HEADER    HYDROLASE/HYDROLASE INHIBITOR           03-DEC-18   6N9D              
TITLE     COMPLEX OF TISSUE INHIBITOR OF METALLOPROTEINASES-1 (TIMP-1) MUTANT   
TITLE    2 (L34G/L133P/L151C/G154A) WITH MATRIX METALLOPROTEINASE-3 CATALYTIC   
TITLE    3 DOMAIN (MMP-3CD)                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: STROMELYSIN-1;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SL-1,MATRIX METALLOPROTEINASE-3,MMP-3,TRANSIN-1;            
COMPND   5 EC: 3.4.24.17;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: METALLOPROTEINASE INHIBITOR 1;                             
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: ERYTHROID-POTENTIATING ACTIVITY,EPA,FIBROBLAST COLLAGENASE  
COMPND  11 INHIBITOR,COLLAGENASE INHIBITOR,TISSUE INHIBITOR OF                  
COMPND  12 METALLOPROTEINASES 1,TIMP-1;                                         
COMPND  13 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: MMP3, STMY1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: TIMP1, CLGI, TIMP;                                             
SOURCE  14 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  15 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    TISSUE INHIBITOR OF METALLOPROTEINASES, MATRIX METALLOPROTEINASE,     
KEYWDS   2 HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.RAEESZADEH-SARMAZDEH,E.S.RADISKY,B.SANKARAN                         
REVDAT   4   11-OCT-23 6N9D    1       REMARK LINK                              
REVDAT   3   04-DEC-19 6N9D    1       REMARK                                   
REVDAT   2   26-JUN-19 6N9D    1       JRNL                                     
REVDAT   1   15-MAY-19 6N9D    0                                                
JRNL        AUTH   M.RAEESZADEH-SARMAZDEH,K.A.GREENE,B.SANKARAN,G.P.DOWNEY,     
JRNL        AUTH 2 D.C.RADISKY,E.S.RADISKY                                      
JRNL        TITL   DIRECTED EVOLUTION OF THE METALLOPROTEINASE INHIBITOR TIMP-1 
JRNL        TITL 2 REVEALS THAT ITS N- AND C-TERMINAL DOMAINS COOPERATE IN      
JRNL        TITL 3 MATRIX METALLOPROTEINASE RECOGNITION.                        
JRNL        REF    J.BIOL.CHEM.                  V. 294  9476 2019              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   31040180                                                     
JRNL        DOI    10.1074/JBC.RA119.008321                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.67 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.67                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.99                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 14140                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.350                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1039                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 43.9963 -  5.1052    1.00     2069   162  0.1680 0.2409        
REMARK   3     2  5.1052 -  4.0531    1.00     1904   151  0.1412 0.2140        
REMARK   3     3  4.0531 -  3.5410    1.00     1857   148  0.1648 0.2305        
REMARK   3     4  3.5410 -  3.2174    1.00     1840   146  0.2120 0.3155        
REMARK   3     5  3.2174 -  2.9868    1.00     1834   146  0.2207 0.3261        
REMARK   3     6  2.9868 -  2.8107    1.00     1799   143  0.2549 0.2659        
REMARK   3     7  2.8107 -  2.6700    0.99     1798   143  0.3221 0.4075        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.200           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 55.93                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           2706                                  
REMARK   3   ANGLE     :  1.304           3680                                  
REMARK   3   CHIRALITY :  0.049            402                                  
REMARK   3   PLANARITY :  0.007            476                                  
REMARK   3   DIHEDRAL  : 16.368            949                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 87 THROUGH 147 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  25.4035  27.1386  10.2626              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3339 T22:   0.5127                                     
REMARK   3      T33:   0.5186 T12:   0.0236                                     
REMARK   3      T13:  -0.0328 T23:  -0.0911                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6401 L22:   5.9231                                     
REMARK   3      L33:   4.5513 L12:   2.0652                                     
REMARK   3      L13:   0.1833 L23:  -2.1618                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1169 S12:  -0.2328 S13:  -0.1394                       
REMARK   3      S21:   0.2511 S22:  -0.3101 S23:  -1.0575                       
REMARK   3      S31:   0.1399 S32:   0.6620 S33:   0.1443                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 148 THROUGH 207 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.7458  20.6886  13.7329              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5081 T22:   0.2821                                     
REMARK   3      T33:   0.3635 T12:  -0.0444                                     
REMARK   3      T13:  -0.0433 T23:  -0.0490                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0548 L22:   2.7607                                     
REMARK   3      L33:   4.5577 L12:   0.1535                                     
REMARK   3      L13:  -0.1441 L23:   0.5903                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0761 S12:  -0.0320 S13:  -0.7159                       
REMARK   3      S21:   0.4231 S22:  -0.3094 S23:  -0.2601                       
REMARK   3      S31:   0.8346 S32:  -0.2583 S33:   0.2354                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 208 THROUGH 247 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.1675  29.5753   0.5633              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3632 T22:   0.4182                                     
REMARK   3      T33:   0.4755 T12:   0.0455                                     
REMARK   3      T13:  -0.0582 T23:  -0.1341                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8107 L22:   2.6802                                     
REMARK   3      L33:   3.0647 L12:   2.8080                                     
REMARK   3      L13:  -0.5366 L23:  -2.1117                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0055 S12:   0.6196 S13:   0.0606                       
REMARK   3      S21:  -0.2623 S22:  -0.0039 S23:   0.7312                       
REMARK   3      S31:   0.2527 S32:  -0.3108 S33:   0.0455                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 90 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.8736  23.6341  20.7732              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5745 T22:   0.3144                                     
REMARK   3      T33:   0.3100 T12:  -0.0607                                     
REMARK   3      T13:   0.0442 T23:  -0.0747                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3852 L22:   3.3491                                     
REMARK   3      L33:   4.1670 L12:   1.4013                                     
REMARK   3      L13:   0.2489 L23:   1.1305                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1652 S12:  -0.3803 S13:   0.4206                       
REMARK   3      S21:   0.7122 S22:  -0.2779 S23:   0.2628                       
REMARK   3      S31:   0.3489 S32:  -0.4264 S33:   0.0686                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 91 THROUGH 179 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.7266   9.3658   8.1272              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4813 T22:   0.3146                                     
REMARK   3      T33:   0.3257 T12:  -0.0965                                     
REMARK   3      T13:   0.0211 T23:  -0.0277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0151 L22:   5.2375                                     
REMARK   3      L33:   3.3935 L12:  -1.1303                                     
REMARK   3      L13:  -0.4156 L23:   3.3570                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0545 S12:   0.2083 S13:   0.0059                       
REMARK   3      S21:   0.2424 S22:  -0.0611 S23:   0.0467                       
REMARK   3      S31:   0.3439 S32:   0.0098 S33:  -0.0069                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6N9D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-DEC-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000238376.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAY-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14162                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.670                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.990                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 20.40                              
REMARK 200  R MERGE                    (I) : 0.24690                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.1100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.67                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.77                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 21.10                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.160                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1UEA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE, 0.1 M SODIUM       
REMARK 280  CACODYLATE: HCL, PH 6.5 18 % (W/V) PEG 8000, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      213.00800            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      106.50400            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      159.75600            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       53.25200            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      266.26000            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      213.00800            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      106.50400            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       53.25200            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      159.75600            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      266.26000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 220  LIES ON A SPECIAL POSITION.                          
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     PHE A    83                                                      
REMARK 465     ARG A    84                                                      
REMARK 465     THR A    85                                                      
REMARK 465     PHE A    86                                                      
REMARK 465     GLY B    53                                                      
REMARK 465     ASP B    54                                                      
REMARK 465     ALA B    55                                                      
REMARK 465     ALA B    56                                                      
REMARK 465     ARG B   180                                                      
REMARK 465     SER B   181                                                      
REMARK 465     GLN B   182                                                      
REMARK 465     ILE B   183                                                      
REMARK 465     ALA B   184                                                      
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     ARG A 233    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B  59    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  75    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 114    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 118    CG   CD   CE   NZ                                   
REMARK 470     LYS B 138    CG   CD   CE   NZ                                   
REMARK 470     LYS B 157    CG   CD   CE   NZ                                   
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLN B   31   CG   CD   OE1  NE2                                  
REMARK 480     GLU B  126   CG   CD   OE1  OE2                                  
REMARK 480     GLU B  156   CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ALA A   167     OG   SER B    68              2.03            
REMARK 500   O    ASN B    78     O    HOH B   201              2.04            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU B  52   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 110       38.55    -75.12                                   
REMARK 500    ASP A 111      -48.72   -156.73                                   
REMARK 500    ARG A 149     -107.07     43.44                                   
REMARK 500    HIS A 151      -50.55     72.60                                   
REMARK 500    ASN A 162     -107.74     52.05                                   
REMARK 500    ASP A 189     -147.10    -98.38                                   
REMARK 500    LEU A 229      -33.07     79.83                                   
REMARK 500    ASN B  30       75.60     49.20                                   
REMARK 500    CYS B  70       31.65     81.61                                   
REMARK 500    ASN B  78     -111.54     65.24                                   
REMARK 500    LYS B 118      -62.43   -133.72                                   
REMARK 500    PRO B 133      -88.69    -71.02                                   
REMARK 500    GLN B 153       50.78   -101.75                                   
REMARK 500    HIS B 163      -13.56   -140.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A  150     HIS A  151                  139.41                    
REMARK 500 HIS B   77     ASN B   78                  136.38                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 302  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 107   OD1                                                    
REMARK 620 2 ASP A 107   OD2  52.4                                              
REMARK 620 3 ASP A 182   O   177.1 125.3                                        
REMARK 620 4 ASP A 182   OD1 105.9  88.1  71.8                                  
REMARK 620 5 GLU A 184   O   109.1  61.3  69.6  93.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 305  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 141   O                                                      
REMARK 620 2 GLY A 173   O   164.7                                              
REMARK 620 3 ASN A 175   O    93.5  81.5                                        
REMARK 620 4 ASP A 177   OD1  86.2  78.8  81.7                                  
REMARK 620 5 HOH A 406   O   111.2  70.1 149.9  83.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 151   NE2                                                    
REMARK 620 2 ASP A 153   OD2 115.5                                              
REMARK 620 3 HIS A 166   NE2 133.4 107.6                                        
REMARK 620 4 HIS A 179   ND1  80.4 100.2 109.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 158   OD1                                                    
REMARK 620 2 GLY A 159   O    85.5                                              
REMARK 620 3 GLY A 161   O    82.9  99.2                                        
REMARK 620 4 VAL A 163   O    92.4 171.3  88.9                                  
REMARK 620 5 ASP A 181   OD2  93.6  77.7 175.5  94.0                            
REMARK 620 6 GLU A 184   OE2 175.2  95.6 101.6  85.9  82.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 304  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 201   NE2                                                    
REMARK 620 2 HIS A 205   NE2  90.4                                              
REMARK 620 3 HIS A 211   NE2 117.9  93.7                                        
REMARK 620 4 CYS B   1   N   110.6  91.4 131.1                                  
REMARK 620 5 CYS B   1   O    82.0 164.3 102.0  78.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 305                  
DBREF  6N9D A   83   247  UNP    P08254   MMP3_HUMAN     100    264             
DBREF  6N9D B    1   184  UNP    P01033   TIMP1_HUMAN     24    207             
SEQADV 6N9D GLY B   34  UNP  P01033    LEU    57 ENGINEERED MUTATION            
SEQADV 6N9D PRO B  133  UNP  P01033    LEU   156 ENGINEERED MUTATION            
SEQADV 6N9D CYS B  151  UNP  P01033    LEU   174 ENGINEERED MUTATION            
SEQADV 6N9D ALA B  154  UNP  P01033    GLY   177 ENGINEERED MUTATION            
SEQRES   1 A  165  PHE ARG THR PHE PRO GLY ILE PRO LYS TRP ARG LYS THR          
SEQRES   2 A  165  HIS LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP LEU          
SEQRES   3 A  165  PRO LYS ASP ALA VAL ASP SER ALA VAL GLU LYS ALA LEU          
SEQRES   4 A  165  LYS VAL TRP GLU GLU VAL THR PRO LEU THR PHE SER ARG          
SEQRES   5 A  165  LEU TYR GLU GLY GLU ALA ASP ILE MET ILE SER PHE ALA          
SEQRES   6 A  165  VAL ARG GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO          
SEQRES   7 A  165  GLY ASN VAL LEU ALA HIS ALA TYR ALA PRO GLY PRO GLY          
SEQRES   8 A  165  ILE ASN GLY ASP ALA HIS PHE ASP ASP ASP GLU GLN TRP          
SEQRES   9 A  165  THR LYS ASP THR THR GLY THR ASN LEU PHE LEU VAL ALA          
SEQRES  10 A  165  ALA HIS GLU ILE GLY HIS SER LEU GLY LEU PHE HIS SER          
SEQRES  11 A  165  ALA ASN THR GLU ALA LEU MET TYR PRO LEU TYR HIS SER          
SEQRES  12 A  165  LEU THR ASP LEU THR ARG PHE ARG LEU SER GLN ASP ASP          
SEQRES  13 A  165  ILE ASN GLY ILE GLN SER LEU TYR GLY                          
SEQRES   1 B  184  CYS THR CYS VAL PRO PRO HIS PRO GLN THR ALA PHE CYS          
SEQRES   2 B  184  ASN SER ASP LEU VAL ILE ARG ALA LYS PHE VAL GLY THR          
SEQRES   3 B  184  PRO GLU VAL ASN GLN THR THR GLY TYR GLN ARG TYR GLU          
SEQRES   4 B  184  ILE LYS MET THR LYS MET TYR LYS GLY PHE GLN ALA LEU          
SEQRES   5 B  184  GLY ASP ALA ALA ASP ILE ARG PHE VAL TYR THR PRO ALA          
SEQRES   6 B  184  MET GLU SER VAL CYS GLY TYR PHE HIS ARG SER HIS ASN          
SEQRES   7 B  184  ARG SER GLU GLU PHE LEU ILE ALA GLY LYS LEU GLN ASP          
SEQRES   8 B  184  GLY LEU LEU HIS ILE THR THR CYS SER PHE VAL ALA PRO          
SEQRES   9 B  184  TRP ASN SER LEU SER LEU ALA GLN ARG ARG GLY PHE THR          
SEQRES  10 B  184  LYS THR TYR THR VAL GLY CYS GLU GLU CYS THR VAL PHE          
SEQRES  11 B  184  PRO CYS PRO SER ILE PRO CYS LYS LEU GLN SER GLY THR          
SEQRES  12 B  184  HIS CYS LEU TRP THR ASP GLN CYS LEU GLN ALA SER GLU          
SEQRES  13 B  184  LYS GLY PHE GLN SER ARG HIS LEU ALA CYS LEU PRO ARG          
SEQRES  14 B  184  GLU PRO GLY LEU CYS THR TRP GLN SER LEU ARG SER GLN          
SEQRES  15 B  184  ILE ALA                                                      
HET     CA  A 301       1                                                       
HET     CA  A 302       1                                                       
HET     ZN  A 303       1                                                       
HET     ZN  A 304       1                                                       
HET     CA  A 305       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      ZN ZINC ION                                                         
FORMUL   3   CA    3(CA 2+)                                                     
FORMUL   5   ZN    2(ZN 2+)                                                     
FORMUL   8  HOH   *46(H2 O)                                                     
HELIX    1 AA1 ASP A  111  GLU A  126  1                                  16    
HELIX    2 AA2 LEU A  195  GLY A  208  1                                  14    
HELIX    3 AA3 SER A  235  GLY A  247  1                                  13    
HELIX    4 AA4 HIS B    7  SER B   15  1                                   9    
HELIX    5 AA5 MET B   66  CYS B   70  5                                   5    
HELIX    6 AA6 ASN B  106  LEU B  108  5                                   3    
HELIX    7 AA7 SER B  109  THR B  117  1                                   9    
HELIX    8 AA8 TYR B  120  GLU B  125  1                                   6    
HELIX    9 AA9 GLN B  153  GLY B  158  1                                   6    
HELIX   10 AB1 GLY B  158  HIS B  163  1                                   6    
SHEET    1 AA1 6 THR A 131  ARG A 134  0                                        
SHEET    2 AA1 6 HIS A  96  ILE A 101  1  N  LEU A  97   O  THR A 131           
SHEET    3 AA1 6 ILE A 142  ALA A 147  1  O  ILE A 144   N  ARG A 100           
SHEET    4 AA1 6 ALA A 178  ASP A 181  1  O  PHE A 180   N  ALA A 147           
SHEET    5 AA1 6 ASN A 162  ALA A 167 -1  N  HIS A 166   O  HIS A 179           
SHEET    6 AA1 6 THR B   2  VAL B   4 -1  O  THR B   2   N  LEU A 164           
SHEET    1 AA2 2 TRP A 186  THR A 187  0                                        
SHEET    2 AA2 2 THR A 193  ASN A 194  1  O  THR A 193   N  THR A 187           
SHEET    1 AA3 7 PHE B 101  PRO B 104  0                                        
SHEET    2 AA3 7 PHE B  83  GLN B  90 -1  N  LEU B  84   O  ALA B 103           
SHEET    3 AA3 7 LEU B  93  HIS B  95 -1  O  HIS B  95   N  LYS B  88           
SHEET    4 AA3 7 PHE B  60  PRO B  64  1  N  TYR B  62   O  LEU B  94           
SHEET    5 AA3 7 TYR B  35  LYS B  47 -1  N  GLN B  36   O  THR B  63           
SHEET    6 AA3 7 LEU B  17  PHE B  23 -1  N  ARG B  20   O  THR B  43           
SHEET    7 AA3 7 PHE B  83  GLN B  90 -1  O  ILE B  85   N  ILE B  19           
SHEET    1 AA4 2 THR B 128  PRO B 131  0                                        
SHEET    2 AA4 2 HIS B 144  TRP B 147  1  O  CYS B 145   N  THR B 128           
SHEET    1 AA5 2 LEU B 164  GLU B 170  0                                        
SHEET    2 AA5 2 LEU B 173  SER B 178 -1  O  GLN B 177   N  ALA B 165           
SSBOND   1 CYS B    1    CYS B   70                          1555   1555  2.04  
SSBOND   2 CYS B    3    CYS B   99                          1555   1555  2.03  
SSBOND   3 CYS B   13    CYS B  124                          1555   1555  2.04  
SSBOND   4 CYS B  127    CYS B  174                          1555   1555  2.06  
SSBOND   5 CYS B  132    CYS B  137                          1555   1555  2.04  
SSBOND   6 CYS B  145    CYS B  166                          1555   1555  2.04  
LINK         OD1 ASP A 107                CA    CA A 302     1555   1555  2.56  
LINK         OD2 ASP A 107                CA    CA A 302     1555   1555  2.43  
LINK         O   ASP A 141                CA    CA A 305     1555   1555  2.36  
LINK         NE2 HIS A 151                ZN    ZN A 303     1555   1555  2.30  
LINK         OD2 ASP A 153                ZN    ZN A 303     1555   1555  2.37  
LINK         OD1 ASP A 158                CA    CA A 301     1555   1555  2.37  
LINK         O   GLY A 159                CA    CA A 301     1555   1555  2.27  
LINK         O   GLY A 161                CA    CA A 301     1555   1555  2.45  
LINK         O   VAL A 163                CA    CA A 301     1555   1555  2.22  
LINK         NE2 HIS A 166                ZN    ZN A 303     1555   1555  2.09  
LINK         O   GLY A 173                CA    CA A 305     1555   1555  2.39  
LINK         O   ASN A 175                CA    CA A 305     1555   1555  2.32  
LINK         OD1 ASP A 177                CA    CA A 305     1555   1555  2.74  
LINK         ND1 HIS A 179                ZN    ZN A 303     1555   1555  1.99  
LINK         OD2 ASP A 181                CA    CA A 301     1555   1555  2.52  
LINK         O   ASP A 182                CA    CA A 302     1555   1555  2.42  
LINK         OD1 ASP A 182                CA    CA A 302     1555   1555  2.54  
LINK         OE2 GLU A 184                CA    CA A 301     1555   1555  2.46  
LINK         O   GLU A 184                CA    CA A 302     1555   1555  3.11  
LINK         NE2 HIS A 201                ZN    ZN A 304     1555   1555  2.03  
LINK         NE2 HIS A 205                ZN    ZN A 304     1555   1555  2.24  
LINK         NE2 HIS A 211                ZN    ZN A 304     1555   1555  1.99  
LINK        ZN    ZN A 304                 N   CYS B   1     1555   1555  2.18  
LINK        ZN    ZN A 304                 O   CYS B   1     1555   1555  2.36  
LINK        CA    CA A 305                 O   HOH A 406     1555   1555  2.49  
CISPEP   1 ASN B   78    ARG B   79          0       -22.11                     
CISPEP   2 ILE B  135    PRO B  136          0         2.73                     
SITE     1 AC1  6 ASP A 158  GLY A 159  GLY A 161  VAL A 163                    
SITE     2 AC1  6 ASP A 181  GLU A 184                                          
SITE     1 AC2  4 THR A 105  ASP A 107  ASP A 182  GLU A 184                    
SITE     1 AC3  4 HIS A 151  ASP A 153  HIS A 166  HIS A 179                    
SITE     1 AC4  4 HIS A 201  HIS A 205  HIS A 211  CYS B   1                    
SITE     1 AC5  6 ALA A 140  ASP A 141  GLY A 173  ASN A 175                    
SITE     2 AC5  6 ASP A 177  HOH A 406                                          
CRYST1   70.031   70.031  319.512  90.00  90.00 120.00 P 65 2 2     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014279  0.008244  0.000000        0.00000                         
SCALE2      0.000000  0.016488  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003130        0.00000                         
ATOM      1  N   PRO A  87       7.821  46.970  18.178  1.00101.82           N  
ATOM      2  CA  PRO A  87       7.074  45.754  17.833  1.00103.45           C  
ATOM      3  C   PRO A  87       8.021  44.580  17.543  1.00103.30           C  
ATOM      4  O   PRO A  87       7.614  43.412  17.567  1.00 92.64           O  
ATOM      5  CB  PRO A  87       6.277  46.174  16.596  1.00103.30           C  
ATOM      6  CG  PRO A  87       6.212  47.680  16.675  1.00105.12           C  
ATOM      7  CD  PRO A  87       7.517  48.088  17.271  1.00102.21           C  
ATOM      8  N   GLY A  88       9.281  44.916  17.270  1.00109.64           N  
ATOM      9  CA  GLY A  88      10.371  43.958  17.278  1.00103.45           C  
ATOM     10  C   GLY A  88      10.562  43.108  16.041  1.00100.34           C  
ATOM     11  O   GLY A  88       9.945  42.051  15.914  1.00103.82           O  
ATOM     12  N   ILE A  89      11.431  43.554  15.135  1.00 87.49           N  
ATOM     13  CA  ILE A  89      11.830  42.719  14.003  1.00 73.77           C  
ATOM     14  C   ILE A  89      13.265  42.215  14.132  1.00 62.38           C  
ATOM     15  O   ILE A  89      14.224  42.937  13.843  1.00 53.50           O  
ATOM     16  CB  ILE A  89      11.725  43.450  12.671  1.00 70.69           C  
ATOM     17  CG1 ILE A  89      10.480  44.322  12.637  1.00 74.82           C  
ATOM     18  CG2 ILE A  89      11.740  42.438  11.522  1.00 61.01           C  
ATOM     19  CD1 ILE A  89      10.379  45.135  11.376  1.00 79.82           C  
ATOM     20  N   PRO A  90      13.411  40.950  14.523  1.00 62.18           N  
ATOM     21  CA  PRO A  90      14.719  40.366  14.803  1.00 58.01           C  
ATOM     22  C   PRO A  90      15.568  40.197  13.550  1.00 55.63           C  
ATOM     23  O   PRO A  90      15.131  39.665  12.526  1.00 63.04           O  
ATOM     24  CB  PRO A  90      14.365  39.009  15.391  1.00 64.75           C  
ATOM     25  CG  PRO A  90      13.103  38.631  14.649  1.00 69.40           C  
ATOM     26  CD  PRO A  90      12.346  39.933  14.504  1.00 71.15           C  
ATOM     27  N   LYS A  91      16.792  40.682  13.645  1.00 48.22           N  
ATOM     28  CA  LYS A  91      17.800  40.409  12.654  1.00 45.15           C  
ATOM     29  C   LYS A  91      19.124  40.449  13.386  1.00 43.95           C  
ATOM     30  O   LYS A  91      19.262  41.146  14.392  1.00 46.76           O  
ATOM     31  CB  LYS A  91      17.756  41.420  11.499  1.00 49.87           C  
ATOM     32  CG  LYS A  91      18.090  42.848  11.899  1.00 54.45           C  
ATOM     33  CD  LYS A  91      18.278  43.753  10.698  1.00 57.11           C  
ATOM     34  CE  LYS A  91      19.755  43.950  10.388  1.00 70.89           C  
ATOM     35  NZ  LYS A  91      20.007  45.005   9.354  1.00 85.09           N  
ATOM     36  N   TRP A  92      20.078  39.665  12.905  1.00 42.10           N  
ATOM     37  CA  TRP A  92      21.441  39.742  13.388  1.00 43.38           C  
ATOM     38  C   TRP A  92      21.964  41.155  13.185  1.00 45.80           C  
ATOM     39  O   TRP A  92      21.694  41.785  12.168  1.00 45.47           O  
ATOM     40  CB  TRP A  92      22.314  38.726  12.657  1.00 44.96           C  
ATOM     41  CG  TRP A  92      22.063  37.314  13.099  1.00 51.56           C  
ATOM     42  CD1 TRP A  92      21.422  36.336  12.402  1.00 48.36           C  
ATOM     43  CD2 TRP A  92      22.437  36.732  14.354  1.00 44.15           C  
ATOM     44  NE1 TRP A  92      21.387  35.177  13.137  1.00 36.94           N  
ATOM     45  CE2 TRP A  92      22.000  35.397  14.341  1.00 40.79           C  
ATOM     46  CE3 TRP A  92      23.104  37.209  15.479  1.00 43.85           C  
ATOM     47  CZ2 TRP A  92      22.206  34.539  15.420  1.00 39.92           C  
ATOM     48  CZ3 TRP A  92      23.312  36.366  16.523  1.00 44.69           C  
ATOM     49  CH2 TRP A  92      22.864  35.047  16.498  1.00 42.71           C  
ATOM     50  N   ARG A  93      22.710  41.662  14.153  1.00 56.23           N  
ATOM     51  CA  ARG A  93      23.282  42.998  14.015  1.00 55.36           C  
ATOM     52  C   ARG A  93      24.668  42.992  13.350  1.00 60.06           C  
ATOM     53  O   ARG A  93      25.125  44.015  12.888  1.00 61.30           O  
ATOM     54  CB  ARG A  93      23.328  43.671  15.377  1.00 59.53           C  
ATOM     55  CG  ARG A  93      21.963  44.220  15.793  1.00 68.62           C  
ATOM     56  CD  ARG A  93      21.780  44.244  17.310  1.00 88.08           C  
ATOM     57  NE  ARG A  93      23.009  44.581  18.026  1.00101.76           N  
ATOM     58  CZ  ARG A  93      23.330  44.114  19.233  1.00107.38           C  
ATOM     59  NH1 ARG A  93      22.508  43.282  19.864  1.00103.63           N  
ATOM     60  NH2 ARG A  93      24.474  44.478  19.810  1.00111.82           N  
ATOM     61  N   LYS A  94      25.315  41.834  13.270  1.00 63.59           N  
ATOM     62  CA  LYS A  94      26.538  41.682  12.483  1.00 59.26           C  
