CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***  BLOOD CLOTTING 03-MAR-09 3GHG  ***

elNémo ID: 210727062943118893

Job options:

ID        	=	 210727062943118893
JOBID     	=	 BLOOD CLOTTING 03-MAR-09 3GHG
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    BLOOD CLOTTING                          03-MAR-09   3GHG              
TITLE     CRYSTAL STRUCTURE OF HUMAN FIBRINOGEN                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBRINOGEN ALPHA CHAIN;                                    
COMPND   3 CHAIN: A, D, G, J;                                                   
COMPND   4 FRAGMENT: MATURE CHAIN;                                              
COMPND   5 SYNONYM: FIBRINOPEPTIDE A;                                           
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: FIBRINOGEN BETA CHAIN;                                     
COMPND   8 CHAIN: B, E, H, K;                                                   
COMPND   9 FRAGMENT: MATURE CHAIN;                                              
COMPND  10 SYNONYM: FIBRINOPEPTIDE B;                                           
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: FIBRINOGEN GAMMA CHAIN;                                    
COMPND  13 CHAIN: C, F, I, L;                                                   
COMPND  14 FRAGMENT: MATURE CHAIN;                                              
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: A KNOB;                                                    
COMPND  17 CHAIN: M, N, Q, R;                                                   
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 5;                                                           
COMPND  20 MOLECULE: B KNOB;                                                    
COMPND  21 CHAIN: O, P, S, T;                                                   
COMPND  22 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: BLOOD PLASMA;                                                
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 TISSUE: BLOOD PLASMA;                                                
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 TISSUE: BLOOD PLASMA;                                                
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 SYNTHETIC: YES;                                                      
SOURCE  18 MOL_ID: 5;                                                           
SOURCE  19 SYNTHETIC: YES                                                       
KEYWDS    TRIPLE-STRANDED COILED COIL, BETA SHEETS, ALPHA HELICES, AMYLOID,     
KEYWDS   2 AMYLOIDOSIS, BLOOD COAGULATION, DISEASE MUTATION, GLYCOPROTEIN,      
KEYWDS   3 PHOSPHOPROTEIN, SECRETED, PYRROLIDONE CARBOXYLIC ACID, SULFATION,    
KEYWDS   4 BLOOD CLOTTING                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.F.DOOLITTLE,J.M.KOLLMAN,M.R.SAWAYA,L.PANDI,M.RILEY                  
REVDAT   2   13-JUL-11 3GHG    1       VERSN                                    
REVDAT   1   19-MAY-09 3GHG    0                                                
JRNL        AUTH   J.M.KOLLMAN,L.PANDI,M.R.SAWAYA,M.RILEY,R.F.DOOLITTLE         
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN FIBRINOGEN.                       
JRNL        REF    BIOCHEMISTRY                  V.  48  3877 2009              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   19296670                                                     
JRNL        DOI    10.1021/BI802205G                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0061                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 116461                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.255                           
REMARK   3   R VALUE            (WORKING SET) : 0.252                           
REMARK   3   FREE R VALUE                     : 0.309                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5820                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 400                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2640                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 19                           
REMARK   3   BIN FREE R VALUE                    : 0.3230                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 31283                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 550                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 80.58                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.25000                                             
REMARK   3    B22 (A**2) : 2.38000                                              
REMARK   3    B33 (A**2) : -0.03000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.60000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.489         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.338         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 36.137        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.883                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 32743 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A): 22470 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 44076 ; 1.316 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 54494 ; 1.948 ; 3.004       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3872 ; 7.329 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1652 ;36.846 ;24.909       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  5702 ;19.466 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   190 ;15.141 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4664 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 35993 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  6437 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 22321 ; 3.904 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  7924 ; 1.088 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31037 ; 5.184 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 13687 ; 3.564 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 13012 ; 5.246 ; 3.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : B E H K                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B    202       B     458      5                      
REMARK   3           1     E    202       E     458      5                      
REMARK   3           1     H    202       H     458      5                      
REMARK   3           1     K    202       K     458      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1501 ;  0.32 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1501 ;  0.34 ;  0.00           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1501 ;  0.28 ;  0.00           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1501 ;  0.33 ;  0.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   2044 ;  0.54 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   2044 ;  0.55 ;  0.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   2044 ;  0.48 ;  0.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   2044 ;  0.61 ;  0.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1501 ;  7.23 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1501 ;  4.36 ;  0.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1501 ;  2.60 ;  0.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1501 ;  3.80 ;  0.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):   2044 ;  6.44 ; 10.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):   2044 ;  3.68 ;  0.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):   2044 ;  2.49 ;  0.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):   2044 ;  3.22 ;  0.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 24                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    27        A   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.5933  16.9807 -42.7224              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3693 T22:   0.3628                                     
REMARK   3      T33:   0.3647 T12:  -0.0013                                     
REMARK   3      T13:  -0.0018 T23:  -0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7182 L22:   0.0231                                     
REMARK   3      L33:   0.6820 L12:   0.1889                                     
REMARK   3      L13:  -1.6373 L23:   0.0249                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0924 S12:   1.0895 S13:  -0.0408                       
REMARK   3      S21:   0.0232 S22:   0.0285 S23:   0.0321                       
REMARK   3      S31:  -0.0945 S32:  -0.1127 S33:  -0.1209                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   151        A   200                          
REMARK   3    ORIGIN FOR THE GROUP (A): -80.9758   8.9859 -18.0775              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3359 T22:   0.3770                                     
REMARK   3      T33:   0.2722 T12:   0.0175                                     
REMARK   3      T13:  -0.0369 T23:  -0.0664                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7865 L22:   1.1551                                     
REMARK   3      L33:   1.5880 L12:   2.0684                                     
REMARK   3      L13:  -2.5733 L23:  -0.4903                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1754 S12:   0.0880 S13:  -0.8523                       
REMARK   3      S21:  -0.0112 S22:   0.1297 S23:  -0.1644                       
REMARK   3      S31:  -0.0648 S32:   0.3118 S33:   0.0457                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    58        B   248                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.9951  11.4572 -27.6554              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2871 T22:   0.2800                                     
REMARK   3      T33:   0.2822 T12:  -0.0007                                     
REMARK   3      T13:  -0.0019 T23:  -0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0467 L22:   0.0275                                     
REMARK   3      L33:   0.1385 L12:  -0.0583                                     
REMARK   3      L13:  -0.2974 L23:   0.0466                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1206 S12:   0.3192 S13:   0.2278                       
REMARK   3      S21:  -0.0621 S22:   0.0043 S23:  -0.0570                       
REMARK   3      S31:  -0.0773 S32:   0.0495 S33:  -0.1249                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   249        B   458                          
REMARK   3    ORIGIN FOR THE GROUP (A): -95.1149   4.7892   7.4249              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0593 T22:   0.0355                                     
REMARK   3      T33:   0.1597 T12:   0.0204                                     
REMARK   3      T13:  -0.0116 T23:  -0.0169                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1582 L22:   0.8196                                     
REMARK   3      L33:   1.9687 L12:  -0.0805                                     
REMARK   3      L13:   0.3110 L23:  -0.0169                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0969 S12:  -0.0143 S13:  -0.0798                       
REMARK   3      S21:  -0.0733 S22:  -0.0051 S23:   0.0004                       
REMARK   3      S31:  -0.0308 S32:   0.1606 S33:  -0.0918                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    14        C   162                          
REMARK   3    ORIGIN FOR THE GROUP (A): -41.8673  16.8978 -32.0731              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2799 T22:   0.2567                                     
REMARK   3      T33:   0.2736 T12:   0.0014                                     
REMARK   3      T13:  -0.0014 T23:   0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8203 L22:   0.0119                                     
REMARK   3      L33:   0.4808 L12:   0.1058                                     
REMARK   3      L13:  -1.1907 L23:  -0.0061                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0359 S12:   0.5121 S13:   0.0137                       
REMARK   3      S21:  -0.0326 S22:   0.0499 S23:  -0.0316                       
REMARK   3      S31:   0.0141 S32:   0.0178 S33:  -0.0140                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   163        C   394                          
REMARK   3    ORIGIN FOR THE GROUP (A):-140.8027  -8.0725  10.0963              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0987 T22:  -0.0831                                     
REMARK   3      T33:   0.0494 T12:   0.0080                                     
REMARK   3      T13:  -0.0201 T23:   0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7064 L22:   1.8386                                     
REMARK   3      L33:   1.5104 L12:   0.4767                                     
REMARK   3      L13:  -0.0053 L23:  -0.0389                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0166 S12:  -0.1049 S13:  -0.0775                       
REMARK   3      S21:   0.0158 S22:  -0.0402 S23:   0.1001                       
REMARK   3      S31:   0.1172 S32:  -0.0807 S33:   0.0236                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    27        D   149                          
REMARK   3    ORIGIN FOR THE GROUP (A): 120.1930  12.6991 -69.1885              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3727 T22:   0.3694                                     
REMARK   3      T33:   0.3698 T12:   0.0011                                     
REMARK   3      T13:  -0.0013 T23:   0.0024                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4451 L22:   0.0540                                     
REMARK   3      L33:   0.9146 L12:  -0.0367                                     
REMARK   3      L13:  -2.0375 L23:   0.1486                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3899 S12:  -1.3422 S13:   0.7428                       
REMARK   3      S21:   0.0209 S22:  -0.1035 S23:  -0.0177                       
REMARK   3      S31:  -0.1278 S32:   0.3249 S33:  -0.2864                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   150        D   200                          
REMARK   3    ORIGIN FOR THE GROUP (A): 195.2027   0.0681 -91.2298              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3889 T22:   0.4758                                     
REMARK   3      T33:   0.1887 T12:  -0.0355                                     
REMARK   3      T13:  -0.0112 T23:  -0.0744                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4547 L22:   0.9806                                     
REMARK   3      L33:   0.5384 L12:   0.5357                                     
REMARK   3      L13:  -1.5605 L23:   0.1261                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0983 S12:  -0.6461 S13:  -0.1385                       
REMARK   3      S21:   0.0082 S22:  -0.1319 S23:   0.1073                       
REMARK   3      S31:   0.0910 S32:  -0.0574 S33:   0.0336                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E    58        E   248                          
REMARK   3    ORIGIN FOR THE GROUP (A): 158.9648   5.5330 -83.0682              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2923 T22:   0.2923                                     
REMARK   3      T33:   0.2923 T12:   0.0000                                     
REMARK   3      T13:   0.0000 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9986 L22:   0.0838                                     
REMARK   3      L33:   0.6283 L12:  -0.4176                                     
REMARK   3      L13:  -1.2043 L23:   0.2287                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0086 S12:  -0.3888 S13:   0.4095                       
REMARK   3      S21:   0.0474 S22:   0.1005 S23:  -0.0125                       
REMARK   3      S31:   0.0257 S32:   0.0810 S33:  -0.0918                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   249        E   458                          
REMARK   3    ORIGIN FOR THE GROUP (A): 210.1003  -7.6081-115.5453              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2237 T22:   0.3697                                     
REMARK   3      T33:   0.1478 T12:   0.0492                                     
REMARK   3      T13:  -0.0120 T23:  -0.0622                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5467 L22:   0.8370                                     
REMARK   3      L33:   2.0264 L12:   0.8105                                     
REMARK   3      L13:  -0.1852 L23:   0.0511                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0094 S12:  -0.3076 S13:   0.1271                       
REMARK   3      S21:   0.1788 S22:   0.0215 S23:  -0.0207                       
REMARK   3      S31:  -0.0500 S32:  -0.0066 S33:  -0.0121                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F    14        F   287                          
REMARK   3    ORIGIN FOR THE GROUP (A): 200.0542   2.5512 -97.3855              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2433 T22:   0.2423                                     
REMARK   3      T33:   0.2426 T12:  -0.0003                                     
REMARK   3      T13:  -0.0003 T23:   0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8461 L22:   0.2410                                     
REMARK   3      L33:   0.2706 L12:  -0.6323                                     
REMARK   3      L13:  -0.3743 L23:   0.1972                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1265 S12:  -0.7034 S13:   0.1482                       
REMARK   3      S21:   0.0614 S22:   0.1835 S23:  -0.0213                       
REMARK   3      S31:   0.0090 S32:   0.1736 S33:  -0.0570                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   288        F   395                          
REMARK   3    ORIGIN FOR THE GROUP (A): 261.6536 -21.3203-114.8281              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1011 T22:   0.4755                                     
REMARK   3      T33:   0.1276 T12:   0.0166                                     
REMARK   3      T13:  -0.0199 T23:   0.0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5754 L22:   1.7523                                     
REMARK   3      L33:   3.0019 L12:  -1.0478                                     
REMARK   3      L13:  -0.1033 L23:   1.1319                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1407 S12:  -0.8015 S13:  -0.0439                       
REMARK   3      S21:   0.1379 S22:  -0.0531 S23:  -0.3393                       
REMARK   3      S31:   0.4814 S32:   0.1616 S33:  -0.0876                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G    27        G   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.4922 -30.5304 -82.3447              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3749 T22:   0.3673                                     
REMARK   3      T33:   0.3673 T12:  -0.0026                                     
REMARK   3      T13:  -0.0032 T23:  -0.0071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0288 L22:   0.0086                                     
REMARK   3      L33:   0.6228 L12:  -0.2008                                     
REMARK   3      L13:  -1.5698 L23:   0.0727                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2909 S12:   0.7124 S13:   0.3276                       
REMARK   3      S21:   0.0361 S22:  -0.0709 S23:  -0.0489                       
REMARK   3      S31:  -0.0777 S32:  -0.0719 S33:  -0.2200                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   151        G   200                          
REMARK   3    ORIGIN FOR THE GROUP (A): -46.4784 -33.9538 -60.1915              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3014 T22:   0.4720                                     
REMARK   3      T33:   0.1510 T12:   0.0470                                     
REMARK   3      T13:   0.0183 T23:   0.0861                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9470 L22:   0.7421                                     
REMARK   3      L33:   0.6994 L12:   0.0247                                     
REMARK   3      L13:  -2.0906 L23:  -0.2620                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0692 S12:   0.5117 S13:  -0.2408                       
REMARK   3      S21:   0.0019 S22:  -0.1445 S23:  -0.0878                       
REMARK   3      S31:   0.1776 S32:   0.0252 S33:   0.0753                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H    58        H   248                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.2846 -33.9297 -68.6299              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2803 T22:   0.2752                                     
REMARK   3      T33:   0.2749 T12:  -0.0011                                     
REMARK   3      T13:  -0.0022 T23:  -0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8690 L22:   0.0279                                     
REMARK   3      L33:   0.3298 L12:   0.2268                                     
REMARK   3      L13:  -0.5753 L23:  -0.0671                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0169 S12:   0.5202 S13:  -0.0312                       
REMARK   3      S21:  -0.0624 S22:   0.0456 S23:  -0.0710                       
REMARK   3      S31:  -0.0281 S32:  -0.0635 S33:  -0.0288                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   249        H   458                          
REMARK   3    ORIGIN FOR THE GROUP (A): -61.2503 -39.7074 -35.1182              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0787 T22:   0.2250                                     
REMARK   3      T33:   0.1266 T12:  -0.0358                                     
REMARK   3      T13:  -0.0028 T23:   0.0269                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3071 L22:   1.1901                                     
REMARK   3      L33:   1.5974 L12:  -0.3433                                     
REMARK   3      L13:   0.1537 L23:  -0.3343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0714 S12:   0.2679 S13:  -0.0638                       
REMARK   3      S21:  -0.1024 S22:   0.0156 S23:  -0.0145                       
REMARK   3      S31:  -0.0419 S32:   0.0049 S33:  -0.0870                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I     2        I   288                          
REMARK   3    ORIGIN FOR THE GROUP (A): -51.6922 -34.1001 -53.7264              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2562 T22:   0.2355                                     
REMARK   3      T33:   0.2451 T12:   0.0001                                     
REMARK   3      T13:  -0.0031 T23:  -0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8954 L22:   0.0659                                     
REMARK   3      L33:   0.3092 L12:   0.0804                                     
REMARK   3      L13:  -0.6155 L23:  -0.0452                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1464 S12:   0.3865 S13:   0.3538                       
REMARK   3      S21:  -0.0486 S22:   0.0120 S23:  -0.0411                       
REMARK   3      S31:  -0.0503 S32:  -0.0126 S33:  -0.1583                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I   289        I   395                          
REMARK   3    ORIGIN FOR THE GROUP (A):-112.5471 -53.4674 -35.4082              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1767 T22:   0.2463                                     
REMARK   3      T33:   0.1967 T12:   0.0072                                     
REMARK   3      T13:  -0.0505 T23:  -0.0779                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3322 L22:   2.5505                                     
REMARK   3      L33:   1.8533 L12:   0.7563                                     
REMARK   3      L13:   0.2443 L23:  -0.8672                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0434 S12:   0.5556 S13:  -0.2507                       
REMARK   3      S21:  -0.4183 S22:   0.0362 S23:   0.3437                       
REMARK   3      S31:   0.3324 S32:  -0.0472 S33:  -0.0796                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J    27        J   150                          
REMARK   3    ORIGIN FOR THE GROUP (A): 155.9658 -44.6791-105.8683              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3857 T22:   0.3749                                     
REMARK   3      T33:   0.3804 T12:   0.0009                                     
REMARK   3      T13:  -0.0018 T23:   0.0042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9760 L22:   0.0577                                     
REMARK   3      L33:   0.9590 L12:  -0.5281                                     
REMARK   3      L13:  -1.8992 L23:   0.2330                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3203 S12:  -1.2853 S13:   0.4235                       
REMARK   3      S21:  -0.1557 S22:  -0.0736 S23:   0.0198                       
REMARK   3      S31:  -0.0983 S32:   0.2024 S33:  -0.2467                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J   151        J   200                          
REMARK   3    ORIGIN FOR THE GROUP (A): 229.8177 -55.1282-132.0335              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3415 T22:   0.4541                                     
REMARK   3      T33:   0.1695 T12:  -0.0296                                     
REMARK   3      T13:  -0.0024 T23:  -0.0252                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2632 L22:   0.7172                                     
REMARK   3      L33:   0.9536 L12:  -0.1400                                     
REMARK   3      L13:  -2.1670 L23:   0.0291                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1512 S12:  -0.2898 S13:   0.0865                       
REMARK   3      S21:   0.0950 S22:  -0.0588 S23:   0.1005                       
REMARK   3      S31:  -0.0458 S32:  -0.1778 S33:  -0.0924                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K    58        K   249                          
REMARK   3    ORIGIN FOR THE GROUP (A): 194.4076 -50.7755-122.3018              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2733 T22:   0.2683                                     
REMARK   3      T33:   0.2712 T12:   0.0000                                     
REMARK   3      T13:  -0.0007 T23:   0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5471 L22:   0.0858                                     
REMARK   3      L33:   0.3522 L12:  -0.3568                                     
REMARK   3      L13:  -0.7964 L23:   0.1723                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0242 S12:  -0.5996 S13:   0.1783                       
REMARK   3      S21:   0.0443 S22:   0.0496 S23:   0.0465                       
REMARK   3      S31:   0.0079 S32:   0.1085 S33:  -0.0254                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K   250        K   458                          
REMARK   3    ORIGIN FOR THE GROUP (A): 243.8539 -58.4279-157.6609              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1773 T22:   0.2744                                     
REMARK   3      T33:   0.1064 T12:   0.0177                                     
REMARK   3      T13:   0.0246 T23:  -0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3524 L22:   0.9051                                     
REMARK   3      L33:   1.9651 L12:   0.1194                                     
REMARK   3      L13:   0.4874 L23:  -0.2333                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0089 S12:  -0.1718 S13:   0.0263                       
REMARK   3      S21:   0.1184 S22:   0.0610 S23:  -0.0251                       
REMARK   3      S31:  -0.0091 S32:  -0.1832 S33:  -0.0699                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     5        L   163                          
REMARK   3    ORIGIN FOR THE GROUP (A): 191.4011 -45.8424-117.4431              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3698 T22:   0.3619                                     
REMARK   3      T33:   0.3659 T12:  -0.0009                                     
REMARK   3      T13:  -0.0011 T23:  -0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9232 L22:   0.0233                                     
REMARK   3      L33:   1.0295 L12:  -0.2340                                     
REMARK   3      L13:  -2.0216 L23:   0.1453                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1538 S12:  -1.0116 S13:   0.4366                       
REMARK   3      S21:   0.0136 S22:   0.0235 S23:  -0.0006                       
REMARK   3      S31:  -0.0440 S32:   0.2291 S33:  -0.1773                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   164        L   395                          
REMARK   3    ORIGIN FOR THE GROUP (A): 289.7523 -71.3264-160.6678              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1067 T22:  -0.0116                                     
REMARK   3      T33:   0.1071 T12:  -0.0011                                     
REMARK   3      T13:   0.0065 T23:  -0.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0689 L22:   2.1931                                     
REMARK   3      L33:   2.0172 L12:  -0.4325                                     
REMARK   3      L13:   0.2619 L23:   0.0681                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0638 S12:   0.1007 S13:  -0.1198                       
REMARK   3      S21:  -0.0098 S22:  -0.0482 S23:  -0.1949                       
REMARK   3      S31:   0.2321 S32:   0.0386 S33:  -0.0155                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3GHG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB051864.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : SUPERBEND                          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 116461                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10200                            
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2% PEG 3350, 0.2 M TMAO, 75 MM NACL,     
REMARK 280  50 MM TRIS, 1 MM CACL2, 1 MM HPRPAM, 1 MM GHRPAM, 1 MM SODIUM       
REMARK 280  AZIDE, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       47.43300            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: DECAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, F, D, E, M, N, O, P          
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L, Q, R, S, T          
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     ASP A     7                                                      
REMARK 465     PHE A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     ARG A    16                                                      
REMARK 465     GLY A    17                                                      
REMARK 465     PRO A    18                                                      
REMARK 465     ARG A    19                                                      
REMARK 465     VAL A    20                                                      
REMARK 465     VAL A    21                                                      
REMARK 465     GLU A    22                                                      
REMARK 465     ARG A    23                                                      
REMARK 465     HIS A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     HIS A   201                                                      
REMARK 465     LEU A   202                                                      
REMARK 465     PRO A   203                                                      
REMARK 465     LEU A   204                                                      
REMARK 465     ILE A   205                                                      
REMARK 465     LYS A   206                                                      
REMARK 465     MET A   207                                                      
REMARK 465     LYS A   208                                                      
REMARK 465     PRO A   209                                                      
REMARK 465     VAL A   210                                                      
REMARK 465     PRO A   211                                                      
REMARK 465     ASP A   212                                                      
REMARK 465     LEU A   213                                                      
REMARK 465     VAL A   214                                                      
REMARK 465     PRO A   215                                                      
REMARK 465     GLY A   216                                                      
REMARK 465     ASN A   217                                                      
REMARK 465     PHE A   218                                                      
REMARK 465     LYS A   219                                                      
REMARK 465     SER A   220                                                      
REMARK 465     GLN A   221                                                      
REMARK 465     LEU A   222                                                      
REMARK 465     GLN A   223                                                      
REMARK 465     LYS A   224                                                      
REMARK 465     VAL A   225                                                      
REMARK 465     PRO A   226                                                      
REMARK 465     PRO A   227                                                      
REMARK 465     GLU A   228                                                      
REMARK 465     TRP A   229                                                      
REMARK 465     LYS A   230                                                      
REMARK 465     ALA A   231                                                      
REMARK 465     LEU A   232                                                      
REMARK 465     THR A   233                                                      
REMARK 465     ASP A   234                                                      
REMARK 465     MET A   235                                                      
REMARK 465     PRO A   236                                                      
REMARK 465     GLN A   237                                                      
REMARK 465     MET A   238                                                      
REMARK 465     ARG A   239                                                      
REMARK 465     MET A   240                                                      
REMARK 465     GLU A   241                                                      
REMARK 465     LEU A   242                                                      
REMARK 465     GLU A   243                                                      
REMARK 465     ARG A   244                                                      
REMARK 465     PRO A   245                                                      
REMARK 465     GLY A   246                                                      
REMARK 465     GLY A   247                                                      
REMARK 465     ASN A   248                                                      
REMARK 465     GLU A   249                                                      
REMARK 465     ILE A   250                                                      
REMARK 465     THR A   251                                                      
REMARK 465     ARG A   252                                                      
REMARK 465     GLY A   253                                                      
REMARK 465     GLY A   254                                                      
REMARK 465     SER A   255                                                      
REMARK 465     THR A   256                                                      
REMARK 465     SER A   257                                                      
REMARK 465     TYR A   258                                                      
REMARK 465     GLY A   259                                                      
REMARK 465     THR A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     SER A   262                                                      
REMARK 465     GLU A   263                                                      
REMARK 465     THR A   264                                                      
REMARK 465     GLU A   265                                                      
REMARK 465     SER A   266                                                      
REMARK 465     PRO A   267                                                      
REMARK 465     ARG A   268                                                      
REMARK 465     ASN A   269                                                      
REMARK 465     PRO A   270                                                      
REMARK 465     SER A   271                                                      
REMARK 465     SER A   272                                                      
REMARK 465     ALA A   273                                                      
REMARK 465     GLY A   274                                                      
REMARK 465     SER A   275                                                      
REMARK 465     TRP A   276                                                      
REMARK 465     ASN A   277                                                      
REMARK 465     SER A   278                                                      
REMARK 465     GLY A   279                                                      
REMARK 465     SER A   280                                                      
REMARK 465     SER A   281                                                      
REMARK 465     GLY A   282                                                      
REMARK 465     PRO A   283                                                      
REMARK 465     GLY A   284                                                      
REMARK 465     SER A   285                                                      
REMARK 465     THR A   286                                                      
REMARK 465     GLY A   287                                                      
REMARK 465     ASN A   288                                                      
REMARK 465     ARG A   289                                                      
REMARK 465     ASN A   290                                                      
REMARK 465     PRO A   291                                                      
REMARK 465     GLY A   292                                                      
REMARK 465     SER A   293                                                      
REMARK 465     SER A   294                                                      
REMARK 465     GLY A   295                                                      
REMARK 465     THR A   296                                                      
REMARK 465     GLY A   297                                                      
REMARK 465     GLY A   298                                                      
REMARK 465     THR A   299                                                      
REMARK 465     ALA A   300                                                      
REMARK 465     THR A   301                                                      
REMARK 465     TRP A   302                                                      
REMARK 465     LYS A   303                                                      
REMARK 465     PRO A   304                                                      
REMARK 465     GLY A   305                                                      
REMARK 465     SER A   306                                                      
REMARK 465     SER A   307                                                      
REMARK 465     GLY A   308                                                      
REMARK 465     PRO A   309                                                      
REMARK 465     GLY A   310                                                      
REMARK 465     SER A   311                                                      
REMARK 465     THR A   312                                                      
REMARK 465     GLY A   313                                                      
REMARK 465     SER A   314                                                      
REMARK 465     TRP A   315                                                      
REMARK 465     ASN A   316                                                      
REMARK 465     SER A   317                                                      
REMARK 465     GLY A   318                                                      
REMARK 465     SER A   319                                                      
REMARK 465     SER A   320                                                      
REMARK 465     GLY A   321                                                      
REMARK 465     THR A   322                                                      
REMARK 465     GLY A   323                                                      
REMARK 465     SER A   324                                                      
REMARK 465     THR A   325                                                      
REMARK 465     GLY A   326                                                      
REMARK 465     ASN A   327                                                      
REMARK 465     GLN A   328                                                      
REMARK 465     ASN A   329                                                      
REMARK 465     PRO A   330                                                      
REMARK 465     GLY A   331                                                      
REMARK 465     SER A   332                                                      
REMARK 465     PRO A   333                                                      
REMARK 465     ARG A   334                                                      
REMARK 465     PRO A   335                                                      
REMARK 465     GLY A   336                                                      
REMARK 465     SER A   337                                                      
REMARK 465     THR A   338                                                      
REMARK 465     GLY A   339                                                      
REMARK 465     THR A   340                                                      
REMARK 465     TRP A   341                                                      
REMARK 465     ASN A   342                                                      
REMARK 465     PRO A   343                                                      
REMARK 465     GLY A   344                                                      
REMARK 465     SER A   345                                                      
REMARK 465     SER A   346                                                      
REMARK 465     GLU A   347                                                      
REMARK 465     ARG A   348                                                      
REMARK 465     GLY A   349                                                      
REMARK 465     SER A   350                                                      
REMARK 465     ALA A   351                                                      
REMARK 465     GLY A   352                                                      
REMARK 465     HIS A   353                                                      
REMARK 465     TRP A   354                                                      
REMARK 465     THR A   355                                                      
REMARK 465     SER A   356                                                      
REMARK 465     GLU A   357                                                      
REMARK 465     SER A   358                                                      
REMARK 465     SER A   359                                                      
REMARK 465     VAL A   360                                                      
REMARK 465     SER A   361                                                      
REMARK 465     GLY A   362                                                      
REMARK 465     SER A   363                                                      
REMARK 465     THR A   364                                                      
REMARK 465     GLY A   365                                                      
REMARK 465     GLN A   366                                                      
REMARK 465     TRP A   367                                                      
REMARK 465     HIS A   368                                                      
REMARK 465     SER A   369                                                      
REMARK 465     GLU A   370                                                      
REMARK 465     SER A   371                                                      
REMARK 465     GLY A   372                                                      
REMARK 465     SER A   373                                                      
REMARK 465     PHE A   374                                                      
REMARK 465     ARG A   375                                                      
REMARK 465     PRO A   376                                                      
REMARK 465     ASP A   377                                                      
REMARK 465     SER A   378                                                      
REMARK 465     PRO A   379                                                      
REMARK 465     GLY A   380                                                      
REMARK 465     SER A   381                                                      
REMARK 465     GLY A   382                                                      
REMARK 465     ASN A   383                                                      
REMARK 465     ALA A   384                                                      
REMARK 465     ARG A   385                                                      
REMARK 465     PRO A   386                                                      
REMARK 465     ASN A   387                                                      
REMARK 465     ASN A   388                                                      
REMARK 465     PRO A   389                                                      
REMARK 465     ASP A   390                                                      
REMARK 465     TRP A   391                                                      
REMARK 465     GLY A   392                                                      
REMARK 465     THR A   393                                                      
REMARK 465     PHE A   394                                                      
REMARK 465     GLU A   395                                                      
REMARK 465     GLU A   396                                                      
REMARK 465     VAL A   397                                                      
REMARK 465     SER A   398                                                      
REMARK 465     GLY A   399                                                      
REMARK 465     ASN A   400                                                      
REMARK 465     VAL A   401                                                      
REMARK 465     SER A   402                                                      
REMARK 465     PRO A   403                                                      
REMARK 465     GLY A   404                                                      
REMARK 465     THR A   405                                                      
REMARK 465     ARG A   406                                                      
REMARK 465     ARG A   407                                                      
REMARK 465     GLU A   408                                                      
REMARK 465     TYR A   409                                                      
REMARK 465     HIS A   410                                                      
REMARK 465     THR A   411                                                      
REMARK 465     GLU A   412                                                      
REMARK 465     LYS A   413                                                      
REMARK 465     LEU A   414                                                      
REMARK 465     VAL A   415                                                      
REMARK 465     THR A   416                                                      
REMARK 465     SER A   417                                                      
REMARK 465     LYS A   418                                                      
REMARK 465     GLY A   419                                                      
REMARK 465     ASP A   420                                                      
REMARK 465     LYS A   421                                                      
REMARK 465     GLU A   422                                                      
REMARK 465     LEU A   423                                                      
REMARK 465     ARG A   424                                                      
REMARK 465     THR A   425                                                      
REMARK 465     GLY A   426                                                      
REMARK 465     LYS A   427                                                      
REMARK 465     GLU A   428                                                      
REMARK 465     LYS A   429                                                      
REMARK 465     VAL A   430                                                      
REMARK 465     THR A   431                                                      
REMARK 465     SER A   432                                                      
REMARK 465     GLY A   433                                                      
REMARK 465     SER A   434                                                      
REMARK 465     THR A   435                                                      
REMARK 465     THR A   436                                                      
REMARK 465     THR A   437                                                      
REMARK 465     THR A   438                                                      
REMARK 465     ARG A   439                                                      
REMARK 465     ARG A   440                                                      
REMARK 465     SER A   441                                                      
REMARK 465     CYS A   442                                                      
REMARK 465     SER A   443                                                      
REMARK 465     LYS A   444                                                      
REMARK 465     THR A   445                                                      
REMARK 465     VAL A   446                                                      
REMARK 465     THR A   447                                                      
REMARK 465     LYS A   448                                                      
REMARK 465     THR A   449                                                      
REMARK 465     VAL A   450                                                      
REMARK 465     ILE A   451                                                      
REMARK 465     GLY A   452                                                      
REMARK 465     PRO A   453                                                      
REMARK 465     ASP A   454                                                      
REMARK 465     GLY A   455                                                      
REMARK 465     HIS A   456                                                      
REMARK 465     LYS A   457                                                      
REMARK 465     GLU A   458                                                      
REMARK 465     VAL A   459                                                      
REMARK 465     THR A   460                                                      
REMARK 465     LYS A   461                                                      
REMARK 465     GLU A   462                                                      
REMARK 465     VAL A   463                                                      
REMARK 465     VAL A   464                                                      
REMARK 465     THR A   465                                                      
REMARK 465     SER A   466                                                      
REMARK 465     GLU A   467                                                      
REMARK 465     ASP A   468                                                      
REMARK 465     GLY A   469                                                      
REMARK 465     SER A   470                                                      
REMARK 465     ASP A   471                                                      
REMARK 465     CYS A   472                                                      
REMARK 465     PRO A   473                                                      
REMARK 465     GLU A   474                                                      
REMARK 465     ALA A   475                                                      
REMARK 465     MET A   476                                                      
REMARK 465     ASP A   477                                                      
REMARK 465     LEU A   478                                                      
REMARK 465     GLY A   479                                                      
REMARK 465     THR A   480                                                      
REMARK 465     LEU A   481                                                      
REMARK 465     SER A   482                                                      
REMARK 465     GLY A   483                                                      
REMARK 465     ILE A   484                                                      
REMARK 465     GLY A   485                                                      
REMARK 465     THR A   486                                                      
REMARK 465     LEU A   487                                                      
REMARK 465     ASP A   488                                                      
REMARK 465     GLY A   489                                                      
REMARK 465     PHE A   490                                                      
REMARK 465     ARG A   491                                                      
REMARK 465     HIS A   492                                                      
REMARK 465     ARG A   493                                                      
REMARK 465     HIS A   494                                                      
REMARK 465     PRO A   495                                                      
REMARK 465     ASP A   496                                                      
REMARK 465     GLU A   497                                                      
REMARK 465     ALA A   498                                                      
REMARK 465     ALA A   499                                                      
REMARK 465     PHE A   500                                                      
REMARK 465     PHE A   501                                                      
REMARK 465     ASP A   502                                                      
REMARK 465     THR A   503                                                      
REMARK 465     ALA A   504                                                      
REMARK 465     SER A   505                                                      
REMARK 465     THR A   506                                                      
REMARK 465     GLY A   507                                                      
REMARK 465     LYS A   508                                                      
REMARK 465     THR A   509                                                      
REMARK 465     PHE A   510                                                      
REMARK 465     PRO A   511                                                      
REMARK 465     GLY A   512                                                      
REMARK 465     PHE A   513                                                      
REMARK 465     PHE A   514                                                      
REMARK 465     SER A   515                                                      
REMARK 465     PRO A   516                                                      
REMARK 465     MET A   517                                                      
REMARK 465     LEU A   518                                                      
REMARK 465     GLY A   519                                                      
REMARK 465     GLU A   520                                                      
REMARK 465     PHE A   521                                                      
REMARK 465     VAL A   522                                                      
REMARK 465     SER A   523                                                      
REMARK 465     GLU A   524                                                      
REMARK 465     THR A   525                                                      
REMARK 465     GLU A   526                                                      
REMARK 465     SER A   527                                                      
REMARK 465     ARG A   528                                                      
REMARK 465     GLY A   529                                                      
REMARK 465     SER A   530                                                      
REMARK 465     GLU A   531                                                      
REMARK 465     SER A   532                                                      
REMARK 465     GLY A   533                                                      
REMARK 465     ILE A   534                                                      
REMARK 465     PHE A   535                                                      
REMARK 465     THR A   536                                                      
REMARK 465     ASN A   537                                                      
REMARK 465     THR A   538                                                      
REMARK 465     LYS A   539                                                      
REMARK 465     GLU A   540                                                      
REMARK 465     SER A   541                                                      
REMARK 465     SER A   542                                                      
REMARK 465     SER A   543                                                      
REMARK 465     HIS A   544                                                      
REMARK 465     HIS A   545                                                      
REMARK 465     PRO A   546                                                      
REMARK 465     GLY A   547                                                      
REMARK 465     ILE A   548                                                      
REMARK 465     ALA A   549                                                      
REMARK 465     GLU A   550                                                      
REMARK 465     PHE A   551                                                      
REMARK 465     PRO A   552                                                      
REMARK 465     SER A   553                                                      
REMARK 465     ARG A   554                                                      
REMARK 465     GLY A   555                                                      
REMARK 465     LYS A   556                                                      
REMARK 465     SER A   557                                                      
REMARK 465     SER A   558                                                      
REMARK 465     SER A   559                                                      
REMARK 465     TYR A   560                                                      
REMARK 465     SER A   561                                                      
REMARK 465     LYS A   562                                                      
REMARK 465     GLN B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     ASN B     4                                                      
REMARK 465     ASP B     5                                                      
REMARK 465     ASN B     6                                                      
REMARK 465     GLU B     7                                                      
REMARK 465     GLU B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     PHE B    10                                                      
REMARK 465     PHE B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     ARG B    14                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     HIS B    16                                                      
REMARK 465     ARG B    17                                                      
REMARK 465     PRO B    18                                                      
REMARK 465     LEU B    19                                                      
REMARK 465     ASP B    20                                                      
REMARK 465     LYS B    21                                                      
REMARK 465     LYS B    22                                                      
REMARK 465     ARG B    23                                                      
REMARK 465     GLU B    24                                                      
REMARK 465     GLU B    25                                                      
REMARK 465     ALA B    26                                                      
REMARK 465     PRO B    27                                                      
REMARK 465     SER B    28                                                      
REMARK 465     LEU B    29                                                      
REMARK 465     ARG B    30                                                      
REMARK 465     PRO B    31                                                      
REMARK 465     ALA B    32                                                      
REMARK 465     PRO B    33                                                      
REMARK 465     PRO B    34                                                      
REMARK 465     PRO B    35                                                      
REMARK 465     ILE B    36                                                      
REMARK 465     SER B    37                                                      
REMARK 465     GLY B    38                                                      
REMARK 465     GLY B    39                                                      
REMARK 465     GLY B    40                                                      
REMARK 465     TYR B    41                                                      
REMARK 465     ARG B    42                                                      
REMARK 465     ALA B    43                                                      
REMARK 465     ARG B    44                                                      
REMARK 465     PRO B    45                                                      
REMARK 465     ALA B    46                                                      
REMARK 465     LYS B    47                                                      
REMARK 465     ALA B    48                                                      
REMARK 465     ALA B    49                                                      
REMARK 465     ALA B    50                                                      
REMARK 465     THR B    51                                                      
REMARK 465     GLN B    52                                                      
REMARK 465     LYS B    53                                                      
REMARK 465     LYS B    54                                                      
REMARK 465     VAL B    55                                                      
REMARK 465     GLU B    56                                                      
REMARK 465     ARG B    57                                                      
REMARK 465     PRO B   459                                                      
REMARK 465     GLN B   460                                                      
REMARK 465     GLN B   461                                                      
REMARK 465     TYR C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     ALA C     3                                                      
REMARK 465     THR C     4                                                      
REMARK 465     ARG C     5                                                      
REMARK 465     ASP C     6                                                      
REMARK 465     ASN C     7                                                      
REMARK 465     CYS C     8                                                      
REMARK 465     CYS C     9                                                      
REMARK 465     ILE C    10                                                      
REMARK 465     LEU C    11                                                      
REMARK 465     ASP C    12                                                      
REMARK 465     GLU C    13                                                      
REMARK 465     GLY C   395                                                      
REMARK 465     GLU C   396                                                      
REMARK 465     GLY C   397                                                      
REMARK 465     GLN C   398                                                      
REMARK 465     GLN C   399                                                      
REMARK 465     HIS C   400                                                      
REMARK 465     HIS C   401                                                      
REMARK 465     LEU C   402                                                      
REMARK 465     GLY C   403                                                      
REMARK 465     GLY C   404                                                      
REMARK 465     ALA C   405                                                      
REMARK 465     LYS C   406                                                      
REMARK 465     GLN C   407                                                      
REMARK 465     ALA C   408                                                      
REMARK 465     GLY C   409                                                      
REMARK 465     ASP C   410                                                      
REMARK 465     VAL C   411                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     ASP D     2                                                      
REMARK 465     SER D     3                                                      
REMARK 465     GLY D     4                                                      
REMARK 465     GLU D     5                                                      
REMARK 465     GLY D     6                                                      
REMARK 465     ASP D     7                                                      
REMARK 465     PHE D     8                                                      
REMARK 465     LEU D     9                                                      
REMARK 465     ALA D    10                                                      
REMARK 465     GLU D    11                                                      
REMARK 465     GLY D    12                                                      
REMARK 465     GLY D    13                                                      
REMARK 465     GLY D    14                                                      
REMARK 465     VAL D    15                                                      
REMARK 465     ARG D    16                                                      
REMARK 465     GLY D    17                                                      
REMARK 465     PRO D    18                                                      
REMARK 465     ARG D    19                                                      
REMARK 465     VAL D    20                                                      
REMARK 465     VAL D    21                                                      
REMARK 465     GLU D    22                                                      
REMARK 465     ARG D    23                                                      
REMARK 465     HIS D    24                                                      
REMARK 465     GLN D    25                                                      
REMARK 465     SER D    26                                                      
REMARK 465     HIS D   201                                                      
REMARK 465     LEU D   202                                                      
REMARK 465     PRO D   203                                                      
REMARK 465     LEU D   204                                                      
REMARK 465     ILE D   205                                                      
REMARK 465     LYS D   206                                                      
REMARK 465     MET D   207                                                      
REMARK 465     LYS D   208                                                      
REMARK 465     PRO D   209                                                      
REMARK 465     VAL D   210                                                      
REMARK 465     PRO D   211                                                      
REMARK 465     ASP D   212                                                      
REMARK 465     LEU D   213                                                      
REMARK 465     VAL D   214                                                      
REMARK 465     PRO D   215                                                      
REMARK 465     GLY D   216                                                      
REMARK 465     ASN D   217                                                      
REMARK 465     PHE D   218                                                      
REMARK 465     LYS D   219                                                      
REMARK 465     SER D   220                                                      
REMARK 465     GLN D   221                                                      
REMARK 465     LEU D   222                                                      
REMARK 465     GLN D   223                                                      
REMARK 465     LYS D   224                                                      
REMARK 465     VAL D   225                                                      
REMARK 465     PRO D   226                                                      
REMARK 465     PRO D   227                                                      
REMARK 465     GLU D   228                                                      
REMARK 465     TRP D   229                                                      
REMARK 465     LYS D   230                                                      
REMARK 465     ALA D   231                                                      
REMARK 465     LEU D   232                                                      
REMARK 465     THR D   233                                                      
REMARK 465     ASP D   234                                                      
REMARK 465     MET D   235                                                      
REMARK 465     PRO D   236                                                      
REMARK 465     GLN D   237                                                      
REMARK 465     MET D   238                                                      
REMARK 465     ARG D   239                                                      
REMARK 465     MET D   240                                                      
REMARK 465     GLU D   241                                                      
REMARK 465     LEU D   242                                                      
REMARK 465     GLU D   243                                                      
REMARK 465     ARG D   244                                                      
REMARK 465     PRO D   245                                                      
REMARK 465     GLY D   246                                                      
REMARK 465     GLY D   247                                                      
REMARK 465     ASN D   248                                                      
REMARK 465     GLU D   249                                                      
REMARK 465     ILE D   250                                                      
REMARK 465     THR D   251                                                      
REMARK 465     ARG D   252                                                      
REMARK 465     GLY D   253                                                      
REMARK 465     GLY D   254                                                      
REMARK 465     SER D   255                                                      
REMARK 465     THR D   256                                                      
REMARK 465     SER D   257                                                      
REMARK 465     TYR D   258                                                      
REMARK 465     GLY D   259                                                      
REMARK 465     THR D   260                                                      
REMARK 465     GLY D   261                                                      
REMARK 465     SER D   262                                                      
REMARK 465     GLU D   263                                                      
REMARK 465     THR D   264                                                      
REMARK 465     GLU D   265                                                      
REMARK 465     SER D   266                                                      
REMARK 465     PRO D   267                                                      
REMARK 465     ARG D   268                                                      
REMARK 465     ASN D   269                                                      
REMARK 465     PRO D   270                                                      
REMARK 465     SER D   271                                                      
REMARK 465     SER D   272                                                      
REMARK 465     ALA D   273                                                      
REMARK 465     GLY D   274                                                      
REMARK 465     SER D   275                                                      
REMARK 465     TRP D   276                                                      
REMARK 465     ASN D   277                                                      
REMARK 465     SER D   278                                                      
REMARK 465     GLY D   279                                                      
REMARK 465     SER D   280                                                      
REMARK 465     SER D   281                                                      
REMARK 465     GLY D   282                                                      
REMARK 465     PRO D   283                                                      
REMARK 465     GLY D   284                                                      
REMARK 465     SER D   285                                                      
REMARK 465     THR D   286                                                      
REMARK 465     GLY D   287                                                      
REMARK 465     ASN D   288                                                      
REMARK 465     ARG D   289                                                      
REMARK 465     ASN D   290                                                      
REMARK 465     PRO D   291                                                      
REMARK 465     GLY D   292                                                      
REMARK 465     SER D   293                                                      
REMARK 465     SER D   294                                                      
REMARK 465     GLY D   295                                                      
REMARK 465     THR D   296                                                      
REMARK 465     GLY D   297                                                      
REMARK 465     GLY D   298                                                      
REMARK 465     THR D   299                                                      
REMARK 465     ALA D   300                                                      
REMARK 465     THR D   301                                                      
REMARK 465     TRP D   302                                                      
REMARK 465     LYS D   303                                                      
REMARK 465     PRO D   304                                                      
REMARK 465     GLY D   305                                                      
REMARK 465     SER D   306                                                      
REMARK 465     SER D   307                                                      
REMARK 465     GLY D   308                                                      
REMARK 465     PRO D   309                                                      
REMARK 465     GLY D   310                                                      
REMARK 465     SER D   311                                                      
REMARK 465     THR D   312                                                      
REMARK 465     GLY D   313                                                      
REMARK 465     SER D   314                                                      
REMARK 465     TRP D   315                                                      
REMARK 465     ASN D   316                                                      
REMARK 465     SER D   317                                                      
REMARK 465     GLY D   318                                                      
REMARK 465     SER D   319                                                      
REMARK 465     SER D   320                                                      
REMARK 465     GLY D   321                                                      
REMARK 465     THR D   322                                                      
REMARK 465     GLY D   323                                                      
REMARK 465     SER D   324                                                      
REMARK 465     THR D   325                                                      
REMARK 465     GLY D   326                                                      
REMARK 465     ASN D   327                                                      
REMARK 465     GLN D   328                                                      
REMARK 465     ASN D   329                                                      
REMARK 465     PRO D   330                                                      
REMARK 465     GLY D   331                                                      
REMARK 465     SER D   332                                                      
REMARK 465     PRO D   333                                                      
REMARK 465     ARG D   334                                                      
REMARK 465     PRO D   335                                                      
REMARK 465     GLY D   336                                                      
REMARK 465     SER D   337                                                      
REMARK 465     THR D   338                                                      
REMARK 465     GLY D   339                                                      
REMARK 465     THR D   340                                                      
REMARK 465     TRP D   341                                                      
REMARK 465     ASN D   342                                                      
REMARK 465     PRO D   343                                                      
REMARK 465     GLY D   344                                                      
REMARK 465     SER D   345                                                      
REMARK 465     SER D   346                                                      
REMARK 465     GLU D   347                                                      
REMARK 465     ARG D   348                                                      
REMARK 465     GLY D   349                                                      
REMARK 465     SER D   350                                                      
REMARK 465     ALA D   351                                                      
REMARK 465     GLY D   352                                                      
REMARK 465     HIS D   353                                                      
REMARK 465     TRP D   354                                                      
REMARK 465     THR D   355                                                      
REMARK 465     SER D   356                                                      
REMARK 465     GLU D   357                                                      
REMARK 465     SER D   358                                                      
REMARK 465     SER D   359                                                      
REMARK 465     VAL D   360                                                      
REMARK 465     SER D   361                                                      
REMARK 465     GLY D   362                                                      
REMARK 465     SER D   363                                                      
REMARK 465     THR D   364                                                      
REMARK 465     GLY D   365                                                      
REMARK 465     GLN D   366                                                      
REMARK 465     TRP D   367                                                      
REMARK 465     HIS D   368                                                      
REMARK 465     SER D   369                                                      
REMARK 465     GLU D   370                                                      
REMARK 465     SER D   371                                                      
REMARK 465     GLY D   372                                                      
REMARK 465     SER D   373                                                      
REMARK 465     PHE D   374                                                      
REMARK 465     ARG D   375                                                      
REMARK 465     PRO D   376                                                      
REMARK 465     ASP D   377                                                      
REMARK 465     SER D   378                                                      
REMARK 465     PRO D   379                                                      
REMARK 465     GLY D   380                                                      
REMARK 465     SER D   381                                                      
REMARK 465     GLY D   382                                                      
REMARK 465     ASN D   383                                                      
REMARK 465     ALA D   384                                                      
REMARK 465     ARG D   385                                                      
REMARK 465     PRO D   386                                                      
REMARK 465     ASN D   387                                                      
REMARK 465     ASN D   388                                                      
REMARK 465     PRO D   389                                                      
REMARK 465     ASP D   390                                                      
REMARK 465     TRP D   391                                                      
REMARK 465     GLY D   392                                                      
REMARK 465     THR D   393                                                      
REMARK 465     PHE D   394                                                      
REMARK 465     GLU D   395                                                      
REMARK 465     GLU D   396                                                      
REMARK 465     VAL D   397                                                      
REMARK 465     SER D   398                                                      
REMARK 465     GLY D   399                                                      
REMARK 465     ASN D   400                                                      
REMARK 465     VAL D   401                                                      
REMARK 465     SER D   402                                                      
REMARK 465     PRO D   403                                                      
REMARK 465     GLY D   404                                                      
REMARK 465     THR D   405                                                      
REMARK 465     ARG D   406                                                      
REMARK 465     ARG D   407                                                      
REMARK 465     GLU D   408                                                      
REMARK 465     TYR D   409                                                      
REMARK 465     HIS D   410                                                      
REMARK 465     THR D   411                                                      
REMARK 465     GLU D   412                                                      
REMARK 465     LYS D   413                                                      
REMARK 465     LEU D   414                                                      
REMARK 465     VAL D   415                                                      
REMARK 465     THR D   416                                                      
REMARK 465     SER D   417                                                      
REMARK 465     LYS D   418                                                      
REMARK 465     GLY D   419                                                      
REMARK 465     ASP D   420                                                      
REMARK 465     LYS D   421                                                      
REMARK 465     GLU D   422                                                      
REMARK 465     LEU D   423                                                      
REMARK 465     ARG D   424                                                      
REMARK 465     THR D   425                                                      
REMARK 465     GLY D   426                                                      
REMARK 465     LYS D   427                                                      
REMARK 465     GLU D   428                                                      
REMARK 465     LYS D   429                                                      
REMARK 465     VAL D   430                                                      
REMARK 465     THR D   431                                                      
REMARK 465     SER D   432                                                      
REMARK 465     GLY D   433                                                      
REMARK 465     SER D   434                                                      
REMARK 465     THR D   435                                                      
REMARK 465     THR D   436                                                      
REMARK 465     THR D   437                                                      
REMARK 465     THR D   438                                                      
REMARK 465     ARG D   439                                                      
REMARK 465     ARG D   440                                                      
REMARK 465     SER D   441                                                      
REMARK 465     CYS D   442                                                      
REMARK 465     SER D   443                                                      
REMARK 465     LYS D   444                                                      
REMARK 465     THR D   445                                                      
REMARK 465     VAL D   446                                                      
REMARK 465     THR D   447                                                      
REMARK 465     LYS D   448                                                      
REMARK 465     THR D   449                                                      
REMARK 465     VAL D   450                                                      
REMARK 465     ILE D   451                                                      
REMARK 465     GLY D   452                                                      
REMARK 465     PRO D   453                                                      
REMARK 465     ASP D   454                                                      
REMARK 465     GLY D   455                                                      
REMARK 465     HIS D   456                                                      
REMARK 465     LYS D   457                                                      
REMARK 465     GLU D   458                                                      
REMARK 465     VAL D   459                                                      
REMARK 465     THR D   460                                                      
REMARK 465     LYS D   461                                                      
REMARK 465     GLU D   462                                                      
REMARK 465     VAL D   463                                                      
REMARK 465     VAL D   464                                                      
REMARK 465     THR D   465                                                      
REMARK 465     SER D   466                                                      
REMARK 465     GLU D   467                                                      
REMARK 465     ASP D   468                                                      
REMARK 465     GLY D   469                                                      
REMARK 465     SER D   470                                                      
REMARK 465     ASP D   471                                                      
REMARK 465     CYS D   472                                                      
REMARK 465     PRO D   473                                                      
REMARK 465     GLU D   474                                                      
REMARK 465     ALA D   475                                                      
REMARK 465     MET D   476                                                      
REMARK 465     ASP D   477                                                      
REMARK 465     LEU D   478                                                      
REMARK 465     GLY D   479                                                      
REMARK 465     THR D   480                                                      
REMARK 465     LEU D   481                                                      
REMARK 465     SER D   482                                                      
REMARK 465     GLY D   483                                                      
REMARK 465     ILE D   484                                                      
REMARK 465     GLY D   485                                                      
REMARK 465     THR D   486                                                      
REMARK 465     LEU D   487                                                      
REMARK 465     ASP D   488                                                      
REMARK 465     GLY D   489                                                      
REMARK 465     PHE D   490                                                      
REMARK 465     ARG D   491                                                      
REMARK 465     HIS D   492                                                      
REMARK 465     ARG D   493                                                      
REMARK 465     HIS D   494                                                      
REMARK 465     PRO D   495                                                      
REMARK 465     ASP D   496                                                      
REMARK 465     GLU D   497                                                      
REMARK 465     ALA D   498                                                      
REMARK 465     ALA D   499                                                      
REMARK 465     PHE D   500                                                      
REMARK 465     PHE D   501                                                      
REMARK 465     ASP D   502                                                      
REMARK 465     THR D   503                                                      
REMARK 465     ALA D   504                                                      
REMARK 465     SER D   505                                                      
REMARK 465     THR D   506                                                      
REMARK 465     GLY D   507                                                      
REMARK 465     LYS D   508                                                      
REMARK 465     THR D   509                                                      
REMARK 465     PHE D   510                                                      
REMARK 465     PRO D   511                                                      
REMARK 465     GLY D   512                                                      
REMARK 465     PHE D   513                                                      
REMARK 465     PHE D   514                                                      
REMARK 465     SER D   515                                                      
REMARK 465     PRO D   516                                                      
REMARK 465     MET D   517                                                      
REMARK 465     LEU D   518                                                      
REMARK 465     GLY D   519                                                      
REMARK 465     GLU D   520                                                      
REMARK 465     PHE D   521                                                      
REMARK 465     VAL D   522                                                      
REMARK 465     SER D   523                                                      
REMARK 465     GLU D   524                                                      
REMARK 465     THR D   525                                                      
REMARK 465     GLU D   526                                                      
REMARK 465     SER D   527                                                      
REMARK 465     ARG D   528                                                      
REMARK 465     GLY D   529                                                      
REMARK 465     SER D   530                                                      
REMARK 465     GLU D   531                                                      
REMARK 465     SER D   532                                                      
REMARK 465     GLY D   533                                                      
REMARK 465     ILE D   534                                                      
REMARK 465     PHE D   535                                                      
REMARK 465     THR D   536                                                      
REMARK 465     ASN D   537                                                      
REMARK 465     THR D   538                                                      
REMARK 465     LYS D   539                                                      
REMARK 465     GLU D   540                                                      
REMARK 465     SER D   541                                                      
REMARK 465     SER D   542                                                      
REMARK 465     SER D   543                                                      
REMARK 465     HIS D   544                                                      
REMARK 465     HIS D   545                                                      
REMARK 465     PRO D   546                                                      
REMARK 465     GLY D   547                                                      
REMARK 465     ILE D   548                                                      
REMARK 465     ALA D   549                                                      
REMARK 465     GLU D   550                                                      
REMARK 465     PHE D   551                                                      
REMARK 465     PRO D   552                                                      
REMARK 465     SER D   553                                                      
REMARK 465     ARG D   554                                                      
REMARK 465     GLY D   555                                                      
REMARK 465     LYS D   556                                                      
REMARK 465     SER D   557                                                      
REMARK 465     SER D   558                                                      
REMARK 465     SER D   559                                                      
REMARK 465     TYR D   560                                                      
REMARK 465     SER D   561                                                      
REMARK 465     LYS D   562                                                      
REMARK 465     GLN E     1                                                      
REMARK 465     GLY E     2                                                      
REMARK 465     VAL E     3                                                      
REMARK 465     ASN E     4                                                      
REMARK 465     ASP E     5                                                      
REMARK 465     ASN E     6                                                      
REMARK 465     GLU E     7                                                      
REMARK 465     GLU E     8                                                      
REMARK 465     GLY E     9                                                      
REMARK 465     PHE E    10                                                      
REMARK 465     PHE E    11                                                      
REMARK 465     SER E    12                                                      
REMARK 465     ALA E    13                                                      
REMARK 465     ARG E    14                                                      
REMARK 465     GLY E    15                                                      
REMARK 465     HIS E    16                                                      
REMARK 465     ARG E    17                                                      
REMARK 465     PRO E    18                                                      
REMARK 465     LEU E    19                                                      
REMARK 465     ASP E    20                                                      
REMARK 465     LYS E    21                                                      
REMARK 465     LYS E    22                                                      
REMARK 465     ARG E    23                                                      
REMARK 465     GLU E    24                                                      
REMARK 465     GLU E    25                                                      
REMARK 465     ALA E    26                                                      
REMARK 465     PRO E    27                                                      
REMARK 465     SER E    28                                                      
REMARK 465     LEU E    29                                                      
REMARK 465     ARG E    30                                                      
REMARK 465     PRO E    31                                                      
REMARK 465     ALA E    32                                                      
REMARK 465     PRO E    33                                                      
REMARK 465     PRO E    34                                                      
REMARK 465     PRO E    35                                                      
REMARK 465     ILE E    36                                                      
REMARK 465     SER E    37                                                      
REMARK 465     GLY E    38                                                      
REMARK 465     GLY E    39                                                      
REMARK 465     GLY E    40                                                      
REMARK 465     TYR E    41                                                      
REMARK 465     ARG E    42                                                      
REMARK 465     ALA E    43                                                      
REMARK 465     ARG E    44                                                      
REMARK 465     PRO E    45                                                      
REMARK 465     ALA E    46                                                      
REMARK 465     LYS E    47                                                      
REMARK 465     ALA E    48                                                      
REMARK 465     ALA E    49                                                      
REMARK 465     ALA E    50                                                      
REMARK 465     THR E    51                                                      
REMARK 465     GLN E    52                                                      
REMARK 465     LYS E    53                                                      
REMARK 465     LYS E    54                                                      
REMARK 465     VAL E    55                                                      
REMARK 465     GLU E    56                                                      
REMARK 465     ARG E    57                                                      
REMARK 465     PRO E   459                                                      
REMARK 465     GLN E   460                                                      
REMARK 465     GLN E   461                                                      
REMARK 465     TYR F     1                                                      
REMARK 465     VAL F     2                                                      
REMARK 465     ALA F     3                                                      
REMARK 465     THR F     4                                                      
REMARK 465     ARG F     5                                                      
REMARK 465     ASP F     6                                                      
REMARK 465     ASN F     7                                                      
REMARK 465     CYS F     8                                                      
REMARK 465     CYS F     9                                                      
REMARK 465     ILE F    10                                                      
REMARK 465     LEU F    11                                                      
REMARK 465     ASP F    12                                                      
REMARK 465     GLU F    13                                                      
REMARK 465     GLU F   396                                                      
REMARK 465     GLY F   397                                                      
REMARK 465     GLN F   398                                                      
REMARK 465     GLN F   399                                                      
REMARK 465     HIS F   400                                                      
REMARK 465     HIS F   401                                                      
REMARK 465     LEU F   402                                                      
REMARK 465     GLY F   403                                                      
REMARK 465     GLY F   404                                                      
REMARK 465     ALA F   405                                                      
REMARK 465     LYS F   406                                                      
REMARK 465     GLN F   407                                                      
REMARK 465     ALA F   408                                                      
REMARK 465     GLY F   409                                                      
REMARK 465     ASP F   410                                                      
REMARK 465     VAL F   411                                                      
REMARK 465     ALA G     1                                                      
REMARK 465     ASP G     2                                                      
REMARK 465     SER G     3                                                      
REMARK 465     GLY G     4                                                      
REMARK 465     GLU G     5                                                      
REMARK 465     GLY G     6                                                      
REMARK 465     ASP G     7                                                      
REMARK 465     PHE G     8                                                      
REMARK 465     LEU G     9                                                      
REMARK 465     ALA G    10                                                      
REMARK 465     GLU G    11                                                      
REMARK 465     GLY G    12                                                      
REMARK 465     GLY G    13                                                      
REMARK 465     GLY G    14                                                      
REMARK 465     VAL G    15                                                      
REMARK 465     ARG G    16                                                      
REMARK 465     GLY G    17                                                      
REMARK 465     PRO G    18                                                      
REMARK 465     ARG G    19                                                      
REMARK 465     VAL G    20                                                      
REMARK 465     VAL G    21                                                      
REMARK 465     GLU G    22                                                      
REMARK 465     ARG G    23                                                      
REMARK 465     HIS G    24                                                      
REMARK 465     GLN G    25                                                      
REMARK 465     SER G    26                                                      
REMARK 465     HIS G   201                                                      
REMARK 465     LEU G   202                                                      
REMARK 465     PRO G   203                                                      
REMARK 465     LEU G   204                                                      
REMARK 465     ILE G   205                                                      
REMARK 465     LYS G   206                                                      
REMARK 465     MET G   207                                                      
REMARK 465     LYS G   208                                                      
REMARK 465     PRO G   209                                                      
REMARK 465     VAL G   210                                                      
REMARK 465     PRO G   211                                                      
REMARK 465     ASP G   212                                                      
REMARK 465     LEU G   213                                                      
REMARK 465     VAL G   214                                                      
REMARK 465     PRO G   215                                                      
REMARK 465     GLY G   216                                                      
REMARK 465     ASN G   217                                                      
REMARK 465     PHE G   218                                                      
REMARK 465     LYS G   219                                                      
REMARK 465     SER G   220                                                      
REMARK 465     GLN G   221                                                      
REMARK 465     LEU G   222                                                      
REMARK 465     GLN G   223                                                      
REMARK 465     LYS G   224                                                      
REMARK 465     VAL G   225                                                      
REMARK 465     PRO G   226                                                      
REMARK 465     PRO G   227                                                      
REMARK 465     GLU G   228                                                      
REMARK 465     TRP G   229                                                      
REMARK 465     LYS G   230                                                      
REMARK 465     ALA G   231                                                      
REMARK 465     LEU G   232                                                      
REMARK 465     THR G   233                                                      
REMARK 465     ASP G   234                                                      
REMARK 465     MET G   235                                                      
REMARK 465     PRO G   236                                                      
REMARK 465     GLN G   237                                                      
REMARK 465     MET G   238                                                      
REMARK 465     ARG G   239                                                      
REMARK 465     MET G   240                                                      
REMARK 465     GLU G   241                                                      
REMARK 465     LEU G   242                                                      
REMARK 465     GLU G   243                                                      
REMARK 465     ARG G   244                                                      
REMARK 465     PRO G   245                                                      
REMARK 465     GLY G   246                                                      
REMARK 465     GLY G   247                                                      
REMARK 465     ASN G   248                                                      
REMARK 465     GLU G   249                                                      
REMARK 465     ILE G   250                                                      
REMARK 465     THR G   251                                                      
REMARK 465     ARG G   252                                                      
REMARK 465     GLY G   253                                                      
REMARK 465     GLY G   254                                                      
REMARK 465     SER G   255                                                      
REMARK 465     THR G   256                                                      
REMARK 465     SER G   257                                                      
REMARK 465     TYR G   258                                                      
REMARK 465     GLY G   259                                                      
REMARK 465     THR G   260                                                      
REMARK 465     GLY G   261                                                      
REMARK 465     SER G   262                                                      
REMARK 465     GLU G   263                                                      
REMARK 465     THR G   264                                                      
REMARK 465     GLU G   265                                                      
REMARK 465     SER G   266                                                      
REMARK 465     PRO G   267                                                      
REMARK 465     ARG G   268                                                      
REMARK 465     ASN G   269                                                      
REMARK 465     PRO G   270                                                      
REMARK 465     SER G   271                                                      
REMARK 465     SER G   272                                                      
REMARK 465     ALA G   273                                                      
REMARK 465     GLY G   274                                                      
REMARK 465     SER G   275                                                      
REMARK 465     TRP G   276                                                      
REMARK 465     ASN G   277                                                      
REMARK 465     SER G   278                                                      
REMARK 465     GLY G   279                                                      
REMARK 465     SER G   280                                                      
REMARK 465     SER G   281                                                      
REMARK 465     GLY G   282                                                      
REMARK 465     PRO G   283                                                      
REMARK 465     GLY G   284                                                      
REMARK 465     SER G   285                                                      
REMARK 465     THR G   286                                                      
REMARK 465     GLY G   287                                                      
REMARK 465     ASN G   288                                                      
REMARK 465     ARG G   289                                                      
REMARK 465     ASN G   290                                                      
REMARK 465     PRO G   291                                                      
REMARK 465     GLY G   292                                                      
REMARK 465     SER G   293                                                      
REMARK 465     SER G   294                                                      
REMARK 465     GLY G   295                                                      
REMARK 465     THR G   296                                                      
REMARK 465     GLY G   297                                                      
REMARK 465     GLY G   298                                                      
REMARK 465     THR G   299                                                      
REMARK 465     ALA G   300                                                      
REMARK 465     THR G   301                                                      
REMARK 465     TRP G   302                                                      
REMARK 465     LYS G   303                                                      
REMARK 465     PRO G   304                                                      
REMARK 465     GLY G   305                                                      
REMARK 465     SER G   306                                                      
REMARK 465     SER G   307                                                      
REMARK 465     GLY G   308                                                      
REMARK 465     PRO G   309                                                      
REMARK 465     GLY G   310                                                      
REMARK 465     SER G   311                                                      
REMARK 465     THR G   312                                                      
REMARK 465     GLY G   313                                                      
REMARK 465     SER G   314                                                      
REMARK 465     TRP G   315                                                      
REMARK 465     ASN G   316                                                      
REMARK 465     SER G   317                                                      
REMARK 465     GLY G   318                                                      
REMARK 465     SER G   319                                                      
REMARK 465     SER G   320                                                      
REMARK 465     GLY G   321                                                      
REMARK 465     THR G   322                                                      
REMARK 465     GLY G   323                                                      
REMARK 465     SER G   324                                                      
REMARK 465     THR G   325                                                      
REMARK 465     GLY G   326                                                      
REMARK 465     ASN G   327                                                      
REMARK 465     GLN G   328                                                      
REMARK 465     ASN G   329                                                      
REMARK 465     PRO G   330                                                      
REMARK 465     GLY G   331                                                      
REMARK 465     SER G   332                                                      
REMARK 465     PRO G   333                                                      
REMARK 465     ARG G   334                                                      
REMARK 465     PRO G   335                                                      
REMARK 465     GLY G   336                                                      
REMARK 465     SER G   337                                                      
REMARK 465     THR G   338                                                      
REMARK 465     GLY G   339                                                      
REMARK 465     THR G   340                                                      
REMARK 465     TRP G   341                                                      
REMARK 465     ASN G   342                                                      
REMARK 465     PRO G   343                                                      
REMARK 465     GLY G   344                                                      
REMARK 465     SER G   345                                                      
REMARK 465     SER G   346                                                      
REMARK 465     GLU G   347                                                      
REMARK 465     ARG G   348                                                      
REMARK 465     GLY G   349                                                      
REMARK 465     SER G   350                                                      
REMARK 465     ALA G   351                                                      
REMARK 465     GLY G   352                                                      
REMARK 465     HIS G   353                                                      
REMARK 465     TRP G   354                                                      
REMARK 465     THR G   355                                                      
REMARK 465     SER G   356                                                      
REMARK 465     GLU G   357                                                      
REMARK 465     SER G   358                                                      
REMARK 465     SER G   359                                                      
REMARK 465     VAL G   360                                                      
REMARK 465     SER G   361                                                      
REMARK 465     GLY G   362                                                      
REMARK 465     SER G   363                                                      
REMARK 465     THR G   364                                                      
REMARK 465     GLY G   365                                                      
REMARK 465     GLN G   366                                                      
REMARK 465     TRP G   367                                                      
REMARK 465     HIS G   368                                                      
REMARK 465     SER G   369                                                      
REMARK 465     GLU G   370                                                      
REMARK 465     SER G   371                                                      
REMARK 465     GLY G   372                                                      
REMARK 465     SER G   373                                                      
REMARK 465     PHE G   374                                                      
REMARK 465     ARG G   375                                                      
REMARK 465     PRO G   376                                                      
REMARK 465     ASP G   377                                                      
REMARK 465     SER G   378                                                      
REMARK 465     PRO G   379                                                      
REMARK 465     GLY G   380                                                      
REMARK 465     SER G   381                                                      
REMARK 465     GLY G   382                                                      
REMARK 465     ASN G   383                                                      
REMARK 465     ALA G   384                                                      
REMARK 465     ARG G   385                                                      
REMARK 465     PRO G   386                                                      
REMARK 465     ASN G   387                                                      
REMARK 465     ASN G   388                                                      
REMARK 465     PRO G   389                                                      
REMARK 465     ASP G   390                                                      
REMARK 465     TRP G   391                                                      
REMARK 465     GLY G   392                                                      
REMARK 465     THR G   393                                                      
REMARK 465     PHE G   394                                                      
REMARK 465     GLU G   395                                                      
REMARK 465     GLU G   396                                                      
REMARK 465     VAL G   397                                                      
REMARK 465     SER G   398                                                      
REMARK 465     GLY G   399                                                      
REMARK 465     ASN G   400                                                      
REMARK 465     VAL G   401                                                      
REMARK 465     SER G   402                                                      
REMARK 465     PRO G   403                                                      
REMARK 465     GLY G   404                                                      
REMARK 465     THR G   405                                                      
REMARK 465     ARG G   406                                                      
REMARK 465     ARG G   407                                                      
REMARK 465     GLU G   408                                                      
REMARK 465     TYR G   409                                                      
REMARK 465     HIS G   410                                                      
REMARK 465     THR G   411                                                      
REMARK 465     GLU G   412                                                      
REMARK 465     LYS G   413                                                      
REMARK 465     LEU G   414                                                      
REMARK 465     VAL G   415                                                      
REMARK 465     THR G   416                                                      
REMARK 465     SER G   417                                                      
REMARK 465     LYS G   418                                                      
REMARK 465     GLY G   419                                                      
REMARK 465     ASP G   420                                                      
REMARK 465     LYS G   421                                                      
REMARK 465     GLU G   422                                                      
REMARK 465     LEU G   423                                                      
REMARK 465     ARG G   424                                                      
REMARK 465     THR G   425                                                      
REMARK 465     GLY G   426                                                      
REMARK 465     LYS G   427                                                      
REMARK 465     GLU G   428                                                      
REMARK 465     LYS G   429                                                      
REMARK 465     VAL G   430                                                      
REMARK 465     THR G   431                                                      
REMARK 465     SER G   432                                                      
REMARK 465     GLY G   433                                                      
REMARK 465     SER G   434                                                      
REMARK 465     THR G   435                                                      
REMARK 465     THR G   436                                                      
REMARK 465     THR G   437                                                      
REMARK 465     THR G   438                                                      
REMARK 465     ARG G   439                                                      
REMARK 465     ARG G   440                                                      
REMARK 465     SER G   441                                                      
REMARK 465     CYS G   442                                                      
REMARK 465     SER G   443                                                      
REMARK 465     LYS G   444                                                      
REMARK 465     THR G   445                                                      
REMARK 465     VAL G   446                                                      
REMARK 465     THR G   447                                                      
REMARK 465     LYS G   448                                                      
REMARK 465     THR G   449                                                      
REMARK 465     VAL G   450                                                      
REMARK 465     ILE G   451                                                      
REMARK 465     GLY G   452                                                      
REMARK 465     PRO G   453                                                      
REMARK 465     ASP G   454                                                      
REMARK 465     GLY G   455                                                      
REMARK 465     HIS G   456                                                      
REMARK 465     LYS G   457                                                      
REMARK 465     GLU G   458                                                      
REMARK 465     VAL G   459                                                      
REMARK 465     THR G   460                                                      
REMARK 465     LYS G   461                                                      
REMARK 465     GLU G   462                                                      
REMARK 465     VAL G   463                                                      
REMARK 465     VAL G   464                                                      
REMARK 465     THR G   465                                                      
REMARK 465     SER G   466                                                      
REMARK 465     GLU G   467                                                      
REMARK 465     ASP G   468                                                      
REMARK 465     GLY G   469                                                      
REMARK 465     SER G   470                                                      
REMARK 465     ASP G   471                                                      
REMARK 465     CYS G   472                                                      
REMARK 465     PRO G   473                                                      
REMARK 465     GLU G   474                                                      
REMARK 465     ALA G   475                                                      
REMARK 465     MET G   476                                                      
REMARK 465     ASP G   477                                                      
REMARK 465     LEU G   478                                                      
REMARK 465     GLY G   479                                                      
REMARK 465     THR G   480                                                      
REMARK 465     LEU G   481                                                      
REMARK 465     SER G   482                                                      
REMARK 465     GLY G   483                                                      
REMARK 465     ILE G   484                                                      
REMARK 465     GLY G   485                                                      
REMARK 465     THR G   486                                                      
REMARK 465     LEU G   487                                                      
REMARK 465     ASP G   488                                                      
REMARK 465     GLY G   489                                                      
REMARK 465     PHE G   490                                                      
REMARK 465     ARG G   491                                                      
REMARK 465     HIS G   492                                                      
REMARK 465     ARG G   493                                                      
REMARK 465     HIS G   494                                                      
REMARK 465     PRO G   495                                                      
REMARK 465     ASP G   496                                                      
REMARK 465     GLU G   497                                                      
REMARK 465     ALA G   498                                                      
REMARK 465     ALA G   499                                                      
REMARK 465     PHE G   500                                                      
REMARK 465     PHE G   501                                                      
REMARK 465     ASP G   502                                                      
REMARK 465     THR G   503                                                      
REMARK 465     ALA G   504                                                      
REMARK 465     SER G   505                                                      
REMARK 465     THR G   506                                                      
REMARK 465     GLY G   507                                                      
REMARK 465     LYS G   508                                                      
REMARK 465     THR G   509                                                      
REMARK 465     PHE G   510                                                      
REMARK 465     PRO G   511                                                      
REMARK 465     GLY G   512                                                      
REMARK 465     PHE G   513                                                      
REMARK 465     PHE G   514                                                      
REMARK 465     SER G   515                                                      
REMARK 465     PRO G   516                                                      
REMARK 465     MET G   517                                                      
REMARK 465     LEU G   518                                                      
REMARK 465     GLY G   519                                                      
REMARK 465     GLU G   520                                                      
REMARK 465     PHE G   521                                                      
REMARK 465     VAL G   522                                                      
REMARK 465     SER G   523                                                      
REMARK 465     GLU G   524                                                      
REMARK 465     THR G   525                                                      
REMARK 465     GLU G   526                                                      
REMARK 465     SER G   527                                                      
REMARK 465     ARG G   528                                                      
REMARK 465     GLY G   529                                                      
REMARK 465     SER G   530                                                      
REMARK 465     GLU G   531                                                      
REMARK 465     SER G   532                                                      
REMARK 465     GLY G   533                                                      
REMARK 465     ILE G   534                                                      
REMARK 465     PHE G   535                                                      
REMARK 465     THR G   536                                                      
REMARK 465     ASN G   537                                                      
REMARK 465     THR G   538                                                      
REMARK 465     LYS G   539                                                      
REMARK 465     GLU G   540                                                      
REMARK 465     SER G   541                                                      
REMARK 465     SER G   542                                                      
REMARK 465     SER G   543                                                      
REMARK 465     HIS G   544                                                      
REMARK 465     HIS G   545                                                      
REMARK 465     PRO G   546                                                      
REMARK 465     GLY G   547                                                      
REMARK 465     ILE G   548                                                      
REMARK 465     ALA G   549                                                      
REMARK 465     GLU G   550                                                      
REMARK 465     PHE G   551                                                      
REMARK 465     PRO G   552                                                      
REMARK 465     SER G   553                                                      
REMARK 465     ARG G   554                                                      
REMARK 465     GLY G   555                                                      
REMARK 465     LYS G   556                                                      
REMARK 465     SER G   557                                                      
REMARK 465     SER G   558                                                      
REMARK 465     SER G   559                                                      
REMARK 465     TYR G   560                                                      
REMARK 465     SER G   561                                                      
REMARK 465     LYS G   562                                                      
REMARK 465     GLN H     1                                                      
REMARK 465     GLY H     2                                                      
REMARK 465     VAL H     3                                                      
REMARK 465     ASN H     4                                                      
REMARK 465     ASP H     5                                                      
REMARK 465     ASN H     6                                                      
REMARK 465     GLU H     7                                                      
REMARK 465     GLU H     8                                                      
REMARK 465     GLY H     9                                                      
REMARK 465     PHE H    10                                                      
REMARK 465     PHE H    11                                                      
REMARK 465     SER H    12                                                      
REMARK 465     ALA H    13                                                      
REMARK 465     ARG H    14                                                      
REMARK 465     GLY H    15                                                      
REMARK 465     HIS H    16                                                      
REMARK 465     ARG H    17                                                      
REMARK 465     PRO H    18                                                      
REMARK 465     LEU H    19                                                      
REMARK 465     ASP H    20                                                      
REMARK 465     LYS H    21                                                      
REMARK 465     LYS H    22                                                      
REMARK 465     ARG H    23                                                      
REMARK 465     GLU H    24                                                      
REMARK 465     GLU H    25                                                      
REMARK 465     ALA H    26                                                      
REMARK 465     PRO H    27                                                      
REMARK 465     SER H    28                                                      
REMARK 465     LEU H    29                                                      
REMARK 465     ARG H    30                                                      
REMARK 465     PRO H    31                                                      
REMARK 465     ALA H    32                                                      
REMARK 465     PRO H    33                                                      
REMARK 465     PRO H    34                                                      
REMARK 465     PRO H    35                                                      
REMARK 465     ILE H    36                                                      
REMARK 465     SER H    37                                                      
REMARK 465     GLY H    38                                                      
REMARK 465     GLY H    39                                                      
REMARK 465     GLY H    40                                                      
REMARK 465     TYR H    41                                                      
REMARK 465     ARG H    42                                                      
REMARK 465     ALA H    43                                                      
REMARK 465     ARG H    44                                                      
REMARK 465     PRO H    45                                                      
REMARK 465     ALA H    46                                                      
REMARK 465     LYS H    47                                                      
REMARK 465     ALA H    48                                                      
REMARK 465     ALA H    49                                                      
REMARK 465     ALA H    50                                                      
REMARK 465     THR H    51                                                      
REMARK 465     GLN H    52                                                      
REMARK 465     LYS H    53                                                      
REMARK 465     LYS H    54                                                      
REMARK 465     VAL H    55                                                      
REMARK 465     GLU H    56                                                      
REMARK 465     ARG H    57                                                      
REMARK 465     PRO H   459                                                      
REMARK 465     GLN H   460                                                      
REMARK 465     GLN H   461                                                      
REMARK 465     TYR I     1                                                      
REMARK 465     GLU I   396                                                      
REMARK 465     GLY I   397                                                      
REMARK 465     GLN I   398                                                      
REMARK 465     GLN I   399                                                      
REMARK 465     HIS I   400                                                      
REMARK 465     HIS I   401                                                      
REMARK 465     LEU I   402                                                      
REMARK 465     GLY I   403                                                      
REMARK 465     GLY I   404                                                      
REMARK 465     ALA I   405                                                      
REMARK 465     LYS I   406                                                      
REMARK 465     GLN I   407                                                      
REMARK 465     ALA I   408                                                      
REMARK 465     GLY I   409                                                      
REMARK 465     ASP I   410                                                      
REMARK 465     VAL I   411                                                      
REMARK 465     ALA J     1                                                      
REMARK 465     ASP J     2                                                      
REMARK 465     SER J     3                                                      
REMARK 465     GLY J     4                                                      
REMARK 465     GLU J     5                                                      
REMARK 465     GLY J     6                                                      
REMARK 465     ASP J     7                                                      
REMARK 465     PHE J     8                                                      
REMARK 465     LEU J     9                                                      
REMARK 465     ALA J    10                                                      
REMARK 465     GLU J    11                                                      
REMARK 465     GLY J    12                                                      
REMARK 465     GLY J    13                                                      
REMARK 465     GLY J    14                                                      
REMARK 465     VAL J    15                                                      
REMARK 465     ARG J    16                                                      
REMARK 465     GLY J    17                                                      
REMARK 465     PRO J    18                                                      
REMARK 465     ARG J    19                                                      
REMARK 465     VAL J    20                                                      
REMARK 465     VAL J    21                                                      
REMARK 465     GLU J    22                                                      
REMARK 465     ARG J    23                                                      
REMARK 465     HIS J    24                                                      
REMARK 465     GLN J    25                                                      
REMARK 465     SER J    26                                                      
REMARK 465     LEU J   213                                                      
REMARK 465     VAL J   214                                                      
REMARK 465     PRO J   215                                                      
REMARK 465     GLY J   216                                                      
REMARK 465     ASN J   217                                                      
REMARK 465     PHE J   218                                                      
REMARK 465     LYS J   219                                                      
REMARK 465     SER J   220                                                      
REMARK 465     GLN J   221                                                      
REMARK 465     LEU J   222                                                      
REMARK 465     GLN J   223                                                      
REMARK 465     LYS J   224                                                      
REMARK 465     VAL J   225                                                      
REMARK 465     PRO J   226                                                      
REMARK 465     PRO J   227                                                      
REMARK 465     GLU J   228                                                      
REMARK 465     TRP J   229                                                      
REMARK 465     LYS J   230                                                      
REMARK 465     ALA J   231                                                      
REMARK 465     LEU J   232                                                      
REMARK 465     THR J   233                                                      
REMARK 465     ASP J   234                                                      
REMARK 465     MET J   235                                                      
REMARK 465     PRO J   236                                                      
REMARK 465     GLN J   237                                                      
REMARK 465     MET J   238                                                      
REMARK 465     ARG J   239                                                      
REMARK 465     MET J   240                                                      
REMARK 465     GLU J   241                                                      
REMARK 465     LEU J   242                                                      
REMARK 465     GLU J   243                                                      
REMARK 465     ARG J   244                                                      
REMARK 465     PRO J   245                                                      
REMARK 465     GLY J   246                                                      
REMARK 465     GLY J   247                                                      
REMARK 465     ASN J   248                                                      
REMARK 465     GLU J   249                                                      
REMARK 465     ILE J   250                                                      
REMARK 465     THR J   251                                                      
REMARK 465     ARG J   252                                                      
REMARK 465     GLY J   253                                                      
REMARK 465     GLY J   254                                                      
REMARK 465     SER J   255                                                      
REMARK 465     THR J   256                                                      
REMARK 465     SER J   257                                                      
REMARK 465     TYR J   258                                                      
REMARK 465     GLY J   259                                                      
REMARK 465     THR J   260                                                      
REMARK 465     GLY J   261                                                      
REMARK 465     SER J   262                                                      
REMARK 465     GLU J   263                                                      
REMARK 465     THR J   264                                                      
REMARK 465     GLU J   265                                                      
REMARK 465     SER J   266                                                      
REMARK 465     PRO J   267                                                      
REMARK 465     ARG J   268                                                      
REMARK 465     ASN J   269                                                      
REMARK 465     PRO J   270                                                      
REMARK 465     SER J   271                                                      
REMARK 465     SER J   272                                                      
REMARK 465     ALA J   273                                                      
REMARK 465     GLY J   274                                                      
REMARK 465     SER J   275                                                      
REMARK 465     TRP J   276                                                      
REMARK 465     ASN J   277                                                      
REMARK 465     SER J   278                                                      
REMARK 465     GLY J   279                                                      
REMARK 465     SER J   280                                                      
REMARK 465     SER J   281                                                      
REMARK 465     GLY J   282                                                      
REMARK 465     PRO J   283                                                      
REMARK 465     GLY J   284                                                      
REMARK 465     SER J   285                                                      
REMARK 465     THR J   286                                                      
REMARK 465     GLY J   287                                                      
REMARK 465     ASN J   288                                                      
REMARK 465     ARG J   289                                                      
REMARK 465     ASN J   290                                                      
REMARK 465     PRO J   291                                                      
REMARK 465     GLY J   292                                                      
REMARK 465     SER J   293                                                      
REMARK 465     SER J   294                                                      
REMARK 465     GLY J   295                                                      
REMARK 465     THR J   296                                                      
REMARK 465     GLY J   297                                                      
REMARK 465     GLY J   298                                                      
REMARK 465     THR J   299                                                      
REMARK 465     ALA J   300                                                      
REMARK 465     THR J   301                                                      
REMARK 465     TRP J   302                                                      
REMARK 465     LYS J   303                                                      
REMARK 465     PRO J   304                                                      
REMARK 465     GLY J   305                                                      
REMARK 465     SER J   306                                                      
REMARK 465     SER J   307                                                      
REMARK 465     GLY J   308                                                      
REMARK 465     PRO J   309                                                      
REMARK 465     GLY J   310                                                      
REMARK 465     SER J   311                                                      
REMARK 465     THR J   312                                                      
REMARK 465     GLY J   313                                                      
REMARK 465     SER J   314                                                      
REMARK 465     TRP J   315                                                      
REMARK 465     ASN J   316                                                      
REMARK 465     SER J   317                                                      
REMARK 465     GLY J   318                                                      
REMARK 465     SER J   319                                                      
REMARK 465     SER J   320                                                      
REMARK 465     GLY J   321                                                      
REMARK 465     THR J   322                                                      
REMARK 465     GLY J   323                                                      
REMARK 465     SER J   324                                                      
REMARK 465     THR J   325                                                      
REMARK 465     GLY J   326                                                      
REMARK 465     ASN J   327                                                      
REMARK 465     GLN J   328                                                      
REMARK 465     ASN J   329                                                      
REMARK 465     PRO J   330                                                      
REMARK 465     GLY J   331                                                      
REMARK 465     SER J   332                                                      
REMARK 465     PRO J   333                                                      
REMARK 465     ARG J   334                                                      
REMARK 465     PRO J   335                                                      
REMARK 465     GLY J   336                                                      
REMARK 465     SER J   337                                                      
REMARK 465     THR J   338                                                      
REMARK 465     GLY J   339                                                      
REMARK 465     THR J   340                                                      
REMARK 465     TRP J   341                                                      
REMARK 465     ASN J   342                                                      
REMARK 465     PRO J   343                                                      
REMARK 465     GLY J   344                                                      
REMARK 465     SER J   345                                                      
REMARK 465     SER J   346                                                      
REMARK 465     GLU J   347                                                      
REMARK 465     ARG J   348                                                      
REMARK 465     GLY J   349                                                      
REMARK 465     SER J   350                                                      
REMARK 465     ALA J   351                                                      
REMARK 465     GLY J   352                                                      
REMARK 465     HIS J   353                                                      
REMARK 465     TRP J   354                                                      
REMARK 465     THR J   355                                                      
REMARK 465     SER J   356                                                      
REMARK 465     GLU J   357                                                      
REMARK 465     SER J   358                                                      
REMARK 465     SER J   359                                                      
REMARK 465     VAL J   360                                                      
REMARK 465     SER J   361                                                      
REMARK 465     GLY J   362                                                      
REMARK 465     SER J   363                                                      
REMARK 465     THR J   364                                                      
REMARK 465     GLY J   365                                                      
REMARK 465     GLN J   366                                                      
REMARK 465     TRP J   367                                                      
REMARK 465     HIS J   368                                                      
REMARK 465     SER J   369                                                      
REMARK 465     GLU J   370                                                      
REMARK 465     SER J   371                                                      
REMARK 465     GLY J   372                                                      
REMARK 465     SER J   373                                                      
REMARK 465     PHE J   374                                                      
REMARK 465     ARG J   375                                                      
REMARK 465     PRO J   376                                                      
REMARK 465     ASP J   377                                                      
REMARK 465     SER J   378                                                      
REMARK 465     PRO J   379                                                      
REMARK 465     GLY J   380                                                      
REMARK 465     SER J   381                                                      
REMARK 465     GLY J   382                                                      
REMARK 465     ASN J   383                                                      
REMARK 465     ALA J   384                                                      
REMARK 465     ARG J   385                                                      
REMARK 465     PRO J   386                                                      
REMARK 465     ASN J   387                                                      
REMARK 465     ASN J   388                                                      
REMARK 465     PRO J   389                                                      
REMARK 465     ASP J   390                                                      
REMARK 465     TRP J   391                                                      
REMARK 465     GLY J   392                                                      
REMARK 465     THR J   393                                                      
REMARK 465     PHE J   394                                                      
REMARK 465     GLU J   395                                                      
REMARK 465     GLU J   396                                                      
REMARK 465     VAL J   397                                                      
REMARK 465     SER J   398                                                      
REMARK 465     GLY J   399                                                      
REMARK 465     ASN J   400                                                      
REMARK 465     VAL J   401                                                      
REMARK 465     SER J   402                                                      
REMARK 465     PRO J   403                                                      
REMARK 465     GLY J   404                                                      
REMARK 465     THR J   405                                                      
REMARK 465     ARG J   406                                                      
REMARK 465     ARG J   407                                                      
REMARK 465     GLU J   408                                                      
REMARK 465     TYR J   409                                                      
REMARK 465     HIS J   410                                                      
REMARK 465     THR J   411                                                      
REMARK 465     GLU J   412                                                      
REMARK 465     LYS J   413                                                      
REMARK 465     LEU J   414                                                      
REMARK 465     VAL J   415                                                      
REMARK 465     THR J   416                                                      
REMARK 465     SER J   417                                                      
REMARK 465     LYS J   418                                                      
REMARK 465     GLY J   419                                                      
REMARK 465     ASP J   420                                                      
REMARK 465     LYS J   421                                                      
REMARK 465     GLU J   422                                                      
REMARK 465     LEU J   423                                                      
REMARK 465     ARG J   424                                                      
REMARK 465     THR J   425                                                      
REMARK 465     GLY J   426                                                      
REMARK 465     LYS J   427                                                      
REMARK 465     GLU J   428                                                      
REMARK 465     LYS J   429                                                      
REMARK 465     VAL J   430                                                      
REMARK 465     THR J   431                                                      
REMARK 465     SER J   432                                                      
REMARK 465     GLY J   433                                                      
REMARK 465     SER J   434                                                      
REMARK 465     THR J   435                                                      
REMARK 465     THR J   436                                                      
REMARK 465     THR J   437                                                      
REMARK 465     THR J   438                                                      
REMARK 465     ARG J   439                                                      
REMARK 465     ARG J   440                                                      
REMARK 465     SER J   441                                                      
REMARK 465     CYS J   442                                                      
REMARK 465     SER J   443                                                      
REMARK 465     LYS J   444                                                      
REMARK 465     THR J   445                                                      
REMARK 465     VAL J   446                                                      
REMARK 465     THR J   447                                                      
REMARK 465     LYS J   448                                                      
REMARK 465     THR J   449                                                      
REMARK 465     VAL J   450                                                      
REMARK 465     ILE J   451                                                      
REMARK 465     GLY J   452                                                      
REMARK 465     PRO J   453                                                      
REMARK 465     ASP J   454                                                      
REMARK 465     GLY J   455                                                      
REMARK 465     HIS J   456                                                      
REMARK 465     LYS J   457                                                      
REMARK 465     GLU J   458                                                      
REMARK 465     VAL J   459                                                      
REMARK 465     THR J   460                                                      
REMARK 465     LYS J   461                                                      
REMARK 465     GLU J   462                                                      
REMARK 465     VAL J   463                                                      
REMARK 465     VAL J   464                                                      
REMARK 465     THR J   465                                                      
REMARK 465     SER J   466                                                      
REMARK 465     GLU J   467                                                      
REMARK 465     ASP J   468                                                      
REMARK 465     GLY J   469                                                      
REMARK 465     SER J   470                                                      
REMARK 465     ASP J   471                                                      
REMARK 465     CYS J   472                                                      
REMARK 465     PRO J   473                                                      
REMARK 465     GLU J   474                                                      
REMARK 465     ALA J   475                                                      
REMARK 465     MET J   476                                                      
REMARK 465     ASP J   477                                                      
REMARK 465     LEU J   478                                                      
REMARK 465     GLY J   479                                                      
REMARK 465     THR J   480                                                      
REMARK 465     LEU J   481                                                      
REMARK 465     SER J   482                                                      
REMARK 465     GLY J   483                                                      
REMARK 465     ILE J   484                                                      
REMARK 465     GLY J   485                                                      
REMARK 465     THR J   486                                                      
REMARK 465     LEU J   487                                                      
REMARK 465     ASP J   488                                                      
REMARK 465     GLY J   489                                                      
REMARK 465     PHE J   490                                                      
REMARK 465     ARG J   491                                                      
REMARK 465     HIS J   492                                                      
REMARK 465     ARG J   493                                                      
REMARK 465     HIS J   494                                                      
REMARK 465     PRO J   495                                                      
REMARK 465     ASP J   496                                                      
REMARK 465     GLU J   497                                                      
REMARK 465     ALA J   498                                                      
REMARK 465     ALA J   499                                                      
REMARK 465     PHE J   500                                                      
REMARK 465     PHE J   501                                                      
REMARK 465     ASP J   502                                                      
REMARK 465     THR J   503                                                      
REMARK 465     ALA J   504                                                      
REMARK 465     SER J   505                                                      
REMARK 465     THR J   506                                                      
REMARK 465     GLY J   507                                                      
REMARK 465     LYS J   508                                                      
REMARK 465     THR J   509                                                      
REMARK 465     PHE J   510                                                      
REMARK 465     PRO J   511                                                      
REMARK 465     GLY J   512                                                      
REMARK 465     PHE J   513                                                      
REMARK 465     PHE J   514                                                      
REMARK 465     SER J   515                                                      
REMARK 465     PRO J   516                                                      
REMARK 465     MET J   517                                                      
REMARK 465     LEU J   518                                                      
REMARK 465     GLY J   519                                                      
REMARK 465     GLU J   520                                                      
REMARK 465     PHE J   521                                                      
REMARK 465     VAL J   522                                                      
REMARK 465     SER J   523                                                      
REMARK 465     GLU J   524                                                      
REMARK 465     THR J   525                                                      
REMARK 465     GLU J   526                                                      
REMARK 465     SER J   527                                                      
REMARK 465     ARG J   528                                                      
REMARK 465     GLY J   529                                                      
REMARK 465     SER J   530                                                      
REMARK 465     GLU J   531                                                      
REMARK 465     SER J   532                                                      
REMARK 465     GLY J   533                                                      
REMARK 465     ILE J   534                                                      
REMARK 465     PHE J   535                                                      
REMARK 465     THR J   536                                                      
REMARK 465     ASN J   537                                                      
REMARK 465     THR J   538                                                      
REMARK 465     LYS J   539                                                      
REMARK 465     GLU J   540                                                      
REMARK 465     SER J   541                                                      
REMARK 465     SER J   542                                                      
REMARK 465     SER J   543                                                      
REMARK 465     HIS J   544                                                      
REMARK 465     HIS J   545                                                      
REMARK 465     PRO J   546                                                      
REMARK 465     GLY J   547                                                      
REMARK 465     ILE J   548                                                      
REMARK 465     ALA J   549                                                      
REMARK 465     GLU J   550                                                      
REMARK 465     PHE J   551                                                      
REMARK 465     PRO J   552                                                      
REMARK 465     SER J   553                                                      
REMARK 465     ARG J   554                                                      
REMARK 465     GLY J   555                                                      
REMARK 465     LYS J   556                                                      
REMARK 465     SER J   557                                                      
REMARK 465     SER J   558                                                      
REMARK 465     SER J   559                                                      
REMARK 465     TYR J   560                                                      
REMARK 465     SER J   561                                                      
REMARK 465     LYS J   562                                                      
REMARK 465     GLN K     1                                                      
REMARK 465     GLY K     2                                                      
REMARK 465     VAL K     3                                                      
REMARK 465     ASN K     4                                                      
REMARK 465     ASP K     5                                                      
REMARK 465     ASN K     6                                                      
REMARK 465     GLU K     7                                                      
REMARK 465     GLU K     8                                                      
REMARK 465     GLY K     9                                                      
REMARK 465     PHE K    10                                                      
REMARK 465     PHE K    11                                                      
REMARK 465     SER K    12                                                      
REMARK 465     ALA K    13                                                      
REMARK 465     ARG K    14                                                      
REMARK 465     GLY K    15                                                      
REMARK 465     HIS K    16                                                      
REMARK 465     ARG K    17                                                      
REMARK 465     PRO K    18                                                      
REMARK 465     LEU K    19                                                      
REMARK 465     ASP K    20                                                      
REMARK 465     LYS K    21                                                      
REMARK 465     LYS K    22                                                      
REMARK 465     ARG K    23                                                      
REMARK 465     GLU K    24                                                      
REMARK 465     GLU K    25                                                      
REMARK 465     ALA K    26                                                      
REMARK 465     PRO K    27                                                      
REMARK 465     SER K    28                                                      
REMARK 465     LEU K    29                                                      
REMARK 465     ARG K    30                                                      
REMARK 465     PRO K    31                                                      
REMARK 465     ALA K    32                                                      
REMARK 465     PRO K    33                                                      
REMARK 465     PRO K    34                                                      
REMARK 465     PRO K    35                                                      
REMARK 465     ILE K    36                                                      
REMARK 465     SER K    37                                                      
REMARK 465     GLY K    38                                                      
REMARK 465     GLY K    39                                                      
REMARK 465     GLY K    40                                                      
REMARK 465     TYR K    41                                                      
REMARK 465     ARG K    42                                                      
REMARK 465     ALA K    43                                                      
REMARK 465     ARG K    44                                                      
REMARK 465     PRO K    45                                                      
REMARK 465     ALA K    46                                                      
REMARK 465     LYS K    47                                                      
REMARK 465     ALA K    48                                                      
REMARK 465     ALA K    49                                                      
REMARK 465     ALA K    50                                                      
REMARK 465     THR K    51                                                      
REMARK 465     GLN K    52                                                      
REMARK 465     LYS K    53                                                      
REMARK 465     LYS K    54                                                      
REMARK 465     VAL K    55                                                      
REMARK 465     GLU K    56                                                      
REMARK 465     ARG K    57                                                      
REMARK 465     PRO K   459                                                      
REMARK 465     GLN K   460                                                      
REMARK 465     GLN K   461                                                      
REMARK 465     TYR L     1                                                      
REMARK 465     VAL L     2                                                      
REMARK 465     ALA L     3                                                      
REMARK 465     THR L     4                                                      
REMARK 465     GLU L   396                                                      
REMARK 465     GLY L   397                                                      
REMARK 465     GLN L   398                                                      
REMARK 465     GLN L   399                                                      
REMARK 465     HIS L   400                                                      
REMARK 465     HIS L   401                                                      
REMARK 465     LEU L   402                                                      
REMARK 465     GLY L   403                                                      
REMARK 465     GLY L   404                                                      
REMARK 465     ALA L   405                                                      
REMARK 465     LYS L   406                                                      
REMARK 465     GLN L   407                                                      
REMARK 465     ALA L   408                                                      
REMARK 465     GLY L   409                                                      
REMARK 465     ASP L   410                                                      
REMARK 465     VAL L   411                                                      
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    ILE I    10     OH   TYR I    18              1.65            
REMARK 500   ND2  ASN B   364     C1   NAG B   470              1.70            
REMARK 500   O    TYR A   108     OG   SER A   112              1.74            
REMARK 500   OD1  ASP B   154     OH   TYR C    96              1.79            
REMARK 500   O    GLN J    60     OD1  ASN J    64              1.81            
REMARK 500   ND2  ASN K   364     C1   NAG K   470              1.85            
REMARK 500   OH   TYR J   108     C    THR L    83              1.85            
REMARK 500   OD1  ASP E   241     OG1  THR E   244              1.85            
REMARK 500   OH   TYR B   239     O    GLY B   287              1.85            
REMARK 500   OH   TYR J   108     N    LEU L    84              1.87            
REMARK 500   OG1  THR K   423     OD1  ASP K   425              1.99            
REMARK 500   OG   SER E   222     N    MET E   242              2.01            
REMARK 500   ND2  ASN L    52     O5   NAG L   570              2.07            
REMARK 500   OE2  GLU H   210     N    GLU H   212              2.09            
REMARK 500   O    HIS C   217     OG1  THR C   224              2.10            
REMARK 500   OD1  ASP H   257     OG   SER H   259              2.10            
REMARK 500   OD1  ASP K   432     OG   SER K   443              2.10            
REMARK 500   ND1  HIS F   234     O    VAL F   267              2.11            
REMARK 500   OE2  GLU K   210     N    GLU K   212              2.14            
REMARK 500   CB   GLU L    56     O3   NAG L   570              2.15            
REMARK 500   OH   TYR F   262     OD1  ASP F   288              2.16            
REMARK 500   O    VAL E   199     OD2  ASP F   141              2.16            
REMARK 500   OG1  THR L   221     OG1  THR L   223              2.16            
REMARK 500   O    GLU I    51     OG1  THR I    54              2.16            
REMARK 500   OE1  GLU C   231     OH   TYR C   274              2.16            
REMARK 500   N    GLY F   296     OD2  ASP F   301              2.18            
REMARK 500   O    ASN B   160     OG1  THR B   163              2.19            
REMARK 500   OD1  ASP E   432     OG   SER E   443              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE2  GLU I    72     NE2  HIS J    84     1455     2.15            
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    PRO C  70   C   -  N   -  CD  ANGL. DEV. = -17.8 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    ASP A  30       90.18    -38.67                                   
REMARK 500    ASP A  32       35.76    -93.44                                   
REMARK 500    ASN A  42      -19.26     85.40                                   
REMARK 500    SER A 164      -43.51   -130.21                                   
REMARK 500    SER A 166      -75.86    -68.60                                   
REMARK 500    LEU A 194       62.70     62.96                                   
REMARK 500    PRO A 195      -81.00    -89.07                                   
REMARK 500    SER A 196      -55.19    -28.17                                   
REMARK 500    PRO B  60      113.41    -30.01                                   
REMARK 500    LEU B  72      -61.79   -106.63                                   
REMARK 500    ASN B 103      -62.11    -96.62                                   
REMARK 500    LYS B 127      -63.41   -106.49                                   
REMARK 500    VAL B 138      -60.20   -104.73                                   
REMARK 500    GLU B 141        7.02   -159.37                                   
REMARK 500    SER B 159      -57.98   -145.29                                   
REMARK 500    GLU B 210     -169.38   -176.17                                   
REMARK 500    GLU B 212      -72.72    -80.84                                   
REMARK 500    GLU B 213      -45.30    -28.36                                   
REMARK 500    GLN B 228       88.70   -153.39                                   
REMARK 500    SER B 232       49.42    -91.28                                   
REMARK 500    VAL B 233      138.10   -173.27                                   
REMARK 500    GLN B 256       -5.48   -153.69                                   
REMARK 500    ASP B 257     -168.55   -161.47                                   
REMARK 500    SER B 259      -41.06    -16.28                                   
REMARK 500    ASP B 281       95.11    -14.41                                   
REMARK 500    ASN B 296      -71.01    -57.91                                   
REMARK 500    ASN B 351       97.66    -45.17                                   
REMARK 500    ARG B 380       87.64   -162.13                                   
REMARK 500    ASP B 398       39.78    -93.47                                   
REMARK 500    ASN B 405       40.97   -152.59                                   
REMARK 500    ARG B 406       44.88     71.32                                   
REMARK 500    CYS B 407      -51.46   -129.97                                   
REMARK 500    ALA B 409      -61.49    -94.84                                   
REMARK 500    ASP B 425       48.32    -85.50                                   
REMARK 500    MET B 426      -23.38   -155.88                                   
REMARK 500    THR B 431     -163.90   -101.72                                   
REMARK 500    ASP B 432       55.75   -107.40                                   
REMARK 500    VAL B 435       75.91    -62.82                                   
REMARK 500    LYS B 453      148.93   -172.97                                   
REMARK 500    ARG B 455      149.42   -170.18                                   
REMARK 500    PHE B 457      -70.37    -92.11                                   
REMARK 500    THR C  21      150.21    -48.77                                   
REMARK 500    ASN C  69       67.33     82.21                                   
REMARK 500    PRO C  70       81.30    -36.46                                   
REMARK 500    ASP C  71       54.78     33.76                                   
REMARK 500    LYS C  75      118.79    -36.15                                   
REMARK 500    ALA C 133       16.01    -69.65                                   
REMARK 500    CYS C 135       44.94   -154.04                                   
REMARK 500    HIS C 146      156.20    -42.14                                   
REMARK 500    LYS C 159       15.85    -67.05                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     247 RAMACHANDRAN OUTLIERS.                        
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 B 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 381   OD1                                                    
REMARK 620 2 ASP B 381   OD2  46.1                                              
REMARK 620 3 ASP B 383   OD1 103.5  68.3                                        
REMARK 620 4 TRP B 385   O   141.9 138.0  70.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 318   OD1                                                    
REMARK 620 2 ASP C 320   OD1  86.1                                              
REMARK 620 3 PHE C 322   O   112.3  83.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 381   OD1                                                    
REMARK 620 2 ASP E 381   OD2  43.7                                              
REMARK 620 3 ASP E 383   OD1 114.9  75.5                                        
REMARK 620 4 TRP E 385   O   141.3 169.7  95.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 318   OD2                                                    
REMARK 620 2 ASP F 320   OD2  85.1                                              
REMARK 620 3 GLY F 324   O    62.8 120.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H 381   OD1                                                    
REMARK 620 2 ASP H 381   OD2  49.8                                              
REMARK 620 3 ASP H 383   OD1 106.6  71.6                                        
REMARK 620 4 TRP H 385   O   142.1 163.2  91.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA I 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP I 318   OD1                                                    
REMARK 620 2 ASP I 320   OD2  70.0                                              
REMARK 620 3 PHE I 322   O   128.7  59.8                                        
REMARK 620 4 GLY I 324   O   107.6 104.2  76.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA K 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP K 381   OD1                                                    
REMARK 620 2 ASP K 381   OD2  53.2                                              
REMARK 620 3 ASP K 383   OD1 124.1  76.3                                        
REMARK 620 4 TRP K 385   O   149.0 143.2  67.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP L 318   OD1                                                    
REMARK 620 2 ASP L 318   OD2  48.7                                              
REMARK 620 3 ASP L 320   OD2  71.4 111.6                                        
REMARK 620 4 PHE L 322   O   122.8 110.0  74.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 470                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 471                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 473                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 474                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL B 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA B 479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL B 478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA B 480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 470                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG E 471                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA E 472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN E 473                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG E 475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN E 474                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG E 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL E 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA E 479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL E 478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA E 480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG H 470                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG H 471                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA H 472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN H 473                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN H 474                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG K 470                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG K 471                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA K 472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN K 473                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG K 475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN K 474                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG K 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL K 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA K 479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL K 478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA K 480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG L 570                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG L 571                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA I 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA K 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 601                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1M1J   RELATED DB: PDB                                   
REMARK 900 CHICKEN FIBRINOGEN                                                   
REMARK 900 RELATED ID: 1FZC   RELATED DB: PDB                                   
REMARK 900 HUMAN FRAGMENT D-DIMER                                               
REMARK 900 RELATED ID: 1DEQ   RELATED DB: PDB                                   
REMARK 900 BOVINE FIBRINOGEN                                                    
REMARK 900 RELATED ID: 2A45   RELATED DB: PDB                                   
REMARK 900 HUMAN THROMBIN-FIBRINOGEN FRAGMENT E COMPLEX                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE FOR CHAINS C,F,I,L BELONGS TO ISOFORM 2 OF FIBRINOGEN   
REMARK 999 GAMMA CHAIN (UNP ENTRY P02679-2).                                    
