HEADER    OXIDOREDUCTASE                          23-JUL-18   6H55              
TITLE     CORE OF THE HUMAN PYRUVATE DEHYDROGENASE (E2)                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF 
COMPND   3 PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL;                       
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: 70 KDA MITOCHONDRIAL AUTOANTIGEN OF PRIMARY BILIARY         
COMPND   6 CIRRHOSIS,PBC,DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF        
COMPND   7 PYRUVATE DEHYDROGENASE COMPLEX,M2 ANTIGEN COMPLEX 70 KDA SUBUNIT,    
COMPND   8 PYRUVATE DEHYDROGENASE COMPLEX COMPONENT E2,PDCE2;                   
COMPND   9 EC: 2.3.1.12;                                                        
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DLAT, DLTA;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PYRUVATE DEHYDROGENASE, HUMAN, OXIDOREDUCTASE                         
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    D.HASELBACH,S.PRAJAPATI,K.TITTMANN,H.STARK                            
REVDAT   4   18-DEC-19 6H55    1       SCALE                                    
REVDAT   3   10-JUL-19 6H55    1       JRNL                                     
REVDAT   2   12-JUN-19 6H55    1       REMARK                                   
REVDAT   1   05-JUN-19 6H55    0                                                
JRNL        AUTH   S.PRAJAPATI,D.HASELBACH,S.WITTIG,M.S.PATEL,A.CHARI,          
JRNL        AUTH 2 C.SCHMIDT,H.STARK,K.TITTMANN                                 
JRNL        TITL   STRUCTURAL AND FUNCTIONAL ANALYSES OF THE HUMAN PDH COMPLEX  
JRNL        TITL 2 SUGGEST A "DIVISION-OF-LABOR" MECHANISM BY LOCAL E1 AND E3   
JRNL        TITL 3 CLUSTERS.                                                    
JRNL        REF    STRUCTURE                     V.  27  1124 2019              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   31130485                                                     
JRNL        DOI    10.1016/J.STR.2019.04.009                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    6.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
REMARK   3   RECONSTRUCTION SCHEMA  : FOURIER SPACE                             
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
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)  : 6.000                          
REMARK   3   NUMBER OF PARTICLES               : 29788                          
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 6H55 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUL-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200011041.                                   
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                 : SINGLE PARTICLE CRYO EM-DERIVED   
REMARK 245                                    MAP OF THE FULL-LENGTH NATIVE     
REMARK 245                                    HUMAN E2-E3BP CORE OF THE         
REMARK 245                                    PYRUVATE DEHYDROGENASE            
REMARK 245                                    MULTIENZYME COMPLEX               
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 8.00                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : 2250                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : FEI FALCON II (4K X 4K)        
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 0.01                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 41.00                          
REMARK 245   ILLUMINATION MODE                 : SPOT SCAN                      
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 60-MERIC                   
REMARK 350 SOFTWARE USED: UCSF CHIMERA 1.12_B41600.                             
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  0.500000 -0.809017      161.90000            
REMARK 350   BIOMT2   2  0.500000 -0.809017 -0.309017      261.95970            
REMARK 350   BIOMT3   2 -0.809017 -0.309017 -0.500000      423.85970            
REMARK 350   BIOMT1   3  0.000000  0.000000 -1.000000      323.80000            
REMARK 350   BIOMT2   3 -1.000000  0.000000  0.000000      323.80000            
REMARK 350   BIOMT3   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1   4 -0.309017  0.500000 -0.809017      261.95970            
REMARK 350   BIOMT2   4  0.500000  0.809017  0.309017     -100.05970            
REMARK 350   BIOMT3   4  0.809017 -0.309017 -0.500000      161.90000            
REMARK 350   BIOMT1   5 -0.809017  0.309017 -0.500000      323.80000            
REMARK 350   BIOMT2   5 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT3   5  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1   6  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2   6  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT3   6  0.309017 -0.500000 -0.809017      323.80000            
REMARK 350   BIOMT1   7  0.309017 -0.500000 -0.809017      323.80000            
REMARK 350   BIOMT2   7 -0.500000 -0.809017  0.309017      323.80000            
REMARK 350   BIOMT3   7 -0.809017  0.309017 -0.500000      323.80000            
REMARK 350   BIOMT1   8 -0.309017 -0.500000 -0.809017      423.85970            
REMARK 350   BIOMT2   8  0.500000 -0.809017  0.309017      161.90000            
REMARK 350   BIOMT3   8 -0.809017 -0.309017  0.500000      261.95970            
REMARK 350   BIOMT1   9 -0.500000  0.809017 -0.309017      161.90000            
REMARK 350   BIOMT2   9 -0.809017 -0.309017  0.500000      261.95970            
REMARK 350   BIOMT3   9  0.309017  0.500000  0.809017     -100.05970            
REMARK 350   BIOMT1  10  0.809017  0.309017 -0.500000       61.84030            
REMARK 350   BIOMT2  10  0.309017  0.500000  0.809017     -100.05970            
REMARK 350   BIOMT3  10  0.500000 -0.809017  0.309017      161.90000            
REMARK 350   BIOMT1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  11  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3  11  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  12  0.809017 -0.309017 -0.500000      161.90000            
REMARK 350   BIOMT2  12  0.309017 -0.500000  0.809017       61.84030            
REMARK 350   BIOMT3  12 -0.500000 -0.809017 -0.309017      423.85970            
REMARK 350   BIOMT1  13 -0.809017 -0.309017 -0.500000      423.85970            
REMARK 350   BIOMT2  13 -0.309017 -0.500000  0.809017      161.90000            
REMARK 350   BIOMT3  13 -0.500000  0.809017  0.309017       61.84030            
REMARK 350   BIOMT1  14 -0.500000 -0.809017  0.309017      323.80000            
REMARK 350   BIOMT2  14  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT3  14 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT1  15 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  15 -0.500000 -0.809017  0.309017      323.80000            
REMARK 350   BIOMT3  15  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  16  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  16 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  16 -0.500000 -0.809017  0.309017      323.80000            
REMARK 350   BIOMT1  17  0.809017  0.309017  0.500000     -100.05970            
REMARK 350   BIOMT2  17 -0.309017 -0.500000  0.809017      161.90000            
REMARK 350   BIOMT3  17  0.500000 -0.809017 -0.309017      261.95970            
REMARK 350   BIOMT1  18  0.000000 -1.000000  0.000000      323.80000            
REMARK 350   BIOMT2  18  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3  18 -1.000000  0.000000  0.000000      323.80000            
REMARK 350   BIOMT1  19 -0.809017  0.309017  0.500000      161.90000            
REMARK 350   BIOMT2  19  0.309017 -0.500000  0.809017       61.84030            
REMARK 350   BIOMT3  19  0.500000  0.809017  0.309017     -100.05970            
REMARK 350   BIOMT1  20  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2  20  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  20  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1  21  0.309017 -0.500000  0.809017       61.84030            
REMARK 350   BIOMT2  21 -0.500000 -0.809017 -0.309017      423.85970            
REMARK 350   BIOMT3  21  0.809017 -0.309017 -0.500000      161.90000            
REMARK 350   BIOMT1  22 -0.309017 -0.500000  0.809017      161.90000            
REMARK 350   BIOMT2  22 -0.500000  0.809017  0.309017       61.84030            
REMARK 350   BIOMT3  22 -0.809017 -0.309017 -0.500000      423.85970            
REMARK 350   BIOMT1  23  0.500000 -0.809017  0.309017      161.90000            
REMARK 350   BIOMT2  23 -0.809017 -0.309017  0.500000      261.95970            
REMARK 350   BIOMT3  23 -0.309017 -0.500000 -0.809017      423.85970            
REMARK 350   BIOMT1  24 -0.809017 -0.309017  0.500000      261.95970            
REMARK 350   BIOMT2  24  0.309017  0.500000  0.809017     -100.05970            
REMARK 350   BIOMT3  24 -0.500000  0.809017 -0.309017      161.90000            
REMARK 350   BIOMT1  25  0.309017  0.500000  0.809017     -100.05970            
REMARK 350   BIOMT2  25  0.500000 -0.809017  0.309017      161.90000            
REMARK 350   BIOMT3  25  0.809017  0.309017 -0.500000       61.84030            
REMARK 350   BIOMT1  26  0.500000  0.809017  0.309017     -100.05970            
REMARK 350   BIOMT2  26  0.809017 -0.309017 -0.500000      161.90000            
REMARK 350   BIOMT3  26 -0.309017  0.500000 -0.809017      261.95970            
REMARK 350   BIOMT1  27  0.500000 -0.809017 -0.309017      261.95970            
REMARK 350   BIOMT2  27 -0.809017 -0.309017 -0.500000      423.85970            
REMARK 350   BIOMT3  27  0.309017  0.500000 -0.809017      161.90000            
REMARK 350   BIOMT1  28 -1.000000  0.000000  0.000000      323.80000            
REMARK 350   BIOMT2  28  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3  28  0.000000  0.000000 -1.000000      323.80000            
REMARK 350   BIOMT1  29 -0.500000 -0.809017 -0.309017      423.85970            
REMARK 350   BIOMT2  29 -0.809017  0.309017  0.500000      161.90000            
REMARK 350   BIOMT3  29 -0.309017  0.500000 -0.809017      261.95970            
REMARK 350   BIOMT1  30 -0.500000  0.809017  0.309017       61.84030            
REMARK 350   BIOMT2  30  0.809017  0.309017  0.500000     -100.05970            
REMARK 350   BIOMT3  30  0.309017  0.500000 -0.809017      161.90000            
REMARK 350   BIOMT1  31  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2  31  0.000000 -1.000000  0.000000      323.80000            
REMARK 350   BIOMT3  31  0.000000  0.000000 -1.000000      323.80000            
REMARK 350   BIOMT1  32  0.309017  0.500000 -0.809017      161.90000            
REMARK 350   BIOMT2  32 -0.500000  0.809017  0.309017       61.84030            
REMARK 350   BIOMT3  32  0.809017  0.309017  0.500000     -100.05970            
REMARK 350   BIOMT1  33  0.000000  0.000000 -1.000000      323.80000            
REMARK 350   BIOMT2  33  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  33  0.000000 -1.000000  0.000000      323.80000            
REMARK 350   BIOMT1  34 -0.309017  0.500000 -0.809017      261.95970            
REMARK 350   BIOMT2  34 -0.500000 -0.809017 -0.309017      423.85970            
REMARK 350   BIOMT3  34 -0.809017  0.309017  0.500000      161.90000            
REMARK 350   BIOMT1  35 -0.809017  0.309017 -0.500000      323.80000            
REMARK 350   BIOMT2  35  0.309017 -0.500000 -0.809017      323.80000            
REMARK 350   BIOMT3  35 -0.500000 -0.809017  0.309017      323.80000            
REMARK 350   BIOMT1  36  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  36 -0.809017  0.309017 -0.500000      323.80000            
REMARK 350   BIOMT3  36 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT1  37  0.309017 -0.500000 -0.809017      323.80000            
REMARK 350   BIOMT2  37  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  37  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  38 -0.309017 -0.500000 -0.809017      423.85970            
REMARK 350   BIOMT2  38 -0.500000  0.809017 -0.309017      161.90000            
REMARK 350   BIOMT3  38  0.809017  0.309017 -0.500000       61.84030            
REMARK 350   BIOMT1  39 -0.500000  0.809017 -0.309017      161.90000            
REMARK 350   BIOMT2  39  0.809017  0.309017 -0.500000       61.84030            
REMARK 350   BIOMT3  39 -0.309017 -0.500000 -0.809017      423.85970            
REMARK 350   BIOMT1  40  0.809017  0.309017 -0.500000       61.84030            
REMARK 350   BIOMT2  40 -0.309017 -0.500000 -0.809017      423.85970            
REMARK 350   BIOMT3  40 -0.500000  0.809017 -0.309017      161.90000            
REMARK 350   BIOMT1  41  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  41  0.000000  0.000000 -1.000000      323.80000            
REMARK 350   BIOMT3  41 -1.000000  0.000000  0.000000      323.80000            
REMARK 350   BIOMT1  42  0.809017 -0.309017 -0.500000      161.90000            
REMARK 350   BIOMT2  42 -0.309017  0.500000 -0.809017      261.95970            
REMARK 350   BIOMT3  42  0.500000  0.809017  0.309017     -100.05970            
REMARK 350   BIOMT1  43 -0.809017 -0.309017 -0.500000      423.85970            
REMARK 350   BIOMT2  43  0.309017  0.500000 -0.809017      161.90000            
REMARK 350   BIOMT3  43  0.500000 -0.809017 -0.309017      261.95970            
REMARK 350   BIOMT1  44 -0.500000 -0.809017  0.309017      323.80000            
REMARK 350   BIOMT2  44 -0.809017  0.309017 -0.500000      323.80000            
REMARK 350   BIOMT3  44  0.309017 -0.500000 -0.809017      323.80000            
REMARK 350   BIOMT1  45 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  45  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  45 -0.809017  0.309017 -0.500000      323.80000            
REMARK 350   BIOMT1  46  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  46  0.309017 -0.500000 -0.809017      323.80000            
REMARK 350   BIOMT3  46  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  47  0.809017  0.309017  0.500000     -100.05970            
REMARK 350   BIOMT2  47  0.309017  0.500000 -0.809017      161.90000            
REMARK 350   BIOMT3  47 -0.500000  0.809017  0.309017       61.84030            
REMARK 350   BIOMT1  48  0.000000 -1.000000  0.000000      323.80000            
REMARK 350   BIOMT2  48  0.000000  0.000000 -1.000000      323.80000            
REMARK 350   BIOMT3  48  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  49 -0.809017  0.309017  0.500000      161.90000            
REMARK 350   BIOMT2  49 -0.309017  0.500000 -0.809017      261.95970            
REMARK 350   BIOMT3  49 -0.500000 -0.809017 -0.309017      423.85970            
REMARK 350   BIOMT1  50  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2  50 -1.000000  0.000000  0.000000      323.80000            
REMARK 350   BIOMT3  50  0.000000 -1.000000  0.000000      323.80000            
REMARK 350   BIOMT1  51  0.309017 -0.500000  0.809017       61.84030            
REMARK 350   BIOMT2  51  0.500000  0.809017  0.309017     -100.05970            
REMARK 350   BIOMT3  51 -0.809017  0.309017  0.500000      161.90000            
REMARK 350   BIOMT1  52 -0.309017 -0.500000  0.809017      161.90000            
REMARK 350   BIOMT2  52  0.500000 -0.809017 -0.309017      261.95970            
REMARK 350   BIOMT3  52  0.809017  0.309017  0.500000     -100.05970            
REMARK 350   BIOMT1  53  0.500000 -0.809017  0.309017      161.90000            
REMARK 350   BIOMT2  53  0.809017  0.309017 -0.500000       61.84030            
REMARK 350   BIOMT3  53  0.309017  0.500000  0.809017     -100.05970            
REMARK 350   BIOMT1  54 -0.809017 -0.309017  0.500000      261.95970            
REMARK 350   BIOMT2  54 -0.309017 -0.500000 -0.809017      423.85970            
REMARK 350   BIOMT3  54  0.500000 -0.809017  0.309017      161.90000            
REMARK 350   BIOMT1  55  0.309017  0.500000  0.809017     -100.05970            
REMARK 350   BIOMT2  55 -0.500000  0.809017 -0.309017      161.90000            
REMARK 350   BIOMT3  55 -0.809017 -0.309017  0.500000      261.95970            
REMARK 350   BIOMT1  56  0.500000  0.809017  0.309017     -100.05970            
REMARK 350   BIOMT2  56 -0.809017  0.309017  0.500000      161.90000            
REMARK 350   BIOMT3  56  0.309017 -0.500000  0.809017       61.84030            
REMARK 350   BIOMT1  57  0.500000 -0.809017 -0.309017      261.95970            
REMARK 350   BIOMT2  57  0.809017  0.309017  0.500000     -100.05970            
REMARK 350   BIOMT3  57 -0.309017 -0.500000  0.809017      161.90000            
REMARK 350   BIOMT1  58 -1.000000  0.000000  0.000000      323.80000            
REMARK 350   BIOMT2  58  0.000000 -1.000000  0.000000      323.80000            
REMARK 350   BIOMT3  58  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  59 -0.500000 -0.809017 -0.309017      423.85970            
REMARK 350   BIOMT2  59  0.809017 -0.309017 -0.500000      161.90000            
REMARK 350   BIOMT3  59  0.309017 -0.500000  0.809017       61.84030            
REMARK 350   BIOMT1  60 -0.500000  0.809017  0.309017       61.84030            
REMARK 350   BIOMT2  60 -0.809017 -0.309017 -0.500000      423.85970            
REMARK 350   BIOMT3  60 -0.309017 -0.500000  0.809017      161.90000            
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  -413                                                      
REMARK 465     TRP A  -412                                                      
REMARK 465     ARG A  -411                                                      
REMARK 465     VAL A  -410                                                      
REMARK 465     CYS A  -409                                                      
REMARK 465     ALA A  -408                                                      
REMARK 465     ARG A  -407                                                      
REMARK 465     ARG A  -406                                                      
REMARK 465     ALA A  -405                                                      
REMARK 465     GLN A  -404                                                      
REMARK 465     ASN A  -403                                                      
REMARK 465     VAL A  -402                                                      
REMARK 465     ALA A  -401                                                      
REMARK 465     PRO A  -400                                                      
REMARK 465     TRP A  -399                                                      
REMARK 465     ALA A  -398                                                      
REMARK 465     GLY A  -397                                                      
REMARK 465     LEU A  -396                                                      