ATOM     63  C   LYS A  94      26.176  41.000  11.150  1.00 57.76           C  
ATOM     64  O   LYS A  94      25.127  40.373  11.055  1.00 53.41           O  
ATOM     65  CB  LYS A  94      27.583  40.874  13.266  1.00 56.73           C  
ATOM     66  CG  LYS A  94      26.980  39.706  14.051  1.00 65.42           C  
ATOM     67  CD  LYS A  94      28.008  38.933  14.866  1.00 70.14           C  
ATOM     68  CE  LYS A  94      27.315  38.135  15.972  1.00 72.06           C  
ATOM     69  NZ  LYS A  94      28.243  37.446  16.923  1.00 76.16           N  
ATOM     70  N   THR A  95      27.011  41.129  10.119  1.00 66.75           N  
ATOM     71  CA  THR A  95      26.731  40.448   8.840  1.00 62.58           C  
ATOM     72  C   THR A  95      27.555  39.172   8.702  1.00 53.94           C  
ATOM     73  O   THR A  95      27.199  38.267   7.948  1.00 52.49           O  
ATOM     74  CB  THR A  95      27.006  41.348   7.604  1.00 66.06           C  
ATOM     75  OG1 THR A  95      28.410  41.356   7.297  1.00 68.55           O  
ATOM     76  CG2 THR A  95      26.504  42.762   7.844  1.00 70.81           C  
ATOM     77  N   HIS A  96      28.658  39.104   9.437  1.00 53.15           N  
ATOM     78  CA  HIS A  96      29.420  37.874   9.529  1.00 46.47           C  
ATOM     79  C   HIS A  96      28.950  36.994  10.711  1.00 55.35           C  
ATOM     80  O   HIS A  96      29.060  37.377  11.878  1.00 63.80           O  
ATOM     81  CB  HIS A  96      30.905  38.194   9.651  1.00 49.87           C  
ATOM     82  CG  HIS A  96      31.773  36.979   9.694  1.00 66.10           C  
ATOM     83  ND1 HIS A  96      31.854  36.087   8.645  1.00 71.65           N  
ATOM     84  CD2 HIS A  96      32.578  36.492  10.667  1.00 66.61           C  
ATOM     85  CE1 HIS A  96      32.677  35.107   8.969  1.00 77.37           C  
ATOM     86  NE2 HIS A  96      33.132  35.330  10.190  1.00 73.90           N  
ATOM     87  N   LEU A  97      28.416  35.817  10.409  1.00 48.47           N  
ATOM     88  CA  LEU A  97      27.980  34.897  11.455  1.00 46.41           C  
ATOM     89  C   LEU A  97      28.870  33.676  11.558  1.00 48.79           C  
ATOM     90  O   LEU A  97      29.653  33.390  10.660  1.00 53.51           O  
ATOM     91  CB  LEU A  97      26.531  34.425  11.228  1.00 39.91           C  
ATOM     92  CG  LEU A  97      25.285  35.319  11.378  1.00 38.98           C  
ATOM     93  CD1 LEU A  97      25.598  36.621  12.057  1.00 41.29           C  
ATOM     94  CD2 LEU A  97      24.586  35.557  10.041  1.00 37.26           C  
ATOM     95  N   THR A  98      28.719  32.946  12.657  1.00 57.51           N  
ATOM     96  CA  THR A  98      29.373  31.652  12.827  1.00 61.13           C  
ATOM     97  C   THR A  98      28.369  30.534  13.085  1.00 43.08           C  
ATOM     98  O   THR A  98      27.248  30.780  13.507  1.00 42.24           O  
ATOM     99  CB  THR A  98      30.391  31.668  13.983  1.00 59.52           C  
ATOM    100  OG1 THR A  98      29.824  32.341  15.114  1.00 60.88           O  
ATOM    101  CG2 THR A  98      31.665  32.363  13.551  1.00 51.31           C  
ATOM    102  N   TYR A  99      28.791  29.305  12.822  1.00 43.56           N  
ATOM    103  CA  TYR A  99      27.942  28.130  12.989  1.00 48.22           C  
ATOM    104  C   TYR A  99      28.774  26.914  13.401  1.00 50.29           C  
ATOM    105  O   TYR A  99      29.960  26.775  13.054  1.00 46.80           O  
ATOM    106  CB  TYR A  99      27.151  27.818  11.700  1.00 43.78           C  
ATOM    107  CG  TYR A  99      27.951  27.178  10.584  1.00 40.64           C  
ATOM    108  CD1 TYR A  99      28.687  27.951   9.698  1.00 44.21           C  
ATOM    109  CD2 TYR A  99      27.979  25.796  10.426  1.00 48.25           C  
ATOM    110  CE1 TYR A  99      29.432  27.364   8.678  1.00 54.29           C  
ATOM    111  CE2 TYR A  99      28.717  25.197   9.406  1.00 56.36           C  
ATOM    112  CZ  TYR A  99      29.437  25.987   8.532  1.00 59.33           C  
ATOM    113  OH  TYR A  99      30.167  25.407   7.517  1.00 60.65           O  
ATOM    114  N   ARG A 100      28.147  26.033  14.159  1.00 44.08           N  
ATOM    115  CA  ARG A 100      28.822  24.830  14.569  1.00 48.65           C  
ATOM    116  C   ARG A 100      27.840  23.686  14.553  1.00 50.69           C  
ATOM    117  O   ARG A 100      26.703  23.829  15.000  1.00 43.10           O  
ATOM    118  CB  ARG A 100      29.444  24.991  15.955  1.00 51.09           C  
ATOM    119  CG  ARG A 100      29.805  23.659  16.586  1.00 56.62           C  
ATOM    120  CD  ARG A 100      30.811  23.787  17.702  1.00 67.93           C  
ATOM    121  NE  ARG A 100      30.955  22.510  18.390  1.00 75.77           N  
ATOM    122  CZ  ARG A 100      30.910  22.370  19.710  1.00 76.70           C  
ATOM    123  NH1 ARG A 100      30.737  23.436  20.478  1.00 73.96           N  
ATOM    124  NH2 ARG A 100      31.030  21.168  20.258  1.00 73.46           N  
ATOM    125  N   ILE A 101      28.275  22.561  14.003  1.00 52.28           N  
ATOM    126  CA  ILE A 101      27.479  21.356  14.049  1.00 52.12           C  
ATOM    127  C   ILE A 101      27.943  20.606  15.267  1.00 54.08           C  
ATOM    128  O   ILE A 101      28.995  19.969  15.265  1.00 64.22           O  
ATOM    129  CB  ILE A 101      27.633  20.499  12.790  1.00 55.35           C  
ATOM    130  CG1 ILE A 101      27.214  21.294  11.556  1.00 52.82           C  
ATOM    131  CG2 ILE A 101      26.809  19.234  12.912  1.00 53.07           C  
ATOM    132  CD1 ILE A 101      27.810  20.756  10.283  1.00 56.71           C  
ATOM    133  N   VAL A 102      27.144  20.696  16.312  1.00 49.20           N  
ATOM    134  CA  VAL A 102      27.537  20.218  17.616  1.00 59.40           C  
ATOM    135  C   VAL A 102      27.332  18.723  17.746  1.00 68.87           C  
ATOM    136  O   VAL A 102      27.715  18.106  18.733  1.00 74.60           O  
ATOM    137  CB  VAL A 102      26.725  20.930  18.694  1.00 58.32           C  
ATOM    138  CG1 VAL A 102      27.445  20.867  20.024  1.00 63.78           C  
ATOM    139  CG2 VAL A 102      26.485  22.378  18.279  1.00 50.61           C  
ATOM    140  N   ASN A 103      26.747  18.132  16.722  1.00 71.48           N  
ATOM    141  CA  ASN A 103      26.012  16.909  16.929  1.00 61.72           C  
ATOM    142  C   ASN A 103      25.738  16.207  15.620  1.00 60.27           C  
ATOM    143  O   ASN A 103      25.526  16.866  14.611  1.00 59.85           O  
ATOM    144  CB  ASN A 103      24.707  17.258  17.623  1.00 56.13           C  
ATOM    145  CG  ASN A 103      24.134  16.117  18.332  1.00 52.16           C  
ATOM    146  OD1 ASN A 103      24.841  15.177  18.651  1.00 55.13           O  
ATOM    147  ND2 ASN A 103      22.845  16.176  18.610  1.00 52.67           N  
ATOM    148  N   TYR A 104      25.715  14.882  15.615  1.00 63.66           N  
ATOM    149  CA  TYR A 104      25.484  14.189  14.354  1.00 62.01           C  
ATOM    150  C   TYR A 104      24.426  13.098  14.402  1.00 57.60           C  
ATOM    151  O   TYR A 104      24.456  12.237  15.267  1.00 56.18           O  
ATOM    152  CB  TYR A 104      26.795  13.602  13.845  1.00 55.30           C  
ATOM    153  CG  TYR A 104      27.688  14.644  13.228  1.00 55.07           C  
ATOM    154  CD1 TYR A 104      28.794  15.133  13.908  1.00 59.58           C  
ATOM    155  CD2 TYR A 104      27.411  15.160  11.975  1.00 56.50           C  
ATOM    156  CE1 TYR A 104      29.611  16.091  13.352  1.00 62.92           C  
ATOM    157  CE2 TYR A 104      28.223  16.127  11.409  1.00 64.39           C  
ATOM    158  CZ  TYR A 104      29.323  16.587  12.102  1.00 66.70           C  
ATOM    159  OH  TYR A 104      30.132  17.550  11.543  1.00 71.64           O  
ATOM    160  N   THR A 105      23.495  13.134  13.454  1.00 52.58           N  
ATOM    161  CA  THR A 105      22.560  12.032  13.289  1.00 50.05           C  
ATOM    162  C   THR A 105      23.249  10.796  12.694  1.00 61.90           C  
ATOM    163  O   THR A 105      24.124  10.908  11.825  1.00 60.46           O  
ATOM    164  CB  THR A 105      21.376  12.419  12.396  1.00 51.46           C  
ATOM    165  OG1 THR A 105      20.448  11.331  12.338  1.00 57.05           O  
ATOM    166  CG2 THR A 105      21.841  12.760  10.982  1.00 49.66           C  
ATOM    167  N   PRO A 106      22.866   9.606  13.184  1.00 66.28           N  
ATOM    168  CA  PRO A 106      23.343   8.313  12.678  1.00 65.88           C  
ATOM    169  C   PRO A 106      22.747   7.917  11.326  1.00 59.69           C  
ATOM    170  O   PRO A 106      23.201   6.942  10.738  1.00 67.74           O  
ATOM    171  CB  PRO A 106      22.888   7.322  13.761  1.00 61.83           C  
ATOM    172  CG  PRO A 106      22.597   8.141  14.950  1.00 59.69           C  
ATOM    173  CD  PRO A 106      22.097   9.446  14.427  1.00 59.20           C  
ATOM    174  N   ASP A 107      21.756   8.662  10.849  1.00 56.13           N  
ATOM    175  CA  ASP A 107      21.064   8.332   9.613  1.00 56.17           C  
ATOM    176  C   ASP A 107      21.871   8.705   8.384  1.00 56.90           C  
ATOM    177  O   ASP A 107      21.451   8.470   7.246  1.00 63.43           O  
ATOM    178  CB  ASP A 107      19.718   9.041   9.559  1.00 52.56           C  
ATOM    179  CG  ASP A 107      18.998   9.036  10.886  1.00 63.80           C  
ATOM    180  OD1 ASP A 107      19.375   8.239  11.779  1.00 75.29           O  
ATOM    181  OD2 ASP A 107      18.049   9.836  11.027  1.00 52.34           O  
ATOM    182  N   LEU A 108      23.026   9.304   8.628  1.00 57.22           N  
ATOM    183  CA  LEU A 108      23.871   9.852   7.578  1.00 57.85           C  
ATOM    184  C   LEU A 108      25.324   9.778   7.997  1.00 60.76           C  
ATOM    185  O   LEU A 108      25.616   9.721   9.188  1.00 61.14           O  
ATOM    186  CB  LEU A 108      23.500  11.307   7.278  1.00 53.73           C  
ATOM    187  CG  LEU A 108      22.269  11.579   6.421  1.00 54.87           C  
ATOM    188  CD1 LEU A 108      22.113  13.080   6.168  1.00 58.06           C  
ATOM    189  CD2 LEU A 108      22.412  10.835   5.125  1.00 54.58           C  
ATOM    190  N   PRO A 109      26.240   9.757   7.019  1.00 67.89           N  
ATOM    191  CA  PRO A 109      27.665   9.941   7.307  1.00 71.23           C  
ATOM    192  C   PRO A 109      27.942  11.316   7.899  1.00 69.32           C  
ATOM    193  O   PRO A 109      27.180  12.254   7.666  1.00 68.55           O  
ATOM    194  CB  PRO A 109      28.318   9.785   5.936  1.00 72.37           C  
ATOM    195  CG  PRO A 109      27.403   8.865   5.213  1.00 71.10           C  
ATOM    196  CD  PRO A 109      26.021   9.257   5.650  1.00 67.26           C  
ATOM    197  N   LYS A 110      29.028  11.431   8.654  1.00 76.03           N  
ATOM    198  CA  LYS A 110      29.349  12.652   9.388  1.00 83.16           C  
ATOM    199  C   LYS A 110      29.866  13.715   8.436  1.00 88.34           C  
ATOM    200  O   LYS A 110      30.760  14.488   8.772  1.00104.30           O  
ATOM    201  CB  LYS A 110      30.389  12.353  10.474  1.00 88.58           C  
ATOM    202  CG  LYS A 110      31.521  11.437   9.996  1.00 96.53           C  
ATOM    203  CD  LYS A 110      32.511  11.107  11.110  1.00 95.08           C  
ATOM    204  CE  LYS A 110      33.841  10.618  10.548  1.00 91.56           C  
ATOM    205  NZ  LYS A 110      34.907  10.613  11.584  1.00 89.23           N  
ATOM    206  N   ASP A 111      29.266  13.771   7.258  1.00 78.31           N  
ATOM    207  CA  ASP A 111      29.959  14.269   6.089  1.00 82.24           C  
ATOM    208  C   ASP A 111      28.956  14.761   5.064  1.00 75.06           C  
ATOM    209  O   ASP A 111      29.082  15.851   4.506  1.00 68.98           O  
ATOM    210  CB  ASP A 111      30.831  13.146   5.516  1.00 91.07           C  
ATOM    211  CG  ASP A 111      31.499  13.525   4.223  1.00100.56           C  
ATOM    212  OD1 ASP A 111      30.801  13.554   3.186  1.00102.66           O  
ATOM    213  OD2 ASP A 111      32.727  13.769   4.238  1.00106.32           O  
ATOM    214  N   ALA A 112      27.966  13.922   4.806  1.00 73.15           N  
ATOM    215  CA  ALA A 112      26.815  14.329   4.036  1.00 55.98           C  
ATOM    216  C   ALA A 112      26.091  15.365   4.863  1.00 51.50           C  
ATOM    217  O   ALA A 112      25.602  16.376   4.346  1.00 53.70           O  
ATOM    218  CB  ALA A 112      25.920  13.144   3.731  1.00 57.63           C  
ATOM    219  N   VAL A 113      26.032  15.095   6.163  1.00 54.17           N  
ATOM    220  CA  VAL A 113      25.477  16.033   7.129  1.00 55.61           C  
ATOM    221  C   VAL A 113      26.099  17.416   6.961  1.00 54.84           C  
ATOM    222  O   VAL A 113      25.385  18.420   6.904  1.00 45.87           O  
ATOM    223  CB  VAL A 113      25.695  15.538   8.573  1.00 58.77           C  
ATOM    224  CG1 VAL A 113      25.276  16.604   9.577  1.00 45.66           C  
ATOM    225  CG2 VAL A 113      24.933  14.232   8.797  1.00 62.65           C  
ATOM    226  N   ASP A 114      27.426  17.456   6.855  1.00 59.89           N  
ATOM    227  CA  ASP A 114      28.139  18.718   6.664  1.00 61.03           C  
ATOM    228  C   ASP A 114      27.686  19.406   5.365  1.00 62.01           C  
ATOM    229  O   ASP A 114      27.333  20.587   5.376  1.00 59.15           O  
ATOM    230  CB  ASP A 114      29.660  18.492   6.664  1.00 64.50           C  
ATOM    231  CG  ASP A 114      30.222  18.156   8.061  1.00 68.92           C  
ATOM    232  OD1 ASP A 114      29.500  18.363   9.056  1.00 68.28           O  
ATOM    233  OD2 ASP A 114      31.393  17.694   8.167  1.00 58.69           O  
ATOM    234  N   SER A 115      27.664  18.661   4.262  1.00 60.88           N  
ATOM    235  CA  SER A 115      27.239  19.211   2.975  1.00 60.51           C  
ATOM    236  C   SER A 115      25.844  19.793   3.076  1.00 50.63           C  
ATOM    237  O   SER A 115      25.604  20.907   2.625  1.00 51.08           O  
ATOM    238  CB  SER A 115      27.271  18.149   1.874  1.00 69.81           C  
ATOM    239  OG  SER A 115      28.496  17.443   1.880  1.00 78.79           O  
ATOM    240  N   ALA A 116      24.936  19.038   3.684  1.00 44.77           N  
ATOM    241  CA  ALA A 116      23.570  19.503   3.875  1.00 40.59           C  
ATOM    242  C   ALA A 116      23.551  20.887   4.485  1.00 42.56           C  
ATOM    243  O   ALA A 116      23.020  21.830   3.885  1.00 44.16           O  
ATOM    244  CB  ALA A 116      22.804  18.551   4.733  1.00 40.19           C  
ATOM    245  N   VAL A 117      24.145  21.017   5.667  1.00 48.92           N  
ATOM    246  CA  VAL A 117      24.191  22.307   6.357  1.00 46.83           C  
ATOM    247  C   VAL A 117      24.848  23.342   5.469  1.00 39.65           C  
ATOM    248  O   VAL A 117      24.305  24.429   5.285  1.00 41.11           O  
ATOM    249  CB  VAL A 117      24.961  22.230   7.695  1.00 47.67           C  
ATOM    250  CG1 VAL A 117      25.063  23.615   8.357  1.00 42.27           C  
ATOM    251  CG2 VAL A 117      24.301  21.258   8.620  1.00 44.32           C  
ATOM    252  N   GLU A 118      26.007  22.990   4.911  1.00 47.62           N  
ATOM    253  CA  GLU A 118      26.745  23.905   4.033  1.00 56.94           C  
ATOM    254  C   GLU A 118      25.856  24.470   2.922  1.00 47.84           C  
ATOM    255  O   GLU A 118      25.749  25.688   2.769  1.00 40.68           O  
ATOM    256  CB  GLU A 118      27.971  23.212   3.433  1.00 69.74           C  
ATOM    257  CG  GLU A 118      29.071  22.902   4.450  1.00 87.50           C  
ATOM    258  CD  GLU A 118      30.250  22.141   3.850  1.00109.96           C  
ATOM    259  OE1 GLU A 118      30.161  21.715   2.675  1.00120.09           O  
ATOM    260  OE2 GLU A 118      31.265  21.960   4.559  1.00115.44           O  
ATOM    261  N   LYS A 119      25.189  23.596   2.180  1.00 39.71           N  
ATOM    262  CA  LYS A 119      24.288  24.050   1.134  1.00 47.15           C  
ATOM    263  C   LYS A 119      23.163  24.927   1.693  1.00 49.90           C  
ATOM    264  O   LYS A 119      22.790  25.940   1.090  1.00 44.12           O  
ATOM    265  CB  LYS A 119      23.703  22.859   0.363  1.00 57.86           C  
ATOM    266  CG  LYS A 119      24.708  22.140  -0.530  1.00 66.15           C  
ATOM    267  CD  LYS A 119      25.678  23.145  -1.138  1.00 73.08           C  
ATOM    268  CE  LYS A 119      25.767  23.044  -2.645  1.00 77.61           C  
ATOM    269  NZ  LYS A 119      26.499  24.237  -3.144  1.00 77.81           N  
ATOM    270  N   ALA A 120      22.633  24.559   2.851  1.00 47.12           N  
ATOM    271  CA  ALA A 120      21.512  25.309   3.402  1.00 32.43           C  
ATOM    272  C   ALA A 120      21.939  26.699   3.843  1.00 38.42           C  
ATOM    273  O   ALA A 120      21.163  27.635   3.755  1.00 44.40           O  
ATOM    274  CB  ALA A 120      20.895  24.568   4.536  1.00 31.63           C  
ATOM    275  N   LEU A 121      23.167  26.843   4.328  1.00 40.31           N  
ATOM    276  CA  LEU A 121      23.681  28.173   4.632  1.00 40.91           C  
ATOM    277  C   LEU A 121      23.913  28.944   3.337  1.00 50.80           C  
ATOM    278  O   LEU A 121      23.811  30.169   3.280  1.00 51.17           O  
ATOM    279  CB  LEU A 121      24.981  28.089   5.412  1.00 35.22           C  
ATOM    280  CG  LEU A 121      24.920  27.553   6.836  1.00 37.27           C  
ATOM    281  CD1 LEU A 121      26.326  27.219   7.248  1.00 36.79           C  
ATOM    282  CD2 LEU A 121      24.299  28.585   7.787  1.00 33.35           C  
ATOM    283  N   LYS A 122      24.222  28.199   2.286  1.00 46.36           N  
ATOM    284  CA  LYS A 122      24.664  28.797   1.052  1.00 41.05           C  
ATOM    285  C   LYS A 122      23.488  29.425   0.290  1.00 43.45           C  
ATOM    286  O   LYS A 122      23.659  30.424  -0.400  1.00 41.67           O  
ATOM    287  CB  LYS A 122      25.397  27.734   0.221  1.00 41.10           C  
ATOM    288  CG  LYS A 122      25.919  28.196  -1.118  1.00 51.72           C  
ATOM    289  CD  LYS A 122      27.420  27.985  -1.223  1.00 74.33           C  
ATOM    290  CE  LYS A 122      28.170  28.818  -0.183  1.00 86.34           C  
ATOM    291  NZ  LYS A 122      29.576  29.116  -0.603  1.00 95.37           N  
ATOM    292  N   VAL A 123      22.287  28.872   0.436  1.00 42.92           N  
ATOM    293  CA  VAL A 123      21.153  29.420  -0.303  1.00 36.99           C  
ATOM    294  C   VAL A 123      20.881  30.831   0.171  1.00 45.26           C  
ATOM    295  O   VAL A 123      20.498  31.702  -0.621  1.00 46.08           O  
ATOM    296  CB  VAL A 123      19.854  28.573  -0.161  1.00 41.80           C  
ATOM    297  CG1 VAL A 123      20.056  27.144  -0.659  1.00 34.00           C  
ATOM    298  CG2 VAL A 123      19.352  28.566   1.261  1.00 42.46           C  
ATOM    299  N   TRP A 124      21.105  31.063   1.462  1.00 47.55           N  
ATOM    300  CA  TRP A 124      20.869  32.375   2.052  1.00 43.28           C  
ATOM    301  C   TRP A 124      22.044  33.343   1.832  1.00 37.82           C  
ATOM    302  O   TRP A 124      21.844  34.532   1.616  1.00 44.25           O  
ATOM    303  CB  TRP A 124      20.558  32.222   3.535  1.00 37.65           C  
ATOM    304  CG  TRP A 124      19.287  31.464   3.769  1.00 36.44           C  
ATOM    305  CD1 TRP A 124      19.160  30.251   4.369  1.00 38.06           C  
ATOM    306  CD2 TRP A 124      17.965  31.867   3.399  1.00 32.14           C  
ATOM    307  NE1 TRP A 124      17.845  29.868   4.390  1.00 33.35           N  
ATOM    308  CE2 TRP A 124      17.089  30.845   3.805  1.00 34.23           C  
ATOM    309  CE3 TRP A 124      17.436  32.997   2.765  1.00 35.09           C  
ATOM    310  CZ2 TRP A 124      15.709  30.911   3.592  1.00 41.51           C  
ATOM    311  CZ3 TRP A 124      16.068  33.062   2.552  1.00 35.64           C  
ATOM    312  CH2 TRP A 124      15.218  32.027   2.965  1.00 37.74           C  
ATOM    313  N   GLU A 125      23.262  32.827   1.852  1.00 33.98           N  
ATOM    314  CA  GLU A 125      24.432  33.655   1.633  1.00 38.92           C  
ATOM    315  C   GLU A 125      24.512  34.190   0.191  1.00 46.84           C  
ATOM    316  O   GLU A 125      25.083  35.251  -0.055  1.00 52.69           O  
ATOM    317  CB  GLU A 125      25.693  32.859   1.975  1.00 41.85           C  
ATOM    318  CG  GLU A 125      26.971  33.624   1.754  1.00 60.00           C  
ATOM    319  CD  GLU A 125      27.951  32.866   0.904  1.00 80.85           C  
ATOM    320  OE1 GLU A 125      28.185  31.679   1.216  1.00 87.46           O  
ATOM    321  OE2 GLU A 125      28.475  33.453  -0.073  1.00 88.46           O  
ATOM    322  N   GLU A 126      23.937  33.455  -0.758  1.00 47.10           N  
ATOM    323  CA  GLU A 126      24.063  33.792  -2.178  1.00 38.88           C  
ATOM    324  C   GLU A 126      23.265  35.014  -2.584  1.00 46.19           C  
ATOM    325  O   GLU A 126      23.540  35.620  -3.616  1.00 46.24           O  
ATOM    326  CB  GLU A 126      23.613  32.636  -3.051  1.00 45.64           C  
ATOM    327  CG  GLU A 126      24.640  31.576  -3.300  1.00 63.22           C  
ATOM    328  CD  GLU A 126      24.029  30.395  -4.007  1.00 79.68           C  
ATOM    329  OE1 GLU A 126      22.778  30.335  -4.055  1.00 76.27           O  
ATOM    330  OE2 GLU A 126      24.793  29.542  -4.510  1.00 90.40           O  
ATOM    331  N   VAL A 127      22.268  35.368  -1.782  1.00 47.98           N  
ATOM    332  CA  VAL A 127      21.395  36.488  -2.114  1.00 47.02           C  
ATOM    333  C   VAL A 127      21.517  37.666  -1.139  1.00 40.12           C  
ATOM    334  O   VAL A 127      20.774  38.636  -1.237  1.00 40.46           O  
ATOM    335  CB  VAL A 127      19.949  36.020  -2.149  1.00 50.16           C  
ATOM    336  CG1 VAL A 127      19.751  35.021  -3.293  1.00 37.35           C  
ATOM    337  CG2 VAL A 127      19.573  35.414  -0.791  1.00 46.56           C  
ATOM    338  N   THR A 128      22.455  37.574  -0.197  1.00 38.77           N  
ATOM    339  CA  THR A 128      22.621  38.588   0.838  1.00 39.29           C  
ATOM    340  C   THR A 128      24.086  38.921   1.059  1.00 41.86           C  
ATOM    341  O   THR A 128      24.958  38.284   0.498  1.00 41.38           O  
ATOM    342  CB  THR A 128      22.018  38.137   2.195  1.00 47.41           C  
ATOM    343  OG1 THR A 128      22.748  37.014   2.703  1.00 54.54           O  
ATOM    344  CG2 THR A 128      20.587  37.759   2.037  1.00 36.50           C  
ATOM    345  N   PRO A 129      24.358  39.950   1.867  1.00 47.08           N  
ATOM    346  CA  PRO A 129      25.732  40.177   2.322  1.00 50.45           C  
ATOM    347  C   PRO A 129      26.195  39.234   3.436  1.00 51.21           C  
ATOM    348  O   PRO A 129      27.343  39.336   3.866  1.00 56.44           O  
ATOM    349  CB  PRO A 129      25.695  41.619   2.836  1.00 50.41           C  
ATOM    350  CG  PRO A 129      24.254  41.940   3.027  1.00 49.86           C  
ATOM    351  CD  PRO A 129      23.533  41.163   1.991  1.00 52.01           C  
ATOM    352  N   LEU A 130      25.333  38.335   3.894  1.00 54.31           N  
ATOM    353  CA  LEU A 130      25.695  37.439   4.997  1.00 51.91           C  
ATOM    354  C   LEU A 130      26.927  36.593   4.678  1.00 55.09           C  
ATOM    355  O   LEU A 130      27.210  36.310   3.517  1.00 67.00           O  
ATOM    356  CB  LEU A 130      24.518  36.529   5.353  1.00 38.25           C  
ATOM    357  CG  LEU A 130      23.402  37.212   6.130  1.00 41.34           C  
ATOM    358  CD1 LEU A 130      22.339  36.229   6.561  1.00 46.90           C  
ATOM    359  CD2 LEU A 130      24.002  37.880   7.334  1.00 38.66           C  
ATOM    360  N   THR A 131      27.667  36.212   5.711  1.00 49.33           N  
ATOM    361  CA  THR A 131      28.789  35.306   5.543  1.00 52.44           C  
ATOM    362  C   THR A 131      28.857  34.365   6.724  1.00 64.37           C  
ATOM    363  O   THR A 131      28.385  34.697   7.808  1.00 70.24           O  
ATOM    364  CB  THR A 131      30.101  36.055   5.422  1.00 56.65           C  
ATOM    365  OG1 THR A 131      29.861  37.298   4.759  1.00 60.82           O  
ATOM    366  CG2 THR A 131      31.078  35.241   4.604  1.00 65.02           C  
ATOM    367  N   PHE A 132      29.456  33.197   6.517  1.00 62.77           N  
ATOM    368  CA  PHE A 132      29.484  32.166   7.545  1.00 46.99           C  
ATOM    369  C   PHE A 132      30.857  31.545   7.752  1.00 45.42           C  
ATOM    370  O   PHE A 132      31.443  31.007   6.820  1.00 60.53           O  
ATOM    371  CB  PHE A 132      28.477  31.076   7.192  1.00 40.15           C  
ATOM    372  CG  PHE A 132      27.059  31.566   7.132  1.00 42.76           C  
ATOM    373  CD1 PHE A 132      26.296  31.679   8.289  1.00 41.03           C  
ATOM    374  CD2 PHE A 132      26.480  31.924   5.917  1.00 47.96           C  
ATOM    375  CE1 PHE A 132      24.966  32.136   8.235  1.00 41.27           C  
ATOM    376  CE2 PHE A 132      25.155  32.376   5.858  1.00 39.95           C  
ATOM    377  CZ  PHE A 132      24.402  32.485   7.022  1.00 34.80           C  
ATOM    378  N   SER A 133      31.370  31.626   8.977  1.00 51.17           N  
ATOM    379  CA  SER A 133      32.555  30.856   9.387  1.00 50.17           C  
ATOM    380  C   SER A 133      32.103  29.661  10.213  1.00 49.47           C  
ATOM    381  O   SER A 133      31.127  29.759  10.952  1.00 54.26           O  
ATOM    382  CB  SER A 133      33.531  31.712  10.196  1.00 54.64           C  
ATOM    383  OG  SER A 133      34.500  32.331   9.367  1.00 66.02           O  
ATOM    384  N   ARG A 134      32.788  28.531  10.083  1.00 51.52           N  
ATOM    385  CA  ARG A 134      32.419  27.342  10.852  1.00 51.33           C  
ATOM    386  C   ARG A 134      33.290  27.175  12.103  1.00 60.92           C  
ATOM    387  O   ARG A 134      34.499  27.406  12.056  1.00 58.11           O  
ATOM    388  CB  ARG A 134      32.518  26.084   9.992  1.00 51.91           C  
ATOM    389  CG  ARG A 134      31.966  24.870  10.694  1.00 56.13           C  
ATOM    390  CD  ARG A 134      32.125  23.589   9.915  1.00 64.42           C  
ATOM    391  NE  ARG A 134      31.680  22.448  10.716  1.00 71.45           N  
ATOM    392  CZ  ARG A 134      31.709  21.183  10.307  1.00 73.76           C  
ATOM    393  NH1 ARG A 134      32.165  20.884   9.096  1.00 63.15           N  
ATOM    394  NH2 ARG A 134      31.284  20.214  11.113  1.00 80.48           N  
ATOM    395  N   LEU A 135      32.673  26.774  13.217  1.00 58.39           N  
ATOM    396  CA  LEU A 135      33.418  26.487  14.440  1.00 57.36           C  
ATOM    397  C   LEU A 135      33.286  25.028  14.855  1.00 58.20           C  
ATOM    398  O   LEU A 135      32.223  24.439  14.709  1.00 60.68           O  
ATOM    399  CB  LEU A 135      32.947  27.391  15.567  1.00 56.95           C  
ATOM    400  CG  LEU A 135      33.179  28.870  15.286  1.00 59.11           C  
ATOM    401  CD1 LEU A 135      32.737  29.741  16.446  1.00 58.18           C  
ATOM    402  CD2 LEU A 135      34.637  29.091  14.973  1.00 60.82           C  
ATOM    403  N   TYR A 136      34.370  24.449  15.369  1.00 62.47           N  
ATOM    404  CA  TYR A 136      34.364  23.045  15.789  1.00 69.88           C  
ATOM    405  C   TYR A 136      34.476  22.892  17.307  1.00 75.92           C  
ATOM    406  O   TYR A 136      34.485  21.777  17.839  1.00 82.83           O  
ATOM    407  CB  TYR A 136      35.505  22.268  15.127  1.00 67.91           C  
ATOM    408  CG  TYR A 136      35.492  22.270  13.618  1.00 69.81           C  
ATOM    409  CD1 TYR A 136      34.860  21.259  12.906  1.00 69.86           C  
ATOM    410  CD2 TYR A 136      36.140  23.271  12.902  1.00 72.49           C  
ATOM    411  CE1 TYR A 136      34.860  21.254  11.522  1.00 73.14           C  
ATOM    412  CE2 TYR A 136      36.147  23.274  11.519  1.00 73.83           C  
ATOM    413  CZ  TYR A 136      35.508  22.264  10.835  1.00 78.94           C  
ATOM    414  OH  TYR A 136      35.517  22.272   9.460  1.00 88.50           O  
ATOM    415  N   GLU A 137      34.580  24.015  18.000  1.00 75.02           N  
ATOM    416  CA  GLU A 137      34.599  24.011  19.453  1.00 78.37           C  
ATOM    417  C   GLU A 137      34.203  25.391  19.951  1.00 83.42           C  
ATOM    418  O   GLU A 137      34.546  26.406  19.344  1.00 87.02           O  
ATOM    419  CB  GLU A 137      35.974  23.614  19.981  1.00 79.30           C  
ATOM    420  CG  GLU A 137      37.067  24.618  19.679  1.00 87.96           C  
ATOM    421  CD  GLU A 137      38.441  24.127  20.091  1.00103.59           C  
ATOM    422  OE1 GLU A 137      38.549  22.960  20.532  1.00114.03           O  
ATOM    423  OE2 GLU A 137      39.411  24.909  19.973  1.00104.86           O  
ATOM    424  N   GLY A 138      33.455  25.426  21.045  1.00 74.01           N  
ATOM    425  CA  GLY A 138      32.986  26.686  21.582  1.00 74.58           C  
ATOM    426  C   GLY A 138      31.571  27.008  21.140  1.00 76.37           C  
ATOM    427  O   GLY A 138      30.895  26.173  20.534  1.00 76.62           O  
ATOM    428  N   GLU A 139      31.130  28.228  21.446  1.00 76.61           N  
ATOM    429  CA  GLU A 139      29.772  28.673  21.156  1.00 64.64           C  
ATOM    430  C   GLU A 139      29.718  29.499  19.880  1.00 60.47           C  
ATOM    431  O   GLU A 139      30.405  30.513  19.754  1.00 63.66           O  
ATOM    432  CB  GLU A 139      29.221  29.495  22.323  1.00 69.59           C  
ATOM    433  CG  GLU A 139      28.882  28.698  23.564  1.00 82.29           C  
ATOM    434  CD  GLU A 139      27.413  28.360  23.641  1.00 88.37           C  
ATOM    435  OE1 GLU A 139      26.646  28.882  22.798  1.00 78.46           O  
ATOM    436  OE2 GLU A 139      27.028  27.582  24.546  1.00 99.43           O  
ATOM    437  N   ALA A 140      28.892  29.059  18.940  1.00 52.11           N  
ATOM    438  CA  ALA A 140      28.671  29.776  17.693  1.00 53.46           C  
ATOM    439  C   ALA A 140      27.360  30.544  17.749  1.00 52.97           C  
ATOM    440  O   ALA A 140      26.535  30.326  18.641  1.00 62.83           O  
ATOM    441  CB  ALA A 140      28.667  28.812  16.523  1.00 53.99           C  
ATOM    442  N   ASP A 141      27.170  31.449  16.799  1.00 45.97           N  
ATOM    443  CA  ASP A 141      25.927  32.197  16.715  1.00 47.20           C  
