.091  1.00 15.62           C  
ATOM   8521  CG  PHE C  93     150.998 178.449 184.241  1.00 15.62           C  
ATOM   8522  CD1 PHE C  93     151.642 177.231 184.298  1.00 15.62           C  
ATOM   8523  CD2 PHE C  93     151.204 179.354 185.261  1.00 15.62           C  
ATOM   8524  CE1 PHE C  93     152.469 176.919 185.353  1.00 15.62           C  
ATOM   8525  CE2 PHE C  93     152.035 179.044 186.318  1.00 15.62           C  
ATOM   8526  CZ  PHE C  93     152.665 177.823 186.360  1.00 15.62           C  
ATOM   8527  N   THR C  94     147.022 179.347 184.288  1.00 18.55           N  
ATOM   8528  CA  THR C  94     146.295 179.831 185.455  1.00 18.55           C  
ATOM   8529  C   THR C  94     145.241 178.849 185.963  1.00 18.55           C  
ATOM   8530  O   THR C  94     144.704 179.062 187.054  1.00 18.55           O  
ATOM   8531  CB  THR C  94     145.629 181.175 185.139  1.00 18.55           C  
ATOM   8532  OG1 THR C  94     144.714 181.023 184.049  1.00 18.55           O  
ATOM   8533  CG2 THR C  94     146.672 182.241 184.789  1.00 18.55           C  
ATOM   8534  N   VAL C  95     144.936 177.791 185.215  1.00 17.80           N  
ATOM   8535  CA  VAL C  95     143.932 176.798 185.595  1.00 17.80           C  
ATOM   8536  C   VAL C  95     144.656 175.505 185.952  1.00 17.80           C  
ATOM   8537  O   VAL C  95     145.144 174.790 185.069  1.00 17.80           O  
ATOM   8538  CB  VAL C  95     142.907 176.570 184.478  1.00 17.80           C  
ATOM   8539  CG1 VAL C  95     141.900 175.494 184.876  1.00 17.80           C  
ATOM   8540  CG2 VAL C  95     142.207 177.871 184.145  1.00 17.80           C  
ATOM   8541  N   PHE C  96     144.704 175.198 187.248  1.00 21.57           N  
ATOM   8542  CA  PHE C  96     145.381 174.015 187.770  1.00 21.57           C  
ATOM   8543  C   PHE C  96     146.743 173.810 187.117  1.00 21.57           C  
ATOM   8544  O   PHE C  96     147.136 172.677 186.825  1.00 21.57           O  
ATOM   8545  CB  PHE C  96     144.507 172.770 187.586  1.00 21.57           C  
ATOM   8546  CG  PHE C  96     143.155 172.881 188.222  1.00 21.57           C  
ATOM   8547  CD1 PHE C  96     143.000 172.708 189.583  1.00 21.57           C  
ATOM   8548  CD2 PHE C  96     142.038 173.156 187.457  1.00 21.57           C  
ATOM   8549  CE1 PHE C  96     141.755 172.810 190.169  1.00 21.57           C  
ATOM   8550  CE2 PHE C  96     140.793 173.259 188.038  1.00 21.57           C  
ATOM   8551  CZ  PHE C  96     140.653 173.086 189.396  1.00 21.57           C  
ATOM   8552  N   GLY C  97     147.472 174.899 186.900  1.00 19.83           N  
ATOM   8553  CA  GLY C  97     148.784 174.815 186.280  1.00 19.83           C  
ATOM   8554  C   GLY C  97     148.771 174.223 184.889  1.00 19.83           C  
ATOM   8555  O   GLY C  97     149.704 173.503 184.515  1.00 19.83           O  
ATOM   8556  N   GLY C  98     147.732 174.514 184.109  1.00 15.74           N  
ATOM   8557  CA  GLY C  98     147.620 173.991 182.760  1.00 15.74           C  
ATOM   8558  C   GLY C  98     147.603 172.483 182.657  1.00 15.74           C  
ATOM   8559  O   GLY C  98     147.827 171.943 181.571  1.00 15.74           O  