DBREF  3GHG A    1   562  UNP    P02671   FIBA_HUMAN      20    581             
DBREF  3GHG B    1   461  UNP    P02675   FIBB_HUMAN      31    491             
DBREF  3GHG C    1   411  UNP    P02679   FIBG_HUMAN      27    434             
DBREF  3GHG D    1   562  UNP    P02671   FIBA_HUMAN      20    581             
DBREF  3GHG E    1   461  UNP    P02675   FIBB_HUMAN      31    491             
DBREF  3GHG F    1   411  UNP    P02679   FIBG_HUMAN      27    434             
DBREF  3GHG G    1   562  UNP    P02671   FIBA_HUMAN      20    581             
DBREF  3GHG H    1   461  UNP    P02675   FIBB_HUMAN      31    491             
DBREF  3GHG I    1   411  UNP    P02679   FIBG_HUMAN      27    434             
DBREF  3GHG J    1   562  UNP    P02671   FIBA_HUMAN      20    581             
DBREF  3GHG K    1   461  UNP    P02675   FIBB_HUMAN      31    491             
DBREF  3GHG L    1   411  UNP    P02679   FIBG_HUMAN      27    434             
SEQADV 3GHG ALA C  408  UNP  P02679              SEE REMARK 999                 
SEQADV 3GHG GLY C  409  UNP  P02679              SEE REMARK 999                 
SEQADV 3GHG ASP C  410  UNP  P02679              SEE REMARK 999                 
SEQADV 3GHG ALA F  408  UNP  P02679              SEE REMARK 999                 
SEQADV 3GHG GLY F  409  UNP  P02679              SEE REMARK 999                 
SEQADV 3GHG ASP F  410  UNP  P02679              SEE REMARK 999                 
SEQADV 3GHG ALA I  408  UNP  P02679              SEE REMARK 999                 
SEQADV 3GHG GLY I  409  UNP  P02679              SEE REMARK 999                 
SEQADV 3GHG ASP I  410  UNP  P02679              SEE REMARK 999                 
SEQADV 3GHG ALA L  408  UNP  P02679              SEE REMARK 999                 
SEQADV 3GHG GLY L  409  UNP  P02679              SEE REMARK 999                 
SEQADV 3GHG ASP L  410  UNP  P02679              SEE REMARK 999                 
SEQRES   1 A  562  ALA ASP SER GLY GLU GLY ASP PHE LEU ALA GLU GLY GLY          
SEQRES   2 A  562  GLY VAL ARG GLY PRO ARG VAL VAL GLU ARG HIS GLN SER          
SEQRES   3 A  562  ALA CYS LYS ASP SER ASP TRP PRO PHE CYS SER ASP GLU          
SEQRES   4 A  562  ASP TRP ASN TYR LYS CYS PRO SER GLY CYS ARG MET LYS          
SEQRES   5 A  562  GLY LEU ILE ASP GLU VAL ASN GLN ASP PHE THR ASN ARG          
SEQRES   6 A  562  ILE ASN LYS LEU LYS ASN SER LEU PHE GLU TYR GLN LYS          
SEQRES   7 A  562  ASN ASN LYS ASP SER HIS SER LEU THR THR ASN ILE MET          
SEQRES   8 A  562  GLU ILE LEU ARG GLY ASP PHE SER SER ALA ASN ASN ARG          
SEQRES   9 A  562  ASP ASN THR TYR ASN ARG VAL SER GLU ASP LEU ARG SER          
SEQRES  10 A  562  ARG ILE GLU VAL LEU LYS ARG LYS VAL ILE GLU LYS VAL          
SEQRES  11 A  562  GLN HIS ILE GLN LEU LEU GLN LYS ASN VAL ARG ALA GLN          
SEQRES  12 A  562  LEU VAL ASP MET LYS ARG LEU GLU VAL ASP ILE ASP ILE          
SEQRES  13 A  562  LYS ILE ARG SER CYS ARG GLY SER CYS SER ARG ALA LEU          
SEQRES  14 A  562  ALA ARG GLU VAL ASP LEU LYS ASP TYR GLU ASP GLN GLN          
SEQRES  15 A  562  LYS GLN LEU GLU GLN VAL ILE ALA LYS ASP LEU LEU PRO          
SEQRES  16 A  562  SER ARG ASP ARG GLN HIS LEU PRO LEU ILE LYS MET LYS          
SEQRES  17 A  562  PRO VAL PRO ASP LEU VAL PRO GLY ASN PHE LYS SER GLN          
SEQRES  18 A  562  LEU GLN LYS VAL PRO PRO GLU TRP LYS ALA LEU THR ASP          
SEQRES  19 A  562  MET PRO GLN MET ARG MET GLU LEU GLU ARG PRO GLY GLY          
SEQRES  20 A  562  ASN GLU ILE THR ARG GLY GLY SER THR SER TYR GLY THR          
SEQRES  21 A  562  GLY SER GLU THR GLU SER PRO ARG ASN PRO SER SER ALA          
SEQRES  22 A  562  GLY SER TRP ASN SER GLY SER SER GLY PRO GLY SER THR          
SEQRES  23 A  562  GLY ASN ARG ASN PRO GLY SER SER GLY THR GLY GLY THR          
SEQRES  24 A  562  ALA THR TRP LYS PRO GLY SER SER GLY PRO GLY SER THR          
SEQRES  25 A  562  GLY SER TRP ASN SER GLY SER SER GLY THR GLY SER THR          
SEQRES  26 A  562  GLY ASN GLN ASN PRO GLY SER PRO ARG PRO GLY SER THR          
SEQRES  27 A  562  GLY THR TRP ASN PRO GLY SER SER GLU ARG GLY SER ALA          
SEQRES  28 A  562  GLY HIS TRP THR SER GLU SER SER VAL SER GLY SER THR          
SEQRES  29 A  562  GLY GLN TRP HIS SER GLU SER GLY SER PHE ARG PRO ASP          
SEQRES  30 A  562  SER PRO GLY SER GLY ASN ALA ARG PRO ASN ASN PRO ASP          
SEQRES  31 A  562  TRP GLY THR PHE GLU GLU VAL SER GLY ASN VAL SER PRO          
SEQRES  32 A  562  GLY THR ARG ARG GLU TYR HIS THR GLU LYS LEU VAL THR          
SEQRES  33 A  562  SER LYS GLY ASP LYS GLU LEU ARG THR GLY LYS GLU LYS          
SEQRES  34 A  562  VAL THR SER GLY SER THR THR THR THR ARG ARG SER CYS          
SEQRES  35 A  562  SER LYS THR VAL THR LYS THR VAL ILE GLY PRO ASP GLY          
SEQRES  36 A  562  HIS LYS GLU VAL THR LYS GLU VAL VAL THR SER GLU ASP          
SEQRES  37 A  562  GLY SER ASP CYS PRO GLU ALA MET ASP LEU GLY THR LEU          
SEQRES  38 A  562  SER GLY ILE GLY THR LEU ASP GLY PHE ARG HIS ARG HIS          
SEQRES  39 A  562  PRO ASP GLU ALA ALA PHE PHE ASP THR ALA SER THR GLY          
SEQRES  40 A  562  LYS THR PHE PRO GLY PHE PHE SER PRO MET LEU GLY GLU          
SEQRES  41 A  562  PHE VAL SER GLU THR GLU SER ARG GLY SER GLU SER GLY          
SEQRES  42 A  562  ILE PHE THR ASN THR LYS GLU SER SER SER HIS HIS PRO          
SEQRES  43 A  562  GLY ILE ALA GLU PHE PRO SER ARG GLY LYS SER SER SER          
SEQRES  44 A  562  TYR SER LYS                                                  
SEQRES   1 B  461  GLN GLY VAL ASN ASP ASN GLU GLU GLY PHE PHE SER ALA          
SEQRES   2 B  461  ARG GLY HIS ARG PRO LEU ASP LYS LYS ARG GLU GLU ALA          
SEQRES   3 B  461  PRO SER LEU ARG PRO ALA PRO PRO PRO ILE SER GLY GLY          
SEQRES   4 B  461  GLY TYR ARG ALA ARG PRO ALA LYS ALA ALA ALA THR GLN          
SEQRES   5 B  461  LYS LYS VAL GLU ARG LYS ALA PRO ASP ALA GLY GLY CYS          
SEQRES   6 B  461  LEU HIS ALA ASP PRO ASP LEU GLY VAL LEU CYS PRO THR          
SEQRES   7 B  461  GLY CYS GLN LEU GLN GLU ALA LEU LEU GLN GLN GLU ARG          
SEQRES   8 B  461  PRO ILE ARG ASN SER VAL ASP GLU LEU ASN ASN ASN VAL          
SEQRES   9 B  461  GLU ALA VAL SER GLN THR SER SER SER SER PHE GLN TYR          
SEQRES  10 B  461  MET TYR LEU LEU LYS ASP LEU TRP GLN LYS ARG GLN LYS          
SEQRES  11 B  461  GLN VAL LYS ASP ASN GLU ASN VAL VAL ASN GLU TYR SER          
SEQRES  12 B  461  SER GLU LEU GLU LYS HIS GLN LEU TYR ILE ASP GLU THR          
SEQRES  13 B  461  VAL ASN SER ASN ILE PRO THR ASN LEU ARG VAL LEU ARG          
SEQRES  14 B  461  SER ILE LEU GLU ASN LEU ARG SER LYS ILE GLN LYS LEU          
SEQRES  15 B  461  GLU SER ASP VAL SER ALA GLN MET GLU TYR CYS ARG THR          
SEQRES  16 B  461  PRO CYS THR VAL SER CYS ASN ILE PRO VAL VAL SER GLY          
SEQRES  17 B  461  LYS GLU CYS GLU GLU ILE ILE ARG LYS GLY GLY GLU THR          
SEQRES  18 B  461  SER GLU MET TYR LEU ILE GLN PRO ASP SER SER VAL LYS          
SEQRES  19 B  461  PRO TYR ARG VAL TYR CYS ASP MET ASN THR GLU ASN GLY          
SEQRES  20 B  461  GLY TRP THR VAL ILE GLN ASN ARG GLN ASP GLY SER VAL          
SEQRES  21 B  461  ASP PHE GLY ARG LYS TRP ASP PRO TYR LYS GLN GLY PHE          
SEQRES  22 B  461  GLY ASN VAL ALA THR ASN THR ASP GLY LYS ASN TYR CYS          
SEQRES  23 B  461  GLY LEU PRO GLY GLU TYR TRP LEU GLY ASN ASP LYS ILE          
SEQRES  24 B  461  SER GLN LEU THR ARG MET GLY PRO THR GLU LEU LEU ILE          
SEQRES  25 B  461  GLU MET GLU ASP TRP LYS GLY ASP LYS VAL LYS ALA HIS          
SEQRES  26 B  461  TYR GLY GLY PHE THR VAL GLN ASN GLU ALA ASN LYS TYR          
SEQRES  27 B  461  GLN ILE SER VAL ASN LYS TYR ARG GLY THR ALA GLY ASN          
SEQRES  28 B  461  ALA LEU MET ASP GLY ALA SER GLN LEU MET GLY GLU ASN          
SEQRES  29 B  461  ARG THR MET THR ILE HIS ASN GLY MET PHE PHE SER THR          
SEQRES  30 B  461  TYR ASP ARG ASP ASN ASP GLY TRP LEU THR SER ASP PRO          
SEQRES  31 B  461  ARG LYS GLN CYS SER LYS GLU ASP GLY GLY GLY TRP TRP          
SEQRES  32 B  461  TYR ASN ARG CYS HIS ALA ALA ASN PRO ASN GLY ARG TYR          
SEQRES  33 B  461  TYR TRP GLY GLY GLN TYR THR TRP ASP MET ALA LYS HIS          
SEQRES  34 B  461  GLY THR ASP ASP GLY VAL VAL TRP MET ASN TRP LYS GLY          
SEQRES  35 B  461  SER TRP TYR SER MET ARG LYS MET SER MET LYS ILE ARG          
SEQRES  36 B  461  PRO PHE PHE PRO GLN GLN                                      
SEQRES   1 C  411  TYR VAL ALA THR ARG ASP ASN CYS CYS ILE LEU ASP GLU          
SEQRES   2 C  411  ARG PHE GLY SER TYR CYS PRO THR THR CYS GLY ILE ALA          
SEQRES   3 C  411  ASP PHE LEU SER THR TYR GLN THR LYS VAL ASP LYS ASP          
SEQRES   4 C  411  LEU GLN SER LEU GLU ASP ILE LEU HIS GLN VAL GLU ASN          
SEQRES   5 C  411  LYS THR SER GLU VAL LYS GLN LEU ILE LYS ALA ILE GLN          
SEQRES   6 C  411  LEU THR TYR ASN PRO ASP GLU SER SER LYS PRO ASN MET          
SEQRES   7 C  411  ILE ASP ALA ALA THR LEU LYS SER ARG LYS MET LEU GLU          
SEQRES   8 C  411  GLU ILE MET LYS TYR GLU ALA SER ILE LEU THR HIS ASP          
SEQRES   9 C  411  SER SER ILE ARG TYR LEU GLN GLU ILE TYR ASN SER ASN          
SEQRES  10 C  411  ASN GLN LYS ILE VAL ASN LEU LYS GLU LYS VAL ALA GLN          
SEQRES  11 C  411  LEU GLU ALA GLN CYS GLN GLU PRO CYS LYS ASP THR VAL          
SEQRES  12 C  411  GLN ILE HIS ASP ILE THR GLY LYS ASP CYS GLN ASP ILE          
SEQRES  13 C  411  ALA ASN LYS GLY ALA LYS GLN SER GLY LEU TYR PHE ILE          
SEQRES  14 C  411  LYS PRO LEU LYS ALA ASN GLN GLN PHE LEU VAL TYR CYS          
SEQRES  15 C  411  GLU ILE ASP GLY SER GLY ASN GLY TRP THR VAL PHE GLN          
SEQRES  16 C  411  LYS ARG LEU ASP GLY SER VAL ASP PHE LYS LYS ASN TRP          
SEQRES  17 C  411  ILE GLN TYR LYS GLU GLY PHE GLY HIS LEU SER PRO THR          
SEQRES  18 C  411  GLY THR THR GLU PHE TRP LEU GLY ASN GLU LYS ILE HIS          
SEQRES  19 C  411  LEU ILE SER THR GLN SER ALA ILE PRO TYR ALA LEU ARG          
SEQRES  20 C  411  VAL GLU LEU GLU ASP TRP ASN GLY ARG THR SER THR ALA          
SEQRES  21 C  411  ASP TYR ALA MET PHE LYS VAL GLY PRO GLU ALA ASP LYS          
SEQRES  22 C  411  TYR ARG LEU THR TYR ALA TYR PHE ALA GLY GLY ASP ALA          
SEQRES  23 C  411  GLY ASP ALA PHE ASP GLY PHE ASP PHE GLY ASP ASP PRO          
SEQRES  24 C  411  SER ASP LYS PHE PHE THR SER HIS ASN GLY MET GLN PHE          
SEQRES  25 C  411  SER THR TRP ASP ASN ASP ASN ASP LYS PHE GLU GLY ASN          
SEQRES  26 C  411  CYS ALA GLU GLN ASP GLY SER GLY TRP TRP MET ASN LYS          
SEQRES  27 C  411  CYS HIS ALA GLY HIS LEU ASN GLY VAL TYR TYR GLN GLY          
SEQRES  28 C  411  GLY THR TYR SER LYS ALA SER THR PRO ASN GLY TYR ASP          
SEQRES  29 C  411  ASN GLY ILE ILE TRP ALA THR TRP LYS THR ARG TRP TYR          
SEQRES  30 C  411  SER MET LYS LYS THR THR MET LYS ILE ILE PRO PHE ASN          
SEQRES  31 C  411  ARG LEU THR ILE GLY GLU GLY GLN GLN HIS HIS LEU GLY          
SEQRES  32 C  411  GLY ALA LYS GLN ALA GLY ASP VAL                              
SEQRES   1 D  562  ALA ASP SER GLY GLU GLY ASP PHE LEU ALA GLU GLY GLY          
SEQRES   2 D  562  GLY VAL ARG GLY PRO ARG VAL VAL GLU ARG HIS GLN SER          
SEQRES   3 D  562  ALA CYS LYS ASP SER ASP TRP PRO PHE CYS SER ASP GLU          
SEQRES   4 D  562  ASP TRP ASN TYR LYS CYS PRO SER GLY CYS ARG MET LYS          
SEQRES   5 D  562  GLY LEU ILE ASP GLU VAL ASN GLN ASP PHE THR ASN ARG          
SEQRES   6 D  562  ILE ASN LYS LEU LYS ASN SER LEU PHE GLU TYR GLN LYS          
SEQRES   7 D  562  ASN ASN LYS ASP SER HIS SER LEU THR THR ASN ILE MET          
SEQRES   8 D  562  GLU ILE LEU ARG GLY ASP PHE SER SER ALA ASN ASN ARG          
SEQRES   9 D  562  ASP ASN THR TYR ASN ARG VAL SER GLU ASP LEU ARG SER          
SEQRES  10 D  562  ARG ILE GLU VAL LEU LYS ARG LYS VAL ILE GLU LYS VAL          
SEQRES  11 D  562  GLN HIS ILE GLN LEU LEU GLN LYS ASN VAL ARG ALA GLN          
SEQRES  12 D  562  LEU VAL ASP MET LYS ARG LEU GLU VAL ASP ILE ASP ILE          
SEQRES  13 D  562  LYS ILE ARG SER CYS ARG GLY SER CYS SER ARG ALA LEU          
SEQRES  14 D  562  ALA ARG GLU VAL ASP LEU LYS ASP TYR GLU ASP GLN GLN          
SEQRES  15 D  562  LYS GLN LEU GLU GLN VAL ILE ALA LYS ASP LEU LEU PRO          
SEQRES  16 D  562  SER ARG ASP ARG GLN HIS LEU PRO LEU ILE LYS MET LYS          
SEQRES  17 D  562  PRO VAL PRO ASP LEU VAL PRO GLY ASN PHE LYS SER GLN          
SEQRES  18 D  562  LEU GLN LYS VAL PRO PRO GLU TRP LYS ALA LEU THR ASP          
SEQRES  19 D  562  MET PRO GLN MET ARG MET GLU LEU GLU ARG PRO GLY GLY          
SEQRES  20 D  562  ASN GLU ILE THR ARG GLY GLY SER THR SER TYR GLY THR          
SEQRES  21 D  562  GLY SER GLU THR GLU SER PRO ARG ASN PRO SER SER ALA          
SEQRES  22 D  562  GLY SER TRP ASN SER GLY SER SER GLY PRO GLY SER THR          
SEQRES  23 D  562  GLY ASN ARG ASN PRO GLY SER SER GLY THR GLY GLY THR          
SEQRES  24 D  562  ALA THR TRP LYS PRO GLY SER SER GLY PRO GLY SER THR          
SEQRES  25 D  562  GLY SER TRP ASN SER GLY SER SER GLY THR GLY SER THR          
SEQRES  26 D  562  GLY ASN GLN ASN PRO GLY SER PRO ARG PRO GLY SER THR          
SEQRES  27 D  562  GLY THR TRP ASN PRO GLY SER SER GLU ARG GLY SER ALA          
SEQRES  28 D  562  GLY HIS TRP THR SER GLU SER SER VAL SER GLY SER THR          
SEQRES  29 D  562  GLY GLN TRP HIS SER GLU SER GLY SER PHE ARG PRO ASP          
SEQRES  30 D  562  SER PRO GLY SER GLY ASN ALA ARG PRO ASN ASN PRO ASP          
SEQRES  31 D  562  TRP GLY THR PHE GLU GLU VAL SER GLY ASN VAL SER PRO          
SEQRES  32 D  562  GLY THR ARG ARG GLU TYR HIS THR GLU LYS LEU VAL THR          
SEQRES  33 D  562  SER LYS GLY ASP LYS GLU LEU ARG THR GLY LYS GLU LYS          
SEQRES  34 D  562  VAL THR SER GLY SER THR THR THR THR ARG ARG SER CYS          
SEQRES  35 D  562  SER LYS THR VAL THR LYS THR VAL ILE GLY PRO ASP GLY          
SEQRES  36 D  562  HIS LYS GLU VAL THR LYS GLU VAL VAL THR SER GLU ASP          
SEQRES  37 D  562  GLY SER ASP CYS PRO GLU ALA MET ASP LEU GLY THR LEU          
SEQRES  38 D  562  SER GLY ILE GLY THR LEU ASP GLY PHE ARG HIS ARG HIS          
SEQRES  39 D  562  PRO ASP GLU ALA ALA PHE PHE ASP THR ALA SER THR GLY          
SEQRES  40 D  562  LYS THR PHE PRO GLY PHE PHE SER PRO MET LEU GLY GLU          
SEQRES  41 D  562  PHE VAL SER GLU THR GLU SER ARG GLY SER GLU SER GLY          
SEQRES  42 D  562  ILE PHE THR ASN THR LYS GLU SER SER SER HIS HIS PRO          
SEQRES  43 D  562  GLY ILE ALA GLU PHE PRO SER ARG GLY LYS SER SER SER          
SEQRES  44 D  562  TYR SER LYS                                                  
SEQRES   1 E  461  GLN GLY VAL ASN ASP ASN GLU GLU GLY PHE PHE SER ALA          
SEQRES   2 E  461  ARG GLY HIS ARG PRO LEU ASP LYS LYS ARG GLU GLU ALA          
SEQRES   3 E  461  PRO SER LEU ARG PRO ALA PRO PRO PRO ILE SER GLY GLY          
SEQRES   4 E  461  GLY TYR ARG ALA ARG PRO ALA LYS ALA ALA ALA THR GLN          
SEQRES   5 E  461  LYS LYS VAL GLU ARG LYS ALA PRO ASP ALA GLY GLY CYS          
SEQRES   6 E  461  LEU HIS ALA ASP PRO ASP LEU GLY VAL LEU CYS PRO THR          
SEQRES   7 E  461  GLY CYS GLN LEU GLN GLU ALA LEU LEU GLN GLN GLU ARG          
SEQRES   8 E  461  PRO ILE ARG ASN SER VAL ASP GLU LEU ASN ASN ASN VAL          
SEQRES   9 E  461  GLU ALA VAL SER GLN THR SER SER SER SER PHE GLN TYR          
SEQRES  10 E  461  MET TYR LEU LEU LYS ASP LEU TRP GLN LYS ARG GLN LYS          
SEQRES  11 E  461  GLN VAL LYS ASP ASN GLU ASN VAL VAL ASN GLU TYR SER          
SEQRES  12 E  461  SER GLU LEU GLU LYS HIS GLN LEU TYR ILE ASP GLU THR          
SEQRES  13 E  461  VAL ASN SER ASN ILE PRO THR ASN LEU ARG VAL LEU ARG          
SEQRES  14 E  461  SER ILE LEU GLU ASN LEU ARG SER LYS ILE GLN LYS LEU          
SEQRES  15 E  461  GLU SER ASP VAL SER ALA GLN MET GLU TYR CYS ARG THR          
SEQRES  16 E  461  PRO CYS THR VAL SER CYS ASN ILE PRO VAL VAL SER GLY          
SEQRES  17 E  461  LYS GLU CYS GLU GLU ILE ILE ARG LYS GLY GLY GLU THR          
SEQRES  18 E  461  SER GLU MET TYR LEU ILE GLN PRO ASP SER SER VAL LYS          
SEQRES  19 E  461  PRO TYR ARG VAL TYR CYS ASP MET ASN THR GLU ASN GLY          
SEQRES  20 E  461  GLY TRP THR VAL ILE GLN ASN ARG GLN ASP GLY SER VAL          
SEQRES  21 E  461  ASP PHE GLY ARG LYS TRP ASP PRO TYR LYS GLN GLY PHE          
SEQRES  22 E  461  GLY ASN VAL ALA THR ASN THR ASP GLY LYS ASN TYR CYS          
SEQRES  23 E  461  GLY LEU PRO GLY GLU TYR TRP LEU GLY ASN ASP LYS ILE          
SEQRES  24 E  461  SER GLN LEU THR ARG MET GLY PRO THR GLU LEU LEU ILE          
SEQRES  25 E  461  GLU MET GLU ASP TRP LYS GLY ASP LYS VAL LYS ALA HIS          
SEQRES  26 E  461  TYR GLY GLY PHE THR VAL GLN ASN GLU ALA ASN LYS TYR          
SEQRES  27 E  461  GLN ILE SER VAL ASN LYS TYR ARG GLY THR ALA GLY ASN          
SEQRES  28 E  461  ALA LEU MET ASP GLY ALA SER GLN LEU MET GLY GLU ASN          
SEQRES  29 E  461  ARG THR MET THR ILE HIS ASN GLY MET PHE PHE SER THR          
SEQRES  30 E  461  TYR ASP ARG ASP ASN ASP GLY TRP LEU THR SER ASP PRO          
SEQRES  31 E  461  ARG LYS GLN CYS SER LYS GLU ASP GLY GLY GLY TRP TRP          
SEQRES  32 E  461  TYR ASN ARG CYS HIS ALA ALA ASN PRO ASN GLY ARG TYR          
SEQRES  33 E  461  TYR TRP GLY GLY GLN TYR THR TRP ASP MET ALA LYS HIS          
SEQRES  34 E  461  GLY THR ASP ASP GLY VAL VAL TRP MET ASN TRP LYS GLY          
SEQRES  35 E  461  SER TRP TYR SER MET ARG LYS MET SER MET LYS ILE ARG          
SEQRES  36 E  461  PRO PHE PHE PRO GLN GLN                                      
SEQRES   1 F  411  TYR VAL ALA THR ARG ASP ASN CYS CYS ILE LEU ASP GLU          
SEQRES   2 F  411  ARG PHE GLY SER TYR CYS PRO THR THR CYS GLY ILE ALA          
SEQRES   3 F  411  ASP PHE LEU SER THR TYR GLN THR LYS VAL ASP LYS ASP          
SEQRES   4 F  411  LEU GLN SER LEU GLU ASP ILE LEU HIS GLN VAL GLU ASN          
SEQRES   5 F  411  LYS THR SER GLU VAL LYS GLN LEU ILE LYS ALA ILE GLN          
SEQRES   6 F  411  LEU THR TYR ASN PRO ASP GLU SER SER LYS PRO ASN MET          
SEQRES   7 F  411  ILE ASP ALA ALA THR LEU LYS SER ARG LYS MET LEU GLU          
SEQRES   8 F  411  GLU ILE MET LYS TYR GLU ALA SER ILE LEU THR HIS ASP          
SEQRES   9 F  411  SER SER ILE ARG TYR LEU GLN GLU ILE TYR ASN SER ASN          
SEQRES  10 F  411  ASN GLN LYS ILE VAL ASN LEU LYS GLU LYS VAL ALA GLN          
SEQRES  11 F  411  LEU GLU ALA GLN CYS GLN GLU PRO CYS LYS ASP THR VAL          
SEQRES  12 F  411  GLN ILE HIS ASP ILE THR GLY LYS ASP CYS GLN ASP ILE          
SEQRES  13 F  411  ALA ASN LYS GLY ALA LYS GLN SER GLY LEU TYR PHE ILE          
SEQRES  14 F  411  LYS PRO LEU LYS ALA ASN GLN GLN PHE LEU VAL TYR CYS          
SEQRES  15 F  411  GLU ILE ASP GLY SER GLY ASN GLY TRP THR VAL PHE GLN          
SEQRES  16 F  411  LYS ARG LEU ASP GLY SER VAL ASP PHE LYS LYS ASN TRP          
SEQRES  17 F  411  ILE GLN TYR LYS GLU GLY PHE GLY HIS LEU SER PRO THR          
SEQRES  18 F  411  GLY THR THR GLU PHE TRP LEU GLY ASN GLU LYS ILE HIS          
SEQRES  19 F  411  LEU ILE SER THR GLN SER ALA ILE PRO TYR ALA LEU ARG          
SEQRES  20 F  411  VAL GLU LEU GLU ASP TRP ASN GLY ARG THR SER THR ALA          
SEQRES  21 F  411  ASP TYR ALA MET PHE LYS VAL GLY PRO GLU ALA ASP LYS          
SEQRES  22 F  411  TYR ARG LEU THR TYR ALA TYR PHE ALA GLY GLY ASP ALA          
SEQRES  23 F  411  GLY ASP ALA PHE ASP GLY PHE ASP PHE GLY ASP ASP PRO          
SEQRES  24 F  411  SER ASP LYS PHE PHE THR SER HIS ASN GLY MET GLN PHE          
SEQRES  25 F  411  SER THR TRP ASP ASN ASP ASN ASP LYS PHE GLU GLY ASN          
SEQRES  26 F  411  CYS ALA GLU GLN ASP GLY SER GLY TRP TRP MET ASN LYS          
SEQRES  27 F  411  CYS HIS ALA GLY HIS LEU ASN GLY VAL TYR TYR GLN GLY          
SEQRES  28 F  411  GLY THR TYR SER LYS ALA SER THR PRO ASN GLY TYR ASP          
SEQRES  29 F  411  ASN GLY ILE ILE TRP ALA THR TRP LYS THR ARG TRP TYR          
SEQRES  30 F  411  SER MET LYS LYS THR THR MET LYS ILE ILE PRO PHE ASN          
SEQRES  31 F  411  ARG LEU THR ILE GLY GLU GLY GLN GLN HIS HIS LEU GLY          
SEQRES  32 F  411  GLY ALA LYS GLN ALA GLY ASP VAL                              
SEQRES   1 G  562  ALA ASP SER GLY GLU GLY ASP PHE LEU ALA GLU GLY GLY          
SEQRES   2 G  562  GLY VAL ARG GLY PRO ARG VAL VAL GLU ARG HIS GLN SER          
SEQRES   3 G  562  ALA CYS LYS ASP SER ASP TRP PRO PHE CYS SER ASP GLU          
SEQRES   4 G  562  ASP TRP ASN TYR LYS CYS PRO SER GLY CYS ARG MET LYS          
SEQRES   5 G  562  GLY LEU ILE ASP GLU VAL ASN GLN ASP PHE THR ASN ARG          
SEQRES   6 G  562  ILE ASN LYS LEU LYS ASN SER LEU PHE GLU TYR GLN LYS          
SEQRES   7 G  562  ASN ASN LYS ASP SER HIS SER LEU THR THR ASN ILE MET          
SEQRES   8 G  562  GLU ILE LEU ARG GLY ASP PHE SER SER ALA ASN ASN ARG          
SEQRES   9 G  562  ASP ASN THR TYR ASN ARG VAL SER GLU ASP LEU ARG SER          
SEQRES  10 G  562  ARG ILE GLU VAL LEU LYS ARG LYS VAL ILE GLU LYS VAL          
SEQRES  11 G  562  GLN HIS ILE GLN LEU LEU GLN LYS ASN VAL ARG ALA GLN          
SEQRES  12 G  562  LEU VAL ASP MET LYS ARG LEU GLU VAL ASP ILE ASP ILE          
SEQRES  13 G  562  LYS ILE ARG SER CYS ARG GLY SER CYS SER ARG ALA LEU          
SEQRES  14 G  562  ALA ARG GLU VAL ASP LEU LYS ASP TYR GLU ASP GLN GLN          
SEQRES  15 G  562  LYS GLN LEU GLU GLN VAL ILE ALA LYS ASP LEU LEU PRO          
SEQRES  16 G  562  SER ARG ASP ARG GLN HIS LEU PRO LEU ILE LYS MET LYS          
SEQRES  17 G  562  PRO VAL PRO ASP LEU VAL PRO GLY ASN PHE LYS SER GLN          
SEQRES  18 G  562  LEU GLN LYS VAL PRO PRO GLU TRP LYS ALA LEU THR ASP          
SEQRES  19 G  562  MET PRO GLN MET ARG MET GLU LEU GLU ARG PRO GLY GLY          
SEQRES  20 G  562  ASN GLU ILE THR ARG GLY GLY SER THR SER TYR GLY THR          
SEQRES  21 G  562  GLY SER GLU THR GLU SER PRO ARG ASN PRO SER SER ALA          
SEQRES  22 G  562  GLY SER TRP ASN SER GLY SER SER GLY PRO GLY SER THR          
SEQRES  23 G  562  GLY ASN ARG ASN PRO GLY SER SER GLY THR GLY GLY THR          
SEQRES  24 G  562  ALA THR TRP LYS PRO GLY SER SER GLY PRO GLY SER THR          
SEQRES  25 G  562  GLY SER TRP ASN SER GLY SER SER GLY THR GLY SER THR          
SEQRES  26 G  562  GLY ASN GLN ASN PRO GLY SER PRO ARG PRO GLY SER THR          
SEQRES  27 G  562  GLY THR TRP ASN PRO GLY SER SER GLU ARG GLY SER ALA          
SEQRES  28 G  562  GLY HIS TRP THR SER GLU SER SER VAL SER GLY SER THR          
SEQRES  29 G  562  GLY GLN TRP HIS SER GLU SER GLY SER PHE ARG PRO ASP          
SEQRES  30 G  562  SER PRO GLY SER GLY ASN ALA ARG PRO ASN ASN PRO ASP          
SEQRES  31 G  562  TRP GLY THR PHE GLU GLU VAL SER GLY ASN VAL SER PRO          
SEQRES  32 G  562  GLY THR ARG ARG GLU TYR HIS THR GLU LYS LEU VAL THR          
SEQRES  33 G  562  SER LYS GLY ASP LYS GLU LEU ARG THR GLY LYS GLU LYS          
SEQRES  34 G  562  VAL THR SER GLY SER THR THR THR THR ARG ARG SER CYS          
SEQRES  35 G  562  SER LYS THR VAL THR LYS THR VAL ILE GLY PRO ASP GLY          
SEQRES  36 G  562  HIS LYS GLU VAL THR LYS GLU VAL VAL THR SER GLU ASP          
SEQRES  37 G  562  GLY SER ASP CYS PRO GLU ALA MET ASP LEU GLY THR LEU          
SEQRES  38 G  562  SER GLY ILE GLY THR LEU ASP GLY PHE ARG HIS ARG HIS          
SEQRES  39 G  562  PRO ASP GLU ALA ALA PHE PHE ASP THR ALA SER THR GLY          
SEQRES  40 G  562  LYS THR PHE PRO GLY PHE PHE SER PRO MET LEU GLY GLU          
SEQRES  41 G  562  PHE VAL SER GLU THR GLU SER ARG GLY SER GLU SER GLY          
SEQRES  42 G  562  ILE PHE THR ASN THR LYS GLU SER SER SER HIS HIS PRO          
SEQRES  43 G  562  GLY ILE ALA GLU PHE PRO SER ARG GLY LYS SER SER SER          
SEQRES  44 G  562  TYR SER LYS                                                  
SEQRES   1 H  461  GLN GLY VAL ASN ASP ASN GLU GLU GLY PHE PHE SER ALA          
SEQRES   2 H  461  ARG GLY HIS ARG PRO LEU ASP LYS LYS ARG GLU GLU ALA          
SEQRES   3 H  461  PRO SER LEU ARG PRO ALA PRO PRO PRO ILE SER GLY GLY          
SEQRES   4 H  461  GLY TYR ARG ALA ARG PRO ALA LYS ALA ALA ALA THR GLN          
SEQRES   5 H  461  LYS LYS VAL GLU ARG LYS ALA PRO ASP ALA GLY GLY CYS          
SEQRES   6 H  461  LEU HIS ALA ASP PRO ASP LEU GLY VAL LEU CYS PRO THR          
SEQRES   7 H  461  GLY CYS GLN LEU GLN GLU ALA LEU LEU GLN GLN GLU ARG          
SEQRES   8 H  461  PRO ILE ARG ASN SER VAL ASP GLU LEU ASN ASN ASN VAL          
SEQRES   9 H  461  GLU ALA VAL SER GLN THR SER SER SER SER PHE GLN TYR          
SEQRES  10 H  461  MET TYR LEU LEU LYS ASP LEU TRP GLN LYS ARG GLN LYS          
SEQRES  11 H  461  GLN VAL LYS ASP ASN GLU ASN VAL VAL ASN GLU TYR SER          
SEQRES  12 H  461  SER GLU LEU GLU LYS HIS GLN LEU TYR ILE ASP GLU THR          
SEQRES  13 H  461  VAL ASN SER ASN ILE PRO THR ASN LEU ARG VAL LEU ARG          
SEQRES  14 H  461  SER ILE LEU GLU ASN LEU ARG SER LYS ILE GLN LYS LEU          
SEQRES  15 H  461  GLU SER ASP VAL SER ALA GLN MET GLU TYR CYS ARG THR          
SEQRES  16 H  461  PRO CYS THR VAL SER CYS ASN ILE PRO VAL VAL SER GLY          
SEQRES  17 H  461  LYS GLU CYS GLU GLU ILE ILE ARG LYS GLY GLY GLU THR          
SEQRES  18 H  461  SER GLU MET TYR LEU ILE GLN PRO ASP SER SER VAL LYS          
SEQRES  19 H  461  PRO TYR ARG VAL TYR CYS ASP MET ASN THR GLU ASN GLY          
SEQRES  20 H  461  GLY TRP THR VAL ILE GLN ASN ARG GLN ASP GLY SER VAL          
SEQRES  21 H  461  ASP PHE GLY ARG LYS TRP ASP PRO TYR LYS GLN GLY PHE          
SEQRES  22 H  461  GLY ASN VAL ALA THR ASN THR ASP GLY LYS ASN TYR CYS          
SEQRES  23 H  461  GLY LEU PRO GLY GLU TYR TRP LEU GLY ASN ASP LYS ILE          
SEQRES  24 H  461  SER GLN LEU THR ARG MET GLY PRO THR GLU LEU LEU ILE          
SEQRES  25 H  461  GLU MET GLU ASP TRP LYS GLY ASP LYS VAL LYS ALA HIS          
SEQRES  26 H  461  TYR GLY GLY PHE THR VAL GLN ASN GLU ALA ASN LYS TYR          
SEQRES  27 H  461  GLN ILE SER VAL ASN LYS TYR ARG GLY THR ALA GLY ASN          
SEQRES  28 H  461  ALA LEU MET ASP GLY ALA SER GLN LEU MET GLY GLU ASN          
SEQRES  29 H  461  ARG THR MET THR ILE HIS ASN GLY MET PHE PHE SER THR          
SEQRES  30 H  461  TYR ASP ARG ASP ASN ASP GLY TRP LEU THR SER ASP PRO          
SEQRES  31 H  461  ARG LYS GLN CYS SER LYS GLU ASP GLY GLY GLY TRP TRP          
SEQRES  32 H  461  TYR ASN ARG CYS HIS ALA ALA ASN PRO ASN GLY ARG TYR          
SEQRES  33 H  461  TYR TRP GLY GLY GLN TYR THR TRP ASP MET ALA LYS HIS          
SEQRES  34 H  461  GLY THR ASP ASP GLY VAL VAL TRP MET ASN TRP LYS GLY          
SEQRES  35 H  461  SER TRP TYR SER MET ARG LYS MET SER MET LYS ILE ARG          
SEQRES  36 H  461  PRO PHE PHE PRO GLN GLN                                      
SEQRES   1 I  411  TYR VAL ALA THR ARG ASP ASN CYS CYS ILE LEU ASP GLU          
SEQRES   2 I  411  ARG PHE GLY SER TYR CYS PRO THR THR CYS GLY ILE ALA          
SEQRES   3 I  411  ASP PHE LEU SER THR TYR GLN THR LYS VAL ASP LYS ASP          
SEQRES   4 I  411  LEU GLN SER LEU GLU ASP ILE LEU HIS GLN VAL GLU ASN          
SEQRES   5 I  411  LYS THR SER GLU VAL LYS GLN LEU ILE LYS ALA ILE GLN          
SEQRES   6 I  411  LEU THR TYR ASN PRO ASP GLU SER SER LYS PRO ASN MET          
SEQRES   7 I  411  ILE ASP ALA ALA THR LEU LYS SER ARG LYS MET LEU GLU          
SEQRES   8 I  411  GLU ILE MET LYS TYR GLU ALA SER ILE LEU THR HIS ASP          
SEQRES   9 I  411  SER SER ILE ARG TYR LEU GLN GLU ILE TYR ASN SER ASN          
SEQRES  10 I  411  ASN GLN LYS ILE VAL ASN LEU LYS GLU LYS VAL ALA GLN          
SEQRES  11 I  411  LEU GLU ALA GLN CYS GLN GLU PRO CYS LYS ASP THR VAL          
SEQRES  12 I  411  GLN ILE HIS ASP ILE THR GLY LYS ASP CYS GLN ASP ILE          
SEQRES  13 I  411  ALA ASN LYS GLY ALA LYS GLN SER GLY LEU TYR PHE ILE          
SEQRES  14 I  411  LYS PRO LEU LYS ALA ASN GLN GLN PHE LEU VAL TYR CYS          
SEQRES  15 I  411  GLU ILE ASP GLY SER GLY ASN GLY TRP THR VAL PHE GLN          
SEQRES  16 I  411  LYS ARG LEU ASP GLY SER VAL ASP PHE LYS LYS ASN TRP          
SEQRES  17 I  411  ILE GLN TYR LYS GLU GLY PHE GLY HIS LEU SER PRO THR          
SEQRES  18 I  411  GLY THR THR GLU PHE TRP LEU GLY ASN GLU LYS ILE HIS          
SEQRES  19 I  411  LEU ILE SER THR GLN SER ALA ILE PRO TYR ALA LEU ARG          
SEQRES  20 I  411  VAL GLU LEU GLU ASP TRP ASN GLY ARG THR SER THR ALA          
SEQRES  21 I  411  ASP TYR ALA MET PHE LYS VAL GLY PRO GLU ALA ASP LYS          
SEQRES  22 I  411  TYR ARG LEU THR TYR ALA TYR PHE ALA GLY GLY ASP ALA          
SEQRES  23 I  411  GLY ASP ALA PHE ASP GLY PHE ASP PHE GLY ASP ASP PRO          
SEQRES  24 I  411  SER ASP LYS PHE PHE THR SER HIS ASN GLY MET GLN PHE          
SEQRES  25 I  411  SER THR TRP ASP ASN ASP ASN ASP LYS PHE GLU GLY ASN          
SEQRES  26 I  411  CYS ALA GLU GLN ASP GLY SER GLY TRP TRP MET ASN LYS          
SEQRES  27 I  411  CYS HIS ALA GLY HIS LEU ASN GLY VAL TYR TYR GLN GLY          
SEQRES  28 I  411  GLY THR TYR SER LYS ALA SER THR PRO ASN GLY TYR ASP          
SEQRES  29 I  411  ASN GLY ILE ILE TRP ALA THR TRP LYS THR ARG TRP TYR          
SEQRES  30 I  411  SER MET LYS LYS THR THR MET LYS ILE ILE PRO PHE ASN          
SEQRES  31 I  411  ARG LEU THR ILE GLY GLU GLY GLN GLN HIS HIS LEU GLY          
SEQRES  32 I  411  GLY ALA LYS GLN ALA GLY ASP VAL                              
SEQRES   1 J  562  ALA ASP SER GLY GLU GLY ASP PHE LEU ALA GLU GLY GLY          
SEQRES   2 J  562  GLY VAL ARG GLY PRO ARG VAL VAL GLU ARG HIS GLN SER          
SEQRES   3 J  562  ALA CYS LYS ASP SER ASP TRP PRO PHE CYS SER ASP GLU          
SEQRES   4 J  562  ASP TRP ASN TYR LYS CYS PRO SER GLY CYS ARG MET LYS          
SEQRES   5 J  562  GLY LEU ILE ASP GLU VAL ASN GLN ASP PHE THR ASN ARG          
SEQRES   6 J  562  ILE ASN LYS LEU LYS ASN SER LEU PHE GLU TYR GLN LYS          
SEQRES   7 J  562  ASN ASN LYS ASP SER HIS SER LEU THR THR ASN ILE MET          
SEQRES   8 J  562  GLU ILE LEU ARG GLY ASP PHE SER SER ALA ASN ASN ARG          
SEQRES   9 J  562  ASP ASN THR TYR ASN ARG VAL SER GLU ASP LEU ARG SER          
SEQRES  10 J  562  ARG ILE GLU VAL LEU LYS ARG LYS VAL ILE GLU LYS VAL          
SEQRES  11 J  562  GLN HIS ILE GLN LEU LEU GLN LYS ASN VAL ARG ALA GLN          
SEQRES  12 J  562  LEU VAL ASP MET LYS ARG LEU GLU VAL ASP ILE ASP ILE          
SEQRES  13 J  562  LYS ILE ARG SER CYS ARG GLY SER CYS SER ARG ALA LEU          
SEQRES  14 J  562  ALA ARG GLU VAL ASP LEU LYS ASP TYR GLU ASP GLN GLN          
SEQRES  15 J  562  LYS GLN LEU GLU GLN VAL ILE ALA LYS ASP LEU LEU PRO          
SEQRES  16 J  562  SER ARG ASP ARG GLN HIS LEU PRO LEU ILE LYS MET LYS          
SEQRES  17 J  562  PRO VAL PRO ASP LEU VAL PRO GLY ASN PHE LYS SER GLN          
SEQRES  18 J  562  LEU GLN LYS VAL PRO PRO GLU TRP LYS ALA LEU THR ASP          
SEQRES  19 J  562  MET PRO GLN MET ARG MET GLU LEU GLU ARG PRO GLY GLY          
SEQRES  20 J  562  ASN GLU ILE THR ARG GLY GLY SER THR SER TYR GLY THR          
SEQRES  21 J  562  GLY SER GLU THR GLU SER PRO ARG ASN PRO SER SER ALA          
SEQRES  22 J  562  GLY SER TRP ASN SER GLY SER SER GLY PRO GLY SER THR          
SEQRES  23 J  562  GLY ASN ARG ASN PRO GLY SER SER GLY THR GLY GLY THR          
SEQRES  24 J  562  ALA THR TRP LYS PRO GLY SER SER GLY PRO GLY SER THR          
SEQRES  25 J  562  GLY SER TRP ASN SER GLY SER SER GLY THR GLY SER THR          
SEQRES  26 J  562  GLY ASN GLN ASN PRO GLY SER PRO ARG PRO GLY SER THR          
SEQRES  27 J  562  GLY THR TRP ASN PRO GLY SER SER GLU ARG GLY SER ALA          
SEQRES  28 J  562  GLY HIS TRP THR SER GLU SER SER VAL SER GLY SER THR          
SEQRES  29 J  562  GLY GLN TRP HIS SER GLU SER GLY SER PHE ARG PRO ASP          
SEQRES  30 J  562  SER PRO GLY SER GLY ASN ALA ARG PRO ASN ASN PRO ASP          
SEQRES  31 J  562  TRP GLY THR PHE GLU GLU VAL SER GLY ASN VAL SER PRO          
SEQRES  32 J  562  GLY THR ARG ARG GLU TYR HIS THR GLU LYS LEU VAL THR          
SEQRES  33 J  562  SER LYS GLY ASP LYS GLU LEU ARG THR GLY LYS GLU LYS          
SEQRES  34 J  562  VAL THR SER GLY SER THR THR THR THR ARG ARG SER CYS          
SEQRES  35 J  562  SER LYS THR VAL THR LYS THR VAL ILE GLY PRO ASP GLY          
SEQRES  36 J  562  HIS LYS GLU VAL THR LYS GLU VAL VAL THR SER GLU ASP          
SEQRES  37 J  562  GLY SER ASP CYS PRO GLU ALA MET ASP LEU GLY THR LEU          
SEQRES  38 J  562  SER GLY ILE GLY THR LEU ASP GLY PHE ARG HIS ARG HIS          
SEQRES  39 J  562  PRO ASP GLU ALA ALA PHE PHE ASP THR ALA SER THR GLY          
SEQRES  40 J  562  LYS THR PHE PRO GLY PHE PHE SER PRO MET LEU GLY GLU          
SEQRES  41 J  562  PHE VAL SER GLU THR GLU SER ARG GLY SER GLU SER GLY          
SEQRES  42 J  562  ILE PHE THR ASN THR LYS GLU SER SER SER HIS HIS PRO          
SEQRES  43 J  562  GLY ILE ALA GLU PHE PRO SER ARG GLY LYS SER SER SER          
SEQRES  44 J  562  TYR SER LYS                                                  
SEQRES   1 K  461  GLN GLY VAL ASN ASP ASN GLU GLU GLY PHE PHE SER ALA          
SEQRES   2 K  461  ARG GLY HIS ARG PRO LEU ASP LYS LYS ARG GLU GLU ALA          
SEQRES   3 K  461  PRO SER LEU ARG PRO ALA PRO PRO PRO ILE SER GLY GLY          
SEQRES   4 K  461  GLY TYR ARG ALA ARG PRO ALA LYS ALA ALA ALA THR GLN          
SEQRES   5 K  461  LYS LYS VAL GLU ARG LYS ALA PRO ASP ALA GLY GLY CYS          
SEQRES   6 K  461  LEU HIS ALA ASP PRO ASP LEU GLY VAL LEU CYS PRO THR          
SEQRES   7 K  461  GLY CYS GLN LEU GLN GLU ALA LEU LEU GLN GLN GLU ARG          
SEQRES   8 K  461  PRO ILE ARG ASN SER VAL ASP GLU LEU ASN ASN ASN VAL          
SEQRES   9 K  461  GLU ALA VAL SER GLN THR SER SER SER SER PHE GLN TYR          
SEQRES  10 K  461  MET TYR LEU LEU LYS ASP LEU TRP GLN LYS ARG GLN LYS          
SEQRES  11 K  461  GLN VAL LYS ASP ASN GLU ASN VAL VAL ASN GLU TYR SER          
SEQRES  12 K  461  SER GLU LEU GLU LYS HIS GLN LEU TYR ILE ASP GLU THR          
SEQRES  13 K  461  VAL ASN SER ASN ILE PRO THR ASN LEU ARG VAL LEU ARG          
SEQRES  14 K  461  SER ILE LEU GLU ASN LEU ARG SER LYS ILE GLN LYS LEU          
SEQRES  15 K  461  GLU SER ASP VAL SER ALA GLN MET GLU TYR CYS ARG THR          
SEQRES  16 K  461  PRO CYS THR VAL SER CYS ASN ILE PRO VAL VAL SER GLY          
SEQRES  17 K  461  LYS GLU CYS GLU GLU ILE ILE ARG LYS GLY GLY GLU THR          
SEQRES  18 K  461  SER GLU MET TYR LEU ILE GLN PRO ASP SER SER VAL LYS          
SEQRES  19 K  461  PRO TYR ARG VAL TYR CYS ASP MET ASN THR GLU ASN GLY          
SEQRES  20 K  461  GLY TRP THR VAL ILE GLN ASN ARG GLN ASP GLY SER VAL          
SEQRES  21 K  461  ASP PHE GLY ARG LYS TRP ASP PRO TYR LYS GLN GLY PHE          
SEQRES  22 K  461  GLY ASN VAL ALA THR ASN THR ASP GLY LYS ASN TYR CYS          
SEQRES  23 K  461  GLY LEU PRO GLY GLU TYR TRP LEU GLY ASN ASP LYS ILE          
SEQRES  24 K  461  SER GLN LEU THR ARG MET GLY PRO THR GLU LEU LEU ILE          
SEQRES  25 K  461  GLU MET GLU ASP TRP LYS GLY ASP LYS VAL LYS ALA HIS          
SEQRES  26 K  461  TYR GLY GLY PHE THR VAL GLN ASN GLU ALA ASN LYS TYR          
SEQRES  27 K  461  GLN ILE SER VAL ASN LYS TYR ARG GLY THR ALA GLY ASN          
SEQRES  28 K  461  ALA LEU MET ASP GLY ALA SER GLN LEU MET GLY GLU ASN          
SEQRES  29 K  461  ARG THR MET THR ILE HIS ASN GLY MET PHE PHE SER THR          
SEQRES  30 K  461  TYR ASP ARG ASP ASN ASP GLY TRP LEU THR SER ASP PRO          
SEQRES  31 K  461  ARG LYS GLN CYS SER LYS GLU ASP GLY GLY GLY TRP TRP          
SEQRES  32 K  461  TYR ASN ARG CYS HIS ALA ALA ASN PRO ASN GLY ARG TYR          
SEQRES  33 K  461  TYR TRP GLY GLY GLN TYR THR TRP ASP MET ALA LYS HIS          
SEQRES  34 K  461  GLY THR ASP ASP GLY VAL VAL TRP MET ASN TRP LYS GLY          
SEQRES  35 K  461  SER TRP TYR SER MET ARG LYS MET SER MET LYS ILE ARG          
SEQRES  36 K  461  PRO PHE PHE PRO GLN GLN                                      
SEQRES   1 L  411  TYR VAL ALA THR ARG ASP ASN CYS CYS ILE LEU ASP GLU          
SEQRES   2 L  411  ARG PHE GLY SER TYR CYS PRO THR THR CYS GLY ILE ALA          
SEQRES   3 L  411  ASP PHE LEU SER THR TYR GLN THR LYS VAL ASP LYS ASP          
SEQRES   4 L  411  LEU GLN SER LEU GLU ASP ILE LEU HIS GLN VAL GLU ASN          
SEQRES   5 L  411  LYS THR SER GLU VAL LYS GLN LEU ILE LYS ALA ILE GLN          
SEQRES   6 L  411  LEU THR TYR ASN PRO ASP GLU SER SER LYS PRO ASN MET          
SEQRES   7 L  411  ILE ASP ALA ALA THR LEU LYS SER ARG LYS MET LEU GLU          
SEQRES   8 L  411  GLU ILE MET LYS TYR GLU ALA SER ILE LEU THR HIS ASP          
SEQRES   9 L  411  SER SER ILE ARG TYR LEU GLN GLU ILE TYR ASN SER ASN          
SEQRES  10 L  411  ASN GLN LYS ILE VAL ASN LEU LYS GLU LYS VAL ALA GLN          
SEQRES  11 L  411  LEU GLU ALA GLN CYS GLN GLU PRO CYS LYS ASP THR VAL          
SEQRES  12 L  411  GLN ILE HIS ASP ILE THR GLY LYS ASP CYS GLN ASP ILE          
SEQRES  13 L  411  ALA ASN LYS GLY ALA LYS GLN SER GLY LEU TYR PHE ILE          
SEQRES  14 L  411  LYS PRO LEU LYS ALA ASN GLN GLN PHE LEU VAL TYR CYS          
SEQRES  15 L  411  GLU ILE ASP GLY SER GLY ASN GLY TRP THR VAL PHE GLN          
SEQRES  16 L  411  LYS ARG LEU ASP GLY SER VAL ASP PHE LYS LYS ASN TRP          
SEQRES  17 L  411  ILE GLN TYR LYS GLU GLY PHE GLY HIS LEU SER PRO THR          
SEQRES  18 L  411  GLY THR THR GLU PHE TRP LEU GLY ASN GLU LYS ILE HIS          
SEQRES  19 L  411  LEU ILE SER THR GLN SER ALA ILE PRO TYR ALA LEU ARG          
SEQRES  20 L  411  VAL GLU LEU GLU ASP TRP ASN GLY ARG THR SER THR ALA          
SEQRES  21 L  411  ASP TYR ALA MET PHE LYS VAL GLY PRO GLU ALA ASP LYS          
SEQRES  22 L  411  TYR ARG LEU THR TYR ALA TYR PHE ALA GLY GLY ASP ALA          
SEQRES  23 L  411  GLY ASP ALA PHE ASP GLY PHE ASP PHE GLY ASP ASP PRO          
SEQRES  24 L  411  SER ASP LYS PHE PHE THR SER HIS ASN GLY MET GLN PHE          
SEQRES  25 L  411  SER THR TRP ASP ASN ASP ASN ASP LYS PHE GLU GLY ASN          
SEQRES  26 L  411  CYS ALA GLU GLN ASP GLY SER GLY TRP TRP MET ASN LYS          
SEQRES  27 L  411  CYS HIS ALA GLY HIS LEU ASN GLY VAL TYR TYR GLN GLY          
SEQRES  28 L  411  GLY THR TYR SER LYS ALA SER THR PRO ASN GLY TYR ASP          
SEQRES  29 L  411  ASN GLY ILE ILE TRP ALA THR TRP LYS THR ARG TRP TYR          
SEQRES  30 L  411  SER MET LYS LYS THR THR MET LYS ILE ILE PRO PHE ASN          
SEQRES  31 L  411  ARG LEU THR ILE GLY GLU GLY GLN GLN HIS HIS LEU GLY          
SEQRES  32 L  411  GLY ALA LYS GLN ALA GLY ASP VAL                              
SEQRES   1 M    4  GLY PRO ARG PRO                                              
SEQRES   1 N    4  GLY PRO ARG PRO                                              
SEQRES   1 O    4  GLY HIS ARG PRO                                              
SEQRES   1 P    4  GLY HIS ARG PRO                                              
SEQRES   1 Q    4  GLY PRO ARG PRO                                              
SEQRES   1 R    4  GLY PRO ARG PRO                                              
SEQRES   1 S    4  GLY HIS ARG PRO                                              
SEQRES   1 T    4  GLY HIS ARG PRO                                              
MODRES 3GHG ASN E  364  ASN  GLYCOSYLATION SITE                                 
MODRES 3GHG ASN H  364  ASN  GLYCOSYLATION SITE                                 
HET    NAG  B 470      14                                                       
HET    NDG  B 471      14                                                       
HET    BMA  B 472      11                                                       
HET    MAN  B 473      11                                                       
HET    NDG  B 475      14                                                       
HET    MAN  B 474      11                                                       
HET    NDG  B 477      14                                                       
HET    GAL  B 476      11                                                       
HET    SIA  B 479      20                                                       
HET    GAL  B 478      11                                                       
HET    SIA  B 480      20                                                       
HET    NAG  E 470      14                                                       
HET    NDG  E 471      14                                                       
HET    BMA  E 472      11                                                       
HET    MAN  E 473      11                                                       
HET    NDG  E 475      14                                                       
HET    MAN  E 474      11                                                       
HET    NDG  E 477      14                                                       
HET    GAL  E 476      11                                                       
HET    SIA  E 479      20                                                       
HET    GAL  E 478      11                                                       
HET    SIA  E 480      20                                                       
HET    NAG  H 470      14                                                       
HET    NDG  H 471      14                                                       
HET    BMA  H 472      11                                                       
HET    MAN  H 473      11                                                       
HET    MAN  H 474      11                                                       
HET    NAG  K 470      14                                                       
HET    NDG  K 471      14                                                       
HET    BMA  K 472      11                                                       
HET    MAN  K 473      11                                                       
HET    NDG  K 475      14                                                       
HET    MAN  K 474      11                                                       
HET    NDG  K 477      14                                                       
HET    GAL  K 476      11                                                       
HET    SIA  K 479      20                                                       
HET    GAL  K 478      11                                                       
HET    SIA  K 480      20                                                       
HET    NAG  L 570      14                                                       
HET    NAG  L 571      14                                                       
HET     CA  B 501       1                                                       
HET     CA  F 601       1                                                       
HET     CA  C 601       1                                                       
HET     CA  E 501       1                                                       
HET     CA  H 501       1                                                       
HET     CA  I 601       1                                                       
HET     CA  K 501       1                                                       
HET     CA  L 601       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     GAL BETA-D-GALACTOSE                                                 
HETNAM     SIA O-SIALIC ACID                                                    
HETNAM      CA CALCIUM ION                                                      
FORMUL  21  NAG    6(C8 H15 N O6)                                               
FORMUL  21  NDG    10(C8 H15 N O6)                                              
FORMUL  21  BMA    4(C6 H12 O6)                                                 
FORMUL  21  MAN    8(C6 H12 O6)                                                 
FORMUL  21  GAL    6(C6 H12 O6)                                                 
FORMUL  21  SIA    6(C11 H19 N O9)                                              
FORMUL  26   CA    8(CA 2+)                                                     
HELIX    1   1 SER A   47  PHE A   74  1                                  28    
HELIX    2   2 PHE A   74  ILE A   93  1                                  20    
HELIX    3   3 GLY A   96  VAL A  111  1                                  16    
HELIX    4   4 SER A  112  CYS A  161  1                                  50    
HELIX    5   5 ARG A  162  SER A  164  5                                   3    
HELIX    6   6 ASP A  174  ALA A  190  1                                  17    
HELIX    7   7 THR B   78  GLN B  116  1                                  39    
HELIX    8   8 GLN B  116  VAL B  138  1                                  23    
HELIX    9   9 GLU B  141  LEU B  151  1                                  11    
HELIX   10  10 LEU B  151  SER B  159  1                                   9    
HELIX   11  11 SER B  159  CYS B  193  1                                  35    
HELIX   12  12 GLU B  210  LYS B  217  1                                   8    
HELIX   13  13 LYS B  265  GLN B  271  1                                   7    
HELIX   14  14 GLY B  295  MET B  305  1                                  11    
HELIX   15  15 ASN B  333  LYS B  337  5                                   5    
HELIX   16  16 MET B  361  THR B  366  1                                   6    
HELIX   17  17 GLN B  393  ASP B  398  1                                   6    
HELIX   18  18 THR B  423  ALA B  427  5                                   5    
HELIX   19  19 TRP B  437  GLY B  442  1                                   6    
HELIX   20  20 THR C   22  ASN C   69  1                                  48    
HELIX   21  21 MET C   78  ALA C  133  1                                  56    
HELIX   22  22 ASP C  152  LYS C  159  1                                   8    
HELIX   23  23 ASN C  207  GLY C  214  1                                   8    
HELIX   24  24 GLY C  229  THR C  238  1                                  10    
HELIX   25  25 PRO C  269  LYS C  273  5                                   5    
HELIX   26  26 ASP C  288  GLY C  292  5                                   5    
HELIX   27  27 SER C  300  THR C  305  1                                   6    
HELIX   28  28 ASN C  325  GLY C  331  1                                   7    
HELIX   29  29 ASN C  390  LEU C  392  5                                   3    
HELIX   30  30 SER D   47  LYS D   78  1                                  32    
HELIX   31  31 ASN D   79  ILE D   93  1                                  15    
HELIX   32  32 PHE D   98  ARG D  104  1                                   7    
HELIX   33  33 ARG D  104  ARG D  110  1                                   7    
HELIX   34  34 ARG D  116  SER D  160  1                                  45    
HELIX   35  35 ASP D  174  ALA D  190  1                                  17    
HELIX   36  36 THR E   78  LEU E   87  1                                  10    
HELIX   37  37 GLN E   89  SER E   96  1                                   8    
HELIX   38  38 VAL E   97  ASN E  103  1                                   7    
HELIX   39  39 GLU E  105  PHE E  115  1                                  11    
HELIX   40  40 TYR E  117  VAL E  139  1                                  23    
HELIX   41  41 TYR E  142  SER E  187  1                                  46    
HELIX   42  42 SER E  187  TYR E  192  1                                   6    
HELIX   43  43 GLU E  210  LYS E  217  1                                   8    
HELIX   44  44 ASN E  243  GLY E  247  5                                   5    
HELIX   45  45 LYS E  265  GLN E  271  1                                   7    
HELIX   46  46 GLY E  295  ARG E  304  1                                  10    
HELIX   47  47 ASN E  333  LYS E  337  5                                   5    
HELIX   48  48 MET E  361  MET E  367  1                                   7    
HELIX   49  49 GLN E  393  GLY E  399  1                                   7    
HELIX   50  50 THR F   21  THR F   31  1                                  11    
HELIX   51  51 VAL F   36  THR F   67  1                                  32    
HELIX   52  52 LYS F   85  ALA F   98  1                                  14    
HELIX   53  53 SER F   99  ASP F  104  1                                   6    
HELIX   54  54 ASP F  104  GLN F  134  1                                  31    
HELIX   55  55 ASP F  152  GLY F  160  1                                   9    
HELIX   56  56 ASN F  207  GLY F  214  1                                   8    
HELIX   57  57 GLY F  229  THR F  238  1                                  10    
HELIX   58  58 PRO F  269  LYS F  273  5                                   5    
HELIX   59  59 SER F  300  THR F  305  1                                   6    
HELIX   60  60 ASN F  325  GLY F  331  1                                   7    
HELIX   61  61 PHE F  389  GLY F  395  1                                   7    
HELIX   62  62 SER G   47  SER G  160  1                                 114    
HELIX   63  63 ASP G  174  ILE G  189  1                                  16    
HELIX   64  64 THR H   78  GLN H   88  1                                  11    
HELIX   65  65 GLN H   89  ASN H  103  1                                  15    
HELIX   66  66 SER H  108  PHE H  115  1                                   8    
HELIX   67  67 TYR H  117  LYS H  122  1                                   6    
HELIX   68  68 ASP H  123  LEU H  151  1                                  29    
HELIX   69  69 ASP H  154  SER H  159  1                                   6    
HELIX   70  70 ASN H  160  TYR H  192  1                                  33    
HELIX   71  71 GLU H  210  GLY H  218  1                                   9    
HELIX   72  72 ASN H  243  GLY H  247  5                                   5    
HELIX   73  73 LYS H  265  GLY H  272  1                                   8    
HELIX   74  74 GLY H  295  GLY H  306  1                                  12    
HELIX   75  75 MET H  361  MET H  367  1                                   7    
HELIX   76  76 GLN H  393  ASP H  398  1                                   6    
HELIX   77  77 MET H  438  GLY H  442  1                                   5    
HELIX   78  78 THR I    4  CYS I    8  5                                   5    
HELIX   79  79 THR I   21  LYS I   38  1                                  18    
HELIX   80  80 ASP I   39  LEU I   66  1                                  28    
HELIX   81  81 ASN I   77  ILE I  121  1                                  45    
HELIX   82  82 VAL I  122  ALA I  133  1                                  12    
HELIX   83  83 ASP I  152  GLY I  160  1                                   9    
HELIX   84  84 ASN I  207  GLY I  214  1                                   8    
HELIX   85  85 GLY I  229  THR I  238  1                                  10    
HELIX   86  86 PRO I  269  LYS I  273  5                                   5    
HELIX   87  87 ASP I  288  GLY I  292  5                                   5    
HELIX   88  88 ASP I  298  THR I  305  5                                   8    
HELIX   89  89 ASN I  325  ASP I  330  1                                   6    
HELIX   90  90 PHE I  389  GLY I  395  1                                   7    
HELIX   91  91 SER J   47  SER J  160  1                                 114    
HELIX   92  92 ASP J  174  ALA J  190  1                                  17    
HELIX   93  93 THR K   78  GLN K   89  1                                  12    
HELIX   94  94 GLU K   90  ILE K   93  5                                   4    
HELIX   95  95 ARG K   94  GLU K  105  1                                  12    
HELIX   96  96 SER K  108  PHE K  115  1                                   8    
HELIX   97  97 GLN K  116  ASN K  160  1                                  45    
HELIX   98  98 ASN K  160  CYS K  193  1                                  34    
HELIX   99  99 GLU K  210  LYS K  217  1                                   8    
HELIX  100 100 ASN K  243  GLY K  247  5                                   5    
HELIX  101 101 LYS K  265  GLN K  271  1                                   7    
HELIX  102 102 ASN K  296  ARG K  304  1                                   9    
HELIX  103 103 ASN K  333  LYS K  337  5                                   5    
HELIX  104 104 MET K  361  THR K  366  1                                   6    
HELIX  105 105 GLN K  393  GLY K  399  1                                   7    
HELIX  106 106 TRP K  437  GLY K  442  1                                   6    
HELIX  107 107 THR L   21  ASN L   69  1                                  49    
HELIX  108 108 MET L   78  GLU L   91  1                                  14    
HELIX  109 109 ILE L   93  HIS L  103  1                                  11    
HELIX  110 110 SER L  106  CYS L  135  1                                  30    
HELIX  111 111 ASP L  152  GLY L  160  1                                   9    
HELIX  112 112 ASN L  207  GLY L  214  1                                   8    
HELIX  113 113 GLY L  229  GLN L  239  1                                  11    
HELIX  114 114 PRO L  269  LYS L  273  5                                   5    
HELIX  115 115 ASP L  288  GLY L  292  5                                   5    
HELIX  116 116 SER L  300  THR L  305  1                                   6    
HELIX  117 117 ASN L  325  GLY L  331  1                                   7    
HELIX  118 118 PHE L  389  GLY L  395  1                                   7    
SHEET    1   A 2 LYS A  44  PRO A  46  0                                        
SHEET    2   A 2 LEU E  75  PRO E  77 -1  O  CYS E  76   N  CYS A  45           
SHEET    1   B 2 CYS B  76  PRO B  77  0                                        
SHEET    2   B 2 LYS D  44  CYS D  45 -1  O  CYS D  45   N  CYS B  76           
SHEET    1   C 2 THR B 198  VAL B 199  0                                        
SHEET    2   C 2 LYS C 140  ASP C 141  1  O  LYS C 140   N  VAL B 199           
SHEET    1   D 8 ILE B 203  PRO B 204  0                                        
SHEET    2   D 8 PHE C 215  LEU C 218 -1  O  LEU C 218   N  ILE B 203           
SHEET    3   D 8 PHE C 226  TRP C 227 -1  O  TRP C 227   N  PHE C 215           
SHEET    4   D 8 GLY C 190  ARG C 197 -1  N  LYS C 196   O  PHE C 226           
SHEET    5   D 8 LYS C 381  PRO C 388 -1  O  ILE C 386   N  THR C 192           
SHEET    6   D 8 TYR C 244  GLU C 251 -1  N  ARG C 247   O  LYS C 385           
SHEET    7   D 8 THR C 259  VAL C 267 -1  O  TYR C 262   N  LEU C 246           
SHEET    8   D 8 LEU C 276  THR C 277 -1  O  THR C 277   N  LYS C 266           
SHEET    1   E 7 GLY C 165  ILE C 169  0                                        
SHEET    2   E 7 PHE C 178  ILE C 184 -1  O  CYS C 182   N  GLY C 165           
SHEET    3   E 7 GLY C 190  ARG C 197 -1  O  TRP C 191   N  GLU C 183           
SHEET    4   E 7 LYS C 381  PRO C 388 -1  O  ILE C 386   N  THR C 192           
SHEET    5   E 7 TYR C 244  GLU C 251 -1  N  ARG C 247   O  LYS C 385           
SHEET    6   E 7 THR C 259  VAL C 267 -1  O  TYR C 262   N  LEU C 246           
SHEET    7   E 7 TYR C 280  GLY C 283 -1  O  GLY C 283   N  ASP C 261           
SHEET    1   F 6 SER B 207  GLY B 208  0                                        
SHEET    2   F 6 MET B 224  ILE B 227  1  O  LEU B 226   N  GLY B 208           
SHEET    3   F 6 TYR B 236  ASP B 241 -1  O  TYR B 236   N  ILE B 227           
SHEET    4   F 6 TRP B 249  ARG B 255 -1  O  TRP B 249   N  ASP B 241           
SHEET    5   F 6 TYR B 292  LEU B 294 -1  O  TYR B 292   N  ASN B 254           
SHEET    6   F 6 GLY B 272  GLY B 274 -1  N  PHE B 273   O  TRP B 293           
SHEET    1   G 8 SER B 207  GLY B 208  0                                        
SHEET    2   G 8 MET B 224  ILE B 227  1  O  LEU B 226   N  GLY B 208           
SHEET    3   G 8 TYR B 236  ASP B 241 -1  O  TYR B 236   N  ILE B 227           
SHEET    4   G 8 TRP B 249  ARG B 255 -1  O  TRP B 249   N  ASP B 241           
SHEET    5   G 8 MET B 450  PRO B 456 -1  O  MET B 450   N  ARG B 255           
SHEET    6   G 8 THR B 308  MET B 314 -1  N  LEU B 311   O  LYS B 453           
SHEET    7   G 8 VAL B 322  VAL B 331 -1  O  ALA B 324   N  ILE B 312           
SHEET    8   G 8 ILE B 340  ARG B 346 -1  O  ARG B 346   N  HIS B 325           
SHEET    1   H 2 ALA B 277  THR B 278  0                                        
SHEET    2   H 2 LEU B 288  PRO B 289 -1  O  LEU B 288   N  THR B 278           
SHEET    1   I 2 TYR C  18  PRO C  20  0                                        
SHEET    2   I 2 TYR F  18  PRO F  20 -1  O  CYS F  19   N  CYS C  19           
SHEET    1   J 2 SER C 313  THR C 314  0                                        
SHEET    2   J 2 GLY C 333  TRP C 334 -1  O  TRP C 334   N  SER C 313           
SHEET    1   K 2 GLY C 342  HIS C 343  0                                        
SHEET    2   K 2 ILE C 368  TRP C 369 -1  O  ILE C 368   N  HIS C 343           
SHEET    1   L 2 THR E 198  VAL E 199  0                                        
SHEET    2   L 2 LYS F 140  ASP F 141  1  O  LYS F 140   N  VAL E 199           
SHEET    1   M 2 GLU E 223  ILE E 227  0                                        
SHEET    2   M 2 TYR E 236  CYS E 240 -1  O  TYR E 236   N  ILE E 227           
SHEET    1   N 7 GLY E 272  GLY E 274  0                                        
SHEET    2   N 7 TYR E 292  LEU E 294 -1  O  TRP E 293   N  PHE E 273           
SHEET    3   N 7 THR E 250  ARG E 255 -1  N  ILE E 252   O  LEU E 294           
SHEET    4   N 7 LYS E 449  PRO E 456 -1  O  MET E 450   N  ARG E 255           
SHEET    5   N 7 THR E 308  GLU E 315 -1  N  GLU E 309   O  ARG E 455           
SHEET    6   N 7 LYS E 321  VAL E 331 -1  O  ALA E 324   N  ILE E 312           
SHEET    7   N 7 ILE E 340  GLY E 347 -1  O  ASN E 343   N  GLY E 328           
SHEET    1   O 2 ALA E 410  ASN E 411  0                                        
SHEET    2   O 2 VAL E 436  TRP E 437 -1  O  VAL E 436   N  ASN E 411           
SHEET    1   P 6 LEU F 166  ILE F 169  0                                        
SHEET    2   P 6 PHE F 178  GLU F 183 -1  O  VAL F 180   N  TYR F 167           
SHEET    3   P 6 TRP F 191  ARG F 197 -1  O  TRP F 191   N  GLU F 183           
SHEET    4   P 6 LYS F 381  PRO F 388 -1  O  MET F 384   N  PHE F 194           
SHEET    5   P 6 TYR F 244  GLU F 251 -1  N  ALA F 245   O  ILE F 387           
SHEET    6   P 6 THR F 257  THR F 259 -1  O  SER F 258   N  LEU F 250           
SHEET    1   Q 7 PHE F 215  GLY F 216  0                                        
SHEET    2   Q 7 PHE F 226  TRP F 227 -1  O  TRP F 227   N  PHE F 215           
SHEET    3   Q 7 TRP F 191  ARG F 197 -1  N  LYS F 196   O  PHE F 226           
SHEET    4   Q 7 LYS F 381  PRO F 388 -1  O  MET F 384   N  PHE F 194           
SHEET    5   Q 7 TYR F 244  GLU F 251 -1  N  ALA F 245   O  ILE F 387           
SHEET    6   Q 7 TYR F 262  VAL F 267 -1  O  PHE F 265   N  TYR F 244           
SHEET    7   Q 7 LEU F 276  THR F 277 -1  O  THR F 277   N  LYS F 266           
SHEET    1   R 3 LYS G  44  CYS G  45  0                                        
SHEET    2   R 3 VAL K  74  PRO K  77 -1  O  CYS K  76   N  CYS G  45           
SHEET    3   R 3 CYS K  65  LEU K  66 -1  N  CYS K  65   O  LEU K  75           
SHEET    1   S 2 CYS H  76  PRO H  77  0                                        
SHEET    2   S 2 LYS J  44  CYS J  45 -1  O  CYS J  45   N  CYS H  76           
SHEET    1   T 2 THR H 198  VAL H 199  0                                        
SHEET    2   T 2 LYS I 140  ASP I 141  1  O  LYS I 140   N  VAL H 199           
SHEET    1   U 5 GLU H 223  ILE H 227  0                                        
SHEET    2   U 5 TYR H 236  ASP H 241 -1  O  TYR H 236   N  ILE H 227           
SHEET    3   U 5 TRP H 249  ARG H 255 -1  O  VAL H 251   N  TYR H 239           
SHEET    4   U 5 TYR H 292  TRP H 293 -1  O  TYR H 292   N  ASN H 254           
SHEET    5   U 5 PHE H 273  GLY H 274 -1  N  PHE H 273   O  TRP H 293           
SHEET    1   V 7 GLU H 223  ILE H 227  0                                        
SHEET    2   V 7 TYR H 236  ASP H 241 -1  O  TYR H 236   N  ILE H 227           
SHEET    3   V 7 TRP H 249  ARG H 255 -1  O  VAL H 251   N  TYR H 239           
SHEET    4   V 7 LYS H 449  PRO H 456 -1  O  MET H 452   N  ILE H 252           
SHEET    5   V 7 THR H 308  GLU H 315 -1  N  GLU H 309   O  ARG H 455           
SHEET    6   V 7 LYS H 321  PHE H 329 -1  O  TYR H 326   N  LEU H 310           
SHEET    7   V 7 VAL H 342  GLY H 347 -1  O  LYS H 344   N  GLY H 327           
SHEET    1   W 2 ALA H 410  ASN H 411  0                                        
SHEET    2   W 2 VAL H 436  TRP H 437 -1  O  VAL H 436   N  ASN H 411           
SHEET    1   X 2 TYR I  18  PRO I  20  0                                        
SHEET    2   X 2 TYR L  18  PRO L  20 -1  O  CYS L  19   N  CYS I  19           
SHEET    1   Y 5 THR I 149  GLY I 150  0                                        
SHEET    2   Y 5 GLY I 165  ILE I 169  1  O  PHE I 168   N  GLY I 150           
SHEET    3   Y 5 PHE I 178  GLU I 183 -1  O  VAL I 180   N  TYR I 167           
SHEET    4   Y 5 TRP I 191  ARG I 197 -1  O  TRP I 191   N  GLU I 183           
SHEET    5   Y 5 PHE I 226  TRP I 227 -1  O  PHE I 226   N  LYS I 196           
SHEET    1   Z 8 THR I 149  GLY I 150  0                                        
SHEET    2   Z 8 GLY I 165  ILE I 169  1  O  PHE I 168   N  GLY I 150           
SHEET    3   Z 8 PHE I 178  GLU I 183 -1  O  VAL I 180   N  TYR I 167           
SHEET    4   Z 8 TRP I 191  ARG I 197 -1  O  TRP I 191   N  GLU I 183           
SHEET    5   Z 8 LYS I 381  PRO I 388 -1  O  MET I 384   N  GLN I 195           
SHEET    6   Z 8 TYR I 244  GLU I 251 -1  N  ARG I 247   O  LYS I 385           
SHEET    7   Z 8 THR I 259  VAL I 267 -1  O  ALA I 260   N  VAL I 248           
SHEET    8   Z 8 LEU I 276  THR I 277 -1  O  THR I 277   N  LYS I 266           
SHEET    1  AA 2 THR K 198  VAL K 199  0                                        
SHEET    2  AA 2 LYS L 140  ASP L 141  1  O  LYS L 140   N  VAL K 199           
SHEET    1  AB 8 ILE K 203  PRO K 204  0                                        
SHEET    2  AB 8 PHE L 215  LEU L 218 -1  O  LEU L 218   N  ILE K 203           
SHEET    3  AB 8 PHE L 226  TRP L 227 -1  O  TRP L 227   N  PHE L 215           
SHEET    4  AB 8 GLY L 190  ARG L 197 -1  N  LYS L 196   O  PHE L 226           
SHEET    5  AB 8 LYS L 381  ILE L 386 -1  O  MET L 384   N  GLN L 195           
SHEET    6  AB 8 TYR L 244  GLU L 251 -1  N  ARG L 247   O  LYS L 385           
SHEET    7  AB 8 THR L 257  VAL L 267 -1  O  PHE L 265   N  TYR L 244           
SHEET    8  AB 8 LEU L 276  THR L 277 -1  O  THR L 277   N  LYS L 266           
SHEET    1  AC 8 HIS L 146  GLY L 150  0                                        
SHEET    2  AC 8 GLY L 165  ILE L 169  1  O  LEU L 166   N  HIS L 146           
SHEET    3  AC 8 PHE L 178  ILE L 184 -1  O  CYS L 182   N  GLY L 165           
SHEET    4  AC 8 GLY L 190  ARG L 197 -1  O  TRP L 191   N  GLU L 183           
SHEET    5  AC 8 LYS L 381  ILE L 386 -1  O  MET L 384   N  GLN L 195           
SHEET    6  AC 8 TYR L 244  GLU L 251 -1  N  ARG L 247   O  LYS L 385           
SHEET    7  AC 8 THR L 257  VAL L 267 -1  O  PHE L 265   N  TYR L 244           
SHEET    8  AC 8 TYR L 280  GLY L 283 -1  O  TYR L 280   N  ALA L 263           
SHEET    1  AD 6 SER K 207  GLY K 208  0                                        
SHEET    2  AD 6 GLU K 223  ILE K 227  1  O  LEU K 226   N  GLY K 208           
SHEET    3  AD 6 TYR K 236  ASP K 241 -1  O  VAL K 238   N  TYR K 225           
SHEET    4  AD 6 TRP K 249  ARG K 255 -1  O  VAL K 251   N  TYR K 239           
SHEET    5  AD 6 TYR K 292  LEU K 294 -1  O  LEU K 294   N  ILE K 252           
SHEET    6  AD 6 GLY K 272  GLY K 274 -1  N  PHE K 273   O  TRP K 293           
SHEET    1  AE 8 SER K 207  GLY K 208  0                                        
SHEET    2  AE 8 GLU K 223  ILE K 227  1  O  LEU K 226   N  GLY K 208           
SHEET    3  AE 8 TYR K 236  ASP K 241 -1  O  VAL K 238   N  TYR K 225           
SHEET    4  AE 8 TRP K 249  ARG K 255 -1  O  VAL K 251   N  TYR K 239           
SHEET    5  AE 8 LYS K 449  PRO K 456 -1  O  MET K 450   N  ARG K 255           
SHEET    6  AE 8 THR K 308  GLU K 315 -1  N  LEU K 311   O  LYS K 453           
SHEET    7  AE 8 LYS K 321  VAL K 331 -1  O  TYR K 326   N  LEU K 310           
SHEET    8  AE 8 ILE K 340  ARG K 346 -1  O  LYS K 344   N  GLY K 327           
SHEET    1  AF 2 PHE K 374  SER K 376  0                                        
SHEET    2  AF 2 TRP K 402  TYR K 404 -1  O  TRP K 402   N  SER K 376           
SHEET    1  AG 2 GLN L 311  SER L 313  0                                        
SHEET    2  AG 2 TRP L 334  MET L 336 -1  O  TRP L 334   N  SER L 313           
SHEET    1  AH 2 GLY L 342  HIS L 343  0                                        
SHEET    2  AH 2 ILE L 368  TRP L 369 -1  O  ILE L 368   N  HIS L 343           
SSBOND   1 CYS A   28    CYS D   28                          1555   1555  2.05  
SSBOND   2 CYS A   36    CYS E   65                          1555   1555  2.04  
SSBOND   3 CYS A   45    CYS C   23                          1555   1555  2.04  
SSBOND   4 CYS A   49    CYS B   76                          1555   1555  2.03  
SSBOND   5 CYS A  161    CYS C  135                          1555   1555  2.04  
SSBOND   6 CYS A  165    CYS B  193                          1555   1555  2.08  
SSBOND   7 CYS B   65    CYS D   36                          1555   1555  2.04  
SSBOND   8 CYS B   80    CYS C   19                          1555   1555  2.04  
SSBOND   9 CYS B  197    CYS C  139                          1555   1555  2.05  
SSBOND  10 CYS B  201    CYS B  286                          1555   1555  2.02  
SSBOND  11 CYS B  211    CYS B  240                          1555   1555  2.01  
SSBOND  12 CYS B  394    CYS B  407                          1555   1555  2.04  
SSBOND  13 CYS C  153    CYS C  182                          1555   1555  2.02  
SSBOND  14 CYS C  326    CYS C  339                          1555   1555  2.06  
SSBOND  15 CYS D   45    CYS F   23                          1555   1555  2.02  
SSBOND  16 CYS D   49    CYS E   76                          1555   1555  2.04  
SSBOND  17 CYS D  161    CYS F  135                          1555   1555  2.01  
SSBOND  18 CYS D  165    CYS E  193                          1555   1555  2.04  
SSBOND  19 CYS E   80    CYS F   19                          1555   1555  2.03  
SSBOND  20 CYS E  197    CYS F  139                          1555   1555  2.05  
SSBOND  21 CYS E  201    CYS E  286                          1555   1555  2.03  
SSBOND  22 CYS E  211    CYS E  240                          1555   1555  2.04  
SSBOND  23 CYS E  394    CYS E  407                          1555   1555  2.03  
SSBOND  24 CYS F  153    CYS F  182                          1555   1555  2.05  
SSBOND  25 CYS F  326    CYS F  339                          1555   1555  2.03  
SSBOND  26 CYS G   28    CYS J   28                          1555   1555  2.04  
SSBOND  27 CYS G   36    CYS K   65                          1555   1555  2.04  
SSBOND  28 CYS G   45    CYS I   23                          1555   1555  2.03  
SSBOND  29 CYS G   49    CYS H   76                          1555   1555  2.04  
SSBOND  30 CYS G  161    CYS I  135                          1555   1555  2.03  
SSBOND  31 CYS G  165    CYS H  193                          1555   1555  2.04  
SSBOND  32 CYS H   65    CYS J   36                          1555   1555  2.03  
SSBOND  33 CYS H   80    CYS I   19                          1555   1555  2.04  
SSBOND  34 CYS H  197    CYS I  139                          1555   1555  2.05  
SSBOND  35 CYS H  201    CYS H  286                          1555   1555  2.04  
SSBOND  36 CYS H  211    CYS H  240                          1555   1555  2.04  
SSBOND  37 CYS H  394    CYS H  407                          1555   1555  2.06  
SSBOND  38 CYS I    8    CYS L    9                          1555   1555  2.03  
SSBOND  39 CYS I    9    CYS L    8                          1555   1555  2.04  
SSBOND  40 CYS I  153    CYS I  182                          1555   1555  2.04  
SSBOND  41 CYS I  326    CYS I  339                          1555   1555  2.02  
SSBOND  42 CYS J   45    CYS L   23                          1555   1555  2.03  
SSBOND  43 CYS J   49    CYS K   76                          1555   1555  2.03  
SSBOND  44 CYS J  161    CYS L  135                          1555   1555  2.03  
SSBOND  45 CYS J  165    CYS K  193                          1555   1555  2.05  
SSBOND  46 CYS K   80    CYS L   19                          1555   1555  2.04  
SSBOND  47 CYS K  197    CYS L  139                          1555   1555  2.05  
SSBOND  48 CYS K  201    CYS K  286                          1555   1555  2.04  
SSBOND  49 CYS K  211    CYS K  240                          1555   1555  2.03  
SSBOND  50 CYS K  394    CYS K  407                          1555   1555  2.03  
SSBOND  51 CYS L  153    CYS L  182                          1555   1555  2.01  
SSBOND  52 CYS L  326    CYS L  339                          1555   1555  2.05  
LINK         OD1 ASP B 381                CA    CA B 501     1555   1555  2.51  
LINK         OD2 ASP B 381                CA    CA B 501     1555   1555  2.96  
LINK         OD1 ASP B 383                CA    CA B 501     1555   1555  2.52  
LINK         O   TRP B 385                CA    CA B 501     1555   1555  2.40  
LINK         OD1 ASP C 318                CA    CA C 601     1555   1555  2.05  
LINK         OD1 ASP C 320                CA    CA C 601     1555   1555  2.29  
LINK         O   PHE C 322                CA    CA C 601     1555   1555  2.65  
LINK         ND2 ASN E 364                 C1  NAG E 470     1555   1555  1.48  
LINK         OD1 ASP E 381                CA    CA E 501     1555   1555  2.94  
LINK         OD2 ASP E 381                CA    CA E 501     1555   1555  2.97  
LINK         OD1 ASP E 383                CA    CA E 501     1555   1555  2.05  
LINK         O   TRP E 385                CA    CA E 501     1555   1555  2.58  
LINK         OD2 ASP F 318                CA    CA F 601     1555   1555  2.14  
LINK         OD2 ASP F 320                CA    CA F 601     1555   1555  2.30  
LINK         O   GLY F 324                CA    CA F 601     1555   1555  2.81  
LINK         ND2 ASN H 364                 C1  NAG H 470     1555   1555  1.35  
LINK         OD1 ASP H 381                CA    CA H 501     1555   1555  2.57  
LINK         OD2 ASP H 381                CA    CA H 501     1555   1555  2.59  
LINK         OD1 ASP H 383                CA    CA H 501     1555   1555  2.12  
LINK         O   TRP H 385                CA    CA H 501     1555   1555  2.11  
LINK         OD1 ASP I 318                CA    CA I 601     1555   1555  2.88  
LINK         OD2 ASP I 320                CA    CA I 601     1555   1555  2.03  
LINK         O   PHE I 322                CA    CA I 601     1555   1555  2.53  
LINK         O   GLY I 324                CA    CA I 601     1555   1555  2.82  
LINK         OD1 ASP K 381                CA    CA K 501     1555   1555  2.38  
LINK         OD2 ASP K 381                CA    CA K 501     1555   1555  2.52  
LINK         OD1 ASP K 383                CA    CA K 501     1555   1555  2.86  
LINK         O   TRP K 385                CA    CA K 501     1555   1555  2.42  
LINK         OD1 ASP L 318                CA    CA L 601     1555   1555  2.93  
LINK         OD2 ASP L 318                CA    CA L 601     1555   1555  2.07  
LINK         OD2 ASP L 320                CA    CA L 601     1555   1555  2.05  
LINK         O   PHE L 322                CA    CA L 601     1555   1555  2.68  
LINK         O4  NAG B 470                 C1  NDG B 471     1555   1555  1.39  
LINK         O4  NDG B 471                 C1  BMA B 472     1555   1555  1.40  
LINK         O3  BMA B 472                 C1  MAN B 474     1555   1555  1.42  
LINK         O6  BMA B 472                 C1  MAN B 473     1555   1555  1.42  
LINK         O2  MAN B 473                 C1  NDG B 475     1555   1555  1.42  
LINK         O4  NDG B 475                 C1  GAL B 476     1555   1555  1.39  
LINK         O2  MAN B 474                 C1  NDG B 477     1555   1555  1.39  
LINK         O4  NDG B 477                 C1  GAL B 478     1555   1555  1.39  
LINK         O6  GAL B 476                 C2  SIA B 480     1555   1555  1.42  
LINK         C2  SIA B 479                 O6  GAL B 478     1555   1555  1.40  
LINK         O4  NAG E 470                 C1  NDG E 471     1555   1555  1.40  
LINK         O4  NDG E 471                 C1  BMA E 472     1555   1555  1.39  
LINK         O3  BMA E 472                 C1  MAN E 474     1555   1555  1.39  
LINK         O6  BMA E 472                 C1  MAN E 473     1555   1555  1.40  
LINK         O2  MAN E 473                 C1  NDG E 475     1555   1555  1.42  
LINK         O4  NDG E 475                 C1  GAL E 476     1555   1555  1.40  
LINK         O2  MAN E 474                 C1  NDG E 477     1555   1555  1.41  
LINK         O4  NDG E 477                 C1  GAL E 478     1555   1555  1.40  
LINK         O6  GAL E 476                 C2  SIA E 480     1555   1555  1.40  
LINK         C2  SIA E 479                 O6  GAL E 478     1555   1555  1.41  
LINK         O4  NAG H 470                 C1  NDG H 471     1555   1555  1.39  
LINK         O4  NDG H 471                 C1  BMA H 472     1555   1555  1.39  
LINK         O3  BMA H 472                 C1  MAN H 474     1555   1555  1.39  
LINK         O6  BMA H 472                 C1  MAN H 473     1555   1555  1.42  
LINK         O4  NAG K 470                 C1  NDG K 471     1555   1555  1.41  
LINK         O4  NDG K 471                 C1  BMA K 472     1555   1555  1.41  
LINK         O3  BMA K 472                 C1  MAN K 474     1555   1555  1.40  
LINK         O6  BMA K 472                 C1  MAN K 473     1555   1555  1.42  
LINK         O2  MAN K 473                 C1  NDG K 475     1555   1555  1.41  
LINK         O4  NDG K 475                 C1  GAL K 476     1555   1555  1.40  
LINK         O2  MAN K 474                 C1  NDG K 477     1555   1555  1.39  
LINK         O4  NDG K 477                 C1  GAL K 478     1555   1555  1.40  
LINK         O6  GAL K 476                 C2  SIA K 480     1555   1555  1.41  
LINK         C2  SIA K 479                 O6  GAL K 478     1555   1555  1.40  
LINK         O4  NAG L 570                 C1  NAG L 571     1555   1555  1.41  
CISPEP   1 ARG B  406    CYS B  407          0        -3.22                     
CISPEP   2 LYS C  338    CYS C  339          0        -8.78                     
CISPEP   3 ARG E  406    CYS E  407          0       -11.96                     
CISPEP   4 LYS F  338    CYS F  339          0        -6.20                     
CISPEP   5 ARG H  406    CYS H  407          0        -4.74                     
CISPEP   6 LYS I  338    CYS I  339          0         0.38                     
CISPEP   7 ARG K  406    CYS K  407          0       -10.56                     
CISPEP   8 LYS L  338    CYS L  339          0        -7.26                     
SITE     1 AC1  4 MET B 361  ASN B 364  NDG B 471  HIS O   2                    
SITE     1 AC2  4 NAG B 470  BMA B 472  MAN B 474  NDG B 477                    
SITE     1 AC3  4 NDG B 471  MAN B 473  MAN B 474  NDG B 477                    
SITE     1 AC4  3 BMA B 472  NDG B 475  GAL B 476                               
SITE     1 AC5  2 MAN B 473  GAL B 476                                          
SITE     1 AC6  3 NDG B 471  BMA B 472  NDG B 477                               
SITE     1 AC7  5 NDG B 471  BMA B 472  MAN B 474  GAL B 478                    
SITE     2 AC7  5 SIA B 479                                                     
SITE     1 AC8  3 MAN B 473  NDG B 475  SIA B 480                               
SITE     1 AC9  2 NDG B 477  GAL B 478                                          
SITE     1 BC1  2 NDG B 477  SIA B 479                                          
SITE     1 BC2  1 GAL B 476                                                     
SITE     1 BC3  6 MET E 361  GLU E 363  ASN E 364  NDG E 471                    
SITE     2 BC3  6 HIS P   2  PRO P   4                                          
SITE     1 BC4  3 NAG E 470  BMA E 472  NDG E 477                               
SITE     1 BC5  4 NDG E 471  MAN E 473  MAN E 474  NDG E 477                    
SITE     1 BC6  3 BMA E 472  NDG E 475  GAL E 476                               
SITE     1 BC7  2 MAN E 473  GAL E 476                                          
SITE     1 BC8  2 BMA E 472  NDG E 477                                          
SITE     1 BC9  4 NDG E 471  BMA E 472  MAN E 474  GAL E 478                    
SITE     1 CC1  3 MAN E 473  NDG E 475  SIA E 480                               
SITE     1 CC2  2 TRP E 424  GAL E 478                                          
SITE     1 CC3  2 NDG E 477  SIA E 479                                          
SITE     1 CC4  2 GAL E 476  LYS G  81                                          
SITE     1 CC5  5 MET H 361  ASN H 364  NDG H 471  HIS S   2                    
SITE     2 CC5  5 PRO S   4                                                     
SITE     1 CC6  3 NAG H 470  BMA H 472  MAN H 474                               
SITE     1 CC7  3 NDG H 471  MAN H 473  MAN H 474                               
SITE     1 CC8  1 BMA H 472                                                     
SITE     1 CC9  2 NDG H 471  BMA H 472                                          
SITE     1 DC1  5 MET K 361  ASN K 364  NDG K 471  HIS T   2                    
SITE     2 DC1  5 PRO T   4                                                     
SITE     1 DC2  4 NAG K 470  BMA K 472  MAN K 474  NDG K 477                    
SITE     1 DC3  4 NDG K 471  MAN K 473  MAN K 474  NDG K 477                    
SITE     1 DC4  3 BMA K 472  NDG K 475  GAL K 476                               
SITE     1 DC5  2 MAN K 473  GAL K 476                                          
SITE     1 DC6  3 NDG K 471  BMA K 472  NDG K 477                               
SITE     1 DC7  5 NDG K 471  BMA K 472  MAN K 474  GAL K 478                    
SITE     2 DC7  5 SIA K 479                                                     
SITE     1 DC8  3 MAN K 473  NDG K 475  SIA K 480                               
SITE     1 DC9  3 TRP K 424  NDG K 477  GAL K 478                               
SITE     1 EC1  2 NDG K 477  SIA K 479                                          
SITE     1 EC2  1 GAL K 476                                                     
SITE     1 EC3  5 GLN L  49  ASN L  52  LYS L  53  GLU L  56                    
SITE     2 EC3  5 NAG L 571                                                     
SITE     1 EC4  2 GLU L  56  NAG L 570                                          
SITE     1 EC5  3 ASP B 381  ASP B 383  TRP B 385                               
SITE     1 EC6  4 ASP C 318  ASP C 320  PHE C 322  GLY C 324                    
SITE     1 EC7  4 ASP E 381  ASP E 383  TRP E 385  LEU E 386                    
SITE     1 EC8  5 ASP F 318  ASP F 320  PHE F 322  GLU F 323                    
SITE     2 EC8  5 GLY F 324                                                     
SITE     1 EC9  3 ASP H 381  ASP H 383  TRP H 385                               
SITE     1 FC1  4 ASP I 318  ASP I 320  PHE I 322  GLY I 324                    
SITE     1 FC2  3 ASP K 381  ASP K 383  TRP K 385                               
SITE     1 FC3  4 ASP L 318  ASP L 320  PHE L 322  GLY L 324                    
CRYST1  135.238   94.866  300.812  90.00  94.81  90.00 P 1 21 1      8          
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      0.007394  0.000000  0.000622        0.00000                         
SCALE2      0.000000  0.010541  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003336        0.00000                         
ATOM      1  N   ALA A  27      60.434  -5.724 -53.023  1.00152.55           N  
ATOM      2  CA  ALA A  27      59.185  -5.320 -53.728  1.00155.54           C  
ATOM      3  C   ALA A  27      58.771  -3.901 -53.331  1.00159.50           C  
ATOM      4  O   ALA A  27      59.530  -3.185 -52.673  1.00160.92           O  
ATOM      5  CB  ALA A  27      58.066  -6.312 -53.422  1.00152.09           C  
ATOM      6  N   CYS A  28      57.570  -3.504 -53.750  1.00164.08           N  
ATOM      7  CA  CYS A  28      56.951  -2.234 -53.337  1.00167.61           C  
ATOM      8  C   CYS A  28      56.492  -2.328 -51.872  1.00166.53           C  
ATOM      9  O   CYS A  28      56.477  -1.326 -51.150  1.00166.17           O  
ATOM     10  CB  CYS A  28      55.763  -1.895 -54.266  1.00170.09           C  
ATOM     11  SG  CYS A  28      54.810  -0.356 -53.907  1.00171.98           S  
ATOM     12  N   LYS A  29      56.134  -3.543 -51.449  1.00163.92           N  
ATOM     13  CA  LYS A  29      55.668  -3.828 -50.080  1.00159.16           C  
ATOM     14  C   LYS A  29      56.682  -3.520 -48.969  1.00156.98           C  
ATOM     15  O   LYS A  29      56.284  -3.148 -47.862  1.00153.86           O  
ATOM     16  CB  LYS A  29      55.258  -5.305 -49.967  1.00156.37           C  
ATOM     17  CG  LYS A  29      53.823  -5.604 -50.377  1.00153.15           C  
ATOM     18  CD  LYS A  29      52.888  -5.609 -49.174  1.00150.03           C  
ATOM     19  CE  LYS A  29      51.527  -6.185 -49.521  1.00147.63           C  
ATOM     20  NZ  LYS A  29      50.784  -6.581 -48.294  1.00145.45           N  
ATOM     21  N   ASP A  30      57.973  -3.687 -49.269  1.00153.73           N  
ATOM     22  CA  ASP A  30      59.056  -3.622 -48.268  1.00150.19           C  
ATOM     23  C   ASP A  30      58.871  -2.541 -47.191  1.00147.72           C  
ATOM     24  O   ASP A  30      59.331  -1.405 -47.354  1.00144.01           O  
ATOM     25  CB  ASP A  30      60.414  -3.430 -48.965  1.00149.32           C  
ATOM     26  CG  ASP A  30      60.871  -4.673 -49.717  1.00148.04           C  
ATOM     27  OD1 ASP A  30      62.057  -5.041 -49.589  1.00144.57           O  
ATOM     28  OD2 ASP A  30      60.047  -5.286 -50.429  1.00148.96           O  
ATOM     29  N   SER A  31      58.215  -2.913 -46.089  1.00144.92           N  
ATOM     30  CA  SER A  31      57.963  -2.001 -44.966  1.00141.83           C  
ATOM     31  C   SER A  31      59.183  -1.915 -44.049  1.00138.88           C  
ATOM     32  O   SER A  31      59.082  -2.131 -42.837  1.00139.93           O  
ATOM     33  CB  SER A  31      56.736  -2.455 -44.164  1.00140.93           C  
ATOM     34  OG  SER A  31      55.587  -2.541 -44.988  1.00143.39           O  
ATOM     35  N   ASP A  32      60.330  -1.578 -44.638  1.00133.89           N  
ATOM     36  CA  ASP A  32      61.583  -1.420 -43.904  1.00129.11           C  
ATOM     37  C   ASP A  32      61.753   0.046 -43.514  1.00125.24           C  
ATOM     38  O   ASP A  32      62.869   0.564 -43.499  1.00122.07           O  
ATOM     39  CB  ASP A  32      62.771  -1.861 -44.769  1.00129.58           C  
ATOM     40  CG  ASP A  32      62.590  -3.250 -45.360  1.00130.38           C  
ATOM     41  OD1 ASP A  32      61.982  -4.112 -44.692  1.00131.87           O  
ATOM     42  OD2 ASP A  32      63.064  -3.481 -46.493  1.00130.09           O  
ATOM     43  N   TRP A  33      60.643   0.706 -43.193  1.00124.46           N  
ATOM     44  CA  TRP A  33      60.633   2.141 -42.946  1.00123.51           C  
ATOM     45  C   TRP A  33      60.058   2.428 -41.559  1.00120.57           C  
ATOM     46  O   TRP A  33      59.064   1.809 -41.161  1.00114.41           O  
ATOM     47  CB  TRP A  33      59.805   2.849 -44.017  1.00125.74           C  
ATOM     48  CG  TRP A  33      60.167   2.456 -45.421  1.00128.32           C  
ATOM     49  CD1 TRP A  33      59.559   1.502 -46.186  1.00130.55           C  
ATOM     50  CD2 TRP A  33      61.216   3.009 -46.226  1.00129.94           C  
ATOM     51  NE1 TRP A  33      60.165   1.425 -47.419  1.00134.12           N  
ATOM     52  CE2 TRP A  33      61.184   2.339 -47.470  1.00132.37           C  
ATOM     53  CE3 TRP A  33      62.179   4.005 -46.019  1.00129.08           C  
ATOM     54  CZ2 TRP A  33      62.080   2.634 -48.503  1.00132.44           C  
ATOM     55  CZ3 TRP A  33      63.070   4.297 -47.045  1.00129.12           C  
ATOM     56  CH2 TRP A  33      63.013   3.613 -48.271  1.00130.98           C  
ATOM     57  N   PRO A  34      60.677   3.374 -40.822  1.00118.63           N  
ATOM     58  CA  PRO A  34      60.267   3.678 -39.459  1.00117.87           C  
ATOM     59  C   PRO A  34      59.050   4.586 -39.444  1.00117.15           C  
ATOM     60  O   PRO A  34      58.696   5.153 -40.474  1.00116.75           O  
ATOM     61  CB  PRO A  34      61.475   4.422 -38.905  1.00116.86           C  
ATOM     62  CG  PRO A  34      61.976   5.186 -40.077  1.00116.04           C  
ATOM     63  CD  PRO A  34      61.711   4.319 -41.287  1.00116.87           C  
ATOM     64  N   PHE A  35      58.442   4.747 -38.274  1.00116.27           N  
ATOM     65  CA  PHE A  35      57.189   5.488 -38.156  1.00116.18           C  
ATOM     66  C   PHE A  35      57.461   6.989 -38.268  1.00110.98           C  
ATOM     67  O   PHE A  35      58.500   7.469 -37.812  1.00108.48           O  
ATOM     68  CB  PHE A  35      56.474   5.129 -36.845  1.00120.14           C  
ATOM     69  CG  PHE A  35      56.252   3.646 -36.665  1.00121.78           C  
ATOM     70  CD1 PHE A  35      55.116   3.031 -37.179  1.00122.51           C  
ATOM     71  CD2 PHE A  35      57.191   2.866 -35.996  1.00122.86           C  
ATOM     72  CE1 PHE A  35      54.917   1.664 -37.021  1.00124.08           C  
ATOM     73  CE2 PHE A  35      57.002   1.500 -35.835  1.00123.87           C  
ATOM     74  CZ  PHE A  35      55.864   0.897 -36.347  1.00124.96           C  
ATOM     75  N   CYS A  36      56.541   7.718 -38.899  1.00107.97           N  
ATOM     76  CA  CYS A  36      56.741   9.146 -39.173  1.00106.53           C  
ATOM     77  C   CYS A  36      56.493  10.021 -37.956  1.00 99.78           C  
ATOM     78  O   CYS A  36      55.827   9.617 -36.999  1.00100.15           O  
ATOM     79  CB  CYS A  36      55.825   9.634 -40.305  1.00111.09           C  
ATOM     80  SG  CYS A  36      56.267   9.090 -41.974  1.00115.18           S  
ATOM     81  N   SER A  37      57.039  11.231 -38.021  1.00 91.87           N  
ATOM     82  CA  SER A  37      56.760  12.266 -37.042  1.00 89.55           C  
ATOM     83  C   SER A  37      55.652  13.161 -37.576  1.00 83.51           C  
ATOM     84  O   SER A  37      54.976  12.802 -38.540  1.00 80.79           O  
ATOM     85  CB  SER A  37      58.027  13.072 -36.737  1.00 91.51           C  
ATOM     86  OG  SER A  37      59.029  12.233 -36.189  1.00 93.78           O  
ATOM     87  N   ASP A  38      55.461  14.312 -36.937  1.00 83.30           N  
ATOM     88  CA  ASP A  38      54.438  15.277 -37.339  1.00 86.89           C  
ATOM     89  C   ASP A  38      55.027  16.480 -38.085  1.00 84.08           C  
ATOM     90  O   ASP A  38      54.324  17.121 -38.869  1.00 84.23           O  
ATOM     91  CB  ASP A  38      53.584  15.721 -36.134  1.00 92.33           C  
ATOM     92  CG  ASP A  38      54.391  15.867 -34.838  1.00 98.14           C  
ATOM     93  OD1 ASP A  38      55.645  15.823 -34.881  1.00 93.64           O  
ATOM     94  OD2 ASP A  38      53.759  16.019 -33.767  1.00103.92           O  
ATOM     95  N   GLU A  39      56.304  16.789 -37.851  1.00 82.45           N  
ATOM     96  CA  GLU A  39      57.008  17.774 -38.687  1.00 81.53           C  
ATOM     97  C   GLU A  39      57.564  17.070 -39.922  1.00 79.73           C  
ATOM     98  O   GLU A  39      57.852  17.713 -40.931  1.00 79.95           O  
ATOM     99  CB  GLU A  39      58.086  18.558 -37.903  1.00 80.75           C  
ATOM    100  CG  GLU A  39      59.570  18.295 -38.237  1.00 78.38           C  
ATOM    101  CD  GLU A  39      60.277  17.433 -37.201  1.00 77.59           C  
ATOM    102  OE1 GLU A  39      61.190  17.953 -36.518  1.00 69.02           O  
ATOM    103  OE2 GLU A  39      59.916  16.244 -37.065  1.00 80.58           O  
ATOM    104  N   ASP A  40      57.690  15.745 -39.837  1.00 76.73           N  
ATOM    105  CA  ASP A  40      57.933  14.905 -41.011  1.00 75.35           C  
ATOM    106  C   ASP A  40      56.885  15.128 -42.089  1.00 71.55           C  
ATOM    107  O   ASP A  40      57.027  14.633 -43.201  1.00 75.38           O  
ATOM    108  CB  ASP A  40      57.934  13.422 -40.627  1.00 81.37           C  
ATOM    109  CG  ASP A  40      59.293  12.935 -40.147  1.00 87.62           C  
ATOM    110  OD1 ASP A  40      59.336  12.089 -39.226  1.00 91.18           O  
ATOM    111  OD2 ASP A  40      60.321  13.384 -40.699  1.00 94.66           O  
ATOM    112  N   TRP A  41      55.824  15.849 -41.747  1.00 74.04           N  
ATOM    113  CA  TRP A  41      54.833  16.282 -42.716  1.00 80.59           C  
ATOM    114  C   TRP A  41      55.178  17.688 -43.231  1.00 81.26           C  
ATOM    115  O   TRP A  41      55.566  18.560 -42.447  1.00 78.68           O  
ATOM    116  CB  TRP A  41      53.442  16.246 -42.086  1.00 85.44           C  
ATOM    117  CG  TRP A  41      52.440  15.669 -42.992  1.00 88.31           C  
ATOM    118  CD1 TRP A  41      52.225  14.345 -43.237  1.00 93.29           C  
ATOM    119  CD2 TRP A  41      51.519  16.388 -43.805  1.00 90.22           C  
ATOM    120  NE1 TRP A  41      51.211  14.193 -44.154  1.00 94.71           N  
ATOM    121  CE2 TRP A  41      50.761  15.434 -44.520  1.00 94.41           C  
ATOM    122  CE3 TRP A  41      51.255  17.749 -43.999  1.00 91.41           C  
ATOM    123  CZ2 TRP A  41      49.755  15.798 -45.415  1.00 97.79           C  
ATOM    124  CZ3 TRP A  41      50.256  18.111 -44.886  1.00 95.35           C  
ATOM    125  CH2 TRP A  41      49.516  17.137 -45.585  1.00 98.58           C  
ATOM    126  N   ASN A  42      55.000  17.879 -44.545  1.00 82.25           N  
ATOM    127  CA  ASN A  42      55.580  18.986 -45.348  1.00 86.43           C  
ATOM    128  C   ASN A  42      56.996  18.674 -45.841  1.00 79.73           C  
ATOM    129  O   ASN A  42      57.481  19.296 -46.781  1.00 75.45           O  
ATOM    130  CB  ASN A  42      55.594  20.343 -44.616  1.00 95.71           C  
ATOM    131  CG  ASN A  42      54.210  20.956 -44.468  1.00101.95           C  
ATOM    132  OD1 ASN A  42      53.338  20.778 -45.321  1.00104.78           O  
ATOM    133  ND2 ASN A  42      54.012  21.704 -43.386  1.00108.22           N  
ATOM    134  N   TYR A  43      57.647  17.712 -45.198  1.00 77.34           N  
ATOM    135  CA  TYR A  43      59.051  17.421 -45.431  1.00 78.79           C  
ATOM    136  C   TYR A  43      59.129  16.190 -46.314  1.00 77.67           C  
ATOM    137  O   TYR A  43      59.715  16.236 -47.390  1.00 77.05           O  
ATOM    138  CB  TYR A  43      59.772  17.173 -44.100  1.00 81.57           C  
ATOM    139  CG  TYR A  43      60.029  18.414 -43.255  1.00 82.55           C  
ATOM    140  CD1 TYR A  43      61.177  18.508 -42.466  1.00 81.88           C  
ATOM    141  CD2 TYR A  43      59.132  19.488 -43.238  1.00 83.29           C  
ATOM    142  CE1 TYR A  43      61.425  19.631 -41.684  1.00 82.92           C  
ATOM    143  CE2 TYR A  43      59.371  20.613 -42.463  1.00 86.78           C  
ATOM    144  CZ  TYR A  43      60.518  20.681 -41.687  1.00 86.84           C  
ATOM    145  OH  TYR A  43      60.749  21.802 -40.917  1.00 88.10           O  
ATOM    146  N   LYS A  44      58.537  15.093 -45.848  1.00 77.52           N  
ATOM    147  CA  LYS A  44      58.326  13.908 -46.674  1.00 77.69           C  
ATOM    148  C   LYS A  44      56.846  13.893 -47.057  1.00 75.23           C  
ATOM    149  O   LYS A  44      55.999  14.161 -46.210  1.00 67.10           O  
ATOM    150  CB  LYS A  44      58.720  12.632 -45.921  1.00 77.41           C  
ATOM    151  CG  LYS A  44      60.231  12.400 -45.804  1.00 79.47           C  
ATOM    152  CD  LYS A  44      60.893  13.336 -44.785  1.00 80.44           C  
ATOM    153  CE  LYS A  44      62.322  12.904 -44.425  1.00 77.88           C  
ATOM    154  NZ  LYS A  44      63.301  13.108 -45.531  1.00 75.45           N  
ATOM    155  N   CYS A  45      56.542  13.595 -48.324  1.00 79.90           N  
ATOM    156  CA  CYS A  45      55.170  13.714 -48.864  1.00 87.19           C  
ATOM    157  C   CYS A  45      54.718  12.490 -49.702  1.00 85.28           C  
ATOM    158  O   CYS A  45      55.559  11.729 -50.180  1.00 87.61           O  
ATOM    159  CB  CYS A  45      55.067  15.012 -49.675  1.00 91.66           C  
ATOM    160  SG  CYS A  45      55.034  16.518 -48.648  1.00 97.72           S  
ATOM    161  N   PRO A  46      53.387  12.299 -49.886  1.00 80.32           N  
ATOM    162  CA  PRO A  46      52.879  11.042 -50.439  1.00 76.77           C  
ATOM    163  C   PRO A  46      52.857  11.018 -51.960  1.00 76.08           C  
ATOM    164  O   PRO A  46      52.487  12.012 -52.581  1.00 71.17           O  
ATOM    165  CB  PRO A  46      51.448  11.002 -49.912  1.00 75.06           C  
ATOM    166  CG  PRO A  46      51.029  12.439 -49.901  1.00 74.93           C  
ATOM    167  CD  PRO A  46      52.289  13.270 -49.708  1.00 79.49           C  
ATOM    168  N   SER A  47      53.217   9.878 -52.546  1.00 79.12           N  
ATOM    169  CA  SER A  47      53.326   9.760 -54.002  1.00 79.76           C  
ATOM    170  C   SER A  47      51.997  10.083 -54.679  1.00 74.28           C  
ATOM    171  O   SER A  47      50.958   9.541 -54.310  1.00 71.99           O  
ATOM    172  CB  SER A  47      53.799   8.355 -54.412  1.00 79.99           C  
ATOM    173  OG  SER A  47      52.772   7.384 -54.263  1.00 74.52           O  
ATOM    174  N   GLY A  48      52.050  10.966 -55.673  1.00 72.67           N  
ATOM    175  CA  GLY A  48      50.876  11.367 -56.431  1.00 75.95           C  
ATOM    176  C   GLY A  48      49.985  10.227 -56.902  1.00 83.65           C  
ATOM    177  O   GLY A  48      48.770  10.399 -57.005  1.00 88.56           O  
ATOM    178  N   CYS A  49      50.581   9.068 -57.189  1.00 87.49           N  
ATOM    179  CA  CYS A  49      49.834   7.883 -57.646  1.00 93.70           C  
ATOM    180  C   CYS A  49      48.694   7.490 -56.715  1.00 96.16           C  
ATOM    181  O   CYS A  49      47.547   7.304 -57.140  1.00 95.46           O  
ATOM    182  CB  CYS A  49      50.766   6.678 -57.773  1.00 96.20           C  
ATOM    183  SG  CYS A  49      51.889   6.757 -59.161  1.00 97.63           S  
ATOM    184  N   ARG A  50      49.033   7.332 -55.442  1.00 96.18           N  
ATOM    185  CA  ARG A  50      48.050   6.992 -54.429  1.00 94.59           C  
ATOM    186  C   ARG A  50      47.138   8.184 -54.239  1.00 86.53           C  
ATOM    187  O   ARG A  50      45.943   8.019 -54.044  1.00 88.30           O  
ATOM    188  CB  ARG A  50      48.739   6.625 -53.121  1.00100.58           C  
ATOM    189  CG  ARG A  50      47.949   5.692 -52.214  1.00105.77           C  
ATOM    190  CD  ARG A  50      48.786   5.268 -51.007  1.00113.43           C  
ATOM    191  NE  ARG A  50      50.235   5.328 -51.258  1.00122.22           N  
ATOM    192  CZ  ARG A  50      51.044   6.348 -50.936  1.00128.24           C  
ATOM    193  NH1 ARG A  50      50.579   7.444 -50.331  1.00132.47           N  
ATOM    194  NH2 ARG A  50      52.341   6.277 -51.226  1.00126.43           N  
ATOM    195  N   MET A  51      47.703   9.385 -54.317  1.00 81.93           N  
ATOM    196  CA  MET A  51      46.894  10.597 -54.274  1.00 85.57           C  
ATOM    197  C   MET A  51      45.971  10.638 -55.477  1.00 85.75           C  
ATOM    198  O   MET A  51      44.784  10.903 -55.329  1.00 87.93           O  
ATOM    199  CB  MET A  51      47.759  11.859 -54.237  1.00 84.97           C  
ATOM    200  CG  MET A  51      48.661  11.968 -53.019  1.00 86.39           C  
ATOM    201  SD  MET A  51      47.822  11.622 -51.460  1.00 84.91           S  
ATOM    202  CE  MET A  51      46.526  12.856 -51.499  1.00 88.26           C  
ATOM    203  N   LYS A  52      46.512  10.367 -56.662  1.00 87.94           N  
ATOM    204  CA  LYS A  52      45.693  10.269 -57.870  1.00 94.14           C  
ATOM    205  C   LYS A  52      44.546   9.286 -57.649  1.00 96.96           C  
ATOM    206  O   LYS A  52      43.412   9.554 -58.049  1.00 99.23           O  
ATOM    207  CB  LYS A  52      46.535   9.820 -59.066  1.00 97.56           C  
ATOM    208  CG  LYS A  52      45.793   9.783 -60.406  1.00 99.41           C  
ATOM    209  CD  LYS A  52      45.595  11.179 -60.988  1.00101.61           C  
ATOM    210  CE  LYS A  52      45.247  11.124 -62.471  1.00101.92           C  
ATOM    211  NZ  LYS A  52      45.282  12.470 -63.107  1.00102.51           N  
ATOM    212  N   GLY A  53      44.847   8.156 -57.011  1.00 97.03           N  
ATOM    213  CA  GLY A  53      43.828   7.164 -56.667  1.00 95.86           C  
ATOM    214  C   GLY A  53      42.790   7.678 -55.683  1.00 93.58           C  
ATOM    215  O   GLY A  53      41.614   7.321 -55.771  1.00 97.61           O  
ATOM    216  N   LEU A  54      43.226   8.526 -54.755  1.00 90.02           N  
ATOM    217  CA  LEU A  54      42.349   9.067 -53.720  1.00 89.48           C  
ATOM    218  C   LEU A  54      41.626  10.320 -54.207  1.00 89.37           C  
ATOM    219  O   LEU A  54      40.425  10.466 -53.987  1.00 97.76           O  
ATOM    220  CB  LEU A  54      43.153   9.358 -52.450  1.00 89.80           C  
ATOM    221  CG  LEU A  54      43.761   8.097 -51.815  1.00 91.25           C  
ATOM    222  CD1 LEU A  54      45.028   8.419 -51.030  1.00 93.06           C  
ATOM    223  CD2 LEU A  54      42.746   7.361 -50.943  1.00 90.12           C  
ATOM    224  N   ILE A  55      42.355  11.210 -54.878  1.00 88.62           N  
ATOM    225  CA  ILE A  55      41.781  12.427 -55.476  1.00 91.60           C  
ATOM    226  C   ILE A  55      40.505  12.155 -56.262  1.00 93.07           C  
ATOM    227  O   ILE A  55      39.581  12.971 -56.269  1.00 90.72           O  
ATOM    228  CB  ILE A  55      42.782  13.090 -56.439  1.00 98.60           C  
ATOM    229  CG1 ILE A  55      43.849  13.853 -55.653  1.00102.30           C  
ATOM    230  CG2 ILE A  55      42.069  14.034 -57.401  1.00 98.36           C  
ATOM    231  CD1 ILE A  55      45.108  14.106 -56.442  1.00103.69           C  
ATOM    232  N   ASP A  56      40.472  11.008 -56.934  1.00 98.13           N  
ATOM    233  CA  ASP A  56      39.315  10.594 -57.717  1.00101.01           C  
ATOM    234  C   ASP A  56      38.246   9.912 -56.858  1.00104.85           C  
ATOM    235  O   ASP A  56      37.059  10.211 -57.002  1.00110.56           O  
ATOM    236  CB  ASP A  56      39.754   9.665 -58.852  1.00 99.60           C  
ATOM    237  CG  ASP A  56      40.744  10.326 -59.795  1.00100.10           C  
ATOM    238  OD1 ASP A  56      41.649   9.620 -60.290  1.00102.80           O  
ATOM    239  OD2 ASP A  56      40.622  11.548 -60.035  1.00 98.68           O  
ATOM    240  N   GLU A  57      38.660   9.012 -55.962  1.00104.96           N  
ATOM    241  CA  GLU A  57      37.708   8.259 -55.120  1.00104.72           C  
ATOM    242  C   GLU A  57      36.779   9.183 -54.327  1.00 99.76           C  
ATOM    243  O   GLU A  57      35.638   8.823 -54.041  1.00 99.69           O  
ATOM    244  CB  GLU A  57      38.441   7.312 -54.155  1.00106.89           C  
ATOM    245  CG  GLU A  57      37.600   6.115 -53.680  1.00107.96           C  
ATOM    246  CD  GLU A  57      37.946   5.657 -52.264  1.00109.17           C  
ATOM    247  OE1 GLU A  57      38.542   4.567 -52.099  1.00103.66           O  
ATOM    248  OE2 GLU A  57      37.615   6.393 -51.311  1.00115.02           O  
ATOM    249  N   VAL A  58      37.271  10.371 -53.980  1.00 98.40           N  
ATOM    250  CA  VAL A  58      36.455  11.364 -53.291  1.00 99.06           C  
ATOM    251  C   VAL A  58      35.549  12.103 -54.289  1.00103.84           C  
ATOM    252  O   VAL A  58      34.332  12.135 -54.103  1.00113.20           O  
ATOM    253  CB  VAL A  58      37.322  12.359 -52.471  1.00 94.77           C  
ATOM    254  CG1 VAL A  58      37.339  13.747 -53.106  1.00 92.72           C  
ATOM    255  CG2 VAL A  58      36.808  12.445 -51.048  1.00 94.70           C  
ATOM    256  N   ASN A  59      36.130  12.655 -55.359  1.00103.90           N  
ATOM    257  CA  ASN A  59      35.360  13.407 -56.368  1.00101.78           C  
ATOM    258  C   ASN A  59      34.323  12.545 -57.083  1.00102.95           C  
ATOM    259  O   ASN A  59      33.379  13.071 -57.671  1.00105.55           O  
ATOM    260  CB  ASN A  59      36.282  14.041 -57.422  1.00100.64           C  
ATOM    261  CG  ASN A  59      37.247  15.059 -56.835  1.00 98.02           C  
ATOM    262  OD1 ASN A  59      37.032  15.586 -55.746  1.00 96.53           O  
ATOM    263  ND2 ASN A  59      38.320  15.339 -57.563  1.00 91.81           N  
ATOM    264  N   GLN A  60      34.513  11.227 -57.038  1.00106.51           N  
ATOM    265  CA  GLN A  60      33.575  10.274 -57.626  1.00112.69           C  
ATOM    266  C   GLN A  60      32.442   9.912 -56.652  1.00113.31           C  
ATOM    267  O   GLN A  60      31.271   9.917 -57.036  1.00113.20           O  
ATOM    268  CB  GLN A  60      34.324   9.014 -58.084  1.00116.27           C  
ATOM    269  CG  GLN A  60      33.594   8.179 -59.138  1.00118.93           C  
ATOM    270  CD  GLN A  60      32.498   7.297 -58.559  1.00121.46           C  
ATOM    271  OE1 GLN A  60      32.621   6.775 -57.448  1.00122.55           O  
ATOM    272  NE2 GLN A  60      31.420   7.120 -59.319  1.00121.96           N  
ATOM    273  N   ASP A  61      32.787   9.600 -55.400  1.00112.53           N  
ATOM    274  CA  ASP A  61      31.777   9.275 -54.374  1.00113.55           C  
ATOM    275  C   ASP A  61      30.945  10.481 -53.944  1.00112.77           C  
ATOM    276  O   ASP A  61      29.925  10.316 -53.278  1.00110.32           O  
ATOM    277  CB  ASP A  61      32.421   8.625 -53.145  1.00114.34           C  
ATOM    278  CG  ASP A  61      32.786   7.169 -53.377  1.00115.13           C  
ATOM    279  OD1 ASP A  61      32.478   6.637 -54.466  1.00115.16           O  
ATOM    280  OD2 ASP A  61      33.380   6.551 -52.466  1.00116.03           O  
ATOM    281  N   PHE A  62      31.395  11.684 -54.307  1.00113.47           N  
ATOM    282  CA  PHE A  62      30.557  12.881 -54.234  1.00113.87           C  
ATOM    283  C   PHE A  62      29.636  13.009 -55.455  1.00113.42           C  
ATOM    284  O   PHE A  62      28.653  13.745 -55.399  1.00108.51           O  
ATOM    285  CB  PHE A  62      31.406  14.153 -54.087  1.00113.98           C  
ATOM    286  CG  PHE A  62      32.160  14.243 -52.779  1.00114.28           C  
ATOM    287  CD1 PHE A  62      33.502  14.583 -52.764  1.00115.98           C  
ATOM    288  CD2 PHE A  62      31.527  13.989 -51.565  1.00114.86           C  
ATOM    289  CE1 PHE A  62      34.201  14.665 -51.565  1.00117.61           C  
ATOM    290  CE2 PHE A  62      32.220  14.069 -50.365  1.00112.92           C  
ATOM    291  CZ  PHE A  62      33.556  14.408 -50.365  1.00114.49           C  
ATOM    292  N   THR A  63      29.956  12.313 -56.552  1.00115.90           N  
ATOM    293  CA  THR A  63      29.065  12.263 -57.724  1.00114.78           C  
ATOM    294  C   THR A  63      28.128  11.035 -57.706  1.00116.49           C  
ATOM    295  O   THR A  63      27.102  11.033 -58.390  1.00121.39           O  
ATOM    296  CB  THR A  63      29.831  12.343 -59.080  1.00109.99           C  
ATOM    297  OG1 THR A  63      30.780  11.276 -59.177  1.00108.84           O  
ATOM    298  CG2 THR A  63      30.549  13.680 -59.223  1.00105.62           C  
ATOM    299  N   ASN A  64      28.478  10.004 -56.932  1.00114.02           N  
ATOM    300  CA  ASN A  64      27.559   8.877 -56.658  1.00113.30           C  
ATOM    301  C   ASN A  64      26.541   9.265 -55.594  1.00112.31           C  
ATOM    302  O   ASN A  64      25.364   8.896 -55.653  1.00111.14           O  
ATOM    303  CB  ASN A  64      28.323   7.630 -56.188  1.00112.81           C  
ATOM    304  CG  ASN A  64      28.323   6.516 -57.220  1.00112.95           C  
ATOM    305  OD1 ASN A  64      28.477   6.757 -58.417  1.00115.66           O  
ATOM    306  ND2 ASN A  64      28.153   5.284 -56.755  1.00111.79           N  
ATOM    307  N   ARG A  65      27.032  10.000 -54.607  1.00111.73           N  
ATOM    308  CA  ARG A  65      26.204  10.580 -53.575  1.00111.20           C  
ATOM    309  C   ARG A  65      25.262  11.615 -54.181  1.00111.41           C  
ATOM    310  O   ARG A  65      24.056  11.543 -53.965  1.00117.83           O  
ATOM    311  CB  ARG A  65      27.103  11.224 -52.526  1.00112.05           C  
ATOM    312  CG  ARG A  65      26.457  11.497 -51.208  1.00111.19           C  
ATOM    313  CD  ARG A  65      27.505  11.979 -50.231  1.00110.81           C  
ATOM    314  NE  ARG A  65      27.095  11.780 -48.850  1.00114.59           N  
ATOM    315  CZ  ARG A  65      27.825  12.116 -47.790  1.00118.97           C  
ATOM    316  NH1 ARG A  65      29.022  12.678 -47.935  1.00116.97           N  
ATOM    317  NH2 ARG A  65      27.352  11.890 -46.570  1.00126.51           N  
ATOM    318  N   ILE A  66      25.808  12.559 -54.952  1.00110.91           N  
ATOM    319  CA  ILE A  66      24.997  13.615 -55.580  1.00116.41           C  
ATOM    320  C   ILE A  66      23.899  13.036 -56.479  1.00120.43           C  
ATOM    321  O   ILE A  66      22.818  13.615 -56.574  1.00126.19           O  
ATOM    322  CB  ILE A  66      25.856  14.625 -56.415  1.00118.22           C  
ATOM    323  CG1 ILE A  66      25.117  15.956 -56.644  1.00117.07           C  
ATOM    324  CG2 ILE A  66      26.251  14.028 -57.754  1.00122.02           C  
ATOM    325  CD1 ILE A  66      25.694  17.125 -55.865  1.00114.77           C  
ATOM    326  N   ASN A  67      24.171  11.904 -57.133  1.00122.23           N  
ATOM    327  CA  ASN A  67      23.181  11.278 -58.026  1.00123.27           C  
ATOM    328  C   ASN A  67      22.006  10.627 -57.276  1.00125.06           C  
ATOM    329  O   ASN A  67      20.879  10.631 -57.781  1.00128.14           O  
ATOM    330  CB  ASN A  67      23.844  10.268 -58.983  1.00122.28           C  
