HEADER    VIRAL PROTEIN                           08-OCT-22   8EQN              
TITLE     BG505 UFO-E2P-L4P NANOPARTICLE RECONSTRUCTED BY FOCUSED REFINEMENT    
TITLE    2 WITH A MASK AROUND THE NANOPARTICLE CORE                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BG505 UFO-E2P-L4P;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE   3 ORGANISM_TAXID: 11676;                                               
SOURCE   4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   5 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: EXPICHO                                 
KEYWDS    GLYCOPROTEIN, BG505, UFO, VACCINE DESIGN, NANOPARTICLE, PROTEIN       
KEYWDS   2 DESIGN, VIRAL PROTEIN                                                
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    A.ANTANASIJEVIC,Y.N.ZHANG,J.ZHU,A.B.WARD                              
REVDAT   1   19-APR-23 8EQN    0                                                
JRNL        AUTH   Y.N.ZHANG,J.PAYNTER,A.ANTANASIJEVIC,J.D.ALLEN,M.ELDAD,       
JRNL        AUTH 2 Y.Z.LEE,J.COPPS,M.L.NEWBY,L.HE,D.CHAVEZ,P.FROST,A.GOODROE,   
JRNL        AUTH 3 J.DUTTON,R.LANFORD,C.CHEN,I.A.WILSON,M.CRISPIN,A.B.WARD,     
JRNL        AUTH 4 J.ZHU                                                        
JRNL        TITL   SINGLE-COMPONENT MULTILAYERED SELF-ASSEMBLING PROTEIN        
JRNL        TITL 2 NANOPARTICLES PRESENTING GLYCAN-TRIMMED UNCLEAVED PREFUSION  
JRNL        TITL 3 OPTIMIZED ENVELOPE TRIMMERS AS HIV-1 VACCINE CANDIDATES.     
JRNL        REF    NAT COMMUN                    V.  14  1985 2023              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   37031217                                                     
JRNL        DOI    10.1038/S41467-023-37742-Z                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : CRYOSPARC, LEGINON, RELION, UCSF          
REMARK   3                            CHIMERA, COOT, ROSETTAEM, RELION,         
REMARK   3                            RELION, RELION, RELION                    
REMARK   3   RECONSTRUCTION SCHEMA  : BACK PROJECTION                           
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 4ZK7                                
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)  : 3.700                          
REMARK   3   NUMBER OF PARTICLES               : 7672                           
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 8EQN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-OCT-22.                  
REMARK 100 THE DEPOSITION ID IS D_1000269227.                                   
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                 : BG505 UFO-E2P-L4P NANOPARTICLE    
REMARK 245                                    RECONSTRUCTED BY FOCUSED          
REMARK 245                                    REFINEMENT WITH A MASK AROUND     
REMARK 245                                    THE NANOPARTICLE CORE             
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 4.10                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : BLOTTING TIME VARIED BETWEEN 3    
REMARK 245                                    AND 7 SECONDS.                    
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.40                              
REMARK 245   SAMPLE DETAILS                 : THE MAP WAS GENERATED BY          
REMARK 245  FOCUSED REFINEMENT OF THE BG505 UFO-E2P-L4P NANOPARTICLE DATASET    
REMARK 245  USING A MASK AROUND THE NANOPARTICLE CORE (MASKING OUT THE          
REMARK 245  FLEXIBLY LINKED ANTIGENS).                                          
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : 2300                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : 700.00                         
REMARK 245   MAXIMUM DEFOCUS (NM)              : 1500.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 5020.00                        
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 29000                          
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 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR                   
REMARK 300 ICOSAHEDRAL POINT SYMMETRY (SCHOENFLIES SYMBOL = I).                 
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 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.309017 -0.809017  0.500000      268.31499            
REMARK 350   BIOMT2   2  0.809017  0.500000  0.309017     -165.19121            
REMARK 350   BIOMT3   2 -0.500000  0.309017  0.809017      102.09378            
REMARK 350   BIOMT1   3 -0.809017 -0.500000  0.309017      535.91827            
REMARK 350   BIOMT2   3  0.500000 -0.309017  0.809017        0.83329            
REMARK 350   BIOMT3   3 -0.309017  0.809017  0.500000       -0.51500            
REMARK 350   BIOMT1   4 -0.809017  0.500000 -0.309017      432.99120            
REMARK 350   BIOMT2   4 -0.500000 -0.309017  0.809017      268.63328            
REMARK 350   BIOMT3   4  0.309017  0.809017  0.500000     -166.02449            
REMARK 350   BIOMT1   5  0.309017  0.809017 -0.500000      101.77550            
REMARK 350   BIOMT2   5 -0.809017  0.500000  0.309017      268.11828            
REMARK 350   BIOMT3   5  0.500000  0.309017  0.809017     -165.70621            
REMARK 350   BIOMT1   6 -0.809017  0.500000  0.309017      268.11828            
REMARK 350   BIOMT2   6  0.500000  0.309017  0.809017     -164.67621            
REMARK 350   BIOMT3   6  0.309017  0.809017 -0.500000      100.74549            
REMARK 350   BIOMT1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   7  0.000000  0.000000  1.000000        1.03000            
REMARK 350   BIOMT3   7  1.000000  0.000000  0.000000       -1.03001            
REMARK 350   BIOMT1   8  0.809017  0.500000  0.309017     -165.19120            
REMARK 350   BIOMT2   8 -0.500000  0.309017  0.809017      103.12378            
REMARK 350   BIOMT3   8  0.309017 -0.809017  0.500000      267.28498            
REMARK 350   BIOMT1   9  0.500000 -0.309017  0.809017        0.83329            
REMARK 350   BIOMT2   9 -0.309017  0.809017  0.500000        0.51500            
REMARK 350   BIOMT3   9 -0.809017 -0.500000  0.309017      534.88827            
REMARK 350   BIOMT1  10 -0.500000 -0.309017  0.809017      268.63328            
REMARK 350   BIOMT2  10  0.309017  0.809017  0.500000     -164.99450            
REMARK 350   BIOMT3  10 -0.809017  0.500000 -0.309017      431.96120            
REMARK 350   BIOMT1  11 -0.500000  0.309017 -0.809017      534.76670            
REMARK 350   BIOMT2  11  0.309017 -0.809017 -0.500000      535.08497            
REMARK 350   BIOMT3  11 -0.809017 -0.500000  0.309017      534.88827            
REMARK 350   BIOMT1  12  0.500000  0.309017 -0.809017      266.96670            
REMARK 350   BIOMT2  12 -0.309017 -0.809017 -0.500000      700.59447            
REMARK 350   BIOMT3  12 -0.809017  0.500000 -0.309017      431.96120            
REMARK 350   BIOMT1  13  0.809017 -0.500000 -0.309017      267.48170            
REMARK 350   BIOMT2  13 -0.500000 -0.309017 -0.809017      700.27618            
REMARK 350   BIOMT3  13  0.309017  0.809017 -0.500000      100.74549            
REMARK 350   BIOMT1  14  0.000000 -1.000000  0.000000      535.59998            
REMARK 350   BIOMT2  14  0.000000  0.000000 -1.000000      534.56997            
REMARK 350   BIOMT3  14  1.000000  0.000000  0.000000       -1.03000            
REMARK 350   BIOMT1  15 -0.809017 -0.500000 -0.309017      700.79119            
REMARK 350   BIOMT2  15  0.500000 -0.309017 -0.809017      432.47619            
REMARK 350   BIOMT3  15  0.309017 -0.809017  0.500000      267.28499            
REMARK 350   BIOMT1  16  0.309017 -0.809017  0.500000      268.31499            
REMARK 350   BIOMT2  16 -0.809017 -0.500000 -0.309017      700.79118            
REMARK 350   BIOMT3  16  0.500000 -0.309017 -0.809017      431.44619            
REMARK 350   BIOMT1  17 -0.809017 -0.500000  0.309017      535.91827            
REMARK 350   BIOMT2  17 -0.500000  0.309017 -0.809017      534.76669            
REMARK 350   BIOMT3  17  0.309017 -0.809017 -0.500000      534.05497            
REMARK 350   BIOMT1  18 -0.809017  0.500000 -0.309017      432.99120            
REMARK 350   BIOMT2  18  0.500000  0.309017 -0.809017      266.96669            
REMARK 350   BIOMT3  18 -0.309017 -0.809017 -0.500000      699.56447            
REMARK 350   BIOMT1  19  0.309017  0.809017 -0.500000      101.77550            
REMARK 350   BIOMT2  19  0.809017 -0.500000 -0.309017      267.48169            
REMARK 350   BIOMT3  19 -0.500000 -0.309017 -0.809017      699.24618            
REMARK 350   BIOMT1  20  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2  20  0.000000 -1.000000  0.000000      535.59997            
REMARK 350   BIOMT3  20  0.000000  0.000000 -1.000000      533.53997            
REMARK 350   BIOMT1  21  0.000000 -1.000000  0.000000      535.59998            
REMARK 350   BIOMT2  21  0.000000  0.000000  1.000000        1.03000            
REMARK 350   BIOMT3  21 -1.000000  0.000000  0.000000      534.56998            
REMARK 350   BIOMT1  22 -0.809017 -0.500000 -0.309017      700.79119            
REMARK 350   BIOMT2  22 -0.500000  0.309017  0.809017      103.12378            
REMARK 350   BIOMT3  22 -0.309017  0.809017 -0.500000      266.25499            
REMARK 350   BIOMT1  23 -0.500000  0.309017 -0.809017      534.76669            
REMARK 350   BIOMT2  23 -0.309017  0.809017  0.500000        0.51500            
REMARK 350   BIOMT3  23  0.809017  0.500000 -0.309017       -1.34829            
REMARK 350   BIOMT1  24  0.500000  0.309017 -0.809017      266.96670            
REMARK 350   BIOMT2  24  0.309017  0.809017  0.500000     -164.99450            
REMARK 350   BIOMT3  24  0.809017 -0.500000  0.309017      101.57878            
REMARK 350   BIOMT1  25  0.809017 -0.500000 -0.309017      267.48170            
REMARK 350   BIOMT2  25  0.500000  0.309017  0.809017     -164.67621            
REMARK 350   BIOMT3  25 -0.309017 -0.809017  0.500000      432.79448            
REMARK 350   BIOMT1  26 -0.500000 -0.309017 -0.809017      700.27619            
REMARK 350   BIOMT2  26  0.309017  0.809017 -0.500000      101.77549            
REMARK 350   BIOMT3  26  0.809017 -0.500000 -0.309017      266.45170            
REMARK 350   BIOMT1  27  0.000000  0.000000 -1.000000      534.56998            
REMARK 350   BIOMT2  27  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  27  0.000000 -1.000000  0.000000      534.56998            
REMARK 350   BIOMT1  28  0.500000 -0.309017 -0.809017      432.47620            
REMARK 350   BIOMT2  28  0.309017 -0.809017  0.500000      268.31498            
REMARK 350   BIOMT3  28 -0.809017 -0.500000 -0.309017      699.76119            
REMARK 350   BIOMT1  29  0.309017 -0.809017 -0.500000      535.08498            
REMARK 350   BIOMT2  29 -0.809017 -0.500000  0.309017      535.91826            
REMARK 350   BIOMT3  29 -0.500000  0.309017 -0.809017      533.73669            
REMARK 350   BIOMT1  30 -0.309017 -0.809017 -0.500000      700.59448            
REMARK 350   BIOMT2  30 -0.809017  0.500000 -0.309017      432.99120            
REMARK 350   BIOMT3  30  0.500000  0.309017 -0.809017      265.93670            
REMARK 350   BIOMT1  31 -0.309017  0.809017  0.500000        0.51501            
REMARK 350   BIOMT2  31 -0.809017 -0.500000  0.309017      535.91826            
REMARK 350   BIOMT3  31  0.500000 -0.309017  0.809017       -0.19672            
REMARK 350   BIOMT1  32  0.309017  0.809017  0.500000     -164.99449            
REMARK 350   BIOMT2  32 -0.809017  0.500000 -0.309017      432.99120            
REMARK 350   BIOMT3  32 -0.500000 -0.309017  0.809017      267.60328            
REMARK 350   BIOMT1  33  0.500000  0.309017  0.809017     -164.67620            
REMARK 350   BIOMT2  33  0.309017  0.809017 -0.500000      101.77549            
REMARK 350   BIOMT3  33 -0.809017  0.500000  0.309017      267.08828            
REMARK 350   BIOMT1  34  0.000000  0.000000  1.000000        1.03001            
REMARK 350   BIOMT2  34  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  34  0.000000  1.000000  0.000000       -1.03000            
REMARK 350   BIOMT1  35 -0.500000  0.309017  0.809017      103.12379            
REMARK 350   BIOMT2  35  0.309017 -0.809017  0.500000      268.31499            
REMARK 350   BIOMT3  35  0.809017  0.500000  0.309017     -166.22121            
REMARK 350   BIOMT1  36  0.809017  0.500000  0.309017     -165.19120            
REMARK 350   BIOMT2  36  0.500000 -0.309017 -0.809017      432.47619            
REMARK 350   BIOMT3  36 -0.309017  0.809017 -0.500000      266.25499            
REMARK 350   BIOMT1  37  0.500000 -0.309017  0.809017        0.83329            
REMARK 350   BIOMT2  37  0.309017 -0.809017 -0.500000      535.08497            
REMARK 350   BIOMT3  37  0.809017  0.500000 -0.309017       -1.34829            
REMARK 350   BIOMT1  38 -0.500000 -0.309017  0.809017      268.63328            
REMARK 350   BIOMT2  38 -0.309017 -0.809017 -0.500000      700.59447            
REMARK 350   BIOMT3  38  0.809017 -0.500000  0.309017      101.57878            
REMARK 350   BIOMT1  39 -0.809017  0.500000  0.309017      268.11829            
REMARK 350   BIOMT2  39 -0.500000 -0.309017 -0.809017      700.27618            
REMARK 350   BIOMT3  39 -0.309017 -0.809017  0.500000      432.79448            
REMARK 350   BIOMT1  40  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  40  0.000000  0.000000 -1.000000      534.56997            
REMARK 350   BIOMT3  40 -1.000000  0.000000  0.000000      534.56998            
REMARK 350   BIOMT1  41  0.000000  0.000000 -1.000000      534.56998            
REMARK 350   BIOMT2  41 -1.000000  0.000000  0.000000      535.59998            
REMARK 350   BIOMT3  41  0.000000  1.000000  0.000000       -1.03000            
REMARK 350   BIOMT1  42  0.500000 -0.309017 -0.809017      432.47620            
REMARK 350   BIOMT2  42 -0.309017  0.809017 -0.500000      267.28499            
REMARK 350   BIOMT3  42  0.809017  0.500000  0.309017     -166.22121            
REMARK 350   BIOMT1  43  0.309017 -0.809017 -0.500000      535.08498            
REMARK 350   BIOMT2  43  0.809017  0.500000 -0.309017       -0.31829            
REMARK 350   BIOMT3  43  0.500000 -0.309017  0.809017       -0.19671            
REMARK 350   BIOMT1  44 -0.309017 -0.809017 -0.500000      700.59447            
REMARK 350   BIOMT2  44  0.809017 -0.500000  0.309017      102.60878            
REMARK 350   BIOMT3  44 -0.500000 -0.309017  0.809017      267.60328            
REMARK 350   BIOMT1  45 -0.500000 -0.309017 -0.809017      700.27619            
REMARK 350   BIOMT2  45 -0.309017 -0.809017  0.500000      433.82448            
REMARK 350   BIOMT3  45 -0.809017  0.500000  0.309017      267.08828            
REMARK 350   BIOMT1  46 -0.309017 -0.809017  0.500000      433.82449            
REMARK 350   BIOMT2  46  0.809017 -0.500000 -0.309017      267.48170            
REMARK 350   BIOMT3  46  0.500000  0.309017  0.809017     -165.70621            
REMARK 350   BIOMT1  47 -1.000000  0.000000  0.000000      535.59999            
REMARK 350   BIOMT2  47  0.000000 -1.000000  0.000000      535.59997            
REMARK 350   BIOMT3  47  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  48 -0.309017  0.809017 -0.500000      267.28500            
REMARK 350   BIOMT2  48 -0.809017 -0.500000 -0.309017      700.79118            
REMARK 350   BIOMT3  48 -0.500000  0.309017  0.809017      102.09378            
REMARK 350   BIOMT1  49  0.809017  0.500000 -0.309017       -0.31828            
REMARK 350   BIOMT2  49 -0.500000  0.309017 -0.809017      534.76669            
REMARK 350   BIOMT3  49 -0.309017  0.809017  0.500000       -0.51500            
REMARK 350   BIOMT1  50  0.809017 -0.500000  0.309017      102.60878            
REMARK 350   BIOMT2  50  0.500000  0.309017 -0.809017      266.96670            
REMARK 350   BIOMT3  50  0.309017  0.809017  0.500000     -166.02450            
REMARK 350   BIOMT1  51  0.809017  0.500000 -0.309017       -0.31829            
REMARK 350   BIOMT2  51  0.500000 -0.309017  0.809017        0.83328            
REMARK 350   BIOMT3  51  0.309017 -0.809017 -0.500000      534.05497            
REMARK 350   BIOMT1  52  0.809017 -0.500000  0.309017      102.60878            
REMARK 350   BIOMT2  52 -0.500000 -0.309017  0.809017      268.63327            
REMARK 350   BIOMT3  52 -0.309017 -0.809017 -0.500000      699.56447            
REMARK 350   BIOMT1  53 -0.309017 -0.809017  0.500000      433.82449            
REMARK 350   BIOMT2  53 -0.809017  0.500000  0.309017      268.11828            
REMARK 350   BIOMT3  53 -0.500000 -0.309017 -0.809017      699.24618            
REMARK 350   BIOMT1  54 -1.000000  0.000000  0.000000      535.59998            
REMARK 350   BIOMT2  54  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3  54  0.000000  0.000000 -1.000000      533.53998            
REMARK 350   BIOMT1  55 -0.309017  0.809017 -0.500000      267.28499            
REMARK 350   BIOMT2  55  0.809017  0.500000  0.309017     -165.19121            
REMARK 350   BIOMT3  55  0.500000 -0.309017 -0.809017      431.44619            
REMARK 350   BIOMT1  56 -0.500000  0.309017  0.809017      103.12379            
REMARK 350   BIOMT2  56 -0.309017  0.809017 -0.500000      267.28499            
REMARK 350   BIOMT3  56 -0.809017 -0.500000 -0.309017      699.76118            
REMARK 350   BIOMT1  57 -0.309017  0.809017  0.500000        0.51501            
REMARK 350   BIOMT2  57  0.809017  0.500000 -0.309017       -0.31829            
REMARK 350   BIOMT3  57 -0.500000  0.309017 -0.809017      533.73669            
REMARK 350   BIOMT1  58  0.309017  0.809017  0.500000     -164.99449            
REMARK 350   BIOMT2  58  0.809017 -0.500000  0.309017      102.60877            
REMARK 350   BIOMT3  58  0.500000  0.309017 -0.809017      265.93670            
REMARK 350   BIOMT1  59  0.500000  0.309017  0.809017     -164.67620            
REMARK 350   BIOMT2  59 -0.309017 -0.809017  0.500000      433.82448            
REMARK 350   BIOMT3  59  0.809017 -0.500000 -0.309017      266.45169            
REMARK 350   BIOMT1  60  0.000000  0.000000  1.000000        1.03001            
REMARK 350   BIOMT2  60 -1.000000  0.000000  0.000000      535.59998            
REMARK 350   BIOMT3  60  0.000000 -1.000000  0.000000      534.56997            
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  -673                                                      
REMARK 465     ASP A  -672                                                      
REMARK 465     ALA A  -671                                                      
REMARK 465     MET A  -670                                                      
REMARK 465     LYS A  -669                                                      
REMARK 465     ARG A  -668                                                      
REMARK 465     GLY A  -667                                                      
REMARK 465     LEU A  -666                                                      
REMARK 465     CYS A  -665                                                      
REMARK 465     CYS A  -664                                                      
REMARK 465     VAL A  -663                                                      
REMARK 465     LEU A  -662                                                      
REMARK 465     LEU A  -661                                                      
REMARK 465     LEU A  -660                                                      
REMARK 465     CYS A  -659                                                      
REMARK 465     GLY A  -658                                                      
REMARK 465     ALA A  -657                                                      
REMARK 465     VAL A  -656                                                      
REMARK 465     PHE A  -655                                                      
REMARK 465     VAL A  -654                                                      
REMARK 465     SER A  -653                                                      
REMARK 465     PRO A  -652                                                      
REMARK 465     SER A  -651                                                      
REMARK 465     GLN A  -650                                                      
REMARK 465     GLU A  -649                                                      
REMARK 465     ILE A  -648                                                      
REMARK 465     HIS A  -647                                                      
REMARK 465     ALA A  -646                                                      
REMARK 465     ARG A  -645                                                      
REMARK 465     PHE A  -644                                                      
REMARK 465     ARG A  -643                                                      
REMARK 465     ARG A  -642                                                      
REMARK 465     GLY A  -641                                                      
REMARK 465     ALA A  -640                                                      
REMARK 465     ARG A  -639                                                      
REMARK 465     SER A  -638                                                      
REMARK 465     ARG A  -637                                                      
REMARK 465     ALA A  -636                                                      
REMARK 465     GLU A  -635                                                      
REMARK 465     ASN A  -634                                                      
REMARK 465     LEU A  -633                                                      
REMARK 465     TRP A  -632                                                      
REMARK 465     VAL A  -631                                                      
REMARK 465     THR A  -630                                                      
REMARK 465     VAL A  -629                                                      
REMARK 465     TYR A  -628                                                      
REMARK 465     TYR A  -627                                                      
REMARK 465     GLY A  -626                                                      
REMARK 465     VAL A  -625                                                      
REMARK 465     PRO A  -624                                                      
REMARK 465     VAL A  -623                                                      
REMARK 465     TRP A  -622                                                      
REMARK 465     LYS A  -621                                                      
REMARK 465     ASP A  -620                                                      
REMARK 465     ALA A  -619                                                      
REMARK 465     GLU A  -618                                                      
REMARK 465     THR A  -617                                                      
REMARK 465     THR A  -616                                                      
REMARK 465     LEU A  -615                                                      
REMARK 465     PHE A  -614                                                      
REMARK 465     CYS A  -613                                                      
REMARK 465     ALA A  -612                                                      
REMARK 465     SER A  -611                                                      
REMARK 465     ASP A  -610                                                      
REMARK 465     ALA A  -609                                                      
REMARK 465     LYS A  -608                                                      
REMARK 465     ALA A  -607                                                      
REMARK 465     TYR A  -606                                                      
REMARK 465     ASP A  -605                                                      
REMARK 465     THR A  -604                                                      
REMARK 465     GLU A  -603                                                      
REMARK 465     LYS A  -602                                                      
REMARK 465     HIS A  -601                                                      
REMARK 465     ASN A  -600                                                      
REMARK 465     VAL A  -599                                                      
REMARK 465     TRP A  -598                                                      
REMARK 465     ALA A  -597                                                      
REMARK 465     THR A  -596                                                      
REMARK 465     HIS A  -595                                                      
REMARK 465     ALA A  -594                                                      
REMARK 465     CYS A  -593                                                      
REMARK 465     VAL A  -592                                                      
REMARK 465     PRO A  -591                                                      
REMARK 465     THR A  -590                                                      
REMARK 465     ASP A  -589                                                      
REMARK 465     PRO A  -588                                                      
REMARK 465     ASN A  -587                                                      
REMARK 465     PRO A  -586                                                      
REMARK 465     GLN A  -585                                                      
REMARK 465     GLU A  -584                                                      
REMARK 465     ILE A  -583                                                      
REMARK 465     HIS A  -582                                                      
REMARK 465     LEU A  -581                                                      
REMARK 465     GLU A  -580                                                      
REMARK 465     ASN A  -579                                                      
REMARK 465     VAL A  -578                                                      
REMARK 465     THR A  -577                                                      
REMARK 465     GLU A  -576                                                      
REMARK 465     GLU A  -575                                                      
REMARK 465     PHE A  -574                                                      
REMARK 465     ASN A  -573                                                      
REMARK 465     MET A  -572                                                      
REMARK 465     TRP A  -571                                                      
REMARK 465     LYS A  -570                                                      
REMARK 465     ASN A  -569                                                      
REMARK 465     ASN A  -568                                                      
REMARK 465     MET A  -567                                                      
REMARK 465     VAL A  -566                                                      
REMARK 465     GLU A  -565                                                      
REMARK 465     GLN A  -564                                                      
REMARK 465     MET A  -563                                                      
REMARK 465     HIS A  -562                                                      
REMARK 465     THR A  -561                                                      
REMARK 465     ASP A  -560                                                      
REMARK 465     ILE A  -559                                                      
REMARK 465     ILE A  -558                                                      
REMARK 465     SER A  -557                                                      
REMARK 465     LEU A  -556                                                      
REMARK 465     TRP A  -555                                                      
REMARK 465     ASP A  -554                                                      
REMARK 465     GLN A  -553                                                      
REMARK 465     SER A  -552                                                      
REMARK 465     LEU A  -551                                                      
REMARK 465     LYS A  -550                                                      
REMARK 465     PRO A  -549                                                      
REMARK 465     CYS A  -548                                                      
REMARK 465     VAL A  -547                                                      
REMARK 465     LYS A  -546                                                      
REMARK 465     LEU A  -545                                                      
REMARK 465     THR A  -544                                                      
REMARK 465     PRO A  -543                                                      
REMARK 465     LEU A  -542                                                      
REMARK 465     CYS A  -541                                                      