ATOM   8560  N   SER C  99     147.340 171.783 183.755  1.00 15.31           N  
ATOM   8561  CA  SER C  99     147.416 170.329 183.763  1.00 15.31           C  
ATOM   8562  C   SER C  99     146.273 169.708 182.966  1.00 15.31           C  
ATOM   8563  O   SER C  99     145.165 170.241 182.905  1.00 15.31           O  
ATOM   8564  CB  SER C  99     147.390 169.807 185.194  1.00 15.31           C  
ATOM   8565  OG  SER C  99     146.343 170.400 185.930  1.00 15.31           O  
ATOM   8566  N   SER C 100     146.557 168.553 182.368  1.00 15.70           N  
ATOM   8567  CA  SER C 100     145.638 167.890 181.451  1.00 15.70           C  
ATOM   8568  C   SER C 100     144.687 166.977 182.215  1.00 15.70           C  
ATOM   8569  O   SER C 100     145.123 166.110 182.980  1.00 15.70           O  
ATOM   8570  CB  SER C 100     146.403 167.083 180.405  1.00 15.70           C  
ATOM   8571  OG  SER C 100     145.517 166.294 179.636  1.00 15.70           O  
ATOM   8572  N   SER C 101     143.397 167.173 181.996  1.00 15.30           N  
ATOM   8573  CA  SER C 101     142.328 166.348 182.526  1.00 15.30           C  
ATOM   8574  C   SER C 101     141.633 165.600 181.386  1.00 15.30           C  
ATOM   8575  O   SER C 101     142.037 165.680 180.222  1.00 15.30           O  
ATOM   8576  CB  SER C 101     141.351 167.221 183.310  1.00 15.30           C  
ATOM   8577  OG  SER C 101     140.471 167.916 182.453  1.00 15.30           O  
ATOM   8578  N   GLU C 102     140.581 164.857 181.736  1.00 16.36           N  
ATOM   8579  CA  GLU C 102     139.817 164.108 180.742  1.00 16.36           C  
ATOM   8580  C   GLU C 102     139.143 165.043 179.734  1.00 16.36           C  
ATOM   8581  O   GLU C 102     139.277 164.867 178.517  1.00 16.36           O  
ATOM   8582  CB  GLU C 102     138.793 163.217 181.459  1.00 16.36           C  
ATOM   8583  CG  GLU C 102     137.841 162.457 180.554  1.00 16.36           C  
ATOM   8584  CD  GLU C 102     137.042 161.396 181.296  1.00 16.36           C  
ATOM   8585  OE1 GLU C 102     137.155 161.313 182.536  1.00 16.36           O  
ATOM   8586  OE2 GLU C 102     136.296 160.643 180.635  1.00 16.36           O  
ATOM   8587  N   ALA C 103     138.438 166.064 180.225  1.00 11.96           N  
ATOM   8588  CA  ALA C 103     137.695 166.960 179.338  1.00 11.96           C  
ATOM   8589  C   ALA C 103     138.627 167.870 178.534  1.00 11.96           C  
ATOM   8590  O   ALA C 103     138.388 168.129 177.348  1.00 11.96           O  
ATOM   8591  CB  ALA C 103     136.705 167.778 180.164  1.00 11.96           C  
ATOM   8592  N   HIS C 104     139.647 168.416 179.191  1.00  9.76           N  
ATOM   8593  CA  HIS C 104     140.751 169.111 178.530  1.00  9.76           C  
ATOM   8594  C   HIS C 104     141.270 168.321 177.322  1.00  9.76           C  
ATOM   8595  O   HIS C 104     141.314 168.819 176.181  1.00  9.76           O  
ATOM   8596  CB  HIS C 104     141.825 169.327 179.605  1.00  9.76           C  
ATOM   8597  CG  HIS C 104     143.059 170.033 179.156  1.00  9.76           C  
ATOM   8598  ND1 HIS C 104     143.534 171.153 179.800  1.00  9.76           N  