ATOM    444  C   ASP A 141      24.808  31.229  16.456  1.00 48.92           C  
ATOM    445  O   ASP A 141      23.774  31.250  17.129  1.00 50.34           O  
ATOM    446  CB  ASP A 141      25.985  33.243  15.606  1.00 49.80           C  
ATOM    447  CG  ASP A 141      27.025  34.304  15.867  1.00 55.91           C  
ATOM    448  OD1 ASP A 141      27.021  34.890  16.975  1.00 57.37           O  
ATOM    449  OD2 ASP A 141      27.853  34.538  14.965  1.00 56.62           O  
ATOM    450  N   ILE A 142      25.045  30.362  15.477  1.00 46.32           N  
ATOM    451  CA  ILE A 142      24.090  29.330  15.090  1.00 46.52           C  
ATOM    452  C   ILE A 142      24.588  27.932  15.495  1.00 45.92           C  
ATOM    453  O   ILE A 142      25.490  27.371  14.858  1.00 48.11           O  
ATOM    454  CB  ILE A 142      23.836  29.385  13.574  1.00 41.41           C  
ATOM    455  CG1 ILE A 142      23.445  30.798  13.166  1.00 41.52           C  
ATOM    456  CG2 ILE A 142      22.777  28.387  13.151  1.00 40.22           C  
ATOM    457  CD1 ILE A 142      23.493  31.004  11.678  1.00 43.69           C  
ATOM    458  N   MET A 143      24.007  27.377  16.557  1.00 40.68           N  
ATOM    459  CA  MET A 143      24.354  26.026  17.001  1.00 43.45           C  
ATOM    460  C   MET A 143      23.408  24.969  16.409  1.00 41.91           C  
ATOM    461  O   MET A 143      22.188  25.058  16.565  1.00 44.54           O  
ATOM    462  CB  MET A 143      24.345  25.952  18.528  1.00 43.31           C  
ATOM    463  CG  MET A 143      25.337  26.880  19.224  1.00 48.69           C  
ATOM    464  SD  MET A 143      27.084  26.380  19.164  1.00 51.35           S  
ATOM    465  CE  MET A 143      27.200  25.105  20.421  1.00 51.61           C  
ATOM    466  N   ILE A 144      23.971  23.978  15.722  1.00 39.29           N  
ATOM    467  CA  ILE A 144      23.154  22.952  15.074  1.00 46.29           C  
ATOM    468  C   ILE A 144      23.268  21.601  15.751  1.00 52.18           C  
ATOM    469  O   ILE A 144      24.362  21.028  15.854  1.00 55.64           O  
ATOM    470  CB  ILE A 144      23.515  22.728  13.599  1.00 45.67           C  
ATOM    471  CG1 ILE A 144      23.644  24.048  12.848  1.00 44.48           C  
ATOM    472  CG2 ILE A 144      22.438  21.876  12.955  1.00 38.13           C  
ATOM    473  CD1 ILE A 144      22.384  24.860  12.890  1.00 49.55           C  
ATOM    474  N   SER A 145      22.124  21.077  16.174  1.00 41.77           N  
ATOM    475  CA  SER A 145      22.109  19.864  16.969  1.00 44.16           C  
ATOM    476  C   SER A 145      20.933  18.964  16.624  1.00 42.57           C  
ATOM    477  O   SER A 145      19.888  19.404  16.126  1.00 38.04           O  
ATOM    478  CB  SER A 145      22.086  20.215  18.465  1.00 46.73           C  
ATOM    479  OG  SER A 145      21.039  21.125  18.787  1.00 42.41           O  
ATOM    480  N   PHE A 146      21.127  17.684  16.885  1.00 50.76           N  
ATOM    481  CA  PHE A 146      20.074  16.705  16.711  1.00 48.56           C  
ATOM    482  C   PHE A 146      19.633  16.247  18.077  1.00 44.72           C  
ATOM    483  O   PHE A 146      20.459  16.039  18.963  1.00 47.04           O  
ATOM    484  CB  PHE A 146      20.560  15.528  15.870  1.00 51.45           C  
ATOM    485  CG  PHE A 146      20.857  15.893  14.454  1.00 49.50           C  
ATOM    486  CD1 PHE A 146      22.070  16.458  14.116  1.00 47.55           C  
ATOM    487  CD2 PHE A 146      19.920  15.675  13.457  1.00 51.03           C  
ATOM    488  CE1 PHE A 146      22.353  16.807  12.804  1.00 44.17           C  
ATOM    489  CE2 PHE A 146      20.194  16.022  12.143  1.00 52.85           C  
ATOM    490  CZ  PHE A 146      21.420  16.591  11.818  1.00 44.22           C  
ATOM    491  N   ALA A 147      18.330  16.108  18.266  1.00 44.04           N  
ATOM    492  CA  ALA A 147      17.845  15.650  19.553  1.00 46.86           C  
ATOM    493  C   ALA A 147      16.558  14.849  19.445  1.00 49.29           C  
ATOM    494  O   ALA A 147      15.877  14.823  18.412  1.00 54.78           O  
ATOM    495  CB  ALA A 147      17.649  16.830  20.500  1.00 52.22           C  
ATOM    496  N   VAL A 148      16.247  14.198  20.554  1.00 49.01           N  
ATOM    497  CA  VAL A 148      15.044  13.415  20.697  1.00 60.13           C  
ATOM    498  C   VAL A 148      14.311  13.884  21.944  1.00 58.43           C  
ATOM    499  O   VAL A 148      14.941  14.292  22.918  1.00 51.32           O  
ATOM    500  CB  VAL A 148      15.380  11.915  20.775  1.00 65.27           C  
ATOM    501  CG1 VAL A 148      14.787  11.284  22.023  1.00 66.89           C  
ATOM    502  CG2 VAL A 148      14.927  11.214  19.503  1.00 64.13           C  
ATOM    503  N   ARG A 149      12.985  13.861  21.866  1.00 57.39           N  
ATOM    504  CA  ARG A 149      12.092  14.110  22.991  1.00 56.08           C  
ATOM    505  C   ARG A 149      12.499  15.295  23.878  1.00 60.59           C  
ATOM    506  O   ARG A 149      12.376  16.437  23.453  1.00 57.92           O  
ATOM    507  CB  ARG A 149      11.966  12.844  23.846  1.00 56.69           C  
ATOM    508  CG  ARG A 149      11.459  11.632  23.106  1.00 58.94           C  
ATOM    509  CD  ARG A 149      10.083  11.838  22.515  1.00 58.08           C  
ATOM    510  NE  ARG A 149       9.626  10.617  21.852  1.00 61.61           N  
ATOM    511  CZ  ARG A 149       8.367  10.375  21.501  1.00 67.78           C  
ATOM    512  NH1 ARG A 149       7.422  11.273  21.748  1.00 60.30           N  
ATOM    513  NH2 ARG A 149       8.050   9.227  20.909  1.00 72.02           N  
ATOM    514  N   GLU A 150      13.005  14.999  25.084  1.00 66.46           N  
ATOM    515  CA  GLU A 150      13.094  15.953  26.193  1.00 64.95           C  
ATOM    516  C   GLU A 150      14.217  16.972  26.051  1.00 69.96           C  
ATOM    517  O   GLU A 150      14.094  18.083  26.555  1.00 92.38           O  
ATOM    518  CB  GLU A 150      13.233  15.206  27.513  1.00 89.48           C  
ATOM    519  CG  GLU A 150      11.977  14.431  27.930  1.00106.28           C  
ATOM    520  CD  GLU A 150      12.170  12.915  27.919  1.00114.42           C  
ATOM    521  OE1 GLU A 150      12.713  12.383  26.924  1.00112.49           O  
ATOM    522  OE2 GLU A 150      11.793  12.260  28.918  1.00118.09           O  
ATOM    523  N   HIS A 151      15.328  16.603  25.430  1.00 50.20           N  
ATOM    524  CA  HIS A 151      15.965  17.561  24.515  1.00 61.93           C  
ATOM    525  C   HIS A 151      16.706  18.795  25.105  1.00 62.00           C  
ATOM    526  O   HIS A 151      17.844  19.054  24.730  1.00 64.51           O  
ATOM    527  CB  HIS A 151      14.834  17.940  23.553  1.00 63.48           C  
ATOM    528  CG  HIS A 151      15.140  18.998  22.554  1.00 44.20           C  
ATOM    529  ND1 HIS A 151      14.180  19.432  21.669  1.00 39.12           N  
ATOM    530  CD2 HIS A 151      16.240  19.749  22.322  1.00 45.39           C  
ATOM    531  CE1 HIS A 151      14.679  20.403  20.926  1.00 43.92           C  
ATOM    532  NE2 HIS A 151      15.926  20.618  21.303  1.00 43.25           N  
ATOM    533  N   GLY A 152      16.104  19.570  25.998  1.00 63.19           N  
ATOM    534  CA  GLY A 152      16.895  20.569  26.717  1.00 52.86           C  
ATOM    535  C   GLY A 152      16.508  22.039  26.623  1.00 50.32           C  
ATOM    536  O   GLY A 152      17.235  22.927  27.100  1.00 44.67           O  
ATOM    537  N   ASP A 153      15.376  22.306  25.982  1.00 47.43           N  
ATOM    538  CA  ASP A 153      14.751  23.614  26.048  1.00 39.88           C  
ATOM    539  C   ASP A 153      13.271  23.448  26.394  1.00 44.21           C  
ATOM    540  O   ASP A 153      12.852  22.382  26.869  1.00 43.02           O  
ATOM    541  CB  ASP A 153      14.938  24.399  24.738  1.00 37.95           C  
ATOM    542  CG  ASP A 153      14.411  23.668  23.505  1.00 44.74           C  
ATOM    543  OD1 ASP A 153      13.786  22.598  23.624  1.00 37.23           O  
ATOM    544  OD2 ASP A 153      14.622  24.186  22.388  1.00 50.46           O  
ATOM    545  N   PHE A 154      12.484  24.494  26.159  1.00 49.87           N  
ATOM    546  CA  PHE A 154      11.067  24.492  26.532  1.00 46.83           C  
ATOM    547  C   PHE A 154      10.212  23.636  25.631  1.00 42.27           C  
ATOM    548  O   PHE A 154       9.101  23.289  25.990  1.00 43.97           O  
ATOM    549  CB  PHE A 154      10.502  25.908  26.504  1.00 48.97           C  
ATOM    550  CG  PHE A 154      10.847  26.716  27.700  1.00 52.67           C  
ATOM    551  CD1 PHE A 154      11.173  28.059  27.567  1.00 51.15           C  
ATOM    552  CD2 PHE A 154      10.838  26.138  28.958  1.00 49.50           C  
ATOM    553  CE1 PHE A 154      11.494  28.811  28.663  1.00 46.79           C  
ATOM    554  CE2 PHE A 154      11.148  26.873  30.055  1.00 45.30           C  
ATOM    555  CZ  PHE A 154      11.484  28.219  29.915  1.00 51.39           C  
ATOM    556  N   TYR A 155      10.719  23.322  24.446  1.00 45.95           N  
ATOM    557  CA  TYR A 155       9.878  22.759  23.400  1.00 44.23           C  
ATOM    558  C   TYR A 155      10.393  21.395  22.931  1.00 48.43           C  
ATOM    559  O   TYR A 155      11.181  21.292  21.990  1.00 41.17           O  
ATOM    560  CB  TYR A 155       9.775  23.762  22.248  1.00 41.46           C  
ATOM    561  CG  TYR A 155       9.502  25.169  22.745  1.00 46.06           C  
ATOM    562  CD1 TYR A 155       8.246  25.528  23.234  1.00 48.39           C  
ATOM    563  CD2 TYR A 155      10.505  26.126  22.764  1.00 46.57           C  
ATOM    564  CE1 TYR A 155       7.995  26.805  23.705  1.00 46.91           C  
ATOM    565  CE2 TYR A 155      10.261  27.408  23.232  1.00 42.74           C  
ATOM    566  CZ  TYR A 155       9.009  27.744  23.699  1.00 42.79           C  
ATOM    567  OH  TYR A 155       8.778  29.021  24.167  1.00 43.34           O  
ATOM    568  N   PRO A 156       9.943  20.331  23.610  1.00 62.81           N  
ATOM    569  CA  PRO A 156      10.409  18.971  23.330  1.00 64.31           C  
ATOM    570  C   PRO A 156       9.932  18.476  21.975  1.00 59.55           C  
ATOM    571  O   PRO A 156       8.884  18.896  21.484  1.00 51.52           O  
ATOM    572  CB  PRO A 156       9.779  18.136  24.455  1.00 46.76           C  
ATOM    573  CG  PRO A 156       9.225  19.103  25.405  1.00 46.91           C  
ATOM    574  CD  PRO A 156       8.916  20.340  24.659  1.00 51.51           C  
ATOM    575  N   PHE A 157      10.696  17.580  21.374  1.00 53.25           N  
ATOM    576  CA  PHE A 157      10.250  16.995  20.133  1.00 52.04           C  
ATOM    577  C   PHE A 157       9.226  15.911  20.457  1.00 54.54           C  
ATOM    578  O   PHE A 157       8.919  15.678  21.628  1.00 48.12           O  
ATOM    579  CB  PHE A 157      11.439  16.483  19.340  1.00 45.78           C  
ATOM    580  CG  PHE A 157      12.175  17.572  18.637  1.00 44.61           C  
ATOM    581  CD1 PHE A 157      11.473  18.530  17.912  1.00 53.88           C  
ATOM    582  CD2 PHE A 157      13.560  17.670  18.714  1.00 48.21           C  
ATOM    583  CE1 PHE A 157      12.147  19.568  17.250  1.00 51.62           C  
ATOM    584  CE2 PHE A 157      14.244  18.712  18.058  1.00 43.66           C  
ATOM    585  CZ  PHE A 157      13.535  19.658  17.329  1.00 43.25           C  
ATOM    586  N   ASP A 158       8.686  15.267  19.430  1.00 48.63           N  
ATOM    587  CA  ASP A 158       7.472  14.485  19.606  1.00 56.54           C  
ATOM    588  C   ASP A 158       7.522  13.075  19.018  1.00 66.29           C  
ATOM    589  O   ASP A 158       6.476  12.447  18.809  1.00 71.64           O  
ATOM    590  CB  ASP A 158       6.278  15.248  19.004  1.00 53.97           C  
ATOM    591  CG  ASP A 158       6.576  15.863  17.618  1.00 54.31           C  
ATOM    592  OD1 ASP A 158       7.466  15.381  16.878  1.00 44.83           O  
ATOM    593  OD2 ASP A 158       5.875  16.829  17.254  1.00 55.90           O  
ATOM    594  N   GLY A 159       8.725  12.564  18.771  1.00 62.80           N  
ATOM    595  CA  GLY A 159       8.854  11.278  18.109  1.00 62.78           C  
ATOM    596  C   GLY A 159       8.727  11.496  16.612  1.00 63.46           C  
ATOM    597  O   GLY A 159       8.821  12.635  16.158  1.00 57.82           O  
ATOM    598  N   PRO A 160       8.508  10.414  15.840  1.00 62.17           N  
ATOM    599  CA  PRO A 160       8.492  10.441  14.369  1.00 59.59           C  
ATOM    600  C   PRO A 160       7.258  11.131  13.789  1.00 59.83           C  
ATOM    601  O   PRO A 160       6.157  10.853  14.243  1.00 65.88           O  
ATOM    602  CB  PRO A 160       8.513   8.956  13.998  1.00 58.81           C  
ATOM    603  CG  PRO A 160       8.999   8.256  15.216  1.00 61.40           C  
ATOM    604  CD  PRO A 160       8.427   9.039  16.348  1.00 63.82           C  
ATOM    605  N   GLY A 161       7.437  12.019  12.813  1.00 50.47           N  
ATOM    606  CA  GLY A 161       6.313  12.765  12.275  1.00 49.41           C  
ATOM    607  C   GLY A 161       5.992  14.066  12.999  1.00 64.57           C  
ATOM    608  O   GLY A 161       6.699  14.472  13.920  1.00 62.65           O  
ATOM    609  N   ASN A 162       4.918  14.722  12.569  1.00 60.66           N  
ATOM    610  CA  ASN A 162       4.530  16.030  13.095  1.00 51.43           C  
ATOM    611  C   ASN A 162       5.689  17.046  13.055  1.00 49.02           C  
ATOM    612  O   ASN A 162       6.028  17.503  11.966  1.00 49.59           O  
ATOM    613  CB  ASN A 162       3.937  15.867  14.502  1.00 52.40           C  
ATOM    614  CG  ASN A 162       2.581  15.154  14.473  1.00 57.04           C  
ATOM    615  OD1 ASN A 162       2.484  14.020  14.000  1.00 54.15           O  
ATOM    616  ND2 ASN A 162       1.527  15.829  14.950  1.00 54.92           N  
ATOM    617  N   VAL A 163       6.289  17.415  14.194  1.00 40.09           N  
ATOM    618  CA  VAL A 163       7.393  18.379  14.173  1.00 37.34           C  
ATOM    619  C   VAL A 163       8.707  17.718  13.765  1.00 37.31           C  
ATOM    620  O   VAL A 163       9.074  16.693  14.295  1.00 45.89           O  
ATOM    621  CB  VAL A 163       7.603  19.053  15.530  1.00 41.33           C  
ATOM    622  CG1 VAL A 163       8.738  20.090  15.443  1.00 34.20           C  
ATOM    623  CG2 VAL A 163       6.334  19.707  15.999  1.00 37.15           C  
ATOM    624  N   LEU A 164       9.415  18.303  12.814  1.00 35.44           N  
ATOM    625  CA  LEU A 164      10.636  17.685  12.314  1.00 38.70           C  
ATOM    626  C   LEU A 164      11.847  18.445  12.820  1.00 38.71           C  
ATOM    627  O   LEU A 164      12.897  17.862  13.051  1.00 41.33           O  
ATOM    628  CB  LEU A 164      10.656  17.647  10.780  1.00 35.46           C  
ATOM    629  CG  LEU A 164       9.479  16.967  10.094  1.00 37.31           C  
ATOM    630  CD1 LEU A 164       9.636  16.974   8.583  1.00 37.26           C  
ATOM    631  CD2 LEU A 164       9.306  15.572  10.606  1.00 45.40           C  
ATOM    632  N   ALA A 165      11.691  19.755  12.971  1.00 36.73           N  
ATOM    633  CA  ALA A 165      12.766  20.598  13.453  1.00 33.06           C  
ATOM    634  C   ALA A 165      12.210  21.920  13.973  1.00 36.81           C  
ATOM    635  O   ALA A 165      11.023  22.225  13.797  1.00 39.13           O  
ATOM    636  CB  ALA A 165      13.767  20.826  12.359  1.00 33.15           C  
ATOM    637  N   HIS A 166      13.049  22.691  14.652  1.00 36.47           N  
ATOM    638  CA  HIS A 166      12.683  24.070  14.985  1.00 30.61           C  
ATOM    639  C   HIS A 166      13.916  24.911  15.237  1.00 34.08           C  
ATOM    640  O   HIS A 166      15.024  24.390  15.379  1.00 41.84           O  
ATOM    641  CB  HIS A 166      11.716  24.140  16.183  1.00 28.09           C  
ATOM    642  CG  HIS A 166      12.222  23.542  17.465  1.00 29.45           C  
ATOM    643  ND1 HIS A 166      11.401  22.826  18.315  1.00 42.02           N  
ATOM    644  CD2 HIS A 166      13.424  23.610  18.083  1.00 36.33           C  
ATOM    645  CE1 HIS A 166      12.083  22.457  19.384  1.00 42.18           C  
ATOM    646  NE2 HIS A 166      13.313  22.929  19.276  1.00 36.17           N  
ATOM    647  N   ALA A 167      13.729  26.220  15.267  1.00 34.38           N  
ATOM    648  CA  ALA A 167      14.859  27.130  15.355  1.00 33.85           C  
ATOM    649  C   ALA A 167      14.457  28.374  16.119  1.00 44.10           C  
ATOM    650  O   ALA A 167      13.275  28.597  16.361  1.00 46.26           O  
ATOM    651  CB  ALA A 167      15.371  27.489  13.950  1.00 24.29           C  
ATOM    652  N   TYR A 168      15.431  29.187  16.509  1.00 40.59           N  
ATOM    653  CA  TYR A 168      15.107  30.413  17.228  1.00 36.29           C  
ATOM    654  C   TYR A 168      15.553  31.611  16.427  1.00 37.58           C  
ATOM    655  O   TYR A 168      16.576  31.545  15.733  1.00 34.84           O  
ATOM    656  CB  TYR A 168      15.770  30.435  18.609  1.00 31.53           C  
ATOM    657  CG  TYR A 168      15.292  29.343  19.524  1.00 32.70           C  
ATOM    658  CD1 TYR A 168      15.890  28.094  19.504  1.00 33.97           C  
ATOM    659  CD2 TYR A 168      14.242  29.563  20.421  1.00 33.77           C  
ATOM    660  CE1 TYR A 168      15.458  27.080  20.346  1.00 38.71           C  
ATOM    661  CE2 TYR A 168      13.799  28.560  21.274  1.00 31.30           C  
ATOM    662  CZ  TYR A 168      14.414  27.314  21.225  1.00 41.91           C  
ATOM    663  OH  TYR A 168      13.987  26.288  22.037  1.00 49.07           O  
ATOM    664  N   ALA A 169      14.792  32.701  16.534  1.00 37.13           N  
ATOM    665  CA  ALA A 169      15.157  33.979  15.912  1.00 29.34           C  
ATOM    666  C   ALA A 169      16.525  34.501  16.407  1.00 35.19           C  
ATOM    667  O   ALA A 169      16.978  34.118  17.482  1.00 36.99           O  
ATOM    668  CB  ALA A 169      14.073  34.989  16.171  1.00 25.17           C  
ATOM    669  N   PRO A 170      17.197  35.362  15.608  1.00 34.08           N  
ATOM    670  CA  PRO A 170      18.513  35.950  15.932  1.00 31.27           C  
ATOM    671  C   PRO A 170      18.649  36.549  17.329  1.00 37.09           C  
ATOM    672  O   PRO A 170      17.792  37.296  17.786  1.00 45.32           O  
ATOM    673  CB  PRO A 170      18.661  37.060  14.899  1.00 34.78           C  
ATOM    674  CG  PRO A 170      17.919  36.545  13.717  1.00 38.51           C  
ATOM    675  CD  PRO A 170      16.745  35.759  14.262  1.00 29.27           C  
ATOM    676  N   GLY A 171      19.753  36.241  17.991  1.00 32.02           N  
ATOM    677  CA  GLY A 171      19.973  36.721  19.336  1.00 29.96           C  
ATOM    678  C   GLY A 171      21.082  35.930  19.995  1.00 38.50           C  
ATOM    679  O   GLY A 171      21.660  35.010  19.402  1.00 44.55           O  
ATOM    680  N   PRO A 172      21.388  36.277  21.242  1.00 32.61           N  
ATOM    681  CA  PRO A 172      22.441  35.566  21.957  1.00 39.31           C  
ATOM    682  C   PRO A 172      21.877  34.266  22.504  1.00 41.68           C  
ATOM    683  O   PRO A 172      20.665  34.070  22.446  1.00 39.75           O  
ATOM    684  CB  PRO A 172      22.819  36.538  23.055  1.00 36.08           C  
ATOM    685  CG  PRO A 172      21.548  37.231  23.349  1.00 35.86           C  
ATOM    686  CD  PRO A 172      20.778  37.329  22.070  1.00 34.49           C  
ATOM    687  N   GLY A 173      22.734  33.378  22.986  1.00 34.52           N  
ATOM    688  CA  GLY A 173      22.274  32.118  23.535  1.00 34.69           C  
ATOM    689  C   GLY A 173      21.616  31.105  22.616  1.00 41.63           C  
ATOM    690  O   GLY A 173      22.079  30.870  21.502  1.00 51.23           O  
ATOM    691  N   ILE A 174      20.543  30.487  23.116  1.00 44.09           N  
ATOM    692  CA  ILE A 174      19.728  29.506  22.390  1.00 31.62           C  
ATOM    693  C   ILE A 174      19.268  30.128  21.079  1.00 39.66           C  
ATOM    694  O   ILE A 174      18.908  29.432  20.134  1.00 46.97           O  
ATOM    695  CB  ILE A 174      18.474  29.069  23.237  1.00 42.90           C  
ATOM    696  CG1 ILE A 174      17.724  27.864  22.655  1.00 45.01           C  
ATOM    697  CG2 ILE A 174      17.472  30.209  23.376  1.00 32.56           C  
ATOM    698  CD1 ILE A 174      18.392  26.539  22.818  1.00 48.31           C  
ATOM    699  N   ASN A 175      19.268  31.459  21.025  1.00 43.54           N  
ATOM    700  CA  ASN A 175      18.799  32.147  19.839  1.00 40.92           C  
ATOM    701  C   ASN A 175      19.775  31.999  18.707  1.00 44.87           C  
ATOM    702  O   ASN A 175      20.982  32.085  18.898  1.00 53.92           O  
ATOM    703  CB  ASN A 175      18.564  33.612  20.118  1.00 28.40           C  
ATOM    704  CG  ASN A 175      17.300  33.852  20.877  1.00 38.27           C  
ATOM    705  OD1 ASN A 175      17.041  33.202  21.889  1.00 43.96           O  
ATOM    706  ND2 ASN A 175      16.495  34.803  20.403  1.00 40.30           N  
ATOM    707  N   GLY A 176      19.239  31.779  17.520  1.00 34.53           N  
ATOM    708  CA  GLY A 176      20.076  31.497  16.380  1.00 40.16           C  
ATOM    709  C   GLY A 176      20.174  30.002  16.166  1.00 38.95           C  
ATOM    710  O   GLY A 176      20.464  29.536  15.068  1.00 38.80           O  
ATOM    711  N   ASP A 177      19.913  29.234  17.213  1.00 29.16           N  
ATOM    712  CA  ASP A 177      20.118  27.799  17.106  1.00 28.68           C  
ATOM    713  C   ASP A 177      19.034  27.072  16.306  1.00 32.21           C  
ATOM    714  O   ASP A 177      17.894  27.535  16.167  1.00 36.17           O  
ATOM    715  CB  ASP A 177      20.238  27.196  18.499  1.00 33.36           C  
ATOM    716  CG  ASP A 177      21.360  27.842  19.322  1.00 42.16           C  
ATOM    717  OD1 ASP A 177      21.907  28.895  18.907  1.00 42.49           O  
ATOM    718  OD2 ASP A 177      21.684  27.293  20.393  1.00 45.42           O  
ATOM    719  N   ALA A 178      19.414  25.921  15.773  1.00 29.27           N  
ATOM    720  CA  ALA A 178      18.496  25.092  15.015  1.00 34.49           C  
ATOM    721  C   ALA A 178      18.529  23.659  15.546  1.00 46.07           C  
ATOM    722  O   ALA A 178      19.603  23.083  15.758  1.00 53.66           O  
ATOM    723  CB  ALA A 178      18.845  25.132  13.555  1.00 36.65           C  
ATOM    724  N   HIS A 179      17.351  23.093  15.790  1.00 42.73           N  
ATOM    725  CA  HIS A 179      17.274  21.762  16.379  1.00 38.47           C  
ATOM    726  C   HIS A 179      16.584  20.813  15.417  1.00 37.65           C  
ATOM    727  O   HIS A 179      15.584  21.171  14.786  1.00 35.62           O  
ATOM    728  CB  HIS A 179      16.525  21.791  17.712  1.00 36.98           C  
ATOM    729  CG  HIS A 179      17.204  22.595  18.776  1.00 39.19           C  
ATOM    730  ND1 HIS A 179      16.572  22.959  19.948  1.00 44.08           N  
ATOM    731  CD2 HIS A 179      18.461  23.092  18.854  1.00 36.36           C  
ATOM    732  CE1 HIS A 179      17.409  23.655  20.698  1.00 46.27           C  
ATOM    733  NE2 HIS A 179      18.558  23.759  20.052  1.00 41.87           N  
ATOM    734  N   PHE A 180      17.110  19.603  15.297  1.00 34.71           N  
ATOM    735  CA  PHE A 180      16.503  18.641  14.385  1.00 44.79           C  
ATOM    736  C   PHE A 180      16.118  17.372  15.132  1.00 44.03           C  
ATOM    737  O   PHE A 180      16.911  16.799  15.896  1.00 38.50           O  
ATOM    738  CB  PHE A 180      17.442  18.345  13.211  1.00 39.22           C  
ATOM    739  CG  PHE A 180      17.719  19.547  12.362  1.00 38.26           C  
ATOM    740  CD1 PHE A 180      18.514  20.582  12.837  1.00 39.68           C  
ATOM    741  CD2 PHE A 180      17.164  19.666  11.102  1.00 45.59           C  
ATOM    742  CE1 PHE A 180      18.748  21.718  12.065  1.00 43.24           C  
ATOM    743  CE2 PHE A 180      17.410  20.791  10.313  1.00 49.78           C  
ATOM    744  CZ  PHE A 180      18.196  21.820  10.797  1.00 43.60           C  
ATOM    745  N   ASP A 181      14.868  16.973  14.937  1.00 41.92           N  
ATOM    746  CA  ASP A 181      14.329  15.792  15.579  1.00 48.74           C  
ATOM    747  C   ASP A 181      14.921  14.529  14.952  1.00 57.22           C  
ATOM    748  O   ASP A 181      14.591  14.154  13.821  1.00 58.84           O  
ATOM    749  CB  ASP A 181      12.807  15.788  15.478  1.00 41.51           C  
ATOM    750  CG  ASP A 181      12.175  14.699  16.307  1.00 45.27           C  
ATOM    751  OD1 ASP A 181      12.899  13.800  16.783  1.00 45.59           O  
ATOM    752  OD2 ASP A 181      10.945  14.740  16.469  1.00 45.61           O  
ATOM    753  N   ASP A 182      15.785  13.862  15.706  1.00 48.69           N  
ATOM    754  CA  ASP A 182      16.485  12.717  15.179  1.00 49.51           C  
ATOM    755  C   ASP A 182      15.600  11.475  15.152  1.00 58.20           C  
ATOM    756  O   ASP A 182      16.057  10.380  14.812  1.00 63.58           O  
ATOM    757  CB  ASP A 182      17.741  12.449  15.989  1.00 54.22           C  
ATOM    758  CG  ASP A 182      18.834  11.846  15.156  1.00 58.90           C  
ATOM    759  OD1 ASP A 182      18.572  11.572  13.968  1.00 59.74           O  
ATOM    760  OD2 ASP A 182      19.943  11.633  15.686  1.00 67.48           O  
ATOM    761  N   ASP A 183      14.332  11.642  15.506  1.00 50.68           N  
ATOM    762  CA  ASP A 183      13.390  10.543  15.383  1.00 55.38           C  
ATOM    763  C   ASP A 183      12.783  10.508  13.967  1.00 59.64           C  
ATOM    764  O   ASP A 183      11.889   9.722  13.676  1.00 54.66           O  
ATOM    765  CB  ASP A 183      12.301  10.639  16.452  1.00 58.35           C  
ATOM    766  CG  ASP A 183      12.577   9.743  17.651  1.00 66.59           C  
ATOM    767  OD1 ASP A 183      13.484   8.889  17.566  1.00 69.65           O  
ATOM    768  OD2 ASP A 183      11.879   9.877  18.675  1.00 74.76           O  
ATOM    769  N   GLU A 184      13.280  11.372  13.090  1.00 59.92           N  
ATOM    770  CA  GLU A 184      13.043  11.211  11.670  1.00 52.03           C  
ATOM    771  C   GLU A 184      14.244  10.496  11.080  1.00 62.07           C  
ATOM    772  O   GLU A 184      15.316  10.461  11.698  1.00 58.72           O  
ATOM    773  CB  GLU A 184      12.835  12.553  10.963  1.00 48.03           C  
ATOM    774  CG  GLU A 184      12.205  13.643  11.807  1.00 56.14           C  
ATOM    775  CD  GLU A 184      10.850  13.266  12.396  1.00 68.13           C  
ATOM    776  OE1 GLU A 184      10.214  12.290  11.930  1.00 75.08           O  
ATOM    777  OE2 GLU A 184      10.418  13.963  13.343  1.00 65.43           O  
ATOM    778  N   GLN A 185      14.063   9.916   9.895  1.00 60.93           N  
ATOM    779  CA  GLN A 185      15.188   9.405   9.136  1.00 56.18           C  
ATOM    780  C   GLN A 185      15.671  10.490   8.181  1.00 57.02           C  
ATOM    781  O   GLN A 185      14.992  10.832   7.207  1.00 57.22           O  
ATOM    782  CB  GLN A 185      14.815   8.144   8.376  1.00 57.79           C  
ATOM    783  CG  GLN A 185      15.996   7.466   7.697  1.00 65.75           C  
ATOM    784  CD  GLN A 185      16.797   6.586   8.642  1.00 73.19           C  
ATOM    785  OE1 GLN A 185      16.272   6.087   9.643  1.00 77.06           O  
ATOM    786  NE2 GLN A 185      18.077   6.384   8.324  1.00 69.41           N  
ATOM    787  N   TRP A 186      16.840  11.045   8.482  1.00 54.48           N  
ATOM    788  CA  TRP A 186      17.397  12.124   7.682  1.00 52.91           C  
ATOM    789  C   TRP A 186      18.174  11.572   6.502  1.00 55.00           C  
ATOM    790  O   TRP A 186      19.037  10.707   6.656  1.00 69.25           O  
ATOM    791  CB  TRP A 186      18.285  13.024   8.543  1.00 57.62           C  
ATOM    792  CG  TRP A 186      17.506  13.747   9.579  1.00 50.50           C  
ATOM    793  CD1 TRP A 186      17.444  13.454  10.902  1.00 50.64           C  
ATOM    794  CD2 TRP A 186      16.642  14.867   9.371  1.00 45.14           C  
ATOM    795  NE1 TRP A 186      16.604  14.324  11.537  1.00 48.74           N  
ATOM    796  CE2 TRP A 186      16.100  15.208  10.620  1.00 42.06           C  
ATOM    797  CE3 TRP A 186      16.274  15.616   8.245  1.00 46.55           C  
ATOM    798  CZ2 TRP A 186      15.209  16.259  10.784  1.00 37.16           C  
ATOM    799  CZ3 TRP A 186      15.395  16.666   8.404  1.00 40.79           C  
ATOM    800  CH2 TRP A 186      14.870  16.979   9.665  1.00 41.90           C  
ATOM    801  N   THR A 187      17.860  12.066   5.315  1.00 48.03           N  
ATOM    802  CA  THR A 187      18.454  11.514   4.107  1.00 50.26           C  
ATOM    803  C   THR A 187      19.081  12.574   3.202  1.00 48.41           C  
ATOM    804  O   THR A 187      18.794  13.771   3.308  1.00 47.55           O  
ATOM    805  CB  THR A 187      17.410  10.714   3.309  1.00 52.46           C  
ATOM    806  OG1 THR A 187      16.233  11.506   3.143  1.00 50.18           O  
ATOM    807  CG2 THR A 187      17.032   9.460   4.055  1.00 55.43           C  
ATOM    808  N   LYS A 188      19.958  12.117   2.319  1.00 56.84           N  
ATOM    809  CA  LYS A 188      20.518  12.975   1.296  1.00 56.80           C  
ATOM    810  C   LYS A 188      19.445  13.314   0.270  1.00 56.91           C  
ATOM    811  O   LYS A 188      19.308  14.472  -0.122  1.00 61.84           O  
ATOM    812  CB  LYS A 188      21.726  12.310   0.631  1.00 67.88           C  
ATOM    813  CG  LYS A 188      23.047  13.007   0.958  1.00 79.28           C  
ATOM    814  CD  LYS A 188      23.049  14.437   0.404  1.00 84.34           C  
ATOM    815  CE  LYS A 188      23.780  15.421   1.318  1.00 79.75           C  
ATOM    816  NZ  LYS A 188      23.545  16.839   0.912  1.00 69.54           N  
ATOM    817  N   ASP A 189      18.661  12.316  -0.134  1.00 57.49           N  
ATOM    818  CA  ASP A 189      17.624  12.522  -1.149  1.00 57.97           C  
ATOM    819  C   ASP A 189      16.206  12.729  -0.589  1.00 64.00           C  
ATOM    820  O   ASP A 189      16.012  13.302   0.490  1.00 57.16           O  
ATOM    821  CB  ASP A 189      17.613  11.348  -2.138  1.00 55.87           C  
ATOM    822  CG  ASP A 189      17.471  10.001  -1.451  1.00 74.37           C  
ATOM    823  OD1 ASP A 189      17.078   9.953  -0.262  1.00 76.53           O  