REMARK 465     GLU A  -395                                                      
REMARK 465     ALA A  -394                                                      
REMARK 465     ARG A  -393                                                      
REMARK 465     TRP A  -392                                                      
REMARK 465     THR A  -391                                                      
REMARK 465     ALA A  -390                                                      
REMARK 465     LEU A  -389                                                      
REMARK 465     GLN A  -388                                                      
REMARK 465     GLU A  -387                                                      
REMARK 465     VAL A  -386                                                      
REMARK 465     PRO A  -385                                                      
REMARK 465     GLY A  -384                                                      
REMARK 465     THR A  -383                                                      
REMARK 465     PRO A  -382                                                      
REMARK 465     ARG A  -381                                                      
REMARK 465     VAL A  -380                                                      
REMARK 465     THR A  -379                                                      
REMARK 465     SER A  -378                                                      
REMARK 465     ARG A  -377                                                      
REMARK 465     SER A  -376                                                      
REMARK 465     GLY A  -375                                                      
REMARK 465     PRO A  -374                                                      
REMARK 465     ALA A  -373                                                      
REMARK 465     PRO A  -372                                                      
REMARK 465     ALA A  -371                                                      
REMARK 465     ARG A  -370                                                      
REMARK 465     ARG A  -369                                                      
REMARK 465     ASN A  -368                                                      
REMARK 465     SER A  -367                                                      
REMARK 465     VAL A  -366                                                      
REMARK 465     THR A  -365                                                      
REMARK 465     THR A  -364                                                      
REMARK 465     GLY A  -363                                                      
REMARK 465     TYR A  -362                                                      
REMARK 465     GLY A  -361                                                      
REMARK 465     GLY A  -360                                                      
REMARK 465     VAL A  -359                                                      
REMARK 465     ARG A  -358                                                      
REMARK 465     ALA A  -357                                                      
REMARK 465     LEU A  -356                                                      
REMARK 465     CYS A  -355                                                      
REMARK 465     GLY A  -354                                                      
REMARK 465     TRP A  -353                                                      
REMARK 465     THR A  -352                                                      
REMARK 465     PRO A  -351                                                      
REMARK 465     SER A  -350                                                      
REMARK 465     SER A  -349                                                      
REMARK 465     GLY A  -348                                                      
REMARK 465     ALA A  -347                                                      
REMARK 465     THR A  -346                                                      
REMARK 465     PRO A  -345                                                      
REMARK 465     ARG A  -344                                                      
REMARK 465     ASN A  -343                                                      
REMARK 465     ARG A  -342                                                      
REMARK 465     LEU A  -341                                                      
REMARK 465     LEU A  -340                                                      
REMARK 465     LEU A  -339                                                      
REMARK 465     GLN A  -338                                                      
REMARK 465     LEU A  -337                                                      
REMARK 465     LEU A  -336                                                      
REMARK 465     GLY A  -335                                                      
REMARK 465     SER A  -334                                                      
REMARK 465     PRO A  -333                                                      
REMARK 465     GLY A  -332                                                      
REMARK 465     ARG A  -331                                                      
REMARK 465     ARG A  -330                                                      
REMARK 465     TYR A  -329                                                      
REMARK 465     TYR A  -328                                                      
REMARK 465     SER A  -327                                                      
REMARK 465     LEU A  -326                                                      
REMARK 465     PRO A  -325                                                      
REMARK 465     PRO A  -324                                                      
REMARK 465     HIS A  -323                                                      
REMARK 465     GLN A  -322                                                      
REMARK 465     LYS A  -321                                                      
REMARK 465     VAL A  -320                                                      
REMARK 465     PRO A  -319                                                      
REMARK 465     LEU A  -318                                                      
REMARK 465     PRO A  -317                                                      
REMARK 465     SER A  -316                                                      
REMARK 465     LEU A  -315                                                      
REMARK 465     SER A  -314                                                      
REMARK 465     PRO A  -313                                                      
REMARK 465     THR A  -312                                                      
REMARK 465     MET A  -311                                                      
REMARK 465     GLN A  -310                                                      
REMARK 465     ALA A  -309                                                      
REMARK 465     GLY A  -308                                                      
REMARK 465     THR A  -307                                                      
REMARK 465     ILE A  -306                                                      
REMARK 465     ALA A  -305                                                      
REMARK 465     ARG A  -304                                                      
REMARK 465     TRP A  -303                                                      
REMARK 465     GLU A  -302                                                      
REMARK 465     LYS A  -301                                                      
REMARK 465     LYS A  -300                                                      
REMARK 465     GLU A  -299                                                      
REMARK 465     GLY A  -298                                                      
REMARK 465     ASP A  -297                                                      
REMARK 465     LYS A  -296                                                      
REMARK 465     ILE A  -295                                                      
REMARK 465     ASN A  -294                                                      
REMARK 465     GLU A  -293                                                      
REMARK 465     GLY A  -292                                                      
REMARK 465     ASP A  -291                                                      
REMARK 465     LEU A  -290                                                      
REMARK 465     ILE A  -289                                                      
REMARK 465     ALA A  -288                                                      
REMARK 465     GLU A  -287                                                      
REMARK 465     VAL A  -286                                                      
REMARK 465     GLU A  -285                                                      
REMARK 465     THR A  -284                                                      
REMARK 465     ASP A  -283                                                      
REMARK 465     LYS A  -282                                                      
REMARK 465     ALA A  -281                                                      
REMARK 465     THR A  -280                                                      
REMARK 465     VAL A  -279                                                      
REMARK 465     GLY A  -278                                                      
REMARK 465     PHE A  -277                                                      
REMARK 465     GLU A  -276                                                      
REMARK 465     SER A  -275                                                      
REMARK 465     LEU A  -274                                                      
REMARK 465     GLU A  -273                                                      
REMARK 465     GLU A  -272                                                      
REMARK 465     CYS A  -271                                                      
REMARK 465     TYR A  -270                                                      
REMARK 465     MET A  -269                                                      
REMARK 465     ALA A  -268                                                      
REMARK 465     LYS A  -267                                                      
REMARK 465     ILE A  -266                                                      
REMARK 465     LEU A  -265                                                      
REMARK 465     VAL A  -264                                                      
REMARK 465     ALA A  -263                                                      
REMARK 465     GLU A  -262                                                      
REMARK 465     GLY A  -261                                                      
REMARK 465     THR A  -260                                                      
REMARK 465     ARG A  -259                                                      
REMARK 465     ASP A  -258                                                      
REMARK 465     VAL A  -257                                                      
REMARK 465     PRO A  -256                                                      
REMARK 465     ILE A  -255                                                      
REMARK 465     GLY A  -254                                                      
REMARK 465     ALA A  -253                                                      
REMARK 465     ILE A  -252                                                      
REMARK 465     ILE A  -251                                                      
REMARK 465     CYS A  -250                                                      
REMARK 465     ILE A  -249                                                      
REMARK 465     THR A  -248                                                      
REMARK 465     VAL A  -247                                                      
REMARK 465     GLY A  -246                                                      
REMARK 465     LYS A  -245                                                      
REMARK 465     PRO A  -244                                                      
REMARK 465     GLU A  -243                                                      
REMARK 465     ASP A  -242                                                      
REMARK 465     ILE A  -241                                                      
REMARK 465     GLU A  -240                                                      
REMARK 465     ALA A  -239                                                      
REMARK 465     PHE A  -238                                                      
REMARK 465     LYS A  -237                                                      
REMARK 465     ASN A  -236                                                      
REMARK 465     TYR A  -235                                                      
REMARK 465     THR A  -234                                                      
REMARK 465     LEU A  -233                                                      
REMARK 465     ASP A  -232                                                      
REMARK 465     SER A  -231                                                      
REMARK 465     SER A  -230                                                      
REMARK 465     ALA A  -229                                                      
REMARK 465     ALA A  -228                                                      
REMARK 465     PRO A  -227                                                      
REMARK 465     THR A  -226                                                      
REMARK 465     PRO A  -225                                                      
REMARK 465     GLN A  -224                                                      
REMARK 465     ALA A  -223                                                      
REMARK 465     ALA A  -222                                                      
REMARK 465     PRO A  -221                                                      
REMARK 465     ALA A  -220                                                      
REMARK 465     PRO A  -219                                                      
REMARK 465     THR A  -218                                                      
REMARK 465     PRO A  -217                                                      
REMARK 465     ALA A  -216                                                      
REMARK 465     ALA A  -215                                                      
REMARK 465     THR A  -214                                                      
REMARK 465     ALA A  -213                                                      
REMARK 465     SER A  -212                                                      
REMARK 465     PRO A  -211                                                      
REMARK 465     PRO A  -210                                                      
REMARK 465     THR A  -209                                                      
REMARK 465     PRO A  -208                                                      
REMARK 465     SER A  -207                                                      
REMARK 465     ALA A  -206                                                      
REMARK 465     GLN A  -205                                                      
REMARK 465     ALA A  -204                                                      
REMARK 465     PRO A  -203                                                      
REMARK 465     GLY A  -202                                                      
REMARK 465     SER A  -201                                                      
REMARK 465     SER A  -200                                                      
REMARK 465     TYR A  -199                                                      
REMARK 465     PRO A  -198                                                      
REMARK 465     PRO A  -197                                                      
REMARK 465     HIS A  -196                                                      
REMARK 465     MET A  -195                                                      
REMARK 465     GLN A  -194                                                      
REMARK 465     VAL A  -193                                                      
REMARK 465     LEU A  -192                                                      
REMARK 465     LEU A  -191                                                      
REMARK 465     PRO A  -190                                                      
REMARK 465     ALA A  -189                                                      
REMARK 465     LEU A  -188                                                      
REMARK 465     SER A  -187                                                      
REMARK 465     PRO A  -186                                                      
REMARK 465     THR A  -185                                                      
REMARK 465     MET A  -184                                                      
REMARK 465     THR A  -183                                                      
REMARK 465     MET A  -182                                                      
REMARK 465     GLY A  -181                                                      
REMARK 465     THR A  -180                                                      
REMARK 465     VAL A  -179                                                      
REMARK 465     GLN A  -178                                                      
REMARK 465     ARG A  -177                                                      
REMARK 465     TRP A  -176                                                      
REMARK 465     GLU A  -175                                                      
REMARK 465     LYS A  -174                                                      
REMARK 465     LYS A  -173                                                      
REMARK 465     VAL A  -172                                                      
REMARK 465     GLY A  -171                                                      
REMARK 465     GLU A  -170                                                      
REMARK 465     LYS A  -169                                                      
REMARK 465     LEU A  -168                                                      
REMARK 465     SER A  -167                                                      
REMARK 465     GLU A  -166                                                      
REMARK 465     GLY A  -165                                                      
REMARK 465     ASP A  -164                                                      