ATOM   8599  CD2 HIS C 104     143.960 169.743 178.192  1.00  9.76           C  
ATOM   8600  CE1 HIS C 104     144.657 171.543 179.229  1.00  9.76           C  
ATOM   8601  NE2 HIS C 104     144.934 170.708 178.246  1.00  9.76           N  
ATOM   8602  N   ALA C 105     141.639 167.060 177.562  1.00  7.73           N  
ATOM   8603  CA  ALA C 105     142.115 166.199 176.485  1.00  7.73           C  
ATOM   8604  C   ALA C 105     141.049 166.005 175.414  1.00  7.73           C  
ATOM   8605  O   ALA C 105     141.375 165.938 174.225  1.00  7.73           O  
ATOM   8606  CB  ALA C 105     142.565 164.850 177.049  1.00  7.73           C  
ATOM   8607  N   ALA C 106     139.775 165.934 175.806  1.00  7.72           N  
ATOM   8608  CA  ALA C 106     138.715 165.772 174.813  1.00  7.72           C  
ATOM   8609  C   ALA C 106     138.636 166.981 173.885  1.00  7.72           C  
ATOM   8610  O   ALA C 106     138.430 166.835 172.675  1.00  7.72           O  
ATOM   8611  CB  ALA C 106     137.372 165.530 175.502  1.00  7.72           C  
ATOM   8612  N   LYS C 107     138.783 168.186 174.438  1.00 12.11           N  
ATOM   8613  CA  LYS C 107     138.827 169.391 173.608  1.00 12.11           C  
ATOM   8614  C   LYS C 107     139.963 169.313 172.586  1.00 12.11           C  
ATOM   8615  O   LYS C 107     139.768 169.568 171.379  1.00 12.11           O  
ATOM   8616  CB  LYS C 107     138.986 170.632 174.497  1.00 12.11           C  
ATOM   8617  CG  LYS C 107     137.765 170.976 175.348  1.00 12.11           C  
ATOM   8618  CD  LYS C 107     137.938 172.245 176.195  1.00 12.11           C  
ATOM   8619  CE  LYS C 107     138.045 173.518 175.371  1.00 12.11           C  
ATOM   8620  NZ  LYS C 107     138.039 174.739 176.205  1.00 12.11           N  
ATOM   8621  N   ILE C 108     141.159 168.939 173.054  1.00 12.77           N  
ATOM   8622  CA  ILE C 108     142.300 168.852 172.138  1.00 12.77           C  
ATOM   8623  C   ILE C 108     142.026 167.820 171.046  1.00 12.77           C  
ATOM   8624  O   ILE C 108     142.345 168.036 169.868  1.00 12.77           O  
ATOM   8625  CB  ILE C 108     143.604 168.538 172.903  1.00 12.77           C  
ATOM   8626  CG1 ILE C 108     143.971 169.675 173.864  1.00 12.77           C  
ATOM   8627  CG2 ILE C 108     144.753 168.304 171.925  1.00 12.77           C  
ATOM   8628  CD1 ILE C 108     145.180 169.389 174.749  1.00 12.77           C  
ATOM   8629  N   VAL C 109     141.425 166.688 171.419  1.00  7.70           N  
ATOM   8630  CA  VAL C 109     141.115 165.636 170.452  1.00  7.70           C  
ATOM   8631  C   VAL C 109     140.128 166.146 169.406  1.00  7.70           C  
ATOM   8632  O   VAL C 109     140.256 165.843 168.214  1.00  7.70           O  
ATOM   8633  CB  VAL C 109     140.592 164.379 171.180  1.00  7.70           C  
ATOM   8634  CG1 VAL C 109     139.903 163.432 170.217  1.00  7.70           C  
ATOM   8635  CG2 VAL C 109     141.733 163.667 171.894  1.00  7.70           C  
ATOM   8636  N   LYS C 110     139.131 166.928 169.833  1.00  7.33           N  
ATOM   8637  CA  LYS C 110     138.191 167.521 168.883  1.00  7.33           C  