ATOM    824  OD2 ASP A 189      17.746   8.976  -2.110  1.00 86.02           O  
ATOM    825  N   THR A 190      15.227  12.251  -1.354  1.00 69.86           N  
ATOM    826  CA  THR A 190      13.812  12.501  -1.111  1.00 65.97           C  
ATOM    827  C   THR A 190      13.178  11.313  -0.402  1.00 61.99           C  
ATOM    828  O   THR A 190      12.067  11.397   0.109  1.00 65.69           O  
ATOM    829  CB  THR A 190      13.055  12.765  -2.447  1.00 95.49           C  
ATOM    830  OG1 THR A 190      13.878  13.537  -3.328  1.00 99.41           O  
ATOM    831  CG2 THR A 190      11.758  13.508  -2.216  1.00 92.84           C  
ATOM    832  N   THR A 191      13.896  10.201  -0.367  1.00 56.51           N  
ATOM    833  CA  THR A 191      13.327   8.953   0.123  1.00 61.99           C  
ATOM    834  C   THR A 191      12.950   9.024   1.592  1.00 66.54           C  
ATOM    835  O   THR A 191      12.084   8.285   2.053  1.00 74.51           O  
ATOM    836  CB  THR A 191      14.296   7.798  -0.078  1.00 63.17           C  
ATOM    837  OG1 THR A 191      15.390   7.936   0.840  1.00 66.34           O  
ATOM    838  CG2 THR A 191      14.806   7.802  -1.515  1.00 64.66           C  
ATOM    839  N   GLY A 192      13.600   9.920   2.324  1.00 54.97           N  
ATOM    840  CA  GLY A 192      13.286  10.128   3.725  1.00 53.52           C  
ATOM    841  C   GLY A 192      12.938  11.571   3.990  1.00 49.55           C  
ATOM    842  O   GLY A 192      12.234  12.204   3.215  1.00 58.44           O  
ATOM    843  N   THR A 193      13.421  12.104   5.098  1.00 47.54           N  
ATOM    844  CA  THR A 193      13.245  13.523   5.337  1.00 57.43           C  
ATOM    845  C   THR A 193      14.563  14.194   4.976  1.00 55.30           C  
ATOM    846  O   THR A 193      15.612  13.869   5.528  1.00 59.14           O  
ATOM    847  CB  THR A 193      12.826  13.843   6.796  1.00 52.91           C  
ATOM    848  OG1 THR A 193      11.682  13.051   7.160  1.00 44.94           O  
ATOM    849  CG2 THR A 193      12.496  15.348   6.938  1.00 39.58           C  
ATOM    850  N   ASN A 194      14.501  15.113   4.023  1.00 45.04           N  
ATOM    851  CA  ASN A 194      15.701  15.653   3.425  1.00 44.78           C  
ATOM    852  C   ASN A 194      16.362  16.677   4.323  1.00 47.78           C  
ATOM    853  O   ASN A 194      15.790  17.736   4.572  1.00 39.94           O  
ATOM    854  CB  ASN A 194      15.385  16.278   2.074  1.00 41.04           C  
ATOM    855  CG  ASN A 194      16.631  16.780   1.376  1.00 52.94           C  
ATOM    856  OD1 ASN A 194      16.957  17.972   1.438  1.00 54.42           O  
ATOM    857  ND2 ASN A 194      17.362  15.862   0.734  1.00 49.80           N  
ATOM    858  N   LEU A 195      17.569  16.367   4.794  1.00 51.93           N  
ATOM    859  CA  LEU A 195      18.224  17.215   5.776  1.00 46.11           C  
ATOM    860  C   LEU A 195      18.444  18.610   5.200  1.00 42.26           C  
ATOM    861  O   LEU A 195      18.230  19.616   5.878  1.00 33.55           O  
ATOM    862  CB  LEU A 195      19.549  16.611   6.236  1.00 47.59           C  
ATOM    863  CG  LEU A 195      20.168  17.442   7.368  1.00 43.66           C  
ATOM    864  CD1 LEU A 195      19.119  17.635   8.461  1.00 39.37           C  
ATOM    865  CD2 LEU A 195      21.454  16.845   7.948  1.00 38.68           C  
ATOM    866  N   PHE A 196      18.825  18.671   3.932  1.00 47.16           N  
ATOM    867  CA  PHE A 196      19.100  19.957   3.312  1.00 50.06           C  
ATOM    868  C   PHE A 196      17.879  20.866   3.320  1.00 46.88           C  
ATOM    869  O   PHE A 196      17.963  22.017   3.787  1.00 40.75           O  
ATOM    870  CB  PHE A 196      19.590  19.783   1.879  1.00 51.52           C  
ATOM    871  CG  PHE A 196      19.453  21.022   1.054  1.00 51.49           C  
ATOM    872  CD1 PHE A 196      20.302  22.100   1.253  1.00 48.58           C  
ATOM    873  CD2 PHE A 196      18.467  21.122   0.085  1.00 54.30           C  
ATOM    874  CE1 PHE A 196      20.174  23.257   0.494  1.00 45.97           C  
ATOM    875  CE2 PHE A 196      18.333  22.276  -0.680  1.00 46.40           C  
ATOM    876  CZ  PHE A 196      19.189  23.343  -0.475  1.00 41.72           C  
ATOM    877  N   LEU A 197      16.757  20.350   2.805  1.00 37.06           N  
ATOM    878  CA  LEU A 197      15.506  21.115   2.777  1.00 32.55           C  
ATOM    879  C   LEU A 197      15.141  21.694   4.130  1.00 39.18           C  
ATOM    880  O   LEU A 197      14.997  22.906   4.257  1.00 49.65           O  
ATOM    881  CB  LEU A 197      14.349  20.266   2.269  1.00 38.54           C  
ATOM    882  CG  LEU A 197      14.441  20.021   0.754  1.00 53.71           C  
ATOM    883  CD1 LEU A 197      13.162  19.414   0.175  1.00 57.25           C  
ATOM    884  CD2 LEU A 197      14.815  21.304   0.021  1.00 46.75           C  
ATOM    885  N   VAL A 198      15.019  20.845   5.144  1.00 39.91           N  
ATOM    886  CA  VAL A 198      14.554  21.321   6.439  1.00 36.23           C  
ATOM    887  C   VAL A 198      15.530  22.321   7.054  1.00 37.32           C  
ATOM    888  O   VAL A 198      15.116  23.332   7.621  1.00 36.86           O  
ATOM    889  CB  VAL A 198      14.326  20.176   7.412  1.00 34.03           C  
ATOM    890  CG1 VAL A 198      13.796  20.739   8.743  1.00 29.63           C  
ATOM    891  CG2 VAL A 198      13.357  19.153   6.804  1.00 32.47           C  
ATOM    892  N   ALA A 199      16.821  22.042   6.917  1.00 39.85           N  
ATOM    893  CA  ALA A 199      17.857  22.943   7.414  1.00 38.35           C  
ATOM    894  C   ALA A 199      17.743  24.320   6.789  1.00 40.46           C  
ATOM    895  O   ALA A 199      17.922  25.325   7.458  1.00 40.67           O  
ATOM    896  CB  ALA A 199      19.233  22.375   7.142  1.00 28.98           C  
ATOM    897  N   ALA A 200      17.450  24.371   5.498  1.00 46.82           N  
ATOM    898  CA  ALA A 200      17.432  25.657   4.824  1.00 41.72           C  
ATOM    899  C   ALA A 200      16.325  26.502   5.423  1.00 38.37           C  
ATOM    900  O   ALA A 200      16.560  27.659   5.765  1.00 41.21           O  
ATOM    901  CB  ALA A 200      17.257  25.486   3.333  1.00 27.44           C  
ATOM    902  N   HIS A 201      15.141  25.904   5.584  1.00 35.17           N  
ATOM    903  CA  HIS A 201      14.015  26.552   6.262  1.00 34.54           C  
ATOM    904  C   HIS A 201      14.377  27.012   7.668  1.00 36.65           C  
ATOM    905  O   HIS A 201      14.041  28.140   8.059  1.00 34.58           O  
ATOM    906  CB  HIS A 201      12.804  25.619   6.351  1.00 36.68           C  
ATOM    907  CG  HIS A 201      11.675  26.162   7.179  1.00 40.09           C  
ATOM    908  ND1 HIS A 201      10.492  26.612   6.623  1.00 34.50           N  
ATOM    909  CD2 HIS A 201      11.546  26.332   8.521  1.00 35.81           C  
ATOM    910  CE1 HIS A 201       9.688  27.028   7.584  1.00 33.88           C  
ATOM    911  NE2 HIS A 201      10.305  26.871   8.745  1.00 37.52           N  
ATOM    912  N   GLU A 202      15.040  26.153   8.439  1.00 33.38           N  
ATOM    913  CA  GLU A 202      15.296  26.504   9.838  1.00 40.59           C  
ATOM    914  C   GLU A 202      16.377  27.589   9.978  1.00 35.41           C  
ATOM    915  O   GLU A 202      16.276  28.444  10.853  1.00 36.35           O  
ATOM    916  CB  GLU A 202      15.663  25.259  10.663  1.00 39.43           C  
ATOM    917  CG  GLU A 202      14.613  24.137  10.636  1.00 34.15           C  
ATOM    918  CD  GLU A 202      13.251  24.522  11.237  1.00 40.57           C  
ATOM    919  OE1 GLU A 202      13.082  25.665  11.726  1.00 37.90           O  
ATOM    920  OE2 GLU A 202      12.335  23.663  11.215  1.00 38.48           O  
ATOM    921  N   ILE A 203      17.396  27.556   9.121  1.00 27.67           N  
ATOM    922  CA  ILE A 203      18.376  28.637   9.054  1.00 34.55           C  
ATOM    923  C   ILE A 203      17.704  29.980   8.731  1.00 42.53           C  
ATOM    924  O   ILE A 203      18.086  31.038   9.278  1.00 41.31           O  
ATOM    925  CB  ILE A 203      19.458  28.349   8.007  1.00 37.35           C  
ATOM    926  CG1 ILE A 203      20.336  27.191   8.472  1.00 38.68           C  
ATOM    927  CG2 ILE A 203      20.328  29.579   7.782  1.00 30.93           C  
ATOM    928  CD1 ILE A 203      21.029  27.476   9.760  1.00 35.38           C  
ATOM    929  N   GLY A 204      16.704  29.931   7.850  1.00 33.79           N  
ATOM    930  CA  GLY A 204      15.854  31.083   7.607  1.00 36.51           C  
ATOM    931  C   GLY A 204      15.340  31.688   8.907  1.00 39.49           C  
ATOM    932  O   GLY A 204      15.323  32.905   9.074  1.00 45.06           O  
ATOM    933  N   HIS A 205      14.934  30.841   9.845  1.00 41.22           N  
ATOM    934  CA  HIS A 205      14.505  31.330  11.154  1.00 40.62           C  
ATOM    935  C   HIS A 205      15.647  31.947  11.958  1.00 36.38           C  
ATOM    936  O   HIS A 205      15.453  32.970  12.600  1.00 50.65           O  
ATOM    937  CB  HIS A 205      13.852  30.208  11.950  1.00 39.80           C  
ATOM    938  CG  HIS A 205      12.464  29.901  11.504  1.00 33.79           C  
ATOM    939  ND1 HIS A 205      11.552  30.887  11.202  1.00 38.51           N  
ATOM    940  CD2 HIS A 205      11.832  28.725  11.279  1.00 43.08           C  
ATOM    941  CE1 HIS A 205      10.414  30.331  10.829  1.00 45.36           C  
ATOM    942  NE2 HIS A 205      10.559  29.019  10.866  1.00 43.60           N  
ATOM    943  N   SER A 206      16.832  31.351  11.889  1.00 30.61           N  
ATOM    944  CA  SER A 206      18.016  31.880  12.565  1.00 33.69           C  
ATOM    945  C   SER A 206      18.461  33.241  12.048  1.00 41.17           C  
ATOM    946  O   SER A 206      19.217  33.943  12.725  1.00 50.37           O  
ATOM    947  CB  SER A 206      19.189  30.921  12.423  1.00 23.73           C  
ATOM    948  OG  SER A 206      18.801  29.635  12.793  1.00 34.76           O  
ATOM    949  N   LEU A 207      18.044  33.588  10.834  1.00 28.65           N  
ATOM    950  CA  LEU A 207      18.456  34.848  10.226  1.00 34.40           C  
ATOM    951  C   LEU A 207      17.374  35.892  10.447  1.00 35.64           C  
ATOM    952  O   LEU A 207      17.615  37.091  10.321  1.00 45.79           O  
ATOM    953  CB  LEU A 207      18.759  34.663   8.735  1.00 42.79           C  
ATOM    954  CG  LEU A 207      19.833  33.587   8.502  1.00 47.13           C  
ATOM    955  CD1 LEU A 207      20.111  33.318   6.997  1.00 33.61           C  
ATOM    956  CD2 LEU A 207      21.132  33.892   9.290  1.00 32.25           C  
ATOM    957  N   GLY A 208      16.182  35.430  10.802  1.00 31.20           N  
ATOM    958  CA  GLY A 208      15.145  36.327  11.273  1.00 32.81           C  
ATOM    959  C   GLY A 208      13.857  36.282  10.486  1.00 33.19           C  
ATOM    960  O   GLY A 208      12.997  37.135  10.676  1.00 36.90           O  
ATOM    961  N   LEU A 209      13.730  35.292   9.608  1.00 31.78           N  
ATOM    962  CA  LEU A 209      12.537  35.122   8.794  1.00 32.31           C  
ATOM    963  C   LEU A 209      11.385  34.440   9.542  1.00 36.92           C  
ATOM    964  O   LEU A 209      11.583  33.515  10.325  1.00 39.90           O  
ATOM    965  CB  LEU A 209      12.879  34.329   7.527  1.00 30.86           C  
ATOM    966  CG  LEU A 209      13.731  35.104   6.509  1.00 34.03           C  
ATOM    967  CD1 LEU A 209      14.277  34.184   5.462  1.00 32.65           C  
ATOM    968  CD2 LEU A 209      12.952  36.224   5.836  1.00 31.85           C  
ATOM    969  N   PHE A 210      10.175  34.915   9.290  1.00 36.79           N  
ATOM    970  CA  PHE A 210       8.974  34.259   9.781  1.00 40.91           C  
ATOM    971  C   PHE A 210       8.386  33.378   8.683  1.00 40.55           C  
ATOM    972  O   PHE A 210       8.885  33.374   7.552  1.00 57.72           O  
ATOM    973  CB  PHE A 210       7.959  35.299  10.251  1.00 50.14           C  
ATOM    974  CG  PHE A 210       8.417  36.106  11.438  1.00 61.84           C  
ATOM    975  CD1 PHE A 210       8.483  35.532  12.701  1.00 73.56           C  
ATOM    976  CD2 PHE A 210       8.766  37.440  11.298  1.00 59.55           C  
ATOM    977  CE1 PHE A 210       8.896  36.277  13.808  1.00 68.86           C  
ATOM    978  CE2 PHE A 210       9.175  38.189  12.395  1.00 56.74           C  
ATOM    979  CZ  PHE A 210       9.238  37.598  13.652  1.00 63.42           C  
ATOM    980  N   HIS A 211       7.340  32.624   9.006  1.00 36.67           N  
ATOM    981  CA  HIS A 211       6.718  31.721   8.023  1.00 46.10           C  
ATOM    982  C   HIS A 211       6.052  32.471   6.870  1.00 52.81           C  
ATOM    983  O   HIS A 211       5.600  33.614   7.010  1.00 51.59           O  
ATOM    984  CB  HIS A 211       5.693  30.785   8.687  1.00 37.75           C  
ATOM    985  CG  HIS A 211       6.319  29.693   9.503  1.00 39.46           C  
ATOM    986  ND1 HIS A 211       5.635  29.003  10.477  1.00 45.56           N  
ATOM    987  CD2 HIS A 211       7.571  29.171   9.487  1.00 34.93           C  
ATOM    988  CE1 HIS A 211       6.437  28.104  11.022  1.00 38.43           C  
ATOM    989  NE2 HIS A 211       7.615  28.187  10.438  1.00 35.09           N  
ATOM    990  N   SER A 212       6.023  31.818   5.716  1.00 50.17           N  
ATOM    991  CA  SER A 212       5.397  32.397   4.544  1.00 41.79           C  
ATOM    992  C   SER A 212       4.053  31.759   4.300  1.00 40.85           C  
ATOM    993  O   SER A 212       3.875  30.562   4.504  1.00 46.03           O  
ATOM    994  CB  SER A 212       6.276  32.228   3.315  1.00 43.91           C  
ATOM    995  OG  SER A 212       5.632  32.803   2.199  1.00 54.32           O  
ATOM    996  N   ALA A 213       3.098  32.552   3.845  1.00 43.17           N  
ATOM    997  CA  ALA A 213       1.790  32.000   3.524  1.00 56.40           C  
ATOM    998  C   ALA A 213       1.829  31.378   2.137  1.00 64.72           C  
ATOM    999  O   ALA A 213       0.866  30.743   1.710  1.00 68.81           O  
ATOM   1000  CB  ALA A 213       0.718  33.066   3.607  1.00 48.26           C  
ATOM   1001  N   ASN A 214       2.961  31.563   1.454  1.00 60.35           N  
ATOM   1002  CA  ASN A 214       3.158  31.078   0.094  1.00 52.94           C  
ATOM   1003  C   ASN A 214       3.774  29.673   0.034  1.00 57.52           C  
ATOM   1004  O   ASN A 214       4.904  29.440   0.485  1.00 57.45           O  
ATOM   1005  CB  ASN A 214       4.020  32.071  -0.680  1.00 52.32           C  
ATOM   1006  CG  ASN A 214       4.278  31.633  -2.108  1.00 66.03           C  
ATOM   1007  OD1 ASN A 214       3.617  30.731  -2.622  1.00 67.49           O  
ATOM   1008  ND2 ASN A 214       5.243  32.278  -2.762  1.00 73.98           N  
ATOM   1009  N   THR A 215       3.015  28.750  -0.551  1.00 44.93           N  
ATOM   1010  CA  THR A 215       3.405  27.357  -0.686  1.00 44.55           C  
ATOM   1011  C   THR A 215       4.638  27.145  -1.585  1.00 55.02           C  
ATOM   1012  O   THR A 215       5.289  26.096  -1.538  1.00 50.85           O  
ATOM   1013  CB  THR A 215       2.224  26.546  -1.235  1.00 57.66           C  
ATOM   1014  OG1 THR A 215       1.823  27.058  -2.517  1.00 64.10           O  
ATOM   1015  CG2 THR A 215       1.044  26.615  -0.270  1.00 48.17           C  
ATOM   1016  N   GLU A 216       4.955  28.149  -2.398  1.00 63.06           N  
ATOM   1017  CA  GLU A 216       6.163  28.146  -3.224  1.00 61.30           C  
ATOM   1018  C   GLU A 216       7.423  28.430  -2.402  1.00 56.65           C  
ATOM   1019  O   GLU A 216       8.537  28.117  -2.823  1.00 51.42           O  
ATOM   1020  CB  GLU A 216       6.054  29.191  -4.343  1.00 69.67           C  
ATOM   1021  CG  GLU A 216       4.713  29.216  -5.083  1.00 92.32           C  
ATOM   1022  CD  GLU A 216       4.482  28.009  -5.989  1.00104.79           C  
ATOM   1023  OE1 GLU A 216       4.446  28.193  -7.228  1.00110.31           O  
ATOM   1024  OE2 GLU A 216       4.314  26.884  -5.466  1.00104.27           O  
ATOM   1025  N   ALA A 217       7.244  29.037  -1.233  1.00 53.80           N  
ATOM   1026  CA  ALA A 217       8.381  29.502  -0.455  1.00 44.34           C  
ATOM   1027  C   ALA A 217       8.999  28.407   0.391  1.00 42.82           C  
ATOM   1028  O   ALA A 217       8.337  27.471   0.824  1.00 46.85           O  
ATOM   1029  CB  ALA A 217       7.980  30.654   0.418  1.00 44.64           C  
ATOM   1030  N   LEU A 218      10.293  28.539   0.618  1.00 46.52           N  
ATOM   1031  CA  LEU A 218      10.967  27.703   1.576  1.00 40.00           C  
ATOM   1032  C   LEU A 218      10.389  27.971   2.970  1.00 39.01           C  
ATOM   1033  O   LEU A 218      10.255  27.070   3.777  1.00 41.44           O  
ATOM   1034  CB  LEU A 218      12.458  27.972   1.527  1.00 31.72           C  
ATOM   1035  CG  LEU A 218      13.330  27.187   2.494  1.00 42.08           C  
ATOM   1036  CD1 LEU A 218      13.163  25.676   2.331  1.00 32.73           C  
ATOM   1037  CD2 LEU A 218      14.774  27.596   2.278  1.00 37.65           C  
ATOM   1038  N   MET A 219      10.003  29.207   3.246  1.00 35.04           N  
ATOM   1039  CA  MET A 219       9.546  29.533   4.590  1.00 40.93           C  
ATOM   1040  C   MET A 219       8.067  29.171   4.802  1.00 49.00           C  
ATOM   1041  O   MET A 219       7.411  29.624   5.746  1.00 43.26           O  
ATOM   1042  CB  MET A 219       9.803  31.014   4.889  1.00 34.90           C  
ATOM   1043  CG  MET A 219      11.278  31.337   4.970  1.00 31.98           C  
ATOM   1044  SD  MET A 219      12.185  30.136   5.967  1.00 47.44           S  
ATOM   1045  CE  MET A 219      11.724  30.684   7.610  1.00 48.89           C  
ATOM   1046  N   TYR A 220       7.536  28.345   3.919  1.00 48.67           N  
ATOM   1047  CA  TYR A 220       6.258  27.733   4.196  1.00 47.32           C  
ATOM   1048  C   TYR A 220       6.542  26.615   5.210  1.00 54.92           C  
ATOM   1049  O   TYR A 220       7.544  25.906   5.099  1.00 61.18           O  
ATOM   1050  CB  TYR A 220       5.619  27.220   2.909  1.00 42.93           C  
ATOM   1051  CG  TYR A 220       4.181  26.777   3.046  1.00 48.25           C  
ATOM   1052  CD1 TYR A 220       3.168  27.692   3.339  1.00 50.51           C  
ATOM   1053  CD2 TYR A 220       3.831  25.445   2.858  1.00 46.61           C  
ATOM   1054  CE1 TYR A 220       1.845  27.284   3.456  1.00 51.40           C  
ATOM   1055  CE2 TYR A 220       2.516  25.029   2.969  1.00 54.43           C  
ATOM   1056  CZ  TYR A 220       1.527  25.949   3.266  1.00 54.67           C  
ATOM   1057  OH  TYR A 220       0.227  25.514   3.372  1.00 53.75           O  
ATOM   1058  N   PRO A 221       5.684  26.483   6.231  1.00 49.27           N  
ATOM   1059  CA  PRO A 221       5.959  25.586   7.359  1.00 49.49           C  
ATOM   1060  C   PRO A 221       5.663  24.102   7.119  1.00 51.72           C  
ATOM   1061  O   PRO A 221       6.126  23.284   7.923  1.00 51.96           O  
ATOM   1062  CB  PRO A 221       5.054  26.138   8.461  1.00 37.67           C  
ATOM   1063  CG  PRO A 221       3.936  26.757   7.741  1.00 42.18           C  
ATOM   1064  CD  PRO A 221       4.515  27.340   6.487  1.00 47.26           C  
ATOM   1065  N   LEU A 222       4.916  23.749   6.070  1.00 44.65           N  
ATOM   1066  CA  LEU A 222       4.792  22.336   5.711  1.00 40.07           C  
ATOM   1067  C   LEU A 222       6.050  21.878   4.959  1.00 45.87           C  
ATOM   1068  O   LEU A 222       6.673  22.651   4.218  1.00 42.10           O  
ATOM   1069  CB  LEU A 222       3.546  22.091   4.884  1.00 47.15           C  
ATOM   1070  CG  LEU A 222       2.246  22.585   5.534  1.00 57.09           C  
ATOM   1071  CD1 LEU A 222       1.039  22.119   4.752  1.00 53.40           C  
ATOM   1072  CD2 LEU A 222       2.156  22.144   6.983  1.00 64.54           C  
ATOM   1073  N   TYR A 223       6.457  20.636   5.180  1.00 49.56           N  
ATOM   1074  CA  TYR A 223       7.669  20.129   4.538  1.00 53.12           C  
ATOM   1075  C   TYR A 223       7.365  19.751   3.090  1.00 57.80           C  
ATOM   1076  O   TYR A 223       6.440  18.977   2.833  1.00 48.17           O  
ATOM   1077  CB  TYR A 223       8.221  18.942   5.320  1.00 49.62           C  
ATOM   1078  CG  TYR A 223       9.197  18.074   4.575  1.00 47.55           C  
ATOM   1079  CD1 TYR A 223       8.831  16.798   4.161  1.00 50.19           C  
ATOM   1080  CD2 TYR A 223      10.486  18.512   4.295  1.00 46.37           C  
ATOM   1081  CE1 TYR A 223       9.714  15.982   3.481  1.00 46.06           C  
ATOM   1082  CE2 TYR A 223      11.383  17.699   3.614  1.00 46.13           C  
ATOM   1083  CZ  TYR A 223      10.985  16.428   3.215  1.00 44.91           C  
ATOM   1084  OH  TYR A 223      11.849  15.600   2.545  1.00 46.98           O  
ATOM   1085  N   HIS A 224       8.109  20.335   2.151  1.00 60.87           N  
ATOM   1086  CA  HIS A 224       7.858  20.103   0.723  1.00 72.90           C  
ATOM   1087  C   HIS A 224       8.349  18.720   0.319  1.00 64.05           C  
ATOM   1088  O   HIS A 224       9.455  18.580  -0.184  1.00 46.55           O  
ATOM   1089  CB  HIS A 224       8.540  21.170  -0.150  1.00 81.82           C  
ATOM   1090  CG  HIS A 224       8.005  22.557   0.043  1.00 86.85           C  
ATOM   1091  ND1 HIS A 224       8.425  23.385   1.065  1.00 88.98           N  
ATOM   1092  CD2 HIS A 224       7.090  23.267  -0.662  1.00 84.90           C  
ATOM   1093  CE1 HIS A 224       7.790  24.541   0.981  1.00 85.41           C  
ATOM   1094  NE2 HIS A 224       6.971  24.494  -0.056  1.00 82.24           N  
ATOM   1095  N   SER A 225       7.522  17.703   0.527  1.00 82.02           N  
ATOM   1096  CA  SER A 225       7.985  16.325   0.422  1.00 89.41           C  
ATOM   1097  C   SER A 225       8.406  15.955  -0.998  1.00 92.04           C  
ATOM   1098  O   SER A 225       9.089  14.953  -1.203  1.00 89.80           O  
ATOM   1099  CB  SER A 225       6.900  15.370   0.920  1.00 93.21           C  
ATOM   1100  OG  SER A 225       5.837  15.290  -0.004  1.00104.98           O  
ATOM   1101  N   LEU A 226       8.032  16.785  -1.967  1.00 96.52           N  
ATOM   1102  CA  LEU A 226       8.169  16.415  -3.371  1.00106.67           C  
ATOM   1103  C   LEU A 226       9.157  17.215  -4.197  1.00102.03           C  
ATOM   1104  O   LEU A 226       9.153  17.103  -5.425  1.00118.70           O  
ATOM   1105  CB  LEU A 226       6.824  16.515  -4.071  1.00110.00           C  
ATOM   1106  CG  LEU A 226       5.729  15.561  -3.650  1.00108.23           C  
ATOM   1107  CD1 LEU A 226       4.528  15.942  -4.460  1.00103.31           C  
ATOM   1108  CD2 LEU A 226       6.183  14.146  -3.940  1.00110.14           C  
ATOM   1109  N   THR A 227       9.980  18.032  -3.558  1.00 73.75           N  
ATOM   1110  CA  THR A 227      11.044  18.688  -4.296  1.00 71.32           C  
ATOM   1111  C   THR A 227      11.984  17.607  -4.846  1.00 87.28           C  
ATOM   1112  O   THR A 227      12.295  16.644  -4.145  1.00 91.03           O  
ATOM   1113  CB  THR A 227      11.798  19.685  -3.405  1.00 69.20           C  
ATOM   1114  OG1 THR A 227      10.856  20.563  -2.781  1.00 72.09           O  
ATOM   1115  CG2 THR A 227      12.762  20.519  -4.209  1.00 63.12           C  
ATOM   1116  N   ASP A 228      12.402  17.742  -6.104  1.00100.26           N  
ATOM   1117  CA  ASP A 228      13.296  16.757  -6.720  1.00115.13           C  
ATOM   1118  C   ASP A 228      14.762  17.084  -6.426  1.00110.29           C  
ATOM   1119  O   ASP A 228      15.638  16.233  -6.624  1.00118.00           O  
ATOM   1120  CB  ASP A 228      13.078  16.695  -8.231  1.00122.38           C  
ATOM   1121  CG  ASP A 228      13.615  17.924  -8.942  1.00124.08           C  
ATOM   1122  OD1 ASP A 228      14.013  17.800 -10.120  1.00125.13           O  
ATOM   1123  OD2 ASP A 228      13.651  19.012  -8.315  1.00119.18           O  
ATOM   1124  N   LEU A 229      14.996  18.332  -5.996  1.00 91.59           N  
ATOM   1125  CA  LEU A 229      16.296  18.861  -5.539  1.00 79.47           C  
ATOM   1126  C   LEU A 229      17.222  19.244  -6.674  1.00 79.24           C  
ATOM   1127  O   LEU A 229      18.030  20.155  -6.548  1.00 73.28           O  
ATOM   1128  CB  LEU A 229      17.030  17.865  -4.642  1.00 74.51           C  
ATOM   1129  CG  LEU A 229      16.456  17.559  -3.271  1.00 62.54           C  
ATOM   1130  CD1 LEU A 229      17.285  16.447  -2.632  1.00 63.02           C  
ATOM   1131  CD2 LEU A 229      16.436  18.826  -2.415  1.00 48.69           C  
ATOM   1132  N   THR A 230      17.125  18.507  -7.767  1.00 86.70           N  
ATOM   1133  CA  THR A 230      17.925  18.771  -8.946  1.00 87.55           C  
ATOM   1134  C   THR A 230      17.770  20.223  -9.388  1.00 95.23           C  
ATOM   1135  O   THR A 230      18.761  20.918  -9.607  1.00 94.05           O  
ATOM   1136  CB  THR A 230      17.524  17.830 -10.084  1.00 82.06           C  
ATOM   1137  OG1 THR A 230      17.680  16.472  -9.643  1.00 81.21           O  
ATOM   1138  CG2 THR A 230      18.371  18.090 -11.320  1.00 79.83           C  
ATOM   1139  N   ARG A 231      16.522  20.681  -9.479  1.00 99.82           N  
ATOM   1140  CA  ARG A 231      16.223  22.018  -9.985  1.00 96.69           C  
ATOM   1141  C   ARG A 231      15.689  22.954  -8.895  1.00 82.03           C  
ATOM   1142  O   ARG A 231      14.960  23.901  -9.185  1.00 76.35           O  
ATOM   1143  CB  ARG A 231      15.220  21.930 -11.142  1.00102.18           C  
ATOM   1144  CG  ARG A 231      15.763  21.250 -12.397  1.00108.07           C  
ATOM   1145  CD  ARG A 231      14.704  21.184 -13.485  1.00114.06           C  
ATOM   1146  NE  ARG A 231      14.278  22.523 -13.891  1.00114.53           N  
ATOM   1147  CZ  ARG A 231      14.875  23.260 -14.825  1.00112.97           C  
ATOM   1148  NH1 ARG A 231      15.928  22.793 -15.486  1.00113.73           N  
ATOM   1149  NH2 ARG A 231      14.402  24.465 -15.108  1.00110.03           N  
ATOM   1150  N   PHE A 232      16.071  22.695  -7.648  1.00 77.03           N  
ATOM   1151  CA  PHE A 232      15.680  23.563  -6.539  1.00 71.29           C  
ATOM   1152  C   PHE A 232      16.283  24.951  -6.630  1.00 71.48           C  
ATOM   1153  O   PHE A 232      17.489  25.098  -6.774  1.00 75.95           O  
ATOM   1154  CB  PHE A 232      16.085  22.963  -5.199  1.00 73.13           C  
ATOM   1155  CG  PHE A 232      15.871  23.901  -4.028  1.00 68.90           C  
ATOM   1156  CD1 PHE A 232      14.595  24.116  -3.511  1.00 72.78           C  
ATOM   1157  CD2 PHE A 232      16.939  24.557  -3.439  1.00 55.73           C  
ATOM   1158  CE1 PHE A 232      14.391  24.978  -2.423  1.00 62.84           C  
ATOM   1159  CE2 PHE A 232      16.737  25.435  -2.355  1.00 56.36           C  
ATOM   1160  CZ  PHE A 232      15.466  25.640  -1.845  1.00 52.41           C  
ATOM   1161  N   ARG A 233      15.430  25.963  -6.515  1.00 66.88           N  
ATOM   1162  CA  ARG A 233      15.852  27.358  -6.497  1.00 63.05           C  
ATOM   1163  C   ARG A 233      15.182  28.068  -5.316  1.00 62.19           C  
ATOM   1164  O   ARG A 233      14.149  27.628  -4.816  1.00 57.50           O  
ATOM   1165  CB  ARG A 233      15.505  28.062  -7.825  1.00 63.09           C  
ATOM   1166  CG  ARG A 233      16.549  27.922  -8.949  1.00 63.48           C  
ATOM   1167  N   LEU A 234      15.780  29.156  -4.852  1.00 62.60           N  
ATOM   1168  CA  LEU A 234      15.189  29.915  -3.765  1.00 48.86           C  
ATOM   1169  C   LEU A 234      14.010  30.687  -4.339  1.00 51.01           C  
ATOM   1170  O   LEU A 234      14.107  31.237  -5.422  1.00 59.88           O  
ATOM   1171  CB  LEU A 234      16.237  30.836  -3.124  1.00 40.16           C  
ATOM   1172  CG  LEU A 234      15.961  31.399  -1.734  1.00 40.93           C  
ATOM   1173  CD1 LEU A 234      15.421  30.311  -0.823  1.00 38.12           C  
ATOM   1174  CD2 LEU A 234      17.223  32.033  -1.123  1.00 41.74           C  
ATOM   1175  N   SER A 235      12.890  30.698  -3.629  1.00 53.29           N  
ATOM   1176  CA  SER A 235      11.668  31.374  -4.080  1.00 46.53           C  
ATOM   1177  C   SER A 235      11.784  32.899  -4.018  1.00 40.92           C  
ATOM   1178  O   SER A 235      12.576  33.418  -3.250  1.00 44.17           O  
ATOM   1179  CB  SER A 235      10.487  30.877  -3.233  1.00 48.84           C  
ATOM   1180  OG  SER A 235       9.510  31.866  -2.987  1.00 46.77           O  
ATOM   1181  N   GLN A 236      10.994  33.620  -4.815  1.00 49.01           N  
ATOM   1182  CA  GLN A 236      11.061  35.091  -4.831  1.00 53.51           C  
ATOM   1183  C   GLN A 236      10.566  35.737  -3.518  1.00 56.31           C  
ATOM   1184  O   GLN A 236      11.153  36.704  -3.038  1.00 55.12           O  
ATOM   1185  CB  GLN A 236      10.268  35.650  -6.021  1.00 55.19           C  
ATOM   1186  CG  GLN A 236      10.559  37.132  -6.356  1.00 58.97           C  
ATOM   1187  CD  GLN A 236      12.000  37.379  -6.806  1.00 63.88           C  
ATOM   1188  OE1 GLN A 236      12.460  36.809  -7.793  1.00 66.47           O  
ATOM   1189  NE2 GLN A 236      12.717  38.228  -6.076  1.00 64.49           N  
ATOM   1190  N   ASP A 237       9.485  35.204  -2.956  1.00 56.66           N  
ATOM   1191  CA  ASP A 237       9.034  35.573  -1.621  1.00 63.29           C  
ATOM   1192  C   ASP A 237      10.159  35.403  -0.595  1.00 54.51           C  
ATOM   1193  O   ASP A 237      10.274  36.170   0.355  1.00 53.94           O  
ATOM   1194  CB  ASP A 237       7.819  34.723  -1.221  1.00 76.24           C  
ATOM   1195  CG  ASP A 237       7.167  35.187   0.076  1.00 93.83           C  
ATOM   1196  OD1 ASP A 237       7.843  35.243   1.130  1.00 98.52           O  
ATOM   1197  OD2 ASP A 237       5.958  35.496   0.043  1.00101.55           O  
ATOM   1198  N   ASP A 238      10.992  34.394  -0.785  1.00 49.05           N  
ATOM   1199  CA  ASP A 238      12.034  34.111   0.190  1.00 55.37           C  
ATOM   1200  C   ASP A 238      13.184  35.112   0.068  1.00 59.32           C  
ATOM   1201  O   ASP A 238      13.742  35.557   1.070  1.00 60.41           O  
ATOM   1202  CB  ASP A 238      12.550  32.671   0.024  1.00 65.38           C  
ATOM   1203  CG  ASP A 238      11.527  31.608   0.463  1.00 69.53           C  
ATOM   1204  OD1 ASP A 238      10.879  31.771   1.526  1.00 63.82           O  