REMARK 465     LEU A  -163                                                      
REMARK 465     LEU A  -162                                                      
REMARK 465     ALA A  -161                                                      
REMARK 465     GLU A  -160                                                      
REMARK 465     ILE A  -159                                                      
REMARK 465     GLU A  -158                                                      
REMARK 465     THR A  -157                                                      
REMARK 465     ASP A  -156                                                      
REMARK 465     LYS A  -155                                                      
REMARK 465     ALA A  -154                                                      
REMARK 465     THR A  -153                                                      
REMARK 465     ILE A  -152                                                      
REMARK 465     GLY A  -151                                                      
REMARK 465     PHE A  -150                                                      
REMARK 465     GLU A  -149                                                      
REMARK 465     VAL A  -148                                                      
REMARK 465     GLN A  -147                                                      
REMARK 465     GLU A  -146                                                      
REMARK 465     GLU A  -145                                                      
REMARK 465     GLY A  -144                                                      
REMARK 465     TYR A  -143                                                      
REMARK 465     LEU A  -142                                                      
REMARK 465     ALA A  -141                                                      
REMARK 465     LYS A  -140                                                      
REMARK 465     ILE A  -139                                                      
REMARK 465     LEU A  -138                                                      
REMARK 465     VAL A  -137                                                      
REMARK 465     PRO A  -136                                                      
REMARK 465     GLU A  -135                                                      
REMARK 465     GLY A  -134                                                      
REMARK 465     THR A  -133                                                      
REMARK 465     ARG A  -132                                                      
REMARK 465     ASP A  -131                                                      
REMARK 465     VAL A  -130                                                      
REMARK 465     PRO A  -129                                                      
REMARK 465     LEU A  -128                                                      
REMARK 465     GLY A  -127                                                      
REMARK 465     THR A  -126                                                      
REMARK 465     PRO A  -125                                                      
REMARK 465     LEU A  -124                                                      
REMARK 465     CYS A  -123                                                      
REMARK 465     ILE A  -122                                                      
REMARK 465     ILE A  -121                                                      
REMARK 465     VAL A  -120                                                      
REMARK 465     GLU A  -119                                                      
REMARK 465     LYS A  -118                                                      
REMARK 465     GLU A  -117                                                      
REMARK 465     ALA A  -116                                                      
REMARK 465     ASP A  -115                                                      
REMARK 465     ILE A  -114                                                      
REMARK 465     SER A  -113                                                      
REMARK 465     ALA A  -112                                                      
REMARK 465     PHE A  -111                                                      
REMARK 465     ALA A  -110                                                      
REMARK 465     ASP A  -109                                                      
REMARK 465     TYR A  -108                                                      
REMARK 465     ARG A  -107                                                      
REMARK 465     PRO A  -106                                                      
REMARK 465     THR A  -105                                                      
REMARK 465     GLU A  -104                                                      
REMARK 465     VAL A  -103                                                      
REMARK 465     THR A  -102                                                      
REMARK 465     ASP A  -101                                                      
REMARK 465     LEU A  -100                                                      
REMARK 465     LYS A   -99                                                      
REMARK 465     PRO A   -98                                                      
REMARK 465     GLN A   -97                                                      
REMARK 465     VAL A   -96                                                      
REMARK 465     PRO A   -95                                                      
REMARK 465     PRO A   -94                                                      
REMARK 465     PRO A   -93                                                      
REMARK 465     THR A   -92                                                      
REMARK 465     PRO A   -91                                                      
REMARK 465     PRO A   -90                                                      
REMARK 465     PRO A   -89                                                      
REMARK 465     VAL A   -88                                                      
REMARK 465     ALA A   -87                                                      
REMARK 465     ALA A   -86                                                      
REMARK 465     VAL A   -85                                                      
REMARK 465     PRO A   -84                                                      
REMARK 465     PRO A   -83                                                      
REMARK 465     THR A   -82                                                      
REMARK 465     PRO A   -81                                                      
REMARK 465     GLN A   -80                                                      
REMARK 465     PRO A   -79                                                      
REMARK 465     LEU A   -78                                                      
REMARK 465     ALA A   -77                                                      
REMARK 465     PRO A   -76                                                      
REMARK 465     THR A   -75                                                      
REMARK 465     PRO A   -74                                                      
REMARK 465     SER A   -73                                                      
REMARK 465     ALA A   -72                                                      
REMARK 465     PRO A   -71                                                      
REMARK 465     CYS A   -70                                                      
REMARK 465     PRO A   -69                                                      
REMARK 465     ALA A   -68                                                      
REMARK 465     THR A   -67                                                      
REMARK 465     PRO A   -66                                                      
REMARK 465     ALA A   -65                                                      
REMARK 465     GLY A   -64                                                      
REMARK 465     PRO A   -63                                                      
REMARK 465     LYS A   -62                                                      
REMARK 465     GLY A   -61                                                      
REMARK 465     ARG A   -60                                                      
REMARK 465     VAL A   -59                                                      
REMARK 465     PHE A   -58                                                      
REMARK 465     VAL A   -57                                                      
REMARK 465     SER A   -56                                                      
REMARK 465     PRO A   -55                                                      
REMARK 465     LEU A   -54                                                      
REMARK 465     ALA A   -53                                                      
REMARK 465     LYS A   -52                                                      
REMARK 465     LYS A   -51                                                      
REMARK 465     LEU A   -50                                                      
REMARK 465     ALA A   -49                                                      
REMARK 465     VAL A   -48                                                      
REMARK 465     GLU A   -47                                                      
REMARK 465     LYS A   -46                                                      
REMARK 465     GLY A   -45                                                      
REMARK 465     ILE A   -44                                                      
REMARK 465     ASP A   -43                                                      
REMARK 465     LEU A   -42                                                      
REMARK 465     THR A   -41                                                      
REMARK 465     GLN A   -40                                                      
REMARK 465     VAL A   -39                                                      
REMARK 465     LYS A   -38                                                      
REMARK 465     GLY A   -37                                                      
REMARK 465     THR A   -36                                                      
REMARK 465     GLY A   -35                                                      
REMARK 465     PRO A   -34                                                      
REMARK 465     ASP A   -33                                                      
REMARK 465     GLY A   -32                                                      
REMARK 465     ARG A   -31                                                      
REMARK 465     ILE A   -30                                                      
REMARK 465     THR A   -29                                                      
REMARK 465     LYS A   -28                                                      
REMARK 465     LYS A   -27                                                      
REMARK 465     ASP A   -26                                                      
REMARK 465     ILE A   -25                                                      
REMARK 465     ASP A   -24                                                      
REMARK 465     SER A   -23                                                      
REMARK 465     PHE A   -22                                                      
REMARK 465     VAL A   -21                                                      
REMARK 465     PRO A   -20                                                      
REMARK 465     SER A   -19                                                      
REMARK 465     LYS A   -18                                                      
REMARK 465     VAL A   -17                                                      
REMARK 465     ALA A   -16                                                      
REMARK 465     PRO A   -15                                                      
REMARK 465     ALA A   -14                                                      
REMARK 465     PRO A   -13                                                      
REMARK 465     ALA A   -12                                                      
REMARK 465     ALA A   -11                                                      
REMARK 465     VAL A   -10                                                      
REMARK 465     VAL A    -9                                                      
REMARK 465     PRO A    -8                                                      
REMARK 465     PRO A    -7                                                      
REMARK 465     THR A    -6                                                      
REMARK 465     GLY A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     MET A    -2                                                      
REMARK 465     ALA A    -1                                                      
REMARK 465     PRO A     0                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A   1    CB   CG1  CG2                                       
REMARK 470     PRO A   2    CB   CG   CD                                        
REMARK 470     THR A   3    CB   OG1  CG2                                       
REMARK 470     VAL A   5    CB   CG1  CG2                                       
REMARK 470     PHE A   6    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     THR A   7    CB   OG1  CG2                                       
REMARK 470     ASP A   8    CB   CG   OD1  OD2                                  
REMARK 470     ILE A   9    CB   CG1  CG2  CD1                                  
REMARK 470     PRO A  10    CB   CG   CD                                        
REMARK 470     ILE A  11    CB   CG1  CG2  CD1                                  
REMARK 470     SER A  12    CB   OG                                             
REMARK 470     ASN A  13    CB   CG   OD1  ND2                                  
REMARK 470     ILE A  14    CB   CG1  CG2  CD1                                  
REMARK 470     ARG A  15    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ARG A  16    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     VAL A  17    CB   CG1  CG2                                       
REMARK 470     ILE A  18    CB   CG1  CG2  CD1                                  
REMARK 470     ALA A  19    CB                                                  
REMARK 470     GLN A  20    CB   CG   CD   OE1  NE2                             
REMARK 470     ARG A  21    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LEU A  22    CB   CG   CD1  CD2                                  
REMARK 470     MET A  23    CB   CG   SD   CE                                   
REMARK 470     GLN A  24    CB   CG   CD   OE1  NE2                             
REMARK 470     SER A  25    CB   OG                                             
REMARK 470     LYS A  26    CB   CG   CD   CE   NZ                              
REMARK 470     GLN A  27    CB   CG   CD   OE1  NE2                             
REMARK 470     THR A  28    CB   OG1  CG2                                       
REMARK 470     ILE A  29    CB   CG1  CG2  CD1                                  
REMARK 470     PRO A  30    CB   CG   CD                                        
REMARK 470     HIS A  31    CB   CG   ND1  CD2  CE1  NE2                        
REMARK 470     TYR A  32    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     TYR A  32    OH                                                  
REMARK 470     TYR A  33    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     TYR A  33    OH                                                  
REMARK 470     LEU A  34    CB   CG   CD1  CD2                                  
REMARK 470     SER A  35    CB   OG                                             
REMARK 470     ILE A  36    CB   CG1  CG2  CD1                                  
REMARK 470     ASP A  37    CB   CG   OD1  OD2                                  
REMARK 470     VAL A  38    CB   CG1  CG2                                       
REMARK 470     ASN A  39    CB   CG   OD1  ND2                                  
REMARK 470     MET A  40    CB   CG   SD   CE                                   
REMARK 470     GLU A  42    CB   CG   CD   OE1  OE2                             
REMARK 470     VAL A  43    CB   CG1  CG2                                       
REMARK 470     LEU A  44    CB   CG   CD1  CD2                                  
REMARK 470     LEU A  45    CB   CG   CD1  CD2                                  
REMARK 470     VAL A  46    CB   CG1  CG2                                       
REMARK 470     ARG A  47    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LYS A  48    CB   CG   CD   CE   NZ                              
REMARK 470     GLU A  49    CB   CG   CD   OE1  OE2                             
REMARK 470     LEU A  50    CB   CG   CD1  CD2                                  
REMARK 470     ASN A  51    CB   CG   OD1  ND2                                  
REMARK 470     LYS A  52    CB   CG   CD   CE   NZ                              
REMARK 470     ILE A  53    CB   CG1  CG2  CD1                                  
REMARK 470     LEU A  54    CB   CG   CD1  CD2                                  
REMARK 470     GLU A  55    CB   CG   CD   OE1  OE2                             
REMARK 470     ARG A  57    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     SER A  58    CB   OG                                             
REMARK 470     LYS A  59    CB   CG   CD   CE   NZ                              
REMARK 470     ILE A  60    CB   CG1  CG2  CD1                                  
REMARK 470     SER A  61    CB   OG                                             
REMARK 470     VAL A  62    CB   CG1  CG2                                       
REMARK 470     ASN A  63    CB   CG   OD1  ND2                                  
REMARK 470     ASP A  64    CB   CG   OD1  OD2                                  
REMARK 470     PHE A  65    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     ILE A  66    CB   CG1  CG2  CD1                                  
REMARK 470     ILE A  67    CB   CG1  CG2  CD1                                  
REMARK 470     LYS A  68    CB   CG   CD   CE   NZ                              
REMARK 470     ALA A  69    CB                                                  
REMARK 470     SER A  70    CB   OG                                             
REMARK 470     ALA A  71    CB                                                  
REMARK 470     LEU A  72    CB   CG   CD1  CD2                                  
REMARK 470     ALA A  73    CB                                                  