REMARK 465     VAL A  -540                                                      
REMARK 465     THR A  -539                                                      
REMARK 465     LEU A  -538                                                      
REMARK 465     GLN A  -537                                                      
REMARK 465     CYS A  -536                                                      
REMARK 465     THR A  -535                                                      
REMARK 465     ASN A  -534                                                      
REMARK 465     VAL A  -533                                                      
REMARK 465     THR A  -532                                                      
REMARK 465     ASN A  -531                                                      
REMARK 465     ASN A  -530                                                      
REMARK 465     ILE A  -529                                                      
REMARK 465     THR A  -528                                                      
REMARK 465     ASP A  -527                                                      
REMARK 465     ASP A  -526                                                      
REMARK 465     MET A  -525                                                      
REMARK 465     ARG A  -524                                                      
REMARK 465     GLY A  -523                                                      
REMARK 465     GLU A  -522                                                      
REMARK 465     LEU A  -521                                                      
REMARK 465     LYS A  -520                                                      
REMARK 465     ASN A  -519                                                      
REMARK 465     CYS A  -518                                                      
REMARK 465     SER A  -517                                                      
REMARK 465     PHE A  -516                                                      
REMARK 465     ASN A  -515                                                      
REMARK 465     MET A  -514                                                      
REMARK 465     THR A  -513                                                      
REMARK 465     THR A  -512                                                      
REMARK 465     GLU A  -511                                                      
REMARK 465     LEU A  -510                                                      
REMARK 465     ARG A  -509                                                      
REMARK 465     ASP A  -508                                                      
REMARK 465     LYS A  -507                                                      
REMARK 465     LYS A  -506                                                      
REMARK 465     GLN A  -505                                                      
REMARK 465     LYS A  -504                                                      
REMARK 465     VAL A  -503                                                      
REMARK 465     TYR A  -502                                                      
REMARK 465     SER A  -501                                                      
REMARK 465     LEU A  -500                                                      
REMARK 465     PHE A  -499                                                      
REMARK 465     TYR A  -498                                                      
REMARK 465     ARG A  -497                                                      
REMARK 465     LEU A  -496                                                      
REMARK 465     ASP A  -495                                                      
REMARK 465     VAL A  -494                                                      
REMARK 465     VAL A  -493                                                      
REMARK 465     GLN A  -492                                                      
REMARK 465     ILE A  -491                                                      
REMARK 465     ASN A  -490                                                      
REMARK 465     GLU A  -489                                                      
REMARK 465     ASN A  -488                                                      
REMARK 465     GLN A  -487                                                      
REMARK 465     GLY A  -486                                                      
REMARK 465     ASN A  -485                                                      
REMARK 465     ARG A  -484                                                      
REMARK 465     SER A  -483                                                      
REMARK 465     ASN A  -482                                                      
REMARK 465     ASN A  -481                                                      
REMARK 465     SER A  -480                                                      
REMARK 465     ASN A  -479                                                      
REMARK 465     LYS A  -478                                                      
REMARK 465     GLU A  -477                                                      
REMARK 465     TYR A  -476                                                      
REMARK 465     ARG A  -475                                                      
REMARK 465     LEU A  -474                                                      
REMARK 465     ILE A  -473                                                      
REMARK 465     ASN A  -472                                                      
REMARK 465     CYS A  -471                                                      
REMARK 465     ASN A  -470                                                      
REMARK 465     THR A  -469                                                      
REMARK 465     SER A  -468                                                      
REMARK 465     ALA A  -467                                                      
REMARK 465     ILE A  -466                                                      
REMARK 465     THR A  -465                                                      
REMARK 465     GLN A  -464                                                      
REMARK 465     ALA A  -463                                                      
REMARK 465     CYS A  -462                                                      
REMARK 465     PRO A  -461                                                      
REMARK 465     LYS A  -460                                                      
REMARK 465     VAL A  -459                                                      
REMARK 465     SER A  -458                                                      
REMARK 465     PHE A  -457                                                      
REMARK 465     GLU A  -456                                                      
REMARK 465     PRO A  -455                                                      
REMARK 465     ILE A  -454                                                      
REMARK 465     PRO A  -453                                                      
REMARK 465     ILE A  -452                                                      
REMARK 465     HIS A  -451                                                      
REMARK 465     TYR A  -450                                                      
REMARK 465     CYS A  -449                                                      
REMARK 465     ALA A  -448                                                      
REMARK 465     PRO A  -447                                                      
REMARK 465     ALA A  -446                                                      
REMARK 465     GLY A  -445                                                      
REMARK 465     PHE A  -444                                                      
REMARK 465     ALA A  -443                                                      
REMARK 465     ILE A  -442                                                      
REMARK 465     LEU A  -441                                                      
REMARK 465     LYS A  -440                                                      
REMARK 465     CYS A  -439                                                      
REMARK 465     LYS A  -438                                                      
REMARK 465     ASP A  -437                                                      
REMARK 465     LYS A  -436                                                      
REMARK 465     LYS A  -435                                                      
REMARK 465     PHE A  -434                                                      
REMARK 465     ASN A  -433                                                      
REMARK 465     GLY A  -432                                                      
REMARK 465     THR A  -431                                                      
REMARK 465     GLY A  -430                                                      
REMARK 465     PRO A  -429                                                      
REMARK 465     CYS A  -428                                                      
REMARK 465     PRO A  -427                                                      
REMARK 465     SER A  -426                                                      
REMARK 465     VAL A  -425                                                      
REMARK 465     SER A  -424                                                      
REMARK 465     THR A  -423                                                      
REMARK 465     VAL A  -422                                                      
REMARK 465     GLN A  -421                                                      
REMARK 465     CYS A  -420                                                      
REMARK 465     THR A  -419                                                      
REMARK 465     HIS A  -418                                                      
REMARK 465     GLY A  -417                                                      
REMARK 465     ILE A  -416                                                      
REMARK 465     LYS A  -415                                                      
REMARK 465     PRO A  -414                                                      
REMARK 465     VAL A  -413                                                      
REMARK 465     VAL A  -412                                                      
REMARK 465     SER A  -411                                                      
REMARK 465     THR A  -410                                                      
REMARK 465     GLN A  -409                                                      
REMARK 465     LEU A  -408                                                      
REMARK 465     LEU A  -407                                                      
REMARK 465     LEU A  -406                                                      
REMARK 465     ASN A  -405                                                      
REMARK 465     GLY A  -404                                                      
REMARK 465     SER A  -403                                                      
REMARK 465     LEU A  -402                                                      
REMARK 465     ALA A  -401                                                      
REMARK 465     GLU A  -400                                                      
REMARK 465     GLU A  -399                                                      
REMARK 465     GLU A  -398                                                      
REMARK 465     VAL A  -397                                                      
REMARK 465     MET A  -396                                                      
REMARK 465     ILE A  -395                                                      
REMARK 465     ARG A  -394                                                      
REMARK 465     SER A  -393                                                      
REMARK 465     GLU A  -392                                                      
REMARK 465     ASN A  -391                                                      
REMARK 465     ILE A  -390                                                      
REMARK 465     THR A  -389                                                      
REMARK 465     ASN A  -388                                                      
REMARK 465     ASN A  -387                                                      
REMARK 465     ALA A  -386                                                      
REMARK 465     LYS A  -385                                                      
REMARK 465     ASN A  -384                                                      
REMARK 465     ILE A  -383                                                      
REMARK 465     LEU A  -382                                                      
REMARK 465     VAL A  -381                                                      
REMARK 465     GLN A  -380                                                      
REMARK 465     PHE A  -379                                                      
REMARK 465     ASN A  -378                                                      
REMARK 465     THR A  -377                                                      
REMARK 465     PRO A  -376                                                      
REMARK 465     VAL A  -375                                                      
REMARK 465     GLN A  -374                                                      
REMARK 465     ILE A  -373                                                      
REMARK 465     ASN A  -372                                                      
REMARK 465     CYS A  -371                                                      
REMARK 465     THR A  -370                                                      
REMARK 465     ARG A  -369                                                      
REMARK 465     PRO A  -368                                                      
REMARK 465     ASN A  -367                                                      
REMARK 465     ASN A  -366                                                      
REMARK 465     ASN A  -365                                                      
REMARK 465     THR A  -364                                                      
REMARK 465     ARG A  -363                                                      
REMARK 465     LYS A  -362                                                      
REMARK 465     SER A  -361                                                      
REMARK 465     ILE A  -360                                                      
REMARK 465     ARG A  -359                                                      
REMARK 465     ILE A  -358                                                      
REMARK 465     GLY A  -357                                                      
REMARK 465     PRO A  -356                                                      
REMARK 465     GLY A  -355                                                      
REMARK 465     GLN A  -354                                                      
REMARK 465     ALA A  -353                                                      
REMARK 465     PHE A  -352                                                      
REMARK 465     TYR A  -351                                                      
REMARK 465     ALA A  -350                                                      
REMARK 465     THR A  -349                                                      
REMARK 465     GLY A  -348                                                      
REMARK 465     ASP A  -347                                                      
REMARK 465     ILE A  -346                                                      
REMARK 465     ILE A  -345                                                      
REMARK 465     GLY A  -344                                                      
REMARK 465     ASP A  -343                                                      
REMARK 465     ILE A  -342                                                      
REMARK 465     ARG A  -341                                                      
REMARK 465     GLN A  -340                                                      
REMARK 465     ALA A  -339                                                      
REMARK 465     HIS A  -338                                                      
REMARK 465     CYS A  -337                                                      
REMARK 465     ASN A  -336                                                      
REMARK 465     VAL A  -335                                                      
REMARK 465     SER A  -334                                                      
REMARK 465     LYS A  -333                                                      
REMARK 465     ALA A  -332                                                      
REMARK 465     THR A  -331                                                      
REMARK 465     TRP A  -330                                                      
REMARK 465     ASN A  -329                                                      
REMARK 465     GLU A  -328                                                      
REMARK 465     THR A  -327                                                      
REMARK 465     LEU A  -326                                                      
REMARK 465     GLY A  -325                                                      
REMARK 465     LYS A  -324                                                      
REMARK 465     VAL A  -323                                                      
REMARK 465     VAL A  -322                                                      
REMARK 465     LYS A  -321                                                      
REMARK 465     GLN A  -320                                                      
REMARK 465     LEU A  -319                                                      
REMARK 465     ARG A  -318                                                      
REMARK 465     LYS A  -317                                                      
REMARK 465     HIS A  -316                                                      
REMARK 465     PHE A  -315                                                      
REMARK 465     GLY A  -314                                                      
REMARK 465     ASN A  -313                                                      
REMARK 465     ASN A  -312                                                      
REMARK 465     THR A  -311                                                      
REMARK 465     ILE A  -310                                                      
REMARK 465     ILE A  -309                                                      
REMARK 465     ARG A  -308                                                      
REMARK 465     PHE A  -307                                                      
REMARK 465     ALA A  -306                                                      
REMARK 465     ASN A  -305                                                      
REMARK 465     SER A  -304                                                      
REMARK 465     SER A  -303                                                      
REMARK 465     GLY A  -302                                                      
REMARK 465     GLY A  -301                                                      
REMARK 465     ASP A  -300                                                      
REMARK 465     LEU A  -299                                                      
REMARK 465     GLU A  -298                                                      
REMARK 465     VAL A  -297                                                      
REMARK 465     THR A  -296                                                      
REMARK 465     THR A  -295                                                      
REMARK 465     HIS A  -294                                                      
REMARK 465     SER A  -293                                                      
REMARK 465     PHE A  -292                                                      
REMARK 465     ASN A  -291                                                      
REMARK 465     CYS A  -290                                                      
REMARK 465     GLY A  -289                                                      
REMARK 465     GLY A  -288                                                      
REMARK 465     GLU A  -287                                                      
REMARK 465     PHE A  -286                                                      
REMARK 465     PHE A  -285                                                      
REMARK 465     TYR A  -284                                                      
REMARK 465     CYS A  -283                                                      
REMARK 465     ASN A  -282                                                      
REMARK 465     THR A  -281                                                      
REMARK 465     SER A  -280                                                      
REMARK 465     GLY A  -279                                                      
REMARK 465     LEU A  -278                                                      
REMARK 465     PHE A  -277                                                      
REMARK 465     ASN A  -276                                                      
REMARK 465     SER A  -275                                                      
REMARK 465     THR A  -274                                                      
REMARK 465     TRP A  -273                                                      
REMARK 465     ILE A  -272                                                      
REMARK 465     SER A  -271                                                      
REMARK 465     ASN A  -270                                                      
REMARK 465     THR A  -269                                                      
REMARK 465     SER A  -268                                                      
REMARK 465     VAL A  -267                                                      
REMARK 465     GLN A  -266                                                      
REMARK 465     GLY A  -265                                                      
REMARK 465     SER A  -264                                                      
REMARK 465     ASN A  -263                                                      
REMARK 465     SER A  -262                                                      
REMARK 465     THR A  -261                                                      
REMARK 465     GLY A  -260                                                      
REMARK 465     SER A  -259                                                      
REMARK 465     ASN A  -258                                                      
REMARK 465     ASP A  -257                                                      
REMARK 465     SER A  -256                                                      
REMARK 465     ILE A  -255                                                      
REMARK 465     THR A  -254                                                      
REMARK 465     LEU A  -253                                                      
REMARK 465     PRO A  -252                                                      
REMARK 465     CYS A  -251                                                      
REMARK 465     ARG A  -250                                                      
REMARK 465     ILE A  -249                                                      
REMARK 465     LYS A  -248                                                      
REMARK 465     GLN A  -247                                                      
REMARK 465     ILE A  -246                                                      
REMARK 465     ILE A  -245                                                      
REMARK 465     ASN A  -244                                                      
REMARK 465     MET A  -243                                                      
REMARK 465     TRP A  -242                                                      
REMARK 465     GLN A  -241                                                      
REMARK 465     ARG A  -240                                                      
REMARK 465     ILE A  -239                                                      
REMARK 465     GLY A  -238                                                      
REMARK 465     GLN A  -237                                                      
REMARK 465     ALA A  -236                                                      
REMARK 465     MET A  -235                                                      
REMARK 465     TYR A  -234                                                      
REMARK 465     ALA A  -233                                                      
REMARK 465     PRO A  -232                                                      
REMARK 465     PRO A  -231                                                      
REMARK 465     ILE A  -230                                                      
REMARK 465     GLN A  -229                                                      
REMARK 465     GLY A  -228                                                      
REMARK 465     VAL A  -227                                                      
REMARK 465     ILE A  -226                                                      
REMARK 465     ARG A  -225                                                      
REMARK 465     CYS A  -224                                                      
REMARK 465     VAL A  -223                                                      
REMARK 465     SER A  -222                                                      
REMARK 465     ASN A  -221                                                      
REMARK 465     ILE A  -220                                                      
REMARK 465     THR A  -219                                                      
REMARK 465     GLY A  -218                                                      
REMARK 465     LEU A  -217                                                      
REMARK 465     ILE A  -216                                                      
REMARK 465     LEU A  -215                                                      
REMARK 465     THR A  -214                                                      
REMARK 465     ARG A  -213                                                      
REMARK 465     ASP A  -212                                                      
REMARK 465     GLY A  -211                                                      
REMARK 465     GLY A  -210                                                      
REMARK 465     SER A  -209                                                      
REMARK 465     THR A  -208                                                      
REMARK 465     ASN A  -207                                                      
REMARK 465     SER A  -206                                                      
REMARK 465     THR A  -205                                                      
REMARK 465     THR A  -204                                                      
REMARK 465     GLU A  -203                                                      
REMARK 465     THR A  -202                                                      
REMARK 465     PHE A  -201                                                      
REMARK 465     ARG A  -200                                                      
REMARK 465     PRO A  -199                                                      
REMARK 465     GLY A  -198                                                      
REMARK 465     GLY A  -197                                                      
REMARK 465     GLY A  -196                                                      
REMARK 465     ASP A  -195                                                      
REMARK 465     MET A  -194                                                      
REMARK 465     ARG A  -193                                                      
REMARK 465     ASP A  -192                                                      
REMARK 465     ASN A  -191                                                      
REMARK 465     TRP A  -190                                                      
REMARK 465     ARG A  -189                                                      
REMARK 465     SER A  -188                                                      
REMARK 465     GLU A  -187                                                      
REMARK 465     LEU A  -186                                                      
REMARK 465     TYR A  -185                                                      
REMARK 465     LYS A  -184                                                      
REMARK 465     TYR A  -183                                                      
REMARK 465     LYS A  -182                                                      
REMARK 465     VAL A  -181                                                      
REMARK 465     VAL A  -180                                                      