ATOM    331  CG  ASN A  67      24.453  10.929 -60.230  1.00120.17           C  
ATOM    332  OD1 ASN A  67      24.060  12.025 -60.637  1.00116.96           O  
ATOM    333  ND2 ASN A  67      25.413  10.246 -60.842  1.00118.68           N  
ATOM    334  N   LYS A  68      22.259  10.080 -56.085  1.00122.37           N  
ATOM    335  CA  LYS A  68      21.181   9.529 -55.246  1.00121.57           C  
ATOM    336  C   LYS A  68      20.460  10.625 -54.445  1.00120.63           C  
ATOM    337  O   LYS A  68      19.327  10.434 -53.993  1.00120.27           O  
ATOM    338  CB  LYS A  68      21.720   8.450 -54.306  1.00119.74           C  
ATOM    339  CG  LYS A  68      20.655   7.458 -53.857  1.00119.10           C  
ATOM    340  CD  LYS A  68      21.222   6.353 -52.976  1.00118.56           C  
ATOM    341  CE  LYS A  68      22.113   5.389 -53.748  1.00116.68           C  
ATOM    342  NZ  LYS A  68      23.496   5.906 -53.929  1.00116.60           N  
ATOM    343  N   LEU A  69      21.134  11.761 -54.274  1.00121.72           N  
ATOM    344  CA  LEU A  69      20.555  12.960 -53.662  1.00122.76           C  
ATOM    345  C   LEU A  69      19.641  13.667 -54.668  1.00123.59           C  
ATOM    346  O   LEU A  69      18.464  13.899 -54.395  1.00127.67           O  
ATOM    347  CB  LEU A  69      21.684  13.898 -53.203  1.00120.77           C  
ATOM    348  CG  LEU A  69      21.398  15.165 -52.387  1.00118.32           C  
ATOM    349  CD1 LEU A  69      20.693  16.235 -53.225  1.00117.34           C  
ATOM    350  CD2 LEU A  69      20.621  14.841 -51.121  1.00116.19           C  
ATOM    351  N   LYS A  70      20.192  14.001 -55.833  1.00124.75           N  
ATOM    352  CA  LYS A  70      19.424  14.637 -56.904  1.00126.33           C  
ATOM    353  C   LYS A  70      18.190  13.821 -57.278  1.00127.29           C  
ATOM    354  O   LYS A  70      17.097  14.373 -57.350  1.00132.92           O  
ATOM    355  CB  LYS A  70      20.286  14.853 -58.151  1.00129.13           C  
ATOM    356  CG  LYS A  70      21.245  16.035 -58.057  1.00131.82           C  
ATOM    357  CD  LYS A  70      22.007  16.270 -59.363  1.00132.54           C  
ATOM    358  CE  LYS A  70      22.958  15.124 -59.702  1.00132.56           C  
ATOM    359  NZ  LYS A  70      23.752  15.396 -60.933  1.00132.32           N  
ATOM    360  N   ASN A  71      18.353  12.513 -57.494  1.00127.03           N  
ATOM    361  CA  ASN A  71      17.222  11.656 -57.905  1.00125.48           C  
ATOM    362  C   ASN A  71      16.067  11.596 -56.894  1.00125.75           C  
ATOM    363  O   ASN A  71      14.984  11.118 -57.224  1.00125.45           O  
ATOM    364  CB  ASN A  71      17.683  10.234 -58.306  1.00124.60           C  
ATOM    365  CG  ASN A  71      17.952   9.303 -57.107  1.00124.46           C  
ATOM    366  OD1 ASN A  71      18.447   8.188 -57.292  1.00121.82           O  
ATOM    367  ND2 ASN A  71      17.624   9.743 -55.898  1.00122.19           N  
ATOM    368  N   SER A  72      16.310  12.061 -55.669  1.00127.82           N  
ATOM    369  CA  SER A  72      15.251  12.237 -54.684  1.00127.38           C  
ATOM    370  C   SER A  72      14.686  13.661 -54.778  1.00131.29           C  
ATOM    371  O   SER A  72      13.475  13.846 -54.687  1.00138.94           O  
ATOM    372  CB  SER A  72      15.770  11.939 -53.276  1.00124.32           C  
ATOM    373  OG  SER A  72      16.190  10.588 -53.173  1.00121.42           O  
ATOM    374  N   LEU A  73      15.559  14.652 -54.989  1.00131.54           N  
ATOM    375  CA  LEU A  73      15.150  16.074 -55.096  1.00131.53           C  
ATOM    376  C   LEU A  73      14.083  16.323 -56.167  1.00133.22           C  
ATOM    377  O   LEU A  73      13.239  17.210 -56.022  1.00132.21           O  
ATOM    378  CB  LEU A  73      16.371  16.973 -55.368  1.00130.59           C  
ATOM    379  CG  LEU A  73      16.181  18.450 -55.770  1.00130.08           C  
ATOM    380  CD1 LEU A  73      15.842  18.611 -57.252  1.00128.32           C  
ATOM    381  CD2 LEU A  73      15.142  19.155 -54.904  1.00129.47           C  
ATOM    382  N   PHE A  74      14.134  15.551 -57.245  1.00137.23           N  
ATOM    383  CA  PHE A  74      13.165  15.695 -58.331  1.00142.38           C  
ATOM    384  C   PHE A  74      11.909  14.840 -58.096  1.00143.43           C  
ATOM    385  O   PHE A  74      10.869  15.095 -58.702  1.00143.81           O  
ATOM    386  CB  PHE A  74      13.827  15.381 -59.679  1.00145.61           C  
ATOM    387  CG  PHE A  74      15.010  16.275 -59.992  1.00149.74           C  
ATOM    388  CD1 PHE A  74      14.818  17.592 -60.395  1.00150.71           C  
ATOM    389  CD2 PHE A  74      16.316  15.803 -59.868  1.00151.30           C  
ATOM    390  CE1 PHE A  74      15.907  18.422 -60.678  1.00150.95           C  
ATOM    391  CE2 PHE A  74      17.411  16.629 -60.145  1.00150.88           C  
ATOM    392  CZ  PHE A  74      17.204  17.938 -60.554  1.00150.73           C  
ATOM    393  N   GLU A  75      12.007  13.843 -57.212  1.00143.76           N  
ATOM    394  CA  GLU A  75      10.840  13.058 -56.780  1.00145.39           C  
ATOM    395  C   GLU A  75       9.846  13.939 -56.032  1.00143.89           C  
ATOM    396  O   GLU A  75       8.650  13.931 -56.326  1.00145.14           O  
ATOM    397  CB  GLU A  75      11.257  11.898 -55.863  1.00146.93           C  
ATOM    398  CG  GLU A  75      11.890  10.713 -56.577  1.00147.63           C  
ATOM    399  CD  GLU A  75      10.873   9.742 -57.153  1.00148.35           C  
ATOM    400  OE1 GLU A  75       9.756   9.624 -56.598  1.00148.32           O  
ATOM    401  OE2 GLU A  75      11.201   9.083 -58.161  1.00150.03           O  
ATOM    402  N   TYR A  76      10.359  14.702 -55.070  1.00141.20           N  
ATOM    403  CA  TYR A  76       9.525  15.559 -54.227  1.00141.46           C  
ATOM    404  C   TYR A  76       9.196  16.884 -54.919  1.00138.76           C  
ATOM    405  O   TYR A  76       8.368  17.652 -54.428  1.00142.03           O  
ATOM    406  CB  TYR A  76      10.189  15.782 -52.862  1.00145.18           C  
ATOM    407  CG  TYR A  76      10.605  14.480 -52.197  1.00149.27           C  
ATOM    408  CD1 TYR A  76       9.652  13.568 -51.746  1.00150.47           C  
ATOM    409  CD2 TYR A  76      11.950  14.149 -52.043  1.00152.00           C  
ATOM    410  CE1 TYR A  76      10.027  12.366 -51.150  1.00150.22           C  
ATOM    411  CE2 TYR A  76      12.335  12.948 -51.448  1.00152.73           C  
ATOM    412  CZ  TYR A  76      11.367  12.064 -51.004  1.00151.15           C  
ATOM    413  OH  TYR A  76      11.734  10.875 -50.421  1.00149.40           O  
ATOM    414  N   GLN A  77       9.847  17.142 -56.054  1.00137.18           N  
ATOM    415  CA  GLN A  77       9.453  18.220 -56.961  1.00138.10           C  
ATOM    416  C   GLN A  77       8.460  17.713 -58.022  1.00140.74           C  
ATOM    417  O   GLN A  77       7.835  18.514 -58.720  1.00141.21           O  
ATOM    418  CB  GLN A  77      10.688  18.835 -57.626  1.00137.47           C  
ATOM    419  CG  GLN A  77      10.424  20.170 -58.318  1.00136.38           C  
ATOM    420  CD  GLN A  77      11.694  20.960 -58.598  1.00134.40           C  
ATOM    421  OE1 GLN A  77      12.806  20.434 -58.514  1.00131.09           O  
ATOM    422  NE2 GLN A  77      11.529  22.235 -58.933  1.00132.85           N  
ATOM    423  N   LYS A  78       8.336  16.388 -58.148  1.00143.31           N  
ATOM    424  CA  LYS A  78       7.260  15.750 -58.929  1.00145.42           C  
ATOM    425  C   LYS A  78       6.090  15.317 -58.032  1.00146.90           C  
ATOM    426  O   LYS A  78       4.941  15.287 -58.476  1.00145.11           O  
ATOM    427  CB  LYS A  78       7.784  14.529 -59.687  1.00146.35           C  
ATOM    428  CG  LYS A  78       8.691  14.848 -60.869  1.00148.04           C  
ATOM    429  CD  LYS A  78       9.371  13.578 -61.383  1.00150.20           C  
ATOM    430  CE  LYS A  78      10.659  13.864 -62.151  1.00150.30           C  
ATOM    431  NZ  LYS A  78      10.417  14.473 -63.485  1.00150.89           N  
ATOM    432  N   ASN A  79       6.397  14.952 -56.786  1.00148.66           N  
ATOM    433  CA  ASN A  79       5.381  14.739 -55.746  1.00150.18           C  
ATOM    434  C   ASN A  79       4.708  16.060 -55.343  1.00153.26           C  
ATOM    435  O   ASN A  79       3.568  16.070 -54.878  1.00158.65           O  
ATOM    436  CB  ASN A  79       6.014  14.083 -54.513  1.00148.38           C  
ATOM    437  CG  ASN A  79       5.003  13.774 -53.427  1.00146.36           C  
ATOM    438  OD1 ASN A  79       3.919  13.269 -53.704  1.00146.99           O  
ATOM    439  ND2 ASN A  79       5.353  14.080 -52.184  1.00144.07           N  
ATOM    440  N   ASN A  80       5.441  17.163 -55.501  1.00154.90           N  
ATOM    441  CA  ASN A  80       4.889  18.519 -55.402  1.00158.46           C  
ATOM    442  C   ASN A  80       3.727  18.720 -56.379  1.00162.88           C  
ATOM    443  O   ASN A  80       2.627  19.092 -55.977  1.00168.95           O  
ATOM    444  CB  ASN A  80       6.009  19.549 -55.657  1.00157.25           C  
ATOM    445  CG  ASN A  80       5.490  20.964 -55.893  1.00155.23           C  
ATOM    446  OD1 ASN A  80       5.073  21.313 -56.999  1.00152.33           O  
ATOM    447  ND2 ASN A  80       5.558  21.796 -54.862  1.00154.77           N  
ATOM    448  N   LYS A  81       3.972  18.448 -57.659  1.00166.09           N  
ATOM    449  CA  LYS A  81       2.972  18.675 -58.712  1.00167.42           C  
ATOM    450  C   LYS A  81       1.639  17.953 -58.439  1.00170.58           C  
ATOM    451  O   LYS A  81       0.565  18.505 -58.697  1.00170.07           O  
ATOM    452  CB  LYS A  81       3.527  18.251 -60.083  1.00166.10           C  
ATOM    453  CG  LYS A  81       3.425  19.327 -61.153  1.00165.72           C  
ATOM    454  CD  LYS A  81       4.456  20.426 -60.931  1.00166.84           C  
ATOM    455  CE  LYS A  81       4.496  21.404 -62.096  1.00167.69           C  
ATOM    456  NZ  LYS A  81       5.591  22.409 -61.953  1.00168.68           N  
ATOM    457  N   ASP A  82       1.722  16.734 -57.903  1.00174.10           N  
ATOM    458  CA  ASP A  82       0.542  15.891 -57.650  1.00175.57           C  
ATOM    459  C   ASP A  82      -0.180  16.234 -56.339  1.00176.98           C  
ATOM    460  O   ASP A  82      -1.415  16.266 -56.295  1.00176.62           O  
ATOM    461  CB  ASP A  82       0.943  14.407 -57.620  1.00175.43           C  
ATOM    462  CG  ASP A  82       1.579  13.935 -58.920  1.00174.70           C  
ATOM    463  OD1 ASP A  82       1.996  14.783 -59.737  1.00175.52           O  
ATOM    464  OD2 ASP A  82       1.668  12.705 -59.120  1.00173.69           O  
ATOM    465  N   SER A  83       0.592  16.474 -55.277  1.00175.63           N  
ATOM    466  CA  SER A  83       0.035  16.702 -53.935  1.00177.22           C  
ATOM    467  C   SER A  83      -0.605  18.091 -53.774  1.00178.99           C  
ATOM    468  O   SER A  83      -1.526  18.251 -52.972  1.00181.03           O  
ATOM    469  CB  SER A  83       1.107  16.477 -52.860  1.00175.60           C  
ATOM    470  OG  SER A  83       0.517  16.168 -51.609  1.00173.45           O  
ATOM    471  N   HIS A  84      -0.118  19.084 -54.523  1.00179.42           N  
ATOM    472  CA  HIS A  84      -0.759  20.411 -54.583  1.00181.95           C  
ATOM    473  C   HIS A  84      -2.042  20.375 -55.428  1.00179.44           C  
ATOM    474  O   HIS A  84      -2.875  21.284 -55.346  1.00178.01           O  
ATOM    475  CB  HIS A  84       0.205  21.474 -55.135  1.00186.01           C  
ATOM    476  CG  HIS A  84       1.321  21.836 -54.197  1.00191.04           C  
ATOM    477  ND1 HIS A  84       1.265  22.927 -53.355  1.00192.99           N  
ATOM    478  CD2 HIS A  84       2.527  21.258 -53.978  1.00193.18           C  
ATOM    479  CE1 HIS A  84       2.385  23.001 -52.656  1.00193.30           C  
ATOM    480  NE2 HIS A  84       3.167  22.000 -53.015  1.00193.44           N  
ATOM    481  N   SER A  85      -2.184  19.330 -56.246  1.00177.37           N  
ATOM    482  CA  SER A  85      -3.430  19.053 -56.961  1.00176.10           C  
ATOM    483  C   SER A  85      -4.419  18.294 -56.065  1.00177.36           C  
ATOM    484  O   SER A  85      -5.614  18.594 -56.071  1.00176.87           O  
ATOM    485  CB  SER A  85      -3.149  18.260 -58.241  1.00174.10           C  
ATOM    486  OG  SER A  85      -4.352  17.870 -58.879  1.00171.99           O  
ATOM    487  N   LEU A  86      -3.917  17.323 -55.299  1.00178.37           N  
ATOM    488  CA  LEU A  86      -4.747  16.543 -54.359  1.00179.12           C  
ATOM    489  C   LEU A  86      -5.163  17.345 -53.110  1.00180.62           C  
ATOM    490  O   LEU A  86      -6.171  17.021 -52.477  1.00179.40           O  
ATOM    491  CB  LEU A  86      -4.023  15.250 -53.938  1.00177.86           C  
ATOM    492  CG  LEU A  86      -4.783  14.237 -53.067  1.00176.73           C  
ATOM    493  CD1 LEU A  86      -6.079  13.797 -53.733  1.00176.41           C  
ATOM    494  CD2 LEU A  86      -3.912  13.027 -52.755  1.00174.86           C  
ATOM    495  N   THR A  87      -4.387  18.375 -52.761  1.00182.30           N  
ATOM    496  CA  THR A  87      -4.692  19.261 -51.621  1.00181.71           C  
ATOM    497  C   THR A  87      -5.745  20.307 -51.977  1.00178.99           C  
ATOM    498  O   THR A  87      -6.649  20.576 -51.186  1.00176.56           O  
ATOM    499  CB  THR A  87      -3.430  19.994 -51.107  1.00183.14           C  
ATOM    500  OG1 THR A  87      -2.572  19.058 -50.445  1.00184.40           O  
ATOM    501  CG2 THR A  87      -3.801  21.117 -50.133  1.00182.49           C  
ATOM    502  N   THR A  88      -5.612  20.908 -53.157  1.00176.98           N  
ATOM    503  CA  THR A  88      -6.644  21.802 -53.670  1.00175.87           C  
ATOM    504  C   THR A  88      -7.878  20.996 -54.117  1.00176.14           C  
ATOM    505  O   THR A  88      -8.969  21.552 -54.232  1.00174.47           O  
ATOM    506  CB  THR A  88      -6.117  22.683 -54.821  1.00175.50           C  
ATOM    507  OG1 THR A  88      -4.806  23.160 -54.498  1.00175.73           O  
ATOM    508  CG2 THR A  88      -7.039  23.876 -55.053  1.00174.66           C  
ATOM    509  N   ASN A  89      -7.700  19.692 -54.359  1.00177.30           N  
ATOM    510  CA  ASN A  89      -8.820  18.765 -54.611  1.00178.55           C  
ATOM    511  C   ASN A  89      -9.637  18.491 -53.349  1.00177.33           C  
ATOM    512  O   ASN A  89     -10.856  18.677 -53.336  1.00175.83           O  
ATOM    513  CB  ASN A  89      -8.311  17.435 -55.185  1.00179.44           C  
ATOM    514  CG  ASN A  89      -9.401  16.375 -55.279  1.00180.02           C  
ATOM    515  OD1 ASN A  89     -10.470  16.614 -55.842  1.00180.68           O  
ATOM    516  ND2 ASN A  89      -9.129  15.195 -54.728  1.00179.96           N  
ATOM    517  N   ILE A  90      -8.961  18.036 -52.296  1.00176.75           N  
ATOM    518  CA  ILE A  90      -9.601  17.871 -50.986  1.00175.18           C  
ATOM    519  C   ILE A  90      -9.949  19.230 -50.353  1.00172.96           C  
ATOM    520  O   ILE A  90     -10.639  19.280 -49.338  1.00172.50           O  
ATOM    521  CB  ILE A  90      -8.755  16.999 -50.012  1.00175.69           C  
ATOM    522  CG1 ILE A  90      -7.446  17.703 -49.628  1.00176.07           C  
ATOM    523  CG2 ILE A  90      -8.505  15.615 -50.621  1.00174.71           C  
ATOM    524  CD1 ILE A  90      -6.348  16.762 -49.153  1.00175.60           C  
ATOM    525  N   MET A  91      -9.463  20.321 -50.950  1.00172.55           N  
ATOM    526  CA  MET A  91      -9.928  21.672 -50.629  1.00171.86           C  
ATOM    527  C   MET A  91     -11.333  21.892 -51.196  1.00171.61           C  
ATOM    528  O   MET A  91     -12.272  22.116 -50.438  1.00172.58           O  
ATOM    529  CB  MET A  91      -8.955  22.722 -51.185  1.00172.53           C  
ATOM    530  CG  MET A  91      -9.240  24.170 -50.809  1.00172.40           C  
ATOM    531  SD  MET A  91      -7.998  25.312 -51.481  1.00173.98           S  
ATOM    532  CE  MET A  91      -6.495  24.774 -50.661  1.00169.93           C  
ATOM    533  N   GLU A  92     -11.485  21.795 -52.517  1.00170.66           N  
ATOM    534  CA  GLU A  92     -12.762  22.131 -53.173  1.00167.89           C  
ATOM    535  C   GLU A  92     -13.943  21.194 -52.873  1.00169.78           C  
ATOM    536  O   GLU A  92     -15.093  21.614 -53.017  1.00168.12           O  
ATOM    537  CB  GLU A  92     -12.585  22.264 -54.693  1.00164.18           C  
ATOM    538  CG  GLU A  92     -11.625  23.369 -55.126  1.00161.50           C  
ATOM    539  CD  GLU A  92     -11.744  24.630 -54.287  1.00158.77           C  
ATOM    540  OE1 GLU A  92     -12.862  25.175 -54.181  1.00155.92           O  
ATOM    541  OE2 GLU A  92     -10.717  25.074 -53.731  1.00156.74           O  
ATOM    542  N   ILE A  93     -13.683  19.947 -52.469  1.00172.45           N  
ATOM    543  CA  ILE A  93     -14.774  19.051 -52.036  1.00171.12           C  
ATOM    544  C   ILE A  93     -15.272  19.370 -50.617  1.00170.26           C  
ATOM    545  O   ILE A  93     -16.381  18.976 -50.252  1.00171.88           O  
ATOM    546  CB  ILE A  93     -14.423  17.522 -52.153  1.00170.16           C  
ATOM    547  CG1 ILE A  93     -13.300  17.100 -51.198  1.00169.82           C  
ATOM    548  CG2 ILE A  93     -14.047  17.169 -53.581  1.00169.47           C  
ATOM    549  CD1 ILE A  93     -13.131  15.586 -51.085  1.00167.90           C  
ATOM    550  N   LEU A  94     -14.459  20.075 -49.825  1.00168.68           N  
ATOM    551  CA  LEU A  94     -14.826  20.423 -48.446  1.00165.95           C  
ATOM    552  C   LEU A  94     -14.455  21.868 -48.042  1.00166.14           C  
ATOM    553  O   LEU A  94     -14.520  22.213 -46.860  1.00165.11           O  
ATOM    554  CB  LEU A  94     -14.216  19.400 -47.468  1.00164.66           C  
ATOM    555  CG  LEU A  94     -14.692  17.940 -47.599  1.00163.83           C  
ATOM    556  CD1 LEU A  94     -13.702  16.954 -46.986  1.00161.04           C  
ATOM    557  CD2 LEU A  94     -16.074  17.759 -46.989  1.00165.94           C  
ATOM    558  N   ARG A  95     -14.081  22.704 -49.017  1.00168.67           N  
ATOM    559  CA  ARG A  95     -13.869  24.150 -48.794  1.00169.60           C  
ATOM    560  C   ARG A  95     -15.213  24.874 -48.887  1.00167.47           C  
ATOM    561  O   ARG A  95     -15.383  25.961 -48.332  1.00167.79           O  
ATOM    562  CB  ARG A  95     -12.858  24.731 -49.809  1.00172.20           C  
ATOM    563  CG  ARG A  95     -12.582  26.249 -49.733  1.00173.83           C  
ATOM    564  CD  ARG A  95     -11.859  26.672 -48.447  1.00175.39           C  
ATOM    565  NE  ARG A  95     -10.464  26.212 -48.378  1.00176.95           N  
ATOM    566  CZ  ARG A  95      -9.383  26.928 -48.708  1.00177.66           C  
ATOM    567  NH1 ARG A  95      -9.484  28.177 -49.159  1.00178.23           N  
ATOM    568  NH2 ARG A  95      -8.175  26.383 -48.587  1.00176.60           N  
ATOM    569  N   GLY A  96     -16.158  24.263 -49.601  1.00165.52           N  
ATOM    570  CA  GLY A  96     -17.538  24.743 -49.667  1.00165.29           C  
ATOM    571  C   GLY A  96     -18.555  23.866 -48.943  1.00165.21           C  
ATOM    572  O   GLY A  96     -19.609  24.359 -48.539  1.00162.03           O  
ATOM    573  N   ASP A  97     -18.256  22.572 -48.780  1.00164.51           N  
ATOM    574  CA  ASP A  97     -19.175  21.619 -48.117  1.00161.30           C  
ATOM    575  C   ASP A  97     -19.839  22.235 -46.897  1.00159.83           C  
ATOM    576  O   ASP A  97     -21.057  22.165 -46.741  1.00160.56           O  
ATOM    577  CB  ASP A  97     -18.436  20.346 -47.680  1.00159.48           C  
ATOM    578  CG  ASP A  97     -19.278  19.454 -46.766  1.00156.49           C  
ATOM    579  OD1 ASP A  97     -18.822  19.144 -45.642  1.00154.09           O  
ATOM    580  OD2 ASP A  97     -20.396  19.069 -47.169  1.00154.52           O  
ATOM    581  N   PHE A  98     -19.026  22.832 -46.032  1.00157.30           N  
ATOM    582  CA  PHE A  98     -19.528  23.467 -44.822  1.00155.80           C  
ATOM    583  C   PHE A  98     -20.199  24.820 -45.092  1.00155.37           C  
ATOM    584  O   PHE A  98     -20.727  25.443 -44.168  1.00156.26           O  
ATOM    585  CB  PHE A  98     -18.409  23.573 -43.788  1.00154.04           C  
ATOM    586  CG  PHE A  98     -18.005  22.243 -43.220  1.00154.19           C  
ATOM    587  CD1 PHE A  98     -18.729  21.669 -42.181  1.00154.77           C  
ATOM    588  CD2 PHE A  98     -16.924  21.547 -43.743  1.00152.58           C  
ATOM    589  CE1 PHE A  98     -18.372  20.434 -41.660  1.00154.39           C  
ATOM    590  CE2 PHE A  98     -16.560  20.313 -43.226  1.00152.86           C  
ATOM    591  CZ  PHE A  98     -17.285  19.755 -42.182  1.00154.00           C  
ATOM    592  N   SER A  99     -20.167  25.270 -46.350  1.00155.57           N  
ATOM    593  CA  SER A  99     -21.069  26.322 -46.833  1.00153.91           C  
ATOM    594  C   SER A  99     -22.306  25.721 -47.510  1.00155.18           C  
ATOM    595  O   SER A  99     -23.265  26.441 -47.794  1.00152.43           O  
ATOM    596  CB  SER A  99     -20.363  27.268 -47.808  1.00151.63           C  
ATOM    597  OG  SER A  99     -19.312  27.971 -47.171  1.00150.88           O  
ATOM    598  N   SER A 100     -22.268  24.415 -47.785  1.00158.62           N  
ATOM    599  CA  SER A 100     -23.427  23.682 -48.318  1.00159.10           C  
ATOM    600  C   SER A 100     -24.239  23.052 -47.185  1.00159.27           C  
ATOM    601  O   SER A 100     -25.403  22.695 -47.371  1.00159.31           O  
ATOM    602  CB  SER A 100     -22.985  22.592 -49.302  1.00159.77           C  
ATOM    603  OG  SER A 100     -22.644  21.388 -48.635  1.00160.81           O  
ATOM    604  N   ALA A 101     -23.606  22.904 -46.022  1.00159.74           N  
ATOM    605  CA  ALA A 101     -24.276  22.427 -44.812  1.00158.36           C  
ATOM    606  C   ALA A 101     -25.152  23.524 -44.216  1.00158.26           C  
ATOM    607  O   ALA A 101     -26.198  23.233 -43.641  1.00158.62           O  
ATOM    608  CB  ALA A 101     -23.256  21.957 -43.787  1.00157.89           C  
ATOM    609  N   ASN A 102     -24.713  24.778 -44.341  1.00158.22           N  
ATOM    610  CA  ASN A 102     -25.521  25.927 -43.916  1.00157.64           C  
ATOM    611  C   ASN A 102     -26.698  26.151 -44.875  1.00157.22           C  
ATOM    612  O   ASN A 102     -27.793  26.536 -44.453  1.00154.71           O  
ATOM    613  CB  ASN A 102     -24.651  27.193 -43.765  1.00157.84           C  
ATOM    614  CG  ASN A 102     -24.547  28.010 -45.047  1.00160.02           C  
ATOM    615  OD1 ASN A 102     -25.542  28.538 -45.543  1.00164.06           O  
ATOM    616  ND2 ASN A 102     -23.334  28.144 -45.567  1.00159.93           N  
ATOM    617  N   ASN A 103     -26.456  25.905 -46.163  1.00158.69           N  
ATOM    618  CA  ASN A 103     -27.508  25.935 -47.182  1.00159.89           C  
ATOM    619  C   ASN A 103     -28.506  24.793 -46.986  1.00160.12           C  
ATOM    620  O   ASN A 103     -29.681  24.925 -47.320  1.00159.44           O  
ATOM    621  CB  ASN A 103     -26.906  25.854 -48.593  1.00161.45           C  
ATOM    622  CG  ASN A 103     -26.121  27.104 -48.981  1.00162.80           C  
ATOM    623  OD1 ASN A 103     -25.561  27.177 -50.075  1.00163.60           O  
ATOM    624  ND2 ASN A 103     -26.075  28.088 -48.088  1.00164.36           N  
ATOM    625  N   ARG A 104     -28.020  23.674 -46.450  1.00160.83           N  
ATOM    626  CA  ARG A 104     -28.863  22.527 -46.089  1.00160.05           C  
ATOM    627  C   ARG A 104     -29.924  22.933 -45.065  1.00157.58           C  
ATOM    628  O   ARG A 104     -31.037  22.396 -45.054  1.00157.24           O  
ATOM    629  CB  ARG A 104     -27.995  21.400 -45.513  1.00160.93           C  
ATOM    630  CG  ARG A 104     -28.467  20.006 -45.853  1.00161.27           C  
ATOM    631  CD  ARG A 104     -27.373  18.974 -45.607  1.00162.29           C  
ATOM    632  NE  ARG A 104     -27.657  17.738 -46.330  1.00164.00           N  
ATOM    633  CZ  ARG A 104     -27.196  16.528 -46.010  1.00164.70           C  
ATOM    634  NH1 ARG A 104     -26.406  16.339 -44.956  1.00163.76           N  
ATOM    635  NH2 ARG A 104     -27.542  15.491 -46.764  1.00166.27           N  
ATOM    636  N   ASP A 105     -29.562  23.883 -44.208  1.00154.59           N  
ATOM    637  CA  ASP A 105     -30.465  24.390 -43.188  1.00151.31           C  
ATOM    638  C   ASP A 105     -31.456  25.418 -43.727  1.00153.00           C  
ATOM    639  O   ASP A 105     -32.484  25.650 -43.099  1.00151.70           O  
ATOM    640  CB  ASP A 105     -29.667  24.984 -42.029  1.00147.26           C  
ATOM    641  CG  ASP A 105     -28.848  23.939 -41.300  1.00144.21           C  
ATOM    642  OD1 ASP A 105     -28.169  23.131 -41.964  1.00138.26           O  
ATOM    643  OD2 ASP A 105     -28.890  23.918 -40.056  1.00144.62           O  
ATOM    644  N   ASN A 106     -31.160  26.022 -44.881  1.00157.10           N  
ATOM    645  CA  ASN A 106     -32.059  27.017 -45.495  1.00159.18           C  
ATOM    646  C   ASN A 106     -33.532  26.647 -45.352  1.00160.07           C  
ATOM    647  O   ASN A 106     -34.337  27.464 -44.903  1.00161.29           O  
ATOM    648  CB  ASN A 106     -31.739  27.223 -46.985  1.00159.67           C  
ATOM    649  CG  ASN A 106     -30.500  28.078 -47.215  1.00158.75           C  
ATOM    650  OD1 ASN A 106     -29.738  28.362 -46.288  1.00159.79           O  
ATOM    651  ND2 ASN A 106     -30.297  28.494 -48.461  1.00155.13           N  
ATOM    652  N   THR A 107     -33.874  25.417 -45.738  1.00160.87           N  
ATOM    653  CA  THR A 107     -35.235  24.895 -45.572  1.00161.56           C  
ATOM    654  C   THR A 107     -35.526  24.626 -44.097  1.00158.23           C  
ATOM    655  O   THR A 107     -36.650  24.814 -43.625  1.00156.46           O  
ATOM    656  CB  THR A 107     -35.448  23.580 -46.353  1.00163.24           C  
ATOM    657  OG1 THR A 107     -34.873  23.692 -47.661  1.00165.26           O  
ATOM    658  CG2 THR A 107     -36.942  23.259 -46.472  1.00162.64           C  
ATOM    659  N   TYR A 108     -34.500  24.185 -43.378  1.00151.77           N  
ATOM    660  CA  TYR A 108     -34.622  23.898 -41.960  1.00146.42           C  
ATOM    661  C   TYR A 108     -34.789  25.180 -41.142  1.00146.68           C  
ATOM    662  O   TYR A 108     -35.421  25.176 -40.089  1.00142.64           O  
ATOM    663  CB  TYR A 108     -33.388  23.147 -41.482  1.00143.11           C  
ATOM    664  CG  TYR A 108     -33.671  22.253 -40.322  1.00140.21           C  
ATOM    665  CD1 TYR A 108     -33.818  22.774 -39.044  1.00140.65           C  
ATOM    666  CD2 TYR A 108     -33.804  20.885 -40.497  1.00138.86           C  
ATOM    667  CE1 TYR A 108     -34.085  21.955 -37.968  1.00141.46           C  
ATOM    668  CE2 TYR A 108     -34.068  20.056 -39.429  1.00140.12           C  
ATOM    669  CZ  TYR A 108     -34.208  20.596 -38.165  1.00140.69           C  
ATOM    670  OH  TYR A 108     -34.472  19.780 -37.092  1.00141.91           O  
ATOM    671  N   ASN A 109     -34.215  26.271 -41.638  1.00149.57           N  
ATOM    672  CA  ASN A 109     -34.274  27.563 -40.954  1.00150.16           C  
ATOM    673  C   ASN A 109     -35.701  28.108 -40.871  1.00148.04           C  
ATOM    674  O   ASN A 109     -36.160  28.479 -39.793  1.00144.22           O  
ATOM    675  CB  ASN A 109     -33.366  28.589 -41.656  1.00151.68           C  
ATOM    676  CG  ASN A 109     -31.888  28.191 -41.640  1.00153.06           C  
ATOM    677  OD1 ASN A 109     -31.168  28.396 -42.619  1.00153.13           O  
ATOM    678  ND2 ASN A 109     -31.437  27.619 -40.530  1.00154.60           N  
ATOM    679  N   ARG A 110     -36.392  28.136 -42.011  1.00148.77           N  
ATOM    680  CA  ARG A 110     -37.723  28.747 -42.121  1.00149.52           C  
ATOM    681  C   ARG A 110     -38.820  27.685 -42.156  1.00145.62           C  
ATOM    682  O   ARG A 110     -39.712  27.672 -41.301  1.00138.47           O  
ATOM    683  CB  ARG A 110     -37.837  29.614 -43.390  1.00152.41           C  
ATOM    684  CG  ARG A 110     -36.575  30.385 -43.802  1.00153.75           C  
ATOM    685  CD  ARG A 110     -36.796  31.169 -45.103  1.00154.76           C  
ATOM    686  NE  ARG A 110     -37.329  30.333 -46.185  1.00155.97           N  
ATOM    687  CZ  ARG A 110     -36.613  29.501 -46.944  1.00156.47           C  
ATOM    688  NH1 ARG A 110     -35.301  29.363 -46.765  1.00157.77           N  
ATOM    689  NH2 ARG A 110     -37.216  28.793 -47.895  1.00155.47           N  
ATOM    690  N   VAL A 111     -38.742  26.795 -43.147  1.00145.65           N  
ATOM    691  CA  VAL A 111     -39.791  25.798 -43.389  1.00143.28           C  
ATOM    692  C   VAL A 111     -40.023  24.950 -42.143  1.00141.42           C  
ATOM    693  O   VAL A 111     -41.092  24.381 -41.977  1.00139.77           O  
ATOM    694  CB  VAL A 111     -39.482  24.888 -44.619  1.00143.26           C  
ATOM    695  CG1 VAL A 111     -40.593  23.865 -44.838  1.00143.06           C  
ATOM    696  CG2 VAL A 111     -39.297  25.728 -45.877  1.00141.31           C  
ATOM    697  N   SER A 112     -39.025  24.869 -41.270  1.00138.76           N  
ATOM    698  CA  SER A 112     -39.223  24.278 -39.957  1.00136.47           C  
ATOM    699  C   SER A 112     -39.740  25.322 -38.955  1.00134.76           C  
ATOM    700  O   SER A 112     -40.738  25.077 -38.287  1.00136.29           O  
ATOM    701  CB  SER A 112     -37.932  23.629 -39.465  1.00135.55           C  
ATOM    702  OG  SER A 112     -36.896  24.585 -39.371  1.00138.12           O  
ATOM    703  N   GLU A 113     -39.094  26.486 -38.868  1.00132.65           N  
ATOM    704  CA  GLU A 113     -39.431  27.466 -37.818  1.00129.63           C  
ATOM    705  C   GLU A 113     -40.856  27.985 -37.914  1.00131.31           C  
ATOM    706  O   GLU A 113     -41.627  27.859 -36.962  1.00131.75           O  
ATOM    707  CB  GLU A 113     -38.452  28.645 -37.803  1.00129.66           C  
ATOM    708  CG  GLU A 113     -38.466  29.483 -36.507  1.00130.42           C  
ATOM    709  CD  GLU A 113     -39.718  30.335 -36.314  1.00131.68           C  
ATOM    710  OE1 GLU A 113     -40.324  30.771 -37.316  1.00132.48           O  
ATOM    711  OE2 GLU A 113     -40.092  30.579 -35.145  1.00130.98           O  
ATOM    712  N   ASP A 114     -41.204  28.593 -39.042  1.00133.80           N  
ATOM    713  CA  ASP A 114     -42.552  29.133 -39.211  1.00135.55           C  
ATOM    714  C   ASP A 114     -43.596  28.059 -38.930  1.00134.99           C  
ATOM    715  O   ASP A 114     -44.606  28.325 -38.275  1.00129.26           O  
ATOM    716  CB  ASP A 114     -42.736  29.721 -40.610  1.00139.65           C  
ATOM    717  CG  ASP A 114     -42.041  31.061 -40.770  1.00144.93           C  
ATOM    718  OD1 ASP A 114     -42.305  31.966 -39.947  1.00147.69           O  
ATOM    719  OD2 ASP A 114     -41.235  31.211 -41.715  1.00148.73           O  
ATOM    720  N   LEU A 115     -43.331  26.839 -39.397  1.00135.08           N  
ATOM    721  CA  LEU A 115     -44.208  25.704 -39.111  1.00134.37           C  
ATOM    722  C   LEU A 115     -44.360  25.453 -37.615  1.00132.18           C  
ATOM    723  O   LEU A 115     -45.475  25.254 -37.136  1.00128.51           O  
ATOM    724  CB  LEU A 115     -43.705  24.428 -39.793  1.00135.49           C  
ATOM    725  CG  LEU A 115     -43.881  24.362 -41.307  1.00137.56           C  
ATOM    726  CD1 LEU A 115     -43.310  23.043 -41.798  1.00137.66           C  
ATOM    727  CD2 LEU A 115     -45.343  24.492 -41.681  1.00137.65           C  
ATOM    728  N   ARG A 116     -43.251  25.463 -36.879  1.00132.37           N  
ATOM    729  CA  ARG A 116     -43.299  25.209 -35.435  1.00133.16           C  
ATOM    730  C   ARG A 116     -44.240  26.189 -34.739  1.00126.84           C  
ATOM    731  O   ARG A 116     -44.915  25.827 -33.775  1.00125.70           O  
ATOM    732  CB  ARG A 116     -41.902  25.272 -34.802  1.00139.36           C  
ATOM    733  CG  ARG A 116     -41.011  24.078 -35.134  1.00145.86           C  
ATOM    734  CD  ARG A 116     -39.759  24.030 -34.259  1.00149.74           C  
ATOM    735  NE  ARG A 116     -38.926  25.229 -34.384  1.00153.54           N  
ATOM    736  CZ  ARG A 116     -38.087  25.484 -35.390  1.00157.24           C  
ATOM    737  NH1 ARG A 116     -37.956  24.636 -36.405  1.00158.22           N  
ATOM    738  NH2 ARG A 116     -37.379  26.610 -35.390  1.00158.89           N  
ATOM    739  N   SER A 117     -44.296  27.420 -35.238  1.00120.93           N  
ATOM    740  CA  SER A 117     -45.230  28.407 -34.710  1.00116.63           C  
ATOM    741  C   SER A 117     -46.664  28.097 -35.146  1.00117.78           C  
ATOM    742  O   SER A 117     -47.603  28.352 -34.396  1.00115.79           O  
ATOM    743  CB  SER A 117     -44.839  29.819 -35.145  1.00116.63           C  
ATOM    744  OG  SER A 117     -45.026  30.003 -36.536  1.00120.11           O  
ATOM    745  N   ARG A 118     -46.830  27.547 -36.349  1.00120.80           N  
ATOM    746  CA  ARG A 118     -48.159  27.172 -36.852  1.00118.93           C  
ATOM    747  C   ARG A 118     -48.736  25.957 -36.126  1.00117.78           C  
ATOM    748  O   ARG A 118     -49.924  25.933 -35.810  1.00114.42           O  
ATOM    749  CB  ARG A 118     -48.115  26.891 -38.351  1.00121.93           C  
ATOM    750  CG  ARG A 118     -47.878  28.122 -39.198  1.00126.26           C  
ATOM    751  CD  ARG A 118     -47.485  27.746 -40.618  1.00131.09           C  
ATOM    752  NE  ARG A 118     -46.969  28.889 -41.370  1.00135.03           N  
ATOM    753  CZ  ARG A 118     -46.372  28.814 -42.560  1.00137.18           C  
ATOM    754  NH1 ARG A 118     -46.197  27.641 -43.169  1.00137.58           N  
ATOM    755  NH2 ARG A 118     -45.942  29.926 -43.148  1.00137.24           N  
ATOM    756  N   ILE A 119     -47.895  24.953 -35.876  1.00118.38           N  
ATOM    757  CA  ILE A 119     -48.285  23.773 -35.090  1.00114.73           C  
ATOM    758  C   ILE A 119     -48.704  24.181 -33.687  1.00114.49           C  
ATOM    759  O   ILE A 119     -49.633  23.613 -33.119  1.00114.06           O  
ATOM    760  CB  ILE A 119     -47.124  22.764 -34.933  1.00116.01           C  
ATOM    761  CG1 ILE A 119     -46.767  22.124 -36.274  1.00118.80           C  
ATOM    762  CG2 ILE A 119     -47.488  21.670 -33.923  1.00111.32           C  
ATOM    763  CD1 ILE A 119     -47.749  21.068 -36.722  1.00120.47           C  
ATOM    764  N   GLU A 120     -47.996  25.153 -33.121  1.00115.67           N  
ATOM    765  CA  GLU A 120     -48.311  25.639 -31.787  1.00113.83           C  
ATOM    766  C   GLU A 120     -49.604  26.461 -31.793  1.00111.20           C  
ATOM    767  O   GLU A 120     -50.526  26.146 -31.044  1.00110.91           O  
ATOM    768  CB  GLU A 120     -47.145  26.450 -31.229  1.00116.91           C  
ATOM    769  CG  GLU A 120     -47.353  26.948 -29.806  1.00121.52           C  
ATOM    770  CD  GLU A 120     -48.282  28.153 -29.719  1.00129.13           C  
ATOM    771  OE1 GLU A 120     -48.327  28.970 -30.669  1.00132.45           O  
ATOM    772  OE2 GLU A 120     -48.974  28.285 -28.687  1.00135.52           O  
ATOM    773  N   VAL A 121     -49.673  27.501 -32.632  1.00106.50           N  
ATOM    774  CA  VAL A 121     -50.883  28.345 -32.744  1.00101.17           C  
ATOM    775  C   VAL A 121     -52.126  27.526 -33.107  1.00103.52           C  
ATOM    776  O   VAL A 121     -53.257  27.988 -32.943  1.00106.05           O  
ATOM    777  CB  VAL A 121     -50.695  29.503 -33.760  1.00 99.71           C  
ATOM    778  CG1 VAL A 121     -52.032  29.991 -34.308  1.00 96.47           C  
ATOM    779  CG2 VAL A 121     -49.945  30.657 -33.110  1.00100.99           C  
ATOM    780  N   LEU A 122     -51.897  26.318 -33.616  1.00105.52           N  
ATOM    781  CA  LEU A 122     -52.928  25.281 -33.729  1.00100.37           C  
ATOM    782  C   LEU A 122     -53.546  24.903 -32.372  1.00104.86           C  
ATOM    783  O   LEU A 122     -54.760  24.719 -32.274  1.00108.38           O  
ATOM    784  CB  LEU A 122     -52.317  24.044 -34.400  1.00 91.52           C  
ATOM    785  CG  LEU A 122     -53.050  22.710 -34.447  1.00 81.93           C  
ATOM    786  CD1 LEU A 122     -53.080  22.056 -33.066  1.00 73.50           C  
ATOM    787  CD2 LEU A 122     -54.435  22.921 -35.032  1.00 82.02           C  
ATOM    788  N   LYS A 123     -52.720  24.779 -31.334  1.00106.44           N  
ATOM    789  CA  LYS A 123     -53.215  24.403 -30.004  1.00103.61           C  
ATOM    790  C   LYS A 123     -54.021  25.498 -29.308  1.00102.42           C  
ATOM    791  O   LYS A 123     -55.018  25.197 -28.657  1.00101.43           O  
ATOM    792  CB  LYS A 123     -52.073  23.987 -29.086  1.00105.36           C  
ATOM    793  CG  LYS A 123     -51.398  22.690 -29.454  1.00105.57           C  
ATOM    794  CD  LYS A 123     -50.464  22.292 -28.323  1.00109.00           C  
ATOM    795  CE  LYS A 123     -49.232  21.569 -28.808  1.00114.51           C  
ATOM    796  NZ  LYS A 123     -48.148  21.612 -27.773  1.00117.98           N  
ATOM    797  N   ARG A 124     -53.583  26.754 -29.431  1.00105.45           N  
ATOM    798  CA  ARG A 124     -54.309  27.897 -28.852  1.00108.59           C  
ATOM    799  C   ARG A 124     -55.784  27.854 -29.223  1.00105.76           C  
ATOM    800  O   ARG A 124     -56.633  28.292 -28.449  1.00105.29           O  
ATOM    801  CB  ARG A 124     -53.708  29.235 -29.300  1.00114.10           C  
ATOM    802  CG  ARG A 124     -52.370  29.568 -28.651  1.00120.97           C  
ATOM    803  CD  ARG A 124     -51.948  31.014 -28.921  1.00126.40           C  
ATOM    804  NE  ARG A 124     -50.517  31.239 -28.682  1.00130.84           N  
ATOM    805  CZ  ARG A 124     -49.899  32.417 -28.799  1.00130.83           C  
ATOM    806  NH1 ARG A 124     -50.571  33.509 -29.155  1.00132.70           N  
ATOM    807  NH2 ARG A 124     -48.595  32.506 -28.555  1.00129.27           N  
ATOM    808  N   LYS A 125     -56.073  27.334 -30.414  1.00103.88           N  
ATOM    809  CA  LYS A 125     -57.439  27.006 -30.808  1.00104.94           C  
ATOM    810  C   LYS A 125     -57.883  25.635 -30.270  1.00103.11           C  
ATOM    811  O   LYS A 125     -58.927  25.539 -29.624  1.00103.12           O  
ATOM    812  CB  LYS A 125     -57.589  27.030 -32.330  1.00106.92           C  
ATOM    813  CG  LYS A 125     -57.424  28.399 -32.978  1.00108.83           C  
ATOM    814  CD  LYS A 125     -57.991  28.382 -34.399  1.00111.18           C  
ATOM    815  CE  LYS A 125     -57.328  29.405 -35.307  1.00113.03           C  
ATOM    816  NZ  LYS A 125     -57.725  29.199 -36.730  1.00114.31           N  
ATOM    817  N   VAL A 126     -57.101  24.580 -30.519  1.00 99.05           N  
ATOM    818  CA  VAL A 126     -57.538  23.213 -30.175  1.00 96.09           C  
ATOM    819  C   VAL A 126     -57.750  22.980 -28.677  1.00 98.44           C  
ATOM    820  O   VAL A 126     -58.343  21.973 -28.290  1.00 98.71           O  
ATOM    821  CB  VAL A 126     -56.569  22.122 -30.685  1.00 95.60           C  
ATOM    822  CG1 VAL A 126     -55.459  21.883 -29.684  1.00100.81           C  
ATOM    823  CG2 VAL A 126     -57.316  20.815 -30.929  1.00 91.43           C  
ATOM    824  N   ILE A 127     -57.252  23.883 -27.836  1.00 99.03           N  
ATOM    825  CA  ILE A 127     -57.560  23.822 -26.413  1.00 99.73           C  
ATOM    826  C   ILE A 127     -58.933  24.433 -26.118  1.00100.58           C  
ATOM    827  O   ILE A 127     -59.651  23.951 -25.244  1.00100.53           O  
ATOM    828  CB  ILE A 127     -56.482  24.501 -25.552  1.00 99.10           C  
ATOM    829  CG1 ILE A 127     -56.647  24.090 -24.083  1.00101.99           C  
ATOM    830  CG2 ILE A 127     -56.543  26.022 -25.705  1.00 98.34           C  
ATOM    831  CD1 ILE A 127     -56.794  22.578 -23.855  1.00 99.54           C  
ATOM    832  N   GLU A 128     -59.298  25.489 -26.842  1.00102.11           N  
ATOM    833  CA  GLU A 128     -60.642  26.042 -26.727  1.00104.57           C  
ATOM    834  C   GLU A 128     -61.611  24.899 -26.971  1.00100.65           C  
ATOM    835  O   GLU A 128     -62.493  24.617 -26.152  1.00 98.15           O  
ATOM    836  CB  GLU A 128     -60.903  27.150 -27.767  1.00106.74           C  
ATOM    837  CG  GLU A 128     -59.942  28.326 -27.733  1.00106.96           C  
ATOM    838  CD  GLU A 128     -59.848  28.950 -26.367  1.00109.30           C  
ATOM    839  OE1 GLU A 128     -60.900  29.079 -25.702  1.00114.25           O  
ATOM    840  OE2 GLU A 128     -58.722  29.304 -25.959  1.00108.68           O  
ATOM    841  N   LYS A 129     -61.395  24.219 -28.093  1.00 96.26           N  
ATOM    842  CA  LYS A 129     -62.356  23.245 -28.603  1.00 93.92           C  
ATOM    843  C   LYS A 129     -62.467  22.022 -27.700  1.00 90.85           C  
ATOM    844  O   LYS A 129     -63.548  21.477 -27.528  1.00 92.61           O  
ATOM    845  CB  LYS A 129     -62.034  22.851 -30.055  1.00 90.49           C  
ATOM    846  CG  LYS A 129     -62.686  23.779 -31.095  1.00 89.23           C  
ATOM    847  CD  LYS A 129     -61.978  25.135 -31.212  1.00 88.68           C  
ATOM    848  CE  LYS A 129     -62.941  26.312 -31.117  1.00 88.19           C  
ATOM    849  NZ  LYS A 129     -63.397  26.567 -29.721  1.00 87.48           N  
ATOM    850  N   VAL A 130     -61.359  21.605 -27.107  1.00 89.48           N  
ATOM    851  CA  VAL A 130     -61.413  20.565 -26.093  1.00 85.37           C  
ATOM    852  C   VAL A 130     -62.042  21.119 -24.823  1.00 84.62           C  
ATOM    853  O   VAL A 130     -62.941  20.506 -24.245  1.00 76.68           O  
ATOM    854  CB  VAL A 130     -60.022  20.045 -25.752  1.00 86.28           C  
ATOM    855  CG1 VAL A 130     -60.096  19.068 -24.593  1.00 89.61           C  
ATOM    856  CG2 VAL A 130     -59.404  19.389 -26.967  1.00 90.08           C  
ATOM    857  N   GLN A 131     -61.567  22.283 -24.389  1.00 90.95           N  
ATOM    858  CA  GLN A 131     -62.062  22.869 -23.155  1.00 93.00           C  
ATOM    859  C   GLN A 131     -63.578  22.805 -23.174  1.00 89.26           C  
ATOM    860  O   GLN A 131     -64.187  22.053 -22.407  1.00 77.61           O  
ATOM    861  CB  GLN A 131     -61.568  24.315 -22.960  1.00 97.55           C  
ATOM    862  CG  GLN A 131     -61.937  24.909 -21.603  1.00104.00           C  
ATOM    863  CD  GLN A 131     -61.556  23.989 -20.446  1.00109.37           C  
ATOM    864  OE1 GLN A 131     -62.414  23.540 -19.677  1.00109.02           O  
ATOM    865  NE2 GLN A 131     -60.266  23.681 -20.339  1.00112.87           N  
ATOM    866  N   HIS A 132     -64.178  23.542 -24.103  1.00 88.27           N  
ATOM    867  CA  HIS A 132     -65.628  23.635 -24.182  1.00 85.03           C  
ATOM    868  C   HIS A 132     -66.299  22.264 -24.102  1.00 80.00           C  
ATOM    869  O   HIS A 132     -67.342  22.120 -23.462  1.00 75.85           O  
ATOM    870  CB  HIS A 132     -66.051  24.380 -25.447  1.00 87.70           C  
ATOM    871  CG  HIS A 132     -65.665  25.826 -25.439  1.00 96.67           C  
ATOM    872  ND1 HIS A 132     -65.253  26.497 -26.571  1.00100.58           N  
ATOM    873  CD2 HIS A 132     -65.600  26.723 -24.426  1.00102.36           C  
ATOM    874  CE1 HIS A 132     -64.968  27.750 -26.259  1.00102.02           C  
ATOM    875  NE2 HIS A 132     -65.169  27.913 -24.963  1.00103.69           N  
ATOM    876  N   ILE A 133     -65.689  21.253 -24.711  1.00 69.26           N  
ATOM    877  CA  ILE A 133     -66.288  19.920 -24.729  1.00 67.06           C  
ATOM    878  C   ILE A 133     -66.272  19.260 -23.355  1.00 71.09           C  
ATOM    879  O   ILE A 133     -67.127  18.434 -23.042  1.00 67.52           O  
ATOM    880  CB  ILE A 133     -65.608  19.012 -25.763  1.00 68.00           C  
ATOM    881  CG1 ILE A 133     -66.190  19.283 -27.148  1.00 72.17           C  
ATOM    882  CG2 ILE A 133     -65.817  17.548 -25.429  1.00 64.36           C  
ATOM    883  CD1 ILE A 133     -66.313  20.761 -27.500  1.00 76.09           C  
ATOM    884  N   GLN A 134     -65.311  19.629 -22.525  1.00 74.59           N  
ATOM    885  CA  GLN A 134     -65.271  19.079 -21.182  1.00 74.37           C  
ATOM    886  C   GLN A 134     -66.363  19.716 -20.342  1.00 64.05           C  
ATOM    887  O   GLN A 134     -66.915  19.085 -19.445  1.00 58.11           O  
ATOM    888  CB  GLN A 134     -63.890  19.270 -20.570  1.00 78.13           C  
ATOM    889  CG  GLN A 134     -62.832  18.473 -21.300  1.00 80.06           C  
ATOM    890  CD  GLN A 134     -61.439  18.816 -20.849  1.00 85.98           C  
ATOM    891  OE1 GLN A 134     -61.039  19.982 -20.863  1.00 87.97           O  
ATOM    892  NE2 GLN A 134     -60.683  17.801 -20.446  1.00 95.32           N  
ATOM    893  N   LEU A 135     -66.680  20.964 -20.661  1.00 58.84           N  
ATOM    894  CA  LEU A 135     -67.722  21.673 -19.957  1.00 55.20           C  
ATOM    895  C   LEU A 135     -69.041  21.084 -20.387  1.00 56.13           C  
ATOM    896  O   LEU A 135     -69.918  20.822 -19.556  1.00 52.61           O  
ATOM    897  CB  LEU A 135     -67.668  23.175 -20.258  1.00 61.17           C  
ATOM    898  CG  LEU A 135     -68.936  24.005 -20.018  1.00 62.78           C  
ATOM    899  CD1 LEU A 135     -68.598  25.428 -19.605  1.00 65.67           C  
ATOM    900  CD2 LEU A 135     -69.818  24.013 -21.260  1.00 68.47           C  
ATOM    901  N   LEU A 136     -69.179  20.863 -21.690  1.00 58.26           N  
ATOM    902  CA  LEU A 136     -70.442  20.360 -22.220  1.00 62.76           C  
ATOM    903  C   LEU A 136     -70.688  18.928 -21.769  1.00 62.12           C  
ATOM    904  O   LEU A 136     -71.829  18.554 -21.505  1.00 65.46           O  
ATOM    905  CB  LEU A 136     -70.526  20.493 -23.746  1.00 65.74           C  
ATOM    906  CG  LEU A 136     -70.979  21.867 -24.280  1.00 69.16           C  
ATOM    907  CD1 LEU A 136     -72.171  22.414 -23.486  1.00 68.30           C  
ATOM    908  CD2 LEU A 136     -69.841  22.897 -24.299  1.00 64.94           C  
ATOM    909  N   GLN A 137     -69.616  18.145 -21.659  1.00 61.82           N  
ATOM    910  CA  GLN A 137     -69.674  16.820 -21.039  1.00 58.81           C  
ATOM    911  C   GLN A 137     -70.316  16.888 -19.650  1.00 59.38           C  
ATOM    912  O   GLN A 137     -71.247  16.131 -19.347  1.00 60.60           O  
ATOM    913  CB  GLN A 137     -68.270  16.222 -20.942  1.00 61.61           C  
ATOM    914  CG  GLN A 137     -67.790  15.555 -22.231  1.00 65.45           C  
ATOM    915  CD  GLN A 137     -66.279  15.337 -22.273  1.00 63.98           C  
ATOM    916  OE1 GLN A 137     -65.501  16.229 -21.933  1.00 53.15           O  
ATOM    917  NE2 GLN A 137     -65.862  14.143 -22.701  1.00 62.76           N  
ATOM    918  N   LYS A 138     -69.836  17.804 -18.813  1.00 55.65           N  
ATOM    919  CA  LYS A 138     -70.392  17.954 -17.473  1.00 61.87           C  
ATOM    920  C   LYS A 138     -71.820  18.528 -17.540  1.00 53.94           C  
ATOM    921  O   LYS A 138     -72.749  17.936 -16.996  1.00 41.81           O  
ATOM    922  CB  LYS A 138     -69.459  18.792 -16.576  1.00 73.16           C  
ATOM    923  CG  LYS A 138     -70.025  19.150 -15.175  1.00 86.35           C  
ATOM    924  CD  LYS A 138     -70.455  17.914 -14.337  1.00 89.69           C  
ATOM    925  CE  LYS A 138     -69.595  17.698 -13.086  1.00 89.59           C  
ATOM    926  NZ  LYS A 138     -68.144  17.574 -13.395  1.00 89.79           N  
ATOM    927  N   ASN A 139     -71.990  19.664 -18.210  1.00 47.05           N  
ATOM    928  CA  ASN A 139     -73.319  20.194 -18.488  1.00 49.73           C  
ATOM    929  C   ASN A 139     -74.354  19.112 -18.779  1.00 52.32           C  
ATOM    930  O   ASN A 139     -75.434  19.084 -18.173  1.00 48.96           O  
ATOM    931  CB  ASN A 139     -73.266  21.133 -19.691  1.00 56.28           C  
ATOM    932  CG  ASN A 139     -73.148  22.587 -19.296  1.00 63.51           C  
ATOM    933  OD1 ASN A 139     -73.436  22.961 -18.160  1.00 66.32           O  
ATOM    934  ND2 ASN A 139     -72.736  23.424 -20.243  1.00 69.46           N  
ATOM    935  N   VAL A 140     -74.015  18.221 -19.708  1.00 56.29           N  
ATOM    936  CA  VAL A 140     -74.956  17.192 -20.154  1.00 57.38           C  
ATOM    937  C   VAL A 140     -75.105  16.051 -19.158  1.00 59.81           C  
ATOM    938  O   VAL A 140     -76.207  15.555 -18.955  1.00 64.10           O  
ATOM    939  CB  VAL A 140     -74.580  16.583 -21.513  1.00 57.04           C  
ATOM    940  CG1 VAL A 140     -74.449  17.674 -22.566  1.00 55.58           C  
ATOM    941  CG2 VAL A 140     -73.312  15.752 -21.398  1.00 59.86           C  
ATOM    942  N   ARG A 141     -74.014  15.620 -18.537  1.00 54.97           N  
ATOM    943  CA  ARG A 141     -74.132  14.647 -17.456  1.00 52.77           C  
ATOM    944  C   ARG A 141     -75.281  15.072 -16.526  1.00 44.59           C  
ATOM    945  O   ARG A 141     -76.190  14.289 -16.253  1.00 37.57           O  
ATOM    946  CB  ARG A 141     -72.825  14.582 -16.685  1.00 57.34           C  
ATOM    947  CG  ARG A 141     -72.689  13.397 -15.749  1.00 61.03           C  
ATOM    948  CD  ARG A 141     -71.698  13.725 -14.635  1.00 66.65           C  
ATOM    949  NE  ARG A 141     -70.480  14.380 -15.140  1.00 72.09           N  
ATOM    950  CZ  ARG A 141     -69.252  13.854 -15.153  1.00 71.34           C  
ATOM    951  NH1 ARG A 141     -69.018  12.632 -14.668  1.00 68.51           N  
ATOM    952  NH2 ARG A 141     -68.237  14.569 -15.652  1.00 67.39           N  
ATOM    953  N   ALA A 142     -75.221  16.325 -16.067  1.00 44.38           N  
ATOM    954  CA  ALA A 142     -76.332  17.006 -15.387  1.00 45.35           C  
ATOM    955  C   ALA A 142     -77.670  16.723 -16.074  1.00 45.42           C  
ATOM    956  O   ALA A 142     -78.550  16.037 -15.517  1.00 28.46           O  
ATOM    957  CB  ALA A 142     -76.078  18.536 -15.356  1.00 33.28           C  
ATOM    958  N   GLN A 143     -77.799  17.244 -17.296  1.00 42.95           N  
ATOM    959  CA  GLN A 143     -79.032  17.122 -18.066  1.00 41.28           C  
ATOM    960  C   GLN A 143     -79.563  15.696 -18.144  1.00 41.22           C  
ATOM    961  O   GLN A 143     -80.770  15.490 -18.234  1.00 49.73           O  
ATOM    962  CB  GLN A 143     -78.848  17.660 -19.483  1.00 40.94           C  
ATOM    963  CG  GLN A 143     -80.066  17.420 -20.386  1.00 39.67           C  
ATOM    964  CD  GLN A 143     -80.127  18.328 -21.606  1.00 40.88           C  
ATOM    965  OE1 GLN A 143     -80.405  17.872 -22.724  1.00 34.70           O  
ATOM    966  NE2 GLN A 143     -79.884  19.622 -21.395  1.00 46.70           N  
ATOM    967  N   LEU A 144     -78.681  14.711 -18.111  1.00 39.03           N  
ATOM    968  CA  LEU A 144     -79.130  13.349 -18.251  1.00 34.58           C  
ATOM    969  C   LEU A 144     -79.773  12.899 -16.946  1.00 35.58           C  
ATOM    970  O   LEU A 144     -80.974  12.620 -16.918  1.00 39.97           O  
ATOM    971  CB  LEU A 144     -77.980  12.444 -18.691  1.00 39.23           C  
ATOM    972  CG  LEU A 144     -78.338  11.067 -19.270  1.00 42.40           C  
ATOM    973  CD1 LEU A 144     -79.611  11.085 -20.101  1.00 40.45           C  
ATOM    974  CD2 LEU A 144     -77.169  10.526 -20.096  1.00 38.36           C  
ATOM    975  N   VAL A 145     -79.011  12.868 -15.856  1.00 35.56           N  
ATOM    976  CA  VAL A 145     -79.584  12.484 -14.551  1.00 40.57           C  
ATOM    977  C   VAL A 145     -80.941  13.189 -14.318  1.00 33.40           C  
ATOM    978  O   VAL A 145     -81.936  12.564 -13.954  1.00 21.93           O  
ATOM    979  CB  VAL A 145     -78.614  12.788 -13.379  1.00 42.41           C  
ATOM    980  CG1 VAL A 145     -77.997  14.177 -13.518  1.00 46.49           C  
ATOM    981  CG2 VAL A 145     -79.339  12.685 -12.067  1.00 48.50           C  
ATOM    982  N   ASP A 146     -80.962  14.487 -14.582  1.00 27.59           N  
ATOM    983  CA  ASP A 146     -82.152  15.296 -14.447  1.00 23.42           C  
ATOM    984  C   ASP A 146     -83.402  14.648 -15.060  1.00 25.72           C  
ATOM    985  O   ASP A 146     -84.474  14.601 -14.432  1.00 22.80           O  
ATOM    986  CB  ASP A 146     -81.900  16.652 -15.107  1.00 23.82           C  
ATOM    987  CG  ASP A 146     -82.784  17.744 -14.560  1.00 27.93           C  
ATOM    988  OD1 ASP A 146     -83.554  17.485 -13.610  1.00 44.97           O  
ATOM    989  OD2 ASP A 146     -82.707  18.872 -15.078  1.00 25.58           O  
ATOM    990  N   MET A 147     -83.273  14.168 -16.291  1.00 28.66           N  
ATOM    991  CA  MET A 147     -84.410  13.562 -16.984  1.00 34.25           C  
ATOM    992  C   MET A 147     -84.731  12.232 -16.348  1.00 35.96           C  
ATOM    993  O   MET A 147     -85.875  11.965 -15.993  1.00 35.78           O  
ATOM    994  CB  MET A 147     -84.103  13.327 -18.457  1.00 35.91           C  
ATOM    995  CG  MET A 147     -83.916  14.576 -19.252  1.00 33.96           C  
ATOM    996  SD  MET A 147     -85.457  15.437 -19.443  1.00 36.47           S  
ATOM    997  CE  MET A 147     -85.995  15.022 -21.103  1.00 38.97           C  
ATOM    998  N   LYS A 148     -83.710  11.394 -16.211  1.00 31.45           N  
ATOM    999  CA  LYS A 148     -83.857  10.166 -15.469  1.00 25.22           C  
ATOM   1000  C   LYS A 148     -84.738  10.504 -14.267  1.00 18.20           C  
ATOM   1001  O   LYS A 148     -85.818   9.942 -14.103  1.00 20.24           O  
ATOM   1002  CB  LYS A 148     -82.484   9.633 -15.061  1.00 27.59           C  
ATOM   1003  CG  LYS A 148     -82.463   8.171 -14.712  1.00 30.46           C  
ATOM   1004  CD  LYS A 148     -81.030   7.688 -14.691  1.00 40.21           C  
ATOM   1005  CE  LYS A 148     -80.908   6.186 -14.430  1.00 47.06           C  
ATOM   1006  NZ  LYS A 148     -80.255   5.858 -13.127  1.00 52.11           N  
ATOM   1007  N   ARG A 149     -84.304  11.479 -13.476  1.00 18.22           N  
ATOM   1008  CA  ARG A 149     -85.104  11.998 -12.368  1.00 20.72           C  
ATOM   1009  C   ARG A 149     -86.516  12.395 -12.779  1.00 21.76           C  
ATOM   1010  O   ARG A 149     -87.495  11.774 -12.372  1.00 19.81           O  
ATOM   1011  CB  ARG A 149     -84.400  13.205 -11.722  1.00 26.43           C  
ATOM   1012  CG  ARG A 149     -83.762  12.862 -10.410  1.00 29.28           C  
ATOM   1013  CD  ARG A 149     -82.373  13.407 -10.212  1.00 31.12           C  
ATOM   1014  NE  ARG A 149     -81.745  12.657  -9.125  1.00 39.44           N  
ATOM   1015  CZ  ARG A 149     -80.627  12.999  -8.496  1.00 40.65           C  
ATOM   1016  NH1 ARG A 149     -79.973  14.106  -8.836  1.00 46.06           N  
ATOM   1017  NH2 ARG A 149     -80.161  12.222  -7.521  1.00 37.71           N  
ATOM   1018  N   LEU A 150     -86.606  13.446 -13.582  1.00 24.49           N  
ATOM   1019  CA  LEU A 150     -87.887  14.006 -13.999  1.00 22.43           C  
ATOM   1020  C   LEU A 150     -88.812  12.976 -14.615  1.00 20.22           C  
ATOM   1021  O   LEU A 150     -90.033  13.023 -14.431  1.00 16.48           O  
ATOM   1022  CB  LEU A 150     -87.629  15.091 -15.030  1.00 23.38           C  
ATOM   1023  CG  LEU A 150     -88.860  15.809 -15.535  1.00 17.37           C  
ATOM   1024  CD1 LEU A 150     -89.661  16.236 -14.337  1.00 26.24           C  
ATOM   1025  CD2 LEU A 150     -88.456  17.002 -16.359  1.00 15.11           C  
ATOM   1026  N   GLU A 151     -88.200  12.073 -15.375  1.00 26.29           N  
ATOM   1027  CA  GLU A 151     -88.890  10.989 -16.050  1.00 30.10           C  
ATOM   1028  C   GLU A 151     -89.500  10.061 -15.024  1.00 30.72           C  
ATOM   1029  O   GLU A 151     -90.660   9.693 -15.137  1.00 33.49           O  
ATOM   1030  CB  GLU A 151     -87.924  10.212 -16.957  1.00 38.22           C  
ATOM   1031  CG  GLU A 151     -88.523   9.001 -17.693  1.00 47.52           C  
ATOM   1032  CD  GLU A 151     -89.367   9.372 -18.914  1.00 60.20           C  
ATOM   1033  OE1 GLU A 151     -90.607   9.152 -18.869  1.00 61.04           O  
ATOM   1034  OE2 GLU A 151     -88.786   9.870 -19.917  1.00 57.51           O  
ATOM   1035  N   VAL A 152     -88.730   9.669 -14.018  1.00 30.74           N  
ATOM   1036  CA  VAL A 152     -89.316   8.857 -12.958  1.00 32.61           C  
ATOM   1037  C   VAL A 152     -90.295   9.706 -12.199  1.00 25.12           C  
ATOM   1038  O   VAL A 152     -91.353   9.233 -11.801  1.00 32.94           O  
ATOM   1039  CB  VAL A 152     -88.296   8.315 -11.967  1.00 35.10           C  
ATOM   1040  CG1 VAL A 152     -87.378   9.409 -11.497  1.00 47.54           C  
ATOM   1041  CG2 VAL A 152     -89.023   7.713 -10.785  1.00 28.18           C  
ATOM   1042  N   ASP A 153     -89.952  10.974 -12.017  1.00 26.23           N  
ATOM   1043  CA  ASP A 153     -90.828  11.867 -11.279  1.00 32.88           C  
ATOM   1044  C   ASP A 153     -92.137  12.178 -11.999  1.00 28.61           C  
ATOM   1045  O   ASP A 153     -93.107  12.518 -11.348  1.00 27.06           O  
ATOM   1046  CB  ASP A 153     -90.142  13.173 -10.906  1.00 41.52           C  
ATOM   1047  CG  ASP A 153     -91.041  14.068 -10.061  1.00 46.19           C  
ATOM   1048  OD1 ASP A 153     -91.436  13.634  -8.952  1.00 46.39           O  
ATOM   1049  OD2 ASP A 153     -91.376  15.190 -10.518  1.00 50.78           O  
ATOM   1050  N   ILE A 154     -92.194  12.082 -13.319  1.00 22.61           N  
ATOM   1051  CA  ILE A 154     -93.509  12.124 -13.943  1.00 25.81           C  
ATOM   1052  C   ILE A 154     -94.247  10.796 -13.737  1.00 23.18           C  
ATOM   1053  O   ILE A 154     -95.461  10.797 -13.490  1.00 21.73           O  
ATOM   1054  CB  ILE A 154     -93.448  12.482 -15.425  1.00 27.71           C  
ATOM   1055  CG1 ILE A 154     -93.025  13.945 -15.593  1.00 26.54           C  
ATOM   1056  CG2 ILE A 154     -94.800  12.266 -16.069  1.00 16.82           C  
ATOM   1057  CD1 ILE A 154     -93.146  14.476 -17.019  1.00 20.37           C  
ATOM   1058  N   ASP A 155     -93.522   9.679 -13.808  1.00 19.66           N  
ATOM   1059  CA  ASP A 155     -94.166   8.362 -13.791  1.00 24.41           C  
ATOM   1060  C   ASP A 155     -94.887   8.149 -12.494  1.00 24.55           C  
ATOM   1061  O   ASP A 155     -95.998   7.595 -12.482  1.00 18.35           O  
ATOM   1062  CB  ASP A 155     -93.169   7.216 -13.997  1.00 37.64           C  
ATOM   1063  CG  ASP A 155     -93.861   5.842 -14.166  1.00 37.23           C  
ATOM   1064  OD1 ASP A 155     -93.558   4.890 -13.406  1.00 32.78           O  
ATOM   1065  OD2 ASP A 155     -94.707   5.718 -15.071  1.00 42.93           O  
ATOM   1066  N   ILE A 156     -94.250   8.584 -11.408  1.00 26.78           N  
ATOM   1067  CA  ILE A 156     -94.914   8.588 -10.109  1.00 35.01           C  
ATOM   1068  C   ILE A 156     -96.168   9.461 -10.142  1.00 31.72           C  
ATOM   1069  O   ILE A 156     -97.231   9.024  -9.712  1.00 34.68           O  
ATOM   1070  CB  ILE A 156     -94.022   9.116  -8.986  1.00 28.99           C  
ATOM   1071  CG1 ILE A 156     -93.049   8.046  -8.546  1.00 25.98           C  
ATOM   1072  CG2 ILE A 156     -94.877   9.506  -7.782  1.00 36.40           C  
ATOM   1073  CD1 ILE A 156     -91.834   8.596  -7.891  1.00 23.21           C  
ATOM   1074  N   LYS A 157     -96.029  10.684 -10.645  1.00 21.95           N  
ATOM   1075  CA  LYS A 157     -97.104  11.657 -10.570  1.00 24.87           C  
ATOM   1076  C   LYS A 157     -98.257  11.163 -11.377  1.00 17.75           C  
ATOM   1077  O   LYS A 157     -99.391  11.181 -10.908  1.00 13.18           O  
ATOM   1078  CB  LYS A 157     -96.688  13.038 -11.102  1.00 35.98           C  
ATOM   1079  CG  LYS A 157     -95.530  13.713 -10.347  1.00 35.96           C  
ATOM   1080  CD  LYS A 157     -95.991  14.700  -9.286  1.00 34.07           C  
ATOM   1081  CE  LYS A 157     -94.830  15.101  -8.402  1.00 29.71           C  
ATOM   1082  NZ  LYS A 157     -93.689  15.575  -9.204  1.00 37.26           N  
ATOM   1083  N   ILE A 158     -97.987  10.710 -12.595  1.00 20.70           N  
ATOM   1084  CA  ILE A 158     -99.100  10.245 -13.418  1.00 23.83           C  
ATOM   1085  C   ILE A 158     -99.796   9.099 -12.721  1.00 21.56           C  
ATOM   1086  O   ILE A 158    -101.004   9.119 -12.618  1.00 23.17           O  
ATOM   1087  CB  ILE A 158     -98.717   9.794 -14.824  1.00 20.06           C  
ATOM   1088  CG1 ILE A 158     -98.271  10.990 -15.646  1.00 19.29           C  
ATOM   1089  CG2 ILE A 158     -99.922   9.147 -15.482  1.00 13.95           C  
ATOM   1090  CD1 ILE A 158     -98.042  10.668 -17.091  1.00 24.95           C  
ATOM   1091  N   ARG A 159     -99.038   8.113 -12.229  1.00 25.51           N  
ATOM   1092  CA  ARG A 159     -99.664   6.961 -11.591  1.00 20.64           C  
ATOM   1093  C   ARG A 159    -100.444   7.367 -10.346  1.00 23.47           C  
ATOM   1094  O   ARG A 159    -101.516   6.812 -10.079  1.00 28.55           O  
ATOM   1095  CB  ARG A 159     -98.677   5.860 -11.249  1.00 14.54           C  
ATOM   1096  CG  ARG A 159     -99.426   4.594 -10.783  1.00 21.29           C  
ATOM   1097  CD  ARG A 159     -98.577   3.379 -10.550  1.00 16.22           C  
ATOM   1098  NE  ARG A 159     -97.672   3.189 -11.669  1.00 23.87           N  
ATOM   1099  CZ  ARG A 159     -96.445   3.692 -11.757  1.00 21.18           C  
ATOM   1100  NH1 ARG A 159     -95.935   4.412 -10.765  1.00 27.97           N  
ATOM   1101  NH2 ARG A 159     -95.723   3.468 -12.848  1.00 25.52           N  
ATOM   1102  N   SER A 160     -99.910   8.346  -9.622  1.00 23.12           N  
ATOM   1103  CA  SER A 160    -100.570   8.951  -8.469  1.00 25.27           C  
ATOM   1104  C   SER A 160    -101.971   9.479  -8.768  1.00 33.27           C  
ATOM   1105  O   SER A 160    -102.811   9.564  -7.858  1.00 33.03           O  
ATOM   1106  CB  SER A 160     -99.713  10.095  -7.926  1.00 31.67           C  
ATOM   1107  OG  SER A 160    -100.382  10.798  -6.906  1.00 32.89           O  
ATOM   1108  N   CYS A 161    -102.228   9.830 -10.029  1.00 33.04           N  
ATOM   1109  CA  CYS A 161    -103.559  10.297 -10.442  1.00 29.93           C  
ATOM   1110  C   CYS A 161    -104.636   9.221 -10.482  1.00 29.90           C  
ATOM   1111  O   CYS A 161    -105.811   9.531 -10.670  1.00 32.86           O  
ATOM   1112  CB  CYS A 161    -103.492  11.008 -11.791  1.00 29.18           C  
ATOM   1113  SG  CYS A 161    -102.673  12.583 -11.617  1.00 44.59           S  
ATOM   1114  N   ARG A 162    -104.257   7.962 -10.296  1.00 36.41           N  
ATOM   1115  CA  ARG A 162    -105.240   6.879 -10.310  1.00 39.41           C  
ATOM   1116  C   ARG A 162    -106.388   7.142  -9.326  1.00 33.43           C  
ATOM   1117  O   ARG A 162    -107.554   7.002  -9.682  1.00 36.36           O  
ATOM   1118  CB  ARG A 162    -104.564   5.546 -10.026  1.00 41.39           C  
ATOM   1119  CG  ARG A 162    -104.791   4.518 -11.098  1.00 47.26           C  
ATOM   1120  CD  ARG A 162    -103.891   3.303 -10.886  1.00 53.44           C  
ATOM   1121  NE  ARG A 162    -104.595   2.068 -11.208  1.00 49.07           N  
ATOM   1122  CZ  ARG A 162    -105.393   1.403 -10.377  1.00 57.40           C  
ATOM   1123  NH1 ARG A 162    -105.604   1.816  -9.132  1.00 60.03           N  
ATOM   1124  NH2 ARG A 162    -105.992   0.302 -10.801  1.00 69.25           N  
ATOM   1125  N   GLY A 163    -106.060   7.584  -8.117  1.00 34.71           N  
ATOM   1126  CA  GLY A 163    -107.080   7.855  -7.098  1.00 33.10           C  
ATOM   1127  C   GLY A 163    -107.846   9.175  -7.124  1.00 28.68           C  
ATOM   1128  O   GLY A 163    -108.600   9.443  -6.189  1.00 30.96           O  
ATOM   1129  N   SER A 164    -107.674   9.996  -8.163  1.00 27.83           N  
ATOM   1130  CA  SER A 164    -108.264  11.352  -8.206  1.00 22.71           C  
ATOM   1131  C   SER A 164    -109.003  11.604  -9.499  1.00 21.54           C  
ATOM   1132  O   SER A 164    -110.093  12.163  -9.467  1.00 24.31           O  
ATOM   1133  CB  SER A 164    -107.183  12.411  -8.053  1.00 28.30           C  
ATOM   1134  OG  SER A 164    -106.267  12.081  -7.017  1.00 33.68           O  
ATOM   1135  N   CYS A 165    -108.394  11.192 -10.619  1.00 29.93           N  
ATOM   1136  CA  CYS A 165    -109.031  11.139 -11.958  1.00 37.72           C  
ATOM   1137  C   CYS A 165    -109.435   9.723 -12.413  1.00 40.67           C  
ATOM   1138  O   CYS A 165    -108.986   8.720 -11.852  1.00 39.38           O  
ATOM   1139  CB  CYS A 165    -108.109  11.747 -13.013  1.00 39.09           C  
ATOM   1140  SG  CYS A 165    -107.507  13.341 -12.489  1.00 54.19           S  
ATOM   1141  N   SER A 166    -110.269   9.655 -13.451  1.00 46.54           N  
ATOM   1142  CA  SER A 166    -110.883   8.390 -13.859  1.00 55.42           C  
ATOM   1143  C   SER A 166    -109.838   7.450 -14.428  1.00 59.17           C  
ATOM   1144  O   SER A 166    -109.429   6.508 -13.747  1.00 69.43           O  
ATOM   1145  CB  SER A 166    -112.017   8.612 -14.868  1.00 59.59           C  
ATOM   1146  OG  SER A 166    -111.526   9.171 -16.072  1.00 65.44           O  
ATOM   1147  N   ARG A 167    -109.405   7.709 -15.663  1.00 58.38           N  
ATOM   1148  CA  ARG A 167    -108.286   6.979 -16.256  1.00 58.59           C  
ATOM   1149  C   ARG A 167    -106.956   7.602 -15.823  1.00 47.98           C  
ATOM   1150  O   ARG A 167    -106.895   8.777 -15.481  1.00 50.64           O  
ATOM   1151  CB  ARG A 167    -108.383   6.975 -17.785  1.00 68.95           C  
ATOM   1152  CG  ARG A 167    -107.326   6.070 -18.448  1.00 83.04           C  
ATOM   1153  CD  ARG A 167    -107.607   5.725 -19.930  1.00 88.39           C  
ATOM   1154  NE  ARG A 167    -107.151   4.371 -20.284  1.00 92.35           N  
ATOM   1155  CZ  ARG A 167    -105.877   3.981 -20.412  1.00 94.65           C  
ATOM   1156  NH1 ARG A 167    -104.868   4.825 -20.222  1.00 96.23           N  
ATOM   1157  NH2 ARG A 167    -105.606   2.721 -20.735  1.00 96.85           N  
ATOM   1158  N   ALA A 168    -105.901   6.796 -15.817  1.00 37.60           N  
ATOM   1159  CA  ALA A 168    -104.533   7.283 -15.613  1.00 30.28           C  
ATOM   1160  C   ALA A 168    -103.636   6.670 -16.670  1.00 28.37           C  
ATOM   1161  O   ALA A 168    -103.620   5.451 -16.858  1.00 38.00           O  
ATOM   1162  CB  ALA A 168    -104.037   6.903 -14.249  1.00 33.94           C  
ATOM   1163  N   LEU A 169    -102.863   7.501 -17.343  1.00 26.26           N  
ATOM   1164  CA  LEU A 169    -102.217   7.083 -18.567  1.00 26.85           C  
ATOM   1165  C   LEU A 169    -101.265   5.946 -18.287  1.00 33.00           C  
ATOM   1166  O   LEU A 169    -100.354   6.097 -17.476  1.00 37.75           O  
ATOM   1167  CB  LEU A 169    -101.441   8.231 -19.174  1.00 26.61           C  
ATOM   1168  CG  LEU A 169    -100.865   7.844 -20.525  1.00 33.14           C  
ATOM   1169  CD1 LEU A 169    -101.942   7.993 -21.603  1.00 36.21           C  
ATOM   1170  CD2 LEU A 169     -99.643   8.676 -20.814  1.00 26.97           C  
ATOM   1171  N   ALA A 170    -101.472   4.814 -18.957  1.00 39.20           N  
ATOM   1172  CA  ALA A 170    -100.573   3.668 -18.813  1.00 42.21           C  
ATOM   1173  C   ALA A 170     -99.341   3.897 -19.668  1.00 39.89           C  
ATOM   1174  O   ALA A 170     -99.441   4.312 -20.823  1.00 41.87           O  
ATOM   1175  CB  ALA A 170    -101.263   2.364 -19.206  1.00 44.84           C  
ATOM   1176  N   ARG A 171     -98.180   3.631 -19.087  1.00 40.01           N  
ATOM   1177  CA  ARG A 171     -96.919   3.851 -19.767  1.00 45.83           C  
ATOM   1178  C   ARG A 171     -95.791   3.189 -18.997  1.00 53.37           C  
ATOM   1179  O   ARG A 171     -95.811   3.133 -17.768  1.00 51.01           O  
ATOM   1180  CB  ARG A 171     -96.638   5.345 -19.906  1.00 49.40           C  
ATOM   1181  CG  ARG A 171     -96.655   6.123 -18.582  1.00 49.26           C  
ATOM   1182  CD  ARG A 171     -96.776   7.629 -18.813  1.00 47.44           C  
ATOM   1183  NE  ARG A 171     -95.518   8.211 -19.259  1.00 44.70           N  
ATOM   1184  CZ  ARG A 171     -94.510   8.533 -18.453  1.00 52.79           C  
ATOM   1185  NH1 ARG A 171     -94.599   8.329 -17.145  1.00 53.10           N  
ATOM   1186  NH2 ARG A 171     -93.396   9.061 -18.957  1.00 58.37           N  
ATOM   1187  N   GLU A 172     -94.811   2.686 -19.737  1.00 64.41           N  
ATOM   1188  CA  GLU A 172     -93.652   2.011 -19.161  1.00 72.36           C  
ATOM   1189  C   GLU A 172     -92.435   2.929 -19.337  1.00 69.98           C  
ATOM   1190  O   GLU A 172     -92.280   3.572 -20.378  1.00 66.06           O  
ATOM   1191  CB  GLU A 172     -93.431   0.634 -19.833  1.00 76.66           C  
ATOM   1192  CG  GLU A 172     -94.382  -0.509 -19.358  1.00 80.40           C  
ATOM   1193  CD  GLU A 172     -95.809  -0.462 -19.962  1.00 80.62           C  
ATOM   1194  OE1 GLU A 172     -96.791  -0.643 -19.201  1.00 70.14           O  
ATOM   1195  OE2 GLU A 172     -95.953  -0.264 -21.193  1.00 78.94           O  
ATOM   1196  N   VAL A 173     -91.588   2.993 -18.313  1.00 71.49           N  
ATOM   1197  CA  VAL A 173     -90.410   3.859 -18.321  1.00 77.37           C  
ATOM   1198  C   VAL A 173     -89.150   3.081 -18.703  1.00 77.63           C  
ATOM   1199  O   VAL A 173     -88.737   2.188 -17.964  1.00 86.22           O  
ATOM   1200  CB  VAL A 173     -90.190   4.465 -16.934  1.00 80.35           C  
ATOM   1201  CG1 VAL A 173     -89.003   5.420 -16.959  1.00 82.10           C  
ATOM   1202  CG2 VAL A 173     -91.457   5.167 -16.463  1.00 83.34           C  
ATOM   1203  N   ASP A 174     -88.534   3.411 -19.839  1.00 74.83           N  
ATOM   1204  CA  ASP A 174     -87.368   2.645 -20.307  1.00 79.82           C  
ATOM   1205  C   ASP A 174     -86.074   3.292 -19.823  1.00 72.43           C  
ATOM   1206  O   ASP A 174     -85.286   3.823 -20.606  1.00 65.58           O  
ATOM   1207  CB  ASP A 174     -87.369   2.456 -21.843  1.00 85.63           C  
ATOM   1208  CG  ASP A 174     -86.449   1.299 -22.309  1.00 83.93           C  
ATOM   1209  OD1 ASP A 174     -85.681   1.485 -23.283  1.00 79.71           O  
ATOM   1210  OD2 ASP A 174     -86.496   0.201 -21.705  1.00 78.98           O  
ATOM   1211  N   LEU A 175     -85.866   3.240 -18.514  1.00 66.51           N  
ATOM   1212  CA  LEU A 175     -84.630   3.728 -17.914  1.00 61.70           C  
ATOM   1213  C   LEU A 175     -83.433   2.852 -18.317  1.00 58.76           C  
ATOM   1214  O   LEU A 175     -82.301   3.326 -18.370  1.00 57.09           O  
ATOM   1215  CB  LEU A 175     -84.780   3.857 -16.387  1.00 58.47           C  
ATOM   1216  CG  LEU A 175     -84.888   2.629 -15.470  1.00 50.99           C  
ATOM   1217  CD1 LEU A 175     -85.549   3.083 -14.188  1.00 39.93           C  
ATOM   1218  CD2 LEU A 175     -85.655   1.442 -16.069  1.00 45.47           C  
ATOM   1219  N   LYS A 176     -83.691   1.584 -18.626  1.00 57.77           N  
ATOM   1220  CA  LYS A 176     -82.704   0.732 -19.288  1.00 54.52           C  
ATOM   1221  C   LYS A 176     -81.933   1.554 -20.341  1.00 48.08           C  
ATOM   1222  O   LYS A 176     -80.705   1.562 -20.347  1.00 50.08           O  
ATOM   1223  CB  LYS A 176     -83.413  -0.496 -19.895  1.00 57.97           C  
ATOM   1224  CG  LYS A 176     -82.625  -1.326 -20.906  1.00 57.94           C  
ATOM   1225  CD  LYS A 176     -81.392  -1.969 -20.292  1.00 61.67           C  
ATOM   1226  CE  LYS A 176     -80.469  -2.532 -21.373  1.00 62.02           C  
ATOM   1227  NZ  LYS A 176     -79.070  -2.746 -20.888  1.00 63.47           N  
ATOM   1228  N   ASP A 177     -82.655   2.275 -21.195  1.00 46.93           N  
ATOM   1229  CA  ASP A 177     -82.041   3.189 -22.164  1.00 50.47           C  
ATOM   1230  C   ASP A 177     -81.198   4.272 -21.471  1.00 43.09           C  
ATOM   1231  O   ASP A 177     -80.023   4.434 -21.774  1.00 49.47           O  
ATOM   1232  CB  ASP A 177     -83.129   3.832 -23.050  1.00 61.52           C  
ATOM   1233  CG  ASP A 177     -82.572   4.851 -24.058  1.00 69.14           C  
ATOM   1234  OD1 ASP A 177     -81.538   4.567 -24.699  1.00 75.24           O  
ATOM   1235  OD2 ASP A 177     -83.191   5.931 -24.230  1.00 67.34           O  
ATOM   1236  N   TYR A 178     -81.798   5.005 -20.545  1.00 40.00           N  
ATOM   1237  CA  TYR A 178     -81.092   6.048 -19.801  1.00 41.81           C  
ATOM   1238  C   TYR A 178     -79.754   5.589 -19.197  1.00 45.81           C  
ATOM   1239  O   TYR A 178     -78.758   6.306 -19.274  1.00 42.25           O  
ATOM   1240  CB  TYR A 178     -81.978   6.566 -18.670  1.00 41.47           C  
ATOM   1241  CG  TYR A 178     -82.949   7.653 -19.057  1.00 41.01           C  
ATOM   1242  CD1 TYR A 178     -84.252   7.357 -19.430  1.00 34.98           C  
ATOM   1243  CD2 TYR A 178     -82.570   8.992 -18.998  1.00 44.56           C  
ATOM   1244  CE1 TYR A 178     -85.143   8.368 -19.759  1.00 42.27           C  
ATOM   1245  CE2 TYR A 178     -83.450  10.008 -19.327  1.00 38.80           C  
ATOM   1246  CZ  TYR A 178     -84.732   9.698 -19.707  1.00 45.11           C  
ATOM   1247  OH  TYR A 178     -85.604  10.716 -20.028  1.00 51.79           O  
ATOM   1248  N   GLU A 179     -79.746   4.403 -18.585  1.00 52.65           N  
ATOM   1249  CA  GLU A 179     -78.551   3.867 -17.913  1.00 54.71           C  
ATOM   1250  C   GLU A 179     -77.428   3.657 -18.908  1.00 50.61           C  
ATOM   1251  O   GLU A 179     -76.312   4.102 -18.675  1.00 43.73           O  
ATOM   1252  CB  GLU A 179     -78.839   2.517 -17.235  1.00 65.52           C  
ATOM   1253  CG  GLU A 179     -79.894   2.529 -16.121  1.00 73.66           C  
ATOM   1254  CD  GLU A 179     -79.434   3.212 -14.838  1.00 80.18           C  
ATOM   1255  OE1 GLU A 179     -80.242   3.245 -13.875  1.00 74.54           O  
ATOM   1256  OE2 GLU A 179     -78.287   3.718 -14.789  1.00 81.57           O  
ATOM   1257  N   ASP A 180     -77.740   2.950 -19.997  1.00 52.74           N  
ATOM   1258  CA  ASP A 180     -76.806   2.722 -21.106  1.00 50.19           C  
ATOM   1259  C   ASP A 180     -76.235   4.032 -21.593  1.00 51.87           C  
ATOM   1260  O   ASP A 180     -75.025   4.181 -21.685  1.00 60.27           O  
ATOM   1261  CB  ASP A 180     -77.491   2.030 -22.282  1.00 52.16           C  
ATOM   1262  CG  ASP A 180     -78.107   0.703 -21.900  1.00 62.66           C  
ATOM   1263  OD1 ASP A 180     -77.601   0.069 -20.942  1.00 69.08           O  
ATOM   1264  OD2 ASP A 180     -79.102   0.303 -22.556  1.00 63.46           O  
ATOM   1265  N   GLN A 181     -77.104   4.993 -21.881  1.00 50.25           N  
ATOM   1266  CA  GLN A 181     -76.651   6.320 -22.290  1.00 53.22           C  
ATOM   1267  C   GLN A 181     -75.765   7.020 -21.238  1.00 52.50           C  
ATOM   1268  O   GLN A 181     -75.009   7.917 -21.580  1.00 51.18           O  
ATOM   1269  CB  GLN A 181     -77.844   7.197 -22.677  1.00 57.41           C  
ATOM   1270  CG  GLN A 181     -78.626   6.644 -23.865  1.00 62.95           C  
ATOM   1271  CD  GLN A 181     -79.397   7.710 -24.625  1.00 68.33           C  
ATOM   1272  OE1 GLN A 181     -80.347   8.300 -24.104  1.00 60.94           O  
ATOM   1273  NE2 GLN A 181     -78.996   7.950 -25.875  1.00 76.58           N  
ATOM   1274  N   GLN A 182     -75.847   6.609 -19.974  1.00 50.41           N  
ATOM   1275  CA  GLN A 182     -74.918   7.093 -18.943  1.00 56.39           C  
ATOM   1276  C   GLN A 182     -73.652   6.209 -18.853  1.00 53.45           C  
ATOM   1277  O   GLN A 182     -72.534   6.709 -18.965  1.00 49.37           O  
ATOM   1278  CB  GLN A 182     -75.630   7.188 -17.579  1.00 62.10           C  
ATOM   1279  CG  GLN A 182     -76.675   8.327 -17.497  1.00 61.55           C  
ATOM   1280  CD  GLN A 182     -77.525   8.333 -16.211  1.00 59.51           C  
ATOM   1281  OE1 GLN A 182     -78.394   9.190 -16.049  1.00 65.01           O  
ATOM   1282  NE2 GLN A 182     -77.276   7.388 -15.306  1.00 57.14           N  
ATOM   1283  N   LYS A 183     -73.853   4.907 -18.646  1.00 52.62           N  
ATOM   1284  CA  LYS A 183     -72.785   3.891 -18.608  1.00 46.67           C  
ATOM   1285  C   LYS A 183     -71.934   3.917 -19.877  1.00 49.99           C  
ATOM   1286  O   LYS A 183     -70.713   3.748 -19.826  1.00 55.85           O  
ATOM   1287  CB  LYS A 183     -73.420   2.507 -18.437  1.00 47.72           C  
ATOM   1288  CG  LYS A 183     -72.490   1.324 -18.575  1.00 52.04           C  
ATOM   1289  CD  LYS A 183     -73.033   0.316 -19.587  1.00 56.12           C  
ATOM   1290  CE  LYS A 183     -72.125  -0.917 -19.717  1.00 58.87           C  
ATOM   1291  NZ  LYS A 183     -70.733  -0.584 -20.143  1.00 57.69           N  
ATOM   1292  N   GLN A 184     -72.583   4.111 -21.017  1.00 48.80           N  
ATOM   1293  CA  GLN A 184     -71.875   4.373 -22.265  1.00 52.70           C  
ATOM   1294  C   GLN A 184     -71.137   5.706 -22.182  1.00 49.27           C  
ATOM   1295  O   GLN A 184     -69.955   5.785 -22.483  1.00 49.45           O  
ATOM   1296  CB  GLN A 184     -72.863   4.419 -23.432  1.00 60.57           C  
ATOM   1297  CG  GLN A 184     -72.255   4.616 -24.813  1.00 62.38           C  
ATOM   1298  CD  GLN A 184     -73.289   5.025 -25.848  1.00 65.42           C  
ATOM   1299  OE1 GLN A 184     -74.495   4.782 -25.688  1.00 63.67           O  
ATOM   1300  NE2 GLN A 184     -72.822   5.654 -26.920  1.00 67.51           N  
ATOM   1301  N   LEU A 185     -71.844   6.755 -21.778  1.00 49.98           N  
ATOM   1302  CA  LEU A 185     -71.259   8.094 -21.720  1.00 47.13           C  
ATOM   1303  C   LEU A 185     -70.062   8.201 -20.780  1.00 46.26           C  
ATOM   1304  O   LEU A 185     -69.051   8.768 -21.168  1.00 56.93           O  
ATOM   1305  CB  LEU A 185     -72.320   9.127 -21.338  1.00 44.59           C  
ATOM   1306  CG  LEU A 185     -71.930  10.603 -21.203  1.00 38.37           C  
ATOM   1307  CD1 LEU A 185     -71.640  10.967 -19.767  1.00 41.55           C  
ATOM   1308  CD2 LEU A 185     -70.771  10.948 -22.096  1.00 29.81           C  
ATOM   1309  N   GLU A 186     -70.153   7.666 -19.563  1.00 45.67           N  
ATOM   1310  CA  GLU A 186     -69.036   7.801 -18.613  1.00 54.43           C  
ATOM   1311  C   GLU A 186     -67.758   7.170 -19.137  1.00 55.27           C  
ATOM   1312  O   GLU A 186     -66.675   7.707 -18.929  1.00 49.71           O  
ATOM   1313  CB  GLU A 186     -69.368   7.248 -17.226  1.00 61.29           C  
ATOM   1314  CG  GLU A 186     -69.998   8.289 -16.280  1.00 69.22           C  
ATOM   1315  CD  GLU A 186     -69.175   9.584 -16.137  1.00 71.51           C  
ATOM   1316  OE1 GLU A 186     -69.784  10.679 -16.165  1.00 66.82           O  
ATOM   1317  OE2 GLU A 186     -67.928   9.510 -16.002  1.00 69.70           O  
ATOM   1318  N   GLN A 187     -67.905   6.035 -19.812  1.00 62.85           N  
ATOM   1319  CA  GLN A 187     -66.862   5.459 -20.666  1.00 66.54           C  
ATOM   1320  C   GLN A 187     -65.995   6.540 -21.344  1.00 69.38           C  
ATOM   1321  O   GLN A 187     -64.759   6.451 -21.339  1.00 70.42           O  
ATOM   1322  CB  GLN A 187     -67.532   4.590 -21.745  1.00 68.33           C  
ATOM   1323  CG  GLN A 187     -66.766   3.374 -22.225  1.00 72.39           C  
ATOM   1324  CD  GLN A 187     -67.518   2.622 -23.325  1.00 76.40           C  
ATOM   1325  OE1 GLN A 187     -67.952   3.218 -24.319  1.00 75.69           O  
ATOM   1326  NE2 GLN A 187     -67.674   1.308 -23.149  1.00 77.49           N  
ATOM   1327  N   VAL A 188     -66.656   7.566 -21.889  1.00 66.72           N  
ATOM   1328  CA  VAL A 188     -66.038   8.553 -22.795  1.00 73.52           C  
ATOM   1329  C   VAL A 188     -65.453   9.836 -22.160  1.00 76.47           C  
ATOM   1330  O   VAL A 188     -64.482  10.394 -22.676  1.00 72.40           O  
ATOM   1331  CB  VAL A 188     -67.070   8.988 -23.865  1.00 74.34           C  
ATOM   1332  CG1 VAL A 188     -66.462   9.980 -24.844  1.00 72.42           C  
ATOM   1333  CG2 VAL A 188     -67.623   7.766 -24.599  1.00 77.43           C  
ATOM   1334  N   ILE A 189     -66.038  10.317 -21.068  1.00 81.46           N  
ATOM   1335  CA  ILE A 189     -65.605  11.593 -20.487  1.00 87.71           C  
ATOM   1336  C   ILE A 189     -64.309  11.459 -19.696  1.00 96.12           C  
ATOM   1337  O   ILE A 189     -63.498  12.390 -19.672  1.00 98.02           O  
ATOM   1338  CB  ILE A 189     -66.674  12.213 -19.558  1.00 87.33           C  
ATOM   1339  CG1 ILE A 189     -68.018  12.322 -20.281  1.00 86.89           C  
ATOM   1340  CG2 ILE A 189     -66.220  13.600 -19.057  1.00 83.05           C  
ATOM   1341  CD1 ILE A 189     -69.069  13.077 -19.503  1.00 85.33           C  
ATOM   1342  N   ALA A 190     -64.110  10.299 -19.069  1.00102.21           N  
ATOM   1343  CA  ALA A 190     -63.021  10.099 -18.107  1.00107.38           C  
ATOM   1344  C   ALA A 190     -61.626   9.926 -18.726  1.00114.21           C  
ATOM   1345  O   ALA A 190     -60.685   9.559 -18.017  1.00119.61           O  
ATOM   1346  CB  ALA A 190     -63.340   8.909 -17.206  1.00104.67           C  
ATOM   1347  N   LYS A 191     -61.487  10.202 -20.025  1.00118.41           N  
ATOM   1348  CA  LYS A 191     -60.211  10.033 -20.737  1.00119.12           C  
ATOM   1349  C   LYS A 191     -59.495  11.338 -21.082  1.00118.58           C  
ATOM   1350  O   LYS A 191     -58.357  11.562 -20.675  1.00115.49           O  
ATOM   1351  CB  LYS A 191     -60.441   9.284 -22.048  1.00119.47           C  
ATOM   1352  CG  LYS A 191     -60.699   7.808 -21.897  1.00122.92           C  
ATOM   1353  CD  LYS A 191     -60.768   7.119 -23.259  1.00126.80           C  
ATOM   1354  CE  LYS A 191     -59.382   6.873 -23.881  1.00128.47           C  
ATOM   1355  NZ  LYS A 191     -58.788   8.070 -24.540  1.00126.92           N  
ATOM   1356  N   ASP A 192     -60.183  12.197 -21.828  1.00121.61           N  
ATOM   1357  CA  ASP A 192     -59.526  13.207 -22.665  1.00122.98           C  
ATOM   1358  C   ASP A 192     -59.254  14.529 -21.952  1.00123.32           C  
ATOM   1359  O   ASP A 192     -60.170  15.324 -21.714  1.00117.61           O  
ATOM   1360  CB  ASP A 192     -60.368  13.461 -23.920  1.00123.70           C  
ATOM   1361  CG  ASP A 192     -61.078  12.214 -24.399  1.00124.36           C  
ATOM   1362  OD1 ASP A 192     -62.314  12.266 -24.566  1.00124.53           O  
ATOM   1363  OD2 ASP A 192     -60.404  11.177 -24.567  1.00125.95           O  
ATOM   1364  N   LEU A 193     -57.988  14.738 -21.602  1.00121.60           N  
ATOM   1365  CA  LEU A 193     -57.503  16.025 -21.097  1.00121.65           C  
ATOM   1366  C   LEU A 193     -56.298  16.522 -21.924  1.00123.40           C  
ATOM   1367  O   LEU A 193     -56.122  17.729 -22.098  1.00115.53           O  
ATOM   1368  CB  LEU A 193     -57.138  15.913 -19.601  1.00117.75           C  
ATOM   1369  CG  LEU A 193     -58.232  15.491 -18.595  1.00110.57           C  
ATOM   1370  CD1 LEU A 193     -57.632  14.731 -17.416  1.00106.29           C  
ATOM   1371  CD2 LEU A 193     -59.049  16.676 -18.089  1.00103.83           C  
ATOM   1372  N   LEU A 194     -55.497  15.581 -22.437  1.00131.49           N  
ATOM   1373  CA  LEU A 194     -54.256  15.850 -23.197  1.00139.37           C  
ATOM   1374  C   LEU A 194     -53.161  16.574 -22.380  1.00143.86           C  
ATOM   1375  O   LEU A 194     -52.745  17.684 -22.730  1.00140.73           O  
ATOM   1376  CB  LEU A 194     -54.555  16.578 -24.528  1.00141.15           C  
ATOM   1377  CG  LEU A 194     -54.637  15.683 -25.774  1.00139.89           C  
ATOM   1378  CD1 LEU A 194     -55.968  14.941 -25.822  1.00138.20           C  
ATOM   1379  CD2 LEU A 194     -54.416  16.475 -27.063  1.00137.17           C  
ATOM   1380  N   PRO A 195     -52.663  15.925 -21.306  1.00150.65           N  
ATOM   1381  CA  PRO A 195     -51.752  16.611 -20.393  1.00153.07           C  
ATOM   1382  C   PRO A 195     -50.271  16.496 -20.777  1.00152.70           C  
ATOM   1383  O   PRO A 195     -49.739  17.407 -21.410  1.00154.16           O  
ATOM   1384  CB  PRO A 195     -52.040  15.930 -19.043  1.00154.40           C  
ATOM   1385  CG  PRO A 195     -52.621  14.561 -19.396  1.00154.06           C  
ATOM   1386  CD  PRO A 195     -52.878  14.528 -20.889  1.00152.73           C  
ATOM   1387  N   SER A 196     -49.644  15.370 -20.432  1.00152.51           N  
ATOM   1388  CA  SER A 196     -48.177  15.215 -20.396  1.00152.02           C  
ATOM   1389  C   SER A 196     -47.364  16.101 -21.359  1.00151.46           C  
ATOM   1390  O   SER A 196     -46.465  16.830 -20.925  1.00148.44           O  
ATOM   1391  CB  SER A 196     -47.807  13.741 -20.615  1.00151.58           C  
ATOM   1392  OG  SER A 196     -48.454  12.903 -19.671  1.00150.18           O  
ATOM   1393  N   ARG A 197     -47.676  16.032 -22.653  1.00149.37           N  
ATOM   1394  CA  ARG A 197     -46.949  16.803 -23.672  1.00144.40           C  
ATOM   1395  C   ARG A 197     -47.426  18.259 -23.709  1.00140.39           C  
ATOM   1396  O   ARG A 197     -48.318  18.620 -24.482  1.00133.32           O  
ATOM   1397  CB  ARG A 197     -47.071  16.142 -25.053  1.00145.05           C  
ATOM   1398  CG  ARG A 197     -45.840  15.328 -25.482  1.00146.28           C  
ATOM   1399  CD  ARG A 197     -45.718  13.978 -24.781  1.00145.40           C  
ATOM   1400  NE  ARG A 197     -45.376  14.104 -23.366  1.00144.55           N  
ATOM   1401  CZ  ARG A 197     -44.167  14.402 -22.894  1.00144.53           C  
ATOM   1402  NH1 ARG A 197     -43.143  14.619 -23.716  1.00144.43           N  
ATOM   1403  NH2 ARG A 197     -43.980  14.488 -21.580  1.00145.05           N  
ATOM   1404  N   ASP A 198     -46.809  19.079 -22.858  1.00140.42           N  
ATOM   1405  CA  ASP A 198     -47.190  20.483 -22.669  1.00137.52           C  
ATOM   1406  C   ASP A 198     -46.282  21.453 -23.425  1.00133.77           C  
ATOM   1407  O   ASP A 198     -46.748  22.468 -23.949  1.00127.41           O  
ATOM   1408  CB  ASP A 198     -47.135  20.841 -21.176  1.00138.22           C  
ATOM   1409  CG  ASP A 198     -48.199  20.128 -20.354  1.00139.24           C  
ATOM   1410  OD1 ASP A 198     -49.398  20.247 -20.691  1.00141.80           O  
ATOM   1411  OD2 ASP A 198     -47.838  19.465 -19.356  1.00136.47           O  
ATOM   1412  N   ARG A 199     -44.994  21.115 -23.492  1.00132.73           N  
ATOM   1413  CA  ARG A 199     -43.928  22.074 -23.804  1.00131.25           C  
ATOM   1414  C   ARG A 199     -42.911  21.515 -24.806  1.00127.97           C  
ATOM   1415  O   ARG A 199     -42.539  20.341 -24.730  1.00128.35           O  
ATOM   1416  CB  ARG A 199     -43.217  22.470 -22.506  1.00132.43           C  
ATOM   1417  CG  ARG A 199     -43.075  21.318 -21.519  1.00132.79           C  
ATOM   1418  CD  ARG A 199     -42.452  21.746 -20.213  1.00134.14           C  
ATOM   1419  NE  ARG A 199     -42.714  20.767 -19.156  1.00135.13           N  
ATOM   1420  CZ  ARG A 199     -42.291  20.874 -17.897  1.00134.29           C  
ATOM   1421  NH1 ARG A 199     -41.573  21.925 -17.509  1.00135.11           N  
ATOM   1422  NH2 ARG A 199     -42.588  19.923 -17.017  1.00132.63           N  
ATOM   1423  N   GLN A 200     -42.474  22.361 -25.743  1.00122.97           N  
ATOM   1424  CA  GLN A 200     -41.620  21.935 -26.858  1.00117.99           C  
ATOM   1425  C   GLN A 200     -40.640  23.035 -27.265  1.00111.76           C  
ATOM   1426  O   GLN A 200     -39.920  22.906 -28.257  1.00101.90           O  
ATOM   1427  CB  GLN A 200     -42.481  21.553 -28.063  1.00119.23           C  
ATOM   1428  CG  GLN A 200     -43.494  20.433 -27.804  1.00122.07           C  
ATOM   1429  CD  GLN A 200     -44.736  20.892 -27.045  1.00122.66           C  
ATOM   1430  OE1 GLN A 200     -45.301  21.947 -27.329  1.00121.89           O  
ATOM   1431  NE2 GLN A 200     -45.168  20.087 -26.079  1.00123.50           N  
TER    1432      GLN A 200                                                      
ATOM   1433  N   LYS B  58      44.322  -3.031 -50.937  1.00128.24           N  
ATOM   1434  CA  LYS B  58      44.866  -2.063 -51.934  1.00127.66           C  
ATOM   1435  C   LYS B  58      44.267  -0.680 -51.650  1.00125.10           C  
ATOM   1436  O   LYS B  58      43.074  -0.453 -51.865  1.00125.82           O  
ATOM   1437  CB  LYS B  58      44.551  -2.541 -53.369  1.00127.30           C  
ATOM   1438  CG  LYS B  58      45.512  -2.050 -54.481  1.00126.16           C  
ATOM   1439  CD  LYS B  58      45.412  -2.937 -55.746  1.00122.59           C  
ATOM   1440  CE  LYS B  58      46.378  -2.520 -56.866  1.00118.33           C  
ATOM   1441  NZ  LYS B  58      45.737  -1.663 -57.901  1.00113.94           N  
ATOM   1442  N   ALA B  59      45.092   0.226 -51.129  1.00120.45           N  
ATOM   1443  CA  ALA B  59      44.695   1.620 -50.949  1.00118.47           C  
ATOM   1444  C   ALA B  59      44.757   2.318 -52.311  1.00116.97           C  
ATOM   1445  O   ALA B  59      45.841   2.439 -52.882  1.00122.77           O  
ATOM   1446  CB  ALA B  59      45.618   2.310 -49.959  1.00119.03           C  
ATOM   1447  N   PRO B  60      43.603   2.787 -52.831  1.00110.22           N  
ATOM   1448  CA  PRO B  60      43.471   3.281 -54.207  1.00106.98           C  
ATOM   1449  C   PRO B  60      44.737   3.909 -54.803  1.00108.69           C  
ATOM   1450  O   PRO B  60      45.195   4.951 -54.325  1.00112.27           O  
ATOM   1451  CB  PRO B  60      42.365   4.327 -54.091  1.00104.66           C  
ATOM   1452  CG  PRO B  60      41.510   3.840 -52.981  1.00107.33           C  
ATOM   1453  CD  PRO B  60      42.352   2.979 -52.074  1.00108.61           C  
ATOM   1454  N   ASP B  61      45.297   3.253 -55.819  1.00106.43           N  
ATOM   1455  CA  ASP B  61      46.378   3.814 -56.634  1.00 98.40           C  
ATOM   1456  C   ASP B  61      45.818   4.127 -58.017  1.00 97.63           C  
ATOM   1457  O   ASP B  61      45.042   3.342 -58.573  1.00 97.63           O  
ATOM   1458  CB  ASP B  61      47.532   2.816 -56.774  1.00 93.41           C  
ATOM   1459  CG  ASP B  61      48.348   2.660 -55.501  1.00 89.51           C  
ATOM   1460  OD1 ASP B  61      48.485   3.641 -54.746  1.00 89.24           O  
ATOM   1461  OD2 ASP B  61      48.877   1.551 -55.266  1.00 85.49           O  
ATOM   1462  N   ALA B  62      46.199   5.274 -58.568  1.00 93.97           N  
ATOM   1463  CA  ALA B  62      45.784   5.640 -59.921  1.00 95.34           C  
ATOM   1464  C   ALA B  62      46.863   6.456 -60.597  1.00 95.28           C  
ATOM   1465  O   ALA B  62      47.793   6.922 -59.949  1.00 93.07           O  
ATOM   1466  CB  ALA B  62      44.481   6.410 -59.894  1.00 96.11           C  
ATOM   1467  N   GLY B  63      46.739   6.607 -61.911  1.00 97.44           N  
ATOM   1468  CA  GLY B  63      47.708   7.364 -62.697  1.00 99.18           C  
ATOM   1469  C   GLY B  63      49.101   6.760 -62.719  1.00 98.50           C  
ATOM   1470  O   GLY B  63      49.348   5.700 -62.136  1.00 95.68           O  
ATOM   1471  N   GLY B  64      50.010   7.446 -63.406  1.00 98.55           N  
ATOM   1472  CA  GLY B  64      51.400   7.024 -63.509  1.00101.85           C  
ATOM   1473  C   GLY B  64      51.623   5.960 -64.567  1.00104.65           C  
ATOM   1474  O   GLY B  64      50.701   5.224 -64.924  1.00105.09           O  
ATOM   1475  N   CYS B  65      52.858   5.882 -65.062  1.00107.68           N  
ATOM   1476  CA  CYS B  65      53.244   4.898 -66.076  1.00108.19           C  
ATOM   1477  C   CYS B  65      54.532   4.165 -65.677  1.00109.10           C  
ATOM   1478  O   CYS B  65      55.288   4.649 -64.828  1.00104.64           O  
ATOM   1479  CB  CYS B  65      53.400   5.575 -67.451  1.00108.78           C  
ATOM   1480  SG  CYS B  65      54.318   7.158 -67.474  1.00105.27           S  
ATOM   1481  N   LEU B  66      54.754   2.991 -66.278  1.00112.41           N  
ATOM   1482  CA  LEU B  66      55.987   2.207 -66.084  1.00109.78           C  
ATOM   1483  C   LEU B  66      57.034   2.662 -67.094  1.00104.46           C  
ATOM   1484  O   LEU B  66      56.837   2.529 -68.298  1.00100.37           O  
ATOM   1485  CB  LEU B  66      55.719   0.699 -66.259  1.00110.54           C  
ATOM   1486  CG  LEU B  66      56.722  -0.312 -65.678  1.00109.09           C  
ATOM   1487  CD1 LEU B  66      56.420  -1.710 -66.202  1.00108.48           C  
ATOM   1488  CD2 LEU B  66      58.165   0.049 -65.984  1.00106.51           C  
ATOM   1489  N   HIS B  67      58.147   3.195 -66.605  1.00104.45           N  
ATOM   1490  CA  HIS B  67      59.216   3.652 -67.484  1.00107.06           C  
ATOM   1491  C   HIS B  67      59.982   2.437 -68.008  1.00111.21           C  
ATOM   1492  O   HIS B  67      60.431   1.600 -67.221  1.00108.70           O  
ATOM   1493  CB  HIS B  67      60.140   4.612 -66.730  1.00105.91           C  
ATOM   1494  CG  HIS B  67      61.129   5.325 -67.600  1.00106.59           C  
ATOM   1495  ND1 HIS B  67      60.966   5.463 -68.962  1.00106.63           N  
ATOM   1496  CD2 HIS B  67      62.280   5.971 -67.292  1.00105.88           C  
ATOM   1497  CE1 HIS B  67      61.986   6.142 -69.458  1.00107.15           C  
ATOM   1498  NE2 HIS B  67      62.796   6.463 -68.465  1.00104.56           N  
ATOM   1499  N   ALA B  68      60.107   2.339 -69.335  1.00118.02           N  
ATOM   1500  CA  ALA B  68      60.822   1.230 -69.989  1.00122.53           C  
ATOM   1501  C   ALA B  68      62.269   1.097 -69.493  1.00127.12           C  
ATOM   1502  O   ALA B  68      62.844   0.007 -69.532  1.00127.87           O  
ATOM   1503  CB  ALA B  68      60.793   1.395 -71.513  1.00119.23           C  
ATOM   1504  N   ASP B  69      62.842   2.217 -69.043  1.00130.80           N  
ATOM   1505  CA  ASP B  69      64.137   2.252 -68.351  1.00129.59           C  
ATOM   1506  C   ASP B  69      63.986   1.726 -66.914  1.00130.34           C  
ATOM   1507  O   ASP B  69      63.240   2.310 -66.126  1.00128.95           O  
ATOM   1508  CB  ASP B  69      64.659   3.698 -68.324  1.00127.43           C  
ATOM   1509  CG  ASP B  69      65.990   3.847 -67.603  1.00125.43           C  
ATOM   1510  OD1 ASP B  69      66.697   2.838 -67.396  1.00127.40           O  
ATOM   1511  OD2 ASP B  69      66.332   4.997 -67.249  1.00120.93           O  
ATOM   1512  N   PRO B  70      64.688   0.626 -66.567  1.00132.81           N  
ATOM   1513  CA  PRO B  70      64.645   0.116 -65.187  1.00133.07           C  
ATOM   1514  C   PRO B  70      65.471   0.912 -64.163  1.00130.89           C  
ATOM   1515  O   PRO B  70      65.409   0.609 -62.966  1.00131.11           O  
ATOM   1516  CB  PRO B  70      65.209  -1.311 -65.313  1.00134.68           C  
ATOM   1517  CG  PRO B  70      65.238  -1.612 -66.774  1.00135.58           C  
ATOM   1518  CD  PRO B  70      65.419  -0.299 -67.451  1.00135.08           C  
ATOM   1519  N   ASP B  71      66.238   1.903 -64.624  1.00126.80           N  
ATOM   1520  CA  ASP B  71      67.020   2.775 -63.735  1.00122.57           C  
ATOM   1521  C   ASP B  71      66.129   3.493 -62.707  1.00115.88           C  
ATOM   1522  O   ASP B  71      66.557   3.738 -61.575  1.00110.17           O  
ATOM   1523  CB  ASP B  71      67.810   3.805 -64.567  1.00124.30           C  
ATOM   1524  CG  ASP B  71      68.896   4.524 -63.765  1.00125.17           C  
ATOM   1525  OD1 ASP B  71      69.343   3.995 -62.721  1.00125.85           O  
ATOM   1526  OD2 ASP B  71      69.310   5.625 -64.195  1.00123.17           O  
ATOM   1527  N   LEU B  72      64.894   3.807 -63.110  1.00110.05           N  
ATOM   1528  CA  LEU B  72      63.945   4.561 -62.284  1.00104.35           C  
ATOM   1529  C   LEU B  72      62.819   3.676 -61.723  1.00104.40           C  
ATOM   1530  O   LEU B  72      62.694   3.545 -60.508  1.00106.39           O  
ATOM   1531  CB  LEU B  72      63.362   5.735 -63.085  1.00 99.75           C  
ATOM   1532  CG  LEU B  72      64.330   6.884 -63.410  1.00 95.10           C  
ATOM   1533  CD1 LEU B  72      63.770   7.781 -64.506  1.00 92.83           C  
ATOM   1534  CD2 LEU B  72      64.645   7.703 -62.170  1.00 91.78           C  
ATOM   1535  N   GLY B  73      62.008   3.072 -62.595  1.00104.45           N  
ATOM   1536  CA  GLY B  73      60.943   2.155 -62.153  1.00103.25           C  
ATOM   1537  C   GLY B  73      59.538   2.552 -62.578  1.00101.07           C  
ATOM   1538  O   GLY B  73      59.107   2.207 -63.683  1.00102.39           O  
ATOM   1539  N   VAL B  74      58.821   3.259 -61.697  1.00 99.23           N  
ATOM   1540  CA  VAL B  74      57.425   3.669 -61.954  1.00 97.86           C  
ATOM   1541  C   VAL B  74      57.145   5.137 -61.586  1.00 93.62           C  
ATOM   1542  O   VAL B  74      57.217   5.516 -60.416  1.00 90.92           O  
ATOM   1543  CB  VAL B  74      56.416   2.781 -61.185  1.00 97.77           C  
ATOM   1544  CG1 VAL B  74      54.999   3.067 -61.663  1.00 94.37           C  
ATOM   1545  CG2 VAL B  74      56.751   1.293 -61.347  1.00 98.18           C  
ATOM   1546  N   LEU B  75      56.802   5.945 -62.588  1.00 92.49           N  
ATOM   1547  CA  LEU B  75      56.558   7.375 -62.389  1.00 90.05           C  
ATOM   1548  C   LEU B  75      55.169   7.615 -61.830  1.00 86.26           C  
ATOM   1549  O   LEU B  75      54.287   6.781 -62.000  1.00 80.63           O  
ATOM   1550  CB  LEU B  75      56.712   8.140 -63.707  1.00 93.09           C  
ATOM   1551  CG  LEU B  75      58.106   8.117 -64.341  1.00 95.65           C  
ATOM   1552  CD1 LEU B  75      58.147   8.909 -65.645  1.00 94.85           C  
ATOM   1553  CD2 LEU B  75      59.134   8.657 -63.369  1.00 98.89           C  
ATOM   1554  N   CYS B  76      54.992   8.765 -61.176  1.00 91.44           N  
ATOM   1555  CA  CYS B  76      53.729   9.153 -60.520  1.00 95.36           C  
ATOM   1556  C   CYS B  76      53.321  10.586 -60.890  1.00 90.04           C  
ATOM   1557  O   CYS B  76      54.181  11.461 -61.008  1.00 92.72           O  
ATOM   1558  CB  CYS B  76      53.868   9.047 -58.994  1.00 99.39           C  
ATOM   1559  SG  CYS B  76      53.627   7.386 -58.313  1.00104.78           S  
ATOM   1560  N   PRO B  77      52.007  10.839 -61.052  1.00 83.01           N  
ATOM   1561  CA  PRO B  77      51.577  12.163 -61.528  1.00 79.73           C  
ATOM   1562  C   PRO B  77      52.100  13.314 -60.663  1.00 75.16           C  
ATOM   1563  O   PRO B  77      52.221  13.170 -59.448  1.00 74.86           O  
ATOM   1564  CB  PRO B  77      50.043  12.085 -61.493  1.00 79.50           C  
ATOM   1565  CG  PRO B  77      49.708  10.843 -60.719  1.00 79.62           C  
ATOM   1566  CD  PRO B  77      50.870   9.927 -60.825  1.00 80.62           C  
ATOM   1567  N   THR B  78      52.404  14.440 -61.302  1.00 72.84           N  
ATOM   1568  CA  THR B  78      53.028  15.579 -60.628  1.00 68.61           C  
ATOM   1569  C   THR B  78      52.022  16.389 -59.816  1.00 67.70           C  
ATOM   1570  O   THR B  78      50.821  16.096 -59.814  1.00 67.72           O  
ATOM   1571  CB  THR B  78      53.670  16.533 -61.642  1.00 70.09           C  
ATOM   1572  OG1 THR B  78      52.646  17.232 -62.362  1.00 72.39           O  
ATOM   1573  CG2 THR B  78      54.515  15.770 -62.612  1.00 73.44           C  
ATOM   1574  N   GLY B  79      52.523  17.419 -59.138  1.00 61.19           N  
ATOM   1575  CA  GLY B  79      51.680  18.304 -58.352  1.00 65.02           C  
ATOM   1576  C   GLY B  79      50.514  18.867 -59.144  1.00 67.76           C  
ATOM   1577  O   GLY B  79      49.358  18.755 -58.723  1.00 65.65           O  
ATOM   1578  N   CYS B  80      50.815  19.447 -60.305  1.00 70.23           N  
ATOM   1579  CA  CYS B  80      49.801  20.140 -61.101  1.00 73.40           C  
ATOM   1580  C   CYS B  80      48.710  19.192 -61.539  1.00 69.67           C  
ATOM   1581  O   CYS B  80      47.563  19.345 -61.141  1.00 68.03           O  
ATOM   1582  CB  CYS B  80      50.419  20.816 -62.318  1.00 77.21           C  
ATOM   1583  SG  CYS B  80      51.584  22.087 -61.852  1.00 82.26           S  
ATOM   1584  N   GLN B  81      49.084  18.187 -62.322  1.00 69.92           N  
ATOM   1585  CA  GLN B  81      48.117  17.214 -62.837  1.00 73.70           C  
ATOM   1586  C   GLN B  81      47.149  16.723 -61.749  1.00 72.29           C  
ATOM   1587  O   GLN B  81      45.968  16.483 -62.027  1.00 69.66           O  
ATOM   1588  CB  GLN B  81      48.838  16.028 -63.502  1.00 71.99           C  
ATOM   1589  CG  GLN B  81      49.779  16.423 -64.643  1.00 70.68           C  
ATOM   1590  CD  GLN B  81      49.242  17.572 -65.486  1.00 66.57           C  
ATOM   1591  OE1 GLN B  81      49.796  18.673 -65.480  1.00 62.91           O  
ATOM   1592  NE2 GLN B  81      48.145  17.325 -66.192  1.00 63.01           N  
ATOM   1593  N   LEU B  82      47.652  16.589 -60.520  1.00 71.27           N  
ATOM   1594  CA  LEU B  82      46.808  16.259 -59.372  1.00 70.22           C  
ATOM   1595  C   LEU B  82      45.975  17.463 -58.931  1.00 70.97           C  
ATOM   1596  O   LEU B  82      44.738  17.398 -58.923  1.00 72.52           O  
ATOM   1597  CB  LEU B  82      47.648  15.745 -58.197  1.00 66.29           C  
ATOM   1598  CG  LEU B  82      48.225  14.328 -58.307  1.00 65.23           C  
ATOM   1599  CD1 LEU B  82      48.970  13.978 -57.034  1.00 67.36           C  
ATOM   1600  CD2 LEU B  82      47.155  13.285 -58.588  1.00 60.07           C  
ATOM   1601  N   GLN B  83      46.646  18.557 -58.569  1.00 66.20           N  
ATOM   1602  CA  GLN B  83      45.936  19.756 -58.110  1.00 67.13           C  
ATOM   1603  C   GLN B  83      45.074  20.346 -59.228  1.00 69.44           C  
ATOM   1604  O   GLN B  83      43.967  20.831 -58.983  1.00 76.19           O  
ATOM   1605  CB  GLN B  83      46.906  20.802 -57.535  1.00 64.84           C  
ATOM   1606  CG  GLN B  83      47.720  21.593 -58.557  1.00 65.18           C  
ATOM   1607  CD  GLN B  83      47.109  22.939 -58.915  1.00 61.13           C  
ATOM   1608  OE1 GLN B  83      45.946  23.023 -59.308  1.00 57.25           O  
ATOM   1609  NE2 GLN B  83      47.901  23.998 -58.792  1.00 56.50           N  
ATOM   1610  N   GLU B  84      45.582  20.291 -60.454  1.00 73.04           N  
ATOM   1611  CA  GLU B  84      44.820  20.707 -61.620  1.00 79.49           C  
ATOM   1612  C   GLU B  84      43.518  19.930 -61.637  1.00 77.18           C  
ATOM   1613  O   GLU B  84      42.436  20.518 -61.569  1.00 78.08           O  
ATOM   1614  CB  GLU B  84      45.611  20.440 -62.908  1.00 88.10           C  
ATOM   1615  CG  GLU B  84      44.892  20.841 -64.178  1.00 91.99           C  
ATOM   1616  CD  GLU B  84      44.683  22.336 -64.260  1.00 96.51           C  
ATOM   1617  OE1 GLU B  84      45.607  23.034 -64.734  1.00100.42           O  
ATOM   1618  OE2 GLU B  84      43.604  22.812 -63.841  1.00 97.05           O  
ATOM   1619  N   ALA B  85      43.641  18.604 -61.703  1.00 76.04           N  
ATOM   1620  CA  ALA B  85      42.489  17.707 -61.692  1.00 79.84           C  
ATOM   1621  C   ALA B  85      41.431  18.209 -60.718  1.00 81.72           C  
ATOM   1622  O   ALA B  85      40.289  18.476 -61.102  1.00 87.06           O  
ATOM   1623  CB  ALA B  85      42.920  16.295 -61.320  1.00 78.50           C  
ATOM   1624  N   LEU B  86      41.827  18.379 -59.462  1.00 78.86           N  
ATOM   1625  CA  LEU B  86      40.882  18.772 -58.425  1.00 76.10           C  
ATOM   1626  C   LEU B  86      40.223  20.124 -58.692  1.00 77.28           C  
ATOM   1627  O   LEU B  86      39.036  20.278 -58.410  1.00 82.55           O  
ATOM   1628  CB  LEU B  86      41.549  18.749 -57.048  1.00 73.49           C  
ATOM   1629  CG  LEU B  86      41.910  17.338 -56.569  1.00 73.40           C  
ATOM   1630  CD1 LEU B  86      42.674  17.386 -55.264  1.00 72.22           C  
ATOM   1631  CD2 LEU B  86      40.670  16.475 -56.416  1.00 72.48           C  
ATOM   1632  N   LEU B  87      40.966  21.086 -59.249  1.00 76.43           N  
ATOM   1633  CA  LEU B  87      40.410  22.428 -59.510  1.00 79.12           C  
ATOM   1634  C   LEU B  87      39.156  22.391 -60.386  1.00 81.10           C  
ATOM   1635  O   LEU B  87      38.151  23.038 -60.074  1.00 80.27           O  
ATOM   1636  CB  LEU B  87      41.441  23.353 -60.165  1.00 78.63           C  
ATOM   1637  CG  LEU B  87      41.000  24.824 -60.310  1.00 80.63           C  
ATOM   1638  CD1 LEU B  87      42.206  25.717 -60.565  1.00 82.31           C  
ATOM   1639  CD2 LEU B  87      39.940  25.052 -61.403  1.00 75.94           C  
ATOM   1640  N   GLN B  88      39.224  21.646 -61.487  1.00 81.95           N  
ATOM   1641  CA  GLN B  88      38.084  21.550 -62.398  1.00 82.38           C  
ATOM   1642  C   GLN B  88      37.122  20.453 -61.960  1.00 85.06           C  
ATOM   1643  O   GLN B  88      36.105  20.246 -62.616  1.00 83.54           O  
ATOM   1644  CB  GLN B  88      38.500  21.297 -63.851  1.00 84.04           C  
ATOM   1645  CG  GLN B  88      39.836  21.884 -64.281  1.00 87.48           C  
ATOM   1646  CD  GLN B  88      40.923  20.832 -64.417  1.00 90.90           C  
ATOM   1647  OE1 GLN B  88      41.827  20.973 -65.236  1.00 92.12           O  