REMARK 470     CYS A  74    CB   SG                                             
REMARK 470     LEU A  75    CB   CG   CD1  CD2                                  
REMARK 470     LYS A  76    CB   CG   CD   CE   NZ                              
REMARK 470     VAL A  77    CB   CG1  CG2                                       
REMARK 470     PRO A  78    CB   CG   CD                                        
REMARK 470     GLU A  79    CB   CG   CD   OE1  OE2                             
REMARK 470     ALA A  80    CB                                                  
REMARK 470     ASN A  81    CB   CG   OD1  ND2                                  
REMARK 470     SER A  82    CB   OG                                             
REMARK 470     SER A  83    CB   OG                                             
REMARK 470     TRP A  84    CB   CG   CD1  CD2  NE1  CE2  CE3                   
REMARK 470     TRP A  84    CZ2  CZ3  CH2                                       
REMARK 470     MET A  85    CB   CG   SD   CE                                   
REMARK 470     ASP A  86    CB   CG   OD1  OD2                                  
REMARK 470     THR A  87    CB   OG1  CG2                                       
REMARK 470     VAL A  88    CB   CG1  CG2                                       
REMARK 470     ILE A  89    CB   CG1  CG2  CD1                                  
REMARK 470     ARG A  90    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     GLN A  91    CB   CG   CD   OE1  NE2                             
REMARK 470     ASN A  92    CB   CG   OD1  ND2                                  
REMARK 470     HIS A  93    CB   CG   ND1  CD2  CE1  NE2                        
REMARK 470     VAL A  94    CB   CG1  CG2                                       
REMARK 470     VAL A  95    CB   CG1  CG2                                       
REMARK 470     ASP A  96    CB   CG   OD1  OD2                                  
REMARK 470     VAL A  97    CB   CG1  CG2                                       
REMARK 470     SER A  98    CB   OG                                             
REMARK 470     VAL A  99    CB   CG1  CG2                                       
REMARK 470     ALA A 100    CB                                                  
REMARK 470     VAL A 101    CB   CG1  CG2                                       
REMARK 470     SER A 102    CB   OG                                             
REMARK 470     THR A 103    CB   OG1  CG2                                       
REMARK 470     PRO A 104    CB   CG   CD                                        
REMARK 470     ALA A 105    CB                                                  
REMARK 470     LEU A 107    CB   CG   CD1  CD2                                  
REMARK 470     ILE A 108    CB   CG1  CG2  CD1                                  
REMARK 470     THR A 109    CB   OG1  CG2                                       
REMARK 470     PRO A 110    CB   CG   CD                                        
REMARK 470     ILE A 111    CB   CG1  CG2  CD1                                  
REMARK 470     VAL A 112    CB   CG1  CG2                                       
REMARK 470     PHE A 113    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     ASN A 114    CB   CG   OD1  ND2                                  
REMARK 470     ALA A 115    CB                                                  
REMARK 470     HIS A 116    CB   CG   ND1  CD2  CE1  NE2                        
REMARK 470     ILE A 117    CB   CG1  CG2  CD1                                  
REMARK 470     LYS A 118    CB   CG   CD   CE   NZ                              
REMARK 470     VAL A 120    CB   CG1  CG2                                       
REMARK 470     GLU A 121    CB   CG   CD   OE1  OE2                             
REMARK 470     THR A 122    CB   OG1  CG2                                       
REMARK 470     ILE A 123    CB   CG1  CG2  CD1                                  
REMARK 470     ALA A 124    CB                                                  
REMARK 470     ASN A 125    CB   CG   OD1  ND2                                  
REMARK 470     ASP A 126    CB   CG   OD1  OD2                                  
REMARK 470     VAL A 127    CB   CG1  CG2                                       
REMARK 470     VAL A 128    CB   CG1  CG2                                       
REMARK 470     SER A 129    CB   OG                                             
REMARK 470     LEU A 130    CB   CG   CD1  CD2                                  
REMARK 470     ALA A 131    CB                                                  
REMARK 470     THR A 132    CB   OG1  CG2                                       
REMARK 470     LYS A 133    CB   CG   CD   CE   NZ                              
REMARK 470     ALA A 134    CB                                                  
REMARK 470     ARG A 135    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     GLU A 136    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS A 138    CB   CG   CD   CE   NZ                              
REMARK 470     LEU A 139    CB   CG   CD1  CD2                                  
REMARK 470     GLN A 140    CB   CG   CD   OE1  NE2                             
REMARK 470     PRO A 141    CB   CG   CD                                        
REMARK 470     HIS A 142    CB   CG   ND1  CD2  CE1  NE2                        
REMARK 470     GLU A 143    CB   CG   CD   OE1  OE2                             
REMARK 470     PHE A 144    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     GLN A 145    CB   CG   CD   OE1  NE2                             
REMARK 470     THR A 148    CB   OG1  CG2                                       
REMARK 470     PHE A 149    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     THR A 150    CB   OG1  CG2                                       
REMARK 470     ILE A 151    CB   CG1  CG2  CD1                                  
REMARK 470     SER A 152    CB   OG                                             
REMARK 470     ASN A 153    CB   CG   OD1  ND2                                  
REMARK 470     LEU A 154    CB   CG   CD1  CD2                                  
REMARK 470     MET A 156    CB   CG   SD   CE                                   
REMARK 470     PHE A 157    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     ILE A 159    CB   CG1  CG2  CD1                                  
REMARK 470     LYS A 160    CB   CG   CD   CE   NZ                              
REMARK 470     ASN A 161    CB   CG   OD1  ND2                                  
REMARK 470     PHE A 162    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     SER A 163    CB   OG                                             
REMARK 470     ALA A 164    CB                                                  
REMARK 470     ILE A 165    CB   CG1  CG2  CD1                                  
REMARK 470     ILE A 166    CB   CG1  CG2  CD1                                  
REMARK 470     ASN A 167    CB   CG   OD1  ND2                                  
REMARK 470     PRO A 168    CB   CG   CD                                        
REMARK 470     PRO A 169    CB   CG   CD                                        
REMARK 470     GLN A 170    CB   CG   CD   OE1  NE2                             
REMARK 470     ALA A 171    CB                                                  
REMARK 470     CYS A 172    CB   SG                                             
REMARK 470     ILE A 173    CB   CG1  CG2  CD1                                  
REMARK 470     LEU A 174    CB   CG   CD1  CD2                                  
REMARK 470     ALA A 175    CB                                                  
REMARK 470     ILE A 176    CB   CG1  CG2  CD1                                  
REMARK 470     ALA A 178    CB                                                  
REMARK 470     SER A 179    CB   OG                                             
REMARK 470     GLU A 180    CB   CG   CD   OE1  OE2                             
REMARK 470     ASP A 181    CB   CG   OD1  OD2                                  
REMARK 470     LYS A 182    CB   CG   CD   CE   NZ                              
REMARK 470     LEU A 183    CB   CG   CD1  CD2                                  
REMARK 470     VAL A 184    CB   CG1  CG2                                       
REMARK 470     PRO A 185    CB   CG   CD                                        
REMARK 470     ALA A 186    CB                                                  
REMARK 470     ASP A 187    CB   CG   OD1  OD2                                  
REMARK 470     ASN A 188    CB   CG   OD1  ND2                                  
REMARK 470     GLU A 189    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS A 190    CB   CG   CD   CE   NZ                              
REMARK 470     PHE A 192    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     ASP A 193    CB   CG   OD1  OD2                                  
REMARK 470     VAL A 194    CB   CG1  CG2                                       
REMARK 470     ALA A 195    CB                                                  
REMARK 470     SER A 196    CB   OG                                             
REMARK 470     MET A 197    CB   CG   SD   CE                                   
REMARK 470     MET A 198    CB   CG   SD   CE                                   
REMARK 470     SER A 199    CB   OG                                             
REMARK 470     VAL A 200    CB   CG1  CG2                                       
REMARK 470     THR A 201    CB   OG1  CG2                                       
REMARK 470     LEU A 202    CB   CG   CD1  CD2                                  
REMARK 470     SER A 203    CB   OG                                             
REMARK 470     CYS A 204    CB   SG                                             
REMARK 470     ASP A 205    CB   CG   OD1  OD2                                  
REMARK 470     HIS A 206    CB   CG   ND1  CD2  CE1  NE2                        
REMARK 470     ARG A 207    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     VAL A 208    CB   CG1  CG2                                       
REMARK 470     VAL A 209    CB   CG1  CG2                                       
REMARK 470     ASP A 210    CB   CG   OD1  OD2                                  
REMARK 470     ALA A 212    CB                                                  
REMARK 470     VAL A 213    CB   CG1  CG2                                       
REMARK 470     ALA A 215    CB                                                  
REMARK 470     GLN A 216    CB   CG   CD   OE1  NE2                             
REMARK 470     TRP A 217    CB   CG   CD1  CD2  NE1  CE2  CE3                   
REMARK 470     TRP A 217    CZ2  CZ3  CH2                                       
REMARK 470     LEU A 218    CB   CG   CD1  CD2                                  
REMARK 470     ALA A 219    CB                                                  
REMARK 470     GLU A 220    CB   CG   CD   OE1  OE2                             
REMARK 470     PHE A 221    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     ARG A 222    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LYS A 223    CB   CG   CD   CE   NZ                              
REMARK 470     TYR A 224    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     TYR A 224    OH                                                  
REMARK 470     LEU A 225    CB   CG   CD1  CD2                                  
REMARK 470     GLU A 226    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS A 227    CB   CG   CD   CE   NZ                              
REMARK 470     PRO A 228    CB   CG   CD                                        
REMARK 470     ILE A 229    CB   CG1  CG2  CD1                                  
REMARK 470     THR A 230    CB   OG1  CG2                                       
REMARK 470     MET A 231    CB   CG   SD   CE                                   
REMARK 470     LEU A 232    CB   CG   CD1  CD2                                  
REMARK 470     LEU A 233    O    CB   CG   CD1  CD2                             
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    ARG A  57      -63.97   -126.97                                   
REMARK 500    ASP A  86     -112.36     64.73                                   
REMARK 500    GLU A 189     -115.24     53.76                                   
REMARK 500    VAL A 208      -73.39   -122.47                                   
REMARK 500    LEU A 232      -75.45    -91.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-0138   RELATED DB: EMDB                              
REMARK 900 CORE OF THE HUMAN PYRUVATE DEHYDROGENASE (E2)                        
DBREF  6H55 A -413   233  UNP    P10515   ODP2_HUMAN       1    647             
SEQRES   1 A  647  MET TRP ARG VAL CYS ALA ARG ARG ALA GLN ASN VAL ALA          
SEQRES   2 A  647  PRO TRP ALA GLY LEU GLU ALA ARG TRP THR ALA LEU GLN          
SEQRES   3 A  647  GLU VAL PRO GLY THR PRO ARG VAL THR SER ARG SER GLY          
SEQRES   4 A  647  PRO ALA PRO ALA ARG ARG ASN SER VAL THR THR GLY TYR          
SEQRES   5 A  647  GLY GLY VAL ARG ALA LEU CYS GLY TRP THR PRO SER SER          
SEQRES   6 A  647  GLY ALA THR PRO ARG ASN ARG LEU LEU LEU GLN LEU LEU          
SEQRES   7 A  647  GLY SER PRO GLY ARG ARG TYR TYR SER LEU PRO PRO HIS          
SEQRES   8 A  647  GLN LYS VAL PRO LEU PRO SER LEU SER PRO THR MET GLN          
SEQRES   9 A  647  ALA GLY THR ILE ALA ARG TRP GLU LYS LYS GLU GLY ASP          
SEQRES  10 A  647  LYS ILE ASN GLU GLY ASP LEU ILE ALA GLU VAL GLU THR          
SEQRES  11 A  647  ASP LYS ALA THR VAL GLY PHE GLU SER LEU GLU GLU CYS          
SEQRES  12 A  647  TYR MET ALA LYS ILE LEU VAL ALA GLU GLY THR ARG ASP          
SEQRES  13 A  647  VAL PRO ILE GLY ALA ILE ILE CYS ILE THR VAL GLY LYS          
SEQRES  14 A  647  PRO GLU ASP ILE GLU ALA PHE LYS ASN TYR THR LEU ASP          
SEQRES  15 A  647  SER SER ALA ALA PRO THR PRO GLN ALA ALA PRO ALA PRO          
SEQRES  16 A  647  THR PRO ALA ALA THR ALA SER PRO PRO THR PRO SER ALA          
SEQRES  17 A  647  GLN ALA PRO GLY SER SER TYR PRO PRO HIS MET GLN VAL          
SEQRES  18 A  647  LEU LEU PRO ALA LEU SER PRO THR MET THR MET GLY THR          
SEQRES  19 A  647  VAL GLN ARG TRP GLU LYS LYS VAL GLY GLU LYS LEU SER          
SEQRES  20 A  647  GLU GLY ASP LEU LEU ALA GLU ILE GLU THR ASP LYS ALA          
SEQRES  21 A  647  THR ILE GLY PHE GLU VAL GLN GLU GLU GLY TYR LEU ALA          
SEQRES  22 A  647  LYS ILE LEU VAL PRO GLU GLY THR ARG ASP VAL PRO LEU          
SEQRES  23 A  647  GLY THR PRO LEU CYS ILE ILE VAL GLU LYS GLU ALA ASP          
SEQRES  24 A  647  ILE SER ALA PHE ALA ASP TYR ARG PRO THR GLU VAL THR          
SEQRES  25 A  647  ASP LEU LYS PRO GLN VAL PRO PRO PRO THR PRO PRO PRO          
SEQRES  26 A  647  VAL ALA ALA VAL PRO PRO THR PRO GLN PRO LEU ALA PRO          
SEQRES  27 A  647  THR PRO SER ALA PRO CYS PRO ALA THR PRO ALA GLY PRO          
SEQRES  28 A  647  LYS GLY ARG VAL PHE VAL SER PRO LEU ALA LYS LYS LEU          
SEQRES  29 A  647  ALA VAL GLU LYS GLY ILE ASP LEU THR GLN VAL LYS GLY          
SEQRES  30 A  647  THR GLY PRO ASP GLY ARG ILE THR LYS LYS ASP ILE ASP          
SEQRES  31 A  647  SER PHE VAL PRO SER LYS VAL ALA PRO ALA PRO ALA ALA          
SEQRES  32 A  647  VAL VAL PRO PRO THR GLY PRO GLY MET ALA PRO VAL PRO          
SEQRES  33 A  647  THR GLY VAL PHE THR ASP ILE PRO ILE SER ASN ILE ARG          
SEQRES  34 A  647  ARG VAL ILE ALA GLN ARG LEU MET GLN SER LYS GLN THR          
SEQRES  35 A  647  ILE PRO HIS TYR TYR LEU SER ILE ASP VAL ASN MET GLY          
SEQRES  36 A  647  GLU VAL LEU LEU VAL ARG LYS GLU LEU ASN LYS ILE LEU          
SEQRES  37 A  647  GLU GLY ARG SER LYS ILE SER VAL ASN ASP PHE ILE ILE          
SEQRES  38 A  647  LYS ALA SER ALA LEU ALA CYS LEU LYS VAL PRO GLU ALA          
SEQRES  39 A  647  ASN SER SER TRP MET ASP THR VAL ILE ARG GLN ASN HIS          
SEQRES  40 A  647  VAL VAL ASP VAL SER VAL ALA VAL SER THR PRO ALA GLY          
SEQRES  41 A  647  LEU ILE THR PRO ILE VAL PHE ASN ALA HIS ILE LYS GLY          
SEQRES  42 A  647  VAL GLU THR ILE ALA ASN ASP VAL VAL SER LEU ALA THR          
SEQRES  43 A  647  LYS ALA ARG GLU GLY LYS LEU GLN PRO HIS GLU PHE GLN          
SEQRES  44 A  647  GLY GLY THR PHE THR ILE SER ASN LEU GLY MET PHE GLY          
SEQRES  45 A  647  ILE LYS ASN PHE SER ALA ILE ILE ASN PRO PRO GLN ALA          
SEQRES  46 A  647  CYS ILE LEU ALA ILE GLY ALA SER GLU ASP LYS LEU VAL          
SEQRES  47 A  647  PRO ALA ASP ASN GLU LYS GLY PHE ASP VAL ALA SER MET          
SEQRES  48 A  647  MET SER VAL THR LEU SER CYS ASP HIS ARG VAL VAL ASP          
SEQRES  49 A  647  GLY ALA VAL GLY ALA GLN TRP LEU ALA GLU PHE ARG LYS          
SEQRES  50 A  647  TYR LEU GLU LYS PRO ILE THR MET LEU LEU                      
HELIX    1 AA1 SER A   12  ILE A   29  1                                  18    
HELIX    2 AA2 MET A   40  GLU A   55  1                                  16    
HELIX    3 AA3 VAL A   62  VAL A   77  1                                  16    
HELIX    4 AA4 PRO A   78  ALA A   80  5                                   3    
HELIX    5 AA5 THR A  122  GLU A  136  1                                  15    
HELIX    6 AA6 GLN A  140  GLN A  145  5                                   6    
HELIX    7 AA7 GLY A  155  GLY A  158  5                                   4    
HELIX    8 AA8 ASP A  210  LYS A  227  1                                  18    
HELIX    9 AA9 PRO A  228  LEU A  232  5                                   5    
SHEET    1 AA1 4 HIS A  31  ASN A  39  0                                        
SHEET    2 AA1 4 ALA A 195  ASP A 205 -1  O  LEU A 202   N  LEU A  34           
SHEET    3 AA1 4 ILE A 173  ILE A 176 -1  N  ALA A 175   O  THR A 201           
SHEET    4 AA1 4 ILE A 151  ASN A 153  1  N  SER A 152   O  ILE A 176           
SHEET    1 AA2 3 HIS A  31  ASN A  39  0                                        
SHEET    2 AA2 3 ALA A 195  ASP A 205 -1  O  LEU A 202   N  LEU A  34           
SHEET    3 AA2 3 GLU A 180  LYS A 182 -1  N  LYS A 182   O  ALA A 195           
SHEET    1 AA3 2 SER A  82  TRP A  84  0                                        
SHEET    2 AA3 2 ILE A  89  GLN A  91 -1  O  ARG A  90   N  SER A  83           
SHEET    1 AA4 2 VAL A 101  SER A 102  0                                        
SHEET    2 AA4 2 LEU A 107  ILE A 108 -1  O  ILE A 108   N  VAL A 101           
CISPEP   1 PRO A  168    PRO A  169          0        -5.98                     
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   VAL A   1     199.915 104.000 255.745  1.00400.00           N  
ATOM      2  CA  VAL A   1     198.767 104.530 256.467  1.00400.00           C  
ATOM      3  C   VAL A   1     197.942 105.449 255.544  1.00400.00           C  