REMARK 465     LYS A  -179                                                      
REMARK 465     ILE A  -178                                                      
REMARK 465     GLU A  -177                                                      
REMARK 465     PRO A  -176                                                      
REMARK 465     LEU A  -175                                                      
REMARK 465     GLY A  -174                                                      
REMARK 465     VAL A  -173                                                      
REMARK 465     ALA A  -172                                                      
REMARK 465     PRO A  -171                                                      
REMARK 465     THR A  -170                                                      
REMARK 465     ARG A  -169                                                      
REMARK 465     CYS A  -168                                                      
REMARK 465     LYS A  -167                                                      
REMARK 465     ARG A  -166                                                      
REMARK 465     ARG A  -165                                                      
REMARK 465     VAL A  -164                                                      
REMARK 465     VAL A  -163                                                      
REMARK 465     GLY A  -162                                                      
REMARK 465     GLY A  -161                                                      
REMARK 465     GLY A  -160                                                      
REMARK 465     GLY A  -159                                                      
REMARK 465     GLY A  -158                                                      
REMARK 465     SER A  -157                                                      
REMARK 465     GLY A  -156                                                      
REMARK 465     GLY A  -155                                                      
REMARK 465     GLY A  -154                                                      
REMARK 465     GLY A  -153                                                      
REMARK 465     SER A  -152                                                      
REMARK 465     ALA A  -151                                                      
REMARK 465     VAL A  -150                                                      
REMARK 465     GLY A  -149                                                      
REMARK 465     ILE A  -148                                                      
REMARK 465     GLY A  -147                                                      
REMARK 465     ALA A  -146                                                      
REMARK 465     VAL A  -145                                                      
REMARK 465     PHE A  -144                                                      
REMARK 465     LEU A  -143                                                      
REMARK 465     GLY A  -142                                                      
REMARK 465     PHE A  -141                                                      
REMARK 465     LEU A  -140                                                      
REMARK 465     GLY A  -139                                                      
REMARK 465     ALA A  -138                                                      
REMARK 465     ALA A  -137                                                      
REMARK 465     GLY A  -136                                                      
REMARK 465     SER A  -135                                                      
REMARK 465     THR A  -134                                                      
REMARK 465     MET A  -133                                                      
REMARK 465     GLY A  -132                                                      
REMARK 465     ALA A  -131                                                      
REMARK 465     ALA A  -130                                                      
REMARK 465     SER A  -129                                                      
REMARK 465     MET A  -128                                                      
REMARK 465     THR A  -127                                                      
REMARK 465     LEU A  -126                                                      
REMARK 465     THR A  -125                                                      
REMARK 465     VAL A  -124                                                      
REMARK 465     GLN A  -123                                                      
REMARK 465     ALA A  -122                                                      
REMARK 465     ARG A  -121                                                      
REMARK 465     ASN A  -120                                                      
REMARK 465     LEU A  -119                                                      
REMARK 465     LEU A  -118                                                      
REMARK 465     SER A  -117                                                      
REMARK 465     GLY A  -116                                                      
REMARK 465     ASN A  -115                                                      
REMARK 465     PRO A  -114                                                      
REMARK 465     ASP A  -113                                                      
REMARK 465     TRP A  -112                                                      
REMARK 465     LEU A  -111                                                      
REMARK 465     PRO A  -110                                                      
REMARK 465     ASP A  -109                                                      
REMARK 465     MET A  -108                                                      
REMARK 465     THR A  -107                                                      
REMARK 465     VAL A  -106                                                      
REMARK 465     TRP A  -105                                                      
REMARK 465     GLY A  -104                                                      
REMARK 465     ILE A  -103                                                      
REMARK 465     LYS A  -102                                                      
REMARK 465     GLN A  -101                                                      
REMARK 465     LEU A  -100                                                      
REMARK 465     GLN A   -99                                                      
REMARK 465     ALA A   -98                                                      
REMARK 465     ARG A   -97                                                      
REMARK 465     VAL A   -96                                                      
REMARK 465     LEU A   -95                                                      
REMARK 465     ALA A   -94                                                      
REMARK 465     VAL A   -93                                                      
REMARK 465     GLU A   -92                                                      
REMARK 465     ARG A   -91                                                      
REMARK 465     TYR A   -90                                                      
REMARK 465     LEU A   -89                                                      
REMARK 465     ARG A   -88                                                      
REMARK 465     ASP A   -87                                                      
REMARK 465     GLN A   -86                                                      
REMARK 465     GLN A   -85                                                      
REMARK 465     LEU A   -84                                                      
REMARK 465     LEU A   -83                                                      
REMARK 465     GLY A   -82                                                      
REMARK 465     ILE A   -81                                                      
REMARK 465     TRP A   -80                                                      
REMARK 465     GLY A   -79                                                      
REMARK 465     CYS A   -78                                                      
REMARK 465     SER A   -77                                                      
REMARK 465     GLY A   -76                                                      
REMARK 465     LYS A   -75                                                      
REMARK 465     LEU A   -74                                                      
REMARK 465     ILE A   -73                                                      
REMARK 465     CYS A   -72                                                      
REMARK 465     CYS A   -71                                                      
REMARK 465     THR A   -70                                                      
REMARK 465     ASN A   -69                                                      
REMARK 465     VAL A   -68                                                      
REMARK 465     PRO A   -67                                                      
REMARK 465     TRP A   -66                                                      
REMARK 465     ASN A   -65                                                      
REMARK 465     SER A   -64                                                      
REMARK 465     SER A   -63                                                      
REMARK 465     TRP A   -62                                                      
REMARK 465     SER A   -61                                                      
REMARK 465     ASN A   -60                                                      
REMARK 465     ARG A   -59                                                      
REMARK 465     ASN A   -58                                                      
REMARK 465     LEU A   -57                                                      
REMARK 465     SER A   -56                                                      
REMARK 465     GLU A   -55                                                      
REMARK 465     ILE A   -54                                                      
REMARK 465     TRP A   -53                                                      
REMARK 465     ASP A   -52                                                      
REMARK 465     ASN A   -51                                                      
REMARK 465     MET A   -50                                                      
REMARK 465     THR A   -49                                                      
REMARK 465     TRP A   -48                                                      
REMARK 465     LEU A   -47                                                      
REMARK 465     GLN A   -46                                                      
REMARK 465     TRP A   -45                                                      
REMARK 465     ASP A   -44                                                      
REMARK 465     LYS A   -43                                                      
REMARK 465     GLU A   -42                                                      
REMARK 465     ILE A   -41                                                      
REMARK 465     SER A   -40                                                      
REMARK 465     ASN A   -39                                                      
REMARK 465     TYR A   -38                                                      
REMARK 465     THR A   -37                                                      
REMARK 465     GLN A   -36                                                      
REMARK 465     ILE A   -35                                                      
REMARK 465     ILE A   -34                                                      
REMARK 465     TYR A   -33                                                      
REMARK 465     GLY A   -32                                                      
REMARK 465     LEU A   -31                                                      
REMARK 465     LEU A   -30                                                      
REMARK 465     GLU A   -29                                                      
REMARK 465     GLU A   -28                                                      
REMARK 465     SER A   -27                                                      
REMARK 465     GLN A   -26                                                      
REMARK 465     ASN A   -25                                                      
REMARK 465     GLN A   -24                                                      
REMARK 465     GLN A   -23                                                      
REMARK 465     GLU A   -22                                                      
REMARK 465     LYS A   -21                                                      
REMARK 465     ASN A   -20                                                      
REMARK 465     GLU A   -19                                                      
REMARK 465     GLN A   -18                                                      
REMARK 465     ASP A   -17                                                      
REMARK 465     LEU A   -16                                                      
REMARK 465     LEU A   -15                                                      
REMARK 465     ALA A   -14                                                      
REMARK 465     LEU A   -13                                                      
REMARK 465     ASP A   -12                                                      
REMARK 465     ALA A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     ALA A    -8                                                      
REMARK 465     ALA A    -7                                                      
REMARK 465     ALA A    -6                                                      
REMARK 465     LYS A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ALA A    -3                                                      
REMARK 465     THR A    -2                                                      
REMARK 465     THR A    -1                                                      
REMARK 465     GLU A     0                                                      
REMARK 465     GLY A   234                                                      
REMARK 465     GLY A   235                                                      
REMARK 465     GLY A   236                                                      
REMARK 465     GLY A   237                                                      
REMARK 465     SER A   238                                                      
REMARK 465     PHE A   239                                                      
REMARK 465     SER A   240                                                      
REMARK 465     GLU A   241                                                      
REMARK 465     GLU A   242                                                      
REMARK 465     GLN A   243                                                      
REMARK 465     LYS A   244                                                      
REMARK 465     LYS A   245                                                      
REMARK 465     ALA A   246                                                      
REMARK 465     LEU A   247                                                      
REMARK 465     ASP A   248                                                      
REMARK 465     LEU A   249                                                      
REMARK 465     ALA A   250                                                      
REMARK 465     PHE A   251                                                      
REMARK 465     TYR A   252                                                      
REMARK 465     PHE A   253                                                      
REMARK 465     ASP A   254                                                      
REMARK 465     ARG A   255                                                      
REMARK 465     ARG A   256                                                      
REMARK 465     LEU A   257                                                      
REMARK 465     THR A   258                                                      
REMARK 465     PRO A   259                                                      
REMARK 465     GLU A   260                                                      
REMARK 465     TRP A   261                                                      
REMARK 465     ARG A   262                                                      
REMARK 465     ARG A   263                                                      
REMARK 465     TYR A   264                                                      
REMARK 465     LEU A   265                                                      
REMARK 465     SER A   266                                                      
REMARK 465     GLN A   267                                                      
REMARK 465     ARG A   268                                                      
REMARK 465     LEU A   269                                                      
REMARK 465     GLY A   270                                                      
REMARK 465     LEU A   271                                                      
REMARK 465     ASN A   272                                                      
REMARK 465     GLU A   273                                                      
REMARK 465     GLU A   274                                                      
REMARK 465     GLN A   275                                                      
REMARK 465     ILE A   276                                                      
REMARK 465     GLU A   277                                                      
REMARK 465     ARG A   278                                                      
REMARK 465     TRP A   279                                                      
REMARK 465     PHE A   280                                                      
REMARK 465     ARG A   281                                                      
REMARK 465     ARG A   282                                                      
REMARK 465     LYS A   283                                                      
REMARK 465     GLU A   284                                                      
REMARK 465     GLN A   285                                                      
REMARK 465     GLN A   286                                                      
REMARK 465     ILE A   287                                                      
REMARK 465     GLY A   288                                                      
REMARK 465     TRP A   289                                                      
REMARK 465     SER A   290                                                      
REMARK 465     HIS A   291                                                      
REMARK 465     PRO A   292                                                      
REMARK 465     GLN A   293                                                      
REMARK 465     PHE A   294                                                      
REMARK 465     GLU A   295                                                      
REMARK 465     LYS A   296                                                      
REMARK 465     GLY A   297                                                      
REMARK 465     SER A   298                                                      
REMARK 465     ALA A   299                                                      
REMARK 465     LYS A   300                                                      
REMARK 465     PHE A   301                                                      
REMARK 465     VAL A   302                                                      
REMARK 465     ALA A   303                                                      
REMARK 465     ALA A   304                                                      
REMARK 465     TRP A   305                                                      
REMARK 465     THR A   306                                                      
REMARK 465     LEU A   307                                                      
REMARK 465     LYS A   308                                                      
REMARK 465     ALA A   309                                                      
REMARK 465     ALA A   310                                                      
REMARK 465     ALA A   311                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  78   C   -  N   -  CA  ANGL. DEV. =   9.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TRP A 163       70.63     39.52                                   
REMARK 500    ASP A 189     -121.39     53.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-28540   RELATED DB: EMDB                             
REMARK 900 RELATED ID: EMD-28541   RELATED DB: EMDB                             
REMARK 900 RELATED ID: EMD-28542   RELATED DB: EMDB                             
REMARK 900 RELATED ID: EMD-28543   RELATED DB: EMDB                             
DBREF  8EQN A -673   311  PDB    8EQN     8EQN          -673    311             
SEQRES   1 A  985  MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU          
SEQRES   2 A  985  LEU CYS GLY ALA VAL PHE VAL SER PRO SER GLN GLU ILE          
SEQRES   3 A  985  HIS ALA ARG PHE ARG ARG GLY ALA ARG SER ARG ALA GLU          
SEQRES   4 A  985  ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP          
SEQRES   5 A  985  LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA          
SEQRES   6 A  985  LYS ALA TYR ASP THR GLU LYS HIS ASN VAL TRP ALA THR          
SEQRES   7 A  985  HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE          
SEQRES   8 A  985  HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS          
SEQRES   9 A  985  ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE ILE SER          
SEQRES  10 A  985  LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR          
SEQRES  11 A  985  PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN          
SEQRES  12 A  985  ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS          
SEQRES  13 A  985  SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN          
SEQRES  14 A  985  LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN          
SEQRES  15 A  985  ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN          
SEQRES  16 A  985  LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE          
SEQRES  17 A  985  THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO          
SEQRES  18 A  985  ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS          
SEQRES  19 A  985  CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO          
SEQRES  20 A  985  SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO          
SEQRES  21 A  985  VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA          
SEQRES  22 A  985  GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE THR ASN          
SEQRES  23 A  985  ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR PRO VAL          
SEQRES  24 A  985  GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS          
SEQRES  25 A  985  SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA THR          
SEQRES  26 A  985  GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN          
SEQRES  27 A  985  VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL          
SEQRES  28 A  985  VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE          
SEQRES  29 A  985  ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU GLU VAL          
SEQRES  30 A  985  THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR          
SEQRES  31 A  985  CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SER          
SEQRES  32 A  985  ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER ASN          
SEQRES  33 A  985  ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE          
SEQRES  34 A  985  ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO          
SEQRES  35 A  985  PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR          
SEQRES  36 A  985  GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SER          
SEQRES  37 A  985  THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG          
SEQRES  38 A  985  ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL          
SEQRES  39 A  985  LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS          
SEQRES  40 A  985  ARG ARG VAL VAL GLY GLY GLY GLY GLY SER GLY GLY GLY          
SEQRES  41 A  985  GLY SER ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE          
SEQRES  42 A  985  LEU GLY ALA ALA GLY SER THR MET GLY ALA ALA SER MET          
SEQRES  43 A  985  THR LEU THR VAL GLN ALA ARG ASN LEU LEU SER GLY ASN          
SEQRES  44 A  985  PRO ASP TRP LEU PRO ASP MET THR VAL TRP GLY ILE LYS          
SEQRES  45 A  985  GLN LEU GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU          
SEQRES  46 A  985  ARG ASP GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY          
SEQRES  47 A  985  LYS LEU ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER          
SEQRES  48 A  985  TRP SER ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET          
SEQRES  49 A  985  THR TRP LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR          
SEQRES  50 A  985  GLN ILE ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN          
SEQRES  51 A  985  GLN GLU LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP ALA          
SEQRES  52 A  985  SER GLY ALA ALA ALA LYS PRO ALA THR THR GLU GLY GLU          
SEQRES  53 A  985  PHE PRO GLU THR ARG GLU LYS MET SER GLY ILE ARG ARG          
SEQRES  54 A  985  ALA ILE ALA LYS ALA MET VAL HIS SER LYS HIS THR ALA          
SEQRES  55 A  985  PRO HIS VAL THR LEU MET ASP GLU ALA ASP VAL THR LYS          
SEQRES  56 A  985  LEU VAL ALA HIS ARG LYS LYS PHE LYS ALA ILE ALA ALA          
SEQRES  57 A  985  GLU LYS GLY ILE LYS LEU THR PHE LEU PRO TYR VAL VAL          
SEQRES  58 A  985  LYS ALA LEU VAL SER ALA LEU ARG GLU TYR PRO VAL LEU          
SEQRES  59 A  985  ASN THR SER ILE ASP ASP GLU THR GLU GLU ILE ILE GLN          
SEQRES  60 A  985  LYS HIS TYR TYR ASN ILE GLY ILE ALA ALA ASP THR ASP          
SEQRES  61 A  985  ARG GLY LEU LEU VAL PRO VAL ILE LYS HIS ALA ASP ARG          
SEQRES  62 A  985  LYS PRO ILE PHE ALA LEU ALA GLN GLU ILE ASN GLU LEU          
SEQRES  63 A  985  ALA GLU LYS ALA ARG ASP GLY LYS LEU THR PRO GLY GLU          
SEQRES  64 A  985  MET LYS GLY ALA SER CYS THR ILE THR ASN ILE GLY SER          
SEQRES  65 A  985  ALA GLY GLY GLN TRP PHE THR PRO VAL ILE ASN HIS PRO          
SEQRES  66 A  985  GLU VAL ALA ILE LEU GLY ILE GLY ARG ILE ALA GLU LYS          
SEQRES  67 A  985  PRO ILE VAL ARG ASP GLY GLU ILE VAL ALA ALA PRO MET          
SEQRES  68 A  985  LEU ALA LEU SER LEU SER PHE ASP HIS ARG MET ILE ASP          
SEQRES  69 A  985  GLY ALA THR ALA GLN LYS ALA LEU ASN HIS ILE LYS ARG          
SEQRES  70 A  985  LEU LEU SER ASP PRO GLU LEU LEU LEU MET GLY GLY GLY          
SEQRES  71 A  985  GLY SER PHE SER GLU GLU GLN LYS LYS ALA LEU ASP LEU          
SEQRES  72 A  985  ALA PHE TYR PHE ASP ARG ARG LEU THR PRO GLU TRP ARG          
SEQRES  73 A  985  ARG TYR LEU SER GLN ARG LEU GLY LEU ASN GLU GLU GLN          
SEQRES  74 A  985  ILE GLU ARG TRP PHE ARG ARG LYS GLU GLN GLN ILE GLY          
SEQRES  75 A  985  TRP SER HIS PRO GLN PHE GLU LYS GLY SER ALA LYS PHE          
SEQRES  76 A  985  VAL ALA ALA TRP THR LEU LYS ALA ALA ALA                      
HELIX    1 AA1 ILE A   13  LYS A   25  1                                  13    
HELIX    2 AA2 VAL A   39  PHE A   49  1                                  11    
HELIX    3 AA3 PHE A   49  LYS A   56  1                                   8    
HELIX    4 AA4 PHE A   62  TYR A   77  1                                  16    
HELIX    5 AA5 PRO A   78  LEU A   80  5                                   3    
HELIX    6 AA6 HIS A  116  LYS A  120  5                                   5    
HELIX    7 AA7 PRO A  121  GLY A  139  1                                  19    
HELIX    8 AA8 THR A  142  LYS A  147  5                                   6    
HELIX    9 AA9 GLY A  157  GLY A  160  5                                   4    
HELIX   10 AB1 ASP A  210  SER A  226  1                                  17    
HELIX   11 AB2 ASP A  227  MET A  233  1                                   7    
SHEET    1 AA1 6 HIS A  30  ASP A  38  0                                        
SHEET    2 AA1 6 GLU A 191  ASP A 205 -1  O  LEU A 198   N  ALA A  37           
SHEET    3 AA1 6 ALA A 174  ARG A 188 -1  N  GLY A 177   O  SER A 201           
SHEET    4 AA1 6 CYS A 151  ASN A 155  1  N  THR A 154   O  ILE A 178           
SHEET    5 AA1 6 ILE A  99  THR A 105  1  N  GLY A 100   O  ILE A 153           
SHEET    6 AA1 6 GLY A 108  LEU A 110 -1  O  LEU A 110   N  ALA A 103           
SHEET    1 AA2 6 HIS A  30  ASP A  38  0                                        
SHEET    2 AA2 6 GLU A 191  ASP A 205 -1  O  LEU A 198   N  ALA A  37           