ATOM   1648  NE2 GLN B  88      40.830  19.765 -63.627  1.00 92.95           N  
ATOM   1649  N   GLN B  89      37.451  19.722 -60.893  1.00 88.13           N  
ATOM   1650  CA  GLN B  89      36.454  18.889 -60.218  1.00 94.14           C  
ATOM   1651  C   GLN B  89      35.687  19.782 -59.261  1.00 95.37           C  
ATOM   1652  O   GLN B  89      34.466  19.897 -59.347  1.00101.07           O  
ATOM   1653  CB  GLN B  89      37.087  17.721 -59.451  1.00 95.72           C  
ATOM   1654  CG  GLN B  89      37.171  16.435 -60.251  1.00 98.38           C  
ATOM   1655  CD  GLN B  89      38.378  16.397 -61.151  1.00100.26           C  
ATOM   1656  OE1 GLN B  89      39.362  15.718 -60.857  1.00104.49           O  
ATOM   1657  NE2 GLN B  89      38.323  17.144 -62.248  1.00100.03           N  
ATOM   1658  N   GLU B  90      36.433  20.424 -58.368  1.00 94.26           N  
ATOM   1659  CA  GLU B  90      35.880  21.325 -57.357  1.00 96.07           C  
ATOM   1660  C   GLU B  90      34.827  22.290 -57.908  1.00 96.90           C  
ATOM   1661  O   GLU B  90      33.703  22.309 -57.418  1.00103.49           O  
ATOM   1662  CB  GLU B  90      37.025  22.083 -56.658  1.00 98.80           C  
ATOM   1663  CG  GLU B  90      36.651  23.383 -55.931  1.00101.21           C  
ATOM   1664  CD  GLU B  90      36.820  24.631 -56.799  1.00104.81           C  
ATOM   1665  OE1 GLU B  90      37.800  24.707 -57.575  1.00104.98           O  
ATOM   1666  OE2 GLU B  90      35.971  25.542 -56.701  1.00108.19           O  
ATOM   1667  N   ARG B  91      35.175  23.071 -58.928  1.00 97.26           N  
ATOM   1668  CA  ARG B  91      34.289  24.149 -59.392  1.00104.35           C  
ATOM   1669  C   ARG B  91      32.919  23.650 -59.898  1.00108.77           C  
ATOM   1670  O   ARG B  91      31.890  24.191 -59.486  1.00110.14           O  
ATOM   1671  CB  ARG B  91      34.994  25.056 -60.420  1.00107.41           C  
ATOM   1672  CG  ARG B  91      34.046  25.927 -61.248  1.00109.54           C  
ATOM   1673  CD  ARG B  91      34.752  27.131 -61.864  1.00110.59           C  
ATOM   1674  NE  ARG B  91      35.146  28.121 -60.860  1.00111.79           N  
ATOM   1675  CZ  ARG B  91      34.308  28.929 -60.206  1.00111.13           C  
ATOM   1676  NH1 ARG B  91      32.994  28.884 -60.425  1.00111.39           N  
ATOM   1677  NH2 ARG B  91      34.788  29.789 -59.313  1.00109.67           N  
ATOM   1678  N   PRO B  92      32.901  22.642 -60.800  1.00115.35           N  
ATOM   1679  CA  PRO B  92      31.652  21.949 -61.172  1.00117.14           C  
ATOM   1680  C   PRO B  92      30.970  21.155 -60.048  1.00117.41           C  
ATOM   1681  O   PRO B  92      29.738  21.054 -60.036  1.00114.78           O  
ATOM   1682  CB  PRO B  92      32.104  20.991 -62.276  1.00117.67           C  
ATOM   1683  CG  PRO B  92      33.241  21.674 -62.907  1.00118.51           C  
ATOM   1684  CD  PRO B  92      33.965  22.374 -61.785  1.00117.86           C  
ATOM   1685  N   ILE B  93      31.758  20.583 -59.137  1.00114.76           N  
ATOM   1686  CA  ILE B  93      31.211  19.845 -57.989  1.00115.64           C  
ATOM   1687  C   ILE B  93      30.690  20.779 -56.879  1.00118.27           C  
ATOM   1688  O   ILE B  93      29.911  20.339 -56.033  1.00121.72           O  
ATOM   1689  CB  ILE B  93      32.242  18.834 -57.407  1.00113.08           C  
ATOM   1690  CG1 ILE B  93      32.528  17.719 -58.419  1.00115.71           C  
ATOM   1691  CG2 ILE B  93      31.731  18.201 -56.119  1.00107.98           C  
ATOM   1692  CD1 ILE B  93      33.821  16.952 -58.151  1.00116.64           C  
ATOM   1693  N   ARG B  94      31.101  22.053 -56.885  1.00118.13           N  
ATOM   1694  CA  ARG B  94      30.628  23.041 -55.889  1.00120.46           C  
ATOM   1695  C   ARG B  94      29.373  23.805 -56.331  1.00120.46           C  
ATOM   1696  O   ARG B  94      28.407  23.902 -55.568  1.00122.32           O  
ATOM   1697  CB  ARG B  94      31.732  24.045 -55.525  1.00121.55           C  
ATOM   1698  CG  ARG B  94      32.669  23.573 -54.420  1.00122.81           C  
ATOM   1699  CD  ARG B  94      33.652  24.667 -54.019  1.00124.17           C  
ATOM   1700  NE  ARG B  94      34.590  24.220 -52.988  1.00126.02           N  
ATOM   1701  CZ  ARG B  94      35.576  24.962 -52.484  1.00127.66           C  
ATOM   1702  NH1 ARG B  94      35.772  26.208 -52.910  1.00128.85           N  
ATOM   1703  NH2 ARG B  94      36.373  24.455 -51.546  1.00127.30           N  
ATOM   1704  N   ASN B  95      29.389  24.352 -57.548  1.00118.10           N  
ATOM   1705  CA  ASN B  95      28.237  25.110 -58.072  1.00118.20           C  
ATOM   1706  C   ASN B  95      27.012  24.246 -58.426  1.00117.39           C  
ATOM   1707  O   ASN B  95      25.926  24.776 -58.669  1.00115.71           O  
ATOM   1708  CB  ASN B  95      28.650  25.966 -59.275  1.00117.50           C  
ATOM   1709  CG  ASN B  95      29.533  27.137 -58.880  1.00117.98           C  
ATOM   1710  OD1 ASN B  95      30.688  26.957 -58.488  1.00119.11           O  
ATOM   1711  ND2 ASN B  95      28.992  28.348 -58.982  1.00116.34           N  
ATOM   1712  N   SER B  96      27.200  22.927 -58.463  1.00118.93           N  
ATOM   1713  CA  SER B  96      26.093  21.967 -58.569  1.00119.11           C  
ATOM   1714  C   SER B  96      25.444  21.665 -57.203  1.00121.75           C  
ATOM   1715  O   SER B  96      24.324  21.151 -57.153  1.00127.22           O  
ATOM   1716  CB  SER B  96      26.581  20.664 -59.224  1.00117.31           C  
ATOM   1717  OG  SER B  96      25.656  19.601 -59.053  1.00114.40           O  
ATOM   1718  N   VAL B  97      26.139  21.974 -56.105  1.00121.80           N  
ATOM   1719  CA  VAL B  97      25.599  21.743 -54.760  1.00120.47           C  
ATOM   1720  C   VAL B  97      24.814  22.963 -54.274  1.00124.15           C  
ATOM   1721  O   VAL B  97      23.800  22.810 -53.596  1.00127.57           O  
ATOM   1722  CB  VAL B  97      26.705  21.362 -53.731  1.00117.81           C  
ATOM   1723  CG1 VAL B  97      27.302  22.597 -53.065  1.00116.79           C  
ATOM   1724  CG2 VAL B  97      26.150  20.419 -52.674  1.00114.93           C  
ATOM   1725  N   ASP B  98      25.272  24.165 -54.631  1.00125.68           N  
ATOM   1726  CA  ASP B  98      24.574  25.399 -54.238  1.00126.55           C  
ATOM   1727  C   ASP B  98      23.296  25.596 -55.060  1.00129.08           C  
ATOM   1728  O   ASP B  98      22.367  26.265 -54.602  1.00131.12           O  
ATOM   1729  CB  ASP B  98      25.505  26.634 -54.295  1.00126.04           C  
ATOM   1730  CG  ASP B  98      25.426  27.401 -55.620  1.00126.21           C  
ATOM   1731  OD1 ASP B  98      26.482  27.585 -56.266  1.00125.01           O  
ATOM   1732  OD2 ASP B  98      24.325  27.852 -56.001  1.00125.93           O  
ATOM   1733  N   GLU B  99      23.254  25.018 -56.264  1.00131.31           N  
ATOM   1734  CA  GLU B  99      22.024  24.990 -57.065  1.00133.99           C  
ATOM   1735  C   GLU B  99      21.064  23.911 -56.538  1.00132.60           C  
ATOM   1736  O   GLU B  99      19.845  24.100 -56.571  1.00133.56           O  
ATOM   1737  CB  GLU B  99      22.320  24.824 -58.572  1.00137.36           C  
ATOM   1738  CG  GLU B  99      22.435  23.380 -59.112  1.00141.79           C  
ATOM   1739  CD  GLU B  99      21.115  22.793 -59.635  1.00145.69           C  
ATOM   1740  OE1 GLU B  99      20.043  23.417 -59.464  1.00148.86           O  
ATOM   1741  OE2 GLU B  99      21.153  21.690 -60.224  1.00147.47           O  
ATOM   1742  N   LEU B 100      21.610  22.792 -56.053  1.00128.98           N  
ATOM   1743  CA  LEU B 100      20.795  21.776 -55.375  1.00126.84           C  
ATOM   1744  C   LEU B 100      20.243  22.335 -54.065  1.00129.39           C  
ATOM   1745  O   LEU B 100      19.056  22.194 -53.784  1.00133.29           O  
ATOM   1746  CB  LEU B 100      21.580  20.481 -55.107  1.00123.66           C  
ATOM   1747  CG  LEU B 100      21.414  19.327 -56.104  1.00121.92           C  
ATOM   1748  CD1 LEU B 100      22.173  18.111 -55.611  1.00120.45           C  
ATOM   1749  CD2 LEU B 100      19.950  18.968 -56.320  1.00120.75           C  
ATOM   1750  N   ASN B 101      21.102  22.981 -53.280  1.00130.36           N  
ATOM   1751  CA  ASN B 101      20.689  23.571 -52.001  1.00132.31           C  
ATOM   1752  C   ASN B 101      19.651  24.687 -52.149  1.00132.95           C  
ATOM   1753  O   ASN B 101      18.554  24.575 -51.608  1.00136.63           O  
ATOM   1754  CB  ASN B 101      21.900  24.088 -51.216  1.00132.74           C  
ATOM   1755  CG  ASN B 101      22.779  22.970 -50.702  1.00132.66           C  
ATOM   1756  OD1 ASN B 101      22.741  21.856 -51.214  1.00134.19           O  
ATOM   1757  ND2 ASN B 101      23.583  23.265 -49.688  1.00132.00           N  
ATOM   1758  N   ASN B 102      19.981  25.747 -52.890  1.00133.03           N  
ATOM   1759  CA  ASN B 102      19.057  26.886 -53.047  1.00133.21           C  
ATOM   1760  C   ASN B 102      17.762  26.541 -53.815  1.00134.05           C  
ATOM   1761  O   ASN B 102      16.874  27.387 -53.949  1.00136.14           O  
ATOM   1762  CB  ASN B 102      19.765  28.110 -53.664  1.00133.39           C  
ATOM   1763  CG  ASN B 102      19.789  28.087 -55.188  1.00133.92           C  
ATOM   1764  OD1 ASN B 102      19.811  27.027 -55.810  1.00134.55           O  
ATOM   1765  ND2 ASN B 102      19.790  29.271 -55.793  1.00133.58           N  
ATOM   1766  N   ASN B 103      17.682  25.316 -54.343  1.00133.20           N  
ATOM   1767  CA  ASN B 103      16.407  24.730 -54.763  1.00131.43           C  
ATOM   1768  C   ASN B 103      15.830  23.826 -53.673  1.00132.61           C  
ATOM   1769  O   ASN B 103      14.758  24.112 -53.150  1.00138.18           O  
ATOM   1770  CB  ASN B 103      16.550  23.944 -56.074  1.00128.60           C  
ATOM   1771  CG  ASN B 103      16.482  24.833 -57.306  1.00126.58           C  
ATOM   1772  OD1 ASN B 103      16.122  26.011 -57.226  1.00123.89           O  
ATOM   1773  ND2 ASN B 103      16.820  24.264 -58.458  1.00125.06           N  
ATOM   1774  N   VAL B 104      16.547  22.755 -53.321  1.00131.86           N  
ATOM   1775  CA  VAL B 104      16.065  21.758 -52.339  1.00131.69           C  
ATOM   1776  C   VAL B 104      15.381  22.368 -51.107  1.00136.38           C  
ATOM   1777  O   VAL B 104      14.304  21.924 -50.721  1.00137.95           O  
ATOM   1778  CB  VAL B 104      17.204  20.809 -51.857  1.00128.20           C  
ATOM   1779  CG1 VAL B 104      16.793  20.041 -50.610  1.00125.60           C  
ATOM   1780  CG2 VAL B 104      17.584  19.833 -52.948  1.00128.78           C  
ATOM   1781  N   GLU B 105      16.003  23.383 -50.503  1.00140.72           N  
ATOM   1782  CA  GLU B 105      15.481  24.014 -49.272  1.00142.16           C  
ATOM   1783  C   GLU B 105      14.779  25.368 -49.488  1.00141.30           C  
ATOM   1784  O   GLU B 105      13.950  25.752 -48.672  1.00138.98           O  
ATOM   1785  CB  GLU B 105      16.598  24.166 -48.222  1.00143.71           C  
ATOM   1786  CG  GLU B 105      16.544  23.163 -47.056  1.00144.12           C  
ATOM   1787  CD  GLU B 105      16.754  21.713 -47.480  1.00144.40           C  
ATOM   1788  OE1 GLU B 105      17.859  21.174 -47.245  1.00143.82           O  
ATOM   1789  OE2 GLU B 105      15.815  21.107 -48.040  1.00143.85           O  
ATOM   1790  N   ALA B 106      15.119  26.098 -50.549  1.00141.71           N  
ATOM   1791  CA  ALA B 106      14.391  27.327 -50.891  1.00142.18           C  
ATOM   1792  C   ALA B 106      13.090  27.016 -51.637  1.00143.14           C  
ATOM   1793  O   ALA B 106      12.178  27.845 -51.655  1.00144.20           O  
ATOM   1794  CB  ALA B 106      15.262  28.266 -51.709  1.00142.37           C  
ATOM   1795  N   VAL B 107      13.015  25.829 -52.249  1.00143.55           N  
ATOM   1796  CA  VAL B 107      11.804  25.366 -52.946  1.00145.11           C  
ATOM   1797  C   VAL B 107      10.998  24.361 -52.109  1.00143.41           C  
ATOM   1798  O   VAL B 107       9.784  24.522 -51.966  1.00145.48           O  
ATOM   1799  CB  VAL B 107      12.129  24.744 -54.329  1.00147.18           C  
ATOM   1800  CG1 VAL B 107      10.845  24.398 -55.076  1.00148.47           C  
ATOM   1801  CG2 VAL B 107      12.985  25.701 -55.159  1.00148.14           C  
ATOM   1802  N   SER B 108      11.656  23.339 -51.554  1.00140.81           N  
ATOM   1803  CA  SER B 108      10.966  22.373 -50.676  1.00141.10           C  
ATOM   1804  C   SER B 108      10.714  22.926 -49.260  1.00143.81           C  
ATOM   1805  O   SER B 108      10.253  22.193 -48.382  1.00146.13           O  
ATOM   1806  CB  SER B 108      11.719  21.037 -50.596  1.00138.61           C  
ATOM   1807  OG  SER B 108      10.877  19.997 -50.122  1.00136.07           O  
ATOM   1808  N   GLN B 109      11.043  24.203 -49.041  1.00145.41           N  
ATOM   1809  CA  GLN B 109      10.554  24.963 -47.881  1.00144.21           C  
ATOM   1810  C   GLN B 109       9.073  25.307 -48.058  1.00146.62           C  
ATOM   1811  O   GLN B 109       8.344  25.415 -47.073  1.00151.65           O  
ATOM   1812  CB  GLN B 109      11.388  26.238 -47.661  1.00142.03           C  
ATOM   1813  CG  GLN B 109      10.792  27.297 -46.722  1.00138.55           C  
ATOM   1814  CD  GLN B 109       9.945  28.339 -47.443  1.00136.08           C  
ATOM   1815  OE1 GLN B 109      10.269  28.770 -48.551  1.00132.07           O  
ATOM   1816  NE2 GLN B 109       8.861  28.757 -46.803  1.00135.90           N  
ATOM   1817  N   THR B 110       8.636  25.488 -49.307  1.00146.60           N  
ATOM   1818  CA  THR B 110       7.212  25.703 -49.603  1.00145.66           C  
ATOM   1819  C   THR B 110       6.463  24.381 -49.439  1.00145.67           C  
ATOM   1820  O   THR B 110       5.366  24.344 -48.879  1.00148.61           O  
ATOM   1821  CB  THR B 110       6.961  26.252 -51.030  1.00144.36           C  
ATOM   1822  OG1 THR B 110       6.929  25.170 -51.970  1.00144.97           O  
ATOM   1823  CG2 THR B 110       8.029  27.269 -51.434  1.00142.83           C  
ATOM   1824  N   SER B 111       7.065  23.301 -49.937  1.00145.48           N  
ATOM   1825  CA  SER B 111       6.604  21.946 -49.635  1.00145.48           C  
ATOM   1826  C   SER B 111       6.620  21.719 -48.123  1.00147.80           C  
ATOM   1827  O   SER B 111       5.658  21.199 -47.560  1.00151.21           O  
ATOM   1828  CB  SER B 111       7.489  20.905 -50.330  1.00144.11           C  
ATOM   1829  OG  SER B 111       7.121  19.585 -49.968  1.00141.05           O  
ATOM   1830  N   SER B 112       7.713  22.119 -47.473  1.00150.01           N  
ATOM   1831  CA  SER B 112       7.828  22.027 -46.012  1.00151.93           C  
ATOM   1832  C   SER B 112       6.807  22.919 -45.278  1.00154.10           C  
ATOM   1833  O   SER B 112       6.275  22.530 -44.233  1.00155.44           O  
ATOM   1834  CB  SER B 112       9.257  22.352 -45.551  1.00150.47           C  
ATOM   1835  OG  SER B 112      10.200  21.430 -46.082  1.00147.03           O  
ATOM   1836  N   SER B 113       6.533  24.101 -45.833  1.00153.45           N  
ATOM   1837  CA  SER B 113       5.559  25.039 -45.256  1.00150.65           C  
ATOM   1838  C   SER B 113       4.124  24.517 -45.307  1.00150.88           C  
ATOM   1839  O   SER B 113       3.276  24.980 -44.545  1.00153.95           O  
ATOM   1840  CB  SER B 113       5.625  26.395 -45.970  1.00148.84           C  
ATOM   1841  OG  SER B 113       4.582  27.255 -45.543  1.00147.64           O  
ATOM   1842  N   SER B 114       3.854  23.573 -46.210  1.00151.38           N  
ATOM   1843  CA  SER B 114       2.524  22.971 -46.334  1.00152.86           C  
ATOM   1844  C   SER B 114       2.438  21.553 -45.740  1.00155.66           C  
ATOM   1845  O   SER B 114       1.348  20.980 -45.686  1.00156.11           O  
ATOM   1846  CB  SER B 114       2.066  22.974 -47.798  1.00151.02           C  
ATOM   1847  OG  SER B 114       1.689  24.278 -48.210  1.00149.21           O  
ATOM   1848  N   PHE B 115       3.566  20.994 -45.287  1.00159.19           N  
ATOM   1849  CA  PHE B 115       3.536  19.736 -44.511  1.00166.21           C  
ATOM   1850  C   PHE B 115       2.747  19.950 -43.205  1.00167.05           C  
ATOM   1851  O   PHE B 115       2.100  19.024 -42.702  1.00166.06           O  
ATOM   1852  CB  PHE B 115       4.951  19.224 -44.142  1.00170.72           C  
ATOM   1853  CG  PHE B 115       5.808  18.759 -45.318  1.00173.93           C  
ATOM   1854  CD1 PHE B 115       5.256  18.229 -46.485  1.00175.81           C  
ATOM   1855  CD2 PHE B 115       7.196  18.804 -45.212  1.00174.75           C  
ATOM   1856  CE1 PHE B 115       6.078  17.800 -47.536  1.00175.18           C  
ATOM   1857  CE2 PHE B 115       8.017  18.379 -46.254  1.00175.11           C  
ATOM   1858  CZ  PHE B 115       7.459  17.877 -47.415  1.00174.59           C  
ATOM   1859  N   GLN B 116       2.822  21.175 -42.673  1.00168.39           N  
ATOM   1860  CA  GLN B 116       2.192  21.552 -41.394  1.00167.56           C  
ATOM   1861  C   GLN B 116       0.794  22.172 -41.528  1.00167.38           C  
ATOM   1862  O   GLN B 116       0.168  22.506 -40.518  1.00170.77           O  
ATOM   1863  CB  GLN B 116       3.109  22.497 -40.585  1.00167.21           C  
ATOM   1864  CG  GLN B 116       3.583  23.794 -41.294  1.00166.15           C  
ATOM   1865  CD  GLN B 116       2.542  24.913 -41.332  1.00165.07           C  
ATOM   1866  OE1 GLN B 116       1.645  24.983 -40.492  1.00165.58           O  
ATOM   1867  NE2 GLN B 116       2.677  25.805 -42.306  1.00161.40           N  
ATOM   1868  N   TYR B 117       0.302  22.326 -42.757  1.00164.05           N  
ATOM   1869  CA  TYR B 117      -1.074  22.795 -42.978  1.00162.38           C  
ATOM   1870  C   TYR B 117      -2.109  21.782 -42.460  1.00163.00           C  
ATOM   1871  O   TYR B 117      -3.255  22.148 -42.209  1.00164.47           O  
ATOM   1872  CB  TYR B 117      -1.321  23.113 -44.466  1.00159.10           C  
ATOM   1873  CG  TYR B 117      -0.983  24.538 -44.899  1.00154.15           C  
ATOM   1874  CD1 TYR B 117       0.035  25.270 -44.280  1.00150.90           C  
ATOM   1875  CD2 TYR B 117      -1.670  25.141 -45.953  1.00149.94           C  
ATOM   1876  CE1 TYR B 117       0.340  26.567 -44.688  1.00147.75           C  
ATOM   1877  CE2 TYR B 117      -1.368  26.434 -46.368  1.00146.74           C  
ATOM   1878  CZ  TYR B 117      -0.365  27.139 -45.733  1.00145.89           C  
ATOM   1879  OH  TYR B 117      -0.073  28.417 -46.145  1.00141.28           O  
ATOM   1880  N   MET B 118      -1.706  20.521 -42.292  1.00165.02           N  
ATOM   1881  CA  MET B 118      -2.583  19.496 -41.718  1.00165.65           C  
ATOM   1882  C   MET B 118      -3.004  19.825 -40.292  1.00169.19           C  
ATOM   1883  O   MET B 118      -4.195  19.870 -40.004  1.00169.76           O  
ATOM   1884  CB  MET B 118      -1.918  18.114 -41.744  1.00162.96           C  
ATOM   1885  CG  MET B 118      -1.709  17.545 -43.136  1.00162.20           C  
ATOM   1886  SD  MET B 118      -3.214  17.502 -44.132  1.00160.04           S  
ATOM   1887  CE  MET B 118      -3.211  19.141 -44.869  1.00156.40           C  
ATOM   1888  N   TYR B 119      -2.036  20.061 -39.408  1.00173.44           N  
ATOM   1889  CA  TYR B 119      -2.323  20.310 -37.984  1.00177.38           C  
ATOM   1890  C   TYR B 119      -3.432  21.335 -37.738  1.00177.54           C  
ATOM   1891  O   TYR B 119      -4.247  21.155 -36.833  1.00181.39           O  
ATOM   1892  CB  TYR B 119      -1.064  20.755 -37.236  1.00180.34           C  
ATOM   1893  CG  TYR B 119      -0.145  19.622 -36.854  1.00185.14           C  
ATOM   1894  CD1 TYR B 119      -0.339  18.910 -35.672  1.00186.46           C  
ATOM   1895  CD2 TYR B 119       0.925  19.264 -37.669  1.00188.43           C  
ATOM   1896  CE1 TYR B 119       0.507  17.868 -35.314  1.00188.17           C  
ATOM   1897  CE2 TYR B 119       1.777  18.225 -37.321  1.00190.28           C  
ATOM   1898  CZ  TYR B 119       1.562  17.531 -36.141  1.00189.94           C  
ATOM   1899  OH  TYR B 119       2.403  16.501 -35.788  1.00190.84           O  
ATOM   1900  N   LEU B 120      -3.452  22.407 -38.528  1.00175.36           N  
ATOM   1901  CA  LEU B 120      -4.489  23.442 -38.401  1.00173.21           C  
ATOM   1902  C   LEU B 120      -5.747  23.164 -39.254  1.00171.54           C  
ATOM   1903  O   LEU B 120      -6.832  23.656 -38.925  1.00168.97           O  
ATOM   1904  CB  LEU B 120      -3.905  24.831 -38.705  1.00171.59           C  
ATOM   1905  CG  LEU B 120      -3.454  25.144 -40.137  1.00170.72           C  
ATOM   1906  CD1 LEU B 120      -4.586  25.771 -40.935  1.00170.38           C  
ATOM   1907  CD2 LEU B 120      -2.240  26.065 -40.146  1.00168.94           C  
ATOM   1908  N   LEU B 121      -5.605  22.382 -40.331  1.00168.53           N  
ATOM   1909  CA  LEU B 121      -6.746  22.008 -41.189  1.00165.50           C  
ATOM   1910  C   LEU B 121      -7.277  20.591 -40.911  1.00164.25           C  
ATOM   1911  O   LEU B 121      -8.433  20.295 -41.213  1.00162.44           O  
ATOM   1912  CB  LEU B 121      -6.391  22.155 -42.679  1.00164.37           C  
ATOM   1913  CG  LEU B 121      -6.019  23.554 -43.200  1.00163.35           C  
ATOM   1914  CD1 LEU B 121      -5.806  23.536 -44.710  1.00162.83           C  
ATOM   1915  CD2 LEU B 121      -7.067  24.598 -42.838  1.00160.42           C  
ATOM   1916  N   LYS B 122      -6.445  19.718 -40.345  1.00166.45           N  
ATOM   1917  CA  LYS B 122      -6.908  18.396 -39.902  1.00167.03           C  
ATOM   1918  C   LYS B 122      -7.930  18.592 -38.799  1.00166.98           C  
ATOM   1919  O   LYS B 122      -9.061  18.125 -38.905  1.00164.33           O  
ATOM   1920  CB  LYS B 122      -5.752  17.529 -39.384  1.00168.88           C  
ATOM   1921  CG  LYS B 122      -6.179  16.169 -38.830  1.00168.58           C  
ATOM   1922  CD  LYS B 122      -4.976  15.288 -38.554  1.00169.78           C  
ATOM   1923  CE  LYS B 122      -5.397  13.893 -38.138  1.00170.97           C  
ATOM   1924  NZ  LYS B 122      -4.256  12.940 -38.198  1.00172.77           N  
ATOM   1925  N   ASP B 123      -7.515  19.295 -37.746  1.00169.34           N  
ATOM   1926  CA  ASP B 123      -8.389  19.626 -36.618  1.00171.81           C  
ATOM   1927  C   ASP B 123      -9.733  20.182 -37.085  1.00170.93           C  
ATOM   1928  O   ASP B 123     -10.784  19.718 -36.641  1.00169.20           O  
ATOM   1929  CB  ASP B 123      -7.704  20.633 -35.683  1.00173.57           C  
ATOM   1930  CG  ASP B 123      -6.615  20.000 -34.833  1.00175.33           C  
ATOM   1931  OD1 ASP B 123      -6.274  18.818 -35.068  1.00178.43           O  
ATOM   1932  OD2 ASP B 123      -6.098  20.687 -33.926  1.00176.17           O  
ATOM   1933  N   LEU B 124      -9.691  21.158 -37.991  1.00167.58           N  
ATOM   1934  CA  LEU B 124     -10.907  21.764 -38.535  1.00162.31           C  
ATOM   1935  C   LEU B 124     -11.790  20.729 -39.240  1.00162.04           C  
ATOM   1936  O   LEU B 124     -13.016  20.811 -39.173  1.00161.63           O  
ATOM   1937  CB  LEU B 124     -10.557  22.911 -39.484  1.00158.90           C  
ATOM   1938  CG  LEU B 124     -11.733  23.809 -39.868  1.00156.83           C  
ATOM   1939  CD1 LEU B 124     -11.268  25.245 -40.076  1.00155.13           C  
ATOM   1940  CD2 LEU B 124     -12.445  23.272 -41.104  1.00155.75           C  
ATOM   1941  N   TRP B 125     -11.169  19.758 -39.907  1.00162.66           N  
ATOM   1942  CA  TRP B 125     -11.906  18.624 -40.459  1.00163.28           C  
ATOM   1943  C   TRP B 125     -12.368  17.709 -39.333  1.00159.76           C  
ATOM   1944  O   TRP B 125     -13.484  17.212 -39.355  1.00157.34           O  
ATOM   1945  CB  TRP B 125     -11.053  17.836 -41.455  1.00168.41           C  
ATOM   1946  CG  TRP B 125     -11.748  16.617 -41.992  1.00173.88           C  
ATOM   1947  CD1 TRP B 125     -11.371  15.315 -41.823  1.00175.89           C  
ATOM   1948  CD2 TRP B 125     -12.952  16.589 -42.771  1.00177.01           C  
ATOM   1949  NE1 TRP B 125     -12.260  14.479 -42.455  1.00177.48           N  
ATOM   1950  CE2 TRP B 125     -13.240  15.234 -43.045  1.00177.74           C  
ATOM   1951  CE3 TRP B 125     -13.813  17.577 -43.267  1.00177.03           C  
ATOM   1952  CZ2 TRP B 125     -14.354  14.841 -43.794  1.00177.04           C  
ATOM   1953  CZ3 TRP B 125     -14.920  17.184 -44.009  1.00176.36           C  
ATOM   1954  CH2 TRP B 125     -15.178  15.829 -44.266  1.00176.48           C  
ATOM   1955  N   GLN B 126     -11.502  17.498 -38.345  1.00160.11           N  
ATOM   1956  CA  GLN B 126     -11.845  16.676 -37.182  1.00159.97           C  
ATOM   1957  C   GLN B 126     -12.669  17.450 -36.140  1.00159.77           C  
ATOM   1958  O   GLN B 126     -13.027  16.890 -35.105  1.00161.85           O  
ATOM   1959  CB  GLN B 126     -10.581  16.106 -36.513  1.00159.56           C  
ATOM   1960  CG  GLN B 126      -9.605  15.356 -37.436  1.00160.13           C  
ATOM   1961  CD  GLN B 126     -10.145  14.045 -37.994  1.00160.60           C  
ATOM   1962  OE1 GLN B 126     -11.351  13.792 -38.001  1.00158.59           O  
ATOM   1963  NE2 GLN B 126      -9.237  13.205 -38.481  1.00160.10           N  
ATOM   1964  N   LYS B 127     -12.960  18.725 -36.407  1.00159.80           N  
ATOM   1965  CA  LYS B 127     -13.774  19.556 -35.512  1.00157.70           C  
ATOM   1966  C   LYS B 127     -15.177  19.796 -36.074  1.00156.27           C  
ATOM   1967  O   LYS B 127     -16.164  19.376 -35.473  1.00152.15           O  
ATOM   1968  CB  LYS B 127     -13.092  20.904 -35.247  1.00158.95           C  
ATOM   1969  CG  LYS B 127     -12.092  20.896 -34.092  1.00159.04           C  
ATOM   1970  CD  LYS B 127     -11.051  22.022 -34.193  1.00159.33           C  
ATOM   1971  CE  LYS B 127     -11.637  23.380 -34.596  1.00159.23           C  
ATOM   1972  NZ  LYS B 127     -12.837  23.768 -33.811  1.00158.73           N  
ATOM   1973  N   ARG B 128     -15.261  20.474 -37.220  1.00156.72           N  
ATOM   1974  CA  ARG B 128     -16.561  20.845 -37.806  1.00154.69           C  
ATOM   1975  C   ARG B 128     -17.360  19.653 -38.328  1.00153.68           C  
ATOM   1976  O   ARG B 128     -18.587  19.646 -38.229  1.00153.42           O  
ATOM   1977  CB  ARG B 128     -16.412  21.885 -38.926  1.00154.34           C  
ATOM   1978  CG  ARG B 128     -16.700  23.318 -38.491  1.00154.32           C  
ATOM   1979  CD  ARG B 128     -17.415  24.115 -39.579  1.00153.64           C  
ATOM   1980  NE  ARG B 128     -18.853  23.840 -39.623  1.00152.58           N  
ATOM   1981  CZ  ARG B 128     -19.736  24.524 -40.350  1.00151.11           C  
ATOM   1982  NH1 ARG B 128     -19.350  25.543 -41.115  1.00151.52           N  
ATOM   1983  NH2 ARG B 128     -21.020  24.187 -40.316  1.00149.49           N  
ATOM   1984  N   GLN B 129     -16.673  18.665 -38.898  1.00153.12           N  
ATOM   1985  CA  GLN B 129     -17.316  17.403 -39.279  1.00153.41           C  
ATOM   1986  C   GLN B 129     -17.778  16.639 -38.035  1.00153.92           C  
ATOM   1987  O   GLN B 129     -18.741  15.878 -38.107  1.00158.26           O  
ATOM   1988  CB  GLN B 129     -16.375  16.540 -40.140  1.00154.37           C  
ATOM   1989  CG  GLN B 129     -16.730  15.046 -40.268  1.00154.36           C  
ATOM   1990  CD  GLN B 129     -16.036  14.166 -39.226  1.00153.88           C  
ATOM   1991  OE1 GLN B 129     -14.834  14.298 -38.979  1.00153.14           O  
ATOM   1992  NE2 GLN B 129     -16.792  13.253 -38.628  1.00151.65           N  
ATOM   1993  N   LYS B 130     -17.102  16.848 -36.903  1.00151.79           N  
ATOM   1994  CA  LYS B 130     -17.453  16.161 -35.655  1.00150.37           C  
ATOM   1995  C   LYS B 130     -18.351  16.989 -34.721  1.00148.69           C  
ATOM   1996  O   LYS B 130     -18.932  16.448 -33.776  1.00147.53           O  
ATOM   1997  CB  LYS B 130     -16.187  15.714 -34.920  1.00150.17           C  
ATOM   1998  CG  LYS B 130     -15.320  14.746 -35.720  1.00148.15           C  
ATOM   1999  CD  LYS B 130     -14.392  13.949 -34.815  1.00147.19           C  
ATOM   2000  CE  LYS B 130     -13.239  13.352 -35.592  1.00145.92           C  
ATOM   2001  NZ  LYS B 130     -12.393  12.466 -34.751  1.00145.73           N  
ATOM   2002  N   GLN B 131     -18.463  18.290 -34.980  1.00148.36           N  
ATOM   2003  CA  GLN B 131     -19.408  19.141 -34.248  1.00146.72           C  
ATOM   2004  C   GLN B 131     -20.820  18.941 -34.798  1.00146.51           C  
ATOM   2005  O   GLN B 131     -21.790  18.959 -34.043  1.00144.20           O  
ATOM   2006  CB  GLN B 131     -18.994  20.620 -34.331  1.00144.64           C  
ATOM   2007  CG  GLN B 131     -19.666  21.543 -33.302  1.00140.39           C  
ATOM   2008  CD  GLN B 131     -21.004  22.101 -33.757  1.00137.69           C  
ATOM   2009  OE1 GLN B 131     -21.415  21.923 -34.903  1.00135.97           O  
ATOM   2010  NE2 GLN B 131     -21.686  22.790 -32.853  1.00138.48           N  
ATOM   2011  N   VAL B 132     -20.921  18.738 -36.113  1.00150.54           N  
ATOM   2012  CA  VAL B 132     -22.216  18.599 -36.796  1.00153.33           C  
ATOM   2013  C   VAL B 132     -22.818  17.175 -36.777  1.00154.97           C  
ATOM   2014  O   VAL B 132     -24.014  17.013 -37.038  1.00153.06           O  
ATOM   2015  CB  VAL B 132     -22.142  19.098 -38.266  1.00153.91           C  
ATOM   2016  CG1 VAL B 132     -21.642  20.542 -38.318  1.00152.42           C  
ATOM   2017  CG2 VAL B 132     -21.264  18.182 -39.113  1.00155.59           C  
ATOM   2018  N   LYS B 133     -22.006  16.156 -36.480  1.00156.96           N  
ATOM   2019  CA  LYS B 133     -22.501  14.768 -36.383  1.00158.28           C  
ATOM   2020  C   LYS B 133     -23.097  14.447 -35.008  1.00158.19           C  
ATOM   2021  O   LYS B 133     -23.896  13.515 -34.883  1.00160.44           O  
ATOM   2022  CB  LYS B 133     -21.404  13.749 -36.738  1.00160.11           C  
ATOM   2023  CG  LYS B 133     -20.385  13.446 -35.628  1.00161.10           C  
ATOM   2024  CD  LYS B 133     -19.213  12.623 -36.172  1.00160.00           C  
ATOM   2025  CE  LYS B 133     -18.133  12.390 -35.122  1.00158.44           C  
ATOM   2026  NZ  LYS B 133     -16.935  11.718 -35.699  1.00155.96           N  
ATOM   2027  N   ASP B 134     -22.692  15.196 -33.980  1.00155.68           N  
ATOM   2028  CA  ASP B 134     -23.346  15.120 -32.673  1.00151.76           C  
ATOM   2029  C   ASP B 134     -24.447  16.185 -32.580  1.00149.94           C  
ATOM   2030  O   ASP B 134     -25.488  15.934 -31.977  1.00151.19           O  
ATOM   2031  CB  ASP B 134     -22.334  15.263 -31.528  1.00149.54           C  
ATOM   2032  CG  ASP B 134     -22.721  14.451 -30.292  1.00147.01           C  
ATOM   2033  OD1 ASP B 134     -23.338  13.371 -30.439  1.00142.12           O  
ATOM   2034  OD2 ASP B 134     -22.396  14.888 -29.168  1.00146.46           O  
ATOM   2035  N   ASN B 135     -24.223  17.357 -33.185  1.00145.23           N  
ATOM   2036  CA  ASN B 135     -25.291  18.354 -33.388  1.00142.81           C  
ATOM   2037  C   ASN B 135     -26.517  17.711 -34.037  1.00141.65           C  
ATOM   2038  O   ASN B 135     -27.648  18.113 -33.768  1.00138.71           O  
ATOM   2039  CB  ASN B 135     -24.788  19.531 -34.243  1.00143.50           C  
ATOM   2040  CG  ASN B 135     -25.831  20.640 -34.424  1.00142.47           C  
ATOM   2041  OD1 ASN B 135     -26.872  20.436 -35.049  1.00139.69           O  
ATOM   2042  ND2 ASN B 135     -25.533  21.828 -33.900  1.00141.89           N  
ATOM   2043  N   GLU B 136     -26.287  16.716 -34.893  1.00144.62           N  
ATOM   2044  CA  GLU B 136     -27.373  15.886 -35.403  1.00145.89           C  
ATOM   2045  C   GLU B 136     -28.110  15.197 -34.252  1.00145.48           C  
ATOM   2046  O   GLU B 136     -29.258  15.519 -33.976  1.00144.84           O  
ATOM   2047  CB  GLU B 136     -26.862  14.837 -36.401  1.00147.84           C  
ATOM   2048  CG  GLU B 136     -27.966  13.922 -36.953  1.00151.39           C  
ATOM   2049  CD  GLU B 136     -27.431  12.653 -37.590  1.00153.33           C  
ATOM   2050  OE1 GLU B 136     -26.587  12.753 -38.506  1.00155.74           O  
ATOM   2051  OE2 GLU B 136     -27.866  11.554 -37.180  1.00154.32           O  
ATOM   2052  N   ASN B 137     -27.450  14.259 -33.578  1.00143.64           N  
ATOM   2053  CA  ASN B 137     -28.128  13.437 -32.573  1.00142.97           C  
ATOM   2054  C   ASN B 137     -28.394  14.146 -31.236  1.00142.80           C  
ATOM   2055  O   ASN B 137     -29.275  13.719 -30.488  1.00140.43           O  
ATOM   2056  CB  ASN B 137     -27.365  12.124 -32.343  1.00142.34           C  
ATOM   2057  CG  ASN B 137     -27.379  11.218 -33.566  1.00141.49           C  
ATOM   2058  OD1 ASN B 137     -26.602  11.406 -34.499  1.00140.57           O  
ATOM   2059  ND2 ASN B 137     -28.262  10.227 -33.561  1.00141.37           N  
ATOM   2060  N   VAL B 138     -27.661  15.227 -30.949  1.00146.27           N  
ATOM   2061  CA  VAL B 138     -27.794  15.953 -29.665  1.00147.95           C  
ATOM   2062  C   VAL B 138     -28.563  17.288 -29.804  1.00148.67           C  
ATOM   2063  O   VAL B 138     -29.622  17.452 -29.190  1.00147.42           O  
ATOM   2064  CB  VAL B 138     -26.399  16.131 -28.929  1.00147.55           C  
ATOM   2065  CG1 VAL B 138     -25.640  17.387 -29.381  1.00145.53           C  
ATOM   2066  CG2 VAL B 138     -26.581  16.145 -27.412  1.00143.69           C  
ATOM   2067  N   VAL B 139     -28.057  18.218 -30.621  1.00147.52           N  
ATOM   2068  CA  VAL B 139     -28.695  19.535 -30.804  1.00141.94           C  
ATOM   2069  C   VAL B 139     -29.986  19.373 -31.610  1.00137.92           C  
ATOM   2070  O   VAL B 139     -30.897  20.199 -31.514  1.00130.65           O  
ATOM   2071  CB  VAL B 139     -27.748  20.557 -31.502  1.00141.66           C  
ATOM   2072  CG1 VAL B 139     -28.416  21.926 -31.642  1.00138.96           C  
ATOM   2073  CG2 VAL B 139     -26.434  20.688 -30.738  1.00140.61           C  
ATOM   2074  N   ASN B 140     -30.048  18.299 -32.397  1.00138.23           N  
ATOM   2075  CA  ASN B 140     -31.264  17.904 -33.098  1.00139.55           C  
ATOM   2076  C   ASN B 140     -31.843  16.584 -32.588  1.00140.88           C  
ATOM   2077  O   ASN B 140     -31.337  15.501 -32.892  1.00138.35           O  
ATOM   2078  CB  ASN B 140     -31.015  17.798 -34.606  1.00139.25           C  
ATOM   2079  CG  ASN B 140     -31.967  16.821 -35.287  1.00137.73           C  
ATOM   2080  OD1 ASN B 140     -33.161  17.088 -35.408  1.00135.60           O  
ATOM   2081  ND2 ASN B 140     -31.443  15.678 -35.717  1.00139.64           N  
ATOM   2082  N   GLU B 141     -32.894  16.689 -31.786  1.00143.71           N  
ATOM   2083  CA  GLU B 141     -33.845  15.586 -31.628  1.00142.37           C  
ATOM   2084  C   GLU B 141     -35.206  16.046 -31.092  1.00143.11           C  
ATOM   2085  O   GLU B 141     -36.059  15.203 -30.803  1.00138.29           O  
ATOM   2086  CB  GLU B 141     -33.265  14.460 -30.749  1.00138.41           C  
ATOM   2087  CG  GLU B 141     -33.691  13.029 -31.133  1.00130.90           C  
ATOM   2088  CD  GLU B 141     -33.228  12.603 -32.528  1.00126.67           C  
ATOM   2089  OE1 GLU B 141     -32.424  11.655 -32.620  1.00125.47           O  
ATOM   2090  OE2 GLU B 141     -33.659  13.204 -33.534  1.00123.24           O  
ATOM   2091  N   TYR B 142     -35.423  17.361 -30.972  1.00146.27           N  
ATOM   2092  CA  TYR B 142     -36.735  17.856 -30.568  1.00151.29           C  
ATOM   2093  C   TYR B 142     -37.719  17.725 -31.717  1.00151.36           C  
ATOM   2094  O   TYR B 142     -38.872  17.378 -31.487  1.00152.21           O  
ATOM   2095  CB  TYR B 142     -36.717  19.281 -29.972  1.00155.93           C  
ATOM   2096  CG  TYR B 142     -36.228  20.429 -30.842  1.00159.88           C  
ATOM   2097  CD1 TYR B 142     -35.033  21.084 -30.539  1.00162.79           C  
ATOM   2098  CD2 TYR B 142     -36.984  20.906 -31.917  1.00159.12           C  
ATOM   2099  CE1 TYR B 142     -34.580  22.153 -31.300  1.00162.92           C  
ATOM   2100  CE2 TYR B 142     -36.536  21.977 -32.688  1.00160.80           C  
ATOM   2101  CZ  TYR B 142     -35.331  22.595 -32.371  1.00162.38           C  
ATOM   2102  OH  TYR B 142     -34.865  23.656 -33.115  1.00161.14           O  
ATOM   2103  N   SER B 143     -37.261  17.952 -32.948  1.00149.52           N  
ATOM   2104  CA  SER B 143     -38.106  17.722 -34.125  1.00152.36           C  
ATOM   2105  C   SER B 143     -38.643  16.280 -34.156  1.00154.39           C  
ATOM   2106  O   SER B 143     -39.822  16.056 -34.448  1.00159.56           O  
ATOM   2107  CB  SER B 143     -37.346  18.014 -35.421  1.00151.56           C  
ATOM   2108  OG  SER B 143     -36.560  16.901 -35.817  1.00150.91           O  
ATOM   2109  N   SER B 144     -37.773  15.315 -33.853  1.00150.64           N  
ATOM   2110  CA  SER B 144     -38.157  13.897 -33.790  1.00144.37           C  
ATOM   2111  C   SER B 144     -39.106  13.609 -32.620  1.00140.62           C  
ATOM   2112  O   SER B 144     -40.096  12.887 -32.774  1.00138.86           O  
ATOM   2113  CB  SER B 144     -36.910  13.012 -33.694  1.00142.08           C  
ATOM   2114  OG  SER B 144     -35.993  13.529 -32.750  1.00135.39           O  
ATOM   2115  N   GLU B 145     -38.799  14.182 -31.459  1.00137.04           N  
ATOM   2116  CA  GLU B 145     -39.666  14.080 -30.285  1.00135.60           C  
ATOM   2117  C   GLU B 145     -41.013  14.784 -30.508  1.00135.02           C  
ATOM   2118  O   GLU B 145     -42.016  14.401 -29.905  1.00136.81           O  
ATOM   2119  CB  GLU B 145     -38.952  14.657 -29.057  1.00134.70           C  
ATOM   2120  CG  GLU B 145     -39.598  14.319 -27.718  1.00134.41           C  
ATOM   2121  CD  GLU B 145     -40.731  15.254 -27.349  1.00136.76           C  
ATOM   2122  OE1 GLU B 145     -40.619  16.472 -27.615  1.00137.05           O  
ATOM   2123  OE2 GLU B 145     -41.737  14.767 -26.792  1.00139.80           O  
ATOM   2124  N   LEU B 146     -41.031  15.798 -31.376  1.00135.58           N  
ATOM   2125  CA  LEU B 146     -42.262  16.531 -31.699  1.00128.85           C  
ATOM   2126  C   LEU B 146     -43.128  15.895 -32.809  1.00131.51           C  
ATOM   2127  O   LEU B 146     -44.093  16.522 -33.248  1.00127.41           O  
ATOM   2128  CB  LEU B 146     -41.959  17.996 -32.066  1.00122.19           C  
ATOM   2129  CG  LEU B 146     -41.271  18.905 -31.034  1.00119.54           C  
ATOM   2130  CD1 LEU B 146     -41.613  20.355 -31.305  1.00118.36           C  
ATOM   2131  CD2 LEU B 146     -41.610  18.541 -29.595  1.00116.38           C  
ATOM   2132  N   GLU B 147     -42.805  14.678 -33.264  1.00136.59           N  
ATOM   2133  CA  GLU B 147     -43.691  13.955 -34.207  1.00139.72           C  
ATOM   2134  C   GLU B 147     -44.676  13.017 -33.493  1.00142.98           C  
ATOM   2135  O   GLU B 147     -45.845  12.936 -33.880  1.00144.24           O  
ATOM   2136  CB  GLU B 147     -42.907  13.181 -35.273  1.00140.29           C  
ATOM   2137  CG  GLU B 147     -43.829  12.442 -36.269  1.00143.09           C  
ATOM   2138  CD  GLU B 147     -43.279  12.344 -37.691  1.00146.40           C  
ATOM   2139  OE1 GLU B 147     -42.533  13.249 -38.128  1.00145.01           O  
ATOM   2140  OE2 GLU B 147     -43.619  11.358 -38.385  1.00149.48           O  
ATOM   2141  N   LYS B 148     -44.205  12.304 -32.470  1.00143.86           N  
ATOM   2142  CA  LYS B 148     -45.098  11.531 -31.593  1.00141.32           C  
ATOM   2143  C   LYS B 148     -45.885  12.481 -30.678  1.00137.35           C  
ATOM   2144  O   LYS B 148     -46.959  12.134 -30.186  1.00137.54           O  
ATOM   2145  CB  LYS B 148     -44.320  10.500 -30.761  1.00142.30           C  
ATOM   2146  CG  LYS B 148     -43.829   9.274 -31.552  1.00142.92           C  
ATOM   2147  CD  LYS B 148     -42.409   9.442 -32.118  1.00142.15           C  
ATOM   2148  CE  LYS B 148     -41.337   9.264 -31.038  1.00140.80           C  
ATOM   2149  NZ  LYS B 148     -39.949   9.282 -31.584  1.00136.92           N  
ATOM   2150  N   HIS B 149     -45.333  13.673 -30.459  1.00132.98           N  
ATOM   2151  CA  HIS B 149     -46.033  14.753 -29.770  1.00130.17           C  
ATOM   2152  C   HIS B 149     -47.238  15.275 -30.562  1.00127.56           C  
ATOM   2153  O   HIS B 149     -48.274  15.569 -29.970  1.00132.62           O  
ATOM   2154  CB  HIS B 149     -45.077  15.910 -29.494  1.00130.29           C  
ATOM   2155  CG  HIS B 149     -45.758  17.144 -29.001  1.00133.64           C  
ATOM   2156  ND1 HIS B 149     -46.529  17.940 -29.820  1.00134.92           N  
ATOM   2157  CD2 HIS B 149     -45.796  17.715 -27.776  1.00136.56           C  
ATOM   2158  CE1 HIS B 149     -47.012  18.949 -29.119  1.00137.57           C  
ATOM   2159  NE2 HIS B 149     -46.587  18.833 -27.874  1.00138.10           N  
ATOM   2160  N   GLN B 150     -47.099  15.426 -31.880  1.00121.75           N  
ATOM   2161  CA  GLN B 150     -48.231  15.840 -32.723  1.00115.45           C  
ATOM   2162  C   GLN B 150     -49.373  14.820 -32.699  1.00116.35           C  
ATOM   2163  O   GLN B 150     -50.533  15.208 -32.808  1.00118.13           O  
ATOM   2164  CB  GLN B 150     -47.802  16.103 -34.177  1.00114.50           C  
ATOM   2165  CG  GLN B 150     -48.978  16.160 -35.180  1.00115.48           C  
ATOM   2166  CD  GLN B 150     -48.594  16.658 -36.572  1.00116.06           C  
ATOM   2167  OE1 GLN B 150     -48.786  15.953 -37.568  1.00116.86           O  
ATOM   2168  NE2 GLN B 150     -48.072  17.880 -36.648  1.00111.96           N  
ATOM   2169  N   LEU B 151     -49.052  13.531 -32.554  1.00117.59           N  
ATOM   2170  CA  LEU B 151     -50.068  12.454 -32.583  1.00117.60           C  
ATOM   2171  C   LEU B 151     -51.132  12.547 -31.476  1.00117.11           C  
ATOM   2172  O   LEU B 151     -52.155  11.852 -31.529  1.00109.93           O  
ATOM   2173  CB  LEU B 151     -49.400  11.075 -32.559  1.00118.75           C  
ATOM   2174  CG  LEU B 151     -48.650  10.694 -33.840  1.00121.00           C  
ATOM   2175  CD1 LEU B 151     -47.888   9.394 -33.634  1.00123.58           C  
ATOM   2176  CD2 LEU B 151     -49.587  10.591 -35.044  1.00120.30           C  
ATOM   2177  N   TYR B 152     -50.872  13.385 -30.471  1.00120.47           N  
ATOM   2178  CA  TYR B 152     -51.925  13.912 -29.597  1.00121.64           C  
ATOM   2179  C   TYR B 152     -52.888  14.787 -30.404  1.00117.15           C  
ATOM   2180  O   TYR B 152     -54.106  14.655 -30.278  1.00113.69           O  
ATOM   2181  CB  TYR B 152     -51.340  14.772 -28.464  1.00125.45           C  
ATOM   2182  CG  TYR B 152     -51.126  14.072 -27.137  1.00130.61           C  
ATOM   2183  CD1 TYR B 152     -49.889  14.111 -26.499  1.00133.53           C  
ATOM   2184  CD2 TYR B 152     -52.169  13.399 -26.502  1.00133.75           C  
ATOM   2185  CE1 TYR B 152     -49.692  13.486 -25.270  1.00137.38           C  
ATOM   2186  CE2 TYR B 152     -51.983  12.771 -25.270  1.00136.25           C  
ATOM   2187  CZ  TYR B 152     -50.739  12.819 -24.659  1.00137.92           C  
ATOM   2188  OH  TYR B 152     -50.533  12.204 -23.440  1.00135.68           O  
ATOM   2189  N   ILE B 153     -52.326  15.670 -31.232  1.00111.25           N  
ATOM   2190  CA  ILE B 153     -53.095  16.689 -31.969  1.00105.99           C  
ATOM   2191  C   ILE B 153     -53.512  16.244 -33.375  1.00 94.69           C  
ATOM   2192  O   ILE B 153     -53.897  17.065 -34.208  1.00 73.43           O  
ATOM   2193  CB  ILE B 153     -52.296  18.017 -32.078  1.00113.87           C  
ATOM   2194  CG1 ILE B 153     -51.626  18.371 -30.734  1.00120.70           C  
ATOM   2195  CG2 ILE B 153     -53.194  19.153 -32.560  1.00110.87           C  
ATOM   2196  CD1 ILE B 153     -52.475  18.091 -29.474  1.00120.63           C  
ATOM   2197  N   ASP B 154     -53.428  14.943 -33.629  1.00100.02           N  
ATOM   2198  CA  ASP B 154     -53.933  14.350 -34.859  1.00107.82           C  
ATOM   2199  C   ASP B 154     -55.048  13.374 -34.501  1.00110.19           C  
ATOM   2200  O   ASP B 154     -56.187  13.560 -34.940  1.00107.06           O  
ATOM   2201  CB  ASP B 154     -52.811  13.637 -35.623  1.00112.76           C  
ATOM   2202  CG  ASP B 154     -53.158  13.380 -37.085  1.00113.96           C  
ATOM   2203  OD1 ASP B 154     -52.245  13.502 -37.929  1.00114.41           O  
ATOM   2204  OD2 ASP B 154     -54.327  13.053 -37.391  1.00112.13           O  
ATOM   2205  N   GLU B 155     -54.736  12.359 -33.688  1.00108.63           N  
ATOM   2206  CA  GLU B 155     -55.732  11.335 -33.327  1.00109.52           C  
ATOM   2207  C   GLU B 155     -56.861  11.915 -32.457  1.00106.14           C  
ATOM   2208  O   GLU B 155     -57.981  11.389 -32.454  1.00 98.95           O  
ATOM   2209  CB  GLU B 155     -55.073  10.107 -32.674  1.00111.58           C  
ATOM   2210  CG  GLU B 155     -53.915   9.480 -33.494  1.00114.90           C  
ATOM   2211  CD  GLU B 155     -54.207   9.320 -34.998  1.00114.29           C  
ATOM   2212  OE1 GLU B 155     -55.368   9.027 -35.366  1.00114.81           O  
ATOM   2213  OE2 GLU B 155     -53.262   9.476 -35.811  1.00103.49           O  
ATOM   2214  N   THR B 156     -56.566  13.002 -31.741  1.00101.77           N  
ATOM   2215  CA  THR B 156     -57.608  13.895 -31.237  1.00 91.80           C  
ATOM   2216  C   THR B 156     -58.542  14.177 -32.403  1.00 84.70           C  
ATOM   2217  O   THR B 156     -59.669  13.686 -32.453  1.00 83.52           O  
ATOM   2218  CB  THR B 156     -57.014  15.244 -30.688  1.00 91.46           C  
ATOM   2219  OG1 THR B 156     -56.748  15.129 -29.285  1.00 96.70           O  
ATOM   2220  CG2 THR B 156     -57.956  16.427 -30.910  1.00 88.05           C  
ATOM   2221  N   VAL B 157     -58.017  14.915 -33.373  1.00 82.77           N  
ATOM   2222  CA  VAL B 157     -58.817  15.541 -34.414  1.00 78.87           C  
ATOM   2223  C   VAL B 157     -59.359  14.537 -35.421  1.00 81.79           C  
ATOM   2224  O   VAL B 157     -60.372  14.780 -36.075  1.00 83.37           O  
ATOM   2225  CB  VAL B 157     -57.987  16.630 -35.127  1.00 72.00           C  
ATOM   2226  CG1 VAL B 157     -58.687  17.134 -36.382  1.00 70.25           C  
ATOM   2227  CG2 VAL B 157     -57.706  17.774 -34.154  1.00 63.18           C  
ATOM   2228  N   ASN B 158     -58.696  13.398 -35.532  1.00 89.67           N  
ATOM   2229  CA  ASN B 158     -59.075  12.404 -36.523  1.00 93.09           C  
ATOM   2230  C   ASN B 158     -59.864  11.232 -35.922  1.00 92.37           C  
ATOM   2231  O   ASN B 158     -60.340  10.363 -36.660  1.00 92.93           O  
ATOM   2232  CB  ASN B 158     -57.823  11.900 -37.260  1.00 94.41           C  
ATOM   2233  CG  ASN B 158     -57.991  11.883 -38.769  1.00 93.28           C  
ATOM   2234  OD1 ASN B 158     -57.022  12.045 -39.508  1.00 98.97           O  
ATOM   2235  ND2 ASN B 158     -59.217  11.688 -39.232  1.00 93.79           N  
ATOM   2236  N   SER B 159     -60.013  11.204 -34.596  1.00 88.94           N  
ATOM   2237  CA  SER B 159     -60.791  10.142 -33.954  1.00 86.34           C  
ATOM   2238  C   SER B 159     -61.564  10.608 -32.718  1.00 81.93           C  
ATOM   2239  O   SER B 159     -62.782  10.502 -32.676  1.00 78.67           O  
ATOM   2240  CB  SER B 159     -59.892   8.955 -33.605  1.00 86.28           C  
ATOM   2241  OG  SER B 159     -60.653   7.760 -33.555  1.00 86.79           O  
ATOM   2242  N   ASN B 160     -60.868  11.145 -31.727  1.00 83.89           N  
ATOM   2243  CA  ASN B 160     -61.505  11.458 -30.447  1.00 85.48           C  
ATOM   2244  C   ASN B 160     -62.658  12.462 -30.554  1.00 81.82           C  
ATOM   2245  O   ASN B 160     -63.815  12.097 -30.352  1.00 77.79           O  
ATOM   2246  CB  ASN B 160     -60.471  11.942 -29.428  1.00 92.77           C  
ATOM   2247  CG  ASN B 160     -59.398  10.903 -29.144  1.00 97.89           C  
ATOM   2248  OD1 ASN B 160     -58.291  11.242 -28.709  1.00 99.55           O  
ATOM   2249  ND2 ASN B 160     -59.715   9.631 -29.399  1.00 98.26           N  
ATOM   2250  N   ILE B 161     -62.343  13.717 -30.867  1.00 75.58           N  
ATOM   2251  CA  ILE B 161     -63.364  14.758 -31.046  1.00 69.93           C  
ATOM   2252  C   ILE B 161     -64.540  14.314 -31.923  1.00 67.77           C  
ATOM   2253  O   ILE B 161     -65.692  14.576 -31.585  1.00 62.49           O  
ATOM   2254  CB  ILE B 161     -62.757  16.037 -31.662  1.00 69.98           C  
ATOM   2255  CG1 ILE B 161     -61.914  16.794 -30.624  1.00 70.75           C  
ATOM   2256  CG2 ILE B 161     -63.855  16.921 -32.241  1.00 65.88           C  
ATOM   2257  CD1 ILE B 161     -62.496  18.127 -30.158  1.00 67.42           C  
ATOM   2258  N   PRO B 162     -64.258  13.667 -33.066  1.00 71.82           N  
ATOM   2259  CA  PRO B 162     -65.382  13.098 -33.817  1.00 76.88           C  
ATOM   2260  C   PRO B 162     -66.090  11.989 -33.054  1.00 73.37           C  
ATOM   2261  O   PRO B 162     -67.319  11.956 -33.044  1.00 73.04           O  
ATOM   2262  CB  PRO B 162     -64.741  12.549 -35.099  1.00 76.88           C  
ATOM   2263  CG  PRO B 162     -63.290  12.773 -34.978  1.00 76.58           C  
ATOM   2264  CD  PRO B 162     -63.016  13.693 -33.849  1.00 71.18           C  
ATOM   2265  N   THR B 163     -65.323  11.101 -32.422  1.00 73.15           N  
ATOM   2266  CA  THR B 163     -65.905  10.043 -31.600  1.00 73.62           C  
ATOM   2267  C   THR B 163     -66.736  10.682 -30.506  1.00 71.69           C  
ATOM   2268  O   THR B 163     -67.866  10.280 -30.236  1.00 71.27           O  
ATOM   2269  CB  THR B 163     -64.844   9.140 -30.922  1.00 74.74           C  
ATOM   2270  OG1 THR B 163     -63.993   9.935 -30.088  1.00 73.73           O  
ATOM   2271  CG2 THR B 163     -64.003   8.386 -31.949  1.00 78.69           C  
ATOM   2272  N   ASN B 164     -66.164  11.697 -29.886  1.00 70.66           N  
ATOM   2273  CA  ASN B 164     -66.822  12.359 -28.788  1.00 69.94           C  
ATOM   2274  C   ASN B 164     -68.131  12.985 -29.263  1.00 68.61           C  
ATOM   2275  O   ASN B 164     -69.173  12.766 -28.657  1.00 76.03           O  
ATOM   2276  CB  ASN B 164     -65.896  13.409 -28.169  1.00 75.11           C  
ATOM   2277  CG  ASN B 164     -66.054  13.521 -26.667  1.00 77.21           C  
ATOM   2278  OD1 ASN B 164     -66.246  14.616 -26.141  1.00 80.90           O  
ATOM   2279  ND2 ASN B 164     -65.958  12.393 -25.964  1.00 75.58           N  
ATOM   2280  N   LEU B 165     -68.089  13.733 -30.362  1.00 66.00           N  
ATOM   2281  CA  LEU B 165     -69.304  14.372 -30.879  1.00 66.31           C  
ATOM   2282  C   LEU B 165     -70.294  13.349 -31.407  1.00 67.20           C  
ATOM   2283  O   LEU B 165     -71.497  13.566 -31.364  1.00 63.00           O  
ATOM   2284  CB  LEU B 165     -68.986  15.390 -31.974  1.00 65.40           C  
ATOM   2285  CG  LEU B 165     -68.240  16.664 -31.560  1.00 64.01           C  
ATOM   2286  CD1 LEU B 165     -68.858  17.864 -32.268  1.00 61.05           C  
ATOM   2287  CD2 LEU B 165     -68.239  16.877 -30.047  1.00 57.67           C  
ATOM   2288  N   ARG B 166     -69.782  12.237 -31.912  1.00 77.95           N  
ATOM   2289  CA  ARG B 166     -70.636  11.126 -32.299  1.00 87.96           C  
ATOM   2290  C   ARG B 166     -71.477  10.700 -31.094  1.00 82.97           C  
ATOM   2291  O   ARG B 166     -72.715  10.765 -31.134  1.00 75.18           O  
ATOM   2292  CB  ARG B 166     -69.778   9.957 -32.810  1.00 97.63           C  
ATOM   2293  CG  ARG B 166     -70.537   8.677 -33.179  1.00106.04           C  
ATOM   2294  CD  ARG B 166     -69.607   7.450 -33.223  1.00110.55           C  
ATOM   2295  NE  ARG B 166     -68.378   7.692 -33.998  1.00112.47           N  
ATOM   2296  CZ  ARG B 166     -67.127   7.473 -33.575  1.00113.56           C  
ATOM   2297  NH1 ARG B 166     -66.874   6.980 -32.359  1.00117.22           N  
ATOM   2298  NH2 ARG B 166     -66.106   7.746 -34.386  1.00110.51           N  
ATOM   2299  N   VAL B 167     -70.787  10.297 -30.024  1.00 79.10           N  
ATOM   2300  CA  VAL B 167     -71.434   9.723 -28.833  1.00 82.46           C  
ATOM   2301  C   VAL B 167     -72.150  10.767 -27.971  1.00 78.92           C  
ATOM   2302  O   VAL B 167     -73.051  10.421 -27.209  1.00 87.76           O  
ATOM   2303  CB  VAL B 167     -70.443   8.862 -27.964  1.00 83.40           C  
ATOM   2304  CG1 VAL B 167     -69.259   9.684 -27.477  1.00 86.71           C  
ATOM   2305  CG2 VAL B 167     -71.164   8.221 -26.784  1.00 81.84           C  
ATOM   2306  N   LEU B 168     -71.774  12.037 -28.098  1.00 72.09           N  
ATOM   2307  CA  LEU B 168     -72.519  13.103 -27.432  1.00 67.05           C  
ATOM   2308  C   LEU B 168     -73.823  13.378 -28.198  1.00 61.21           C  
ATOM   2309  O   LEU B 168     -74.912  13.122 -27.692  1.00 60.24           O  
ATOM   2310  CB  LEU B 168     -71.667  14.375 -27.294  1.00 67.28           C  
ATOM   2311  CG  LEU B 168     -71.874  15.177 -26.006  1.00 66.26           C  
ATOM   2312  CD1 LEU B 168     -71.278  14.438 -24.810  1.00 64.69           C  
ATOM   2313  CD2 LEU B 168     -71.271  16.575 -26.120  1.00 67.45           C  
ATOM   2314  N   ARG B 169     -73.701  13.870 -29.425  1.00 63.32           N  
ATOM   2315  CA  ARG B 169     -74.850  14.219 -30.252  1.00 67.69           C  
ATOM   2316  C   ARG B 169     -75.978  13.214 -30.130  1.00 66.72           C  
ATOM   2317  O   ARG B 169     -77.123  13.591 -29.910  1.00 61.95           O  
ATOM   2318  CB  ARG B 169     -74.416  14.296 -31.704  1.00 81.79           C  
ATOM   2319  CG  ARG B 169     -75.525  14.572 -32.712  1.00 93.02           C  
ATOM   2320  CD  ARG B 169     -75.055  14.200 -34.117  1.00100.44           C  
ATOM   2321  NE  ARG B 169     -73.771  14.826 -34.441  1.00107.63           N  
ATOM   2322  CZ  ARG B 169     -73.007  14.513 -35.486  1.00111.26           C  
ATOM   2323  NH1 ARG B 169     -73.378  13.570 -36.348  1.00110.42           N  
ATOM   2324  NH2 ARG B 169     -71.855  15.155 -35.668  1.00114.88           N  
ATOM   2325  N   SER B 170     -75.650  11.934 -30.273  1.00 69.14           N  
ATOM   2326  CA  SER B 170     -76.639  10.860 -30.107  1.00 72.62           C  
ATOM   2327  C   SER B 170     -77.565  11.081 -28.922  1.00 71.62           C  
ATOM   2328  O   SER B 170     -78.767  10.820 -28.996  1.00 71.38           O  
ATOM   2329  CB  SER B 170     -75.946   9.516 -29.891  1.00 74.41           C  
ATOM   2330  OG  SER B 170     -76.811   8.620 -29.207  1.00 75.04           O  
ATOM   2331  N   ILE B 171     -76.985  11.538 -27.821  1.00 64.74           N  
ATOM   2332  CA  ILE B 171     -77.700  11.627 -26.574  1.00 56.60           C  
ATOM   2333  C   ILE B 171     -78.620  12.833 -26.551  1.00 52.70           C  
ATOM   2334  O   ILE B 171     -79.797  12.696 -26.240  1.00 55.94           O  
ATOM   2335  CB  ILE B 171     -76.725  11.668 -25.388  1.00 56.91           C  
ATOM   2336  CG1 ILE B 171     -77.072  10.559 -24.392  1.00 58.92           C  
ATOM   2337  CG2 ILE B 171     -76.718  13.044 -24.728  1.00 53.46           C  
ATOM   2338  CD1 ILE B 171     -75.902  10.125 -23.573  1.00 61.79           C  
ATOM   2339  N   LEU B 172     -78.096  14.006 -26.886  1.00 50.43           N  
ATOM   2340  CA  LEU B 172     -78.897  15.236 -26.840  1.00 52.71           C  
ATOM   2341  C   LEU B 172     -80.078  15.115 -27.784  1.00 49.46           C  
ATOM   2342  O   LEU B 172     -81.224  15.387 -27.442  1.00 47.87           O  
ATOM   2343  CB  LEU B 172     -78.048  16.432 -27.246  1.00 54.80           C  
ATOM   2344  CG  LEU B 172     -77.239  17.103 -26.139  1.00 55.60           C  
ATOM   2345  CD1 LEU B 172     -76.698  16.105 -25.121  1.00 49.96           C  
ATOM   2346  CD2 LEU B 172     -76.116  17.900 -26.773  1.00 54.87           C  
ATOM   2347  N   GLU B 173     -79.745  14.718 -28.995  1.00 55.08           N  
ATOM   2348  CA  GLU B 173     -80.680  14.205 -29.973  1.00 62.79           C  
ATOM   2349  C   GLU B 173     -81.745  13.289 -29.365  1.00 59.49           C  
ATOM   2350  O   GLU B 173     -82.934  13.419 -29.654  1.00 61.52           O  
ATOM   2351  CB  GLU B 173     -79.839  13.420 -30.978  1.00 76.10           C  
ATOM   2352  CG  GLU B 173     -80.523  12.886 -32.201  1.00 81.24           C  
ATOM   2353  CD  GLU B 173     -79.517  12.593 -33.299  1.00 79.87           C  
ATOM   2354  OE1 GLU B 173     -78.421  12.062 -32.987  1.00 81.28           O  
ATOM   2355  OE2 GLU B 173     -79.819  12.916 -34.465  1.00 76.31           O  
ATOM   2356  N   ASN B 174     -81.304  12.359 -28.525  1.00 60.42           N  
ATOM   2357  CA  ASN B 174     -82.201  11.390 -27.906  1.00 54.27           C  
ATOM   2358  C   ASN B 174     -83.014  11.988 -26.762  1.00 48.23           C  
ATOM   2359  O   ASN B 174     -84.165  11.618 -26.565  1.00 52.70           O  
ATOM   2360  CB  ASN B 174     -81.414  10.167 -27.425  1.00 53.56           C  
ATOM   2361  CG  ASN B 174     -82.239   9.247 -26.548  1.00 57.25           C  
ATOM   2362  OD1 ASN B 174     -82.419   9.510 -25.360  1.00 60.51           O  
ATOM   2363  ND2 ASN B 174     -82.741   8.159 -27.127  1.00 54.61           N  
ATOM   2364  N   LEU B 175     -82.425  12.901 -26.004  1.00 45.83           N  
ATOM   2365  CA  LEU B 175     -83.156  13.541 -24.905  1.00 42.93           C  
ATOM   2366  C   LEU B 175     -84.166  14.565 -25.414  1.00 43.29           C  
ATOM   2367  O   LEU B 175     -85.162  14.849 -24.747  1.00 43.14           O  
ATOM   2368  CB  LEU B 175     -82.194  14.154 -23.881  1.00 37.42           C  
ATOM   2369  CG  LEU B 175     -81.356  13.065 -23.175  1.00 35.63           C  
ATOM   2370  CD1 LEU B 175     -80.431  13.638 -22.088  1.00 31.84           C  
ATOM   2371  CD2 LEU B 175     -82.249  11.955 -22.593  1.00 28.00           C  
ATOM   2372  N   ARG B 176     -83.934  15.078 -26.614  1.00 43.81           N  
ATOM   2373  CA  ARG B 176     -84.893  15.953 -27.281  1.00 47.93           C  
ATOM   2374  C   ARG B 176     -86.183  15.206 -27.654  1.00 43.65           C  
ATOM   2375  O   ARG B 176     -87.268  15.805 -27.734  1.00 37.59           O  
ATOM   2376  CB  ARG B 176     -84.234  16.528 -28.525  1.00 61.94           C  
ATOM   2377  CG  ARG B 176     -84.978  17.639 -29.231  1.00 72.06           C  
ATOM   2378  CD  ARG B 176     -84.062  18.240 -30.324  1.00 84.19           C  
ATOM   2379  NE  ARG B 176     -84.407  19.620 -30.690  1.00 95.03           N  
ATOM   2380  CZ  ARG B 176     -84.254  20.694 -29.902  1.00 96.13           C  
ATOM   2381  NH1 ARG B 176     -83.778  20.580 -28.661  1.00 89.28           N  
ATOM   2382  NH2 ARG B 176     -84.594  21.902 -30.353  1.00 89.61           N  
ATOM   2383  N   SER B 177     -86.058  13.901 -27.884  1.00 43.55           N  
ATOM   2384  CA  SER B 177     -87.206  13.060 -28.221  1.00 44.00           C  
ATOM   2385  C   SER B 177     -87.880  12.510 -26.969  1.00 40.24           C  
ATOM   2386  O   SER B 177     -88.998  11.998 -27.034  1.00 38.66           O  
ATOM   2387  CB  SER B 177     -86.771  11.891 -29.105  1.00 47.00           C  
ATOM   2388  OG  SER B 177     -86.262  10.822 -28.314  1.00 54.22           O  
ATOM   2389  N   LYS B 178     -87.187  12.586 -25.840  1.00 34.95           N  
ATOM   2390  CA  LYS B 178     -87.745  12.121 -24.594  1.00 40.31           C  
ATOM   2391  C   LYS B 178     -88.491  13.275 -23.983  1.00 36.97           C  
ATOM   2392  O   LYS B 178     -89.664  13.141 -23.642  1.00 43.60           O  
ATOM   2393  CB  LYS B 178     -86.662  11.613 -23.646  1.00 51.66           C  
ATOM   2394  CG  LYS B 178     -86.023  10.302 -24.068  1.00 56.20           C  
ATOM   2395  CD  LYS B 178     -86.955   9.127 -23.839  1.00 60.65           C  
ATOM   2396  CE  LYS B 178     -86.273   7.790 -24.175  1.00 71.19           C  
ATOM   2397  NZ  LYS B 178     -85.100   7.442 -23.305  1.00 64.15           N  
ATOM   2398  N   ILE B 179     -87.836  14.422 -23.861  1.00 33.74           N  
ATOM   2399  CA  ILE B 179     -88.573  15.618 -23.472  1.00 43.30           C  
ATOM   2400  C   ILE B 179     -89.965  15.595 -24.141  1.00 46.14           C  
ATOM   2401  O   ILE B 179     -90.982  15.418 -23.475  1.00 49.23           O  
ATOM   2402  CB  ILE B 179     -87.835  16.929 -23.850  1.00 42.26           C  
ATOM   2403  CG1 ILE B 179     -88.556  18.153 -23.292  1.00 41.78           C  
ATOM   2404  CG2 ILE B 179     -87.767  17.102 -25.346  1.00 48.73           C  
ATOM   2405  CD1 ILE B 179     -89.821  18.537 -24.050  1.00 36.79           C  
ATOM   2406  N   GLN B 180     -90.005  15.699 -25.461  1.00 41.20           N  
ATOM   2407  CA  GLN B 180     -91.246  16.009 -26.134  1.00 46.08           C  
ATOM   2408  C   GLN B 180     -92.325  14.944 -25.927  1.00 45.19           C  
ATOM   2409  O   GLN B 180     -93.518  15.245 -25.971  1.00 41.45           O  
ATOM   2410  CB  GLN B 180     -90.976  16.227 -27.615  1.00 58.97           C  
ATOM   2411  CG  GLN B 180     -90.755  14.955 -28.404  1.00 67.95           C  
ATOM   2412  CD  GLN B 180     -92.041  14.444 -29.022  1.00 71.08           C  
ATOM   2413  OE1 GLN B 180     -92.664  15.135 -29.833  1.00 67.21           O  
ATOM   2414  NE2 GLN B 180     -92.446  13.231 -28.644  1.00 75.35           N  
ATOM   2415  N   LYS B 181     -91.920  13.699 -25.703  1.00 46.67           N  
ATOM   2416  CA  LYS B 181     -92.902  12.631 -25.523  1.00 52.11           C  
ATOM   2417  C   LYS B 181     -93.444  12.650 -24.104  1.00 50.85           C  
ATOM   2418  O   LYS B 181     -94.566  12.193 -23.861  1.00 52.62           O  
ATOM   2419  CB  LYS B 181     -92.319  11.260 -25.877  1.00 55.73           C  
ATOM   2420  CG  LYS B 181     -91.430  10.619 -24.806  1.00 62.09           C  
ATOM   2421  CD  LYS B 181     -92.171   9.841 -23.709  1.00 64.18           C  
ATOM   2422  CE  LYS B 181     -93.197   8.873 -24.248  1.00 63.91           C  
ATOM   2423  NZ  LYS B 181     -94.502   9.551 -24.401  1.00 68.88           N  
ATOM   2424  N   LEU B 182     -92.632  13.159 -23.175  1.00 45.94           N  
ATOM   2425  CA  LEU B 182     -93.113  13.478 -21.834  1.00 41.77           C  
ATOM   2426  C   LEU B 182     -94.062  14.650 -21.941  1.00 47.39           C  
ATOM   2427  O   LEU B 182     -95.188  14.578 -21.464  1.00 47.20           O  
ATOM   2428  CB  LEU B 182     -91.974  13.835 -20.885  1.00 41.32           C  
ATOM   2429  CG  LEU B 182     -91.397  12.663 -20.094  1.00 48.97           C  
ATOM   2430  CD1 LEU B 182     -91.172  11.463 -20.991  1.00 55.95           C  
ATOM   2431  CD2 LEU B 182     -90.095  13.056 -19.389  1.00 46.83           C  
ATOM   2432  N   GLU B 183     -93.621  15.719 -22.602  1.00 48.12           N  
ATOM   2433  CA  GLU B 183     -94.460  16.895 -22.756  1.00 45.57           C  
ATOM   2434  C   GLU B 183     -95.836  16.448 -23.216  1.00 40.90           C  
ATOM   2435  O   GLU B 183     -96.844  16.958 -22.737  1.00 41.66           O  
ATOM   2436  CB  GLU B 183     -93.842  17.932 -23.706  1.00 59.58           C  
ATOM   2437  CG  GLU B 183     -94.640  19.268 -23.776  1.00 74.96           C  
ATOM   2438  CD  GLU B 183     -93.796  20.523 -23.483  1.00 86.08           C  
ATOM   2439  OE1 GLU B 183     -92.756  20.739 -24.156  1.00 89.04           O  
ATOM   2440  OE2 GLU B 183     -94.191  21.300 -22.575  1.00 90.57           O  
ATOM   2441  N   SER B 184     -95.878  15.470 -24.114  1.00 42.15           N  
ATOM   2442  CA  SER B 184     -97.152  14.845 -24.485  1.00 51.10           C  
ATOM   2443  C   SER B 184     -97.717  13.931 -23.376  1.00 57.99           C  
ATOM   2444  O   SER B 184     -98.731  14.295 -22.772  1.00 58.33           O  
ATOM   2445  CB  SER B 184     -97.062  14.108 -25.830  1.00 55.33           C  
ATOM   2446  OG  SER B 184     -97.476  14.947 -26.905  1.00 49.50           O  
ATOM   2447  N   ASP B 185     -97.092  12.775 -23.096  1.00 52.19           N  
ATOM   2448  CA  ASP B 185     -97.580  11.866 -22.019  1.00 51.57           C  
ATOM   2449  C   ASP B 185     -98.257  12.633 -20.851  1.00 46.44           C  
ATOM   2450  O   ASP B 185     -99.281  12.193 -20.352  1.00 50.09           O  
ATOM   2451  CB  ASP B 185     -96.456  10.943 -21.462  1.00 57.25           C  
ATOM   2452  CG  ASP B 185     -96.515   9.458 -21.984  1.00 55.79           C  
ATOM   2453  OD1 ASP B 185     -95.508   8.724 -21.807  1.00 47.60           O  
ATOM   2454  OD2 ASP B 185     -97.531   9.002 -22.551  1.00 56.68           O  
ATOM   2455  N   VAL B 186     -97.699  13.772 -20.432  1.00 48.87           N  
ATOM   2456  CA  VAL B 186     -98.342  14.651 -19.412  1.00 50.09           C  
ATOM   2457  C   VAL B 186     -99.671  15.309 -19.826  1.00 45.86           C  
ATOM   2458  O   VAL B 186    -100.684  15.154 -19.139  1.00 43.67           O  
ATOM   2459  CB  VAL B 186     -97.399  15.792 -18.929  1.00 47.71           C  
ATOM   2460  CG1 VAL B 186     -98.161  17.094 -18.730  1.00 47.40           C  
ATOM   2461  CG2 VAL B 186     -96.703  15.398 -17.644  1.00 45.10           C  
ATOM   2462  N   SER B 187     -99.672  16.060 -20.922  1.00 44.43           N  
ATOM   2463  CA  SER B 187    -100.905  16.711 -21.365  1.00 46.08           C  
ATOM   2464  C   SER B 187    -101.967  15.689 -21.720  1.00 44.18           C  
ATOM   2465  O   SER B 187    -103.108  16.047 -21.982  1.00 46.28           O  
ATOM   2466  CB  SER B 187    -100.658  17.641 -22.543  1.00 46.94           C  
ATOM   2467  OG  SER B 187    -100.067  18.849 -22.092  1.00 56.72           O  
ATOM   2468  N   ALA B 188    -101.578  14.417 -21.723  1.00 47.78           N  
ATOM   2469  CA  ALA B 188    -102.512  13.301 -21.877  1.00 43.27           C  
ATOM   2470  C   ALA B 188    -103.305  13.119 -20.624  1.00 40.46           C  
ATOM   2471  O   ALA B 188    -104.471  12.714 -20.664  1.00 38.58           O  
ATOM   2472  CB  ALA B 188    -101.757  12.012 -22.166  1.00 45.44           C  
ATOM   2473  N   GLN B 189    -102.643  13.379 -19.502  1.00 45.16           N  
ATOM   2474  CA  GLN B 189    -103.242  13.132 -18.213  1.00 46.04           C  
ATOM   2475  C   GLN B 189    -104.078  14.308 -17.802  1.00 44.18           C  
ATOM   2476  O   GLN B 189    -105.170  14.131 -17.256  1.00 48.03           O  
ATOM   2477  CB  GLN B 189    -102.187  12.851 -17.156  1.00 39.56           C  
ATOM   2478  CG  GLN B 189    -102.787  12.233 -15.926  1.00 37.45           C  
ATOM   2479  CD  GLN B 189    -103.616  11.042 -16.271  1.00 31.59           C  
ATOM   2480  OE1 GLN B 189    -104.668  10.808 -15.694  1.00 32.14           O  
ATOM   2481  NE2 GLN B 189    -103.160  10.292 -17.248  1.00 35.96           N  
ATOM   2482  N   MET B 190    -103.581  15.508 -18.080  1.00 40.62           N  
ATOM   2483  CA  MET B 190    -104.404  16.697 -17.910  1.00 46.18           C  
ATOM   2484  C   MET B 190    -105.790  16.391 -18.453  1.00 43.57           C  
ATOM   2485  O   MET B 190    -106.801  16.707 -17.810  1.00 49.96           O  
ATOM   2486  CB  MET B 190    -103.819  17.897 -18.646  1.00 48.36           C  
ATOM   2487  CG  MET B 190    -102.558  18.448 -18.019  1.00 56.32           C  
ATOM   2488  SD  MET B 190    -102.828  19.145 -16.376  1.00 57.01           S  
ATOM   2489  CE  MET B 190    -101.546  20.411 -16.403  1.00 60.04           C  
ATOM   2490  N   GLU B 191    -105.824  15.737 -19.611  1.00 29.05           N  
ATOM   2491  CA  GLU B 191    -107.068  15.466 -20.292  1.00 30.51           C  
ATOM   2492  C   GLU B 191    -107.912  14.361 -19.638  1.00 36.59           C  
ATOM   2493  O   GLU B 191    -109.145  14.444 -19.655  1.00 35.74           O  
ATOM   2494  CB  GLU B 191    -106.789  15.146 -21.754  1.00 38.61           C  
ATOM   2495  CG  GLU B 191    -107.850  15.650 -22.692  1.00 52.34           C  
ATOM   2496  CD  GLU B 191    -108.044  17.151 -22.580  1.00 69.66           C  
ATOM   2497  OE1 GLU B 191    -109.178  17.608 -22.851  1.00 81.85           O  
ATOM   2498  OE2 GLU B 191    -107.075  17.867 -22.208  1.00 72.27           O  
ATOM   2499  N   TYR B 192    -107.268  13.341 -19.062  1.00 40.66           N  
ATOM   2500  CA  TYR B 192    -107.991  12.298 -18.323  1.00 38.06           C  
ATOM   2501  C   TYR B 192    -108.464  12.829 -17.010  1.00 36.90           C  
ATOM   2502  O   TYR B 192    -109.310  12.218 -16.341  1.00 32.49           O  
ATOM   2503  CB  TYR B 192    -107.106  11.112 -18.015  1.00 40.87           C  
ATOM   2504  CG  TYR B 192    -106.732  10.283 -19.193  1.00 50.78           C  
ATOM   2505  CD1 TYR B 192    -107.301  10.495 -20.448  1.00 51.81           C  
ATOM   2506  CD2 TYR B 192    -105.811   9.250 -19.044  1.00 63.61           C  
ATOM   2507  CE1 TYR B 192    -106.940   9.711 -21.529  1.00 68.47           C  
ATOM   2508  CE2 TYR B 192    -105.438   8.459 -20.112  1.00 68.78           C  
ATOM   2509  CZ  TYR B 192    -106.004   8.684 -21.356  1.00 76.07           C  
ATOM   2510  OH  TYR B 192    -105.628   7.882 -22.419  1.00 79.30           O  
ATOM   2511  N   CYS B 193    -107.880  13.959 -16.638  1.00 39.20           N  
ATOM   2512  CA  CYS B 193    -108.190  14.591 -15.386  1.00 41.21           C  
ATOM   2513  C   CYS B 193    -109.361  15.546 -15.444  1.00 35.87           C  
ATOM   2514  O   CYS B 193    -109.874  15.948 -14.416  1.00 33.89           O  
ATOM   2515  CB  CYS B 193    -106.938  15.228 -14.803  1.00 46.93           C  
ATOM   2516  SG  CYS B 193    -106.060  13.969 -13.840  1.00 62.31           S  
ATOM   2517  N   ARG B 194    -109.824  15.869 -16.637  1.00 40.11           N  
ATOM   2518  CA  ARG B 194    -111.091  16.542 -16.745  1.00 47.56           C  
ATOM   2519  C   ARG B 194    -112.147  15.778 -15.925  1.00 45.91           C  
ATOM   2520  O   ARG B 194    -112.731  16.366 -15.023  1.00 47.17           O  
ATOM   2521  CB  ARG B 194    -111.505  16.711 -18.212  1.00 62.60           C  
ATOM   2522  CG  ARG B 194    -110.616  17.703 -18.994  1.00 70.30           C  
ATOM   2523  CD  ARG B 194    -111.328  18.350 -20.203  1.00 81.14           C  
ATOM   2524  NE  ARG B 194    -110.786  19.687 -20.503  1.00 94.88           N  
ATOM   2525  CZ  ARG B 194    -111.189  20.845 -19.950  1.00105.05           C  
ATOM   2526  NH1 ARG B 194    -112.170  20.892 -19.041  1.00109.49           N  
ATOM   2527  NH2 ARG B 194    -110.600  21.987 -20.308  1.00102.02           N  
ATOM   2528  N   THR B 195    -112.366  14.484 -16.188  1.00 42.28           N  
ATOM   2529  CA  THR B 195    -113.396  13.715 -15.441  1.00 48.27           C  
ATOM   2530  C   THR B 195    -112.813  12.843 -14.312  1.00 47.54           C  
ATOM   2531  O   THR B 195    -111.996  11.964 -14.590  1.00 51.39           O  
ATOM   2532  CB  THR B 195    -114.228  12.791 -16.369  1.00 55.12           C  
ATOM   2533  OG1 THR B 195    -113.470  11.622 -16.704  1.00 62.74           O  
ATOM   2534  CG2 THR B 195    -114.653  13.518 -17.660  1.00 61.03           C  
ATOM   2535  N   PRO B 196    -113.250  13.057 -13.043  1.00 48.86           N  
ATOM   2536  CA  PRO B 196    -112.676  12.339 -11.884  1.00 48.43           C  
ATOM   2537  C   PRO B 196    -113.256  10.932 -11.613  1.00 40.29           C  
ATOM   2538  O   PRO B 196    -114.305  10.598 -12.141  1.00 30.96           O  
ATOM   2539  CB  PRO B 196    -112.987  13.278 -10.708  1.00 42.44           C  
ATOM   2540  CG  PRO B 196    -114.245  13.940 -11.089  1.00 35.76           C  
ATOM   2541  CD  PRO B 196    -114.306  13.995 -12.610  1.00 41.15           C  
ATOM   2542  N   CYS B 197    -112.560  10.138 -10.792  1.00 40.67           N  
ATOM   2543  CA  CYS B 197    -113.022   8.804 -10.366  1.00 46.66           C  
ATOM   2544  C   CYS B 197    -114.004   8.917  -9.229  1.00 45.20           C  
ATOM   2545  O   CYS B 197    -113.921   9.842  -8.423  1.00 43.38           O  
ATOM   2546  CB  CYS B 197    -111.870   7.941  -9.863  1.00 51.48           C  
ATOM   2547  SG  CYS B 197    -110.929   8.760  -8.584  1.00 64.34           S  
ATOM   2548  N   THR B 198    -114.913   7.950  -9.150  1.00 45.44           N  
ATOM   2549  CA  THR B 198    -115.963   7.977  -8.135  1.00 45.66           C  
ATOM   2550  C   THR B 198    -116.207   6.612  -7.541  1.00 42.00           C  
ATOM   2551  O   THR B 198    -116.087   5.589  -8.232  1.00 50.29           O  
ATOM   2552  CB  THR B 198    -117.304   8.461  -8.702  1.00 45.42           C  
ATOM   2553  OG1 THR B 198    -117.897   7.422  -9.497  1.00 34.04           O  
ATOM   2554  CG2 THR B 198    -117.114   9.768  -9.514  1.00 46.31           C  
ATOM   2555  N   VAL B 199    -116.572   6.612  -6.264  1.00 25.32           N  
ATOM   2556  CA  VAL B 199    -116.864   5.392  -5.568  1.00 21.68           C  
ATOM   2557  C   VAL B 199    -118.306   5.407  -5.074  1.00 28.19           C  
ATOM   2558  O   VAL B 199    -118.955   6.444  -5.077  1.00 31.63           O  
ATOM   2559  CB  VAL B 199    -115.915   5.198  -4.396  1.00 16.58           C  
ATOM   2560  CG1 VAL B 199    -114.502   5.560  -4.806  1.00 14.08           C  
ATOM   2561  CG2 VAL B 199    -116.374   5.995  -3.195  1.00 12.28           C  
ATOM   2562  N   SER B 200    -118.814   4.230  -4.718  1.00 35.94           N  
ATOM   2563  CA  SER B 200    -120.054   4.103  -3.953  1.00 36.28           C  
ATOM   2564  C   SER B 200    -119.788   2.998  -2.952  1.00 37.88           C  
ATOM   2565  O   SER B 200    -119.643   1.842  -3.318  1.00 41.54           O  
ATOM   2566  CB  SER B 200    -121.269   3.744  -4.819  1.00 36.44           C  
ATOM   2567  OG  SER B 200    -121.120   4.136  -6.181  1.00 39.34           O  
ATOM   2568  N   CYS B 201    -119.662   3.390  -1.695  1.00 38.91           N  
ATOM   2569  CA  CYS B 201    -119.502   2.483  -0.594  1.00 30.44           C  
ATOM   2570  C   CYS B 201    -120.650   2.719   0.352  1.00 37.94           C  
ATOM   2571  O   CYS B 201    -120.522   3.406   1.375  1.00 48.99           O  
ATOM   2572  CB  CYS B 201    -118.183   2.737   0.086  1.00 30.86           C  
ATOM   2573  SG  CYS B 201    -116.892   2.824  -1.101  1.00 45.27           S  
ATOM   2574  N   ASN B 202    -121.793   2.193  -0.054  1.00 34.44           N  
ATOM   2575  CA  ASN B 202    -122.901   1.974   0.841  1.00 36.38           C  
ATOM   2576  C   ASN B 202    -122.423   1.445   2.221  1.00 31.40           C  
ATOM   2577  O   ASN B 202    -121.742   0.420   2.345  1.00 19.58           O  
ATOM   2578  CB  ASN B 202    -123.847   0.968   0.190  1.00 48.56           C  
ATOM   2579  CG  ASN B 202    -124.413   1.455  -1.144  1.00 49.03           C  
ATOM   2580  OD1 ASN B 202    -125.176   2.422  -1.184  1.00 55.41           O  
ATOM   2581  ND2 ASN B 202    -124.066   0.768  -2.233  1.00 41.53           N  
ATOM   2582  N   ILE B 203    -122.792   2.153   3.272  1.00 31.66           N  
ATOM   2583  CA  ILE B 203    -122.177   1.924   4.570  1.00 33.73           C  
ATOM   2584  C   ILE B 203    -122.749   0.663   5.157  1.00 33.40           C  
ATOM   2585  O   ILE B 203    -123.946   0.455   5.077  1.00 42.45           O  
ATOM   2586  CB  ILE B 203    -122.435   3.084   5.546  1.00 29.43           C  
ATOM   2587  CG1 ILE B 203    -121.826   4.371   5.003  1.00 36.94           C  
ATOM   2588  CG2 ILE B 203    -121.806   2.809   6.872  1.00 20.91           C  
ATOM   2589  CD1 ILE B 203    -122.566   5.007   3.792  1.00 27.40           C  
ATOM   2590  N   PRO B 204    -121.896  -0.201   5.705  1.00 32.97           N  
ATOM   2591  CA  PRO B 204    -122.292  -1.265   6.597  1.00 38.72           C  
ATOM   2592  C   PRO B 204    -123.170  -0.852   7.780  1.00 40.28           C  
ATOM   2593  O   PRO B 204    -122.933   0.195   8.390  1.00 35.88           O  
ATOM   2594  CB  PRO B 204    -120.952  -1.746   7.124  1.00 42.39           C  
ATOM   2595  CG  PRO B 204    -120.076  -1.653   5.958  1.00 41.34           C  
ATOM   2596  CD  PRO B 204    -120.541  -0.448   5.185  1.00 45.11           C  
ATOM   2597  N   VAL B 205    -124.142  -1.710   8.119  1.00 38.94           N  
ATOM   2598  CA  VAL B 205    -125.083  -1.442   9.219  1.00 34.37           C  
ATOM   2599  C   VAL B 205    -124.567  -1.813  10.625  1.00 38.12           C  
ATOM   2600  O   VAL B 205    -125.312  -1.759  11.597  1.00 37.88           O  
ATOM   2601  CB  VAL B 205    -126.417  -2.154   8.966  1.00 16.42           C  
ATOM   2602  CG1 VAL B 205    -127.389  -1.958  10.174  1.00  8.51           C  
ATOM   2603  CG2 VAL B 205    -127.019  -1.677   7.600  1.00 10.25           C  
ATOM   2604  N   VAL B 206    -123.303  -2.190  10.735  1.00 39.21           N  
ATOM   2605  CA  VAL B 206    -122.702  -2.503  12.031  1.00 41.29           C  
ATOM   2606  C   VAL B 206    -121.569  -1.495  12.238  1.00 42.83           C  
ATOM   2607  O   VAL B 206    -120.995  -0.976  11.271  1.00 40.47           O  
ATOM   2608  CB  VAL B 206    -122.235  -4.018  12.109  1.00 43.81           C  
ATOM   2609  CG1 VAL B 206    -121.294  -4.385  10.943  1.00 39.10           C  
ATOM   2610  CG2 VAL B 206    -121.617  -4.371  13.473  1.00 35.96           C  
ATOM   2611  N   SER B 207    -121.284  -1.193  13.498  1.00 41.07           N  
ATOM   2612  CA  SER B 207    -120.291  -0.187  13.840  1.00 45.70           C  
ATOM   2613  C   SER B 207    -119.992  -0.263  15.309  1.00 48.32           C  
ATOM   2614  O   SER B 207    -120.712  -0.912  16.062  1.00 51.12           O  
ATOM   2615  CB  SER B 207    -120.792   1.222  13.502  1.00 51.22           C  
ATOM   2616  OG  SER B 207    -120.261   2.202  14.394  1.00 55.00           O  
ATOM   2617  N   GLY B 208    -118.933   0.414  15.716  1.00 50.43           N  
ATOM   2618  CA  GLY B 208    -118.546   0.421  17.099  1.00 48.86           C  
ATOM   2619  C   GLY B 208    -117.348   1.302  17.256  1.00 48.75           C  
ATOM   2620  O   GLY B 208    -117.097   2.176  16.427  1.00 44.28           O  
ATOM   2621  N   LYS B 209    -116.599   1.064  18.321  1.00 49.16           N  
ATOM   2622  CA  LYS B 209    -115.494   1.933  18.657  1.00 53.06           C  
ATOM   2623  C   LYS B 209    -114.357   1.744  17.656  1.00 54.09           C  
ATOM   2624  O   LYS B 209    -113.559   2.670  17.454  1.00 54.21           O  
ATOM   2625  CB  LYS B 209    -115.010   1.697  20.092  1.00 56.43           C  
ATOM   2626  CG  LYS B 209    -115.892   2.289  21.196  1.00 56.05           C  
ATOM   2627  CD  LYS B 209    -117.120   1.423  21.518  1.00 62.73           C  
ATOM   2628  CE  LYS B 209    -118.404   1.944  20.832  1.00 67.97           C  
ATOM   2629  NZ  LYS B 209    -119.641   1.120  21.046  1.00 60.39           N  
ATOM   2630  N   GLU B 210    -114.284   0.559  17.043  1.00 40.72           N  
ATOM   2631  CA  GLU B 210    -113.355   0.315  15.945  1.00 43.42           C  
ATOM   2632  C   GLU B 210    -113.508  -1.074  15.337  1.00 51.27           C  
ATOM   2633  O   GLU B 210    -114.463  -1.786  15.656  1.00 61.35           O  
ATOM   2634  CB  GLU B 210    -111.918   0.541  16.401  1.00 55.13           C  
ATOM   2635  CG  GLU B 210    -111.629   0.163  17.822  1.00 62.32           C  
ATOM   2636  CD  GLU B 210    -112.029  -1.245  18.145  1.00 72.05           C  
ATOM   2637  OE1 GLU B 210    -112.217  -1.513  19.355  1.00 79.60           O  
ATOM   2638  OE2 GLU B 210    -112.137  -2.075  17.204  1.00 62.99           O  
ATOM   2639  N   CYS B 211    -112.574  -1.483  14.478  1.00 45.28           N  
ATOM   2640  CA  CYS B 211    -112.737  -2.740  13.738  1.00 45.81           C  
ATOM   2641  C   CYS B 211    -112.733  -4.024  14.569  1.00 47.01           C  
ATOM   2642  O   CYS B 211    -113.083  -5.087  14.040  1.00 41.13           O  
ATOM   2643  CB  CYS B 211    -111.683  -2.841  12.653  1.00 45.38           C  
ATOM   2644  SG  CYS B 211    -111.948  -1.643  11.364  1.00 38.40           S  
ATOM   2645  N   GLU B 212    -112.320  -3.933  15.840  1.00 50.96           N  
ATOM   2646  CA  GLU B 212    -112.418  -5.061  16.780  1.00 54.27           C  
ATOM   2647  C   GLU B 212    -113.827  -5.108  17.297  1.00 52.71           C  
ATOM   2648  O   GLU B 212    -114.611  -5.986  16.952  1.00 55.59           O  
ATOM   2649  CB  GLU B 212    -111.433  -4.942  17.964  1.00 54.11           C  
ATOM   2650  CG  GLU B 212    -111.689  -5.899  19.175  1.00 61.69           C  
ATOM   2651  CD  GLU B 212    -111.328  -7.373  18.902  1.00 67.52           C  
ATOM   2652  OE1 GLU B 212    -111.163  -8.150  19.877  1.00 66.98           O  
ATOM   2653  OE2 GLU B 212    -111.204  -7.754  17.716  1.00 67.10           O  
ATOM   2654  N   GLU B 213    -114.137  -4.153  18.148  1.00 46.00           N  
ATOM   2655  CA  GLU B 213    -115.483  -3.964  18.601  1.00 45.55           C  
ATOM   2656  C   GLU B 213    -116.460  -4.441  17.534  1.00 43.89           C  
ATOM   2657  O   GLU B 213    -117.414  -5.163  17.848  1.00 41.23           O  
ATOM   2658  CB  GLU B 213    -115.684  -2.482  18.890  1.00 51.81           C  
ATOM   2659  CG  GLU B 213    -116.174  -2.186  20.280  1.00 48.36           C  
ATOM   2660  CD  GLU B 213    -117.648  -2.073  20.324  1.00 47.92           C  
ATOM   2661  OE1 GLU B 213    -118.206  -2.137  21.436  1.00 50.50           O  
ATOM   2662  OE2 GLU B 213    -118.243  -1.917  19.241  1.00 41.79           O  
ATOM   2663  N   ILE B 214    -116.207  -4.065  16.275  1.00 42.85           N  
ATOM   2664  CA  ILE B 214    -117.103  -4.461  15.182  1.00 40.70           C  
ATOM   2665  C   ILE B 214    -117.077  -5.930  14.879  1.00 36.88           C  
ATOM   2666  O   ILE B 214    -118.106  -6.511  14.627  1.00 41.45           O  
ATOM   2667  CB  ILE B 214    -116.790  -3.802  13.856  1.00 39.25           C  
ATOM   2668  CG1 ILE B 214    -117.405  -2.401  13.814  1.00 32.92           C  
ATOM   2669  CG2 ILE B 214    -117.303  -4.724  12.693  1.00 28.92           C  
ATOM   2670  CD1 ILE B 214    -116.871  -1.564  12.680  1.00 32.91           C  
ATOM   2671  N   ILE B 215    -115.901  -6.530  14.839  1.00 46.05           N  
ATOM   2672  CA  ILE B 215    -115.840  -7.951  14.523  1.00 47.17           C  
ATOM   2673  C   ILE B 215    -116.519  -8.739  15.635  1.00 53.30           C  
ATOM   2674  O   ILE B 215    -117.184  -9.734  15.364  1.00 57.06           O  
ATOM   2675  CB  ILE B 215    -114.401  -8.453  14.223  1.00 42.66           C  
ATOM   2676  CG1 ILE B 215    -114.406  -9.958  13.944  1.00 37.39           C  
ATOM   2677  CG2 ILE B 215    -113.442  -8.088  15.340  1.00 39.84           C  
ATOM   2678  CD1 ILE B 215    -113.209 -10.419  13.144  1.00 37.13           C  
ATOM   2679  N   ARG B 216    -116.395  -8.271  16.873  1.00 53.84           N  
ATOM   2680  CA  ARG B 216    -117.062  -8.927  17.991  1.00 55.63           C  
ATOM   2681  C   ARG B 216    -118.572  -8.891  17.811  1.00 54.90           C  
ATOM   2682  O   ARG B 216    -119.273  -9.828  18.180  1.00 56.45           O  
ATOM   2683  CB  ARG B 216    -116.687  -8.266  19.303  1.00 62.50           C  
ATOM   2684  CG  ARG B 216    -115.290  -8.605  19.785  1.00 71.42           C  
ATOM   2685  CD  ARG B 216    -114.857  -7.643  20.878  1.00 82.39           C  
ATOM   2686  NE  ARG B 216    -116.005  -7.182  21.673  1.00 92.28           N  
ATOM   2687  CZ  ARG B 216    -116.137  -5.962  22.206  1.00 96.75           C  
ATOM   2688  NH1 ARG B 216    -115.190  -5.034  22.062  1.00 97.44           N  
ATOM   2689  NH2 ARG B 216    -117.235  -5.663  22.898  1.00 97.16           N  
ATOM   2690  N   LYS B 217    -119.069  -7.809  17.229  1.00 51.28           N  
ATOM   2691  CA  LYS B 217    -120.491  -7.678  16.948  1.00 47.59           C  
ATOM   2692  C   LYS B 217    -120.834  -8.433  15.704  1.00 41.83           C  
ATOM   2693  O   LYS B 217    -121.954  -8.342  15.235  1.00 53.56           O  
ATOM   2694  CB  LYS B 217    -120.876  -6.218  16.739  1.00 47.96           C  
ATOM   2695  CG  LYS B 217    -120.658  -5.357  17.954  1.00 51.19           C  
ATOM   2696  CD  LYS B 217    -120.718  -3.891  17.600  1.00 45.88           C  
ATOM   2697  CE  LYS B 217    -121.431  -3.081  18.662  1.00 46.29           C  
ATOM   2698  NZ  LYS B 217    -122.441  -2.227  17.990  1.00 50.15           N  
ATOM   2699  N   GLY B 218    -119.873  -9.140  15.130  1.00 39.49           N  
ATOM   2700  CA  GLY B 218    -120.179 -10.070  14.055  1.00 47.83           C  
ATOM   2701  C   GLY B 218    -120.323  -9.435  12.694  1.00 48.77           C  
ATOM   2702  O   GLY B 218    -121.354  -9.580  12.027  1.00 52.75           O  
ATOM   2703  N   GLY B 219    -119.295  -8.694  12.312  1.00 44.39           N  
ATOM   2704  CA  GLY B 219    -119.080  -8.310  10.942  1.00 48.34           C  
ATOM   2705  C   GLY B 219    -117.803  -9.033  10.630  1.00 57.90           C  
ATOM   2706  O   GLY B 219    -116.813  -8.866  11.333  1.00 60.70           O  
ATOM   2707  N   GLU B 220    -117.816  -9.861   9.599  1.00 65.96           N  
ATOM   2708  CA  GLU B 220    -116.707 -10.771   9.379  1.00 65.63           C  
ATOM   2709  C   GLU B 220    -116.226 -10.673   7.951  1.00 60.46           C  
ATOM   2710  O   GLU B 220    -115.938 -11.669   7.305  1.00 75.50           O  
ATOM   2711  CB  GLU B 220    -117.115 -12.205   9.762  1.00 69.23           C  
ATOM   2712  CG  GLU B 220    -118.568 -12.552   9.457  1.00 76.49           C  
ATOM   2713  CD  GLU B 220    -118.909 -14.002   9.748  1.00 86.17           C  
ATOM   2714  OE1 GLU B 220    -117.988 -14.778  10.080  1.00 96.92           O  
ATOM   2715  OE2 GLU B 220    -120.104 -14.369   9.635  1.00 82.72           O  
ATOM   2716  N   THR B 221    -116.126  -9.462   7.445  1.00 52.05           N  
ATOM   2717  CA  THR B 221    -115.596  -9.297   6.111  1.00 55.23           C  
ATOM   2718  C   THR B 221    -114.783  -8.021   6.071  1.00 55.05           C  
ATOM   2719  O   THR B 221    -115.125  -7.052   6.732  1.00 48.32           O  
ATOM   2720  CB  THR B 221    -116.708  -9.274   5.081  1.00 51.57           C  
ATOM   2721  OG1 THR B 221    -117.372  -8.015   5.136  1.00 54.46           O  
ATOM   2722  CG2 THR B 221    -117.708 -10.390   5.361  1.00 51.30           C  
ATOM   2723  N   SER B 222    -113.681  -8.046   5.331  1.00 49.64           N  
ATOM   2724  CA  SER B 222    -112.819  -6.896   5.244  1.00 45.19           C  
ATOM   2725  C   SER B 222    -113.435  -5.993   4.204  1.00 44.60           C  
ATOM   2726  O   SER B 222    -113.464  -6.315   3.035  1.00 51.84           O  
ATOM   2727  CB  SER B 222    -111.404  -7.308   4.855  1.00 50.83           C  
ATOM   2728  OG  SER B 222    -110.778  -8.059   5.892  1.00 53.33           O  
ATOM   2729  N   GLU B 223    -113.991  -4.887   4.664  1.00 44.46           N  
ATOM   2730  CA  GLU B 223    -114.586  -3.889   3.808  1.00 38.08           C  
ATOM   2731  C   GLU B 223    -114.502  -2.610   4.580  1.00 35.24           C  
ATOM   2732  O   GLU B 223    -113.943  -2.592   5.672  1.00 32.95           O  
ATOM   2733  CB  GLU B 223    -116.048  -4.226   3.519  1.00 45.62           C  
ATOM   2734  CG  GLU B 223    -116.990  -4.151   4.725  1.00 44.99           C  
ATOM   2735  CD  GLU B 223    -118.388  -4.722   4.445  1.00 52.91           C  
ATOM   2736  OE1 GLU B 223    -118.941  -4.479   3.349  1.00 51.11           O  
ATOM   2737  OE2 GLU B 223    -118.951  -5.419   5.329  1.00 57.38           O  
ATOM   2738  N   MET B 224    -115.071  -1.547   4.030  1.00 37.06           N  
ATOM   2739  CA  MET B 224    -115.064  -0.254   4.694  1.00 36.01           C  
ATOM   2740  C   MET B 224    -116.237  -0.150   5.612  1.00 33.18           C  
ATOM   2741  O   MET B 224    -117.365  -0.376   5.171  1.00 31.75           O  
ATOM   2742  CB  MET B 224    -115.169   0.871   3.687  1.00 42.25           C  
ATOM   2743  CG  MET B 224    -115.303   2.238   4.347  1.00 47.99           C  
ATOM   2744  SD  MET B 224    -116.962   2.953   4.227  1.00 47.22           S  
ATOM   2745  CE  MET B 224    -116.755   3.945   2.748  1.00 42.69           C  
ATOM   2746  N   TYR B 225    -115.966   0.228   6.863  1.00 30.39           N  
ATOM   2747  CA  TYR B 225    -116.972   0.270   7.938  1.00 30.72           C  
ATOM   2748  C   TYR B 225    -116.971   1.610   8.551  1.00 23.79           C  
ATOM   2749  O   TYR B 225    -115.979   2.276   8.521  1.00 21.52           O  
ATOM   2750  CB  TYR B 225    -116.616  -0.645   9.105  1.00 27.26           C  
ATOM   2751  CG  TYR B 225    -116.781  -2.090   8.843  1.00 27.43           C  
ATOM   2752  CD1 TYR B 225    -117.805  -2.796   9.428  1.00 30.99           C  
ATOM   2753  CD2 TYR B 225    -115.893  -2.764   8.026  1.00 32.54           C  
ATOM   2754  CE1 TYR B 225    -117.951  -4.144   9.208  1.00 33.71           C  
ATOM   2755  CE2 TYR B 225    -116.031  -4.098   7.798  1.00 37.64           C  
ATOM   2756  CZ  TYR B 225    -117.070  -4.788   8.395  1.00 33.34           C  
ATOM   2757  OH  TYR B 225    -117.233  -6.126   8.185  1.00 41.19           O  
ATOM   2758  N   LEU B 226    -118.060   1.958   9.204  1.00 27.47           N  
ATOM   2759  CA  LEU B 226    -118.079   3.174   9.983  1.00 36.42           C  
ATOM   2760  C   LEU B 226    -117.634   2.859  11.389  1.00 36.45           C  
ATOM   2761  O   LEU B 226    -117.864   1.775  11.882  1.00 38.66           O  
ATOM   2762  CB  LEU B 226    -119.480   3.774  10.002  1.00 33.80           C  
ATOM   2763  CG  LEU B 226    -119.540   5.270   9.736  1.00 25.95           C  
ATOM   2764  CD1 LEU B 226    -118.527   5.656   8.711  1.00 19.72           C  
ATOM   2765  CD2 LEU B 226    -120.911   5.633   9.240  1.00 26.21           C  
ATOM   2766  N   ILE B 227    -116.978   3.791  12.048  1.00 35.62           N  
ATOM   2767  CA  ILE B 227    -116.631   3.541  13.424  1.00 36.11           C  
ATOM   2768  C   ILE B 227    -116.628   4.856  14.125  1.00 35.68           C  
ATOM   2769  O   ILE B 227    -116.572   5.903  13.490  1.00 33.73           O  
ATOM   2770  CB  ILE B 227    -115.279   2.791  13.591  1.00 34.52           C  
ATOM   2771  CG1 ILE B 227    -114.112   3.756  13.759  1.00 35.56           C  
ATOM   2772  CG2 ILE B 227    -115.022   1.868  12.417  1.00 32.19           C  
ATOM   2773  CD1 ILE B 227    -112.793   3.163  13.291  1.00 45.56           C  
ATOM   2774  N   GLN B 228    -116.727   4.778  15.441  1.00 39.12           N  
ATOM   2775  CA  GLN B 228    -116.862   5.943  16.261  1.00 42.98           C  
ATOM   2776  C   GLN B 228    -116.301   5.601  17.614  1.00 40.23           C  
ATOM   2777  O   GLN B 228    -117.008   5.138  18.493  1.00 40.25           O  
ATOM   2778  CB  GLN B 228    -118.317   6.394  16.358  1.00 50.12           C  
ATOM   2779  CG  GLN B 228    -118.446   7.824  16.874  1.00 50.89           C  
ATOM   2780  CD  GLN B 228    -119.768   8.091  17.543  1.00 41.66           C  
ATOM   2781  OE1 GLN B 228    -120.810   7.832  16.972  1.00 41.02           O  
ATOM   2782  NE2 GLN B 228    -119.732   8.608  18.761  1.00 45.99           N  
ATOM   2783  N   PRO B 229    -115.003   5.820  17.765  1.00 51.13           N  
ATOM   2784  CA  PRO B 229    -114.231   5.641  18.976  1.00 61.01           C  
ATOM   2785  C   PRO B 229    -114.627   6.559  20.116  1.00 65.61           C  
ATOM   2786  O   PRO B 229    -114.265   6.304  21.262  1.00 67.60           O  
ATOM   2787  CB  PRO B 229    -112.829   6.032  18.541  1.00 64.39           C  
ATOM   2788  CG  PRO B 229    -112.827   5.900  17.081  1.00 64.65           C  
ATOM   2789  CD  PRO B 229    -114.160   6.245  16.638  1.00 58.01           C  
ATOM   2790  N   ASP B 230    -115.325   7.642  19.806  1.00 72.90           N  
ATOM   2791  CA  ASP B 230    -115.587   8.664  20.806  1.00 78.67           C  
ATOM   2792  C   ASP B 230    -116.935   9.344  20.596  1.00 75.26           C  
ATOM   2793  O   ASP B 230    -117.342   9.583  19.463  1.00 67.65           O  
ATOM   2794  CB  ASP B 230    -114.470   9.711  20.751  1.00 84.32           C  
ATOM   2795  CG  ASP B 230    -114.395  10.550  22.004  1.00 89.79           C  
ATOM   2796  OD1 ASP B 230    -115.345  10.478  22.821  1.00 82.72           O  
ATOM   2797  OD2 ASP B 230    -113.387  11.282  22.166  1.00 95.22           O  
ATOM   2798  N   SER B 231    -117.621   9.653  21.692  1.00 71.62           N  
ATOM   2799  CA  SER B 231    -118.820  10.472  21.636  1.00 71.79           C  
ATOM   2800  C   SER B 231    -118.442  11.946  21.423  1.00 69.95           C  
ATOM   2801  O   SER B 231    -119.293  12.777  21.123  1.00 62.64           O  
ATOM   2802  CB  SER B 231    -119.629  10.305  22.913  1.00 79.35           C  
ATOM   2803  OG  SER B 231    -118.856  10.659  24.050  1.00 88.13           O  
ATOM   2804  N   SER B 232    -117.160  12.260  21.585  1.00 71.75           N  
ATOM   2805  CA  SER B 232    -116.619  13.551  21.163  1.00 74.75           C  
ATOM   2806  C   SER B 232    -116.094  13.464  19.722  1.00 77.52           C  
ATOM   2807  O   SER B 232    -114.964  13.880  19.457  1.00 83.52           O  
ATOM   2808  CB  SER B 232    -115.463  13.987  22.084  1.00 73.87           C  
ATOM   2809  OG  SER B 232    -115.818  13.946  23.449  1.00 75.57           O  
ATOM   2810  N   VAL B 233    -116.888  12.929  18.795  1.00 73.82           N  
ATOM   2811  CA  VAL B 233    -116.423  12.715  17.412  1.00 75.42           C  
ATOM   2812  C   VAL B 233    -117.547  12.247  16.494  1.00 72.84           C  
ATOM   2813  O   VAL B 233    -118.361  11.406  16.879  1.00 75.48           O  
ATOM   2814  CB  VAL B 233    -115.260  11.655  17.331  1.00 79.10           C  
ATOM   2815  CG1 VAL B 233    -115.777  10.240  17.479  1.00 70.21           C  
ATOM   2816  CG2 VAL B 233    -114.509  11.777  16.013  1.00 85.70           C  
ATOM   2817  N   LYS B 234    -117.608  12.779  15.279  1.00 67.71           N  
ATOM   2818  CA  LYS B 234    -118.551  12.218  14.334  1.00 65.21           C  
ATOM   2819  C   LYS B 234    -117.916  10.957  13.813  1.00 54.99           C  
ATOM   2820  O   LYS B 234    -116.704  10.887  13.662  1.00 54.17           O  
ATOM   2821  CB  LYS B 234    -118.936  13.172  13.189  1.00 79.96           C  
ATOM   2822  CG  LYS B 234    -118.158  13.037  11.842  1.00 85.28           C  
ATOM   2823  CD  LYS B 234    -119.102  13.229  10.613  1.00 82.45           C  
ATOM   2824  CE  LYS B 234    -118.349  13.634   9.324  1.00 76.07           C  
ATOM   2825  NZ  LYS B 234    -116.983  13.025   9.152  1.00 60.95           N  
ATOM   2826  N   PRO B 235    -118.736   9.949  13.563  1.00 48.98           N  
ATOM   2827  CA  PRO B 235    -118.335   8.710  12.959  1.00 51.84           C  
ATOM   2828  C   PRO B 235    -117.642   8.854  11.611  1.00 47.18           C  
ATOM   2829  O   PRO B 235    -118.169   9.495  10.707  1.00 40.28           O  
ATOM   2830  CB  PRO B 235    -119.670   7.999  12.759  1.00 56.68           C  
ATOM   2831  CG  PRO B 235    -120.449   8.403  13.886  1.00 55.75           C  
ATOM   2832  CD  PRO B 235    -120.083   9.840  14.136  1.00 56.74           C  
ATOM   2833  N   TYR B 236    -116.491   8.203  11.488  1.00 44.40           N  
ATOM   2834  CA  TYR B 236    -115.753   8.139  10.243  1.00 42.24           C  
ATOM   2835  C   TYR B 236    -115.516   6.682   9.788  1.00 40.17           C  
ATOM   2836  O   TYR B 236    -115.875   5.715  10.474  1.00 35.29           O  
ATOM   2837  CB  TYR B 236    -114.432   8.874  10.410  1.00 44.38           C  
ATOM   2838  CG  TYR B 236    -113.535   8.349  11.517  1.00 43.23           C  
ATOM   2839  CD1 TYR B 236    -113.585   8.904  12.781  1.00 41.11           C  
ATOM   2840  CD2 TYR B 236    -112.620   7.314  11.286  1.00 45.67           C  
ATOM   2841  CE1 TYR B 236    -112.765   8.454  13.792  1.00 47.79           C  
ATOM   2842  CE2 TYR B 236    -111.778   6.854  12.299  1.00 42.82           C  
ATOM   2843  CZ  TYR B 236    -111.855   7.434  13.554  1.00 46.68           C  
ATOM   2844  OH  TYR B 236    -111.031   7.023  14.587  1.00 38.63           O  
ATOM   2845  N   ARG B 237    -114.896   6.557   8.623  1.00 34.84           N  
ATOM   2846  CA  ARG B 237    -114.815   5.314   7.919  1.00 31.46           C  
ATOM   2847  C   ARG B 237    -113.373   4.921   7.834  1.00 26.40           C  
ATOM   2848  O   ARG B 237    -112.519   5.722   7.598  1.00 24.76           O  
ATOM   2849  CB  ARG B 237    -115.367   5.431   6.499  1.00 33.37           C  
ATOM   2850  CG  ARG B 237    -115.880   6.782   6.155  1.00 36.52           C  
ATOM   2851  CD  ARG B 237    -116.635   6.779   4.869  1.00 37.38           C  
ATOM   2852  NE  ARG B 237    -117.793   7.654   4.991  1.00 40.08           N  
ATOM   2853  CZ  ARG B 237    -118.749   7.773   4.082  1.00 46.34           C  
ATOM   2854  NH1 ARG B 237    -118.704   7.081   2.944  1.00 55.34           N  
ATOM   2855  NH2 ARG B 237    -119.760   8.590   4.315  1.00 49.41           N  
ATOM   2856  N   VAL B 238    -113.153   3.636   7.969  1.00 32.01           N  
ATOM   2857  CA  VAL B 238    -111.872   3.055   8.086  1.00 30.10           C  
ATOM   2858  C   VAL B 238    -112.055   1.649   7.609  1.00 31.55           C  
ATOM   2859  O   VAL B 238    -113.009   0.993   8.006  1.00 29.80           O  
ATOM   2860  CB  VAL B 238    -111.480   2.951   9.550  1.00 34.19           C  
ATOM   2861  CG1 VAL B 238    -110.052   2.445   9.643  1.00 48.79           C  
ATOM   2862  CG2 VAL B 238    -111.645   4.299  10.248  1.00 37.21           C  
ATOM   2863  N   TYR B 239    -111.134   1.181   6.780  1.00 37.58           N  
ATOM   2864  CA  TYR B 239    -111.127  -0.205   6.363  1.00 31.33           C  
ATOM   2865  C   TYR B 239    -110.839  -1.081   7.574  1.00 33.29           C  
ATOM   2866  O   TYR B 239    -109.883  -0.852   8.319  1.00 32.54           O  
ATOM   2867  CB  TYR B 239    -110.066  -0.423   5.305  1.00 29.82           C  
ATOM   2868  CG  TYR B 239    -110.312  -1.636   4.482  1.00 35.77           C  
ATOM   2869  CD1 TYR B 239    -109.779  -2.871   4.838  1.00 45.96           C  
ATOM   2870  CD2 TYR B 239    -111.066  -1.562   3.343  1.00 40.31           C  
ATOM   2871  CE1 TYR B 239    -110.001  -3.998   4.069  1.00 41.55           C  
ATOM   2872  CE2 TYR B 239    -111.288  -2.679   2.563  1.00 46.11           C  
ATOM   2873  CZ  TYR B 239    -110.758  -3.891   2.930  1.00 41.70           C  
ATOM   2874  OH  TYR B 239    -111.001  -4.986   2.155  1.00 40.28           O  
ATOM   2875  N   CYS B 240    -111.695  -2.066   7.787  1.00 33.67           N  
ATOM   2876  CA  CYS B 240    -111.418  -3.100   8.737  1.00 28.89           C  
ATOM   2877  C   CYS B 240    -110.777  -4.216   7.991  1.00 28.75           C  
ATOM   2878  O   CYS B 240    -111.276  -4.632   6.953  1.00 28.10           O  
ATOM   2879  CB  CYS B 240    -112.703  -3.616   9.306  1.00 31.26           C  
ATOM   2880  SG  CYS B 240    -113.477  -2.485  10.377  1.00 33.77           S  
ATOM   2881  N   ASP B 241    -109.656  -4.696   8.503  1.00 37.19           N  
ATOM   2882  CA  ASP B 241    -109.165  -5.990   8.078  1.00 40.01           C  
ATOM   2883  C   ASP B 241    -109.621  -7.079   9.009  1.00 34.44           C  
ATOM   2884  O   ASP B 241    -109.195  -7.154  10.144  1.00 40.08           O  
ATOM   2885  CB  ASP B 241    -107.666  -6.053   8.021  1.00 38.65           C  
ATOM   2886  CG  ASP B 241    -107.219  -7.336   7.455  1.00 38.93           C  
ATOM   2887  OD1 ASP B 241    -105.987  -7.543   7.331  1.00 41.09           O  
ATOM   2888  OD2 ASP B 241    -108.152  -8.112   7.102  1.00 39.57           O  
ATOM   2889  N   MET B 242    -110.458  -7.957   8.516  1.00 36.03           N  
ATOM   2890  CA  MET B 242    -111.132  -8.869   9.396  1.00 44.63           C  
ATOM   2891  C   MET B 242    -110.656 -10.307   9.152  1.00 54.01           C  
ATOM   2892  O   MET B 242    -111.243 -11.269   9.648  1.00 55.20           O  
ATOM   2893  CB  MET B 242    -112.635  -8.704   9.183  1.00 45.88           C  
ATOM   2894  CG  MET B 242    -113.066  -7.268   9.327  1.00 39.03           C  
ATOM   2895  SD  MET B 242    -113.071  -6.742  11.044  1.00 33.84           S  
ATOM   2896  CE  MET B 242    -114.836  -6.395  11.184  1.00 39.85           C  
ATOM   2897  N   ASN B 243    -109.556 -10.439   8.419  1.00 53.48           N  
ATOM   2898  CA  ASN B 243    -109.030 -11.735   8.045  1.00 51.42           C  
ATOM   2899  C   ASN B 243    -107.676 -12.009   8.652  1.00 54.04           C  
ATOM   2900  O   ASN B 243    -107.471 -13.049   9.283  1.00 70.91           O  
ATOM   2901  CB  ASN B 243    -108.942 -11.825   6.531  1.00 50.37           C  
ATOM   2902  CG  ASN B 243    -110.293 -11.828   5.896  1.00 49.62           C  
ATOM   2903  OD1 ASN B 243    -110.621 -10.971   5.085  1.00 54.07           O  
ATOM   2904  ND2 ASN B 243    -111.110 -12.780   6.291  1.00 58.77           N  
ATOM   2905  N   THR B 244    -106.741 -11.094   8.478  1.00 45.10           N  
ATOM   2906  CA  THR B 244    -105.389 -11.420   8.841  1.00 54.26           C  
ATOM   2907  C   THR B 244    -105.235 -11.386  10.360  1.00 58.77           C  
ATOM   2908  O   THR B 244    -105.569 -10.383  10.996  1.00 49.62           O  
ATOM   2909  CB  THR B 244    -104.394 -10.506   8.162  1.00 56.44           C  
ATOM   2910  OG1 THR B 244    -104.296  -9.285   8.899  1.00 53.55           O  
ATOM   2911  CG2 THR B 244    -104.826 -10.259   6.705  1.00 53.01           C  
ATOM   2912  N   GLU B 245    -104.759 -12.514  10.908  1.00 57.64           N  
ATOM   2913  CA  GLU B 245    -104.520 -12.698  12.339  1.00 55.35           C  
ATOM   2914  C   GLU B 245    -105.780 -12.484  13.152  1.00 57.65           C  
ATOM   2915  O   GLU B 245    -105.846 -11.586  13.999  1.00 53.83           O  
ATOM   2916  CB  GLU B 245    -103.393 -11.796  12.840  1.00 58.24           C  
ATOM   2917  CG  GLU B 245    -102.064 -12.014  12.114  1.00 65.45           C  
ATOM   2918  CD  GLU B 245    -100.868 -12.087  13.061  1.00 75.65           C  
ATOM   2919  OE1 GLU B 245     -99.808 -11.464  12.783  1.00 76.63           O  
ATOM   2920  OE2 GLU B 245    -100.988 -12.780  14.096  1.00 83.26           O  
ATOM   2921  N   ASN B 246    -106.776 -13.324  12.866  1.00 60.03           N  
ATOM   2922  CA  ASN B 246    -108.070 -13.319  13.557  1.00 59.13           C  
ATOM   2923  C   ASN B 246    -108.869 -12.029  13.394  1.00 56.97           C  
ATOM   2924  O   ASN B 246    -109.752 -11.747  14.212  1.00 56.34           O  
ATOM   2925  CB  ASN B 246    -107.903 -13.591  15.061  1.00 62.98           C  
ATOM   2926  CG  ASN B 246    -107.103 -14.834  15.353  1.00 63.51           C  
ATOM   2927  OD1 ASN B 246    -107.481 -15.935  14.953  1.00 69.89           O  
ATOM   2928  ND2 ASN B 246    -105.996 -14.670  16.074  1.00 60.65           N  
ATOM   2929  N   GLY B 247    -108.571 -11.247  12.358  1.00 56.31           N  
ATOM   2930  CA  GLY B 247    -109.293  -9.997  12.103  1.00 53.23           C  
ATOM   2931  C   GLY B 247    -109.204  -9.012  13.250  1.00 47.22           C  
ATOM   2932  O   GLY B 247    -108.367  -9.154  14.133  1.00 47.57           O  
ATOM   2933  N   GLY B 248    -110.080  -8.019  13.245  1.00 42.92           N  
ATOM   2934  CA  GLY B 248    -110.078  -6.991  14.288  1.00 45.06           C  
ATOM   2935  C   GLY B 248    -109.187  -5.797  13.968  1.00 43.24           C  
ATOM   2936  O   GLY B 248    -108.969  -4.911  14.797  1.00 42.96           O  
ATOM   2937  N   TRP B 249    -108.696  -5.739  12.745  1.00 40.00           N  
ATOM   2938  CA  TRP B 249    -107.588  -4.871  12.452  1.00 41.67           C  
ATOM   2939  C   TRP B 249    -108.043  -3.624  11.776  1.00 38.58           C  
ATOM   2940  O   TRP B 249    -108.522  -3.677  10.650  1.00 41.61           O  
ATOM   2941  CB  TRP B 249    -106.590  -5.604  11.573  1.00 50.03           C  
ATOM   2942  CG  TRP B 249    -105.808  -6.604  12.335  1.00 51.17           C  
ATOM   2943  CD1 TRP B 249    -105.981  -7.951  12.342  1.00 50.34           C  
ATOM   2944  CD2 TRP B 249    -104.746  -6.327  13.228  1.00 46.17           C  
ATOM   2945  NE1 TRP B 249    -105.076  -8.535  13.179  1.00 49.62           N  
ATOM   2946  CE2 TRP B 249    -104.305  -7.554  13.740  1.00 44.95           C  
ATOM   2947  CE3 TRP B 249    -104.121  -5.155  13.643  1.00 52.62           C  
ATOM   2948  CZ2 TRP B 249    -103.270  -7.647  14.639  1.00 48.44           C  
ATOM   2949  CZ3 TRP B 249    -103.101  -5.244  14.536  1.00 56.16           C  
ATOM   2950  CH2 TRP B 249    -102.678  -6.486  15.028  1.00 55.96           C  
ATOM   2951  N   THR B 250    -107.887  -2.498  12.459  1.00 37.47           N  
ATOM   2952  CA  THR B 250    -108.192  -1.207  11.861  1.00 37.35           C  
ATOM   2953  C   THR B 250    -107.024  -0.754  11.010  1.00 42.39           C  
ATOM   2954  O   THR B 250    -105.903  -0.663  11.493  1.00 47.06           O  
ATOM   2955  CB  THR B 250    -108.425  -0.163  12.920  1.00 34.20           C  
ATOM   2956  OG1 THR B 250    -109.435  -0.629  13.826  1.00 38.08           O  
ATOM   2957  CG2 THR B 250    -108.816   1.143  12.275  1.00 30.84           C  
ATOM   2958  N   VAL B 251    -107.277  -0.473   9.742  1.00 43.82           N  
ATOM   2959  CA  VAL B 251    -106.209  -0.061   8.853  1.00 40.83           C  
ATOM   2960  C   VAL B 251    -105.942   1.426   9.053  1.00 42.47           C  
ATOM   2961  O   VAL B 251    -106.855   2.250   8.994  1.00 39.63           O  
ATOM   2962  CB  VAL B 251    -106.536  -0.387   7.402  1.00 38.65           C  
ATOM   2963  CG1 VAL B 251    -105.564   0.320   6.473  1.00 37.41           C  