ATOM      4  O   VAL A   1     198.509 106.191 254.737  1.00400.00           O  
ATOM      5  N   PRO A   2     196.594 105.374 255.654  1.00400.00           N  
ATOM      6  CA  PRO A   2     195.710 106.075 254.698  1.00400.00           C  
ATOM      7  C   PRO A   2     195.320 107.526 254.996  1.00400.00           C  
ATOM      8  O   PRO A   2     195.904 108.211 255.843  1.00400.00           O  
ATOM      9  N   THR A   3     194.338 107.994 254.207  1.00400.00           N  
ATOM     10  CA  THR A   3     193.778 109.349 254.215  1.00400.00           C  
ATOM     11  C   THR A   3     192.503 109.459 255.065  1.00337.70           C  
ATOM     12  O   THR A   3     192.213 108.589 255.893  1.00400.00           O  
ATOM     13  N   GLY A   4     191.740 110.538 254.834  1.00229.46           N  
ATOM     14  CA  GLY A   4     190.509 110.882 255.521  1.00190.45           C  
ATOM     15  C   GLY A   4     190.617 112.119 256.391  1.00126.68           C  
ATOM     16  O   GLY A   4     189.804 112.308 257.300  1.00201.57           O  
ATOM     17  N   VAL A   5     191.625 112.950 256.134  1.00 56.51           N  
ATOM     18  CA  VAL A   5     191.923 114.144 256.912  1.00 39.42           C  
ATOM     19  C   VAL A   5     190.725 115.073 256.994  1.00 30.78           C  
ATOM     20  O   VAL A   5     189.898 115.146 256.079  1.00 54.73           O  
ATOM     21  N   PHE A   6     190.627 115.780 258.104  1.00 43.29           N  
ATOM     22  CA  PHE A   6     189.723 116.905 258.210  1.00 46.31           C  
ATOM     23  C   PHE A   6     190.225 117.756 259.361  1.00 18.82           C  
ATOM     24  O   PHE A   6     191.265 117.473 259.963  1.00 24.44           O  
ATOM     25  N   THR A   7     189.467 118.791 259.679  1.00 22.21           N  
ATOM     26  CA  THR A   7     189.933 119.848 260.572  1.00 19.14           C  
ATOM     27  C   THR A   7     188.933 120.026 261.705  1.00 10.96           C  
ATOM     28  O   THR A   7     187.748 120.272 261.461  1.00 10.97           O  
ATOM     29  N   ASP A   8     189.413 119.902 262.941  1.00 13.21           N  
ATOM     30  CA  ASP A   8     188.635 120.265 264.120  1.00 12.43           C  
ATOM     31  C   ASP A   8     188.998 121.700 264.481  1.00 10.06           C  
ATOM     32  O   ASP A   8     190.115 121.972 264.933  1.00 15.62           O  
ATOM     33  N   ILE A   9     188.056 122.612 264.289  1.00  6.43           N  
ATOM     34  CA  ILE A   9     188.297 124.048 264.391  1.00  7.10           C  
ATOM     35  C   ILE A   9     187.667 124.545 265.687  1.00  5.27           C  
ATOM     36  O   ILE A   9     186.467 124.336 265.898  1.00  6.89           O  
ATOM     37  N   PRO A  10     188.420 125.199 266.572  1.00 10.65           N  
ATOM     38  CA  PRO A  10     187.784 125.853 267.719  1.00 16.04           C  
ATOM     39  C   PRO A  10     186.914 127.012 267.257  1.00  7.90           C  
ATOM     40  O   PRO A  10     187.297 127.803 266.392  1.00  8.23           O  
ATOM     41  N   ILE A  11     185.728 127.105 267.849  1.00 10.59           N  
ATOM     42  CA  ILE A  11     184.711 128.053 267.417  1.00  8.90           C  
ATOM     43  C   ILE A  11     184.731 129.256 268.348  1.00  7.82           C  
ATOM     44  O   ILE A  11     184.991 129.136 269.549  1.00  7.83           O  
ATOM     45  N   SER A  12     184.452 130.425 267.779  1.00  8.53           N  
ATOM     46  CA  SER A  12     184.508 131.683 268.509  1.00  9.67           C  
ATOM     47  C   SER A  12     183.140 132.021 269.085  1.00  7.99           C  
ATOM     48  O   SER A  12     182.105 131.706 268.490  1.00  6.82           O  
ATOM     49  N   ASN A  13     183.145 132.662 270.258  1.00  8.59           N  
ATOM     50  CA  ASN A  13     181.893 132.993 270.935  1.00  7.65           C  
ATOM     51  C   ASN A  13     180.944 133.754 270.018  1.00  6.20           C  
ATOM     52  O   ASN A  13     179.725 133.735 270.221  1.00  4.98           O  
ATOM     53  N   ILE A  14     181.481 134.450 269.018  1.00  6.72           N  
ATOM     54  CA  ILE A  14     180.653 135.094 268.006  1.00  5.07           C  
ATOM     55  C   ILE A  14     179.806 134.030 267.320  1.00  4.83           C  
ATOM     56  O   ILE A  14     178.576 134.003 267.464  1.00  4.31           O  
ATOM     57  N   ARG A  15     180.464 133.120 266.597  1.00  5.72           N  
ATOM     58  CA  ARG A  15     179.745 132.033 265.941  1.00  5.99           C  
ATOM     59  C   ARG A  15     178.874 131.275 266.931  1.00  5.65           C  
ATOM     60  O   ARG A  15     177.680 131.079 266.697  1.00  5.20           O  
ATOM     61  N   ARG A  16     179.464 130.830 268.041  1.00  6.20           N  
ATOM     62  CA  ARG A  16     178.758 129.980 268.995  1.00  5.90           C  
ATOM     63  C   ARG A  16     177.460 130.631 269.470  1.00  5.05           C  
ATOM     64  O   ARG A  16     176.379 130.036 269.389  1.00  5.15           O  
ATOM     65  N   VAL A  17     177.552 131.869 269.958  1.00  4.32           N  
ATOM     66  CA  VAL A  17     176.379 132.557 270.498  1.00  3.71           C  
ATOM     67  C   VAL A  17     175.361 132.804 269.391  1.00  3.23           C  
ATOM     68  O   VAL A  17     174.157 132.571 269.562  1.00  3.13           O  
ATOM     69  N   ILE A  18     175.832 133.281 268.236  1.00  3.20           N  
ATOM     70  CA  ILE A  18     174.930 133.518 267.109  1.00  3.08           C  
ATOM     71  C   ILE A  18     174.191 132.233 266.753  1.00  3.58           C  
ATOM     72  O   ILE A  18     173.022 132.251 266.351  1.00  3.59           O  
ATOM     73  N   ALA A  19     174.866 131.093 266.911  1.00  4.18           N  
ATOM     74  CA  ALA A  19     174.246 129.815 266.579  1.00  4.91           C  
ATOM     75  C   ALA A  19     173.218 129.413 267.626  1.00  4.28           C  
ATOM     76  O   ALA A  19     172.139 128.910 267.291  1.00  4.09           O  
ATOM     77  N   GLN A  20     173.535 129.624 268.904  1.00  4.25           N  
ATOM     78  CA  GLN A  20     172.601 129.274 269.969  1.00  4.17           C  
ATOM     79  C   GLN A  20     171.339 130.122 269.883  1.00  3.29           C  
ATOM     80  O   GLN A  20     170.233 129.650 270.174  1.00  3.08           O  
ATOM     81  N   ARG A  21     171.486 131.387 269.484  1.00  3.04           N  
ATOM     82  CA  ARG A  21     170.326 132.266 269.391  1.00  2.57           C  
ATOM     83  C   ARG A  21     169.531 131.994 268.119  1.00  2.31           C  
ATOM     84  O   ARG A  21     168.296 131.929 268.149  1.00  2.15           O  
ATOM     85  N   LEU A  22     170.224 131.815 266.992  1.00  2.53           N  
ATOM     86  CA  LEU A  22     169.533 131.562 265.731  1.00  2.63           C  
ATOM     87  C   LEU A  22     168.823 130.213 265.745  1.00  2.47           C  
ATOM     88  O   LEU A  22     167.774 130.054 265.110  1.00  2.66           O  
ATOM     89  N   MET A  23     169.380 129.228 266.449  1.00  2.51           N  
ATOM     90  CA  MET A  23     168.737 127.926 266.580  1.00  2.62           C  
ATOM     91  C   MET A  23     167.353 128.072 267.201  1.00  2.38           C  
ATOM     92  O   MET A  23     166.335 127.787 266.557  1.00  2.47           O  
ATOM     93  N   GLN A  24     167.311 128.512 268.461  1.00  2.31           N  
ATOM     94  CA  GLN A  24     166.032 128.713 269.133  1.00  2.48           C  
ATOM     95  C   GLN A  24     165.155 129.688 268.361  1.00  2.12           C  
ATOM     96  O   GLN A  24     163.924 129.649 268.470  1.00  2.22           O  
ATOM     97  N   SER A  25     165.770 130.579 267.580  1.00  1.93           N  
ATOM     98  CA  SER A  25     165.001 131.421 266.671  1.00  1.90           C  
ATOM     99  C   SER A  25     164.216 130.564 265.684  1.00  1.65           C  
ATOM    100  O   SER A  25     162.995 130.701 265.548  1.00  1.75           O  
ATOM    101  N   LYS A  26     164.913 129.666 264.989  1.00  1.76           N  
ATOM    102  CA  LYS A  26     164.289 128.733 264.059  1.00  2.03           C  
ATOM    103  C   LYS A  26     163.199 127.930 264.752  1.00  1.88           C  
ATOM    104  O   LYS A  26     162.027 128.010 264.371  1.00  2.04           O  
ATOM    105  N   GLN A  27     163.579 127.143 265.762  1.00  1.78           N  
ATOM    106  CA  GLN A  27     162.600 126.313 266.456  1.00  1.91           C  
ATOM    107  C   GLN A  27     161.387 127.128 266.887  1.00  2.02           C  
ATOM    108  O   GLN A  27     160.254 126.634 266.862  1.00  2.53           O  
ATOM    109  N   THR A  28     161.607 128.382 267.287  1.00  1.82           N  
ATOM    110  CA  THR A  28     160.504 129.224 267.740  1.00  2.28           C  
ATOM    111  C   THR A  28     159.754 129.852 266.568  1.00  1.65           C  
ATOM    112  O   THR A  28     158.519 129.909 266.575  1.00  1.67           O  
ATOM    113  N   ILE A  29     160.478 130.323 265.558  1.00  1.88           N  
ATOM    114  CA  ILE A  29     159.924 131.128 264.478  1.00  1.80           C  
ATOM    115  C   ILE A  29     159.743 130.246 263.246  1.00  2.42           C  
ATOM    116  O   ILE A  29     160.728 129.745 262.697  1.00  3.77           O  
ATOM    117  N   PRO A  30     158.512 130.027 262.770  1.00  2.75           N  
ATOM    118  CA  PRO A  30     158.332 129.361 261.472  1.00  3.37           C  
ATOM    119  C   PRO A  30     158.721 130.259 260.309  1.00  2.36           C  
ATOM    120  O   PRO A  30     157.855 130.856 259.662  1.00  1.90           O  
ATOM    121  N   HIS A  31     160.020 130.365 260.039  1.00  2.91           N  
ATOM    122  CA  HIS A  31     160.501 131.278 259.010  1.00  1.90           C  
ATOM    123  C   HIS A  31     159.874 130.973 257.654  1.00  1.25           C  
ATOM    124  O   HIS A  31     159.897 129.834 257.179  1.00  1.30           O  
ATOM    125  N   TYR A  32     159.313 132.008 257.031  1.00  1.38           N  
ATOM    126  CA  TYR A  32     158.921 131.953 255.630  1.00  1.40           C  
ATOM    127  C   TYR A  32     159.383 133.243 254.969  1.00  1.02           C  
ATOM    128  O   TYR A  32     159.650 134.242 255.642  1.00  0.80           O  
ATOM    129  N   TYR A  33     159.471 133.211 253.640  1.00  1.35           N  
ATOM    130  CA  TYR A  33     160.093 134.291 252.888  1.00  1.60           C  
ATOM    131  C   TYR A  33     159.151 134.784 251.799  1.00  1.83           C  
ATOM    132  O   TYR A  33     158.279 134.055 251.322  1.00  2.75           O  
ATOM    133  N   LEU A  34     159.343 136.046 251.419  1.00  1.31           N  
ATOM    134  CA  LEU A  34     158.623 136.673 250.320  1.00  1.32           C  
ATOM    135  C   LEU A  34     159.617 137.475 249.492  1.00  1.54           C  
ATOM    136  O   LEU A  34     160.400 138.261 250.032  1.00  2.52           O  
ATOM    137  N   SER A  35     159.580 137.272 248.176  1.00  0.96           N  
ATOM    138  CA  SER A  35     160.575 137.883 247.305  1.00  1.02           C  
ATOM    139  C   SER A  35     159.895 138.479 246.081  1.00  1.55           C  
ATOM    140  O   SER A  35     158.941 137.917 245.539  1.00  3.05           O  
ATOM    141  N   ILE A  36     160.418 139.627 245.649  1.00  1.13           N  
ATOM    142  CA  ILE A  36     159.938 140.321 244.459  1.00  1.82           C  
ATOM    143  C   ILE A  36     161.091 141.131 243.878  1.00  1.49           C  
ATOM    144  O   ILE A  36     162.197 141.137 244.431  1.00  1.46           O  
ATOM    145  N   ASP A  37     160.845 141.815 242.762  1.00  1.76           N  
ATOM    146  CA  ASP A  37     161.850 142.633 242.102  1.00  1.70           C  
ATOM    147  C   ASP A  37     161.221 143.935 241.631  1.00  1.89           C  
ATOM    148  O   ASP A  37     160.023 143.995 241.338  1.00  2.89           O  
ATOM    149  N   VAL A  38     162.041 144.980 241.564  1.00  1.72           N  
ATOM    150  CA  VAL A  38     161.592 146.300 241.131  1.00  2.12           C  
ATOM    151  C   VAL A  38     162.704 146.939 240.314  1.00  1.96           C  
ATOM    152  O   VAL A  38     163.889 146.717 240.575  1.00  1.73           O  
ATOM    153  N   ASN A  39     162.315 147.742 239.326  1.00  2.22           N  
ATOM    154  CA  ASN A  39     163.266 148.374 238.417  1.00  2.13           C  
ATOM    155  C   ASN A  39     163.876 149.591 239.103  1.00  2.13           C  
ATOM    156  O   ASN A  39     163.161 150.522 239.488  1.00  3.41           O  
ATOM    157  N   MET A  40     165.198 149.580 239.256  1.00  1.80           N  
ATOM    158  CA  MET A  40     165.938 150.694 239.831  1.00  1.81           C  
ATOM    159  C   MET A  40     166.524 151.621 238.775  1.00  1.65           C  
ATOM    160  O   MET A  40     167.210 152.584 239.131  1.00  3.98           O  
ATOM    161  N   GLY A  41     166.272 151.358 237.494  1.00  3.18           N  
ATOM    162  CA  GLY A  41     166.866 152.139 236.426  1.00  2.60           C  
ATOM    163  C   GLY A  41     166.708 153.632 236.616  1.00  2.66           C  
ATOM    164  O   GLY A  41     167.691 154.377 236.574  1.00  2.68           O  
ATOM    165  N   GLU A  42     165.475 154.083 236.835  1.00  3.57           N  
ATOM    166  CA  GLU A  42     165.234 155.488 237.134  1.00  4.88           C  
ATOM    167  C   GLU A  42     165.895 155.846 238.458  1.00  4.20           C  
ATOM    168  O   GLU A  42     166.379 156.968 238.640  1.00  5.50           O  
ATOM    169  N   VAL A  43     165.927 154.886 239.386  1.00  3.27           N  
ATOM    170  CA  VAL A  43     166.571 155.118 240.677  1.00  3.98           C  
ATOM    171  C   VAL A  43     168.085 155.134 240.518  1.00  2.34           C  
ATOM    172  O   VAL A  43     168.792 155.868 241.219  1.00  2.10           O  
ATOM    173  N   LEU A  44     168.609 154.320 239.598  1.00  2.06           N  
ATOM    174  CA  LEU A  44     170.039 154.363 239.308  1.00  2.23           C  
ATOM    175  C   LEU A  44     170.424 155.703 238.695  1.00  2.71           C  
ATOM    176  O   LEU A  44     171.445 156.298 239.061  1.00  3.31           O  
ATOM    177  N   LEU A  45     169.615 156.196 237.755  1.00  3.05           N  
ATOM    178  CA  LEU A  45     169.844 157.529 237.207  1.00  4.27           C  
ATOM    179  C   LEU A  45     169.723 158.585 238.297  1.00  3.58           C  
ATOM    180  O   LEU A  45     170.394 159.622 238.255  1.00  3.94           O  
ATOM    181  N   VAL A  46     168.863 158.336 239.288  1.00  3.07           N  
ATOM    182  CA  VAL A  46     168.803 159.212 240.455  1.00  2.76           C  
ATOM    183  C   VAL A  46     170.088 159.091 241.263  1.00  2.26           C  
ATOM    184  O   VAL A  46     170.458 159.994 242.021  1.00  2.38           O  
ATOM    185  N   ARG A  47     170.787 157.966 241.112  1.00  2.09           N  
ATOM    186  CA  ARG A  47     172.071 157.775 241.773  1.00  2.31           C  
ATOM    187  C   ARG A  47     173.149 158.563 241.042  1.00  2.97           C  
ATOM    188  O   ARG A  47     174.062 159.110 241.669  1.00  3.56           O  
ATOM    189  N   LYS A  48     173.047 158.628 239.713  1.00  3.65           N  
ATOM    190  CA  LYS A  48     174.012 159.394 238.931  1.00  5.53           C  
ATOM    191  C   LYS A  48     173.746 160.889 239.056  1.00  6.99           C  
ATOM    192  O   LYS A  48     174.646 161.713 238.855  1.00 10.06           O  
ATOM    193  N   GLU A  49     172.508 161.257 239.382  1.00  6.12           N  
ATOM    194  CA  GLU A  49     172.140 162.654 239.573  1.00  7.84           C  
ATOM    195  C   GLU A  49     172.518 163.108 240.977  1.00  7.21           C  
ATOM    196  O   GLU A  49     173.368 163.991 241.151  1.00 11.73           O  
ATOM    197  N   LEU A  50     171.885 162.508 241.987  1.00  4.57           N  
ATOM    198  CA  LEU A  50     172.254 162.803 243.366  1.00  6.25           C  
ATOM    199  C   LEU A  50     173.758 162.677 243.559  1.00  8.22           C  
ATOM    200  O   LEU A  50     174.354 163.408 244.358  1.00  8.72           O  
ATOM    201  N   ASN A  51     174.406 161.757 242.848  1.00 14.45           N  
ATOM    202  CA  ASN A  51     175.859 161.709 242.967  1.00 16.87           C  
ATOM    203  C   ASN A  51     176.551 162.724 242.067  1.00 12.70           C  
ATOM    204  O   ASN A  51     177.686 163.114 242.361  1.00 25.91           O  
ATOM    205  N   LYS A  52     175.911 163.189 240.992  1.00 17.42           N  
ATOM    206  CA  LYS A  52     176.573 164.241 240.228  1.00 27.58           C  
ATOM    207  C   LYS A  52     176.586 165.545 241.009  1.00 25.14           C  
ATOM    208  O   LYS A  52     177.455 166.397 240.787  1.00 50.28           O  
ATOM    209  N   ILE A  53     175.640 165.747 241.921  1.00 16.16           N  
ATOM    210  CA  ILE A  53     175.804 166.874 242.837  1.00 19.04           C  
ATOM    211  C   ILE A  53     176.693 166.507 244.019  1.00 17.76           C  
ATOM    212  O   ILE A  53     177.562 167.288 244.413  1.00 33.59           O  
ATOM    213  N   LEU A  54     176.513 165.319 244.593  1.00  7.73           N  
ATOM    214  CA  LEU A  54     177.073 165.019 245.904  1.00  7.94           C  
ATOM    215  C   LEU A  54     178.475 164.429 245.860  1.00  7.12           C  
ATOM    216  O   LEU A  54     179.030 164.127 246.921  1.00  7.69           O  
ATOM    217  N   GLU A  55     179.054 164.250 244.671  1.00  8.38           N  
ATOM    218  CA  GLU A  55     180.426 163.764 244.588  1.00  9.92           C  
ATOM    219  C   GLU A  55     181.385 164.659 245.361  1.00 10.75           C  
ATOM    220  O   GLU A  55     182.463 164.212 245.769  1.00 15.03           O  
ATOM    221  N   GLY A  56     181.010 165.922 245.571  1.00  9.87           N  
ATOM    222  CA  GLY A  56     181.863 166.877 246.251  1.00 14.63           C  
ATOM    223  C   GLY A  56     182.326 166.434 247.623  1.00 14.24           C  
ATOM    224  O   GLY A  56     183.386 166.869 248.084  1.00 33.47           O  
ATOM    225  N   ARG A  57     181.551 165.576 248.290  1.00  8.70           N  
ATOM    226  CA  ARG A  57     181.923 165.105 249.619  1.00 12.13           C  
ATOM    227  C   ARG A  57     181.919 163.582 249.697  1.00  8.01           C  
ATOM    228  O   ARG A  57     182.970 162.970 249.910  1.00 13.57           O  
ATOM    229  N   SER A  58     180.756 162.959 249.523  1.00  9.34           N  
ATOM    230  CA  SER A  58     180.595 161.528 249.720  1.00  7.05           C  
ATOM    231  C   SER A  58     179.928 160.890 248.509  1.00  6.41           C  
ATOM    232  O   SER A  58     179.396 161.573 247.629  1.00 21.83           O  
ATOM    233  N   LYS A  59     179.974 159.561 248.475  1.00  5.87           N  
ATOM    234  CA  LYS A  59     179.366 158.761 247.424  1.00  4.08           C  
ATOM    235  C   LYS A  59     178.174 158.001 247.992  1.00  1.65           C  
ATOM    236  O   LYS A  59     178.125 157.681 249.183  1.00  3.25           O  