SHEET    3 AA2 6 ALA A 174  ARG A 188 -1  N  GLY A 177   O  SER A 201           
SHEET    4 AA2 6 CYS A 151  ASN A 155  1  N  THR A 154   O  ILE A 178           
SHEET    5 AA2 6 ILE A  99  THR A 105  1  N  GLY A 100   O  ILE A 153           
SHEET    6 AA2 6 VAL A 113  ILE A 114 -1  O  ILE A 114   N  ILE A  99           
SHEET    1 AA3 2 THR A  82  ILE A  84  0                                        
SHEET    2 AA3 2 ILE A  91  GLN A  93 -1  O  ILE A  92   N  SER A  83           
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           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   GLY A   1     237.518 364.514 327.449  1.00 78.56           N  
ATOM      2  CA  GLY A   1     236.166 364.058 327.160  1.00 82.67           C  
ATOM      3  C   GLY A   1     236.173 363.155 325.942  1.00 84.42           C  
ATOM      4  O   GLY A   1     235.611 362.061 325.963  1.00 83.46           O  
ATOM      5  N   GLU A   2     236.825 363.628 324.890  1.00 83.04           N  
ATOM      6  CA  GLU A   2     236.961 362.904 323.632  1.00 80.60           C  
ATOM      7  C   GLU A   2     238.313 363.250 323.061  1.00 77.83           C  
ATOM      8  O   GLU A   2     238.862 364.302 323.376  1.00 78.25           O  
ATOM      9  CB  GLU A   2     235.815 363.247 322.675  1.00 81.84           C  
ATOM     10  CG  GLU A   2     235.831 362.506 321.335  1.00 80.24           C  
ATOM     11  CD  GLU A   2     235.834 361.013 321.456  1.00 79.39           C  
ATOM     12  OE1 GLU A   2     236.888 360.478 321.758  1.00 77.51           O  
ATOM     13  OE2 GLU A   2     234.819 360.404 321.231  1.00 83.13           O  
ATOM     14  N   PHE A   3     238.857 362.366 322.243  1.00 76.12           N  
ATOM     15  CA  PHE A   3     240.189 362.542 321.682  1.00 74.50           C  
ATOM     16  C   PHE A   3     241.116 363.074 322.766  1.00 71.93           C  
ATOM     17  O   PHE A   3     241.683 364.151 322.604  1.00 74.37           O  
ATOM     18  CB  PHE A   3     240.200 363.529 320.511  1.00 73.55           C  
ATOM     19  CG  PHE A   3     239.385 363.145 319.336  1.00 70.34           C  
ATOM     20  CD1 PHE A   3     238.301 363.892 318.962  1.00 74.25           C  
ATOM     21  CD2 PHE A   3     239.699 362.036 318.598  1.00 73.27           C  
ATOM     22  CE1 PHE A   3     237.546 363.536 317.871  1.00 73.11           C  
ATOM     23  CE2 PHE A   3     238.957 361.676 317.512  1.00 69.86           C  
ATOM     24  CZ  PHE A   3     237.877 362.428 317.147  1.00 66.73           C  
ATOM     25  N   PRO A   4     241.333 362.344 323.869  1.00 72.11           N  
ATOM     26  CA  PRO A   4     242.056 362.819 325.016  1.00 72.69           C  
ATOM     27  C   PRO A   4     243.493 363.060 324.665  1.00 73.51           C  
ATOM     28  O   PRO A   4     244.039 362.323 323.836  1.00 79.28           O  
ATOM     29  CB  PRO A   4     241.960 361.648 325.998  1.00 74.41           C  
ATOM     30  CG  PRO A   4     240.848 360.782 325.470  1.00 73.42           C  
ATOM     31  CD  PRO A   4     240.941 360.925 323.978  1.00 74.40           C  
ATOM     32  N   GLU A   5     244.099 364.042 325.329  1.00 76.99           N  
ATOM     33  CA  GLU A   5     245.519 364.322 325.186  1.00 76.82           C  
ATOM     34  C   GLU A   5     246.143 364.630 326.542  1.00 79.46           C  
ATOM     35  O   GLU A   5     245.538 365.318 327.365  1.00 81.48           O  
ATOM     36  CB  GLU A   5     245.752 365.509 324.244  1.00 77.75           C  
ATOM     37  CG  GLU A   5     245.290 365.280 322.810  1.00 81.09           C  
ATOM     38  CD  GLU A   5     245.609 366.397 321.860  1.00 78.83           C  
ATOM     39  OE1 GLU A   5     246.072 367.412 322.312  1.00 83.93           O  
ATOM     40  OE2 GLU A   5     245.404 366.232 320.667  1.00 76.22           O  
ATOM     41  N   THR A   6     247.372 364.185 326.744  1.00 79.11           N  
ATOM     42  CA  THR A   6     248.118 364.490 327.961  1.00 82.04           C  
ATOM     43  C   THR A   6     249.272 365.435 327.686  1.00 84.32           C  
ATOM     44  O   THR A   6     250.061 365.232 326.762  1.00 91.19           O  
ATOM     45  CB  THR A   6     248.673 363.222 328.655  1.00 84.22           C  
ATOM     46  OG1 THR A   6     247.597 362.370 329.056  1.00 82.41           O  
ATOM     47  CG2 THR A   6     249.488 363.602 329.896  1.00 89.12           C  
ATOM     48  N   ARG A   7     249.375 366.483 328.485  1.00 91.06           N  
ATOM     49  CA  ARG A   7     250.469 367.435 328.336  1.00 96.95           C  
ATOM     50  C   ARG A   7     251.617 367.123 329.286  1.00 99.33           C  
ATOM     51  O   ARG A   7     251.388 366.852 330.465  1.00101.36           O  
ATOM     52  CB  ARG A   7     249.972 368.839 328.586  1.00 98.53           C  
ATOM     53  CG  ARG A   7     250.998 369.950 328.393  1.00104.38           C  
ATOM     54  CD  ARG A   7     250.376 371.264 328.629  1.00106.02           C  
ATOM     55  NE  ARG A   7     249.312 371.510 327.674  1.00112.16           N  
ATOM     56  CZ  ARG A   7     249.466 372.037 326.443  1.00110.76           C  
ATOM     57  NH1 ARG A   7     250.645 372.423 326.002  1.00107.17           N  
ATOM     58  NH2 ARG A   7     248.406 372.166 325.659  1.00112.44           N  
ATOM     59  N   GLU A   8     252.843 367.234 328.776  1.00 97.77           N  
ATOM     60  CA  GLU A   8     254.071 367.013 329.527  1.00106.20           C  
ATOM     61  C   GLU A   8     255.106 368.109 329.219  1.00108.03           C  
ATOM     62  O   GLU A   8     255.037 368.788 328.185  1.00100.91           O  
ATOM     63  CB  GLU A   8     254.609 365.610 329.205  1.00106.60           C  
ATOM     64  CG  GLU A   8     255.892 365.181 329.934  1.00112.54           C  
ATOM     65  CD  GLU A   8     255.756 365.174 331.433  1.00112.73           C  
ATOM     66  OE1 GLU A   8     255.616 364.123 332.006  1.00119.76           O  
ATOM     67  OE2 GLU A   8     255.777 366.251 332.000  1.00116.94           O  
ATOM     68  N   LYS A   9     256.039 368.316 330.151  1.00119.66           N  
ATOM     69  CA  LYS A   9     257.082 369.321 329.987  1.00114.09           C  
ATOM     70  C   LYS A   9     258.349 368.801 329.308  1.00108.35           C  
ATOM     71  O   LYS A   9     258.943 367.798 329.709  1.00116.45           O  
ATOM     72  CB  LYS A   9     257.419 369.912 331.342  1.00121.72           C  
ATOM     73  CG  LYS A   9     256.235 370.620 331.975  1.00125.28           C  
ATOM     74  CD  LYS A   9     256.613 371.315 333.269  1.00129.34           C  
ATOM     75  CE  LYS A   9     255.401 371.976 333.910  1.00133.41           C  
ATOM     76  NZ  LYS A   9     255.751 372.661 335.183  1.00122.97           N  
ATOM     77  N   MET A  10     258.843 369.585 328.355  1.00147.77           N  
ATOM     78  CA  MET A  10     260.034 369.279 327.583  1.00116.27           C  
ATOM     79  C   MET A  10     261.343 369.423 328.379  1.00111.57           C  
ATOM     80  O   MET A  10     262.388 368.908 327.972  1.00133.03           O  
ATOM     81  CB  MET A  10     260.050 370.216 326.370  1.00116.95           C  
ATOM     82  CG  MET A  10     261.044 369.936 325.323  1.00117.24           C  
ATOM     83  SD  MET A  10     260.951 371.035 323.946  1.00123.78           S  
ATOM     84  CE  MET A  10     262.098 370.200 322.862  1.00118.96           C  
ATOM     85  N   SER A  11     261.303 370.131 329.498  1.00122.02           N  
ATOM     86  CA  SER A  11     262.512 370.467 330.243  1.00122.47           C  
ATOM     87  C   SER A  11     263.300 369.320 330.880  1.00131.40           C  
ATOM     88  O   SER A  11     264.495 369.481 331.117  1.00123.77           O  
ATOM     89  CB  SER A  11     262.167 371.450 331.337  1.00123.59           C  
ATOM     90  OG  SER A  11     261.346 370.858 332.306  1.00123.36           O  
ATOM     91  N   GLY A  12     262.692 368.160 331.135  1.00122.24           N  
ATOM     92  CA  GLY A  12     263.439 367.068 331.768  1.00124.10           C  
ATOM     93  C   GLY A  12     264.634 366.588 330.932  1.00120.53           C  
ATOM     94  O   GLY A  12     265.789 366.712 331.343  1.00122.22           O  
ATOM     95  N   ILE A  13     264.353 366.003 329.769  1.00123.81           N  
ATOM     96  CA  ILE A  13     265.422 365.549 328.869  1.00122.70           C  
ATOM     97  C   ILE A  13     265.285 366.063 327.443  1.00126.37           C  
ATOM     98  O   ILE A  13     266.279 366.193 326.720  1.00115.53           O  
ATOM     99  CB  ILE A  13     265.539 364.002 328.836  1.00119.56           C  
ATOM    100  CG1 ILE A  13     266.914 363.617 328.196  1.00115.40           C  
ATOM    101  CG2 ILE A  13     264.363 363.350 328.058  1.00120.20           C  
ATOM    102  CD1 ILE A  13     267.337 362.158 328.346  1.00 95.96           C  
ATOM    103  N   ARG A  14     264.049 366.288 327.012  1.00120.12           N  
ATOM    104  CA  ARG A  14     263.773 366.575 325.619  1.00124.02           C  
ATOM    105  C   ARG A  14     264.385 367.889 325.186  1.00112.49           C  
ATOM    106  O   ARG A  14     264.880 368.007 324.067  1.00124.50           O  
ATOM    107  CB  ARG A  14     262.277 366.632 325.413  1.00116.96           C  
ATOM    108  CG  ARG A  14     261.491 365.359 325.675  1.00115.74           C  
ATOM    109  CD  ARG A  14     261.750 364.325 324.708  1.00103.46           C  
ATOM    110  NE  ARG A  14     260.888 363.185 324.922  1.00107.72           N  
ATOM    111  CZ  ARG A  14     260.940 362.077 324.185  1.00 92.44           C  
ATOM    112  NH1 ARG A  14     261.816 362.020 323.226  1.00 87.74           N  
ATOM    113  NH2 ARG A  14     260.121 361.069 324.418  1.00101.05           N  
ATOM    114  N   ARG A  15     264.382 368.870 326.078  1.00111.93           N  
ATOM    115  CA  ARG A  15     264.934 370.168 325.768  1.00132.36           C  
ATOM    116  C   ARG A  15     266.418 370.071 325.515  1.00111.12           C  
ATOM    117  O   ARG A  15     266.941 370.788 324.658  1.00136.07           O  
ATOM    118  CB  ARG A  15     264.653 371.158 326.885  1.00124.91           C  
ATOM    119  CG  ARG A  15     265.118 372.587 326.641  1.00127.90           C  
ATOM    120  CD  ARG A  15     264.265 373.300 325.640  1.00130.54           C  
ATOM    121  NE  ARG A  15     264.733 373.086 324.262  1.00122.98           N  
ATOM    122  CZ  ARG A  15     264.107 373.552 323.154  1.00119.68           C  
ATOM    123  NH1 ARG A  15     262.999 374.255 323.270  1.00133.06           N  
ATOM    124  NH2 ARG A  15     264.604 373.307 321.955  1.00125.86           N  
ATOM    125  N   ALA A  16     267.108 369.229 326.296  1.00117.62           N  
ATOM    126  CA  ALA A  16     268.544 369.060 326.145  1.00119.30           C  
ATOM    127  C   ALA A  16     268.872 368.401 324.814  1.00123.94           C  
ATOM    128  O   ALA A  16     269.803 368.814 324.106  1.00119.24           O  
ATOM    129  CB  ALA A  16     269.082 368.218 327.284  1.00118.40           C  
ATOM    130  N   ILE A  17     268.059 367.418 324.437  1.00118.11           N  
ATOM    131  CA  ILE A  17     268.293 366.736 323.186  1.00121.20           C  
ATOM    132  C   ILE A  17     268.029 367.691 322.056  1.00111.63           C  
ATOM    133  O   ILE A  17     268.833 367.801 321.126  1.00111.65           O  
ATOM    134  CB  ILE A  17     267.397 365.492 323.043  1.00116.43           C  
ATOM    135  CG1 ILE A  17     267.828 364.430 324.109  1.00116.06           C  
ATOM    136  CG2 ILE A  17     267.488 364.931 321.572  1.00102.53           C  
ATOM    137  CD1 ILE A  17     266.844 363.285 324.301  1.00116.00           C  
ATOM    138  N   ALA A  18     266.908 368.398 322.126  1.00118.92           N  
ATOM    139  CA  ALA A  18     266.581 369.316 321.075  1.00110.34           C  
ATOM    140  C   ALA A  18     267.621 370.400 320.955  1.00105.89           C  
ATOM    141  O   ALA A  18     268.022 370.723 319.851  1.00123.31           O  
ATOM    142  CB  ALA A  18     265.233 369.932 321.314  1.00114.91           C  
ATOM    143  N   LYS A  19     268.163 370.910 322.059  1.00122.07           N  
ATOM    144  CA  LYS A  19     269.147 371.969 321.940  1.00117.29           C  
ATOM    145  C   LYS A  19     270.302 371.554 321.037  1.00116.60           C  
ATOM    146  O   LYS A  19     270.859 372.384 320.310  1.00115.47           O  
ATOM    147  CB  LYS A  19     269.662 372.388 323.310  1.00120.60           C  
ATOM    148  CG  LYS A  19     270.642 373.555 323.271  1.00127.80           C  
ATOM    149  CD  LYS A  19     271.024 374.007 324.671  1.00138.00           C  
ATOM    150  CE  LYS A  19     272.013 375.162 324.625  1.00147.60           C  
ATOM    151  NZ  LYS A  19     272.378 375.637 325.990  1.00143.91           N  
ATOM    152  N   ALA A  20     270.742 370.301 321.140  1.00117.12           N  
ATOM    153  CA  ALA A  20     271.808 369.866 320.255  1.00116.30           C  
ATOM    154  C   ALA A  20     271.293 369.591 318.826  1.00115.69           C  
ATOM    155  O   ALA A  20     271.912 370.003 317.832  1.00108.84           O  
ATOM    156  CB  ALA A  20     272.448 368.611 320.809  1.00106.42           C  
ATOM    157  N   MET A  21     270.116 368.967 318.714  1.00113.28           N  
ATOM    158  CA  MET A  21     269.598 368.585 317.403  1.00108.73           C  
ATOM    159  C   MET A  21     269.238 369.769 316.528  1.00118.04           C  
ATOM    160  O   MET A  21     269.451 369.728 315.308  1.00105.04           O  
ATOM    161  CB  MET A  21     268.375 367.698 317.567  1.00101.29           C  
ATOM    162  CG  MET A  21     268.627 366.313 318.129  1.00 94.60           C  
ATOM    163  SD  MET A  21     269.666 365.306 317.110  1.00 96.92           S  
ATOM    164  CE  MET A  21     269.668 363.843 318.151  1.00 80.67           C  
ATOM    165  N   VAL A  22     268.789 370.853 317.148  1.00110.12           N  
ATOM    166  CA  VAL A  22     268.392 372.039 316.410  1.00116.11           C  
ATOM    167  C   VAL A  22     269.587 372.788 315.849  1.00108.08           C  
ATOM    168  O   VAL A  22     269.400 373.751 315.122  1.00113.74           O  
ATOM    169  CB  VAL A  22     267.488 372.991 317.224  1.00109.86           C  
ATOM    170  CG1 VAL A  22     266.206 372.239 317.634  1.00106.66           C  
ATOM    171  CG2 VAL A  22     268.243 373.562 318.401  1.00114.60           C  
ATOM    172  N   HIS A  23     270.800 372.437 316.265  1.00112.35           N  
ATOM    173  CA  HIS A  23     271.994 373.034 315.703  1.00111.99           C  
ATOM    174  C   HIS A  23     272.480 372.138 314.571  1.00109.82           C  
ATOM    175  O   HIS A  23     272.835 372.581 313.469  1.00111.14           O  
ATOM    176  CB  HIS A  23     273.096 373.175 316.741  1.00112.04           C  
ATOM    177  CG  HIS A  23     274.321 373.794 316.184  1.00105.08           C  
ATOM    178  ND1 HIS A  23     274.413 375.134 315.862  1.00108.13           N  
ATOM    179  CD2 HIS A  23     275.497 373.249 315.859  1.00104.52           C  
ATOM    180  CE1 HIS A  23     275.612 375.376 315.370  1.00109.26           C  
ATOM    181  NE2 HIS A  23     276.289 374.249 315.359  1.00105.43           N  
ATOM    182  N   SER A  24     272.471 370.829 314.826  1.00110.95           N  
ATOM    183  CA  SER A  24     272.977 369.888 313.843  1.00105.86           C  
ATOM    184  C   SER A  24     272.168 369.973 312.546  1.00107.53           C  
ATOM    185  O   SER A  24     272.743 369.934 311.453  1.00106.27           O  
ATOM    186  CB  SER A  24     272.939 368.471 314.398  1.00 99.61           C  
ATOM    187  OG  SER A  24     273.849 368.302 315.480  1.00 97.50           O  
ATOM    188  N   LYS A  25     270.854 370.224 312.658  1.00108.06           N  
ATOM    189  CA  LYS A  25     269.961 370.274 311.499  1.00111.02           C  
ATOM    190  C   LYS A  25     270.306 371.322 310.455  1.00112.96           C  
ATOM    191  O   LYS A  25     269.859 371.203 309.315  1.00111.89           O  
ATOM    192  CB  LYS A  25     268.511 370.548 311.899  1.00101.45           C  
ATOM    193  CG  LYS A  25     268.209 371.984 312.370  1.00106.66           C  
ATOM    194  CD  LYS A  25     266.718 372.208 312.629  1.00110.47           C  
ATOM    195  CE  LYS A  25     266.426 373.558 313.341  1.00109.44           C  
ATOM    196  NZ  LYS A  25     266.983 374.779 312.629  1.00113.11           N  
ATOM    197  N   HIS A  26     271.030 372.377 310.815  1.00107.49           N  
ATOM    198  CA  HIS A  26     271.334 373.377 309.813  1.00110.57           C  
ATOM    199  C   HIS A  26     272.814 373.645 309.756  1.00106.85           C  
ATOM    200  O   HIS A  26     273.243 374.695 309.269  1.00109.97           O  
ATOM    201  CB  HIS A  26     270.575 374.690 310.060  1.00112.41           C  
ATOM    202  CG  HIS A  26     270.807 375.340 311.409  1.00114.12           C  
ATOM    203  ND1 HIS A  26     269.857 375.328 312.423  1.00115.62           N  
ATOM    204  CD2 HIS A  26     271.881 376.020 311.908  1.00110.86           C  
ATOM    205  CE1 HIS A  26     270.351 375.979 313.483  1.00115.96           C  
ATOM    206  NE2 HIS A  26     271.565 376.402 313.189  1.00114.58           N  
ATOM    207  N   THR A  27     273.601 372.690 310.226  1.00106.66           N  
ATOM    208  CA  THR A  27     275.039 372.830 310.197  1.00106.11           C  
ATOM    209  C   THR A  27     275.610 372.805 308.791  1.00101.90           C  
ATOM    210  O   THR A  27     276.534 373.557 308.476  1.00100.73           O  
ATOM    211  CB  THR A  27     275.701 371.758 311.078  1.00103.08           C  
ATOM    212  OG1 THR A  27     275.333 371.985 312.455  1.00103.93           O  
ATOM    213  CG2 THR A  27     277.225 371.781 310.936  1.00 97.55           C  
ATOM    214  N   ALA A  28     275.105 371.913 307.958  1.00 97.83           N  
ATOM    215  CA  ALA A  28     275.638 371.738 306.629  1.00 92.09           C  
ATOM    216  C   ALA A  28     274.641 370.975 305.794  1.00 92.77           C  
ATOM    217  O   ALA A  28     273.721 370.385 306.357  1.00 90.16           O  
ATOM    218  CB  ALA A  28     276.948 370.978 306.716  1.00 88.99           C  
ATOM    219  N   PRO A  29     274.688 371.049 304.466  1.00 92.26           N  
ATOM    220  CA  PRO A  29     273.960 370.143 303.632  1.00 85.92           C  
ATOM    221  C   PRO A  29     274.641 368.809 303.837  1.00 75.88           C  
ATOM    222  O   PRO A  29     275.880 368.755 303.841  1.00 73.02           O  
ATOM    223  CB  PRO A  29     274.140 370.730 302.237  1.00 88.53           C  
ATOM    224  CG  PRO A  29     275.417 371.540 302.325  1.00 92.57           C  
ATOM    225  CD  PRO A  29     275.524 372.023 303.757  1.00 95.46           C  
ATOM    226  N   HIS A  30     273.859 367.763 303.969  1.00 68.34           N  
ATOM    227  CA  HIS A  30     274.391 366.439 304.183  1.00 57.53           C  
ATOM    228  C   HIS A  30     273.991 365.556 303.043  1.00 48.77           C  
ATOM    229  O   HIS A  30     272.871 365.649 302.548  1.00 51.44           O  
ATOM    230  CB  HIS A  30     273.845 365.854 305.474  1.00 61.04           C  
ATOM    231  CG  HIS A  30     274.223 366.584 306.720  1.00 65.97           C  
ATOM    232  ND1 HIS A  30     273.666 366.272 307.930  1.00 65.87           N  
ATOM    233  CD2 HIS A  30     275.110 367.578 306.962  1.00 72.68           C  
ATOM    234  CE1 HIS A  30     274.180 367.045 308.863  1.00 69.45           C  
ATOM    235  NE2 HIS A  30     275.062 367.849 308.317  1.00 75.20           N  
ATOM    236  N   VAL A  31     274.893 364.696 302.646  1.00 45.71           N  
ATOM    237  CA  VAL A  31     274.633 363.754 301.578  1.00 41.11           C  
ATOM    238  C   VAL A  31     274.840 362.337 302.042  1.00 41.18           C  
ATOM    239  O   VAL A  31     275.850 362.036 302.674  1.00 48.22           O  
ATOM    240  CB  VAL A  31     275.567 364.040 300.402  1.00 43.69           C  
ATOM    241  CG1 VAL A  31     275.359 363.018 299.273  1.00 42.00           C  
ATOM    242  CG2 VAL A  31     275.321 365.441 299.899  1.00 50.49           C  
ATOM    243  N   THR A  32     273.897 361.449 301.762  1.00 37.20           N  
ATOM    244  CA  THR A  32     274.109 360.077 302.186  1.00 34.67           C  
ATOM    245  C   THR A  32     274.310 359.166 301.011  1.00 34.99           C  
ATOM    246  O   THR A  32     273.599 359.269 300.017  1.00 38.46           O  
ATOM    247  CB  THR A  32     272.914 359.530 302.942  1.00 35.01           C  
ATOM    248  OG1 THR A  32     271.788 359.539 302.081  1.00 40.42           O  
ATOM    249  CG2 THR A  32     272.624 360.382 304.114  1.00 39.73           C  
ATOM    250  N   LEU A  33     275.215 358.220 301.148  1.00 32.44           N  
ATOM    251  CA  LEU A  33     275.444 357.235 300.111  1.00 30.64           C  
ATOM    252  C   LEU A  33     274.971 355.885 300.571  1.00 33.05           C  
ATOM    253  O   LEU A  33     275.490 355.345 301.553  1.00 35.18           O  
ATOM    254  CB  LEU A  33     276.928 357.105 299.811  1.00 30.52           C  
ATOM    255  CG  LEU A  33     277.676 358.366 299.534  1.00 33.78           C  
ATOM    256  CD1 LEU A  33     279.127 358.023 299.284  1.00 38.27           C  
ATOM    257  CD2 LEU A  33     277.090 359.091 298.376  1.00 36.54           C  
ATOM    258  N   MET A  34     274.004 355.315 299.880  1.00 32.62           N  
ATOM    259  CA  MET A  34     273.512 354.016 300.293  1.00 29.86           C  
ATOM    260  C   MET A  34     274.096 352.930 299.420  1.00 32.50           C  
ATOM    261  O   MET A  34     274.001 352.987 298.203  1.00 37.53           O  
ATOM    262  CB  MET A  34     272.011 354.062 300.249  1.00 33.34           C  
ATOM    263  CG  MET A  34     271.472 355.022 301.257  1.00 34.71           C  
ATOM    264  SD  MET A  34     269.747 355.196 301.186  1.00 44.59           S  
ATOM    265  CE  MET A  34     269.492 356.325 302.546  1.00 42.96           C  
ATOM    266  N   ASP A  35     274.687 351.920 300.035  1.00 29.95           N  
ATOM    267  CA  ASP A  35     275.332 350.867 299.262  1.00 28.25           C  
ATOM    268  C   ASP A  35     275.331 349.550 300.033  1.00 31.05           C  
ATOM    269  O   ASP A  35     274.775 349.501 301.135  1.00 33.27           O  
ATOM    270  CB  ASP A  35     276.753 351.348 298.913  1.00 31.95           C  
ATOM    271  CG  ASP A  35     277.348 350.740 297.659  1.00 36.51           C  
ATOM    272  OD1 ASP A  35     276.862 349.694 297.256  1.00 37.03           O  
ATOM    273  OD2 ASP A  35     278.335 351.247 297.116  1.00 37.82           O  
ATOM    274  N   GLU A  36     275.885 348.481 299.442  1.00 31.22           N  
ATOM    275  CA  GLU A  36     275.937 347.173 300.122  1.00 30.19           C  
ATOM    276  C   GLU A  36     277.251 346.426 299.989  1.00 31.96           C  
ATOM    277  O   GLU A  36     277.828 346.321 298.907  1.00 36.02           O  
ATOM    278  CB  GLU A  36     274.882 346.225 299.579  1.00 31.42           C  
ATOM    279  CG  GLU A  36     273.513 346.665 299.743  1.00 35.36           C  
ATOM    280  CD  GLU A  36     272.524 345.671 299.265  1.00 39.23           C  
ATOM    281  OE1 GLU A  36     272.555 345.307 298.118  1.00 38.82           O  
ATOM    282  OE2 GLU A  36     271.720 345.267 300.069  1.00 39.87           O  
ATOM    283  N   ALA A  37     277.668 345.776 301.060  1.00 29.92           N  
ATOM    284  CA  ALA A  37     278.876 344.972 300.979  1.00 29.02           C  
ATOM    285  C   ALA A  37     278.589 343.489 301.081  1.00 30.24           C  
ATOM    286  O   ALA A  37     277.760 343.051 301.876  1.00 34.12           O  
ATOM    287  CB  ALA A  37     279.838 345.371 302.080  1.00 30.98           C  
ATOM    288  N   ASP A  38     279.333 342.702 300.320  1.00 29.57           N  
ATOM    289  CA  ASP A  38     279.276 341.242 300.404  1.00 29.29           C  
ATOM    290  C   ASP A  38     280.165 340.834 301.537  1.00 31.72           C  
ATOM    291  O   ASP A  38     281.358 341.119 301.520  1.00 35.95           O  
ATOM    292  CB  ASP A  38     279.694 340.557 299.107  1.00 30.18           C  
ATOM    293  CG  ASP A  38     279.582 338.993 299.164  1.00 31.23           C  
ATOM    294  OD1 ASP A  38     279.595 338.413 300.261  1.00 30.77           O  
ATOM    295  OD2 ASP A  38     279.502 338.393 298.108  1.00 33.44           O  
ATOM    296  N   VAL A  39     279.585 340.269 302.569  1.00 28.06           N  
ATOM    297  CA  VAL A  39     280.335 339.975 303.763  1.00 26.83           C  
ATOM    298  C   VAL A  39     280.481 338.492 304.011  1.00 29.61           C  
ATOM    299  O   VAL A  39     280.774 338.073 305.129  1.00 33.41           O  
ATOM    300  CB  VAL A  39     279.709 340.700 304.965  1.00 26.93           C  
ATOM    301  CG1 VAL A  39     279.835 342.192 304.773  1.00 30.04           C  
ATOM    302  CG2 VAL A  39     278.277 340.335 305.116  1.00 32.41           C  
ATOM    303  N   THR A  40     280.370 337.680 302.972  1.00 28.83           N  
ATOM    304  CA  THR A  40     280.478 336.237 303.168  1.00 27.00           C  
ATOM    305  C   THR A  40     281.723 335.824 303.941  1.00 31.60           C  
ATOM    306  O   THR A  40     281.642 334.977 304.840  1.00 35.80           O  
ATOM    307  CB  THR A  40     280.509 335.496 301.827  1.00 27.89           C  
ATOM    308  OG1 THR A  40     279.322 335.772 301.097  1.00 32.86           O  
ATOM    309  CG2 THR A  40     280.571 334.009 302.082  1.00 29.30           C  
ATOM    310  N   LYS A  41     282.878 336.384 303.594  1.00 30.75           N  
ATOM    311  CA  LYS A  41     284.105 336.009 304.277  1.00 30.23           C  
ATOM    312  C   LYS A  41     284.161 336.557 305.681  1.00 31.23           C  
ATOM    313  O   LYS A  41     284.821 335.983 306.545  1.00 34.82           O  
ATOM    314  CB  LYS A  41     285.325 336.458 303.515  1.00 32.37           C  
ATOM    315  CG  LYS A  41     285.568 335.711 302.235  1.00 33.44           C  
ATOM    316  CD  LYS A  41     286.821 336.225 301.540  1.00 39.22           C  
ATOM    317  CE  LYS A  41     287.116 335.458 300.268  1.00 41.93           C  
ATOM    318  NZ  LYS A  41     288.332 335.982 299.561  1.00 42.80           N  
ATOM    319  N   LEU A  42     283.529 337.692 305.908  1.00 30.55           N  
ATOM    320  CA  LEU A  42     283.541 338.307 307.210  1.00 28.67           C  
ATOM    321  C   LEU A  42     282.752 337.471 308.155  1.00 32.15           C  
ATOM    322  O   LEU A  42     283.128 337.294 309.315  1.00 36.68           O  
ATOM    323  CB  LEU A  42     282.941 339.686 307.131  1.00 30.16           C  
ATOM    324  CG  LEU A  42     282.900 340.504 308.372  1.00 29.21           C  
ATOM    325  CD1 LEU A  42     284.251 340.742 308.911  1.00 31.54           C  
ATOM    326  CD2 LEU A  42     282.224 341.824 308.063  1.00 34.27           C  
ATOM    327  N   VAL A  43     281.636 336.963 307.681  1.00 32.32           N  
ATOM    328  CA  VAL A  43     280.820 336.159 308.538  1.00 31.79           C  
ATOM    329  C   VAL A  43     281.560 334.898 308.873  1.00 33.28           C  
ATOM    330  O   VAL A  43     281.614 334.506 310.039  1.00 37.23           O  
ATOM    331  CB  VAL A  43     279.482 335.840 307.887  1.00 30.61           C  
ATOM    332  CG1 VAL A  43     278.727 334.851 308.741  1.00 32.14           C  
ATOM    333  CG2 VAL A  43     278.673 337.139 307.715  1.00 33.63           C  
ATOM    334  N   ALA A  44     282.154 334.263 307.873  1.00 33.08           N  
ATOM    335  CA  ALA A  44     282.884 333.045 308.138  1.00 34.81           C  
ATOM    336  C   ALA A  44     284.057 333.267 309.081  1.00 35.26           C  
ATOM    337  O   ALA A  44     284.314 332.444 309.964  1.00 38.46           O  
ATOM    338  CB  ALA A  44     283.386 332.475 306.838  1.00 34.35           C  
ATOM    339  N   HIS A  45     284.751 334.386 308.942  1.00 33.83           N  
ATOM    340  CA  HIS A  45     285.885 334.654 309.792  1.00 32.43           C  
ATOM    341  C   HIS A  45     285.461 334.880 311.225  1.00 33.95           C  
ATOM    342  O   HIS A  45     286.062 334.323 312.150  1.00 38.84           O  
ATOM    343  CB  HIS A  45     286.655 335.844 309.266  1.00 33.91           C  
ATOM    344  CG  HIS A  45     287.873 336.116 309.993  1.00 33.91           C  
ATOM    345  ND1 HIS A  45     287.937 336.991 311.047  1.00 37.13           N  
ATOM    346  CD2 HIS A  45     289.105 335.619 309.839  1.00 34.89           C  
ATOM    347  CE1 HIS A  45     289.165 337.020 311.500  1.00 39.82           C  
ATOM    348  NE2 HIS A  45     289.891 336.193 310.786  1.00 39.91           N  
ATOM    349  N   ARG A  46     284.427 335.687 311.437  1.00 34.24           N  
ATOM    350  CA  ARG A  46     284.021 335.930 312.799  1.00 34.03           C  
ATOM    351  C   ARG A  46     283.595 334.628 313.421  1.00 36.56           C  
ATOM    352  O   ARG A  46     283.893 334.371 314.584  1.00 40.14           O  
ATOM    353  CB  ARG A  46     282.882 336.908 312.903  1.00 35.46           C  
ATOM    354  CG  ARG A  46     282.558 337.322 314.347  1.00 40.03           C  