ATOM   2964  CG2 VAL B 251    -106.500  -1.903   7.210  1.00 36.82           C  
ATOM   2965  N   ILE B 252    -104.669   1.727   9.299  1.00 43.45           N  
ATOM   2966  CA  ILE B 252    -104.173   3.052   9.671  1.00 40.91           C  
ATOM   2967  C   ILE B 252    -103.505   3.706   8.483  1.00 40.23           C  
ATOM   2968  O   ILE B 252    -103.595   4.910   8.307  1.00 43.36           O  
ATOM   2969  CB  ILE B 252    -103.112   2.907  10.775  1.00 42.87           C  
ATOM   2970  CG1 ILE B 252    -103.757   2.863  12.142  1.00 44.21           C  
ATOM   2971  CG2 ILE B 252    -102.126   4.019  10.774  1.00 39.10           C  
ATOM   2972  CD1 ILE B 252    -102.724   2.595  13.192  1.00 51.10           C  
ATOM   2973  N   GLN B 253    -102.825   2.898   7.677  1.00 37.98           N  
ATOM   2974  CA  GLN B 253    -102.066   3.384   6.540  1.00 34.65           C  
ATOM   2975  C   GLN B 253    -101.955   2.272   5.507  1.00 34.31           C  
ATOM   2976  O   GLN B 253    -101.896   1.103   5.871  1.00 33.81           O  
ATOM   2977  CB  GLN B 253    -100.702   3.808   7.022  1.00 30.33           C  
ATOM   2978  CG  GLN B 253     -99.730   4.151   5.920  1.00 35.84           C  
ATOM   2979  CD  GLN B 253     -98.892   2.985   5.496  1.00 33.17           C  
ATOM   2980  OE1 GLN B 253     -97.801   3.155   4.988  1.00 38.66           O  
ATOM   2981  NE2 GLN B 253     -99.388   1.793   5.716  1.00 39.10           N  
ATOM   2982  N   ASN B 254    -101.921   2.609   4.226  1.00 30.44           N  
ATOM   2983  CA  ASN B 254    -101.972   1.564   3.230  1.00 32.13           C  
ATOM   2984  C   ASN B 254    -101.433   1.939   1.876  1.00 39.44           C  
ATOM   2985  O   ASN B 254    -101.842   2.943   1.302  1.00 44.33           O  
ATOM   2986  CB  ASN B 254    -103.404   1.096   3.058  1.00 36.24           C  
ATOM   2987  CG  ASN B 254    -103.505  -0.187   2.260  1.00 34.80           C  
ATOM   2988  OD1 ASN B 254    -102.888  -1.203   2.600  1.00 34.79           O  
ATOM   2989  ND2 ASN B 254    -104.306  -0.156   1.205  1.00 34.58           N  
ATOM   2990  N   ARG B 255    -100.541   1.085   1.370  1.00 45.90           N  
ATOM   2991  CA  ARG B 255     -99.858   1.265   0.096  1.00 42.22           C  
ATOM   2992  C   ARG B 255     -99.955  -0.032  -0.689  1.00 39.05           C  
ATOM   2993  O   ARG B 255     -99.637  -1.092  -0.155  1.00 43.21           O  
ATOM   2994  CB  ARG B 255     -98.371   1.587   0.304  1.00 41.44           C  
ATOM   2995  CG  ARG B 255     -98.054   2.588   1.384  1.00 40.65           C  
ATOM   2996  CD  ARG B 255     -98.686   3.949   1.153  1.00 42.61           C  
ATOM   2997  NE  ARG B 255     -98.191   4.645  -0.032  1.00 44.24           N  
ATOM   2998  CZ  ARG B 255     -96.999   5.235  -0.138  1.00 45.50           C  
ATOM   2999  NH1 ARG B 255     -96.113   5.223   0.858  1.00 41.12           N  
ATOM   3000  NH2 ARG B 255     -96.684   5.838  -1.276  1.00 49.31           N  
ATOM   3001  N   GLN B 256    -100.377   0.049  -1.946  1.00 35.04           N  
ATOM   3002  CA  GLN B 256    -100.422  -1.126  -2.798  1.00 33.68           C  
ATOM   3003  C   GLN B 256    -100.309  -0.889  -4.291  1.00 34.92           C  
ATOM   3004  O   GLN B 256    -100.235  -1.842  -5.058  1.00 41.86           O  
ATOM   3005  CB  GLN B 256    -101.696  -1.893  -2.509  1.00 38.29           C  
ATOM   3006  CG  GLN B 256    -102.978  -1.097  -2.629  1.00 43.75           C  
ATOM   3007  CD  GLN B 256    -104.063  -1.687  -1.768  1.00 41.13           C  
ATOM   3008  OE1 GLN B 256    -105.221  -1.248  -1.782  1.00 32.70           O  
ATOM   3009  NE2 GLN B 256    -103.684  -2.700  -0.990  1.00 41.06           N  
ATOM   3010  N   ASP B 257    -100.292   0.372  -4.694  1.00 36.72           N  
ATOM   3011  CA  ASP B 257    -100.220   0.779  -6.089  1.00 39.04           C  
ATOM   3012  C   ASP B 257     -99.757   2.237  -6.071  1.00 46.26           C  
ATOM   3013  O   ASP B 257     -99.322   2.738  -5.030  1.00 46.19           O  
ATOM   3014  CB  ASP B 257    -101.597   0.633  -6.741  1.00 42.32           C  
ATOM   3015  CG  ASP B 257    -102.729   1.034  -5.807  1.00 43.79           C  
ATOM   3016  OD1 ASP B 257    -102.427   1.347  -4.641  1.00 41.24           O  
ATOM   3017  OD2 ASP B 257    -103.912   1.033  -6.222  1.00 43.73           O  
ATOM   3018  N   GLY B 258     -99.826   2.932  -7.198  1.00 48.94           N  
ATOM   3019  CA  GLY B 258     -99.418   4.337  -7.211  1.00 46.64           C  
ATOM   3020  C   GLY B 258    -100.528   5.286  -6.830  1.00 40.04           C  
ATOM   3021  O   GLY B 258    -100.264   6.378  -6.378  1.00 44.17           O  
ATOM   3022  N   SER B 259    -101.766   4.853  -7.013  1.00 33.76           N  
ATOM   3023  CA  SER B 259    -102.973   5.664  -6.796  1.00 39.24           C  
ATOM   3024  C   SER B 259    -102.917   6.984  -5.979  1.00 46.09           C  
ATOM   3025  O   SER B 259    -103.595   7.969  -6.350  1.00 40.43           O  
ATOM   3026  CB  SER B 259    -104.030   4.770  -6.174  1.00 37.35           C  
ATOM   3027  OG  SER B 259    -103.489   4.115  -5.049  1.00 41.20           O  
ATOM   3028  N   VAL B 260    -102.170   7.003  -4.870  1.00 41.65           N  
ATOM   3029  CA  VAL B 260    -102.259   8.115  -3.904  1.00 41.22           C  
ATOM   3030  C   VAL B 260    -100.932   8.828  -3.651  1.00 40.95           C  
ATOM   3031  O   VAL B 260     -99.986   8.146  -3.318  1.00 40.76           O  
ATOM   3032  CB  VAL B 260    -102.738   7.583  -2.556  1.00 34.38           C  
ATOM   3033  CG1 VAL B 260    -102.812   8.706  -1.560  1.00 38.46           C  
ATOM   3034  CG2 VAL B 260    -104.081   6.939  -2.701  1.00 36.43           C  
ATOM   3035  N   ASP B 261    -100.875  10.170  -3.770  1.00 43.06           N  
ATOM   3036  CA  ASP B 261     -99.650  10.963  -3.479  1.00 43.21           C  
ATOM   3037  C   ASP B 261     -99.487  11.113  -1.989  1.00 41.48           C  
ATOM   3038  O   ASP B 261    -100.386  11.632  -1.357  1.00 45.02           O  
ATOM   3039  CB  ASP B 261     -99.724  12.388  -4.083  1.00 57.93           C  
ATOM   3040  CG  ASP B 261     -98.434  13.256  -3.813  1.00 62.44           C  
ATOM   3041  OD1 ASP B 261     -97.394  12.729  -3.361  1.00 57.55           O  
ATOM   3042  OD2 ASP B 261     -98.455  14.485  -4.066  1.00 60.11           O  
ATOM   3043  N   PHE B 262     -98.332  10.716  -1.441  1.00 44.89           N  
ATOM   3044  CA  PHE B 262     -98.102  10.746   0.012  1.00 40.42           C  
ATOM   3045  C   PHE B 262     -97.223  11.889   0.441  1.00 41.55           C  
ATOM   3046  O   PHE B 262     -97.018  12.099   1.626  1.00 44.98           O  
ATOM   3047  CB  PHE B 262     -97.517   9.430   0.506  1.00 40.36           C  
ATOM   3048  CG  PHE B 262     -98.549   8.479   1.024  1.00 43.13           C  
ATOM   3049  CD1 PHE B 262     -99.562   8.028   0.202  1.00 50.75           C  
ATOM   3050  CD2 PHE B 262     -98.514   8.030   2.324  1.00 51.05           C  
ATOM   3051  CE1 PHE B 262    -100.528   7.151   0.663  1.00 54.57           C  
ATOM   3052  CE2 PHE B 262     -99.483   7.141   2.798  1.00 55.71           C  
ATOM   3053  CZ  PHE B 262    -100.495   6.710   1.962  1.00 54.68           C  
ATOM   3054  N   GLY B 263     -96.723  12.650  -0.519  1.00 45.79           N  
ATOM   3055  CA  GLY B 263     -95.975  13.853  -0.217  1.00 47.32           C  
ATOM   3056  C   GLY B 263     -96.928  15.009  -0.049  1.00 46.57           C  
ATOM   3057  O   GLY B 263     -97.085  15.812  -0.961  1.00 52.01           O  
ATOM   3058  N   ARG B 264     -97.561  15.077   1.121  1.00 46.11           N  
ATOM   3059  CA  ARG B 264     -98.524  16.117   1.456  1.00 43.62           C  
ATOM   3060  C   ARG B 264     -98.079  16.935   2.668  1.00 40.43           C  
ATOM   3061  O   ARG B 264     -97.183  16.533   3.400  1.00 41.74           O  
ATOM   3062  CB  ARG B 264     -99.859  15.464   1.770  1.00 48.59           C  
ATOM   3063  CG  ARG B 264    -100.525  14.740   0.615  1.00 47.24           C  
ATOM   3064  CD  ARG B 264    -101.950  14.339   1.021  1.00 49.23           C  
ATOM   3065  NE  ARG B 264    -102.523  13.389   0.073  1.00 51.55           N  
ATOM   3066  CZ  ARG B 264    -103.346  13.681  -0.935  1.00 55.99           C  
ATOM   3067  NH1 ARG B 264    -103.771  14.922  -1.165  1.00 56.39           N  
ATOM   3068  NH2 ARG B 264    -103.755  12.700  -1.728  1.00 60.30           N  
ATOM   3069  N   LYS B 265     -98.726  18.071   2.895  1.00 39.90           N  
ATOM   3070  CA  LYS B 265     -98.387  18.937   4.026  1.00 45.26           C  
ATOM   3071  C   LYS B 265     -98.949  18.453   5.366  1.00 43.36           C  
ATOM   3072  O   LYS B 265     -99.751  17.536   5.416  1.00 44.30           O  
ATOM   3073  CB  LYS B 265     -98.887  20.353   3.765  1.00 54.79           C  
ATOM   3074  CG  LYS B 265     -98.123  21.116   2.710  1.00 58.28           C  
ATOM   3075  CD  LYS B 265     -98.880  22.396   2.367  1.00 65.56           C  
ATOM   3076  CE  LYS B 265     -97.970  23.522   1.896  1.00 66.40           C  
ATOM   3077  NZ  LYS B 265     -97.309  24.213   3.046  1.00 68.38           N  
ATOM   3078  N   TRP B 266     -98.530  19.116   6.443  1.00 47.94           N  
ATOM   3079  CA  TRP B 266     -98.874  18.748   7.819  1.00 49.00           C  
ATOM   3080  C   TRP B 266    -100.355  18.573   8.018  1.00 50.24           C  
ATOM   3081  O   TRP B 266    -100.820  17.493   8.366  1.00 53.75           O  
ATOM   3082  CB  TRP B 266     -98.358  19.819   8.794  1.00 52.99           C  
ATOM   3083  CG  TRP B 266     -98.746  19.651  10.255  1.00 47.22           C  
ATOM   3084  CD1 TRP B 266     -99.861  20.130  10.851  1.00 49.60           C  
ATOM   3085  CD2 TRP B 266     -97.992  19.003  11.289  1.00 37.16           C  
ATOM   3086  NE1 TRP B 266     -99.868  19.807  12.182  1.00 46.76           N  
ATOM   3087  CE2 TRP B 266     -98.733  19.108  12.475  1.00 35.53           C  
ATOM   3088  CE3 TRP B 266     -96.779  18.327  11.320  1.00 46.40           C  
ATOM   3089  CZ2 TRP B 266     -98.299  18.579  13.680  1.00 40.27           C  
ATOM   3090  CZ3 TRP B 266     -96.339  17.798  12.527  1.00 49.85           C  
ATOM   3091  CH2 TRP B 266     -97.095  17.930  13.686  1.00 50.94           C  
ATOM   3092  N   ASP B 267    -101.112  19.633   7.820  1.00 56.07           N  
ATOM   3093  CA  ASP B 267    -102.532  19.545   8.110  1.00 61.38           C  
ATOM   3094  C   ASP B 267    -103.132  18.264   7.470  1.00 58.94           C  
ATOM   3095  O   ASP B 267    -103.722  17.437   8.177  1.00 52.79           O  
ATOM   3096  CB  ASP B 267    -103.264  20.843   7.721  1.00 66.02           C  
ATOM   3097  CG  ASP B 267    -104.673  20.923   8.293  1.00 81.00           C  
ATOM   3098  OD1 ASP B 267    -105.075  20.041   9.087  1.00 85.34           O  
ATOM   3099  OD2 ASP B 267    -105.393  21.886   7.948  1.00 95.36           O  
ATOM   3100  N   PRO B 268    -102.944  18.061   6.151  1.00 54.61           N  
ATOM   3101  CA  PRO B 268    -103.467  16.825   5.581  1.00 51.61           C  
ATOM   3102  C   PRO B 268    -103.109  15.573   6.347  1.00 42.20           C  
ATOM   3103  O   PRO B 268    -103.974  14.746   6.579  1.00 43.12           O  
ATOM   3104  CB  PRO B 268    -102.849  16.798   4.189  1.00 51.32           C  
ATOM   3105  CG  PRO B 268    -102.798  18.209   3.812  1.00 56.39           C  
ATOM   3106  CD  PRO B 268    -102.593  19.012   5.086  1.00 56.34           C  
ATOM   3107  N   TYR B 269    -101.856  15.421   6.739  1.00 43.00           N  
ATOM   3108  CA  TYR B 269    -101.472  14.225   7.470  1.00 42.33           C  
ATOM   3109  C   TYR B 269    -102.257  14.146   8.771  1.00 48.73           C  
ATOM   3110  O   TYR B 269    -102.542  13.045   9.282  1.00 46.40           O  
ATOM   3111  CB  TYR B 269     -99.974  14.197   7.731  1.00 41.77           C  
ATOM   3112  CG  TYR B 269     -99.241  13.341   6.747  1.00 44.69           C  
ATOM   3113  CD1 TYR B 269     -99.102  11.983   6.969  1.00 48.98           C  
ATOM   3114  CD2 TYR B 269     -98.704  13.872   5.582  1.00 46.05           C  
ATOM   3115  CE1 TYR B 269     -98.417  11.172   6.073  1.00 46.04           C  
ATOM   3116  CE2 TYR B 269     -98.029  13.060   4.673  1.00 44.49           C  
ATOM   3117  CZ  TYR B 269     -97.894  11.715   4.935  1.00 39.10           C  
ATOM   3118  OH  TYR B 269     -97.238  10.898   4.075  1.00 38.30           O  
ATOM   3119  N   LYS B 270    -102.632  15.319   9.280  1.00 47.38           N  
ATOM   3120  CA  LYS B 270    -103.375  15.413  10.526  1.00 45.01           C  
ATOM   3121  C   LYS B 270    -104.850  15.032  10.351  1.00 44.84           C  
ATOM   3122  O   LYS B 270    -105.452  14.399  11.240  1.00 42.99           O  
ATOM   3123  CB  LYS B 270    -103.199  16.804  11.130  1.00 46.90           C  
ATOM   3124  CG  LYS B 270    -104.354  17.300  11.961  1.00 48.60           C  
ATOM   3125  CD  LYS B 270    -103.980  18.579  12.676  1.00 50.96           C  
ATOM   3126  CE  LYS B 270    -105.199  19.264  13.210  1.00 54.80           C  
ATOM   3127  NZ  LYS B 270    -105.922  18.383  14.160  1.00 56.93           N  
ATOM   3128  N   GLN B 271    -105.421  15.384   9.201  1.00 46.01           N  
ATOM   3129  CA  GLN B 271    -106.819  15.037   8.905  1.00 42.87           C  
ATOM   3130  C   GLN B 271    -106.898  13.641   8.346  1.00 40.86           C  
ATOM   3131  O   GLN B 271    -107.869  12.948   8.595  1.00 52.31           O  
ATOM   3132  CB  GLN B 271    -107.459  15.983   7.887  1.00 41.63           C  
ATOM   3133  CG  GLN B 271    -107.247  17.466   8.155  1.00 43.09           C  
ATOM   3134  CD  GLN B 271    -108.160  18.016   9.211  1.00 38.31           C  
ATOM   3135  OE1 GLN B 271    -107.999  17.747  10.401  1.00 40.05           O  
ATOM   3136  NE2 GLN B 271    -109.123  18.817   8.784  1.00 47.62           N  
ATOM   3137  N   GLY B 272    -105.870  13.231   7.603  1.00 38.95           N  
ATOM   3138  CA  GLY B 272    -105.889  11.992   6.836  1.00 35.35           C  
ATOM   3139  C   GLY B 272    -106.240  12.284   5.387  1.00 36.12           C  
ATOM   3140  O   GLY B 272    -106.813  13.316   5.068  1.00 37.51           O  
ATOM   3141  N   PHE B 273    -105.903  11.370   4.496  1.00 42.65           N  
ATOM   3142  CA  PHE B 273    -106.082  11.620   3.082  1.00 39.65           C  
ATOM   3143  C   PHE B 273    -106.121  10.365   2.250  1.00 40.49           C  
ATOM   3144  O   PHE B 273    -105.858   9.233   2.727  1.00 34.58           O  
ATOM   3145  CB  PHE B 273    -104.943  12.498   2.557  1.00 50.66           C  
ATOM   3146  CG  PHE B 273    -103.563  11.904   2.746  1.00 52.35           C  
ATOM   3147  CD1 PHE B 273    -103.102  10.888   1.925  1.00 51.16           C  
ATOM   3148  CD2 PHE B 273    -102.716  12.382   3.745  1.00 56.04           C  
ATOM   3149  CE1 PHE B 273    -101.822  10.350   2.107  1.00 52.45           C  
ATOM   3150  CE2 PHE B 273    -101.435  11.859   3.924  1.00 48.31           C  
ATOM   3151  CZ  PHE B 273    -100.991  10.847   3.108  1.00 50.20           C  
ATOM   3152  N   GLY B 274    -106.418  10.610   0.979  1.00 36.47           N  
ATOM   3153  CA  GLY B 274    -106.444   9.590  -0.024  1.00 34.68           C  
ATOM   3154  C   GLY B 274    -107.827   9.006  -0.054  1.00 36.65           C  
ATOM   3155  O   GLY B 274    -108.808   9.692   0.275  1.00 24.10           O  
ATOM   3156  N   ASN B 275    -107.876   7.728  -0.436  1.00 39.38           N  
ATOM   3157  CA  ASN B 275    -109.107   6.991  -0.670  1.00 35.58           C  
ATOM   3158  C   ASN B 275    -109.092   5.877   0.336  1.00 32.32           C  
ATOM   3159  O   ASN B 275    -108.068   5.239   0.458  1.00 36.22           O  
ATOM   3160  CB  ASN B 275    -109.099   6.395  -2.087  1.00 36.07           C  
ATOM   3161  CG  ASN B 275    -109.366   7.435  -3.179  1.00 34.64           C  
ATOM   3162  OD1 ASN B 275    -110.410   8.090  -3.190  1.00 40.91           O  
ATOM   3163  ND2 ASN B 275    -108.435   7.565  -4.111  1.00 33.58           N  
ATOM   3164  N   VAL B 276    -110.196   5.636   1.048  1.00 38.36           N  
ATOM   3165  CA  VAL B 276    -110.250   4.572   2.074  1.00 42.46           C  
ATOM   3166  C   VAL B 276    -110.546   3.172   1.550  1.00 41.78           C  
ATOM   3167  O   VAL B 276    -109.964   2.215   2.019  1.00 41.39           O  
ATOM   3168  CB  VAL B 276    -111.289   4.856   3.143  1.00 44.95           C  
ATOM   3169  CG1 VAL B 276    -111.357   3.677   4.143  1.00 43.26           C  
ATOM   3170  CG2 VAL B 276    -110.961   6.165   3.839  1.00 47.80           C  
ATOM   3171  N   ALA B 277    -111.468   3.051   0.608  1.00 42.59           N  
ATOM   3172  CA  ALA B 277    -111.810   1.756   0.030  1.00 44.76           C  
ATOM   3173  C   ALA B 277    -112.455   1.971  -1.332  1.00 46.72           C  
ATOM   3174  O   ALA B 277    -112.737   3.109  -1.704  1.00 44.18           O  
ATOM   3175  CB  ALA B 277    -112.744   1.000   0.959  1.00 39.67           C  
ATOM   3176  N   THR B 278    -112.690   0.896  -2.081  1.00 46.18           N  
ATOM   3177  CA  THR B 278    -113.292   1.047  -3.404  1.00 51.70           C  
ATOM   3178  C   THR B 278    -114.079  -0.162  -3.839  1.00 56.20           C  
ATOM   3179  O   THR B 278    -113.959  -1.238  -3.248  1.00 53.65           O  
ATOM   3180  CB  THR B 278    -112.244   1.333  -4.470  1.00 52.82           C  
ATOM   3181  OG1 THR B 278    -111.450   0.160  -4.689  1.00 55.01           O  
ATOM   3182  CG2 THR B 278    -111.353   2.499  -4.040  1.00 57.57           C  
ATOM   3183  N   ASN B 279    -114.878   0.028  -4.887  1.00 57.90           N  
ATOM   3184  CA  ASN B 279    -115.810  -0.997  -5.323  1.00 63.86           C  
ATOM   3185  C   ASN B 279    -115.112  -2.201  -5.902  1.00 64.85           C  
ATOM   3186  O   ASN B 279    -114.197  -2.060  -6.708  1.00 61.23           O  
ATOM   3187  CB  ASN B 279    -116.778  -0.450  -6.371  1.00 65.52           C  
ATOM   3188  CG  ASN B 279    -117.758   0.530  -5.790  1.00 63.96           C  
ATOM   3189  OD1 ASN B 279    -117.395   1.655  -5.435  1.00 54.88           O  
ATOM   3190  ND2 ASN B 279    -119.013   0.110  -5.678  1.00 62.47           N  
ATOM   3191  N   THR B 280    -115.557  -3.382  -5.481  1.00 72.68           N  
ATOM   3192  CA  THR B 280    -115.247  -4.618  -6.191  1.00 76.21           C  
ATOM   3193  C   THR B 280    -116.135  -4.677  -7.418  1.00 79.73           C  
ATOM   3194  O   THR B 280    -117.224  -4.115  -7.420  1.00 85.20           O  
ATOM   3195  CB  THR B 280    -115.566  -5.858  -5.354  1.00 72.85           C  
ATOM   3196  OG1 THR B 280    -116.043  -5.459  -4.062  1.00 69.89           O  
ATOM   3197  CG2 THR B 280    -114.326  -6.747  -5.233  1.00 68.80           C  
ATOM   3198  N   ASP B 281    -115.665  -5.350  -8.456  1.00 82.24           N  
ATOM   3199  CA  ASP B 281    -116.450  -5.598  -9.669  1.00 88.91           C  
ATOM   3200  C   ASP B 281    -117.963  -5.340  -9.558  1.00 89.95           C  
ATOM   3201  O   ASP B 281    -118.717  -6.219  -9.121  1.00 87.72           O  
ATOM   3202  CB  ASP B 281    -116.246  -7.055 -10.072  1.00 96.44           C  
ATOM   3203  CG  ASP B 281    -116.533  -8.019  -8.925  1.00 99.73           C  
ATOM   3204  OD1 ASP B 281    -115.751  -8.985  -8.747  1.00100.01           O  
ATOM   3205  OD2 ASP B 281    -117.534  -7.795  -8.199  1.00 94.65           O  
ATOM   3206  N   GLY B 282    -118.395  -4.142  -9.955  1.00 88.88           N  
ATOM   3207  CA  GLY B 282    -119.822  -3.776  -9.996  1.00 82.88           C  
ATOM   3208  C   GLY B 282    -120.611  -3.858  -8.693  1.00 81.49           C  
ATOM   3209  O   GLY B 282    -121.843  -3.831  -8.719  1.00 84.74           O  
ATOM   3210  N   LYS B 283    -119.916  -3.920  -7.555  1.00 84.52           N  
ATOM   3211  CA  LYS B 283    -120.546  -4.264  -6.266  1.00 84.63           C  
ATOM   3212  C   LYS B 283    -121.210  -3.110  -5.538  1.00 80.87           C  
ATOM   3213  O   LYS B 283    -120.903  -1.941  -5.770  1.00 80.15           O  
ATOM   3214  CB  LYS B 283    -119.541  -4.921  -5.300  1.00 88.10           C  
ATOM   3215  CG  LYS B 283    -119.335  -6.416  -5.513  1.00 87.39           C  
ATOM   3216  CD  LYS B 283    -120.638  -7.212  -5.394  1.00 79.01           C  
ATOM   3217  CE  LYS B 283    -120.851  -8.068  -6.619  1.00 77.89           C  
ATOM   3218  NZ  LYS B 283    -120.514  -7.362  -7.886  1.00 78.82           N  
ATOM   3219  N   ASN B 284    -122.104  -3.476  -4.624  1.00 77.62           N  
ATOM   3220  CA  ASN B 284    -122.884  -2.513  -3.845  1.00 77.50           C  
ATOM   3221  C   ASN B 284    -122.217  -2.057  -2.532  1.00 75.52           C  
ATOM   3222  O   ASN B 284    -122.824  -1.330  -1.740  1.00 64.93           O  
ATOM   3223  CB  ASN B 284    -124.324  -3.023  -3.617  1.00 76.04           C  
ATOM   3224  CG  ASN B 284    -124.411  -4.238  -2.694  1.00 76.50           C  
ATOM   3225  OD1 ASN B 284    -125.474  -4.521  -2.143  1.00 84.17           O  
ATOM   3226  ND2 ASN B 284    -123.315  -4.963  -2.536  1.00 79.65           N  
ATOM   3227  N   TYR B 285    -120.972  -2.479  -2.314  1.00 70.09           N  
ATOM   3228  CA  TYR B 285    -120.144  -1.920  -1.243  1.00 67.24           C  
ATOM   3229  C   TYR B 285    -118.675  -1.915  -1.656  1.00 58.34           C  
ATOM   3230  O   TYR B 285    -118.354  -2.145  -2.831  1.00 63.37           O  
ATOM   3231  CB  TYR B 285    -120.364  -2.668   0.075  1.00 72.77           C  
ATOM   3232  CG  TYR B 285    -120.182  -4.162  -0.006  1.00 75.58           C  
ATOM   3233  CD1 TYR B 285    -121.283  -5.002  -0.068  1.00 81.41           C  
ATOM   3234  CD2 TYR B 285    -118.913  -4.739  -0.008  1.00 73.93           C  
ATOM   3235  CE1 TYR B 285    -121.134  -6.377  -0.137  1.00 85.66           C  
ATOM   3236  CE2 TYR B 285    -118.752  -6.111  -0.077  1.00 77.62           C  
ATOM   3237  CZ  TYR B 285    -119.870  -6.929  -0.140  1.00 84.21           C  
ATOM   3238  OH  TYR B 285    -119.740  -8.300  -0.208  1.00 87.83           O  
ATOM   3239  N   CYS B 286    -117.787  -1.630  -0.712  1.00 42.16           N  
ATOM   3240  CA  CYS B 286    -116.388  -1.503  -1.037  1.00 47.31           C  
ATOM   3241  C   CYS B 286    -115.558  -2.361  -0.120  1.00 49.48           C  
ATOM   3242  O   CYS B 286    -115.295  -1.996   1.022  1.00 49.29           O  
ATOM   3243  CB  CYS B 286    -115.964  -0.044  -0.949  1.00 55.03           C  
ATOM   3244  SG  CYS B 286    -116.907   1.048  -2.069  1.00 55.19           S  
ATOM   3245  N   GLY B 287    -115.153  -3.514  -0.642  1.00 54.93           N  
ATOM   3246  CA  GLY B 287    -114.390  -4.509   0.105  1.00 53.95           C  
ATOM   3247  C   GLY B 287    -112.912  -4.408  -0.161  1.00 48.80           C  
ATOM   3248  O   GLY B 287    -112.086  -4.773   0.666  1.00 47.85           O  
ATOM   3249  N   LEU B 288    -112.577  -3.925  -1.340  1.00 53.00           N  
ATOM   3250  CA  LEU B 288    -111.205  -3.559  -1.638  1.00 53.86           C  
ATOM   3251  C   LEU B 288    -110.811  -2.276  -0.896  1.00 50.85           C  
ATOM   3252  O   LEU B 288    -111.440  -1.222  -1.072  1.00 49.27           O  
ATOM   3253  CB  LEU B 288    -111.055  -3.331  -3.134  1.00 52.94           C  
ATOM   3254  CG  LEU B 288    -110.713  -4.564  -3.940  1.00 50.04           C  
ATOM   3255  CD1 LEU B 288    -111.420  -4.531  -5.282  1.00 48.33           C  
ATOM   3256  CD2 LEU B 288    -109.184  -4.609  -4.083  1.00 63.46           C  
ATOM   3257  N   PRO B 289    -109.765  -2.350  -0.079  1.00 42.15           N  
ATOM   3258  CA  PRO B 289    -109.228  -1.152   0.536  1.00 44.27           C  
ATOM   3259  C   PRO B 289    -108.509  -0.284  -0.494  1.00 41.83           C  
ATOM   3260  O   PRO B 289    -108.305  -0.712  -1.634  1.00 41.61           O  
ATOM   3261  CB  PRO B 289    -108.222  -1.707   1.524  1.00 49.31           C  
ATOM   3262  CG  PRO B 289    -107.722  -2.908   0.852  1.00 54.59           C  
ATOM   3263  CD  PRO B 289    -108.859  -3.490   0.073  1.00 46.35           C  
ATOM   3264  N   GLY B 290    -108.133   0.926  -0.097  1.00 37.33           N  
ATOM   3265  CA  GLY B 290    -107.506   1.874  -1.024  1.00 40.80           C  
ATOM   3266  C   GLY B 290    -106.274   2.437  -0.393  1.00 33.58           C  
ATOM   3267  O   GLY B 290    -106.037   2.176   0.763  1.00 35.60           O  
ATOM   3268  N   GLU B 291    -105.470   3.193  -1.127  1.00 35.55           N  
ATOM   3269  CA  GLU B 291    -104.281   3.787  -0.493  1.00 39.66           C  
ATOM   3270  C   GLU B 291    -104.673   5.036   0.308  1.00 39.14           C  
ATOM   3271  O   GLU B 291    -105.339   5.966  -0.191  1.00 34.08           O  
ATOM   3272  CB  GLU B 291    -103.175   4.098  -1.501  1.00 40.59           C  
ATOM   3273  CG  GLU B 291    -102.337   2.904  -1.920  1.00 37.79           C  
ATOM   3274  CD  GLU B 291    -101.141   3.314  -2.763  1.00 42.58           C  
ATOM   3275  OE1 GLU B 291    -101.337   3.907  -3.844  1.00 46.32           O  
ATOM   3276  OE2 GLU B 291     -99.997   3.061  -2.351  1.00 38.14           O  
ATOM   3277  N   TYR B 292    -104.303   5.035   1.576  1.00 37.97           N  
ATOM   3278  CA  TYR B 292    -104.682   6.135   2.425  1.00 40.59           C  
ATOM   3279  C   TYR B 292    -103.803   6.185   3.614  1.00 40.47           C  
ATOM   3280  O   TYR B 292    -103.114   5.222   3.921  1.00 37.88           O  
ATOM   3281  CB  TYR B 292    -106.159   6.083   2.855  1.00 42.39           C  
ATOM   3282  CG  TYR B 292    -106.582   5.057   3.926  1.00 44.24           C  
ATOM   3283  CD1 TYR B 292    -106.456   5.336   5.283  1.00 47.74           C  
ATOM   3284  CD2 TYR B 292    -107.197   3.864   3.580  1.00 37.26           C  
ATOM   3285  CE1 TYR B 292    -106.874   4.437   6.258  1.00 39.62           C  
ATOM   3286  CE2 TYR B 292    -107.616   2.970   4.545  1.00 38.20           C  
ATOM   3287  CZ  TYR B 292    -107.445   3.259   5.883  1.00 40.15           C  
ATOM   3288  OH  TYR B 292    -107.847   2.365   6.853  1.00 41.02           O  
ATOM   3289  N   TRP B 293    -103.808   7.362   4.224  1.00 42.59           N  
ATOM   3290  CA  TRP B 293    -103.286   7.598   5.551  1.00 44.03           C  
ATOM   3291  C   TRP B 293    -104.543   8.043   6.250  1.00 41.06           C  
ATOM   3292  O   TRP B 293    -105.303   8.811   5.673  1.00 45.39           O  
ATOM   3293  CB  TRP B 293    -102.247   8.724   5.519  1.00 45.45           C  
ATOM   3294  CG  TRP B 293    -101.718   9.145   6.867  1.00 43.53           C  
ATOM   3295  CD1 TRP B 293    -101.974  10.312   7.523  1.00 44.84           C  
ATOM   3296  CD2 TRP B 293    -100.827   8.413   7.695  1.00 38.38           C  
ATOM   3297  NE1 TRP B 293    -101.304  10.340   8.717  1.00 40.03           N  
ATOM   3298  CE2 TRP B 293    -100.595   9.179   8.847  1.00 33.38           C  
ATOM   3299  CE3 TRP B 293    -100.190   7.184   7.569  1.00 44.37           C  
ATOM   3300  CZ2 TRP B 293     -99.778   8.742   9.877  1.00 31.54           C  
ATOM   3301  CZ3 TRP B 293     -99.353   6.754   8.597  1.00 38.59           C  
ATOM   3302  CH2 TRP B 293     -99.171   7.526   9.736  1.00 32.10           C  
ATOM   3303  N   LEU B 294    -104.809   7.511   7.440  1.00 38.20           N  
ATOM   3304  CA  LEU B 294    -105.935   7.951   8.245  1.00 32.86           C  
ATOM   3305  C   LEU B 294    -105.428   9.213   8.882  1.00 36.89           C  
ATOM   3306  O   LEU B 294    -104.235   9.439   8.894  1.00 43.43           O  
ATOM   3307  CB  LEU B 294    -106.271   6.889   9.298  1.00 33.92           C  
ATOM   3308  CG  LEU B 294    -107.518   7.126  10.155  1.00 37.77           C  
ATOM   3309  CD1 LEU B 294    -108.520   7.909   9.369  1.00 36.22           C  
ATOM   3310  CD2 LEU B 294    -108.181   5.848  10.686  1.00 29.20           C  
ATOM   3311  N   GLY B 295    -106.276  10.062   9.416  1.00 42.65           N  
ATOM   3312  CA  GLY B 295    -105.730  11.234  10.109  1.00 50.87           C  
ATOM   3313  C   GLY B 295    -104.732  10.894  11.205  1.00 44.75           C  
ATOM   3314  O   GLY B 295    -104.829   9.838  11.813  1.00 41.45           O  
ATOM   3315  N   ASN B 296    -103.765  11.776  11.454  1.00 43.63           N  
ATOM   3316  CA  ASN B 296    -102.954  11.662  12.674  1.00 46.49           C  
ATOM   3317  C   ASN B 296    -103.781  11.697  13.962  1.00 48.39           C  
ATOM   3318  O   ASN B 296    -103.905  10.674  14.633  1.00 46.18           O  
ATOM   3319  CB  ASN B 296    -101.881  12.743  12.768  1.00 46.54           C  
ATOM   3320  CG  ASN B 296    -100.651  12.426  11.954  1.00 50.59           C  
ATOM   3321  OD1 ASN B 296     -99.923  13.329  11.526  1.00 54.46           O  
ATOM   3322  ND2 ASN B 296    -100.394  11.151  11.751  1.00 46.17           N  
ATOM   3323  N   ASP B 297    -104.348  12.840  14.341  1.00 45.32           N  
ATOM   3324  CA  ASP B 297    -104.972  12.860  15.671  1.00 53.31           C  
ATOM   3325  C   ASP B 297    -106.122  11.871  15.749  1.00 49.14           C  
ATOM   3326  O   ASP B 297    -106.424  11.359  16.826  1.00 43.18           O  
ATOM   3327  CB  ASP B 297    -105.341  14.258  16.230  1.00 56.96           C  
ATOM   3328  CG  ASP B 297    -105.689  15.257  15.175  1.00 52.47           C  
ATOM   3329  OD1 ASP B 297    -104.936  16.246  15.062  1.00 46.46           O  
ATOM   3330  OD2 ASP B 297    -106.718  15.062  14.495  1.00 58.27           O  
ATOM   3331  N   LYS B 298    -106.709  11.539  14.606  1.00 48.53           N  
ATOM   3332  CA  LYS B 298    -107.547  10.339  14.540  1.00 54.87           C  
ATOM   3333  C   LYS B 298    -106.833   9.096  15.093  1.00 52.40           C  
ATOM   3334  O   LYS B 298    -107.452   8.237  15.722  1.00 53.60           O  
ATOM   3335  CB  LYS B 298    -108.002  10.062  13.105  1.00 54.10           C  
ATOM   3336  CG  LYS B 298    -109.466  10.388  12.848  1.00 55.73           C  
ATOM   3337  CD  LYS B 298    -109.798  10.121  11.411  1.00 56.73           C  
ATOM   3338  CE  LYS B 298    -110.824  11.061  10.858  1.00 55.88           C  
ATOM   3339  NZ  LYS B 298    -111.022  10.761   9.407  1.00 59.92           N  
ATOM   3340  N   ILE B 299    -105.533   9.008  14.847  1.00 45.63           N  
ATOM   3341  CA  ILE B 299    -104.783   7.819  15.159  1.00 38.27           C  
ATOM   3342  C   ILE B 299    -104.313   7.814  16.597  1.00 44.41           C  
ATOM   3343  O   ILE B 299    -104.276   6.756  17.222  1.00 48.01           O  
ATOM   3344  CB  ILE B 299    -103.570   7.700  14.264  1.00 34.43           C  
ATOM   3345  CG1 ILE B 299    -103.987   7.266  12.874  1.00 33.65           C  
ATOM   3346  CG2 ILE B 299    -102.600   6.693  14.827  1.00 37.04           C  
ATOM   3347  CD1 ILE B 299    -102.835   7.303  11.906  1.00 34.05           C  
ATOM   3348  N   SER B 300    -103.929   8.974  17.125  1.00 41.41           N  
ATOM   3349  CA  SER B 300    -103.419   9.022  18.489  1.00 35.18           C  
ATOM   3350  C   SER B 300    -104.574   8.692  19.399  1.00 34.73           C  
ATOM   3351  O   SER B 300    -104.485   7.835  20.278  1.00 37.37           O  
ATOM   3352  CB  SER B 300    -102.865  10.393  18.832  1.00 34.33           C  
ATOM   3353  OG  SER B 300    -103.874  11.236  19.315  1.00 45.39           O  
ATOM   3354  N   GLN B 301    -105.686   9.361  19.151  1.00 35.24           N  
ATOM   3355  CA  GLN B 301    -106.838   9.204  19.999  1.00 37.52           C  
ATOM   3356  C   GLN B 301    -107.340   7.793  19.914  1.00 35.91           C  
ATOM   3357  O   GLN B 301    -107.862   7.282  20.882  1.00 40.25           O  
ATOM   3358  CB  GLN B 301    -107.922  10.206  19.626  1.00 48.94           C  
ATOM   3359  CG  GLN B 301    -109.251   9.989  20.320  1.00 46.97           C  
ATOM   3360  CD  GLN B 301    -110.063   8.912  19.655  1.00 54.85           C  
ATOM   3361  OE1 GLN B 301    -110.628   8.041  20.334  1.00 54.01           O  
ATOM   3362  NE2 GLN B 301    -110.116   8.943  18.310  1.00 50.98           N  
ATOM   3363  N   LEU B 302    -107.184   7.175  18.748  1.00 45.97           N  
ATOM   3364  CA  LEU B 302    -107.374   5.725  18.580  1.00 46.06           C  
ATOM   3365  C   LEU B 302    -106.452   4.919  19.508  1.00 45.83           C  
ATOM   3366  O   LEU B 302    -106.920   4.102  20.305  1.00 47.79           O  
ATOM   3367  CB  LEU B 302    -107.081   5.311  17.133  1.00 46.89           C  
ATOM   3368  CG  LEU B 302    -108.207   5.189  16.120  1.00 43.31           C  
ATOM   3369  CD1 LEU B 302    -107.647   5.086  14.707  1.00 36.21           C  
ATOM   3370  CD2 LEU B 302    -109.033   3.975  16.440  1.00 52.35           C  
ATOM   3371  N   THR B 303    -105.147   5.143  19.403  1.00 37.23           N  
ATOM   3372  CA  THR B 303    -104.221   4.390  20.212  1.00 40.05           C  
ATOM   3373  C   THR B 303    -104.388   4.725  21.676  1.00 48.20           C  
ATOM   3374  O   THR B 303    -104.165   3.870  22.528  1.00 52.98           O  
ATOM   3375  CB  THR B 303    -102.765   4.679  19.888  1.00 37.99           C  
ATOM   3376  OG1 THR B 303    -102.427   5.979  20.365  1.00 38.26           O  
ATOM   3377  CG2 THR B 303    -102.511   4.596  18.424  1.00 40.99           C  
ATOM   3378  N   ARG B 304    -104.762   5.965  21.977  1.00 46.35           N  
ATOM   3379  CA  ARG B 304    -104.778   6.416  23.373  1.00 49.00           C  
ATOM   3380  C   ARG B 304    -106.022   6.067  24.217  1.00 45.92           C  
ATOM   3381  O   ARG B 304    -106.024   6.300  25.416  1.00 44.11           O  
ATOM   3382  CB  ARG B 304    -104.519   7.910  23.448  1.00 49.24           C  
ATOM   3383  CG  ARG B 304    -103.117   8.264  23.879  1.00 52.70           C  
ATOM   3384  CD  ARG B 304    -103.022   9.730  24.334  1.00 60.16           C  
ATOM   3385  NE  ARG B 304    -103.402  10.654  23.260  1.00 63.75           N  
ATOM   3386  CZ  ARG B 304    -104.632  11.128  23.037  1.00 66.47           C  
ATOM   3387  NH1 ARG B 304    -105.670  10.796  23.815  1.00 66.27           N  
ATOM   3388  NH2 ARG B 304    -104.834  11.945  22.005  1.00 65.69           N  
ATOM   3389  N   MET B 305    -107.058   5.501  23.608  1.00 41.32           N  
ATOM   3390  CA  MET B 305    -108.169   4.908  24.353  1.00 44.54           C  
ATOM   3391  C   MET B 305    -107.743   3.921  25.437  1.00 51.50           C  
ATOM   3392  O   MET B 305    -108.426   3.764  26.460  1.00 46.90           O  
ATOM   3393  CB  MET B 305    -109.024   4.112  23.392  1.00 57.22           C  
ATOM   3394  CG  MET B 305    -110.009   4.924  22.600  1.00 67.72           C  
ATOM   3395  SD  MET B 305    -110.478   4.114  21.060  1.00 69.65           S  
ATOM   3396  CE  MET B 305    -110.047   2.390  21.372  1.00 77.26           C  
ATOM   3397  N   GLY B 306    -106.632   3.233  25.173  1.00 54.56           N  
ATOM   3398  CA  GLY B 306    -106.171   2.090  25.955  1.00 51.73           C  
ATOM   3399  C   GLY B 306    -105.138   1.352  25.123  1.00 53.26           C  
ATOM   3400  O   GLY B 306    -104.933   1.712  23.968  1.00 56.73           O  
ATOM   3401  N   PRO B 307    -104.520   0.289  25.673  1.00 53.44           N  
ATOM   3402  CA  PRO B 307    -103.332  -0.346  25.080  1.00 48.38           C  
ATOM   3403  C   PRO B 307    -103.565  -0.929  23.687  1.00 41.73           C  
ATOM   3404  O   PRO B 307    -104.561  -1.581  23.440  1.00 49.66           O  
ATOM   3405  CB  PRO B 307    -102.982  -1.457  26.071  1.00 54.18           C  
ATOM   3406  CG  PRO B 307    -104.141  -1.570  27.028  1.00 58.77           C  
ATOM   3407  CD  PRO B 307    -105.208  -0.614  26.609  1.00 59.98           C  
ATOM   3408  N   THR B 308    -102.616  -0.714  22.796  1.00 42.99           N  
ATOM   3409  CA  THR B 308    -102.872  -0.821  21.384  1.00 39.28           C  
ATOM   3410  C   THR B 308    -101.703  -1.461  20.669  1.00 41.54           C  
ATOM   3411  O   THR B 308    -100.600  -0.926  20.700  1.00 45.89           O  
ATOM   3412  CB  THR B 308    -103.037   0.576  20.828  1.00 37.09           C  
ATOM   3413  OG1 THR B 308    -104.154   1.202  21.458  1.00 38.40           O  
ATOM   3414  CG2 THR B 308    -103.240   0.541  19.332  1.00 39.50           C  
ATOM   3415  N   GLU B 309    -101.937  -2.598  20.025  1.00 40.76           N  
ATOM   3416  CA  GLU B 309    -100.881  -3.244  19.270  1.00 41.83           C  
ATOM   3417  C   GLU B 309    -100.964  -2.806  17.826  1.00 37.50           C  
ATOM   3418  O   GLU B 309    -102.045  -2.630  17.295  1.00 35.43           O  
ATOM   3419  CB  GLU B 309    -100.913  -4.777  19.409  1.00 49.30           C  
ATOM   3420  CG  GLU B 309    -102.109  -5.500  18.780  1.00 53.11           C  
ATOM   3421  CD  GLU B 309    -102.034  -7.036  18.892  1.00 50.46           C  
ATOM   3422  OE1 GLU B 309    -100.925  -7.611  18.973  1.00 49.25           O  
ATOM   3423  OE2 GLU B 309    -103.107  -7.672  18.880  1.00 49.78           O  
ATOM   3424  N   LEU B 310     -99.795  -2.620  17.219  1.00 45.57           N  
ATOM   3425  CA  LEU B 310     -99.656  -2.199  15.835  1.00 44.27           C  
ATOM   3426  C   LEU B 310     -98.969  -3.297  15.077  1.00 41.94           C  
ATOM   3427  O   LEU B 310     -97.877  -3.694  15.468  1.00 45.22           O  
ATOM   3428  CB  LEU B 310     -98.749  -0.976  15.737  1.00 43.06           C  
ATOM   3429  CG  LEU B 310     -98.218  -0.694  14.323  1.00 37.57           C  
ATOM   3430  CD1 LEU B 310     -99.149   0.226  13.579  1.00 32.46           C  
ATOM   3431  CD2 LEU B 310     -96.847  -0.128  14.357  1.00 29.89           C  
ATOM   3432  N   LEU B 311     -99.570  -3.740  13.976  1.00 35.83           N  
ATOM   3433  CA  LEU B 311     -98.910  -4.652  13.043  1.00 36.30           C  
ATOM   3434  C   LEU B 311     -98.662  -3.927  11.721  1.00 37.47           C  
ATOM   3435  O   LEU B 311     -99.521  -3.182  11.244  1.00 36.78           O  
ATOM   3436  CB  LEU B 311     -99.762  -5.908  12.837  1.00 40.43           C  
ATOM   3437  CG  LEU B 311     -99.728  -6.675  11.511  1.00 33.07           C  
ATOM   3438  CD1 LEU B 311     -98.330  -7.105  11.204  1.00 29.88           C  
ATOM   3439  CD2 LEU B 311    -100.656  -7.856  11.587  1.00 25.26           C  
ATOM   3440  N   ILE B 312     -97.476  -4.144  11.151  1.00 35.63           N  
ATOM   3441  CA  ILE B 312     -97.092  -3.568   9.870  1.00 35.19           C  
ATOM   3442  C   ILE B 312     -96.748  -4.714   8.954  1.00 39.19           C  
ATOM   3443  O   ILE B 312     -95.866  -5.515   9.252  1.00 41.70           O  
ATOM   3444  CB  ILE B 312     -95.838  -2.694   9.958  1.00 37.21           C  
ATOM   3445  CG1 ILE B 312     -96.021  -1.580  10.973  1.00 38.06           C  
ATOM   3446  CG2 ILE B 312     -95.503  -2.103   8.599  1.00 35.27           C  
ATOM   3447  CD1 ILE B 312     -94.746  -1.169  11.569  1.00 33.77           C  
ATOM   3448  N   GLU B 313     -97.430  -4.762   7.823  1.00 40.71           N  
ATOM   3449  CA  GLU B 313     -97.275  -5.835   6.885  1.00 41.90           C  
ATOM   3450  C   GLU B 313     -96.748  -5.293   5.576  1.00 42.97           C  
ATOM   3451  O   GLU B 313     -97.360  -4.400   4.998  1.00 44.73           O  
ATOM   3452  CB  GLU B 313     -98.628  -6.485   6.642  1.00 50.66           C  
ATOM   3453  CG  GLU B 313     -99.305  -7.071   7.886  1.00 59.06           C  
ATOM   3454  CD  GLU B 313    -100.199  -8.279   7.551  1.00 65.51           C  
ATOM   3455  OE1 GLU B 313    -101.388  -8.322   7.985  1.00 55.72           O  
ATOM   3456  OE2 GLU B 313     -99.700  -9.185   6.834  1.00 60.45           O  
ATOM   3457  N   MET B 314     -95.627  -5.839   5.101  1.00 45.71           N  
ATOM   3458  CA  MET B 314     -95.132  -5.512   3.762  1.00 45.09           C  
ATOM   3459  C   MET B 314     -95.004  -6.734   2.859  1.00 39.80           C  
ATOM   3460  O   MET B 314     -94.709  -7.821   3.332  1.00 38.35           O  
ATOM   3461  CB  MET B 314     -93.811  -4.739   3.826  1.00 40.18           C  
ATOM   3462  CG  MET B 314     -92.665  -5.434   4.489  1.00 42.52           C  
ATOM   3463  SD  MET B 314     -91.717  -4.336   5.592  1.00 44.25           S  
ATOM   3464  CE  MET B 314     -92.673  -4.495   7.092  1.00 40.45           C  
ATOM   3465  N   GLU B 315     -95.301  -6.528   1.572  1.00 42.17           N  
ATOM   3466  CA  GLU B 315     -95.006  -7.462   0.483  1.00 43.36           C  
ATOM   3467  C   GLU B 315     -93.906  -6.851  -0.389  1.00 42.41           C  
ATOM   3468  O   GLU B 315     -93.463  -5.744  -0.131  1.00 49.96           O  
ATOM   3469  CB  GLU B 315     -96.263  -7.675  -0.349  1.00 49.11           C  
ATOM   3470  CG  GLU B 315     -96.195  -8.780  -1.408  1.00 52.65           C  
ATOM   3471  CD  GLU B 315     -97.557  -9.107  -2.012  1.00 57.23           C  
ATOM   3472  OE1 GLU B 315     -97.592  -9.455  -3.215  1.00 61.28           O  
ATOM   3473  OE2 GLU B 315     -98.587  -9.009  -1.292  1.00 52.39           O  
ATOM   3474  N   ASP B 316     -93.442  -7.553  -1.409  1.00 40.70           N  
ATOM   3475  CA  ASP B 316     -92.507  -6.946  -2.342  1.00 44.91           C  
ATOM   3476  C   ASP B 316     -92.728  -7.431  -3.763  1.00 46.97           C  
ATOM   3477  O   ASP B 316     -93.524  -8.333  -4.001  1.00 52.63           O  
ATOM   3478  CB  ASP B 316     -91.104  -7.294  -1.929  1.00 53.27           C  
ATOM   3479  CG  ASP B 316     -90.715  -8.651  -2.388  1.00 56.01           C  
ATOM   3480  OD1 ASP B 316     -89.652  -8.743  -3.029  1.00 52.75           O  
ATOM   3481  OD2 ASP B 316     -91.507  -9.600  -2.150  1.00 56.54           O  
ATOM   3482  N   TRP B 317     -91.971  -6.879  -4.701  1.00 48.28           N  
ATOM   3483  CA  TRP B 317     -92.328  -7.011  -6.111  1.00 52.30           C  
ATOM   3484  C   TRP B 317     -92.255  -8.418  -6.662  1.00 51.36           C  
ATOM   3485  O   TRP B 317     -92.743  -8.655  -7.764  1.00 54.90           O  
ATOM   3486  CB  TRP B 317     -91.539  -6.025  -6.984  1.00 52.02           C  
ATOM   3487  CG  TRP B 317     -91.973  -4.626  -6.699  1.00 52.19           C  
ATOM   3488  CD1 TRP B 317     -91.479  -3.795  -5.747  1.00 49.92           C  
ATOM   3489  CD2 TRP B 317     -93.059  -3.935  -7.307  1.00 48.36           C  
ATOM   3490  NE1 TRP B 317     -92.162  -2.614  -5.750  1.00 49.65           N  
ATOM   3491  CE2 TRP B 317     -93.141  -2.677  -6.702  1.00 52.16           C  
ATOM   3492  CE3 TRP B 317     -93.959  -4.255  -8.322  1.00 46.29           C  
ATOM   3493  CZ2 TRP B 317     -94.083  -1.735  -7.080  1.00 56.15           C  
ATOM   3494  CZ3 TRP B 317     -94.889  -3.327  -8.694  1.00 47.68           C  
ATOM   3495  CH2 TRP B 317     -94.951  -2.081  -8.075  1.00 54.44           C  
ATOM   3496  N   LYS B 318     -91.683  -9.347  -5.897  1.00 54.06           N  
ATOM   3497  CA  LYS B 318     -91.697 -10.763  -6.270  1.00 57.09           C  
ATOM   3498  C   LYS B 318     -92.898 -11.485  -5.657  1.00 56.66           C  
ATOM   3499  O   LYS B 318     -93.423 -12.428  -6.248  1.00 58.71           O  
ATOM   3500  CB  LYS B 318     -90.405 -11.449  -5.844  1.00 60.99           C  
ATOM   3501  CG  LYS B 318     -89.922 -12.487  -6.830  1.00 71.33           C  
ATOM   3502  CD  LYS B 318     -88.729 -11.978  -7.640  1.00 78.86           C  
ATOM   3503  CE  LYS B 318     -87.455 -11.901  -6.783  1.00 79.19           C  
ATOM   3504  NZ  LYS B 318     -86.196 -12.067  -7.583  1.00 78.05           N  
ATOM   3505  N   GLY B 319     -93.318 -11.051  -4.470  1.00 51.60           N  
ATOM   3506  CA  GLY B 319     -94.544 -11.554  -3.857  1.00 49.43           C  
ATOM   3507  C   GLY B 319     -94.335 -12.235  -2.522  1.00 47.61           C  
ATOM   3508  O   GLY B 319     -95.032 -13.191  -2.193  1.00 43.37           O  
ATOM   3509  N   ASP B 320     -93.386 -11.736  -1.740  1.00 46.84           N  
ATOM   3510  CA  ASP B 320     -93.082 -12.330  -0.448  1.00 48.55           C  
ATOM   3511  C   ASP B 320     -93.326 -11.266   0.567  1.00 45.40           C  
ATOM   3512  O   ASP B 320     -93.085 -10.100   0.298  1.00 46.81           O  
ATOM   3513  CB  ASP B 320     -91.627 -12.774  -0.345  1.00 57.42           C  
ATOM   3514  CG  ASP B 320     -90.853 -12.551  -1.626  1.00 68.74           C  
ATOM   3515  OD1 ASP B 320     -89.599 -12.663  -1.593  1.00 72.79           O  
ATOM   3516  OD2 ASP B 320     -91.496 -12.244  -2.658  1.00 69.25           O  
ATOM   3517  N   LYS B 321     -93.772 -11.679   1.744  1.00 48.39           N  
ATOM   3518  CA  LYS B 321     -94.200 -10.755   2.776  1.00 51.20           C  
ATOM   3519  C   LYS B 321     -93.503 -11.024   4.097  1.00 45.63           C  
ATOM   3520  O   LYS B 321     -92.957 -12.096   4.328  1.00 40.53           O  
ATOM   3521  CB  LYS B 321     -95.718 -10.850   2.998  1.00 59.55           C  
ATOM   3522  CG  LYS B 321     -96.580 -10.767   1.741  1.00 63.87           C  
ATOM   3523  CD  LYS B 321     -96.594 -12.070   0.932  1.00 68.87           C  
ATOM   3524  CE  LYS B 321     -97.886 -12.249   0.120  1.00 72.44           C  
ATOM   3525  NZ  LYS B 321     -99.089 -12.493   0.980  1.00 68.53           N  
ATOM   3526  N   VAL B 322     -93.585 -10.029   4.970  1.00 52.69           N  
ATOM   3527  CA  VAL B 322     -92.976 -10.066   6.291  1.00 52.86           C  
ATOM   3528  C   VAL B 322     -93.714  -9.077   7.212  1.00 49.78           C  
ATOM   3529  O   VAL B 322     -93.983  -7.948   6.829  1.00 55.10           O  
ATOM   3530  CB  VAL B 322     -91.476  -9.711   6.204  1.00 55.80           C  
ATOM   3531  CG1 VAL B 322     -90.646 -10.933   5.771  1.00 50.18           C  
ATOM   3532  CG2 VAL B 322     -91.249  -8.530   5.252  1.00 48.72           C  
ATOM   3533  N   LYS B 323     -94.075  -9.512   8.407  1.00 46.47           N  
ATOM   3534  CA  LYS B 323     -94.747  -8.637   9.335  1.00 43.09           C  
ATOM   3535  C   LYS B 323     -93.677  -7.930  10.124  1.00 43.34           C  
ATOM   3536  O   LYS B 323     -92.538  -8.382  10.183  1.00 40.53           O  
ATOM   3537  CB  LYS B 323     -95.606  -9.393  10.338  1.00 45.97           C  
ATOM   3538  CG  LYS B 323     -96.310 -10.639   9.857  1.00 60.34           C  
ATOM   3539  CD  LYS B 323     -97.131 -11.249  11.026  1.00 71.51           C  
ATOM   3540  CE  LYS B 323     -96.739 -12.700  11.351  1.00 73.49           C  
ATOM   3541  NZ  LYS B 323     -97.128 -13.663  10.274  1.00 71.75           N  
ATOM   3542  N   ALA B 324     -94.061  -6.805  10.708  1.00 43.22           N  
ATOM   3543  CA  ALA B 324     -93.404  -6.260  11.883  1.00 43.78           C  
ATOM   3544  C   ALA B 324     -94.550  -6.033  12.842  1.00 47.13           C  
ATOM   3545  O   ALA B 324     -95.560  -5.429  12.492  1.00 48.50           O  
ATOM   3546  CB  ALA B 324     -92.695  -4.959  11.577  1.00 46.23           C  
ATOM   3547  N   HIS B 325     -94.403  -6.528  14.052  1.00 48.88           N  
ATOM   3548  CA  HIS B 325     -95.508  -6.631  14.971  1.00 44.37           C  
ATOM   3549  C   HIS B 325     -95.083  -5.889  16.213  1.00 44.46           C  
ATOM   3550  O   HIS B 325     -94.047  -6.189  16.782  1.00 55.79           O  
ATOM   3551  CB  HIS B 325     -95.666  -8.097  15.270  1.00 50.00           C  
ATOM   3552  CG  HIS B 325     -97.060  -8.525  15.537  1.00 61.77           C  
ATOM   3553  ND1 HIS B 325     -97.841  -7.955  16.518  1.00 66.11           N  
ATOM   3554  CD2 HIS B 325     -97.797  -9.521  14.989  1.00 70.37           C  
ATOM   3555  CE1 HIS B 325     -99.014  -8.564  16.542  1.00 71.69           C  
ATOM   3556  NE2 HIS B 325     -99.012  -9.518  15.626  1.00 72.78           N  
ATOM   3557  N   TYR B 326     -95.824  -4.890  16.629  1.00 47.06           N  
ATOM   3558  CA  TYR B 326     -95.418  -4.160  17.814  1.00 48.58           C  
ATOM   3559  C   TYR B 326     -96.545  -4.256  18.814  1.00 47.61           C  
ATOM   3560  O   TYR B 326     -97.644  -3.754  18.574  1.00 44.38           O  
ATOM   3561  CB  TYR B 326     -95.074  -2.707  17.480  1.00 49.34           C  
ATOM   3562  CG  TYR B 326     -93.755  -2.549  16.752  1.00 37.94           C  
ATOM   3563  CD1 TYR B 326     -93.633  -2.872  15.401  1.00 34.79           C  
ATOM   3564  CD2 TYR B 326     -92.651  -2.066  17.403  1.00 39.17           C  
ATOM   3565  CE1 TYR B 326     -92.451  -2.720  14.729  1.00 30.88           C  
ATOM   3566  CE2 TYR B 326     -91.454  -1.926  16.746  1.00 46.27           C  
ATOM   3567  CZ  TYR B 326     -91.348  -2.253  15.404  1.00 43.25           C  
ATOM   3568  OH  TYR B 326     -90.116  -2.106  14.761  1.00 43.67           O  
ATOM   3569  N   GLY B 327     -96.260  -4.928  19.923  1.00 45.61           N  
ATOM   3570  CA  GLY B 327     -97.234  -5.137  20.987  1.00 49.12           C  
ATOM   3571  C   GLY B 327     -97.796  -3.867  21.599  1.00 46.60           C  
ATOM   3572  O   GLY B 327     -98.985  -3.777  21.885  1.00 45.29           O  
ATOM   3573  N   GLY B 328     -96.934  -2.886  21.821  1.00 49.60           N  
ATOM   3574  CA  GLY B 328     -97.355  -1.621  22.396  1.00 50.67           C  
ATOM   3575  C   GLY B 328     -97.170  -0.565  21.341  1.00 49.64           C  
ATOM   3576  O   GLY B 328     -96.202  -0.612  20.572  1.00 54.31           O  
ATOM   3577  N   PHE B 329     -98.088   0.386  21.298  1.00 37.54           N  
ATOM   3578  CA  PHE B 329     -98.063   1.378  20.257  1.00 38.81           C  
ATOM   3579  C   PHE B 329     -98.962   2.509  20.632  1.00 44.43           C  
ATOM   3580  O   PHE B 329    -100.104   2.285  21.056  1.00 49.90           O  
ATOM   3581  CB  PHE B 329     -98.543   0.787  18.943  1.00 38.02           C  
ATOM   3582  CG  PHE B 329     -98.758   1.813  17.873  1.00 40.94           C  
ATOM   3583  CD1 PHE B 329     -97.719   2.607  17.448  1.00 41.36           C  
ATOM   3584  CD2 PHE B 329     -99.996   1.987  17.293  1.00 46.36           C  
ATOM   3585  CE1 PHE B 329     -97.900   3.543  16.463  1.00 39.03           C  
ATOM   3586  CE2 PHE B 329    -100.182   2.931  16.301  1.00 44.56           C  
ATOM   3587  CZ  PHE B 329     -99.127   3.707  15.890  1.00 41.83           C  
ATOM   3588  N   THR B 330     -98.472   3.728  20.474  1.00 34.04           N  
ATOM   3589  CA  THR B 330     -99.235   4.857  20.932  1.00 40.50           C  
ATOM   3590  C   THR B 330     -98.706   6.098  20.269  1.00 37.82           C  
ATOM   3591  O   THR B 330     -97.520   6.219  20.052  1.00 51.61           O  
ATOM   3592  CB  THR B 330     -99.181   5.009  22.498  1.00 46.85           C  
ATOM   3593  OG1 THR B 330     -98.295   6.067  22.861  1.00 50.81           O  
ATOM   3594  CG2 THR B 330     -98.710   3.724  23.199  1.00 52.23           C  
ATOM   3595  N   VAL B 331     -99.585   7.030  19.963  1.00 34.37           N  
ATOM   3596  CA  VAL B 331     -99.181   8.262  19.342  1.00 32.62           C  
ATOM   3597  C   VAL B 331     -99.747   9.372  20.186  1.00 34.48           C  
ATOM   3598  O   VAL B 331    -100.845   9.239  20.687  1.00 38.24           O  
ATOM   3599  CB  VAL B 331     -99.724   8.329  17.905  1.00 34.44           C  
ATOM   3600  CG1 VAL B 331     -99.703   9.761  17.362  1.00 38.38           C  
ATOM   3601  CG2 VAL B 331     -98.916   7.406  17.013  1.00 33.37           C  
ATOM   3602  N   GLN B 332     -99.016  10.463  20.361  1.00 34.56           N  
ATOM   3603  CA  GLN B 332     -99.552  11.582  21.129  1.00 39.22           C  
ATOM   3604  C   GLN B 332    -100.385  12.501  20.270  1.00 37.14           C  
ATOM   3605  O   GLN B 332    -100.497  12.306  19.064  1.00 34.94           O  
ATOM   3606  CB  GLN B 332     -98.430  12.405  21.778  1.00 41.93           C  
ATOM   3607  CG  GLN B 332     -97.672  11.710  22.896  1.00 41.34           C  
ATOM   3608  CD  GLN B 332     -98.544  10.852  23.752  1.00 39.07           C  
ATOM   3609  OE1 GLN B 332     -99.470  11.337  24.397  1.00 44.78           O  
ATOM   3610  NE2 GLN B 332     -98.277   9.557  23.744  1.00 38.11           N  
ATOM   3611  N   ASN B 333    -100.954  13.507  20.929  1.00 34.97           N  
ATOM   3612  CA  ASN B 333    -101.584  14.668  20.283  1.00 35.43           C  
ATOM   3613  C   ASN B 333    -100.652  15.652  19.576  1.00 33.47           C  
ATOM   3614  O   ASN B 333     -99.431  15.654  19.779  1.00 33.54           O  
ATOM   3615  CB  ASN B 333    -102.360  15.450  21.333  1.00 39.80           C  
ATOM   3616  CG  ASN B 333    -101.569  15.639  22.593  1.00 42.69           C  
ATOM   3617  OD1 ASN B 333    -100.362  15.367  22.625  1.00 44.62           O  
ATOM   3618  ND2 ASN B 333    -102.236  16.084  23.652  1.00 39.83           N  
ATOM   3619  N   GLU B 334    -101.278  16.503  18.762  1.00 40.40           N  
ATOM   3620  CA  GLU B 334    -100.599  17.550  17.981  1.00 45.26           C  
ATOM   3621  C   GLU B 334     -99.845  18.476  18.913  1.00 41.25           C  
ATOM   3622  O   GLU B 334     -98.792  19.023  18.557  1.00 40.64           O  
ATOM   3623  CB  GLU B 334    -101.610  18.365  17.154  1.00 47.14           C  
ATOM   3624  CG  GLU B 334    -100.982  19.196  16.027  1.00 50.86           C  
ATOM   3625  CD  GLU B 334    -101.981  20.103  15.289  1.00 53.65           C  
ATOM   3626  OE1 GLU B 334    -103.211  19.887  15.412  1.00 49.33           O  
ATOM   3627  OE2 GLU B 334    -101.524  21.031  14.571  1.00 50.32           O  
ATOM   3628  N   ALA B 335    -100.425  18.648  20.098  1.00 40.83           N  
ATOM   3629  CA  ALA B 335     -99.763  19.266  21.227  1.00 42.66           C  
ATOM   3630  C   ALA B 335     -98.317  18.789  21.346  1.00 45.02           C  
ATOM   3631  O   ALA B 335     -97.411  19.592  21.554  1.00 44.20           O  
ATOM   3632  CB  ALA B 335    -100.530  18.951  22.499  1.00 47.48           C  
ATOM   3633  N   ASN B 336     -98.106  17.485  21.193  1.00 46.73           N  
ATOM   3634  CA  ASN B 336     -96.763  16.912  21.231  1.00 47.66           C  
ATOM   3635  C   ASN B 336     -96.317  16.354  19.900  1.00 51.68           C  
ATOM   3636  O   ASN B 336     -95.586  15.352  19.825  1.00 47.24           O  
ATOM   3637  CB  ASN B 336     -96.709  15.820  22.264  1.00 43.07           C  
ATOM   3638  CG  ASN B 336     -97.083  16.311  23.589  1.00 38.08           C  
ATOM   3639  OD1 ASN B 336     -96.224  16.577  24.406  1.00 36.92           O  
ATOM   3640  ND2 ASN B 336     -98.372  16.488  23.814  1.00 37.74           N  
ATOM   3641  N   LYS B 337     -96.765  17.001  18.836  1.00 50.06           N  
ATOM   3642  CA  LYS B 337     -96.272  16.670  17.517  1.00 51.97           C  
ATOM   3643  C   LYS B 337     -96.355  15.158  17.253  1.00 38.88           C  
ATOM   3644  O   LYS B 337     -95.482  14.563  16.633  1.00 34.85           O  
ATOM   3645  CB  LYS B 337     -94.840  17.170  17.407  1.00 53.43           C  
ATOM   3646  CG  LYS B 337     -94.638  18.554  17.966  1.00 47.27           C  
ATOM   3647  CD  LYS B 337     -93.175  18.796  18.271  1.00 52.44           C  
ATOM   3648  CE  LYS B 337     -92.809  18.426  19.701  1.00 54.36           C  
ATOM   3649  NZ  LYS B 337     -91.359  18.764  19.965  1.00 55.43           N  
ATOM   3650  N   TYR B 338     -97.418  14.548  17.753  1.00 39.89           N  
ATOM   3651  CA  TYR B 338     -97.693  13.148  17.488  1.00 43.58           C  
ATOM   3652  C   TYR B 338     -96.517  12.249  17.830  1.00 37.83           C  
ATOM   3653  O   TYR B 338     -96.272  11.252  17.156  1.00 33.19           O  
ATOM   3654  CB  TYR B 338     -98.123  12.983  16.034  1.00 40.34           C  
ATOM   3655  CG  TYR B 338     -99.288  13.879  15.713  1.00 40.66           C  
ATOM   3656  CD1 TYR B 338    -100.530  13.644  16.269  1.00 36.30           C  
ATOM   3657  CD2 TYR B 338     -99.148  14.976  14.878  1.00 41.74           C  
ATOM   3658  CE1 TYR B 338    -101.602  14.461  15.992  1.00 42.19           C  
ATOM   3659  CE2 TYR B 338    -100.236  15.809  14.590  1.00 43.48           C  
ATOM   3660  CZ  TYR B 338    -101.459  15.545  15.152  1.00 38.59           C  
ATOM   3661  OH  TYR B 338    -102.543  16.360  14.892  1.00 40.87           O  
ATOM   3662  N   GLN B 339     -95.814  12.598  18.900  1.00 34.61           N  
ATOM   3663  CA  GLN B 339     -94.741  11.769  19.395  1.00 38.14           C  
ATOM   3664  C   GLN B 339     -95.123  10.303  19.371  1.00 36.91           C  
ATOM   3665  O   GLN B 339     -96.212   9.944  19.813  1.00 37.70           O  
ATOM   3666  CB  GLN B 339     -94.395  12.151  20.826  1.00 44.33           C  
ATOM   3667  CG  GLN B 339     -93.065  11.555  21.308  1.00 53.47           C  
ATOM   3668  CD  GLN B 339     -92.577  12.229  22.570  1.00 56.83           C  
ATOM   3669  OE1 GLN B 339     -91.641  13.028  22.544  1.00 49.11           O  
ATOM   3670  NE2 GLN B 339     -93.240  11.937  23.686  1.00 63.54           N  
ATOM   3671  N   ILE B 340     -94.230   9.451  18.880  1.00 35.39           N  
ATOM   3672  CA  ILE B 340     -94.543   8.025  18.824  1.00 38.59           C  
ATOM   3673  C   ILE B 340     -94.005   7.311  20.035  1.00 39.06           C  
ATOM   3674  O   ILE B 340     -93.123   7.827  20.718  1.00 37.15           O  
ATOM   3675  CB  ILE B 340     -93.925   7.347  17.600  1.00 38.64           C  
ATOM   3676  CG1 ILE B 340     -94.454   5.893  17.468  1.00 32.13           C  
ATOM   3677  CG2 ILE B 340     -92.382   7.461  17.675  1.00 25.25           C  
ATOM   3678  CD1 ILE B 340     -94.493   5.364  16.029  1.00 26.49           C  
ATOM   3679  N   SER B 341     -94.536   6.124  20.295  1.00 33.54           N  
ATOM   3680  CA  SER B 341     -93.811   5.172  21.100  1.00 42.87           C  
ATOM   3681  C   SER B 341     -94.290   3.773  20.815  1.00 47.99           C  
ATOM   3682  O   SER B 341     -95.452   3.457  21.060  1.00 51.65           O  
ATOM   3683  CB  SER B 341     -93.990   5.461  22.582  1.00 50.64           C  
ATOM   3684  OG  SER B 341     -93.552   4.353  23.355  1.00 49.89           O  
ATOM   3685  N   VAL B 342     -93.390   2.926  20.330  1.00 48.81           N  
ATOM   3686  CA  VAL B 342     -93.723   1.534  20.067  1.00 49.28           C  
ATOM   3687  C   VAL B 342     -92.864   0.675  20.961  1.00 45.35           C  
ATOM   3688  O   VAL B 342     -91.811   1.113  21.397  1.00 46.20           O  
ATOM   3689  CB  VAL B 342     -93.463   1.160  18.592  1.00 53.32           C  
ATOM   3690  CG1 VAL B 342     -94.191   2.110  17.648  1.00 51.02           C  
ATOM   3691  CG2 VAL B 342     -91.985   1.183  18.301  1.00 55.14           C  
ATOM   3692  N   ASN B 343     -93.315  -0.540  21.247  1.00 51.14           N  
ATOM   3693  CA  ASN B 343     -92.517  -1.493  22.041  1.00 54.56           C  
ATOM   3694  C   ASN B 343     -93.048  -2.917  21.935  1.00 55.85           C  
ATOM   3695  O   ASN B 343     -94.053  -3.155  21.254  1.00 58.15           O  
ATOM   3696  CB  ASN B 343     -92.404  -1.058  23.515  1.00 53.08           C  
ATOM   3697  CG  ASN B 343     -93.682  -0.482  24.046  1.00 59.39           C  
ATOM   3698  OD1 ASN B 343     -94.357  -1.098  24.875  1.00 62.22           O  
ATOM   3699  ND2 ASN B 343     -94.047   0.704  23.555  1.00 61.45           N  
ATOM   3700  N   LYS B 344     -92.354  -3.852  22.588  1.00 53.50           N  
ATOM   3701  CA  LYS B 344     -92.717  -5.277  22.587  1.00 54.17           C  
ATOM   3702  C   LYS B 344     -92.820  -5.811  21.160  1.00 47.91           C  
ATOM   3703  O   LYS B 344     -93.853  -6.310  20.741  1.00 46.79           O  
ATOM   3704  CB  LYS B 344     -94.009  -5.524  23.390  1.00 54.18           C  
ATOM   3705  CG  LYS B 344     -93.869  -5.240  24.890  1.00 57.28           C  
ATOM   3706  CD  LYS B 344     -95.026  -5.780  25.742  1.00 62.21           C  
ATOM   3707  CE  LYS B 344     -96.268  -4.887  25.669  1.00 65.08           C  
ATOM   3708  NZ  LYS B 344     -97.281  -5.148  26.747  1.00 65.09           N  
ATOM   3709  N   TYR B 345     -91.733  -5.684  20.413  1.00 52.04           N  
ATOM   3710  CA  TYR B 345     -91.749  -6.039  19.005  1.00 49.32           C  
ATOM   3711  C   TYR B 345     -91.549  -7.511  18.829  1.00 49.28           C  
ATOM   3712  O   TYR B 345     -90.886  -8.156  19.629  1.00 53.64           O  
ATOM   3713  CB  TYR B 345     -90.645  -5.326  18.233  1.00 47.46           C  
ATOM   3714  CG  TYR B 345     -90.191  -6.077  16.994  1.00 49.70           C  
ATOM   3715  CD1 TYR B 345     -90.684  -5.758  15.735  1.00 53.17           C  
ATOM   3716  CD2 TYR B 345     -89.272  -7.119  17.084  1.00 49.34           C  
ATOM   3717  CE1 TYR B 345     -90.255  -6.448  14.587  1.00 51.54           C  
ATOM   3718  CE2 TYR B 345     -88.848  -7.815  15.950  1.00 46.76           C  
ATOM   3719  CZ  TYR B 345     -89.336  -7.474  14.709  1.00 44.28           C  
ATOM   3720  OH  TYR B 345     -88.897  -8.159  13.601  1.00 43.36           O  
ATOM   3721  N   ARG B 346     -92.096  -8.025  17.740  1.00 49.56           N  
ATOM   3722  CA  ARG B 346     -91.784  -9.361  17.283  1.00 53.35           C  
ATOM   3723  C   ARG B 346     -91.997  -9.396  15.771  1.00 52.91           C  
ATOM   3724  O   ARG B 346     -92.456  -8.408  15.184  1.00 48.45           O  
ATOM   3725  CB  ARG B 346     -92.665 -10.378  18.007  1.00 54.43           C  
ATOM   3726  CG  ARG B 346     -94.126 -10.300  17.615  1.00 62.79           C  
ATOM   3727  CD  ARG B 346     -95.102 -10.683  18.735  1.00 69.30           C  
ATOM   3728  NE  ARG B 346     -96.468 -10.838  18.213  1.00 75.92           N  
ATOM   3729  CZ  ARG B 346     -96.959 -11.952  17.661  1.00 76.71           C  
ATOM   3730  NH1 ARG B 346     -96.208 -13.052  17.566  1.00 81.10           N  
ATOM   3731  NH2 ARG B 346     -98.211 -11.971  17.201  1.00 67.36           N  
ATOM   3732  N   GLY B 347     -91.633 -10.511  15.141  1.00 53.54           N  
ATOM   3733  CA  GLY B 347     -91.880 -10.711  13.708  1.00 52.09           C  
ATOM   3734  C   GLY B 347     -90.626 -10.688  12.853  1.00 50.58           C  
ATOM   3735  O   GLY B 347     -89.513 -10.506  13.364  1.00 50.35           O  
ATOM   3736  N   THR B 348     -90.823 -10.839  11.543  1.00 43.68           N  
ATOM   3737  CA  THR B 348     -89.734 -11.133  10.608  1.00 43.02           C  
ATOM   3738  C   THR B 348     -89.179  -9.952   9.788  1.00 43.19           C  
ATOM   3739  O   THR B 348     -88.066 -10.019   9.282  1.00 42.87           O  
ATOM   3740  CB  THR B 348     -90.173 -12.246   9.635  1.00 40.69           C  
ATOM   3741  OG1 THR B 348     -91.439 -11.916   9.051  1.00 43.75           O  
ATOM   3742  CG2 THR B 348     -90.314 -13.555  10.378  1.00 40.34           C  
ATOM   3743  N   ALA B 349     -89.942  -8.876   9.643  1.00 48.22           N  
ATOM   3744  CA  ALA B 349     -89.519  -7.782   8.774  1.00 42.46           C  
ATOM   3745  C   ALA B 349     -88.197  -7.268   9.256  1.00 45.54           C  
ATOM   3746  O   ALA B 349     -87.339  -6.903   8.460  1.00 49.57           O  
ATOM   3747  CB  ALA B 349     -90.524  -6.681   8.779  1.00 44.83           C  
ATOM   3748  N   GLY B 350     -88.041  -7.260  10.573  1.00 49.26           N  
ATOM   3749  CA  GLY B 350     -86.831  -6.785  11.202  1.00 49.76           C  
ATOM   3750  C   GLY B 350     -87.148  -5.461  11.838  1.00 40.36           C  
ATOM   3751  O   GLY B 350     -87.338  -4.470  11.143  1.00 37.73           O  
ATOM   3752  N   ASN B 351     -87.221  -5.486  13.166  1.00 43.39           N  
ATOM   3753  CA  ASN B 351     -87.474  -4.322  14.013  1.00 43.04           C  
ATOM   3754  C   ASN B 351     -86.677  -3.064  13.659  1.00 43.47           C  
ATOM   3755  O   ASN B 351     -85.528  -2.904  14.080  1.00 36.98           O  
ATOM   3756  CB  ASN B 351     -87.160  -4.692  15.459  1.00 40.37           C  
ATOM   3757  CG  ASN B 351     -87.549  -3.628  16.408  1.00 41.79           C  
ATOM   3758  OD1 ASN B 351     -88.160  -3.896  17.429  1.00 47.72           O  
ATOM   3759  ND2 ASN B 351     -87.233  -2.395  16.067  1.00 46.26           N  
ATOM   3760  N   ALA B 352     -87.303  -2.161  12.915  1.00 41.76           N  
ATOM   3761  CA  ALA B 352     -86.663  -0.912  12.563  1.00 37.03           C  
ATOM   3762  C   ALA B 352     -87.141   0.181  13.484  1.00 40.19           C  
ATOM   3763  O   ALA B 352     -86.366   1.054  13.849  1.00 45.38           O  
ATOM   3764  CB  ALA B 352     -86.944  -0.555  11.148  1.00 34.48           C  
ATOM   3765  N   LEU B 353     -88.404   0.153  13.888  1.00 41.71           N  
ATOM   3766  CA  LEU B 353     -88.930   1.314  14.596  1.00 42.59           C  
ATOM   3767  C   LEU B 353     -88.222   1.499  15.910  1.00 45.31           C  
ATOM   3768  O   LEU B 353     -87.980   2.635  16.318  1.00 50.29           O  
ATOM   3769  CB  LEU B 353     -90.417   1.229  14.883  1.00 38.74           C  
ATOM   3770  CG  LEU B 353     -91.465   0.967  13.808  1.00 34.59           C  
ATOM   3771  CD1 LEU B 353     -92.836   0.962  14.527  1.00 24.17           C  
ATOM   3772  CD2 LEU B 353     -91.402   1.946  12.652  1.00 24.75           C  
ATOM   3773  N   MET B 354     -87.914   0.396  16.582  1.00 44.60           N  
ATOM   3774  CA  MET B 354     -87.228   0.478  17.873  1.00 51.91           C  
ATOM   3775  C   MET B 354     -85.738   0.639  17.696  1.00 50.91           C  
ATOM   3776  O   MET B 354     -85.156   1.612  18.166  1.00 44.63           O  
ATOM   3777  CB  MET B 354     -87.479  -0.758  18.733  1.00 48.53           C  
ATOM   3778  CG  MET B 354     -88.922  -1.154  18.852  1.00 47.98           C  
ATOM   3779  SD  MET B 354     -89.322  -1.517  20.560  1.00 54.57           S  
ATOM   3780  CE  MET B 354     -89.079  -3.296  20.770  1.00 48.20           C  
ATOM   3781  N   ASP B 355     -85.148  -0.329  16.995  1.00 58.34           N  
ATOM   3782  CA  ASP B 355     -83.705  -0.575  17.003  1.00 55.96           C  
ATOM   3783  C   ASP B 355     -82.976  -0.068  15.776  1.00 44.93           C  
ATOM   3784  O   ASP B 355     -81.765  -0.158  15.720  1.00 48.57           O  
ATOM   3785  CB  ASP B 355     -83.444  -2.073  17.147  1.00 62.78           C  
ATOM   3786  CG  ASP B 355     -83.734  -2.587  18.554  1.00 73.56           C  
ATOM   3787  OD1 ASP B 355     -84.675  -2.084  19.212  1.00 74.42           O  
ATOM   3788  OD2 ASP B 355     -83.012  -3.504  19.007  1.00 79.09           O  
ATOM   3789  N   GLY B 356     -83.707   0.449  14.795  1.00 44.70           N  
ATOM   3790  CA  GLY B 356     -83.115   1.152  13.666  1.00 42.47           C  
ATOM   3791  C   GLY B 356     -82.376   0.269  12.677  1.00 46.27           C  
ATOM   3792  O   GLY B 356     -82.243  -0.934  12.870  1.00 47.70           O  
ATOM   3793  N   ALA B 357     -81.864   0.897  11.629  1.00 45.94           N  
ATOM   3794  CA  ALA B 357     -81.320   0.206  10.469  1.00 47.08           C  
ATOM   3795  C   ALA B 357     -80.168  -0.724  10.792  1.00 53.58           C  
ATOM   3796  O   ALA B 357     -79.111  -0.269  11.221  1.00 58.65           O  
ATOM   3797  CB  ALA B 357     -80.855   1.227   9.480  1.00 57.79           C  
ATOM   3798  N   SER B 358     -80.337  -2.017  10.523  1.00 58.56           N  
ATOM   3799  CA  SER B 358     -79.352  -3.033  10.957  1.00 59.73           C  
ATOM   3800  C   SER B 358     -78.051  -3.154  10.134  1.00 58.58           C  
ATOM   3801  O   SER B 358     -77.106  -3.799  10.578  1.00 56.88           O  
ATOM   3802  CB  SER B 358     -80.007  -4.411  11.023  1.00 57.83           C  
ATOM   3803  OG  SER B 358     -79.986  -5.027   9.748  1.00 57.81           O  
ATOM   3804  N   GLN B 359     -78.018  -2.585   8.932  1.00 59.26           N  
ATOM   3805  CA  GLN B 359     -76.794  -2.567   8.116  1.00 53.31           C  
ATOM   3806  C   GLN B 359     -75.917  -1.364   8.440  1.00 52.20           C  
ATOM   3807  O   GLN B 359     -74.711  -1.386   8.187  1.00 57.92           O  
ATOM   3808  CB  GLN B 359     -77.112  -2.561   6.624  1.00 55.21           C  
ATOM   3809  CG  GLN B 359     -78.059  -1.465   6.178  1.00 56.43           C  
ATOM   3810  CD  GLN B 359     -79.393  -2.014   5.729  1.00 60.07           C  
ATOM   3811  OE1 GLN B 359     -79.493  -2.530   4.614  1.00 61.68           O  
ATOM   3812  NE2 GLN B 359     -80.429  -1.909   6.585  1.00 49.23           N  
ATOM   3813  N   LEU B 360     -76.528  -0.312   8.975  1.00 45.81           N  
ATOM   3814  CA  LEU B 360     -75.774   0.787   9.541  1.00 45.33           C  
ATOM   3815  C   LEU B 360     -75.139   0.339  10.842  1.00 45.17           C  
ATOM   3816  O   LEU B 360     -75.532  -0.664  11.434  1.00 41.24           O  
ATOM   3817  CB  LEU B 360     -76.679   1.966   9.843  1.00 46.31           C  
ATOM   3818  CG  LEU B 360     -77.438   2.569   8.687  1.00 45.00           C  
ATOM   3819  CD1 LEU B 360     -78.291   3.724   9.199  1.00 41.05           C  
ATOM   3820  CD2 LEU B 360     -76.461   2.997   7.625  1.00 37.83           C  
ATOM   3821  N   MET B 361     -74.185   1.126  11.307  1.00 48.17           N  
ATOM   3822  CA  MET B 361     -73.421   0.766  12.468  1.00 56.01           C  
ATOM   3823  C   MET B 361     -73.352   1.902  13.468  1.00 59.27           C  
ATOM   3824  O   MET B 361     -73.249   3.071  13.091  1.00 58.22           O  
ATOM   3825  CB  MET B 361     -72.027   0.349  12.023  1.00 66.06           C  
ATOM   3826  CG  MET B 361     -71.945  -1.113  11.747  1.00 72.48           C  
ATOM   3827  SD  MET B 361     -71.922  -1.958  13.325  1.00 86.06           S  
ATOM   3828  CE  MET B 361     -70.172  -1.790  13.713  1.00 82.64           C  
ATOM   3829  N   GLY B 362     -73.440   1.535  14.746  1.00 63.87           N  
ATOM   3830  CA  GLY B 362     -73.258   2.452  15.870  1.00 65.54           C  
ATOM   3831  C   GLY B 362     -74.031   3.763  15.829  1.00 63.72           C  
ATOM   3832  O   GLY B 362     -75.253   3.779  15.862  1.00 61.75           O  
ATOM   3833  N   GLU B 363     -73.285   4.860  15.777  1.00 63.62           N  
ATOM   3834  CA  GLU B 363     -73.818   6.218  15.737  1.00 62.69           C  
ATOM   3835  C   GLU B 363     -74.741   6.443  14.542  1.00 63.23           C  
ATOM   3836  O   GLU B 363     -75.808   7.034  14.691  1.00 70.10           O  
ATOM   3837  CB  GLU B 363     -72.631   7.189  15.714  1.00 70.14           C  
ATOM   3838  CG  GLU B 363     -72.840   8.564  15.098  1.00 74.40           C  
ATOM   3839  CD  GLU B 363     -71.519   9.175  14.622  1.00 79.19           C  
ATOM   3840  OE1 GLU B 363     -71.553  10.021  13.702  1.00 84.90           O  
ATOM   3841  OE2 GLU B 363     -70.447   8.800  15.158  1.00 76.35           O  
ATOM   3842  N   ASN B 364     -74.337   5.965  13.366  1.00 62.87           N  
ATOM   3843  CA  ASN B 364     -75.138   6.139  12.159  1.00 59.04           C  
ATOM   3844  C   ASN B 364     -76.421   5.340  12.220  1.00 57.33           C  
ATOM   3845  O   ASN B 364     -77.353   5.645  11.490  1.00 67.84           O  
ATOM   3846  CB  ASN B 364     -74.360   5.749  10.906  1.00 66.62           C  
ATOM   3847  CG  ASN B 364     -73.183   6.670  10.634  1.00 77.63           C  
ATOM   3848  OD1 ASN B 364     -73.349   7.851  10.320  1.00 74.47           O  
ATOM   3849  ND2 ASN B 364     -71.977   6.127  10.772  1.00 92.34           N  
ATOM   3850  N   ARG B 365     -76.477   4.318  13.073  1.00 50.69           N  
ATOM   3851  CA  ARG B 365     -77.714   3.563  13.260  1.00 49.87           C  
ATOM   3852  C   ARG B 365     -78.696   4.293  14.160  1.00 55.67           C  
ATOM   3853  O   ARG B 365     -79.861   4.471  13.806  1.00 57.30           O  
ATOM   3854  CB  ARG B 365     -77.449   2.189  13.866  1.00 51.39           C  
ATOM   3855  CG  ARG B 365     -78.708   1.512  14.464  1.00 52.28           C  
ATOM   3856  CD  ARG B 365     -78.323   0.415  15.429  1.00 57.39           C  
ATOM   3857  NE  ARG B 365     -77.364  -0.483  14.795  1.00 60.89           N  
ATOM   3858  CZ  ARG B 365     -77.650  -1.673  14.275  1.00 66.93           C  
ATOM   3859  NH1 ARG B 365     -78.884  -2.178  14.334  1.00 69.42           N  
ATOM   3860  NH2 ARG B 365     -76.676  -2.381  13.715  1.00 69.17           N  
ATOM   3861  N   THR B 366     -78.233   4.701  15.339  1.00 57.52           N  
ATOM   3862  CA  THR B 366     -79.142   5.205  16.370  1.00 49.55           C  
ATOM   3863  C   THR B 366     -79.631   6.598  15.997  1.00 50.84           C  
ATOM   3864  O   THR B 366     -80.295   7.261  16.785  1.00 57.59           O  
ATOM   3865  CB  THR B 366     -78.516   5.196  17.799  1.00 44.68           C  
ATOM   3866  OG1 THR B 366     -77.726   6.365  17.995  1.00 48.82           O  
ATOM   3867  CG2 THR B 366     -77.640   3.957  18.038  1.00 38.30           C  
ATOM   3868  N   MET B 367     -79.287   7.051  14.798  1.00 49.84           N  
ATOM   3869  CA  MET B 367     -79.992   8.167  14.198  1.00 56.19           C  
ATOM   3870  C   MET B 367     -81.031   7.671  13.160  1.00 57.23           C  
ATOM   3871  O   MET B 367     -81.471   8.433  12.298  1.00 58.73           O  
ATOM   3872  CB  MET B 367     -78.995   9.158  13.595  1.00 53.06           C  
ATOM   3873  CG  MET B 367     -78.116   8.595  12.511  1.00 52.02           C  
ATOM   3874  SD  MET B 367     -77.139   9.886  11.726  1.00 57.05           S  
ATOM   3875  CE  MET B 367     -75.525   9.674  12.458  1.00 52.48           C  
ATOM   3876  N   THR B 368     -81.418   6.398  13.239  1.00 50.15           N  
ATOM   3877  CA  THR B 368     -82.483   5.866  12.386  1.00 49.13           C  
ATOM   3878  C   THR B 368     -83.644   5.284  13.200  1.00 46.61           C  
ATOM   3879  O   THR B 368     -84.617   4.771  12.639  1.00 40.89           O  
ATOM   3880  CB  THR B 368     -81.953   4.799  11.392  1.00 51.31           C  
ATOM   3881  OG1 THR B 368     -81.440   3.664  12.099  1.00 52.34           O  
ATOM   3882  CG2 THR B 368     -80.869   5.376  10.515  1.00 45.48           C  
ATOM   3883  N   ILE B 369     -83.547   5.394  14.521  1.00 47.92           N  
ATOM   3884  CA  ILE B 369     -84.609   4.940  15.410  1.00 47.53           C  
ATOM   3885  C   ILE B 369     -85.801   5.901  15.403  1.00 48.14           C  
ATOM   3886  O   ILE B 369     -85.654   7.126  15.536  1.00 47.40           O  
ATOM   3887  CB  ILE B 369     -84.101   4.755  16.845  1.00 37.78           C  
ATOM   3888  CG1 ILE B 369     -82.926   3.785  16.839  1.00 41.82           C  
ATOM   3889  CG2 ILE B 369     -85.209   4.234  17.729  1.00 39.76           C  
ATOM   3890  CD1 ILE B 369     -82.758   2.986  18.115  1.00 47.92           C  
ATOM   3891  N   HIS B 370     -86.985   5.326  15.250  1.00 42.32           N  
ATOM   3892  CA  HIS B 370     -88.205   6.103  15.200  1.00 41.36           C  
ATOM   3893  C   HIS B 370     -88.828   6.177  16.568  1.00 38.05           C  
ATOM   3894  O   HIS B 370     -89.552   7.136  16.899  1.00 30.94           O  
ATOM   3895  CB  HIS B 370     -89.123   5.473  14.183  1.00 39.37           C  
ATOM   3896  CG  HIS B 370     -88.472   5.349  12.854  1.00 40.84           C  
ATOM   3897  ND1 HIS B 370     -88.476   6.374  11.937  1.00 41.34           N  
ATOM   3898  CD2 HIS B 370     -87.700   4.373  12.329  1.00 38.96           C  
ATOM   3899  CE1 HIS B 370     -87.788   6.009  10.874  1.00 39.61           C  
ATOM   3900  NE2 HIS B 370     -87.305   4.799  11.086  1.00 41.02           N  
ATOM   3901  N   ASN B 371     -88.513   5.176  17.381  1.00 36.87           N  
ATOM   3902  CA  ASN B 371     -89.057   5.128  18.716  1.00 39.21           C  
ATOM   3903  C   ASN B 371     -88.757   6.453  19.468  1.00 35.15           C  
ATOM   3904  O   ASN B 371     -87.603   6.867  19.610  1.00 33.61           O  
ATOM   3905  CB  ASN B 371     -88.552   3.887  19.446  1.00 34.35           C  
ATOM   3906  CG  ASN B 371     -89.287   3.644  20.730  1.00 42.84           C  
ATOM   3907  OD1 ASN B 371     -89.502   4.563  21.514  1.00 50.25           O  
ATOM   3908  ND2 ASN B 371     -89.689   2.403  20.958  1.00 48.64           N  
ATOM   3909  N   GLY B 372     -89.809   7.140  19.896  1.00 24.86           N  
ATOM   3910  CA  GLY B 372     -89.643   8.414  20.578  1.00 30.26           C  
ATOM   3911  C   GLY B 372     -89.648   9.651  19.682  1.00 33.74           C  
ATOM   3912  O   GLY B 372     -89.808  10.783  20.165  1.00 25.06           O  
ATOM   3913  N   MET B 373     -89.528   9.453  18.374  1.00 32.74           N  
ATOM   3914  CA  MET B 373     -89.447  10.582  17.454  1.00 33.33           C  
ATOM   3915  C   MET B 373     -90.748  11.345  17.263  1.00 29.54           C  
ATOM   3916  O   MET B 373     -91.797  10.953  17.755  1.00 35.67           O  
ATOM   3917  CB  MET B 373     -88.921  10.092  16.112  1.00 46.20           C  
ATOM   3918  CG  MET B 373     -87.525   9.434  16.196  1.00 47.15           C  
ATOM   3919  SD  MET B 373     -86.292  10.362  17.154  1.00 46.48           S  
ATOM   3920  CE  MET B 373     -86.664  12.086  16.709  1.00 49.30           C  
ATOM   3921  N   PHE B 374     -90.668  12.465  16.569  1.00 33.80           N  
ATOM   3922  CA  PHE B 374     -91.854  13.266  16.315  1.00 37.12           C  
ATOM   3923  C   PHE B 374     -92.198  13.210  14.871  1.00 35.46           C  
ATOM   3924  O   PHE B 374     -91.326  13.223  13.994  1.00 36.44           O  
ATOM   3925  CB  PHE B 374     -91.633  14.718  16.676  1.00 40.21           C  
ATOM   3926  CG  PHE B 374     -91.213  14.913  18.075  1.00 43.43           C  
ATOM   3927  CD1 PHE B 374     -92.150  14.985  19.087  1.00 45.87           C  
ATOM   3928  CD2 PHE B 374     -89.870  14.991  18.396  1.00 45.09           C  
ATOM   3929  CE1 PHE B 374     -91.752  15.152  20.403  1.00 47.75           C  
ATOM   3930  CE2 PHE B 374     -89.461  15.154  19.709  1.00 42.61           C  
ATOM   3931  CZ  PHE B 374     -90.396  15.239  20.711  1.00 43.30           C  
ATOM   3932  N   PHE B 375     -93.487  13.177  14.627  1.00 31.67           N  
ATOM   3933  CA  PHE B 375     -93.963  13.189  13.290  1.00 39.65           C  
ATOM   3934  C   PHE B 375     -93.534  14.503  12.608  1.00 42.43           C  
ATOM   3935  O   PHE B 375     -93.676  15.582  13.182  1.00 44.23           O  
ATOM   3936  CB  PHE B 375     -95.478  13.040  13.291  1.00 48.09           C  
ATOM   3937  CG  PHE B 375     -96.020  12.707  11.964  1.00 50.79           C  
ATOM   3938  CD1 PHE B 375     -96.330  11.397  11.648  1.00 51.22           C  
ATOM   3939  CD2 PHE B 375     -96.151  13.697  10.990  1.00 50.85           C  
ATOM   3940  CE1 PHE B 375     -96.794  11.081  10.399  1.00 53.28           C  
ATOM   3941  CE2 PHE B 375     -96.609  13.389   9.735  1.00 52.10           C  
ATOM   3942  CZ  PHE B 375     -96.937  12.080   9.436  1.00 54.48           C  
ATOM   3943  N   SER B 376     -93.020  14.392  11.383  1.00 41.76           N  
ATOM   3944  CA  SER B 376     -92.515  15.531  10.614  1.00 38.65           C  
ATOM   3945  C   SER B 376     -93.098  15.514   9.193  1.00 42.11           C  
ATOM   3946  O   SER B 376     -93.227  14.451   8.579  1.00 40.13           O  
ATOM   3947  CB  SER B 376     -90.984  15.461  10.535  1.00 38.26           C  
ATOM   3948  OG  SER B 376     -90.440  14.530  11.482  1.00 37.31           O  
ATOM   3949  N   THR B 377     -93.472  16.690   8.691  1.00 45.71           N  
ATOM   3950  CA  THR B 377     -93.764  16.899   7.266  1.00 44.42           C  
ATOM   3951  C   THR B 377     -92.829  17.996   6.798  1.00 49.14           C  
ATOM   3952  O   THR B 377     -92.146  18.615   7.616  1.00 47.25           O  
ATOM   3953  CB  THR B 377     -95.186  17.377   7.022  1.00 42.00           C  
ATOM   3954  OG1 THR B 377     -95.438  18.529   7.826  1.00 40.41           O  
ATOM   3955  CG2 THR B 377     -96.173  16.312   7.369  1.00 46.82           C  
ATOM   3956  N   TYR B 378     -92.790  18.244   5.494  1.00 50.69           N  
ATOM   3957  CA  TYR B 378     -91.810  19.178   4.958  1.00 52.59           C  
ATOM   3958  C   TYR B 378     -92.079  20.629   5.352  1.00 55.35           C  
ATOM   3959  O   TYR B 378     -91.129  21.417   5.499  1.00 61.02           O  
ATOM   3960  CB  TYR B 378     -91.660  19.026   3.445  1.00 57.55           C  
ATOM   3961  CG  TYR B 378     -92.833  19.452   2.609  1.00 55.03           C  
ATOM   3962  CD1 TYR B 378     -92.949  20.751   2.161  1.00 53.22           C  
ATOM   3963  CD2 TYR B 378     -93.792  18.536   2.211  1.00 67.57           C  
ATOM   3964  CE1 TYR B 378     -94.006  21.145   1.369  1.00 54.50           C  
ATOM   3965  CE2 TYR B 378     -94.864  18.922   1.412  1.00 68.91           C  
ATOM   3966  CZ  TYR B 378     -94.962  20.234   0.996  1.00 58.15           C  
ATOM   3967  OH  TYR B 378     -96.020  20.630   0.211  1.00 58.19           O  
ATOM   3968  N   ASP B 379     -93.346  20.985   5.547  1.00 43.74           N  
ATOM   3969  CA  ASP B 379     -93.655  22.293   6.111  1.00 46.79           C  
ATOM   3970  C   ASP B 379     -93.744  22.251   7.631  1.00 48.35           C  
ATOM   3971  O   ASP B 379     -94.397  23.102   8.229  1.00 54.06           O  
ATOM   3972  CB  ASP B 379     -94.956  22.850   5.533  1.00 53.48           C  
ATOM   3973  CG  ASP B 379     -96.172  22.109   6.021  1.00 49.65           C  
ATOM   3974  OD1 ASP B 379     -96.104  20.871   6.068  1.00 49.82           O  
ATOM   3975  OD2 ASP B 379     -97.184  22.755   6.356  1.00 43.01           O  
ATOM   3976  N   ARG B 380     -93.100  21.266   8.258  1.00 50.70           N  
ATOM   3977  CA  ARG B 380     -93.087  21.164   9.720  1.00 48.65           C  
ATOM   3978  C   ARG B 380     -91.971  20.259  10.251  1.00 46.20           C  
ATOM   3979  O   ARG B 380     -92.183  19.066  10.463  1.00 46.83           O  
ATOM   3980  CB  ARG B 380     -94.437  20.660  10.205  1.00 52.29           C  
ATOM   3981  CG  ARG B 380     -94.809  21.196  11.545  1.00 53.14           C  
ATOM   3982  CD  ARG B 380     -95.318  22.622  11.448  1.00 54.27           C  
ATOM   3983  NE  ARG B 380     -96.759  22.707  11.635  1.00 55.69           N  
ATOM   3984  CZ  ARG B 380     -97.381  22.418  12.771  1.00 58.47           C  
ATOM   3985  NH1 ARG B 380     -96.696  21.992  13.828  1.00 67.42           N  
ATOM   3986  NH2 ARG B 380     -98.696  22.537  12.854  1.00 61.33           N  
ATOM   3987  N   ASP B 381     -90.789  20.843  10.469  1.00 44.89           N  
ATOM   3988  CA  ASP B 381     -89.580  20.086  10.823  1.00 43.93           C  
ATOM   3989  C   ASP B 381     -89.593  19.746  12.315  1.00 45.64           C  
ATOM   3990  O   ASP B 381     -89.401  20.618  13.171  1.00 47.33           O  
ATOM   3991  CB  ASP B 381     -88.318  20.861  10.350  1.00 48.89           C  
ATOM   3992  CG  ASP B 381     -87.016  20.534  11.135  1.00 47.52           C  
ATOM   3993  OD1 ASP B 381     -85.952  21.135  10.808  1.00 45.01           O  
ATOM   3994  OD2 ASP B 381     -87.022  19.720  12.073  1.00 49.84           O  
ATOM   3995  N   ASN B 382     -89.867  18.471  12.605  1.00 42.54           N  
ATOM   3996  CA  ASN B 382     -89.723  17.909  13.944  1.00 45.26           C  
ATOM   3997  C   ASN B 382     -88.716  16.774  13.962  1.00 46.96           C  
ATOM   3998  O   ASN B 382     -88.727  15.926  14.863  1.00 52.59           O  
ATOM   3999  CB  ASN B 382     -91.056  17.388  14.450  1.00 46.84           C  
ATOM   4000  CG  ASN B 382     -92.122  18.430  14.426  1.00 49.31           C  
ATOM   4001  OD1 ASN B 382     -91.875  19.600  14.730  1.00 50.16           O  
ATOM   4002  ND2 ASN B 382     -93.333  18.017  14.070  1.00 55.72           N  
ATOM   4003  N   ASP B 383     -87.834  16.771  12.970  1.00 47.25           N  
ATOM   4004  CA  ASP B 383     -86.878  15.691  12.788  1.00 49.74           C  
ATOM   4005  C   ASP B 383     -85.786  15.716  13.866  1.00 49.91           C  
ATOM   4006  O   ASP B 383     -85.800  16.572  14.750  1.00 48.49           O  
ATOM   4007  CB  ASP B 383     -86.283  15.748  11.374  1.00 50.49           C  
ATOM   4008  CG  ASP B 383     -85.475  17.030  11.107  1.00 58.15           C  
ATOM   4009  OD1 ASP B 383     -84.800  17.561  12.033  1.00 54.80           O  
ATOM   4010  OD2 ASP B 383     -85.501  17.499   9.942  1.00 58.79           O  
ATOM   4011  N   GLY B 384     -84.858  14.761  13.789  1.00 53.29           N  
ATOM   4012  CA  GLY B 384     -83.728  14.679  14.720  1.00 55.59           C  
ATOM   4013  C   GLY B 384     -82.437  15.241  14.145  1.00 50.57           C  
ATOM   4014  O   GLY B 384     -81.351  15.058  14.704  1.00 47.66           O  
ATOM   4015  N   TRP B 385     -82.575  15.950  13.037  1.00 47.38           N  
ATOM   4016  CA  TRP B 385     -81.460  16.379  12.247  1.00 49.75           C  
ATOM   4017  C   TRP B 385     -81.454  17.882  12.342  1.00 53.36           C  
ATOM   4018  O   TRP B 385     -82.173  18.567  11.618  1.00 53.83           O  
ATOM   4019  CB  TRP B 385     -81.699  15.920  10.827  1.00 52.83           C  
ATOM   4020  CG  TRP B 385     -80.582  16.066   9.907  1.00 53.40           C  
ATOM   4021  CD1 TRP B 385     -79.270  16.175  10.214  1.00 59.34           C  
ATOM   4022  CD2 TRP B 385     -80.667  16.053   8.488  1.00 52.95           C  
ATOM   4023  NE1 TRP B 385     -78.520  16.256   9.068  1.00 61.44           N  
ATOM   4024  CE2 TRP B 385     -79.362  16.183   7.991  1.00 57.47           C  
ATOM   4025  CE3 TRP B 385     -81.725  15.953   7.586  1.00 53.60           C  
ATOM   4026  CZ2 TRP B 385     -79.087  16.213   6.629  1.00 60.37           C  
ATOM   4027  CZ3 TRP B 385     -81.451  15.991   6.229  1.00 55.98           C  
ATOM   4028  CH2 TRP B 385     -80.148  16.115   5.764  1.00 59.11           C  
ATOM   4029  N   LEU B 386     -80.657  18.389  13.268  1.00 55.82           N  
ATOM   4030  CA  LEU B 386     -80.722  19.783  13.646  1.00 58.25           C  
ATOM   4031  C   LEU B 386     -79.752  20.544  12.781  1.00 63.26           C  
ATOM   4032  O   LEU B 386     -78.539  20.298  12.832  1.00 64.97           O  
ATOM   4033  CB  LEU B 386     -80.390  19.950  15.124  1.00 58.37           C  
ATOM   4034  CG  LEU B 386     -81.031  18.899  16.032  1.00 64.05           C  
ATOM   4035  CD1 LEU B 386     -80.848  19.319  17.478  1.00 71.67           C  
ATOM   4036  CD2 LEU B 386     -82.521  18.676  15.700  1.00 64.76           C  
ATOM   4037  N   THR B 387     -80.288  21.439  11.957  1.00 65.41           N  
ATOM   4038  CA  THR B 387     -79.450  22.216  11.063  1.00 67.65           C  
ATOM   4039  C   THR B 387     -80.035  23.579  10.823  1.00 69.18           C  
ATOM   4040  O   THR B 387     -81.247  23.728  10.679  1.00 73.63           O  
ATOM   4041  CB  THR B 387     -79.269  21.548   9.679  1.00 67.57           C  
ATOM   4042  OG1 THR B 387     -79.545  20.140   9.752  1.00 67.68           O  
ATOM   4043  CG2 THR B 387     -77.842  21.785   9.168  1.00 65.84           C  
ATOM   4044  N   SER B 388     -79.145  24.563  10.772  1.00 69.98           N  
ATOM   4045  CA  SER B 388     -79.447  25.902  10.289  1.00 72.20           C  
ATOM   4046  C   SER B 388     -80.047  25.852   8.879  1.00 69.34           C  
ATOM   4047  O   SER B 388     -80.798  26.748   8.489  1.00 63.67           O  
ATOM   4048  CB  SER B 388     -78.140  26.720  10.280  1.00 78.99           C  
ATOM   4049  OG  SER B 388     -78.315  28.045   9.793  1.00 83.25           O  
ATOM   4050  N   ASP B 389     -79.714  24.789   8.141  1.00 69.68           N  
ATOM   4051  CA  ASP B 389     -80.029  24.639   6.712  1.00 68.66           C  
ATOM   4052  C   ASP B 389     -81.511  24.403   6.386  1.00 66.86           C  
ATOM   4053  O   ASP B 389     -82.115  23.471   6.911  1.00 64.37           O  
ATOM   4054  CB  ASP B 389     -79.211  23.476   6.147  1.00 63.47           C  
ATOM   4055  CG  ASP B 389     -79.269  23.394   4.639  1.00 60.52           C  
ATOM   4056  OD1 ASP B 389     -80.379  23.520   4.080  1.00 59.29           O  
ATOM   4057  OD2 ASP B 389     -78.197  23.195   4.015  1.00 54.52           O  
ATOM   4058  N   PRO B 390     -82.092  25.240   5.497  1.00 71.80           N  
ATOM   4059  CA  PRO B 390     -83.468  25.002   5.018  1.00 69.45           C  
ATOM   4060  C   PRO B 390     -83.640  23.663   4.296  1.00 68.48           C  
ATOM   4061  O   PRO B 390     -84.368  22.802   4.769  1.00 69.31           O  
ATOM   4062  CB  PRO B 390     -83.724  26.175   4.061  1.00 70.61           C  
ATOM   4063  CG  PRO B 390     -82.751  27.255   4.499  1.00 74.28           C  
ATOM   4064  CD  PRO B 390     -81.560  26.550   5.060  1.00 71.52           C  
ATOM   4065  N   ARG B 391     -82.938  23.479   3.184  1.00 73.16           N  
ATOM   4066  CA  ARG B 391     -83.138  22.312   2.311  1.00 74.92           C  
ATOM   4067  C   ARG B 391     -82.892  20.970   2.986  1.00 63.62           C  
ATOM   4068  O   ARG B 391     -83.308  19.940   2.460  1.00 59.07           O  
ATOM   4069  CB  ARG B 391     -82.237  22.416   1.069  1.00 81.45           C  
ATOM   4070  CG  ARG B 391     -82.698  23.447   0.033  1.00 83.47           C  
ATOM   4071  CD  ARG B 391     -81.591  23.825  -0.939  1.00 85.08           C  
ATOM   4072  NE  ARG B 391     -80.594  24.704  -0.318  1.00 87.62           N  
ATOM   4073  CZ  ARG B 391     -79.414  24.321   0.180  1.00 89.58           C  
ATOM   4074  NH1 ARG B 391     -79.028  23.048   0.148  1.00 92.00           N  
ATOM   4075  NH2 ARG B 391     -78.600  25.226   0.719  1.00 89.70           N  
ATOM   4076  N   LYS B 392     -82.217  20.989   4.134  1.00 58.40           N  
ATOM   4077  CA  LYS B 392     -81.808  19.762   4.808  1.00 63.90           C  
ATOM   4078  C   LYS B 392     -82.751  19.401   5.946  1.00 61.64           C  
ATOM   4079  O   LYS B 392     -82.370  19.413   7.112  1.00 64.57           O  
ATOM   4080  CB  LYS B 392     -80.369  19.880   5.327  1.00 71.11           C  
ATOM   4081  CG  LYS B 392     -79.293  19.857   4.233  1.00 79.16           C  
ATOM   4082  CD  LYS B 392     -78.876  18.430   3.871  1.00 84.33           C  
ATOM   4083  CE  LYS B 392     -77.693  18.350   2.893  1.00 88.01           C  
ATOM   4084  NZ  LYS B 392     -77.401  16.934   2.454  1.00 86.92           N  
ATOM   4085  N   GLN B 393     -83.989  19.077   5.591  1.00 63.80           N  
ATOM   4086  CA  GLN B 393     -84.964  18.505   6.523  1.00 57.24           C  
ATOM   4087  C   GLN B 393     -85.321  17.114   6.014  1.00 52.16           C  
ATOM   4088  O   GLN B 393     -85.335  16.904   4.807  1.00 54.62           O  
ATOM   4089  CB  GLN B 393     -86.230  19.349   6.544  1.00 57.06           C  
ATOM   4090  CG  GLN B 393     -86.065  20.785   6.989  1.00 49.80           C  
ATOM   4091  CD  GLN B 393     -87.210  21.624   6.500  1.00 47.67           C  
ATOM   4092  OE1 GLN B 393     -87.238  22.023   5.342  1.00 50.79           O  
ATOM   4093  NE2 GLN B 393     -88.182  21.873   7.365  1.00 51.73           N  
ATOM   4094  N   CYS B 394     -85.637  16.177   6.905  1.00 52.10           N  
ATOM   4095  CA  CYS B 394     -85.907  14.785   6.483  1.00 53.21           C  
ATOM   4096  C   CYS B 394     -87.080  14.595   5.491  1.00 54.08           C  
ATOM   4097  O   CYS B 394     -86.890  14.000   4.424  1.00 49.43           O  
ATOM   4098  CB  CYS B 394     -86.129  13.893   7.698  1.00 55.25           C  
ATOM   4099  SG  CYS B 394     -84.675  13.629   8.697  1.00 50.88           S  
ATOM   4100  N   SER B 395     -88.275  15.087   5.833  1.00 49.78           N  
ATOM   4101  CA  SER B 395     -89.422  14.968   4.928  1.00 52.98           C  
ATOM   4102  C   SER B 395     -89.179  15.565   3.540  1.00 53.81           C  
ATOM   4103  O   SER B 395     -89.607  14.995   2.541  1.00 60.69           O  
ATOM   4104  CB  SER B 395     -90.690  15.571   5.535  1.00 59.60           C  
ATOM   4105  OG  SER B 395     -91.839  15.328   4.712  1.00 58.00           O  
ATOM   4106  N   LYS B 396     -88.502  16.700   3.457  1.00 49.79           N  
ATOM   4107  CA  LYS B 396     -88.179  17.258   2.152  1.00 49.38           C  
ATOM   4108  C   LYS B 396     -87.547  16.200   1.270  1.00 51.83           C  
ATOM   4109  O   LYS B 396     -87.985  15.966   0.145  1.00 58.05           O  
ATOM   4110  CB  LYS B 396     -87.203  18.407   2.289  1.00 53.78           C  
ATOM   4111  CG  LYS B 396     -87.798  19.661   2.867  1.00 59.70           C  
ATOM   4112  CD  LYS B 396     -88.287  20.631   1.800  1.00 61.84           C  
ATOM   4113  CE  LYS B 396     -88.225  22.073   2.324  1.00 65.94           C  
ATOM   4114  NZ  LYS B 396     -86.823  22.599   2.406  1.00 57.24           N  
ATOM   4115  N   GLU B 397     -86.521  15.553   1.808  1.00 50.98           N  
ATOM   4116  CA  GLU B 397     -85.727  14.608   1.054  1.00 51.39           C  
ATOM   4117  C   GLU B 397     -86.490  13.295   0.889  1.00 53.80           C  
ATOM   4118  O   GLU B 397     -86.692  12.825  -0.242  1.00 49.76           O  
ATOM   4119  CB  GLU B 397     -84.365  14.407   1.737  1.00 53.43           C  
ATOM   4120  CG  GLU B 397     -83.607  15.744   1.952  1.00 59.19           C  
ATOM   4121  CD  GLU B 397     -82.091  15.611   2.150  1.00 59.31           C  
ATOM   4122  OE1 GLU B 397     -81.580  14.485   2.297  1.00 64.42           O  
ATOM   4123  OE2 GLU B 397     -81.397  16.649   2.151  1.00 55.29           O  
ATOM   4124  N   ASP B 398     -86.963  12.744   2.007  1.00 50.58           N  
ATOM   4125  CA  ASP B 398     -87.568  11.410   2.024  1.00 47.05           C  
ATOM   4126  C   ASP B 398     -89.097  11.470   1.859  1.00 47.17           C  
ATOM   4127  O   ASP B 398     -89.860  10.744   2.506  1.00 46.88           O  
ATOM   4128  CB  ASP B 398     -87.125  10.647   3.279  1.00 53.36           C  
ATOM   4129  CG  ASP B 398     -85.596  10.459   3.345  1.00 55.99           C  
ATOM   4130  OD1 ASP B 398     -84.994  10.253   2.276  1.00 59.82           O  
ATOM   4131  OD2 ASP B 398     -84.988  10.514   4.444  1.00 46.97           O  
ATOM   4132  N   GLY B 399     -89.509  12.375   0.978  1.00 50.50           N  
ATOM   4133  CA  GLY B 399     -90.843  12.427   0.361  1.00 57.23           C  
ATOM   4134  C   GLY B 399     -92.132  12.060   1.073  1.00 54.15           C  
ATOM   4135  O   GLY B 399     -93.126  11.768   0.409  1.00 49.53           O  
ATOM   4136  N   GLY B 400     -92.157  12.094   2.400  1.00 52.42           N  
ATOM   4137  CA  GLY B 400     -93.410  11.850   3.102  1.00 52.42           C  
ATOM   4138  C   GLY B 400     -93.389  12.071   4.594  1.00 43.76           C  
ATOM   4139  O   GLY B 400     -92.336  12.178   5.196  1.00 41.36           O  
ATOM   4140  N   GLY B 401     -94.580  12.094   5.176  1.00 42.22           N  
ATOM   4141  CA  GLY B 401     -94.764  12.367   6.593  1.00 45.68           C  
ATOM   4142  C   GLY B 401     -94.515  11.172   7.487  1.00 45.58           C  
ATOM   4143  O   GLY B 401     -95.140  10.119   7.328  1.00 40.94           O  
ATOM   4144  N   TRP B 402     -93.620  11.349   8.458  1.00 43.52           N  
ATOM   4145  CA  TRP B 402     -93.156  10.237   9.256  1.00 40.24           C  
ATOM   4146  C   TRP B 402     -92.486  10.664  10.548  1.00 39.15           C  
ATOM   4147  O   TRP B 402     -92.013  11.782  10.654  1.00 43.95           O  
ATOM   4148  CB  TRP B 402     -92.160   9.435   8.424  1.00 41.25           C  
ATOM   4149  CG  TRP B 402     -91.921   8.112   8.983  1.00 40.35           C  
ATOM   4150  CD1 TRP B 402     -90.758   7.626   9.465  1.00 41.06           C  
ATOM   4151  CD2 TRP B 402     -92.891   7.100   9.181  1.00 35.65           C  
ATOM   4152  NE1 TRP B 402     -90.939   6.366   9.942  1.00 34.52           N  
ATOM   4153  CE2 TRP B 402     -92.247   6.022   9.778  1.00 27.98           C  
ATOM   4154  CE3 TRP B 402     -94.247   7.000   8.900  1.00 41.34           C  
ATOM   4155  CZ2 TRP B 402     -92.898   4.856  10.086  1.00 31.95           C  
ATOM   4156  CZ3 TRP B 402     -94.897   5.840   9.221  1.00 38.67           C  
ATOM   4157  CH2 TRP B 402     -94.224   4.782   9.804  1.00 34.22           C  
ATOM   4158  N   TRP B 403     -92.428   9.749  11.517  1.00 40.45           N  
ATOM   4159  CA  TRP B 403     -91.634   9.928  12.744  1.00 37.34           C  
ATOM   4160  C   TRP B 403     -90.166   9.826  12.429  1.00 38.28           C  
ATOM   4161  O   TRP B 403     -89.488   8.869  12.838  1.00 35.88           O  
ATOM   4162  CB  TRP B 403     -91.978   8.883  13.797  1.00 37.77           C  
ATOM   4163  CG  TRP B 403     -93.340   9.033  14.298  1.00 33.09           C  
ATOM   4164  CD1 TRP B 403     -93.730   9.742  15.370  1.00 37.80           C  
ATOM   4165  CD2 TRP B 403     -94.513   8.492  13.722  1.00 29.62           C  
ATOM   4166  NE1 TRP B 403     -95.085   9.673  15.513  1.00 36.59           N  
ATOM   4167  CE2 TRP B 403     -95.587   8.909  14.501  1.00 31.10           C  
ATOM   4168  CE3 TRP B 403     -94.762   7.696  12.609  1.00 36.42           C  
ATOM   4169  CZ2 TRP B 403     -96.885   8.554  14.215  1.00 37.75           C  
ATOM   4170  CZ3 TRP B 403     -96.049   7.346  12.322  1.00 33.07           C  
ATOM   4171  CH2 TRP B 403     -97.097   7.772  13.119  1.00 33.83           C  
ATOM   4172  N   TYR B 404     -89.681  10.828  11.697  1.00 47.80           N  
ATOM   4173  CA  TYR B 404     -88.289  10.862  11.256  1.00 51.06           C  
ATOM   4174  C   TYR B 404     -87.334  11.311  12.383  1.00 50.01           C  
ATOM   4175  O   TYR B 404     -87.732  12.030  13.323  1.00 44.56           O  
ATOM   4176  CB  TYR B 404     -88.123  11.811  10.054  1.00 53.28           C  
ATOM   4177  CG  TYR B 404     -88.708  11.392   8.690  1.00 47.47           C  
ATOM   4178  CD1 TYR B 404     -88.514  10.127   8.162  1.00 43.64           C  
ATOM   4179  CD2 TYR B 404     -89.374  12.322   7.895  1.00 45.51           C  
ATOM   4180  CE1 TYR B 404     -89.020   9.786   6.903  1.00 42.83           C  
ATOM   4181  CE2 TYR B 404     -89.867  11.995   6.658  1.00 44.13           C  
ATOM   4182  CZ  TYR B 404     -89.696  10.727   6.154  1.00 40.66           C  
ATOM   4183  OH  TYR B 404     -90.206  10.409   4.905  1.00 37.01           O  
ATOM   4184  N   ASN B 405     -86.063  10.923  12.221  1.00 54.41           N  
ATOM   4185  CA  ASN B 405     -84.992  11.131  13.209  1.00 48.98           C  
ATOM   4186  C   ASN B 405     -83.603  11.227  12.600  1.00 42.02           C  
ATOM   4187  O   ASN B 405     -82.654  10.677  13.148  1.00 53.09           O  
ATOM   4188  CB  ASN B 405     -84.983   9.945  14.179  1.00 52.71           C  
ATOM   4189  CG  ASN B 405     -83.915  10.061  15.277  1.00 51.74           C  
ATOM   4190  OD1 ASN B 405     -83.493  11.159  15.648  1.00 55.46           O  
ATOM   4191  ND2 ASN B 405     -83.483   8.919  15.799  1.00 48.39           N  
ATOM   4192  N   ARG B 406     -83.442  11.906  11.481  1.00 41.87           N  
ATOM   4193  CA  ARG B 406     -82.098  11.975  10.852  1.00 52.39           C  
ATOM   4194  C   ARG B 406     -81.541  10.679  10.175  1.00 48.88           C  
ATOM   4195  O   ARG B 406     -80.367  10.361  10.379  1.00 45.40           O  
ATOM   4196  CB  ARG B 406     -81.071  12.447  11.907  1.00 49.84           C  
ATOM   4197  CG  ARG B 406     -79.809  13.106  11.353  1.00 50.39           C  
ATOM   4198  CD  ARG B 406     -78.612  12.706  12.174  1.00 53.85           C  
ATOM   4199  NE  ARG B 406     -77.363  13.315  11.732  1.00 52.22           N  
ATOM   4200  CZ  ARG B 406     -76.994  14.559  12.015  1.00 50.28           C  
ATOM   4201  NH1 ARG B 406     -75.843  15.025  11.553  1.00 42.49           N  
ATOM   4202  NH2 ARG B 406     -77.763  15.336  12.768  1.00 56.24           N  
ATOM   4203  N   CYS B 407     -82.323   9.935   9.379  1.00 45.79           N  
ATOM   4204  CA  CYS B 407     -83.737  10.193   9.117  1.00 41.40           C  
ATOM   4205  C   CYS B 407     -84.601   8.967   9.310  1.00 34.70           C  
ATOM   4206  O   CYS B 407     -85.605   9.060  10.005  1.00 42.29           O  
ATOM   4207  CB  CYS B 407     -83.968  10.770   7.721  1.00 47.59           C  
ATOM   4208  SG  CYS B 407     -83.440  12.506   7.520  1.00 54.70           S  
ATOM   4209  N   HIS B 408     -84.256   7.834   8.694  1.00 38.59           N  
ATOM   4210  CA  HIS B 408     -85.057   6.601   8.891  1.00 38.34           C  
ATOM   4211  C   HIS B 408     -84.360   5.265   8.769  1.00 36.41           C  
ATOM   4212  O   HIS B 408     -83.302   5.141   8.157  1.00 38.48           O  
ATOM   4213  CB  HIS B 408     -86.258   6.563   7.948  1.00 38.49           C  
ATOM   4214  CG  HIS B 408     -85.907   6.463   6.502  1.00 36.55           C  
ATOM   4215  ND1 HIS B 408     -85.385   7.521   5.791  1.00 43.80           N  
ATOM   4216  CD2 HIS B 408     -86.039   5.446   5.621  1.00 41.58           C  
ATOM   4217  CE1 HIS B 408     -85.191   7.153   4.538  1.00 46.28           C  
ATOM   4218  NE2 HIS B 408     -85.591   5.901   4.404  1.00 43.65           N  
ATOM   4219  N   ALA B 409     -84.966   4.269   9.403  1.00 38.47           N  
ATOM   4220  CA  ALA B 409     -84.788   2.890   8.992  1.00 43.61           C  
ATOM   4221  C   ALA B 409     -85.967   2.654   8.084  1.00 42.86           C  
ATOM   4222  O   ALA B 409     -85.804   2.414   6.891  1.00 45.82           O  
ATOM   4223  CB  ALA B 409     -84.823   1.942  10.168  1.00 44.73           C  
ATOM   4224  N   ALA B 410     -87.162   2.780   8.642  1.00 35.41           N  
ATOM   4225  CA  ALA B 410     -88.361   2.567   7.870  1.00 36.01           C  
ATOM   4226  C   ALA B 410     -88.912   3.893   7.407  1.00 46.80           C  
ATOM   4227  O   ALA B 410     -88.851   4.895   8.125  1.00 46.94           O  
ATOM   4228  CB  ALA B 410     -89.383   1.850   8.672  1.00 39.12           C  
ATOM   4229  N   ASN B 411     -89.456   3.876   6.194  1.00 48.89           N  
ATOM   4230  CA  ASN B 411     -90.136   5.013   5.602  1.00 42.55           C  
ATOM   4231  C   ASN B 411     -91.213   4.433   4.685  1.00 44.85           C  
ATOM   4232  O   ASN B 411     -90.953   4.175   3.508  1.00 49.89           O  
ATOM   4233  CB  ASN B 411     -89.139   5.881   4.844  1.00 34.05           C  
ATOM   4234  CG  ASN B 411     -89.793   7.015   4.116  1.00 37.10           C  
ATOM   4235  OD1 ASN B 411     -90.799   7.567   4.573  1.00 40.93           O  
ATOM   4236  ND2 ASN B 411     -89.244   7.366   2.962  1.00 34.36           N  
ATOM   4237  N   PRO B 412     -92.395   4.138   5.249  1.00 41.59           N  
ATOM   4238  CA  PRO B 412     -93.546   3.638   4.493  1.00 44.77           C  
ATOM   4239  C   PRO B 412     -94.406   4.710   3.857  1.00 51.43           C  
ATOM   4240  O   PRO B 412     -95.388   4.371   3.207  1.00 48.82           O  
ATOM   4241  CB  PRO B 412     -94.395   2.915   5.548  1.00 38.88           C  
ATOM   4242  CG  PRO B 412     -93.566   2.842   6.749  1.00 43.11           C  
ATOM   4243  CD  PRO B 412     -92.593   3.953   6.693  1.00 42.16           C  
ATOM   4244  N   ASN B 413     -94.095   5.985   4.062  1.00 53.81           N  
ATOM   4245  CA  ASN B 413     -94.828   7.021   3.347  1.00 51.60           C  
ATOM   4246  C   ASN B 413     -93.960   7.610   2.235  1.00 55.87           C  
ATOM   4247  O   ASN B 413     -94.318   8.565   1.516  1.00 47.30           O  
ATOM   4248  CB  ASN B 413     -95.366   8.021   4.335  1.00 43.93           C  
ATOM   4249  CG  ASN B 413     -96.362   7.393   5.262  1.00 39.80           C  
ATOM   4250  OD1 ASN B 413     -97.177   6.570   4.859  1.00 33.34           O  
ATOM   4251  ND2 ASN B 413     -96.289   7.756   6.517  1.00 47.72           N  
ATOM   4252  N   GLY B 414     -92.821   6.961   2.061  1.00 57.22           N  
ATOM   4253  CA  GLY B 414     -91.992   7.185   0.905  1.00 65.36           C  
ATOM   4254  C   GLY B 414     -92.683   6.915  -0.417  1.00 57.18           C  
ATOM   4255  O   GLY B 414     -93.741   6.294  -0.472  1.00 46.76           O  
ATOM   4256  N   ARG B 415     -92.014   7.369  -1.471  1.00 60.96           N  
ATOM   4257  CA  ARG B 415     -92.528   7.417  -2.833  1.00 58.73           C  
ATOM   4258  C   ARG B 415     -92.686   6.019  -3.421  1.00 56.64           C  
ATOM   4259  O   ARG B 415     -91.974   5.091  -3.017  1.00 47.57           O  
ATOM   4260  CB  ARG B 415     -91.550   8.218  -3.698  1.00 59.70           C  
ATOM   4261  CG  ARG B 415     -91.190   9.609  -3.148  1.00 60.41           C  
ATOM   4262  CD  ARG B 415     -91.732  10.724  -4.016  1.00 59.37           C  
ATOM   4263  NE  ARG B 415     -90.855  10.973  -5.162  1.00 56.15           N  
ATOM   4264  CZ  ARG B 415     -91.264  11.349  -6.374  1.00 55.70           C  
ATOM   4265  NH1 ARG B 415     -92.557  11.511  -6.647  1.00 58.31           N  
ATOM   4266  NH2 ARG B 415     -90.369  11.544  -7.334  1.00 52.90           N  
ATOM   4267  N   TYR B 416     -93.602   5.870  -4.382  1.00 53.01           N  
ATOM   4268  CA  TYR B 416     -93.912   4.548  -4.918  1.00 53.73           C  
ATOM   4269  C   TYR B 416     -93.123   4.222  -6.182  1.00 56.40           C  
ATOM   4270  O   TYR B 416     -93.581   4.486  -7.293  1.00 63.43           O  
ATOM   4271  CB  TYR B 416     -95.412   4.400  -5.169  1.00 50.84           C  
ATOM   4272  CG  TYR B 416     -95.875   2.960  -5.162  1.00 46.18           C  
ATOM   4273  CD1 TYR B 416     -96.323   2.337  -6.319  1.00 45.82           C  
ATOM   4274  CD2 TYR B 416     -95.843   2.215  -3.990  1.00 45.54           C  
ATOM   4275  CE1 TYR B 416     -96.739   0.998  -6.299  1.00 46.15           C  
ATOM   4276  CE2 TYR B 416     -96.251   0.895  -3.964  1.00 45.36           C  
ATOM   4277  CZ  TYR B 416     -96.698   0.295  -5.114  1.00 42.07           C  
ATOM   4278  OH  TYR B 416     -97.109  -1.001  -5.067  1.00 41.77           O  
ATOM   4279  N   TYR B 417     -91.945   3.627  -6.002  1.00 53.86           N  
ATOM   4280  CA  TYR B 417     -91.099   3.241  -7.129  1.00 52.20           C  