ATOM   1205  OD2 ASP A 238      11.378  30.601  -0.264  1.00 70.45           O  
ATOM   1206  N   ILE A 239      13.530  35.475  -1.162  1.00 60.05           N  
ATOM   1207  CA  ILE A 239      14.619  36.419  -1.398  1.00 51.56           C  
ATOM   1208  C   ILE A 239      14.239  37.828  -0.929  1.00 43.15           C  
ATOM   1209  O   ILE A 239      15.044  38.517  -0.288  1.00 39.96           O  
ATOM   1210  CB  ILE A 239      15.025  36.441  -2.895  1.00 47.46           C  
ATOM   1211  CG1 ILE A 239      15.555  35.061  -3.313  1.00 38.31           C  
ATOM   1212  CG2 ILE A 239      16.074  37.530  -3.157  1.00 43.54           C  
ATOM   1213  CD1 ILE A 239      15.665  34.854  -4.803  1.00 36.22           C  
ATOM   1214  N   ASN A 240      13.013  38.246  -1.240  1.00 36.54           N  
ATOM   1215  CA  ASN A 240      12.479  39.510  -0.730  1.00 40.44           C  
ATOM   1216  C   ASN A 240      12.526  39.564   0.798  1.00 45.70           C  
ATOM   1217  O   ASN A 240      12.826  40.593   1.385  1.00 59.39           O  
ATOM   1218  CB  ASN A 240      11.027  39.736  -1.177  1.00 44.79           C  
ATOM   1219  CG  ASN A 240      10.874  39.888  -2.677  1.00 50.29           C  
ATOM   1220  OD1 ASN A 240      11.779  40.341  -3.370  1.00 52.49           O  
ATOM   1221  ND2 ASN A 240       9.702  39.515  -3.183  1.00 61.69           N  
ATOM   1222  N   GLY A 241      12.212  38.448   1.438  1.00 38.85           N  
ATOM   1223  CA  GLY A 241      12.207  38.384   2.882  1.00 44.51           C  
ATOM   1224  C   GLY A 241      13.591  38.601   3.456  1.00 50.70           C  
ATOM   1225  O   GLY A 241      13.781  39.471   4.309  1.00 54.30           O  
ATOM   1226  N   ILE A 242      14.563  37.821   2.990  1.00 37.77           N  
ATOM   1227  CA  ILE A 242      15.900  37.891   3.568  1.00 39.57           C  
ATOM   1228  C   ILE A 242      16.571  39.211   3.174  1.00 45.61           C  
ATOM   1229  O   ILE A 242      17.386  39.747   3.917  1.00 49.34           O  
ATOM   1230  CB  ILE A 242      16.772  36.665   3.149  1.00 37.74           C  
ATOM   1231  CG1 ILE A 242      17.920  36.459   4.133  1.00 33.56           C  
ATOM   1232  CG2 ILE A 242      17.255  36.769   1.710  1.00 36.79           C  
ATOM   1233  CD1 ILE A 242      17.445  36.212   5.534  1.00 35.83           C  
ATOM   1234  N   GLN A 243      16.193  39.763   2.027  1.00 50.72           N  
ATOM   1235  CA  GLN A 243      16.782  41.021   1.598  1.00 51.37           C  
ATOM   1236  C   GLN A 243      16.091  42.229   2.236  1.00 50.32           C  
ATOM   1237  O   GLN A 243      16.590  43.346   2.164  1.00 37.28           O  
ATOM   1238  CB  GLN A 243      16.747  41.143   0.072  1.00 49.49           C  
ATOM   1239  CG  GLN A 243      17.822  40.341  -0.644  1.00 42.77           C  
ATOM   1240  CD  GLN A 243      17.905  40.677  -2.129  1.00 42.66           C  
ATOM   1241  OE1 GLN A 243      17.197  41.559  -2.629  1.00 37.97           O  
ATOM   1242  NE2 GLN A 243      18.780  39.983  -2.837  1.00 40.03           N  
ATOM   1243  N   SER A 244      14.934  42.029   2.855  1.00 55.19           N  
ATOM   1244  CA  SER A 244      14.328  43.147   3.573  1.00 52.53           C  
ATOM   1245  C   SER A 244      15.065  43.303   4.892  1.00 51.17           C  
ATOM   1246  O   SER A 244      15.236  44.404   5.368  1.00 55.70           O  
ATOM   1247  CB  SER A 244      12.830  42.951   3.794  1.00 53.85           C  
ATOM   1248  OG  SER A 244      12.551  41.664   4.314  1.00 70.15           O  
ATOM   1249  N   LEU A 245      15.535  42.190   5.449  1.00 51.63           N  
ATOM   1250  CA  LEU A 245      16.356  42.212   6.657  1.00 52.48           C  
ATOM   1251  C   LEU A 245      17.786  42.719   6.438  1.00 52.89           C  
ATOM   1252  O   LEU A 245      18.201  43.679   7.095  1.00 58.05           O  
ATOM   1253  CB  LEU A 245      16.413  40.819   7.292  1.00 45.90           C  
ATOM   1254  CG  LEU A 245      15.087  40.268   7.826  1.00 41.78           C  
ATOM   1255  CD1 LEU A 245      15.307  39.008   8.664  1.00 42.49           C  
ATOM   1256  CD2 LEU A 245      14.344  41.321   8.619  1.00 39.80           C  
ATOM   1257  N   TYR A 246      18.536  42.089   5.532  1.00 46.73           N  
ATOM   1258  CA  TYR A 246      19.954  42.431   5.363  1.00 46.04           C  
ATOM   1259  C   TYR A 246      20.308  43.152   4.052  1.00 39.96           C  
ATOM   1260  O   TYR A 246      21.480  43.512   3.836  1.00 37.33           O  
ATOM   1261  CB  TYR A 246      20.808  41.170   5.493  1.00 41.49           C  
ATOM   1262  CG  TYR A 246      20.555  40.425   6.765  1.00 42.45           C  
ATOM   1263  CD1 TYR A 246      21.109  40.858   7.948  1.00 36.42           C  
ATOM   1264  CD2 TYR A 246      19.739  39.295   6.789  1.00 47.47           C  
ATOM   1265  CE1 TYR A 246      20.873  40.191   9.136  1.00 42.52           C  
ATOM   1266  CE2 TYR A 246      19.490  38.618   7.976  1.00 49.19           C  
ATOM   1267  CZ  TYR A 246      20.066  39.078   9.153  1.00 48.54           C  
ATOM   1268  OH  TYR A 246      19.851  38.437  10.357  1.00 47.88           O  
ATOM   1269  N   GLY A 247      19.316  43.357   3.187  1.00 37.43           N  
ATOM   1270  CA  GLY A 247      19.491  44.177   1.990  1.00 44.47           C  
ATOM   1271  C   GLY A 247      20.608  43.806   1.028  1.00 47.08           C  
ATOM   1272  O   GLY A 247      20.632  42.707   0.483  1.00 50.57           O  
TER    1273      GLY A 247                                                      
ATOM   1274  N   CYS B   1      10.318  26.127  12.120  1.00 40.13           N  
ATOM   1275  CA  CYS B   1       9.384  25.037  12.372  1.00 46.15           C  
ATOM   1276  C   CYS B   1       8.993  24.336  11.084  1.00 44.77           C  
ATOM   1277  O   CYS B   1       8.619  24.971  10.112  1.00 45.08           O  
ATOM   1278  CB  CYS B   1       8.122  25.534  13.078  1.00 40.67           C  
ATOM   1279  SG  CYS B   1       7.122  24.155  13.715  1.00 41.10           S  
ATOM   1280  N   THR B   2       9.056  23.014  11.098  1.00 43.97           N  
ATOM   1281  CA  THR B   2       8.814  22.221   9.903  1.00 39.73           C  
ATOM   1282  C   THR B   2       7.906  21.058  10.224  1.00 41.38           C  
ATOM   1283  O   THR B   2       8.248  20.218  11.063  1.00 39.91           O  
ATOM   1284  CB  THR B   2      10.114  21.665   9.316  1.00 44.86           C  
ATOM   1285  OG1 THR B   2      10.977  22.743   8.949  1.00 48.00           O  
ATOM   1286  CG2 THR B   2       9.817  20.821   8.101  1.00 41.17           C  
ATOM   1287  N   CYS B   3       6.772  20.991   9.533  1.00 38.99           N  
ATOM   1288  CA  CYS B   3       5.722  20.047   9.882  1.00 36.66           C  
ATOM   1289  C   CYS B   3       5.392  19.068   8.786  1.00 37.04           C  
ATOM   1290  O   CYS B   3       5.409  19.420   7.614  1.00 43.68           O  
ATOM   1291  CB  CYS B   3       4.436  20.797  10.244  1.00 38.73           C  
ATOM   1292  SG  CYS B   3       4.616  21.906  11.606  1.00 74.53           S  
ATOM   1293  N   VAL B   4       5.078  17.839   9.189  1.00 41.96           N  
ATOM   1294  CA  VAL B   4       4.284  16.916   8.377  1.00 41.83           C  
ATOM   1295  C   VAL B   4       2.975  16.672   9.121  1.00 44.44           C  
ATOM   1296  O   VAL B   4       2.883  15.756   9.942  1.00 50.02           O  
ATOM   1297  CB  VAL B   4       5.006  15.582   8.123  1.00 39.96           C  
ATOM   1298  CG1 VAL B   4       4.082  14.593   7.423  1.00 40.65           C  
ATOM   1299  CG2 VAL B   4       6.264  15.813   7.315  1.00 36.97           C  
ATOM   1300  N   PRO B   5       1.972  17.524   8.878  1.00 37.91           N  
ATOM   1301  CA  PRO B   5       0.736  17.382   9.653  1.00 38.84           C  
ATOM   1302  C   PRO B   5       0.096  16.037   9.362  1.00 42.71           C  
ATOM   1303  O   PRO B   5       0.180  15.536   8.243  1.00 46.88           O  
ATOM   1304  CB  PRO B   5      -0.139  18.561   9.186  1.00 37.26           C  
ATOM   1305  CG  PRO B   5       0.493  19.069   7.935  1.00 36.59           C  
ATOM   1306  CD  PRO B   5       1.951  18.677   7.965  1.00 31.95           C  
ATOM   1307  N   PRO B   6      -0.513  15.435  10.384  1.00 42.98           N  
ATOM   1308  CA  PRO B   6      -0.907  14.034  10.290  1.00 38.91           C  
ATOM   1309  C   PRO B   6      -2.201  13.819   9.535  1.00 40.12           C  
ATOM   1310  O   PRO B   6      -3.020  14.719   9.418  1.00 33.75           O  
ATOM   1311  CB  PRO B   6      -1.091  13.644  11.759  1.00 35.67           C  
ATOM   1312  CG  PRO B   6      -1.612  14.905  12.369  1.00 31.37           C  
ATOM   1313  CD  PRO B   6      -0.884  16.021  11.689  1.00 30.27           C  
ATOM   1314  N   HIS B   7      -2.398  12.602   9.052  1.00 48.44           N  
ATOM   1315  CA  HIS B   7      -3.702  12.209   8.568  1.00 41.53           C  
ATOM   1316  C   HIS B   7      -4.722  12.308   9.712  1.00 45.01           C  
ATOM   1317  O   HIS B   7      -4.410  11.987  10.872  1.00 35.65           O  
ATOM   1318  CB  HIS B   7      -3.634  10.806   8.007  1.00 38.59           C  
ATOM   1319  CG  HIS B   7      -4.869  10.389   7.278  1.00 40.44           C  
ATOM   1320  ND1 HIS B   7      -6.059  10.129   7.921  1.00 46.96           N  
ATOM   1321  CD2 HIS B   7      -5.095  10.180   5.959  1.00 42.34           C  
ATOM   1322  CE1 HIS B   7      -6.971   9.782   7.025  1.00 53.50           C  
ATOM   1323  NE2 HIS B   7      -6.410   9.800   5.830  1.00 47.83           N  
ATOM   1324  N   PRO B   8      -5.940  12.767   9.392  1.00 47.31           N  
ATOM   1325  CA  PRO B   8      -7.015  12.920  10.384  1.00 41.87           C  
ATOM   1326  C   PRO B   8      -7.184  11.697  11.308  1.00 41.15           C  
ATOM   1327  O   PRO B   8      -7.322  11.862  12.535  1.00 38.50           O  
ATOM   1328  CB  PRO B   8      -8.262  13.107   9.518  1.00 44.76           C  
ATOM   1329  CG  PRO B   8      -7.771  13.625   8.212  1.00 35.62           C  
ATOM   1330  CD  PRO B   8      -6.365  13.142   8.028  1.00 35.64           C  
ATOM   1331  N   GLN B   9      -7.174  10.491  10.733  1.00 38.99           N  
ATOM   1332  CA  GLN B   9      -7.278   9.269  11.539  1.00 42.65           C  
ATOM   1333  C   GLN B   9      -6.106   9.163  12.510  1.00 45.32           C  
ATOM   1334  O   GLN B   9      -6.296   8.838  13.675  1.00 45.62           O  
ATOM   1335  CB  GLN B   9      -7.346   8.018  10.666  1.00 43.84           C  
ATOM   1336  CG  GLN B   9      -7.208   6.724  11.461  1.00 46.60           C  
ATOM   1337  CD  GLN B   9      -7.649   5.488  10.680  1.00 52.55           C  
ATOM   1338  OE1 GLN B   9      -8.558   5.554   9.860  1.00 50.13           O  
ATOM   1339  NE2 GLN B   9      -7.004   4.351  10.940  1.00 57.73           N  
ATOM   1340  N   THR B  10      -4.897   9.445  12.031  1.00 46.29           N  
ATOM   1341  CA  THR B  10      -3.737   9.460  12.906  1.00 43.23           C  
ATOM   1342  C   THR B  10      -3.940  10.489  14.001  1.00 44.36           C  
ATOM   1343  O   THR B  10      -3.725  10.207  15.169  1.00 51.94           O  
ATOM   1344  CB  THR B  10      -2.432   9.788  12.163  1.00 43.23           C  
ATOM   1345  OG1 THR B  10      -2.227   8.864  11.087  1.00 47.69           O  
ATOM   1346  CG2 THR B  10      -1.272   9.685  13.115  1.00 39.96           C  
ATOM   1347  N   ALA B  11      -4.361  11.685  13.609  1.00 45.92           N  
ATOM   1348  CA  ALA B  11      -4.612  12.758  14.554  1.00 40.25           C  
ATOM   1349  C   ALA B  11      -5.601  12.322  15.643  1.00 49.30           C  
ATOM   1350  O   ALA B  11      -5.416  12.625  16.819  1.00 51.51           O  
ATOM   1351  CB  ALA B  11      -5.122  13.963  13.835  1.00 33.01           C  
ATOM   1352  N   PHE B  12      -6.646  11.605  15.252  1.00 43.30           N  
ATOM   1353  CA  PHE B  12      -7.613  11.113  16.220  1.00 41.31           C  
ATOM   1354  C   PHE B  12      -6.950  10.142  17.179  1.00 53.15           C  
ATOM   1355  O   PHE B  12      -7.052  10.278  18.406  1.00 63.45           O  
ATOM   1356  CB  PHE B  12      -8.785  10.424  15.517  1.00 46.62           C  
ATOM   1357  CG  PHE B  12      -9.872   9.975  16.449  1.00 54.15           C  
ATOM   1358  CD1 PHE B  12      -9.833   8.725  17.040  1.00 56.01           C  
ATOM   1359  CD2 PHE B  12     -10.945  10.804  16.736  1.00 62.25           C  
ATOM   1360  CE1 PHE B  12     -10.844   8.312  17.910  1.00 60.75           C  
ATOM   1361  CE2 PHE B  12     -11.964  10.387  17.599  1.00 64.73           C  
ATOM   1362  CZ  PHE B  12     -11.906   9.142  18.185  1.00 61.70           C  
ATOM   1363  N   CYS B  13      -6.272   9.153  16.611  1.00 49.62           N  
ATOM   1364  CA  CYS B  13      -5.755   8.042  17.396  1.00 52.49           C  
ATOM   1365  C   CYS B  13      -4.646   8.449  18.356  1.00 56.73           C  
ATOM   1366  O   CYS B  13      -4.491   7.858  19.425  1.00 66.05           O  
ATOM   1367  CB  CYS B  13      -5.266   6.932  16.463  1.00 47.36           C  
ATOM   1368  SG  CYS B  13      -6.624   6.124  15.581  1.00 73.56           S  
ATOM   1369  N   ASN B  14      -3.880   9.467  17.985  1.00 46.58           N  
ATOM   1370  CA  ASN B  14      -2.681   9.791  18.742  1.00 53.00           C  
ATOM   1371  C   ASN B  14      -2.846  10.993  19.638  1.00 53.46           C  
ATOM   1372  O   ASN B  14      -1.979  11.282  20.461  1.00 64.15           O  
ATOM   1373  CB  ASN B  14      -1.504  10.008  17.797  1.00 54.68           C  
ATOM   1374  CG  ASN B  14      -0.980   8.706  17.219  1.00 61.52           C  
ATOM   1375  OD1 ASN B  14      -1.581   7.638  17.398  1.00 58.79           O  
ATOM   1376  ND2 ASN B  14       0.161   8.784  16.539  1.00 65.93           N  
ATOM   1377  N   SER B  15      -3.958  11.694  19.476  1.00 43.87           N  
ATOM   1378  CA  SER B  15      -4.249  12.804  20.354  1.00 46.74           C  
ATOM   1379  C   SER B  15      -4.902  12.292  21.620  1.00 57.13           C  
ATOM   1380  O   SER B  15      -5.578  11.265  21.603  1.00 64.03           O  
ATOM   1381  CB  SER B  15      -5.132  13.826  19.652  1.00 40.03           C  
ATOM   1382  OG  SER B  15      -4.356  14.534  18.705  1.00 34.68           O  
ATOM   1383  N   ASP B  16      -4.677  12.992  22.726  1.00 53.71           N  
ATOM   1384  CA  ASP B  16      -5.310  12.607  23.984  1.00 52.47           C  
ATOM   1385  C   ASP B  16      -6.705  13.215  24.057  1.00 48.26           C  
ATOM   1386  O   ASP B  16      -7.607  12.615  24.622  1.00 53.12           O  
ATOM   1387  CB  ASP B  16      -4.458  13.029  25.182  1.00 56.22           C  
ATOM   1388  CG  ASP B  16      -3.125  12.300  25.236  1.00 70.82           C  
ATOM   1389  OD1 ASP B  16      -3.125  11.061  25.099  1.00 80.25           O  
ATOM   1390  OD2 ASP B  16      -2.077  12.965  25.407  1.00 72.66           O  
ATOM   1391  N   LEU B  17      -6.886  14.397  23.468  1.00 50.53           N  
ATOM   1392  CA  LEU B  17      -8.207  15.036  23.419  1.00 48.94           C  
ATOM   1393  C   LEU B  17      -8.602  15.331  21.985  1.00 52.59           C  
ATOM   1394  O   LEU B  17      -7.769  15.731  21.159  1.00 48.77           O  
ATOM   1395  CB  LEU B  17      -8.249  16.347  24.226  1.00 41.38           C  
ATOM   1396  CG  LEU B  17      -8.125  16.374  25.759  1.00 47.83           C  
ATOM   1397  CD1 LEU B  17      -8.399  17.779  26.266  1.00 54.74           C  
ATOM   1398  CD2 LEU B  17      -9.057  15.407  26.425  1.00 47.05           C  
ATOM   1399  N   VAL B  18      -9.877  15.133  21.681  1.00 53.58           N  
ATOM   1400  CA  VAL B  18     -10.405  15.544  20.391  1.00 46.05           C  
ATOM   1401  C   VAL B  18     -11.736  16.197  20.634  1.00 46.24           C  
ATOM   1402  O   VAL B  18     -12.665  15.539  21.133  1.00 42.31           O  
ATOM   1403  CB  VAL B  18     -10.573  14.378  19.422  1.00 41.61           C  
ATOM   1404  CG1 VAL B  18     -11.247  14.866  18.151  1.00 38.32           C  
ATOM   1405  CG2 VAL B  18      -9.226  13.731  19.125  1.00 38.68           C  
ATOM   1406  N   ILE B  19     -11.806  17.492  20.307  1.00 41.20           N  
ATOM   1407  CA  ILE B  19     -12.968  18.325  20.615  1.00 49.71           C  
ATOM   1408  C   ILE B  19     -13.265  19.351  19.556  1.00 43.04           C  
ATOM   1409  O   ILE B  19     -12.383  19.751  18.795  1.00 36.66           O  
ATOM   1410  CB  ILE B  19     -12.813  19.129  21.942  1.00 41.38           C  
ATOM   1411  CG1 ILE B  19     -11.601  20.068  21.862  1.00 44.74           C  
ATOM   1412  CG2 ILE B  19     -12.719  18.209  23.134  1.00 48.42           C  
ATOM   1413  CD1 ILE B  19     -11.581  21.153  22.920  1.00 45.43           C  
ATOM   1414  N   ARG B  20     -14.527  19.771  19.544  1.00 42.68           N  
ATOM   1415  CA  ARG B  20     -14.957  21.000  18.897  1.00 47.37           C  
ATOM   1416  C   ARG B  20     -14.956  22.164  19.877  1.00 48.42           C  
ATOM   1417  O   ARG B  20     -15.533  22.063  20.969  1.00 48.62           O  
ATOM   1418  CB  ARG B  20     -16.364  20.856  18.333  1.00 57.41           C  
ATOM   1419  CG  ARG B  20     -16.492  20.014  17.098  1.00 65.23           C  
ATOM   1420  CD  ARG B  20     -17.751  20.444  16.384  1.00 67.42           C  
ATOM   1421  NE  ARG B  20     -18.667  19.350  16.108  1.00 65.51           N  
ATOM   1422  CZ  ARG B  20     -19.979  19.509  16.018  1.00 68.23           C  
ATOM   1423  NH1 ARG B  20     -20.507  20.714  16.212  1.00 69.37           N  
ATOM   1424  NH2 ARG B  20     -20.757  18.466  15.752  1.00 70.79           N  
ATOM   1425  N   ALA B  21     -14.356  23.283  19.479  1.00 42.65           N  
ATOM   1426  CA  ALA B  21     -14.368  24.457  20.344  1.00 42.80           C  
ATOM   1427  C   ALA B  21     -14.345  25.783  19.584  1.00 44.90           C  
ATOM   1428  O   ALA B  21     -13.938  25.836  18.431  1.00 44.75           O  
ATOM   1429  CB  ALA B  21     -13.208  24.388  21.297  1.00 43.99           C  
ATOM   1430  N   LYS B  22     -14.803  26.850  20.240  1.00 53.42           N  
ATOM   1431  CA  LYS B  22     -14.699  28.214  19.707  1.00 51.85           C  
ATOM   1432  C   LYS B  22     -13.533  28.963  20.372  1.00 48.27           C  
ATOM   1433  O   LYS B  22     -13.242  28.728  21.538  1.00 51.10           O  
ATOM   1434  CB  LYS B  22     -16.008  28.976  19.918  1.00 47.15           C  
ATOM   1435  CG  LYS B  22     -17.218  28.349  19.242  1.00 48.40           C  
ATOM   1436  CD  LYS B  22     -18.417  29.282  19.273  1.00 59.37           C  
ATOM   1437  CE  LYS B  22     -19.555  28.739  20.150  1.00 76.49           C  
ATOM   1438  NZ  LYS B  22     -19.743  29.469  21.451  1.00 82.28           N  
ATOM   1439  N   PHE B  23     -12.855  29.841  19.636  1.00 42.29           N  
ATOM   1440  CA  PHE B  23     -11.754  30.625  20.215  1.00 42.01           C  
ATOM   1441  C   PHE B  23     -12.242  31.971  20.683  1.00 48.42           C  
ATOM   1442  O   PHE B  23     -12.739  32.772  19.886  1.00 50.40           O  
ATOM   1443  CB  PHE B  23     -10.619  30.838  19.218  1.00 39.91           C  
ATOM   1444  CG  PHE B  23      -9.724  29.661  19.067  1.00 37.47           C  
ATOM   1445  CD1 PHE B  23      -8.418  29.717  19.504  1.00 36.10           C  
ATOM   1446  CD2 PHE B  23     -10.194  28.488  18.487  1.00 43.53           C  
ATOM   1447  CE1 PHE B  23      -7.595  28.631  19.366  1.00 34.10           C  
ATOM   1448  CE2 PHE B  23      -9.373  27.392  18.346  1.00 34.24           C  
ATOM   1449  CZ  PHE B  23      -8.076  27.457  18.790  1.00 33.20           C  
ATOM   1450  N   VAL B  24     -12.071  32.252  21.967  1.00 46.39           N  
ATOM   1451  CA  VAL B  24     -12.819  33.359  22.531  1.00 51.55           C  
ATOM   1452  C   VAL B  24     -12.001  34.625  22.789  1.00 62.09           C  
ATOM   1453  O   VAL B  24     -12.536  35.722  22.715  1.00 66.27           O  
ATOM   1454  CB  VAL B  24     -13.512  32.913  23.815  1.00 51.98           C  
ATOM   1455  CG1 VAL B  24     -14.133  31.547  23.608  1.00 50.77           C  
ATOM   1456  CG2 VAL B  24     -12.532  32.840  24.924  1.00 57.84           C  
ATOM   1457  N   GLY B  25     -10.709  34.489  23.058  1.00 65.83           N  
ATOM   1458  CA  GLY B  25      -9.915  35.647  23.422  1.00 57.77           C  
ATOM   1459  C   GLY B  25      -8.617  35.729  22.658  1.00 49.64           C  
ATOM   1460  O   GLY B  25      -8.398  34.996  21.705  1.00 62.52           O  
ATOM   1461  N   THR B  26      -7.770  36.653  23.073  1.00 53.47           N  
ATOM   1462  CA  THR B  26      -6.414  36.779  22.571  1.00 58.56           C  
ATOM   1463  C   THR B  26      -5.556  35.897  23.450  1.00 58.26           C  
ATOM   1464  O   THR B  26      -5.854  35.740  24.632  1.00 68.76           O  
ATOM   1465  CB  THR B  26      -5.922  38.234  22.650  1.00 69.91           C  
ATOM   1466  OG1 THR B  26      -7.028  39.115  22.434  1.00 72.95           O  
ATOM   1467  CG2 THR B  26      -4.827  38.522  21.626  1.00 72.49           C  
ATOM   1468  N   PRO B  27      -4.492  35.311  22.899  1.00 50.30           N  
ATOM   1469  CA  PRO B  27      -3.641  34.498  23.771  1.00 52.58           C  
ATOM   1470  C   PRO B  27      -2.894  35.336  24.805  1.00 53.93           C  
ATOM   1471  O   PRO B  27      -2.626  36.508  24.553  1.00 49.37           O  
ATOM   1472  CB  PRO B  27      -2.663  33.840  22.792  1.00 51.61           C  
ATOM   1473  CG  PRO B  27      -2.659  34.743  21.612  1.00 51.81           C  
ATOM   1474  CD  PRO B  27      -4.062  35.246  21.498  1.00 51.54           C  
ATOM   1475  N   GLU B  28      -2.592  34.745  25.959  1.00 51.39           N  
ATOM   1476  CA  GLU B  28      -1.748  35.389  26.956  1.00 49.05           C  
ATOM   1477  C   GLU B  28      -0.396  34.689  26.921  1.00 52.87           C  
ATOM   1478  O   GLU B  28      -0.340  33.468  26.810  1.00 49.85           O  
ATOM   1479  CB  GLU B  28      -2.363  35.310  28.351  1.00 53.59           C  
ATOM   1480  CG  GLU B  28      -3.813  35.725  28.456  1.00 63.09           C  
ATOM   1481  CD  GLU B  28      -4.458  35.229  29.752  1.00 77.08           C  
ATOM   1482  OE1 GLU B  28      -5.111  34.157  29.734  1.00 77.99           O  
ATOM   1483  OE2 GLU B  28      -4.302  35.909  30.791  1.00 83.82           O  
ATOM   1484  N   VAL B  29       0.688  35.447  27.040  1.00 69.97           N  
ATOM   1485  CA  VAL B  29       2.000  34.927  26.661  1.00 82.73           C  
ATOM   1486  C   VAL B  29       2.748  34.114  27.735  1.00 82.41           C  
ATOM   1487  O   VAL B  29       3.495  33.222  27.366  1.00 88.42           O  
ATOM   1488  CB  VAL B  29       2.930  36.071  26.187  1.00 93.79           C  
ATOM   1489  CG1 VAL B  29       4.029  35.516  25.291  1.00 83.15           C  
ATOM   1490  CG2 VAL B  29       2.135  37.136  25.442  1.00102.14           C  
ATOM   1491  N   ASN B  30       2.585  34.415  29.027  1.00 73.31           N  
ATOM   1492  CA  ASN B  30       3.221  33.615  30.102  1.00 77.08           C  
ATOM   1493  C   ASN B  30       4.725  33.340  29.912  1.00 77.32           C  
ATOM   1494  O   ASN B  30       5.094  32.209  29.577  1.00 67.78           O  
ATOM   1495  CB  ASN B  30       2.484  32.264  30.242  1.00 74.52           C  
ATOM   1496  CG  ASN B  30       2.894  31.456  31.503  1.00 82.31           C  
ATOM   1497  OD1 ASN B  30       4.013  31.562  32.016  1.00 64.34           O  
ATOM   1498  ND2 ASN B  30       1.968  30.624  31.984  1.00 93.65           N  
ATOM   1499  N   GLN B  31       5.589  34.334  30.149  1.00 80.21           N  
ATOM   1500  CA  GLN B  31       7.004  34.195  29.767  1.00 80.50           C  
ATOM   1501  C   GLN B  31       7.797  33.370  30.788  1.00 79.71           C  
ATOM   1502  O   GLN B  31       8.958  33.033  30.574  1.00 76.40           O  
ATOM   1503  CB  GLN B  31       7.651  35.582  29.542  1.00 76.24           C  
ATOM   1504  CG  GLN B  31       9.152  35.594  29.160  0.00 70.72           C  
ATOM   1505  CD  GLN B  31       9.600  34.370  28.359  0.00 65.01           C  
ATOM   1506  OE1 GLN B  31       8.971  33.984  27.376  0.00 62.00           O  
ATOM   1507  NE2 GLN B  31      10.683  33.738  28.809  0.00 65.96           N  
ATOM   1508  N   THR B  32       7.176  32.979  31.888  1.00 82.50           N  
ATOM   1509  CA  THR B  32       7.908  32.081  32.765  1.00 78.47           C  
ATOM   1510  C   THR B  32       8.051  30.686  32.095  1.00 80.24           C  
ATOM   1511  O   THR B  32       9.135  30.110  32.130  1.00 79.34           O  
ATOM   1512  CB  THR B  32       7.261  31.996  34.181  1.00 82.01           C  
ATOM   1513  OG1 THR B  32       8.264  31.625  35.128  1.00 90.18           O  
ATOM   1514  CG2 THR B  32       6.087  31.015  34.265  1.00 77.80           C  
ATOM   1515  N   THR B  33       7.002  30.185  31.431  1.00 74.96           N  
ATOM   1516  CA  THR B  33       7.003  28.832  30.850  1.00 65.90           C  
ATOM   1517  C   THR B  33       7.473  28.732  29.384  1.00 65.79           C  
ATOM   1518  O   THR B  33       8.042  27.717  28.981  1.00 69.08           O  
ATOM   1519  CB  THR B  33       5.591  28.192  30.923  1.00 82.86           C  
ATOM   1520  OG1 THR B  33       5.631  26.864  30.388  1.00 80.53           O  
ATOM   1521  CG2 THR B  33       4.586  28.990  30.115  1.00 73.36           C  
ATOM   1522  N   GLY B  34       7.224  29.766  28.585  1.00 55.06           N  
ATOM   1523  CA  GLY B  34       7.534  29.727  27.165  1.00 45.43           C  
ATOM   1524  C   GLY B  34       6.319  29.448  26.292  1.00 47.22           C  
ATOM   1525  O   GLY B  34       6.431  29.322  25.074  1.00 45.68           O  
ATOM   1526  N   TYR B  35       5.151  29.361  26.918  1.00 46.11           N  
ATOM   1527  CA  TYR B  35       3.922  29.024  26.213  1.00 40.28           C  
ATOM   1528  C   TYR B  35       2.865  30.107  26.305  1.00 48.60           C  
ATOM   1529  O   TYR B  35       2.741  30.778  27.310  1.00 64.78           O  
ATOM   1530  CB  TYR B  35       3.339  27.709  26.749  1.00 39.37           C  
ATOM   1531  CG  TYR B  35       4.138  26.497  26.334  1.00 38.66           C  
ATOM   1532  CD1 TYR B  35       5.318  26.174  26.972  1.00 40.39           C  
ATOM   1533  CD2 TYR B  35       3.739  25.709  25.273  1.00 36.64           C  
ATOM   1534  CE1 TYR B  35       6.051  25.091  26.594  1.00 40.22           C  
ATOM   1535  CE2 TYR B  35       4.476  24.633  24.878  1.00 36.42           C  
ATOM   1536  CZ  TYR B  35       5.632  24.323  25.541  1.00 38.25           C  
ATOM   1537  OH  TYR B  35       6.376  23.219  25.162  1.00 40.12           O  
ATOM   1538  N   GLN B  36       2.087  30.259  25.245  1.00 51.09           N  
ATOM   1539  CA  GLN B  36       0.923  31.130  25.256  1.00 45.65           C  
ATOM   1540  C   GLN B  36      -0.329  30.264  25.286  1.00 49.31           C  
ATOM   1541  O   GLN B  36      -0.309  29.126  24.784  1.00 36.54           O  
ATOM   1542  CB  GLN B  36       0.924  32.015  24.022  1.00 43.91           C  
ATOM   1543  CG  GLN B  36       1.395  31.226  22.812  1.00 52.66           C  
ATOM   1544  CD  GLN B  36       0.927  31.790  21.502  1.00 47.59           C  
ATOM   1545  OE1 GLN B  36       0.072  32.672  21.452  1.00 52.53           O  
ATOM   1546  NE2 GLN B  36       1.486  31.280  20.424  1.00 41.28           N  
ATOM   1547  N   ARG B  37      -1.416  30.782  25.859  1.00 42.27           N  
ATOM   1548  CA  ARG B  37      -2.644  29.996  25.903  1.00 39.53           C  
ATOM   1549  C   ARG B  37      -3.834  30.761  25.370  1.00 41.34           C  
ATOM   1550  O   ARG B  37      -3.949  31.968  25.558  1.00 47.79           O  
ATOM   1551  CB  ARG B  37      -2.946  29.507  27.327  1.00 41.67           C  
ATOM   1552  CG  ARG B  37      -3.203  30.608  28.322  1.00 44.59           C  
ATOM   1553  CD  ARG B  37      -3.817  30.086  29.587  1.00 48.88           C  
ATOM   1554  NE  ARG B  37      -4.008  31.175  30.544  1.00 64.15           N  
ATOM   1555  CZ  ARG B  37      -4.798  31.116  31.611  1.00 68.92           C  
ATOM   1556  NH1 ARG B  37      -5.495  30.019  31.870  1.00 67.25           N  
ATOM   1557  NH2 ARG B  37      -4.899  32.162  32.414  1.00 75.81           N  
ATOM   1558  N   TYR B  38      -4.709  30.031  24.690  1.00 38.82           N  
ATOM   1559  CA  TYR B  38      -5.977  30.554  24.227  1.00 39.63           C  
ATOM   1560  C   TYR B  38      -7.115  30.059  25.109  1.00 45.34           C  
ATOM   1561  O   TYR B  38      -7.152  28.902  25.523  1.00 46.02           O  
ATOM   1562  CB  TYR B  38      -6.263  30.132  22.790  1.00 37.60           C  
ATOM   1563  CG  TYR B  38      -5.255  30.554  21.758  1.00 36.14           C  
ATOM   1564  CD1 TYR B  38      -4.166  29.745  21.453  1.00 40.42           C  
ATOM   1565  CD2 TYR B  38      -5.417  31.737  21.041  1.00 36.99           C  
ATOM   1566  CE1 TYR B  38      -3.248  30.113  20.466  1.00 47.95           C  
ATOM   1567  CE2 TYR B  38      -4.508  32.116  20.061  1.00 39.49           C  
ATOM   1568  CZ  TYR B  38      -3.428  31.301  19.776  1.00 49.41           C  
ATOM   1569  OH  TYR B  38      -2.521  31.675  18.811  1.00 50.23           O  
ATOM   1570  N   GLU B  39      -8.069  30.928  25.369  1.00 43.67           N  
ATOM   1571  CA  GLU B  39      -9.244  30.500  26.057  1.00 45.63           C  
ATOM   1572  C   GLU B  39     -10.234  30.034  24.995  1.00 50.45           C  
ATOM   1573  O   GLU B  39     -10.331  30.612  23.917  1.00 53.07           O  
ATOM   1574  CB  GLU B  39      -9.764  31.639  26.921  1.00 52.47           C  
ATOM   1575  CG  GLU B  39     -11.086  31.457  27.607  1.00 57.18           C  
ATOM   1576  CD  GLU B  39     -11.559  32.784  28.188  1.00 73.36           C  
ATOM   1577  OE1 GLU B  39     -10.895  33.825  27.912  1.00 69.63           O  
ATOM   1578  OE2 GLU B  39     -12.592  32.788  28.898  1.00 81.66           O  
ATOM   1579  N   ILE B  40     -10.925  28.947  25.290  1.00 53.35           N  
ATOM   1580  CA  ILE B  40     -11.829  28.328  24.345  1.00 58.40           C  
ATOM   1581  C   ILE B  40     -13.096  27.867  25.052  1.00 62.18           C  
ATOM   1582  O   ILE B  40     -13.059  27.510  26.239  1.00 52.67           O  
ATOM   1583  CB  ILE B  40     -11.180  27.118  23.643  1.00 46.79           C  
ATOM   1584  CG1 ILE B  40     -10.528  26.196  24.670  1.00 41.61           C  