ATOM    237  N   ILE A  60     177.206 157.716 247.123  1.00  3.27           N  
ATOM    238  CA  ILE A  60     175.944 157.112 247.527  1.00  2.04           C  
ATOM    239  C   ILE A  60     175.836 155.721 246.921  1.00  1.90           C  
ATOM    240  O   ILE A  60     176.423 155.428 245.874  1.00  3.34           O  
ATOM    241  N   SER A  61     175.077 154.859 247.594  1.00  1.03           N  
ATOM    242  CA  SER A  61     174.795 153.511 247.129  1.00  1.21           C  
ATOM    243  C   SER A  61     173.288 153.318 247.016  1.00  1.15           C  
ATOM    244  O   SER A  61     172.498 154.058 247.608  1.00  1.00           O  
ATOM    245  N   VAL A  62     172.896 152.304 246.242  1.00  1.35           N  
ATOM    246  CA  VAL A  62     171.479 152.080 245.978  1.00  1.37           C  
ATOM    247  C   VAL A  62     170.784 151.504 247.205  1.00  1.09           C  
ATOM    248  O   VAL A  62     169.631 151.843 247.496  1.00  1.01           O  
ATOM    249  N   ASN A  63     171.471 150.629 247.945  1.00  1.57           N  
ATOM    250  CA  ASN A  63     170.856 149.977 249.099  1.00  1.37           C  
ATOM    251  C   ASN A  63     170.251 150.984 250.067  1.00  1.17           C  
ATOM    252  O   ASN A  63     169.218 150.706 250.689  1.00  1.24           O  
ATOM    253  N   ASP A  64     170.873 152.155 250.207  1.00  1.08           N  
ATOM    254  CA  ASP A  64     170.365 153.156 251.138  1.00  1.11           C  
ATOM    255  C   ASP A  64     168.937 153.556 250.785  1.00  1.08           C  
ATOM    256  O   ASP A  64     168.117 153.823 251.671  1.00  1.29           O  
ATOM    257  N   PHE A  65     168.621 153.601 249.492  1.00  0.95           N  
ATOM    258  CA  PHE A  65     167.273 153.936 249.051  1.00  0.96           C  
ATOM    259  C   PHE A  65     166.291 152.848 249.468  1.00  0.89           C  
ATOM    260  O   PHE A  65     165.198 153.146 249.959  1.00  0.97           O  
ATOM    261  N   ILE A  66     166.671 151.586 249.275  1.00  0.82           N  
ATOM    262  CA  ILE A  66     165.838 150.458 249.677  1.00  0.84           C  
ATOM    263  C   ILE A  66     165.577 150.524 251.176  1.00  0.79           C  
ATOM    264  O   ILE A  66     164.459 150.258 251.635  1.00  0.86           O  
ATOM    265  N   ILE A  67     166.602 150.888 251.950  1.00  0.70           N  
ATOM    266  CA  ILE A  67     166.431 151.020 253.396  1.00  0.65           C  
ATOM    267  C   ILE A  67     165.449 152.143 253.708  1.00  0.71           C  
ATOM    268  O   ILE A  67     164.547 151.996 254.542  1.00  0.70           O  
ATOM    269  N   LYS A  68     165.614 153.285 253.038  1.00  0.82           N  
ATOM    270  CA  LYS A  68     164.715 154.415 253.251  1.00  0.88           C  
ATOM    271  C   LYS A  68     163.268 154.015 252.992  1.00  0.94           C  
ATOM    272  O   LYS A  68     162.381 154.265 253.817  1.00  1.02           O  
ATOM    273  N   ALA A  69     163.011 153.388 251.842  1.00  0.97           N  
ATOM    274  CA  ALA A  69     161.661 152.926 251.542  1.00  1.11           C  
ATOM    275  C   ALA A  69     161.190 151.895 252.556  1.00  1.08           C  
ATOM    276  O   ALA A  69     159.988 151.794 252.825  1.00  1.41           O  
ATOM    277  N   SER A  70     162.115 151.123 253.128  1.00  0.88           N  
ATOM    278  CA  SER A  70     161.738 150.154 254.151  1.00  0.96           C  
ATOM    279  C   SER A  70     161.225 150.856 255.402  1.00  1.02           C  
ATOM    280  O   SER A  70     160.194 150.475 255.967  1.00  1.09           O  
ATOM    281  N   ALA A  71     161.941 151.888 255.854  1.00  1.04           N  
ATOM    282  CA  ALA A  71     161.492 152.657 257.009  1.00  1.18           C  
ATOM    283  C   ALA A  71     160.095 153.222 256.778  1.00  1.34           C  
ATOM    284  O   ALA A  71     159.137 152.855 257.468  1.00  1.57           O  
ATOM    285  N   LEU A  72     159.965 154.122 255.800  1.00  1.42           N  
ATOM    286  CA  LEU A  72     158.679 154.759 255.531  1.00  1.77           C  
ATOM    287  C   LEU A  72     157.585 153.722 255.306  1.00  1.72           C  
ATOM    288  O   LEU A  72     156.423 153.937 255.670  1.00  1.87           O  
ATOM    289  N   ALA A  73     157.939 152.589 254.699  1.00  1.65           N  
ATOM    290  CA  ALA A  73     156.973 151.512 254.515  1.00  1.80           C  
ATOM    291  C   ALA A  73     156.421 151.051 255.858  1.00  1.78           C  
ATOM    292  O   ALA A  73     155.245 150.688 255.973  1.00  2.12           O  
ATOM    293  N   CYS A  74     157.264 151.063 256.892  1.00  1.67           N  
ATOM    294  CA  CYS A  74     156.800 150.722 258.232  1.00  2.05           C  
ATOM    295  C   CYS A  74     156.041 151.887 258.854  1.00  2.00           C  
ATOM    296  O   CYS A  74     155.096 151.690 259.625  1.00  2.35           O  
ATOM    297  N   LEU A  75     156.447 153.116 258.527  1.00  1.90           N  
ATOM    298  CA  LEU A  75     155.753 154.289 259.048  1.00  2.38           C  
ATOM    299  C   LEU A  75     154.298 154.306 258.597  1.00  2.67           C  
ATOM    300  O   LEU A  75     153.396 154.638 259.373  1.00  3.34           O  
ATOM    301  N   LYS A  76     154.052 153.948 257.336  1.00  2.50           N  
ATOM    302  CA  LYS A  76     152.689 153.885 256.825  1.00  3.26           C  
ATOM    303  C   LYS A  76     151.954 152.634 257.283  1.00  4.11           C  
ATOM    304  O   LYS A  76     150.724 152.664 257.404  1.00  6.61           O  
ATOM    305  N   VAL A  77     152.671 151.545 257.537  1.00  2.69           N  
ATOM    306  CA  VAL A  77     152.065 150.299 258.002  1.00  3.13           C  
ATOM    307  C   VAL A  77     152.913 149.756 259.145  1.00  2.43           C  
ATOM    308  O   VAL A  77     153.747 148.864 258.928  1.00  2.02           O  
ATOM    309  N   PRO A  78     152.743 150.261 260.369  1.00  2.91           N  
ATOM    310  CA  PRO A  78     153.579 149.781 261.481  1.00  2.88           C  
ATOM    311  C   PRO A  78     153.494 148.283 261.706  1.00  2.18           C  
ATOM    312  O   PRO A  78     154.401 147.717 262.327  1.00  3.18           O  
ATOM    313  N   GLU A  79     152.440 147.620 261.220  1.00  1.61           N  
ATOM    314  CA  GLU A  79     152.304 146.183 261.431  1.00  1.52           C  
ATOM    315  C   GLU A  79     153.491 145.415 260.867  1.00  1.22           C  
ATOM    316  O   GLU A  79     153.744 144.275 261.275  1.00  1.58           O  
ATOM    317  N   ALA A  80     154.231 146.016 259.934  1.00  1.26           N  
ATOM    318  CA  ALA A  80     155.382 145.334 259.351  1.00  1.46           C  
ATOM    319  C   ALA A  80     156.514 145.206 260.363  1.00  1.52           C  
ATOM    320  O   ALA A  80     157.102 144.130 260.522  1.00  3.68           O  
ATOM    321  N   ASN A  81     156.830 146.294 261.062  1.00  1.49           N  
ATOM    322  CA  ASN A  81     157.925 146.314 262.027  1.00  1.89           C  
ATOM    323  C   ASN A  81     157.362 146.009 263.410  1.00  3.93           C  
ATOM    324  O   ASN A  81     156.615 146.814 263.976  1.00 21.88           O  
ATOM    325  N   SER A  82     157.726 144.851 263.956  1.00  3.42           N  
ATOM    326  CA  SER A  82     157.269 144.444 265.275  1.00  2.59           C  
ATOM    327  C   SER A  82     158.241 143.417 265.837  1.00  3.45           C  
ATOM    328  O   SER A  82     159.035 142.826 265.101  1.00  4.94           O  
ATOM    329  N   SER A  83     158.173 143.218 267.149  1.00  3.38           N  
ATOM    330  CA  SER A  83     159.011 142.255 267.852  1.00  4.68           C  
ATOM    331  C   SER A  83     158.111 141.278 268.596  1.00  3.19           C  
ATOM    332  O   SER A  83     157.038 141.662 269.075  1.00  2.25           O  
ATOM    333  N   TRP A  84     158.546 140.023 268.689  1.00  8.77           N  
ATOM    334  CA  TRP A  84     157.753 139.006 269.370  1.00  9.09           C  
ATOM    335  C   TRP A  84     158.196 138.888 270.823  1.00  8.97           C  
ATOM    336  O   TRP A  84     159.302 138.419 271.113  1.00 18.48           O  
ATOM    337  N   MET A  85     157.319 139.308 271.732  1.00  7.14           N  
ATOM    338  CA  MET A  85     157.567 139.307 273.166  1.00  8.93           C  
ATOM    339  C   MET A  85     157.042 138.045 273.844  1.00 13.63           C  
ATOM    340  O   MET A  85     157.000 137.989 275.077  1.00 64.33           O  
ATOM    341  N   ASP A  86     156.645 137.032 273.072  1.00 10.45           N  
ATOM    342  CA  ASP A  86     155.874 135.915 273.607  1.00 11.64           C  
ATOM    343  C   ASP A  86     154.517 136.416 274.085  1.00 13.54           C  
ATOM    344  O   ASP A  86     153.689 136.815 273.261  1.00 63.45           O  
ATOM    345  N   THR A  87     154.270 136.390 275.396  1.00 26.08           N  
ATOM    346  CA  THR A  87     152.939 136.638 275.942  1.00 30.04           C  
ATOM    347  C   THR A  87     152.259 137.816 275.252  1.00 14.79           C  
ATOM    348  O   THR A  87     151.050 137.776 275.001  1.00 14.49           O  
ATOM    349  N   VAL A  88     153.020 138.863 274.940  1.00 10.54           N  
ATOM    350  CA  VAL A  88     152.520 139.952 274.106  1.00  7.69           C  
ATOM    351  C   VAL A  88     153.494 140.167 272.955  1.00  5.28           C  
ATOM    352  O   VAL A  88     154.513 139.475 272.854  1.00  8.53           O  
ATOM    353  N   ILE A  89     153.183 141.117 272.074  1.00  3.30           N  
ATOM    354  CA  ILE A  89     154.028 141.445 270.933  1.00  3.66           C  
ATOM    355  C   ILE A  89     154.570 142.854 271.119  1.00  2.68           C  
ATOM    356  O   ILE A  89     153.917 143.715 271.716  1.00  3.38           O  
ATOM    357  N   ARG A  90     155.774 143.086 270.600  1.00  1.69           N  
ATOM    358  CA  ARG A  90     156.416 144.399 270.646  1.00  1.48           C  
ATOM    359  C   ARG A  90     156.268 145.048 269.274  1.00  1.12           C  
ATOM    360  O   ARG A  90     156.877 144.606 268.296  1.00  1.51           O  
ATOM    361  N   GLN A  91     155.455 146.099 269.206  1.00  1.43           N  
ATOM    362  CA  GLN A  91     155.255 146.870 267.985  1.00  1.60           C  
ATOM    363  C   GLN A  91     156.032 148.175 268.107  1.00  1.52           C  
ATOM    364  O   GLN A  91     155.684 149.037 268.921  1.00  2.11           O  
ATOM    365  N   ASN A  92     157.075 148.318 267.296  1.00  1.70           N  
ATOM    366  CA  ASN A  92     158.027 149.414 267.418  1.00  2.79           C  
ATOM    367  C   ASN A  92     157.638 150.552 266.486  1.00  4.57           C  
ATOM    368  O   ASN A  92     157.634 150.388 265.262  1.00 34.64           O  
ATOM    369  N   HIS A  93     157.313 151.706 267.070  1.00 14.73           N  
ATOM    370  CA  HIS A  93     157.145 152.927 266.291  1.00 16.78           C  
ATOM    371  C   HIS A  93     158.484 153.536 265.900  1.00 15.16           C  
ATOM    372  O   HIS A  93     158.616 154.091 264.805  1.00 33.35           O  
ATOM    373  N   VAL A  94     159.483 153.443 266.781  1.00  7.58           N  
ATOM    374  CA  VAL A  94     160.823 153.890 266.432  1.00  6.55           C  
ATOM    375  C   VAL A  94     161.465 152.866 265.508  1.00  2.94           C  
ATOM    376  O   VAL A  94     161.535 151.673 265.823  1.00  5.20           O  
ATOM    377  N   VAL A  95     161.936 153.335 264.356  1.00  2.77           N  
ATOM    378  CA  VAL A  95     162.461 152.472 263.304  1.00  2.21           C  
ATOM    379  C   VAL A  95     163.980 152.578 263.323  1.00  1.51           C  
ATOM    380  O   VAL A  95     164.536 153.654 263.068  1.00  2.99           O  
ATOM    381  N   ASP A  96     164.649 151.467 263.622  1.00  0.97           N  
ATOM    382  CA  ASP A  96     166.098 151.369 263.546  1.00  0.95           C  
ATOM    383  C   ASP A  96     166.461 150.221 262.617  1.00  0.92           C  
ATOM    384  O   ASP A  96     166.180 149.055 262.905  1.00  1.60           O  
ATOM    385  N   VAL A  97     167.089 150.564 261.495  1.00  0.48           N  
ATOM    386  CA  VAL A  97     167.338 149.625 260.408  1.00  0.40           C  
ATOM    387  C   VAL A  97     168.739 149.054 260.572  1.00  0.36           C  
ATOM    388  O   VAL A  97     169.732 149.777 260.426  1.00  0.65           O  
ATOM    389  N   SER A  98     168.817 147.761 260.873  1.00  0.39           N  
ATOM    390  CA  SER A  98     170.095 147.071 260.870  1.00  0.36           C  
ATOM    391  C   SER A  98     170.488 146.699 259.443  1.00  0.44           C  
ATOM    392  O   SER A  98     169.644 146.527 258.559  1.00  0.62           O  
ATOM    393  N   VAL A  99     171.794 146.579 259.223  1.00  0.64           N  
ATOM    394  CA  VAL A  99     172.347 146.266 257.912  1.00  0.97           C  
ATOM    395  C   VAL A  99     173.318 145.105 258.061  1.00  1.02           C  
ATOM    396  O   VAL A  99     174.074 145.037 259.035  1.00  1.49           O  
ATOM    397  N   ALA A 100     173.294 144.189 257.096  1.00  0.87           N  
ATOM    398  CA  ALA A 100     174.204 143.050 257.104  1.00  1.16           C  
ATOM    399  C   ALA A 100     175.425 143.373 256.252  1.00  1.66           C  
ATOM    400  O   ALA A 100     175.317 143.515 255.029  1.00  6.13           O  
ATOM    401  N   VAL A 101     176.584 143.488 256.896  1.00  0.66           N  
ATOM    402  CA  VAL A 101     177.828 143.863 256.234  1.00  0.65           C  
ATOM    403  C   VAL A 101     178.639 142.599 255.993  1.00  1.26           C  
ATOM    404  O   VAL A 101     178.693 141.718 256.860  1.00  2.98           O  
ATOM    405  N   SER A 102     179.270 142.512 254.825  1.00  2.07           N  
ATOM    406  CA  SER A 102     180.120 141.377 254.490  1.00  3.52           C  
ATOM    407  C   SER A 102     181.565 141.714 254.834  1.00  2.85           C  
ATOM    408  O   SER A 102     182.150 142.635 254.254  1.00  2.87           O  
ATOM    409  N   THR A 103     182.140 140.972 255.777  1.00  2.46           N  
ATOM    410  CA  THR A 103     183.509 141.197 256.215  1.00  2.02           C  
ATOM    411  C   THR A 103     184.191 139.852 256.386  1.00  2.18           C  
ATOM    412  O   THR A 103     183.514 138.844 256.625  1.00  2.22           O  
ATOM    413  N   PRO A 104     185.521 139.796 256.265  1.00  2.30           N  
ATOM    414  CA  PRO A 104     186.213 138.513 256.468  1.00  2.62           C  
ATOM    415  C   PRO A 104     185.969 137.908 257.837  1.00  2.82           C  
ATOM    416  O   PRO A 104     185.932 136.677 257.961  1.00  3.30           O  
ATOM    417  N   ALA A 105     185.803 138.734 258.873  1.00  2.84           N  
ATOM    418  CA  ALA A 105     185.587 138.200 260.213  1.00  3.05           C  
ATOM    419  C   ALA A 105     184.275 137.430 260.295  1.00  3.00           C  
ATOM    420  O   ALA A 105     184.235 136.317 260.833  1.00  3.64           O  
ATOM    421  N   GLY A 106     183.200 138.000 259.774  1.00  2.50           N  
ATOM    422  CA  GLY A 106     181.910 137.344 259.814  1.00  2.46           C  
ATOM    423  C   GLY A 106     180.788 138.333 259.611  1.00  1.68           C  
ATOM    424  O   GLY A 106     180.982 139.449 259.130  1.00  2.87           O  
ATOM    425  N   LEU A 107     179.592 137.897 259.997  1.00  1.25           N  
ATOM    426  CA  LEU A 107     178.408 138.730 259.843  1.00  1.04           C  
ATOM    427  C   LEU A 107     178.423 139.868 260.857  1.00  1.42           C  
ATOM    428  O   LEU A 107     178.726 139.667 262.037  1.00  3.82           O  
ATOM    429  N   ILE A 108     178.093 141.070 260.387  1.00  0.95           N  
ATOM    430  CA  ILE A 108     178.020 142.255 261.232  1.00  2.48           C  
ATOM    431  C   ILE A 108     176.670 142.918 261.009  1.00  0.90           C  
ATOM    432  O   ILE A 108     176.162 142.973 259.885  1.00  0.93           O  
ATOM    433  N   THR A 109     176.087 143.427 262.094  1.00  1.07           N  
ATOM    434  CA  THR A 109     174.737 143.992 262.069  1.00  1.07           C  
ATOM    435  C   THR A 109     174.770 145.432 262.570  1.00  0.91           C  
ATOM    436  O   THR A 109     174.236 145.749 263.636  1.00  0.99           O  
ATOM    437  N   PRO A 110     175.390 146.336 261.815  1.00  0.92           N  
ATOM    438  CA  PRO A 110     175.348 147.754 262.194  1.00  0.85           C  
ATOM    439  C   PRO A 110     173.919 148.276 262.181  1.00  0.82           C  
ATOM    440  O   PRO A 110     173.179 148.088 261.213  1.00  1.12           O  
ATOM    441  N   ILE A 111     173.537 148.940 263.267  1.00  0.66           N  
ATOM    442  CA  ILE A 111     172.166 149.401 263.455  1.00  0.90           C  
ATOM    443  C   ILE A 111     172.097 150.876 263.081  1.00  0.65           C  
ATOM    444  O   ILE A 111     172.910 151.684 263.539  1.00  0.61           O  
ATOM    445  N   VAL A 112     171.120 151.225 262.242  1.00  0.73           N  
ATOM    446  CA  VAL A 112     170.885 152.623 261.918  1.00  0.82           C  
ATOM    447  C   VAL A 112     169.864 153.195 262.895  1.00  0.72           C  
ATOM    448  O   VAL A 112     168.889 152.534 263.274  1.00  0.65           O  
ATOM    449  N   PHE A 113     170.093 154.437 263.312  1.00  1.02           N  
ATOM    450  CA  PHE A 113     169.263 155.104 264.313  1.00  1.16           C  
ATOM    451  C   PHE A 113     168.335 156.086 263.603  1.00  1.32           C  
ATOM    452  O   PHE A 113     168.786 157.115 263.089  1.00  1.49           O  
ATOM    453  N   ASN A 114     167.039 155.767 263.582  1.00  1.67           N  
ATOM    454  CA  ASN A 114     166.015 156.661 263.037  1.00  1.80           C  
ATOM    455  C   ASN A 114     166.398 157.179 261.653  1.00  1.71           C  
ATOM    456  O   ASN A 114     166.426 158.388 261.413  1.00  1.93           O  
ATOM    457  N   ALA A 115     166.700 156.266 260.731  1.00  1.51           N  
ATOM    458  CA  ALA A 115     167.085 156.663 259.382  1.00  1.33           C  
ATOM    459  C   ALA A 115     165.979 157.404 258.643  1.00  1.72           C  
ATOM    460  O   ALA A 115     166.285 158.207 257.756  1.00  1.63           O  
ATOM    461  N   HIS A 116     164.713 157.168 258.987  1.00  2.62           N  
ATOM    462  CA  HIS A 116     163.596 157.759 258.260  1.00  3.35           C  
ATOM    463  C   HIS A 116     163.605 159.281 258.350  1.00  4.37           C  
ATOM    464  O   HIS A 116     163.062 159.959 257.471  1.00  7.72           O  
ATOM    465  N   ILE A 117     164.210 159.831 259.404  1.00  2.94           N  
ATOM    466  CA  ILE A 117     164.308 161.284 259.524  1.00  2.97           C  
ATOM    467  C   ILE A 117     165.451 161.809 258.665  1.00  1.87           C  
ATOM    468  O   ILE A 117     165.393 162.921 258.128  1.00  1.80           O  
ATOM    469  N   LYS A 118     166.505 161.012 258.522  1.00  1.62           N  