ATOM   4281  C   TYR B 417     -91.578   1.920  -7.714  1.00 52.39           C  
ATOM   4282  O   TYR B 417     -91.549   0.866  -7.061  1.00 44.59           O  
ATOM   4283  CB  TYR B 417     -89.616   3.172  -6.739  1.00 50.99           C  
ATOM   4284  CG  TYR B 417     -88.971   4.541  -6.490  1.00 53.19           C  
ATOM   4285  CD1 TYR B 417     -88.780   5.452  -7.525  1.00 47.51           C  
ATOM   4286  CD2 TYR B 417     -88.549   4.918  -5.220  1.00 51.90           C  
ATOM   4287  CE1 TYR B 417     -88.201   6.689  -7.298  1.00 38.36           C  
ATOM   4288  CE2 TYR B 417     -87.966   6.155  -4.997  1.00 43.62           C  
ATOM   4289  CZ  TYR B 417     -87.793   7.030  -6.030  1.00 38.71           C  
ATOM   4290  OH  TYR B 417     -87.217   8.261  -5.771  1.00 44.69           O  
ATOM   4291  N   TRP B 418     -92.034   2.008  -8.959  1.00 56.33           N  
ATOM   4292  CA  TRP B 418     -92.602   0.871  -9.641  1.00 54.10           C  
ATOM   4293  C   TRP B 418     -91.535  -0.147  -9.943  1.00 52.37           C  
ATOM   4294  O   TRP B 418     -90.410   0.215 -10.295  1.00 45.89           O  
ATOM   4295  CB  TRP B 418     -93.279   1.284 -10.943  1.00 57.63           C  
ATOM   4296  CG  TRP B 418     -94.132   0.176 -11.470  1.00 62.05           C  
ATOM   4297  CD1 TRP B 418     -93.746  -0.827 -12.305  1.00 64.44           C  
ATOM   4298  CD2 TRP B 418     -95.506  -0.081 -11.142  1.00 58.77           C  
ATOM   4299  NE1 TRP B 418     -94.798  -1.676 -12.536  1.00 68.40           N  
ATOM   4300  CE2 TRP B 418     -95.890  -1.239 -11.832  1.00 58.56           C  
ATOM   4301  CE3 TRP B 418     -96.447   0.562 -10.334  1.00 61.41           C  
ATOM   4302  CZ2 TRP B 418     -97.176  -1.764 -11.749  1.00 60.40           C  
ATOM   4303  CZ3 TRP B 418     -97.730   0.037 -10.251  1.00 62.69           C  
ATOM   4304  CH2 TRP B 418     -98.081  -1.111 -10.955  1.00 61.50           C  
ATOM   4305  N   GLY B 419     -91.905  -1.420  -9.813  1.00 53.38           N  
ATOM   4306  CA  GLY B 419     -90.953  -2.508  -9.915  1.00 58.40           C  
ATOM   4307  C   GLY B 419     -89.975  -2.507  -8.756  1.00 60.53           C  
ATOM   4308  O   GLY B 419     -89.065  -3.330  -8.711  1.00 64.23           O  
ATOM   4309  N   GLY B 420     -90.144  -1.564  -7.834  1.00 58.95           N  
ATOM   4310  CA  GLY B 420     -89.407  -1.554  -6.584  1.00 61.59           C  
ATOM   4311  C   GLY B 420     -87.938  -1.193  -6.576  1.00 55.22           C  
ATOM   4312  O   GLY B 420     -87.486  -0.515  -5.665  1.00 57.96           O  
ATOM   4313  N   GLN B 421     -87.168  -1.673  -7.535  1.00 51.69           N  
ATOM   4314  CA  GLN B 421     -85.730  -1.459  -7.475  1.00 53.97           C  
ATOM   4315  C   GLN B 421     -85.510  -0.015  -7.836  1.00 48.71           C  
ATOM   4316  O   GLN B 421     -86.146   0.461  -8.774  1.00 48.20           O  
ATOM   4317  CB  GLN B 421     -85.000  -2.367  -8.467  1.00 62.92           C  
ATOM   4318  CG  GLN B 421     -84.629  -3.734  -7.925  1.00 62.67           C  
ATOM   4319  CD  GLN B 421     -83.383  -3.714  -7.041  1.00 70.91           C  
ATOM   4320  OE1 GLN B 421     -83.056  -4.720  -6.412  1.00 78.08           O  
ATOM   4321  NE2 GLN B 421     -82.677  -2.579  -6.997  1.00 66.94           N  
ATOM   4322  N   TYR B 422     -84.651   0.687  -7.095  1.00 39.47           N  
ATOM   4323  CA  TYR B 422     -84.309   2.062  -7.454  1.00 40.11           C  
ATOM   4324  C   TYR B 422     -82.937   2.490  -6.990  1.00 50.68           C  
ATOM   4325  O   TYR B 422     -82.314   1.831  -6.166  1.00 56.72           O  
ATOM   4326  CB  TYR B 422     -85.363   3.054  -6.965  1.00 43.83           C  
ATOM   4327  CG  TYR B 422     -85.425   3.296  -5.466  1.00 46.17           C  
ATOM   4328  CD1 TYR B 422     -85.756   2.272  -4.579  1.00 46.49           C  
ATOM   4329  CD2 TYR B 422     -85.204   4.562  -4.939  1.00 43.24           C  
ATOM   4330  CE1 TYR B 422     -85.835   2.502  -3.217  1.00 41.36           C  
ATOM   4331  CE2 TYR B 422     -85.281   4.793  -3.578  1.00 38.62           C  
ATOM   4332  CZ  TYR B 422     -85.592   3.761  -2.725  1.00 40.37           C  
ATOM   4333  OH  TYR B 422     -85.670   3.990  -1.372  1.00 49.06           O  
ATOM   4334  N   THR B 423     -82.480   3.611  -7.547  1.00 58.24           N  
ATOM   4335  CA  THR B 423     -81.101   4.083  -7.401  1.00 54.43           C  
ATOM   4336  C   THR B 423     -81.104   5.563  -7.046  1.00 47.65           C  
ATOM   4337  O   THR B 423     -82.129   6.222  -7.147  1.00 48.20           O  
ATOM   4338  CB  THR B 423     -80.349   3.932  -8.715  1.00 52.68           C  
ATOM   4339  OG1 THR B 423     -80.931   4.820  -9.677  1.00 53.20           O  
ATOM   4340  CG2 THR B 423     -80.417   2.481  -9.233  1.00 46.01           C  
ATOM   4341  N   TRP B 424     -79.960   6.087  -6.636  1.00 41.18           N  
ATOM   4342  CA  TRP B 424     -79.896   7.474  -6.210  1.00 44.75           C  
ATOM   4343  C   TRP B 424     -80.246   8.446  -7.333  1.00 48.35           C  
ATOM   4344  O   TRP B 424     -80.912   9.460  -7.090  1.00 46.70           O  
ATOM   4345  CB  TRP B 424     -78.515   7.800  -5.646  1.00 53.55           C  
ATOM   4346  CG  TRP B 424     -77.487   8.007  -6.689  1.00 59.92           C  
ATOM   4347  CD1 TRP B 424     -76.753   7.049  -7.324  1.00 59.92           C  
ATOM   4348  CD2 TRP B 424     -77.078   9.262  -7.241  1.00 66.63           C  
ATOM   4349  NE1 TRP B 424     -75.908   7.632  -8.242  1.00 62.07           N  
ATOM   4350  CE2 TRP B 424     -76.083   8.990  -8.207  1.00 59.12           C  
ATOM   4351  CE3 TRP B 424     -77.460  10.592  -7.015  1.00 69.48           C  
ATOM   4352  CZ2 TRP B 424     -75.464   9.996  -8.945  1.00 56.46           C  
ATOM   4353  CZ3 TRP B 424     -76.838  11.598  -7.753  1.00 68.90           C  
ATOM   4354  CH2 TRP B 424     -75.850  11.290  -8.705  1.00 61.85           C  
ATOM   4355  N   ASP B 425     -79.822   8.130  -8.560  1.00 54.62           N  
ATOM   4356  CA  ASP B 425     -79.992   9.049  -9.705  1.00 55.99           C  
ATOM   4357  C   ASP B 425     -81.355   8.923 -10.393  1.00 52.52           C  
ATOM   4358  O   ASP B 425     -81.457   8.817 -11.610  1.00 55.66           O  
ATOM   4359  CB  ASP B 425     -78.827   8.948 -10.720  1.00 60.49           C  
ATOM   4360  CG  ASP B 425     -78.529   7.524 -11.164  1.00 63.53           C  
ATOM   4361  OD1 ASP B 425     -78.532   6.617 -10.307  1.00 62.40           O  
ATOM   4362  OD2 ASP B 425     -78.253   7.319 -12.371  1.00 61.20           O  
ATOM   4363  N   MET B 426     -82.394   8.931  -9.571  1.00 50.90           N  
ATOM   4364  CA  MET B 426     -83.785   8.995  -9.999  1.00 46.27           C  
ATOM   4365  C   MET B 426     -84.594   9.580  -8.841  1.00 46.48           C  
ATOM   4366  O   MET B 426     -85.685  10.114  -9.047  1.00 44.44           O  
ATOM   4367  CB  MET B 426     -84.349   7.616 -10.361  1.00 48.46           C  
ATOM   4368  CG  MET B 426     -83.365   6.463 -10.280  1.00 53.06           C  
ATOM   4369  SD  MET B 426     -84.145   4.843 -10.409  1.00 51.86           S  
ATOM   4370  CE  MET B 426     -83.723   4.430 -12.101  1.00 53.24           C  
ATOM   4371  N   ALA B 427     -84.074   9.457  -7.619  1.00 47.05           N  
ATOM   4372  CA  ALA B 427     -84.635  10.163  -6.475  1.00 54.02           C  
ATOM   4373  C   ALA B 427     -84.378  11.664  -6.579  1.00 50.23           C  
ATOM   4374  O   ALA B 427     -83.314  12.102  -7.010  1.00 48.39           O  
ATOM   4375  CB  ALA B 427     -84.062   9.622  -5.184  1.00 59.37           C  
ATOM   4376  N   LYS B 428     -85.365  12.431  -6.143  1.00 47.08           N  
ATOM   4377  CA  LYS B 428     -85.442  13.864  -6.385  1.00 53.80           C  
ATOM   4378  C   LYS B 428     -84.394  14.656  -5.596  1.00 56.45           C  
ATOM   4379  O   LYS B 428     -83.896  15.681  -6.069  1.00 58.57           O  
ATOM   4380  CB  LYS B 428     -86.860  14.328  -6.022  1.00 59.51           C  
ATOM   4381  CG  LYS B 428     -87.230  15.758  -6.366  1.00 62.56           C  
ATOM   4382  CD  LYS B 428     -88.680  16.050  -5.966  1.00 62.85           C  
ATOM   4383  CE  LYS B 428     -89.694  15.341  -6.881  1.00 64.70           C  
ATOM   4384  NZ  LYS B 428     -91.129  15.415  -6.408  1.00 56.91           N  
ATOM   4385  N   HIS B 429     -84.077  14.189  -4.390  1.00 55.60           N  
ATOM   4386  CA  HIS B 429     -83.008  14.775  -3.584  1.00 51.53           C  
ATOM   4387  C   HIS B 429     -81.916  13.715  -3.324  1.00 55.13           C  
ATOM   4388  O   HIS B 429     -81.117  13.828  -2.393  1.00 51.88           O  
ATOM   4389  CB  HIS B 429     -83.589  15.344  -2.293  1.00 50.93           C  
ATOM   4390  CG  HIS B 429     -84.810  16.188  -2.505  1.00 57.16           C  
ATOM   4391  ND1 HIS B 429     -84.743  17.504  -2.904  1.00 62.43           N  
ATOM   4392  CD2 HIS B 429     -86.130  15.900  -2.387  1.00 62.08           C  
ATOM   4393  CE1 HIS B 429     -85.967  17.991  -3.022  1.00 64.06           C  
ATOM   4394  NE2 HIS B 429     -86.827  17.038  -2.713  1.00 61.70           N  
ATOM   4395  N   GLY B 430     -81.896  12.686  -4.172  1.00 53.50           N  
ATOM   4396  CA  GLY B 430     -80.858  11.663  -4.165  1.00 46.52           C  
ATOM   4397  C   GLY B 430     -80.811  10.735  -2.972  1.00 41.79           C  
ATOM   4398  O   GLY B 430     -79.862   9.999  -2.799  1.00 51.11           O  
ATOM   4399  N   THR B 431     -81.849  10.729  -2.166  1.00 51.03           N  
ATOM   4400  CA  THR B 431     -81.825  10.002  -0.913  1.00 54.37           C  
ATOM   4401  C   THR B 431     -82.594   8.710  -1.111  1.00 52.22           C  
ATOM   4402  O   THR B 431     -82.821   8.335  -2.248  1.00 55.22           O  
ATOM   4403  CB  THR B 431     -82.486  10.866   0.084  1.00 57.52           C  
ATOM   4404  OG1 THR B 431     -83.738  11.282  -0.476  1.00 56.42           O  
ATOM   4405  CG2 THR B 431     -81.604  12.100   0.328  1.00 53.28           C  
ATOM   4406  N   ASP B 432     -82.989   8.029  -0.036  1.00 48.90           N  
ATOM   4407  CA  ASP B 432     -83.814   6.810  -0.157  1.00 45.56           C  
ATOM   4408  C   ASP B 432     -85.268   7.031   0.280  1.00 44.04           C  
ATOM   4409  O   ASP B 432     -85.783   6.332   1.172  1.00 35.22           O  
ATOM   4410  CB  ASP B 432     -83.188   5.625   0.587  1.00 46.88           C  
ATOM   4411  CG  ASP B 432     -82.726   5.983   1.998  1.00 58.41           C  
ATOM   4412  OD1 ASP B 432     -82.386   5.055   2.767  1.00 55.30           O  
ATOM   4413  OD2 ASP B 432     -82.686   7.190   2.341  1.00 63.71           O  
ATOM   4414  N   ASP B 433     -85.904   8.021  -0.354  1.00 41.60           N  
ATOM   4415  CA  ASP B 433     -87.357   8.157  -0.349  1.00 46.61           C  
ATOM   4416  C   ASP B 433     -87.920   6.887  -0.945  1.00 43.13           C  
ATOM   4417  O   ASP B 433     -87.275   6.287  -1.784  1.00 46.95           O  
ATOM   4418  CB  ASP B 433     -87.816   9.374  -1.172  1.00 52.76           C  
ATOM   4419  CG  ASP B 433     -87.221   9.407  -2.569  1.00 49.52           C  
ATOM   4420  OD1 ASP B 433     -87.704  10.182  -3.428  1.00 46.37           O  
ATOM   4421  OD2 ASP B 433     -86.259   8.657  -2.808  1.00 51.74           O  
ATOM   4422  N   GLY B 434     -89.085   6.442  -0.498  1.00 38.17           N  
ATOM   4423  CA  GLY B 434     -89.607   5.141  -0.963  1.00 43.85           C  
ATOM   4424  C   GLY B 434     -90.013   4.090   0.071  1.00 36.91           C  
ATOM   4425  O   GLY B 434     -89.491   4.025   1.177  1.00 33.53           O  
ATOM   4426  N   VAL B 435     -90.958   3.247  -0.309  1.00 37.75           N  
ATOM   4427  CA  VAL B 435     -91.515   2.299   0.628  1.00 41.62           C  
ATOM   4428  C   VAL B 435     -90.426   1.326   1.113  1.00 49.15           C  
ATOM   4429  O   VAL B 435     -90.372   0.148   0.706  1.00 43.82           O  
ATOM   4430  CB  VAL B 435     -92.704   1.500   0.030  1.00 44.50           C  
ATOM   4431  CG1 VAL B 435     -93.539   0.904   1.151  1.00 39.23           C  
ATOM   4432  CG2 VAL B 435     -93.568   2.364  -0.855  1.00 45.41           C  
ATOM   4433  N   VAL B 436     -89.568   1.817   2.006  1.00 49.84           N  
ATOM   4434  CA  VAL B 436     -88.448   1.020   2.512  1.00 49.85           C  
ATOM   4435  C   VAL B 436     -88.632   0.529   3.928  1.00 44.02           C  
ATOM   4436  O   VAL B 436     -88.880   1.299   4.845  1.00 43.64           O  
ATOM   4437  CB  VAL B 436     -87.160   1.832   2.531  1.00 51.20           C  
ATOM   4438  CG1 VAL B 436     -86.113   1.096   3.306  1.00 58.17           C  
ATOM   4439  CG2 VAL B 436     -86.689   2.129   1.110  1.00 52.13           C  
ATOM   4440  N   TRP B 437     -88.500  -0.773   4.095  1.00 52.86           N  
ATOM   4441  CA  TRP B 437     -88.116  -1.336   5.377  1.00 53.69           C  
ATOM   4442  C   TRP B 437     -86.631  -1.573   5.230  1.00 42.56           C  
ATOM   4443  O   TRP B 437     -86.193  -2.354   4.386  1.00 42.18           O  
ATOM   4444  CB  TRP B 437     -88.849  -2.643   5.679  1.00 54.16           C  
ATOM   4445  CG  TRP B 437     -89.015  -2.908   7.155  1.00 54.83           C  
ATOM   4446  CD1 TRP B 437     -88.375  -3.852   7.903  1.00 59.85           C  
ATOM   4447  CD2 TRP B 437     -89.867  -2.205   8.051  1.00 41.70           C  
ATOM   4448  NE1 TRP B 437     -88.791  -3.784   9.207  1.00 49.41           N  
ATOM   4449  CE2 TRP B 437     -89.708  -2.779   9.318  1.00 38.58           C  
ATOM   4450  CE3 TRP B 437     -90.746  -1.139   7.902  1.00 51.31           C  
ATOM   4451  CZ2 TRP B 437     -90.396  -2.333  10.421  1.00 46.16           C  
ATOM   4452  CZ3 TRP B 437     -91.437  -0.692   9.006  1.00 55.02           C  
ATOM   4453  CH2 TRP B 437     -91.256  -1.287  10.249  1.00 51.98           C  
ATOM   4454  N   MET B 438     -85.857  -0.860   6.025  1.00 41.44           N  
ATOM   4455  CA  MET B 438     -84.419  -0.877   5.871  1.00 44.01           C  
ATOM   4456  C   MET B 438     -83.920  -2.262   6.145  1.00 35.79           C  
ATOM   4457  O   MET B 438     -83.189  -2.829   5.365  1.00 33.55           O  
ATOM   4458  CB  MET B 438     -83.797   0.063   6.881  1.00 47.21           C  
ATOM   4459  CG  MET B 438     -82.495   0.577   6.448  1.00 48.08           C  
ATOM   4460  SD  MET B 438     -82.624   2.243   5.821  1.00 44.46           S  
ATOM   4461  CE  MET B 438     -80.826   2.540   5.802  1.00 38.59           C  
ATOM   4462  N   ASN B 439     -84.395  -2.782   7.271  1.00 41.92           N  
ATOM   4463  CA  ASN B 439     -84.011  -4.055   7.841  1.00 39.72           C  
ATOM   4464  C   ASN B 439     -84.275  -5.245   6.972  1.00 37.68           C  
ATOM   4465  O   ASN B 439     -83.819  -6.341   7.290  1.00 42.92           O  
ATOM   4466  CB  ASN B 439     -84.808  -4.290   9.121  1.00 52.63           C  
ATOM   4467  CG  ASN B 439     -84.235  -3.570  10.305  1.00 57.75           C  
ATOM   4468  OD1 ASN B 439     -83.740  -4.205  11.237  1.00 62.26           O  
ATOM   4469  ND2 ASN B 439     -84.302  -2.243  10.292  1.00 59.20           N  
ATOM   4470  N   TRP B 440     -85.052  -5.055   5.918  1.00 38.24           N  
ATOM   4471  CA  TRP B 440     -85.383  -6.134   5.031  1.00 37.20           C  
ATOM   4472  C   TRP B 440     -84.672  -5.991   3.690  1.00 43.27           C  
ATOM   4473  O   TRP B 440     -83.893  -6.836   3.324  1.00 53.28           O  
ATOM   4474  CB  TRP B 440     -86.878  -6.160   4.851  1.00 43.96           C  
ATOM   4475  CG  TRP B 440     -87.388  -7.401   4.245  1.00 52.96           C  
ATOM   4476  CD1 TRP B 440     -86.953  -8.660   4.480  1.00 59.81           C  
ATOM   4477  CD2 TRP B 440     -88.485  -7.519   3.340  1.00 53.66           C  
ATOM   4478  NE1 TRP B 440     -87.695  -9.560   3.764  1.00 56.84           N  
ATOM   4479  CE2 TRP B 440     -88.643  -8.880   3.054  1.00 53.69           C  
ATOM   4480  CE3 TRP B 440     -89.346  -6.603   2.740  1.00 55.68           C  
ATOM   4481  CZ2 TRP B 440     -89.617  -9.350   2.187  1.00 57.26           C  
ATOM   4482  CZ3 TRP B 440     -90.312  -7.073   1.883  1.00 59.28           C  
ATOM   4483  CH2 TRP B 440     -90.438  -8.433   1.609  1.00 57.15           C  
ATOM   4484  N   LYS B 441     -84.901  -4.903   2.973  1.00 51.81           N  
ATOM   4485  CA  LYS B 441     -84.390  -4.758   1.611  1.00 49.23           C  
ATOM   4486  C   LYS B 441     -83.287  -3.742   1.496  1.00 46.03           C  
ATOM   4487  O   LYS B 441     -82.761  -3.514   0.415  1.00 48.96           O  
ATOM   4488  CB  LYS B 441     -85.518  -4.295   0.700  1.00 60.28           C  
ATOM   4489  CG  LYS B 441     -86.607  -5.326   0.494  1.00 66.10           C  
ATOM   4490  CD  LYS B 441     -86.171  -6.388  -0.503  1.00 65.57           C  
ATOM   4491  CE  LYS B 441     -87.353  -7.207  -0.985  1.00 70.03           C  
ATOM   4492  NZ  LYS B 441     -87.035  -7.951  -2.236  1.00 68.00           N  
ATOM   4493  N   GLY B 442     -82.954  -3.088   2.593  1.00 50.25           N  
ATOM   4494  CA  GLY B 442     -82.027  -1.973   2.522  1.00 55.02           C  
ATOM   4495  C   GLY B 442     -82.693  -0.744   1.941  1.00 55.39           C  
ATOM   4496  O   GLY B 442     -83.878  -0.739   1.613  1.00 54.51           O  
ATOM   4497  N   SER B 443     -81.907   0.303   1.791  1.00 55.63           N  
ATOM   4498  CA  SER B 443     -82.444   1.593   1.431  1.00 55.21           C  
ATOM   4499  C   SER B 443     -83.029   1.662   0.037  1.00 52.77           C  
ATOM   4500  O   SER B 443     -83.858   2.511  -0.237  1.00 55.55           O  
ATOM   4501  CB  SER B 443     -81.342   2.638   1.547  1.00 58.83           C  
ATOM   4502  OG  SER B 443     -81.083   2.909   2.906  1.00 58.60           O  
ATOM   4503  N   TRP B 444     -82.597   0.785  -0.851  1.00 53.86           N  
ATOM   4504  CA  TRP B 444     -82.846   1.000  -2.263  1.00 52.86           C  
ATOM   4505  C   TRP B 444     -83.821   0.017  -2.864  1.00 48.25           C  
ATOM   4506  O   TRP B 444     -83.670  -0.429  -3.999  1.00 52.01           O  
ATOM   4507  CB  TRP B 444     -81.523   0.974  -2.997  1.00 56.07           C  
ATOM   4508  CG  TRP B 444     -80.658   2.074  -2.565  1.00 51.72           C  
ATOM   4509  CD1 TRP B 444     -79.590   1.984  -1.756  1.00 50.00           C  
ATOM   4510  CD2 TRP B 444     -80.807   3.452  -2.887  1.00 51.48           C  
ATOM   4511  NE1 TRP B 444     -79.032   3.217  -1.568  1.00 48.22           N  
ATOM   4512  CE2 TRP B 444     -79.758   4.139  -2.262  1.00 42.66           C  
ATOM   4513  CE3 TRP B 444     -81.720   4.171  -3.654  1.00 52.72           C  
ATOM   4514  CZ2 TRP B 444     -79.591   5.505  -2.367  1.00 42.22           C  
ATOM   4515  CZ3 TRP B 444     -81.549   5.537  -3.764  1.00 55.65           C  
ATOM   4516  CH2 TRP B 444     -80.495   6.190  -3.115  1.00 48.57           C  
ATOM   4517  N   TYR B 445     -84.849  -0.305  -2.107  1.00 47.20           N  
ATOM   4518  CA  TYR B 445     -85.911  -1.108  -2.649  1.00 44.99           C  
ATOM   4519  C   TYR B 445     -87.213  -0.724  -1.986  1.00 39.42           C  
ATOM   4520  O   TYR B 445     -87.308  -0.661  -0.744  1.00 35.24           O  
ATOM   4521  CB  TYR B 445     -85.611  -2.581  -2.468  1.00 40.95           C  
ATOM   4522  CG  TYR B 445     -86.568  -3.450  -3.212  1.00 41.74           C  
ATOM   4523  CD1 TYR B 445     -87.743  -3.882  -2.618  1.00 44.54           C  
ATOM   4524  CD2 TYR B 445     -86.317  -3.821  -4.519  1.00 46.89           C  
ATOM   4525  CE1 TYR B 445     -88.622  -4.680  -3.293  1.00 45.82           C  
ATOM   4526  CE2 TYR B 445     -87.198  -4.628  -5.213  1.00 44.96           C  
ATOM   4527  CZ  TYR B 445     -88.341  -5.054  -4.593  1.00 47.19           C  
ATOM   4528  OH  TYR B 445     -89.213  -5.859  -5.273  1.00 53.63           O  
ATOM   4529  N   SER B 446     -88.201  -0.470  -2.840  1.00 39.96           N  
ATOM   4530  CA  SER B 446     -89.476   0.084  -2.439  1.00 41.58           C  
ATOM   4531  C   SER B 446     -90.526  -0.989  -2.576  1.00 35.36           C  
ATOM   4532  O   SER B 446     -90.737  -1.494  -3.661  1.00 40.60           O  
ATOM   4533  CB  SER B 446     -89.816   1.282  -3.325  1.00 43.48           C  
ATOM   4534  OG  SER B 446     -91.174   1.659  -3.168  1.00 53.93           O  
ATOM   4535  N   MET B 447     -91.184  -1.340  -1.480  1.00 40.00           N  
ATOM   4536  CA  MET B 447     -92.169  -2.432  -1.500  1.00 48.29           C  
ATOM   4537  C   MET B 447     -93.278  -2.209  -2.506  1.00 48.12           C  
ATOM   4538  O   MET B 447     -93.522  -1.078  -2.950  1.00 43.77           O  
ATOM   4539  CB  MET B 447     -92.847  -2.623  -0.143  1.00 47.80           C  
ATOM   4540  CG  MET B 447     -91.925  -2.734   1.046  1.00 47.38           C  
ATOM   4541  SD  MET B 447     -90.605  -3.878   0.769  1.00 41.75           S  
ATOM   4542  CE  MET B 447     -89.371  -3.202   1.863  1.00 46.74           C  
ATOM   4543  N   ARG B 448     -93.945  -3.304  -2.855  1.00 52.40           N  
ATOM   4544  CA  ARG B 448     -95.137  -3.234  -3.666  1.00 57.64           C  
ATOM   4545  C   ARG B 448     -96.263  -2.898  -2.716  1.00 54.15           C  
ATOM   4546  O   ARG B 448     -97.003  -1.928  -2.925  1.00 49.08           O  
ATOM   4547  CB  ARG B 448     -95.419  -4.541  -4.415  1.00 58.88           C  
ATOM   4548  CG  ARG B 448     -96.533  -4.377  -5.449  1.00 68.81           C  
ATOM   4549  CD  ARG B 448     -96.618  -5.538  -6.429  1.00 80.86           C  
ATOM   4550  NE  ARG B 448     -97.339  -6.695  -5.881  1.00 89.26           N  
ATOM   4551  CZ  ARG B 448     -97.385  -7.917  -6.428  1.00 87.32           C  
ATOM   4552  NH1 ARG B 448     -96.740  -8.206  -7.563  1.00 83.64           N  
ATOM   4553  NH2 ARG B 448     -98.087  -8.871  -5.820  1.00 83.48           N  
ATOM   4554  N   LYS B 449     -96.373  -3.685  -1.654  1.00 52.69           N  
ATOM   4555  CA  LYS B 449     -97.397  -3.445  -0.651  1.00 56.28           C  
ATOM   4556  C   LYS B 449     -96.752  -3.032   0.657  1.00 50.90           C  
ATOM   4557  O   LYS B 449     -95.648  -3.430   0.960  1.00 47.81           O  
ATOM   4558  CB  LYS B 449     -98.254  -4.686  -0.437  1.00 59.41           C  
ATOM   4559  CG  LYS B 449     -98.674  -5.400  -1.722  1.00 62.51           C  
ATOM   4560  CD  LYS B 449    -100.086  -5.078  -2.144  1.00 65.07           C  
ATOM   4561  CE  LYS B 449    -100.563  -6.014  -3.256  1.00 68.95           C  
ATOM   4562  NZ  LYS B 449    -102.042  -5.896  -3.530  1.00 77.45           N  
ATOM   4563  N   MET B 450     -97.457  -2.212   1.418  1.00 53.04           N  
ATOM   4564  CA  MET B 450     -97.012  -1.794   2.739  1.00 52.44           C  
ATOM   4565  C   MET B 450     -98.218  -1.168   3.424  1.00 46.38           C  
ATOM   4566  O   MET B 450     -98.997  -0.473   2.789  1.00 41.87           O  
ATOM   4567  CB  MET B 450     -95.861  -0.804   2.634  1.00 53.09           C  
ATOM   4568  CG  MET B 450     -95.492  -0.107   3.939  1.00 55.91           C  
ATOM   4569  SD  MET B 450     -94.470  -1.071   5.072  1.00 48.40           S  
ATOM   4570  CE  MET B 450     -92.877  -0.327   4.773  1.00 40.29           C  
ATOM   4571  N   SER B 451     -98.358  -1.425   4.717  1.00 39.37           N  
ATOM   4572  CA  SER B 451     -99.602  -1.192   5.399  1.00 35.67           C  
ATOM   4573  C   SER B 451     -99.366  -1.167   6.872  1.00 33.40           C  
ATOM   4574  O   SER B 451     -98.446  -1.803   7.361  1.00 34.78           O  
ATOM   4575  CB  SER B 451    -100.565  -2.322   5.094  1.00 43.28           C  
ATOM   4576  OG  SER B 451     -99.962  -3.566   5.389  1.00 42.67           O  
ATOM   4577  N   MET B 452    -100.209  -0.422   7.573  1.00 38.47           N  
ATOM   4578  CA  MET B 452    -100.200  -0.381   9.033  1.00 40.78           C  
ATOM   4579  C   MET B 452    -101.613  -0.511   9.560  1.00 37.39           C  
ATOM   4580  O   MET B 452    -102.590  -0.205   8.889  1.00 37.96           O  
ATOM   4581  CB  MET B 452     -99.614   0.918   9.546  1.00 38.93           C  
ATOM   4582  CG  MET B 452     -98.370   1.297   8.840  1.00 41.29           C  
ATOM   4583  SD  MET B 452     -97.705   2.775   9.531  1.00 45.03           S  
ATOM   4584  CE  MET B 452     -97.009   2.078  11.025  1.00 44.25           C  
ATOM   4585  N   LYS B 453    -101.713  -0.960  10.786  1.00 33.88           N  
ATOM   4586  CA  LYS B 453    -102.979  -1.275  11.320  1.00 34.54           C  
ATOM   4587  C   LYS B 453    -102.824  -1.595  12.771  1.00 37.85           C  
ATOM   4588  O   LYS B 453    -101.797  -2.114  13.205  1.00 40.56           O  
ATOM   4589  CB  LYS B 453    -103.567  -2.463  10.581  1.00 43.58           C  
ATOM   4590  CG  LYS B 453    -102.594  -3.583  10.301  1.00 44.72           C  
ATOM   4591  CD  LYS B 453    -103.277  -4.671   9.503  1.00 44.03           C  
ATOM   4592  CE  LYS B 453    -103.377  -4.306   8.036  1.00 45.82           C  
ATOM   4593  NZ  LYS B 453    -103.864  -5.440   7.200  1.00 45.16           N  
ATOM   4594  N   ILE B 454    -103.865  -1.285  13.517  1.00 39.42           N  
ATOM   4595  CA  ILE B 454    -103.819  -1.397  14.948  1.00 42.31           C  
ATOM   4596  C   ILE B 454    -105.045  -2.123  15.409  1.00 42.21           C  
ATOM   4597  O   ILE B 454    -105.945  -2.392  14.624  1.00 44.20           O  
ATOM   4598  CB  ILE B 454    -103.725  -0.022  15.629  1.00 39.23           C  
ATOM   4599  CG1 ILE B 454    -104.900   0.859  15.215  1.00 37.16           C  
ATOM   4600  CG2 ILE B 454    -102.393   0.616  15.301  1.00 35.91           C  
ATOM   4601  CD1 ILE B 454    -104.622   2.297  15.348  1.00 37.69           C  
ATOM   4602  N   ARG B 455    -105.042  -2.453  16.690  1.00 43.60           N  
ATOM   4603  CA  ARG B 455    -106.097  -3.202  17.327  1.00 44.43           C  
ATOM   4604  C   ARG B 455    -105.768  -3.109  18.814  1.00 49.10           C  
ATOM   4605  O   ARG B 455    -104.599  -2.986  19.180  1.00 52.41           O  
ATOM   4606  CB  ARG B 455    -106.085  -4.644  16.823  1.00 42.99           C  
ATOM   4607  CG  ARG B 455    -106.883  -5.621  17.653  1.00 45.51           C  
ATOM   4608  CD  ARG B 455    -106.953  -7.037  17.019  1.00 58.02           C  
ATOM   4609  NE  ARG B 455    -105.800  -7.931  17.273  1.00 52.14           N  
ATOM   4610  CZ  ARG B 455    -105.694  -9.180  16.804  1.00 45.19           C  
ATOM   4611  NH1 ARG B 455    -106.644  -9.732  16.058  1.00 50.12           N  
ATOM   4612  NH2 ARG B 455    -104.627  -9.893  17.071  1.00 52.62           N  
ATOM   4613  N   PRO B 456    -106.782  -3.130  19.681  1.00 51.87           N  
ATOM   4614  CA  PRO B 456    -106.548  -3.072  21.129  1.00 56.98           C  
ATOM   4615  C   PRO B 456    -105.932  -4.343  21.708  1.00 64.02           C  
ATOM   4616  O   PRO B 456    -105.946  -5.374  21.050  1.00 67.87           O  
ATOM   4617  CB  PRO B 456    -107.946  -2.874  21.693  1.00 56.87           C  
ATOM   4618  CG  PRO B 456    -108.713  -2.292  20.584  1.00 60.31           C  
ATOM   4619  CD  PRO B 456    -108.196  -2.932  19.357  1.00 55.12           C  
ATOM   4620  N   PHE B 457    -105.438  -4.279  22.944  1.00 70.16           N  
ATOM   4621  CA  PHE B 457    -104.522  -5.306  23.460  1.00 78.15           C  
ATOM   4622  C   PHE B 457    -105.161  -6.487  24.213  1.00 87.00           C  
ATOM   4623  O   PHE B 457    -105.145  -7.608  23.704  1.00 92.93           O  
ATOM   4624  CB  PHE B 457    -103.450  -4.650  24.321  1.00 78.83           C  
ATOM   4625  CG  PHE B 457    -102.328  -5.563  24.678  1.00 81.00           C  
ATOM   4626  CD1 PHE B 457    -101.479  -6.048  23.698  1.00 78.87           C  
ATOM   4627  CD2 PHE B 457    -102.120  -5.944  26.002  1.00 90.44           C  
ATOM   4628  CE1 PHE B 457    -100.434  -6.899  24.027  1.00 87.82           C  
ATOM   4629  CE2 PHE B 457    -101.074  -6.795  26.348  1.00 92.30           C  
ATOM   4630  CZ  PHE B 457    -100.226  -7.272  25.359  1.00 92.60           C  
ATOM   4631  N   PHE B 458    -105.690  -6.251  25.416  1.00 96.57           N  
ATOM   4632  CA  PHE B 458    -106.252  -7.326  26.274  1.00103.68           C  
ATOM   4633  C   PHE B 458    -105.182  -8.211  26.945  1.00101.52           C  
ATOM   4634  O   PHE B 458    -104.770  -9.255  26.427  1.00 94.61           O  
ATOM   4635  CB  PHE B 458    -107.246  -8.227  25.509  1.00108.02           C  
ATOM   4636  CG  PHE B 458    -108.468  -7.505  24.991  1.00109.50           C  
ATOM   4637  CD1 PHE B 458    -109.455  -7.065  25.872  1.00111.56           C  
ATOM   4638  CD2 PHE B 458    -108.650  -7.299  23.624  1.00107.90           C  
ATOM   4639  CE1 PHE B 458    -110.594  -6.409  25.403  1.00112.12           C  
ATOM   4640  CE2 PHE B 458    -109.785  -6.644  23.145  1.00108.86           C  
ATOM   4641  CZ  PHE B 458    -110.758  -6.197  24.036  1.00110.79           C  
TER    4642      PHE B 458                                                      
ATOM   4643  N   ARG C  14      65.148  27.065 -61.425  1.00 96.73           N  
ATOM   4644  CA  ARG C  14      65.754  26.445 -62.645  1.00 97.55           C  
ATOM   4645  C   ARG C  14      65.780  24.900 -62.589  1.00 96.00           C  
ATOM   4646  O   ARG C  14      66.535  24.248 -63.322  1.00 88.46           O  
ATOM   4647  CB  ARG C  14      67.156  27.023 -62.894  1.00 98.46           C  
ATOM   4648  CG  ARG C  14      67.907  27.443 -61.630  1.00 99.86           C  
ATOM   4649  CD  ARG C  14      69.422  27.380 -61.830  1.00 98.36           C  
ATOM   4650  NE  ARG C  14      70.153  28.226 -60.886  1.00 96.79           N  
ATOM   4651  CZ  ARG C  14      71.472  28.193 -60.697  1.00 94.59           C  
ATOM   4652  NH1 ARG C  14      72.237  27.343 -61.377  1.00 91.22           N  
ATOM   4653  NH2 ARG C  14      72.033  29.014 -59.814  1.00 96.20           N  
ATOM   4654  N   PHE C  15      64.940  24.326 -61.726  1.00 93.09           N  
ATOM   4655  CA  PHE C  15      64.695  22.884 -61.701  1.00 90.19           C  
ATOM   4656  C   PHE C  15      63.399  22.616 -62.459  1.00 91.39           C  
ATOM   4657  O   PHE C  15      62.423  22.121 -61.889  1.00 90.19           O  
ATOM   4658  CB  PHE C  15      64.564  22.372 -60.261  1.00 89.05           C  
ATOM   4659  CG  PHE C  15      65.865  22.298 -59.510  1.00 86.92           C  
ATOM   4660  CD1 PHE C  15      66.415  21.065 -59.174  1.00 85.93           C  
ATOM   4661  CD2 PHE C  15      66.531  23.455 -59.120  1.00 85.70           C  
ATOM   4662  CE1 PHE C  15      67.613  20.984 -58.473  1.00 85.07           C  
ATOM   4663  CE2 PHE C  15      67.733  23.383 -58.418  1.00 84.22           C  
ATOM   4664  CZ  PHE C  15      68.273  22.146 -58.094  1.00 84.00           C  
ATOM   4665  N   GLY C  16      63.387  22.975 -63.740  1.00 96.11           N  
ATOM   4666  CA  GLY C  16      62.215  22.785 -64.598  1.00 98.84           C  
ATOM   4667  C   GLY C  16      60.924  23.392 -64.063  1.00 97.75           C  
ATOM   4668  O   GLY C  16      60.942  24.425 -63.384  1.00 96.13           O  
ATOM   4669  N   SER C  17      59.806  22.732 -64.369  1.00 94.39           N  
ATOM   4670  CA  SER C  17      58.473  23.208 -63.998  1.00 91.76           C  
ATOM   4671  C   SER C  17      58.321  23.368 -62.487  1.00 87.54           C  
ATOM   4672  O   SER C  17      59.109  22.812 -61.712  1.00 76.98           O  
ATOM   4673  CB  SER C  17      57.397  22.237 -64.510  1.00 93.42           C  
ATOM   4674  OG  SER C  17      57.558  21.951 -65.890  1.00 94.76           O  
ATOM   4675  N   TYR C  18      57.298  24.127 -62.086  1.00 88.04           N  
ATOM   4676  CA  TYR C  18      56.968  24.318 -60.665  1.00 89.54           C  
ATOM   4677  C   TYR C  18      55.478  24.102 -60.296  1.00 90.55           C  
ATOM   4678  O   TYR C  18      54.610  24.915 -60.632  1.00 86.77           O  
ATOM   4679  CB  TYR C  18      57.478  25.678 -60.176  1.00 87.10           C  
ATOM   4680  CG  TYR C  18      58.764  25.517 -59.410  1.00 91.96           C  
ATOM   4681  CD1 TYR C  18      59.989  25.438 -60.072  1.00 93.65           C  
ATOM   4682  CD2 TYR C  18      58.753  25.376 -58.022  1.00 91.67           C  
ATOM   4683  CE1 TYR C  18      61.175  25.259 -59.365  1.00 91.22           C  
ATOM   4684  CE2 TYR C  18      59.933  25.202 -57.306  1.00 89.08           C  
ATOM   4685  CZ  TYR C  18      61.140  25.143 -57.981  1.00 88.03           C  
ATOM   4686  OH  TYR C  18      62.312  24.964 -57.280  1.00 80.24           O  
ATOM   4687  N   CYS C  19      55.224  22.987 -59.597  1.00 87.56           N  
ATOM   4688  CA  CYS C  19      53.900  22.594 -59.104  1.00 83.25           C  
ATOM   4689  C   CYS C  19      53.902  22.581 -57.567  1.00 77.24           C  
ATOM   4690  O   CYS C  19      54.973  22.583 -56.954  1.00 66.66           O  
ATOM   4691  CB  CYS C  19      53.532  21.196 -59.622  1.00 85.50           C  
ATOM   4692  SG  CYS C  19      53.274  21.028 -61.422  1.00 88.21           S  
ATOM   4693  N   PRO C  20      52.703  22.554 -56.939  1.00 73.06           N  
ATOM   4694  CA  PRO C  20      52.655  22.576 -55.476  1.00 69.95           C  
ATOM   4695  C   PRO C  20      53.110  21.284 -54.819  1.00 68.04           C  
ATOM   4696  O   PRO C  20      53.138  20.227 -55.452  1.00 59.14           O  
ATOM   4697  CB  PRO C  20      51.173  22.816 -55.172  1.00 70.77           C  
ATOM   4698  CG  PRO C  20      50.462  22.302 -56.347  1.00 71.39           C  
ATOM   4699  CD  PRO C  20      51.348  22.579 -57.522  1.00 70.29           C  
ATOM   4700  N   THR C  21      53.462  21.395 -53.545  1.00 72.98           N  
ATOM   4701  CA  THR C  21      53.838  20.251 -52.729  1.00 77.23           C  
ATOM   4702  C   THR C  21      52.819  19.124 -52.860  1.00 74.87           C  
ATOM   4703  O   THR C  21      51.637  19.371 -53.094  1.00 69.11           O  
ATOM   4704  CB  THR C  21      53.962  20.651 -51.240  1.00 82.48           C  
ATOM   4705  OG1 THR C  21      54.142  19.478 -50.436  1.00 87.67           O  
ATOM   4706  CG2 THR C  21      52.717  21.417 -50.767  1.00 77.66           C  
ATOM   4707  N   THR C  22      53.292  17.891 -52.708  1.00 79.03           N  
ATOM   4708  CA  THR C  22      52.437  16.709 -52.823  1.00 87.06           C  
ATOM   4709  C   THR C  22      51.550  16.550 -51.598  1.00 90.22           C  
ATOM   4710  O   THR C  22      50.507  15.893 -51.646  1.00 89.81           O  
ATOM   4711  CB  THR C  22      53.260  15.413 -52.962  1.00 92.71           C  
ATOM   4712  OG1 THR C  22      54.551  15.697 -53.530  1.00 96.01           O  
ATOM   4713  CG2 THR C  22      52.499  14.405 -53.823  1.00 94.79           C  
ATOM   4714  N   CYS C  23      51.999  17.133 -50.492  1.00 94.02           N  
ATOM   4715  CA  CYS C  23      51.249  17.141 -49.243  1.00 97.13           C  
ATOM   4716  C   CYS C  23      50.041  18.081 -49.346  1.00 95.11           C  
ATOM   4717  O   CYS C  23      48.900  17.662 -49.149  1.00 92.54           O  
ATOM   4718  CB  CYS C  23      52.173  17.571 -48.095  1.00101.22           C  
ATOM   4719  SG  CYS C  23      53.348  16.287 -47.521  1.00107.30           S  
ATOM   4720  N   GLY C  24      50.307  19.345 -49.682  1.00 93.59           N  
ATOM   4721  CA  GLY C  24      49.273  20.383 -49.829  1.00 89.36           C  
ATOM   4722  C   GLY C  24      48.117  20.028 -50.751  1.00 85.58           C  
ATOM   4723  O   GLY C  24      47.097  20.719 -50.780  1.00 82.69           O  
ATOM   4724  N   ILE C  25      48.298  18.972 -51.535  1.00 86.53           N  
ATOM   4725  CA  ILE C  25      47.192  18.296 -52.193  1.00 87.99           C  
ATOM   4726  C   ILE C  25      46.337  17.587 -51.144  1.00 87.90           C  
ATOM   4727  O   ILE C  25      45.126  17.787 -51.101  1.00 86.96           O  
ATOM   4728  CB  ILE C  25      47.705  17.277 -53.235  1.00 89.36           C  
ATOM   4729  CG1 ILE C  25      48.248  18.020 -54.458  1.00 92.86           C  
ATOM   4730  CG2 ILE C  25      46.606  16.308 -53.641  1.00 82.30           C  
ATOM   4731  CD1 ILE C  25      48.952  17.130 -55.451  1.00 97.64           C  
ATOM   4732  N   ALA C  26      46.976  16.783 -50.291  1.00 89.16           N  
ATOM   4733  CA  ALA C  26      46.272  15.995 -49.260  1.00 90.88           C  
ATOM   4734  C   ALA C  26      45.596  16.847 -48.161  1.00 94.14           C  
ATOM   4735  O   ALA C  26      44.655  16.387 -47.495  1.00 90.89           O  
ATOM   4736  CB  ALA C  26      47.224  14.977 -48.630  1.00 84.81           C  
ATOM   4737  N   ASP C  27      46.088  18.073 -47.968  1.00 93.28           N  
ATOM   4738  CA  ASP C  27      45.443  19.043 -47.074  1.00 87.38           C  
ATOM   4739  C   ASP C  27      44.152  19.513 -47.704  1.00 86.58           C  
ATOM   4740  O   ASP C  27      43.081  19.423 -47.097  1.00 89.39           O  
ATOM   4741  CB  ASP C  27      46.338  20.264 -46.831  1.00 88.62           C  
ATOM   4742  CG  ASP C  27      47.409  20.015 -45.784  1.00 91.92           C  
ATOM   4743  OD1 ASP C  27      47.270  19.057 -44.992  1.00 95.26           O  
ATOM   4744  OD2 ASP C  27      48.385  20.795 -45.743  1.00 89.39           O  
ATOM   4745  N   PHE C  28      44.269  20.018 -48.930  1.00 83.26           N  
ATOM   4746  CA  PHE C  28      43.118  20.475 -49.698  1.00 78.72           C  
ATOM   4747  C   PHE C  28      42.084  19.368 -49.824  1.00 75.79           C  
ATOM   4748  O   PHE C  28      40.895  19.642 -49.868  1.00 78.98           O  
ATOM   4749  CB  PHE C  28      43.553  20.933 -51.083  1.00 80.21           C  
ATOM   4750  CG  PHE C  28      42.570  21.828 -51.755  1.00 82.25           C  
ATOM   4751  CD1 PHE C  28      41.526  21.296 -52.496  1.00 87.06           C  
ATOM   4752  CD2 PHE C  28      42.689  23.207 -51.656  1.00 85.40           C  
ATOM   4753  CE1 PHE C  28      40.606  22.127 -53.128  1.00 91.34           C  
ATOM   4754  CE2 PHE C  28      41.778  24.046 -52.283  1.00 88.97           C  
ATOM   4755  CZ  PHE C  28      40.732  23.507 -53.021  1.00 90.51           C  
ATOM   4756  N   LEU C  29      42.552  18.123 -49.880  1.00 78.12           N  
ATOM   4757  CA  LEU C  29      41.686  16.942 -49.826  1.00 82.65           C  
ATOM   4758  C   LEU C  29      40.945  16.831 -48.482  1.00 86.52           C  
ATOM   4759  O   LEU C  29      39.716  16.847 -48.448  1.00 86.46           O  
ATOM   4760  CB  LEU C  29      42.524  15.681 -50.060  1.00 82.43           C  
ATOM   4761  CG  LEU C  29      41.824  14.319 -50.046  1.00 83.30           C  
ATOM   4762  CD1 LEU C  29      41.692  13.783 -51.463  1.00 80.72           C  
ATOM   4763  CD2 LEU C  29      42.587  13.328 -49.163  1.00 84.60           C  
ATOM   4764  N   SER C  30      41.700  16.721 -47.387  1.00 86.94           N  
ATOM   4765  CA  SER C  30      41.135  16.596 -46.037  1.00 82.52           C  
ATOM   4766  C   SER C  30      40.045  17.633 -45.764  1.00 81.68           C  
ATOM   4767  O   SER C  30      39.005  17.302 -45.188  1.00 84.04           O  
ATOM   4768  CB  SER C  30      42.251  16.720 -44.988  1.00 83.55           C  
ATOM   4769  OG  SER C  30      41.738  16.821 -43.668  1.00 85.72           O  
ATOM   4770  N   THR C  31      40.278  18.872 -46.199  1.00 80.97           N  
ATOM   4771  CA  THR C  31      39.365  19.989 -45.920  1.00 81.24           C  
ATOM   4772  C   THR C  31      38.117  19.976 -46.824  1.00 83.40           C  
ATOM   4773  O   THR C  31      37.003  19.729 -46.354  1.00 86.34           O  
ATOM   4774  CB  THR C  31      40.078  21.367 -46.042  1.00 79.43           C  
ATOM   4775  OG1 THR C  31      40.248  21.713 -47.424  1.00 80.21           O  
ATOM   4776  CG2 THR C  31      41.440  21.354 -45.327  1.00 78.11           C  
ATOM   4777  N   TYR C  32      38.313  20.253 -48.111  1.00 80.78           N  
ATOM   4778  CA  TYR C  32      37.231  20.233 -49.115  1.00 80.12           C  
ATOM   4779  C   TYR C  32      36.441  18.919 -49.095  1.00 78.59           C  
ATOM   4780  O   TYR C  32      35.267  18.907 -49.451  1.00 79.98           O  
ATOM   4781  CB  TYR C  32      37.826  20.543 -50.505  1.00 83.94           C  
ATOM   4782  CG  TYR C  32      37.161  19.953 -51.746  1.00 82.54           C  
ATOM   4783  CD1 TYR C  32      36.525  20.779 -52.669  1.00 81.79           C  
ATOM   4784  CD2 TYR C  32      37.244  18.585 -52.037  1.00 78.31           C  
ATOM   4785  CE1 TYR C  32      35.953  20.261 -53.822  1.00 80.75           C  
ATOM   4786  CE2 TYR C  32      36.671  18.059 -53.185  1.00 76.27           C  
ATOM   4787  CZ  TYR C  32      36.027  18.902 -54.075  1.00 78.85           C  
ATOM   4788  OH  TYR C  32      35.457  18.387 -55.220  1.00 83.68           O  
ATOM   4789  N   GLN C  33      37.089  17.824 -48.690  1.00 77.92           N  
ATOM   4790  CA  GLN C  33      36.392  16.576 -48.389  1.00 78.80           C  
ATOM   4791  C   GLN C  33      35.396  16.801 -47.248  1.00 87.45           C  
ATOM   4792  O   GLN C  33      34.229  16.414 -47.355  1.00 94.56           O  
ATOM   4793  CB  GLN C  33      37.383  15.483 -47.990  1.00 77.43           C  
ATOM   4794  CG  GLN C  33      36.750  14.188 -47.505  1.00 81.15           C  
ATOM   4795  CD  GLN C  33      37.172  13.843 -46.088  1.00 87.39           C  
ATOM   4796  OE1 GLN C  33      36.342  13.781 -45.175  1.00 91.65           O  
ATOM   4797  NE2 GLN C  33      38.470  13.641 -45.892  1.00 88.99           N  
ATOM   4798  N   THR C  34      35.856  17.418 -46.160  1.00 86.29           N  
ATOM   4799  CA  THR C  34      34.984  17.713 -45.019  1.00 83.06           C  
ATOM   4800  C   THR C  34      33.995  18.838 -45.341  1.00 80.30           C  
ATOM   4801  O   THR C  34      32.841  18.769 -44.934  1.00 82.49           O  
ATOM   4802  CB  THR C  34      35.799  18.057 -43.751  1.00 83.20           C  
ATOM   4803  OG1 THR C  34      36.429  16.868 -43.255  1.00 81.82           O  
ATOM   4804  CG2 THR C  34      34.902  18.630 -42.664  1.00 85.32           C  
ATOM   4805  N   LYS C  35      34.448  19.849 -46.087  1.00 80.85           N  
ATOM   4806  CA  LYS C  35      33.608  21.004 -46.466  1.00 80.22           C  
ATOM   4807  C   LYS C  35      32.448  20.621 -47.385  1.00 77.84           C  
ATOM   4808  O   LYS C  35      31.451  21.339 -47.462  1.00 71.92           O  
ATOM   4809  CB  LYS C  35      34.451  22.090 -47.150  1.00 87.37           C  
ATOM   4810  CG  LYS C  35      33.765  23.462 -47.294  1.00 90.97           C  
ATOM   4811  CD  LYS C  35      33.799  24.256 -45.990  1.00 94.94           C  
ATOM   4812  CE  LYS C  35      32.971  25.533 -46.075  1.00 98.03           C  
ATOM   4813  NZ  LYS C  35      31.500  25.286 -45.912  1.00103.29           N  
ATOM   4814  N   VAL C  36      32.596  19.509 -48.102  1.00 81.01           N  
ATOM   4815  CA  VAL C  36      31.492  18.923 -48.857  1.00 80.61           C  
ATOM   4816  C   VAL C  36      30.682  18.007 -47.947  1.00 84.24           C  
ATOM   4817  O   VAL C  36      29.459  18.129 -47.887  1.00 95.88           O  
ATOM   4818  CB  VAL C  36      31.981  18.144 -50.094  1.00 80.33           C  
ATOM   4819  CG1 VAL C  36      30.948  17.122 -50.523  1.00 80.63           C  
ATOM   4820  CG2 VAL C  36      32.287  19.103 -51.237  1.00 81.10           C  
ATOM   4821  N   ASP C  37      31.354  17.103 -47.231  1.00 87.35           N  
ATOM   4822  CA  ASP C  37      30.670  16.232 -46.260  1.00 91.76           C  
ATOM   4823  C   ASP C  37      29.722  17.047 -45.382  1.00 93.73           C  
ATOM   4824  O   ASP C  37      28.615  16.608 -45.078  1.00 97.94           O  
ATOM   4825  CB  ASP C  37      31.667  15.457 -45.380  1.00 94.47           C  
ATOM   4826  CG  ASP C  37      31.791  13.985 -45.775  1.00 96.55           C  
ATOM   4827  OD1 ASP C  37      31.906  13.137 -44.863  1.00 93.90           O  
ATOM   4828  OD2 ASP C  37      31.772  13.671 -46.985  1.00103.68           O  
ATOM   4829  N   LYS C  38      30.169  18.237 -44.992  1.00 94.68           N  
ATOM   4830  CA  LYS C  38      29.329  19.203 -44.285  1.00100.02           C  
ATOM   4831  C   LYS C  38      28.053  19.502 -45.070  1.00102.10           C  
ATOM   4832  O   LYS C  38      26.957  19.219 -44.593  1.00109.23           O  
ATOM   4833  CB  LYS C  38      30.104  20.510 -44.045  1.00101.07           C  
ATOM   4834  CG  LYS C  38      29.433  21.511 -43.097  1.00 97.38           C  
ATOM   4835  CD  LYS C  38      30.008  21.436 -41.679  1.00 94.40           C  
ATOM   4836  CE  LYS C  38      31.384  22.087 -41.575  1.00 89.98           C  
ATOM   4837  NZ  LYS C  38      31.819  22.226 -40.160  1.00 87.13           N  
ATOM   4838  N   ASP C  39      28.203  20.058 -46.273  1.00101.38           N  
ATOM   4839  CA  ASP C  39      27.061  20.551 -47.056  1.00105.14           C  
ATOM   4840  C   ASP C  39      26.189  19.420 -47.590  1.00104.90           C  
ATOM   4841  O   ASP C  39      25.012  19.628 -47.916  1.00107.96           O  
ATOM   4842  CB  ASP C  39      27.537  21.427 -48.218  1.00109.26           C  
ATOM   4843  CG  ASP C  39      28.183  22.724 -47.751  1.00115.35           C  
ATOM   4844  OD1 ASP C  39      28.075  23.729 -48.487  1.00116.40           O  
ATOM   4845  OD2 ASP C  39      28.795  22.742 -46.655  1.00119.04           O  
ATOM   4846  N   LEU C  40      26.770  18.226 -47.673  1.00102.21           N  
ATOM   4847  CA  LEU C  40      26.026  17.034 -48.062  1.00103.40           C  
ATOM   4848  C   LEU C  40      25.475  16.262 -46.860  1.00105.65           C  
ATOM   4849  O   LEU C  40      24.714  15.317 -47.042  1.00113.36           O  
ATOM   4850  CB  LEU C  40      26.887  16.122 -48.939  1.00102.35           C  
ATOM   4851  CG  LEU C  40      27.377  16.717 -50.267  1.00101.67           C  
ATOM   4852  CD1 LEU C  40      27.831  15.604 -51.193  1.00 99.74           C  
ATOM   4853  CD2 LEU C  40      26.323  17.572 -50.957  1.00101.05           C  
ATOM   4854  N   GLN C  41      25.860  16.653 -45.644  1.00107.37           N  
ATOM   4855  CA  GLN C  41      25.152  16.212 -44.432  1.00112.31           C  
ATOM   4856  C   GLN C  41      23.935  17.111 -44.226  1.00111.03           C  
ATOM   4857  O   GLN C  41      22.861  16.644 -43.852  1.00111.53           O  
ATOM   4858  CB  GLN C  41      26.054  16.256 -43.186  1.00116.06           C  
ATOM   4859  CG  GLN C  41      26.497  14.884 -42.656  1.00117.69           C  
ATOM   4860  CD  GLN C  41      25.483  14.249 -41.702  1.00117.56           C  
ATOM   4861  OE1 GLN C  41      24.272  14.291 -41.936  1.00115.80           O  
ATOM   4862  NE2 GLN C  41      25.982  13.653 -40.622  1.00116.10           N  
ATOM   4863  N   SER C  42      24.131  18.405 -44.476  1.00114.77           N  
ATOM   4864  CA  SER C  42      23.069  19.411 -44.393  1.00116.80           C  
ATOM   4865  C   SER C  42      21.897  19.063 -45.300  1.00121.10           C  
ATOM   4866  O   SER C  42      20.748  19.268 -44.922  1.00128.87           O  
ATOM   4867  CB  SER C  42      23.608  20.799 -44.766  1.00113.17           C  
ATOM   4868  OG  SER C  42      22.567  21.755 -44.854  1.00106.60           O  
ATOM   4869  N   LEU C  43      22.188  18.540 -46.491  1.00119.50           N  
ATOM   4870  CA  LEU C  43      21.130  18.126 -47.415  1.00120.65           C  
ATOM   4871  C   LEU C  43      20.550  16.757 -47.079  1.00129.41           C  
ATOM   4872  O   LEU C  43      19.339  16.637 -46.889  1.00139.40           O  
ATOM   4873  CB  LEU C  43      21.616  18.145 -48.861  1.00113.22           C  
ATOM   4874  CG  LEU C  43      21.361  19.489 -49.526  1.00110.39           C  
ATOM   4875  CD1 LEU C  43      22.056  20.594 -48.742  1.00108.81           C  
ATOM   4876  CD2 LEU C  43      21.814  19.431 -50.967  1.00111.19           C  
ATOM   4877  N   GLU C  44      21.403  15.733 -47.004  1.00131.15           N  
ATOM   4878  CA  GLU C  44      20.939  14.345 -46.796  1.00137.62           C  
ATOM   4879  C   GLU C  44      20.140  14.159 -45.493  1.00140.16           C  
ATOM   4880  O   GLU C  44      19.173  13.387 -45.450  1.00141.60           O  
ATOM   4881  CB  GLU C  44      22.122  13.359 -46.831  1.00138.35           C  
ATOM   4882  CG  GLU C  44      22.923  13.274 -45.519  1.00138.97           C  
ATOM   4883  CD  GLU C  44      24.217  12.478 -45.638  1.00137.58           C  
ATOM   4884  OE1 GLU C  44      24.689  12.253 -46.773  1.00133.67           O  
ATOM   4885  OE2 GLU C  44      24.764  12.080 -44.585  1.00137.18           O  
ATOM   4886  N   ASP C  45      20.565  14.865 -44.443  1.00137.78           N  
ATOM   4887  CA  ASP C  45      19.917  14.820 -43.132  1.00141.10           C  
ATOM   4888  C   ASP C  45      18.614  15.617 -43.168  1.00139.44           C  
ATOM   4889  O   ASP C  45      17.590  15.155 -42.663  1.00139.02           O  
ATOM   4890  CB  ASP C  45      20.869  15.379 -42.061  1.00144.05           C  
ATOM   4891  CG  ASP C  45      20.398  15.112 -40.635  1.00147.23           C  
ATOM   4892  OD1 ASP C  45      19.392  14.394 -40.441  1.00149.46           O  
ATOM   4893  OD2 ASP C  45      21.056  15.624 -39.700  1.00148.25           O  
ATOM   4894  N   ILE C  46      18.655  16.803 -43.779  1.00138.50           N  
ATOM   4895  CA  ILE C  46      17.458  17.642 -43.934  1.00142.15           C  
ATOM   4896  C   ILE C  46      16.563  17.158 -45.096  1.00141.51           C  
ATOM   4897  O   ILE C  46      15.511  17.742 -45.352  1.00141.39           O  
ATOM   4898  CB  ILE C  46      17.831  19.152 -44.086  1.00144.43           C  
ATOM   4899  CG1 ILE C  46      18.607  19.641 -42.849  1.00145.56           C  
ATOM   4900  CG2 ILE C  46      16.586  20.013 -44.273  1.00145.07           C  
ATOM   4901  CD1 ILE C  46      19.090  21.080 -42.938  1.00144.21           C  
ATOM   4902  N   LEU C  47      16.986  16.094 -45.785  1.00143.92           N  
ATOM   4903  CA  LEU C  47      16.137  15.371 -46.748  1.00147.66           C  
ATOM   4904  C   LEU C  47      15.564  14.086 -46.147  1.00150.27           C  
ATOM   4905  O   LEU C  47      14.407  13.748 -46.393  1.00155.98           O  
ATOM   4906  CB  LEU C  47      16.912  15.027 -48.027  1.00147.27           C  
ATOM   4907  CG  LEU C  47      16.215  14.055 -48.997  1.00146.26           C  
ATOM   4908  CD1 LEU C  47      16.606  14.338 -50.444  1.00145.98           C  
ATOM   4909  CD2 LEU C  47      16.493  12.589 -48.634  1.00143.63           C  
ATOM   4910  N   HIS C  48      16.378  13.360 -45.385  1.00151.11           N  
ATOM   4911  CA  HIS C  48      15.920  12.147 -44.706  1.00154.92           C  
ATOM   4912  C   HIS C  48      14.701  12.415 -43.810  1.00156.49           C  
ATOM   4913  O   HIS C  48      13.897  11.512 -43.564  1.00157.48           O  
ATOM   4914  CB  HIS C  48      17.056  11.537 -43.879  1.00156.68           C  
ATOM   4915  CG  HIS C  48      16.701  10.236 -43.231  1.00158.03           C  
ATOM   4916  ND1 HIS C  48      15.913  10.157 -42.102  1.00159.06           N  
ATOM   4917  CD2 HIS C  48      17.027   8.962 -43.551  1.00157.74           C  
ATOM   4918  CE1 HIS C  48      15.767   8.891 -41.757  1.00159.25           C  
ATOM   4919  NE2 HIS C  48      16.434   8.145 -42.619  1.00158.90           N  
ATOM   4920  N   GLN C  49      14.573  13.651 -43.326  1.00159.05           N  
ATOM   4921  CA  GLN C  49      13.432  14.049 -42.502  1.00160.92           C  
ATOM   4922  C   GLN C  49      12.228  14.474 -43.349  1.00163.66           C  
ATOM   4923  O   GLN C  49      11.093  14.112 -43.033  1.00166.10           O  
ATOM   4924  CB  GLN C  49      13.830  15.175 -41.540  1.00160.11           C  
ATOM   4925  CG  GLN C  49      12.967  15.253 -40.278  1.00160.32           C  
ATOM   4926  CD  GLN C  49      13.059  14.006 -39.402  1.00158.43           C  
ATOM   4927  OE1 GLN C  49      14.006  13.226 -39.504  1.00158.01           O  
ATOM   4928  NE2 GLN C  49      12.067  13.816 -38.538  1.00156.61           N  
ATOM   4929  N   VAL C  50      12.473  15.235 -44.416  1.00163.65           N  
ATOM   4930  CA  VAL C  50      11.402  15.651 -45.335  1.00163.17           C  
ATOM   4931  C   VAL C  50      10.815  14.460 -46.120  1.00164.38           C  
ATOM   4932  O   VAL C  50       9.640  14.488 -46.498  1.00166.90           O  
ATOM   4933  CB  VAL C  50      11.880  16.774 -46.300  1.00161.80           C  
ATOM   4934  CG1 VAL C  50      10.863  17.025 -47.412  1.00159.61           C  
ATOM   4935  CG2 VAL C  50      12.145  18.061 -45.524  1.00161.51           C  
ATOM   4936  N   GLU C  51      11.621  13.419 -46.352  1.00163.50           N  
ATOM   4937  CA  GLU C  51      11.128  12.176 -46.975  1.00164.59           C  
ATOM   4938  C   GLU C  51      10.308  11.336 -45.990  1.00165.70           C  
ATOM   4939  O   GLU C  51       9.288  10.750 -46.368  1.00169.15           O  
ATOM   4940  CB  GLU C  51      12.275  11.347 -47.584  1.00164.94           C  
ATOM   4941  CG  GLU C  51      13.306  10.765 -46.605  1.00164.82           C  
ATOM   4942  CD  GLU C  51      13.023   9.327 -46.161  1.00163.91           C  
ATOM   4943  OE1 GLU C  51      12.369   8.564 -46.905  1.00163.33           O  
ATOM   4944  OE2 GLU C  51      13.482   8.952 -45.061  1.00161.72           O  
ATOM   4945  N   ASN C  52      10.754  11.287 -44.734  1.00164.84           N  
ATOM   4946  CA  ASN C  52      10.017  10.609 -43.658  1.00164.79           C  
ATOM   4947  C   ASN C  52       8.732  11.361 -43.283  1.00164.69           C  
ATOM   4948  O   ASN C  52       7.765  10.753 -42.821  1.00165.26           O  
ATOM   4949  CB  ASN C  52      10.919  10.449 -42.421  1.00162.64           C  
ATOM   4950  CG  ASN C  52      10.349   9.489 -41.381  1.00160.17           C  
ATOM   4951  OD1 ASN C  52       9.619   8.555 -41.708  1.00160.39           O  
ATOM   4952  ND2 ASN C  52      10.701   9.713 -40.120  1.00156.97           N  
ATOM   4953  N   LYS C  53       8.732  12.678 -43.493  1.00164.37           N  
ATOM   4954  CA  LYS C  53       7.589  13.538 -43.173  1.00162.71           C  
ATOM   4955  C   LYS C  53       6.560  13.581 -44.305  1.00165.35           C  
ATOM   4956  O   LYS C  53       5.356  13.647 -44.052  1.00172.70           O  
ATOM   4957  CB  LYS C  53       8.075  14.954 -42.865  1.00159.34           C  
ATOM   4958  CG  LYS C  53       7.101  15.785 -42.063  1.00157.84           C  
ATOM   4959  CD  LYS C  53       7.677  17.159 -41.759  1.00156.67           C  
ATOM   4960  CE  LYS C  53       7.125  17.721 -40.459  1.00155.96           C  
ATOM   4961  NZ  LYS C  53       7.791  18.995 -40.078  1.00154.85           N  
ATOM   4962  N   THR C  54       7.036  13.560 -45.548  1.00167.26           N  
ATOM   4963  CA  THR C  54       6.150  13.499 -46.709  1.00168.88           C  
ATOM   4964  C   THR C  54       5.337  12.204 -46.707  1.00172.47           C  
ATOM   4965  O   THR C  54       4.142  12.223 -47.003  1.00179.91           O  
ATOM   4966  CB  THR C  54       6.937  13.594 -48.037  1.00168.55           C  
ATOM   4967  OG1 THR C  54       7.598  14.861 -48.119  1.00168.71           O  
ATOM   4968  CG2 THR C  54       6.008  13.449 -49.230  1.00167.49           C  
ATOM   4969  N   SER C  55       5.987  11.091 -46.362  1.00174.42           N  
ATOM   4970  CA  SER C  55       5.348   9.765 -46.388  1.00176.17           C  
ATOM   4971  C   SER C  55       4.372   9.489 -45.226  1.00181.47           C  
ATOM   4972  O   SER C  55       3.558   8.565 -45.313  1.00180.26           O  
ATOM   4973  CB  SER C  55       6.411   8.660 -46.452  1.00173.51           C  
ATOM   4974  OG  SER C  55       7.447   8.883 -45.512  1.00170.32           O  
ATOM   4975  N   GLU C  56       4.460  10.271 -44.147  1.00187.45           N  
ATOM   4976  CA  GLU C  56       3.496  10.180 -43.036  1.00189.58           C  
ATOM   4977  C   GLU C  56       2.207  10.933 -43.362  1.00191.84           C  
ATOM   4978  O   GLU C  56       1.108  10.383 -43.235  1.00195.81           O  
ATOM   4979  CB  GLU C  56       4.097  10.721 -41.729  1.00189.49           C  
ATOM   4980  CG  GLU C  56       3.052  11.112 -40.668  1.00189.18           C  
ATOM   4981  CD  GLU C  56       3.626  11.270 -39.270  1.00188.77           C  
ATOM   4982  OE1 GLU C  56       4.749  10.786 -39.008  1.00188.00           O  
ATOM   4983  OE2 GLU C  56       2.938  11.879 -38.423  1.00188.64           O  
ATOM   4984  N   VAL C  57       2.354  12.195 -43.770  1.00190.71           N  
ATOM   4985  CA  VAL C  57       1.210  13.050 -44.119  1.00194.51           C  
ATOM   4986  C   VAL C  57       0.437  12.502 -45.342  1.00197.57           C  
ATOM   4987  O   VAL C  57      -0.745  12.808 -45.528  1.00200.59           O  
ATOM   4988  CB  VAL C  57       1.660  14.527 -44.342  1.00192.63           C  
ATOM   4989  CG1 VAL C  57       0.489  15.403 -44.754  1.00192.50           C  
ATOM   4990  CG2 VAL C  57       2.313  15.088 -43.078  1.00189.39           C  
ATOM   4991  N   LYS C  58       1.108  11.690 -46.161  1.00196.76           N  
ATOM   4992  CA  LYS C  58       0.449  10.912 -47.223  1.00200.21           C  
ATOM   4993  C   LYS C  58      -0.483   9.834 -46.645  1.00201.31           C  
ATOM   4994  O   LYS C  58      -1.547   9.562 -47.210  1.00203.07           O  
ATOM   4995  CB  LYS C  58       1.503  10.303 -48.172  1.00201.05           C  
ATOM   4996  CG  LYS C  58       1.128   8.984 -48.871  1.00202.22           C  
ATOM   4997  CD  LYS C  58       1.617   7.762 -48.086  1.00203.66           C  
ATOM   4998  CE  LYS C  58       3.099   7.494 -48.322  1.00204.67           C  
ATOM   4999  NZ  LYS C  58       3.326   6.696 -49.555  1.00205.88           N  
ATOM   5000  N   GLN C  59      -0.081   9.227 -45.527  1.00200.76           N  
ATOM   5001  CA  GLN C  59      -0.903   8.215 -44.859  1.00200.54           C  
ATOM   5002  C   GLN C  59      -2.089   8.869 -44.155  1.00200.49           C  
ATOM   5003  O   GLN C  59      -3.093   8.209 -43.882  1.00203.44           O  
ATOM   5004  CB  GLN C  59      -0.075   7.400 -43.863  1.00199.07           C  
ATOM   5005  CG  GLN C  59      -0.770   6.131 -43.392  1.00197.64           C  
ATOM   5006  CD  GLN C  59       0.118   5.252 -42.539  1.00197.45           C  
ATOM   5007  OE1 GLN C  59       1.342   5.261 -42.673  1.00197.16           O  
ATOM   5008  NE2 GLN C  59      -0.500   4.476 -41.659  1.00197.84           N  
ATOM   5009  N   LEU C  60      -1.966  10.164 -43.863  1.00198.81           N  
ATOM   5010  CA  LEU C  60      -3.100  10.955 -43.379  1.00199.56           C  
ATOM   5011  C   LEU C  60      -4.079  11.272 -44.518  1.00202.20           C  
ATOM   5012  O   LEU C  60      -5.287  11.163 -44.330  1.00206.44           O  
ATOM   5013  CB  LEU C  60      -2.642  12.257 -42.703  1.00197.38           C  
ATOM   5014  CG  LEU C  60      -1.865  12.168 -41.384  1.00195.97           C  
ATOM   5015  CD1 LEU C  60      -1.813  13.542 -40.715  1.00194.58           C  
ATOM   5016  CD2 LEU C  60      -2.465  11.137 -40.434  1.00193.87           C  
ATOM   5017  N   ILE C  61      -3.565  11.663 -45.687  1.00203.05           N  
ATOM   5018  CA  ILE C  61      -4.411  11.903 -46.875  1.00203.54           C  
ATOM   5019  C   ILE C  61      -5.117  10.626 -47.350  1.00205.20           C  
ATOM   5020  O   ILE C  61      -6.300  10.655 -47.708  1.00207.70           O  
ATOM   5021  CB  ILE C  61      -3.600  12.506 -48.063  1.00202.09           C  
ATOM   5022  CG1 ILE C  61      -3.610  14.036 -48.003  1.00200.95           C  
ATOM   5023  CG2 ILE C  61      -4.166  12.044 -49.409  1.00201.33           C  
ATOM   5024  CD1 ILE C  61      -2.884  14.699 -49.158  1.00199.69           C  
ATOM   5025  N   LYS C  62      -4.382   9.516 -47.350  1.00204.93           N  
ATOM   5026  CA  LYS C  62      -4.917   8.218 -47.763  1.00204.22           C  
ATOM   5027  C   LYS C  62      -5.912   7.644 -46.751  1.00207.08           C  
ATOM   5028  O   LYS C  62      -6.926   7.059 -47.139  1.00209.20           O  
ATOM   5029  CB  LYS C  62      -3.772   7.228 -47.974  1.00201.26           C  
ATOM   5030  CG  LYS C  62      -4.217   5.880 -48.499  1.00199.22           C  
ATOM   5031  CD  LYS C  62      -3.052   5.103 -49.071  1.00197.75           C  
ATOM   5032  CE  LYS C  62      -3.524   3.853 -49.787  1.00196.58           C  
ATOM   5033  NZ  LYS C  62      -2.481   3.312 -50.699  1.00195.09           N  
ATOM   5034  N   ALA C  63      -5.612   7.805 -45.462  1.00208.65           N  
ATOM   5035  CA  ALA C  63      -6.475   7.306 -44.382  1.00210.21           C  
ATOM   5036  C   ALA C  63      -7.699   8.201 -44.118  1.00211.55           C  
ATOM   5037  O   ALA C  63      -8.766   7.693 -43.764  1.00214.28           O  
ATOM   5038  CB  ALA C  63      -5.665   7.120 -43.101  1.00209.19           C  
ATOM   5039  N   ILE C  64      -7.541   9.519 -44.274  1.00211.54           N  
ATOM   5040  CA  ILE C  64      -8.662  10.472 -44.136  1.00211.62           C  
ATOM   5041  C   ILE C  64      -9.672  10.325 -45.278  1.00213.61           C  
ATOM   5042  O   ILE C  64     -10.874  10.510 -45.072  1.00217.67           O  
ATOM   5043  CB  ILE C  64      -8.180  11.956 -44.078  1.00209.36           C  
ATOM   5044  CG1 ILE C  64      -7.608  12.291 -42.695  1.00208.07           C  
ATOM   5045  CG2 ILE C  64      -9.322  12.921 -44.401  1.00207.67           C  
ATOM   5046  CD1 ILE C  64      -8.657  12.593 -41.638  1.00206.52           C  
ATOM   5047  N   GLN C  65      -9.182   9.998 -46.474  1.00213.49           N  
ATOM   5048  CA  GLN C  65     -10.052   9.807 -47.638  1.00215.04           C  
ATOM   5049  C   GLN C  65     -10.693   8.408 -47.692  1.00215.68           C  
ATOM   5050  O   GLN C  65     -11.720   8.230 -48.351  1.00216.26           O  
ATOM   5051  CB  GLN C  65      -9.285  10.102 -48.931  1.00215.78           C  
ATOM   5052  CG  GLN C  65     -10.180  10.295 -50.152  1.00217.07           C  
ATOM   5053  CD  GLN C  65      -9.699  11.410 -51.068  1.00218.02           C  
ATOM   5054  OE1 GLN C  65      -9.709  12.585 -50.690  1.00216.71           O  
ATOM   5055  NE2 GLN C  65      -9.289  11.049 -52.280  1.00220.11           N  
ATOM   5056  N   LEU C  66     -10.092   7.428 -47.011  1.00215.29           N  
ATOM   5057  CA  LEU C  66     -10.708   6.098 -46.839  1.00215.67           C  
ATOM   5058  C   LEU C  66     -11.770   6.108 -45.721  1.00217.65           C  
ATOM   5059  O   LEU C  66     -12.671   5.267 -45.711  1.00218.29           O  
ATOM   5060  CB  LEU C  66      -9.636   5.034 -46.552  1.00213.37           C  
ATOM   5061  CG  LEU C  66     -10.049   3.556 -46.611  1.00210.99           C  
ATOM   5062  CD1 LEU C  66     -10.455   3.158 -48.021  1.00209.52           C  
ATOM   5063  CD2 LEU C  66      -8.920   2.661 -46.112  1.00208.61           C  
ATOM   5064  N   THR C  67     -11.650   7.056 -44.788  1.00218.61           N  
ATOM   5065  CA  THR C  67     -12.646   7.271 -43.725  1.00219.30           C  
ATOM   5066  C   THR C  67     -13.840   8.122 -44.201  1.00221.46           C  
ATOM   5067  O   THR C  67     -14.950   7.995 -43.676  1.00221.17           O  
ATOM   5068  CB  THR C  67     -11.996   7.957 -42.491  1.00217.79           C  
ATOM   5069  OG1 THR C  67     -10.945   7.128 -41.976  1.00216.03           O  
ATOM   5070  CG2 THR C  67     -13.026   8.213 -41.386  1.00216.21           C  
ATOM   5071  N   TYR C  68     -13.600   8.981 -45.196  1.00223.61           N  
ATOM   5072  CA  TYR C  68     -14.606   9.932 -45.710  1.00226.19           C  
ATOM   5073  C   TYR C  68     -15.672   9.331 -46.676  1.00229.42           C  
ATOM   5074  O   TYR C  68     -16.762   9.897 -46.787  1.00232.60           O  
ATOM   5075  CB  TYR C  68     -13.883  11.141 -46.338  1.00225.13           C  
ATOM   5076  CG  TYR C  68     -14.772  12.164 -47.012  1.00223.22           C  
ATOM   5077  CD1 TYR C  68     -15.694  12.910 -46.282  1.00222.97           C  
ATOM   5078  CD2 TYR C  68     -14.672  12.399 -48.382  1.00221.47           C  
ATOM   5079  CE1 TYR C  68     -16.505  13.849 -46.906  1.00223.14           C  
ATOM   5080  CE2 TYR C  68     -15.472  13.331 -49.011  1.00220.67           C  
ATOM   5081  CZ  TYR C  68     -16.385  14.053 -48.271  1.00222.12           C  
ATOM   5082  OH  TYR C  68     -17.177  14.979 -48.904  1.00222.95           O  
ATOM   5083  N   ASN C  69     -15.358   8.233 -47.384  1.00231.16           N  
ATOM   5084  CA  ASN C  69     -16.382   7.333 -48.034  1.00232.24           C  
ATOM   5085  C   ASN C  69     -17.010   7.684 -49.432  1.00233.00           C  
ATOM   5086  O   ASN C  69     -18.310   7.698 -49.517  1.00234.20           O  
ATOM   5087  CB  ASN C  69     -17.613   7.147 -47.097  1.00232.10           C  
ATOM   5088  CG  ASN C  69     -17.432   6.066 -46.046  1.00231.72           C  
ATOM   5089  OD1 ASN C  69     -18.396   5.693 -45.369  1.00230.82           O  
ATOM   5090  ND2 ASN C  69     -16.215   5.552 -45.906  1.00231.93           N  
ATOM   5091  N   PRO C  70     -16.198   7.655 -50.534  1.00232.55           N  
ATOM   5092  CA  PRO C  70     -16.599   8.300 -51.796  1.00231.77           C  
ATOM   5093  C   PRO C  70     -18.112   8.180 -52.086  1.00230.74           C  
ATOM   5094  O   PRO C  70     -18.541   7.300 -52.837  1.00231.31           O  
ATOM   5095  CB  PRO C  70     -15.771   7.558 -52.864  1.00231.82           C  
ATOM   5096  CG  PRO C  70     -15.285   6.297 -52.215  1.00231.72           C  
ATOM   5097  CD  PRO C  70     -15.702   6.290 -50.776  1.00232.43           C  
ATOM   5098  N   ASP C  71     -18.894   9.061 -51.458  1.00228.96           N  
ATOM   5099  CA  ASP C  71     -20.364   9.126 -51.591  1.00227.06           C  
ATOM   5100  C   ASP C  71     -21.110   7.782 -51.794  1.00224.32           C  
ATOM   5101  O   ASP C  71     -21.886   7.627 -52.743  1.00225.77           O  
ATOM   5102  CB  ASP C  71     -20.751  10.162 -52.667  1.00226.93           C  
ATOM   5103  CG  ASP C  71     -19.950  10.016 -53.956  1.00226.58           C  
ATOM   5104  OD1 ASP C  71     -19.115  10.903 -54.241  1.00225.33           O  
ATOM   5105  OD2 ASP C  71     -20.153   9.023 -54.685  1.00227.27           O  
ATOM   5106  N   GLU C  72     -20.886   6.834 -50.879  1.00218.84           N  
ATOM   5107  CA  GLU C  72     -21.552   5.519 -50.908  1.00212.82           C  
ATOM   5108  C   GLU C  72     -22.768   5.484 -49.972  1.00210.73           C  
ATOM   5109  O   GLU C  72     -23.816   4.942 -50.330  1.00210.76           O  
ATOM   5110  CB  GLU C  72     -20.559   4.408 -50.523  1.00209.32           C  
ATOM   5111  CG  GLU C  72     -20.795   3.051 -51.208  1.00206.36           C  
ATOM   5112  CD  GLU C  72     -22.020   2.303 -50.695  1.00204.56           C  
ATOM   5113  OE1 GLU C  72     -22.324   2.386 -49.487  1.00203.05           O  
ATOM   5114  OE2 GLU C  72     -22.674   1.613 -51.505  1.00202.83           O  
ATOM   5115  N   SER C  73     -22.618   6.061 -48.778  1.00207.89           N  
ATOM   5116  CA  SER C  73     -23.660   6.022 -47.745  1.00205.15           C  
ATOM   5117  C   SER C  73     -24.848   6.946 -48.051  1.00205.17           C  
ATOM   5118  O   SER C  73     -24.694   7.980 -48.707  1.00205.50           O  
ATOM   5119  CB  SER C  73     -23.066   6.393 -46.381  1.00202.23           C  
ATOM   5120  OG  SER C  73     -21.980   5.546 -46.044  1.00199.01           O  
ATOM   5121  N   SER C  74     -26.028   6.553 -47.567  1.00203.50           N  
ATOM   5122  CA  SER C  74     -27.250   7.355 -47.674  1.00200.30           C  
ATOM   5123  C   SER C  74     -27.777   7.633 -46.267  1.00199.11           C  
ATOM   5124  O   SER C  74     -28.847   7.158 -45.881  1.00198.07           O  
ATOM   5125  CB  SER C  74     -28.302   6.623 -48.513  1.00199.16           C  
ATOM   5126  OG  SER C  74     -27.866   6.466 -49.853  1.00197.72           O  
ATOM   5127  N   LYS C  75     -27.002   8.417 -45.518  1.00198.34           N  
ATOM   5128  CA  LYS C  75     -27.211   8.649 -44.079  1.00197.42           C  
ATOM   5129  C   LYS C  75     -28.691   8.712 -43.658  1.00194.85           C  
ATOM   5130  O   LYS C  75     -29.437   9.571 -44.138  1.00192.31           O  
ATOM   5131  CB  LYS C  75     -26.492   9.943 -43.655  1.00196.99           C  
ATOM   5132  CG  LYS C  75     -26.398  10.211 -42.141  1.00194.75           C  
ATOM   5133  CD  LYS C  75     -25.104   9.681 -41.509  1.00192.10           C  
ATOM   5134  CE  LYS C  75     -25.220   8.232 -41.058  1.00190.73           C  
ATOM   5135  NZ  LYS C  75     -26.299   8.040 -40.044  1.00189.07           N  
ATOM   5136  N   PRO C  76     -29.121   7.787 -42.772  1.00191.67           N  
ATOM   5137  CA  PRO C  76     -30.451   7.881 -42.165  1.00188.40           C  
ATOM   5138  C   PRO C  76     -30.488   8.893 -41.016  1.00183.48           C  
ATOM   5139  O   PRO C  76     -29.476   9.093 -40.336  1.00186.77           O  
ATOM   5140  CB  PRO C  76     -30.700   6.463 -41.642  1.00188.92           C  
ATOM   5141  CG  PRO C  76     -29.353   5.919 -41.373  1.00189.61           C  
ATOM   5142  CD  PRO C  76     -28.436   6.534 -42.391  1.00190.81           C  
ATOM   5143  N   ASN C  77     -31.650   9.514 -40.815  1.00174.55           N  
ATOM   5144  CA  ASN C  77     -31.847  10.565 -39.802  1.00166.15           C  
ATOM   5145  C   ASN C  77     -30.930  11.787 -39.964  1.00161.56           C  
ATOM   5146  O   ASN C  77     -30.628  12.486 -38.990  1.00157.96           O  
ATOM   5147  CB  ASN C  77     -31.738   9.988 -38.383  1.00161.77           C  
ATOM   5148  CG  ASN C  77     -32.872   9.045 -38.051  1.00157.06           C  
ATOM   5149  OD1 ASN C  77     -33.465   8.429 -38.938  1.00152.95           O  
ATOM   5150  ND2 ASN C  77     -33.185   8.930 -36.766  1.00154.53           N  
ATOM   5151  N   MET C  78     -30.509  12.049 -41.200  1.00156.44           N  
ATOM   5152  CA  MET C  78     -29.715  13.234 -41.508  1.00153.32           C  
ATOM   5153  C   MET C  78     -30.625  14.463 -41.604  1.00153.18           C  
ATOM   5154  O   MET C  78     -31.846  14.335 -41.702  1.00158.45           O  
ATOM   5155  CB  MET C  78     -28.914  13.029 -42.803  1.00149.34           C  
ATOM   5156  CG  MET C  78     -29.742  12.941 -44.086  1.00145.50           C  
ATOM   5157  SD  MET C  78     -28.842  12.248 -45.492  1.00140.65           S  
ATOM   5158  CE  MET C  78     -27.183  12.862 -45.200  1.00138.74           C  
ATOM   5159  N   ILE C  79     -30.020  15.647 -41.559  1.00151.28           N  
ATOM   5160  CA  ILE C  79     -30.745  16.923 -41.679  1.00152.79           C  
ATOM   5161  C   ILE C  79     -31.759  16.962 -42.836  1.00156.47           C  
ATOM   5162  O   ILE C  79     -32.819  17.584 -42.720  1.00157.53           O  
ATOM   5163  CB  ILE C  79     -29.752  18.109 -41.822  1.00152.71           C  
ATOM   5164  CG1 ILE C  79     -30.472  19.399 -42.234  1.00152.85           C  
ATOM   5165  CG2 ILE C  79     -28.668  17.781 -42.832  1.00154.01           C  
ATOM   5166  CD1 ILE C  79     -29.577  20.609 -42.234  1.00152.55           C  
ATOM   5167  N   ASP C  80     -31.420  16.318 -43.950  1.00160.96           N  
ATOM   5168  CA  ASP C  80     -32.325  16.216 -45.099  1.00164.06           C  
ATOM   5169  C   ASP C  80     -33.553  15.343 -44.814  1.00164.84           C  
ATOM   5170  O   ASP C  80     -34.662  15.675 -45.243  1.00165.07           O  
ATOM   5171  CB  ASP C  80     -31.584  15.666 -46.326  1.00167.22           C  
ATOM   5172  CG  ASP C  80     -30.619  16.676 -46.945  1.00170.89           C  
ATOM   5173  OD1 ASP C  80     -30.641  17.864 -46.553  1.00175.56           O  
ATOM   5174  OD2 ASP C  80     -29.837  16.280 -47.838  1.00169.55           O  
ATOM   5175  N   ALA C  81     -33.352  14.230 -44.106  1.00164.43           N  
ATOM   5176  CA  ALA C  81     -34.450  13.319 -43.750  1.00164.05           C  
ATOM   5177  C   ALA C  81     -35.412  13.983 -42.770  1.00162.62           C  
ATOM   5178  O   ALA C  81     -36.576  13.589 -42.661  1.00159.86           O  
ATOM   5179  CB  ALA C  81     -33.904  12.024 -43.158  1.00164.62           C  
ATOM   5180  N   ALA C  82     -34.906  14.981 -42.051  1.00161.78           N  
ATOM   5181  CA  ALA C  82     -35.738  15.834 -41.211  1.00161.10           C  
ATOM   5182  C   ALA C  82     -36.554  16.797 -42.077  1.00161.34           C  
ATOM   5183  O   ALA C  82     -37.775  16.886 -41.933  1.00162.37           O  
ATOM   5184  CB  ALA C  82     -34.876  16.604 -40.226  1.00159.41           C  
ATOM   5185  N   THR C  83     -35.876  17.499 -42.987  1.00161.65           N  
ATOM   5186  CA  THR C  83     -36.529  18.476 -43.873  1.00161.96           C  
ATOM   5187  C   THR C  83     -37.565  17.850 -44.833  1.00164.11           C  
ATOM   5188  O   THR C  83     -38.412  18.565 -45.384  1.00161.84           O  
ATOM   5189  CB  THR C  83     -35.483  19.281 -44.689  1.00159.79           C  
ATOM   5190  OG1 THR C  83     -34.512  19.855 -43.802  1.00157.31           O  
ATOM   5191  CG2 THR C  83     -36.153  20.391 -45.481  1.00157.42           C  
ATOM   5192  N   LEU C  84     -37.490  16.530 -45.036  1.00166.57           N  
ATOM   5193  CA  LEU C  84     -38.526  15.786 -45.779  1.00168.58           C  
ATOM   5194  C   LEU C  84     -39.820  15.693 -44.974  1.00168.47           C  
ATOM   5195  O   LEU C  84     -40.913  15.863 -45.522  1.00170.67           O  
ATOM   5196  CB  LEU C  84     -38.045  14.368 -46.144  1.00168.71           C  
ATOM   5197  CG  LEU C  84     -39.038  13.361 -46.770  1.00167.40           C  
ATOM   5198  CD1 LEU C  84     -39.863  12.621 -45.711  1.00166.10           C  
ATOM   5199  CD2 LEU C  84     -39.961  14.010 -47.809  1.00165.05           C  
ATOM   5200  N   LYS C  85     -39.690  15.406 -43.680  1.00164.01           N  
ATOM   5201  CA  LYS C  85     -40.846  15.315 -42.795  1.00159.28           C  
ATOM   5202  C   LYS C  85     -41.439  16.709 -42.556  1.00160.48           C  
ATOM   5203  O   LYS C  85     -42.615  16.833 -42.232  1.00158.99           O  
ATOM   5204  CB  LYS C  85     -40.470  14.617 -41.482  1.00156.21           C  
ATOM   5205  CG  LYS C  85     -40.024  13.167 -41.685  1.00155.44           C  
ATOM   5206  CD  LYS C  85     -39.608  12.481 -40.388  1.00154.82           C  
ATOM   5207  CE  LYS C  85     -38.951  11.131 -40.672  1.00153.54           C  
ATOM   5208  NZ  LYS C  85     -38.633  10.364 -39.436  1.00151.75           N  
ATOM   5209  N   SER C  86     -40.633  17.755 -42.745  1.00161.72           N  
ATOM   5210  CA  SER C  86     -41.138  19.140 -42.704  1.00160.28           C  
ATOM   5211  C   SER C  86     -42.249  19.361 -43.729  1.00158.38           C  
ATOM   5212  O   SER C  86     -43.319  19.842 -43.376  1.00153.61           O  
ATOM   5213  CB  SER C  86     -40.016  20.168 -42.933  1.00161.75           C  
ATOM   5214  OG  SER C  86     -39.629  20.798 -41.722  1.00161.68           O  
ATOM   5215  N   ARG C  87     -41.981  18.999 -44.985  1.00160.48           N  
ATOM   5216  CA  ARG C  87     -42.935  19.183 -46.095  1.00162.11           C  
ATOM   5217  C   ARG C  87     -44.286  18.477 -45.897  1.00160.42           C  
ATOM   5218  O   ARG C  87     -45.338  19.094 -46.072  1.00157.16           O  
ATOM   5219  CB  ARG C  87     -42.323  18.715 -47.428  1.00163.12           C  
ATOM   5220  CG  ARG C  87     -41.391  19.717 -48.108  1.00163.05           C  
ATOM   5221  CD  ARG C  87     -41.211  19.365 -49.586  1.00163.64           C  
ATOM   5222  NE  ARG C  87     -40.201  20.193 -50.254  1.00164.75           N  
ATOM   5223  CZ  ARG C  87     -39.718  19.972 -51.479  1.00165.52           C  
ATOM   5224  NH1 ARG C  87     -40.131  18.931 -52.200  1.00166.67           N  
ATOM   5225  NH2 ARG C  87     -38.800  20.791 -51.987  1.00164.58           N  
ATOM   5226  N   LYS C  88     -44.252  17.188 -45.555  1.00158.96           N  
ATOM   5227  CA  LYS C  88     -45.484  16.394 -45.402  1.00156.42           C  
ATOM   5228  C   LYS C  88     -46.192  16.639 -44.064  1.00153.38           C  
ATOM   5229  O   LYS C  88     -47.424  16.645 -44.007  1.00147.89           O  
ATOM   5230  CB  LYS C  88     -45.224  14.891 -45.614  1.00156.45           C  
ATOM   5231  CG  LYS C  88     -44.162  14.256 -44.710  1.00156.83           C  
ATOM   5232  CD  LYS C  88     -44.262  12.731 -44.700  1.00155.57           C  
ATOM   5233  CE  LYS C  88     -44.058  12.133 -46.089  1.00154.91           C  
ATOM   5234  NZ  LYS C  88     -44.078  10.648 -46.071  1.00154.39           N  
ATOM   5235  N   MET C  89     -45.420  16.846 -42.998  1.00152.33           N  
ATOM   5236  CA  MET C  89     -45.993  17.196 -41.696  1.00150.45           C  
ATOM   5237  C   MET C  89     -46.334  18.692 -41.645  1.00147.84           C  
ATOM   5238  O   MET C  89     -47.003  19.144 -40.720  1.00146.09           O  
ATOM   5239  CB  MET C  89     -45.060  16.796 -40.543  1.00151.96           C  
ATOM   5240  CG  MET C  89     -44.581  15.323 -40.572  1.00153.44           C  
ATOM   5241  SD  MET C  89     -45.884  14.065 -40.548  1.00153.86           S  
ATOM   5242  CE  MET C  89     -44.956  12.576 -40.930  1.00151.74           C  
ATOM   5243  N   LEU C  90     -45.858  19.450 -42.632  1.00148.79           N  
ATOM   5244  CA  LEU C  90     -46.399  20.781 -42.930  1.00150.11           C  
ATOM   5245  C   LEU C  90     -47.741  20.636 -43.636  1.00148.96           C  
ATOM   5246  O   LEU C  90     -48.708  21.314 -43.293  1.00146.54           O  
ATOM   5247  CB  LEU C  90     -45.443  21.579 -43.829  1.00153.93           C  
ATOM   5248  CG  LEU C  90     -45.975  22.726 -44.703  1.00156.09           C  
ATOM   5249  CD1 LEU C  90     -46.926  23.653 -43.955  1.00156.37           C  
ATOM   5250  CD2 LEU C  90     -44.809  23.513 -45.306  1.00156.25           C  
ATOM   5251  N   GLU C  91     -47.786  19.763 -44.639  1.00149.05           N  
ATOM   5252  CA  GLU C  91     -48.996  19.561 -45.438  1.00146.68           C  
ATOM   5253  C   GLU C  91     -50.177  19.167 -44.554  1.00141.94           C  
ATOM   5254  O   GLU C  91     -51.262  19.730 -44.677  1.00137.16           O  
ATOM   5255  CB  GLU C  91     -48.760  18.490 -46.515  1.00148.45           C  
ATOM   5256  CG  GLU C  91     -49.828  18.432 -47.620  1.00149.04           C  
ATOM   5257  CD  GLU C  91     -49.635  19.475 -48.722  1.00149.23           C  
ATOM   5258  OE1 GLU C  91     -48.955  20.497 -48.485  1.00151.34           O  
ATOM   5259  OE2 GLU C  91     -50.178  19.268 -49.831  1.00145.15           O  
ATOM   5260  N   GLU C  92     -49.950  18.221 -43.646  1.00139.71           N  
ATOM   5261  CA  GLU C  92     -51.004  17.743 -42.746  1.00135.85           C  
ATOM   5262  C   GLU C  92     -51.499  18.779 -41.735  1.00137.01           C  
ATOM   5263  O   GLU C  92     -52.535  18.573 -41.109  1.00141.13           O  
ATOM   5264  CB  GLU C  92     -50.552  16.476 -42.015  1.00132.59           C  
ATOM   5265  CG  GLU C  92     -50.802  15.213 -42.824  1.00132.72           C  
ATOM   5266  CD  GLU C  92     -49.843  14.085 -42.498  1.00132.78           C  
ATOM   5267  OE1 GLU C  92     -48.614  14.303 -42.564  1.00132.70           O  
ATOM   5268  OE2 GLU C  92     -50.318  12.969 -42.197  1.00131.87           O  
ATOM   5269  N   ILE C  93     -50.771  19.882 -41.573  1.00137.60           N  
ATOM   5270  CA  ILE C  93     -51.211  20.955 -40.684  1.00134.78           C  
ATOM   5271  C   ILE C  93     -52.395  21.745 -41.246  1.00133.15           C  
ATOM   5272  O   ILE C  93     -53.224  22.236 -40.480  1.00131.85           O  
ATOM   5273  CB  ILE C  93     -50.062  21.951 -40.365  1.00136.73           C  
ATOM   5274  CG1 ILE C  93     -50.311  22.664 -39.037  1.00137.69           C  
ATOM   5275  CG2 ILE C  93     -49.912  22.994 -41.467  1.00137.85           C  
ATOM   5276  CD1 ILE C  93     -50.470  21.733 -37.867  1.00140.65           C  
ATOM   5277  N   MET C  94     -52.481  21.872 -42.570  1.00133.17           N  
ATOM   5278  CA  MET C  94     -53.486  22.754 -43.174  1.00132.77           C  
ATOM   5279  C   MET C  94     -54.888  22.133 -43.256  1.00126.65           C  
ATOM   5280  O   MET C  94     -55.884  22.858 -43.222  1.00120.62           O  
ATOM   5281  CB  MET C  94     -53.025  23.276 -44.547  1.00138.40           C  
ATOM   5282  CG  MET C  94     -53.086  22.291 -45.709  1.00141.39           C  
ATOM   5283  SD  MET C  94     -52.875  23.134 -47.295  1.00144.24           S  
ATOM   5284  CE  MET C  94     -54.474  23.918 -47.504  1.00140.58           C  
ATOM   5285  N   LYS C  95     -54.967  20.807 -43.362  1.00123.50           N  
ATOM   5286  CA  LYS C  95     -56.259  20.110 -43.343  1.00122.54           C  
ATOM   5287  C   LYS C  95     -56.829  20.042 -41.922  1.00119.30           C  
ATOM   5288  O   LYS C  95     -58.036  19.852 -41.736  1.00111.39           O  
ATOM   5289  CB  LYS C  95     -56.132  18.702 -43.940  1.00124.56           C  
ATOM   5290  CG  LYS C  95     -55.476  17.673 -43.025  1.00127.49           C  
ATOM   5291  CD  LYS C  95     -55.343  16.308 -43.683  1.00130.62           C  
ATOM   5292  CE  LYS C  95     -54.329  16.315 -44.817  1.00132.20           C  
ATOM   5293  NZ  LYS C  95     -53.942  14.938 -45.230  1.00133.33           N  
ATOM   5294  N   TYR C  96     -55.947  20.190 -40.932  1.00117.96           N  
ATOM   5295  CA  TYR C  96     -56.323  20.167 -39.518  1.00116.72           C  
ATOM   5296  C   TYR C  96     -56.953  21.499 -39.105  1.00118.67           C  
ATOM   5297  O   TYR C  96     -58.011  21.516 -38.473  1.00119.44           O  
ATOM   5298  CB  TYR C  96     -55.098  19.842 -38.640  1.00113.57           C  
ATOM   5299  CG  TYR C  96     -54.567  18.413 -38.761  1.00110.98           C  
ATOM   5300  CD1 TYR C  96     -55.142  17.490 -39.644  1.00110.24           C  
ATOM   5301  CD2 TYR C  96     -53.470  17.994 -38.009  1.00108.57           C  
ATOM   5302  CE1 TYR C  96     -54.654  16.201 -39.758  1.00108.11           C  
ATOM   5303  CE2 TYR C  96     -52.974  16.698 -38.121  1.00108.25           C  
ATOM   5304  CZ  TYR C  96     -53.573  15.813 -38.998  1.00108.05           C  
ATOM   5305  OH  TYR C  96     -53.094  14.536 -39.124  1.00110.45           O  
ATOM   5306  N   GLU C  97     -56.318  22.609 -39.473  1.00122.13           N  
ATOM   5307  CA  GLU C  97     -56.877  23.940 -39.201  1.00124.47           C  
ATOM   5308  C   GLU C  97     -58.126  24.262 -40.042  1.00120.17           C  
ATOM   5309  O   GLU C  97     -58.751  25.307 -39.845  1.00118.05           O  
ATOM   5310  CB  GLU C  97     -55.820  25.015 -39.434  1.00132.17           C  
ATOM   5311  CG  GLU C  97     -55.469  25.204 -40.902  1.00141.44           C  
ATOM   5312  CD  GLU C  97     -54.413  26.262 -41.123  1.00149.33           C  
ATOM   5313  OE1 GLU C  97     -53.557  26.456 -40.229  1.00153.22           O  
ATOM   5314  OE2 GLU C  97     -54.444  26.899 -42.200  1.00155.29           O  
ATOM   5315  N   ALA C  98     -58.458  23.391 -40.996  1.00115.80           N  
ATOM   5316  CA  ALA C  98     -59.704  23.487 -41.763  1.00110.96           C  
ATOM   5317  C   ALA C  98     -60.808  22.660 -41.108  1.00108.80           C  
ATOM   5318  O   ALA C  98     -61.967  23.082 -41.082  1.00105.38           O  
ATOM   5319  CB  ALA C  98     -59.482  23.018 -43.187  1.00110.49           C  
ATOM   5320  N   SER C  99     -60.437  21.481 -40.597  1.00108.77           N  
ATOM   5321  CA  SER C  99     -61.355  20.609 -39.845  1.00104.90           C  
ATOM   5322  C   SER C  99     -61.814  21.241 -38.522  1.00105.45           C  
ATOM   5323  O   SER C  99     -62.923  20.969 -38.059  1.00101.90           O  
ATOM   5324  CB  SER C  99     -60.710  19.241 -39.576  1.00100.05           C  
ATOM   5325  OG  SER C  99     -60.424  18.555 -40.785  1.00 96.89           O  
ATOM   5326  N   ILE C 100     -60.964  22.076 -37.921  1.00109.52           N  
ATOM   5327  CA  ILE C 100     -61.342  22.881 -36.748  1.00109.04           C  
ATOM   5328  C   ILE C 100     -62.628  23.680 -36.984  1.00107.41           C  
ATOM   5329  O   ILE C 100     -63.452  23.816 -36.080  1.00103.56           O  
ATOM   5330  CB  ILE C 100     -60.206  23.869 -36.339  1.00111.49           C  
ATOM   5331  CG1 ILE C 100     -60.557  24.634 -35.054  1.00112.58           C  
ATOM   5332  CG2 ILE C 100     -59.928  24.867 -37.449  1.00112.32           C  
ATOM   5333  CD1 ILE C 100     -61.268  25.975 -35.277  1.00109.85           C  
ATOM   5334  N   LEU C 101     -62.793  24.190 -38.204  1.00108.00           N  
ATOM   5335  CA  LEU C 101     -63.930  25.049 -38.558  1.00109.11           C  
ATOM   5336  C   LEU C 101     -65.251  24.277 -38.670  1.00106.60           C  
ATOM   5337  O   LEU C 101     -66.326  24.858 -38.488  1.00103.33           O  
ATOM   5338  CB  LEU C 101     -63.654  25.781 -39.875  1.00109.59           C  
ATOM   5339  CG  LEU C 101     -62.244  26.351 -40.046  1.00111.75           C  
ATOM   5340  CD1 LEU C 101     -62.175  27.149 -41.330  1.00113.59           C  
ATOM   5341  CD2 LEU C 101     -61.833  27.196 -38.840  1.00110.38           C  
ATOM   5342  N   THR C 102     -65.167  22.980 -38.979  1.00102.26           N  
ATOM   5343  CA  THR C 102     -66.349  22.118 -39.052  1.00 96.74           C  
ATOM   5344  C   THR C 102     -66.756  21.666 -37.660  1.00 95.26           C  
ATOM   5345  O   THR C 102     -67.947  21.554 -37.352  1.00 95.18           O  
ATOM   5346  CB  THR C 102     -66.117  20.859 -39.914  1.00 94.75           C  
ATOM   5347  OG1 THR C 102     -65.118  20.029 -39.307  1.00 95.38           O  
ATOM   5348  CG2 THR C 102     -65.694  21.235 -41.328  1.00 94.87           C  
ATOM   5349  N   HIS C 103     -65.765  21.394 -36.818  1.00 94.83           N  
ATOM   5350  CA  HIS C 103     -66.047  21.024 -35.435  1.00 92.87           C  
ATOM   5351  C   HIS C 103     -66.605  22.220 -34.672  1.00 94.15           C  
ATOM   5352  O   HIS C 103     -67.498  22.065 -33.846  1.00 94.56           O  
ATOM   5353  CB  HIS C 103     -64.814  20.425 -34.748  1.00 88.29           C  
ATOM   5354  CG  HIS C 103     -64.465  19.053 -35.241  1.00 89.10           C  
ATOM   5355  ND1 HIS C 103     -65.405  18.189 -35.765  1.00 91.35           N  
ATOM   5356  CD2 HIS C 103     -63.285  18.390 -35.282  1.00 88.49           C  
ATOM   5357  CE1 HIS C 103     -64.818  17.058 -36.116  1.00 90.62           C  
ATOM   5358  NE2 HIS C 103     -63.532  17.153 -35.831  1.00 89.62           N  
ATOM   5359  N   ASP C 104     -66.103  23.414 -34.977  1.00 99.72           N  
ATOM   5360  CA  ASP C 104     -66.638  24.655 -34.404  1.00103.50           C  
ATOM   5361  C   ASP C 104     -68.123  24.859 -34.761  1.00 99.25           C  
ATOM   5362  O   ASP C 104     -68.924  25.267 -33.916  1.00 97.14           O  
ATOM   5363  CB  ASP C 104     -65.802  25.856 -34.873  1.00109.05           C  
ATOM   5364  CG  ASP C 104     -65.877  27.035 -33.920  1.00113.86           C  
ATOM   5365  OD1 ASP C 104     -66.998  27.427 -33.532  1.00116.99           O  
ATOM   5366  OD2 ASP C 104     -64.806  27.580 -33.569  1.00116.90           O  
ATOM   5367  N   SER C 105     -68.488  24.571 -36.007  1.00 94.36           N  
ATOM   5368  CA  SER C 105     -69.893  24.606 -36.417  1.00 89.30           C  
ATOM   5369  C   SER C 105     -70.669  23.342 -36.019  1.00 90.17           C  
ATOM   5370  O   SER C 105     -71.887  23.285 -36.206  1.00 92.88           O  
ATOM   5371  CB  SER C 105     -70.007  24.816 -37.924  1.00 89.79           C  
ATOM   5372  OG  SER C 105     -71.365  24.830 -38.331  1.00 85.20           O  
ATOM   5373  N   SER C 106     -69.974  22.327 -35.503  1.00 89.28           N  
ATOM   5374  CA  SER C 106     -70.634  21.160 -34.913  1.00 86.27           C  
ATOM   5375  C   SER C 106     -70.923  21.413 -33.434  1.00 88.93           C  
ATOM   5376  O   SER C 106     -71.951  20.994 -32.914  1.00 90.24           O  
ATOM   5377  CB  SER C 106     -69.775  19.904 -35.064  1.00 83.92           C  
ATOM   5378  OG  SER C 106     -70.391  18.780 -34.456  1.00 79.30           O  
ATOM   5379  N   ILE C 107     -70.006  22.097 -32.761  1.00 92.05           N  
ATOM   5380  CA  ILE C 107     -70.192  22.466 -31.353  1.00 92.44           C  
ATOM   5381  C   ILE C 107     -71.300  23.517 -31.199  1.00 94.11           C  
ATOM   5382  O   ILE C 107     -72.161  23.393 -30.328  1.00 92.28           O  
ATOM   5383  CB  ILE C 107     -68.857  22.966 -30.718  1.00 89.81           C  
ATOM   5384  CG1 ILE C 107     -68.051  21.781 -30.163  1.00 87.44           C  
ATOM   5385  CG2 ILE C 107     -69.108  23.979 -29.597  1.00 85.63           C  
ATOM   5386  CD1 ILE C 107     -67.960  20.569 -31.083  1.00 81.51           C  
ATOM   5387  N   ARG C 108     -71.285  24.530 -32.063  1.00 93.54           N  
ATOM   5388  CA  ARG C 108     -72.309  25.577 -32.059  1.00 96.08           C  
ATOM   5389  C   ARG C 108     -73.718  25.019 -32.245  1.00 92.05           C  
ATOM   5390  O   ARG C 108     -74.695  25.651 -31.854  1.00 92.14           O  
ATOM   5391  CB  ARG C 108     -72.021  26.597 -33.162  1.00105.84           C  
ATOM   5392  CG  ARG C 108     -72.771  27.916 -33.014  1.00111.31           C  
ATOM   5393  CD  ARG C 108     -72.350  28.932 -34.082  1.00118.52           C  
ATOM   5394  NE  ARG C 108     -70.894  29.037 -34.269  1.00122.60           N  
ATOM   5395  CZ  ARG C 108     -70.049  29.665 -33.447  1.00126.44           C  
ATOM   5396  NH1 ARG C 108     -70.477  30.259 -32.334  1.00128.38           N  
ATOM   5397  NH2 ARG C 108     -68.751  29.692 -33.735  1.00129.01           N  
ATOM   5398  N   TYR C 109     -73.814  23.846 -32.862  1.00 88.43           N  
ATOM   5399  CA  TYR C 109     -75.083  23.139 -32.991  1.00 86.27           C  
ATOM   5400  C   TYR C 109     -75.419  22.389 -31.702  1.00 80.74           C  
ATOM   5401  O   TYR C 109     -76.447  22.669 -31.090  1.00 84.30           O  
ATOM   5402  CB  TYR C 109     -75.043  22.193 -34.191  1.00 91.30           C  
ATOM   5403  CG  TYR C 109     -75.920  20.959 -34.087  1.00 94.03           C  
ATOM   5404  CD1 TYR C 109     -77.255  20.985 -34.495  1.00 92.26           C  
ATOM   5405  CD2 TYR C 109     -75.397  19.750 -33.611  1.00 91.75           C  
ATOM   5406  CE1 TYR C 109     -78.050  19.836 -34.417  1.00 94.78           C  
ATOM   5407  CE2 TYR C 109     -76.172  18.605 -33.528  1.00 90.71           C  
ATOM   5408  CZ  TYR C 109     -77.496  18.643 -33.931  1.00 96.66           C  
ATOM   5409  OH  TYR C 109     -78.249  17.484 -33.838  1.00 94.77           O  
ATOM   5410  N   LEU C 110     -74.563  21.460 -31.277  1.00 73.08           N  
ATOM   5411  CA  LEU C 110     -74.833  20.696 -30.052  1.00 72.58           C  
ATOM   5412  C   LEU C 110     -75.171  21.610 -28.866  1.00 78.59           C  
ATOM   5413  O   LEU C 110     -76.019  21.264 -28.046  1.00 75.42           O  
ATOM   5414  CB  LEU C 110     -73.672  19.748 -29.677  1.00 74.24           C  
ATOM   5415  CG  LEU C 110     -73.689  18.294 -30.211  1.00 75.80           C  
ATOM   5416  CD1 LEU C 110     -72.600  17.425 -29.587  1.00 68.17           C  
ATOM   5417  CD2 LEU C 110     -75.021  17.614 -29.994  1.00 74.30           C  
ATOM   5418  N   GLN C 111     -74.532  22.778 -28.793  1.00 86.19           N  
ATOM   5419  CA  GLN C 111     -74.738  23.730 -27.685  1.00 86.77           C  
ATOM   5420  C   GLN C 111     -76.164  24.295 -27.590  1.00 79.43           C  
ATOM   5421  O   GLN C 111     -76.615  24.683 -26.509  1.00 72.52           O  
ATOM   5422  CB  GLN C 111     -73.744  24.891 -27.790  1.00 96.39           C  
ATOM   5423  CG  GLN C 111     -73.526  25.658 -26.491  1.00105.35           C  
ATOM   5424  CD  GLN C 111     -72.709  26.933 -26.691  1.00112.87           C  
ATOM   5425  OE1 GLN C 111     -73.035  27.769 -27.540  1.00114.82           O  
ATOM   5426  NE2 GLN C 111     -71.650  27.089 -25.901  1.00114.50           N  
ATOM   5427  N   GLU C 112     -76.874  24.353 -28.709  1.00 74.90           N  
ATOM   5428  CA  GLU C 112     -78.243  24.848 -28.681  1.00 81.25           C  
ATOM   5429  C   GLU C 112     -79.240  23.694 -28.634  1.00 73.17           C  
ATOM   5430  O   GLU C 112     -80.432  23.888 -28.844  1.00 72.29           O  
ATOM   5431  CB  GLU C 112     -78.524  25.777 -29.872  1.00 91.98           C  
ATOM   5432  CG  GLU C 112     -77.451  26.860 -30.131  1.00 98.11           C  
ATOM   5433  CD  GLU C 112     -76.933  27.559 -28.866  1.00 98.99           C  
ATOM   5434  OE1 GLU C 112     -75.693  27.683 -28.727  1.00 99.55           O  
ATOM   5435  OE2 GLU C 112     -77.753  27.983 -28.022  1.00 92.74           O  
ATOM   5436  N   ILE C 113     -78.744  22.489 -28.383  1.00 68.13           N  
ATOM   5437  CA  ILE C 113     -79.604  21.375 -28.001  1.00 63.93           C  
ATOM   5438  C   ILE C 113     -79.613  21.334 -26.497  1.00 63.34           C  
ATOM   5439  O   ILE C 113     -80.654  21.111 -25.886  1.00 58.89           O  
ATOM   5440  CB  ILE C 113     -79.090  20.018 -28.528  1.00 62.82           C  
ATOM   5441  CG1 ILE C 113     -79.022  20.034 -30.056  1.00 64.33           C  
ATOM   5442  CG2 ILE C 113     -79.971  18.891 -28.044  1.00 55.25           C  
ATOM   5443  CD1 ILE C 113     -80.104  20.885 -30.729  1.00 68.69           C  
ATOM   5444  N   TYR C 114     -78.441  21.552 -25.907  1.00 61.79           N  
ATOM   5445  CA  TYR C 114     -78.326  21.638 -24.467  1.00 54.75           C  
ATOM   5446  C   TYR C 114     -79.150  22.800 -23.928  1.00 57.74           C  
ATOM   5447  O   TYR C 114     -79.949  22.629 -23.012  1.00 60.26           O  
ATOM   5448  CB  TYR C 114     -76.887  21.813 -24.049  1.00 53.69           C  
ATOM   5449  CG  TYR C 114     -76.750  21.906 -22.564  1.00 60.78           C  
ATOM   5450  CD1 TYR C 114     -76.914  20.782 -21.771  1.00 63.49           C  
ATOM   5451  CD2 TYR C 114     -76.484  23.119 -21.941  1.00 65.69           C  
ATOM   5452  CE1 TYR C 114     -76.801  20.854 -20.402  1.00 64.29           C  
ATOM   5453  CE2 TYR C 114     -76.367  23.202 -20.564  1.00 65.95           C  
ATOM   5454  CZ  TYR C 114     -76.529  22.062 -19.804  1.00 62.82           C  
ATOM   5455  OH  TYR C 114     -76.415  22.124 -18.442  1.00 64.54           O  
ATOM   5456  N   ASN C 115     -78.973  23.980 -24.502  1.00 58.12           N  
ATOM   5457  CA  ASN C 115     -79.760  25.128 -24.067  1.00 59.30           C  
ATOM   5458  C   ASN C 115     -81.243  24.971 -24.392  1.00 48.24           C  
ATOM   5459  O   ASN C 115     -82.104  25.227 -23.548  1.00 44.27           O  
ATOM   5460  CB  ASN C 115     -79.182  26.410 -24.653  1.00 64.94           C  
ATOM   5461  CG  ASN C 115     -77.769  26.674 -24.156  1.00 71.42           C  
ATOM   5462  OD1 ASN C 115     -77.196  25.847 -23.436  1.00 69.35           O  
ATOM   5463  ND2 ASN C 115     -77.198  27.821 -24.534  1.00 68.31           N  
ATOM   5464  N   SER C 116     -81.534  24.523 -25.604  1.00 43.93           N  
ATOM   5465  CA  SER C 116     -82.906  24.208 -25.990  1.00 49.94           C  
ATOM   5466  C   SER C 116     -83.520  23.234 -25.005  1.00 51.26           C  
ATOM   5467  O   SER C 116     -84.594  23.484 -24.450  1.00 45.77           O  
ATOM   5468  CB  SER C 116     -82.942  23.587 -27.391  1.00 54.01           C  
ATOM   5469  OG  SER C 116     -84.147  22.885 -27.627  1.00 62.34           O  
ATOM   5470  N   ASN C 117     -82.817  22.122 -24.795  1.00 55.09           N  
ATOM   5471  CA  ASN C 117     -83.326  21.041 -23.966  1.00 47.67           C  
ATOM   5472  C   ASN C 117     -83.525  21.467 -22.516  1.00 50.17           C  
ATOM   5473  O   ASN C 117     -84.474  21.032 -21.883  1.00 56.85           O  
ATOM   5474  CB  ASN C 117     -82.448  19.783 -24.074  1.00 38.41           C  
ATOM   5475  CG  ASN C 117     -82.900  18.834 -25.206  1.00 39.27           C  
ATOM   5476  OD1 ASN C 117     -82.440  17.684 -25.286  1.00 35.53           O  
ATOM   5477  ND2 ASN C 117     -83.829  19.297 -26.050  1.00 25.45           N  
ATOM   5478  N   ASN C 118     -82.669  22.340 -21.995  1.00 53.21           N  
ATOM   5479  CA  ASN C 118     -82.930  22.931 -20.685  1.00 49.48           C  
ATOM   5480  C   ASN C 118     -84.196  23.783 -20.712  1.00 49.24           C  
ATOM   5481  O   ASN C 118     -85.118  23.577 -19.922  1.00 49.04           O  
ATOM   5482  CB  ASN C 118     -81.748  23.774 -20.209  1.00 47.21           C  
ATOM   5483  CG  ASN C 118     -80.587  22.931 -19.722  1.00 58.11           C  
ATOM   5484  OD1 ASN C 118     -80.727  21.736 -19.441  1.00 55.74           O  
ATOM   5485  ND2 ASN C 118     -79.417  23.558 -19.621  1.00 75.02           N  
ATOM   5486  N   GLN C 119     -84.257  24.734 -21.628  1.00 49.12           N  
ATOM   5487  CA  GLN C 119     -85.416  25.606 -21.684  1.00 53.09           C  
ATOM   5488  C   GLN C 119     -86.724  24.792 -21.742  1.00 52.99           C  
ATOM   5489  O   GLN C 119     -87.643  25.038 -20.959  1.00 45.11           O  
ATOM   5490  CB  GLN C 119     -85.296  26.589 -22.863  1.00 57.13           C  
ATOM   5491  CG  GLN C 119     -86.472  27.562 -23.042  1.00 58.19           C  
ATOM   5492  CD  GLN C 119     -86.991  28.134 -21.724  1.00 63.52           C  
ATOM   5493  OE1 GLN C 119     -88.203  28.342 -21.552  1.00 58.23           O  
ATOM   5494  NE2 GLN C 119     -86.076  28.376 -20.777  1.00 62.67           N  
ATOM   5495  N   LYS C 120     -86.781  23.803 -22.638  1.00 60.29           N  
ATOM   5496  CA  LYS C 120     -87.997  22.977 -22.830  1.00 63.43           C  
ATOM   5497  C   LYS C 120     -88.362  22.114 -21.627  1.00 60.52           C  
ATOM   5498  O   LYS C 120     -89.546  21.797 -21.424  1.00 60.40           O  
ATOM   5499  CB  LYS C 120     -87.878  22.074 -24.062  1.00 66.15           C  
ATOM   5500  CG  LYS C 120     -88.326  22.739 -25.354  1.00 71.40           C  
ATOM   5501  CD  LYS C 120     -88.452  21.719 -26.488  1.00 75.31           C  
ATOM   5502  CE  LYS C 120     -87.091  21.339 -27.065  1.00 76.18           C  
ATOM   5503  NZ  LYS C 120     -87.184  20.264 -28.101  1.00 73.02           N  
ATOM   5504  N   ILE C 121     -87.351  21.718 -20.853  1.00 52.86           N  
ATOM   5505  CA  ILE C 121     -87.583  21.147 -19.526  1.00 51.31           C  
ATOM   5506  C   ILE C 121     -88.237  22.170 -18.593  1.00 54.27           C  
ATOM   5507  O   ILE C 121     -89.383  21.982 -18.173  1.00 56.77           O  
ATOM   5508  CB  ILE C 121     -86.295  20.644 -18.880  1.00 48.46           C  
ATOM   5509  CG1 ILE C 121     -86.103  19.165 -19.200  1.00 44.84           C  
ATOM   5510  CG2 ILE C 121     -86.341  20.859 -17.379  1.00 51.26           C  
ATOM   5511  CD1 ILE C 121     -84.755  18.641 -18.764  1.00 45.41           C  
ATOM   5512  N   VAL C 122     -87.532  23.258 -18.286  1.00 48.27           N  
ATOM   5513  CA  VAL C 122     -88.071  24.276 -17.386  1.00 47.79           C  
ATOM   5514  C   VAL C 122     -89.604  24.331 -17.490  1.00 51.38           C  
ATOM   5515  O   VAL C 122     -90.302  24.213 -16.477  1.00 50.59           O  
ATOM   5516  CB  VAL C 122     -87.434  25.656 -17.659  1.00 44.20           C  
ATOM   5517  CG1 VAL C 122     -88.281  26.793 -17.091  1.00 44.40           C  
ATOM   5518  CG2 VAL C 122     -86.041  25.690 -17.083  1.00 43.87           C  
ATOM   5519  N   ASN C 123     -90.110  24.447 -18.721  1.00 54.33           N  
ATOM   5520  CA  ASN C 123     -91.560  24.534 -18.978  1.00 59.41           C  
ATOM   5521  C   ASN C 123     -92.303  23.234 -18.715  1.00 60.02           C  
ATOM   5522  O   ASN C 123     -93.483  23.255 -18.379  1.00 61.45           O  
ATOM   5523  CB  ASN C 123     -91.839  24.964 -20.412  1.00 58.08           C  
ATOM   5524  CG  ASN C 123     -90.829  25.933 -20.909  1.00 62.51           C  
ATOM   5525  OD1 ASN C 123     -90.162  25.683 -21.911  1.00 67.61           O  
ATOM   5526  ND2 ASN C 123     -90.648  27.026 -20.174  1.00 64.92           N  
ATOM   5527  N   LEU C 124     -91.633  22.104 -18.902  1.00 53.39           N  
ATOM   5528  CA  LEU C 124     -92.233  20.836 -18.530  1.00 50.95           C  
ATOM   5529  C   LEU C 124     -92.455  20.819 -17.022  1.00 51.07           C  
ATOM   5530  O   LEU C 124     -93.503  20.384 -16.538  1.00 51.72           O  
ATOM   5531  CB  LEU C 124     -91.343  19.661 -18.938  1.00 46.06           C  
ATOM   5532  CG  LEU C 124     -91.973  18.271 -18.824  1.00 42.16           C  
ATOM   5533  CD1 LEU C 124     -93.188  18.141 -19.736  1.00 33.39           C  
ATOM   5534  CD2 LEU C 124     -90.954  17.206 -19.153  1.00 37.71           C  
ATOM   5535  N   LYS C 125     -91.472  21.310 -16.278  1.00 51.95           N  
ATOM   5536  CA  LYS C 125     -91.501  21.163 -14.819  1.00 55.33           C  
ATOM   5537  C   LYS C 125     -92.616  21.995 -14.183  1.00 49.59           C  
ATOM   5538  O   LYS C 125     -93.258  21.560 -13.231  1.00 42.56           O  
ATOM   5539  CB  LYS C 125     -90.122  21.438 -14.198  1.00 50.95           C  
ATOM   5540  CG  LYS C 125     -89.166  20.255 -14.382  1.00 51.59           C  
ATOM   5541  CD  LYS C 125     -87.758  20.478 -13.791  1.00 58.49           C  
ATOM   5542  CE  LYS C 125     -87.063  19.112 -13.455  1.00 58.90           C  
ATOM   5543  NZ  LYS C 125     -85.599  19.206 -13.133  1.00 45.07           N  
ATOM   5544  N   GLU C 126     -92.870  23.175 -14.726  1.00 48.21           N  
ATOM   5545  CA  GLU C 126     -93.995  23.944 -14.252  1.00 53.29           C  
ATOM   5546  C   GLU C 126     -95.272  23.163 -14.557  1.00 51.38           C  
ATOM   5547  O   GLU C 126     -96.188  23.133 -13.749  1.00 56.46           O  
ATOM   5548  CB  GLU C 126     -94.024  25.349 -14.866  1.00 60.39           C  
ATOM   5549  CG  GLU C 126     -94.000  25.385 -16.380  1.00 70.13           C  
ATOM   5550  CD  GLU C 126     -94.496  26.697 -16.960  1.00 81.92           C  
ATOM   5551  OE1 GLU C 126     -95.736  26.865 -17.081  1.00 89.04           O  
ATOM   5552  OE2 GLU C 126     -93.645  27.547 -17.315  1.00 82.65           O  
ATOM   5553  N   LYS C 127     -95.306  22.493 -15.704  1.00 51.35           N  
ATOM   5554  CA  LYS C 127     -96.521  21.820 -16.180  1.00 47.82           C  
ATOM   5555  C   LYS C 127     -96.876  20.644 -15.265  1.00 47.43           C  
ATOM   5556  O   LYS C 127     -98.021  20.477 -14.838  1.00 47.56           O  
ATOM   5557  CB  LYS C 127     -96.321  21.338 -17.622  1.00 43.23           C  
ATOM   5558  CG  LYS C 127     -97.541  21.404 -18.505  1.00 46.54           C  
ATOM   5559  CD  LYS C 127     -97.241  20.845 -19.914  1.00 48.48           C  
ATOM   5560  CE  LYS C 127     -98.489  20.770 -20.811  1.00 46.96           C  
ATOM   5561  NZ  LYS C 127     -99.678  20.152 -20.129  1.00 45.17           N  
ATOM   5562  N   VAL C 128     -95.873  19.835 -14.951  1.00 50.08           N  
ATOM   5563  CA  VAL C 128     -96.060  18.711 -14.034  1.00 44.75           C  
ATOM   5564  C   VAL C 128     -96.329  19.219 -12.603  1.00 44.69           C  
ATOM   5565  O   VAL C 128     -96.812  18.487 -11.755  1.00 49.28           O  
ATOM   5566  CB  VAL C 128     -94.881  17.671 -14.148  1.00 36.89           C  
ATOM   5567  CG1 VAL C 128     -93.543  18.338 -14.108  1.00 38.62           C  
ATOM   5568  CG2 VAL C 128     -94.960  16.615 -13.080  1.00 36.70           C  
ATOM   5569  N   ALA C 129     -96.052  20.492 -12.344  1.00 52.03           N  
ATOM   5570  CA  ALA C 129     -96.594  21.131 -11.152  1.00 55.49           C  
ATOM   5571  C   ALA C 129     -98.111  21.209 -11.306  1.00 57.93           C  
ATOM   5572  O   ALA C 129     -98.834  20.744 -10.436  1.00 62.91           O  
ATOM   5573  CB  ALA C 129     -96.005  22.515 -10.949  1.00 50.25           C  
ATOM   5574  N   GLN C 130     -98.582  21.767 -12.425  1.00 53.87           N  
ATOM   5575  CA  GLN C 130    -100.019  21.961 -12.662  1.00 53.21           C  
ATOM   5576  C   GLN C 130    -100.778  20.656 -12.512  1.00 52.94           C  
ATOM   5577  O   GLN C 130    -101.908  20.645 -12.023  1.00 50.25           O  
ATOM   5578  CB  GLN C 130    -100.308  22.525 -14.061  1.00 60.48           C  
ATOM   5579  CG  GLN C 130    -100.180  24.029 -14.209  1.00 65.29           C  
ATOM   5580  CD  GLN C 130     -98.735  24.502 -14.173  1.00 73.88           C  
ATOM   5581  OE1 GLN C 130     -98.089  24.660 -15.218  1.00 73.96           O  
ATOM   5582  NE2 GLN C 130     -98.216  24.726 -12.963  1.00 73.21           N  
ATOM   5583  N   LEU C 131    -100.157  19.561 -12.947  1.00 52.31           N  
ATOM   5584  CA  LEU C 131    -100.770  18.239 -12.817  1.00 54.71           C  
ATOM   5585  C   LEU C 131    -100.717  17.774 -11.356  1.00 62.36           C  
ATOM   5586  O   LEU C 131    -101.721  17.319 -10.808  1.00 54.88           O  
ATOM   5587  CB  LEU C 131    -100.085  17.231 -13.751  1.00 55.07           C  
ATOM   5588  CG  LEU C 131    -100.517  15.748 -13.709  1.00 57.08           C  
ATOM   5589  CD1 LEU C 131    -101.019  15.300 -15.057  1.00 57.32           C  
ATOM   5590  CD2 LEU C 131     -99.397  14.798 -13.235  1.00 57.43           C  
ATOM   5591  N   GLU C 132     -99.547  17.904 -10.725  1.00 65.21           N  
ATOM   5592  CA  GLU C 132     -99.378  17.492  -9.328  1.00 67.52           C  
ATOM   5593  C   GLU C 132    -100.523  18.033  -8.485  1.00 67.19           C  
ATOM   5594  O   GLU C 132    -101.342  17.270  -7.965  1.00 63.50           O  
ATOM   5595  CB  GLU C 132     -98.039  17.986  -8.753  1.00 74.25           C  
ATOM   5596  CG  GLU C 132     -97.878  17.689  -7.244  1.00 83.03           C  
ATOM   5597  CD  GLU C 132     -96.425  17.684  -6.747  1.00 86.83           C  