ATOM   1585  CG2 ILE B  40     -10.142  27.577  22.642  1.00 47.88           C  
ATOM   1586  CD1 ILE B  40     -10.598  24.729  24.306  1.00 40.58           C  
ATOM   1587  N   LYS B  41     -14.216  27.903  24.334  1.00 47.81           N  
ATOM   1588  CA  LYS B  41     -15.418  27.263  24.819  1.00 57.69           C  
ATOM   1589  C   LYS B  41     -15.571  26.008  24.018  1.00 57.42           C  
ATOM   1590  O   LYS B  41     -15.629  26.056  22.798  1.00 64.33           O  
ATOM   1591  CB  LYS B  41     -16.669  28.134  24.677  1.00 65.75           C  
ATOM   1592  CG  LYS B  41     -17.905  27.481  25.306  1.00 77.36           C  
ATOM   1593  CD  LYS B  41     -19.129  27.499  24.387  1.00 86.25           C  
ATOM   1594  CE  LYS B  41     -20.249  26.613  24.935  1.00 89.81           C  
ATOM   1595  NZ  LYS B  41     -20.386  26.708  26.425  1.00 95.93           N  
ATOM   1596  N   MET B  42     -15.613  24.881  24.705  1.00 56.49           N  
ATOM   1597  CA  MET B  42     -15.784  23.610  24.042  1.00 58.40           C  
ATOM   1598  C   MET B  42     -17.254  23.470  23.676  1.00 55.81           C  
ATOM   1599  O   MET B  42     -18.112  23.869  24.456  1.00 54.69           O  
ATOM   1600  CB  MET B  42     -15.326  22.486  24.957  1.00 55.90           C  
ATOM   1601  CG  MET B  42     -15.159  21.171  24.303  1.00 47.12           C  
ATOM   1602  SD  MET B  42     -15.262  19.938  25.583  1.00 77.26           S  
ATOM   1603  CE  MET B  42     -17.043  19.841  25.762  1.00 65.31           C  
ATOM   1604  N   THR B  43     -17.542  22.934  22.492  1.00 52.91           N  
ATOM   1605  CA  THR B  43     -18.924  22.763  22.055  1.00 53.73           C  
ATOM   1606  C   THR B  43     -19.291  21.282  21.984  1.00 57.83           C  
ATOM   1607  O   THR B  43     -20.460  20.925  22.066  1.00 65.59           O  
ATOM   1608  CB  THR B  43     -19.180  23.436  20.686  1.00 52.71           C  
ATOM   1609  OG1 THR B  43     -18.558  22.682  19.638  1.00 53.35           O  
ATOM   1610  CG2 THR B  43     -18.611  24.840  20.685  1.00 60.70           C  
ATOM   1611  N   LYS B  44     -18.283  20.428  21.855  1.00 55.35           N  
ATOM   1612  CA  LYS B  44     -18.478  18.993  21.736  1.00 58.30           C  
ATOM   1613  C   LYS B  44     -17.167  18.321  22.072  1.00 60.77           C  
ATOM   1614  O   LYS B  44     -16.109  18.938  21.946  1.00 62.09           O  
ATOM   1615  CB  LYS B  44     -18.917  18.596  20.318  1.00 69.69           C  
ATOM   1616  CG  LYS B  44     -20.380  18.872  19.985  1.00 86.77           C  
ATOM   1617  CD  LYS B  44     -21.050  17.739  19.223  1.00 94.79           C  
ATOM   1618  CE  LYS B  44     -22.371  18.215  18.607  1.00101.00           C  
ATOM   1619  NZ  LYS B  44     -22.893  17.391  17.469  1.00103.73           N  
ATOM   1620  N   MET B  45     -17.221  17.059  22.486  1.00 62.61           N  
ATOM   1621  CA  MET B  45     -15.995  16.288  22.685  1.00 59.19           C  
ATOM   1622  C   MET B  45     -16.133  14.892  22.072  1.00 63.00           C  
ATOM   1623  O   MET B  45     -17.162  14.252  22.224  1.00 66.72           O  
ATOM   1624  CB  MET B  45     -15.656  16.200  24.175  1.00 53.52           C  
ATOM   1625  CG  MET B  45     -14.532  15.235  24.513  1.00 50.20           C  
ATOM   1626  SD  MET B  45     -14.182  15.199  26.287  1.00 69.54           S  
ATOM   1627  CE  MET B  45     -12.859  16.387  26.405  1.00 50.09           C  
ATOM   1628  N   TYR B  46     -15.102  14.422  21.379  1.00 52.47           N  
ATOM   1629  CA  TYR B  46     -15.177  13.128  20.704  1.00 50.04           C  
ATOM   1630  C   TYR B  46     -14.240  12.111  21.332  1.00 53.03           C  
ATOM   1631  O   TYR B  46     -14.601  10.944  21.516  1.00 59.15           O  
ATOM   1632  CB  TYR B  46     -14.862  13.287  19.212  1.00 46.57           C  
ATOM   1633  CG  TYR B  46     -15.882  14.143  18.500  1.00 48.73           C  
ATOM   1634  CD1 TYR B  46     -17.206  13.724  18.400  1.00 48.29           C  
ATOM   1635  CD2 TYR B  46     -15.535  15.373  17.941  1.00 43.37           C  
ATOM   1636  CE1 TYR B  46     -18.160  14.502  17.764  1.00 48.66           C  
ATOM   1637  CE2 TYR B  46     -16.489  16.161  17.292  1.00 43.80           C  
ATOM   1638  CZ  TYR B  46     -17.803  15.711  17.208  1.00 51.54           C  
ATOM   1639  OH  TYR B  46     -18.778  16.455  16.577  1.00 55.21           O  
ATOM   1640  N   LYS B  47     -13.034  12.564  21.658  1.00 47.46           N  
ATOM   1641  CA  LYS B  47     -12.094  11.750  22.414  1.00 49.76           C  
ATOM   1642  C   LYS B  47     -11.667  12.480  23.704  1.00 55.37           C  
ATOM   1643  O   LYS B  47     -11.454  13.692  23.715  1.00 50.43           O  
ATOM   1644  CB  LYS B  47     -10.885  11.399  21.540  1.00 46.52           C  
ATOM   1645  CG  LYS B  47      -9.982  10.329  22.121  1.00 48.45           C  
ATOM   1646  CD  LYS B  47      -8.917   9.831  21.130  1.00 47.24           C  
ATOM   1647  CE  LYS B  47      -8.029   8.814  21.816  1.00 49.73           C  
ATOM   1648  NZ  LYS B  47      -6.747   8.576  21.157  1.00 48.73           N  
ATOM   1649  N   GLY B  48     -11.580  11.744  24.803  1.00 63.73           N  
ATOM   1650  CA  GLY B  48     -10.978  12.284  26.009  1.00 57.68           C  
ATOM   1651  C   GLY B  48     -11.899  12.463  27.193  1.00 63.64           C  
ATOM   1652  O   GLY B  48     -11.918  13.515  27.815  1.00 72.41           O  
ATOM   1653  N   PHE B  49     -12.647  11.426  27.528  1.00 67.81           N  
ATOM   1654  CA  PHE B  49     -13.588  11.503  28.625  1.00 62.56           C  
ATOM   1655  C   PHE B  49     -12.931  10.995  29.895  1.00 78.89           C  
ATOM   1656  O   PHE B  49     -13.540  10.975  30.968  1.00 84.76           O  
ATOM   1657  CB  PHE B  49     -14.834  10.716  28.282  1.00 64.90           C  
ATOM   1658  CG  PHE B  49     -15.361  11.019  26.920  1.00 67.41           C  
ATOM   1659  CD1 PHE B  49     -16.288  12.038  26.737  1.00 63.72           C  
ATOM   1660  CD2 PHE B  49     -14.902  10.307  25.806  1.00 67.54           C  
ATOM   1661  CE1 PHE B  49     -16.769  12.332  25.471  1.00 65.87           C  
ATOM   1662  CE2 PHE B  49     -15.367  10.594  24.546  1.00 63.31           C  
ATOM   1663  CZ  PHE B  49     -16.306  11.609  24.374  1.00 67.52           C  
ATOM   1664  N   GLN B  50     -11.671  10.594  29.766  1.00 79.99           N  
ATOM   1665  CA  GLN B  50     -10.840  10.317  30.926  1.00 88.55           C  
ATOM   1666  C   GLN B  50      -9.946  11.526  31.201  1.00 98.61           C  
ATOM   1667  O   GLN B  50      -8.738  11.507  30.951  1.00 90.40           O  
ATOM   1668  CB  GLN B  50     -10.023   9.050  30.714  1.00 82.53           C  
ATOM   1669  CG  GLN B  50     -10.878   7.814  30.401  1.00 81.19           C  
ATOM   1670  CD  GLN B  50     -11.863   7.460  31.504  1.00 82.20           C  
ATOM   1671  OE1 GLN B  50     -12.904   8.105  31.668  1.00 78.69           O  
ATOM   1672  NE2 GLN B  50     -11.538   6.421  32.267  1.00 89.24           N  
ATOM   1673  N   ALA B  51     -10.598  12.585  31.684  1.00114.21           N  
ATOM   1674  CA  ALA B  51      -9.981  13.813  32.180  1.00115.32           C  
ATOM   1675  C   ALA B  51     -11.001  14.509  33.081  1.00132.03           C  
ATOM   1676  O   ALA B  51     -12.206  14.288  32.927  1.00139.22           O  
ATOM   1677  CB  ALA B  51      -9.562  14.717  31.052  1.00 99.31           C  
ATOM   1678  N   LEU B  52     -10.499  15.342  33.999  1.00135.13           N  
ATOM   1679  CA  LEU B  52     -11.259  16.038  35.060  1.00130.21           C  
ATOM   1680  C   LEU B  52     -12.560  15.355  35.484  1.00129.24           C  
ATOM   1681  O   LEU B  52     -12.903  15.337  36.671  1.00131.54           O  
ATOM   1682  CB  LEU B  52     -11.555  17.500  34.653  1.00125.87           C  
ATOM   1683  CG  LEU B  52     -12.703  18.062  33.781  1.00126.95           C  
ATOM   1684  CD1 LEU B  52     -13.180  17.170  32.606  1.00136.95           C  
ATOM   1685  CD2 LEU B  52     -13.878  18.535  34.658  1.00129.10           C  
ATOM   1686  N   ASP B  57     -14.938  19.805  31.805  1.00 90.51           N  
ATOM   1687  CA  ASP B  57     -14.778  20.649  30.633  1.00 87.58           C  
ATOM   1688  C   ASP B  57     -13.439  21.411  30.710  1.00 91.08           C  
ATOM   1689  O   ASP B  57     -12.951  21.714  31.800  1.00 90.83           O  
ATOM   1690  CB  ASP B  57     -15.965  21.611  30.521  1.00 96.39           C  
ATOM   1691  CG  ASP B  57     -16.020  22.337  29.185  1.00108.91           C  
ATOM   1692  OD1 ASP B  57     -14.966  22.500  28.533  1.00118.41           O  
ATOM   1693  OD2 ASP B  57     -17.132  22.734  28.773  1.00110.02           O  
ATOM   1694  N   ILE B  58     -12.855  21.700  29.543  1.00 92.46           N  
ATOM   1695  CA  ILE B  58     -11.564  22.397  29.430  1.00 87.83           C  
ATOM   1696  C   ILE B  58     -11.744  23.811  28.858  1.00 73.35           C  
ATOM   1697  O   ILE B  58     -12.562  24.038  27.951  1.00 63.25           O  
ATOM   1698  CB  ILE B  58     -10.555  21.597  28.542  1.00 76.85           C  
ATOM   1699  CG1 ILE B  58      -9.138  22.186  28.633  1.00 83.87           C  
ATOM   1700  CG2 ILE B  58     -11.031  21.520  27.104  1.00 65.21           C  
ATOM   1701  CD1 ILE B  58      -8.536  22.183  30.054  1.00 89.38           C  
ATOM   1702  N   ARG B  59     -10.980  24.761  29.398  1.00 65.20           N  
ATOM   1703  CA  ARG B  59     -11.172  26.173  29.071  1.00 61.98           C  
ATOM   1704  C   ARG B  59     -10.014  26.799  28.274  1.00 51.35           C  
ATOM   1705  O   ARG B  59     -10.088  27.948  27.847  1.00 52.03           O  
ATOM   1706  CB  ARG B  59     -11.398  26.973  30.366  1.00 59.70           C  
ATOM   1707  N   PHE B  60      -8.940  26.051  28.083  1.00 45.68           N  
ATOM   1708  CA  PHE B  60      -7.753  26.614  27.475  1.00 50.32           C  
ATOM   1709  C   PHE B  60      -6.994  25.606  26.642  1.00 53.46           C  
ATOM   1710  O   PHE B  60      -7.022  24.404  26.924  1.00 54.37           O  
ATOM   1711  CB  PHE B  60      -6.814  27.178  28.544  1.00 55.60           C  
ATOM   1712  CG  PHE B  60      -7.399  28.308  29.338  1.00 59.97           C  
ATOM   1713  CD1 PHE B  60      -7.322  29.617  28.873  1.00 62.66           C  
ATOM   1714  CD2 PHE B  60      -8.011  28.072  30.559  1.00 52.74           C  
ATOM   1715  CE1 PHE B  60      -7.854  30.667  29.609  1.00 60.18           C  
ATOM   1716  CE2 PHE B  60      -8.545  29.119  31.288  1.00 54.03           C  
ATOM   1717  CZ  PHE B  60      -8.465  30.414  30.818  1.00 53.98           C  
ATOM   1718  N   VAL B  61      -6.307  26.125  25.626  1.00 44.94           N  
ATOM   1719  CA  VAL B  61      -5.362  25.362  24.815  1.00 41.67           C  
ATOM   1720  C   VAL B  61      -4.000  26.021  24.892  1.00 38.88           C  
ATOM   1721  O   VAL B  61      -3.894  27.231  24.767  1.00 40.17           O  
ATOM   1722  CB  VAL B  61      -5.782  25.310  23.343  1.00 44.98           C  
ATOM   1723  CG1 VAL B  61      -4.938  24.297  22.588  1.00 42.14           C  
ATOM   1724  CG2 VAL B  61      -7.251  24.977  23.225  1.00 51.95           C  
ATOM   1725  N   TYR B  62      -2.949  25.244  25.080  1.00 42.45           N  
ATOM   1726  CA  TYR B  62      -1.622  25.838  25.127  1.00 43.62           C  
ATOM   1727  C   TYR B  62      -0.786  25.483  23.893  1.00 41.47           C  
ATOM   1728  O   TYR B  62      -1.020  24.453  23.249  1.00 32.74           O  
ATOM   1729  CB  TYR B  62      -0.890  25.400  26.387  1.00 37.60           C  
ATOM   1730  CG  TYR B  62      -1.534  25.832  27.677  1.00 40.11           C  
ATOM   1731  CD1 TYR B  62      -0.919  26.767  28.503  1.00 41.85           C  
ATOM   1732  CD2 TYR B  62      -2.747  25.286  28.090  1.00 41.51           C  
ATOM   1733  CE1 TYR B  62      -1.504  27.151  29.699  1.00 44.58           C  
ATOM   1734  CE2 TYR B  62      -3.333  25.659  29.272  1.00 43.85           C  
ATOM   1735  CZ  TYR B  62      -2.711  26.588  30.080  1.00 48.49           C  
ATOM   1736  OH  TYR B  62      -3.299  26.953  31.275  1.00 50.03           O  
ATOM   1737  N   THR B  63       0.193  26.340  23.601  1.00 33.49           N  
ATOM   1738  CA  THR B  63       1.059  26.219  22.446  1.00 32.09           C  
ATOM   1739  C   THR B  63       2.282  27.105  22.618  1.00 32.83           C  
ATOM   1740  O   THR B  63       2.209  28.123  23.295  1.00 43.24           O  
ATOM   1741  CB  THR B  63       0.315  26.614  21.150  1.00 40.85           C  
ATOM   1742  OG1 THR B  63       1.243  26.710  20.068  1.00 45.90           O  
ATOM   1743  CG2 THR B  63      -0.336  27.942  21.312  1.00 31.57           C  
ATOM   1744  N   PRO B  64       3.414  26.718  22.010  1.00 33.65           N  
ATOM   1745  CA  PRO B  64       4.660  27.509  21.978  1.00 35.18           C  
ATOM   1746  C   PRO B  64       4.431  28.986  21.667  1.00 41.44           C  
ATOM   1747  O   PRO B  64       3.587  29.308  20.833  1.00 34.55           O  
ATOM   1748  CB  PRO B  64       5.459  26.854  20.855  1.00 32.38           C  
ATOM   1749  CG  PRO B  64       4.996  25.411  20.866  1.00 32.46           C  
ATOM   1750  CD  PRO B  64       3.592  25.377  21.417  1.00 31.57           C  
ATOM   1751  N   ALA B  65       5.174  29.867  22.330  1.00 47.25           N  
ATOM   1752  CA  ALA B  65       4.901  31.295  22.260  1.00 49.87           C  
ATOM   1753  C   ALA B  65       5.430  31.916  20.971  1.00 48.43           C  
ATOM   1754  O   ALA B  65       5.074  33.031  20.614  1.00 43.38           O  
ATOM   1755  CB  ALA B  65       5.489  31.999  23.462  1.00 45.67           C  
ATOM   1756  N   MET B  66       6.279  31.183  20.273  1.00 46.85           N  
ATOM   1757  CA  MET B  66       6.860  31.683  19.043  1.00 44.80           C  
ATOM   1758  C   MET B  66       6.484  30.817  17.853  1.00 38.37           C  
ATOM   1759  O   MET B  66       6.359  29.600  17.978  1.00 36.71           O  
ATOM   1760  CB  MET B  66       8.377  31.762  19.176  1.00 44.94           C  
ATOM   1761  CG  MET B  66       8.832  32.992  19.925  1.00 51.23           C  
ATOM   1762  SD  MET B  66      10.263  32.658  20.953  1.00 59.06           S  
ATOM   1763  CE  MET B  66       9.529  31.629  22.227  1.00 95.09           C  
ATOM   1764  N   GLU B  67       6.299  31.457  16.704  1.00 37.39           N  
ATOM   1765  CA  GLU B  67       5.950  30.756  15.479  1.00 41.11           C  
ATOM   1766  C   GLU B  67       7.088  29.838  15.083  1.00 45.18           C  
ATOM   1767  O   GLU B  67       6.881  28.694  14.674  1.00 44.52           O  
ATOM   1768  CB  GLU B  67       5.652  31.768  14.389  1.00 36.59           C  
ATOM   1769  CG  GLU B  67       5.477  31.230  13.006  1.00 49.18           C  
ATOM   1770  CD  GLU B  67       5.480  32.346  11.972  1.00 63.11           C  
ATOM   1771  OE1 GLU B  67       6.525  32.550  11.320  1.00 69.33           O  
ATOM   1772  OE2 GLU B  67       4.447  33.034  11.822  1.00 70.58           O  
ATOM   1773  N   SER B  68       8.296  30.358  15.265  1.00 46.84           N  
ATOM   1774  CA  SER B  68       9.533  29.707  14.872  1.00 45.50           C  
ATOM   1775  C   SER B  68       9.683  28.334  15.499  1.00 49.28           C  
ATOM   1776  O   SER B  68      10.363  27.423  14.980  1.00 47.00           O  
ATOM   1777  CB  SER B  68      10.704  30.602  15.263  1.00 45.13           C  
ATOM   1778  OG  SER B  68      11.796  29.821  15.687  1.00 56.51           O  
ATOM   1779  N   VAL B  69       9.029  28.182  16.631  1.00 33.49           N  
ATOM   1780  CA  VAL B  69       9.290  27.024  17.432  1.00 33.59           C  
ATOM   1781  C   VAL B  69       7.981  26.256  17.560  1.00 38.06           C  
ATOM   1782  O   VAL B  69       7.747  25.527  18.517  1.00 39.45           O  
ATOM   1783  CB  VAL B  69       9.935  27.439  18.786  1.00 43.18           C  
ATOM   1784  CG1 VAL B  69       8.907  28.007  19.764  1.00 50.07           C  
ATOM   1785  CG2 VAL B  69      10.721  26.287  19.379  1.00 49.50           C  
ATOM   1786  N   CYS B  70       7.155  26.418  16.528  1.00 40.92           N  
ATOM   1787  CA  CYS B  70       5.968  25.592  16.270  1.00 39.16           C  
ATOM   1788  C   CYS B  70       4.772  26.036  17.095  1.00 45.66           C  
ATOM   1789  O   CYS B  70       3.914  25.232  17.460  1.00 49.72           O  
ATOM   1790  CB  CYS B  70       6.252  24.100  16.513  1.00 29.89           C  
ATOM   1791  SG  CYS B  70       7.615  23.410  15.551  1.00 55.02           S  
ATOM   1792  N   GLY B  71       4.707  27.330  17.366  1.00 42.95           N  
ATOM   1793  CA  GLY B  71       3.543  27.880  18.011  1.00 29.77           C  
ATOM   1794  C   GLY B  71       2.370  28.023  17.066  1.00 37.82           C  
ATOM   1795  O   GLY B  71       2.491  28.593  15.980  1.00 45.98           O  
ATOM   1796  N   TYR B  72       1.220  27.510  17.487  1.00 33.96           N  
ATOM   1797  CA  TYR B  72      -0.029  27.745  16.768  1.00 32.39           C  
ATOM   1798  C   TYR B  72      -0.559  29.152  16.970  1.00 41.09           C  
ATOM   1799  O   TYR B  72      -0.930  29.537  18.085  1.00 51.08           O  
ATOM   1800  CB  TYR B  72      -1.096  26.750  17.202  1.00 32.05           C  
ATOM   1801  CG  TYR B  72      -2.460  27.018  16.614  1.00 38.61           C  
ATOM   1802  CD1 TYR B  72      -2.785  26.552  15.343  1.00 38.89           C  
ATOM   1803  CD2 TYR B  72      -3.438  27.717  17.335  1.00 35.30           C  
ATOM   1804  CE1 TYR B  72      -4.037  26.778  14.793  1.00 35.26           C  
ATOM   1805  CE2 TYR B  72      -4.698  27.944  16.795  1.00 35.14           C  
ATOM   1806  CZ  TYR B  72      -4.988  27.471  15.519  1.00 43.18           C  
ATOM   1807  OH  TYR B  72      -6.227  27.680  14.957  1.00 48.54           O  
ATOM   1808  N   PHE B  73      -0.618  29.905  15.879  1.00 36.03           N  
ATOM   1809  CA  PHE B  73      -1.260  31.207  15.877  1.00 35.50           C  
ATOM   1810  C   PHE B  73      -2.588  31.113  15.153  1.00 31.75           C  
ATOM   1811  O   PHE B  73      -2.663  30.624  14.032  1.00 38.02           O  
ATOM   1812  CB  PHE B  73      -0.353  32.272  15.247  1.00 35.50           C  
ATOM   1813  CG  PHE B  73       0.781  32.679  16.144  1.00 47.31           C  
ATOM   1814  CD1 PHE B  73       1.852  31.815  16.374  1.00 49.65           C  
ATOM   1815  CD2 PHE B  73       0.760  33.900  16.802  1.00 60.95           C  
ATOM   1816  CE1 PHE B  73       2.898  32.176  17.223  1.00 47.03           C  
ATOM   1817  CE2 PHE B  73       1.802  34.271  17.653  1.00 55.35           C  
ATOM   1818  CZ  PHE B  73       2.872  33.406  17.863  1.00 46.58           C  
ATOM   1819  N   HIS B  74      -3.633  31.588  15.816  1.00 34.02           N  
ATOM   1820  CA  HIS B  74      -5.011  31.441  15.347  1.00 39.06           C  
ATOM   1821  C   HIS B  74      -5.396  32.581  14.414  1.00 40.18           C  
ATOM   1822  O   HIS B  74      -5.498  33.719  14.847  1.00 45.51           O  
ATOM   1823  CB  HIS B  74      -5.940  31.395  16.552  1.00 39.61           C  
ATOM   1824  CG  HIS B  74      -7.362  31.088  16.224  1.00 40.28           C  
ATOM   1825  ND1 HIS B  74      -7.767  29.861  15.748  1.00 40.04           N  
ATOM   1826  CD2 HIS B  74      -8.483  31.837  16.342  1.00 47.13           C  
ATOM   1827  CE1 HIS B  74      -9.076  29.870  15.575  1.00 42.39           C  
ATOM   1828  NE2 HIS B  74      -9.535  31.059  15.922  1.00 49.84           N  
ATOM   1829  N   ARG B  75      -5.606  32.284  13.138  1.00 47.96           N  
ATOM   1830  CA  ARG B  75      -5.783  33.346  12.150  1.00 62.05           C  
ATOM   1831  C   ARG B  75      -7.224  33.866  12.110  1.00 61.31           C  
ATOM   1832  O   ARG B  75      -7.462  35.080  12.019  1.00 63.88           O  
ATOM   1833  CB  ARG B  75      -5.350  32.862  10.760  1.00 64.03           C  
ATOM   1834  N   SER B  76      -8.178  32.948  12.186  1.00 56.96           N  
ATOM   1835  CA  SER B  76      -9.595  33.304  12.169  1.00 64.18           C  
ATOM   1836  C   SER B  76      -9.997  34.232  13.330  1.00 76.87           C  
ATOM   1837  O   SER B  76      -9.475  34.107  14.444  1.00 82.17           O  
ATOM   1838  CB  SER B  76     -10.442  32.029  12.197  1.00 50.13           C  
ATOM   1839  OG  SER B  76     -11.729  32.282  12.728  1.00 47.69           O  
ATOM   1840  N   HIS B  77     -10.913  35.167  13.070  1.00 77.27           N  
ATOM   1841  CA  HIS B  77     -11.439  36.014  14.142  1.00 83.10           C  
ATOM   1842  C   HIS B  77     -12.935  35.751  14.304  1.00 81.95           C  
ATOM   1843  O   HIS B  77     -13.699  36.556  14.852  1.00 61.72           O  
ATOM   1844  CB  HIS B  77     -11.107  37.489  13.895  1.00 95.71           C  
ATOM   1845  CG  HIS B  77      -9.654  37.801  14.102  1.00110.42           C  
ATOM   1846  ND1 HIS B  77      -8.960  37.394  15.225  1.00113.46           N  
ATOM   1847  CD2 HIS B  77      -8.755  38.451  13.324  1.00114.31           C  
ATOM   1848  CE1 HIS B  77      -7.702  37.786  15.133  1.00111.05           C  
ATOM   1849  NE2 HIS B  77      -7.551  38.431  13.989  1.00115.16           N  
ATOM   1850  N   ASN B  78     -13.324  34.596  13.774  1.00100.16           N  
ATOM   1851  CA  ASN B  78     -14.241  33.701  14.465  1.00113.60           C  
ATOM   1852  C   ASN B  78     -15.666  34.340  14.638  1.00 73.17           C  
ATOM   1853  O   ASN B  78     -16.339  34.455  13.607  1.00 58.68           O  
ATOM   1854  CB  ASN B  78     -13.500  33.264  15.743  1.00118.41           C  
ATOM   1855  CG  ASN B  78     -13.799  31.838  16.144  1.00121.22           C  
ATOM   1856  OD1 ASN B  78     -14.916  31.350  15.973  1.00131.48           O  
ATOM   1857  ND2 ASN B  78     -12.794  31.160  16.687  1.00110.28           N  
ATOM   1858  N   ARG B  79     -16.208  34.720  15.813  1.00 80.76           N  
ATOM   1859  CA  ARG B  79     -15.900  34.294  17.181  1.00 73.54           C  
ATOM   1860  C   ARG B  79     -16.757  33.067  17.449  1.00 69.58           C  
ATOM   1861  O   ARG B  79     -16.624  32.390  18.462  1.00 66.48           O  
ATOM   1862  CB  ARG B  79     -16.172  35.407  18.191  1.00 77.11           C  
ATOM   1863  CG  ARG B  79     -15.411  35.265  19.507  1.00 81.20           C  
ATOM   1864  CD  ARG B  79     -14.046  35.961  19.466  1.00 89.80           C  
ATOM   1865  NE  ARG B  79     -14.164  37.412  19.319  1.00104.18           N  
ATOM   1866  CZ  ARG B  79     -14.356  38.266  20.326  1.00115.01           C  
ATOM   1867  NH1 ARG B  79     -14.457  39.570  20.088  1.00116.31           N  
ATOM   1868  NH2 ARG B  79     -14.451  37.823  21.572  1.00118.64           N  
ATOM   1869  N   SER B  80     -17.618  32.774  16.483  1.00 69.97           N  
ATOM   1870  CA  SER B  80     -18.613  31.717  16.589  1.00 67.30           C  
ATOM   1871  C   SER B  80     -18.263  30.466  15.763  1.00 64.48           C  
ATOM   1872  O   SER B  80     -18.961  29.450  15.807  1.00 59.51           O  
ATOM   1873  CB  SER B  80     -19.954  32.276  16.142  1.00 68.42           C  
ATOM   1874  OG  SER B  80     -19.753  33.112  15.014  1.00 76.46           O  
ATOM   1875  N   GLU B  81     -17.183  30.552  14.998  1.00 68.75           N  
ATOM   1876  CA  GLU B  81     -16.773  29.451  14.139  1.00 63.31           C  
ATOM   1877  C   GLU B  81     -16.223  28.318  14.984  1.00 53.28           C  
ATOM   1878  O   GLU B  81     -15.261  28.501  15.725  1.00 44.71           O  
ATOM   1879  CB  GLU B  81     -15.724  29.921  13.131  1.00 64.50           C  
ATOM   1880  CG  GLU B  81     -15.495  28.961  11.990  1.00 68.56           C  
ATOM   1881  CD  GLU B  81     -14.476  29.468  10.986  1.00 69.16           C  
ATOM   1882  OE1 GLU B  81     -13.807  30.489  11.265  1.00 59.77           O  
ATOM   1883  OE2 GLU B  81     -14.347  28.833   9.917  1.00 71.74           O  
ATOM   1884  N   GLU B  82     -16.843  27.149  14.888  1.00 51.02           N  
ATOM   1885  CA  GLU B  82     -16.324  25.987  15.589  1.00 46.39           C  
ATOM   1886  C   GLU B  82     -15.110  25.392  14.861  1.00 47.86           C  
ATOM   1887  O   GLU B  82     -15.078  25.278  13.632  1.00 43.41           O  
ATOM   1888  CB  GLU B  82     -17.410  24.931  15.766  1.00 44.05           C  
ATOM   1889  CG  GLU B  82     -18.668  25.454  16.441  1.00 57.31           C  
ATOM   1890  CD  GLU B  82     -19.627  24.343  16.834  1.00 71.68           C  
ATOM   1891  OE1 GLU B  82     -19.213  23.162  16.837  1.00 74.76           O  
ATOM   1892  OE2 GLU B  82     -20.801  24.647  17.131  1.00 81.66           O  
ATOM   1893  N   PHE B  83     -14.106  25.039  15.652  1.00 46.73           N  
ATOM   1894  CA  PHE B  83     -12.889  24.427  15.164  1.00 42.35           C  
ATOM   1895  C   PHE B  83     -12.737  23.034  15.766  1.00 46.78           C  
ATOM   1896  O   PHE B  83     -13.096  22.798  16.923  1.00 47.28           O  
ATOM   1897  CB  PHE B  83     -11.673  25.282  15.523  1.00 37.60           C  
ATOM   1898  CG  PHE B  83     -11.537  26.515  14.705  1.00 37.09           C  
ATOM   1899  CD1 PHE B  83     -12.317  27.618  14.958  1.00 49.20           C  
ATOM   1900  CD2 PHE B  83     -10.622  26.573  13.671  1.00 33.73           C  
ATOM   1901  CE1 PHE B  83     -12.190  28.759  14.188  1.00 47.34           C  
ATOM   1902  CE2 PHE B  83     -10.489  27.695  12.911  1.00 34.58           C  
ATOM   1903  CZ  PHE B  83     -11.272  28.790  13.164  1.00 39.43           C  
ATOM   1904  N   LEU B  84     -12.217  22.105  14.976  1.00 43.88           N  
ATOM   1905  CA  LEU B  84     -11.830  20.831  15.531  1.00 43.56           C  
ATOM   1906  C   LEU B  84     -10.381  20.927  15.994  1.00 49.72           C  
ATOM   1907  O   LEU B  84      -9.494  21.299  15.220  1.00 51.71           O  
ATOM   1908  CB  LEU B  84     -11.998  19.703  14.518  1.00 38.85           C  
ATOM   1909  CG  LEU B  84     -11.619  18.385  15.188  1.00 39.28           C  
ATOM   1910  CD1 LEU B  84     -12.675  17.349  14.956  1.00 38.17           C  
ATOM   1911  CD2 LEU B  84     -10.245  17.897  14.751  1.00 35.07           C  
ATOM   1912  N   ILE B  85     -10.155  20.600  17.262  1.00 46.42           N  
ATOM   1913  CA  ILE B  85      -8.810  20.566  17.839  1.00 41.20           C  
ATOM   1914  C   ILE B  85      -8.439  19.135  18.206  1.00 36.46           C  
ATOM   1915  O   ILE B  85      -9.230  18.432  18.853  1.00 36.82           O  
ATOM   1916  CB  ILE B  85      -8.701  21.429  19.111  1.00 42.95           C  
ATOM   1917  CG1 ILE B  85      -9.403  22.768  18.919  1.00 32.79           C  
ATOM   1918  CG2 ILE B  85      -7.245  21.585  19.537  1.00 40.66           C  
ATOM   1919  CD1 ILE B  85      -9.225  23.669  20.043  1.00 33.65           C  
ATOM   1920  N   ALA B  86      -7.256  18.702  17.779  1.00 34.55           N  
ATOM   1921  CA  ALA B  86      -6.714  17.402  18.161  1.00 34.54           C  
ATOM   1922  C   ALA B  86      -5.382  17.621  18.862  1.00 39.45           C  
ATOM   1923  O   ALA B  86      -4.384  17.939  18.210  1.00 43.28           O  
ATOM   1924  CB  ALA B  86      -6.541  16.502  16.947  1.00 32.00           C  
ATOM   1925  N   GLY B  87      -5.354  17.465  20.183  1.00 34.59           N  
ATOM   1926  CA  GLY B  87      -4.123  17.734  20.906  1.00 41.18           C  
ATOM   1927  C   GLY B  87      -3.751  16.793  22.026  1.00 45.90           C  
ATOM   1928  O   GLY B  87      -4.579  15.995  22.477  1.00 55.64           O  
ATOM   1929  N   LYS B  88      -2.500  16.896  22.483  1.00 43.71           N  
ATOM   1930  CA  LYS B  88      -1.990  16.026  23.542  1.00 45.03           C  
ATOM   1931  C   LYS B  88      -2.179  16.665  24.915  1.00 46.54           C  
ATOM   1932  O   LYS B  88      -2.272  17.888  25.037  1.00 45.17           O  
ATOM   1933  CB  LYS B  88      -0.520  15.679  23.301  1.00 43.51           C  
ATOM   1934  CG  LYS B  88      -0.330  14.344  22.562  1.00 63.86           C  
ATOM   1935  CD  LYS B  88       0.865  14.396  21.610  1.00 76.61           C  
ATOM   1936  CE  LYS B  88       0.759  13.362  20.486  1.00 82.20           C  
ATOM   1937  NZ  LYS B  88       1.267  13.902  19.173  1.00 71.22           N  
ATOM   1938  N   LEU B  89      -2.265  15.824  25.939  1.00 48.10           N  
ATOM   1939  CA  LEU B  89      -2.479  16.293  27.303  1.00 49.10           C  
ATOM   1940  C   LEU B  89      -1.199  16.265  28.113  1.00 50.28           C  
ATOM   1941  O   LEU B  89      -0.805  15.218  28.607  1.00 62.45           O  
ATOM   1942  CB  LEU B  89      -3.534  15.442  27.988  1.00 58.07           C  
ATOM   1943  CG  LEU B  89      -4.537  16.230  28.812  1.00 63.15           C  
ATOM   1944  CD1 LEU B  89      -5.208  17.249  27.915  1.00 59.16           C  
ATOM   1945  CD2 LEU B  89      -5.564  15.282  29.422  1.00 61.39           C  
ATOM   1946  N   GLN B  90      -0.547  17.416  28.230  1.00 52.36           N  
ATOM   1947  CA  GLN B  90       0.662  17.553  29.031  1.00 61.58           C  
ATOM   1948  C   GLN B  90       0.298  18.099  30.395  1.00 62.67           C  
ATOM   1949  O   GLN B  90      -0.187  19.231  30.496  1.00 56.13           O  
ATOM   1950  CB  GLN B  90       1.671  18.489  28.364  1.00 75.94           C  
ATOM   1951  CG  GLN B  90       2.234  18.009  27.029  1.00 94.06           C  
ATOM   1952  CD  GLN B  90       3.589  18.638  26.713  1.00106.13           C  
ATOM   1953  OE1 GLN B  90       4.298  19.101  27.618  1.00118.33           O  
ATOM   1954  NE2 GLN B  90       3.949  18.669  25.427  1.00 92.55           N  
ATOM   1955  N   ASP B  91       0.523  17.294  31.434  1.00 69.33           N  
ATOM   1956  CA  ASP B  91       0.322  17.719  32.819  1.00 72.33           C  
ATOM   1957  C   ASP B  91      -1.063  18.324  33.014  1.00 63.77           C  
ATOM   1958  O   ASP B  91      -1.229  19.329  33.720  1.00 60.65           O  
ATOM   1959  CB  ASP B  91       1.403  18.723  33.240  1.00 85.57           C  
ATOM   1960  CG  ASP B  91       2.790  18.093  33.336  1.00100.84           C  
ATOM   1961  OD1 ASP B  91       2.908  17.016  33.956  1.00111.19           O  
ATOM   1962  OD2 ASP B  91       3.759  18.665  32.786  1.00100.70           O  
ATOM   1963  N   GLY B  92      -2.048  17.721  32.352  1.00 58.00           N  
ATOM   1964  CA  GLY B  92      -3.436  18.100  32.535  1.00 54.28           C  