ATOM    355  CD  ARG A  46     281.381 338.171 314.409  1.00 41.60           C  
ATOM    356  NE  ARG A  46     280.189 337.430 314.070  1.00 40.47           N  
ATOM    357  CZ  ARG A  46     279.444 336.714 314.927  1.00 42.14           C  
ATOM    358  NH1 ARG A  46     279.733 336.685 316.205  1.00 42.97           N  
ATOM    359  NH2 ARG A  46     278.396 336.041 314.478  1.00 39.65           N  
ATOM    360  N   LYS A  47     282.879 333.795 312.666  1.00 37.72           N  
ATOM    361  CA  LYS A  47     282.432 332.533 313.208  1.00 39.12           C  
ATOM    362  C   LYS A  47     283.599 331.689 313.658  1.00 39.29           C  
ATOM    363  O   LYS A  47     283.603 331.169 314.773  1.00 41.44           O  
ATOM    364  CB  LYS A  47     281.636 331.758 312.174  1.00 40.22           C  
ATOM    365  CG  LYS A  47     281.112 330.434 312.659  1.00 40.65           C  
ATOM    366  CD  LYS A  47     280.294 329.758 311.589  1.00 47.33           C  
ATOM    367  CE  LYS A  47     279.803 328.403 312.051  1.00 60.14           C  
ATOM    368  NZ  LYS A  47     279.005 327.715 311.004  1.00 63.52           N  
ATOM    369  N   LYS A  48     284.633 331.611 312.835  1.00 38.40           N  
ATOM    370  CA  LYS A  48     285.787 330.799 313.152  1.00 38.41           C  
ATOM    371  C   LYS A  48     286.396 331.134 314.495  1.00 38.16           C  
ATOM    372  O   LYS A  48     286.830 330.240 315.218  1.00 40.89           O  
ATOM    373  CB  LYS A  48     286.846 330.938 312.077  1.00 38.69           C  
ATOM    374  CG  LYS A  48     288.044 330.075 312.303  1.00 39.10           C  
ATOM    375  CD  LYS A  48     289.004 330.164 311.159  1.00 42.92           C  
ATOM    376  CE  LYS A  48     290.191 329.270 311.401  1.00 51.41           C  
ATOM    377  NZ  LYS A  48     291.157 329.309 310.282  1.00 53.52           N  
ATOM    378  N   PHE A  49     286.428 332.404 314.843  1.00 36.16           N  
ATOM    379  CA  PHE A  49     287.026 332.821 316.094  1.00 35.64           C  
ATOM    380  C   PHE A  49     286.053 333.086 317.211  1.00 39.23           C  
ATOM    381  O   PHE A  49     286.442 333.605 318.264  1.00 42.29           O  
ATOM    382  CB  PHE A  49     287.876 334.036 315.860  1.00 36.58           C  
ATOM    383  CG  PHE A  49     289.051 333.684 315.146  1.00 37.08           C  
ATOM    384  CD1 PHE A  49     289.105 333.708 313.786  1.00 39.66           C  
ATOM    385  CD2 PHE A  49     290.149 333.313 315.846  1.00 40.98           C  
ATOM    386  CE1 PHE A  49     290.253 333.344 313.148  1.00 41.89           C  
ATOM    387  CE2 PHE A  49     291.290 332.955 315.223  1.00 42.04           C  
ATOM    388  CZ  PHE A  49     291.343 332.964 313.876  1.00 42.24           C  
ATOM    389  N   LYS A  50     284.796 332.737 317.018  1.00 40.03           N  
ATOM    390  CA  LYS A  50     283.812 332.986 318.042  1.00 41.46           C  
ATOM    391  C   LYS A  50     284.114 332.221 319.311  1.00 42.96           C  
ATOM    392  O   LYS A  50     284.010 332.769 320.408  1.00 44.89           O  
ATOM    393  CB  LYS A  50     282.434 332.609 317.537  1.00 42.30           C  
ATOM    394  CG  LYS A  50     281.305 332.866 318.505  1.00 46.40           C  
ATOM    395  CD  LYS A  50     279.975 332.467 317.883  1.00 50.13           C  
ATOM    396  CE  LYS A  50     278.829 332.649 318.862  1.00 60.51           C  
ATOM    397  NZ  LYS A  50     277.527 332.192 318.292  1.00 61.11           N  
ATOM    398  N   ALA A  51     284.471 330.944 319.183  1.00 40.24           N  
ATOM    399  CA  ALA A  51     284.734 330.131 320.359  1.00 41.67           C  
ATOM    400  C   ALA A  51     285.933 330.627 321.134  1.00 43.55           C  
ATOM    401  O   ALA A  51     285.933 330.622 322.363  1.00 45.71           O  
ATOM    402  CB  ALA A  51     284.963 328.700 319.952  1.00 44.60           C  
ATOM    403  N   ILE A  52     286.939 331.081 320.417  1.00 40.72           N  
ATOM    404  CA  ILE A  52     288.147 331.559 321.044  1.00 40.30           C  
ATOM    405  C   ILE A  52     287.847 332.790 321.832  1.00 42.20           C  
ATOM    406  O   ILE A  52     288.319 332.963 322.958  1.00 45.47           O  
ATOM    407  CB  ILE A  52     289.215 331.820 319.992  1.00 39.65           C  
ATOM    408  CG1 ILE A  52     289.633 330.463 319.416  1.00 41.35           C  
ATOM    409  CG2 ILE A  52     290.383 332.610 320.582  1.00 41.97           C  
ATOM    410  CD1 ILE A  52     290.451 330.522 318.167  1.00 41.50           C  
ATOM    411  N   ALA A  53     287.094 333.685 321.233  1.00 42.15           N  
ATOM    412  CA  ALA A  53     286.769 334.869 321.955  1.00 42.06           C  
ATOM    413  C   ALA A  53     285.997 334.523 323.205  1.00 42.95           C  
ATOM    414  O   ALA A  53     286.289 335.037 324.284  1.00 48.56           O  
ATOM    415  CB  ALA A  53     285.945 335.756 321.083  1.00 43.55           C  
ATOM    416  N   ALA A  54     285.079 333.561 323.111  1.00 43.11           N  
ATOM    417  CA  ALA A  54     284.291 333.212 324.272  1.00 45.10           C  
ATOM    418  C   ALA A  54     285.157 332.707 325.409  1.00 45.94           C  
ATOM    419  O   ALA A  54     284.987 333.116 326.558  1.00 45.82           O  
ATOM    420  CB  ALA A  54     283.280 332.158 323.900  1.00 48.50           C  
ATOM    421  N   GLU A  55     286.180 331.924 325.086  1.00 46.57           N  
ATOM    422  CA  GLU A  55     287.078 331.389 326.104  1.00 47.81           C  
ATOM    423  C   GLU A  55     287.800 332.497 326.844  1.00 46.34           C  
ATOM    424  O   GLU A  55     288.063 332.393 328.041  1.00 46.14           O  
ATOM    425  CB  GLU A  55     288.107 330.449 325.492  1.00 48.03           C  
ATOM    426  CG  GLU A  55     287.554 329.137 325.003  1.00 49.49           C  
ATOM    427  CD  GLU A  55     288.602 328.294 324.354  1.00 58.14           C  
ATOM    428  OE1 GLU A  55     289.706 328.767 324.219  1.00 54.11           O  
ATOM    429  OE2 GLU A  55     288.307 327.184 323.984  1.00 62.33           O  
ATOM    430  N   LYS A  56     288.090 333.578 326.143  1.00 45.20           N  
ATOM    431  CA  LYS A  56     288.792 334.711 326.713  1.00 46.14           C  
ATOM    432  C   LYS A  56     287.846 335.703 327.391  1.00 46.48           C  
ATOM    433  O   LYS A  56     288.293 336.726 327.911  1.00 46.26           O  
ATOM    434  CB  LYS A  56     289.558 335.440 325.616  1.00 49.28           C  
ATOM    435  CG  LYS A  56     290.686 334.652 324.976  1.00 49.40           C  
ATOM    436  CD  LYS A  56     291.340 335.476 323.857  1.00 51.67           C  
ATOM    437  CE  LYS A  56     292.450 334.713 323.132  1.00 57.57           C  
ATOM    438  NZ  LYS A  56     293.657 334.494 323.989  1.00 64.85           N  
ATOM    439  N   GLY A  57     286.537 335.437 327.357  1.00 46.60           N  
ATOM    440  CA  GLY A  57     285.553 336.344 327.925  1.00 47.17           C  
ATOM    441  C   GLY A  57     285.198 337.493 326.985  1.00 48.34           C  
ATOM    442  O   GLY A  57     284.720 338.540 327.421  1.00 51.90           O  
ATOM    443  N   ILE A  58     285.433 337.306 325.698  1.00 46.62           N  
ATOM    444  CA  ILE A  58     285.192 338.322 324.711  1.00 43.90           C  
ATOM    445  C   ILE A  58     284.063 337.944 323.788  1.00 45.33           C  
ATOM    446  O   ILE A  58     284.058 336.871 323.210  1.00 47.09           O  
ATOM    447  CB  ILE A  58     286.462 338.520 323.878  1.00 42.74           C  
ATOM    448  CG1 ILE A  58     287.586 338.969 324.792  1.00 47.32           C  
ATOM    449  CG2 ILE A  58     286.216 339.493 322.729  1.00 45.92           C  
ATOM    450  CD1 ILE A  58     288.941 338.991 324.148  1.00 48.97           C  
ATOM    451  N   LYS A  59     283.098 338.816 323.630  1.00 45.92           N  
ATOM    452  CA  LYS A  59     282.041 338.527 322.680  1.00 43.35           C  
ATOM    453  C   LYS A  59     282.321 339.208 321.352  1.00 44.70           C  
ATOM    454  O   LYS A  59     282.421 340.438 321.307  1.00 45.99           O  
ATOM    455  CB  LYS A  59     280.697 338.991 323.212  1.00 46.16           C  
ATOM    456  CG  LYS A  59     279.538 338.691 322.296  1.00 48.77           C  
ATOM    457  CD  LYS A  59     278.234 339.155 322.898  1.00 53.96           C  
ATOM    458  CE  LYS A  59     277.077 338.884 321.960  1.00 59.62           C  
ATOM    459  NZ  LYS A  59     275.779 339.329 322.540  1.00 63.34           N  
ATOM    460  N   LEU A  60     282.439 338.436 320.268  1.00 43.48           N  
ATOM    461  CA  LEU A  60     282.684 339.077 318.985  1.00 42.93           C  
ATOM    462  C   LEU A  60     281.383 339.431 318.332  1.00 43.39           C  
ATOM    463  O   LEU A  60     280.420 338.661 318.346  1.00 45.14           O  
ATOM    464  CB  LEU A  60     283.444 338.197 317.984  1.00 40.18           C  
ATOM    465  CG  LEU A  60     284.832 337.743 318.336  1.00 41.15           C  
ATOM    466  CD1 LEU A  60     285.345 336.794 317.238  1.00 41.39           C  
ATOM    467  CD2 LEU A  60     285.782 338.929 318.479  1.00 42.52           C  
ATOM    468  N   THR A  61     281.394 340.577 317.712  1.00 40.38           N  
ATOM    469  CA  THR A  61     280.319 341.120 316.930  1.00 39.49           C  
ATOM    470  C   THR A  61     281.030 341.560 315.689  1.00 39.26           C  
ATOM    471  O   THR A  61     282.238 341.370 315.600  1.00 40.42           O  
ATOM    472  CB  THR A  61     279.606 342.282 317.634  1.00 43.00           C  
ATOM    473  OG1 THR A  61     280.471 343.418 317.698  1.00 43.48           O  
ATOM    474  CG2 THR A  61     279.254 341.858 319.062  1.00 49.53           C  
ATOM    475  N   PHE A  62     280.343 342.105 314.713  1.00 37.30           N  
ATOM    476  CA  PHE A  62     281.070 342.523 313.529  1.00 34.23           C  
ATOM    477  C   PHE A  62     281.689 343.888 313.677  1.00 35.86           C  
ATOM    478  O   PHE A  62     282.601 344.256 312.930  1.00 37.77           O  
ATOM    479  CB  PHE A  62     280.165 342.517 312.332  1.00 32.60           C  
ATOM    480  CG  PHE A  62     279.817 341.183 311.960  1.00 33.87           C  
ATOM    481  CD1 PHE A  62     278.602 340.658 312.260  1.00 36.57           C  
ATOM    482  CD2 PHE A  62     280.718 340.425 311.314  1.00 36.46           C  
ATOM    483  CE1 PHE A  62     278.298 339.382 311.898  1.00 37.47           C  
ATOM    484  CE2 PHE A  62     280.431 339.157 310.949  1.00 36.90           C  
ATOM    485  CZ  PHE A  62     279.214 338.632 311.238  1.00 37.51           C  
ATOM    486  N   LEU A  63     281.229 344.635 314.656  1.00 35.40           N  
ATOM    487  CA  LEU A  63     281.688 345.986 314.807  1.00 35.08           C  
ATOM    488  C   LEU A  63     283.212 346.147 314.851  1.00 37.28           C  
ATOM    489  O   LEU A  63     283.705 347.064 314.211  1.00 39.27           O  
ATOM    490  CB  LEU A  63     280.984 346.650 315.982  1.00 33.33           C  
ATOM    491  CG  LEU A  63     281.340 348.102 316.271  1.00 38.71           C  
ATOM    492  CD1 LEU A  63     281.039 349.003 315.086  1.00 40.71           C  
ATOM    493  CD2 LEU A  63     280.512 348.548 317.411  1.00 44.90           C  
ATOM    494  N   PRO A  64     284.025 345.329 315.543  1.00 34.53           N  
ATOM    495  CA  PRO A  64     285.457 345.478 315.573  1.00 32.01           C  
ATOM    496  C   PRO A  64     286.078 345.462 314.186  1.00 35.77           C  
ATOM    497  O   PRO A  64     287.139 346.044 313.982  1.00 39.04           O  
ATOM    498  CB  PRO A  64     285.897 344.248 316.342  1.00 34.29           C  
ATOM    499  CG  PRO A  64     284.734 343.893 317.171  1.00 37.28           C  
ATOM    500  CD  PRO A  64     283.551 344.225 316.333  1.00 36.57           C  
ATOM    501  N   TYR A  65     285.428 344.818 313.219  1.00 33.61           N  
ATOM    502  CA  TYR A  65     285.991 344.749 311.895  1.00 32.26           C  
ATOM    503  C   TYR A  65     285.647 346.016 311.188  1.00 34.87           C  
ATOM    504  O   TYR A  65     286.421 346.524 310.380  1.00 38.40           O  
ATOM    505  CB  TYR A  65     285.410 343.588 311.148  1.00 32.25           C  
ATOM    506  CG  TYR A  65     285.765 342.270 311.699  1.00 34.32           C  
ATOM    507  CD1 TYR A  65     284.962 341.709 312.656  1.00 36.81           C  
ATOM    508  CD2 TYR A  65     286.830 341.583 311.216  1.00 35.73           C  
ATOM    509  CE1 TYR A  65     285.219 340.465 313.132  1.00 36.17           C  
ATOM    510  CE2 TYR A  65     287.089 340.328 311.686  1.00 36.64           C  
ATOM    511  CZ  TYR A  65     286.284 339.769 312.641  1.00 35.51           C  
ATOM    512  OH  TYR A  65     286.519 338.498 313.083  1.00 39.43           O  
ATOM    513  N   VAL A  66     284.487 346.549 311.516  1.00 33.83           N  
ATOM    514  CA  VAL A  66     284.045 347.778 310.920  1.00 33.23           C  
ATOM    515  C   VAL A  66     284.957 348.872 311.413  1.00 36.00           C  
ATOM    516  O   VAL A  66     285.324 349.759 310.644  1.00 37.67           O  
ATOM    517  CB  VAL A  66     282.588 348.073 311.221  1.00 33.36           C  
ATOM    518  CG1 VAL A  66     282.235 349.436 310.705  1.00 36.06           C  
ATOM    519  CG2 VAL A  66     281.708 347.006 310.573  1.00 34.43           C  
ATOM    520  N   VAL A  67     285.311 348.822 312.691  1.00 35.46           N  
ATOM    521  CA  VAL A  67     286.189 349.822 313.240  1.00 33.56           C  
ATOM    522  C   VAL A  67     287.526 349.755 312.535  1.00 35.32           C  
ATOM    523  O   VAL A  67     288.060 350.797 312.159  1.00 38.47           O  
ATOM    524  CB  VAL A  67     286.395 349.612 314.746  1.00 34.59           C  
ATOM    525  CG1 VAL A  67     287.479 350.540 315.271  1.00 39.78           C  
ATOM    526  CG2 VAL A  67     285.112 349.888 315.481  1.00 38.20           C  
ATOM    527  N   LYS A  68     288.078 348.564 312.322  1.00 35.74           N  
ATOM    528  CA  LYS A  68     289.349 348.522 311.629  1.00 36.00           C  
ATOM    529  C   LYS A  68     289.220 349.017 310.194  1.00 38.05           C  
ATOM    530  O   LYS A  68     290.112 349.714 309.700  1.00 42.03           O  
ATOM    531  CB  LYS A  68     289.910 347.104 311.619  1.00 36.45           C  
ATOM    532  CG  LYS A  68     290.308 346.546 312.971  1.00 36.85           C  
ATOM    533  CD  LYS A  68     291.579 347.121 313.565  1.00 38.61           C  
ATOM    534  CE  LYS A  68     292.816 346.498 312.986  1.00 40.15           C  
ATOM    535  NZ  LYS A  68     294.016 346.980 313.701  1.00 46.07           N  
ATOM    536  N   ALA A  69     288.128 348.664 309.504  1.00 36.11           N  
ATOM    537  CA  ALA A  69     287.966 349.101 308.130  1.00 33.45           C  
ATOM    538  C   ALA A  69     287.866 350.606 308.065  1.00 36.09           C  
ATOM    539  O   ALA A  69     288.429 351.230 307.162  1.00 39.46           O  
ATOM    540  CB  ALA A  69     286.749 348.463 307.504  1.00 34.62           C  
ATOM    541  N   LEU A  70     287.200 351.208 309.045  1.00 35.84           N  
ATOM    542  CA  LEU A  70     287.091 352.642 309.053  1.00 35.71           C  
ATOM    543  C   LEU A  70     288.435 353.276 309.293  1.00 39.91           C  
ATOM    544  O   LEU A  70     288.786 354.219 308.593  1.00 41.92           O  
ATOM    545  CB  LEU A  70     286.085 353.123 310.087  1.00 33.38           C  
ATOM    546  CG  LEU A  70     285.896 354.656 310.187  1.00 36.83           C  
ATOM    547  CD1 LEU A  70     285.467 355.244 308.860  1.00 36.63           C  
ATOM    548  CD2 LEU A  70     284.847 354.948 311.220  1.00 40.23           C  
ATOM    549  N   VAL A  71     289.244 352.729 310.200  1.00 40.20           N  
ATOM    550  CA  VAL A  71     290.536 353.347 310.419  1.00 36.94           C  
ATOM    551  C   VAL A  71     291.304 353.331 309.131  1.00 39.78           C  
ATOM    552  O   VAL A  71     291.967 354.316 308.794  1.00 45.36           O  
ATOM    553  CB  VAL A  71     291.383 352.614 311.469  1.00 37.00           C  
ATOM    554  CG1 VAL A  71     292.803 353.186 311.486  1.00 46.69           C  
ATOM    555  CG2 VAL A  71     290.791 352.778 312.810  1.00 42.23           C  
ATOM    556  N   SER A  72     291.254 352.224 308.413  1.00 38.50           N  
ATOM    557  CA  SER A  72     291.996 352.168 307.186  1.00 39.11           C  
ATOM    558  C   SER A  72     291.519 353.239 306.221  1.00 41.49           C  
ATOM    559  O   SER A  72     292.352 353.925 305.619  1.00 46.45           O  
ATOM    560  CB  SER A  72     291.888 350.804 306.576  1.00 39.68           C  
ATOM    561  OG  SER A  72     292.648 350.725 305.405  1.00 42.85           O  
ATOM    562  N   ALA A  73     290.202 353.417 306.080  1.00 40.92           N  
ATOM    563  CA  ALA A  73     289.690 354.447 305.181  1.00 41.41           C  
ATOM    564  C   ALA A  73     290.098 355.828 305.613  1.00 41.27           C  
ATOM    565  O   ALA A  73     290.406 356.673 304.775  1.00 43.72           O  
ATOM    566  CB  ALA A  73     288.188 354.405 305.118  1.00 41.89           C  
ATOM    567  N   LEU A  74     290.129 356.063 306.914  1.00 41.43           N  
ATOM    568  CA  LEU A  74     290.485 357.364 307.426  1.00 44.15           C  
ATOM    569  C   LEU A  74     291.917 357.673 307.075  1.00 45.68           C  
ATOM    570  O   LEU A  74     292.269 358.827 306.851  1.00 48.66           O  
ATOM    571  CB  LEU A  74     290.309 357.410 308.944  1.00 44.26           C  
ATOM    572  CG  LEU A  74     288.865 357.322 309.514  1.00 45.35           C  
ATOM    573  CD1 LEU A  74     288.933 357.208 311.026  1.00 46.62           C  
ATOM    574  CD2 LEU A  74     288.070 358.505 309.118  1.00 47.74           C  
ATOM    575  N   ARG A  75     292.762 356.656 307.064  1.00 44.35           N  
ATOM    576  CA  ARG A  75     294.147 356.856 306.717  1.00 45.21           C  
ATOM    577  C   ARG A  75     294.332 357.108 305.223  1.00 46.51           C  
ATOM    578  O   ARG A  75     295.094 357.991 304.831  1.00 48.91           O  
ATOM    579  CB  ARG A  75     294.969 355.653 307.118  1.00 47.93           C  
ATOM    580  CG  ARG A  75     296.452 355.818 306.893  1.00 54.58           C  
ATOM    581  CD  ARG A  75     297.241 354.634 307.301  1.00 56.51           C  
ATOM    582  NE  ARG A  75     297.196 354.355 308.746  1.00 52.44           N  
ATOM    583  CZ  ARG A  75     296.544 353.330 309.341  1.00 51.47           C  
ATOM    584  NH1 ARG A  75     295.824 352.487 308.636  1.00 50.30           N  
ATOM    585  NH2 ARG A  75     296.649 353.169 310.647  1.00 55.19           N  
ATOM    586  N   GLU A  76     293.660 356.322 304.380  1.00 44.58           N  
ATOM    587  CA  GLU A  76     293.786 356.487 302.932  1.00 45.05           C  
ATOM    588  C   GLU A  76     293.179 357.793 302.416  1.00 46.47           C  
ATOM    589  O   GLU A  76     293.698 358.391 301.469  1.00 47.83           O  
ATOM    590  CB  GLU A  76     293.198 355.309 302.165  1.00 46.46           C  
ATOM    591  CG  GLU A  76     293.408 355.433 300.632  1.00 49.87           C  
ATOM    592  CD  GLU A  76     292.968 354.239 299.847  1.00 53.75           C  
ATOM    593  OE1 GLU A  76     292.795 353.214 300.429  1.00 50.41           O  
ATOM    594  OE2 GLU A  76     292.789 354.354 298.664  1.00 54.20           O  
ATOM    595  N   TYR A  77     292.078 358.222 303.017  1.00 45.88           N  
ATOM    596  CA  TYR A  77     291.365 359.419 302.622  1.00 44.41           C  
ATOM    597  C   TYR A  77     291.299 360.372 303.807  1.00 48.12           C  
ATOM    598  O   TYR A  77     290.211 360.575 304.349  1.00 49.84           O  
ATOM    599  CB  TYR A  77     289.964 359.062 302.171  1.00 41.76           C  
ATOM    600  CG  TYR A  77     289.983 358.169 301.032  1.00 42.02           C  
ATOM    601  CD1 TYR A  77     289.886 356.827 301.220  1.00 45.42           C  
ATOM    602  CD2 TYR A  77     290.117 358.684 299.785  1.00 41.72           C  
ATOM    603  CE1 TYR A  77     289.935 355.997 300.148  1.00 44.95           C  
ATOM    604  CE2 TYR A  77     290.163 357.856 298.716  1.00 42.81           C  
ATOM    605  CZ  TYR A  77     290.080 356.521 298.894  1.00 43.80           C  
ATOM    606  OH  TYR A  77     290.152 355.696 297.815  1.00 44.89           O  
ATOM    607  N   PRO A  78     292.400 361.081 304.125  1.00 46.85           N  
ATOM    608  CA  PRO A  78     292.654 361.859 305.322  1.00 49.11           C  
ATOM    609  C   PRO A  78     291.708 363.012 305.538  1.00 54.13           C  
ATOM    610  O   PRO A  78     291.647 363.563 306.632  1.00 58.06           O  
ATOM    611  CB  PRO A  78     294.073 362.355 305.100  1.00 53.00           C  
ATOM    612  CG  PRO A  78     294.270 362.334 303.642  1.00 52.33           C  
ATOM    613  CD  PRO A  78     293.511 361.155 303.171  1.00 47.63           C  
ATOM    614  N   VAL A  79     290.966 363.388 304.515  1.00 49.61           N  
ATOM    615  CA  VAL A  79     289.997 364.451 304.645  1.00 52.99           C  
ATOM    616  C   VAL A  79     288.949 364.054 305.677  1.00 55.39           C  
ATOM    617  O   VAL A  79     288.329 364.888 306.331  1.00 59.17           O  
ATOM    618  CB  VAL A  79     289.323 364.732 303.301  1.00 51.92           C  
ATOM    619  CG1 VAL A  79     288.382 363.577 302.907  1.00 55.14           C  
ATOM    620  CG2 VAL A  79     288.540 366.046 303.393  1.00 66.96           C  
ATOM    621  N   LEU A  80     288.755 362.763 305.855  1.00 54.24           N  
ATOM    622  CA  LEU A  80     287.768 362.265 306.774  1.00 49.82           C  
ATOM    623  C   LEU A  80     288.149 362.483 308.217  1.00 53.05           C  
ATOM    624  O   LEU A  80     287.313 362.335 309.100  1.00 53.88           O  
ATOM    625  CB  LEU A  80     287.600 360.791 306.544  1.00 51.40           C  
ATOM    626  CG  LEU A  80     287.018 360.355 305.233  1.00 51.79           C  
ATOM    627  CD1 LEU A  80     287.206 358.861 305.112  1.00 52.50           C  
ATOM    628  CD2 LEU A  80     285.545 360.684 305.188  1.00 45.58           C  
ATOM    629  N   ASN A  81     289.408 362.811 308.478  1.00 55.36           N  
ATOM    630  CA  ASN A  81     289.858 363.048 309.829  1.00 57.04           C  
ATOM    631  C   ASN A  81     289.794 364.513 310.153  1.00 62.58           C  
ATOM    632  O   ASN A  81     290.275 364.943 311.212  1.00 67.97           O  
ATOM    633  CB  ASN A  81     291.274 362.576 310.026  1.00 56.90           C  
ATOM    634  CG  ASN A  81     291.432 361.145 310.099  1.00 57.22           C  
ATOM    635  OD1 ASN A  81     290.635 360.426 310.712  1.00 56.04           O  
ATOM    636  ND2 ASN A  81     292.475 360.678 309.494  1.00 55.40           N  
ATOM    637  N   THR A  82     289.236 365.299 309.248  1.00 61.73           N  
ATOM    638  CA  THR A  82     289.172 366.701 309.514  1.00 65.77           C  
ATOM    639  C   THR A  82     287.924 367.080 310.254  1.00 66.27           C  
ATOM    640  O   THR A  82     286.937 366.349 310.296  1.00 67.37           O  
ATOM    641  CB  THR A  82     289.263 367.550 308.233  1.00 70.28           C  
ATOM    642  OG1 THR A  82     288.133 367.301 307.386  1.00 66.24           O  
ATOM    643  CG2 THR A  82     290.534 367.272 307.482  1.00 68.14           C  
ATOM    644  N   SER A  83     287.963 368.277 310.777  1.00 70.84           N  
ATOM    645  CA  SER A  83     286.841 368.900 311.430  1.00 71.18           C  
ATOM    646  C   SER A  83     286.833 370.355 311.092  1.00 80.82           C  
ATOM    647  O   SER A  83     287.840 370.929 310.661  1.00 85.98           O  
ATOM    648  CB  SER A  83     286.901 368.740 312.922  1.00 72.92           C  
ATOM    649  OG  SER A  83     288.034 369.326 313.452  1.00 77.99           O  
ATOM    650  N   ILE A  84     285.674 370.952 311.222  1.00 85.64           N  
ATOM    651  CA  ILE A  84     285.557 372.356 310.931  1.00 92.22           C  
ATOM    652  C   ILE A  84     284.831 373.147 311.986  1.00 99.85           C  
ATOM    653  O   ILE A  84     283.736 372.771 312.401  1.00 97.03           O  
ATOM    654  CB  ILE A  84     284.886 372.494 309.558  1.00 97.22           C  
ATOM    655  CG1 ILE A  84     284.739 373.945 309.162  1.00102.74           C  
ATOM    656  CG2 ILE A  84     283.546 371.724 309.519  1.00 93.67           C  
ATOM    657  CD1 ILE A  84     284.402 374.158 307.697  1.00105.86           C  
ATOM    658  N   ASP A  85     285.419 374.262 312.402  1.00104.28           N  
ATOM    659  CA  ASP A  85     284.701 375.155 313.307  1.00113.58           C  
ATOM    660  C   ASP A  85     284.186 376.292 312.428  1.00116.00           C  
ATOM    661  O   ASP A  85     284.470 376.310 311.235  1.00113.47           O  
ATOM    662  CB  ASP A  85     285.562 375.612 314.490  1.00116.01           C  
ATOM    663  CG  ASP A  85     284.767 376.076 315.719  1.00115.76           C  
ATOM    664  OD1 ASP A  85     283.684 376.593 315.544  1.00121.50           O  
ATOM    665  OD2 ASP A  85     285.244 375.914 316.807  1.00119.06           O  
ATOM    666  N   ASP A  86     283.487 377.262 312.991  1.00119.25           N  
ATOM    667  CA  ASP A  86     282.909 378.313 312.151  1.00121.53           C  
ATOM    668  C   ASP A  86     283.792 379.502 311.773  1.00117.39           C  
ATOM    669  O   ASP A  86     283.410 380.274 310.889  1.00122.62           O  
ATOM    670  CB  ASP A  86     281.612 378.821 312.771  1.00125.64           C  
ATOM    671  CG  ASP A  86     280.466 377.790 312.677  1.00114.14           C  
ATOM    672  OD1 ASP A  86     280.478 376.987 311.760  1.00129.53           O  
ATOM    673  OD2 ASP A  86     279.590 377.825 313.511  1.00126.31           O  
ATOM    674  N   GLU A  87     284.949 379.669 312.392  1.00116.78           N  
ATOM    675  CA  GLU A  87     285.798 380.795 312.025  1.00122.06           C  
ATOM    676  C   GLU A  87     286.615 380.377 310.804  1.00113.26           C  
ATOM    677  O   GLU A  87     286.703 379.196 310.474  1.00115.96           O  
ATOM    678  CB  GLU A  87     286.661 381.279 313.193  1.00123.32           C  
ATOM    679  CG  GLU A  87     285.865 381.746 314.404  1.00117.22           C  
ATOM    680  CD  GLU A  87     285.035 382.963 314.142  1.00119.83           C  
ATOM    681  OE1 GLU A  87     285.406 383.756 313.308  1.00120.79           O  
ATOM    682  OE2 GLU A  87     284.021 383.105 314.782  1.00123.86           O  
ATOM    683  N   THR A  88     287.152 381.336 310.067  1.00118.03           N  
ATOM    684  CA  THR A  88     287.881 380.997 308.850  1.00120.73           C  
ATOM    685  C   THR A  88     289.115 380.131 309.091  1.00122.79           C  
ATOM    686  O   THR A  88     289.338 379.132 308.401  1.00121.36           O  
ATOM    687  CB  THR A  88     288.328 382.283 308.116  1.00124.95           C  
ATOM    688  OG1 THR A  88     287.175 383.067 307.764  1.00128.24           O  
ATOM    689  CG2 THR A  88     289.082 381.920 306.822  1.00122.88           C  
ATOM    690  N   GLU A  89     289.923 380.444 310.087  1.00119.62           N  
ATOM    691  CA  GLU A  89     291.147 379.673 310.290  1.00103.11           C  
ATOM    692  C   GLU A  89     290.912 378.477 311.206  1.00170.76           C  
ATOM    693  O   GLU A  89     291.631 378.297 312.196  1.00112.88           O  
ATOM    694  CB  GLU A  89     292.194 380.601 310.890  1.00119.59           C  
ATOM    695  CG  GLU A  89     292.481 381.837 310.025  1.00122.57           C  
ATOM    696  CD  GLU A  89     291.466 382.944 310.215  1.00122.86           C  
ATOM    697  OE1 GLU A  89     290.545 382.762 310.992  1.00121.72           O  
ATOM    698  OE2 GLU A  89     291.596 383.954 309.575  1.00125.50           O  
ATOM    699  N   GLU A  90     289.924 377.666 310.834  1.00112.33           N  
ATOM    700  CA  GLU A  90     289.474 376.529 311.609  1.00114.63           C  
ATOM    701  C   GLU A  90     289.338 375.215 310.871  1.00100.76           C  
ATOM    702  O   GLU A  90     288.407 374.450 311.156  1.00 99.01           O  
ATOM    703  CB  GLU A  90     288.152 376.842 312.256  1.00109.33           C  
ATOM    704  CG  GLU A  90     288.166 378.034 313.208  1.00114.41           C  
ATOM    705  CD  GLU A  90     288.921 377.859 314.497  1.00114.29           C  
ATOM    706  OE1 GLU A  90     289.123 376.740 314.912  1.00115.53           O  
ATOM    707  OE2 GLU A  90     289.326 378.847 315.066  1.00115.26           O  
ATOM    708  N   ILE A  91     290.213 374.932 309.909  1.00104.63           N  
ATOM    709  CA  ILE A  91     290.157 373.623 309.288  1.00 99.09           C  
ATOM    710  C   ILE A  91     291.172 372.806 310.021  1.00 95.50           C  
ATOM    711  O   ILE A  91     292.365 373.113 310.025  1.00104.28           O  
ATOM    712  CB  ILE A  91     290.475 373.656 307.789  1.00103.42           C  
ATOM    713  CG1 ILE A  91     289.521 374.628 307.062  1.00109.64           C  
ATOM    714  CG2 ILE A  91     290.449 372.247 307.210  1.00 94.20           C  
ATOM    715  CD1 ILE A  91     288.027 374.319 307.198  1.00104.65           C  