ATOM   5598  OE1 GLU C 132     -96.088  16.788  -5.919  1.00 73.45           O  
ATOM   5599  OE2 GLU C 132     -95.636  18.571  -7.180  1.00 91.19           O  
ATOM   5600  N   ALA C 133    -100.593  19.359  -8.402  1.00 62.24           N  
ATOM   5601  CA  ALA C 133    -101.546  20.049  -7.552  1.00 61.32           C  
ATOM   5602  C   ALA C 133    -102.973  19.899  -8.069  1.00 63.81           C  
ATOM   5603  O   ALA C 133    -103.881  20.645  -7.655  1.00 61.93           O  
ATOM   5604  CB  ALA C 133    -101.168  21.530  -7.451  1.00 65.77           C  
ATOM   5605  N   GLN C 134    -103.167  18.933  -8.966  1.00 61.30           N  
ATOM   5606  CA  GLN C 134    -104.474  18.644  -9.557  1.00 60.20           C  
ATOM   5607  C   GLN C 134    -104.841  17.165  -9.390  1.00 45.02           C  
ATOM   5608  O   GLN C 134    -105.632  16.633 -10.134  1.00 44.96           O  
ATOM   5609  CB  GLN C 134    -104.405  19.002 -11.043  1.00 58.48           C  
ATOM   5610  CG  GLN C 134    -105.728  19.255 -11.727  1.00 53.95           C  
ATOM   5611  CD  GLN C 134    -105.711  18.796 -13.169  1.00 53.14           C  
ATOM   5612  OE1 GLN C 134    -106.614  18.091 -13.614  1.00 54.49           O  
ATOM   5613  NE2 GLN C 134    -104.670  19.173 -13.901  1.00 54.24           N  
ATOM   5614  N   CYS C 135    -104.239  16.497  -8.423  1.00 53.57           N  
ATOM   5615  CA  CYS C 135    -104.361  15.038  -8.308  1.00 60.41           C  
ATOM   5616  C   CYS C 135    -104.152  14.666  -6.867  1.00 58.63           C  
ATOM   5617  O   CYS C 135    -103.430  13.718  -6.534  1.00 64.54           O  
ATOM   5618  CB  CYS C 135    -103.356  14.315  -9.220  1.00 61.25           C  
ATOM   5619  SG  CYS C 135    -104.111  13.752 -10.770  1.00 56.90           S  
ATOM   5620  N   GLN C 136    -104.812  15.454  -6.033  1.00 46.64           N  
ATOM   5621  CA  GLN C 136    -104.696  15.381  -4.613  1.00 46.54           C  
ATOM   5622  C   GLN C 136    -106.013  14.796  -4.120  1.00 49.01           C  
ATOM   5623  O   GLN C 136    -106.054  13.717  -3.517  1.00 55.14           O  
ATOM   5624  CB  GLN C 136    -104.450  16.794  -4.080  1.00 54.06           C  
ATOM   5625  CG  GLN C 136    -103.207  17.473  -4.668  1.00 50.86           C  
ATOM   5626  CD  GLN C 136    -101.928  16.845  -4.153  1.00 58.06           C  
ATOM   5627  OE1 GLN C 136    -101.107  16.344  -4.930  1.00 59.66           O  
ATOM   5628  NE2 GLN C 136    -101.762  16.841  -2.828  1.00 53.32           N  
ATOM   5629  N   GLU C 137    -107.101  15.493  -4.425  1.00 48.81           N  
ATOM   5630  CA  GLU C 137    -108.422  15.056  -4.013  1.00 49.20           C  
ATOM   5631  C   GLU C 137    -108.726  13.557  -4.277  1.00 46.49           C  
ATOM   5632  O   GLU C 137    -108.301  12.964  -5.265  1.00 46.38           O  
ATOM   5633  CB  GLU C 137    -109.487  15.953  -4.650  1.00 51.88           C  
ATOM   5634  CG  GLU C 137    -109.868  17.124  -3.768  1.00 58.19           C  
ATOM   5635  CD  GLU C 137    -110.881  16.737  -2.686  1.00 66.64           C  
ATOM   5636  OE1 GLU C 137    -110.477  16.576  -1.509  1.00 74.20           O  
ATOM   5637  OE2 GLU C 137    -112.081  16.578  -3.013  1.00 62.45           O  
ATOM   5638  N   PRO C 138    -109.468  12.940  -3.369  1.00 38.88           N  
ATOM   5639  CA  PRO C 138    -109.856  11.567  -3.556  1.00 40.26           C  
ATOM   5640  C   PRO C 138    -111.067  11.413  -4.471  1.00 48.28           C  
ATOM   5641  O   PRO C 138    -111.610  12.420  -4.954  1.00 48.04           O  
ATOM   5642  CB  PRO C 138    -110.220  11.147  -2.149  1.00 42.39           C  
ATOM   5643  CG  PRO C 138    -110.765  12.373  -1.566  1.00 45.81           C  
ATOM   5644  CD  PRO C 138    -109.909  13.458  -2.067  1.00 39.16           C  
ATOM   5645  N   CYS C 139    -111.481  10.153  -4.678  1.00 46.04           N  
ATOM   5646  CA  CYS C 139    -112.552   9.808  -5.611  1.00 35.45           C  
ATOM   5647  C   CYS C 139    -113.877  10.147  -5.015  1.00 23.44           C  
ATOM   5648  O   CYS C 139    -114.076  10.044  -3.826  1.00 21.05           O  
ATOM   5649  CB  CYS C 139    -112.558   8.327  -5.961  1.00 42.13           C  
ATOM   5650  SG  CYS C 139    -111.127   7.694  -6.844  1.00 53.96           S  
ATOM   5651  N   LYS C 140    -114.800  10.517  -5.875  1.00 30.26           N  
ATOM   5652  CA  LYS C 140    -116.034  11.123  -5.432  1.00 39.61           C  
ATOM   5653  C   LYS C 140    -116.945  10.067  -4.863  1.00 29.95           C  
ATOM   5654  O   LYS C 140    -117.497   9.299  -5.623  1.00 35.46           O  
ATOM   5655  CB  LYS C 140    -116.727  11.875  -6.607  1.00 47.55           C  
ATOM   5656  CG  LYS C 140    -116.757  13.432  -6.475  1.00 50.46           C  
ATOM   5657  CD  LYS C 140    -115.470  14.164  -6.933  1.00 44.45           C  
ATOM   5658  CE  LYS C 140    -114.252  13.895  -6.018  1.00 55.34           C  
ATOM   5659  NZ  LYS C 140    -114.498  14.024  -4.529  1.00 54.49           N  
ATOM   5660  N   ASP C 141    -117.136  10.008  -3.550  1.00 22.30           N  
ATOM   5661  CA  ASP C 141    -118.160   9.080  -3.091  1.00 28.19           C  
ATOM   5662  C   ASP C 141    -119.538   9.605  -3.396  1.00 27.02           C  
ATOM   5663  O   ASP C 141    -119.861  10.757  -3.126  1.00 33.66           O  
ATOM   5664  CB  ASP C 141    -118.082   8.672  -1.614  1.00 38.22           C  
ATOM   5665  CG  ASP C 141    -118.563   7.189  -1.378  1.00 33.86           C  
ATOM   5666  OD1 ASP C 141    -118.202   6.561  -0.349  1.00 27.14           O  
ATOM   5667  OD2 ASP C 141    -119.290   6.646  -2.244  1.00 28.84           O  
ATOM   5668  N   THR C 142    -120.336   8.718  -3.969  1.00 26.25           N  
ATOM   5669  CA  THR C 142    -121.724   8.970  -4.250  1.00 28.31           C  
ATOM   5670  C   THR C 142    -122.551   8.922  -2.946  1.00 27.66           C  
ATOM   5671  O   THR C 142    -123.539   9.633  -2.827  1.00 33.77           O  
ATOM   5672  CB  THR C 142    -122.259   7.941  -5.276  1.00 25.19           C  
ATOM   5673  OG1 THR C 142    -122.032   6.628  -4.771  1.00 35.44           O  
ATOM   5674  CG2 THR C 142    -121.529   8.043  -6.586  1.00 18.48           C  
ATOM   5675  N   VAL C 143    -122.137   8.118  -1.965  1.00 24.05           N  
ATOM   5676  CA  VAL C 143    -122.917   7.946  -0.723  1.00 24.91           C  
ATOM   5677  C   VAL C 143    -122.562   9.017   0.331  1.00 27.34           C  
ATOM   5678  O   VAL C 143    -121.386   9.344   0.520  1.00 24.50           O  
ATOM   5679  CB  VAL C 143    -122.751   6.509  -0.116  1.00 26.13           C  
ATOM   5680  CG1 VAL C 143    -123.286   5.429  -1.068  1.00 20.54           C  
ATOM   5681  CG2 VAL C 143    -121.287   6.241   0.277  1.00 24.41           C  
ATOM   5682  N   GLN C 144    -123.579   9.536   1.025  1.00 31.47           N  
ATOM   5683  CA  GLN C 144    -123.438  10.758   1.841  1.00 44.35           C  
ATOM   5684  C   GLN C 144    -124.217  10.641   3.135  1.00 36.07           C  
ATOM   5685  O   GLN C 144    -125.314  10.129   3.110  1.00 46.42           O  
ATOM   5686  CB  GLN C 144    -124.013  11.964   1.070  1.00 58.66           C  
ATOM   5687  CG  GLN C 144    -123.273  12.374  -0.246  1.00 60.32           C  
ATOM   5688  CD  GLN C 144    -122.206  13.456  -0.043  1.00 64.60           C  
ATOM   5689  OE1 GLN C 144    -121.182  13.470  -0.742  1.00 69.65           O  
ATOM   5690  NE2 GLN C 144    -122.443  14.367   0.914  1.00 58.14           N  
ATOM   5691  N   ILE C 145    -123.702  11.139   4.255  1.00 35.68           N  
ATOM   5692  CA  ILE C 145    -124.503  11.119   5.499  1.00 39.51           C  
ATOM   5693  C   ILE C 145    -124.876  12.541   5.915  1.00 42.37           C  
ATOM   5694  O   ILE C 145    -124.083  13.277   6.529  1.00 45.27           O  
ATOM   5695  CB  ILE C 145    -123.822  10.368   6.701  1.00 39.93           C  
ATOM   5696  CG1 ILE C 145    -123.282   9.003   6.286  1.00 38.77           C  
ATOM   5697  CG2 ILE C 145    -124.814  10.098   7.828  1.00 37.69           C  
ATOM   5698  CD1 ILE C 145    -122.764   8.190   7.455  1.00 32.12           C  
ATOM   5699  N   HIS C 146    -126.103  12.914   5.584  1.00 30.15           N  
ATOM   5700  CA  HIS C 146    -126.658  14.196   5.982  1.00 29.22           C  
ATOM   5701  C   HIS C 146    -126.323  14.556   7.422  1.00 35.75           C  
ATOM   5702  O   HIS C 146    -126.126  13.688   8.292  1.00 31.35           O  
ATOM   5703  CB  HIS C 146    -128.178  14.189   5.850  1.00 27.20           C  
ATOM   5704  CG  HIS C 146    -128.660  13.760   4.506  1.00 23.80           C  
ATOM   5705  ND1 HIS C 146    -127.888  13.883   3.372  1.00 25.23           N  
ATOM   5706  CD2 HIS C 146    -129.833  13.215   4.108  1.00 21.65           C  
ATOM   5707  CE1 HIS C 146    -128.567  13.436   2.330  1.00 23.82           C  
ATOM   5708  NE2 HIS C 146    -129.759  13.043   2.747  1.00 26.24           N  
ATOM   5709  N   ASP C 147    -126.361  15.865   7.659  1.00 51.62           N  
ATOM   5710  CA  ASP C 147    -125.897  16.508   8.903  1.00 50.44           C  
ATOM   5711  C   ASP C 147    -126.998  16.775   9.930  1.00 43.70           C  
ATOM   5712  O   ASP C 147    -126.698  17.162  11.060  1.00 42.80           O  
ATOM   5713  CB  ASP C 147    -125.202  17.824   8.565  1.00 48.04           C  
ATOM   5714  CG  ASP C 147    -125.573  18.324   7.198  1.00 52.71           C  
ATOM   5715  OD1 ASP C 147    -126.786  18.231   6.853  1.00 53.43           O  
ATOM   5716  OD2 ASP C 147    -124.649  18.765   6.468  1.00 57.59           O  
ATOM   5717  N   ILE C 148    -128.257  16.562   9.555  1.00 41.80           N  
ATOM   5718  CA  ILE C 148    -129.360  16.706  10.507  1.00 45.03           C  
ATOM   5719  C   ILE C 148    -129.438  15.464  11.376  1.00 41.66           C  
ATOM   5720  O   ILE C 148    -129.254  14.343  10.888  1.00 47.42           O  
ATOM   5721  CB  ILE C 148    -130.724  16.894   9.813  1.00 50.42           C  
ATOM   5722  CG1 ILE C 148    -130.670  18.060   8.814  1.00 47.96           C  
ATOM   5723  CG2 ILE C 148    -131.829  17.109  10.864  1.00 51.43           C  
ATOM   5724  CD1 ILE C 148    -131.988  18.393   8.163  1.00 44.71           C  
ATOM   5725  N   THR C 149    -129.706  15.669  12.659  1.00 32.84           N  
ATOM   5726  CA  THR C 149    -129.765  14.570  13.605  1.00 35.79           C  
ATOM   5727  C   THR C 149    -130.977  14.745  14.452  1.00 30.97           C  
ATOM   5728  O   THR C 149    -131.393  15.854  14.695  1.00 38.12           O  
ATOM   5729  CB  THR C 149    -128.527  14.525  14.542  1.00 37.46           C  
ATOM   5730  OG1 THR C 149    -127.355  14.192  13.775  1.00 48.96           O  
ATOM   5731  CG2 THR C 149    -128.728  13.480  15.680  1.00 33.60           C  
ATOM   5732  N   GLY C 150    -131.533  13.645  14.919  1.00 35.86           N  
ATOM   5733  CA  GLY C 150    -132.637  13.712  15.847  1.00 45.18           C  
ATOM   5734  C   GLY C 150    -132.717  12.455  16.680  1.00 50.37           C  
ATOM   5735  O   GLY C 150    -131.758  11.669  16.740  1.00 46.26           O  
ATOM   5736  N   LYS C 151    -133.869  12.285  17.323  1.00 48.23           N  
ATOM   5737  CA  LYS C 151    -134.141  11.124  18.158  1.00 52.96           C  
ATOM   5738  C   LYS C 151    -134.794  10.028  17.328  1.00 46.82           C  
ATOM   5739  O   LYS C 151    -134.930   8.904  17.796  1.00 52.84           O  
ATOM   5740  CB  LYS C 151    -135.031  11.508  19.355  1.00 60.30           C  
ATOM   5741  CG  LYS C 151    -134.246  12.074  20.548  1.00 69.03           C  
ATOM   5742  CD  LYS C 151    -133.635  13.481  20.270  1.00 70.74           C  
ATOM   5743  CE  LYS C 151    -132.284  13.703  20.994  1.00 65.64           C  
ATOM   5744  NZ  LYS C 151    -131.113  13.101  20.266  1.00 61.91           N  
ATOM   5745  N   ASP C 152    -135.205  10.362  16.109  1.00 35.72           N  
ATOM   5746  CA  ASP C 152    -135.780   9.391  15.188  1.00 38.26           C  
ATOM   5747  C   ASP C 152    -135.829  10.019  13.791  1.00 34.99           C  
ATOM   5748  O   ASP C 152    -135.313  11.104  13.584  1.00 34.35           O  
ATOM   5749  CB  ASP C 152    -137.172   8.912  15.666  1.00 45.27           C  
ATOM   5750  CG  ASP C 152    -138.224  10.035  15.706  1.00 60.76           C  
ATOM   5751  OD1 ASP C 152    -138.006  11.088  15.056  1.00 59.93           O  
ATOM   5752  OD2 ASP C 152    -139.279   9.859  16.384  1.00 61.65           O  
ATOM   5753  N   CYS C 153    -136.427   9.343  12.820  1.00 34.57           N  
ATOM   5754  CA  CYS C 153    -136.488   9.913  11.483  1.00 30.49           C  
ATOM   5755  C   CYS C 153    -137.551  10.972  11.409  1.00 26.06           C  
ATOM   5756  O   CYS C 153    -137.396  11.914  10.680  1.00 28.05           O  
ATOM   5757  CB  CYS C 153    -136.755   8.842  10.431  1.00 30.06           C  
ATOM   5758  SG  CYS C 153    -135.303   7.871  10.072  1.00 23.73           S  
ATOM   5759  N   GLN C 154    -138.646  10.786  12.138  1.00 30.85           N  
ATOM   5760  CA  GLN C 154    -139.704  11.786  12.207  1.00 30.41           C  
ATOM   5761  C   GLN C 154    -139.154  13.112  12.609  1.00 30.65           C  
ATOM   5762  O   GLN C 154    -139.434  14.120  11.987  1.00 29.27           O  
ATOM   5763  CB  GLN C 154    -140.750  11.431  13.265  1.00 31.11           C  
ATOM   5764  CG  GLN C 154    -141.900  12.403  13.244  1.00 31.08           C  
ATOM   5765  CD  GLN C 154    -142.469  12.532  11.831  1.00 41.95           C  
ATOM   5766  OE1 GLN C 154    -142.853  11.519  11.205  1.00 37.15           O  
ATOM   5767  NE2 GLN C 154    -142.493  13.765  11.303  1.00 37.20           N  
ATOM   5768  N   ASP C 155    -138.404  13.070  13.704  1.00 36.01           N  
ATOM   5769  CA  ASP C 155    -137.777  14.215  14.316  1.00 33.67           C  
ATOM   5770  C   ASP C 155    -136.953  14.955  13.257  1.00 31.25           C  
ATOM   5771  O   ASP C 155    -137.103  16.159  13.040  1.00 31.54           O  
ATOM   5772  CB  ASP C 155    -136.914  13.700  15.472  1.00 35.92           C  
ATOM   5773  CG  ASP C 155    -136.345  14.798  16.336  1.00 49.75           C  
ATOM   5774  OD1 ASP C 155    -135.536  14.439  17.236  1.00 53.14           O  
ATOM   5775  OD2 ASP C 155    -136.697  15.997  16.137  1.00 44.94           O  
ATOM   5776  N   ILE C 156    -136.114  14.226  12.554  1.00 26.17           N  
ATOM   5777  CA  ILE C 156    -135.418  14.818  11.430  1.00 25.72           C  
ATOM   5778  C   ILE C 156    -136.430  15.507  10.443  1.00 17.55           C  
ATOM   5779  O   ILE C 156    -136.193  16.587   9.940  1.00 22.19           O  
ATOM   5780  CB  ILE C 156    -134.465  13.752  10.794  1.00 23.93           C  
ATOM   5781  CG1 ILE C 156    -133.354  13.431  11.788  1.00 27.32           C  
ATOM   5782  CG2 ILE C 156    -133.816  14.209   9.472  1.00 21.48           C  
ATOM   5783  CD1 ILE C 156    -132.144  12.768  11.145  1.00 30.94           C  
ATOM   5784  N   ALA C 157    -137.567  14.901  10.204  1.00 20.75           N  
ATOM   5785  CA  ALA C 157    -138.528  15.470   9.289  1.00 23.65           C  
ATOM   5786  C   ALA C 157    -139.020  16.757   9.910  1.00 30.38           C  
ATOM   5787  O   ALA C 157    -139.245  17.767   9.229  1.00 32.46           O  
ATOM   5788  CB  ALA C 157    -139.719  14.501   9.071  1.00 23.48           C  
ATOM   5789  N   ASN C 158    -139.208  16.715  11.218  1.00 29.85           N  
ATOM   5790  CA  ASN C 158    -139.796  17.838  11.922  1.00 27.48           C  
ATOM   5791  C   ASN C 158    -138.762  18.932  11.992  1.00 29.08           C  
ATOM   5792  O   ASN C 158    -139.064  20.117  11.838  1.00 32.84           O  
ATOM   5793  CB  ASN C 158    -140.236  17.407  13.307  1.00 24.18           C  
ATOM   5794  CG  ASN C 158    -141.464  16.565  13.263  1.00 34.42           C  
ATOM   5795  OD1 ASN C 158    -142.281  16.677  12.339  1.00 36.03           O  
ATOM   5796  ND2 ASN C 158    -141.622  15.708  14.263  1.00 52.91           N  
ATOM   5797  N   LYS C 159    -137.524  18.515  12.160  1.00 14.70           N  
ATOM   5798  CA  LYS C 159    -136.438  19.414  11.997  1.00 15.20           C  
ATOM   5799  C   LYS C 159    -136.321  19.854  10.514  1.00 15.09           C  
ATOM   5800  O   LYS C 159    -135.306  20.414  10.106  1.00 10.99           O  
ATOM   5801  CB  LYS C 159    -135.170  18.740  12.507  1.00 18.21           C  
ATOM   5802  CG  LYS C 159    -135.221  18.388  14.003  1.00 14.00           C  
ATOM   5803  CD  LYS C 159    -133.830  18.017  14.459  1.00 20.52           C  
ATOM   5804  CE  LYS C 159    -133.607  18.163  15.971  1.00 27.31           C  
ATOM   5805  NZ  LYS C 159    -134.439  17.241  16.833  1.00 33.03           N  
ATOM   5806  N   GLY C 160    -137.381  19.622   9.726  1.00 15.26           N  
ATOM   5807  CA  GLY C 160    -137.468  20.047   8.309  1.00 15.40           C  
ATOM   5808  C   GLY C 160    -136.398  19.540   7.344  1.00 21.30           C  
ATOM   5809  O   GLY C 160    -135.588  20.328   6.839  1.00 23.25           O  
ATOM   5810  N   ALA C 161    -136.387  18.218   7.103  1.00 30.45           N  
ATOM   5811  CA  ALA C 161    -135.515  17.569   6.096  1.00 21.24           C  
ATOM   5812  C   ALA C 161    -136.403  16.935   5.030  1.00 16.30           C  
ATOM   5813  O   ALA C 161    -137.581  16.663   5.287  1.00 13.67           O  
ATOM   5814  CB  ALA C 161    -134.643  16.564   6.746  1.00 16.34           C  
ATOM   5815  N   LYS C 162    -135.890  16.758   3.819  1.00 18.41           N  
ATOM   5816  CA  LYS C 162    -136.802  16.361   2.733  1.00 32.87           C  
ATOM   5817  C   LYS C 162    -136.269  15.195   1.934  1.00 33.83           C  
ATOM   5818  O   LYS C 162    -137.061  14.372   1.462  1.00 36.80           O  
ATOM   5819  CB  LYS C 162    -137.125  17.532   1.781  1.00 41.28           C  
ATOM   5820  CG  LYS C 162    -137.637  18.816   2.455  1.00 47.16           C  
ATOM   5821  CD  LYS C 162    -139.108  18.736   2.866  1.00 56.16           C  
ATOM   5822  CE  LYS C 162    -139.437  19.666   4.054  1.00 61.76           C  
ATOM   5823  NZ  LYS C 162    -138.835  21.033   3.977  1.00 60.74           N  
ATOM   5824  N   GLN C 163    -134.953  15.149   1.733  1.00 27.02           N  
ATOM   5825  CA  GLN C 163    -134.324  13.967   1.154  1.00 27.54           C  
ATOM   5826  C   GLN C 163    -134.481  12.768   2.073  1.00 29.72           C  
ATOM   5827  O   GLN C 163    -134.351  12.880   3.306  1.00 21.36           O  
ATOM   5828  CB  GLN C 163    -132.848  14.178   0.929  1.00 32.49           C  
ATOM   5829  CG  GLN C 163    -132.537  15.155  -0.192  1.00 38.89           C  
ATOM   5830  CD  GLN C 163    -132.321  14.449  -1.520  1.00 37.43           C  
ATOM   5831  OE1 GLN C 163    -131.154  14.343  -2.016  1.00 22.25           O  
ATOM   5832  NE2 GLN C 163    -133.436  13.942  -2.109  1.00 29.02           N  
ATOM   5833  N   SER C 164    -134.810  11.642   1.435  1.00 30.92           N  
ATOM   5834  CA  SER C 164    -134.845  10.331   2.058  1.00 24.40           C  
ATOM   5835  C   SER C 164    -133.457   9.793   1.847  1.00 20.89           C  
ATOM   5836  O   SER C 164    -132.896   9.946   0.750  1.00 25.80           O  
ATOM   5837  CB  SER C 164    -135.870   9.467   1.370  1.00 23.61           C  
ATOM   5838  OG  SER C 164    -137.165  10.051   1.526  1.00 34.60           O  
ATOM   5839  N   GLY C 165    -132.862   9.217   2.882  1.00 10.14           N  
ATOM   5840  CA  GLY C 165    -131.449   8.851   2.750  1.00  8.87           C  
ATOM   5841  C   GLY C 165    -130.832   8.797   4.108  1.00  7.00           C  
ATOM   5842  O   GLY C 165    -131.545   8.740   5.098  1.00  9.18           O  
ATOM   5843  N   LEU C 166    -129.530   8.868   4.181  1.00  3.29           N  
ATOM   5844  CA  LEU C 166    -128.923   8.412   5.401  1.00 12.59           C  
ATOM   5845  C   LEU C 166    -128.714   9.487   6.484  1.00 10.07           C  
ATOM   5846  O   LEU C 166    -128.007  10.440   6.234  1.00 19.33           O  
ATOM   5847  CB  LEU C 166    -127.570   7.744   5.029  1.00 17.33           C  
ATOM   5848  CG  LEU C 166    -127.617   6.471   4.161  1.00 12.51           C  
ATOM   5849  CD1 LEU C 166    -126.253   5.917   3.947  1.00  4.96           C  
ATOM   5850  CD2 LEU C 166    -128.563   5.472   4.868  1.00 12.04           C  
ATOM   5851  N   TYR C 167    -129.227   9.277   7.697  1.00 10.63           N  
ATOM   5852  CA  TYR C 167    -128.913  10.141   8.876  1.00 19.44           C  
ATOM   5853  C   TYR C 167    -128.476   9.408  10.155  1.00 22.55           C  
ATOM   5854  O   TYR C 167    -128.847   8.251  10.364  1.00 25.92           O  
ATOM   5855  CB  TYR C 167    -130.161  10.922   9.299  1.00 22.48           C  
ATOM   5856  CG  TYR C 167    -130.849  11.602   8.168  1.00 29.20           C  
ATOM   5857  CD1 TYR C 167    -131.564  10.863   7.256  1.00 33.37           C  
ATOM   5858  CD2 TYR C 167    -130.794  12.990   8.006  1.00 30.68           C  
ATOM   5859  CE1 TYR C 167    -132.212  11.465   6.211  1.00 37.89           C  
ATOM   5860  CE2 TYR C 167    -131.447  13.607   6.949  1.00 31.07           C  
ATOM   5861  CZ  TYR C 167    -132.163  12.827   6.051  1.00 29.45           C  
ATOM   5862  OH  TYR C 167    -132.803  13.328   4.944  1.00 14.92           O  
ATOM   5863  N   PHE C 168    -127.802  10.113  11.066  1.00 21.68           N  
ATOM   5864  CA  PHE C 168    -127.645   9.582  12.434  1.00 23.75           C  
ATOM   5865  C   PHE C 168    -128.803   9.955  13.309  1.00 23.76           C  
ATOM   5866  O   PHE C 168    -129.378  11.011  13.158  1.00 24.33           O  
ATOM   5867  CB  PHE C 168    -126.397  10.090  13.133  1.00 27.88           C  
ATOM   5868  CG  PHE C 168    -125.147   9.550  12.561  1.00 31.88           C  
ATOM   5869  CD1 PHE C 168    -124.730   8.295  12.869  1.00 42.05           C  
ATOM   5870  CD2 PHE C 168    -124.399  10.287  11.683  1.00 34.39           C  
ATOM   5871  CE1 PHE C 168    -123.568   7.794  12.315  1.00 43.79           C  
ATOM   5872  CE2 PHE C 168    -123.269   9.781  11.131  1.00 35.66           C  
ATOM   5873  CZ  PHE C 168    -122.846   8.540  11.453  1.00 33.66           C  
ATOM   5874  N   ILE C 169    -129.098   9.069  14.250  1.00 28.42           N  
ATOM   5875  CA  ILE C 169    -130.000   9.345  15.356  1.00 27.10           C  
ATOM   5876  C   ILE C 169    -129.477   8.779  16.675  1.00 26.52           C  
ATOM   5877  O   ILE C 169    -128.784   7.774  16.709  1.00 21.77           O  
ATOM   5878  CB  ILE C 169    -131.367   8.761  15.089  1.00 28.01           C  
ATOM   5879  CG1 ILE C 169    -131.302   7.211  15.005  1.00 24.75           C  
ATOM   5880  CG2 ILE C 169    -131.928   9.444  13.850  1.00 32.64           C  
ATOM   5881  CD1 ILE C 169    -132.545   6.537  14.417  1.00 18.97           C  
ATOM   5882  N   LYS C 170    -129.814   9.452  17.758  1.00 32.99           N  
ATOM   5883  CA  LYS C 170    -129.458   9.002  19.080  1.00 34.47           C  
ATOM   5884  C   LYS C 170    -130.725   9.023  19.929  1.00 39.95           C  
ATOM   5885  O   LYS C 170    -131.030  10.023  20.579  1.00 50.04           O  
ATOM   5886  CB  LYS C 170    -128.367   9.894  19.673  1.00 38.59           C  
ATOM   5887  CG  LYS C 170    -127.875   9.409  21.038  1.00 43.92           C  
ATOM   5888  CD  LYS C 170    -126.682  10.213  21.550  1.00 54.13           C  
ATOM   5889  CE  LYS C 170    -126.279   9.828  22.995  1.00 58.67           C  
ATOM   5890  NZ  LYS C 170    -126.932  10.627  24.086  1.00 55.78           N  
ATOM   5891  N   PRO C 171    -131.500   7.935  19.876  1.00 42.25           N  
ATOM   5892  CA  PRO C 171    -132.662   7.719  20.735  1.00 44.62           C  
ATOM   5893  C   PRO C 171    -132.369   7.820  22.214  1.00 48.80           C  
ATOM   5894  O   PRO C 171    -131.257   7.541  22.668  1.00 55.05           O  
ATOM   5895  CB  PRO C 171    -133.082   6.284  20.419  1.00 48.93           C  
ATOM   5896  CG  PRO C 171    -132.273   5.863  19.221  1.00 50.18           C  
ATOM   5897  CD  PRO C 171    -131.535   7.047  18.707  1.00 46.01           C  
ATOM   5898  N   LEU C 172    -133.418   8.144  22.948  1.00 51.58           N  
ATOM   5899  CA  LEU C 172    -133.311   8.787  24.240  1.00 58.67           C  
ATOM   5900  C   LEU C 172    -132.472   8.040  25.275  1.00 60.25           C  
ATOM   5901  O   LEU C 172    -131.622   8.639  25.938  1.00 69.77           O  
ATOM   5902  CB  LEU C 172    -134.721   9.061  24.767  1.00 67.06           C  
ATOM   5903  CG  LEU C 172    -134.834   9.678  26.150  1.00 74.19           C  
ATOM   5904  CD1 LEU C 172    -133.947  10.925  26.237  1.00 80.57           C  
ATOM   5905  CD2 LEU C 172    -136.298   9.982  26.440  1.00 68.89           C  
ATOM   5906  N   LYS C 173    -132.691   6.739  25.410  1.00 62.68           N  
ATOM   5907  CA  LYS C 173    -131.981   5.972  26.443  1.00 74.39           C  
ATOM   5908  C   LYS C 173    -130.630   5.358  25.957  1.00 75.45           C  
ATOM   5909  O   LYS C 173    -129.861   4.826  26.773  1.00 73.03           O  
ATOM   5910  CB  LYS C 173    -132.923   4.910  27.058  1.00 81.37           C  
ATOM   5911  CG  LYS C 173    -134.076   5.495  27.960  1.00 83.93           C  
ATOM   5912  CD  LYS C 173    -134.993   4.395  28.580  1.00 83.18           C  
ATOM   5913  CE  LYS C 173    -136.057   3.882  27.584  1.00 85.02           C  
ATOM   5914  NZ  LYS C 173    -136.530   2.479  27.849  1.00 75.48           N  
ATOM   5915  N   ALA C 174    -130.335   5.485  24.655  1.00 68.67           N  
ATOM   5916  CA  ALA C 174    -129.152   4.871  24.008  1.00 66.31           C  
ATOM   5917  C   ALA C 174    -127.844   5.663  24.205  1.00 67.95           C  
ATOM   5918  O   ALA C 174    -127.872   6.894  24.374  1.00 73.67           O  
ATOM   5919  CB  ALA C 174    -129.423   4.698  22.503  1.00 64.39           C  
ATOM   5920  N   ASN C 175    -126.708   4.961  24.143  1.00 56.01           N  
ATOM   5921  CA  ASN C 175    -125.396   5.582  24.366  1.00 56.62           C  
ATOM   5922  C   ASN C 175    -124.745   6.169  23.121  1.00 51.34           C  
ATOM   5923  O   ASN C 175    -124.547   7.376  23.042  1.00 52.85           O  
ATOM   5924  CB  ASN C 175    -124.435   4.586  25.006  1.00 64.06           C  
ATOM   5925  CG  ASN C 175    -124.814   4.253  26.432  1.00 74.20           C  
ATOM   5926  OD1 ASN C 175    -125.053   5.146  27.252  1.00 75.44           O  
ATOM   5927  ND2 ASN C 175    -124.871   2.957  26.740  1.00 81.01           N  
ATOM   5928  N   GLN C 176    -124.363   5.320  22.171  1.00 49.45           N  
ATOM   5929  CA  GLN C 176    -123.828   5.816  20.905  1.00 48.44           C  
ATOM   5930  C   GLN C 176    -125.010   6.030  19.974  1.00 38.95           C  
ATOM   5931  O   GLN C 176    -126.006   5.322  20.053  1.00 37.21           O  
ATOM   5932  CB  GLN C 176    -122.774   4.865  20.262  1.00 49.71           C  
ATOM   5933  CG  GLN C 176    -121.853   5.609  19.230  1.00 61.26           C  
ATOM   5934  CD  GLN C 176    -121.035   4.723  18.229  1.00 72.62           C  
ATOM   5935  OE1 GLN C 176    -119.917   4.270  18.547  1.00 68.04           O  
ATOM   5936  NE2 GLN C 176    -121.560   4.560  16.987  1.00 58.99           N  
ATOM   5937  N   GLN C 177    -124.902   7.034  19.114  1.00 39.03           N  
ATOM   5938  CA  GLN C 177    -125.793   7.160  17.964  1.00 37.21           C  
ATOM   5939  C   GLN C 177    -125.523   6.098  16.915  1.00 32.23           C  
ATOM   5940  O   GLN C 177    -124.526   5.366  16.994  1.00 36.33           O  
ATOM   5941  CB  GLN C 177    -125.588   8.501  17.306  1.00 37.08           C  
ATOM   5942  CG  GLN C 177    -124.248   8.639  16.636  1.00 33.06           C  
ATOM   5943  CD  GLN C 177    -123.705   9.997  16.870  1.00 39.39           C  
ATOM   5944  OE1 GLN C 177    -123.743  10.865  15.987  1.00 40.33           O  
ATOM   5945  NE2 GLN C 177    -123.250  10.231  18.101  1.00 46.67           N  
ATOM   5946  N   PHE C 178    -126.381   6.054  15.901  1.00 23.78           N  
ATOM   5947  CA  PHE C 178    -126.257   5.025  14.877  1.00 19.36           C  
ATOM   5948  C   PHE C 178    -126.936   5.328  13.570  1.00 12.61           C  
ATOM   5949  O   PHE C 178    -128.142   5.595  13.532  1.00 15.13           O  
ATOM   5950  CB  PHE C 178    -126.794   3.688  15.415  1.00 20.27           C  
ATOM   5951  CG  PHE C 178    -128.188   3.745  15.992  1.00  9.71           C  
ATOM   5952  CD1 PHE C 178    -129.286   3.325  15.257  1.00 10.82           C  
ATOM   5953  CD2 PHE C 178    -128.385   4.149  17.269  1.00  5.37           C  
ATOM   5954  CE1 PHE C 178    -130.587   3.347  15.796  1.00 10.97           C  
ATOM   5955  CE2 PHE C 178    -129.671   4.157  17.808  1.00 10.89           C  
ATOM   5956  CZ  PHE C 178    -130.781   3.767  17.054  1.00  7.26           C  
ATOM   5957  N   LEU C 179    -126.187   5.228  12.486  1.00  9.16           N  
ATOM   5958  CA  LEU C 179    -126.776   5.526  11.166  1.00 14.75           C  
ATOM   5959  C   LEU C 179    -128.019   4.643  10.820  1.00 10.89           C  
ATOM   5960  O   LEU C 179    -128.053   3.457  11.143  1.00 11.28           O  
ATOM   5961  CB  LEU C 179    -125.696   5.442  10.070  1.00  8.45           C  
ATOM   5962  CG  LEU C 179    -125.919   6.164   8.733  1.00  7.32           C  
ATOM   5963  CD1 LEU C 179    -124.812   5.695   7.828  1.00  6.60           C  
ATOM   5964  CD2 LEU C 179    -127.301   5.961   8.059  1.00  2.87           C  
ATOM   5965  N   VAL C 180    -129.012   5.278  10.194  1.00 11.89           N  
ATOM   5966  CA  VAL C 180    -130.257   4.668   9.734  1.00 10.11           C  
ATOM   5967  C   VAL C 180    -130.707   5.314   8.400  1.00 11.02           C  
ATOM   5968  O   VAL C 180    -129.908   5.969   7.690  1.00 10.67           O  
ATOM   5969  CB  VAL C 180    -131.377   4.877  10.763  1.00 14.50           C  
ATOM   5970  CG1 VAL C 180    -131.021   4.146  12.088  1.00  6.49           C  
ATOM   5971  CG2 VAL C 180    -131.720   6.446  10.914  1.00 14.24           C  
ATOM   5972  N   TYR C 181    -131.970   5.088   8.032  1.00  6.01           N  
ATOM   5973  CA  TYR C 181    -132.478   5.500   6.725  1.00  7.73           C  
ATOM   5974  C   TYR C 181    -133.912   5.990   6.940  1.00 13.68           C  
ATOM   5975  O   TYR C 181    -134.852   5.226   7.275  1.00  8.62           O  
ATOM   5976  CB  TYR C 181    -132.380   4.387   5.703  1.00  2.08           C  
ATOM   5977  CG  TYR C 181    -132.913   4.713   4.404  1.00  2.00           C  
ATOM   5978  CD1 TYR C 181    -132.111   5.003   3.408  1.00  6.01           C  
ATOM   5979  CD2 TYR C 181    -134.214   4.713   4.177  1.00  4.25           C  
ATOM   5980  CE1 TYR C 181    -132.576   5.317   2.134  1.00  5.06           C  
ATOM   5981  CE2 TYR C 181    -134.747   5.026   2.931  1.00  8.79           C  
ATOM   5982  CZ  TYR C 181    -133.885   5.337   1.885  1.00 12.25           C  
ATOM   5983  OH  TYR C 181    -134.308   5.678   0.596  1.00 15.68           O  
ATOM   5984  N   CYS C 182    -134.034   7.314   6.770  1.00 21.22           N  
ATOM   5985  CA  CYS C 182    -135.267   8.055   6.901  1.00 22.05           C  
ATOM   5986  C   CYS C 182    -135.802   8.231   5.512  1.00 19.50           C  
ATOM   5987  O   CYS C 182    -135.090   8.701   4.581  1.00 14.00           O  
ATOM   5988  CB  CYS C 182    -134.968   9.381   7.535  1.00 23.93           C  
ATOM   5989  SG  CYS C 182    -134.103   9.145   9.059  1.00 24.25           S  
ATOM   5990  N   GLU C 183    -137.028   7.753   5.386  1.00 23.24           N  
ATOM   5991  CA  GLU C 183    -137.729   7.703   4.141  1.00 32.26           C  
ATOM   5992  C   GLU C 183    -138.726   8.725   4.409  1.00 33.21           C  
ATOM   5993  O   GLU C 183    -139.711   8.449   5.124  1.00 32.72           O  
ATOM   5994  CB  GLU C 183    -138.442   6.367   3.923  1.00 40.83           C  
ATOM   5995  CG  GLU C 183    -139.297   6.333   2.655  1.00 40.53           C  
ATOM   5996  CD  GLU C 183    -140.382   5.269   2.732  1.00 54.84           C  
ATOM   5997  OE1 GLU C 183    -141.571   5.678   2.592  1.00 56.89           O  
ATOM   5998  OE2 GLU C 183    -140.072   4.051   2.942  1.00 38.75           O  
ATOM   5999  N   ILE C 184    -138.433   9.910   3.879  1.00 31.22           N  
ATOM   6000  CA  ILE C 184    -139.178  11.122   4.191  1.00 27.58           C  
ATOM   6001  C   ILE C 184    -140.127  11.354   3.024  1.00 30.30           C  
ATOM   6002  O   ILE C 184    -139.685  11.334   1.857  1.00 26.43           O  
ATOM   6003  CB  ILE C 184    -138.212  12.296   4.400  1.00 20.07           C  
ATOM   6004  CG1 ILE C 184    -137.606  12.260   5.826  1.00 17.65           C  
ATOM   6005  CG2 ILE C 184    -138.915  13.592   4.133  1.00 20.79           C  
ATOM   6006  CD1 ILE C 184    -136.107  12.689   5.883  1.00 10.65           C  
ATOM   6007  N   ASP C 185    -141.421  11.502   3.336  1.00 28.84           N  
ATOM   6008  CA  ASP C 185    -142.447  11.764   2.313  1.00 34.74           C  
ATOM   6009  C   ASP C 185    -142.931  13.232   2.276  1.00 36.11           C  
ATOM   6010  O   ASP C 185    -142.398  14.125   2.966  1.00 33.01           O  
ATOM   6011  CB  ASP C 185    -143.641  10.773   2.439  1.00 39.27           C  
ATOM   6012  CG  ASP C 185    -144.531  11.023   3.682  1.00 41.01           C  
ATOM   6013  OD1 ASP C 185    -145.713  10.558   3.717  1.00 40.34           O  
ATOM   6014  OD2 ASP C 185    -144.033  11.659   4.637  1.00 42.20           O  
ATOM   6015  N   GLY C 186    -143.939  13.462   1.440  1.00 42.53           N  
ATOM   6016  CA  GLY C 186    -144.387  14.805   1.112  1.00 46.86           C  
ATOM   6017  C   GLY C 186    -145.048  15.501   2.276  1.00 47.43           C  
ATOM   6018  O   GLY C 186    -144.932  16.737   2.421  1.00 44.77           O  
ATOM   6019  N   SER C 187    -145.736  14.700   3.094  1.00 43.63           N  
ATOM   6020  CA  SER C 187    -146.388  15.189   4.304  1.00 42.11           C  
ATOM   6021  C   SER C 187    -145.474  15.085   5.533  1.00 35.92           C  
ATOM   6022  O   SER C 187    -145.943  15.182   6.669  1.00 34.70           O  
ATOM   6023  CB  SER C 187    -147.699  14.432   4.538  1.00 43.26           C  
ATOM   6024  OG  SER C 187    -147.485  13.029   4.625  1.00 43.83           O  
ATOM   6025  N   GLY C 188    -144.178  14.870   5.303  1.00 34.54           N  
ATOM   6026  CA  GLY C 188    -143.164  15.083   6.347  1.00 35.05           C  
ATOM   6027  C   GLY C 188    -143.232  14.048   7.440  1.00 28.09           C  
ATOM   6028  O   GLY C 188    -142.951  14.292   8.623  1.00 27.84           O  
ATOM   6029  N   ASN C 189    -143.620  12.875   6.997  1.00 32.47           N  
ATOM   6030  CA  ASN C 189    -143.576  11.702   7.797  1.00 31.37           C  
ATOM   6031  C   ASN C 189    -142.207  11.043   7.581  1.00 25.03           C  
ATOM   6032  O   ASN C 189    -141.788  10.754   6.429  1.00 20.91           O  
ATOM   6033  CB  ASN C 189    -144.770  10.842   7.421  1.00 33.26           C  
ATOM   6034  CG  ASN C 189    -146.087  11.622   7.548  1.00 32.24           C  
ATOM   6035  OD1 ASN C 189    -146.217  12.485   8.434  1.00 31.35           O  
ATOM   6036  ND2 ASN C 189    -147.047  11.338   6.664  1.00 24.51           N  
ATOM   6037  N   GLY C 190    -141.496  10.925   8.707  1.00 26.92           N  
ATOM   6038  CA  GLY C 190    -140.128  10.453   8.765  1.00 29.09           C  
ATOM   6039  C   GLY C 190    -140.169   8.980   9.109  1.00 32.51           C  
ATOM   6040  O   GLY C 190    -140.191   8.580  10.296  1.00 32.88           O  
ATOM   6041  N   TRP C 191    -140.202   8.179   8.048  1.00 28.97           N  
ATOM   6042  CA  TRP C 191    -140.196   6.741   8.157  1.00 29.62           C  
ATOM   6043  C   TRP C 191    -138.784   6.215   8.437  1.00 36.81           C  
ATOM   6044  O   TRP C 191    -137.871   6.336   7.603  1.00 38.41           O  
ATOM   6045  CB  TRP C 191    -140.694   6.140   6.861  1.00 28.20           C  
ATOM   6046  CG  TRP C 191    -142.155   6.148   6.741  1.00 31.54           C  
ATOM   6047  CD1 TRP C 191    -142.906   6.915   5.891  1.00 30.18           C  
ATOM   6048  CD2 TRP C 191    -143.074   5.347   7.482  1.00 34.70           C  
ATOM   6049  NE1 TRP C 191    -144.238   6.651   6.072  1.00 31.74           N  
ATOM   6050  CE2 TRP C 191    -144.375   5.684   7.035  1.00 31.65           C  
ATOM   6051  CE3 TRP C 191    -142.931   4.368   8.467  1.00 28.96           C  
ATOM   6052  CZ2 TRP C 191    -145.527   5.066   7.532  1.00 21.88           C  
ATOM   6053  CZ3 TRP C 191    -144.083   3.775   8.972  1.00 27.57           C  
ATOM   6054  CH2 TRP C 191    -145.367   4.135   8.499  1.00 20.38           C  
ATOM   6055  N   THR C 192    -138.605   5.624   9.608  1.00 33.58           N  
ATOM   6056  CA  THR C 192    -137.367   4.934   9.932  1.00 30.72           C  
ATOM   6057  C   THR C 192    -137.445   3.460   9.572  1.00 34.42           C  
ATOM   6058  O   THR C 192    -138.304   2.776  10.092  1.00 41.36           O  
ATOM   6059  CB  THR C 192    -137.139   4.986  11.407  1.00 30.27           C  
ATOM   6060  OG1 THR C 192    -136.990   6.369  11.811  1.00 28.83           O  
ATOM   6061  CG2 THR C 192    -135.932   4.078  11.755  1.00 26.29           C  
ATOM   6062  N   VAL C 193    -136.552   2.959   8.724  1.00 23.88           N  
ATOM   6063  CA  VAL C 193    -136.726   1.642   8.076  1.00 20.85           C  
ATOM   6064  C   VAL C 193    -135.841   0.648   8.764  1.00 26.77           C  
ATOM   6065  O   VAL C 193    -134.596   0.736   8.612  1.00 28.66           O  
ATOM   6066  CB  VAL C 193    -136.280   1.698   6.576  1.00 17.18           C  
ATOM   6067  CG1 VAL C 193    -136.179   0.371   6.005  1.00 24.07           C  
ATOM   6068  CG2 VAL C 193    -137.229   2.506   5.762  1.00 18.63           C  
ATOM   6069  N   PHE C 194    -136.419  -0.322   9.483  1.00 26.79           N  
ATOM   6070  CA  PHE C 194    -135.528  -1.287  10.186  1.00 34.38           C  
ATOM   6071  C   PHE C 194    -135.324  -2.623   9.476  1.00 33.83           C  
ATOM   6072  O   PHE C 194    -134.515  -3.420   9.901  1.00 34.73           O  
ATOM   6073  CB  PHE C 194    -135.905  -1.519  11.647  1.00 33.23           C  
ATOM   6074  CG  PHE C 194    -137.094  -2.340  11.810  1.00 35.04           C  
ATOM   6075  CD1 PHE C 194    -137.014  -3.715  11.702  1.00 43.25           C  
ATOM   6076  CD2 PHE C 194    -138.322  -1.741  12.019  1.00 37.57           C  
ATOM   6077  CE1 PHE C 194    -138.160  -4.495  11.826  1.00 52.83           C  
ATOM   6078  CE2 PHE C 194    -139.463  -2.492  12.151  1.00 45.10           C  
ATOM   6079  CZ  PHE C 194    -139.397  -3.879  12.057  1.00 48.57           C  
ATOM   6080  N   GLN C 195    -136.018  -2.883   8.398  1.00 24.94           N  
ATOM   6081  CA  GLN C 195    -135.590  -3.967   7.582  1.00 26.98           C  
ATOM   6082  C   GLN C 195    -135.950  -3.517   6.191  1.00 24.01           C  
ATOM   6083  O   GLN C 195    -136.861  -2.734   6.018  1.00 20.47           O  
ATOM   6084  CB  GLN C 195    -136.298  -5.260   8.031  1.00 33.85           C  
ATOM   6085  CG  GLN C 195    -135.891  -6.577   7.314  1.00 34.16           C  
ATOM   6086  CD  GLN C 195    -136.688  -6.840   6.066  1.00 34.92           C  
ATOM   6087  OE1 GLN C 195    -136.354  -6.336   5.015  1.00 38.46           O  
ATOM   6088  NE2 GLN C 195    -137.761  -7.601   6.179  1.00 33.90           N  
ATOM   6089  N   LYS C 196    -135.200  -4.002   5.215  1.00 27.68           N  
ATOM   6090  CA  LYS C 196    -135.507  -3.853   3.795  1.00 31.16           C  
ATOM   6091  C   LYS C 196    -135.054  -5.169   3.087  1.00 31.80           C  
ATOM   6092  O   LYS C 196    -134.092  -5.807   3.534  1.00 27.86           O  
ATOM   6093  CB  LYS C 196    -134.751  -2.640   3.263  1.00 29.20           C  
ATOM   6094  CG  LYS C 196    -135.017  -2.294   1.831  1.00 34.53           C  
ATOM   6095  CD  LYS C 196    -136.454  -1.823   1.643  1.00 43.20           C  
ATOM   6096  CE  LYS C 196    -136.597  -0.926   0.438  1.00 49.72           C  
ATOM   6097  NZ  LYS C 196    -135.622   0.232   0.530  1.00 65.53           N  
ATOM   6098  N   ARG C 197    -135.755  -5.613   2.041  1.00 30.30           N  
ATOM   6099  CA  ARG C 197    -135.308  -6.779   1.236  1.00 32.75           C  
ATOM   6100  C   ARG C 197    -135.613  -6.443  -0.220  1.00 42.20           C  
ATOM   6101  O   ARG C 197    -136.522  -5.630  -0.471  1.00 44.70           O  
ATOM   6102  CB  ARG C 197    -136.042  -8.096   1.612  1.00 35.50           C  
ATOM   6103  CG  ARG C 197    -136.108  -8.415   3.127  1.00 38.19           C  
ATOM   6104  CD  ARG C 197    -135.848  -9.911   3.605  1.00 35.44           C  
ATOM   6105  NE  ARG C 197    -134.433 -10.306   3.482  1.00 26.58           N  
ATOM   6106  CZ  ARG C 197    -133.986 -11.132   2.551  1.00 32.95           C  
ATOM   6107  NH1 ARG C 197    -134.845 -11.696   1.702  1.00 32.66           N  
ATOM   6108  NH2 ARG C 197    -132.694 -11.415   2.448  1.00 36.21           N  
ATOM   6109  N   LEU C 198    -134.902  -7.067  -1.178  1.00 44.80           N  
ATOM   6110  CA  LEU C 198    -135.152  -6.809  -2.648  1.00 39.16           C  
ATOM   6111  C   LEU C 198    -134.381  -7.702  -3.701  1.00 30.50           C  
ATOM   6112  O   LEU C 198    -134.803  -7.806  -4.873  1.00 23.75           O  
ATOM   6113  CB  LEU C 198    -134.941  -5.297  -2.991  1.00 29.51           C  
ATOM   6114  CG  LEU C 198    -133.665  -4.736  -2.361  1.00 26.66           C  
ATOM   6115  CD1 LEU C 198    -132.678  -4.211  -3.379  1.00 23.88           C  
ATOM   6116  CD2 LEU C 198    -134.061  -3.719  -1.323  1.00 29.58           C  
ATOM   6117  N   ASP C 199    -133.255  -8.295  -3.322  1.00 24.65           N  
ATOM   6118  CA  ASP C 199    -132.485  -9.063  -4.291  1.00 31.75           C  
ATOM   6119  C   ASP C 199    -131.821 -10.371  -3.734  1.00 41.72           C  
ATOM   6120  O   ASP C 199    -131.320 -11.226  -4.498  1.00 35.59           O  
ATOM   6121  CB  ASP C 199    -131.457  -8.141  -4.914  1.00 30.01           C  
ATOM   6122  CG  ASP C 199    -130.396  -7.669  -3.909  1.00 35.68           C  
ATOM   6123  OD1 ASP C 199    -130.439  -8.119  -2.737  1.00 37.71           O  
ATOM   6124  OD2 ASP C 199    -129.500  -6.856  -4.296  1.00 33.36           O  
ATOM   6125  N   GLY C 200    -131.838 -10.532  -2.411  1.00 40.76           N  
ATOM   6126  CA  GLY C 200    -131.169 -11.638  -1.776  1.00 41.45           C  
ATOM   6127  C   GLY C 200    -129.650 -11.524  -1.800  1.00 40.16           C  
ATOM   6128  O   GLY C 200    -128.957 -12.434  -1.350  1.00 44.01           O  
ATOM   6129  N   SER C 201    -129.105 -10.414  -2.282  1.00 36.96           N  
ATOM   6130  CA  SER C 201    -127.687 -10.137  -2.056  1.00 39.18           C  
ATOM   6131  C   SER C 201    -127.233 -10.531  -0.647  1.00 30.24           C  
ATOM   6132  O   SER C 201    -126.139 -10.992  -0.469  1.00 39.72           O  
ATOM   6133  CB  SER C 201    -127.368  -8.643  -2.265  1.00 47.34           C  
ATOM   6134  OG  SER C 201    -128.068  -7.786  -1.344  1.00 48.90           O  
ATOM   6135  N   VAL C 202    -128.064 -10.347   0.358  1.00 26.44           N  
ATOM   6136  CA  VAL C 202    -127.608 -10.498   1.737  1.00 27.48           C  
ATOM   6137  C   VAL C 202    -128.073 -11.820   2.344  1.00 19.18           C  
ATOM   6138  O   VAL C 202    -129.217 -12.264   2.181  1.00 15.90           O  
ATOM   6139  CB  VAL C 202    -127.998  -9.209   2.638  1.00 26.78           C  
ATOM   6140  CG1 VAL C 202    -127.547  -9.283   4.168  1.00 11.36           C  
ATOM   6141  CG2 VAL C 202    -127.369  -7.995   2.012  1.00 27.29           C  
ATOM   6142  N   ASP C 203    -127.158 -12.431   3.079  1.00 19.94           N  
ATOM   6143  CA  ASP C 203    -127.497 -13.647   3.732  1.00 24.95           C  
ATOM   6144  C   ASP C 203    -128.151 -13.341   5.040  1.00 15.84           C  
ATOM   6145  O   ASP C 203    -127.483 -12.899   5.951  1.00  9.62           O  
ATOM   6146  CB  ASP C 203    -126.269 -14.546   3.930  1.00 36.33           C  
ATOM   6147  CG  ASP C 203    -126.642 -15.978   4.377  1.00 41.09           C  
ATOM   6148  OD1 ASP C 203    -125.758 -16.607   5.029  1.00 37.25           O  
ATOM   6149  OD2 ASP C 203    -127.787 -16.449   4.076  1.00 29.32           O  
ATOM   6150  N   PHE C 204    -129.454 -13.607   5.118  1.00 24.34           N  
ATOM   6151  CA  PHE C 204    -130.203 -13.537   6.402  1.00 31.10           C  
ATOM   6152  C   PHE C 204    -130.152 -14.787   7.305  1.00 35.43           C  
ATOM   6153  O   PHE C 204    -130.818 -14.834   8.370  1.00 27.45           O  
ATOM   6154  CB  PHE C 204    -131.649 -13.182   6.131  1.00 26.39           C  
ATOM   6155  CG  PHE C 204    -131.855 -11.727   5.961  1.00 25.93           C  
ATOM   6156  CD1 PHE C 204    -132.526 -10.997   6.893  1.00 23.43           C  
ATOM   6157  CD2 PHE C 204    -131.313 -11.078   4.892  1.00 30.32           C  
ATOM   6158  CE1 PHE C 204    -132.682  -9.710   6.728  1.00 20.92           C  
ATOM   6159  CE2 PHE C 204    -131.488  -9.755   4.736  1.00 23.83           C  
ATOM   6160  CZ  PHE C 204    -132.156  -9.085   5.642  1.00 18.52           C  
ATOM   6161  N   LYS C 205    -129.369 -15.779   6.872  1.00 25.16           N  
ATOM   6162  CA  LYS C 205    -129.120 -16.944   7.662  1.00 23.30           C  
ATOM   6163  C   LYS C 205    -127.998 -16.480   8.559  1.00 13.60           C  
ATOM   6164  O   LYS C 205    -126.813 -16.468   8.166  1.00 10.75           O  
ATOM   6165  CB  LYS C 205    -128.763 -18.125   6.729  1.00 39.23           C  
ATOM   6166  CG  LYS C 205    -128.297 -19.464   7.365  1.00 43.24           C  
ATOM   6167  CD  LYS C 205    -129.111 -19.842   8.612  1.00 45.72           C  
ATOM   6168  CE  LYS C 205    -128.269 -20.635   9.593  1.00 48.57           C  
ATOM   6169  NZ  LYS C 205    -127.017 -19.900   9.991  1.00 43.22           N  
ATOM   6170  N   LYS C 206    -128.386 -16.021   9.747  1.00 13.38           N  
ATOM   6171  CA  LYS C 206    -127.455 -15.259  10.614  1.00 15.43           C  
ATOM   6172  C   LYS C 206    -127.726 -15.519  12.080  1.00 12.22           C  
ATOM   6173  O   LYS C 206    -128.882 -15.787  12.506  1.00  9.23           O  
ATOM   6174  CB  LYS C 206    -127.552 -13.706  10.409  1.00 15.70           C  
ATOM   6175  CG  LYS C 206    -127.345 -13.082   8.988  1.00 12.55           C  
ATOM   6176  CD  LYS C 206    -125.876 -13.239   8.479  1.00 14.38           C  
ATOM   6177  CE  LYS C 206    -125.379 -12.063   7.627  1.00 13.69           C  
ATOM   6178  NZ  LYS C 206    -124.796 -12.385   6.217  1.00 13.64           N  
ATOM   6179  N   ASN C 207    -126.674 -15.338  12.864  1.00 14.07           N  
ATOM   6180  CA  ASN C 207    -126.706 -15.771  14.246  1.00 17.19           C  
ATOM   6181  C   ASN C 207    -127.422 -14.801  15.160  1.00 18.28           C  
ATOM   6182  O   ASN C 207    -127.883 -13.785  14.715  1.00 20.90           O  
ATOM   6183  CB  ASN C 207    -125.286 -15.995  14.724  1.00 16.96           C  
ATOM   6184  CG  ASN C 207    -124.613 -14.723  15.088  1.00 11.71           C  
ATOM   6185  OD1 ASN C 207    -125.121 -13.996  15.933  1.00 12.64           O  
ATOM   6186  ND2 ASN C 207    -123.450 -14.447  14.473  1.00  8.98           N  
ATOM   6187  N   TRP C 208    -127.484 -15.111  16.446  1.00 24.33           N  
ATOM   6188  CA  TRP C 208    -128.075 -14.201  17.413  1.00 27.49           C  
ATOM   6189  C   TRP C 208    -127.441 -12.796  17.423  1.00 32.37           C  
ATOM   6190  O   TRP C 208    -128.140 -11.798  17.168  1.00 32.45           O  
ATOM   6191  CB  TRP C 208    -128.017 -14.789  18.812  1.00 26.99           C  
ATOM   6192  CG  TRP C 208    -128.572 -13.862  19.784  1.00 28.31           C  
ATOM   6193  CD1 TRP C 208    -127.880 -12.984  20.553  1.00 33.96           C  
ATOM   6194  CD2 TRP C 208    -129.949 -13.658  20.076  1.00 34.42           C  
ATOM   6195  NE1 TRP C 208    -128.742 -12.257  21.337  1.00 37.47           N  
ATOM   6196  CE2 TRP C 208    -130.022 -12.650  21.060  1.00 33.73           C  
ATOM   6197  CE3 TRP C 208    -131.134 -14.245  19.622  1.00 37.61           C  
ATOM   6198  CZ2 TRP C 208    -131.229 -12.207  21.588  1.00 29.62           C  
ATOM   6199  CZ3 TRP C 208    -132.341 -13.802  20.158  1.00 37.21           C  
ATOM   6200  CH2 TRP C 208    -132.374 -12.793  21.132  1.00 31.48           C  
ATOM   6201  N   ILE C 209    -126.145 -12.710  17.737  1.00 26.93           N  
ATOM   6202  CA  ILE C 209    -125.449 -11.387  17.841  1.00 27.33           C  
ATOM   6203  C   ILE C 209    -125.667 -10.533  16.582  1.00 24.41           C  
ATOM   6204  O   ILE C 209    -126.209  -9.452  16.645  1.00 26.22           O  
ATOM   6205  CB  ILE C 209    -123.887 -11.495  18.005  1.00 24.37           C  
ATOM   6206  CG1 ILE C 209    -123.455 -12.547  19.021  1.00 25.15           C  
ATOM   6207  CG2 ILE C 209    -123.334 -10.179  18.404  1.00 25.47           C  
ATOM   6208  CD1 ILE C 209    -122.014 -13.003  18.782  1.00 29.97           C  
ATOM   6209  N   GLN C 210    -125.214 -11.053  15.447  1.00 25.30           N  
ATOM   6210  CA  GLN C 210    -125.459 -10.485  14.143  1.00 29.23           C  
ATOM   6211  C   GLN C 210    -126.838  -9.848  14.058  1.00 33.74           C  
ATOM   6212  O   GLN C 210    -127.016  -8.722  13.568  1.00 35.14           O  
ATOM   6213  CB  GLN C 210    -125.349 -11.583  13.086  1.00 29.43           C  
ATOM   6214  CG  GLN C 210    -123.955 -11.664  12.514  1.00 35.05           C  
ATOM   6215  CD  GLN C 210    -123.650 -12.956  11.744  1.00 38.80           C  
ATOM   6216  OE1 GLN C 210    -124.496 -13.855  11.595  1.00 34.40           O  
ATOM   6217  NE2 GLN C 210    -122.405 -13.056  11.270  1.00 47.18           N  
ATOM   6218  N   TYR C 211    -127.833 -10.553  14.541  1.00 27.63           N  
ATOM   6219  CA  TYR C 211    -129.157 -10.031  14.379  1.00 28.96           C  
ATOM   6220  C   TYR C 211    -129.442  -8.844  15.298  1.00 32.78           C  
ATOM   6221  O   TYR C 211    -130.312  -8.004  14.985  1.00 29.94           O  
ATOM   6222  CB  TYR C 211    -130.182 -11.144  14.546  1.00 23.91           C  
ATOM   6223  CG  TYR C 211    -130.776 -11.577  13.230  1.00 12.86           C  
ATOM   6224  CD1 TYR C 211    -130.023 -12.161  12.247  1.00  9.22           C  
ATOM   6225  CD2 TYR C 211    -132.102 -11.388  12.989  1.00 12.68           C  
ATOM   6226  CE1 TYR C 211    -130.623 -12.557  11.034  1.00 11.83           C  
ATOM   6227  CE2 TYR C 211    -132.698 -11.767  11.814  1.00 11.78           C  
ATOM   6228  CZ  TYR C 211    -131.968 -12.341  10.833  1.00 11.31           C  
ATOM   6229  OH  TYR C 211    -132.630 -12.727   9.692  1.00 13.61           O  
ATOM   6230  N   LYS C 212    -128.707  -8.783  16.409  1.00 30.18           N  
ATOM   6231  CA  LYS C 212    -128.967  -7.820  17.481  1.00 31.76           C  
ATOM   6232  C   LYS C 212    -128.298  -6.493  17.106  1.00 33.43           C  
ATOM   6233  O   LYS C 212    -128.906  -5.395  17.098  1.00 30.33           O  
ATOM   6234  CB  LYS C 212    -128.454  -8.403  18.817  1.00 29.11           C  
ATOM   6235  CG  LYS C 212    -127.737  -7.436  19.714  1.00 36.31           C  
ATOM   6236  CD  LYS C 212    -127.546  -7.994  21.115  1.00 45.63           C  
ATOM   6237  CE  LYS C 212    -127.128  -6.900  22.136  1.00 48.44           C  
ATOM   6238  NZ  LYS C 212    -125.664  -6.804  22.339  1.00 50.75           N  
ATOM   6239  N   GLU C 213    -127.038  -6.649  16.742  1.00 29.83           N  
ATOM   6240  CA  GLU C 213    -126.188  -5.558  16.378  1.00 31.27           C  
ATOM   6241  C   GLU C 213    -126.518  -5.109  14.983  1.00 28.70           C  
ATOM   6242  O   GLU C 213    -126.213  -3.981  14.593  1.00 30.01           O  
ATOM   6243  CB  GLU C 213    -124.729  -5.997  16.460  1.00 34.92           C  
ATOM   6244  CG  GLU C 213    -124.329  -6.512  17.846  1.00 41.68           C  
ATOM   6245  CD  GLU C 213    -124.258  -5.423  18.929  1.00 52.37           C  
ATOM   6246  OE1 GLU C 213    -123.666  -5.733  20.003  1.00 56.53           O  
ATOM   6247  OE2 GLU C 213    -124.774  -4.278  18.718  1.00 52.64           O  
ATOM   6248  N   GLY C 214    -127.158  -5.983  14.227  1.00 24.29           N  
ATOM   6249  CA  GLY C 214    -127.637  -5.589  12.926  1.00 19.96           C  
ATOM   6250  C   GLY C 214    -126.578  -5.938  11.922  1.00 13.90           C  
ATOM   6251  O   GLY C 214    -125.426  -6.295  12.296  1.00  5.39           O  
ATOM   6252  N   PHE C 215    -126.985  -5.799  10.655  1.00  9.17           N  
ATOM   6253  CA  PHE C 215    -126.260  -6.341   9.506  1.00  8.26           C  
ATOM   6254  C   PHE C 215    -126.941  -5.831   8.204  1.00  8.24           C  
ATOM   6255  O   PHE C 215    -128.145  -5.481   8.189  1.00  4.96           O  
ATOM   6256  CB  PHE C 215    -126.124  -7.912   9.606  1.00  5.32           C  
ATOM   6257  CG  PHE C 215    -127.337  -8.638   9.255  1.00  6.70           C  
ATOM   6258  CD1 PHE C 215    -127.525  -9.115   7.951  1.00  7.84           C  
ATOM   6259  CD2 PHE C 215    -128.335  -8.797  10.179  1.00  6.94           C  
ATOM   6260  CE1 PHE C 215    -128.762  -9.765   7.579  1.00  9.45           C  
ATOM   6261  CE2 PHE C 215    -129.566  -9.429   9.825  1.00  9.73           C  
ATOM   6262  CZ  PHE C 215    -129.776  -9.916   8.520  1.00  9.11           C  
ATOM   6263  N   GLY C 216    -126.160  -5.794   7.128  1.00 14.66           N  
ATOM   6264  CA  GLY C 216    -126.593  -5.256   5.824  1.00 21.74           C  
ATOM   6265  C   GLY C 216    -125.783  -4.014   5.450  1.00 35.37           C  
ATOM   6266  O   GLY C 216    -124.775  -3.676   6.129  1.00 37.80           O  
ATOM   6267  N   HIS C 217    -126.206  -3.342   4.373  1.00 32.62           N  
ATOM   6268  CA  HIS C 217    -125.699  -1.993   4.026  1.00 26.55           C  
ATOM   6269  C   HIS C 217    -126.800  -0.888   3.860  1.00 24.58           C  
ATOM   6270  O   HIS C 217    -127.782  -1.044   3.106  1.00 23.54           O  
ATOM   6271  CB  HIS C 217    -124.845  -2.107   2.780  1.00 29.25           C  
ATOM   6272  CG  HIS C 217    -123.635  -2.976   2.971  1.00 42.63           C  
ATOM   6273  ND1 HIS C 217    -123.680  -4.349   2.854  1.00 43.03           N  
ATOM   6274  CD2 HIS C 217    -122.354  -2.665   3.304  1.00 39.95           C  
ATOM   6275  CE1 HIS C 217    -122.474  -4.840   3.087  1.00 45.23           C  
ATOM   6276  NE2 HIS C 217    -121.653  -3.841   3.365  1.00 35.94           N  
ATOM   6277  N   LEU C 218    -126.646   0.214   4.591  1.00 19.93           N  
ATOM   6278  CA  LEU C 218    -127.462   1.390   4.384  1.00  8.23           C  
ATOM   6279  C   LEU C 218    -126.985   2.018   3.087  1.00 12.28           C  
ATOM   6280  O   LEU C 218    -125.795   2.199   2.878  1.00 10.70           O  
ATOM   6281  CB  LEU C 218    -127.265   2.343   5.533  1.00  7.31           C  
ATOM   6282  CG  LEU C 218    -127.822   1.793   6.845  1.00  8.66           C  
ATOM   6283  CD1 LEU C 218    -127.206   2.456   8.127  1.00  6.30           C  
ATOM   6284  CD2 LEU C 218    -129.347   1.875   6.866  1.00  6.25           C  
ATOM   6285  N   SER C 219    -127.911   2.275   2.180  1.00 18.40           N  
ATOM   6286  CA  SER C 219    -127.654   3.084   0.984  1.00 23.08           C  
ATOM   6287  C   SER C 219    -128.521   4.343   1.209  1.00 23.75           C  
ATOM   6288  O   SER C 219    -129.396   4.321   2.083  1.00 24.77           O  
ATOM   6289  CB  SER C 219    -128.084   2.358  -0.316  1.00 21.65           C  
ATOM   6290  OG  SER C 219    -129.519   2.156  -0.395  1.00 24.04           O  
ATOM   6291  N   PRO C 220    -128.242   5.443   0.472  1.00 17.73           N  
ATOM   6292  CA  PRO C 220    -129.070   6.577   0.241  1.00 10.25           C  
ATOM   6293  C   PRO C 220    -130.297   6.216  -0.501  1.00 11.25           C  
ATOM   6294  O   PRO C 220    -131.434   6.398   0.014  1.00  9.79           O  
ATOM   6295  CB  PRO C 220    -128.214   7.413  -0.680  1.00 17.52           C  
ATOM   6296  CG  PRO C 220    -126.889   7.221  -0.179  1.00 21.14           C  
ATOM   6297  CD  PRO C 220    -126.834   5.801   0.270  1.00 23.73           C  
ATOM   6298  N   THR C 221    -130.090   5.699  -1.713  1.00 10.43           N  
ATOM   6299  CA  THR C 221    -131.203   5.530  -2.690  1.00 13.77           C  
ATOM   6300  C   THR C 221    -132.305   4.568  -2.245  1.00 18.84           C  
ATOM   6301  O   THR C 221    -133.476   4.930  -2.237  1.00 22.14           O  
ATOM   6302  CB  THR C 221    -130.703   5.050  -4.013  1.00 15.68           C  
ATOM   6303  OG1 THR C 221    -129.254   5.093  -4.024  1.00 23.88           O  
ATOM   6304  CG2 THR C 221    -131.314   5.897  -5.118  1.00 13.27           C  
ATOM   6305  N   GLY C 222    -131.923   3.357  -1.849  1.00 27.47           N  
ATOM   6306  CA  GLY C 222    -132.847   2.417  -1.164  1.00 34.97           C  
ATOM   6307  C   GLY C 222    -132.797   1.087  -1.889  1.00 36.57           C  
ATOM   6308  O   GLY C 222    -133.834   0.465  -2.226  1.00 31.39           O  
ATOM   6309  N   THR C 223    -131.563   0.660  -2.120  1.00 30.56           N  
ATOM   6310  CA  THR C 223    -131.277  -0.364  -3.080  1.00 27.59           C  
ATOM   6311  C   THR C 223    -130.260  -1.326  -2.461  1.00 29.79           C  
ATOM   6312  O   THR C 223    -129.310  -1.799  -3.099  1.00 36.15           O  
ATOM   6313  CB  THR C 223    -130.781   0.337  -4.303  1.00 27.80           C  
ATOM   6314  OG1 THR C 223    -129.948   1.441  -3.898  1.00 23.33           O  
ATOM   6315  CG2 THR C 223    -131.977   0.861  -5.068  1.00 31.18           C  
ATOM   6316  N   THR C 224    -130.536  -1.640  -1.202  1.00 25.89           N  
ATOM   6317  CA  THR C 224    -129.570  -2.187  -0.275  1.00 21.58           C  
ATOM   6318  C   THR C 224    -130.457  -2.961   0.677  1.00 24.22           C  
ATOM   6319  O   THR C 224    -131.494  -2.438   1.103  1.00 24.62           O  
ATOM   6320  CB  THR C 224    -128.839  -1.045   0.432  1.00 13.95           C  
ATOM   6321  OG1 THR C 224    -127.671  -1.497   1.060  1.00 15.53           O  
ATOM   6322  CG2 THR C 224    -129.694  -0.454   1.504  1.00 24.49           C  
ATOM   6323  N   GLU C 225    -130.117  -4.224   0.930  1.00 26.37           N  
ATOM   6324  CA  GLU C 225    -130.943  -5.084   1.782  1.00 21.59           C  
ATOM   6325  C   GLU C 225    -130.311  -5.014   3.090  1.00 16.00           C  
ATOM   6326  O   GLU C 225    -129.077  -4.741   3.169  1.00  9.35           O  
ATOM   6327  CB  GLU C 225    -130.881  -6.546   1.353  1.00 28.25           C  
ATOM   6328  CG  GLU C 225    -131.662  -6.852   0.119  1.00 35.09           C  
ATOM   6329  CD  GLU C 225    -131.857  -8.344  -0.102  1.00 40.69           C  
ATOM   6330  OE1 GLU C 225    -130.942  -9.143   0.274  1.00 34.30           O  
ATOM   6331  OE2 GLU C 225    -132.930  -8.690  -0.683  1.00 40.38           O  
ATOM   6332  N   PHE C 226    -131.072  -5.344   4.126  1.00  9.21           N  
ATOM   6333  CA  PHE C 226    -130.426  -5.367   5.424  1.00 10.84           C  
ATOM   6334  C   PHE C 226    -131.328  -5.624   6.572  1.00  8.20           C  
ATOM   6335  O   PHE C 226    -132.549  -5.760   6.415  1.00  7.67           O  
ATOM   6336  CB  PHE C 226    -129.743  -4.005   5.647  1.00 17.02           C  
ATOM   6337  CG  PHE C 226    -130.706  -2.883   5.849  1.00 13.45           C  
ATOM   6338  CD1 PHE C 226    -130.926  -2.407   7.135  1.00 11.43           C  
ATOM   6339  CD2 PHE C 226    -131.386  -2.321   4.774  1.00 11.64           C  
ATOM   6340  CE1 PHE C 226    -131.797  -1.402   7.355  1.00 18.06           C  
ATOM   6341  CE2 PHE C 226    -132.235  -1.280   4.982  1.00 13.23           C  
ATOM   6342  CZ  PHE C 226    -132.464  -0.818   6.282  1.00 16.41           C  
ATOM   6343  N   TRP C 227    -130.726  -5.658   7.746  1.00  7.31           N  
ATOM   6344  CA  TRP C 227    -131.512  -5.758   8.972  1.00 11.04           C  
ATOM   6345  C   TRP C 227    -130.818  -4.848   9.923  1.00  7.42           C  
ATOM   6346  O   TRP C 227    -129.586  -4.897  10.089  1.00  5.55           O  
ATOM   6347  CB  TRP C 227    -131.502  -7.234   9.487  1.00 17.23           C  
ATOM   6348  CG  TRP C 227    -132.118  -7.469  10.812  1.00 11.28           C  
ATOM   6349  CD1 TRP C 227    -131.480  -7.610  12.036  1.00 10.80           C  
ATOM   6350  CD2 TRP C 227    -133.494  -7.601  11.049  1.00  6.31           C  
ATOM   6351  NE1 TRP C 227    -132.430  -7.773  13.029  1.00 13.50           N  
ATOM   6352  CE2 TRP C 227    -133.673  -7.759  12.439  1.00  6.72           C  
ATOM   6353  CE3 TRP C 227    -134.598  -7.571  10.225  1.00  5.68           C  
ATOM   6354  CZ2 TRP C 227    -134.906  -7.907  12.995  1.00  6.31           C  
ATOM   6355  CZ3 TRP C 227    -135.829  -7.689  10.774  1.00  6.75           C  
ATOM   6356  CH2 TRP C 227    -135.979  -7.852  12.145  1.00  9.23           C  
ATOM   6357  N   LEU C 228    -131.584  -4.029  10.585  1.00 10.17           N  
ATOM   6358  CA  LEU C 228    -130.923  -2.959  11.306  1.00 21.73           C  
ATOM   6359  C   LEU C 228    -130.498  -3.426  12.688  1.00 23.18           C  
ATOM   6360  O   LEU C 228    -129.495  -2.968  13.222  1.00 25.16           O  
ATOM   6361  CB  LEU C 228    -131.748  -1.634  11.342  1.00 21.47           C  
ATOM   6362  CG  LEU C 228    -131.367  -0.508  12.337  1.00 14.48           C  
ATOM   6363  CD1 LEU C 228    -130.113   0.164  11.992  1.00  7.74           C  
ATOM   6364  CD2 LEU C 228    -132.515   0.473  12.379  1.00 14.47           C  
ATOM   6365  N   GLY C 229    -131.220  -4.335  13.290  1.00 20.94           N  
ATOM   6366  CA  GLY C 229    -130.638  -4.888  14.498  1.00 29.69           C  
ATOM   6367  C   GLY C 229    -131.455  -4.645  15.732  1.00 32.52           C  
ATOM   6368  O   GLY C 229    -131.713  -3.509  16.128  1.00 31.88           O  
ATOM   6369  N   ASN C 230    -131.838  -5.740  16.359  1.00 32.73           N  
ATOM   6370  CA  ASN C 230    -132.907  -5.671  17.299  1.00 35.29           C  
ATOM   6371  C   ASN C 230    -132.556  -4.664  18.332  1.00 34.24           C  
ATOM   6372  O   ASN C 230    -133.445  -3.958  18.810  1.00 33.81           O  
ATOM   6373  CB  ASN C 230    -133.194  -7.033  17.918  1.00 39.12           C  
ATOM   6374  CG  ASN C 230    -133.484  -8.085  16.871  1.00 45.04           C  
ATOM   6375  OD1 ASN C 230    -133.331  -9.269  17.131  1.00 47.92           O  
ATOM   6376  ND2 ASN C 230    -133.874  -7.654  15.668  1.00 38.42           N  
ATOM   6377  N   GLU C 231    -131.265  -4.544  18.645  1.00 31.02           N  
ATOM   6378  CA  GLU C 231    -130.892  -3.643  19.721  1.00 32.88           C  
ATOM   6379  C   GLU C 231    -131.343  -2.250  19.416  1.00 34.98           C  
ATOM   6380  O   GLU C 231    -132.011  -1.614  20.223  1.00 34.36           O  
ATOM   6381  CB  GLU C 231    -129.408  -3.623  19.975  1.00 33.07           C  
ATOM   6382  CG  GLU C 231    -129.074  -2.912  21.261  1.00 39.13           C  
ATOM   6383  CD  GLU C 231    -129.908  -3.394  22.446  1.00 47.66           C  
ATOM   6384  OE1 GLU C 231    -130.260  -4.591  22.476  1.00 49.95           O  
ATOM   6385  OE2 GLU C 231    -130.206  -2.581  23.357  1.00 49.26           O  
ATOM   6386  N   LYS C 232    -130.986  -1.800  18.225  1.00 32.80           N  
ATOM   6387  CA  LYS C 232    -131.441  -0.523  17.687  1.00 29.87           C  
ATOM   6388  C   LYS C 232    -132.967  -0.468  17.716  1.00 29.27           C  
ATOM   6389  O   LYS C 232    -133.564   0.433  18.338  1.00 26.76           O  
ATOM   6390  CB  LYS C 232    -130.908  -0.349  16.251  1.00 34.05           C  
ATOM   6391  CG  LYS C 232    -129.400  -0.766  16.074  1.00 36.61           C  
ATOM   6392  CD  LYS C 232    -128.690   0.072  15.005  1.00 36.41           C  
ATOM   6393  CE  LYS C 232    -127.354  -0.528  14.477  1.00 32.81           C  
ATOM   6394  NZ  LYS C 232    -126.692   0.422  13.513  1.00 27.33           N  
ATOM   6395  N   ILE C 233    -133.602  -1.476  17.113  1.00 24.98           N  
ATOM   6396  CA  ILE C 233    -135.064  -1.498  17.020  1.00 20.80           C  
ATOM   6397  C   ILE C 233    -135.745  -1.379  18.375  1.00 20.18           C  
ATOM   6398  O   ILE C 233    -136.903  -0.984  18.464  1.00 21.22           O  
ATOM   6399  CB  ILE C 233    -135.606  -2.780  16.391  1.00 21.98           C  
ATOM   6400  CG1 ILE C 233    -134.902  -3.143  15.092  1.00 28.85           C  
ATOM   6401  CG2 ILE C 233    -137.053  -2.602  16.028  1.00 26.47           C  
ATOM   6402  CD1 ILE C 233    -135.853  -3.806  14.058  1.00 24.11           C  
ATOM   6403  N   HIS C 234    -135.056  -1.761  19.435  1.00 24.67           N  
ATOM   6404  CA  HIS C 234    -135.682  -1.773  20.755  1.00 27.89           C  
ATOM   6405  C   HIS C 234    -135.626  -0.414  21.397  1.00 30.04           C  
ATOM   6406  O   HIS C 234    -136.606   0.078  21.979  1.00 30.66           O  
ATOM   6407  CB  HIS C 234    -134.924  -2.708  21.657  1.00 30.80           C  
ATOM   6408  CG  HIS C 234    -135.130  -2.431  23.109  1.00 25.86           C  
ATOM   6409  ND1 HIS C 234    -136.344  -2.624  23.732  1.00 22.64           N  
ATOM   6410  CD2 HIS C 234    -134.271  -2.000  24.063  1.00 24.17           C  
ATOM   6411  CE1 HIS C 234    -136.218  -2.334  25.015  1.00 25.64           C  
ATOM   6412  NE2 HIS C 234    -134.972  -1.948  25.241  1.00 24.02           N  
ATOM   6413  N   LEU C 235    -134.417   0.143  21.322  1.00 33.73           N  
ATOM   6414  CA  LEU C 235    -134.110   1.495  21.789  1.00 33.41           C  
ATOM   6415  C   LEU C 235    -134.986   2.510  21.131  1.00 32.32           C  
ATOM   6416  O   LEU C 235    -135.496   3.417  21.779  1.00 36.10           O  
ATOM   6417  CB  LEU C 235    -132.690   1.864  21.409  1.00 32.35           C  
ATOM   6418  CG  LEU C 235    -131.686   1.503  22.466  1.00 33.71           C  
ATOM   6419  CD1 LEU C 235    -130.299   1.626  21.855  1.00 35.01           C  
ATOM   6420  CD2 LEU C 235    -131.924   2.413  23.673  1.00 36.79           C  
ATOM   6421  N   ILE C 236    -135.103   2.377  19.821  1.00 23.36           N  
ATOM   6422  CA  ILE C 236    -136.003   3.202  19.105  1.00 22.39           C  
ATOM   6423  C   ILE C 236    -137.391   3.001  19.689  1.00 27.64           C  
ATOM   6424  O   ILE C 236    -137.934   3.905  20.310  1.00 35.07           O  
ATOM   6425  CB  ILE C 236    -136.026   2.827  17.654  1.00 21.23           C  
ATOM   6426  CG1 ILE C 236    -134.706   3.162  17.003  1.00 21.57           C  
ATOM   6427  CG2 ILE C 236    -137.101   3.588  16.938  1.00 21.78           C  
ATOM   6428  CD1 ILE C 236    -134.538   2.457  15.697  1.00 24.51           C  
ATOM   6429  N   SER C 237    -137.960   1.811  19.524  1.00 31.54           N  
ATOM   6430  CA  SER C 237    -139.370   1.582  19.880  1.00 37.77           C  
ATOM   6431  C   SER C 237    -139.720   2.090  21.272  1.00 39.49           C  
ATOM   6432  O   SER C 237    -140.788   2.660  21.457  1.00 43.78           O  
ATOM   6433  CB  SER C 237    -139.739   0.090  19.791  1.00 38.85           C  
ATOM   6434  OG  SER C 237    -138.943  -0.752  20.642  1.00 34.48           O  
ATOM   6435  N   THR C 238    -138.810   1.897  22.228  1.00 36.48           N  
ATOM   6436  CA  THR C 238    -139.124   2.036  23.640  1.00 41.19           C  
ATOM   6437  C   THR C 238    -138.387   3.183  24.286  1.00 53.37           C  
ATOM   6438  O   THR C 238    -137.674   2.995  25.283  1.00 57.76           O  
ATOM   6439  CB  THR C 238    -138.656   0.817  24.409  1.00 43.00           C  
ATOM   6440  OG1 THR C 238    -137.233   0.910  24.597  1.00 48.52           O  
ATOM   6441  CG2 THR C 238    -139.011  -0.466  23.662  1.00 44.35           C  
ATOM   6442  N   GLN C 239    -138.529   4.369  23.729  1.00 50.06           N  
ATOM   6443  CA  GLN C 239    -138.003   5.539  24.394  1.00 50.87           C  
ATOM   6444  C   GLN C 239    -139.220   6.375  24.713  1.00 59.44           C  
ATOM   6445  O   GLN C 239    -140.199   6.406  23.949  1.00 62.34           O  
ATOM   6446  CB  GLN C 239    -137.015   6.296  23.512  1.00 45.62           C  
ATOM   6447  CG  GLN C 239    -137.416   6.314  22.037  1.00 47.50           C  
ATOM   6448  CD  GLN C 239    -136.800   7.452  21.221  1.00 49.28           C  
ATOM   6449  OE1 GLN C 239    -136.665   7.342  19.992  1.00 45.76           O  
ATOM   6450  NE2 GLN C 239    -136.453   8.562  21.890  1.00 52.62           N  
ATOM   6451  N   SER C 240    -139.197   6.998  25.877  1.00 56.96           N  
ATOM   6452  CA  SER C 240    -140.076   8.115  26.123  1.00 58.89           C  
ATOM   6453  C   SER C 240    -141.542   7.892  25.748  1.00 56.87           C  
ATOM   6454  O   SER C 240    -142.183   8.783  25.187  1.00 56.43           O  
ATOM   6455  CB  SER C 240    -139.557   9.319  25.337  1.00 62.71           C  
ATOM   6456  OG  SER C 240    -140.031   9.289  24.000  1.00 60.38           O  
ATOM   6457  N   ALA C 241    -142.076   6.715  26.045  1.00 58.07           N  
ATOM   6458  CA  ALA C 241    -143.543   6.537  26.130  1.00 57.36           C  
ATOM   6459  C   ALA C 241    -144.378   6.886  24.882  1.00 58.13           C  
ATOM   6460  O   ALA C 241    -145.371   6.204  24.613  1.00 53.54           O  
ATOM   6461  CB  ALA C 241    -144.093   7.304  27.340  1.00 48.41           C  
ATOM   6462  N   ILE C 242    -144.024   7.936  24.139  1.00 59.41           N  
ATOM   6463  CA  ILE C 242    -144.723   8.195  22.874  1.00 57.69           C  
ATOM   6464  C   ILE C 242    -144.596   6.945  22.000  1.00 48.22           C  
ATOM   6465  O   ILE C 242    -143.507   6.377  21.892  1.00 45.97           O  
ATOM   6466  CB  ILE C 242    -144.232   9.464  22.121  1.00 61.83           C  
ATOM   6467  CG1 ILE C 242    -142.696   9.498  22.004  1.00 64.15           C  
ATOM   6468  CG2 ILE C 242    -144.757  10.719  22.828  1.00 57.37           C  
ATOM   6469  CD1 ILE C 242    -142.155  10.395  20.880  1.00 65.49           C  
ATOM   6470  N   PRO C 243    -145.716   6.499  21.404  1.00 46.43           N  
ATOM   6471  CA  PRO C 243    -145.807   5.175  20.824  1.00 46.52           C  
ATOM   6472  C   PRO C 243    -145.408   5.188  19.381  1.00 40.36           C  
ATOM   6473  O   PRO C 243    -145.539   6.228  18.707  1.00 33.64           O  
ATOM   6474  CB  PRO C 243    -147.290   4.857  20.914  1.00 45.36           C  
ATOM   6475  CG  PRO C 243    -147.969   6.203  20.968  1.00 51.27           C  
ATOM   6476  CD  PRO C 243    -146.911   7.278  21.057  1.00 50.09           C  
ATOM   6477  N   TYR C 244    -144.917   4.043  18.918  1.00 34.01           N  
ATOM   6478  CA  TYR C 244    -144.568   3.912  17.527  1.00 33.44           C  
ATOM   6479  C   TYR C 244    -145.539   2.962  16.888  1.00 28.43           C  
ATOM   6480  O   TYR C 244    -146.259   2.248  17.594  1.00 29.10           O  
ATOM   6481  CB  TYR C 244    -143.160   3.404  17.364  1.00 39.80           C  
ATOM   6482  CG  TYR C 244    -142.041   4.410  17.618  1.00 42.83           C  
ATOM   6483  CD1 TYR C 244    -141.523   4.612  18.917  1.00 45.36           C  
ATOM   6484  CD2 TYR C 244    -141.447   5.095  16.551  1.00 42.64           C  
ATOM   6485  CE1 TYR C 244    -140.468   5.513  19.156  1.00 46.93           C  
ATOM   6486  CE2 TYR C 244    -140.394   5.986  16.771  1.00 50.20           C  
ATOM   6487  CZ  TYR C 244    -139.905   6.194  18.073  1.00 51.63           C  
ATOM   6488  OH  TYR C 244    -138.854   7.077  18.264  1.00 48.24           O  
ATOM   6489  N   ALA C 245    -145.595   3.015  15.559  1.00 19.47           N  
ATOM   6490  CA  ALA C 245    -146.456   2.151  14.762  1.00 17.55           C  
ATOM   6491  C   ALA C 245    -145.618   1.580  13.663  1.00 25.65           C  
ATOM   6492  O   ALA C 245    -144.841   2.310  13.046  1.00 28.33           O  
ATOM   6493  CB  ALA C 245    -147.527   2.895  14.165  1.00 13.26           C  
ATOM   6494  N   LEU C 246    -145.767   0.280  13.414  1.00 23.82           N  
ATOM   6495  CA  LEU C 246    -145.003  -0.381  12.376  1.00 19.13           C  
ATOM   6496  C   LEU C 246    -145.816  -0.385  11.123  1.00 18.56           C  
ATOM   6497  O   LEU C 246    -147.036  -0.510  11.187  1.00 21.07           O  
ATOM   6498  CB  LEU C 246    -144.743  -1.832  12.744  1.00 20.00           C  
ATOM   6499  CG  LEU C 246    -144.139  -2.625  11.555  1.00 17.30           C  
ATOM   6500  CD1 LEU C 246    -142.634  -2.666  11.688  1.00 11.03           C  
ATOM   6501  CD2 LEU C 246    -144.734  -4.022  11.454  1.00 15.10           C  
ATOM   6502  N   ARG C 247    -145.154  -0.284   9.987  1.00 13.08           N  
ATOM   6503  CA  ARG C 247    -145.809  -0.607   8.758  1.00 18.55           C  
ATOM   6504  C   ARG C 247    -144.897  -1.420   7.931  1.00 25.89           C  
ATOM   6505  O   ARG C 247    -143.731  -1.081   7.725  1.00 30.37           O  
ATOM   6506  CB  ARG C 247    -146.149   0.626   7.988  1.00 26.17           C  
ATOM   6507  CG  ARG C 247    -146.150   0.459   6.474  1.00 31.62           C  
ATOM   6508  CD  ARG C 247    -146.325   1.853   5.874  1.00 38.56           C  
ATOM   6509  NE  ARG C 247    -147.650   2.439   6.183  1.00 31.00           N  
ATOM   6510  CZ  ARG C 247    -148.326   3.216   5.349  1.00 25.21           C  
ATOM   6511  NH1 ARG C 247    -147.826   3.541   4.170  1.00 28.38           N  
ATOM   6512  NH2 ARG C 247    -149.508   3.664   5.691  1.00 30.79           N  
ATOM   6513  N   VAL C 248    -145.484  -2.451   7.376  1.00 25.71           N  
ATOM   6514  CA  VAL C 248    -144.792  -3.468   6.638  1.00 27.55           C  
ATOM   6515  C   VAL C 248    -145.238  -3.286   5.192  1.00 33.07           C  
ATOM   6516  O   VAL C 248    -146.401  -2.946   4.955  1.00 36.65           O  
ATOM   6517  CB  VAL C 248    -145.325  -4.786   7.192  1.00 29.42           C  
ATOM   6518  CG1 VAL C 248    -144.754  -5.975   6.453  1.00 29.71           C  
ATOM   6519  CG2 VAL C 248    -145.058  -4.833   8.698  1.00 23.29           C  
ATOM   6520  N   GLU C 249    -144.377  -3.505   4.215  1.00 24.37           N  
ATOM   6521  CA  GLU C 249    -144.734  -3.107   2.858  1.00 26.15           C  
ATOM   6522  C   GLU C 249    -144.139  -4.078   1.894  1.00 19.43           C  
ATOM   6523  O   GLU C 249    -142.909  -4.236   1.843  1.00 17.57           O  
ATOM   6524  CB  GLU C 249    -144.193  -1.697   2.603  1.00 41.24           C  
ATOM   6525  CG  GLU C 249    -144.761  -0.948   1.391  1.00 54.69           C  
ATOM   6526  CD  GLU C 249    -144.387   0.557   1.427  1.00 61.24           C  
ATOM   6527  OE1 GLU C 249    -145.292   1.433   1.242  1.00 65.59           O  
ATOM   6528  OE2 GLU C 249    -143.180   0.844   1.669  1.00 61.34           O  
ATOM   6529  N   LEU C 250    -144.993  -4.730   1.121  1.00 20.05           N  
ATOM   6530  CA  LEU C 250    -144.577  -5.913   0.349  1.00 20.79           C  
ATOM   6531  C   LEU C 250    -144.845  -5.811  -1.138  1.00 19.37           C  
ATOM   6532  O   LEU C 250    -145.966  -5.501  -1.521  1.00 24.73           O  
ATOM   6533  CB  LEU C 250    -145.359  -7.132   0.864  1.00 21.74           C  
ATOM   6534  CG  LEU C 250    -145.066  -7.695   2.267  1.00 24.58           C  
ATOM   6535  CD1 LEU C 250    -144.800  -6.569   3.333  1.00 19.84           C  
ATOM   6536  CD2 LEU C 250    -146.240  -8.640   2.683  1.00 23.05           C  
ATOM   6537  N   GLU C 251    -143.874  -6.138  -1.979  1.00 18.77           N  
ATOM   6538  CA  GLU C 251    -144.127  -6.204  -3.434  1.00 24.25           C  
ATOM   6539  C   GLU C 251    -143.944  -7.633  -3.984  1.00 34.77           C  
ATOM   6540  O   GLU C 251    -142.924  -8.324  -3.726  1.00 33.64           O  
ATOM   6541  CB  GLU C 251    -143.216  -5.230  -4.174  1.00 34.68           C  
ATOM   6542  CG  GLU C 251    -143.306  -5.222  -5.706  1.00 41.78           C  
ATOM   6543  CD  GLU C 251    -142.292  -4.216  -6.349  1.00 52.74           C  
ATOM   6544  OE1 GLU C 251    -141.997  -3.178  -5.690  1.00 51.70           O  
ATOM   6545  OE2 GLU C 251    -141.804  -4.456  -7.500  1.00 52.57           O  
ATOM   6546  N   ASP C 252    -144.938  -8.065  -4.759  1.00 31.11           N  
ATOM   6547  CA  ASP C 252    -144.908  -9.363  -5.421  1.00 26.63           C  
ATOM   6548  C   ASP C 252    -144.042  -9.335  -6.689  1.00 27.91           C  
ATOM   6549  O   ASP C 252    -143.171  -8.464  -6.859  1.00 29.57           O  
ATOM   6550  CB  ASP C 252    -146.333  -9.807  -5.718  1.00 28.93           C  
ATOM   6551  CG  ASP C 252    -146.914  -9.184  -6.978  1.00 33.32           C  
ATOM   6552  OD1 ASP C 252    -146.379  -8.181  -7.499  1.00 36.19           O  
ATOM   6553  OD2 ASP C 252    -147.930  -9.738  -7.460  1.00 31.95           O  
ATOM   6554  N   TRP C 253    -144.240 -10.291  -7.579  1.00 26.33           N  
ATOM   6555  CA  TRP C 253    -143.366 -10.375  -8.755  1.00 28.94           C  
ATOM   6556  C   TRP C 253    -144.079  -9.867 -10.013  1.00 31.37           C  
ATOM   6557  O   TRP C 253    -143.656 -10.142 -11.142  1.00 28.95           O  
ATOM   6558  CB  TRP C 253    -142.811 -11.806  -8.896  1.00 24.84           C  
ATOM   6559  CG  TRP C 253    -141.829 -12.067  -7.852  1.00 14.82           C  
ATOM   6560  CD1 TRP C 253    -142.073 -12.337  -6.536  1.00 13.14           C  
ATOM   6561  CD2 TRP C 253    -140.420 -12.022  -8.004  1.00  9.72           C  
ATOM   6562  NE1 TRP C 253    -140.874 -12.465  -5.850  1.00 12.08           N  
ATOM   6563  CE2 TRP C 253    -139.849 -12.277  -6.742  1.00  9.59           C  
ATOM   6564  CE3 TRP C 253    -139.584 -11.802  -9.087  1.00  9.21           C  
ATOM   6565  CZ2 TRP C 253    -138.494 -12.307  -6.540  1.00 10.53           C  
ATOM   6566  CZ3 TRP C 253    -138.224 -11.836  -8.882  1.00 13.26           C  
ATOM   6567  CH2 TRP C 253    -137.690 -12.088  -7.617  1.00 11.47           C  
ATOM   6568  N   ASN C 254    -145.166  -9.129  -9.791  1.00 32.44           N  
ATOM   6569  CA  ASN C 254    -145.811  -8.328 -10.830  1.00 40.33           C  
ATOM   6570  C   ASN C 254    -145.894  -6.889 -10.376  1.00 35.44           C  
ATOM   6571  O   ASN C 254    -146.810  -6.169 -10.770  1.00 29.05           O  
ATOM   6572  CB  ASN C 254    -147.245  -8.784 -11.074  1.00 45.69           C  
ATOM   6573  CG  ASN C 254    -147.370 -10.259 -11.287  1.00 46.08           C  
ATOM   6574  OD1 ASN C 254    -148.392 -10.704 -11.795  1.00 47.52           O  
ATOM   6575  ND2 ASN C 254    -146.357 -11.034 -10.892  1.00 39.96           N  
ATOM   6576  N   GLY C 255    -144.973  -6.495  -9.498  1.00 49.61           N  
ATOM   6577  CA  GLY C 255    -144.926  -5.127  -8.976  1.00 52.97           C  
ATOM   6578  C   GLY C 255    -146.223  -4.636  -8.331  1.00 55.91           C  
ATOM   6579  O   GLY C 255    -146.597  -3.455  -8.448  1.00 53.41           O  
ATOM   6580  N   ARG C 256    -146.918  -5.544  -7.661  1.00 51.67           N  
ATOM   6581  CA  ARG C 256    -148.008  -5.153  -6.804  1.00 53.74           C  
ATOM   6582  C   ARG C 256    -147.439  -4.870  -5.432  1.00 50.16           C  
ATOM   6583  O   ARG C 256    -146.589  -5.612  -4.951  1.00 42.72           O  
ATOM   6584  CB  ARG C 256    -149.026  -6.269  -6.741  1.00 54.48           C  
ATOM   6585  CG  ARG C 256    -149.444  -6.711  -8.125  1.00 59.41           C  
ATOM   6586  CD  ARG C 256    -150.896  -7.257  -8.178  1.00 63.17           C  
ATOM   6587  NE  ARG C 256    -150.978  -8.314  -9.186  1.00 63.82           N  
ATOM   6588  CZ  ARG C 256    -150.699  -9.598  -8.964  1.00 66.07           C  
ATOM   6589  NH1 ARG C 256    -150.369 -10.036  -7.743  1.00 66.76           N  
ATOM   6590  NH2 ARG C 256    -150.762 -10.457  -9.976  1.00 66.13           N  
ATOM   6591  N   THR C 257    -147.861  -3.777  -4.814  1.00 47.89           N  
ATOM   6592  CA  THR C 257    -147.473  -3.542  -3.430  1.00 50.30           C  
ATOM   6593  C   THR C 257    -148.662  -3.829  -2.512  1.00 46.95           C  
ATOM   6594  O   THR C 257    -149.746  -4.116  -2.983  1.00 47.11           O  
ATOM   6595  CB  THR C 257    -146.875  -2.106  -3.180  1.00 51.65           C  
ATOM   6596  OG1 THR C 257    -147.921  -1.122  -3.133  1.00 55.15           O  
ATOM   6597  CG2 THR C 257    -145.827  -1.745  -4.251  1.00 45.09           C  
ATOM   6598  N   SER C 258    -148.420  -3.768  -1.202  1.00 47.80           N  
ATOM   6599  CA  SER C 258    -149.460  -3.828  -0.157  1.00 42.20           C  
ATOM   6600  C   SER C 258    -148.844  -3.539   1.229  1.00 41.39           C  
ATOM   6601  O   SER C 258    -147.647  -3.738   1.465  1.00 34.95           O  
ATOM   6602  CB  SER C 258    -150.117  -5.194  -0.166  1.00 31.55           C  
ATOM   6603  OG  SER C 258    -149.125  -6.098  -0.576  1.00 28.78           O  
ATOM   6604  N   THR C 259    -149.658  -3.063   2.150  1.00 38.77           N  
ATOM   6605  CA  THR C 259    -149.150  -2.783   3.473  1.00 36.82           C  
ATOM   6606  C   THR C 259    -149.873  -3.640   4.491  1.00 31.62           C  
ATOM   6607  O   THR C 259    -150.916  -4.246   4.190  1.00 24.58           O  
ATOM   6608  CB  THR C 259    -149.289  -1.256   3.842  1.00 44.09           C  
ATOM   6609  OG1 THR C 259    -150.413  -0.681   3.151  1.00 44.50           O  
ATOM   6610  CG2 THR C 259    -148.003  -0.471   3.482  1.00 42.48           C  
ATOM   6611  N   ALA C 260    -149.289  -3.680   5.688  1.00 26.59           N  
ATOM   6612  CA  ALA C 260    -150.001  -4.069   6.897  1.00 26.56           C  
ATOM   6613  C   ALA C 260    -149.564  -3.157   8.017  1.00 20.82           C  
ATOM   6614  O   ALA C 260    -148.398  -3.162   8.334  1.00 26.44           O  
ATOM   6615  CB  ALA C 260    -149.678  -5.513   7.248  1.00 22.48           C  
ATOM   6616  N   ASP C 261    -150.439  -2.368   8.614  1.00 15.24           N  
ATOM   6617  CA  ASP C 261    -149.977  -1.501   9.712  1.00 24.04           C  
ATOM   6618  C   ASP C 261    -150.222  -2.175  11.036  1.00 23.05           C  
ATOM   6619  O   ASP C 261    -151.291  -2.728  11.227  1.00 26.88           O  
ATOM   6620  CB  ASP C 261    -150.748  -0.154   9.784  1.00 31.73           C  
ATOM   6621  CG  ASP C 261    -150.253   0.936   8.805  1.00 31.51           C  
ATOM   6622  OD1 ASP C 261    -150.967   1.972   8.789  1.00 28.82           O  
ATOM   6623  OD2 ASP C 261    -149.208   0.797   8.093  1.00 31.80           O  
ATOM   6624  N   TYR C 262    -149.323  -2.017  11.993  1.00 20.39           N  
ATOM   6625  CA  TYR C 262    -149.570  -2.519  13.358  1.00 28.76           C  
ATOM   6626  C   TYR C 262    -149.393  -1.437  14.414  1.00 27.71           C  
ATOM   6627  O   TYR C 262    -148.308  -0.891  14.539  1.00 33.81           O  
ATOM   6628  CB  TYR C 262    -148.582  -3.664  13.647  1.00 37.71           C  
ATOM   6629  CG  TYR C 262    -148.965  -4.938  12.964  1.00 35.41           C  
ATOM   6630  CD1 TYR C 262    -148.932  -5.043  11.561  1.00 36.14           C  
ATOM   6631  CD2 TYR C 262    -149.419  -6.013  13.702  1.00 39.94           C  
ATOM   6632  CE1 TYR C 262    -149.333  -6.207  10.913  1.00 37.82           C  
ATOM   6633  CE2 TYR C 262    -149.828  -7.173  13.076  1.00 47.83           C  
ATOM   6634  CZ  TYR C 262    -149.777  -7.275  11.676  1.00 49.19           C  
ATOM   6635  OH  TYR C 262    -150.184  -8.441  11.064  1.00 43.97           O  
ATOM   6636  N   ALA C 263    -150.399  -1.135  15.211  1.00 26.49           N  
ATOM   6637  CA  ALA C 263    -150.231  -0.038  16.196  1.00 33.78           C  
ATOM   6638  C   ALA C 263    -149.527  -0.390  17.528  1.00 33.04           C  
ATOM   6639  O   ALA C 263    -149.454  -1.562  17.950  1.00 32.68           O  
ATOM   6640  CB  ALA C 263    -151.547   0.613  16.490  1.00 32.72           C  
ATOM   6641  N   MET C 264    -149.036   0.665  18.184  1.00 33.16           N  
ATOM   6642  CA  MET C 264    -148.247   0.574  19.433  1.00 33.19           C  
ATOM   6643  C   MET C 264    -147.177  -0.505  19.414  1.00 30.69           C  
ATOM   6644  O   MET C 264    -146.926  -1.205  20.399  1.00 29.37           O  
ATOM   6645  CB  MET C 264    -149.162   0.423  20.636  1.00 38.06           C  
ATOM   6646  CG  MET C 264    -149.647   1.780  21.158  1.00 41.33           C  
ATOM   6647  SD  MET C 264    -150.386   2.820  19.860  1.00 40.09           S  
ATOM   6648  CE  MET C 264    -152.074   2.202  19.786  1.00 48.96           C  
ATOM   6649  N   PHE C 265    -146.534  -0.585  18.262  1.00 27.44           N  
ATOM   6650  CA  PHE C 265    -145.486  -1.522  18.003  1.00 27.03           C  
ATOM   6651  C   PHE C 265    -144.309  -1.267  18.910  1.00 29.48           C  
ATOM   6652  O   PHE C 265    -143.987  -0.117  19.194  1.00 32.69           O  
ATOM   6653  CB  PHE C 265    -145.016  -1.361  16.564  1.00 29.58           C  
ATOM   6654  CG  PHE C 265    -143.897  -2.251  16.233  1.00 38.80           C  
ATOM   6655  CD1 PHE C 265    -144.130  -3.591  15.955  1.00 42.15           C  
ATOM   6656  CD2 PHE C 265    -142.604  -1.795  16.273  1.00 39.08           C  
ATOM   6657  CE1 PHE C 265    -143.092  -4.444  15.672  1.00 39.65           C  
ATOM   6658  CE2 PHE C 265    -141.558  -2.644  15.991  1.00 40.76           C  
ATOM   6659  CZ  PHE C 265    -141.802  -3.967  15.691  1.00 42.40           C  
ATOM   6660  N   LYS C 266    -143.666  -2.346  19.349  1.00 28.52           N  
ATOM   6661  CA  LYS C 266    -142.401  -2.267  20.083  1.00 31.66           C  
ATOM   6662  C   LYS C 266    -141.713  -3.615  20.303  1.00 38.18           C  
ATOM   6663  O   LYS C 266    -142.369  -4.629  20.561  1.00 38.15           O  
ATOM   6664  CB  LYS C 266    -142.627  -1.661  21.450  1.00 29.86           C  
ATOM   6665  CG  LYS C 266    -143.867  -2.172  22.126  1.00 30.09           C  
ATOM   6666  CD  LYS C 266    -143.765  -1.918  23.630  1.00 39.21           C  
ATOM   6667  CE  LYS C 266    -143.396  -0.450  23.988  1.00 35.74           C  
ATOM   6668  NZ  LYS C 266    -143.828  -0.065  25.356  1.00 32.61           N  
ATOM   6669  N   VAL C 267    -140.386  -3.616  20.252  1.00 28.64           N  
ATOM   6670  CA  VAL C 267    -139.632  -4.813  20.565  1.00 19.59           C  
ATOM   6671  C   VAL C 267    -139.090  -4.712  21.949  1.00 24.72           C  
ATOM   6672  O   VAL C 267    -138.798  -3.622  22.447  1.00 26.69           O  
ATOM   6673  CB  VAL C 267    -138.463  -4.981  19.639  1.00 20.27           C  
ATOM   6674  CG1 VAL C 267    -137.160  -5.373  20.428  1.00 13.31           C  
ATOM   6675  CG2 VAL C 267    -138.839  -5.950  18.550  1.00 18.01           C  
ATOM   6676  N   GLY C 268    -138.913  -5.867  22.557  1.00 27.00           N  
ATOM   6677  CA  GLY C 268    -138.437  -5.939  23.921  1.00 27.49           C  
ATOM   6678  C   GLY C 268    -136.936  -5.809  24.037  1.00 29.40           C  
ATOM   6679  O   GLY C 268    -136.218  -5.682  23.024  1.00 24.85           O  
ATOM   6680  N   PRO C 269    -136.454  -5.815  25.285  1.00 30.60           N  
ATOM   6681  CA  PRO C 269    -135.047  -5.883  25.584  1.00 29.34           C  
ATOM   6682  C   PRO C 269    -134.509  -7.291  25.394  1.00 36.29           C  
ATOM   6683  O   PRO C 269    -135.288  -8.240  25.481  1.00 38.66           O  
ATOM   6684  CB  PRO C 269    -135.000  -5.491  27.054  1.00 30.63           C  
ATOM   6685  CG  PRO C 269    -136.317  -5.807  27.587  1.00 29.38           C  
ATOM   6686  CD  PRO C 269    -137.260  -5.543  26.488  1.00 30.00           C  
ATOM   6687  N   GLU C 270    -133.197  -7.413  25.138  1.00 45.67           N  
ATOM   6688  CA  GLU C 270    -132.503  -8.718  25.059  1.00 48.04           C  
ATOM   6689  C   GLU C 270    -132.856  -9.568  26.285  1.00 49.80           C  
ATOM   6690  O   GLU C 270    -133.091 -10.792  26.178  1.00 41.66           O  
ATOM   6691  CB  GLU C 270    -130.966  -8.554  24.971  1.00 49.46           C  
ATOM   6692  CG  GLU C 270    -130.199  -9.897  24.688  1.00 50.88           C  
ATOM   6693  CD  GLU C 270    -128.689  -9.754  24.333  1.00 58.52           C  
ATOM   6694  OE1 GLU C 270    -128.027  -8.784  24.780  1.00 61.00           O  
ATOM   6695  OE2 GLU C 270    -128.154 -10.640  23.617  1.00 45.67           O  
ATOM   6696  N   ALA C 271    -132.890  -8.911  27.447  1.00 49.23           N  
ATOM   6697  CA  ALA C 271    -133.422  -9.528  28.655  1.00 49.72           C  
ATOM   6698  C   ALA C 271    -134.650 -10.417  28.335  1.00 51.96           C  
ATOM   6699  O   ALA C 271    -134.724 -11.570  28.763  1.00 51.99           O  
ATOM   6700  CB  ALA C 271    -133.785  -8.447  29.668  1.00 50.56           C  
ATOM   6701  N   ASP C 272    -135.588  -9.875  27.556  1.00 44.32           N  
ATOM   6702  CA  ASP C 272    -136.832 -10.556  27.209  1.00 42.93           C  
ATOM   6703  C   ASP C 272    -136.785 -11.029  25.748  1.00 38.93           C  
ATOM   6704  O   ASP C 272    -137.791 -11.395  25.144  1.00 39.34           O  
ATOM   6705  CB  ASP C 272    -138.009  -9.597  27.452  1.00 47.16           C  
ATOM   6706  CG  ASP C 272    -139.381 -10.266  27.302  1.00 51.32           C  
ATOM   6707  OD1 ASP C 272    -139.457 -11.509  27.483  1.00 51.07           O  
ATOM   6708  OD2 ASP C 272    -140.377  -9.540  27.007  1.00 48.00           O  
ATOM   6709  N   LYS C 273    -135.593 -11.038  25.179  1.00 45.25           N  
ATOM   6710  CA  LYS C 273    -135.390 -11.615  23.851  1.00 42.05           C  
ATOM   6711  C   LYS C 273    -136.034 -10.801  22.752  1.00 40.76           C  
ATOM   6712  O   LYS C 273    -136.555 -11.371  21.813  1.00 41.76           O  
ATOM   6713  CB  LYS C 273    -135.951 -13.044  23.772  1.00 36.02           C  
ATOM   6714  CG  LYS C 273    -135.419 -14.003  24.828  1.00 31.97           C  
ATOM   6715  CD  LYS C 273    -133.959 -14.275  24.620  1.00 27.55           C  
ATOM   6716  CE  LYS C 273    -133.448 -15.310  25.588  1.00 27.73           C  
ATOM   6717  NZ  LYS C 273    -132.002 -15.608  25.322  1.00 27.19           N  
ATOM   6718  N   TYR C 274    -136.010  -9.483  22.847  1.00 35.81           N  
ATOM   6719  CA  TYR C 274    -136.459  -8.683  21.728  1.00 35.11           C  
ATOM   6720  C   TYR C 274    -137.823  -9.164  21.241  1.00 30.53           C  
ATOM   6721  O   TYR C 274    -138.109  -9.265  20.046  1.00 26.41           O  
ATOM   6722  CB  TYR C 274    -135.417  -8.715  20.617  1.00 37.74           C  
ATOM   6723  CG  TYR C 274    -134.062  -8.162  21.044  1.00 42.45           C  
ATOM   6724  CD1 TYR C 274    -133.005  -9.013  21.312  1.00 44.97           C  
ATOM   6725  CD2 TYR C 274    -133.847  -6.787  21.174  1.00 44.97           C  
ATOM   6726  CE1 TYR C 274    -131.770  -8.526  21.684  1.00 48.41           C  
ATOM   6727  CE2 TYR C 274    -132.612  -6.286  21.549  1.00 45.10           C  
ATOM   6728  CZ  TYR C 274    -131.572  -7.169  21.804  1.00 46.65           C  
ATOM   6729  OH  TYR C 274    -130.322  -6.733  22.183  1.00 47.13           O  
ATOM   6730  N   ARG C 275    -138.671  -9.450  22.212  1.00 31.66           N  
ATOM   6731  CA  ARG C 275    -140.014  -9.884  21.934  1.00 34.08           C  
ATOM   6732  C   ARG C 275    -140.725  -8.857  21.095  1.00 34.35           C  
ATOM   6733  O   ARG C 275    -140.713  -7.680  21.447  1.00 35.70           O  
ATOM   6734  CB  ARG C 275    -140.779 -10.041  23.254  1.00 37.01           C  
ATOM   6735  CG  ARG C 275    -142.094 -10.821  23.116  1.00 41.88           C  
ATOM   6736  CD  ARG C 275    -142.966 -10.648  24.342  1.00 47.39           C  
ATOM   6737  NE  ARG C 275    -142.327 -11.120  25.576  1.00 51.61           N  
ATOM   6738  CZ  ARG C 275    -142.436 -12.346  26.088  1.00 52.80           C  
ATOM   6739  NH1 ARG C 275    -141.814 -12.633  27.216  1.00 53.33           N  
ATOM   6740  NH2 ARG C 275    -143.155 -13.288  25.494  1.00 50.89           N  
ATOM   6741  N   LEU C 276    -141.391  -9.278  20.023  1.00 27.36           N  
ATOM   6742  CA  LEU C 276    -142.298  -8.351  19.324  1.00 19.57           C  
ATOM   6743  C   LEU C 276    -143.529  -8.166  20.177  1.00 19.05           C  
ATOM   6744  O   LEU C 276    -144.097  -9.132  20.696  1.00 23.83           O  
ATOM   6745  CB  LEU C 276    -142.696  -8.840  17.934  1.00 16.81           C  
ATOM   6746  CG  LEU C 276    -143.982  -8.224  17.374  1.00 17.15           C  
ATOM   6747  CD1 LEU C 276    -144.055  -8.555  15.946  1.00 19.49           C  
ATOM   6748  CD2 LEU C 276    -145.259  -8.768  18.036  1.00 18.39           C  
ATOM   6749  N   THR C 277    -143.963  -6.928  20.314  1.00 21.11           N  
ATOM   6750  CA  THR C 277    -145.207  -6.665  21.022  1.00 20.91           C  
ATOM   6751  C   THR C 277    -145.928  -5.487  20.401  1.00 19.14           C  
ATOM   6752  O   THR C 277    -145.321  -4.471  20.045  1.00 19.15           O  
ATOM   6753  CB  THR C 277    -144.933  -6.375  22.476  1.00 26.07           C  
ATOM   6754  OG1 THR C 277    -143.593  -6.802  22.788  1.00 33.51           O  
ATOM   6755  CG2 THR C 277    -145.922  -7.092  23.332  1.00 23.55           C  
ATOM   6756  N   TYR C 278    -147.229  -5.624  20.238  1.00 16.08           N  
ATOM   6757  CA  TYR C 278    -147.923  -4.598  19.544  1.00 22.21           C  
ATOM   6758  C   TYR C 278    -149.320  -4.675  19.958  1.00 29.64           C  
ATOM   6759  O   TYR C 278    -149.815  -5.780  20.185  1.00 30.38           O  
ATOM   6760  CB  TYR C 278    -147.819  -4.754  18.030  1.00 24.30           C  
ATOM   6761  CG  TYR C 278    -148.550  -5.949  17.462  1.00 28.77           C  
ATOM   6762  CD1 TYR C 278    -149.937  -5.990  17.360  1.00 25.44           C  
ATOM   6763  CD2 TYR C 278    -147.834  -7.045  17.006  1.00 32.06           C  
ATOM   6764  CE1 TYR C 278    -150.559  -7.110  16.833  1.00 28.97           C  
ATOM   6765  CE2 TYR C 278    -148.448  -8.156  16.476  1.00 27.86           C  
ATOM   6766  CZ  TYR C 278    -149.787  -8.194  16.384  1.00 29.94           C  
ATOM   6767  OH  TYR C 278    -150.318  -9.339  15.830  1.00 32.51           O  
ATOM   6768  N   ALA C 279    -149.954  -3.494  20.006  1.00 38.15           N  
ATOM   6769  CA  ALA C 279    -151.311  -3.333  20.546  1.00 39.82           C  
ATOM   6770  C   ALA C 279    -152.404  -3.984  19.690  1.00 38.74           C  
ATOM   6771  O   ALA C 279    -153.181  -4.806  20.196  1.00 36.66           O  
ATOM   6772  CB  ALA C 279    -151.621  -1.858  20.754  1.00 39.10           C  
ATOM   6773  N   TYR C 280    -152.468  -3.614  18.411  1.00 31.60           N  
ATOM   6774  CA  TYR C 280    -153.551  -4.082  17.542  1.00 33.85           C  
ATOM   6775  C   TYR C 280    -153.237  -3.902  16.090  1.00 34.85           C  
ATOM   6776  O   TYR C 280    -152.413  -3.066  15.737  1.00 36.84           O  
ATOM   6777  CB  TYR C 280    -154.873  -3.355  17.843  1.00 40.00           C  
ATOM   6778  CG  TYR C 280    -154.912  -1.835  17.678  1.00 37.25           C  
ATOM   6779  CD1 TYR C 280    -155.279  -1.249  16.465  1.00 35.49           C  
ATOM   6780  CD2 TYR C 280    -154.638  -0.991  18.767  1.00 39.05           C  
ATOM   6781  CE1 TYR C 280    -155.345   0.136  16.331  1.00 37.85           C  
ATOM   6782  CE2 TYR C 280    -154.691   0.398  18.648  1.00 37.56           C  
ATOM   6783  CZ  TYR C 280    -155.053   0.960  17.436  1.00 39.90           C  
ATOM   6784  OH  TYR C 280    -155.119   2.338  17.334  1.00 34.07           O  
ATOM   6785  N   PHE C 281    -153.908  -4.677  15.245  1.00 30.95           N  
ATOM   6786  CA  PHE C 281    -153.713  -4.563  13.795  1.00 26.76           C  
ATOM   6787  C   PHE C 281    -154.300  -3.224  13.422  1.00 25.64           C  
ATOM   6788  O   PHE C 281    -155.456  -2.923  13.744  1.00 18.18           O  
ATOM   6789  CB  PHE C 281    -154.433  -5.697  13.080  1.00 20.79           C  
ATOM   6790  CG  PHE C 281    -154.261  -5.712  11.616  1.00  6.04           C  
ATOM   6791  CD1 PHE C 281    -153.064  -5.961  11.060  1.00  7.85           C  
ATOM   6792  CD2 PHE C 281    -155.319  -5.560  10.803  1.00  2.92           C  
ATOM   6793  CE1 PHE C 281    -152.939  -6.013   9.656  1.00 10.58           C  
ATOM   6794  CE2 PHE C 281    -155.198  -5.600   9.417  1.00  3.83           C  
ATOM   6795  CZ  PHE C 281    -154.046  -5.823   8.843  1.00  2.63           C  
ATOM   6796  N   ALA C 282    -153.473  -2.397  12.793  1.00 31.54           N  
ATOM   6797  CA  ALA C 282    -153.854  -1.009  12.563  1.00 36.83           C  
ATOM   6798  C   ALA C 282    -154.740  -0.970  11.353  1.00 33.04           C  
ATOM   6799  O   ALA C 282    -155.541  -0.047  11.183  1.00 35.36           O  
ATOM   6800  CB  ALA C 282    -152.628  -0.117  12.374  1.00 37.31           C  
ATOM   6801  N   GLY C 283    -154.617  -2.003  10.539  1.00 21.61           N  
ATOM   6802  CA  GLY C 283    -155.365  -2.084   9.311  1.00 22.66           C  
ATOM   6803  C   GLY C 283    -154.303  -2.345   8.295  1.00 24.15           C  
ATOM   6804  O   GLY C 283    -153.110  -2.237   8.621  1.00 25.19           O  
ATOM   6805  N   GLY C 284    -154.719  -2.698   7.082  1.00 25.33           N  
ATOM   6806  CA  GLY C 284    -153.766  -3.020   6.013  1.00 31.18           C  
ATOM   6807  C   GLY C 284    -154.362  -4.000   5.035  1.00 34.91           C  
ATOM   6808  O   GLY C 284    -155.112  -4.897   5.434  1.00 42.47           O  
ATOM   6809  N   ASP C 285    -154.034  -3.843   3.761  1.00 30.78           N  
ATOM   6810  CA  ASP C 285    -154.657  -4.658   2.715  1.00 35.72           C  
ATOM   6811  C   ASP C 285    -153.891  -5.977   2.379  1.00 32.23           C  
ATOM   6812  O   ASP C 285    -154.179  -6.662   1.385  1.00 27.90           O  
ATOM   6813  CB  ASP C 285    -154.861  -3.791   1.471  1.00 40.77           C  
ATOM   6814  CG  ASP C 285    -153.559  -3.277   0.892  1.00 55.15           C  
ATOM   6815  OD1 ASP C 285    -152.784  -2.600   1.615  1.00 50.99           O  
ATOM   6816  OD2 ASP C 285    -153.308  -3.557  -0.298  1.00 58.20           O  
ATOM   6817  N   ALA C 286    -152.901  -6.309   3.200  1.00 32.59           N  
ATOM   6818  CA  ALA C 286    -152.191  -7.569   3.073  1.00 30.93           C  
ATOM   6819  C   ALA C 286    -152.450  -8.436   4.307  1.00 30.82           C  
ATOM   6820  O   ALA C 286    -151.814  -9.486   4.465  1.00 31.03           O  
ATOM   6821  CB  ALA C 286    -150.682  -7.329   2.873  1.00 24.53           C  
ATOM   6822  N   GLY C 287    -153.372  -8.018   5.177  1.00 19.00           N  
ATOM   6823  CA  GLY C 287    -153.824  -8.883   6.271  1.00 20.34           C  
ATOM   6824  C   GLY C 287    -152.882  -9.114   7.450  1.00 20.78           C  
ATOM   6825  O   GLY C 287    -151.673  -8.822   7.392  1.00 21.93           O  
ATOM   6826  N   ASP C 288    -153.451  -9.675   8.514  1.00 17.67           N  
ATOM   6827  CA  ASP C 288    -152.817  -9.731   9.818  1.00 20.62           C  
ATOM   6828  C   ASP C 288    -152.036 -11.029   9.945  1.00 28.79           C  
ATOM   6829  O   ASP C 288    -152.287 -11.828  10.855  1.00 37.94           O  
ATOM   6830  CB  ASP C 288    -153.904  -9.626  10.930  1.00 21.83           C  
ATOM   6831  CG  ASP C 288    -153.319  -9.341  12.346  1.00 29.65           C  
ATOM   6832  OD1 ASP C 288    -152.054  -9.267  12.484  1.00 32.78           O  
ATOM   6833  OD2 ASP C 288    -154.131  -9.203  13.320  1.00 19.21           O  
ATOM   6834  N   ALA C 289    -151.090 -11.272   9.052  1.00 29.19           N  
ATOM   6835  CA  ALA C 289    -150.208 -12.423   9.239  1.00 31.57           C  
ATOM   6836  C   ALA C 289    -149.874 -12.612  10.737  1.00 35.46           C  
ATOM   6837  O   ALA C 289    -150.036 -13.697  11.276  1.00 40.20           O  
ATOM   6838  CB  ALA C 289    -148.951 -12.271   8.426  1.00 31.03           C  
ATOM   6839  N   PHE C 290    -149.485 -11.546  11.427  1.00 36.47           N  
ATOM   6840  CA  PHE C 290    -149.124 -11.631  12.858  1.00 39.60           C  
ATOM   6841  C   PHE C 290    -150.206 -12.218  13.792  1.00 37.40           C  
ATOM   6842  O   PHE C 290    -149.923 -12.597  14.948  1.00 31.20           O  
ATOM   6843  CB  PHE C 290    -148.690 -10.245  13.342  1.00 42.36           C  
ATOM   6844  CG  PHE C 290    -147.293  -9.817  12.867  1.00 45.70           C  
ATOM   6845  CD1 PHE C 290    -146.561 -10.557  11.922  1.00 46.47           C  
ATOM   6846  CD2 PHE C 290    -146.714  -8.670  13.369  1.00 41.35           C  
ATOM   6847  CE1 PHE C 290    -145.284 -10.165  11.515  1.00 37.75           C  
ATOM   6848  CE2 PHE C 290    -145.457  -8.276  12.954  1.00 41.23           C  
ATOM   6849  CZ  PHE C 290    -144.749  -9.027  12.020  1.00 39.09           C  
ATOM   6850  N   ASP C 291    -151.429 -12.304  13.275  1.00 35.93           N  
ATOM   6851  CA  ASP C 291    -152.497 -13.040  13.929  1.00 40.31           C  
ATOM   6852  C   ASP C 291    -152.330 -14.534  13.671  1.00 43.18           C  
ATOM   6853  O   ASP C 291    -153.015 -15.374  14.277  1.00 44.93           O  
ATOM   6854  CB  ASP C 291    -153.868 -12.602  13.400  1.00 39.75           C  
ATOM   6855  CG  ASP C 291    -154.931 -12.502  14.505  1.00 45.71           C  
ATOM   6856  OD1 ASP C 291    -154.572 -12.220  15.669  1.00 44.46           O  
ATOM   6857  OD2 ASP C 291    -156.138 -12.681  14.206  1.00 44.01           O  
ATOM   6858  N   GLY C 292    -151.414 -14.871  12.773  1.00 40.84           N  
ATOM   6859  CA  GLY C 292    -151.295 -16.232  12.311  1.00 38.90           C  
ATOM   6860  C   GLY C 292    -152.361 -16.501  11.265  1.00 36.71           C  
ATOM   6861  O   GLY C 292    -153.128 -15.601  10.834  1.00 32.86           O  
ATOM   6862  N   PHE C 293    -152.417 -17.764  10.875  1.00 33.53           N  
ATOM   6863  CA  PHE C 293    -153.155 -18.151   9.706  1.00 26.35           C  
ATOM   6864  C   PHE C 293    -153.546 -19.655   9.697  1.00 28.47           C  
ATOM   6865  O   PHE C 293    -152.961 -20.493  10.394  1.00 24.90           O  
ATOM   6866  CB  PHE C 293    -152.306 -17.744   8.515  1.00 17.90           C  
ATOM   6867  CG  PHE C 293    -152.944 -17.984   7.203  1.00 15.69           C  
ATOM   6868  CD1 PHE C 293    -152.285 -18.691   6.230  1.00 18.69           C  
ATOM   6869  CD2 PHE C 293    -154.178 -17.494   6.926  1.00 11.33           C  
ATOM   6870  CE1 PHE C 293    -152.854 -18.910   5.010  1.00 19.00           C  
ATOM   6871  CE2 PHE C 293    -154.740 -17.702   5.714  1.00 13.24           C  
ATOM   6872  CZ  PHE C 293    -154.090 -18.422   4.753  1.00 14.77           C  
ATOM   6873  N   ASP C 294    -154.590 -19.954   8.933  1.00 33.84           N  
ATOM   6874  CA  ASP C 294    -155.148 -21.288   8.829  1.00 32.90           C  
ATOM   6875  C   ASP C 294    -154.749 -21.883   7.508  1.00 27.17           C  
ATOM   6876  O   ASP C 294    -155.511 -21.968   6.551  1.00 27.92           O  
ATOM   6877  CB  ASP C 294    -156.656 -21.237   9.002  1.00 37.33           C  
ATOM   6878  CG  ASP C 294    -157.046 -21.074  10.451  1.00 48.45           C  
ATOM   6879  OD1 ASP C 294    -157.865 -20.168  10.753  1.00 53.25           O  
ATOM   6880  OD2 ASP C 294    -156.504 -21.851  11.292  1.00 47.36           O  
ATOM   6881  N   PHE C 295    -153.496 -22.271   7.495  1.00 27.57           N  
ATOM   6882  CA  PHE C 295    -152.904 -23.062   6.441  1.00 33.22           C  
ATOM   6883  C   PHE C 295    -153.686 -24.385   6.061  1.00 39.07           C  
ATOM   6884  O   PHE C 295    -153.580 -24.867   4.922  1.00 36.37           O  
ATOM   6885  CB  PHE C 295    -151.473 -23.390   6.898  1.00 32.42           C  
ATOM   6886  CG  PHE C 295    -150.607 -22.168   7.174  1.00 32.89           C  
ATOM   6887  CD1 PHE C 295    -150.341 -21.754   8.479  1.00 32.49           C  
ATOM   6888  CD2 PHE C 295    -150.041 -21.443   6.129  1.00 31.04           C  
ATOM   6889  CE1 PHE C 295    -149.508 -20.650   8.730  1.00 26.95           C  
ATOM   6890  CE2 PHE C 295    -149.219 -20.339   6.377  1.00 27.81           C  
ATOM   6891  CZ  PHE C 295    -148.950 -19.957   7.683  1.00 25.38           C  
ATOM   6892  N   GLY C 296    -154.443 -24.970   7.000  1.00 34.76           N  
ATOM   6893  CA  GLY C 296    -155.235 -26.167   6.723  1.00 32.25           C  
ATOM   6894  C   GLY C 296    -154.558 -27.477   7.092  1.00 37.38           C  
ATOM   6895  O   GLY C 296    -155.188 -28.559   7.059  1.00 39.40           O  
ATOM   6896  N   ASP C 297    -153.271 -27.396   7.422  1.00 32.69           N  
ATOM   6897  CA  ASP C 297    -152.562 -28.520   8.036  1.00 36.10           C  
ATOM   6898  C   ASP C 297    -153.271 -28.922   9.333  1.00 41.44           C  
ATOM   6899  O   ASP C 297    -153.362 -30.100   9.645  1.00 43.92           O  
ATOM   6900  CB  ASP C 297    -151.093 -28.172   8.365  1.00 34.69           C  
ATOM   6901  CG  ASP C 297    -150.194 -28.032   7.113  1.00 34.80           C  
ATOM   6902  OD1 ASP C 297    -150.720 -27.989   5.970  1.00 30.85           O  
ATOM   6903  OD2 ASP C 297    -148.940 -27.962   7.292  1.00 28.54           O  
ATOM   6904  N   ASP C 298    -153.771 -27.943  10.085  1.00 46.12           N  
ATOM   6905  CA  ASP C 298    -154.412 -28.201  11.381  1.00 50.16           C  
ATOM   6906  C   ASP C 298    -155.166 -26.956  11.912  1.00 56.74           C  
ATOM   6907  O   ASP C 298    -154.750 -25.808  11.683  1.00 51.97           O  
ATOM   6908  CB  ASP C 298    -153.346 -28.622  12.396  1.00 49.45           C  
ATOM   6909  CG  ASP C 298    -153.910 -29.465  13.528  1.00 46.15           C  
ATOM   6910  OD1 ASP C 298    -153.441 -30.623  13.717  1.00 46.89           O  
ATOM   6911  OD2 ASP C 298    -154.810 -28.968  14.240  1.00 47.06           O  
ATOM   6912  N   PRO C 299    -156.286 -27.174  12.624  1.00 53.90           N  
ATOM   6913  CA  PRO C 299    -156.945 -26.065  13.333  1.00 50.04           C  
ATOM   6914  C   PRO C 299    -155.997 -25.185  14.138  1.00 47.86           C  