ATOM   8638  C   LYS C 110     138.929 168.314 167.809  1.00  7.33           C  
ATOM   8639  O   LYS C 110     138.732 168.092 166.605  1.00  7.33           O  
ATOM   8640  CB  LYS C 110     137.170 168.410 169.612  1.00  7.33           C  
ATOM   8641  CG  LYS C 110     136.162 169.092 168.682  1.00  7.33           C  
ATOM   8642  CD  LYS C 110     135.081 169.911 169.410  1.00  7.33           C  
ATOM   8643  CE  LYS C 110     134.060 169.040 170.128  1.00  7.33           C  
ATOM   8644  NZ  LYS C 110     132.958 169.836 170.736  1.00  7.33           N  
ATOM   8645  N   VAL C 111     139.806 169.232 168.223  1.00 12.77           N  
ATOM   8646  CA  VAL C 111     140.434 170.064 167.190  1.00 12.77           C  
ATOM   8647  C   VAL C 111     141.427 169.254 166.343  1.00 12.77           C  
ATOM   8648  O   VAL C 111     141.543 169.487 165.133  1.00 12.77           O  
ATOM   8649  CB  VAL C 111     141.066 171.339 167.788  1.00 12.77           C  
ATOM   8650  CG1 VAL C 111     142.150 171.033 168.778  1.00 12.77           C  
ATOM   8651  CG2 VAL C 111     141.598 172.232 166.687  1.00 12.77           C  
ATOM   8652  N   GLN C 112     142.115 168.266 166.928  1.00  7.67           N  
ATOM   8653  CA  GLN C 112     142.998 167.406 166.137  1.00  7.67           C  
ATOM   8654  C   GLN C 112     142.222 166.670 165.042  1.00  7.67           C  
ATOM   8655  O   GLN C 112     142.634 166.651 163.871  1.00  7.67           O  
ATOM   8656  CB  GLN C 112     143.720 166.406 167.047  1.00  7.67           C  
ATOM   8657  CG  GLN C 112     144.927 166.957 167.806  1.00  7.67           C  
ATOM   8658  CD  GLN C 112     145.675 165.881 168.569  1.00  7.67           C  
ATOM   8659  OE1 GLN C 112     146.853 165.625 168.327  1.00  7.67           O  
ATOM   8660  NE2 GLN C 112     144.992 165.245 169.496  1.00  7.67           N  
ATOM   8661  N   ASP C 113     141.107 166.033 165.416  1.00  7.46           N  
ATOM   8662  CA  ASP C 113     140.287 165.319 164.443  1.00  7.46           C  
ATOM   8663  C   ASP C 113     139.799 166.255 163.345  1.00  7.46           C  
ATOM   8664  O   ASP C 113     139.859 165.915 162.156  1.00  7.46           O  
ATOM   8665  CB  ASP C 113     139.102 164.649 165.142  1.00  7.46           C  
ATOM   8666  CG  ASP C 113     139.506 163.431 165.953  1.00  7.46           C  
ATOM   8667  OD1 ASP C 113     140.592 162.868 165.710  1.00  7.46           O  
ATOM   8668  OD2 ASP C 113     138.723 163.028 166.835  1.00  7.46           O  
ATOM   8669  N   MET C 114     139.332 167.450 163.716  1.00 10.01           N  
ATOM   8670  CA  MET C 114     138.847 168.369 162.690  1.00 10.01           C  
ATOM   8671  C   MET C 114     139.965 168.755 161.732  1.00 10.01           C  
ATOM   8672  O   MET C 114     139.740 168.870 160.523  1.00 10.01           O  
ATOM   8673  CB  MET C 114     138.225 169.617 163.318  1.00 10.01           C  
ATOM   8674  CG  MET C 114     136.907 169.377 164.031  1.00 10.01           C  
ATOM   8675  SD  MET C 114     136.100 170.910 164.513  1.00 10.01           S  
ATOM   8676  CE  MET C 114     135.638 171.544 162.907  1.00 10.01           C  