ATOM    716  N   ILE A  92     290.709 371.787 310.700  1.00 84.74           N  
ATOM    717  CA  ILE A  92     291.612 371.036 311.529  1.00 84.77           C  
ATOM    718  C   ILE A  92     291.793 369.648 311.019  1.00 79.16           C  
ATOM    719  O   ILE A  92     290.817 368.952 310.770  1.00 80.62           O  
ATOM    720  CB  ILE A  92     291.076 370.950 312.955  1.00 83.06           C  
ATOM    721  CG1 ILE A  92     290.722 372.355 313.491  1.00 90.01           C  
ATOM    722  CG2 ILE A  92     292.087 370.236 313.851  1.00 82.65           C  
ATOM    723  CD1 ILE A  92     291.837 373.355 313.568  1.00 97.68           C  
ATOM    724  N   GLN A  93     293.027 369.219 310.871  1.00 74.91           N  
ATOM    725  CA  GLN A  93     293.264 367.855 310.464  1.00 72.87           C  
ATOM    726  C   GLN A  93     293.876 367.048 311.583  1.00 75.24           C  
ATOM    727  O   GLN A  93     294.946 367.378 312.097  1.00 80.07           O  
ATOM    728  CB  GLN A  93     294.154 367.785 309.249  1.00 75.29           C  
ATOM    729  CG  GLN A  93     294.363 366.382 308.788  1.00 74.60           C  
ATOM    730  CD  GLN A  93     295.141 366.318 307.576  1.00 75.76           C  
ATOM    731  OE1 GLN A  93     295.579 367.336 307.038  1.00 83.26           O  
ATOM    732  NE2 GLN A  93     295.347 365.117 307.099  1.00 73.63           N  
ATOM    733  N   LYS A  94     293.208 365.979 311.963  1.00 70.18           N  
ATOM    734  CA  LYS A  94     293.702 365.138 313.030  1.00 68.64           C  
ATOM    735  C   LYS A  94     294.737 364.173 312.490  1.00 73.43           C  
ATOM    736  O   LYS A  94     294.664 363.765 311.328  1.00 73.05           O  
ATOM    737  CB  LYS A  94     292.541 364.389 313.648  1.00 66.92           C  
ATOM    738  CG  LYS A  94     291.545 365.276 314.322  1.00 71.11           C  
ATOM    739  CD  LYS A  94     290.365 364.469 314.794  1.00 68.27           C  
ATOM    740  CE  LYS A  94     289.385 365.293 315.596  1.00 69.60           C  
ATOM    741  NZ  LYS A  94     288.635 366.220 314.746  1.00 68.68           N  
ATOM    742  N   HIS A  95     295.676 363.770 313.340  1.00 70.68           N  
ATOM    743  CA  HIS A  95     296.687 362.796 312.968  1.00 68.01           C  
ATOM    744  C   HIS A  95     296.653 361.604 313.904  1.00 66.05           C  
ATOM    745  O   HIS A  95     297.684 361.080 314.325  1.00 69.00           O  
ATOM    746  CB  HIS A  95     298.056 363.430 313.005  1.00 72.00           C  
ATOM    747  CG  HIS A  95     298.174 364.569 312.096  1.00 76.05           C  
ATOM    748  ND1 HIS A  95     298.200 364.429 310.733  1.00 76.99           N  
ATOM    749  CD2 HIS A  95     298.280 365.887 312.346  1.00 78.92           C  
ATOM    750  CE1 HIS A  95     298.317 365.617 310.181  1.00 79.74           C  
ATOM    751  NE2 HIS A  95     298.383 366.522 311.139  1.00 80.08           N  
ATOM    752  N   TYR A  96     295.451 361.195 314.234  1.00 65.06           N  
ATOM    753  CA  TYR A  96     295.178 360.091 315.124  1.00 61.86           C  
ATOM    754  C   TYR A  96     293.849 359.468 314.765  1.00 60.04           C  
ATOM    755  O   TYR A  96     293.060 360.071 314.043  1.00 59.95           O  
ATOM    756  CB  TYR A  96     295.240 360.577 316.548  1.00 65.86           C  
ATOM    757  CG  TYR A  96     294.311 361.686 316.833  1.00 66.38           C  
ATOM    758  CD1 TYR A  96     293.068 361.438 317.249  1.00 65.02           C  
ATOM    759  CD2 TYR A  96     294.741 362.972 316.709  1.00 71.98           C  
ATOM    760  CE1 TYR A  96     292.229 362.471 317.566  1.00 65.76           C  
ATOM    761  CE2 TYR A  96     293.914 364.008 317.029  1.00 76.27           C  
ATOM    762  CZ  TYR A  96     292.660 363.758 317.469  1.00 72.45           C  
ATOM    763  OH  TYR A  96     291.796 364.781 317.833  1.00 71.09           O  
ATOM    764  N   TYR A  97     293.579 358.270 315.256  1.00 56.49           N  
ATOM    765  CA  TYR A  97     292.341 357.619 314.871  1.00 52.22           C  
ATOM    766  C   TYR A  97     291.422 357.254 316.018  1.00 54.31           C  
ATOM    767  O   TYR A  97     291.451 356.144 316.553  1.00 55.35           O  
ATOM    768  CB  TYR A  97     292.686 356.403 314.047  1.00 49.77           C  
ATOM    769  CG  TYR A  97     293.513 356.775 312.861  1.00 48.64           C  
ATOM    770  CD1 TYR A  97     294.874 356.732 312.951  1.00 52.85           C  
ATOM    771  CD2 TYR A  97     292.928 357.167 311.698  1.00 50.89           C  
ATOM    772  CE1 TYR A  97     295.646 357.077 311.894  1.00 51.97           C  
ATOM    773  CE2 TYR A  97     293.710 357.512 310.630  1.00 51.93           C  
ATOM    774  CZ  TYR A  97     295.062 357.468 310.733  1.00 50.81           C  
ATOM    775  OH  TYR A  97     295.846 357.826 309.677  1.00 51.53           O  
ATOM    776  N   ASN A  98     290.625 358.220 316.425  1.00 52.16           N  
ATOM    777  CA  ASN A  98     289.705 358.042 317.530  1.00 49.99           C  
ATOM    778  C   ASN A  98     288.298 357.814 316.990  1.00 51.41           C  
ATOM    779  O   ASN A  98     287.751 358.660 316.270  1.00 52.60           O  
ATOM    780  CB  ASN A  98     289.770 359.204 318.456  1.00 52.63           C  
ATOM    781  CG  ASN A  98     291.060 359.348 319.136  1.00 60.10           C  
ATOM    782  OD1 ASN A  98     291.952 358.477 319.086  1.00 60.03           O  
ATOM    783  ND2 ASN A  98     291.184 360.444 319.801  1.00 64.09           N  
ATOM    784  N   ILE A  99     287.735 356.648 317.264  1.00 47.78           N  
ATOM    785  CA  ILE A  99     286.429 356.333 316.702  1.00 44.44           C  
ATOM    786  C   ILE A  99     285.317 356.220 317.713  1.00 45.38           C  
ATOM    787  O   ILE A  99     285.395 355.460 318.681  1.00 49.55           O  
ATOM    788  CB  ILE A  99     286.513 355.079 315.828  1.00 40.15           C  
ATOM    789  CG1 ILE A  99     287.444 355.388 314.655  1.00 41.35           C  
ATOM    790  CG2 ILE A  99     285.133 354.633 315.360  1.00 44.18           C  
ATOM    791  CD1 ILE A  99     287.821 354.216 313.813  1.00 45.66           C  
ATOM    792  N   GLY A 100     284.281 357.004 317.490  1.00 44.20           N  
ATOM    793  CA  GLY A 100     283.146 356.993 318.373  1.00 42.21           C  
ATOM    794  C   GLY A 100     282.188 355.888 318.010  1.00 39.93           C  
ATOM    795  O   GLY A 100     281.929 355.632 316.834  1.00 43.36           O  
ATOM    796  N   ILE A 101     281.582 355.287 319.006  1.00 40.38           N  
ATOM    797  CA  ILE A 101     280.543 354.308 318.750  1.00 39.60           C  
ATOM    798  C   ILE A 101     279.267 354.787 319.353  1.00 45.57           C  
ATOM    799  O   ILE A 101     279.153 354.873 320.562  1.00 50.39           O  
ATOM    800  CB  ILE A 101     280.924 352.942 319.303  1.00 41.61           C  
ATOM    801  CG1 ILE A 101     282.214 352.480 318.598  1.00 44.64           C  
ATOM    802  CG2 ILE A 101     279.765 351.959 319.127  1.00 44.92           C  
ATOM    803  CD1 ILE A 101     282.847 351.261 319.171  1.00 48.75           C  
ATOM    804  N   ALA A 102     278.289 355.078 318.540  1.00 43.33           N  
ATOM    805  CA  ALA A 102     277.078 355.640 319.095  1.00 46.11           C  
ATOM    806  C   ALA A 102     276.227 354.600 319.781  1.00 50.90           C  
ATOM    807  O   ALA A 102     276.114 353.468 319.312  1.00 49.87           O  
ATOM    808  CB  ALA A 102     276.280 356.316 318.009  1.00 46.01           C  
ATOM    809  N   ALA A 103     275.515 355.021 320.821  1.00 53.16           N  
ATOM    810  CA  ALA A 103     274.542 354.155 321.458  1.00 56.63           C  
ATOM    811  C   ALA A 103     273.294 354.926 321.871  1.00 61.78           C  
ATOM    812  O   ALA A 103     273.370 356.019 322.446  1.00 64.55           O  
ATOM    813  CB  ALA A 103     275.161 353.503 322.678  1.00 53.40           C  
ATOM    814  N   ASP A 104     272.136 354.313 321.623  1.00 61.80           N  
ATOM    815  CA  ASP A 104     270.854 354.884 322.018  1.00 66.51           C  
ATOM    816  C   ASP A 104     270.514 354.347 323.394  1.00 68.19           C  
ATOM    817  O   ASP A 104     270.329 353.140 323.563  1.00 68.33           O  
ATOM    818  CB  ASP A 104     269.723 354.524 321.028  1.00 61.91           C  
ATOM    819  CG  ASP A 104     269.855 355.174 319.616  1.00 62.50           C  
ATOM    820  OD1 ASP A 104     270.671 356.042 319.465  1.00 62.75           O  
ATOM    821  OD2 ASP A 104     269.098 354.814 318.701  1.00 62.10           O  
ATOM    822  N   THR A 105     270.470 355.224 324.382  1.00 70.22           N  
ATOM    823  CA  THR A 105     270.238 354.818 325.757  1.00 70.44           C  
ATOM    824  C   THR A 105     269.091 355.626 326.334  1.00 73.43           C  
ATOM    825  O   THR A 105     268.528 356.505 325.681  1.00 72.50           O  
ATOM    826  CB  THR A 105     271.444 355.077 326.645  1.00 69.96           C  
ATOM    827  OG1 THR A 105     271.534 356.484 326.850  1.00 72.12           O  
ATOM    828  CG2 THR A 105     272.748 354.546 326.015  1.00 67.23           C  
ATOM    829  N   ASP A 106     268.770 355.381 327.592  1.00 75.61           N  
ATOM    830  CA  ASP A 106     267.664 356.070 328.246  1.00 76.41           C  
ATOM    831  C   ASP A 106     268.039 357.496 328.618  1.00 75.13           C  
ATOM    832  O   ASP A 106     267.218 358.263 329.117  1.00 76.98           O  
ATOM    833  CB  ASP A 106     267.274 355.315 329.505  1.00 78.62           C  
ATOM    834  CG  ASP A 106     266.674 353.949 329.211  1.00 79.66           C  
ATOM    835  OD1 ASP A 106     266.206 353.721 328.120  1.00 82.77           O  
ATOM    836  OD2 ASP A 106     266.719 353.129 330.086  1.00 91.07           O  
ATOM    837  N   ARG A 107     269.302 357.831 328.401  1.00 75.33           N  
ATOM    838  CA  ARG A 107     269.860 359.127 328.690  1.00 75.18           C  
ATOM    839  C   ARG A 107     270.081 359.894 327.395  1.00 74.31           C  
ATOM    840  O   ARG A 107     270.713 360.952 327.391  1.00 73.97           O  
ATOM    841  CB  ARG A 107     271.179 358.967 329.417  1.00 77.47           C  
ATOM    842  CG  ARG A 107     271.071 358.370 330.808  1.00 79.03           C  
ATOM    843  CD  ARG A 107     272.405 358.004 331.341  1.00 80.17           C  
ATOM    844  NE  ARG A 107     272.340 357.518 332.721  1.00 81.26           N  
ATOM    845  CZ  ARG A 107     272.027 356.255 333.119  1.00 82.21           C  
ATOM    846  NH1 ARG A 107     271.744 355.302 332.250  1.00 77.10           N  
ATOM    847  NH2 ARG A 107     272.022 355.975 334.410  1.00 81.70           N  
ATOM    848  N   GLY A 108     269.564 359.365 326.288  1.00 72.60           N  
ATOM    849  CA  GLY A 108     269.755 359.996 325.000  1.00 74.48           C  
ATOM    850  C   GLY A 108     270.904 359.337 324.260  1.00 70.08           C  
ATOM    851  O   GLY A 108     271.230 358.163 324.491  1.00 69.49           O  
ATOM    852  N   LEU A 109     271.486 360.066 323.318  1.00 68.89           N  
ATOM    853  CA  LEU A 109     272.499 359.479 322.458  1.00 66.92           C  
ATOM    854  C   LEU A 109     273.879 359.776 322.978  1.00 65.40           C  
ATOM    855  O   LEU A 109     274.285 360.932 323.107  1.00 64.53           O  
ATOM    856  CB  LEU A 109     272.355 360.009 321.037  1.00 69.23           C  
ATOM    857  CG  LEU A 109     271.307 359.310 320.128  1.00 73.37           C  
ATOM    858  CD1 LEU A 109     269.889 359.373 320.724  1.00 68.41           C  
ATOM    859  CD2 LEU A 109     271.320 359.997 318.772  1.00 79.78           C  
ATOM    860  N   LEU A 110     274.573 358.709 323.320  1.00 62.94           N  
ATOM    861  CA  LEU A 110     275.892 358.775 323.908  1.00 60.70           C  
ATOM    862  C   LEU A 110     276.895 358.275 322.903  1.00 57.43           C  
ATOM    863  O   LEU A 110     276.600 357.360 322.133  1.00 56.32           O  
ATOM    864  CB  LEU A 110     275.939 357.889 325.164  1.00 61.14           C  
ATOM    865  CG  LEU A 110     275.357 358.452 326.512  1.00 64.26           C  
ATOM    866  CD1 LEU A 110     273.902 358.890 326.372  1.00 66.96           C  
ATOM    867  CD2 LEU A 110     275.439 357.354 327.542  1.00 68.18           C  
ATOM    868  N   VAL A 111     278.093 358.839 322.904  1.00 54.81           N  
ATOM    869  CA  VAL A 111     279.114 358.321 322.013  1.00 50.25           C  
ATOM    870  C   VAL A 111     280.463 358.118 322.683  1.00 52.78           C  
ATOM    871  O   VAL A 111     281.263 359.044 322.685  1.00 55.02           O  
ATOM    872  CB  VAL A 111     279.327 359.266 320.822  1.00 50.91           C  
ATOM    873  CG1 VAL A 111     280.334 358.646 319.858  1.00 49.90           C  
ATOM    874  CG2 VAL A 111     278.016 359.529 320.113  1.00 51.94           C  
ATOM    875  N   PRO A 112     280.724 356.973 323.306  1.00 49.88           N  
ATOM    876  CA  PRO A 112     282.000 356.596 323.856  1.00 51.05           C  
ATOM    877  C   PRO A 112     283.013 356.572 322.730  1.00 50.85           C  
ATOM    878  O   PRO A 112     282.665 356.192 321.607  1.00 52.78           O  
ATOM    879  CB  PRO A 112     281.734 355.206 324.386  1.00 51.87           C  
ATOM    880  CG  PRO A 112     280.279 355.167 324.637  1.00 52.00           C  
ATOM    881  CD  PRO A 112     279.663 356.023 323.585  1.00 50.21           C  
ATOM    882  N   VAL A 113     284.255 356.926 323.013  1.00 49.43           N  
ATOM    883  CA  VAL A 113     285.275 356.952 321.978  1.00 48.11           C  
ATOM    884  C   VAL A 113     286.455 356.031 322.217  1.00 49.62           C  
ATOM    885  O   VAL A 113     287.100 356.088 323.264  1.00 53.60           O  
ATOM    886  CB  VAL A 113     285.782 358.395 321.831  1.00 49.79           C  
ATOM    887  CG1 VAL A 113     286.865 358.488 320.759  1.00 53.84           C  
ATOM    888  CG2 VAL A 113     284.612 359.301 321.507  1.00 52.29           C  
ATOM    889  N   ILE A 114     286.780 355.222 321.215  1.00 48.41           N  
ATOM    890  CA  ILE A 114     287.946 354.371 321.330  1.00 48.88           C  
ATOM    891  C   ILE A 114     289.125 355.109 320.786  1.00 50.97           C  
ATOM    892  O   ILE A 114     289.230 355.356 319.580  1.00 54.42           O  
ATOM    893  CB  ILE A 114     287.805 353.057 320.566  1.00 46.85           C  
ATOM    894  CG1 ILE A 114     286.660 352.293 321.145  1.00 48.62           C  
ATOM    895  CG2 ILE A 114     289.131 352.276 320.608  1.00 50.61           C  
ATOM    896  CD1 ILE A 114     286.271 351.062 320.403  1.00 50.41           C  
ATOM    897  N   LYS A 115     290.029 355.454 321.671  1.00 52.02           N  
ATOM    898  CA  LYS A 115     291.143 356.261 321.277  1.00 52.88           C  
ATOM    899  C   LYS A 115     292.250 355.391 320.774  1.00 51.15           C  
ATOM    900  O   LYS A 115     292.434 354.277 321.253  1.00 51.67           O  
ATOM    901  CB  LYS A 115     291.559 357.119 322.443  1.00 58.48           C  
ATOM    902  CG  LYS A 115     290.442 358.057 322.838  1.00 60.42           C  
ATOM    903  CD  LYS A 115     290.783 358.929 323.999  1.00 64.72           C  
ATOM    904  CE  LYS A 115     289.548 359.713 324.433  1.00 64.72           C  
ATOM    905  NZ  LYS A 115     289.809 360.556 325.625  1.00 67.51           N  
ATOM    906  N   HIS A 116     293.000 355.894 319.819  1.00 54.80           N  
ATOM    907  CA  HIS A 116     294.097 355.136 319.254  1.00 53.11           C  
ATOM    908  C   HIS A 116     293.602 353.784 318.768  1.00 50.81           C  
ATOM    909  O   HIS A 116     294.183 352.740 319.057  1.00 53.82           O  
ATOM    910  CB  HIS A 116     295.224 354.927 320.249  1.00 58.92           C  
ATOM    911  CG  HIS A 116     295.778 356.158 320.819  1.00 63.54           C  
ATOM    912  ND1 HIS A 116     296.427 357.104 320.064  1.00 65.02           N  
ATOM    913  CD2 HIS A 116     295.825 356.588 322.086  1.00 65.43           C  
ATOM    914  CE1 HIS A 116     296.854 358.066 320.855  1.00 68.25           C  
ATOM    915  NE2 HIS A 116     296.503 357.770 322.086  1.00 72.26           N  
ATOM    916  N   ALA A 117     292.527 353.781 317.998  1.00 51.73           N  
ATOM    917  CA  ALA A 117     291.963 352.541 317.497  1.00 48.10           C  
ATOM    918  C   ALA A 117     292.919 351.895 316.517  1.00 49.00           C  
ATOM    919  O   ALA A 117     292.835 350.705 316.223  1.00 49.49           O  
ATOM    920  CB  ALA A 117     290.625 352.793 316.839  1.00 49.23           C  
ATOM    921  N   ASP A 118     293.845 352.674 315.988  1.00 50.19           N  
ATOM    922  CA  ASP A 118     294.789 352.185 315.025  1.00 50.82           C  
ATOM    923  C   ASP A 118     295.814 351.245 315.615  1.00 51.11           C  
ATOM    924  O   ASP A 118     296.479 350.532 314.866  1.00 50.09           O  
ATOM    925  CB  ASP A 118     295.488 353.351 314.378  1.00 53.00           C  
ATOM    926  CG  ASP A 118     296.121 354.213 315.402  1.00 56.87           C  
ATOM    927  OD1 ASP A 118     295.380 354.930 316.054  1.00 57.67           O  
ATOM    928  OD2 ASP A 118     297.314 354.151 315.581  1.00 57.38           O  
ATOM    929  N   ARG A 119     295.950 351.226 316.938  1.00 52.12           N  
ATOM    930  CA  ARG A 119     296.953 350.376 317.542  1.00 50.13           C  
ATOM    931  C   ARG A 119     296.342 349.176 318.221  1.00 48.34           C  
ATOM    932  O   ARG A 119     297.006 348.530 319.030  1.00 50.09           O  
ATOM    933  CB  ARG A 119     297.835 351.123 318.527  1.00 56.47           C  
ATOM    934  CG  ARG A 119     297.268 351.542 319.834  1.00 58.13           C  
ATOM    935  CD  ARG A 119     298.220 352.461 320.542  1.00 65.45           C  
ATOM    936  NE  ARG A 119     299.497 351.789 320.886  1.00 68.98           N  
ATOM    937  CZ  ARG A 119     300.601 352.398 321.408  1.00 68.69           C  
ATOM    938  NH1 ARG A 119     300.587 353.693 321.664  1.00 70.45           N  
ATOM    939  NH2 ARG A 119     301.704 351.691 321.668  1.00 65.57           N  
ATOM    940  N   LYS A 120     295.065 348.888 317.967  1.00 47.55           N  
ATOM    941  CA  LYS A 120     294.490 347.744 318.645  1.00 45.24           C  
ATOM    942  C   LYS A 120     294.162 346.594 317.672  1.00 42.60           C  
ATOM    943  O   LYS A 120     293.841 346.838 316.506  1.00 45.60           O  
ATOM    944  CB  LYS A 120     293.235 348.204 319.361  1.00 46.73           C  
ATOM    945  CG  LYS A 120     293.519 349.223 320.430  1.00 46.77           C  
ATOM    946  CD  LYS A 120     292.259 349.703 321.092  1.00 48.87           C  
ATOM    947  CE  LYS A 120     292.531 350.888 322.012  1.00 50.64           C  
ATOM    948  NZ  LYS A 120     293.282 350.507 323.223  1.00 51.56           N  
ATOM    949  N   PRO A 121     294.305 345.331 318.101  1.00 40.57           N  
ATOM    950  CA  PRO A 121     293.894 344.106 317.435  1.00 39.85           C  
ATOM    951  C   PRO A 121     292.395 343.881 317.576  1.00 40.38           C  
ATOM    952  O   PRO A 121     291.762 344.537 318.404  1.00 44.48           O  
ATOM    953  CB  PRO A 121     294.733 343.060 318.143  1.00 41.92           C  
ATOM    954  CG  PRO A 121     294.926 343.586 319.501  1.00 41.44           C  
ATOM    955  CD  PRO A 121     295.059 345.079 319.332  1.00 42.07           C  
ATOM    956  N   ILE A 122     291.844 342.928 316.826  1.00 37.09           N  
ATOM    957  CA  ILE A 122     290.419 342.640 316.927  1.00 34.05           C  
ATOM    958  C   ILE A 122     289.974 342.177 318.283  1.00 38.42           C  
ATOM    959  O   ILE A 122     288.928 342.627 318.749  1.00 42.16           O  
ATOM    960  CB  ILE A 122     289.953 341.570 315.913  1.00 36.52           C  
ATOM    961  CG1 ILE A 122     290.056 342.060 314.454  1.00 37.02           C  
ATOM    962  CG2 ILE A 122     288.492 341.112 316.227  1.00 39.70           C  
ATOM    963  CD1 ILE A 122     289.135 343.215 314.042  1.00 39.95           C  
ATOM    964  N   PHE A 123     290.698 341.284 318.942  1.00 38.64           N  
ATOM    965  CA  PHE A 123     290.151 340.870 320.218  1.00 39.76           C  
ATOM    966  C   PHE A 123     290.127 342.030 321.191  1.00 41.92           C  
ATOM    967  O   PHE A 123     289.163 342.191 321.940  1.00 44.87           O  
ATOM    968  CB  PHE A 123     290.933 339.717 320.818  1.00 38.48           C  
ATOM    969  CG  PHE A 123     290.701 338.396 320.160  1.00 38.88           C  
ATOM    970  CD1 PHE A 123     291.744 337.747 319.573  1.00 42.08           C  
ATOM    971  CD2 PHE A 123     289.465 337.798 320.111  1.00 39.26           C  
ATOM    972  CE1 PHE A 123     291.578 336.547 318.961  1.00 44.74           C  
ATOM    973  CE2 PHE A 123     289.317 336.581 319.479  1.00 40.84           C  
ATOM    974  CZ  PHE A 123     290.370 335.968 318.914  1.00 41.85           C  
ATOM    975  N   ALA A 124     291.170 342.853 321.183  1.00 40.14           N  
ATOM    976  CA  ALA A 124     291.210 343.983 322.092  1.00 42.59           C  
ATOM    977  C   ALA A 124     290.092 344.945 321.822  1.00 43.12           C  
ATOM    978  O   ALA A 124     289.479 345.448 322.765  1.00 45.85           O  
ATOM    979  CB  ALA A 124     292.497 344.738 321.960  1.00 46.59           C  
ATOM    980  N   LEU A 125     289.783 345.189 320.548  1.00 42.70           N  
ATOM    981  CA  LEU A 125     288.694 346.090 320.287  1.00 42.09           C  
ATOM    982  C   LEU A 125     287.419 345.485 320.761  1.00 44.00           C  
ATOM    983  O   LEU A 125     286.650 346.135 321.451  1.00 45.78           O  
ATOM    984  CB  LEU A 125     288.540 346.370 318.801  1.00 37.48           C  
ATOM    985  CG  LEU A 125     289.573 347.216 318.132  1.00 37.87           C  
ATOM    986  CD1 LEU A 125     289.339 347.137 316.655  1.00 39.45           C  
ATOM    987  CD2 LEU A 125     289.446 348.668 318.590  1.00 42.77           C  
ATOM    988  N   ALA A 126     287.213 344.199 320.533  1.00 43.37           N  
ATOM    989  CA  ALA A 126     285.956 343.639 320.962  1.00 43.75           C  
ATOM    990  C   ALA A 126     285.791 343.809 322.453  1.00 44.44           C  
ATOM    991  O   ALA A 126     284.715 344.191 322.925  1.00 48.95           O  
ATOM    992  CB  ALA A 126     285.893 342.189 320.578  1.00 42.02           C  
ATOM    993  N   GLN A 127     286.868 343.636 323.203  1.00 43.80           N  
ATOM    994  CA  GLN A 127     286.741 343.812 324.623  1.00 46.50           C  
ATOM    995  C   GLN A 127     286.465 345.260 324.992  1.00 51.49           C  
ATOM    996  O   GLN A 127     285.566 345.526 325.791  1.00 53.75           O  
ATOM    997  CB  GLN A 127     288.020 343.340 325.306  1.00 50.03           C  
ATOM    998  CG  GLN A 127     288.031 343.434 326.823  1.00 53.16           C  
ATOM    999  CD  GLN A 127     286.995 342.594 327.470  1.00 57.99           C  
ATOM   1000  OE1 GLN A 127     286.654 341.528 326.970  1.00 54.76           O  
ATOM   1001  NE2 GLN A 127     286.484 343.050 328.606  1.00 62.99           N  
ATOM   1002  N   GLU A 128     287.162 346.210 324.371  1.00 49.49           N  
ATOM   1003  CA  GLU A 128     286.933 347.602 324.720  1.00 46.81           C  
ATOM   1004  C   GLU A 128     285.548 348.056 324.346  1.00 50.08           C  
ATOM   1005  O   GLU A 128     284.921 348.815 325.085  1.00 52.90           O  
ATOM   1006  CB  GLU A 128     287.962 348.530 324.110  1.00 45.75           C  
ATOM   1007  CG  GLU A 128     287.752 349.966 324.542  1.00 48.81           C  
ATOM   1008  CD  GLU A 128     288.857 350.861 324.194  1.00 55.90           C  
ATOM   1009  OE1 GLU A 128     289.855 350.396 323.722  1.00 56.23           O  
ATOM   1010  OE2 GLU A 128     288.713 352.037 324.399  1.00 58.16           O  
ATOM   1011  N   ILE A 129     285.064 347.595 323.207  1.00 47.80           N  
ATOM   1012  CA  ILE A 129     283.759 347.970 322.730  1.00 48.73           C  
ATOM   1013  C   ILE A 129     282.715 347.493 323.690  1.00 50.53           C  
ATOM   1014  O   ILE A 129     281.813 348.253 324.043  1.00 52.94           O  
ATOM   1015  CB  ILE A 129     283.483 347.372 321.341  1.00 46.73           C  
ATOM   1016  CG1 ILE A 129     284.395 348.045 320.308  1.00 45.48           C  
ATOM   1017  CG2 ILE A 129     282.007 347.529 320.981  1.00 46.26           C  
ATOM   1018  CD1 ILE A 129     284.491 347.370 318.963  1.00 46.44           C  
ATOM   1019  N   ASN A 130     282.827 346.253 324.132  1.00 49.24           N  
ATOM   1020  CA  ASN A 130     281.834 345.745 325.035  1.00 50.49           C  
ATOM   1021  C   ASN A 130     281.867 346.501 326.355  1.00 54.20           C  
ATOM   1022  O   ASN A 130     280.808 346.803 326.915  1.00 55.23           O  
ATOM   1023  CB  ASN A 130     282.078 344.277 325.234  1.00 48.66           C  
ATOM   1024  CG  ASN A 130     281.757 343.507 323.988  1.00 52.57           C  
ATOM   1025  OD1 ASN A 130     280.958 343.946 323.155  1.00 52.18           O  
ATOM   1026  ND2 ASN A 130     282.396 342.375 323.824  1.00 51.79           N  
ATOM   1027  N   GLU A 131     283.059 346.877 326.827  1.00 52.61           N  
ATOM   1028  CA  GLU A 131     283.131 347.614 328.074  1.00 53.64           C  
ATOM   1029  C   GLU A 131     282.533 348.993 327.945  1.00 56.35           C  
ATOM   1030  O   GLU A 131     281.802 349.440 328.835  1.00 58.44           O  
ATOM   1031  CB  GLU A 131     284.571 347.775 328.526  1.00 54.64           C  
ATOM   1032  CG  GLU A 131     285.234 346.513 328.972  1.00 63.62           C  
ATOM   1033  CD  GLU A 131     286.676 346.723 329.316  1.00 70.42           C  
ATOM   1034  OE1 GLU A 131     287.131 347.849 329.237  1.00 64.48           O  
ATOM   1035  OE2 GLU A 131     287.336 345.751 329.633  1.00 67.55           O  
ATOM   1036  N   LEU A 132     282.793 349.667 326.828  1.00 53.18           N  
ATOM   1037  CA  LEU A 132     282.245 350.990 326.664  1.00 52.81           C  
ATOM   1038  C   LEU A 132     280.758 350.924 326.534  1.00 56.81           C  
ATOM   1039  O   LEU A 132     280.061 351.807 327.035  1.00 61.53           O  
ATOM   1040  CB  LEU A 132     282.834 351.689 325.452  1.00 50.35           C  
ATOM   1041  CG  LEU A 132     284.313 352.099 325.548  1.00 56.09           C  
ATOM   1042  CD1 LEU A 132     284.775 352.604 324.176  1.00 54.99           C  
ATOM   1043  CD2 LEU A 132     284.514 353.196 326.624  1.00 59.24           C  
ATOM   1044  N   ALA A 133     280.250 349.894 325.865  1.00 53.86           N  
ATOM   1045  CA  ALA A 133     278.824 349.767 325.715  1.00 56.36           C  
ATOM   1046  C   ALA A 133     278.146 349.616 327.062  1.00 58.99           C  
ATOM   1047  O   ALA A 133     277.112 350.246 327.309  1.00 61.87           O  
ATOM   1048  CB  ALA A 133     278.507 348.577 324.848  1.00 57.57           C  
ATOM   1049  N   GLU A 134     278.754 348.852 327.969  1.00 57.53           N  
ATOM   1050  CA  GLU A 134     278.154 348.691 329.280  1.00 60.63           C  
ATOM   1051  C   GLU A 134     278.211 349.983 330.074  1.00 61.44           C  
ATOM   1052  O   GLU A 134     277.245 350.348 330.750  1.00 63.08           O  
ATOM   1053  CB  GLU A 134     278.865 347.577 330.034  1.00 60.53           C  
ATOM   1054  CG  GLU A 134     278.600 346.209 329.462  1.00 64.28           C  
ATOM   1055  CD  GLU A 134     277.182 345.805 329.610  1.00 70.64           C  
ATOM   1056  OE1 GLU A 134     276.731 345.732 330.722  1.00 70.37           O  
ATOM   1057  OE2 GLU A 134     276.531 345.613 328.620  1.00 68.07           O  
ATOM   1058  N   LYS A 135     279.314 350.712 329.960  1.00 58.13           N  
ATOM   1059  CA  LYS A 135     279.419 351.955 330.684  1.00 58.62           C  
ATOM   1060  C   LYS A 135     278.405 352.940 330.154  1.00 61.71           C  
ATOM   1061  O   LYS A 135     277.783 353.686 330.917  1.00 65.99           O  
ATOM   1062  CB  LYS A 135     280.817 352.510 330.566  1.00 59.19           C  
ATOM   1063  CG  LYS A 135     281.834 351.728 331.320  1.00 58.87           C  
ATOM   1064  CD  LYS A 135     283.227 352.257 331.081  1.00 62.27           C  
ATOM   1065  CE  LYS A 135     284.251 351.419 331.827  1.00 71.30           C  
ATOM   1066  NZ  LYS A 135     285.656 351.844 331.551  1.00 74.19           N  
ATOM   1067  N   ALA A 136     278.207 352.962 328.840  1.00 59.73           N  
ATOM   1068  CA  ALA A 136     277.227 353.872 328.304  1.00 61.24           C  
ATOM   1069  C   ALA A 136     275.842 353.508 328.780  1.00 63.89           C  
ATOM   1070  O   ALA A 136     275.086 354.373 329.224  1.00 66.01           O  
ATOM   1071  CB  ALA A 136     277.261 353.843 326.792  1.00 61.76           C  
ATOM   1072  N   ARG A 137     275.535 352.214 328.808  1.00 61.95           N  
ATOM   1073  CA  ARG A 137     274.211 351.770 329.189  1.00 63.23           C  
ATOM   1074  C   ARG A 137     273.849 352.194 330.594  1.00 67.14           C  
ATOM   1075  O   ARG A 137     272.725 352.641 330.840  1.00 69.10           O  
ATOM   1076  CB  ARG A 137     274.097 350.269 329.051  1.00 63.95           C  