ATOM   1965  C   GLY B  92      -3.874  19.306  31.742  1.00 54.82           C  
ATOM   1966  O   GLY B  92      -4.955  19.845  31.980  1.00 51.42           O  
ATOM   1967  N   LEU B  93      -3.038  19.719  30.793  1.00 56.23           N  
ATOM   1968  CA  LEU B  93      -3.344  20.854  29.925  1.00 55.68           C  
ATOM   1969  C   LEU B  93      -3.331  20.481  28.449  1.00 52.67           C  
ATOM   1970  O   LEU B  93      -2.397  19.844  27.965  1.00 44.16           O  
ATOM   1971  CB  LEU B  93      -2.349  21.983  30.151  1.00 51.36           C  
ATOM   1972  CG  LEU B  93      -2.201  22.408  31.598  1.00 52.01           C  
ATOM   1973  CD1 LEU B  93      -1.046  23.388  31.704  1.00 47.79           C  
ATOM   1974  CD2 LEU B  93      -3.516  23.003  32.093  1.00 46.44           C  
ATOM   1975  N   LEU B  94      -4.352  20.925  27.730  1.00 48.73           N  
ATOM   1976  CA  LEU B  94      -4.443  20.648  26.309  1.00 44.51           C  
ATOM   1977  C   LEU B  94      -3.353  21.386  25.521  1.00 40.34           C  
ATOM   1978  O   LEU B  94      -3.259  22.609  25.565  1.00 44.05           O  
ATOM   1979  CB  LEU B  94      -5.826  21.023  25.790  1.00 47.82           C  
ATOM   1980  CG  LEU B  94      -6.021  20.606  24.337  1.00 43.46           C  
ATOM   1981  CD1 LEU B  94      -5.737  19.124  24.219  1.00 39.03           C  
ATOM   1982  CD2 LEU B  94      -7.415  20.932  23.872  1.00 41.01           C  
ATOM   1983  N   HIS B  95      -2.524  20.631  24.806  1.00 40.98           N  
ATOM   1984  CA  HIS B  95      -1.417  21.222  24.064  1.00 36.39           C  
ATOM   1985  C   HIS B  95      -1.508  20.962  22.578  1.00 36.20           C  
ATOM   1986  O   HIS B  95      -1.784  19.836  22.140  1.00 34.59           O  
ATOM   1987  CB  HIS B  95      -0.077  20.693  24.569  1.00 38.37           C  
ATOM   1988  CG  HIS B  95       0.549  21.554  25.613  1.00 54.24           C  
ATOM   1989  ND1 HIS B  95       0.240  21.443  26.951  1.00 57.62           N  
ATOM   1990  CD2 HIS B  95       1.452  22.555  25.513  1.00 57.93           C  
ATOM   1991  CE1 HIS B  95       0.936  22.336  27.633  1.00 58.21           C  
ATOM   1992  NE2 HIS B  95       1.678  23.022  26.785  1.00 59.35           N  
ATOM   1993  N   ILE B  96      -1.249  22.005  21.801  1.00 34.41           N  
ATOM   1994  CA  ILE B  96      -1.116  21.842  20.368  1.00 33.55           C  
ATOM   1995  C   ILE B  96       0.083  22.602  19.854  1.00 38.61           C  
ATOM   1996  O   ILE B  96       0.646  23.471  20.532  1.00 35.60           O  
ATOM   1997  CB  ILE B  96      -2.360  22.313  19.603  1.00 32.10           C  
ATOM   1998  CG1 ILE B  96      -2.545  23.818  19.741  1.00 33.07           C  
ATOM   1999  CG2 ILE B  96      -3.607  21.590  20.090  1.00 31.56           C  
ATOM   2000  CD1 ILE B  96      -3.802  24.303  19.118  1.00 34.67           C  
ATOM   2001  N   THR B  97       0.472  22.228  18.646  1.00 34.29           N  
ATOM   2002  CA  THR B  97       1.435  22.967  17.856  1.00 35.30           C  
ATOM   2003  C   THR B  97       0.814  23.328  16.524  1.00 34.32           C  
ATOM   2004  O   THR B  97      -0.296  22.923  16.215  1.00 35.33           O  
ATOM   2005  CB  THR B  97       2.679  22.166  17.568  1.00 36.68           C  
ATOM   2006  OG1 THR B  97       2.326  21.089  16.680  1.00 40.54           O  
ATOM   2007  CG2 THR B  97       3.274  21.635  18.868  1.00 38.00           C  
ATOM   2008  N   THR B  98       1.565  24.061  15.720  1.00 45.79           N  
ATOM   2009  CA  THR B  98       1.136  24.393  14.383  1.00 55.06           C  
ATOM   2010  C   THR B  98       1.067  23.116  13.502  1.00 57.52           C  
ATOM   2011  O   THR B  98       0.447  23.118  12.441  1.00 50.40           O  
ATOM   2012  CB  THR B  98       2.071  25.478  13.780  1.00 51.75           C  
ATOM   2013  OG1 THR B  98       1.667  25.789  12.441  1.00 62.55           O  
ATOM   2014  CG2 THR B  98       3.513  25.025  13.796  1.00 43.02           C  
ATOM   2015  N   CYS B  99       1.667  22.020  13.965  1.00 55.03           N  
ATOM   2016  CA  CYS B  99       1.571  20.741  13.262  1.00 44.43           C  
ATOM   2017  C   CYS B  99       0.311  19.952  13.604  1.00 43.82           C  
ATOM   2018  O   CYS B  99      -0.023  18.990  12.930  1.00 49.29           O  
ATOM   2019  CB  CYS B  99       2.792  19.867  13.564  1.00 38.00           C  
ATOM   2020  SG  CYS B  99       4.362  20.639  13.168  1.00118.77           S  
ATOM   2021  N   SER B 100      -0.368  20.333  14.673  1.00 43.67           N  
ATOM   2022  CA  SER B 100      -1.534  19.588  15.127  1.00 34.57           C  
ATOM   2023  C   SER B 100      -2.622  19.657  14.092  1.00 30.00           C  
ATOM   2024  O   SER B 100      -2.606  20.525  13.255  1.00 37.30           O  
ATOM   2025  CB  SER B 100      -2.056  20.147  16.455  1.00 34.62           C  
ATOM   2026  OG  SER B 100      -1.102  20.006  17.488  1.00 41.83           O  
ATOM   2027  N   PHE B 101      -3.586  18.751  14.167  1.00 37.88           N  
ATOM   2028  CA  PHE B 101      -4.779  18.863  13.345  1.00 37.84           C  
ATOM   2029  C   PHE B 101      -5.769  19.845  13.955  1.00 43.59           C  
ATOM   2030  O   PHE B 101      -6.535  19.500  14.848  1.00 45.39           O  
ATOM   2031  CB  PHE B 101      -5.464  17.511  13.158  1.00 41.80           C  
ATOM   2032  CG  PHE B 101      -6.383  17.477  11.976  1.00 43.81           C  
ATOM   2033  CD1 PHE B 101      -7.684  17.932  12.079  1.00 44.37           C  
ATOM   2034  CD2 PHE B 101      -5.928  17.031  10.744  1.00 44.24           C  
ATOM   2035  CE1 PHE B 101      -8.527  17.917  10.980  1.00 45.00           C  
ATOM   2036  CE2 PHE B 101      -6.761  17.018   9.640  1.00 41.18           C  
ATOM   2037  CZ  PHE B 101      -8.061  17.463   9.757  1.00 41.86           C  
ATOM   2038  N   VAL B 102      -5.742  21.076  13.465  1.00 45.95           N  
ATOM   2039  CA  VAL B 102      -6.707  22.088  13.864  1.00 37.38           C  
ATOM   2040  C   VAL B 102      -7.347  22.673  12.606  1.00 37.09           C  
ATOM   2041  O   VAL B 102      -6.655  23.142  11.705  1.00 36.91           O  
ATOM   2042  CB  VAL B 102      -6.045  23.215  14.681  1.00 35.15           C  
ATOM   2043  CG1 VAL B 102      -7.071  24.269  15.048  1.00 42.73           C  
ATOM   2044  CG2 VAL B 102      -5.367  22.654  15.908  1.00 29.45           C  
ATOM   2045  N   ALA B 103      -8.667  22.657  12.542  1.00 43.23           N  
ATOM   2046  CA  ALA B 103      -9.353  23.077  11.334  1.00 42.02           C  
ATOM   2047  C   ALA B 103     -10.782  23.473  11.643  1.00 43.51           C  
ATOM   2048  O   ALA B 103     -11.391  22.948  12.580  1.00 38.29           O  
ATOM   2049  CB  ALA B 103      -9.327  21.956  10.300  1.00 42.30           C  
ATOM   2050  N   PRO B 104     -11.333  24.390  10.841  1.00 45.50           N  
ATOM   2051  CA  PRO B 104     -12.737  24.765  11.000  1.00 44.26           C  
ATOM   2052  C   PRO B 104     -13.642  23.578  10.732  1.00 40.35           C  
ATOM   2053  O   PRO B 104     -13.515  22.972   9.680  1.00 42.08           O  
ATOM   2054  CB  PRO B 104     -12.928  25.852   9.943  1.00 40.89           C  
ATOM   2055  CG  PRO B 104     -11.530  26.316   9.622  1.00 33.89           C  
ATOM   2056  CD  PRO B 104     -10.704  25.101   9.718  1.00 32.62           C  
ATOM   2057  N   TRP B 105     -14.525  23.251  11.672  1.00 41.78           N  
ATOM   2058  CA  TRP B 105     -15.424  22.109  11.528  1.00 39.70           C  
ATOM   2059  C   TRP B 105     -16.134  22.074  10.165  1.00 40.97           C  
ATOM   2060  O   TRP B 105     -16.176  21.035   9.498  1.00 42.85           O  
ATOM   2061  CB  TRP B 105     -16.453  22.109  12.664  1.00 41.10           C  
ATOM   2062  CG  TRP B 105     -17.384  20.951  12.626  1.00 36.02           C  
ATOM   2063  CD1 TRP B 105     -18.691  20.964  12.240  1.00 39.24           C  
ATOM   2064  CD2 TRP B 105     -17.078  19.592  12.962  1.00 40.77           C  
ATOM   2065  NE1 TRP B 105     -19.225  19.694  12.322  1.00 41.85           N  
ATOM   2066  CE2 TRP B 105     -18.253  18.834  12.762  1.00 44.56           C  
ATOM   2067  CE3 TRP B 105     -15.926  18.940  13.416  1.00 39.83           C  
ATOM   2068  CZ2 TRP B 105     -18.306  17.457  12.998  1.00 46.19           C  
ATOM   2069  CZ3 TRP B 105     -15.982  17.567  13.646  1.00 39.42           C  
ATOM   2070  CH2 TRP B 105     -17.163  16.847  13.442  1.00 40.76           C  
ATOM   2071  N   ASN B 106     -16.672  23.211   9.745  1.00 43.45           N  
ATOM   2072  CA  ASN B 106     -17.408  23.280   8.489  1.00 48.97           C  
ATOM   2073  C   ASN B 106     -16.549  22.954   7.267  1.00 45.33           C  
ATOM   2074  O   ASN B 106     -17.036  22.411   6.281  1.00 39.59           O  
ATOM   2075  CB  ASN B 106     -18.031  24.665   8.318  1.00 50.69           C  
ATOM   2076  CG  ASN B 106     -19.144  24.922   9.303  1.00 50.66           C  
ATOM   2077  OD1 ASN B 106     -19.568  24.014  10.018  1.00 46.81           O  
ATOM   2078  ND2 ASN B 106     -19.632  26.164   9.344  1.00 57.93           N  
ATOM   2079  N   SER B 107     -15.266  23.278   7.343  1.00 45.40           N  
ATOM   2080  CA  SER B 107     -14.391  23.121   6.194  1.00 43.55           C  
ATOM   2081  C   SER B 107     -13.980  21.655   5.974  1.00 45.52           C  
ATOM   2082  O   SER B 107     -13.420  21.306   4.933  1.00 47.64           O  
ATOM   2083  CB  SER B 107     -13.161  24.007   6.357  1.00 36.24           C  
ATOM   2084  OG  SER B 107     -12.188  23.337   7.118  1.00 53.42           O  
ATOM   2085  N   LEU B 108     -14.282  20.800   6.947  1.00 47.13           N  
ATOM   2086  CA  LEU B 108     -14.010  19.364   6.837  1.00 44.66           C  
ATOM   2087  C   LEU B 108     -14.930  18.680   5.842  1.00 40.61           C  
ATOM   2088  O   LEU B 108     -16.042  19.142   5.595  1.00 38.51           O  
ATOM   2089  CB  LEU B 108     -14.153  18.682   8.201  1.00 36.64           C  
ATOM   2090  CG  LEU B 108     -13.091  19.162   9.176  1.00 39.52           C  
ATOM   2091  CD1 LEU B 108     -13.360  18.659  10.596  1.00 39.42           C  
ATOM   2092  CD2 LEU B 108     -11.722  18.758   8.677  1.00 31.12           C  
ATOM   2093  N   SER B 109     -14.478  17.559   5.287  1.00 39.49           N  
ATOM   2094  CA  SER B 109     -15.340  16.765   4.413  1.00 41.98           C  
ATOM   2095  C   SER B 109     -16.387  16.012   5.231  1.00 51.58           C  
ATOM   2096  O   SER B 109     -16.305  15.967   6.460  1.00 49.95           O  
ATOM   2097  CB  SER B 109     -14.515  15.788   3.587  1.00 36.33           C  
ATOM   2098  OG  SER B 109     -13.984  14.766   4.398  1.00 41.33           O  
ATOM   2099  N   LEU B 110     -17.382  15.437   4.560  1.00 60.58           N  
ATOM   2100  CA  LEU B 110     -18.381  14.648   5.266  1.00 59.74           C  
ATOM   2101  C   LEU B 110     -17.681  13.448   5.871  1.00 54.92           C  
ATOM   2102  O   LEU B 110     -17.832  13.156   7.064  1.00 53.77           O  
ATOM   2103  CB  LEU B 110     -19.510  14.194   4.343  1.00 69.12           C  
ATOM   2104  CG  LEU B 110     -20.543  13.316   5.060  1.00 69.56           C  
ATOM   2105  CD1 LEU B 110     -21.390  14.155   6.010  1.00 80.04           C  
ATOM   2106  CD2 LEU B 110     -21.410  12.561   4.097  1.00 61.06           C  
ATOM   2107  N   ALA B 111     -16.889  12.776   5.040  1.00 45.83           N  
ATOM   2108  CA  ALA B 111     -16.116  11.623   5.478  1.00 40.98           C  
ATOM   2109  C   ALA B 111     -15.160  11.966   6.617  1.00 49.60           C  
ATOM   2110  O   ALA B 111     -14.736  11.088   7.340  1.00 52.15           O  
ATOM   2111  CB  ALA B 111     -15.341  11.049   4.331  1.00 36.72           C  
ATOM   2112  N   GLN B 112     -14.785  13.230   6.762  1.00 46.32           N  
ATOM   2113  CA  GLN B 112     -13.902  13.602   7.857  1.00 42.89           C  
ATOM   2114  C   GLN B 112     -14.704  13.816   9.147  1.00 47.56           C  
ATOM   2115  O   GLN B 112     -14.239  13.484  10.231  1.00 48.43           O  
ATOM   2116  CB  GLN B 112     -13.100  14.847   7.502  1.00 38.34           C  
ATOM   2117  CG  GLN B 112     -11.765  14.556   6.837  1.00 38.24           C  
ATOM   2118  CD  GLN B 112     -11.144  15.779   6.157  1.00 34.29           C  
ATOM   2119  OE1 GLN B 112     -11.828  16.766   5.864  1.00 33.63           O  
ATOM   2120  NE2 GLN B 112      -9.846  15.705   5.893  1.00 32.80           N  
ATOM   2121  N   ARG B 113     -15.921  14.335   9.033  1.00 48.76           N  
ATOM   2122  CA  ARG B 113     -16.750  14.521  10.217  1.00 50.69           C  
ATOM   2123  C   ARG B 113     -17.295  13.171  10.703  1.00 58.37           C  
ATOM   2124  O   ARG B 113     -17.133  12.831  11.876  1.00 65.28           O  
ATOM   2125  CB  ARG B 113     -17.877  15.518   9.942  1.00 47.36           C  
ATOM   2126  CG  ARG B 113     -17.383  16.936   9.643  1.00 47.96           C  
ATOM   2127  CD  ARG B 113     -18.549  17.890   9.380  1.00 57.64           C  
ATOM   2128  NE  ARG B 113     -18.477  18.503   8.058  1.00 64.87           N  
ATOM   2129  CZ  ARG B 113     -19.187  18.109   7.007  1.00 69.66           C  
ATOM   2130  NH1 ARG B 113     -20.046  17.105   7.123  1.00 82.85           N  
ATOM   2131  NH2 ARG B 113     -19.049  18.729   5.843  1.00 62.46           N  
ATOM   2132  N   ARG B 114     -17.929  12.396   9.823  1.00 58.47           N  
ATOM   2133  CA  ARG B 114     -18.121  10.979  10.129  1.00 65.61           C  
ATOM   2134  C   ARG B 114     -16.687  10.539  10.284  1.00 64.69           C  
ATOM   2135  O   ARG B 114     -15.833  11.000   9.552  1.00 67.33           O  
ATOM   2136  CB  ARG B 114     -18.869  10.199   9.021  1.00 52.37           C  
ATOM   2137  N   GLY B 115     -16.361   9.723  11.261  1.00 57.32           N  
ATOM   2138  CA  GLY B 115     -14.947   9.452  11.407  1.00 58.17           C  
ATOM   2139  C   GLY B 115     -14.368  10.152  12.604  1.00 53.56           C  
ATOM   2140  O   GLY B 115     -13.892   9.480  13.509  1.00 54.62           O  
ATOM   2141  N   PHE B 116     -14.400  11.483  12.638  1.00 45.38           N  
ATOM   2142  CA  PHE B 116     -14.065  12.142  13.899  1.00 43.49           C  
ATOM   2143  C   PHE B 116     -15.119  11.727  14.928  1.00 51.77           C  
ATOM   2144  O   PHE B 116     -14.801  11.401  16.064  1.00 51.26           O  
ATOM   2145  CB  PHE B 116     -13.974  13.667  13.755  1.00 36.39           C  
ATOM   2146  CG  PHE B 116     -12.598  14.154  13.388  1.00 44.95           C  
ATOM   2147  CD1 PHE B 116     -11.479  13.714  14.098  1.00 42.73           C  
ATOM   2148  CD2 PHE B 116     -12.407  15.029  12.319  1.00 37.94           C  
ATOM   2149  CE1 PHE B 116     -10.192  14.148  13.750  1.00 30.13           C  
ATOM   2150  CE2 PHE B 116     -11.121  15.450  11.965  1.00 38.98           C  
ATOM   2151  CZ  PHE B 116     -10.016  15.001  12.677  1.00 29.54           C  
ATOM   2152  N   THR B 117     -16.369  11.683  14.489  1.00 55.54           N  
ATOM   2153  CA  THR B 117     -17.484  11.303  15.340  1.00 61.83           C  
ATOM   2154  C   THR B 117     -17.521   9.809  15.705  1.00 70.55           C  
ATOM   2155  O   THR B 117     -17.691   9.464  16.873  1.00 79.48           O  
ATOM   2156  CB  THR B 117     -18.793  11.673  14.663  1.00 66.18           C  
ATOM   2157  OG1 THR B 117     -18.762  11.178  13.322  1.00 80.18           O  
ATOM   2158  CG2 THR B 117     -18.947  13.195  14.607  1.00 59.26           C  
ATOM   2159  N   LYS B 118     -17.369   8.924  14.721  1.00 68.56           N  
ATOM   2160  CA  LYS B 118     -17.492   7.481  14.971  1.00 63.40           C  
ATOM   2161  C   LYS B 118     -16.381   6.671  14.341  1.00 68.22           C  
ATOM   2162  O   LYS B 118     -15.607   6.025  15.036  1.00 80.48           O  
ATOM   2163  CB  LYS B 118     -18.837   6.937  14.458  1.00 57.89           C  
ATOM   2164  N   THR B 119     -16.308   6.721  13.018  1.00 61.30           N  
ATOM   2165  CA  THR B 119     -15.520   5.775  12.235  1.00 57.52           C  
ATOM   2166  C   THR B 119     -14.044   5.619  12.637  1.00 48.71           C  
ATOM   2167  O   THR B 119     -13.562   4.499  12.779  1.00 48.41           O  
ATOM   2168  CB  THR B 119     -15.591   6.154  10.738  1.00 62.65           C  
ATOM   2169  OG1 THR B 119     -16.959   6.116  10.305  1.00 73.56           O  
ATOM   2170  CG2 THR B 119     -14.728   5.218   9.865  1.00 48.82           C  
ATOM   2171  N   TYR B 120     -13.325   6.717  12.826  1.00 47.76           N  
ATOM   2172  CA  TYR B 120     -11.878   6.625  13.073  1.00 52.22           C  
ATOM   2173  C   TYR B 120     -11.471   5.652  14.184  1.00 59.43           C  
ATOM   2174  O   TYR B 120     -10.514   4.896  14.028  1.00 57.55           O  
ATOM   2175  CB  TYR B 120     -11.303   8.003  13.399  1.00 42.95           C  
ATOM   2176  CG  TYR B 120     -11.155   8.874  12.185  1.00 41.18           C  
ATOM   2177  CD1 TYR B 120     -10.950   8.308  10.933  1.00 36.38           C  
ATOM   2178  CD2 TYR B 120     -11.188  10.259  12.285  1.00 37.87           C  
ATOM   2179  CE1 TYR B 120     -10.806   9.094   9.814  1.00 33.58           C  
ATOM   2180  CE2 TYR B 120     -11.039  11.056  11.168  1.00 38.85           C  
ATOM   2181  CZ  TYR B 120     -10.852  10.460   9.938  1.00 39.33           C  
ATOM   2182  OH  TYR B 120     -10.714  11.232   8.819  1.00 47.11           O  
ATOM   2183  N   THR B 121     -12.200   5.663  15.294  1.00 61.47           N  
ATOM   2184  CA  THR B 121     -11.789   4.912  16.472  1.00 58.19           C  
ATOM   2185  C   THR B 121     -11.694   3.386  16.196  1.00 55.40           C  
ATOM   2186  O   THR B 121     -10.983   2.657  16.894  1.00 57.26           O  
ATOM   2187  CB  THR B 121     -12.754   5.217  17.651  1.00 55.32           C  
ATOM   2188  OG1 THR B 121     -12.169   4.798  18.893  1.00 65.06           O  
ATOM   2189  CG2 THR B 121     -14.104   4.537  17.451  1.00 48.13           C  
ATOM   2190  N   VAL B 122     -12.381   2.911  15.159  1.00 48.31           N  
ATOM   2191  CA  VAL B 122     -12.254   1.520  14.728  1.00 51.70           C  
ATOM   2192  C   VAL B 122     -10.819   1.138  14.318  1.00 58.04           C  
ATOM   2193  O   VAL B 122     -10.389  -0.023  14.464  1.00 65.11           O  
ATOM   2194  CB  VAL B 122     -13.183   1.222  13.538  1.00 45.90           C  
ATOM   2195  CG1 VAL B 122     -13.264  -0.293  13.267  1.00 45.22           C  
ATOM   2196  CG2 VAL B 122     -14.553   1.804  13.789  1.00 46.21           C  
ATOM   2197  N   GLY B 123     -10.080   2.116  13.809  1.00 45.55           N  
ATOM   2198  CA  GLY B 123      -8.783   1.848  13.221  1.00 49.84           C  
ATOM   2199  C   GLY B 123      -7.627   2.098  14.157  1.00 49.35           C  
ATOM   2200  O   GLY B 123      -6.497   1.713  13.869  1.00 56.21           O  
ATOM   2201  N   CYS B 124      -7.916   2.722  15.291  1.00 45.17           N  
ATOM   2202  CA  CYS B 124      -6.879   3.111  16.246  1.00 43.14           C  
ATOM   2203  C   CYS B 124      -6.083   1.926  16.790  1.00 46.83           C  
ATOM   2204  O   CYS B 124      -4.868   1.868  16.630  1.00 51.43           O  
ATOM   2205  CB  CYS B 124      -7.513   3.908  17.387  1.00 39.92           C  
ATOM   2206  SG  CYS B 124      -8.117   5.511  16.834  1.00107.10           S  
ATOM   2207  N   GLU B 125      -6.769   0.972  17.408  1.00 55.25           N  
ATOM   2208  CA  GLU B 125      -6.099  -0.186  17.994  1.00 72.52           C  
ATOM   2209  C   GLU B 125      -5.289  -1.025  16.992  1.00 73.61           C  
ATOM   2210  O   GLU B 125      -4.136  -1.366  17.253  1.00 75.44           O  
ATOM   2211  CB  GLU B 125      -7.128  -1.075  18.701  1.00 87.03           C  
ATOM   2212  CG  GLU B 125      -6.907  -1.162  20.215  1.00106.48           C  
ATOM   2213  CD  GLU B 125      -8.199  -1.363  20.999  1.00122.56           C  
ATOM   2214  OE1 GLU B 125      -9.221  -1.724  20.377  1.00130.22           O  
ATOM   2215  OE2 GLU B 125      -8.198  -1.151  22.235  1.00124.69           O  
ATOM   2216  N   GLU B 126      -5.864  -1.342  15.839  1.00 69.03           N  
ATOM   2217  CA  GLU B 126      -5.224  -2.330  14.983  1.00 60.07           C  
ATOM   2218  C   GLU B 126      -4.582  -1.801  13.699  1.00 50.48           C  
ATOM   2219  O   GLU B 126      -3.914  -2.565  13.007  1.00 52.39           O  
ATOM   2220  CB  GLU B 126      -6.237  -3.435  14.637  1.00 58.72           C  
ATOM   2221  CG  GLU B 126      -6.464  -4.419  15.782  0.00 61.35           C  
ATOM   2222  CD  GLU B 126      -7.931  -4.632  16.101  0.00 62.17           C  
ATOM   2223  OE1 GLU B 126      -8.377  -4.181  17.178  0.00 63.26           O  
ATOM   2224  OE2 GLU B 126      -8.637  -5.255  15.281  0.00 62.35           O  
ATOM   2225  N   CYS B 127      -4.745  -0.517  13.385  1.00 47.98           N  
ATOM   2226  CA  CYS B 127      -4.289   0.005  12.083  1.00 38.31           C  
ATOM   2227  C   CYS B 127      -3.446   1.294  12.153  1.00 50.38           C  
ATOM   2228  O   CYS B 127      -3.539   2.070  13.107  1.00 56.54           O  
ATOM   2229  CB  CYS B 127      -5.497   0.238  11.177  1.00 37.32           C  
ATOM   2230  SG  CYS B 127      -6.515  -1.262  10.855  1.00 55.24           S  
ATOM   2231  N   THR B 128      -2.624   1.531  11.137  1.00 47.86           N  
ATOM   2232  CA  THR B 128      -1.746   2.698  11.157  1.00 42.52           C  
ATOM   2233  C   THR B 128      -1.625   3.420   9.813  1.00 44.19           C  
ATOM   2234  O   THR B 128      -1.263   2.820   8.806  1.00 41.03           O  
ATOM   2235  CB  THR B 128      -0.334   2.308  11.615  1.00 47.38           C  
ATOM   2236  OG1 THR B 128      -0.362   1.978  13.014  1.00 47.84           O  
ATOM   2237  CG2 THR B 128       0.648   3.468  11.378  1.00 36.30           C  
ATOM   2238  N   VAL B 129      -1.916   4.717   9.805  1.00 44.68           N  
ATOM   2239  CA  VAL B 129      -1.725   5.519   8.606  1.00 32.07           C  
ATOM   2240  C   VAL B 129      -0.282   6.009   8.514  1.00 38.07           C  
ATOM   2241  O   VAL B 129       0.128   6.904   9.230  1.00 46.07           O  
ATOM   2242  CB  VAL B 129      -2.691   6.713   8.567  1.00 31.08           C  
ATOM   2243  CG1 VAL B 129      -2.419   7.568   7.349  1.00 30.64           C  
ATOM   2244  CG2 VAL B 129      -4.130   6.223   8.544  1.00 30.97           C  
ATOM   2245  N   PHE B 130       0.487   5.400   7.620  1.00 43.87           N  
ATOM   2246  CA  PHE B 130       1.911   5.695   7.475  1.00 46.94           C  
ATOM   2247  C   PHE B 130       2.178   6.681   6.334  1.00 50.65           C  
ATOM   2248  O   PHE B 130       1.833   6.413   5.195  1.00 40.41           O  
ATOM   2249  CB  PHE B 130       2.673   4.398   7.238  1.00 48.44           C  
ATOM   2250  CG  PHE B 130       4.146   4.574   7.105  1.00 60.12           C  
ATOM   2251  CD1 PHE B 130       4.963   4.563   8.231  1.00 64.95           C  
ATOM   2252  CD2 PHE B 130       4.728   4.724   5.854  1.00 62.23           C  
ATOM   2253  CE1 PHE B 130       6.334   4.718   8.114  1.00 66.50           C  
ATOM   2254  CE2 PHE B 130       6.102   4.884   5.728  1.00 68.98           C  
ATOM   2255  CZ  PHE B 130       6.905   4.881   6.858  1.00 69.19           C  
ATOM   2256  N   PRO B 131       2.800   7.829   6.644  1.00 55.36           N  
ATOM   2257  CA  PRO B 131       3.048   8.888   5.658  1.00 54.62           C  
ATOM   2258  C   PRO B 131       4.105   8.529   4.621  1.00 62.45           C  
ATOM   2259  O   PRO B 131       5.246   8.236   4.975  1.00 65.72           O  
ATOM   2260  CB  PRO B 131       3.526  10.061   6.519  1.00 56.15           C  
ATOM   2261  CG  PRO B 131       3.046   9.743   7.907  1.00 55.62           C  
ATOM   2262  CD  PRO B 131       3.169   8.254   7.998  1.00 52.95           C  
ATOM   2263  N   CYS B 132       3.707   8.565   3.351  1.00 69.56           N  
ATOM   2264  CA  CYS B 132       4.595   8.324   2.223  1.00 68.32           C  
ATOM   2265  C   CYS B 132       5.069   9.631   1.606  1.00 79.02           C  
ATOM   2266  O   CYS B 132       4.315  10.274   0.875  1.00 80.94           O  
ATOM   2267  CB  CYS B 132       3.889   7.482   1.153  1.00 56.39           C  
ATOM   2268  SG  CYS B 132       4.284   5.731   1.216  1.00111.33           S  
ATOM   2269  N   PRO B 133       6.325  10.021   1.886  1.00 91.35           N  
ATOM   2270  CA  PRO B 133       6.891  11.236   1.282  1.00102.32           C  
ATOM   2271  C   PRO B 133       7.170  11.049  -0.218  1.00105.79           C  
ATOM   2272  O   PRO B 133       6.322  11.338  -1.067  1.00111.97           O  
ATOM   2273  CB  PRO B 133       8.189  11.450   2.071  1.00 99.63           C  
ATOM   2274  CG  PRO B 133       8.574  10.086   2.563  1.00 95.48           C  
ATOM   2275  CD  PRO B 133       7.303   9.294   2.718  1.00 93.26           C  
ATOM   2276  N   SER B 134       8.360  10.568  -0.537  1.00 91.71           N  
ATOM   2277  CA  SER B 134       8.678  10.212  -1.900  1.00 83.40           C  
ATOM   2278  C   SER B 134       8.180   8.801  -2.179  1.00 79.50           C  
ATOM   2279  O   SER B 134       8.357   7.905  -1.353  1.00 84.05           O  
ATOM   2280  CB  SER B 134      10.188  10.318  -2.131  1.00 86.28           C  
ATOM   2281  OG  SER B 134      10.611   9.622  -3.290  1.00 93.68           O  
ATOM   2282  N   ILE B 135       7.532   8.604  -3.322  1.00 64.23           N  
ATOM   2283  CA  ILE B 135       7.426   7.257  -3.871  1.00 61.90           C  
ATOM   2284  C   ILE B 135       8.746   6.942  -4.595  1.00 60.78           C  
ATOM   2285  O   ILE B 135       9.312   7.791  -5.276  1.00 50.91           O  
ATOM   2286  CB  ILE B 135       6.220   7.088  -4.825  1.00 57.75           C  
ATOM   2287  CG1 ILE B 135       6.073   8.304  -5.737  1.00 74.67           C  
ATOM   2288  CG2 ILE B 135       4.932   6.899  -4.033  1.00 48.05           C  
ATOM   2289  CD1 ILE B 135       6.662   8.118  -7.139  1.00 84.54           C  
ATOM   2290  N   PRO B 136       9.264   5.722  -4.425  1.00 59.40           N  
ATOM   2291  CA  PRO B 136       8.700   4.603  -3.666  1.00 60.90           C  
ATOM   2292  C   PRO B 136       8.746   4.803  -2.153  1.00 63.33           C  
ATOM   2293  O   PRO B 136       9.668   5.457  -1.654  1.00 70.24           O  
ATOM   2294  CB  PRO B 136       9.596   3.421  -4.067  1.00 59.67           C  
ATOM   2295  CG  PRO B 136      10.478   3.921  -5.154  1.00 57.84           C  
ATOM   2296  CD  PRO B 136      10.577   5.384  -4.985  1.00 53.99           C  
ATOM   2297  N   CYS B 137       7.745   4.259  -1.457  1.00 61.28           N  
ATOM   2298  CA  CYS B 137       7.746   4.140   0.004  1.00 57.71           C  
ATOM   2299  C   CYS B 137       7.861   2.663   0.357  1.00 62.31           C  
ATOM   2300  O   CYS B 137       7.370   1.818  -0.388  1.00 62.39           O  
ATOM   2301  CB  CYS B 137       6.470   4.701   0.624  1.00 40.68           C  
ATOM   2302  SG  CYS B 137       5.602   5.970  -0.320  1.00137.89           S  
ATOM   2303  N   LYS B 138       8.496   2.334   1.476  1.00 60.79           N  
ATOM   2304  CA  LYS B 138       8.468   0.947   1.932  1.00 53.52           C  
ATOM   2305  C   LYS B 138       7.225   0.760   2.812  1.00 48.34           C  
ATOM   2306  O   LYS B 138       6.921   1.597   3.665  1.00 48.08           O  
ATOM   2307  CB  LYS B 138       9.757   0.568   2.678  1.00 46.76           C  
ATOM   2308  N   LEU B 139       6.481  -0.313   2.558  1.00 45.69           N  
ATOM   2309  CA  LEU B 139       5.373  -0.709   3.417  1.00 48.34           C  
ATOM   2310  C   LEU B 139       5.919  -1.585   4.534  1.00 58.67           C  
ATOM   2311  O   LEU B 139       6.315  -2.719   4.282  1.00 54.81           O  
ATOM   2312  CB  LEU B 139       4.304  -1.467   2.627  1.00 47.02           C  
ATOM   2313  CG  LEU B 139       3.213  -2.072   3.512  1.00 43.81           C  
ATOM   2314  CD1 LEU B 139       2.192  -1.014   3.904  1.00 44.53           C  
ATOM   2315  CD2 LEU B 139       2.537  -3.269   2.866  1.00 38.99           C  
ATOM   2316  N   GLN B 140       5.950  -1.070   5.761  1.00 69.41           N  
ATOM   2317  CA  GLN B 140       6.635  -1.774   6.848  1.00 67.48           C  
ATOM   2318  C   GLN B 140       5.805  -2.897   7.478  1.00 52.03           C  
ATOM   2319  O   GLN B 140       6.350  -3.747   8.172  1.00 49.77           O  
ATOM   2320  CB  GLN B 140       7.075  -0.781   7.927  1.00 73.34           C  
ATOM   2321  CG  GLN B 140       8.466  -0.172   7.693  1.00 85.03           C  
ATOM   2322  CD  GLN B 140       9.608  -1.166   7.923  1.00101.81           C  
ATOM   2323  OE1 GLN B 140       9.464  -2.145   8.660  1.00105.38           O  
ATOM   2324  NE2 GLN B 140      10.749  -0.910   7.291  1.00111.23           N  
ATOM   2325  N   SER B 141       4.504  -2.926   7.197  1.00 51.60           N  
ATOM   2326  CA  SER B 141       3.598  -3.899   7.808  1.00 47.75           C  
ATOM   2327  C   SER B 141       2.267  -4.009   7.072  1.00 49.59           C  
ATOM   2328  O   SER B 141       1.843  -3.064   6.413  1.00 56.38           O  
ATOM   2329  CB  SER B 141       3.336  -3.522   9.265  1.00 55.20           C  
ATOM   2330  OG  SER B 141       2.174  -4.161   9.757  1.00 58.49           O  
ATOM   2331  N   GLY B 142       1.597  -5.151   7.209  1.00 47.87           N  
ATOM   2332  CA  GLY B 142       0.319  -5.384   6.548  1.00 41.29           C  
ATOM   2333  C   GLY B 142      -0.838  -4.602   7.147  1.00 47.71           C  
ATOM   2334  O   GLY B 142      -1.882  -4.425   6.514  1.00 58.70           O  
ATOM   2335  N   THR B 143      -0.647  -4.127   8.374  1.00 44.31           N  
ATOM   2336  CA  THR B 143      -1.606  -3.239   9.029  1.00 46.20           C  
ATOM   2337  C   THR B 143      -1.292  -1.761   8.795  1.00 39.54           C  
ATOM   2338  O   THR B 143      -1.907  -0.885   9.405  1.00 38.79           O  
ATOM   2339  CB  THR B 143      -1.651  -3.478  10.541  1.00 50.28           C  
ATOM   2340  OG1 THR B 143      -0.412  -3.046  11.121  1.00 49.12           O  
ATOM   2341  CG2 THR B 143      -1.887  -4.958  10.845  1.00 51.43           C  
ATOM   2342  N   HIS B 144      -0.323  -1.482   7.928  1.00 38.77           N  
ATOM   2343  CA  HIS B 144      -0.087  -0.113   7.480  1.00 44.67           C  
ATOM   2344  C   HIS B 144      -0.860   0.228   6.219  1.00 49.26           C  
ATOM   2345  O   HIS B 144      -0.893  -0.541   5.259  1.00 55.41           O  