ATOM   8677  N   ALA C 115     141.182 168.945 162.249  1.00  8.05           N  
ATOM   8678  CA  ALA C 115     142.281 169.379 161.392  1.00  8.05           C  
ATOM   8679  C   ALA C 115     142.695 168.280 160.421  1.00  8.05           C  
ATOM   8680  O   ALA C 115     143.001 168.558 159.257  1.00  8.05           O  
ATOM   8681  CB  ALA C 115     143.471 169.818 162.233  1.00  8.05           C  
ATOM   8682  N   LEU C 116     142.721 167.027 160.876  1.00 12.77           N  
ATOM   8683  CA  LEU C 116     142.989 165.938 159.939  1.00 12.77           C  
ATOM   8684  C   LEU C 116     141.889 165.856 158.884  1.00 12.77           C  
ATOM   8685  O   LEU C 116     142.167 165.638 157.700  1.00 12.77           O  
ATOM   8686  CB  LEU C 116     143.139 164.602 160.671  1.00 12.77           C  
ATOM   8687  CG  LEU C 116     143.674 163.429 159.832  1.00 12.77           C  
ATOM   8688  CD1 LEU C 116     144.944 163.798 159.076  1.00 12.77           C  
ATOM   8689  CD2 LEU C 116     143.915 162.181 160.673  1.00 12.77           C  
ATOM   8690  N   LYS C 117     140.634 166.034 159.299  1.00 10.17           N  
ATOM   8691  CA  LYS C 117     139.507 165.959 158.372  1.00 10.17           C  
ATOM   8692  C   LYS C 117     139.583 167.039 157.289  1.00 10.17           C  
ATOM   8693  O   LYS C 117     139.433 166.746 156.100  1.00 10.17           O  
ATOM   8694  CB  LYS C 117     138.207 166.051 159.175  1.00 10.17           C  
ATOM   8695  CG  LYS C 117     136.943 165.747 158.446  1.00 10.17           C  
ATOM   8696  CD  LYS C 117     135.790 165.618 159.447  1.00 10.17           C  
ATOM   8697  CE  LYS C 117     135.380 166.963 160.032  1.00 10.17           C  
ATOM   8698  NZ  LYS C 117     134.242 166.878 161.004  1.00 10.17           N  
ATOM   8699  N   MET C 118     139.790 168.298 157.682  1.00 10.11           N  
ATOM   8700  CA  MET C 118     139.885 169.399 156.724  1.00 10.11           C  
ATOM   8701  C   MET C 118     141.203 169.430 155.958  1.00 10.11           C  
ATOM   8702  O   MET C 118     141.299 170.166 154.971  1.00 10.11           O  
ATOM   8703  CB  MET C 118     139.721 170.752 157.426  1.00 10.11           C  
ATOM   8704  CG  MET C 118     138.327 171.161 157.825  1.00 10.11           C  
ATOM   8705  SD  MET C 118     137.033 170.720 156.678  1.00 10.11           S  
ATOM   8706  CE  MET C 118     136.324 169.386 157.597  1.00 10.11           C  
ATOM   8707  N   ARG C 119     142.212 168.671 156.383  1.00  9.42           N  
ATOM   8708  CA  ARG C 119     143.555 168.737 155.811  1.00  9.42           C  
ATOM   8709  C   ARG C 119     144.127 170.156 155.914  1.00  9.42           C  
ATOM   8710  O   ARG C 119     144.440 170.806 154.917  1.00  9.42           O  
ATOM   8711  CB  ARG C 119     143.551 168.234 154.362  1.00  9.42           C  
ATOM   8712  CG  ARG C 119     143.001 166.834 154.194  1.00  9.42           C  
ATOM   8713  CD  ARG C 119     143.943 165.777 154.735  1.00  9.42           C  
ATOM   8714  NE  ARG C 119     143.748 164.484 154.084  1.00  9.42           N  
ATOM   8715  CZ  ARG C 119     142.897 163.550 154.500  1.00  9.42           C  