ATOM   1077  CG  ARG A 137     272.729 349.715 329.354  1.00 66.00           C  
ATOM   1078  CD  ARG A 137     272.629 348.258 329.033  1.00 73.37           C  
ATOM   1079  NE  ARG A 137     273.512 347.426 329.850  1.00 71.55           N  
ATOM   1080  CZ  ARG A 137     273.266 347.046 331.123  1.00 72.08           C  
ATOM   1081  NH1 ARG A 137     272.169 347.437 331.744  1.00 76.80           N  
ATOM   1082  NH2 ARG A 137     274.129 346.277 331.753  1.00 69.40           N  
ATOM   1083  N   ASP A 138     274.805 352.104 331.506  1.00 65.71           N  
ATOM   1084  CA  ASP A 138     274.578 352.491 332.886  1.00 66.29           C  
ATOM   1085  C   ASP A 138     274.899 353.938 333.226  1.00 66.58           C  
ATOM   1086  O   ASP A 138     274.806 354.320 334.393  1.00 67.94           O  
ATOM   1087  CB  ASP A 138     275.401 351.636 333.827  1.00 64.37           C  
ATOM   1088  CG  ASP A 138     274.953 350.220 333.984  1.00 69.77           C  
ATOM   1089  OD1 ASP A 138     273.769 349.969 334.012  1.00 69.02           O  
ATOM   1090  OD2 ASP A 138     275.812 349.371 334.081  1.00 68.08           O  
ATOM   1091  N   GLY A 139     275.332 354.746 332.263  1.00 66.83           N  
ATOM   1092  CA  GLY A 139     275.686 356.120 332.592  1.00 68.96           C  
ATOM   1093  C   GLY A 139     276.973 356.235 333.411  1.00 67.25           C  
ATOM   1094  O   GLY A 139     277.116 357.153 334.217  1.00 67.45           O  
ATOM   1095  N   LYS A 140     277.903 355.309 333.227  1.00 63.76           N  
ATOM   1096  CA  LYS A 140     279.142 355.276 333.992  1.00 62.27           C  
ATOM   1097  C   LYS A 140     280.337 355.834 333.248  1.00 64.08           C  
ATOM   1098  O   LYS A 140     281.475 355.661 333.682  1.00 63.95           O  
ATOM   1099  CB  LYS A 140     279.427 353.856 334.437  1.00 65.16           C  
ATOM   1100  CG  LYS A 140     278.428 353.323 335.425  1.00 66.40           C  
ATOM   1101  CD  LYS A 140     278.728 351.880 335.779  1.00 69.90           C  
ATOM   1102  CE  LYS A 140     277.760 351.339 336.821  1.00 73.67           C  
ATOM   1103  NZ  LYS A 140     277.980 349.892 337.084  1.00 78.68           N  
ATOM   1104  N   LEU A 141     280.088 356.460 332.116  1.00 64.53           N  
ATOM   1105  CA  LEU A 141     281.150 357.014 331.303  1.00 64.08           C  
ATOM   1106  C   LEU A 141     281.729 358.255 331.926  1.00 61.76           C  
ATOM   1107  O   LEU A 141     281.006 359.115 332.431  1.00 61.41           O  
ATOM   1108  CB  LEU A 141     280.594 357.435 329.945  1.00 61.34           C  
ATOM   1109  CG  LEU A 141     280.028 356.353 329.073  1.00 62.43           C  
ATOM   1110  CD1 LEU A 141     279.330 357.008 327.928  1.00 62.73           C  
ATOM   1111  CD2 LEU A 141     281.139 355.444 328.533  1.00 60.87           C  
ATOM   1112  N   THR A 142     283.031 358.381 331.823  1.00 62.84           N  
ATOM   1113  CA  THR A 142     283.712 359.579 332.235  1.00 62.51           C  
ATOM   1114  C   THR A 142     283.544 360.520 331.057  1.00 62.72           C  
ATOM   1115  O   THR A 142     283.728 360.082 329.934  1.00 63.36           O  
ATOM   1116  CB  THR A 142     285.199 359.299 332.543  1.00 64.39           C  
ATOM   1117  OG1 THR A 142     285.290 358.376 333.622  1.00 63.40           O  
ATOM   1118  CG2 THR A 142     285.936 360.558 332.912  1.00 64.84           C  
ATOM   1119  N   PRO A 143     283.197 361.794 331.217  1.00 60.68           N  
ATOM   1120  CA  PRO A 143     283.038 362.736 330.124  1.00 61.00           C  
ATOM   1121  C   PRO A 143     284.209 362.768 329.141  1.00 63.25           C  
ATOM   1122  O   PRO A 143     284.003 362.967 327.950  1.00 64.34           O  
ATOM   1123  CB  PRO A 143     282.916 364.053 330.873  1.00 59.62           C  
ATOM   1124  CG  PRO A 143     282.274 363.669 332.179  1.00 64.24           C  
ATOM   1125  CD  PRO A 143     282.861 362.334 332.535  1.00 62.14           C  
ATOM   1126  N   GLY A 144     285.430 362.498 329.592  1.00 63.38           N  
ATOM   1127  CA  GLY A 144     286.580 362.517 328.698  1.00 65.43           C  
ATOM   1128  C   GLY A 144     286.597 361.323 327.738  1.00 63.23           C  
ATOM   1129  O   GLY A 144     287.385 361.293 326.784  1.00 63.52           O  
ATOM   1130  N   GLU A 145     285.727 360.340 327.981  1.00 60.43           N  
ATOM   1131  CA  GLU A 145     285.610 359.149 327.160  1.00 60.22           C  
ATOM   1132  C   GLU A 145     284.625 359.380 326.053  1.00 60.00           C  
ATOM   1133  O   GLU A 145     284.379 358.481 325.255  1.00 59.70           O  
ATOM   1134  CB  GLU A 145     285.128 357.920 327.948  1.00 59.00           C  
ATOM   1135  CG  GLU A 145     286.076 357.392 328.983  1.00 64.60           C  
ATOM   1136  CD  GLU A 145     285.529 356.177 329.740  1.00 66.75           C  
ATOM   1137  OE1 GLU A 145     284.657 356.326 330.587  1.00 67.18           O  
ATOM   1138  OE2 GLU A 145     285.993 355.091 329.470  1.00 65.66           O  
ATOM   1139  N   MET A 146     283.977 360.539 326.047  1.00 59.18           N  
ATOM   1140  CA  MET A 146     282.993 360.834 325.028  1.00 58.92           C  
ATOM   1141  C   MET A 146     283.490 361.926 324.103  1.00 60.81           C  
ATOM   1142  O   MET A 146     282.720 362.529 323.355  1.00 61.65           O  
ATOM   1143  CB  MET A 146     281.714 361.244 325.700  1.00 59.21           C  
ATOM   1144  CG  MET A 146     281.147 360.154 326.562  1.00 59.50           C  
ATOM   1145  SD  MET A 146     279.646 360.628 327.390  1.00 70.56           S  
ATOM   1146  CE  MET A 146     278.478 360.558 326.057  1.00 66.38           C  
ATOM   1147  N   LYS A 147     284.775 362.215 324.193  1.00 60.91           N  
ATOM   1148  CA  LYS A 147     285.383 363.292 323.442  1.00 58.73           C  
ATOM   1149  C   LYS A 147     286.552 362.853 322.585  1.00 60.64           C  
ATOM   1150  O   LYS A 147     287.175 361.825 322.830  1.00 60.51           O  
ATOM   1151  CB  LYS A 147     285.871 364.365 324.406  1.00 63.96           C  
ATOM   1152  CG  LYS A 147     284.801 364.964 325.303  1.00 69.24           C  
ATOM   1153  CD  LYS A 147     283.783 365.796 324.546  1.00 71.82           C  
ATOM   1154  CE  LYS A 147     282.801 366.441 325.509  1.00 74.10           C  
ATOM   1155  NZ  LYS A 147     281.748 367.228 324.797  1.00 77.34           N  
ATOM   1156  N   GLY A 148     286.843 363.642 321.554  1.00 59.73           N  
ATOM   1157  CA  GLY A 148     288.024 363.410 320.737  1.00 57.07           C  
ATOM   1158  C   GLY A 148     287.873 362.495 319.532  1.00 58.66           C  
ATOM   1159  O   GLY A 148     288.881 362.063 318.989  1.00 61.21           O  
ATOM   1160  N   ALA A 149     286.660 362.140 319.126  1.00 55.63           N  
ATOM   1161  CA  ALA A 149     286.538 361.265 317.967  1.00 52.22           C  
ATOM   1162  C   ALA A 149     286.877 362.017 316.693  1.00 53.88           C  
ATOM   1163  O   ALA A 149     286.605 363.211 316.584  1.00 57.00           O  
ATOM   1164  CB  ALA A 149     285.143 360.699 317.854  1.00 50.54           C  
ATOM   1165  N   SER A 150     287.469 361.325 315.725  1.00 51.33           N  
ATOM   1166  CA  SER A 150     287.677 361.892 314.409  1.00 50.35           C  
ATOM   1167  C   SER A 150     286.495 361.506 313.546  1.00 49.89           C  
ATOM   1168  O   SER A 150     286.090 362.233 312.642  1.00 51.21           O  
ATOM   1169  CB  SER A 150     288.923 361.339 313.777  1.00 54.54           C  
ATOM   1170  OG  SER A 150     288.762 359.987 313.498  1.00 53.65           O  
ATOM   1171  N   CYS A 151     285.877 360.385 313.892  1.00 50.41           N  
ATOM   1172  CA  CYS A 151     284.724 359.891 313.156  1.00 44.36           C  
ATOM   1173  C   CYS A 151     283.868 359.035 314.069  1.00 44.94           C  
ATOM   1174  O   CYS A 151     284.380 358.499 315.052  1.00 50.24           O  
ATOM   1175  CB  CYS A 151     285.155 359.098 311.944  1.00 43.38           C  
ATOM   1176  SG  CYS A 151     283.811 358.698 310.875  1.00 43.83           S  
ATOM   1177  N   THR A 152     282.592 358.889 313.734  1.00 39.90           N  
ATOM   1178  CA  THR A 152     281.662 358.054 314.493  1.00 38.57           C  
ATOM   1179  C   THR A 152     280.984 356.996 313.635  1.00 36.95           C  
ATOM   1180  O   THR A 152     280.659 357.242 312.470  1.00 41.60           O  
ATOM   1181  CB  THR A 152     280.596 358.938 315.187  1.00 39.60           C  
ATOM   1182  OG1 THR A 152     281.256 359.815 316.097  1.00 45.93           O  
ATOM   1183  CG2 THR A 152     279.555 358.102 315.969  1.00 42.16           C  
ATOM   1184  N   ILE A 153     280.765 355.834 314.231  1.00 34.72           N  
ATOM   1185  CA  ILE A 153     280.017 354.740 313.638  1.00 31.41           C  
ATOM   1186  C   ILE A 153     278.702 354.567 314.376  1.00 35.99           C  
ATOM   1187  O   ILE A 153     278.687 354.527 315.608  1.00 41.53           O  
ATOM   1188  CB  ILE A 153     280.767 353.402 313.726  1.00 31.33           C  
ATOM   1189  CG1 ILE A 153     282.068 353.490 312.982  1.00 35.80           C  
ATOM   1190  CG2 ILE A 153     279.889 352.278 313.122  1.00 32.17           C  
ATOM   1191  CD1 ILE A 153     283.013 352.336 313.258  1.00 39.37           C  
ATOM   1192  N   THR A 154     277.601 354.513 313.641  1.00 36.28           N  
ATOM   1193  CA  THR A 154     276.304 354.292 314.262  1.00 35.53           C  
ATOM   1194  C   THR A 154     275.703 353.008 313.794  1.00 36.57           C  
ATOM   1195  O   THR A 154     275.457 352.812 312.608  1.00 37.58           O  
ATOM   1196  CB  THR A 154     275.303 355.416 313.976  1.00 36.40           C  
ATOM   1197  OG1 THR A 154     275.797 356.613 314.506  1.00 39.85           O  
ATOM   1198  CG2 THR A 154     273.959 355.110 314.600  1.00 38.24           C  
ATOM   1199  N   ASN A 155     275.430 352.153 314.737  1.00 36.55           N  
ATOM   1200  CA  ASN A 155     274.814 350.887 314.462  1.00 34.08           C  
ATOM   1201  C   ASN A 155     273.321 350.982 314.625  1.00 39.06           C  
ATOM   1202  O   ASN A 155     272.841 351.473 315.646  1.00 42.23           O  
ATOM   1203  CB  ASN A 155     275.388 349.805 315.333  1.00 35.64           C  
ATOM   1204  CG  ASN A 155     274.764 348.506 315.043  1.00 38.96           C  
ATOM   1205  OD1 ASN A 155     273.592 348.343 315.390  1.00 40.43           O  
ATOM   1206  ND2 ASN A 155     275.474 347.597 314.436  1.00 39.09           N  
ATOM   1207  N   ILE A 156     272.583 350.584 313.598  1.00 38.46           N  
ATOM   1208  CA  ILE A 156     271.149 350.572 313.719  1.00 36.12           C  
ATOM   1209  C   ILE A 156     270.819 349.148 313.564  1.00 38.03           C  
ATOM   1210  O   ILE A 156     269.802 348.689 314.060  1.00 41.33           O  
ATOM   1211  CB  ILE A 156     270.386 351.384 312.672  1.00 34.18           C  
ATOM   1212  CG1 ILE A 156     268.976 351.643 313.194  1.00 39.57           C  
ATOM   1213  CG2 ILE A 156     270.310 350.609 311.336  1.00 34.78           C  
ATOM   1214  CD1 ILE A 156     268.210 352.716 312.440  1.00 43.20           C  
ATOM   1215  N   GLY A 157     271.760 348.435 312.951  1.00 38.03           N  
ATOM   1216  CA  GLY A 157     271.608 347.035 312.611  1.00 38.36           C  
ATOM   1217  C   GLY A 157     271.189 346.150 313.769  1.00 40.33           C  
ATOM   1218  O   GLY A 157     270.428 345.204 313.571  1.00 42.39           O  
ATOM   1219  N   SER A 158     271.571 346.469 314.996  1.00 40.25           N  
ATOM   1220  CA  SER A 158     271.171 345.648 316.131  1.00 40.54           C  
ATOM   1221  C   SER A 158     269.654 345.654 316.329  1.00 41.84           C  
ATOM   1222  O   SER A 158     269.110 344.774 316.998  1.00 44.74           O  
ATOM   1223  CB  SER A 158     271.809 346.162 317.395  1.00 42.44           C  
ATOM   1224  OG  SER A 158     271.238 347.380 317.789  1.00 42.29           O  
ATOM   1225  N   ALA A 159     268.966 346.650 315.771  1.00 40.63           N  
ATOM   1226  CA  ALA A 159     267.524 346.782 315.845  1.00 40.06           C  
ATOM   1227  C   ALA A 159     266.878 346.392 314.517  1.00 41.97           C  
ATOM   1228  O   ALA A 159     265.667 346.544 314.359  1.00 42.74           O  
ATOM   1229  CB  ALA A 159     267.140 348.214 316.196  1.00 39.54           C  
ATOM   1230  N   GLY A 160     267.670 345.903 313.571  1.00 42.11           N  
ATOM   1231  CA  GLY A 160     267.205 345.610 312.227  1.00 40.70           C  
ATOM   1232  C   GLY A 160     267.354 346.888 311.420  1.00 39.43           C  
ATOM   1233  O   GLY A 160     267.905 347.863 311.909  1.00 41.81           O  
ATOM   1234  N   GLY A 161     266.887 346.906 310.190  1.00 39.77           N  
ATOM   1235  CA  GLY A 161     267.029 348.114 309.399  1.00 38.88           C  
ATOM   1236  C   GLY A 161     268.134 348.113 308.384  1.00 36.17           C  
ATOM   1237  O   GLY A 161     269.131 347.387 308.478  1.00 36.52           O  
ATOM   1238  N   GLN A 162     267.918 348.933 307.379  1.00 34.02           N  
ATOM   1239  CA  GLN A 162     268.828 349.115 306.286  1.00 31.39           C  
ATOM   1240  C   GLN A 162     268.871 350.578 305.966  1.00 32.83           C  
ATOM   1241  O   GLN A 162     267.934 351.303 306.265  1.00 33.59           O  
ATOM   1242  CB  GLN A 162     268.355 348.358 305.055  1.00 32.82           C  
ATOM   1243  CG  GLN A 162     268.186 346.904 305.274  1.00 34.10           C  
ATOM   1244  CD  GLN A 162     267.808 346.173 304.038  1.00 38.41           C  
ATOM   1245  OE1 GLN A 162     268.669 345.967 303.164  1.00 39.84           O  
ATOM   1246  NE2 GLN A 162     266.541 345.762 303.920  1.00 38.80           N  
ATOM   1247  N   TRP A 163     269.954 351.031 305.399  1.00 33.68           N  
ATOM   1248  CA  TRP A 163     269.957 352.348 304.816  1.00 33.72           C  
ATOM   1249  C   TRP A 163     269.229 353.444 305.547  1.00 33.51           C  
ATOM   1250  O   TRP A 163     268.193 353.929 305.088  1.00 35.07           O  
ATOM   1251  CB  TRP A 163     269.377 352.223 303.453  1.00 33.74           C  
ATOM   1252  CG  TRP A 163     270.148 351.351 302.638  1.00 33.52           C  
ATOM   1253  CD1 TRP A 163     271.498 351.268 302.547  1.00 35.01           C  
ATOM   1254  CD2 TRP A 163     269.635 350.381 301.783  1.00 32.11           C  
ATOM   1255  NE1 TRP A 163     271.836 350.312 301.685  1.00 33.50           N  
ATOM   1256  CE2 TRP A 163     270.706 349.757 301.199  1.00 32.32           C  
ATOM   1257  CE3 TRP A 163     268.356 349.987 301.459  1.00 35.87           C  
ATOM   1258  CZ2 TRP A 163     270.542 348.770 300.308  1.00 34.33           C  
ATOM   1259  CZ3 TRP A 163     268.193 348.987 300.560  1.00 37.67           C  
ATOM   1260  CH2 TRP A 163     269.261 348.393 299.996  1.00 37.85           C  
ATOM   1261  N   PHE A 164     269.764 353.861 306.658  1.00 32.13           N  
ATOM   1262  CA  PHE A 164     269.141 354.941 307.364  1.00 31.26           C  
ATOM   1263  C   PHE A 164     269.950 356.149 307.000  1.00 33.56           C  
ATOM   1264  O   PHE A 164     270.880 356.025 306.203  1.00 35.71           O  
ATOM   1265  CB  PHE A 164     269.051 354.628 308.836  1.00 34.23           C  
ATOM   1266  CG  PHE A 164     270.268 354.509 309.572  1.00 34.10           C  
ATOM   1267  CD1 PHE A 164     270.695 355.531 310.343  1.00 35.31           C  
ATOM   1268  CD2 PHE A 164     271.016 353.375 309.502  1.00 35.99           C  
ATOM   1269  CE1 PHE A 164     271.827 355.405 311.068  1.00 38.28           C  
ATOM   1270  CE2 PHE A 164     272.168 353.254 310.212  1.00 39.13           C  
ATOM   1271  CZ  PHE A 164     272.567 354.269 311.004  1.00 40.10           C  
ATOM   1272  N   THR A 165     269.596 357.308 307.503  1.00 36.07           N  
ATOM   1273  CA  THR A 165     270.281 358.525 307.120  1.00 36.86           C  
ATOM   1274  C   THR A 165     270.815 359.232 308.344  1.00 39.06           C  
ATOM   1275  O   THR A 165     270.197 360.192 308.797  1.00 41.33           O  
ATOM   1276  CB  THR A 165     269.330 359.497 306.436  1.00 37.18           C  
ATOM   1277  OG1 THR A 165     268.262 359.786 307.326  1.00 42.77           O  
ATOM   1278  CG2 THR A 165     268.786 358.866 305.206  1.00 37.03           C  
ATOM   1279  N   PRO A 166     271.945 358.814 308.904  1.00 35.82           N  
ATOM   1280  CA  PRO A 166     272.459 359.293 310.152  1.00 39.25           C  
ATOM   1281  C   PRO A 166     272.824 360.740 310.062  1.00 44.66           C  
ATOM   1282  O   PRO A 166     273.200 361.223 308.994  1.00 45.32           O  
ATOM   1283  CB  PRO A 166     273.705 358.448 310.355  1.00 41.80           C  
ATOM   1284  CG  PRO A 166     274.083 357.989 308.988  1.00 38.37           C  
ATOM   1285  CD  PRO A 166     272.804 357.853 308.238  1.00 35.71           C  
ATOM   1286  N   VAL A 167     272.708 361.412 311.191  1.00 46.22           N  
ATOM   1287  CA  VAL A 167     273.081 362.795 311.325  1.00 47.55           C  
ATOM   1288  C   VAL A 167     274.534 362.856 311.696  1.00 51.97           C  
ATOM   1289  O   VAL A 167     274.970 362.154 312.601  1.00 51.48           O  
ATOM   1290  CB  VAL A 167     272.208 363.484 312.378  1.00 51.87           C  
ATOM   1291  CG1 VAL A 167     272.653 364.927 312.596  1.00 62.23           C  
ATOM   1292  CG2 VAL A 167     270.769 363.446 311.903  1.00 59.07           C  
ATOM   1293  N   ILE A 168     275.279 363.678 310.994  1.00 53.49           N  
ATOM   1294  CA  ILE A 168     276.690 363.806 311.246  1.00 52.97           C  
ATOM   1295  C   ILE A 168     276.811 364.608 312.494  1.00 60.09           C  
ATOM   1296  O   ILE A 168     276.223 365.682 312.590  1.00 63.83           O  
ATOM   1297  CB  ILE A 168     277.369 364.591 310.119  1.00 53.00           C  
ATOM   1298  CG1 ILE A 168     277.180 363.867 308.847  1.00 53.56           C  
ATOM   1299  CG2 ILE A 168     278.885 364.729 310.413  1.00 54.02           C  
ATOM   1300  CD1 ILE A 168     277.491 364.642 307.671  1.00 55.87           C  
ATOM   1301  N   ASN A 169     277.562 364.133 313.462  1.00 59.84           N  
ATOM   1302  CA  ASN A 169     277.689 364.921 314.653  1.00 65.90           C  
ATOM   1303  C   ASN A 169     278.378 366.164 314.159  1.00 68.49           C  
ATOM   1304  O   ASN A 169     279.449 366.075 313.566  1.00 69.11           O  
ATOM   1305  CB  ASN A 169     278.455 364.162 315.689  1.00 65.43           C  
ATOM   1306  CG  ASN A 169     278.512 364.821 316.979  1.00 72.97           C  
ATOM   1307  OD1 ASN A 169     277.511 365.330 317.502  1.00 76.25           O  
ATOM   1308  ND2 ASN A 169     279.692 364.830 317.530  1.00 74.01           N  
ATOM   1309  N   HIS A 170     277.773 367.314 314.380  1.00 72.32           N  
ATOM   1310  CA  HIS A 170     278.259 368.539 313.772  1.00 76.93           C  
ATOM   1311  C   HIS A 170     279.750 368.895 313.815  1.00 75.35           C  
ATOM   1312  O   HIS A 170     280.188 369.552 312.877  1.00 78.07           O  
ATOM   1313  CB  HIS A 170     277.429 369.743 314.238  1.00 86.42           C  
ATOM   1314  CG  HIS A 170     277.425 370.003 315.664  1.00 84.77           C  
ATOM   1315  ND1 HIS A 170     276.574 369.348 316.534  1.00 89.55           N  
ATOM   1316  CD2 HIS A 170     278.174 370.841 316.414  1.00 86.87           C  
ATOM   1317  CE1 HIS A 170     276.804 369.778 317.760  1.00 94.52           C  
ATOM   1318  NE2 HIS A 170     277.771 370.685 317.713  1.00 92.40           N  
ATOM   1319  N   PRO A 171     280.570 368.580 314.838  1.00 71.88           N  
ATOM   1320  CA  PRO A 171     281.974 368.921 314.852  1.00 68.97           C  
ATOM   1321  C   PRO A 171     282.799 368.128 313.840  1.00 68.55           C  
ATOM   1322  O   PRO A 171     283.933 368.490 313.568  1.00 72.20           O  
ATOM   1323  CB  PRO A 171     282.399 368.564 316.275  1.00 69.63           C  
ATOM   1324  CG  PRO A 171     281.121 368.466 317.045  1.00 73.98           C  
ATOM   1325  CD  PRO A 171     280.151 367.918 316.060  1.00 75.20           C  
ATOM   1326  N   GLU A 172     282.266 367.025 313.313  1.00 65.47           N  
ATOM   1327  CA  GLU A 172     283.013 366.164 312.406  1.00 62.15           C  
ATOM   1328  C   GLU A 172     282.515 366.313 310.985  1.00 60.44           C  
ATOM   1329  O   GLU A 172     281.573 367.050 310.724  1.00 64.16           O  
ATOM   1330  CB  GLU A 172     282.928 364.692 312.846  1.00 58.19           C  
ATOM   1331  CG  GLU A 172     283.669 364.339 314.160  1.00 60.65           C  
ATOM   1332  CD  GLU A 172     282.856 364.493 315.427  1.00 67.92           C  
ATOM   1333  OE1 GLU A 172     281.773 363.963 315.489  1.00 67.63           O  
ATOM   1334  OE2 GLU A 172     283.323 365.127 316.344  1.00 71.53           O  
ATOM   1335  N   VAL A 173     283.135 365.602 310.053  1.00 54.23           N  
ATOM   1336  CA  VAL A 173     282.713 365.703 308.668  1.00 53.99           C  
ATOM   1337  C   VAL A 173     281.991 364.482 308.132  1.00 52.46           C  
ATOM   1338  O   VAL A 173     281.414 364.539 307.042  1.00 55.61           O  
ATOM   1339  CB  VAL A 173     283.923 366.006 307.787  1.00 57.83           C  
ATOM   1340  CG1 VAL A 173     284.518 367.332 308.203  1.00 68.48           C  
ATOM   1341  CG2 VAL A 173     284.969 364.880 307.915  1.00 59.71           C  
ATOM   1342  N   ALA A 174     282.022 363.366 308.854  1.00 50.61           N  
ATOM   1343  CA  ALA A 174     281.309 362.202 308.361  1.00 44.95           C  
ATOM   1344  C   ALA A 174     280.920 361.248 309.469  1.00 43.73           C  
ATOM   1345  O   ALA A 174     281.569 361.191 310.516  1.00 45.47           O  
ATOM   1346  CB  ALA A 174     282.151 361.476 307.340  1.00 42.54           C  
ATOM   1347  N   ILE A 175     279.851 360.498 309.220  1.00 40.67           N  
ATOM   1348  CA  ILE A 175     279.400 359.428 310.104  1.00 37.01           C  
ATOM   1349  C   ILE A 175     279.076 358.181 309.288  1.00 34.53           C  
ATOM   1350  O   ILE A 175     278.463 358.267 308.222  1.00 38.06           O  
ATOM   1351  CB  ILE A 175     278.206 359.916 310.943  1.00 40.04           C  
ATOM   1352  CG1 ILE A 175     277.792 358.891 311.982  1.00 38.66           C  
ATOM   1353  CG2 ILE A 175     277.064 360.243 310.058  1.00 44.64           C  
ATOM   1354  CD1 ILE A 175     276.883 359.447 313.045  1.00 43.80           C  
ATOM   1355  N   LEU A 176     279.473 357.019 309.771  1.00 32.92           N  
ATOM   1356  CA  LEU A 176     279.171 355.789 309.052  1.00 29.31           C  
ATOM   1357  C   LEU A 176     278.076 354.986 309.704  1.00 32.30           C  
ATOM   1358  O   LEU A 176     278.224 354.562 310.848  1.00 36.69           O  
ATOM   1359  CB  LEU A 176     280.428 354.935 308.957  1.00 31.19           C  
ATOM   1360  CG  LEU A 176     280.291 353.534 308.320  1.00 31.59           C  
ATOM   1361  CD1 LEU A 176     279.881 353.634 306.855  1.00 32.93           C  
ATOM   1362  CD2 LEU A 176     281.630 352.825 308.456  1.00 33.70           C  
ATOM   1363  N   GLY A 177     276.979 354.760 308.999  1.00 32.89           N  
ATOM   1364  CA  GLY A 177     275.900 353.974 309.556  1.00 32.11           C  
ATOM   1365  C   GLY A 177     276.013 352.510 309.143  1.00 34.71           C  
ATOM   1366  O   GLY A 177     276.269 352.180 307.977  1.00 36.42           O  
ATOM   1367  N   ILE A 178     275.731 351.622 310.082  1.00 33.66           N  
ATOM   1368  CA  ILE A 178     275.758 350.192 309.836  1.00 31.18           C  
ATOM   1369  C   ILE A 178     274.406 349.547 310.042  1.00 34.86           C  
ATOM   1370  O   ILE A 178     273.842 349.588 311.152  1.00 39.78           O  
ATOM   1371  CB  ILE A 178     276.786 349.543 310.768  1.00 34.00           C  
ATOM   1372  CG1 ILE A 178     278.155 350.195 310.578  1.00 36.76           C  
ATOM   1373  CG2 ILE A 178     276.860 348.076 310.574  1.00 35.26           C  
ATOM   1374  CD1 ILE A 178     278.791 350.058 309.193  1.00 39.68           C  
ATOM   1375  N   GLY A 179     273.918 348.894 309.001  1.00 32.86           N  
ATOM   1376  CA  GLY A 179     272.638 348.225 309.049  1.00 34.36           C  
ATOM   1377  C   GLY A 179     272.801 346.771 309.404  1.00 32.86           C  
ATOM   1378  O   GLY A 179     273.832 346.349 309.923  1.00 34.56           O  
ATOM   1379  N   ARG A 180     271.761 346.018 309.158  1.00 33.21           N  
ATOM   1380  CA  ARG A 180     271.736 344.612 309.452  1.00 31.85           C  
ATOM   1381  C   ARG A 180     272.458 343.829 308.391  1.00 32.10           C  
ATOM   1382  O   ARG A 180     272.661 344.316 307.271  1.00 33.30           O  
ATOM   1383  CB  ARG A 180     270.320 344.097 309.462  1.00 36.70           C  
ATOM   1384  CG  ARG A 180     269.684 344.095 308.075  1.00 38.88           C  
ATOM   1385  CD  ARG A 180     268.311 343.662 308.080  1.00 40.72           C  
ATOM   1386  NE  ARG A 180     268.204 342.249 308.387  1.00 44.27           N  
ATOM   1387  CZ  ARG A 180     267.058 341.554 308.432  1.00 52.98           C  
ATOM   1388  NH1 ARG A 180     265.915 342.148 308.189  1.00 49.22           N  
ATOM   1389  NH2 ARG A 180     267.078 340.258 308.714  1.00 51.13           N  
ATOM   1390  N   ILE A 181     272.799 342.596 308.738  1.00 33.91           N  
ATOM   1391  CA  ILE A 181     273.332 341.651 307.782  1.00 31.86           C  
ATOM   1392  C   ILE A 181     272.280 340.621 307.481  1.00 33.78           C  
ATOM   1393  O   ILE A 181     271.711 340.032 308.398  1.00 37.01           O  
ATOM   1394  CB  ILE A 181     274.593 340.933 308.261  1.00 28.42           C  
ATOM   1395  CG1 ILE A 181     275.649 341.938 308.470  1.00 31.54           C  
ATOM   1396  CG2 ILE A 181     275.015 339.889 307.223  1.00 31.90           C  
ATOM   1397  CD1 ILE A 181     276.901 341.451 309.127  1.00 36.18           C  
ATOM   1398  N   ALA A 182     271.996 340.424 306.211  1.00 30.55           N  
ATOM   1399  CA  ALA A 182     271.006 339.433 305.824  1.00 29.17           C  
ATOM   1400  C   ALA A 182     271.329 338.883 304.479  1.00 30.48           C  
ATOM   1401  O   ALA A 182     271.874 339.600 303.642  1.00 33.28           O  
ATOM   1402  CB  ALA A 182     269.634 340.045 305.802  1.00 34.73           C  
ATOM   1403  N   GLU A 183     270.981 337.635 304.242  1.00 29.46           N  
ATOM   1404  CA  GLU A 183     271.195 337.050 302.943  1.00 30.40           C  
ATOM   1405  C   GLU A 183     270.267 337.601 301.919  1.00 30.91           C  
ATOM   1406  O   GLU A 183     269.075 337.760 302.171  1.00 33.80           O  
ATOM   1407  CB  GLU A 183     271.053 335.543 303.009  1.00 30.62           C  
ATOM   1408  CG  GLU A 183     272.053 334.887 303.891  1.00 33.72           C  
ATOM   1409  CD  GLU A 183     271.635 334.884 305.316  1.00 41.49           C  
ATOM   1410  OE1 GLU A 183     270.619 335.477 305.621  1.00 39.54           O  
ATOM   1411  OE2 GLU A 183     272.323 334.310 306.115  1.00 46.74           O  
ATOM   1412  N   LYS A 184     270.804 337.849 300.750  1.00 29.82           N  
ATOM   1413  CA  LYS A 184     270.009 338.264 299.628  1.00 28.98           C  
ATOM   1414  C   LYS A 184     270.524 337.516 298.437  1.00 30.78           C  
ATOM   1415  O   LYS A 184     271.678 337.097 298.456  1.00 34.13           O  
ATOM   1416  CB  LYS A 184     270.141 339.746 299.376  1.00 30.10           C  
ATOM   1417  CG  LYS A 184     269.677 340.586 300.500  1.00 31.83           C  
ATOM   1418  CD  LYS A 184     269.696 342.028 300.126  1.00 34.24           C  
ATOM   1419  CE  LYS A 184     269.268 342.894 301.283  1.00 40.38           C  
ATOM   1420  NZ  LYS A 184     269.208 344.314 300.897  1.00 42.90           N  
ATOM   1421  N   PRO A 185     269.723 337.221 297.432  1.00 30.43           N  
ATOM   1422  CA  PRO A 185     270.212 336.719 296.196  1.00 31.46           C  
ATOM   1423  C   PRO A 185     271.116 337.762 295.618  1.00 33.55           C  
ATOM   1424  O   PRO A 185     270.761 338.938 295.588  1.00 34.93           O  
ATOM   1425  CB  PRO A 185     268.952 336.567 295.378  1.00 32.91           C  
ATOM   1426  CG  PRO A 185     267.894 336.421 296.395  1.00 37.46           C  
ATOM   1427  CD  PRO A 185     268.308 337.310 297.524  1.00 35.72           C  
ATOM   1428  N   ILE A 186     272.250 337.335 295.149  1.00 33.88           N  
ATOM   1429  CA  ILE A 186     273.201 338.182 294.479  1.00 33.36           C  
ATOM   1430  C   ILE A 186     273.642 337.476 293.247  1.00 36.01           C  
ATOM   1431  O   ILE A 186     273.486 336.260 293.141  1.00 38.22           O  
ATOM   1432  CB  ILE A 186     274.429 338.501 295.317  1.00 33.25           C  
ATOM   1433  CG1 ILE A 186     275.184 337.213 295.639  1.00 34.85           C  
ATOM   1434  CG2 ILE A 186     273.997 339.221 296.570  1.00 36.36           C  
ATOM   1435  CD1 ILE A 186     276.535 337.417 296.220  1.00 39.55           C  
ATOM   1436  N   VAL A 187     274.245 338.189 292.332  1.00 36.79           N  
ATOM   1437  CA  VAL A 187     274.816 337.455 291.244  1.00 35.67           C  