ATOM   2346  CB  HIS B 144       1.392   0.144   7.216  1.00 50.83           C  
ATOM   2347  CG  HIS B 144       2.222   0.213   8.448  1.00 58.23           C  
ATOM   2348  ND1 HIS B 144       1.674   0.311   9.708  1.00 59.83           N  
ATOM   2349  CD2 HIS B 144       3.562   0.237   8.617  1.00 68.15           C  
ATOM   2350  CE1 HIS B 144       2.641   0.366  10.601  1.00 63.34           C  
ATOM   2351  NE2 HIS B 144       3.798   0.328   9.965  1.00 67.96           N  
ATOM   2352  N   CYS B 145      -1.482   1.396   6.232  1.00 47.07           N  
ATOM   2353  CA  CYS B 145      -2.016   1.966   5.018  1.00 45.33           C  
ATOM   2354  C   CYS B 145      -1.091   3.089   4.617  1.00 39.97           C  
ATOM   2355  O   CYS B 145      -0.851   3.990   5.414  1.00 32.67           O  
ATOM   2356  CB  CYS B 145      -3.441   2.472   5.211  1.00 46.39           C  
ATOM   2357  SG  CYS B 145      -4.611   1.156   5.558  1.00 86.94           S  
ATOM   2358  N   LEU B 146      -0.557   3.009   3.397  1.00 33.19           N  
ATOM   2359  CA  LEU B 146       0.311   4.039   2.871  1.00 34.71           C  
ATOM   2360  C   LEU B 146      -0.534   5.249   2.506  1.00 43.30           C  
ATOM   2361  O   LEU B 146      -1.564   5.135   1.843  1.00 41.60           O  
ATOM   2362  CB  LEU B 146       1.104   3.537   1.662  1.00 39.78           C  
ATOM   2363  CG  LEU B 146       2.068   2.365   1.906  1.00 40.17           C  
ATOM   2364  CD1 LEU B 146       2.788   2.017   0.647  1.00 36.49           C  
ATOM   2365  CD2 LEU B 146       3.064   2.670   2.990  1.00 43.32           C  
ATOM   2366  N   TRP B 147      -0.104   6.401   3.003  1.00 47.81           N  
ATOM   2367  CA  TRP B 147      -0.745   7.675   2.742  1.00 45.00           C  
ATOM   2368  C   TRP B 147       0.020   8.311   1.591  1.00 46.09           C  
ATOM   2369  O   TRP B 147       1.172   8.727   1.747  1.00 49.68           O  
ATOM   2370  CB  TRP B 147      -0.722   8.538   4.000  1.00 47.03           C  
ATOM   2371  CG  TRP B 147      -1.455   9.818   3.914  1.00 40.72           C  
ATOM   2372  CD1 TRP B 147      -2.435  10.142   3.036  1.00 36.91           C  
ATOM   2373  CD2 TRP B 147      -1.259  10.968   4.748  1.00 39.72           C  
ATOM   2374  NE1 TRP B 147      -2.867  11.432   3.262  1.00 35.29           N  
ATOM   2375  CE2 TRP B 147      -2.160  11.959   4.312  1.00 35.21           C  
ATOM   2376  CE3 TRP B 147      -0.403  11.257   5.819  1.00 31.37           C  
ATOM   2377  CZ2 TRP B 147      -2.248  13.213   4.921  1.00 30.81           C  
ATOM   2378  CZ3 TRP B 147      -0.485  12.506   6.417  1.00 34.85           C  
ATOM   2379  CH2 TRP B 147      -1.404  13.470   5.965  1.00 30.89           C  
ATOM   2380  N   THR B 148      -0.611   8.353   0.423  1.00 45.10           N  
ATOM   2381  CA  THR B 148       0.113   8.641  -0.804  1.00 40.35           C  
ATOM   2382  C   THR B 148      -0.277   9.976  -1.424  1.00 46.12           C  
ATOM   2383  O   THR B 148       0.323  10.384  -2.404  1.00 50.49           O  
ATOM   2384  CB  THR B 148      -0.069   7.498  -1.850  1.00 36.62           C  
ATOM   2385  OG1 THR B 148      -1.381   6.936  -1.759  1.00 46.74           O  
ATOM   2386  CG2 THR B 148       0.918   6.386  -1.586  1.00 42.03           C  
ATOM   2387  N   ASP B 149      -1.277  10.647  -0.864  1.00 52.14           N  
ATOM   2388  CA  ASP B 149      -1.571  12.030  -1.232  1.00 50.23           C  
ATOM   2389  C   ASP B 149      -0.251  12.779  -1.269  1.00 54.80           C  
ATOM   2390  O   ASP B 149       0.447  12.836  -0.257  1.00 61.09           O  
ATOM   2391  CB  ASP B 149      -2.511  12.702  -0.205  1.00 54.88           C  
ATOM   2392  CG  ASP B 149      -3.852  11.956  -0.003  1.00 67.48           C  
ATOM   2393  OD1 ASP B 149      -4.232  11.109  -0.857  1.00 63.54           O  
ATOM   2394  OD2 ASP B 149      -4.518  12.240   1.035  1.00 63.79           O  
ATOM   2395  N   GLN B 150       0.133  13.325  -2.409  1.00 69.67           N  
ATOM   2396  CA  GLN B 150       1.311  14.165  -2.366  1.00 86.62           C  
ATOM   2397  C   GLN B 150       0.939  15.593  -2.712  1.00 87.24           C  
ATOM   2398  O   GLN B 150       1.715  16.305  -3.326  1.00 87.84           O  
ATOM   2399  CB  GLN B 150       2.416  13.652  -3.275  1.00 96.88           C  
ATOM   2400  CG  GLN B 150       2.469  12.151  -3.446  1.00 98.09           C  
ATOM   2401  CD  GLN B 150       3.881  11.659  -3.719  1.00107.98           C  
ATOM   2402  OE1 GLN B 150       4.278  11.428  -4.865  1.00117.12           O  
ATOM   2403  NE2 GLN B 150       4.649  11.482  -2.643  1.00107.07           N  
ATOM   2404  N   CYS B 151      -0.270  15.999  -2.339  1.00 88.91           N  
ATOM   2405  CA  CYS B 151      -0.594  17.406  -2.216  1.00 84.54           C  
ATOM   2406  C   CYS B 151       0.445  18.023  -1.285  1.00 79.82           C  
ATOM   2407  O   CYS B 151       0.978  17.347  -0.406  1.00 79.81           O  
ATOM   2408  CB  CYS B 151      -2.012  17.575  -1.661  1.00 78.74           C  
ATOM   2409  SG  CYS B 151      -3.321  18.049  -2.849  1.00132.65           S  
ATOM   2410  N   LEU B 152       0.762  19.292  -1.477  1.00 75.78           N  
ATOM   2411  CA  LEU B 152       1.548  19.966  -0.463  1.00 75.81           C  
ATOM   2412  C   LEU B 152       0.771  19.976   0.855  1.00 76.35           C  
ATOM   2413  O   LEU B 152       1.342  19.717   1.915  1.00 73.55           O  
ATOM   2414  CB  LEU B 152       1.895  21.390  -0.877  1.00 71.46           C  
ATOM   2415  CG  LEU B 152       2.646  22.088   0.255  1.00 73.15           C  
ATOM   2416  CD1 LEU B 152       3.849  21.259   0.703  1.00 80.35           C  
ATOM   2417  CD2 LEU B 152       3.092  23.448  -0.164  1.00 71.91           C  
ATOM   2418  N   GLN B 153      -0.526  20.279   0.774  1.00 68.38           N  
ATOM   2419  CA  GLN B 153      -1.408  20.311   1.942  1.00 59.57           C  
ATOM   2420  C   GLN B 153      -2.256  19.037   1.997  1.00 55.48           C  
ATOM   2421  O   GLN B 153      -3.491  19.079   2.118  1.00 46.16           O  
ATOM   2422  CB  GLN B 153      -2.291  21.550   1.901  1.00 50.39           C  
ATOM   2423  CG  GLN B 153      -1.508  22.822   1.722  1.00 49.67           C  
ATOM   2424  CD  GLN B 153      -2.270  23.867   0.957  1.00 57.53           C  
ATOM   2425  OE1 GLN B 153      -2.154  23.970  -0.262  1.00 58.23           O  
ATOM   2426  NE2 GLN B 153      -3.062  24.655   1.668  1.00 69.81           N  
ATOM   2427  N   ALA B 154      -1.560  17.909   1.889  1.00 49.86           N  
ATOM   2428  CA  ALA B 154      -2.168  16.589   1.899  1.00 50.10           C  
ATOM   2429  C   ALA B 154      -3.161  16.424   3.035  1.00 53.76           C  
ATOM   2430  O   ALA B 154      -4.223  15.830   2.857  1.00 50.55           O  
ATOM   2431  CB  ALA B 154      -1.085  15.518   1.990  1.00 46.62           C  
ATOM   2432  N   SER B 155      -2.811  16.959   4.201  1.00 60.90           N  
ATOM   2433  CA  SER B 155      -3.649  16.805   5.375  1.00 54.18           C  
ATOM   2434  C   SER B 155      -4.961  17.557   5.166  1.00 44.90           C  
ATOM   2435  O   SER B 155      -6.048  17.006   5.349  1.00 41.45           O  
ATOM   2436  CB  SER B 155      -2.914  17.289   6.629  1.00 58.61           C  
ATOM   2437  OG  SER B 155      -3.627  16.947   7.812  1.00 50.51           O  
ATOM   2438  N   GLU B 156      -4.870  18.816   4.765  1.00 45.51           N  
ATOM   2439  CA  GLU B 156      -6.090  19.576   4.558  1.00 57.19           C  
ATOM   2440  C   GLU B 156      -6.811  19.148   3.265  1.00 68.68           C  
ATOM   2441  O   GLU B 156      -8.033  18.966   3.275  1.00 76.13           O  
ATOM   2442  CB  GLU B 156      -5.799  21.085   4.549  1.00 46.80           C  
ATOM   2443  CG  GLU B 156      -4.560  21.468   5.338  0.00 49.93           C  
ATOM   2444  CD  GLU B 156      -4.296  22.959   5.319  0.00 53.03           C  
ATOM   2445  OE1 GLU B 156      -5.272  23.734   5.213  0.00 54.04           O  
ATOM   2446  OE2 GLU B 156      -3.117  23.359   5.424  0.00 54.44           O  
ATOM   2447  N   LYS B 157      -6.062  18.942   2.178  1.00 57.98           N  
ATOM   2448  CA  LYS B 157      -6.674  18.891   0.852  1.00 50.60           C  
ATOM   2449  C   LYS B 157      -6.553  17.557   0.083  1.00 49.55           C  
ATOM   2450  O   LYS B 157      -6.995  17.465  -1.062  1.00 53.64           O  
ATOM   2451  CB  LYS B 157      -6.093  20.032  -0.005  1.00 43.77           C  
ATOM   2452  N   GLY B 158      -5.987  16.521   0.695  1.00 44.69           N  
ATOM   2453  CA  GLY B 158      -5.721  15.282  -0.032  1.00 40.11           C  
ATOM   2454  C   GLY B 158      -6.896  14.312  -0.154  1.00 45.27           C  
ATOM   2455  O   GLY B 158      -7.763  14.266   0.724  1.00 49.77           O  
ATOM   2456  N   PHE B 159      -6.926  13.520  -1.228  1.00 36.60           N  
ATOM   2457  CA  PHE B 159      -8.028  12.576  -1.423  1.00 35.27           C  
ATOM   2458  C   PHE B 159      -8.196  11.566  -0.276  1.00 34.62           C  
ATOM   2459  O   PHE B 159      -9.270  11.478   0.315  1.00 40.18           O  
ATOM   2460  CB  PHE B 159      -7.877  11.792  -2.734  1.00 36.42           C  
ATOM   2461  CG  PHE B 159      -9.057  10.894  -3.020  1.00 36.96           C  
ATOM   2462  CD1 PHE B 159     -10.151  11.373  -3.733  1.00 39.52           C  
ATOM   2463  CD2 PHE B 159      -9.098   9.599  -2.530  1.00 36.07           C  
ATOM   2464  CE1 PHE B 159     -11.258  10.564  -3.973  1.00 42.61           C  
ATOM   2465  CE2 PHE B 159     -10.206   8.782  -2.759  1.00 42.53           C  
ATOM   2466  CZ  PHE B 159     -11.280   9.262  -3.486  1.00 44.91           C  
ATOM   2467  N   GLN B 160      -7.160  10.767  -0.019  1.00 33.07           N  
ATOM   2468  CA  GLN B 160      -7.143   9.823   1.101  1.00 35.34           C  
ATOM   2469  C   GLN B 160      -7.412  10.512   2.446  1.00 39.76           C  
ATOM   2470  O   GLN B 160      -8.183  10.015   3.251  1.00 31.09           O  
ATOM   2471  CB  GLN B 160      -5.801   9.087   1.165  1.00 32.84           C  
ATOM   2472  CG  GLN B 160      -5.533   8.191  -0.027  1.00 45.42           C  
ATOM   2473  CD  GLN B 160      -4.179   7.513   0.033  1.00 47.81           C  
ATOM   2474  OE1 GLN B 160      -3.189   8.115   0.437  1.00 40.99           O  
ATOM   2475  NE2 GLN B 160      -4.132   6.250  -0.370  1.00 57.61           N  
ATOM   2476  N   SER B 161      -6.776  11.654   2.689  1.00 37.10           N  
ATOM   2477  CA  SER B 161      -7.080  12.411   3.889  1.00 33.66           C  
ATOM   2478  C   SER B 161      -8.545  12.804   3.959  1.00 37.64           C  
ATOM   2479  O   SER B 161      -9.155  12.728   5.018  1.00 37.15           O  
ATOM   2480  CB  SER B 161      -6.222  13.665   3.971  1.00 33.51           C  
ATOM   2481  OG  SER B 161      -6.728  14.535   4.955  1.00 35.10           O  
ATOM   2482  N   ARG B 162      -9.120  13.206   2.831  1.00 44.92           N  
ATOM   2483  CA  ARG B 162     -10.476  13.738   2.846  1.00 42.87           C  
ATOM   2484  C   ARG B 162     -11.580  12.706   2.653  1.00 38.43           C  
ATOM   2485  O   ARG B 162     -12.755  13.050   2.757  1.00 42.61           O  
ATOM   2486  CB  ARG B 162     -10.626  14.828   1.780  1.00 48.58           C  
ATOM   2487  CG  ARG B 162     -10.162  16.196   2.241  1.00 48.29           C  
ATOM   2488  CD  ARG B 162     -10.389  17.253   1.181  1.00 53.11           C  
ATOM   2489  NE  ARG B 162     -11.771  17.732   1.112  1.00 56.64           N  
ATOM   2490  CZ  ARG B 162     -12.313  18.589   1.976  1.00 56.38           C  
ATOM   2491  NH1 ARG B 162     -11.606  19.052   2.998  1.00 56.04           N  
ATOM   2492  NH2 ARG B 162     -13.569  18.979   1.827  1.00 52.19           N  
ATOM   2493  N   HIS B 163     -11.238  11.450   2.378  1.00 38.84           N  
ATOM   2494  CA  HIS B 163     -12.299  10.482   2.069  1.00 46.16           C  
ATOM   2495  C   HIS B 163     -12.122   9.092   2.653  1.00 40.09           C  
ATOM   2496  O   HIS B 163     -13.065   8.305   2.630  1.00 37.06           O  
ATOM   2497  CB  HIS B 163     -12.463  10.326   0.550  1.00 44.58           C  
ATOM   2498  CG  HIS B 163     -12.907  11.572  -0.144  1.00 50.37           C  
ATOM   2499  ND1 HIS B 163     -12.227  12.101  -1.219  1.00 52.80           N  
ATOM   2500  CD2 HIS B 163     -13.957  12.395   0.081  1.00 62.64           C  
ATOM   2501  CE1 HIS B 163     -12.840  13.199  -1.627  1.00 67.11           C  
ATOM   2502  NE2 HIS B 163     -13.891  13.401  -0.853  1.00 71.99           N  
ATOM   2503  N   LEU B 164     -10.932   8.764   3.150  1.00 32.93           N  
ATOM   2504  CA  LEU B 164     -10.645   7.357   3.441  1.00 35.12           C  
ATOM   2505  C   LEU B 164     -10.127   7.095   4.856  1.00 45.16           C  
ATOM   2506  O   LEU B 164      -9.358   7.882   5.420  1.00 43.85           O  
ATOM   2507  CB  LEU B 164      -9.629   6.797   2.421  1.00 36.81           C  
ATOM   2508  CG  LEU B 164      -9.951   6.847   0.921  1.00 39.55           C  
ATOM   2509  CD1 LEU B 164      -8.892   6.096   0.134  1.00 40.61           C  
ATOM   2510  CD2 LEU B 164     -11.353   6.303   0.621  1.00 38.25           C  
ATOM   2511  N   ALA B 165     -10.535   5.962   5.417  1.00 43.26           N  
ATOM   2512  CA  ALA B 165     -10.016   5.543   6.706  1.00 45.00           C  
ATOM   2513  C   ALA B 165      -9.208   4.263   6.548  1.00 45.65           C  
ATOM   2514  O   ALA B 165      -9.426   3.498   5.611  1.00 45.78           O  
ATOM   2515  CB  ALA B 165     -11.146   5.345   7.697  1.00 49.54           C  
ATOM   2516  N   CYS B 166      -8.279   4.030   7.468  1.00 41.83           N  
ATOM   2517  CA  CYS B 166      -7.455   2.831   7.421  1.00 36.75           C  
ATOM   2518  C   CYS B 166      -8.000   1.812   8.406  1.00 44.04           C  
ATOM   2519  O   CYS B 166      -7.707   1.875   9.593  1.00 48.68           O  
ATOM   2520  CB  CYS B 166      -5.995   3.163   7.732  1.00 39.69           C  
ATOM   2521  SG  CYS B 166      -4.846   1.806   7.478  1.00 65.51           S  
ATOM   2522  N   LEU B 167      -8.784   0.869   7.884  1.00 51.40           N  
ATOM   2523  CA  LEU B 167      -9.577  -0.066   8.675  1.00 41.86           C  
ATOM   2524  C   LEU B 167      -9.217  -1.524   8.420  1.00 53.34           C  
ATOM   2525  O   LEU B 167      -8.739  -1.871   7.338  1.00 53.50           O  
ATOM   2526  CB  LEU B 167     -11.050   0.146   8.375  1.00 38.54           C  
ATOM   2527  CG  LEU B 167     -11.483   1.590   8.580  1.00 41.54           C  
ATOM   2528  CD1 LEU B 167     -12.962   1.757   8.254  1.00 38.85           C  
ATOM   2529  CD2 LEU B 167     -11.153   2.026  10.006  1.00 40.10           C  
ATOM   2530  N   PRO B 168      -9.443  -2.391   9.423  1.00 56.61           N  
ATOM   2531  CA  PRO B 168      -9.140  -3.814   9.207  1.00 51.65           C  
ATOM   2532  C   PRO B 168     -10.134  -4.498   8.289  1.00 51.76           C  
ATOM   2533  O   PRO B 168     -11.326  -4.248   8.417  1.00 55.95           O  
ATOM   2534  CB  PRO B 168      -9.216  -4.408  10.616  1.00 46.99           C  
ATOM   2535  CG  PRO B 168     -10.020  -3.412  11.412  1.00 46.58           C  
ATOM   2536  CD  PRO B 168      -9.760  -2.085  10.834  1.00 41.86           C  
ATOM   2537  N   ARG B 169      -9.648  -5.328   7.368  1.00 57.23           N  
ATOM   2538  CA  ARG B 169     -10.519  -6.169   6.546  1.00 55.37           C  
ATOM   2539  C   ARG B 169     -10.548  -7.543   7.185  1.00 59.42           C  
ATOM   2540  O   ARG B 169     -11.514  -8.299   7.032  1.00 56.11           O  
ATOM   2541  CB  ARG B 169     -10.034  -6.272   5.096  1.00 43.57           C  
ATOM   2542  CG  ARG B 169     -10.035  -4.966   4.324  1.00 53.02           C  
ATOM   2543  CD  ARG B 169     -11.336  -4.727   3.536  1.00 64.30           C  
ATOM   2544  NE  ARG B 169     -11.194  -3.606   2.598  1.00 67.30           N  
ATOM   2545  CZ  ARG B 169     -12.171  -3.101   1.842  1.00 65.00           C  
ATOM   2546  NH1 ARG B 169     -13.396  -3.608   1.894  1.00 63.22           N  
ATOM   2547  NH2 ARG B 169     -11.915  -2.081   1.023  1.00 63.73           N  
ATOM   2548  N   GLU B 170      -9.464  -7.842   7.899  1.00 61.46           N  
ATOM   2549  CA  GLU B 170      -9.278  -9.105   8.606  1.00 66.87           C  
ATOM   2550  C   GLU B 170      -8.036  -8.959   9.471  1.00 64.38           C  
ATOM   2551  O   GLU B 170      -7.293  -7.996   9.303  1.00 68.98           O  
ATOM   2552  CB  GLU B 170      -9.137 -10.278   7.626  1.00 70.92           C  
ATOM   2553  CG  GLU B 170      -7.760 -10.389   6.994  1.00 70.54           C  
ATOM   2554  CD  GLU B 170      -7.449 -11.815   6.585  1.00 77.45           C  
ATOM   2555  OE1 GLU B 170      -8.380 -12.654   6.641  1.00 83.73           O  
ATOM   2556  OE2 GLU B 170      -6.283 -12.099   6.219  1.00 70.76           O  
ATOM   2557  N   PRO B 171      -7.812  -9.889  10.413  1.00 71.40           N  
ATOM   2558  CA  PRO B 171      -6.621  -9.770  11.267  1.00 72.45           C  
ATOM   2559  C   PRO B 171      -5.307  -9.786  10.504  1.00 68.25           C  
ATOM   2560  O   PRO B 171      -5.114 -10.636   9.631  1.00 69.20           O  
ATOM   2561  CB  PRO B 171      -6.726 -10.990  12.179  1.00 62.73           C  
ATOM   2562  CG  PRO B 171      -8.186 -11.193  12.302  1.00 69.64           C  
ATOM   2563  CD  PRO B 171      -8.744 -10.903  10.933  1.00 73.02           C  
ATOM   2564  N   GLY B 172      -4.428  -8.841  10.845  1.00 57.32           N  
ATOM   2565  CA  GLY B 172      -3.132  -8.706  10.206  1.00 50.50           C  
ATOM   2566  C   GLY B 172      -3.218  -7.839   8.964  1.00 53.69           C  
ATOM   2567  O   GLY B 172      -2.205  -7.495   8.355  1.00 57.70           O  
ATOM   2568  N   LEU B 173      -4.439  -7.461   8.599  1.00 54.92           N  
ATOM   2569  CA  LEU B 173      -4.669  -6.767   7.345  1.00 52.66           C  
ATOM   2570  C   LEU B 173      -5.526  -5.518   7.468  1.00 57.67           C  
ATOM   2571  O   LEU B 173      -6.691  -5.587   7.871  1.00 62.01           O  
ATOM   2572  CB  LEU B 173      -5.332  -7.700   6.347  1.00 50.72           C  
ATOM   2573  CG  LEU B 173      -5.627  -7.024   5.015  1.00 45.41           C  
ATOM   2574  CD1 LEU B 173      -4.326  -6.541   4.416  1.00 40.45           C  
ATOM   2575  CD2 LEU B 173      -6.327  -7.999   4.094  1.00 47.06           C  
ATOM   2576  N   CYS B 174      -4.949  -4.385   7.080  1.00 53.00           N  
ATOM   2577  CA  CYS B 174      -5.713  -3.149   6.975  1.00 51.74           C  
ATOM   2578  C   CYS B 174      -5.616  -2.560   5.555  1.00 46.27           C  
ATOM   2579  O   CYS B 174      -4.600  -2.703   4.870  1.00 40.52           O  
ATOM   2580  CB  CYS B 174      -5.234  -2.136   8.021  1.00 46.26           C  
ATOM   2581  SG  CYS B 174      -5.521  -2.666   9.726  1.00 65.56           S  
ATOM   2582  N   THR B 175      -6.694  -1.925   5.107  1.00 42.58           N  
ATOM   2583  CA  THR B 175      -6.693  -1.213   3.834  1.00 50.70           C  
ATOM   2584  C   THR B 175      -7.514   0.056   3.950  1.00 54.63           C  
ATOM   2585  O   THR B 175      -8.385   0.173   4.823  1.00 57.67           O  
ATOM   2586  CB  THR B 175      -7.275  -2.055   2.656  1.00 53.03           C  
ATOM   2587  OG1 THR B 175      -8.594  -2.511   2.991  1.00 52.97           O  
ATOM   2588  CG2 THR B 175      -6.369  -3.247   2.294  1.00 50.51           C  
ATOM   2589  N   TRP B 176      -7.224   0.996   3.056  1.00 49.01           N  
ATOM   2590  CA  TRP B 176      -8.039   2.183   2.857  1.00 38.68           C  
ATOM   2591  C   TRP B 176      -9.485   1.839   2.499  1.00 35.13           C  
ATOM   2592  O   TRP B 176      -9.725   1.081   1.566  1.00 51.71           O  
ATOM   2593  CB  TRP B 176      -7.442   3.046   1.747  1.00 34.47           C  
ATOM   2594  CG  TRP B 176      -6.166   3.720   2.070  1.00 39.45           C  
ATOM   2595  CD1 TRP B 176      -4.966   3.523   1.464  1.00 44.29           C  
ATOM   2596  CD2 TRP B 176      -5.959   4.743   3.055  1.00 49.03           C  
ATOM   2597  NE1 TRP B 176      -4.018   4.354   2.014  1.00 48.27           N  
ATOM   2598  CE2 TRP B 176      -4.604   5.110   2.996  1.00 48.90           C  
ATOM   2599  CE3 TRP B 176      -6.790   5.381   3.986  1.00 52.33           C  
ATOM   2600  CZ2 TRP B 176      -4.055   6.082   3.835  1.00 41.88           C  
ATOM   2601  CZ3 TRP B 176      -6.243   6.353   4.815  1.00 43.44           C  
ATOM   2602  CH2 TRP B 176      -4.888   6.688   4.733  1.00 39.33           C  
ATOM   2603  N   GLN B 177     -10.444   2.404   3.228  1.00 43.60           N  
ATOM   2604  CA  GLN B 177     -11.870   2.219   2.916  1.00 51.03           C  
ATOM   2605  C   GLN B 177     -12.608   3.554   2.906  1.00 48.27           C  
ATOM   2606  O   GLN B 177     -12.142   4.553   3.470  1.00 47.24           O  
ATOM   2607  CB  GLN B 177     -12.542   1.256   3.909  1.00 46.32           C  
ATOM   2608  CG  GLN B 177     -11.735  -0.024   4.143  1.00 51.52           C  
ATOM   2609  CD  GLN B 177     -12.460  -1.070   4.977  1.00 57.15           C  
ATOM   2610  OE1 GLN B 177     -13.686  -1.042   5.120  1.00 67.14           O  
ATOM   2611  NE2 GLN B 177     -11.697  -2.010   5.526  1.00 50.36           N  
ATOM   2612  N   SER B 178     -13.765   3.547   2.257  1.00 51.08           N  
ATOM   2613  CA  SER B 178     -14.592   4.733   2.080  1.00 59.59           C  
ATOM   2614  C   SER B 178     -15.684   4.841   3.155  1.00 64.28           C  
ATOM   2615  O   SER B 178     -16.364   3.860   3.473  1.00 69.03           O  
ATOM   2616  CB  SER B 178     -15.219   4.726   0.678  1.00 64.20           C  
ATOM   2617  OG  SER B 178     -15.857   5.962   0.390  1.00 72.41           O  
ATOM   2618  N   LEU B 179     -15.850   6.044   3.701  1.00 64.67           N  
ATOM   2619  CA  LEU B 179     -16.831   6.298   4.749  1.00 74.86           C  
ATOM   2620  C   LEU B 179     -18.181   6.751   4.184  1.00 80.59           C  
ATOM   2621  O   LEU B 179     -18.796   6.052   3.367  1.00 85.48           O  
ATOM   2622  CB  LEU B 179     -16.301   7.347   5.720  1.00 78.27           C  
ATOM   2623  CG  LEU B 179     -15.021   7.062   6.516  1.00 74.50           C  
ATOM   2624  CD1 LEU B 179     -13.780   7.196   5.672  1.00 75.43           C  
ATOM   2625  CD2 LEU B 179     -14.931   7.999   7.690  1.00 66.10           C  
TER    2626      LEU B 179                                                      
HETATM 2627 CA    CA A 301       8.838  14.637  15.097  1.00 47.42          CA  
HETATM 2628 CA    CA A 302      17.658   9.285  13.365  1.00 74.88          CA  
HETATM 2629 ZN    ZN A 303      14.781  22.523  20.708  1.00 50.31          ZN  
HETATM 2630 ZN    ZN A 304       9.331  27.184  10.494  1.00 36.61          ZN  
HETATM 2631 CA    CA A 305      23.111  31.304  19.392  1.00 48.78          CA  
HETATM 2632  O   HOH A 401      21.815  44.900   7.851  1.00 43.57           O  
HETATM 2633  O   HOH A 402      10.878  13.637   1.151  1.00 43.91           O  
HETATM 2634  O   HOH A 403      11.756  12.991  19.007  1.00 37.81           O  
HETATM 2635  O   HOH A 404       5.767  42.614  19.427  1.00 51.46           O  
HETATM 2636  O   HOH A 405      20.269  16.637   2.690  1.00 50.79           O  
HETATM 2637  O   HOH A 406      24.627  29.926  20.809  1.00 54.39           O  
HETATM 2638  O   HOH A 407      13.079  20.180  24.902  1.00 29.72           O  
HETATM 2639  O   HOH A 408      19.906  30.912  -3.618  1.00 32.00           O  
HETATM 2640  O   HOH A 409      12.759  34.221  12.960  1.00 39.81           O  
HETATM 2641  O   HOH A 410       9.587   9.949  29.124  1.00 61.08           O  
HETATM 2642  O   HOH A 411      25.274  34.204  19.606  1.00 42.53           O  
HETATM 2643  O   HOH A 412      23.263  43.779  10.088  1.00 63.47           O  
HETATM 2644  O   HOH A 413      28.231  37.530   0.212  1.00 47.40           O  
HETATM 2645  O   HOH A 414      26.119  34.241  22.311  1.00 35.95           O  
HETATM 2646  O   HOH A 415       6.505  36.537   5.018  1.00 35.07           O  
HETATM 2647  O   HOH A 416      18.344  31.895  -5.361  1.00 37.67           O  
HETATM 2648  O   HOH A 417      31.703  41.385   5.019  1.00 55.75           O  
HETATM 2649  O   HOH A 418      -0.735  28.278   6.564  1.00 54.69           O  
HETATM 2650  O   HOH A 419      16.106   9.743  25.849  1.00 50.27           O  
HETATM 2651  O   HOH A 420      32.973  17.239  16.005  1.00 54.37           O  
HETATM 2652  O   HOH A 421      32.813  16.048  17.954  1.00 81.70           O  
HETATM 2653  O   HOH B 201     -18.201  34.006  12.917  1.00 65.66           O  
HETATM 2654  O   HOH B 202     -22.443  23.462  18.401  1.00 70.47           O  
HETATM 2655  O   HOH B 203      -0.702  -1.343  12.859  1.00 33.92           O  
HETATM 2656  O   HOH B 204     -19.242  21.340   6.282  1.00 40.03           O  
HETATM 2657  O   HOH B 205     -10.386  10.495   6.448  1.00 37.87           O  
HETATM 2658  O   HOH B 206       8.619  23.031  19.026  1.00 47.98           O  
HETATM 2659  O   HOH B 207      -5.093   4.843  12.856  1.00 43.31           O  
HETATM 2660  O   HOH B 208     -19.528  22.046  27.559  1.00 74.78           O  
HETATM 2661  O   HOH B 209      -2.412   6.147  12.162  1.00 34.07           O  
HETATM 2662  O   HOH B 210      -1.182  15.257  18.825  1.00 48.70           O  
HETATM 2663  O   HOH B 211       2.209  22.289  22.621  1.00 49.92           O  
HETATM 2664  O   HOH B 212      -0.362  10.283   9.435  1.00 30.46           O  
HETATM 2665  O   HOH B 213     -14.471  -1.262  -0.138  1.00 51.46           O  
HETATM 2666  O   HOH B 214       0.011  28.762  13.246  1.00 45.73           O  
HETATM 2667  O   HOH B 215      -2.155   3.992  -1.369  1.00 69.19           O  
HETATM 2668  O   HOH B 216      -2.039  -2.278   3.002  1.00 61.03           O  
HETATM 2669  O   HOH B 217       2.989  12.732  10.662  1.00 45.85           O  
HETATM 2670  O   HOH B 218     -15.985   9.137   1.543  1.00 51.28           O  
HETATM 2671  O   HOH B 219      -3.708   7.786  22.629  1.00 44.18           O  
HETATM 2672  O   HOH B 220      -5.972   0.000   0.000  0.50 57.87           O  
HETATM 2673  O   HOH B 221      -3.928  -0.086   2.093  1.00 50.61           O  
HETATM 2674  O   HOH B 222      12.986  -3.458   8.932  1.00 53.39           O  
HETATM 2675  O   HOH B 223      -1.411   7.567  21.672  1.00 68.05           O  
HETATM 2676  O   HOH B 224     -12.649  -1.917  18.360  1.00 40.48           O  
HETATM 2677  O   HOH B 225       0.152  27.628   8.879  1.00 42.18           O  
CONECT  180 2628                                                                
CONECT  181 2628                                                                
CONECT  445 2631                                                                
CONECT  532 2629                                                                
CONECT  544 2629                                                                
CONECT  592 2627                                                                
CONECT  597 2627                                                                
CONECT  608 2627                                                                
CONECT  620 2627                                                                
CONECT  646 2629                                                                
CONECT  690 2631                                                                
CONECT  702 2631                                                                
CONECT  717 2631                                                                
CONECT  730 2629                                                                
CONECT  752 2627                                                                
CONECT  756 2628                                                                
CONECT  759 2628                                                                
CONECT  772 2628                                                                
CONECT  777 2627                                                                
CONECT  911 2630                                                                
CONECT  942 2630                                                                
CONECT  989 2630                                                                
CONECT 1274 2630                                                                
CONECT 1277 2630                                                                
CONECT 1279 1791                                                                
CONECT 1292 2020                                                                
CONECT 1368 2206                                                                
CONECT 1791 1279                                                                
CONECT 2020 1292                                                                
CONECT 2206 1368                                                                
CONECT 2230 2581                                                                
CONECT 2268 2302                                                                
CONECT 2302 2268                                                                
CONECT 2357 2521                                                                
CONECT 2521 2357                                                                
CONECT 2581 2230                                                                
CONECT 2627  592  597  608  620                                                 
CONECT 2627  752  777                                                           
CONECT 2628  180  181  756  759                                                 
CONECT 2628  772                                                                
CONECT 2629  532  544  646  730                                                 
CONECT 2630  911  942  989 1274                                                 
CONECT 2630 1277                                                                
CONECT 2631  445  690  702  717                                                 
CONECT 2631 2637                                                                
CONECT 2637 2631                                                                
MASTER      506    0    5   10   19    0    7    6 2675    2   46   28          
END                                                                             