ATOM   8716  NH1 ARG C 119     142.790 162.410 153.833  1.00  9.42           N  
ATOM   8717  NH2 ARG C 119     142.149 163.746 155.573  1.00  9.42           N  
ATOM   8718  N   ALA C 120     144.253 170.629 157.148  1.00  7.90           N  
ATOM   8719  CA  ALA C 120     144.825 171.926 157.474  1.00  7.90           C  
ATOM   8720  C   ALA C 120     145.842 171.804 158.601  1.00  7.90           C  
ATOM   8721  O   ALA C 120     145.779 170.867 159.401  1.00  7.90           O  
ATOM   8722  CB  ALA C 120     143.731 172.926 157.876  1.00  7.90           C  
ATOM   8723  N   PRO C 121     146.786 172.743 158.697  1.00 12.77           N  
ATOM   8724  CA  PRO C 121     147.806 172.675 159.755  1.00 12.77           C  
ATOM   8725  C   PRO C 121     147.229 172.865 161.152  1.00 12.77           C  
ATOM   8726  O   PRO C 121     146.155 173.437 161.341  1.00 12.77           O  
ATOM   8727  CB  PRO C 121     148.761 173.824 159.408  1.00 12.77           C  
ATOM   8728  CG  PRO C 121     148.427 174.245 158.051  1.00 12.77           C  
ATOM   8729  CD  PRO C 121     147.006 173.892 157.807  1.00 12.77           C  
ATOM   8730  N   ILE C 122     147.988 172.394 162.147  1.00 12.77           N  
ATOM   8731  CA  ILE C 122     147.625 172.524 163.558  1.00 12.77           C  
ATOM   8732  C   ILE C 122     148.827 173.006 164.379  1.00 12.77           C  
ATOM   8733  O   ILE C 122     149.935 172.454 164.279  1.00 12.77           O  
ATOM   8734  CB  ILE C 122     147.053 171.204 164.120  1.00 12.77           C  
ATOM   8735  CG1 ILE C 122     146.497 171.395 165.541  1.00 12.77           C  
ATOM   8736  CG2 ILE C 122     148.071 170.096 164.068  1.00 12.77           C  
ATOM   8737  CD1 ILE C 122     145.573 170.291 165.984  1.00 12.77           C  
ATOM   8738  N   ILE C 123     148.592 174.045 165.186  1.00 12.77           N  
ATOM   8739  CA  ILE C 123     149.583 174.659 166.071  1.00 12.77           C  
ATOM   8740  C   ILE C 123     149.174 174.420 167.523  1.00 12.77           C  
ATOM   8741  O   ILE C 123     148.028 174.685 167.901  1.00 12.77           O  
ATOM   8742  CB  ILE C 123     149.716 176.172 165.809  1.00 12.77           C  
ATOM   8743  CG1 ILE C 123     149.757 176.496 164.304  1.00 12.77           C  
ATOM   8744  CG2 ILE C 123     150.908 176.758 166.566  1.00 12.77           C  
ATOM   8745  CD1 ILE C 123     150.913 175.936 163.557  1.00 12.77           C  
ATOM   8746  N   GLY C 124     150.109 173.930 168.329  1.00  6.74           N  
ATOM   8747  CA  GLY C 124     149.923 173.775 169.769  1.00  6.74           C  
ATOM   8748  C   GLY C 124     150.859 174.686 170.547  1.00  6.74           C  
ATOM   8749  O   GLY C 124     152.040 174.803 170.213  1.00  6.74           O  
ATOM   8750  N   ILE C 125     150.321 175.329 171.582  1.00  6.02           N  
ATOM   8751  CA  ILE C 125     151.060 176.250 172.444  1.00  6.02           C  
ATOM   8752  C   ILE C 125     151.035 175.693 173.866  1.00  6.02           C  
ATOM   8753  O   ILE C 125     149.957 175.495 174.441  1.00  6.02           O  
ATOM   8754  CB  ILE C 125     150.474 177.672 172.389  1.00  6.02           C  