ATOM    470  CA  LYS A 118     167.730 161.477 257.890  1.00  1.35           C  
ATOM    471  C   LYS A 118     167.516 161.738 256.403  1.00  1.26           C  
ATOM    472  O   LYS A 118     166.682 161.106 255.749  1.00  1.55           O  
ATOM    473  N   GLY A 119     168.289 162.686 255.870  1.00  1.23           N  
ATOM    474  CA  GLY A 119     168.217 163.068 254.480  1.00  1.13           C  
ATOM    475  C   GLY A 119     169.270 162.378 253.624  1.00  1.18           C  
ATOM    476  O   GLY A 119     169.779 161.306 253.941  1.00  1.30           O  
ATOM    477  N   VAL A 120     169.594 163.036 252.511  1.00  1.33           N  
ATOM    478  CA  VAL A 120     170.535 162.485 251.541  1.00  1.69           C  
ATOM    479  C   VAL A 120     171.966 162.768 251.981  1.00  1.62           C  
ATOM    480  O   VAL A 120     172.913 162.142 251.491  1.00  1.79           O  
ATOM    481  N   GLU A 121     172.133 163.703 252.913  1.00  1.47           N  
ATOM    482  CA  GLU A 121     173.446 164.068 253.427  1.00  1.56           C  
ATOM    483  C   GLU A 121     173.793 163.336 254.718  1.00  1.53           C  
ATOM    484  O   GLU A 121     174.873 163.560 255.274  1.00  2.04           O  
ATOM    485  N   THR A 122     172.913 162.457 255.200  1.00  1.11           N  
ATOM    486  CA  THR A 122     173.097 161.827 256.514  1.00  1.03           C  
ATOM    487  C   THR A 122     173.267 160.314 256.382  1.00  0.91           C  
ATOM    488  O   THR A 122     174.330 159.773 256.692  1.00  0.85           O  
ATOM    489  N   ILE A 123     172.221 159.628 255.927  1.00  0.89           N  
ATOM    490  CA  ILE A 123     172.215 158.166 255.897  1.00  0.79           C  
ATOM    491  C   ILE A 123     173.442 157.614 255.182  1.00  0.76           C  
ATOM    492  O   ILE A 123     173.959 156.559 255.555  1.00  0.65           O  
ATOM    493  N   ALA A 124     173.925 158.307 254.149  1.00  0.85           N  
ATOM    494  CA  ALA A 124     175.102 157.834 253.429  1.00  0.79           C  
ATOM    495  C   ALA A 124     176.318 157.783 254.345  1.00  0.74           C  
ATOM    496  O   ALA A 124     176.973 156.742 254.475  1.00  0.61           O  
ATOM    497  N   ASN A 125     176.627 158.903 255.000  1.00  0.93           N  
ATOM    498  CA  ASN A 125     177.789 158.953 255.880  1.00  1.07           C  
ATOM    499  C   ASN A 125     177.556 158.125 257.138  1.00  0.82           C  
ATOM    500  O   ASN A 125     178.496 157.812 257.877  1.00  0.85           O  
ATOM    501  N   ASP A 126     176.297 157.770 257.405  1.00  0.73           N  
ATOM    502  CA  ASP A 126     175.996 156.924 258.555  1.00  0.66           C  
ATOM    503  C   ASP A 126     176.288 155.461 258.243  1.00  0.63           C  
ATOM    504  O   ASP A 126     176.869 154.740 259.062  1.00  0.66           O  
ATOM    505  N   VAL A 127     175.891 155.007 257.056  1.00  0.60           N  
ATOM    506  CA  VAL A 127     176.175 153.645 256.620  1.00  0.59           C  
ATOM    507  C   VAL A 127     177.679 153.510 256.440  1.00  0.64           C  
ATOM    508  O   VAL A 127     178.291 152.544 256.911  1.00  0.60           O  
ATOM    509  N   VAL A 128     178.285 154.484 255.758  1.00  0.75           N  
ATOM    510  CA  VAL A 128     179.736 154.481 255.591  1.00  0.82           C  
ATOM    511  C   VAL A 128     180.421 154.559 256.948  1.00  0.82           C  
ATOM    512  O   VAL A 128     181.532 154.051 257.131  1.00  0.76           O  
ATOM    513  N   SER A 129     179.785 155.227 257.910  1.00  0.91           N  
ATOM    514  CA  SER A 129     180.264 155.264 259.287  1.00  1.01           C  
ATOM    515  C   SER A 129     180.317 153.866 259.891  1.00  0.85           C  
ATOM    516  O   SER A 129     181.398 153.354 260.208  1.00  0.90           O  
ATOM    517  N   LEU A 130     179.146 153.249 260.065  1.00  0.74           N  
ATOM    518  CA  LEU A 130     179.071 151.925 260.673  1.00  0.63           C  
ATOM    519  C   LEU A 130     179.967 150.935 259.937  1.00  0.58           C  
ATOM    520  O   LEU A 130     180.463 149.967 260.523  1.00  0.59           O  
ATOM    521  N   ALA A 131     180.178 151.161 258.639  1.00  0.58           N  
ATOM    522  CA  ALA A 131     181.127 150.339 257.898  1.00  0.58           C  
ATOM    523  C   ALA A 131     182.558 150.657 258.311  1.00  0.69           C  
ATOM    524  O   ALA A 131     183.402 149.759 258.411  1.00  0.71           O  
ATOM    525  N   THR A 132     182.852 151.936 258.540  1.00  0.82           N  
ATOM    526  CA  THR A 132     184.164 152.373 259.002  1.00  0.98           C  
ATOM    527  C   THR A 132     184.506 151.725 260.335  1.00  1.05           C  
ATOM    528  O   THR A 132     185.434 150.914 260.420  1.00  1.17           O  
ATOM    529  N   LYS A 133     183.760 152.078 261.385  1.00  0.99           N  
ATOM    530  CA  LYS A 133     184.063 151.544 262.708  1.00  1.09           C  
ATOM    531  C   LYS A 133     183.777 150.051 262.789  1.00  0.91           C  
ATOM    532  O   LYS A 133     184.266 149.374 263.701  1.00  1.01           O  
ATOM    533  N   ALA A 134     182.993 149.519 261.850  1.00  0.84           N  
ATOM    534  CA  ALA A 134     182.701 148.090 261.849  1.00  0.90           C  
ATOM    535  C   ALA A 134     183.877 147.294 261.297  1.00  1.07           C  
ATOM    536  O   ALA A 134     184.237 146.239 261.832  1.00  1.63           O  
ATOM    537  N   ARG A 135     184.495 147.796 260.223  1.00  0.93           N  
ATOM    538  CA  ARG A 135     185.645 147.117 259.636  1.00  1.08           C  
ATOM    539  C   ARG A 135     186.800 147.018 260.623  1.00  1.02           C  
ATOM    540  O   ARG A 135     187.562 146.045 260.591  1.00  1.23           O  
ATOM    541  N   GLU A 136     186.953 148.012 261.497  1.00  0.95           N  
ATOM    542  CA  GLU A 136     187.989 147.981 262.520  1.00  1.02           C  
ATOM    543  C   GLU A 136     187.552 147.251 263.783  1.00  1.65           C  
ATOM    544  O   GLU A 136     188.372 147.072 264.690  1.00  7.04           O  
ATOM    545  N   GLY A 137     186.291 146.832 263.868  1.00  1.51           N  
ATOM    546  CA  GLY A 137     185.793 146.165 265.054  1.00  1.45           C  
ATOM    547  C   GLY A 137     185.592 147.114 266.216  1.00  1.53           C  
ATOM    548  O   GLY A 137     185.455 146.682 267.365  1.00  1.90           O  
ATOM    549  N   LYS A 138     185.572 148.418 265.927  1.00  1.44           N  
ATOM    550  CA  LYS A 138     185.421 149.408 266.987  1.00  1.65           C  
ATOM    551  C   LYS A 138     183.985 149.482 267.488  1.00  1.38           C  
ATOM    552  O   LYS A 138     183.753 149.759 268.671  1.00  1.66           O  
ATOM    553  N   LEU A 139     183.012 149.244 266.610  1.00  1.20           N  
ATOM    554  CA  LEU A 139     181.617 149.275 267.020  1.00  1.57           C  
ATOM    555  C   LEU A 139     181.354 148.228 268.098  1.00  1.90           C  
ATOM    556  O   LEU A 139     181.770 147.070 267.998  1.00  5.37           O  
ATOM    557  N   GLN A 140     180.648 148.652 269.143  1.00  3.98           N  
ATOM    558  CA  GLN A 140     180.353 147.767 270.262  1.00  3.93           C  
ATOM    559  C   GLN A 140     179.211 146.831 269.900  1.00  4.21           C  
ATOM    560  O   GLN A 140     178.362 147.196 269.073  1.00  6.70           O  
ATOM    561  N   PRO A 141     179.153 145.629 270.479  1.00  3.32           N  
ATOM    562  CA  PRO A 141     178.054 144.711 270.142  1.00  3.07           C  
ATOM    563  C   PRO A 141     176.673 145.286 270.403  1.00  2.91           C  
ATOM    564  O   PRO A 141     175.736 144.985 269.653  1.00  2.63           O  
ATOM    565  N   HIS A 142     176.512 146.104 271.448  1.00  3.17           N  
ATOM    566  CA  HIS A 142     175.192 146.649 271.754  1.00  3.16           C  
ATOM    567  C   HIS A 142     174.659 147.482 270.596  1.00  2.91           C  
ATOM    568  O   HIS A 142     173.446 147.520 270.355  1.00  5.61           O  
ATOM    569  N   GLU A 143     175.544 148.161 269.862  1.00  1.75           N  
ATOM    570  CA  GLU A 143     175.101 148.849 268.656  1.00  1.56           C  
ATOM    571  C   GLU A 143     174.857 147.886 267.505  1.00  1.29           C  
ATOM    572  O   GLU A 143     174.322 148.301 266.471  1.00  1.68           O  
ATOM    573  N   PHE A 144     175.252 146.624 267.653  1.00  1.21           N  
ATOM    574  CA  PHE A 144     174.811 145.557 266.767  1.00  1.41           C  
ATOM    575  C   PHE A 144     173.625 144.790 267.335  1.00  2.31           C  
ATOM    576  O   PHE A 144     173.119 143.878 266.674  1.00  6.36           O  
ATOM    577  N   GLN A 145     173.173 145.141 268.535  1.00  1.87           N  
ATOM    578  CA  GLN A 145     172.085 144.453 269.212  1.00  3.01           C  
ATOM    579  C   GLN A 145     170.921 145.406 269.448  1.00  1.84           C  
ATOM    580  O   GLN A 145     171.092 146.627 269.498  1.00  2.99           O  
ATOM    581  N   GLY A 146     169.729 144.833 269.596  1.00  2.81           N  
ATOM    582  CA  GLY A 146     168.537 145.607 269.863  1.00  1.83           C  
ATOM    583  C   GLY A 146     167.837 146.165 268.645  1.00  3.70           C  
ATOM    584  O   GLY A 146     166.767 146.770 268.792  1.00 39.54           O  
ATOM    585  N   GLY A 147     168.397 145.987 267.451  1.00  4.88           N  
ATOM    586  CA  GLY A 147     167.774 146.489 266.243  1.00  1.01           C  
ATOM    587  C   GLY A 147     166.414 145.878 265.977  1.00  1.01           C  
ATOM    588  O   GLY A 147     166.217 144.675 266.175  1.00  2.49           O  
ATOM    589  N   THR A 148     165.465 146.701 265.525  1.00  0.71           N  
ATOM    590  CA  THR A 148     164.122 146.199 265.250  1.00  1.02           C  
ATOM    591  C   THR A 148     164.147 145.118 264.178  1.00  0.62           C  
ATOM    592  O   THR A 148     163.557 144.045 264.350  1.00  0.74           O  
ATOM    593  N   PHE A 149     164.819 145.384 263.069  1.00  0.61           N  
ATOM    594  CA  PHE A 149     164.968 144.429 261.974  1.00  0.64           C  
ATOM    595  C   PHE A 149     166.342 144.667 261.356  1.00  0.46           C  
ATOM    596  O   PHE A 149     167.146 145.447 261.880  1.00  0.42           O  
ATOM    597  N   THR A 150     166.614 143.999 260.239  1.00  0.45           N  
ATOM    598  CA  THR A 150     167.903 144.121 259.574  1.00  0.43           C  
ATOM    599  C   THR A 150     167.665 144.075 258.067  1.00  0.38           C  
ATOM    600  O   THR A 150     166.533 143.903 257.605  1.00  0.40           O  
ATOM    601  N   ILE A 151     168.741 144.235 257.296  1.00  0.41           N  
ATOM    602  CA  ILE A 151     168.686 144.107 255.845  1.00  0.39           C  
ATOM    603  C   ILE A 151     170.034 143.580 255.380  1.00  0.38           C  
ATOM    604  O   ILE A 151     171.080 143.946 255.919  1.00  0.46           O  
ATOM    605  N   SER A 152     170.011 142.713 254.370  1.00  0.39           N  
ATOM    606  CA  SER A 152     171.222 142.087 253.858  1.00  0.39           C  
ATOM    607  C   SER A 152     171.137 141.984 252.345  1.00  0.33           C  
ATOM    608  O   SER A 152     170.111 141.558 251.808  1.00  0.44           O  
ATOM    609  N   ASN A 153     172.211 142.375 251.661  1.00  0.50           N  
ATOM    610  CA  ASN A 153     172.328 142.200 250.218  1.00  0.63           C  
ATOM    611  C   ASN A 153     173.543 141.324 249.944  1.00  1.31           C  
ATOM    612  O   ASN A 153     174.685 141.771 250.101  1.00  2.41           O  
ATOM    613  N   LEU A 154     173.297 140.082 249.535  1.00  1.26           N  
ATOM    614  CA  LEU A 154     174.339 139.189 249.050  1.00  1.98           C  
ATOM    615  C   LEU A 154     174.398 139.134 247.530  1.00  0.85           C  
ATOM    616  O   LEU A 154     175.265 138.448 246.980  1.00  0.44           O  
ATOM    617  N   GLY A 155     173.500 139.840 246.842  1.00  2.17           N  
ATOM    618  CA  GLY A 155     173.424 139.769 245.394  1.00  1.38           C  
ATOM    619  C   GLY A 155     174.614 140.365 244.671  1.00  1.49           C  
ATOM    620  O   GLY A 155     174.702 140.223 243.446  1.00  1.41           O  
ATOM    621  N   MET A 156     175.527 141.020 245.388  1.00  2.43           N  
ATOM    622  CA  MET A 156     176.687 141.638 244.758  1.00  3.19           C  
ATOM    623  C   MET A 156     177.440 140.629 243.901  1.00  2.76           C  
ATOM    624  O   MET A 156     178.107 141.005 242.932  1.00  4.00           O  
ATOM    625  N   PHE A 157     177.343 139.348 244.251  1.00  1.69           N  
ATOM    626  CA  PHE A 157     177.981 138.280 243.495  1.00  1.83           C  
ATOM    627  C   PHE A 157     177.045 137.623 242.488  1.00  1.86           C  
ATOM    628  O   PHE A 157     177.475 136.723 241.760  1.00  2.55           O  
ATOM    629  N   GLY A 158     175.787 138.048 242.423  1.00  1.32           N  
ATOM    630  CA  GLY A 158     174.899 137.593 241.369  1.00  1.40           C  
ATOM    631  C   GLY A 158     173.897 136.522 241.745  1.00  5.32           C  
ATOM    632  O   GLY A 158     173.263 135.938 240.857  1.00 36.20           O  
ATOM    633  N   ILE A 159     173.727 136.245 243.040  1.00  2.79           N  
ATOM    634  CA  ILE A 159     172.753 135.243 243.453  1.00  1.69           C  
ATOM    635  C   ILE A 159     171.352 135.717 243.090  1.00  0.77           C  
ATOM    636  O   ILE A 159     170.949 136.836 243.427  1.00  0.76           O  
ATOM    637  N   LYS A 160     170.609 134.873 242.369  1.00  1.21           N  
ATOM    638  CA  LYS A 160     169.250 135.251 241.988  1.00  1.32           C  
ATOM    639  C   LYS A 160     168.407 135.540 243.223  1.00  1.32           C  
ATOM    640  O   LYS A 160     167.951 136.669 243.435  1.00  3.60           O  
ATOM    641  N   ASN A 161     168.175 134.519 244.039  1.00  1.20           N  
ATOM    642  CA  ASN A 161     167.437 134.655 245.290  1.00  1.37           C  
ATOM    643  C   ASN A 161     168.095 133.729 246.305  1.00  1.42           C  
ATOM    644  O   ASN A 161     169.052 133.014 245.989  1.00  1.85           O  
ATOM    645  N   PHE A 162     167.574 133.741 247.530  1.00  1.40           N  
ATOM    646  CA  PHE A 162     168.160 132.923 248.584  1.00  1.77           C  
ATOM    647  C   PHE A 162     167.408 133.070 249.899  1.00  5.46           C  
ATOM    648  O   PHE A 162     166.496 133.895 250.018  1.00 24.44           O  
ATOM    649  N   SER A 163     167.790 132.269 250.889  1.00  0.74           N  
ATOM    650  CA  SER A 163     167.216 132.313 252.223  1.00  1.00           C  
ATOM    651  C   SER A 163     168.227 132.898 253.199  1.00  1.25           C  
ATOM    652  O   SER A 163     169.422 132.595 253.137  1.00  2.10           O  
ATOM    653  N   ALA A 164     167.737 133.739 254.103  1.00  1.40           N  
ATOM    654  CA  ALA A 164     168.586 134.405 255.083  1.00  1.55           C  
ATOM    655  C   ALA A 164     168.124 133.994 256.477  1.00  2.50           C  
ATOM    656  O   ALA A 164     167.180 133.213 256.630  1.00 10.21           O  
ATOM    657  N   ILE A 165     168.808 134.560 257.468  1.00  1.52           N  
ATOM    658  CA  ILE A 165     168.596 134.357 258.888  1.00  1.61           C  
ATOM    659  C   ILE A 165     168.009 135.642 259.447  1.00  1.36           C  
ATOM    660  O   ILE A 165     168.473 136.738 259.103  1.00  2.38           O  
ATOM    661  N   ILE A 166     167.009 135.516 260.319  1.00  1.59           N  
ATOM    662  CA  ILE A 166     166.654 136.639 261.178  1.00  1.50           C  
ATOM    663  C   ILE A 166     167.176 136.331 262.576  1.00  1.24           C  
ATOM    664  O   ILE A 166     167.721 135.248 262.821  1.00  1.81           O  
ATOM    665  N   ASN A 167     167.015 137.274 263.501  1.00  1.26           N  
ATOM    666  CA  ASN A 167     167.390 137.072 264.887  1.00  1.38           C  
ATOM    667  C   ASN A 167     166.261 137.555 265.788  1.00  1.22           C  
ATOM    668  O   ASN A 167     165.674 138.613 265.529  1.00  1.12           O  
ATOM    669  N   PRO A 168     165.936 136.814 266.859  1.00  1.46           N  
ATOM    670  CA  PRO A 168     164.882 137.285 267.761  1.00  2.21           C  
ATOM    671  C   PRO A 168     165.317 138.477 268.614  1.00  2.05           C  
ATOM    672  O   PRO A 168     166.513 138.621 268.873  1.00  2.90           O  
ATOM    673  N   PRO A 169     164.365 139.320 269.051  1.00  1.71           N  
ATOM    674  CA  PRO A 169     162.941 139.301 268.703  1.00  1.47           C  
ATOM    675  C   PRO A 169     162.620 140.147 267.471  1.00  1.11           C  
ATOM    676  O   PRO A 169     161.795 141.053 267.568  1.00  1.23           O  
ATOM    677  N   GLN A 170     163.257 139.861 266.337  1.00  0.93           N  
ATOM    678  CA  GLN A 170     163.061 140.642 265.121  1.00  0.73           C  
ATOM    679  C   GLN A 170     162.103 139.902 264.195  1.00  0.73           C  
ATOM    680  O   GLN A 170     162.423 138.814 263.702  1.00  0.90           O  
ATOM    681  N   ALA A 171     160.934 140.497 263.952  1.00  0.74           N  
ATOM    682  CA  ALA A 171     159.893 139.819 263.186  1.00  0.86           C  
ATOM    683  C   ALA A 171     160.326 139.586 261.744  1.00  0.87           C  
ATOM    684  O   ALA A 171     160.322 138.449 261.258  1.00  1.11           O  
ATOM    685  N   CYS A 172     160.707 140.653 261.043  1.00  1.01           N  
ATOM    686  CA  CYS A 172     160.982 140.578 259.616  1.00  1.07           C  
ATOM    687  C   CYS A 172     162.328 141.215 259.310  1.00  1.33           C  
ATOM    688  O   CYS A 172     162.775 142.130 260.005  1.00  1.49           O  
ATOM    689  N   ILE A 173     162.971 140.712 258.256  1.00  1.30           N  
ATOM    690  CA  ILE A 173     164.219 141.272 257.751  1.00  1.35           C  
ATOM    691  C   ILE A 173     164.275 141.023 256.252  1.00  1.75           C  
ATOM    692  O   ILE A 173     163.746 140.028 255.748  1.00  2.39           O  
ATOM    693  N   LEU A 174     164.918 141.934 255.529  1.00  1.67           N  
ATOM    694  CA  LEU A 174     165.012 141.814 254.079  1.00  1.83           C  
ATOM    695  C   LEU A 174     166.392 141.422 253.561  1.00  2.08           C  
ATOM    696  O   LEU A 174     167.417 141.825 254.109  1.00  5.83           O  
ATOM    697  N   ALA A 175     166.397 140.628 252.495  1.00  0.87           N  
ATOM    698  CA  ALA A 175     167.627 140.175 251.855  1.00  0.89           C  
ATOM    699  C   ALA A 175     167.526 140.520 250.374  1.00  0.78           C  
ATOM    700  O   ALA A 175     166.555 140.154 249.712  1.00  1.09           O  
ATOM    701  N   ILE A 176     168.525 141.225 249.854  1.00  0.60           N  