ATOM   1438  C   VAL A 187     276.294 337.531 291.440  1.00 38.64           C  
ATOM   1439  O   VAL A 187     276.866 338.602 291.638  1.00 38.57           O  
ATOM   1440  CB  VAL A 187     274.348 337.962 289.882  1.00 33.29           C  
ATOM   1441  CG1 VAL A 187     274.657 339.395 289.700  1.00 34.48           C  
ATOM   1442  CG2 VAL A 187     274.997 337.124 288.791  1.00 39.29           C  
ATOM   1443  N   ARG A 188     276.890 336.372 291.438  1.00 40.18           N  
ATOM   1444  CA  ARG A 188     278.295 336.207 291.644  1.00 43.35           C  
ATOM   1445  C   ARG A 188     278.811 335.496 290.438  1.00 45.51           C  
ATOM   1446  O   ARG A 188     278.351 334.400 290.117  1.00 44.85           O  
ATOM   1447  CB  ARG A 188     278.543 335.413 292.902  1.00 43.62           C  
ATOM   1448  CG  ARG A 188     279.973 335.147 293.226  1.00 46.02           C  
ATOM   1449  CD  ARG A 188     280.101 334.416 294.499  1.00 45.36           C  
ATOM   1450  NE  ARG A 188     279.799 335.241 295.677  1.00 38.49           N  
ATOM   1451  CZ  ARG A 188     279.551 334.747 296.910  1.00 37.21           C  
ATOM   1452  NH1 ARG A 188     279.522 333.450 297.109  1.00 36.48           N  
ATOM   1453  NH2 ARG A 188     279.347 335.556 297.936  1.00 35.32           N  
ATOM   1454  N   ASP A 189     279.756 336.099 289.758  1.00 48.04           N  
ATOM   1455  CA  ASP A 189     280.251 335.511 288.541  1.00 49.82           C  
ATOM   1456  C   ASP A 189     279.053 335.234 287.628  1.00 47.55           C  
ATOM   1457  O   ASP A 189     278.332 336.162 287.270  1.00 45.93           O  
ATOM   1458  CB  ASP A 189     281.055 334.261 288.872  1.00 52.21           C  
ATOM   1459  CG  ASP A 189     282.242 334.614 289.744  1.00 55.48           C  
ATOM   1460  OD1 ASP A 189     282.810 335.669 289.555  1.00 60.30           O  
ATOM   1461  OD2 ASP A 189     282.559 333.841 290.616  1.00 56.44           O  
ATOM   1462  N   GLY A 190     278.841 333.984 287.230  1.00 47.96           N  
ATOM   1463  CA  GLY A 190     277.736 333.648 286.337  1.00 47.57           C  
ATOM   1464  C   GLY A 190     276.528 333.006 287.022  1.00 45.27           C  
ATOM   1465  O   GLY A 190     275.648 332.474 286.343  1.00 45.25           O  
ATOM   1466  N   GLU A 191     276.492 333.001 288.345  1.00 44.46           N  
ATOM   1467  CA  GLU A 191     275.424 332.310 289.056  1.00 43.11           C  
ATOM   1468  C   GLU A 191     274.659 333.161 290.049  1.00 42.18           C  
ATOM   1469  O   GLU A 191     275.189 334.095 290.653  1.00 41.66           O  
ATOM   1470  CB  GLU A 191     276.004 331.113 289.801  1.00 46.26           C  
ATOM   1471  CG  GLU A 191     276.625 330.051 288.908  1.00 52.08           C  
ATOM   1472  CD  GLU A 191     277.161 328.876 289.681  1.00 61.67           C  
ATOM   1473  OE1 GLU A 191     277.127 328.927 290.886  1.00 59.97           O  
ATOM   1474  OE2 GLU A 191     277.601 327.929 289.070  1.00 65.37           O  
ATOM   1475  N   ILE A 192     273.402 332.805 290.263  1.00 39.26           N  
ATOM   1476  CA  ILE A 192     272.645 333.492 291.281  1.00 37.03           C  
ATOM   1477  C   ILE A 192     272.674 332.643 292.520  1.00 37.22           C  
ATOM   1478  O   ILE A 192     272.248 331.490 292.524  1.00 38.93           O  
ATOM   1479  CB  ILE A 192     271.230 333.816 290.818  1.00 35.70           C  
ATOM   1480  CG1 ILE A 192     271.345 334.733 289.586  1.00 37.75           C  
ATOM   1481  CG2 ILE A 192     270.455 334.464 291.968  1.00 39.13           C  
ATOM   1482  CD1 ILE A 192     270.066 335.005 288.862  1.00 39.25           C  
ATOM   1483  N   VAL A 193     273.260 333.221 293.540  1.00 35.28           N  
ATOM   1484  CA  VAL A 193     273.527 332.572 294.801  1.00 35.36           C  
ATOM   1485  C   VAL A 193     273.036 333.458 295.903  1.00 36.72           C  
ATOM   1486  O   VAL A 193     272.798 334.629 295.657  1.00 38.44           O  
ATOM   1487  CB  VAL A 193     275.042 332.358 294.941  1.00 35.10           C  
ATOM   1488  CG1 VAL A 193     275.547 331.498 293.806  1.00 40.37           C  
ATOM   1489  CG2 VAL A 193     275.765 333.701 294.918  1.00 39.42           C  
ATOM   1490  N   ALA A 194     272.867 332.952 297.111  1.00 32.68           N  
ATOM   1491  CA  ALA A 194     272.524 333.886 298.170  1.00 32.64           C  
ATOM   1492  C   ALA A 194     273.744 334.119 299.012  1.00 31.28           C  
ATOM   1493  O   ALA A 194     274.556 333.214 299.199  1.00 33.90           O  
ATOM   1494  CB  ALA A 194     271.369 333.396 299.011  1.00 36.56           C  
ATOM   1495  N   ALA A 195     273.869 335.313 299.538  1.00 28.85           N  
ATOM   1496  CA  ALA A 195     274.982 335.606 300.406  1.00 27.09           C  
ATOM   1497  C   ALA A 195     274.605 336.717 301.332  1.00 28.52           C  
ATOM   1498  O   ALA A 195     273.821 337.567 300.924  1.00 32.78           O  
ATOM   1499  CB  ALA A 195     276.166 336.023 299.573  1.00 30.86           C  
ATOM   1500  N   PRO A 196     275.142 336.774 302.553  1.00 27.55           N  
ATOM   1501  CA  PRO A 196     274.901 337.827 303.493  1.00 28.08           C  
ATOM   1502  C   PRO A 196     275.435 339.113 302.972  1.00 28.40           C  
ATOM   1503  O   PRO A 196     276.597 339.168 302.564  1.00 31.56           O  
ATOM   1504  CB  PRO A 196     275.658 337.354 304.718  1.00 29.60           C  
ATOM   1505  CG  PRO A 196     276.681 336.419 304.200  1.00 29.84           C  
ATOM   1506  CD  PRO A 196     276.052 335.750 303.024  1.00 29.33           C  
ATOM   1507  N   MET A 197     274.627 340.143 303.077  1.00 29.01           N  
ATOM   1508  CA  MET A 197     275.006 341.457 302.649  1.00 26.89           C  
ATOM   1509  C   MET A 197     274.862 342.405 303.792  1.00 28.12           C  
ATOM   1510  O   MET A 197     273.931 342.284 304.588  1.00 31.80           O  
ATOM   1511  CB  MET A 197     274.109 341.932 301.525  1.00 29.60           C  
ATOM   1512  CG  MET A 197     274.070 341.048 300.323  1.00 30.12           C  
ATOM   1513  SD  MET A 197     275.623 340.909 299.493  1.00 37.99           S  
ATOM   1514  CE  MET A 197     275.935 342.549 298.866  1.00 36.96           C  
ATOM   1515  N   LEU A 198     275.757 343.359 303.877  1.00 27.88           N  
ATOM   1516  CA  LEU A 198     275.660 344.381 304.894  1.00 28.17           C  
ATOM   1517  C   LEU A 198     275.212 345.702 304.322  1.00 30.67           C  
ATOM   1518  O   LEU A 198     275.833 346.239 303.400  1.00 33.52           O  
ATOM   1519  CB  LEU A 198     276.990 344.543 305.612  1.00 29.30           C  
ATOM   1520  CG  LEU A 198     277.069 345.688 306.620  1.00 30.67           C  
ATOM   1521  CD1 LEU A 198     276.093 345.480 307.742  1.00 35.20           C  
ATOM   1522  CD2 LEU A 198     278.476 345.734 307.175  1.00 32.23           C  
ATOM   1523  N   ALA A 199     274.125 346.242 304.855  1.00 29.21           N  
ATOM   1524  CA  ALA A 199     273.669 347.530 304.346  1.00 28.15           C  
ATOM   1525  C   ALA A 199     274.514 348.647 304.935  1.00 29.67           C  
ATOM   1526  O   ALA A 199     274.611 348.794 306.156  1.00 34.87           O  
ATOM   1527  CB  ALA A 199     272.207 347.749 304.678  1.00 34.24           C  
ATOM   1528  N   LEU A 200     275.081 349.485 304.085  1.00 30.02           N  
ATOM   1529  CA  LEU A 200     275.904 350.587 304.567  1.00 29.92           C  
ATOM   1530  C   LEU A 200     275.304 351.928 304.222  1.00 30.85           C  
ATOM   1531  O   LEU A 200     274.773 352.115 303.123  1.00 34.90           O  
ATOM   1532  CB  LEU A 200     277.288 350.505 303.929  1.00 29.01           C  
ATOM   1533  CG  LEU A 200     278.078 349.222 304.180  1.00 29.73           C  
ATOM   1534  CD1 LEU A 200     279.325 349.235 303.340  1.00 30.29           C  
ATOM   1535  CD2 LEU A 200     278.455 349.126 305.639  1.00 31.58           C  
ATOM   1536  N   SER A 201     275.447 352.896 305.120  1.00 29.48           N  
ATOM   1537  CA  SER A 201     275.011 354.249 304.804  1.00 28.90           C  
ATOM   1538  C   SER A 201     276.013 355.291 305.251  1.00 29.88           C  
ATOM   1539  O   SER A 201     276.201 355.525 306.444  1.00 34.46           O  
ATOM   1540  CB  SER A 201     273.691 354.537 305.442  1.00 31.13           C  
ATOM   1541  OG  SER A 201     273.309 355.843 305.170  1.00 36.91           O  
ATOM   1542  N   LEU A 202     276.674 355.931 304.304  1.00 29.78           N  
ATOM   1543  CA  LEU A 202     277.693 356.906 304.670  1.00 29.25           C  
ATOM   1544  C   LEU A 202     277.207 358.318 304.521  1.00 33.28           C  
ATOM   1545  O   LEU A 202     276.752 358.709 303.455  1.00 39.32           O  
ATOM   1546  CB  LEU A 202     278.957 356.704 303.844  1.00 30.17           C  
ATOM   1547  CG  LEU A 202     280.087 357.727 304.048  1.00 29.15           C  
ATOM   1548  CD1 LEU A 202     280.619 357.654 305.466  1.00 33.60           C  
ATOM   1549  CD2 LEU A 202     281.197 357.421 303.063  1.00 33.52           C  
ATOM   1550  N   SER A 203     277.275 359.094 305.589  1.00 35.62           N  
ATOM   1551  CA  SER A 203     276.799 360.470 305.547  1.00 36.62           C  
ATOM   1552  C   SER A 203     277.932 361.443 305.706  1.00 40.59           C  
ATOM   1553  O   SER A 203     278.738 361.338 306.634  1.00 42.91           O  
ATOM   1554  CB  SER A 203     275.756 360.710 306.594  1.00 36.88           C  
ATOM   1555  OG  SER A 203     275.373 362.049 306.623  1.00 44.17           O  
ATOM   1556  N   PHE A 204     278.013 362.401 304.794  1.00 43.96           N  
ATOM   1557  CA  PHE A 204     279.099 363.365 304.853  1.00 45.47           C  
ATOM   1558  C   PHE A 204     278.675 364.805 304.612  1.00 50.11           C  
ATOM   1559  O   PHE A 204     277.611 365.097 304.050  1.00 55.14           O  
ATOM   1560  CB  PHE A 204     280.187 362.950 303.887  1.00 43.35           C  
ATOM   1561  CG  PHE A 204     279.769 362.967 302.494  1.00 43.43           C  
ATOM   1562  CD1 PHE A 204     279.986 364.060 301.709  1.00 51.73           C  
ATOM   1563  CD2 PHE A 204     279.134 361.885 301.946  1.00 42.30           C  
ATOM   1564  CE1 PHE A 204     279.592 364.064 300.400  1.00 53.52           C  
ATOM   1565  CE2 PHE A 204     278.741 361.905 300.645  1.00 44.58           C  
ATOM   1566  CZ  PHE A 204     278.977 362.989 299.873  1.00 47.71           C  
ATOM   1567  N   ASP A 205     279.515 365.708 305.119  1.00 53.68           N  
ATOM   1568  CA  ASP A 205     279.364 367.154 305.025  1.00 56.75           C  
ATOM   1569  C   ASP A 205     279.865 367.665 303.694  1.00 61.54           C  
ATOM   1570  O   ASP A 205     281.077 367.646 303.422  1.00 66.36           O  
ATOM   1571  CB  ASP A 205     280.125 367.809 306.170  1.00 64.13           C  
ATOM   1572  CG  ASP A 205     280.005 369.322 306.251  1.00 76.77           C  
ATOM   1573  OD1 ASP A 205     279.683 369.992 305.275  1.00 76.16           O  
ATOM   1574  OD2 ASP A 205     280.230 369.824 307.330  1.00 76.89           O  
ATOM   1575  N   HIS A 206     278.924 368.107 302.876  1.00 65.11           N  
ATOM   1576  CA  HIS A 206     279.149 368.485 301.494  1.00 65.99           C  
ATOM   1577  C   HIS A 206     280.075 369.687 301.351  1.00 73.28           C  
ATOM   1578  O   HIS A 206     280.588 369.953 300.267  1.00 74.81           O  
ATOM   1579  CB  HIS A 206     277.835 368.764 300.788  1.00 74.33           C  
ATOM   1580  CG  HIS A 206     277.880 368.561 299.342  1.00 70.52           C  
ATOM   1581  ND1 HIS A 206     276.845 368.913 298.522  1.00 73.38           N  
ATOM   1582  CD2 HIS A 206     278.819 368.005 298.549  1.00 75.09           C  
ATOM   1583  CE1 HIS A 206     277.142 368.573 297.287  1.00 75.83           C  
ATOM   1584  NE2 HIS A 206     278.332 368.022 297.282  1.00 76.33           N  
ATOM   1585  N   ARG A 207     280.240 370.473 302.416  1.00 76.31           N  
ATOM   1586  CA  ARG A 207     281.079 371.660 302.338  1.00 83.24           C  
ATOM   1587  C   ARG A 207     282.548 371.289 302.282  1.00 74.96           C  
ATOM   1588  O   ARG A 207     283.393 372.144 302.023  1.00 85.97           O  
ATOM   1589  CB  ARG A 207     280.920 372.533 303.556  1.00 86.90           C  
ATOM   1590  CG  ARG A 207     279.575 373.136 303.751  1.00 92.45           C  
ATOM   1591  CD  ARG A 207     279.525 373.888 305.002  1.00 95.39           C  
ATOM   1592  NE  ARG A 207     279.738 373.019 306.122  1.00 88.44           N  
ATOM   1593  CZ  ARG A 207     279.844 373.407 307.413  1.00 90.00           C  
ATOM   1594  NH1 ARG A 207     279.733 374.675 307.759  1.00 98.64           N  
ATOM   1595  NH2 ARG A 207     280.059 372.494 308.334  1.00 90.68           N  
ATOM   1596  N   MET A 208     282.886 370.055 302.642  1.00 72.78           N  
ATOM   1597  CA  MET A 208     284.284 369.665 302.643  1.00 72.42           C  
ATOM   1598  C   MET A 208     284.577 368.435 301.802  1.00 67.86           C  
ATOM   1599  O   MET A 208     285.643 368.325 301.182  1.00 77.90           O  
ATOM   1600  CB  MET A 208     284.762 369.461 304.063  1.00 76.08           C  
ATOM   1601  CG  MET A 208     284.787 370.736 304.863  1.00 83.11           C  
ATOM   1602  SD  MET A 208     285.259 370.499 306.555  1.00 91.16           S  
ATOM   1603  CE  MET A 208     287.015 370.188 306.512  1.00 86.85           C  
ATOM   1604  N   ILE A 209     283.665 367.485 301.792  1.00 65.45           N  
ATOM   1605  CA  ILE A 209     283.926 366.252 301.095  1.00 55.71           C  
ATOM   1606  C   ILE A 209     282.986 366.107 299.928  1.00 57.27           C  
ATOM   1607  O   ILE A 209     281.777 366.178 300.092  1.00 62.44           O  
ATOM   1608  CB  ILE A 209     283.790 365.083 302.065  1.00 55.39           C  
ATOM   1609  CG1 ILE A 209     284.815 365.276 303.185  1.00 58.00           C  
ATOM   1610  CG2 ILE A 209     283.997 363.750 301.329  1.00 54.62           C  
ATOM   1611  CD1 ILE A 209     284.659 364.367 304.337  1.00 56.81           C  
ATOM   1612  N   ASP A 210     283.518 365.896 298.742  1.00 53.40           N  
ATOM   1613  CA  ASP A 210     282.645 365.756 297.600  1.00 54.06           C  
ATOM   1614  C   ASP A 210     282.149 364.329 297.401  1.00 49.56           C  
ATOM   1615  O   ASP A 210     282.499 363.407 298.149  1.00 50.45           O  
ATOM   1616  CB  ASP A 210     283.343 366.316 296.357  1.00 56.95           C  
ATOM   1617  CG  ASP A 210     284.619 365.577 295.939  1.00 57.94           C  
ATOM   1618  OD1 ASP A 210     284.843 364.456 296.378  1.00 54.44           O  
ATOM   1619  OD2 ASP A 210     285.390 366.158 295.217  1.00 58.53           O  
ATOM   1620  N   GLY A 211     281.320 364.150 296.381  1.00 51.28           N  
ATOM   1621  CA  GLY A 211     280.728 362.863 296.087  1.00 47.21           C  
ATOM   1622  C   GLY A 211     281.752 361.811 295.762  1.00 44.26           C  
ATOM   1623  O   GLY A 211     281.744 360.726 296.352  1.00 43.68           O  
ATOM   1624  N   ALA A 212     282.637 362.102 294.821  1.00 46.26           N  
ATOM   1625  CA  ALA A 212     283.600 361.092 294.459  1.00 42.74           C  
ATOM   1626  C   ALA A 212     284.480 360.689 295.618  1.00 42.96           C  
ATOM   1627  O   ALA A 212     284.780 359.506 295.768  1.00 44.66           O  
ATOM   1628  CB  ALA A 212     284.469 361.588 293.336  1.00 48.49           C  
ATOM   1629  N   THR A 213     284.897 361.629 296.459  1.00 44.44           N  
ATOM   1630  CA  THR A 213     285.773 361.244 297.538  1.00 43.44           C  
ATOM   1631  C   THR A 213     285.057 360.368 298.529  1.00 41.93           C  
ATOM   1632  O   THR A 213     285.611 359.369 298.998  1.00 41.90           O  
ATOM   1633  CB  THR A 213     286.351 362.460 298.253  1.00 43.12           C  
ATOM   1634  OG1 THR A 213     287.099 363.237 297.323  1.00 46.22           O  
ATOM   1635  CG2 THR A 213     287.267 362.006 299.368  1.00 41.21           C  
ATOM   1636  N   ALA A 214     283.836 360.734 298.888  1.00 42.36           N  
ATOM   1637  CA  ALA A 214     283.129 359.936 299.849  1.00 37.98           C  
ATOM   1638  C   ALA A 214     282.872 358.551 299.311  1.00 37.30           C  
ATOM   1639  O   ALA A 214     282.987 357.570 300.048  1.00 40.86           O  
ATOM   1640  CB  ALA A 214     281.831 360.594 300.203  1.00 42.88           C  
ATOM   1641  N   GLN A 215     282.552 358.434 298.025  1.00 38.23           N  
ATOM   1642  CA  GLN A 215     282.300 357.115 297.513  1.00 35.29           C  
ATOM   1643  C   GLN A 215     283.564 356.305 297.494  1.00 39.22           C  
ATOM   1644  O   GLN A 215     283.523 355.117 297.800  1.00 42.62           O  
ATOM   1645  CB  GLN A 215     281.701 357.158 296.138  1.00 37.39           C  
ATOM   1646  CG  GLN A 215     281.318 355.809 295.597  1.00 39.50           C  
ATOM   1647  CD  GLN A 215     280.211 355.073 296.353  1.00 41.22           C  
ATOM   1648  OE1 GLN A 215     279.155 355.651 296.631  1.00 40.74           O  
ATOM   1649  NE2 GLN A 215     280.412 353.768 296.622  1.00 41.92           N  
ATOM   1650  N   LYS A 216     284.699 356.919 297.180  1.00 38.35           N  
ATOM   1651  CA  LYS A 216     285.931 356.161 297.172  1.00 38.23           C  
ATOM   1652  C   LYS A 216     286.246 355.643 298.557  1.00 40.53           C  
ATOM   1653  O   LYS A 216     286.706 354.504 298.706  1.00 41.15           O  
ATOM   1654  CB  LYS A 216     287.070 357.002 296.651  1.00 40.36           C  
ATOM   1655  CG  LYS A 216     287.015 357.269 295.181  1.00 41.86           C  
ATOM   1656  CD  LYS A 216     288.139 358.178 294.773  1.00 46.97           C  
ATOM   1657  CE  LYS A 216     288.093 358.487 293.299  1.00 50.93           C  
ATOM   1658  NZ  LYS A 216     289.186 359.416 292.899  1.00 49.05           N  
ATOM   1659  N   ALA A 217     286.004 356.460 299.577  1.00 38.60           N  
ATOM   1660  CA  ALA A 217     286.242 356.009 300.926  1.00 36.47           C  
ATOM   1661  C   ALA A 217     285.338 354.845 301.250  1.00 35.31           C  
ATOM   1662  O   ALA A 217     285.752 353.869 301.881  1.00 39.81           O  
ATOM   1663  CB  ALA A 217     286.009 357.125 301.895  1.00 37.58           C  
ATOM   1664  N   LEU A 218     284.111 354.906 300.773  1.00 33.95           N  
ATOM   1665  CA  LEU A 218     283.192 353.838 301.043  1.00 32.10           C  
ATOM   1666  C   LEU A 218     283.631 352.592 300.310  1.00 34.82           C  
ATOM   1667  O   LEU A 218     283.523 351.495 300.855  1.00 37.67           O  
ATOM   1668  CB  LEU A 218     281.776 354.245 300.659  1.00 33.46           C  
ATOM   1669  CG  LEU A 218     280.625 353.282 301.000  1.00 32.10           C  
ATOM   1670  CD1 LEU A 218     280.567 353.002 302.496  1.00 30.47           C  
ATOM   1671  CD2 LEU A 218     279.322 353.939 300.554  1.00 37.09           C  
ATOM   1672  N   ASN A 219     284.142 352.737 299.092  1.00 35.16           N  
ATOM   1673  CA  ASN A 219     284.563 351.578 298.335  1.00 35.83           C  
ATOM   1674  C   ASN A 219     285.706 350.888 299.039  1.00 37.67           C  
ATOM   1675  O   ASN A 219     285.784 349.659 299.046  1.00 39.28           O  
ATOM   1676  CB  ASN A 219     285.003 351.972 296.959  1.00 38.63           C  
ATOM   1677  CG  ASN A 219     283.896 352.402 296.106  1.00 40.52           C  
ATOM   1678  OD1 ASN A 219     282.722 352.104 296.351  1.00 40.48           O  
ATOM   1679  ND2 ASN A 219     284.251 353.109 295.081  1.00 43.27           N  
ATOM   1680  N   HIS A 220     286.568 351.675 299.666  1.00 37.34           N  
ATOM   1681  CA  HIS A 220     287.685 351.146 300.415  1.00 37.51           C  
ATOM   1682  C   HIS A 220     287.161 350.267 301.529  1.00 35.82           C  
ATOM   1683  O   HIS A 220     287.605 349.127 301.711  1.00 38.77           O  
ATOM   1684  CB  HIS A 220     288.499 352.283 300.996  1.00 40.10           C  
ATOM   1685  CG  HIS A 220     289.639 351.881 301.746  1.00 40.29           C  
ATOM   1686  ND1 HIS A 220     290.854 351.591 301.178  1.00 44.37           N  
ATOM   1687  CD2 HIS A 220     289.775 351.684 303.043  1.00 40.90           C  
ATOM   1688  CE1 HIS A 220     291.673 351.240 302.128  1.00 45.78           C  
ATOM   1689  NE2 HIS A 220     291.048 351.312 303.258  1.00 43.23           N  
ATOM   1690  N   ILE A 221     286.180 350.779 302.257  1.00 34.85           N  
ATOM   1691  CA  ILE A 221     285.608 350.028 303.348  1.00 32.70           C  
ATOM   1692  C   ILE A 221     284.952 348.765 302.851  1.00 32.61           C  
ATOM   1693  O   ILE A 221     285.129 347.709 303.459  1.00 36.60           O  
ATOM   1694  CB  ILE A 221     284.595 350.865 304.128  1.00 29.87           C  
ATOM   1695  CG1 ILE A 221     285.350 351.969 304.838  1.00 31.43           C  
ATOM   1696  CG2 ILE A 221     283.787 349.987 305.101  1.00 32.06           C  
ATOM   1697  CD1 ILE A 221     284.499 353.058 305.426  1.00 33.83           C  
ATOM   1698  N   LYS A 222     284.195 348.852 301.766  1.00 32.36           N  
ATOM   1699  CA  LYS A 222     283.526 347.675 301.256  1.00 31.88           C  
ATOM   1700  C   LYS A 222     284.521 346.587 300.896  1.00 34.57           C  
ATOM   1701  O   LYS A 222     284.295 345.412 301.210  1.00 36.64           O  
ATOM   1702  CB  LYS A 222     282.756 348.023 300.000  1.00 33.26           C  
ATOM   1703  CG  LYS A 222     281.533 348.884 300.208  1.00 35.93           C  
ATOM   1704  CD  LYS A 222     281.033 349.424 298.876  1.00 35.67           C  
ATOM   1705  CE  LYS A 222     280.257 348.422 298.103  1.00 35.20           C  
ATOM   1706  NZ  LYS A 222     279.906 348.923 296.771  1.00 38.88           N  
ATOM   1707  N   ARG A 223     285.637 346.963 300.262  1.00 35.58           N  
ATOM   1708  CA  ARG A 223     286.621 345.963 299.884  1.00 35.35           C  
ATOM   1709  C   ARG A 223     287.248 345.302 301.072  1.00 35.36           C  
ATOM   1710  O   ARG A 223     287.510 344.103 301.049  1.00 38.68           O  
ATOM   1711  CB  ARG A 223     287.748 346.541 299.068  1.00 37.44           C  
ATOM   1712  CG  ARG A 223     287.401 346.925 297.685  1.00 43.50           C  
ATOM   1713  CD  ARG A 223     288.612 347.166 296.884  1.00 46.85           C  
ATOM   1714  NE  ARG A 223     289.427 348.256 297.414  1.00 46.28           N  
ATOM   1715  CZ  ARG A 223     289.268 349.566 297.133  1.00 48.78           C  
ATOM   1716  NH1 ARG A 223     288.301 349.977 296.343  1.00 49.02           N  
ATOM   1717  NH2 ARG A 223     290.099 350.446 297.653  1.00 48.94           N  
ATOM   1718  N   LEU A 224     287.526 346.058 302.112  1.00 33.59           N  
ATOM   1719  CA  LEU A 224     288.126 345.425 303.254  1.00 31.62           C  
ATOM   1720  C   LEU A 224     287.165 344.548 304.018  1.00 34.81           C  
ATOM   1721  O   LEU A 224     287.532 343.461 304.454  1.00 37.40           O  
ATOM   1722  CB  LEU A 224     288.671 346.470 304.183  1.00 33.06           C  
ATOM   1723  CG  LEU A 224     289.850 347.255 303.677  1.00 35.06           C  
ATOM   1724  CD1 LEU A 224     290.114 348.364 304.623  1.00 39.04           C  
ATOM   1725  CD2 LEU A 224     291.083 346.368 303.573  1.00 38.11           C  
ATOM   1726  N   LEU A 225     285.911 344.954 304.153  1.00 33.39           N  
ATOM   1727  CA  LEU A 225     285.002 344.125 304.919  1.00 30.92           C  
ATOM   1728  C   LEU A 225     284.744 342.817 304.235  1.00 32.38           C  
ATOM   1729  O   LEU A 225     284.586 341.797 304.896  1.00 35.48           O  
ATOM   1730  CB  LEU A 225     283.685 344.829 305.184  1.00 31.10           C  
ATOM   1731  CG  LEU A 225     283.733 346.017 306.136  1.00 33.06           C  
ATOM   1732  CD1 LEU A 225     282.369 346.666 306.153  1.00 34.88           C  
ATOM   1733  CD2 LEU A 225     284.133 345.577 307.551  1.00 34.98           C  
ATOM   1734  N   SER A 226     284.761 342.807 302.917  1.00 32.98           N  
ATOM   1735  CA  SER A 226     284.526 341.584 302.184  1.00 32.99           C  
ATOM   1736  C   SER A 226     285.683 340.589 302.310  1.00 38.17           C  
ATOM   1737  O   SER A 226     285.531 339.444 301.890  1.00 37.68           O  
ATOM   1738  CB  SER A 226     284.285 341.864 300.725  1.00 36.49           C  
ATOM   1739  OG  SER A 226     285.461 342.248 300.077  1.00 40.45           O  
ATOM   1740  N   ASP A 227     286.857 341.006 302.835  1.00 39.09           N  
ATOM   1741  CA  ASP A 227     287.998 340.099 302.970  1.00 38.03           C  
ATOM   1742  C   ASP A 227     288.886 340.462 304.187  1.00 35.32           C  
ATOM   1743  O   ASP A 227     289.930 341.124 304.037  1.00 38.03           O  
ATOM   1744  CB  ASP A 227     288.840 340.076 301.705  1.00 39.66           C  
ATOM   1745  CG  ASP A 227     289.910 338.976 301.767  1.00 44.83           C  
ATOM   1746  OD1 ASP A 227     290.141 338.468 302.851  1.00 43.54           O  
ATOM   1747  OD2 ASP A 227     290.429 338.591 300.732  1.00 47.51           O  
ATOM   1748  N   PRO A 228     288.514 339.986 305.387  1.00 34.05           N  
ATOM   1749  CA  PRO A 228     289.105 340.277 306.671  1.00 34.30           C  
ATOM   1750  C   PRO A 228     290.585 339.993 306.775  1.00 39.96           C  
ATOM   1751  O   PRO A 228     291.268 340.609 307.587  1.00 41.78           O  
ATOM   1752  CB  PRO A 228     288.378 339.308 307.588  1.00 36.10           C  
ATOM   1753  CG  PRO A 228     287.099 339.063 306.922  1.00 35.57           C  
ATOM   1754  CD  PRO A 228     287.384 339.073 305.474  1.00 35.07           C  
ATOM   1755  N   GLU A 229     291.114 339.079 305.983  1.00 39.89           N  
ATOM   1756  CA  GLU A 229     292.520 338.790 306.143  1.00 38.98           C  
ATOM   1757  C   GLU A 229     293.371 339.946 305.678  1.00 37.74           C  
ATOM   1758  O   GLU A 229     294.463 340.181 306.207  1.00 40.42           O  
ATOM   1759  CB  GLU A 229     292.861 337.520 305.420  1.00 38.97           C  
ATOM   1760  CG  GLU A 229     292.212 336.306 306.027  1.00 45.14           C  
ATOM   1761  CD  GLU A 229     292.498 335.083 305.250  1.00 52.19           C  
ATOM   1762  OE1 GLU A 229     293.274 335.170 304.333  1.00 52.60           O  
ATOM   1763  OE2 GLU A 229     291.930 334.065 305.524  1.00 56.33           O  
ATOM   1764  N   LEU A 230     292.888 340.664 304.675  1.00 37.11           N  
ATOM   1765  CA  LEU A 230     293.654 341.762 304.164  1.00 34.54           C  
ATOM   1766  C   LEU A 230     293.484 342.899 305.116  1.00 35.20           C  
ATOM   1767  O   LEU A 230     294.379 343.712 305.299  1.00 39.67           O  
ATOM   1768  CB  LEU A 230     293.214 342.136 302.765  1.00 36.10           C  
ATOM   1769  CG  LEU A 230     294.014 343.246 302.070  1.00 39.30           C  
ATOM   1770  CD1 LEU A 230     295.501 342.873 301.965  1.00 41.90           C  
ATOM   1771  CD2 LEU A 230     293.428 343.448 300.692  1.00 44.79           C  
ATOM   1772  N   LEU A 231     292.319 342.957 305.730  1.00 36.01           N  
ATOM   1773  CA  LEU A 231     292.056 343.981 306.715  1.00 35.37           C  
ATOM   1774  C   LEU A 231     292.982 343.849 307.911  1.00 37.78           C  
ATOM   1775  O   LEU A 231     293.479 344.851 308.422  1.00 40.13           O  
ATOM   1776  CB  LEU A 231     290.604 343.894 307.180  1.00 35.50           C  
ATOM   1777  CG  LEU A 231     290.155 344.845 308.279  1.00 36.25           C  
ATOM   1778  CD1 LEU A 231     290.340 346.258 307.870  1.00 39.67           C  
ATOM   1779  CD2 LEU A 231     288.676 344.572 308.571  1.00 37.59           C  
ATOM   1780  N   LEU A 232     293.202 342.624 308.375  1.00 37.53           N  
ATOM   1781  CA  LEU A 232     294.074 342.412 309.518  1.00 35.60           C  
ATOM   1782  C   LEU A 232     295.549 342.722 309.275  1.00 38.20           C  
ATOM   1783  O   LEU A 232     296.225 343.207 310.184  1.00 39.60           O  
ATOM   1784  CB  LEU A 232     293.986 340.964 309.976  1.00 36.54           C  
ATOM   1785  CG  LEU A 232     292.687 340.499 310.619  1.00 37.35           C  
ATOM   1786  CD1 LEU A 232     292.746 338.998 310.790  1.00 41.37           C  
ATOM   1787  CD2 LEU A 232     292.503 341.136 311.965  1.00 39.09           C  
ATOM   1788  N   MET A 233     296.063 342.417 308.088  1.00 37.03           N  
ATOM   1789  CA  MET A 233     297.469 342.653 307.800  1.00 35.56           C  
ATOM   1790  C   MET A 233     297.821 344.095 307.479  1.00 38.02           C  
ATOM   1791  O   MET A 233     299.004 344.429 307.344  1.00 41.03           O  
ATOM   1792  CB  MET A 233     297.910 341.777 306.667  1.00 35.28           C  
ATOM   1793  CG  MET A 233     297.941 340.354 306.994  1.00 36.82           C  
ATOM   1794  SD  MET A 233     298.442 339.392 305.619  1.00 41.16           S  
ATOM   1795  CE  MET A 233     300.205 339.645 305.501  1.00 39.20           C  
TER    1796      MET A 233                                                      
MASTER     1083    0    0   11   14    0    0    6 1795    1    0   76          
END                                                                             