ATOM   8755  CG1 ILE C 125     150.314 178.130 170.935  1.00  6.02           C  
ATOM   8756  CG2 ILE C 125     151.350 178.644 173.148  1.00  6.02           C  
ATOM   8757  CD1 ILE C 125     149.735 179.504 170.775  1.00  6.02           C  
ATOM   8758  N   PHE C 126     152.215 175.464 174.439  1.00  7.70           N  
ATOM   8759  CA  PHE C 126     152.362 174.709 175.677  1.00  7.70           C  
ATOM   8760  C   PHE C 126     152.859 175.594 176.814  1.00  7.70           C  
ATOM   8761  O   PHE C 126     153.877 176.281 176.683  1.00  7.70           O  
ATOM   8762  CB  PHE C 126     153.309 173.527 175.476  1.00  7.70           C  
ATOM   8763  CG  PHE C 126     152.775 172.493 174.541  1.00  7.70           C  
ATOM   8764  CD1 PHE C 126     152.822 172.688 173.178  1.00  7.70           C  
ATOM   8765  CD2 PHE C 126     152.199 171.335 175.023  1.00  7.70           C  
ATOM   8766  CE1 PHE C 126     152.324 171.751 172.321  1.00  7.70           C  
ATOM   8767  CE2 PHE C 126     151.696 170.394 174.162  1.00  7.70           C  
ATOM   8768  CZ  PHE C 126     151.758 170.605 172.809  1.00  7.70           C  
ATOM   8769  N   ASP C 127     152.113 175.581 177.917  1.00 13.51           N  
ATOM   8770  CA  ASP C 127     152.468 176.232 179.179  1.00 13.51           C  
ATOM   8771  C   ASP C 127     151.684 175.459 180.245  1.00 13.51           C  
ATOM   8772  O   ASP C 127     150.531 175.784 180.532  1.00 13.51           O  
ATOM   8773  CB  ASP C 127     152.109 177.711 179.129  1.00 13.51           C  
ATOM   8774  CG  ASP C 127     152.589 178.489 180.335  1.00 13.51           C  
ATOM   8775  OD1 ASP C 127     153.220 177.902 181.233  1.00 13.51           O  
ATOM   8776  OD2 ASP C 127     152.343 179.710 180.366  1.00 13.51           O  
ATOM   8777  N   ALA C 128     152.324 174.452 180.837  1.00 19.17           N  
ATOM   8778  CA  ALA C 128     151.575 173.330 181.394  1.00 19.17           C  
ATOM   8779  C   ALA C 128     152.375 172.643 182.495  1.00 19.17           C  
ATOM   8780  O   ALA C 128     153.496 173.040 182.826  1.00 19.17           O  
ATOM   8781  CB  ALA C 128     151.204 172.332 180.294  1.00 19.17           C  
ATOM   8782  N   GLY C 129     151.768 171.603 183.069  1.00 25.14           N  
ATOM   8783  CA  GLY C 129     152.365 170.837 184.146  1.00 25.14           C  
ATOM   8784  C   GLY C 129     152.106 169.341 184.100  1.00 25.14           C  
ATOM   8785  O   GLY C 129     152.431 168.631 185.055  1.00 25.14           O  
ATOM   8786  N   GLY C 130     151.523 168.842 183.012  1.00 21.12           N  
ATOM   8787  CA  GLY C 130     151.325 167.411 182.872  1.00 21.12           C  
ATOM   8788  C   GLY C 130     149.961 166.907 183.298  1.00 21.12           C  
ATOM   8789  O   GLY C 130     148.970 167.640 183.244  1.00 21.12           O  
ATOM   8790  N   ALA C 131     149.907 165.647 183.727  1.00 19.31           N  
ATOM   8791  CA  ALA C 131     148.648 165.001 184.071  1.00 19.31           C  
ATOM   8792  C   ALA C 131     148.174 165.442 185.451  1.00 19.31           C  
ATOM   8793  O   ALA C 131     148.922 165.360 186.430  1.00 19.31           O  
ATOM   8794  CB  ALA C 131