ATOM    702  CA  ILE A 176     168.505 141.631 248.454  1.00  0.56           C  
ATOM    703  C   ILE A 176     169.576 140.998 247.572  1.00  0.73           C  
ATOM    704  O   ILE A 176     170.697 140.739 248.010  1.00  1.38           O  
ATOM    705  N   GLY A 177     169.204 140.754 246.319  1.00  0.57           N  
ATOM    706  CA  GLY A 177     170.089 140.182 245.328  1.00  0.61           C  
ATOM    707  C   GLY A 177     170.708 141.237 244.436  1.00  0.85           C  
ATOM    708  O   GLY A 177     170.913 142.387 244.842  1.00  1.34           O  
ATOM    709  N   ALA A 178     171.016 140.842 243.202  1.00  0.78           N  
ATOM    710  CA  ALA A 178     171.571 141.738 242.191  1.00  1.04           C  
ATOM    711  C   ALA A 178     170.523 141.942 241.106  1.00  1.34           C  
ATOM    712  O   ALA A 178     169.912 140.975 240.638  1.00  1.79           O  
ATOM    713  N   SER A 179     170.318 143.195 240.706  1.00  1.64           N  
ATOM    714  CA  SER A 179     169.360 143.495 239.651  1.00  2.23           C  
ATOM    715  C   SER A 179     169.848 142.942 238.320  1.00  2.12           C  
ATOM    716  O   SER A 179     170.968 143.228 237.887  1.00  2.85           O  
ATOM    717  N   GLU A 180     168.998 142.151 237.672  1.00  2.09           N  
ATOM    718  CA  GLU A 180     169.314 141.530 236.395  1.00  2.82           C  
ATOM    719  C   GLU A 180     168.225 141.877 235.391  1.00  3.03           C  
ATOM    720  O   GLU A 180     167.032 141.714 235.671  1.00  2.95           O  
ATOM    721  N   ASP A 181     168.642 142.353 234.221  1.00  4.25           N  
ATOM    722  CA  ASP A 181     167.700 142.799 233.203  1.00  5.18           C  
ATOM    723  C   ASP A 181     166.758 141.669 232.805  1.00  6.43           C  
ATOM    724  O   ASP A 181     167.203 140.576 232.441  1.00 11.79           O  
ATOM    725  N   LYS A 182     165.455 141.939 232.865  1.00  5.39           N  
ATOM    726  CA  LYS A 182     164.430 140.975 232.497  1.00  7.90           C  
ATOM    727  C   LYS A 182     163.507 141.593 231.456  1.00 10.05           C  
ATOM    728  O   LYS A 182     163.366 142.816 231.376  1.00 13.39           O  
ATOM    729  N   LEU A 183     162.872 140.733 230.661  1.00  9.31           N  
ATOM    730  CA  LEU A 183     162.074 141.206 229.537  1.00 12.53           C  
ATOM    731  C   LEU A 183     160.700 141.673 229.997  1.00 12.94           C  
ATOM    732  O   LEU A 183     159.931 140.912 230.591  1.00 26.03           O  
ATOM    733  N   VAL A 184     160.401 142.936 229.714  1.00  7.77           N  
ATOM    734  CA  VAL A 184     159.075 143.505 229.939  1.00  7.55           C  
ATOM    735  C   VAL A 184     158.500 143.904 228.584  1.00 10.13           C  
ATOM    736  O   VAL A 184     158.992 144.861 227.969  1.00 17.50           O  
ATOM    737  N   PRO A 185     157.476 143.218 228.077  1.00 14.71           N  
ATOM    738  CA  PRO A 185     156.935 143.585 226.762  1.00 24.82           C  
ATOM    739  C   PRO A 185     156.399 145.008 226.771  1.00 23.74           C  
ATOM    740  O   PRO A 185     155.729 145.431 227.714  1.00 27.74           O  
ATOM    741  N   ALA A 186     156.705 145.745 225.708  1.00 21.04           N  
ATOM    742  CA  ALA A 186     156.368 147.158 225.653  1.00 21.46           C  
ATOM    743  C   ALA A 186     155.443 147.456 224.480  1.00 17.25           C  
ATOM    744  O   ALA A 186     155.414 146.735 223.480  1.00 14.86           O  
ATOM    745  N   ASP A 187     154.691 148.551 224.613  1.00 20.52           N  
ATOM    746  CA  ASP A 187     153.841 149.026 223.529  1.00 23.08           C  
ATOM    747  C   ASP A 187     154.654 149.622 222.390  1.00 21.97           C  
ATOM    748  O   ASP A 187     154.079 150.029 221.374  1.00 29.09           O  
ATOM    749  N   ASN A 188     155.973 149.691 222.539  1.00 19.76           N  
ATOM    750  CA  ASN A 188     156.861 150.281 221.545  1.00 26.13           C  
ATOM    751  C   ASN A 188     157.297 149.285 220.486  1.00 27.35           C  
ATOM    752  O   ASN A 188     158.213 149.589 219.715  1.00 39.27           O  
ATOM    753  N   GLU A 189     156.696 148.096 220.465  1.00 20.14           N  
ATOM    754  CA  GLU A 189     157.031 147.057 219.499  1.00 20.32           C  
ATOM    755  C   GLU A 189     158.529 146.774 219.526  1.00 16.86           C  
ATOM    756  O   GLU A 189     159.042 146.311 220.549  1.00 26.50           O  
ATOM    757  N   LYS A 190     159.239 147.055 218.431  1.00 19.55           N  
ATOM    758  CA  LYS A 190     160.571 146.496 218.218  1.00 15.71           C  
ATOM    759  C   LYS A 190     161.439 146.568 219.469  1.00 12.40           C  
ATOM    760  O   LYS A 190     162.036 145.560 219.861  1.00 12.33           O  
ATOM    761  N   GLY A 191     161.522 147.729 220.115  1.00 17.48           N  
ATOM    762  CA  GLY A 191     162.311 147.770 221.330  1.00 21.57           C  
ATOM    763  C   GLY A 191     161.696 146.957 222.452  1.00 21.30           C  
ATOM    764  O   GLY A 191     160.606 147.269 222.940  1.00 46.07           O  
ATOM    765  N   PHE A 192     162.404 145.909 222.870  1.00 15.41           N  
ATOM    766  CA  PHE A 192     162.061 145.093 224.028  1.00 16.49           C  
ATOM    767  C   PHE A 192     162.909 145.423 225.249  1.00 18.39           C  
ATOM    768  O   PHE A 192     162.842 144.696 226.246  1.00 27.51           O  
ATOM    769  N   ASP A 193     163.704 146.490 225.193  1.00 17.32           N  
ATOM    770  CA  ASP A 193     164.860 146.645 226.067  1.00 20.58           C  
ATOM    771  C   ASP A 193     164.510 146.323 227.512  1.00 16.02           C  
ATOM    772  O   ASP A 193     163.527 146.829 228.061  1.00 32.70           O  
ATOM    773  N   VAL A 194     165.332 145.473 228.117  1.00 17.82           N  
ATOM    774  CA  VAL A 194     165.062 144.911 229.435  1.00 24.15           C  
ATOM    775  C   VAL A 194     165.596 145.861 230.498  1.00 16.71           C  
ATOM    776  O   VAL A 194     166.656 146.472 230.327  1.00 30.05           O  
ATOM    777  N   ALA A 195     164.857 145.991 231.597  1.00  7.68           N  
ATOM    778  CA  ALA A 195     165.257 146.808 232.732  1.00  3.44           C  
ATOM    779  C   ALA A 195     165.667 145.902 233.885  1.00  2.64           C  
ATOM    780  O   ALA A 195     165.107 144.816 234.063  1.00  5.24           O  
ATOM    781  N   SER A 196     166.643 146.355 234.668  1.00  1.69           N  
ATOM    782  CA  SER A 196     167.188 145.551 235.757  1.00  1.59           C  
ATOM    783  C   SER A 196     166.241 145.613 236.948  1.00  1.51           C  
ATOM    784  O   SER A 196     165.971 146.694 237.482  1.00  3.37           O  
ATOM    785  N   MET A 197     165.743 144.453 237.367  1.00  1.87           N  
ATOM    786  CA  MET A 197     164.870 144.351 238.528  1.00  2.00           C  
ATOM    787  C   MET A 197     165.672 143.826 239.711  1.00  1.46           C  
ATOM    788  O   MET A 197     166.136 142.681 239.695  1.00  1.43           O  
ATOM    789  N   MET A 198     165.830 144.660 240.736  1.00  1.25           N  
ATOM    790  CA  MET A 198     166.638 144.311 241.899  1.00  0.98           C  
ATOM    791  C   MET A 198     165.859 143.317 242.751  1.00  0.73           C  
ATOM    792  O   MET A 198     164.750 143.613 243.208  1.00  1.48           O  
ATOM    793  N   SER A 199     166.443 142.141 242.973  1.00  0.82           N  
ATOM    794  CA  SER A 199     165.780 141.120 243.770  1.00  1.05           C  
ATOM    795  C   SER A 199     165.651 141.587 245.213  1.00  1.58           C  
ATOM    796  O   SER A 199     166.638 141.978 245.844  1.00  2.93           O  
ATOM    797  N   VAL A 200     164.427 141.548 245.731  1.00  1.30           N  
ATOM    798  CA  VAL A 200     164.142 141.977 247.096  1.00  1.75           C  
ATOM    799  C   VAL A 200     163.398 140.853 247.799  1.00  1.27           C  
ATOM    800  O   VAL A 200     162.266 140.520 247.435  1.00  1.46           O  
ATOM    801  N   THR A 201     164.037 140.273 248.814  1.00  1.00           N  
ATOM    802  CA  THR A 201     163.483 139.139 249.543  1.00  0.80           C  
ATOM    803  C   THR A 201     163.290 139.527 250.999  1.00  0.60           C  
ATOM    804  O   THR A 201     164.231 139.989 251.650  1.00  0.80           O  
ATOM    805  N   LEU A 202     162.074 139.336 251.505  1.00  0.71           N  
ATOM    806  CA  LEU A 202     161.732 139.662 252.880  1.00  0.77           C  
ATOM    807  C   LEU A 202     161.279 138.408 253.613  1.00  0.61           C  
ATOM    808  O   LEU A 202     160.703 137.492 253.017  1.00  0.65           O  
ATOM    809  N   SER A 203     161.545 138.378 254.915  1.00  0.91           N  
ATOM    810  CA  SER A 203     161.174 137.268 255.778  1.00  1.53           C  
ATOM    811  C   SER A 203     160.163 137.741 256.813  1.00  1.14           C  
ATOM    812  O   SER A 203     160.139 138.912 257.199  1.00  2.31           O  
ATOM    813  N   CYS A 204     159.320 136.812 257.258  1.00  0.72           N  
ATOM    814  CA  CYS A 204     158.313 137.128 258.262  1.00  0.63           C  
ATOM    815  C   CYS A 204     158.007 135.879 259.073  1.00  0.87           C  
ATOM    816  O   CYS A 204     158.156 134.751 258.596  1.00  1.07           O  
ATOM    817  N   ASP A 205     157.573 136.103 260.310  1.00  0.88           N  
ATOM    818  CA  ASP A 205     157.112 135.044 261.198  1.00  1.12           C  
ATOM    819  C   ASP A 205     155.592 135.104 261.268  1.00  1.64           C  
ATOM    820  O   ASP A 205     155.025 136.142 261.627  1.00  1.91           O  
ATOM    821  N   HIS A 206     154.933 133.995 260.923  1.00  2.00           N  
ATOM    822  CA  HIS A 206     153.475 134.008 260.881  1.00  3.10           C  
ATOM    823  C   HIS A 206     152.870 134.181 262.266  1.00  3.77           C  
ATOM    824  O   HIS A 206     151.703 134.573 262.382  1.00  5.48           O  
ATOM    825  N   ARG A 207     153.637 133.903 263.320  1.00  3.18           N  
ATOM    826  CA  ARG A 207     153.153 134.132 264.675  1.00  3.89           C  
ATOM    827  C   ARG A 207     153.093 135.625 264.971  1.00  2.65           C  
ATOM    828  O   ARG A 207     152.503 136.045 265.972  1.00  2.68           O  
ATOM    829  N   VAL A 208     153.706 136.433 264.106  1.00  2.03           N  
ATOM    830  CA  VAL A 208     153.669 137.884 264.267  1.00  1.79           C  
ATOM    831  C   VAL A 208     153.077 138.542 263.027  1.00  1.90           C  
ATOM    832  O   VAL A 208     151.941 139.031 263.043  1.00  2.21           O  
ATOM    833  N   VAL A 209     153.845 138.573 261.938  1.00  1.85           N  
ATOM    834  CA  VAL A 209     153.366 139.152 260.689  1.00  2.00           C  
ATOM    835  C   VAL A 209     152.508 138.137 259.938  1.00  2.17           C  
ATOM    836  O   VAL A 209     152.667 136.923 260.072  1.00  3.10           O  
ATOM    837  N   ASP A 210     151.585 138.652 259.128  1.00  2.25           N  
ATOM    838  CA  ASP A 210     150.748 137.836 258.256  1.00  3.07           C  
ATOM    839  C   ASP A 210     151.061 138.186 256.809  1.00  2.28           C  
ATOM    840  O   ASP A 210     151.517 139.297 256.521  1.00  1.88           O  
ATOM    841  N   GLY A 211     150.815 137.240 255.906  1.00  2.74           N  
ATOM    842  CA  GLY A 211     151.225 137.365 254.519  1.00  2.67           C  
ATOM    843  C   GLY A 211     150.731 138.594 253.785  1.00  2.12           C  
ATOM    844  O   GLY A 211     151.525 139.315 253.173  1.00  1.78           O  
ATOM    845  N   ALA A 212     149.420 138.845 253.829  1.00  2.39           N  
ATOM    846  CA  ALA A 212     148.853 139.951 253.064  1.00  2.40           C  
ATOM    847  C   ALA A 212     149.476 141.284 253.461  1.00  2.31           C  
ATOM    848  O   ALA A 212     149.724 142.144 252.607  1.00  2.51           O  
ATOM    849  N   VAL A 213     149.765 141.463 254.749  1.00  2.26           N  
ATOM    850  CA  VAL A 213     150.209 142.756 255.257  1.00  2.18           C  
ATOM    851  C   VAL A 213     151.630 143.019 254.781  1.00  1.70           C  
ATOM    852  O   VAL A 213     151.871 143.971 254.032  1.00  1.74           O  
ATOM    853  N   GLY A 214     152.581 142.194 255.221  1.00  1.44           N  
ATOM    854  CA  GLY A 214     153.946 142.337 254.736  1.00  1.18           C  
ATOM    855  C   GLY A 214     154.016 142.417 253.225  1.00  1.20           C  
ATOM    856  O   GLY A 214     154.748 143.237 252.662  1.00  1.12           O  
ATOM    857  N   ALA A 215     153.246 141.565 252.543  1.00  1.50           N  
ATOM    858  CA  ALA A 215     153.140 141.640 251.093  1.00  1.84           C  
ATOM    859  C   ALA A 215     152.757 143.049 250.656  1.00  1.96           C  
ATOM    860  O   ALA A 215     153.207 143.541 249.615  1.00  2.01           O  
ATOM    861  N   GLN A 216     151.916 143.704 251.461  1.00  2.08           N  
ATOM    862  CA  GLN A 216     151.572 145.106 251.237  1.00  2.26           C  
ATOM    863  C   GLN A 216     152.775 146.009 251.476  1.00  1.97           C  
ATOM    864  O   GLN A 216     152.971 147.007 250.776  1.00  2.08           O  
ATOM    865  N   TRP A 217     153.583 145.673 252.483  1.00  1.72           N  
ATOM    866  CA  TRP A 217     154.823 146.388 252.750  1.00  1.61           C  
ATOM    867  C   TRP A 217     155.692 146.396 251.500  1.00  1.52           C  
ATOM    868  O   TRP A 217     156.308 147.414 251.164  1.00  1.62           O  
ATOM    869  N   LEU A 218     155.729 145.266 250.792  1.00  1.49           N  
ATOM    870  CA  LEU A 218     156.461 145.204 249.533  1.00  1.55           C  
ATOM    871  C   LEU A 218     155.690 145.875 248.401  1.00  1.91           C  
ATOM    872  O   LEU A 218     156.291 146.303 247.410  1.00  2.00           O  
ATOM    873  N   ALA A 219     154.363 145.963 248.519  1.00  2.21           N  
ATOM    874  CA  ALA A 219     153.566 146.583 247.464  1.00  2.76           C  
ATOM    875  C   ALA A 219     153.775 148.093 247.434  1.00  2.86           C  
ATOM    876  O   ALA A 219     154.160 148.663 246.406  1.00  3.19           O  
ATOM    877  N   GLU A 220     153.534 148.759 248.565  1.00  2.70           N  
ATOM    878  CA  GLU A 220     153.776 150.195 248.644  1.00  2.90           C  
ATOM    879  C   GLU A 220     155.268 150.490 248.689  1.00  2.53           C  
ATOM    880  O   GLU A 220     155.704 151.577 248.295  1.00  2.90           O  
ATOM    881  N   PHE A 221     156.061 149.540 249.181  1.00  2.07           N  
ATOM    882  CA  PHE A 221     157.511 149.639 249.098  1.00  1.77           C  
ATOM    883  C   PHE A 221     157.933 149.797 247.643  1.00  1.79           C  
ATOM    884  O   PHE A 221     158.493 150.829 247.255  1.00  1.81           O  
ATOM    885  N   ARG A 222     157.667 148.771 246.832  1.00  1.89           N  
ATOM    886  CA  ARG A 222     157.990 148.821 245.411  1.00  2.04           C  
ATOM    887  C   ARG A 222     157.350 150.034 244.749  1.00  2.11           C  
ATOM    888  O   ARG A 222     157.923 150.627 243.829  1.00  2.14           O  
ATOM    889  N   LYS A 223     156.152 150.413 245.201  1.00  2.20           N  
ATOM    890  CA  LYS A 223     155.535 151.635 244.694  1.00  2.29           C  
ATOM    891  C   LYS A 223     156.423 152.841 244.970  1.00  2.12           C  
ATOM    892  O   LYS A 223     156.497 153.773 244.161  1.00  2.02           O  
ATOM    893  N   TYR A 224     157.109 152.840 246.115  1.00  2.23           N  
ATOM    894  CA  TYR A 224     158.093 153.880 246.390  1.00  2.28           C  
ATOM    895  C   TYR A 224     159.300 153.736 245.476  1.00  2.04           C  
ATOM    896  O   TYR A 224     159.864 154.736 245.017  1.00  2.17           O  
ATOM    897  N   LEU A 225     159.710 152.496 245.201  1.00  2.03           N  
ATOM    898  CA  LEU A 225     160.829 152.269 244.294  1.00  2.42           C  
ATOM    899  C   LEU A 225     160.550 152.805 242.898  1.00  2.59           C  
ATOM    900  O   LEU A 225     161.482 153.248 242.218  1.00  4.37           O  
ATOM    901  N   GLU A 226     159.292 152.776 242.456  1.00  1.85           N  
ATOM    902  CA  GLU A 226     158.940 153.350 241.162  1.00  2.10           C  
ATOM    903  C   GLU A 226     159.236 154.843 241.136  1.00  2.70           C  
ATOM    904  O   GLU A 226     159.899 155.346 240.222  1.00  3.71           O  
ATOM    905  N   LYS A 227     158.747 155.570 242.140  1.00  2.39           N  
ATOM    906  CA  LYS A 227     158.965 157.012 242.262  1.00  2.56           C  
ATOM    907  C   LYS A 227     159.435 157.312 243.679  1.00  2.08           C  
ATOM    908  O   LYS A 227     158.632 157.601 244.573  1.00  2.25           O  
ATOM    909  N   PRO A 228     160.752 157.257 243.920  1.00  2.12           N  
ATOM    910  CA  PRO A 228     161.272 157.546 245.264  1.00  1.67           C  
ATOM    911  C   PRO A 228     160.896 158.936 245.754  1.00  2.55           C  
ATOM    912  O   PRO A 228     160.978 159.225 246.952  1.00  4.48           O  
ATOM    913  N   ILE A 229     160.473 159.801 244.833  1.00  2.18           N  
ATOM    914  CA  ILE A 229     160.032 161.154 245.156  1.00  2.75           C  
ATOM    915  C   ILE A 229     158.833 161.093 246.095  1.00  2.80           C  
ATOM    916  O   ILE A 229     158.439 162.106 246.685  1.00  3.04           O  
ATOM    917  N   THR A 230     158.247 159.905 246.238  1.00  2.77           N  
ATOM    918  CA  THR A 230     157.094 159.706 247.108  1.00  3.21           C  
ATOM    919  C   THR A 230     157.475 159.886 248.574  1.00  2.85           C  
ATOM    920  O   THR A 230     156.614 159.856 249.459  1.00  3.54           O  
ATOM    921  N   MET A 231     158.767 160.047 248.844  1.00  2.87           N  
ATOM    922  CA  MET A 231     159.280 160.141 250.205  1.00  3.00           C  
ATOM    923  C   MET A 231     159.495 161.581 250.672  1.00  2.44           C  
ATOM    924  O   MET A 231     159.964 161.798 251.792  1.00  3.06           O  
ATOM    925  N   LEU A 232     159.160 162.562 249.834  1.00  1.93           N  
ATOM    926  CA  LEU A 232     159.616 163.935 250.049  1.00  2.16           C  
ATOM    927  C   LEU A 232     158.667 164.815 250.862  1.00  3.80           C  
ATOM    928  O   LEU A 232     158.912 165.071 252.043  1.00  6.83           O  
ATOM    929  N   LEU A 233     157.578 165.258 250.238  1.00  3.76           N  
ATOM    930  CA  LEU A 233     156.768 166.352 250.776  1.00  7.14           C  
ATOM    931  C   LEU A 233     157.654 167.436 251.383  1.00 11.65           C  
TER     932      LEU A 233                                                      
MASTER      952    0    0    9   11    0    0    6  931    1    0   50          
END                                                                             