ATOM   6915  O   PRO C 299    -156.236 -23.977  14.267  1.00 49.36           O  
ATOM   6916  CB  PRO C 299    -157.903 -26.794  14.268  1.00 53.84           C  
ATOM   6917  CG  PRO C 299    -158.337 -28.003  13.446  1.00 51.74           C  
ATOM   6918  CD  PRO C 299    -157.158 -28.364  12.548  1.00 51.69           C  
ATOM   6919  N   SER C 300    -154.936 -25.804  14.656  1.00 42.49           N  
ATOM   6920  CA  SER C 300    -153.900 -25.135  15.437  1.00 43.35           C  
ATOM   6921  C   SER C 300    -153.082 -24.116  14.658  1.00 44.11           C  
ATOM   6922  O   SER C 300    -152.579 -23.142  15.240  1.00 40.95           O  
ATOM   6923  CB  SER C 300    -152.937 -26.174  15.984  1.00 41.68           C  
ATOM   6924  OG  SER C 300    -153.644 -27.261  16.511  1.00 45.72           O  
ATOM   6925  N   ASP C 301    -152.910 -24.359  13.361  1.00 44.18           N  
ATOM   6926  CA  ASP C 301    -152.267 -23.381  12.477  1.00 45.49           C  
ATOM   6927  C   ASP C 301    -152.457 -21.948  12.978  1.00 49.10           C  
ATOM   6928  O   ASP C 301    -151.483 -21.243  13.295  1.00 40.49           O  
ATOM   6929  CB  ASP C 301    -152.866 -23.454  11.072  1.00 45.76           C  
ATOM   6930  CG  ASP C 301    -152.505 -24.699  10.352  1.00 42.45           C  
ATOM   6931  OD1 ASP C 301    -151.469 -25.284  10.698  1.00 45.28           O  
ATOM   6932  OD2 ASP C 301    -153.268 -25.091   9.441  1.00 47.95           O  
ATOM   6933  N   LYS C 302    -153.722 -21.534  13.013  1.00 36.42           N  
ATOM   6934  CA  LYS C 302    -154.112 -20.251  13.522  1.00 40.81           C  
ATOM   6935  C   LYS C 302    -153.290 -19.857  14.747  1.00 42.35           C  
ATOM   6936  O   LYS C 302    -152.486 -18.930  14.683  1.00 45.54           O  
ATOM   6937  CB  LYS C 302    -155.602 -20.309  13.883  1.00 51.65           C  
ATOM   6938  CG  LYS C 302    -156.257 -18.942  14.153  1.00 56.38           C  
ATOM   6939  CD  LYS C 302    -156.388 -18.038  12.890  1.00 54.54           C  
ATOM   6940  CE  LYS C 302    -156.295 -16.604  13.292  1.00 47.41           C  
ATOM   6941  NZ  LYS C 302    -155.000 -16.437  14.002  1.00 43.88           N  
ATOM   6942  N   PHE C 303    -153.473 -20.603  15.833  1.00 38.64           N  
ATOM   6943  CA  PHE C 303    -152.881 -20.330  17.156  1.00 41.36           C  
ATOM   6944  C   PHE C 303    -151.382 -20.194  17.137  1.00 40.89           C  
ATOM   6945  O   PHE C 303    -150.790 -19.426  17.897  1.00 44.07           O  
ATOM   6946  CB  PHE C 303    -153.200 -21.536  18.057  1.00 43.62           C  
ATOM   6947  CG  PHE C 303    -152.751 -21.402  19.505  1.00 40.58           C  
ATOM   6948  CD1 PHE C 303    -153.644 -21.001  20.482  1.00 39.00           C  
ATOM   6949  CD2 PHE C 303    -151.476 -21.762  19.894  1.00 38.54           C  
ATOM   6950  CE1 PHE C 303    -153.259 -20.916  21.800  1.00 39.92           C  
ATOM   6951  CE2 PHE C 303    -151.086 -21.676  21.211  1.00 36.58           C  
ATOM   6952  CZ  PHE C 303    -151.973 -21.255  22.164  1.00 36.30           C  
ATOM   6953  N   PHE C 304    -150.769 -21.015  16.304  1.00 41.39           N  
ATOM   6954  CA  PHE C 304    -149.352 -21.268  16.420  1.00 43.51           C  
ATOM   6955  C   PHE C 304    -148.593 -20.404  15.500  1.00 33.62           C  
ATOM   6956  O   PHE C 304    -147.513 -20.013  15.822  1.00 32.36           O  
ATOM   6957  CB  PHE C 304    -149.027 -22.738  16.111  1.00 49.58           C  
ATOM   6958  CG  PHE C 304    -149.182 -23.643  17.303  1.00 52.97           C  
ATOM   6959  CD1 PHE C 304    -148.203 -23.701  18.284  1.00 55.92           C  
ATOM   6960  CD2 PHE C 304    -150.314 -24.394  17.471  1.00 48.77           C  
ATOM   6961  CE1 PHE C 304    -148.348 -24.513  19.396  1.00 55.71           C  
ATOM   6962  CE2 PHE C 304    -150.460 -25.208  18.580  1.00 50.88           C  
ATOM   6963  CZ  PHE C 304    -149.477 -25.260  19.542  1.00 52.09           C  
ATOM   6964  N   THR C 305    -149.142 -20.126  14.332  1.00 32.09           N  
ATOM   6965  CA  THR C 305    -148.404 -19.353  13.360  1.00 29.16           C  
ATOM   6966  C   THR C 305    -148.603 -17.870  13.603  1.00 27.69           C  
ATOM   6967  O   THR C 305    -148.242 -17.086  12.748  1.00 27.54           O  
ATOM   6968  CB  THR C 305    -148.774 -19.721  11.895  1.00 29.97           C  
ATOM   6969  OG1 THR C 305    -150.163 -20.073  11.814  1.00 27.39           O  
ATOM   6970  CG2 THR C 305    -147.899 -20.873  11.384  1.00 20.69           C  
ATOM   6971  N   SER C 306    -149.155 -17.483  14.757  1.00 20.79           N  
ATOM   6972  CA  SER C 306    -149.213 -16.063  15.144  1.00 17.69           C  
ATOM   6973  C   SER C 306    -147.932 -15.637  15.836  1.00 17.11           C  
ATOM   6974  O   SER C 306    -147.404 -16.369  16.731  1.00 10.33           O  
ATOM   6975  CB  SER C 306    -150.355 -15.752  16.108  1.00 14.53           C  
ATOM   6976  OG  SER C 306    -149.843 -15.604  17.429  1.00 15.80           O  
ATOM   6977  N   HIS C 307    -147.489 -14.418  15.464  1.00 27.54           N  
ATOM   6978  CA  HIS C 307    -146.254 -13.823  16.006  1.00 26.73           C  
ATOM   6979  C   HIS C 307    -146.465 -12.834  17.117  1.00 20.92           C  
ATOM   6980  O   HIS C 307    -145.490 -12.503  17.815  1.00 14.86           O  
ATOM   6981  CB  HIS C 307    -145.482 -13.098  14.949  1.00 24.28           C  
ATOM   6982  CG  HIS C 307    -145.334 -13.876  13.702  1.00 25.26           C  
ATOM   6983  ND1 HIS C 307    -146.315 -13.879  12.734  1.00 27.44           N  
ATOM   6984  CD2 HIS C 307    -144.338 -14.680  13.254  1.00 24.24           C  
ATOM   6985  CE1 HIS C 307    -145.911 -14.625  11.723  1.00 29.73           C  
ATOM   6986  NE2 HIS C 307    -144.721 -15.132  12.013  1.00 26.02           N  
ATOM   6987  N   ASN C 308    -147.690 -12.342  17.303  1.00 20.03           N  
ATOM   6988  CA  ASN C 308    -147.797 -11.355  18.344  1.00 26.12           C  
ATOM   6989  C   ASN C 308    -147.421 -11.959  19.668  1.00 31.93           C  
ATOM   6990  O   ASN C 308    -147.905 -13.056  20.011  1.00 32.42           O  
ATOM   6991  CB  ASN C 308    -149.150 -10.689  18.509  1.00 25.13           C  
ATOM   6992  CG  ASN C 308    -149.045  -9.435  19.397  1.00 18.43           C  
ATOM   6993  OD1 ASN C 308    -148.021  -8.753  19.400  1.00 14.72           O  
ATOM   6994  ND2 ASN C 308    -150.063  -9.177  20.176  1.00 14.92           N  
ATOM   6995  N   GLY C 309    -146.579 -11.218  20.401  1.00 33.66           N  
ATOM   6996  CA  GLY C 309    -146.096 -11.637  21.705  1.00 33.90           C  
ATOM   6997  C   GLY C 309    -144.893 -12.561  21.635  1.00 38.80           C  
ATOM   6998  O   GLY C 309    -144.357 -12.955  22.661  1.00 42.12           O  
ATOM   6999  N   MET C 310    -144.443 -12.915  20.442  1.00 33.90           N  
ATOM   7000  CA  MET C 310    -143.369 -13.891  20.350  1.00 42.51           C  
ATOM   7001  C   MET C 310    -142.013 -13.244  20.602  1.00 41.32           C  
ATOM   7002  O   MET C 310    -141.789 -12.096  20.227  1.00 39.66           O  
ATOM   7003  CB  MET C 310    -143.392 -14.604  18.991  1.00 50.06           C  
ATOM   7004  CG  MET C 310    -144.650 -15.481  18.751  1.00 54.39           C  
ATOM   7005  SD  MET C 310    -144.863 -16.830  19.928  1.00 52.18           S  
ATOM   7006  CE  MET C 310    -145.674 -15.968  21.288  1.00 58.94           C  
ATOM   7007  N   GLN C 311    -141.138 -13.994  21.272  1.00 30.51           N  
ATOM   7008  CA  GLN C 311    -139.760 -13.607  21.502  1.00 28.18           C  
ATOM   7009  C   GLN C 311    -139.026 -13.883  20.200  1.00 29.81           C  
ATOM   7010  O   GLN C 311    -139.587 -14.469  19.266  1.00 31.16           O  
ATOM   7011  CB  GLN C 311    -139.125 -14.427  22.645  1.00 35.10           C  
ATOM   7012  CG  GLN C 311    -139.461 -14.022  24.117  1.00 40.77           C  
ATOM   7013  CD  GLN C 311    -138.701 -14.884  25.170  1.00 42.16           C  
ATOM   7014  OE1 GLN C 311    -138.497 -16.087  24.972  1.00 44.25           O  
ATOM   7015  NE2 GLN C 311    -138.281 -14.257  26.278  1.00 42.03           N  
ATOM   7016  N   PHE C 312    -137.762 -13.482  20.149  1.00 28.25           N  
ATOM   7017  CA  PHE C 312    -137.002 -13.536  18.929  1.00 27.38           C  
ATOM   7018  C   PHE C 312    -136.076 -14.720  19.006  1.00 37.28           C  
ATOM   7019  O   PHE C 312    -135.486 -14.979  20.062  1.00 34.16           O  
ATOM   7020  CB  PHE C 312    -136.174 -12.268  18.744  1.00 28.11           C  
ATOM   7021  CG  PHE C 312    -135.751 -12.031  17.322  1.00 30.83           C  
ATOM   7022  CD1 PHE C 312    -136.655 -11.524  16.392  1.00 32.06           C  
ATOM   7023  CD2 PHE C 312    -134.465 -12.315  16.901  1.00 19.01           C  
ATOM   7024  CE1 PHE C 312    -136.263 -11.289  15.047  1.00 28.64           C  
ATOM   7025  CE2 PHE C 312    -134.081 -12.084  15.574  1.00 18.42           C  
ATOM   7026  CZ  PHE C 312    -134.987 -11.578  14.645  1.00 18.70           C  
ATOM   7027  N   SER C 313    -135.951 -15.425  17.878  1.00 36.51           N  
ATOM   7028  CA  SER C 313    -135.120 -16.608  17.785  1.00 33.35           C  
ATOM   7029  C   SER C 313    -134.180 -16.485  16.612  1.00 36.98           C  
ATOM   7030  O   SER C 313    -134.565 -15.995  15.546  1.00 35.32           O  
ATOM   7031  CB  SER C 313    -135.988 -17.842  17.590  1.00 33.61           C  
ATOM   7032  OG  SER C 313    -136.751 -18.085  18.742  1.00 35.91           O  
ATOM   7033  N   THR C 314    -132.946 -16.913  16.832  1.00 35.33           N  
ATOM   7034  CA  THR C 314    -132.030 -17.176  15.763  1.00 39.94           C  
ATOM   7035  C   THR C 314    -131.593 -18.622  15.820  1.00 37.17           C  
ATOM   7036  O   THR C 314    -131.852 -19.334  16.785  1.00 31.60           O  
ATOM   7037  CB  THR C 314    -130.769 -16.305  15.875  1.00 45.24           C  
ATOM   7038  OG1 THR C 314    -130.225 -16.413  17.201  1.00 42.91           O  
ATOM   7039  CG2 THR C 314    -131.103 -14.854  15.523  1.00 44.87           C  
ATOM   7040  N   TRP C 315    -130.876 -19.032  14.789  1.00 33.17           N  
ATOM   7041  CA  TRP C 315    -130.366 -20.367  14.738  1.00 33.56           C  
ATOM   7042  C   TRP C 315    -129.665 -20.805  16.037  1.00 33.54           C  
ATOM   7043  O   TRP C 315    -129.727 -21.967  16.409  1.00 30.23           O  
ATOM   7044  CB  TRP C 315    -129.472 -20.533  13.506  1.00 38.38           C  
ATOM   7045  CG  TRP C 315    -128.056 -20.074  13.586  1.00 34.63           C  
ATOM   7046  CD1 TRP C 315    -127.522 -19.005  12.952  1.00 38.25           C  
ATOM   7047  CD2 TRP C 315    -126.973 -20.725  14.251  1.00 37.60           C  
ATOM   7048  NE1 TRP C 315    -126.170 -18.913  13.209  1.00 41.83           N  
ATOM   7049  CE2 TRP C 315    -125.810 -19.963  14.004  1.00 43.78           C  
ATOM   7050  CE3 TRP C 315    -126.874 -21.858  15.059  1.00 39.79           C  
ATOM   7051  CZ2 TRP C 315    -124.569 -20.304  14.525  1.00 45.58           C  
ATOM   7052  CZ3 TRP C 315    -125.634 -22.202  15.576  1.00 39.45           C  
ATOM   7053  CH2 TRP C 315    -124.501 -21.432  15.307  1.00 43.54           C  
ATOM   7054  N   ASP C 316    -129.009 -19.877  16.724  1.00 35.38           N  
ATOM   7055  CA  ASP C 316    -128.353 -20.187  17.989  1.00 32.46           C  
ATOM   7056  C   ASP C 316    -129.113 -19.588  19.148  1.00 29.72           C  
ATOM   7057  O   ASP C 316    -128.509 -19.220  20.142  1.00 34.94           O  
ATOM   7058  CB  ASP C 316    -126.875 -19.730  18.006  1.00 32.37           C  
ATOM   7059  CG  ASP C 316    -126.642 -18.348  17.362  1.00 31.56           C  
ATOM   7060  OD1 ASP C 316    -127.388 -17.962  16.440  1.00 32.75           O  
ATOM   7061  OD2 ASP C 316    -125.680 -17.654  17.759  1.00 28.02           O  
ATOM   7062  N   ASN C 317    -130.431 -19.471  19.002  1.00 28.45           N  
ATOM   7063  CA  ASN C 317    -131.347 -19.176  20.128  1.00 31.19           C  
ATOM   7064  C   ASN C 317    -132.756 -19.794  19.869  1.00 31.60           C  
ATOM   7065  O   ASN C 317    -133.411 -19.427  18.899  1.00 32.05           O  
ATOM   7066  CB  ASN C 317    -131.442 -17.654  20.350  1.00 28.90           C  
ATOM   7067  CG  ASN C 317    -130.870 -17.210  21.682  1.00 27.38           C  
ATOM   7068  OD1 ASN C 317    -131.529 -17.329  22.701  1.00 32.85           O  
ATOM   7069  ND2 ASN C 317    -129.668 -16.657  21.672  1.00 19.22           N  
ATOM   7070  N   ASP C 318    -133.213 -20.735  20.704  1.00 35.20           N  
ATOM   7071  CA  ASP C 318    -134.530 -21.386  20.478  1.00 39.72           C  
ATOM   7072  C   ASP C 318    -135.582 -20.740  21.326  1.00 40.82           C  
ATOM   7073  O   ASP C 318    -135.863 -21.217  22.430  1.00 46.68           O  
ATOM   7074  CB  ASP C 318    -134.507 -22.885  20.818  1.00 42.60           C  
ATOM   7075  CG  ASP C 318    -134.709 -23.775  19.599  1.00 39.46           C  
ATOM   7076  OD1 ASP C 318    -135.842 -24.321  19.438  1.00 32.36           O  
ATOM   7077  OD2 ASP C 318    -133.705 -23.943  18.847  1.00 44.80           O  
ATOM   7078  N   ASN C 319    -136.161 -19.651  20.833  1.00 38.35           N  
ATOM   7079  CA  ASN C 319    -137.227 -18.958  21.576  1.00 35.49           C  
ATOM   7080  C   ASN C 319    -138.568 -19.087  20.835  1.00 39.23           C  
ATOM   7081  O   ASN C 319    -139.408 -18.166  20.831  1.00 39.93           O  
ATOM   7082  CB  ASN C 319    -136.818 -17.519  21.865  1.00 21.78           C  
ATOM   7083  CG  ASN C 319    -135.502 -17.449  22.583  1.00 22.98           C  
ATOM   7084  OD1 ASN C 319    -134.436 -17.228  21.985  1.00 18.29           O  
ATOM   7085  ND2 ASN C 319    -135.553 -17.694  23.877  1.00 25.86           N  
ATOM   7086  N   ASP C 320    -138.748 -20.265  20.226  1.00 36.59           N  
ATOM   7087  CA  ASP C 320    -139.967 -20.601  19.511  1.00 38.50           C  
ATOM   7088  C   ASP C 320    -140.728 -21.554  20.394  1.00 39.63           C  
ATOM   7089  O   ASP C 320    -140.154 -22.053  21.358  1.00 40.64           O  
ATOM   7090  CB  ASP C 320    -139.690 -21.208  18.119  1.00 40.95           C  
ATOM   7091  CG  ASP C 320    -138.584 -22.254  18.119  1.00 44.69           C  
ATOM   7092  OD1 ASP C 320    -138.479 -22.994  19.132  1.00 46.54           O  
ATOM   7093  OD2 ASP C 320    -137.836 -22.327  17.097  1.00 36.37           O  
ATOM   7094  N   LYS C 321    -142.008 -21.773  20.074  1.00 33.27           N  
ATOM   7095  CA  LYS C 321    -142.880 -22.694  20.822  1.00 40.53           C  
ATOM   7096  C   LYS C 321    -142.855 -24.071  20.139  1.00 45.41           C  
ATOM   7097  O   LYS C 321    -143.900 -24.685  19.856  1.00 46.17           O  
ATOM   7098  CB  LYS C 321    -144.330 -22.189  20.872  1.00 42.69           C  
ATOM   7099  CG  LYS C 321    -144.534 -20.708  21.208  1.00 46.43           C  
ATOM   7100  CD  LYS C 321    -144.212 -20.424  22.662  1.00 51.26           C  
ATOM   7101  CE  LYS C 321    -144.720 -19.056  23.104  1.00 53.89           C  
ATOM   7102  NZ  LYS C 321    -144.439 -18.844  24.561  1.00 51.97           N  
ATOM   7103  N   PHE C 322    -141.642 -24.545  19.891  1.00 43.27           N  
ATOM   7104  CA  PHE C 322    -141.401 -25.693  19.046  1.00 41.87           C  
ATOM   7105  C   PHE C 322    -140.387 -26.527  19.747  1.00 43.14           C  
ATOM   7106  O   PHE C 322    -139.300 -26.047  20.067  1.00 39.96           O  
ATOM   7107  CB  PHE C 322    -140.799 -25.214  17.728  1.00 39.42           C  
ATOM   7108  CG  PHE C 322    -140.778 -26.236  16.605  1.00 29.32           C  
ATOM   7109  CD1 PHE C 322    -139.762 -26.185  15.663  1.00 27.05           C  
ATOM   7110  CD2 PHE C 322    -141.765 -27.171  16.436  1.00 18.70           C  
ATOM   7111  CE1 PHE C 322    -139.739 -27.038  14.597  1.00 21.33           C  
ATOM   7112  CE2 PHE C 322    -141.729 -28.012  15.371  1.00 16.34           C  
ATOM   7113  CZ  PHE C 322    -140.727 -27.945  14.452  1.00 18.42           C  
ATOM   7114  N   GLU C 323    -140.774 -27.755  20.032  1.00 46.28           N  
ATOM   7115  CA  GLU C 323    -139.843 -28.826  20.317  1.00 45.76           C  
ATOM   7116  C   GLU C 323    -138.517 -28.623  19.549  1.00 37.68           C  
ATOM   7117  O   GLU C 323    -137.420 -28.624  20.141  1.00 35.02           O  
ATOM   7118  CB  GLU C 323    -140.513 -30.169  19.948  1.00 52.72           C  
ATOM   7119  CG  GLU C 323    -141.481 -30.145  18.698  1.00 55.65           C  
ATOM   7120  CD  GLU C 323    -142.973 -29.851  19.032  1.00 60.57           C  
ATOM   7121  OE1 GLU C 323    -143.865 -30.471  18.394  1.00 59.55           O  
ATOM   7122  OE2 GLU C 323    -143.262 -29.000  19.913  1.00 60.31           O  
ATOM   7123  N   GLY C 324    -138.640 -28.417  18.238  1.00 35.63           N  
ATOM   7124  CA  GLY C 324    -137.493 -28.189  17.371  1.00 34.22           C  
ATOM   7125  C   GLY C 324    -137.115 -26.722  17.267  1.00 27.83           C  
ATOM   7126  O   GLY C 324    -137.434 -25.926  18.152  1.00 25.62           O  
ATOM   7127  N   ASN C 325    -136.431 -26.373  16.178  1.00 26.22           N  
ATOM   7128  CA  ASN C 325    -135.988 -25.013  15.975  1.00 29.63           C  
ATOM   7129  C   ASN C 325    -136.304 -24.455  14.614  1.00 28.43           C  
ATOM   7130  O   ASN C 325    -135.501 -24.570  13.685  1.00 27.11           O  
ATOM   7131  CB  ASN C 325    -134.496 -24.863  16.196  1.00 33.58           C  
ATOM   7132  CG  ASN C 325    -134.060 -23.385  16.253  1.00 35.80           C  
ATOM   7133  OD1 ASN C 325    -132.846 -23.078  16.204  1.00 32.94           O  
ATOM   7134  ND2 ASN C 325    -135.056 -22.461  16.384  1.00 34.90           N  
ATOM   7135  N   CYS C 326    -137.450 -23.780  14.538  1.00 26.99           N  
ATOM   7136  CA  CYS C 326    -137.878 -23.093  13.336  1.00 23.44           C  
ATOM   7137  C   CYS C 326    -136.720 -22.315  12.704  1.00 31.71           C  
ATOM   7138  O   CYS C 326    -136.358 -22.566  11.545  1.00 28.48           O  
ATOM   7139  CB  CYS C 326    -138.969 -22.116  13.703  1.00 24.17           C  
ATOM   7140  SG  CYS C 326    -140.352 -22.756  14.669  1.00 29.25           S  
ATOM   7141  N   ALA C 327    -136.139 -21.396  13.508  1.00 39.61           N  
ATOM   7142  CA  ALA C 327    -135.059 -20.462  13.108  1.00 33.65           C  
ATOM   7143  C   ALA C 327    -133.989 -21.155  12.294  1.00 36.69           C  
ATOM   7144  O   ALA C 327    -133.329 -20.522  11.447  1.00 42.08           O  
ATOM   7145  CB  ALA C 327    -134.420 -19.795  14.342  1.00 23.04           C  
ATOM   7146  N   GLU C 328    -133.818 -22.452  12.545  1.00 29.46           N  
ATOM   7147  CA  GLU C 328    -132.789 -23.216  11.871  1.00 31.59           C  
ATOM   7148  C   GLU C 328    -133.356 -23.912  10.644  1.00 24.05           C  
ATOM   7149  O   GLU C 328    -132.725 -23.957   9.590  1.00 22.97           O  
ATOM   7150  CB  GLU C 328    -132.234 -24.219  12.850  1.00 34.98           C  
ATOM   7151  CG  GLU C 328    -130.876 -24.748  12.535  1.00 40.25           C  
ATOM   7152  CD  GLU C 328    -130.553 -25.932  13.439  1.00 52.16           C  
ATOM   7153  OE1 GLU C 328    -129.363 -26.094  13.839  1.00 54.07           O  
ATOM   7154  OE2 GLU C 328    -131.513 -26.684  13.770  1.00 47.09           O  
ATOM   7155  N   GLN C 329    -134.572 -24.424  10.784  1.00 30.18           N  
ATOM   7156  CA  GLN C 329    -135.184 -25.258   9.750  1.00 33.91           C  
ATOM   7157  C   GLN C 329    -135.350 -24.431   8.507  1.00 39.98           C  
ATOM   7158  O   GLN C 329    -135.184 -24.917   7.372  1.00 38.13           O  
ATOM   7159  CB  GLN C 329    -136.541 -25.783  10.214  1.00 32.24           C  
ATOM   7160  CG  GLN C 329    -136.432 -26.631  11.473  1.00 33.72           C  
ATOM   7161  CD  GLN C 329    -137.573 -27.599  11.640  1.00 45.80           C  
ATOM   7162  OE1 GLN C 329    -138.761 -27.233  11.524  1.00 47.69           O  
ATOM   7163  NE2 GLN C 329    -137.228 -28.856  11.914  1.00 41.75           N  
ATOM   7164  N   ASP C 330    -135.670 -23.161   8.773  1.00 45.29           N  
ATOM   7165  CA  ASP C 330    -135.903 -22.139   7.762  1.00 44.38           C  
ATOM   7166  C   ASP C 330    -134.592 -21.452   7.441  1.00 47.37           C  
ATOM   7167  O   ASP C 330    -134.130 -21.493   6.299  1.00 47.30           O  
ATOM   7168  CB  ASP C 330    -136.931 -21.139   8.276  1.00 40.16           C  
ATOM   7169  CG  ASP C 330    -138.325 -21.738   8.373  1.00 46.11           C  
ATOM   7170  OD1 ASP C 330    -138.540 -22.863   7.857  1.00 49.27           O  
ATOM   7171  OD2 ASP C 330    -139.216 -21.082   8.961  1.00 45.88           O  
ATOM   7172  N   GLY C 331    -133.962 -20.865   8.450  1.00 40.59           N  
ATOM   7173  CA  GLY C 331    -132.640 -20.297   8.249  1.00 42.58           C  
ATOM   7174  C   GLY C 331    -132.777 -18.808   8.126  1.00 46.94           C  
ATOM   7175  O   GLY C 331    -132.409 -18.185   7.101  1.00 43.47           O  
ATOM   7176  N   SER C 332    -133.336 -18.259   9.200  1.00 42.53           N  
ATOM   7177  CA  SER C 332    -133.457 -16.835   9.378  1.00 41.68           C  
ATOM   7178  C   SER C 332    -133.422 -16.536  10.882  1.00 41.03           C  
ATOM   7179  O   SER C 332    -132.807 -17.229  11.660  1.00 46.34           O  
ATOM   7180  CB  SER C 332    -134.756 -16.363   8.706  1.00 47.73           C  
ATOM   7181  OG  SER C 332    -135.921 -16.932   9.306  1.00 42.40           O  
ATOM   7182  N   GLY C 333    -134.067 -15.479  11.288  1.00 34.79           N  
ATOM   7183  CA  GLY C 333    -134.157 -15.149  12.677  1.00 34.26           C  
ATOM   7184  C   GLY C 333    -135.373 -14.251  12.768  1.00 35.25           C  
ATOM   7185  O   GLY C 333    -135.542 -13.258  12.022  1.00 34.16           O  
ATOM   7186  N   TRP C 334    -136.251 -14.601  13.677  1.00 30.01           N  
ATOM   7187  CA  TRP C 334    -137.580 -14.074  13.567  1.00 33.42           C  
ATOM   7188  C   TRP C 334    -138.238 -14.319  14.891  1.00 32.44           C  
ATOM   7189  O   TRP C 334    -137.562 -14.837  15.819  1.00 25.84           O  
ATOM   7190  CB  TRP C 334    -138.302 -14.766  12.420  1.00 32.39           C  
ATOM   7191  CG  TRP C 334    -139.465 -14.075  11.974  1.00 33.79           C  
ATOM   7192  CD1 TRP C 334    -140.724 -14.513  12.052  1.00 38.64           C  
ATOM   7193  CD2 TRP C 334    -139.519 -12.793  11.351  1.00 42.32           C  
ATOM   7194  NE1 TRP C 334    -141.583 -13.601  11.493  1.00 38.07           N  
ATOM   7195  CE2 TRP C 334    -140.864 -12.531  11.055  1.00 35.26           C  
ATOM   7196  CE3 TRP C 334    -138.560 -11.844  11.004  1.00 46.32           C  
ATOM   7197  CZ2 TRP C 334    -141.287 -11.362  10.444  1.00 32.96           C  
ATOM   7198  CZ3 TRP C 334    -138.990 -10.664  10.381  1.00 47.09           C  
ATOM   7199  CH2 TRP C 334    -140.346 -10.438  10.121  1.00 36.86           C  
ATOM   7200  N   TRP C 335    -139.503 -13.905  14.987  1.00 21.47           N  
ATOM   7201  CA  TRP C 335    -140.224 -14.003  16.217  1.00 25.79           C  
ATOM   7202  C   TRP C 335    -141.022 -15.233  15.994  1.00 25.97           C  
ATOM   7203  O   TRP C 335    -142.185 -15.171  15.640  1.00 30.46           O  
ATOM   7204  CB  TRP C 335    -141.117 -12.792  16.458  1.00 30.10           C  
ATOM   7205  CG  TRP C 335    -140.369 -11.491  16.730  1.00 33.16           C  
ATOM   7206  CD1 TRP C 335    -139.916 -11.046  17.942  1.00 32.53           C  
ATOM   7207  CD2 TRP C 335    -140.038 -10.471  15.783  1.00 30.23           C  
ATOM   7208  NE1 TRP C 335    -139.318  -9.830  17.810  1.00 29.86           N  
ATOM   7209  CE2 TRP C 335    -139.369  -9.448  16.493  1.00 31.07           C  
ATOM   7210  CE3 TRP C 335    -140.217 -10.334  14.403  1.00 32.15           C  
ATOM   7211  CZ2 TRP C 335    -138.877  -8.286  15.867  1.00 32.52           C  
ATOM   7212  CZ3 TRP C 335    -139.722  -9.189  13.774  1.00 36.38           C  
ATOM   7213  CH2 TRP C 335    -139.061  -8.174  14.515  1.00 35.91           C  
ATOM   7214  N   MET C 336    -140.356 -16.366  16.182  1.00 30.02           N  
ATOM   7215  CA  MET C 336    -140.874 -17.665  15.780  1.00 24.07           C  
ATOM   7216  C   MET C 336    -141.822 -18.190  16.818  1.00 25.43           C  
ATOM   7217  O   MET C 336    -141.730 -17.843  18.001  1.00 17.93           O  
ATOM   7218  CB  MET C 336    -139.732 -18.645  15.598  1.00 22.87           C  
ATOM   7219  CG  MET C 336    -138.908 -18.419  14.338  1.00 17.89           C  
ATOM   7220  SD  MET C 336    -140.068 -18.648  12.987  1.00 20.17           S  
ATOM   7221  CE  MET C 336    -138.802 -18.620  11.698  1.00 14.95           C  
ATOM   7222  N   ASN C 337    -142.757 -19.012  16.344  1.00 30.36           N  
ATOM   7223  CA  ASN C 337    -143.750 -19.653  17.196  1.00 31.83           C  
ATOM   7224  C   ASN C 337    -143.809 -21.147  16.867  1.00 32.43           C  
ATOM   7225  O   ASN C 337    -142.966 -21.922  17.367  1.00 33.84           O  
ATOM   7226  CB  ASN C 337    -145.090 -18.949  17.041  1.00 33.03           C  
ATOM   7227  CG  ASN C 337    -146.175 -19.566  17.896  1.00 37.39           C  
ATOM   7228  OD1 ASN C 337    -146.012 -20.668  18.404  1.00 38.27           O  
ATOM   7229  ND2 ASN C 337    -147.309 -18.869  18.026  1.00 36.13           N  
ATOM   7230  N   LYS C 338    -144.759 -21.567  16.032  1.00 32.12           N  
ATOM   7231  CA  LYS C 338    -144.722 -22.948  15.517  1.00 38.82           C  
ATOM   7232  C   LYS C 338    -145.359 -23.074  14.127  1.00 37.60           C  
ATOM   7233  O   LYS C 338    -146.456 -23.631  13.992  1.00 38.19           O  
ATOM   7234  CB  LYS C 338    -145.355 -23.944  16.511  1.00 36.86           C  
ATOM   7235  CG  LYS C 338    -144.810 -25.380  16.357  1.00 37.04           C  
ATOM   7236  CD  LYS C 338    -145.544 -26.423  17.213  1.00 36.83           C  
ATOM   7237  CE  LYS C 338    -146.945 -26.773  16.687  1.00 38.44           C  
ATOM   7238  NZ  LYS C 338    -147.063 -26.806  15.179  1.00 37.88           N  
ATOM   7239  N   CYS C 339    -144.706 -22.518  13.107  1.00 32.98           N  
ATOM   7240  CA  CYS C 339    -143.528 -21.646  13.276  1.00 38.16           C  
ATOM   7241  C   CYS C 339    -143.761 -20.144  12.993  1.00 35.24           C  
ATOM   7242  O   CYS C 339    -143.180 -19.282  13.679  1.00 26.45           O  
ATOM   7243  CB  CYS C 339    -142.366 -22.167  12.424  1.00 38.70           C  
ATOM   7244  SG  CYS C 339    -141.532 -23.575  13.189  1.00 34.54           S  
ATOM   7245  N   HIS C 340    -144.594 -19.851  11.986  1.00 32.81           N  
ATOM   7246  CA  HIS C 340    -144.828 -18.485  11.515  1.00 30.83           C  
ATOM   7247  C   HIS C 340    -145.931 -18.362  10.434  1.00 32.70           C  
ATOM   7248  O   HIS C 340    -146.030 -19.217   9.543  1.00 36.00           O  
ATOM   7249  CB  HIS C 340    -143.513 -17.979  10.945  1.00 32.75           C  
ATOM   7250  CG  HIS C 340    -143.167 -18.538   9.594  1.00 33.47           C  
ATOM   7251  ND1 HIS C 340    -144.063 -18.563   8.540  1.00 27.83           N  
ATOM   7252  CD2 HIS C 340    -141.988 -18.982   9.094  1.00 34.37           C  
ATOM   7253  CE1 HIS C 340    -143.458 -19.025   7.461  1.00 30.25           C  
ATOM   7254  NE2 HIS C 340    -142.200 -19.285   7.770  1.00 31.89           N  
ATOM   7255  N   ALA C 341    -146.761 -17.320  10.498  1.00 26.52           N  
ATOM   7256  CA  ALA C 341    -147.707 -17.010   9.384  1.00 24.04           C  
ATOM   7257  C   ALA C 341    -147.177 -15.962   8.398  1.00 26.69           C  
ATOM   7258  O   ALA C 341    -147.532 -16.000   7.204  1.00 24.98           O  
ATOM   7259  CB  ALA C 341    -149.092 -16.612   9.906  1.00 18.37           C  
ATOM   7260  N   GLY C 342    -146.329 -15.056   8.911  1.00 22.21           N  
ATOM   7261  CA  GLY C 342    -145.543 -14.104   8.118  1.00 22.14           C  
ATOM   7262  C   GLY C 342    -144.090 -14.167   8.560  1.00 21.04           C  
ATOM   7263  O   GLY C 342    -143.849 -14.248   9.757  1.00 24.66           O  
ATOM   7264  N   HIS C 343    -143.135 -14.113   7.626  1.00 14.55           N  
ATOM   7265  CA  HIS C 343    -141.749 -14.465   7.911  1.00 20.68           C  
ATOM   7266  C   HIS C 343    -140.952 -13.753   6.840  1.00 33.96           C  
ATOM   7267  O   HIS C 343    -140.884 -14.257   5.697  1.00 34.71           O  
ATOM   7268  CB  HIS C 343    -141.655 -15.996   7.769  1.00 25.39           C  
ATOM   7269  CG  HIS C 343    -140.282 -16.593   7.900  1.00 26.63           C  
ATOM   7270  ND1 HIS C 343    -139.650 -17.256   6.855  1.00 22.76           N  
ATOM   7271  CD2 HIS C 343    -139.460 -16.709   8.970  1.00 25.92           C  
ATOM   7272  CE1 HIS C 343    -138.478 -17.708   7.267  1.00 24.43           C  
ATOM   7273  NE2 HIS C 343    -138.333 -17.377   8.543  1.00 31.95           N  
ATOM   7274  N   LEU C 344    -140.396 -12.573   7.169  1.00 31.59           N  
ATOM   7275  CA  LEU C 344    -139.850 -11.638   6.137  1.00 26.54           C  
ATOM   7276  C   LEU C 344    -138.331 -11.585   6.175  1.00 27.88           C  
ATOM   7277  O   LEU C 344    -137.678 -10.752   5.481  1.00 22.39           O  
ATOM   7278  CB  LEU C 344    -140.380 -10.224   6.325  1.00 26.33           C  
ATOM   7279  CG  LEU C 344    -141.859 -10.004   6.549  1.00 25.78           C  
ATOM   7280  CD1 LEU C 344    -142.053  -8.524   6.799  1.00 27.89           C  
ATOM   7281  CD2 LEU C 344    -142.605 -10.480   5.352  1.00 27.46           C  
ATOM   7282  N   ASN C 345    -137.757 -12.473   6.985  1.00 28.04           N  
ATOM   7283  CA  ASN C 345    -136.323 -12.748   6.867  1.00 25.93           C  
ATOM   7284  C   ASN C 345    -136.128 -13.958   6.007  1.00 16.28           C  
ATOM   7285  O   ASN C 345    -135.096 -14.601   6.046  1.00 16.74           O  
ATOM   7286  CB  ASN C 345    -135.674 -12.885   8.234  1.00 24.86           C  
ATOM   7287  CG  ASN C 345    -135.721 -11.577   9.012  1.00 27.21           C  
ATOM   7288  OD1 ASN C 345    -136.010 -10.486   8.448  1.00 21.53           O  
ATOM   7289  ND2 ASN C 345    -135.476 -11.675  10.321  1.00 28.16           N  
ATOM   7290  N   GLY C 346    -137.111 -14.191   5.152  1.00 17.10           N  
ATOM   7291  CA  GLY C 346    -137.156 -15.383   4.354  1.00 26.35           C  
ATOM   7292  C   GLY C 346    -135.935 -15.584   3.493  1.00 25.51           C  
ATOM   7293  O   GLY C 346    -135.207 -14.612   3.213  1.00 20.54           O  
ATOM   7294  N   VAL C 347    -135.697 -16.843   3.095  1.00 28.67           N  
ATOM   7295  CA  VAL C 347    -134.671 -17.086   2.083  1.00 34.67           C  
ATOM   7296  C   VAL C 347    -135.238 -16.524   0.797  1.00 31.07           C  
ATOM   7297  O   VAL C 347    -136.414 -16.766   0.445  1.00 24.78           O  
ATOM   7298  CB  VAL C 347    -134.254 -18.567   1.893  1.00 38.81           C  
ATOM   7299  CG1 VAL C 347    -133.845 -19.168   3.229  1.00 43.82           C  
ATOM   7300  CG2 VAL C 347    -135.337 -19.372   1.209  1.00 41.21           C  
ATOM   7301  N   TYR C 348    -134.424 -15.712   0.140  1.00 27.58           N  
ATOM   7302  CA  TYR C 348    -134.945 -14.933  -0.949  1.00 29.26           C  
ATOM   7303  C   TYR C 348    -135.026 -15.892  -2.107  1.00 20.07           C  
ATOM   7304  O   TYR C 348    -134.041 -16.127  -2.778  1.00 22.50           O  
ATOM   7305  CB  TYR C 348    -134.058 -13.676  -1.253  1.00 30.04           C  
ATOM   7306  CG  TYR C 348    -134.656 -12.791  -2.335  1.00 22.40           C  
ATOM   7307  CD1 TYR C 348    -135.743 -11.982  -2.060  1.00 19.22           C  
ATOM   7308  CD2 TYR C 348    -134.174 -12.832  -3.629  1.00 20.69           C  
ATOM   7309  CE1 TYR C 348    -136.316 -11.235  -3.010  1.00 21.85           C  
ATOM   7310  CE2 TYR C 348    -134.747 -12.092  -4.606  1.00 23.51           C  
ATOM   7311  CZ  TYR C 348    -135.822 -11.283  -4.292  1.00 31.50           C  
ATOM   7312  OH  TYR C 348    -136.404 -10.504  -5.275  1.00 38.19           O  
ATOM   7313  N   TYR C 349    -136.176 -16.493  -2.328  1.00 23.11           N  
ATOM   7314  CA  TYR C 349    -136.318 -17.253  -3.570  1.00 29.49           C  
ATOM   7315  C   TYR C 349    -136.571 -16.205  -4.652  1.00 29.03           C  
ATOM   7316  O   TYR C 349    -137.507 -15.388  -4.551  1.00 28.47           O  
ATOM   7317  CB  TYR C 349    -137.443 -18.324  -3.542  1.00 26.87           C  
ATOM   7318  CG  TYR C 349    -137.228 -19.448  -2.553  1.00 21.86           C  
ATOM   7319  CD1 TYR C 349    -137.826 -19.418  -1.301  1.00 28.34           C  
ATOM   7320  CD2 TYR C 349    -136.431 -20.536  -2.867  1.00 23.65           C  
ATOM   7321  CE1 TYR C 349    -137.614 -20.443  -0.363  1.00 32.56           C  
ATOM   7322  CE2 TYR C 349    -136.221 -21.590  -1.956  1.00 25.25           C  
ATOM   7323  CZ  TYR C 349    -136.799 -21.540  -0.696  1.00 28.80           C  
ATOM   7324  OH  TYR C 349    -136.579 -22.574   0.217  1.00 22.62           O  
ATOM   7325  N   GLN C 350    -135.710 -16.221  -5.661  1.00 24.11           N  
ATOM   7326  CA  GLN C 350    -135.918 -15.488  -6.909  1.00 26.49           C  
ATOM   7327  C   GLN C 350    -137.265 -15.812  -7.510  1.00 26.21           C  
ATOM   7328  O   GLN C 350    -138.058 -16.520  -6.924  1.00 26.00           O  
ATOM   7329  CB  GLN C 350    -134.847 -15.876  -7.938  1.00 29.47           C  
ATOM   7330  CG  GLN C 350    -134.349 -14.749  -8.748  1.00 31.47           C  
ATOM   7331  CD  GLN C 350    -133.773 -13.679  -7.862  1.00 45.54           C  
ATOM   7332  OE1 GLN C 350    -132.804 -13.928  -7.136  1.00 43.99           O  
ATOM   7333  NE2 GLN C 350    -134.383 -12.482  -7.881  1.00 48.87           N  
ATOM   7334  N   GLY C 351    -137.531 -15.251  -8.678  1.00 27.93           N  
ATOM   7335  CA  GLY C 351    -138.706 -15.590  -9.466  1.00 28.30           C  
ATOM   7336  C   GLY C 351    -140.037 -15.498  -8.760  1.00 25.96           C  
ATOM   7337  O   GLY C 351    -141.054 -15.220  -9.387  1.00 28.24           O  
ATOM   7338  N   GLY C 352    -140.063 -15.779  -7.470  1.00 22.56           N  
ATOM   7339  CA  GLY C 352    -141.302 -15.665  -6.744  1.00 30.14           C  
ATOM   7340  C   GLY C 352    -141.765 -16.996  -6.255  1.00 30.67           C  
ATOM   7341  O   GLY C 352    -141.793 -17.236  -5.041  1.00 29.18           O  
ATOM   7342  N   THR C 353    -142.110 -17.888  -7.178  1.00 33.81           N  
ATOM   7343  CA  THR C 353    -142.678 -19.189  -6.741  1.00 35.81           C  
ATOM   7344  C   THR C 353    -141.637 -20.250  -6.396  1.00 26.84           C  
ATOM   7345  O   THR C 353    -140.546 -20.287  -6.992  1.00 21.57           O  
ATOM   7346  CB  THR C 353    -143.693 -19.768  -7.735  1.00 34.62           C  
ATOM   7347  OG1 THR C 353    -144.657 -18.752  -8.056  1.00 38.04           O  
ATOM   7348  CG2 THR C 353    -144.422 -20.962  -7.106  1.00 32.09           C  
ATOM   7349  N   TYR C 354    -141.995 -21.074  -5.404  1.00 29.57           N  
ATOM   7350  CA  TYR C 354    -141.159 -22.188  -4.961  1.00 31.85           C  
ATOM   7351  C   TYR C 354    -141.939 -23.410  -4.409  1.00 39.54           C  
ATOM   7352  O   TYR C 354    -143.155 -23.506  -4.607  1.00 40.83           O  
ATOM   7353  CB  TYR C 354    -140.117 -21.678  -3.985  1.00 30.07           C  
ATOM   7354  CG  TYR C 354    -140.564 -21.345  -2.576  1.00 30.43           C  
ATOM   7355  CD1 TYR C 354    -139.919 -21.916  -1.499  1.00 31.83           C  
ATOM   7356  CD2 TYR C 354    -141.568 -20.434  -2.311  1.00 30.89           C  
ATOM   7357  CE1 TYR C 354    -140.240 -21.607  -0.194  1.00 30.97           C  
ATOM   7358  CE2 TYR C 354    -141.930 -20.132  -0.968  1.00 34.35           C  
ATOM   7359  CZ  TYR C 354    -141.235 -20.722   0.084  1.00 33.08           C  
ATOM   7360  OH  TYR C 354    -141.515 -20.463   1.424  1.00 25.77           O  
ATOM   7361  N   SER C 355    -141.239 -24.346  -3.754  1.00 41.06           N  
ATOM   7362  CA  SER C 355    -141.781 -25.696  -3.449  1.00 36.95           C  
ATOM   7363  C   SER C 355    -141.047 -26.458  -2.338  1.00 31.78           C  
ATOM   7364  O   SER C 355    -139.810 -26.432  -2.263  1.00 28.70           O  
ATOM   7365  CB  SER C 355    -141.716 -26.586  -4.703  1.00 37.75           C  
ATOM   7366  OG  SER C 355    -142.083 -27.934  -4.401  1.00 38.96           O  
ATOM   7367  N   LYS C 356    -141.824 -27.164  -1.519  1.00 25.15           N  
ATOM   7368  CA  LYS C 356    -141.323 -28.179  -0.583  1.00 28.46           C  
ATOM   7369  C   LYS C 356    -140.172 -29.034  -1.214  1.00 36.50           C  
ATOM   7370  O   LYS C 356    -138.998 -28.986  -0.747  1.00 30.69           O  
ATOM   7371  CB  LYS C 356    -142.519 -29.053  -0.136  1.00 35.98           C  
ATOM   7372  CG  LYS C 356    -142.197 -30.431   0.522  1.00 40.33           C  
ATOM   7373  CD  LYS C 356    -143.358 -31.454   0.445  1.00 41.21           C  
ATOM   7374  CE  LYS C 356    -144.570 -31.040   1.279  1.00 45.81           C  
ATOM   7375  NZ  LYS C 356    -145.430 -30.016   0.586  1.00 47.44           N  
ATOM   7376  N   ALA C 357    -140.521 -29.800  -2.265  1.00 28.00           N  
ATOM   7377  CA  ALA C 357    -139.566 -30.331  -3.280  1.00 22.39           C  
ATOM   7378  C   ALA C 357    -138.216 -29.597  -3.395  1.00 27.64           C  
ATOM   7379  O   ALA C 357    -137.174 -30.223  -3.745  1.00 20.86           O  
ATOM   7380  CB  ALA C 357    -140.232 -30.295  -4.651  1.00 20.48           C  
ATOM   7381  N   SER C 358    -138.273 -28.268  -3.135  1.00 30.65           N  
ATOM   7382  CA  SER C 358    -137.191 -27.304  -3.401  1.00 22.62           C  
ATOM   7383  C   SER C 358    -136.514 -26.792  -2.189  1.00 15.18           C  
ATOM   7384  O   SER C 358    -135.312 -26.551  -2.238  1.00 11.50           O  
ATOM   7385  CB  SER C 358    -137.697 -26.112  -4.202  1.00 21.90           C  
ATOM   7386  OG  SER C 358    -137.210 -26.198  -5.546  1.00 22.83           O  
ATOM   7387  N   THR C 359    -137.267 -26.606  -1.110  1.00 23.17           N  
ATOM   7388  CA  THR C 359    -136.630 -26.257   0.167  1.00 31.02           C  
ATOM   7389  C   THR C 359    -135.845 -27.479   0.544  1.00 34.21           C  
ATOM   7390  O   THR C 359    -136.048 -28.545  -0.044  1.00 32.18           O  
ATOM   7391  CB  THR C 359    -137.597 -25.856   1.359  1.00 31.54           C  
ATOM   7392  OG1 THR C 359    -137.577 -26.864   2.385  1.00 33.86           O  
ATOM   7393  CG2 THR C 359    -139.062 -25.505   0.903  1.00 27.39           C  
ATOM   7394  N   PRO C 360    -134.963 -27.345   1.538  1.00 37.33           N  
ATOM   7395  CA  PRO C 360    -134.014 -28.447   1.734  1.00 41.61           C  
ATOM   7396  C   PRO C 360    -134.699 -29.659   2.357  1.00 39.43           C  
ATOM   7397  O   PRO C 360    -134.492 -30.782   1.920  1.00 34.93           O  
ATOM   7398  CB  PRO C 360    -132.956 -27.842   2.686  1.00 44.14           C  
ATOM   7399  CG  PRO C 360    -133.518 -26.489   3.164  1.00 37.08           C  
ATOM   7400  CD  PRO C 360    -134.921 -26.365   2.641  1.00 30.37           C  
ATOM   7401  N   ASN C 361    -135.517 -29.371   3.367  1.00 36.45           N  
ATOM   7402  CA  ASN C 361    -136.378 -30.307   4.083  1.00 35.64           C  
ATOM   7403  C   ASN C 361    -137.845 -29.978   3.796  1.00 24.37           C  
ATOM   7404  O   ASN C 361    -138.718 -30.079   4.666  1.00 20.33           O  
ATOM   7405  CB  ASN C 361    -136.101 -30.205   5.605  1.00 47.99           C  
ATOM   7406  CG  ASN C 361    -135.934 -28.721   6.128  1.00 56.85           C  
ATOM   7407  OD1 ASN C 361    -136.269 -27.719   5.447  1.00 53.74           O  
ATOM   7408  ND2 ASN C 361    -135.406 -28.607   7.349  1.00 42.28           N  
ATOM   7409  N   GLY C 362    -138.091 -29.544   2.563  1.00 32.08           N  
ATOM   7410  CA  GLY C 362    -139.426 -29.206   2.081  1.00 32.66           C  
ATOM   7411  C   GLY C 362    -140.416 -28.685   3.098  1.00 34.43           C  
ATOM   7412  O   GLY C 362    -141.545 -29.161   3.182  1.00 37.09           O  
ATOM   7413  N   TYR C 363    -139.961 -27.700   3.866  1.00 38.47           N  
ATOM   7414  CA  TYR C 363    -140.756 -26.905   4.814  1.00 34.12           C  
ATOM   7415  C   TYR C 363    -140.591 -25.532   4.191  1.00 26.05           C  
ATOM   7416  O   TYR C 363    -139.506 -25.223   3.684  1.00 28.62           O  
ATOM   7417  CB  TYR C 363    -140.024 -26.939   6.140  1.00 39.64           C  
ATOM   7418  CG  TYR C 363    -140.735 -26.884   7.498  1.00 47.23           C  
ATOM   7419  CD1 TYR C 363    -141.010 -28.077   8.217  1.00 45.18           C  
ATOM   7420  CD2 TYR C 363    -140.935 -25.639   8.174  1.00 52.24           C  
ATOM   7421  CE1 TYR C 363    -141.570 -28.032   9.537  1.00 51.84           C  
ATOM   7422  CE2 TYR C 363    -141.494 -25.577   9.510  1.00 44.70           C  
ATOM   7423  CZ  TYR C 363    -141.813 -26.781  10.179  1.00 46.93           C  
ATOM   7424  OH  TYR C 363    -142.367 -26.758  11.458  1.00 35.10           O  
ATOM   7425  N   ASP C 364    -141.656 -24.738   4.180  1.00 29.04           N  
ATOM   7426  CA  ASP C 364    -141.655 -23.358   3.624  1.00 29.91           C  
ATOM   7427  C   ASP C 364    -140.733 -22.409   4.394  1.00 27.08           C  
ATOM   7428  O   ASP C 364    -140.832 -22.307   5.627  1.00 28.56           O  
ATOM   7429  CB  ASP C 364    -143.064 -22.755   3.693  1.00 27.34           C  
ATOM   7430  CG  ASP C 364    -143.509 -22.406   5.144  1.00 23.32           C  
ATOM   7431  OD1 ASP C 364    -142.783 -22.585   6.144  1.00 26.30           O  
ATOM   7432  OD2 ASP C 364    -144.624 -21.949   5.329  1.00 20.90           O  
ATOM   7433  N   ASN C 365    -139.849 -21.703   3.703  1.00 22.14           N  
ATOM   7434  CA  ASN C 365    -138.897 -20.879   4.424  1.00 18.63           C  
ATOM   7435  C   ASN C 365    -138.713 -19.550   3.738  1.00 28.02           C  
ATOM   7436  O   ASN C 365    -137.907 -18.717   4.192  1.00 30.54           O  
ATOM   7437  CB  ASN C 365    -137.572 -21.639   4.660  1.00 10.77           C  
ATOM   7438  CG  ASN C 365    -136.880 -22.037   3.379  1.00  5.91           C  
ATOM   7439  OD1 ASN C 365    -135.660 -22.306   3.368  1.00  5.02           O  
ATOM   7440  ND2 ASN C 365    -137.630 -22.071   2.284  1.00 10.26           N  
ATOM   7441  N   GLY C 366    -139.501 -19.326   2.678  1.00 30.49           N  
ATOM   7442  CA  GLY C 366    -139.420 -18.075   1.914  1.00 31.05           C  
ATOM   7443  C   GLY C 366    -139.821 -16.780   2.637  1.00 23.01           C  
ATOM   7444  O   GLY C 366    -140.148 -16.733   3.849  1.00 14.01           O  
ATOM   7445  N   ILE C 367    -139.749 -15.693   1.883  1.00 27.14           N  
ATOM   7446  CA  ILE C 367    -140.237 -14.423   2.398  1.00 26.64           C  
ATOM   7447  C   ILE C 367    -141.715 -14.543   2.142  1.00 30.86           C  
ATOM   7448  O   ILE C 367    -142.112 -14.627   0.979  1.00 32.81           O  
ATOM   7449  CB  ILE C 367    -139.623 -13.163   1.708  1.00 13.32           C  
ATOM   7450  CG1 ILE C 367    -138.127 -13.149   1.946  1.00 12.03           C  
ATOM   7451  CG2 ILE C 367    -140.206 -11.949   2.344  1.00 14.41           C  
ATOM   7452  CD1 ILE C 367    -137.390 -12.824   0.783  1.00 13.88           C  
ATOM   7453  N   ILE C 368    -142.515 -14.643   3.197  1.00 23.08           N  
ATOM   7454  CA  ILE C 368    -143.932 -14.734   2.969  1.00 25.93           C  
ATOM   7455  C   ILE C 368    -144.735 -14.013   4.024  1.00 27.87           C  
ATOM   7456  O   ILE C 368    -144.296 -13.838   5.170  1.00 24.98           O  
ATOM   7457  CB  ILE C 368    -144.494 -16.229   2.817  1.00 24.59           C  
ATOM   7458  CG1 ILE C 368    -143.807 -17.239   3.771  1.00 23.07           C  
ATOM   7459  CG2 ILE C 368    -144.432 -16.667   1.387  1.00 23.85           C  
ATOM   7460  CD1 ILE C 368    -144.739 -18.372   4.218  1.00 19.69           C  
ATOM   7461  N   TRP C 369    -145.944 -13.674   3.578  1.00 27.53           N  
ATOM   7462  CA  TRP C 369    -146.970 -12.980   4.311  1.00 25.86           C  
ATOM   7463  C   TRP C 369    -148.305 -13.701   3.964  1.00 29.19           C  
ATOM   7464  O   TRP C 369    -149.010 -13.339   2.995  1.00 24.32           O  
ATOM   7465  CB  TRP C 369    -146.967 -11.491   3.891  1.00 26.71           C  
ATOM   7466  CG  TRP C 369    -147.606 -10.619   4.879  1.00 20.10           C  
ATOM   7467  CD1 TRP C 369    -148.828 -10.076   4.797  1.00 25.01           C  
ATOM   7468  CD2 TRP C 369    -147.089 -10.263   6.144  1.00 17.84           C  
ATOM   7469  NE1 TRP C 369    -149.125  -9.390   5.937  1.00 22.31           N  
ATOM   7470  CE2 TRP C 369    -148.056  -9.489   6.783  1.00 20.89           C  
ATOM   7471  CE3 TRP C 369    -145.891 -10.516   6.801  1.00 22.92           C  
ATOM   7472  CZ2 TRP C 369    -147.861  -8.944   8.058  1.00 26.09           C  
ATOM   7473  CZ3 TRP C 369    -145.694  -9.979   8.063  1.00 25.69           C  
ATOM   7474  CH2 TRP C 369    -146.676  -9.192   8.675  1.00 27.34           C  
ATOM   7475  N   ALA C 370    -148.615 -14.722   4.782  1.00 32.24           N  
ATOM   7476  CA  ALA C 370    -149.683 -15.740   4.552  1.00 30.72           C  
ATOM   7477  C   ALA C 370    -151.108 -15.213   4.246  1.00 29.01           C  
ATOM   7478  O   ALA C 370    -151.925 -15.904   3.624  1.00 25.10           O  
ATOM   7479  CB  ALA C 370    -149.730 -16.698   5.761  1.00 25.98           C  
ATOM   7480  N   THR C 371    -151.381 -13.984   4.678  1.00 29.67           N  
ATOM   7481  CA  THR C 371    -152.697 -13.369   4.557  1.00 26.63           C  
ATOM   7482  C   THR C 371    -152.782 -12.510   3.277  1.00 29.09           C  
ATOM   7483  O   THR C 371    -153.685 -11.675   3.145  1.00 32.19           O  
ATOM   7484  CB  THR C 371    -152.924 -12.441   5.756  1.00 19.73           C  
ATOM   7485  OG1 THR C 371    -151.882 -11.456   5.729  1.00 23.57           O  
ATOM   7486  CG2 THR C 371    -152.898 -13.221   7.111  1.00  9.06           C  
ATOM   7487  N   TRP C 372    -151.842 -12.688   2.354  1.00 27.33           N  
ATOM   7488  CA  TRP C 372    -151.834 -11.925   1.096  1.00 26.75           C  
ATOM   7489  C   TRP C 372    -151.466 -12.821  -0.083  1.00 21.10           C  
ATOM   7490  O   TRP C 372    -152.030 -12.702  -1.156  1.00 16.45           O  
ATOM   7491  CB  TRP C 372    -150.841 -10.715   1.156  1.00 25.07           C  
ATOM   7492  CG  TRP C 372    -150.948  -9.826  -0.071  1.00 23.42           C  
ATOM   7493  CD1 TRP C 372    -152.088  -9.248  -0.527  1.00 25.46           C  
ATOM   7494  CD2 TRP C 372    -149.915  -9.479  -1.015  1.00  8.18           C  
ATOM   7495  NE1 TRP C 372    -151.832  -8.561  -1.690  1.00 24.12           N  
ATOM   7496  CE2 TRP C 372    -150.510  -8.689  -2.006  1.00  7.38           C  
ATOM   7497  CE3 TRP C 372    -148.554  -9.757  -1.112  1.00 15.66           C  
ATOM   7498  CZ2 TRP C 372    -149.811  -8.174  -3.080  1.00 12.65           C  
ATOM   7499  CZ3 TRP C 372    -147.833  -9.230  -2.205  1.00 16.94           C  
ATOM   7500  CH2 TRP C 372    -148.478  -8.447  -3.170  1.00 17.68           C  
ATOM   7501  N   LYS C 373    -150.462 -13.660   0.110  1.00 22.59           N  
ATOM   7502  CA  LYS C 373    -150.102 -14.663  -0.872  1.00 25.72           C  
ATOM   7503  C   LYS C 373    -149.876 -16.011  -0.179  1.00 31.84           C  
ATOM   7504  O   LYS C 373    -149.760 -16.094   1.070  1.00 29.04           O  
ATOM   7505  CB  LYS C 373    -148.833 -14.255  -1.604  1.00 21.87           C  
ATOM   7506  CG  LYS C 373    -148.888 -12.917  -2.291  1.00 20.12           C  
ATOM   7507  CD  LYS C 373    -149.949 -12.843  -3.411  1.00 19.89           C  
ATOM   7508  CE  LYS C 373    -149.601 -11.795  -4.520  1.00 19.67           C  
ATOM   7509  NZ  LYS C 373    -148.184 -11.894  -5.017  1.00 15.71           N  
ATOM   7510  N   THR C 374    -149.800 -17.062  -0.995  1.00 33.23           N  
ATOM   7511  CA  THR C 374    -149.540 -18.404  -0.460  1.00 36.55           C  
ATOM   7512  C   THR C 374    -148.120 -18.709   0.067  1.00 38.79           C  
ATOM   7513  O   THR C 374    -147.125 -18.002  -0.223  1.00 38.51           O  
ATOM   7514  CB  THR C 374    -149.768 -19.477  -1.486  1.00 38.19           C  
ATOM   7515  OG1 THR C 374    -149.719 -20.725  -0.804  1.00 40.90           O  
ATOM   7516  CG2 THR C 374    -148.662 -19.472  -2.530  1.00 43.32           C  
ATOM   7517  N   ARG C 375    -148.052 -19.823   0.797  1.00 28.64           N  
ATOM   7518  CA  ARG C 375    -146.842 -20.279   1.500  1.00 27.36           C  
ATOM   7519  C   ARG C 375    -145.636 -20.574   0.578  1.00 15.13           C  
ATOM   7520  O   ARG C 375    -144.480 -20.542   0.983  1.00  9.04           O  
ATOM   7521  CB  ARG C 375    -147.271 -21.519   2.253  1.00 35.71           C  
ATOM   7522  CG  ARG C 375    -146.247 -22.152   3.137  1.00 43.42           C  
ATOM   7523  CD  ARG C 375    -146.757 -23.496   3.796  1.00 44.00           C  
ATOM   7524  NE  ARG C 375    -148.217 -23.545   3.936  1.00 43.32           N  
ATOM   7525  CZ  ARG C 375    -148.935 -24.643   4.163  1.00 57.67           C  
ATOM   7526  NH1 ARG C 375    -148.358 -25.829   4.310  1.00 60.44           N  
ATOM   7527  NH2 ARG C 375    -150.259 -24.553   4.236  1.00 57.44           N  
ATOM   7528  N   TRP C 376    -145.931 -20.875  -0.679  1.00 27.23           N  
ATOM   7529  CA  TRP C 376    -144.912 -21.223  -1.673  1.00 33.15           C  
ATOM   7530  C   TRP C 376    -144.869 -20.116  -2.696  1.00 37.41           C  
ATOM   7531  O   TRP C 376    -144.651 -20.359  -3.907  1.00 34.72           O  
ATOM   7532  CB  TRP C 376    -145.201 -22.597  -2.328  1.00 30.45           C  
ATOM   7533  CG  TRP C 376    -145.038 -23.668  -1.331  1.00 31.29           C  
ATOM   7534  CD1 TRP C 376    -143.850 -24.248  -0.884  1.00 34.02           C  
ATOM   7535  CD2 TRP C 376    -146.058 -24.210  -0.549  1.00 17.26           C  
ATOM   7536  NE1 TRP C 376    -144.117 -25.149   0.125  1.00 27.30           N  
ATOM   7537  CE2 TRP C 376    -145.468 -25.135   0.344  1.00 18.20           C  
ATOM   7538  CE3 TRP C 376    -147.423 -24.007  -0.504  1.00 32.45           C  
ATOM   7539  CZ2 TRP C 376    -146.217 -25.872   1.240  1.00 38.62           C  
ATOM   7540  CZ3 TRP C 376    -148.187 -24.748   0.402  1.00 43.02           C  
ATOM   7541  CH2 TRP C 376    -147.581 -25.673   1.256  1.00 42.49           C  
ATOM   7542  N   TYR C 377    -145.109 -18.899  -2.203  1.00 32.21           N  
ATOM   7543  CA  TYR C 377    -144.787 -17.704  -2.953  1.00 32.89           C  
ATOM   7544  C   TYR C 377    -143.990 -16.737  -2.065  1.00 29.70           C  
ATOM   7545  O   TYR C 377    -144.430 -16.412  -0.973  1.00 30.28           O  
ATOM   7546  CB  TYR C 377    -146.064 -17.080  -3.449  1.00 33.51           C  
ATOM   7547  CG  TYR C 377    -145.852 -15.930  -4.389  1.00 42.73           C  
ATOM   7548  CD1 TYR C 377    -145.863 -16.139  -5.762  1.00 41.13           C  
ATOM   7549  CD2 TYR C 377    -145.661 -14.620  -3.904  1.00 43.48           C  
ATOM   7550  CE1 TYR C 377    -145.690 -15.090  -6.642  1.00 44.46           C  
ATOM   7551  CE2 TYR C 377    -145.491 -13.568  -4.773  1.00 42.24           C  
ATOM   7552  CZ  TYR C 377    -145.500 -13.808  -6.150  1.00 45.19           C  
ATOM   7553  OH  TYR C 377    -145.314 -12.787  -7.056  1.00 39.99           O  
ATOM   7554  N   SER C 378    -142.821 -16.307  -2.544  1.00 25.37           N  
ATOM   7555  CA  SER C 378    -141.876 -15.510  -1.770  1.00 20.79           C  
ATOM   7556  C   SER C 378    -141.688 -14.102  -2.394  1.00 27.33           C  
ATOM   7557  O   SER C 378    -141.506 -13.906  -3.622  1.00 14.40           O  
ATOM   7558  CB  SER C 378    -140.543 -16.245  -1.660  1.00 21.46           C  
ATOM   7559  OG  SER C 378    -139.566 -15.548  -0.915  1.00 19.57           O  
ATOM   7560  N   MET C 379    -141.683 -13.126  -1.493  1.00 32.00           N  
ATOM   7561  CA  MET C 379    -141.799 -11.733  -1.838  1.00 32.78           C  
ATOM   7562  C   MET C 379    -140.572 -11.202  -2.564  1.00 28.40           C  
ATOM   7563  O   MET C 379    -139.457 -11.594  -2.270  1.00 28.45           O  
ATOM   7564  CB  MET C 379    -142.032 -10.948  -0.561  1.00 37.21           C  
ATOM   7565  CG  MET C 379    -143.244 -11.406   0.255  1.00 43.71           C  
ATOM   7566  SD  MET C 379    -144.744 -11.663  -0.727  1.00 50.91           S  
ATOM   7567  CE  MET C 379    -144.978 -10.038  -1.449  1.00 42.81           C  
ATOM   7568  N   LYS C 380    -140.803 -10.288  -3.503  1.00 32.51           N  
ATOM   7569  CA  LYS C 380    -139.746  -9.760  -4.365  1.00 32.78           C  
ATOM   7570  C   LYS C 380    -139.063  -8.604  -3.715  1.00 33.70           C  
ATOM   7571  O   LYS C 380    -137.855  -8.391  -3.880  1.00 31.67           O  
ATOM   7572  CB  LYS C 380    -140.317  -9.211  -5.653  1.00 31.22           C  
ATOM   7573  CG  LYS C 380    -139.238  -8.800  -6.599  1.00 24.76           C  
ATOM   7574  CD  LYS C 380    -139.845  -8.092  -7.743  1.00 26.43           C  
ATOM   7575  CE  LYS C 380    -138.777  -7.401  -8.546  1.00 26.38           C  
ATOM   7576  NZ  LYS C 380    -139.425  -6.275  -9.265  1.00 32.16           N  
ATOM   7577  N   LYS C 381    -139.872  -7.802  -3.047  1.00 28.72           N  
ATOM   7578  CA  LYS C 381    -139.345  -6.728  -2.255  1.00 33.71           C  
ATOM   7579  C   LYS C 381    -140.129  -6.736  -1.002  1.00 33.96           C  
ATOM   7580  O   LYS C 381    -141.323  -7.016  -1.035  1.00 34.88           O  
ATOM   7581  CB  LYS C 381    -139.560  -5.401  -2.956  1.00 39.41           C  
ATOM   7582  CG  LYS C 381    -138.585  -5.128  -4.071  1.00 43.30           C  
ATOM   7583  CD  LYS C 381    -139.030  -3.946  -4.902  1.00 48.38           C  
ATOM   7584  CE  LYS C 381    -138.260  -3.854  -6.223  1.00 52.62           C  
ATOM   7585  NZ  LYS C 381    -136.763  -3.971  -6.063  1.00 53.09           N  
ATOM   7586  N   THR C 382    -139.489  -6.438   0.114  1.00 34.42           N  
ATOM   7587  CA  THR C 382    -140.257  -6.170   1.325  1.00 34.15           C  
ATOM   7588  C   THR C 382    -139.655  -4.959   1.986  1.00 30.42           C  
ATOM   7589  O   THR C 382    -138.534  -4.567   1.640  1.00 27.35           O  
ATOM   7590  CB  THR C 382    -140.290  -7.389   2.308  1.00 29.17           C  
ATOM   7591  OG1 THR C 382    -139.137  -7.380   3.164  1.00 31.41           O  
ATOM   7592  CG2 THR C 382    -140.309  -8.623   1.540  1.00 27.93           C  
ATOM   7593  N   THR C 383    -140.386  -4.387   2.938  1.00 21.55           N  
ATOM   7594  CA  THR C 383    -139.776  -3.431   3.826  1.00 26.45           C  
ATOM   7595  C   THR C 383    -140.509  -3.333   5.154  1.00 20.74           C  
ATOM   7596  O   THR C 383    -141.732  -3.406   5.210  1.00 15.72           O  
ATOM   7597  CB  THR C 383    -139.671  -2.071   3.110  1.00 33.14           C  
ATOM   7598  OG1 THR C 383    -139.897  -0.995   4.036  1.00 36.28           O  
ATOM   7599  CG2 THR C 383    -140.663  -2.024   1.938  1.00 32.04           C  
ATOM   7600  N   MET C 384    -139.762  -3.210   6.237  1.00 19.36           N  
ATOM   7601  CA  MET C 384    -140.390  -3.026   7.543  1.00 23.05           C  
ATOM   7602  C   MET C 384    -139.896  -1.748   8.042  1.00 28.26           C  
ATOM   7603  O   MET C 384    -138.656  -1.536   8.097  1.00 26.46           O  
ATOM   7604  CB  MET C 384    -139.985  -4.079   8.568  1.00 23.60           C  
ATOM   7605  CG  MET C 384    -140.747  -5.365   8.413  1.00 30.56           C  
ATOM   7606  SD  MET C 384    -139.947  -6.738   9.213  1.00 29.39           S  
ATOM   7607  CE  MET C 384    -140.709  -6.852  10.819  1.00 22.25           C  
ATOM   7608  N   LYS C 385    -140.838  -0.903   8.441  1.00 25.30           N  
ATOM   7609  CA  LYS C 385    -140.479   0.430   8.858  1.00 25.84           C  
ATOM   7610  C   LYS C 385    -141.370   0.891   9.933  1.00 25.61           C  
ATOM   7611  O   LYS C 385    -142.466   0.374  10.065  1.00 26.25           O  
ATOM   7612  CB  LYS C 385    -140.543   1.395   7.678  1.00 25.99           C  
ATOM   7613  CG  LYS C 385    -141.867   1.454   6.929  1.00 24.04           C  
ATOM   7614  CD  LYS C 385    -141.662   2.392   5.756  1.00 22.24           C  
ATOM   7615  CE  LYS C 385    -142.899   2.902   5.115  1.00 20.66           C  
ATOM   7616  NZ  LYS C 385    -142.488   3.408   3.796  1.00 21.22           N  
ATOM   7617  N   ILE C 386    -140.917   1.876  10.696  1.00 27.61           N  
ATOM   7618  CA  ILE C 386    -141.735   2.429  11.775  1.00 32.51           C  
ATOM   7619  C   ILE C 386    -141.571   3.942  11.917  1.00 36.23           C  
ATOM   7620  O   ILE C 386    -140.652   4.532  11.348  1.00 38.67           O  
ATOM   7621  CB  ILE C 386    -141.475   1.705  13.121  1.00 32.99           C  
ATOM   7622  CG1 ILE C 386    -140.115   2.052  13.707  1.00 32.97           C  
ATOM   7623  CG2 ILE C 386    -141.530   0.179  12.952  1.00 33.49           C  
ATOM   7624  CD1 ILE C 386    -139.787   1.145  14.908  1.00 31.81           C  
ATOM   7625  N   ILE C 387    -142.460   4.540  12.712  1.00 36.06           N  
ATOM   7626  CA  ILE C 387    -142.867   5.948  12.577  1.00 32.81           C  
ATOM   7627  C   ILE C 387    -143.779   6.260  13.750  1.00 30.74           C  
ATOM   7628  O   ILE C 387    -144.677   5.469  14.048  1.00 28.72           O  
ATOM   7629  CB  ILE C 387    -143.705   6.143  11.285  1.00 33.91           C  
ATOM   7630  CG1 ILE C 387    -144.052   7.621  11.054  1.00 35.36           C  
ATOM   7631  CG2 ILE C 387    -144.986   5.243  11.324  1.00 26.67           C  
ATOM   7632  CD1 ILE C 387    -145.236   7.826  10.089  1.00 30.91           C  
ATOM   7633  N   PRO C 388    -143.604   7.412  14.409  1.00 31.59           N  
ATOM   7634  CA  PRO C 388    -144.410   7.553  15.624  1.00 34.31           C  
ATOM   7635  C   PRO C 388    -145.882   7.328  15.336  1.00 28.68           C  
ATOM   7636  O   PRO C 388    -146.322   7.582  14.210  1.00 30.31           O  
ATOM   7637  CB  PRO C 388    -144.129   8.994  16.062  1.00 34.22           C  
ATOM   7638  CG  PRO C 388    -142.760   9.260  15.534  1.00 32.70           C  
ATOM   7639  CD  PRO C 388    -142.836   8.635  14.146  1.00 33.32           C  
ATOM   7640  N   PHE C 389    -146.612   6.819  16.326  1.00 26.89           N  
ATOM   7641  CA  PHE C 389    -148.020   6.443  16.142  1.00 30.55           C  
ATOM   7642  C   PHE C 389    -148.852   7.660  15.728  1.00 39.05           C  
ATOM   7643  O   PHE C 389    -149.654   7.604  14.787  1.00 46.51           O  
ATOM   7644  CB  PHE C 389    -148.571   5.824  17.444  1.00 25.41           C  
ATOM   7645  CG  PHE C 389    -150.047   5.416  17.382  1.00 21.31           C  
ATOM   7646  CD1 PHE C 389    -150.556   4.712  16.290  1.00 21.26           C  
ATOM   7647  CD2 PHE C 389    -150.909   5.703  18.435  1.00 19.22           C  
ATOM   7648  CE1 PHE C 389    -151.895   4.318  16.234  1.00 16.63           C  
ATOM   7649  CE2 PHE C 389    -152.243   5.317  18.387  1.00 20.58           C  
ATOM   7650  CZ  PHE C 389    -152.731   4.615  17.273  1.00 18.29           C  
ATOM   7651  N   ASN C 390    -148.619   8.764  16.432  1.00 41.52           N  
ATOM   7652  CA  ASN C 390    -149.372   9.975  16.232  1.00 43.66           C  
ATOM   7653  C   ASN C 390    -149.423  10.435  14.806  1.00 45.27           C  
ATOM   7654  O   ASN C 390    -150.320  11.160  14.435  1.00 59.86           O  
ATOM   7655  CB  ASN C 390    -148.770  11.093  17.060  1.00 48.41           C  
ATOM   7656  CG  ASN C 390    -147.305  11.285  16.797  1.00 59.44           C  
ATOM   7657  OD1 ASN C 390    -146.532  11.498  17.727  1.00 66.76           O  
ATOM   7658  ND2 ASN C 390    -146.903  11.214  15.534  1.00 51.01           N  
ATOM   7659  N   ARG C 391    -148.455  10.029  14.005  1.00 49.22           N  
ATOM   7660  CA  ARG C 391    -148.280  10.620  12.687  1.00 55.34           C  
ATOM   7661  C   ARG C 391    -149.174  10.019  11.602  1.00 55.29           C  
ATOM   7662  O   ARG C 391    -149.278  10.570  10.510  1.00 56.91           O  
ATOM   7663  CB  ARG C 391    -146.815  10.518  12.253  1.00 56.69           C  
ATOM   7664  CG  ARG C 391    -146.417  11.611  11.292  1.00 52.27           C  
ATOM   7665  CD  ARG C 391    -146.282  12.902  12.011  1.00 48.05           C  
ATOM   7666  NE  ARG C 391    -146.053  13.999  11.085  1.00 53.34           N  
ATOM   7667  CZ  ARG C 391    -145.417  15.133  11.402  1.00 73.61           C  
ATOM   7668  NH1 ARG C 391    -144.922  15.321  12.632  1.00 66.45           N  
ATOM   7669  NH2 ARG C 391    -145.254  16.091  10.483  1.00 74.95           N  
ATOM   7670  N   LEU C 392    -149.792   8.884  11.890  1.00 53.51           N  
ATOM   7671  CA  LEU C 392    -150.787   8.309  10.993  1.00 58.90           C  
ATOM   7672  C   LEU C 392    -152.199   8.880  11.358  1.00 66.63           C  
ATOM   7673  O   LEU C 392    -153.094   9.012  10.500  1.00 68.82           O  
ATOM   7674  CB  LEU C 392    -150.706   6.766  11.079  1.00 59.86           C  
ATOM   7675  CG  LEU C 392    -150.406   5.940   9.805  1.00 63.34           C  
ATOM   7676  CD1 LEU C 392    -151.704   5.482   9.088  1.00 61.16           C  
ATOM   7677  CD2 LEU C 392    -149.462   6.664   8.812  1.00 60.21           C  
ATOM   7678  N   THR C 393    -152.350   9.277  12.628  1.00 71.20           N  
ATOM   7679  CA  THR C 393    -153.631   9.715  13.220  1.00 75.51           C  
ATOM   7680  C   THR C 393    -153.858  11.247  13.291  1.00 75.58           C  
ATOM   7681  O   THR C 393    -154.797  11.689  13.964  1.00 69.84           O  
ATOM   7682  CB  THR C 393    -153.820   9.101  14.674  1.00 74.88           C  
ATOM   7683  OG1 THR C 393    -152.541   8.779  15.262  1.00 69.14           O  
ATOM   7684  CG2 THR C 393    -154.703   7.829  14.630  1.00 71.49           C  
ATOM   7685  N   ILE C 394    -153.005  12.044  12.630  1.00 90.22           N  
ATOM   7686  CA  ILE C 394    -153.248  13.503  12.442  1.00 92.02           C  
ATOM   7687  C   ILE C 394    -153.198  13.850  10.944  1.00 94.61           C  
ATOM   7688  O   ILE C 394    -154.141  13.581  10.192  1.00 89.29           O  
ATOM   7689  CB  ILE C 394    -152.230  14.466  13.219  1.00 92.78           C  
ATOM   7690  CG1 ILE C 394    -151.870  13.965  14.638  1.00 90.08           C  
ATOM   7691  CG2 ILE C 394    -152.778  15.916  13.279  1.00 95.25           C  
ATOM   7692  CD1 ILE C 394    -153.048  13.737  15.597  1.00 86.09           C  
TER    7693      ILE C 394                                                      
ATOM   7694  N   ALA D  27      50.713  -5.011 -53.595  1.00161.80           N  
ATOM   7695  CA  ALA D  27      51.889  -4.147 -53.896  1.00162.90           C  
ATOM   7696  C   ALA D  27      51.680  -3.331 -55.174  1.00163.26           C  
ATOM   7697  O   ALA D  27      50.946  -3.741 -56.076  1.00165.56           O  
ATOM   7698  CB  ALA D  27      53.149  -5.000 -54.015  1.00162.81           C  
ATOM   7699  N   CYS D  28      52.338  -2.175 -55.235  1.00164.29           N  
ATOM   7700  CA  CYS D  28      52.376  -1.340 -56.440  1.00163.56           C  
ATOM   7701  C   CYS D  28      53.447  -1.838 -57.420  1.00161.84           C  
ATOM   7702  O   CYS D  28      53.574  -1.315 -58.532  1.00159.61           O  
ATOM   7703  CB  CYS D  28      52.663   0.117 -56.060  1.00165.45           C  
ATOM   7704  SG  CYS D  28      54.418   0.481 -55.733  1.00167.29           S  
ATOM   7705  N   LYS D  29      54.217  -2.840 -56.986  1.00159.09           N  
ATOM   7706  CA  LYS D  29      55.272  -3.462 -57.789  1.00158.49           C  
ATOM   7707  C   LYS D  29      54.673  -4.162 -59.001  1.00160.12           C  
ATOM   7708  O   LYS D  29      55.226  -4.085 -60.105  1.00160.42           O  
ATOM   7709  CB  LYS D  29      56.044  -4.486 -56.944  1.00157.22           C  
ATOM   7710  CG  LYS D  29      57.391  -4.916 -57.521  1.00156.56           C  
ATOM   7711  CD  LYS D  29      58.470  -3.871 -57.270  1.00155.88           C  
ATOM   7712  CE  LYS D  29      59.751  -4.200 -58.017  1.00155.66           C  
ATOM   7713  NZ  LYS D  29      59.589  -4.042 -59.489  1.00156.66           N  
ATOM   7714  N   ASP D  30      53.556  -4.859 -58.773  1.00160.47           N  
ATOM   7715  CA  ASP D  30      52.778  -5.487 -59.843  1.00159.93           C  
ATOM   7716  C   ASP D  30      52.562  -4.449 -60.945  1.00158.39           C  
ATOM   7717  O   ASP D  30      51.586  -3.692 -60.927  1.00156.50           O  
ATOM   7718  CB  ASP D  30      51.436  -6.019 -59.298  1.00160.81           C  
ATOM   7719  CG  ASP D  30      50.802  -7.085 -60.194  1.00160.92           C  
ATOM   7720  OD1 ASP D  30      49.899  -7.801 -59.709  1.00163.42           O  
ATOM   7721  OD2 ASP D  30      51.195  -7.217 -61.373  1.00162.62           O  
ATOM   7722  N   SER D  31      53.503  -4.406 -61.886  1.00158.32           N  
ATOM   7723  CA  SER D  31      53.517  -3.372 -62.911  1.00157.42           C  
ATOM   7724  C   SER D  31      52.288  -3.484 -63.806  1.00155.67           C  
ATOM   7725  O   SER D  31      52.351  -4.018 -64.915  1.00154.63           O  
ATOM   7726  CB  SER D  31      54.806  -3.436 -63.735  1.00157.89           C  
ATOM   7727  OG  SER D  31      55.928  -3.079 -62.945  1.00159.30           O  
ATOM   7728  N   ASP D  32      51.168  -2.976 -63.294  1.00152.73           N  
ATOM   7729  CA  ASP D  32      49.930  -2.850 -64.062  1.00149.80           C  
ATOM   7730  C   ASP D  32      49.993  -1.633 -64.978  1.00146.01           C  
ATOM   7731  O   ASP D  32      49.114  -1.437 -65.817  1.00145.36           O  
ATOM   7732  CB  ASP D  32      48.727  -2.675 -63.127  1.00150.31           C  
ATOM   7733  CG  ASP D  32      48.582  -3.806 -62.129  1.00151.17           C  
ATOM   7734  OD1 ASP D  32      48.863  -4.967 -62.491  1.00151.36           O  
ATOM   7735  OD2 ASP D  32      48.174  -3.528 -60.980  1.00150.52           O  
ATOM   7736  N   TRP D  33      51.040  -0.825 -64.817  1.00144.80           N  
ATOM   7737  CA  TRP D  33      51.087   0.511 -65.397  1.00143.01           C  
ATOM   7738  C   TRP D  33      51.516   0.439 -66.874  1.00136.21           C  
ATOM   7739  O   TRP D  33      52.303  -0.435 -67.248  1.00135.99           O  
ATOM   7740  CB  TRP D  33      52.037   1.429 -64.592  1.00146.23           C  
ATOM   7741  CG  TRP D  33      52.121   1.153 -63.080  1.00148.72           C  
ATOM   7742  CD1 TRP D  33      53.041   0.360 -62.445  1.00150.05           C  
ATOM   7743  CD2 TRP D  33      51.273   1.683 -62.042  1.00149.00           C  
ATOM   7744  NE1 TRP D  33      52.814   0.355 -61.088  1.00152.12           N  
ATOM   7745  CE2 TRP D  33      51.738   1.157 -60.813  1.00150.37           C  
ATOM   7746  CE3 TRP D  33      50.165   2.543 -62.032  1.00148.41           C  
ATOM   7747  CZ2 TRP D  33      51.135   1.464 -59.588  1.00149.53           C  
ATOM   7748  CZ3 TRP D  33      49.566   2.845 -60.811  1.00148.41           C  
ATOM   7749  CH2 TRP D  33      50.056   2.306 -59.609  1.00148.78           C  
ATOM   7750  N   PRO D  34      50.982   1.346 -67.721  1.00132.32           N  
ATOM   7751  CA  PRO D  34      51.426   1.490 -69.113  1.00129.04           C  
ATOM   7752  C   PRO D  34      52.899   1.889 -69.234  1.00124.60           C  
ATOM   7753  O   PRO D  34      53.646   1.780 -68.264  1.00120.00           O  
ATOM   7754  CB  PRO D  34      50.531   2.613 -69.652  1.00130.61           C  
ATOM   7755  CG  PRO D  34      49.335   2.595 -68.801  1.00131.73           C  
ATOM   7756  CD  PRO D  34      49.801   2.186 -67.444  1.00132.07           C  
ATOM   7757  N   PHE D  35      53.308   2.349 -70.416  1.00120.80           N  
ATOM   7758  CA  PHE D  35      54.693   2.767 -70.646  1.00117.85           C  
ATOM   7759  C   PHE D  35      54.791   4.264 -70.928  1.00113.49           C  
ATOM   7760  O   PHE D  35      53.983   4.823 -71.670  1.00112.27           O  
ATOM   7761  CB  PHE D  35      55.325   1.941 -71.770  1.00118.66           C  
ATOM   7762  CG  PHE D  35      55.714   0.548 -71.345  1.00118.23           C  
ATOM   7763  CD1 PHE D  35      57.052   0.207 -71.153  1.00116.81           C  
ATOM   7764  CD2 PHE D  35      54.738  -0.417 -71.109  1.00116.53           C  
ATOM   7765  CE1 PHE D  35      57.411  -1.077 -70.750  1.00116.53           C  
ATOM   7766  CE2 PHE D  35      55.088  -1.701 -70.704  1.00116.24           C  
ATOM   7767  CZ  PHE D  35      56.426  -2.032 -70.525  1.00116.37           C  
ATOM   7768  N   CYS D  36      55.787   4.905 -70.321  1.00112.68           N  
ATOM   7769  CA  CYS D  36      55.901   6.360 -70.357  1.00110.76           C  
ATOM   7770  C   CYS D  36      56.404   6.837 -71.708  1.00107.82           C  
ATOM   7771  O   CYS D  36      57.521   6.524 -72.124  1.00106.62           O  
ATOM   7772  CB  CYS D  36      56.828   6.879 -69.247  1.00110.40           C  
ATOM   7773  SG  CYS D  36      56.268   6.578 -67.535  1.00109.29           S  
ATOM   7774  N   SER D  37      55.556   7.593 -72.386  1.00106.19           N  
ATOM   7775  CA  SER D  37      55.940   8.283 -73.597  1.00106.56           C  
ATOM   7776  C   SER D  37      56.857   9.458 -73.264  1.00109.06           C  
ATOM   7777  O   SER D  37      57.075   9.776 -72.096  1.00110.08           O  
ATOM   7778  CB  SER D  37      54.689   8.756 -74.339  1.00104.95           C  
ATOM   7779  OG  SER D  37      53.544   8.721 -73.504  1.00103.89           O  
ATOM   7780  N   ASP D  38      57.401  10.087 -74.300  1.00112.92           N  
ATOM   7781  CA  ASP D  38      58.281  11.249 -74.135  1.00114.49           C  
ATOM   7782  C   ASP D  38      57.534  12.530 -73.711  1.00114.16           C  
ATOM   7783  O   ASP D  38      58.165  13.490 -73.256  1.00113.06           O  
ATOM   7784  CB  ASP D  38      59.114  11.493 -75.411  1.00116.55           C  
ATOM   7785  CG  ASP D  38      58.261  11.819 -76.637  1.00119.10           C  
ATOM   7786  OD1 ASP D  38      57.023  11.954 -76.509  1.00116.81           O  
ATOM   7787  OD2 ASP D  38      58.842  11.950 -77.738  1.00122.69           O  
ATOM   7788  N   GLU D  39      56.207  12.549 -73.868  1.00110.42           N  
ATOM   7789  CA  GLU D  39      55.382  13.646 -73.350  1.00107.36           C  
ATOM   7790  C   GLU D  39      54.828  13.320 -71.967  1.00102.67           C  
ATOM   7791  O   GLU D  39      54.430  14.226 -71.237  1.00102.07           O  
ATOM   7792  CB  GLU D  39      54.237  13.995 -74.309  1.00108.46           C  
ATOM   7793  CG  GLU D  39      53.039  13.036 -74.296  1.00108.83           C  
ATOM   7794  CD  GLU D  39      51.772  13.671 -74.852  1.00108.35           C  
ATOM   7795  OE1 GLU D  39      50.668  13.249 -74.449  1.00108.48           O  
ATOM   7796  OE2 GLU D  39      51.876  14.595 -75.685  1.00105.18           O  
ATOM   7797  N   ASP D  40      54.782  12.031 -71.617  1.00100.36           N  
ATOM   7798  CA  ASP D  40      54.463  11.621 -70.246  1.00 99.99           C  
ATOM   7799  C   ASP D  40      55.416  12.300 -69.268  1.00101.88           C  
ATOM   7800  O   ASP D  40      55.038  12.599 -68.137  1.00100.56           O  
ATOM   7801  CB  ASP D  40      54.520  10.093 -70.072  1.00 99.41           C  
ATOM   7802  CG  ASP D  40      53.212   9.408 -70.442  1.00 99.24           C  
ATOM   7803  OD1 ASP D  40      52.894   8.359 -69.841  1.00 99.05           O  
ATOM   7804  OD2 ASP D  40      52.498   9.914 -71.331  1.00101.81           O  
ATOM   7805  N   TRP D  41      56.645  12.551 -69.716  1.00102.60           N  
ATOM   7806  CA  TRP D  41      57.603  13.351 -68.951  1.00102.82           C  
ATOM   7807  C   TRP D  41      57.189  14.831 -68.948  1.00105.49           C  
ATOM   7808  O   TRP D  41      56.697  15.347 -69.958  1.00106.71           O  
ATOM   7809  CB  TRP D  41      59.020  13.189 -69.517  1.00100.33           C  
ATOM   7810  CG  TRP D  41      60.095  13.332 -68.484  1.00 97.18           C  
ATOM   7811  CD1 TRP D  41      60.661  12.329 -67.747  1.00 97.61           C  
ATOM   7812  CD2 TRP D  41      60.731  14.549 -68.064  1.00 99.86           C  
ATOM   7813  NE1 TRP D  41      61.611  12.845 -66.897  1.00 99.36           N  
ATOM   7814  CE2 TRP D  41      61.676  14.204 -67.072  1.00100.45           C  
ATOM   7815  CE3 TRP D  41      60.595  15.898 -68.431  1.00100.69           C  
ATOM   7816  CZ2 TRP D  41      62.484  15.163 -66.440  1.00 98.59           C  
ATOM   7817  CZ3 TRP D  41      61.399  16.851 -67.804  1.00 99.63           C  
ATOM   7818  CH2 TRP D  41      62.332  16.476 -66.821  1.00 98.45           C  
ATOM   7819  N   ASN D  42      57.428  15.497 -67.814  1.00108.21           N  
ATOM   7820  CA  ASN D  42      56.828  16.796 -67.459  1.00106.67           C  
ATOM   7821  C   ASN D  42      55.600  16.578 -66.569  1.00102.05           C  
ATOM   7822  O   ASN D  42      55.413  17.303 -65.591  1.00101.51           O  
ATOM   7823  CB  ASN D  42      56.430  17.650 -68.684  1.00109.31           C  
ATOM   7824  CG  ASN D  42      57.589  17.892 -69.650  1.00111.61           C  
ATOM   7825  OD1 ASN D  42      58.682  18.287 -69.240  1.00109.37           O  
ATOM   7826  ND2 ASN D  42      57.340  17.681 -70.944  1.00112.12           N  
ATOM   7827  N   TYR D  43      54.790  15.567 -66.908  1.00 98.32           N  
ATOM   7828  CA  TYR D  43      53.484  15.326 -66.279  1.00 96.29           C  
ATOM   7829  C   TYR D  43      53.436  14.116 -65.349  1.00 93.67           C  
ATOM   7830  O   TYR D  43      52.654  14.108 -64.396  1.00 89.18           O  
ATOM   7831  CB  TYR D  43      52.407  15.151 -67.353  1.00 97.36           C  
ATOM   7832  CG  TYR D  43      52.352  16.278 -68.356  1.00 99.69           C  
ATOM   7833  CD1 TYR D  43      52.234  16.017 -69.717  1.00100.60           C  
ATOM   7834  CD2 TYR D  43      52.428  17.608 -67.946  1.00101.14           C  
ATOM   7835  CE1 TYR D  43      52.182  17.049 -70.642  1.00101.43           C  
ATOM   7836  CE2 TYR D  43      52.380  18.645 -68.862  1.00101.77           C  
ATOM   7837  CZ  TYR D  43      52.257  18.361 -70.207  1.00102.64           C  
ATOM   7838  OH  TYR D  43      52.209  19.388 -71.117  1.00104.66           O  
ATOM   7839  N   LYS D  44      54.230  13.089 -65.648  1.00 91.20           N  
ATOM   7840  CA  LYS D  44      54.372  11.917 -64.772  1.00 87.82           C  
ATOM   7841  C   LYS D  44      55.819  11.810 -64.304  1.00 89.73           C  
ATOM   7842  O   LYS D  44      56.683  11.364 -65.056  1.00 90.41           O  
ATOM   7843  CB  LYS D  44      53.963  10.621 -65.495  1.00 86.34           C  
ATOM   7844  CG  LYS D  44      52.509  10.220 -65.321  1.00 83.58           C  
ATOM   7845  CD  LYS D  44      51.578  11.098 -66.129  1.00 81.31           C  
ATOM   7846  CE  LYS D  44      50.200  10.471 -66.234  1.00 80.28           C  
ATOM   7847  NZ  LYS D  44      49.613  10.181 -64.901  1.00 80.70           N  
ATOM   7848  N   CYS D  45      56.079  12.210 -63.062  1.00 91.04           N  
ATOM   7849  CA  CYS D  45      57.449  12.260 -62.532  1.00 90.10           C  
ATOM   7850  C   CYS D  45      57.729  11.095 -61.556  1.00 91.95           C  
ATOM   7851  O   CYS D  45      56.827  10.315 -61.260  1.00 91.29           O  
ATOM   7852  CB  CYS D  45      57.694  13.627 -61.874  1.00 87.68           C  
ATOM   7853  SG  CYS D  45      57.646  15.048 -63.021  1.00 84.19           S  
ATOM   7854  N   PRO D  46      58.988  10.949 -61.087  1.00 93.26           N  
ATOM   7855  CA  PRO D  46      59.363   9.883 -60.124  1.00 92.59           C  
ATOM   7856  C   PRO D  46      59.301  10.254 -58.624  1.00 94.50           C  
ATOM   7857  O   PRO D  46      59.214  11.438 -58.280  1.00 82.86           O  
ATOM   7858  CB  PRO D  46      60.810   9.572 -60.513  1.00 93.30           C  
ATOM   7859  CG  PRO D  46      61.332  10.856 -61.069  1.00 93.91           C  
ATOM   7860  CD  PRO D  46      60.177  11.559 -61.717  1.00 94.04           C  
ATOM   7861  N   SER D  47      59.384   9.243 -57.752  1.00 95.56           N  
ATOM   7862  CA  SER D  47      59.263   9.446 -56.294  1.00 97.60           C  
ATOM   7863  C   SER D  47      60.483  10.149 -55.704  1.00 97.52           C  
ATOM   7864  O   SER D  47      61.613   9.907 -56.126  1.00 98.94           O  
ATOM   7865  CB  SER D  47      59.059   8.117 -55.548  1.00 97.70           C  
ATOM   7866  OG  SER D  47      60.179   7.800 -54.724  1.00 96.88           O  
ATOM   7867  N   GLY D  48      60.246  10.991 -54.703  1.00 98.42           N  
ATOM   7868  CA  GLY D  48      61.317  11.734 -54.046  1.00 98.06           C  
ATOM   7869  C   GLY D  48      62.294  10.845 -53.304  1.00 97.31           C  
ATOM   7870  O   GLY D  48      63.457  11.204 -53.142  1.00 96.62           O  
ATOM   7871  N   CYS D  49      61.823   9.681 -52.861  1.00 98.20           N  
ATOM   7872  CA  CYS D  49      62.656   8.738 -52.133  1.00100.63           C  
ATOM   7873  C   CYS D  49      63.658   8.120 -53.081  1.00103.48           C  
ATOM   7874  O   CYS D  49      64.867   8.151 -52.849  1.00107.49           O  
ATOM   7875  CB  CYS D  49      61.806   7.622 -51.530  1.00 99.38           C  
ATOM   7876  SG  CYS D  49      60.541   8.182 -50.405  1.00 99.09           S  
ATOM   7877  N   ARG D  50      63.133   7.559 -54.161  1.00102.87           N  
ATOM   7878  CA  ARG D  50      63.950   6.875 -55.148  1.00105.94           C  
ATOM   7879  C   ARG D  50      64.746   7.862 -55.994  1.00103.82           C  
ATOM   7880  O   ARG D  50      65.731   7.482 -56.622  1.00106.38           O  
ATOM   7881  CB  ARG D  50      63.067   6.012 -56.038  1.00109.81           C  
ATOM   7882  CG  ARG D  50      63.773   4.841 -56.689  1.00113.25           C  
ATOM   7883  CD  ARG D  50      62.812   4.097 -57.604  1.00116.06           C  
ATOM   7884  NE  ARG D  50      61.598   3.618 -56.921  1.00119.38           N  
ATOM   7885  CZ  ARG D  50      60.395   4.209 -56.948  1.00122.76           C  
ATOM   7886  NH1 ARG D  50      60.185   5.338 -57.623  1.00122.64           N  
ATOM   7887  NH2 ARG D  50      59.381   3.664 -56.282  1.00122.73           N  
ATOM   7888  N   MET D  51      64.301   9.117 -56.027  1.00103.46           N  
ATOM   7889  CA  MET D  51      65.104  10.203 -56.587  1.00105.32           C  
ATOM   7890  C   MET D  51      66.131  10.698 -55.579  1.00103.17           C  
ATOM   7891  O   MET D  51      67.263  11.002 -55.942  1.00105.41           O  
ATOM   7892  CB  MET D  51      64.228  11.367 -57.042  1.00106.69           C  
ATOM   7893  CG  MET D  51      63.778  11.245 -58.478  1.00107.23           C  
ATOM   7894  SD  MET D  51      65.154  11.397 -59.639  1.00108.52           S  
ATOM   7895  CE  MET D  51      65.710  13.069 -59.303  1.00107.97           C  
ATOM   7896  N   LYS D  52      65.737  10.791 -54.315  1.00102.59           N  
ATOM   7897  CA  LYS D  52      66.700  11.076 -53.258  1.00104.50           C  
ATOM   7898  C   LYS D  52      67.814  10.027 -53.287  1.00106.58           C  
ATOM   7899  O   LYS D  52      68.993  10.375 -53.221  1.00110.41           O  
ATOM   7900  CB  LYS D  52      66.018  11.104 -51.885  1.00103.81           C  
ATOM   7901  CG  LYS D  52      66.949  11.328 -50.687  1.00103.26           C  
ATOM   7902  CD  LYS D  52      67.326  12.797 -50.492  1.00102.87           C  
ATOM   7903  CE  LYS D  52      68.050  13.000 -49.157  1.00103.38           C  
ATOM   7904  NZ  LYS D  52      68.227  14.428 -48.765  1.00103.28           N  
ATOM   7905  N   GLY D  53      67.440   8.753 -53.406  1.00105.99           N  
ATOM   7906  CA  GLY D  53      68.407   7.650 -53.353  1.00105.35           C  
ATOM   7907  C   GLY D  53      69.400   7.554 -54.503  1.00104.08           C  
ATOM   7908  O   GLY D  53      70.448   6.921 -54.366  1.00108.28           O  
ATOM   7909  N   LEU D  54      69.066   8.165 -55.637  1.00104.62           N  
ATOM   7910  CA  LEU D  54      69.979   8.247 -56.779  1.00107.32           C  
ATOM   7911  C   LEU D  54      70.692   9.605 -56.826  1.00108.05           C  
ATOM   7912  O   LEU D  54      71.654   9.769 -57.577  1.00111.34           O  
ATOM   7913  CB  LEU D  54      69.228   7.974 -58.090  1.00108.48           C  
ATOM   7914  CG  LEU D  54      68.565   6.588 -58.194  1.00108.98           C  
ATOM   7915  CD1 LEU D  54      67.572   6.521 -59.349  1.00110.61           C  
ATOM   7916  CD2 LEU D  54      69.608   5.482 -58.319  1.00107.78           C  
ATOM   7917  N   ILE D  55      70.211  10.568 -56.034  1.00110.29           N  
ATOM   7918  CA  ILE D  55      70.932  11.827 -55.782  1.00111.90           C  
ATOM   7919  C   ILE D  55      72.092  11.562 -54.826  1.00114.39           C  
ATOM   7920  O   ILE D  55      73.104  12.268 -54.839  1.00115.51           O  
ATOM   7921  CB  ILE D  55      70.012  12.917 -55.159  1.00109.92           C  
ATOM   7922  CG1 ILE D  55      69.192  13.628 -56.236  1.00109.53           C  
ATOM   7923  CG2 ILE D  55      70.829  13.956 -54.406  1.00108.27           C  
ATOM   7924  CD1 ILE D  55      68.188  14.626 -55.678  1.00107.42           C  
ATOM   7925  N   ASP D  56      71.929  10.539 -53.991  1.00117.21           N  
ATOM   7926  CA  ASP D  56      72.948  10.166 -53.013  1.00120.58           C  
ATOM   7927  C   ASP D  56      73.946   9.164 -53.606  1.00121.19           C  
ATOM   7928  O   ASP D  56      75.153   9.284 -53.375  1.00119.92           O  
ATOM   7929  CB  ASP D  56      72.295   9.597 -51.742  1.00123.67           C  
ATOM   7930  CG  ASP D  56      73.190   9.718 -50.503  1.00126.58           C  
ATOM   7931  OD1 ASP D  56      74.140  10.534 -50.506  1.00127.90           O  
ATOM   7932  OD2 ASP D  56      72.934   8.995 -49.514  1.00127.76           O  
ATOM   7933  N   GLU D  57      73.448   8.179 -54.361  1.00117.75           N  
ATOM   7934  CA  GLU D  57      74.323   7.235 -55.081  1.00119.20           C  
ATOM   7935  C   GLU D  57      75.218   7.988 -56.062  1.00118.63           C  
ATOM   7936  O   GLU D  57      76.406   7.686 -56.177  1.00120.06           O  
ATOM   7937  CB  GLU D  57      73.510   6.169 -55.835  1.00120.16           C  
ATOM   7938  CG  GLU D  57      74.360   5.076 -56.521  1.00121.06           C  
ATOM   7939  CD  GLU D  57      73.544   4.144 -57.424  1.00121.58           C  
ATOM   7940  OE1 GLU D  57      73.764   2.912 -57.375  1.00121.38           O  
ATOM   7941  OE2 GLU D  57      72.687   4.638 -58.189  1.00118.68           O  
ATOM   7942  N   VAL D  58      74.641   8.963 -56.764  1.00118.05           N  
ATOM   7943  CA  VAL D  58      75.416   9.820 -57.652  1.00120.02           C  
ATOM   7944  C   VAL D  58      76.391  10.678 -56.834  1.00121.90           C  
ATOM   7945  O   VAL D  58      77.567  10.745 -57.170  1.00125.32           O  
ATOM   7946  CB  VAL D  58      74.512  10.695 -58.578  1.00119.09           C  
ATOM   7947  CG1 VAL D  58      73.950  11.899 -57.836  1.00119.82           C  
ATOM   7948  CG2 VAL D  58      75.284  11.149 -59.806  1.00117.60           C  
ATOM   7949  N   ASN D  59      75.930  11.292 -55.745  1.00119.35           N  
ATOM   7950  CA  ASN D  59      76.815  12.135 -54.942  1.00120.17           C  
ATOM   7951  C   ASN D  59      77.890  11.359 -54.178  1.00121.64           C  
ATOM   7952  O   ASN D  59      78.992  11.875 -53.978  1.00125.16           O  
ATOM   7953  CB  ASN D  59      76.044  12.997 -53.951  1.00119.70           C  
ATOM   7954  CG  ASN D  59      76.968  13.865 -53.120  1.00119.77           C  
ATOM   7955  OD1 ASN D  59      77.794  14.600 -53.664  1.00120.42           O  
ATOM   7956  ND2 ASN D  59      76.864  13.758 -51.801  1.00121.47           N  
ATOM   7957  N   GLN D  60      77.578  10.142 -53.733  1.00120.58           N  
ATOM   7958  CA  GLN D  60      78.592   9.305 -53.091  1.00122.30           C  
ATOM   7959  C   GLN D  60      79.761   9.089 -54.042  1.00124.18           C  
ATOM   7960  O   GLN D  60      80.910   9.321 -53.673  1.00127.84           O  
ATOM   7961  CB  GLN D  60      78.035   7.956 -52.627  1.00121.26           C  
ATOM   7962  CG  GLN D  60      77.486   7.972 -51.199  1.00120.66           C  
ATOM   7963  CD  GLN D  60      77.711   6.663 -50.443  1.00119.37           C  
ATOM   7964  OE1 GLN D  60      78.190   5.674 -51.002  1.00119.30           O  
ATOM   7965  NE2 GLN D  60      77.366   6.659 -49.158  1.00121.40           N  
ATOM   7966  N   ASP D  61      79.459   8.666 -55.269  1.00123.47           N  
ATOM   7967  CA  ASP D  61      80.490   8.464 -56.291  1.00125.44           C  
ATOM   7968  C   ASP D  61      81.317   9.732 -56.516  1.00127.00           C  
ATOM   7969  O   ASP D  61      82.521   9.722 -56.302  1.00132.06           O  
ATOM   7970  CB  ASP D  61      79.868   7.983 -57.611  1.00125.24           C  
ATOM   7971  CG  ASP D  61      79.370   6.538 -57.540  1.00125.05           C  
ATOM   7972  OD1 ASP D  61      79.601   5.858 -56.514  1.00129.65           O  
ATOM   7973  OD2 ASP D  61      78.744   6.076 -58.519  1.00121.08           O  
ATOM   7974  N   PHE D  62      80.664  10.826 -56.902  1.00129.07           N  
ATOM   7975  CA  PHE D  62      81.356  12.102 -57.167  1.00131.64           C  
ATOM   7976  C   PHE D  62      82.111  12.672 -55.963  1.00128.82           C  
ATOM   7977  O   PHE D  62      82.941  13.566 -56.121  1.00127.79           O  
ATOM   7978  CB  PHE D  62      80.372  13.160 -57.688  1.00135.54           C  
ATOM   7979  CG  PHE D  62      80.019  12.996 -59.141  1.00139.89           C  
ATOM   7980  CD1 PHE D  62      80.626  13.782 -60.110  1.00141.11           C  
ATOM   7981  CD2 PHE D  62      79.083  12.050 -59.542  1.00141.76           C  
ATOM   7982  CE1 PHE D  62      80.300  13.627 -61.454  1.00141.64           C  
ATOM   7983  CE2 PHE D  62      78.753  11.889 -60.880  1.00142.30           C  
ATOM   7984  CZ  PHE D  62      79.363  12.676 -61.837  1.00142.14           C  
ATOM   7985  N   THR D  63      81.803  12.176 -54.767  1.00129.78           N  
ATOM   7986  CA  THR D  63      82.541  12.553 -53.570  1.00132.11           C  
ATOM   7987  C   THR D  63      83.725  11.606 -53.350  1.00135.87           C  
ATOM   7988  O   THR D  63      84.875  12.040 -53.408  1.00144.19           O  
ATOM   7989  CB  THR D  63      81.629  12.572 -52.331  1.00130.64           C  
ATOM   7990  OG1 THR D  63      80.942  11.322 -52.218  1.00127.01           O  
ATOM   7991  CG2 THR D  63      80.610  13.701 -52.437  1.00131.22           C  
ATOM   7992  N   ASN D  64      83.451  10.319 -53.126  1.00135.14           N  
ATOM   7993  CA  ASN D  64      84.520   9.336 -52.850  1.00138.52           C  
ATOM   7994  C   ASN D  64      85.348   8.916 -54.078  1.00139.97           C  
ATOM   7995  O   ASN D  64      86.336   8.191 -53.948  1.00141.28           O  
ATOM   7996  CB  ASN D  64      83.975   8.101 -52.111  1.00139.09           C  
ATOM   7997  CG  ASN D  64      82.993   7.288 -52.941  1.00139.80           C  
ATOM   7998  OD1 ASN D  64      81.904   6.952 -52.473  1.00140.52           O  
ATOM   7999  ND2 ASN D  64      83.374   6.961 -54.170  1.00137.19           N  
ATOM   8000  N   ARG D  65      84.925   9.356 -55.261  1.00140.72           N  
ATOM   8001  CA  ARG D  65      85.761   9.308 -56.460  1.00143.02           C  
ATOM   8002  C   ARG D  65      86.757  10.479 -56.429  1.00145.72           C  
ATOM   8003  O   ARG D  65      87.883  10.347 -56.905  1.00146.01           O  
ATOM   8004  CB  ARG D  65      84.883   9.363 -57.718  1.00142.79           C  
ATOM   8005  CG  ARG D  65      85.607   9.249 -59.053  1.00142.83           C  
ATOM   8006  CD  ARG D  65      84.603   9.010 -60.192  1.00142.54           C  
ATOM   8007  NE  ARG D  65      85.013   9.618 -61.461  1.00141.27           N  
ATOM   8008  CZ  ARG D  65      84.292   9.593 -62.585  1.00140.60           C  
ATOM   8009  NH1 ARG D  65      83.108   8.984 -62.622  1.00139.09           N  
ATOM   8010  NH2 ARG D  65      84.756  10.183 -63.685  1.00138.47           N  
ATOM   8011  N   ILE D  66      86.339  11.610 -55.852  1.00149.07           N  
ATOM   8012  CA  ILE D  66      87.210  12.782 -55.684  1.00154.02           C  
ATOM   8013  C   ILE D  66      88.230  12.525 -54.574  1.00157.65           C  
ATOM   8014  O   ILE D  66      89.264  13.192 -54.508  1.00162.31           O  
ATOM   8015  CB  ILE D  66      86.398  14.081 -55.356  1.00153.88           C  
ATOM   8016  CG1 ILE D  66      86.838  15.247 -56.245  1.00153.65           C  
ATOM   8017  CG2 ILE D  66      86.526  14.473 -53.882  1.00153.22           C  
ATOM   8018  CD1 ILE D  66      86.404  15.120 -57.689  1.00152.96           C  
ATOM   8019  N   ASN D  67      87.925  11.560 -53.706  1.00158.75           N  
ATOM   8020  CA  ASN D  67      88.808  11.193 -52.593  1.00164.68           C  
ATOM   8021  C   ASN D  67      90.090  10.503 -53.066  1.00169.23           C  
ATOM   8022  O   ASN D  67      91.167  10.792 -52.546  1.00170.39           O  
ATOM   8023  CB  ASN D  67      88.070  10.302 -51.581  1.00165.08           C  
ATOM   8024  CG  ASN D  67      88.768  10.234 -50.222  1.00165.31           C  
ATOM   8025  OD1 ASN D  67      89.734  10.953 -49.956  1.00165.89           O  
ATOM   8026  ND2 ASN D  67      88.265   9.367 -49.351  1.00167.61           N  
ATOM   8027  N   LYS D  68      89.974   9.601 -54.045  1.00171.83           N  
ATOM   8028  CA  LYS D  68      91.153   8.952 -54.648  1.00172.32           C  
ATOM   8029  C   LYS D  68      91.988   9.944 -55.486  1.00174.49           C  
ATOM   8030  O   LYS D  68      93.185   9.729 -55.698  1.00176.41           O  
ATOM   8031  CB  LYS D  68      90.743   7.724 -55.488  1.00171.23           C  
ATOM   8032  CG  LYS D  68      91.898   7.040 -56.245  1.00170.18           C  
ATOM   8033  CD  LYS D  68      91.581   5.596 -56.648  1.00169.85           C  
ATOM   8034  CE  LYS D  68      92.243   4.575 -55.725  1.00170.28           C  
ATOM   8035  NZ  LYS D  68      91.806   4.697 -54.307  1.00172.12           N  
ATOM   8036  N   LEU D  69      91.359  11.031 -55.935  1.00175.79           N  
ATOM   8037  CA  LEU D  69      92.026  12.049 -56.756  1.00176.18           C  
ATOM   8038  C   LEU D  69      92.753  13.103 -55.909  1.00174.46           C  
ATOM   8039  O   LEU D  69      93.906  13.435 -56.193  1.00178.76           O  
ATOM   8040  CB  LEU D  69      91.019  12.709 -57.706  1.00177.03           C  
ATOM   8041  CG  LEU D  69      90.641  11.894 -58.955  1.00177.86           C  
ATOM   8042  CD1 LEU D  69      91.690  12.053 -60.044  1.00178.22           C  
ATOM   8043  CD2 LEU D  69      90.426  10.414 -58.645  1.00177.94           C  
ATOM   8044  N   LYS D  70      92.087  13.629 -54.881  1.00170.86           N  
ATOM   8045  CA  LYS D  70      92.755  14.493 -53.893  1.00170.84           C  
ATOM   8046  C   LYS D  70      93.838  13.715 -53.144  1.00170.47           C  
ATOM   8047  O   LYS D  70      94.841  14.286 -52.718  1.00170.55           O  
ATOM   8048  CB  LYS D  70      91.763  15.074 -52.876  1.00169.88           C  
ATOM   8049  CG  LYS D  70      90.980  16.293 -53.360  1.00169.42           C  
ATOM   8050  CD  LYS D  70      90.852  17.365 -52.272  1.00168.83           C  
ATOM   8051  CE  LYS D  70      90.065  16.887 -51.059  1.00168.26           C  
ATOM   8052  NZ  LYS D  70      90.047  17.917 -49.985  1.00166.96           N  
ATOM   8053  N   ASN D  71      93.604  12.415 -52.970  1.00172.98           N  
ATOM   8054  CA  ASN D  71      94.582  11.499 -52.387  1.00176.97           C  
ATOM   8055  C   ASN D  71      95.817  11.342 -53.276  1.00180.08           C  
ATOM   8056  O   ASN D  71      96.945  11.427 -52.791  1.00185.32           O  
ATOM   8057  CB  ASN D  71      93.925  10.131 -52.136  1.00177.12           C  
ATOM   8058  CG  ASN D  71      94.919   9.047 -51.768  1.00177.16           C  
ATOM   8059  OD1 ASN D  71      94.808   7.910 -52.232  1.00179.37           O  
ATOM   8060  ND2 ASN D  71      95.887   9.386 -50.926  1.00177.42           N  
ATOM   8061  N   SER D  72      95.602  11.128 -54.573  1.00179.78           N  
ATOM   8062  CA  SER D  72      96.705  10.848 -55.500  1.00180.22           C  
ATOM   8063  C   SER D  72      97.506  12.082 -55.957  1.00183.26           C  
ATOM   8064  O   SER D  72      98.559  11.924 -56.578  1.00182.80           O  
ATOM   8065  CB  SER D  72      96.194  10.083 -56.722  1.00178.31           C  
ATOM   8066  OG  SER D  72      97.272   9.507 -57.436  1.00176.95           O  
ATOM   8067  N   LEU D  73      97.014  13.291 -55.667  1.00186.37           N  
ATOM   8068  CA  LEU D  73      97.769  14.534 -55.941  1.00190.58           C  
ATOM   8069  C   LEU D  73      99.032  14.609 -55.083  1.00194.08           C  
ATOM   8070  O   LEU D  73     100.108  14.972 -55.567  1.00195.53           O  
ATOM   8071  CB  LEU D  73      96.898  15.779 -55.693  1.00190.38           C  
ATOM   8072  CG  LEU D  73      97.543  17.181 -55.681  1.00190.20           C  
ATOM   8073  CD1 LEU D  73      98.245  17.488 -54.354  1.00189.79           C  
ATOM   8074  CD2 LEU D  73      98.502  17.378 -56.850  1.00190.80           C  
ATOM   8075  N   PHE D  74      98.885  14.275 -53.803  1.00195.88           N  
ATOM   8076  CA  PHE D  74     100.020  14.212 -52.886  1.00196.52           C  
ATOM   8077  C   PHE D  74     100.926  13.028 -53.240  1.00197.10           C  
ATOM   8078  O   PHE D  74     102.152  13.167 -53.250  1.00197.51           O  
ATOM   8079  CB  PHE D  74      99.545  14.093 -51.437  1.00197.03           C  
ATOM   8080  CG  PHE D  74      98.650  15.217 -50.995  1.00197.47           C  
ATOM   8081  CD1 PHE D  74      99.178  16.466 -50.697  1.00198.02           C  
ATOM   8082  CD2 PHE D  74      97.278  15.022 -50.870  1.00198.32           C  
ATOM   8083  CE1 PHE D  74      98.357  17.502 -50.286  1.00198.95           C  
ATOM   8084  CE2 PHE D  74      96.448  16.054 -50.458  1.00199.09           C  
ATOM   8085  CZ  PHE D  74      96.991  17.295 -50.165  1.00199.42           C  
ATOM   8086  N   GLU D  75     100.318  11.879 -53.559  1.00193.91           N  
ATOM   8087  CA  GLU D  75     101.061  10.659 -53.948  1.00193.54           C  
ATOM   8088  C   GLU D  75     102.064  10.918 -55.088  1.00193.93           C  
ATOM   8089  O   GLU D  75     102.998  10.139 -55.294  1.00194.32           O  
ATOM   8090  CB  GLU D  75     100.095   9.533 -54.366  1.00191.49           C  
ATOM   8091  CG  GLU D  75      99.092   9.074 -53.286  1.00189.94           C  
ATOM   8092  CD  GLU D  75      99.672   8.088 -52.286  1.00188.20           C  
ATOM   8093  OE1 GLU D  75     100.356   7.132 -52.711  1.00185.68           O  
ATOM   8094  OE2 GLU D  75      99.427   8.258 -51.071  1.00187.57           O  
ATOM   8095  N   TYR D  76     101.841  12.006 -55.825  1.00197.39           N  
ATOM   8096  CA  TYR D  76     102.750  12.493 -56.867  1.00199.41           C  
ATOM   8097  C   TYR D  76     103.738  13.553 -56.342  1.00199.81           C  
ATOM   8098  O   TYR D  76     104.863  13.636 -56.835  1.00201.91           O  
ATOM   8099  CB  TYR D  76     101.913  13.068 -58.021  1.00201.10           C  
ATOM   8100  CG  TYR D  76     102.683  13.580 -59.227  1.00202.75           C  
ATOM   8101  CD1 TYR D  76     103.149  12.706 -60.209  1.00203.05           C  
ATOM   8102  CD2 TYR D  76     102.904  14.947 -59.407  1.00203.60           C  
ATOM   8103  CE1 TYR D  76     103.839  13.180 -61.328  1.00203.49           C  
ATOM   8104  CE2 TYR D  76     103.592  15.429 -60.521  1.00204.13           C  
ATOM   8105  CZ  TYR D  76     104.057  14.542 -61.478  1.00203.99           C  
ATOM   8106  OH  TYR D  76     104.736  15.020 -62.578  1.00206.32           O  
ATOM   8107  N   GLN D  77     103.324  14.351 -55.351  1.00197.57           N  
ATOM   8108  CA  GLN D  77     104.164  15.442 -54.813  1.00196.64           C  
ATOM   8109  C   GLN D  77     105.278  14.979 -53.857  1.00196.82           C  
ATOM   8110  O   GLN D  77     106.192  15.750 -53.555  1.00195.81           O  
ATOM   8111  CB  GLN D  77     103.305  16.509 -54.113  1.00195.92           C  
ATOM   8112  CG  GLN D  77     102.591  17.469 -55.064  1.00195.30           C  
ATOM   8113  CD  GLN D  77     101.854  18.591 -54.340  1.00194.73           C  
ATOM   8114  OE1 GLN D  77     102.119  18.877 -53.171  1.00192.98           O  
ATOM   8115  NE2 GLN D  77     100.925  19.232 -55.039  1.00194.79           N  
ATOM   8116  N   LYS D  78     105.186  13.743 -53.366  1.00196.91           N  
ATOM   8117  CA  LYS D  78     106.245  13.147 -52.533  1.00198.12           C  
ATOM   8118  C   LYS D  78     107.157  12.265 -53.379  1.00199.62           C  
ATOM   8119  O   LYS D  78     108.332  12.081 -53.055  1.00200.88           O  
ATOM   8120  CB  LYS D  78     105.654  12.333 -51.383  1.00197.51           C  
ATOM   8121  CG  LYS D  78     105.066  13.179 -50.266  1.00196.91           C  
ATOM   8122  CD  LYS D  78     103.892  14.009 -50.759  1.00196.19           C  
ATOM   8123  CE  LYS D  78     103.135  14.653 -49.629  1.00195.48           C  
ATOM   8124  NZ  LYS D  78     102.360  15.840 -50.081  1.00194.16           N  
ATOM   8125  N   ASN D  79     106.591  11.704 -54.447  1.00201.39           N  
ATOM   8126  CA  ASN D  79     107.362  11.075 -55.518  1.00202.56           C  
ATOM   8127  C   ASN D  79     108.092  12.136 -56.358  1.00204.31           C  
ATOM   8128  O   ASN D  79     109.093  11.837 -57.010  1.00203.15           O  
ATOM   8129  CB  ASN D  79     106.430  10.236 -56.407  1.00202.41           C  
ATOM   8130  CG  ASN D  79     107.180   9.267 -57.312  1.00202.43           C  
ATOM   8131  OD1 ASN D  79     108.253   8.770 -56.966  1.00203.30           O  
ATOM   8132  ND2 ASN D  79     106.601   8.982 -58.474  1.00202.17           N  
ATOM   8133  N   ASN D  80     107.573  13.367 -56.340  1.00206.24           N  
ATOM   8134  CA  ASN D  80     108.206  14.532 -56.984  1.00209.52           C  
ATOM   8135  C   ASN D  80     109.530  14.938 -56.311  1.00213.49           C  
ATOM   8136  O   ASN D  80     110.479  15.340 -56.991  1.00217.44           O  
ATOM   8137  CB  ASN D  80     107.213  15.712 -56.998  1.00208.58           C  
ATOM   8138  CG  ASN D  80     107.787  16.990 -57.609  1.00207.49           C  
ATOM   8139  OD1 ASN D  80     108.819  16.981 -58.279  1.00206.10           O  
ATOM   8140  ND2 ASN D  80     107.095  18.101 -57.382  1.00208.67           N  
ATOM   8141  N   LYS D  81     109.593  14.815 -54.983  1.00214.70           N  
ATOM   8142  CA  LYS D  81     110.810  15.145 -54.216  1.00215.27           C  
ATOM   8143  C   LYS D  81     111.982  14.185 -54.479  1.00217.41           C  
ATOM   8144  O   LYS D  81     113.127  14.496 -54.139  1.00219.54           O  
ATOM   8145  CB  LYS D  81     110.515  15.160 -52.709  1.00214.24           C  
ATOM   8146  CG  LYS D  81     109.465  16.170 -52.265  1.00213.65           C  
ATOM   8147  CD  LYS D  81     109.922  17.602 -52.472  1.00213.58           C  
ATOM   8148  CE  LYS D  81     108.905  18.580 -51.917  1.00213.62           C  
ATOM   8149  NZ  LYS D  81     109.382  19.984 -52.007  1.00214.20           N  
ATOM   8150  N   ASP D  82     111.687  13.021 -55.062  1.00218.94           N  
ATOM   8151  CA  ASP D  82     112.706  12.035 -55.436  1.00219.58           C  
ATOM   8152  C   ASP D  82     113.333  12.374 -56.792  1.00219.30           C  
ATOM   8153  O   ASP D  82     114.529  12.151 -57.005  1.00220.80           O  
ATOM   8154  CB  ASP D  82     112.098  10.625 -55.504  1.00219.70           C  
ATOM   8155  CG  ASP D  82     111.317  10.247 -54.246  1.00220.13           C  
ATOM   8156  OD1 ASP D  82     111.198  11.084 -53.324  1.00220.12           O  
ATOM   8157  OD2 ASP D  82     110.820   9.103 -54.182  1.00219.49           O  
ATOM   8158  N   SER D  83     112.516  12.905 -57.703  1.00219.08           N  
ATOM   8159  CA  SER D  83     112.956  13.253 -59.057  1.00219.99           C  
ATOM   8160  C   SER D  83     113.686  14.593 -59.086  1.00221.08           C  
ATOM   8161  O   SER D  83     114.661  14.760 -59.825  1.00224.36           O  
ATOM   8162  CB  SER D  83     111.758  13.304 -60.010  1.00220.11           C  
ATOM   8163  OG  SER D  83     110.876  14.360 -59.666  1.00220.20           O  
ATOM   8164  N   HIS D  84     113.205  15.543 -58.285  1.00219.99           N  
ATOM   8165  CA  HIS D  84     113.835  16.865 -58.176  1.00219.68           C  
ATOM   8166  C   HIS D  84     115.226  16.749 -57.525  1.00222.88           C  
ATOM   8167  O   HIS D  84     116.088  17.607 -57.738  1.00225.48           O  
ATOM   8168  CB  HIS D  84     112.936  17.836 -57.390  1.00216.32           C  
ATOM   8169  CG  HIS D  84     113.030  19.260 -57.849  1.00212.83           C  
ATOM   8170  ND1 HIS D  84     114.008  20.124 -57.404  1.00210.77           N  
ATOM   8171  CD2 HIS D  84     112.261  19.973 -58.706  1.00211.54           C  
ATOM   8172  CE1 HIS D  84     113.841  21.306 -57.972  1.00210.57           C  
ATOM   8173  NE2 HIS D  84     112.788  21.241 -58.766  1.00210.26           N  
ATOM   8174  N   SER D  85     115.434  15.687 -56.742  1.00224.82           N  
ATOM   8175  CA  SER D  85     116.755  15.345 -56.200  1.00225.15           C  
ATOM   8176  C   SER D  85     117.673  14.764 -57.280  1.00226.19           C  
ATOM   8177  O   SER D  85     118.839  15.143 -57.370  1.00229.47           O  
ATOM   8178  CB  SER D  85     116.630  14.344 -55.044  1.00224.64           C  
ATOM   8179  OG  SER D  85     115.908  14.896 -53.956  1.00223.08           O  
ATOM   8180  N   LEU D  86     117.142  13.846 -58.090  1.00224.84           N  
ATOM   8181  CA  LEU D  86     117.910  13.227 -59.185  1.00225.26           C  
ATOM   8182  C   LEU D  86     118.231  14.195 -60.330  1.00227.22           C  
ATOM   8183  O   LEU D  86     119.149  13.940 -61.108  1.00229.64           O  
ATOM   8184  CB  LEU D  86     117.179  11.996 -59.739  1.00223.57           C  
ATOM   8185  CG  LEU D  86     117.436  10.664 -59.024  1.00222.60           C  
ATOM   8186  CD1 LEU D  86     117.507  10.822 -57.511  1.00222.05           C  
ATOM   8187  CD2 LEU D  86     116.365   9.660 -59.395  1.00221.82           C  
ATOM   8188  N   THR D  87     117.474  15.289 -60.435  1.00227.85           N  
ATOM   8189  CA  THR D  87     117.732  16.328 -61.438  1.00229.17           C  
ATOM   8190  C   THR D  87     118.818  17.314 -60.986  1.00230.35           C  
ATOM   8191  O   THR D  87     119.656  17.716 -61.794  1.00232.25           O  
ATOM   8192  CB  THR D  87     116.443  17.100 -61.792  1.00229.31           C  
ATOM   8193  OG1 THR D  87     115.490  16.194 -62.363  1.00228.10           O  
ATOM   8194  CG2 THR D  87     116.729  18.218 -62.790  1.00230.61           C  
ATOM   8195  N   THR D  88     118.795  17.707 -59.709  1.00229.91           N  
ATOM   8196  CA  THR D  88     119.845  18.570 -59.138  1.00230.52           C  
ATOM   8197  C   THR D  88     121.169  17.811 -58.975  1.00233.17           C  
ATOM   8198  O   THR D  88     122.246  18.405 -59.083  1.00234.19           O  
ATOM   8199  CB  THR D  88     119.433  19.164 -57.771  1.00228.76           C  
ATOM   8200  OG1 THR D  88     118.144  19.779 -57.881  1.00226.36           O  
ATOM   8201  CG2 THR D  88     120.449  20.205 -57.304  1.00228.49           C  
ATOM   8202  N   ASN D  89     121.078  16.507 -58.706  1.00234.39           N  
ATOM   8203  CA  ASN D  89     122.255  15.629 -58.657  1.00236.21           C  
ATOM   8204  C   ASN D  89     122.865  15.421 -60.044  1.00235.96           C  
ATOM   8205  O   ASN D  89     124.087  15.386 -60.187  1.00236.48           O  
ATOM   8206  CB  ASN D  89     121.899  14.267 -58.044  1.00237.56           C  
ATOM   8207  CG  ASN D  89     121.493  14.363 -56.580  1.00238.65           C  
ATOM   8208  OD1 ASN D  89     121.649  15.405 -55.942  1.00238.95           O  
ATOM   8209  ND2 ASN D  89     120.963  13.269 -56.044  1.00240.25           N  
ATOM   8210  N   ILE D  90     122.007  15.275 -61.054  1.00234.76           N  
ATOM   8211  CA  ILE D  90     122.444  15.201 -62.454  1.00235.04           C  
ATOM   8212  C   ILE D  90     122.871  16.583 -62.985  1.00236.69           C  
ATOM   8213  O   ILE D  90     123.797  16.673 -63.785  1.00236.03           O  
ATOM   8214  CB  ILE D  90     121.350  14.569 -63.362  1.00234.32           C  
ATOM   8215  CG1 ILE D  90     121.293  13.052 -63.143  1.00233.99           C  
ATOM   8216  CG2 ILE D  90     121.617  14.859 -64.832  1.00234.80           C  
ATOM   8217  CD1 ILE D  90     120.062  12.389 -63.738  1.00233.98           C  
ATOM   8218  N   MET D  91     122.203  17.650 -62.539  1.00236.17           N  
ATOM   8219  CA  MET D  91     122.616  19.032 -62.868  1.00237.50           C  
ATOM   8220  C   MET D  91     123.988  19.419 -62.297  1.00237.64           C  
ATOM   8221  O   MET D  91     124.633  20.336 -62.814  1.00238.43           O  
ATOM   8222  CB  MET D  91     121.585  20.052 -62.356  1.00237.94           C  
ATOM   8223  CG  MET D  91     120.521  20.467 -63.364  1.00238.22           C  
ATOM   8224  SD  MET D  91     120.926  22.020 -64.197  1.00238.02           S  
ATOM   8225  CE  MET D  91     120.871  23.187 -62.834  1.00238.59           C  
ATOM   8226  N   GLU D  92     124.416  18.745 -61.227  1.00236.67           N  
ATOM   8227  CA  GLU D  92     125.652  19.105 -60.521  1.00236.32           C  
ATOM   8228  C   GLU D  92     126.816  18.100 -60.656  1.00236.60           C  
ATOM   8229  O   GLU D  92     127.979  18.497 -60.525  1.00234.78           O  
ATOM   8230  CB  GLU D  92     125.346  19.373 -59.046  1.00236.57           C  
ATOM   8231  CG  GLU D  92     126.501  20.018 -58.289  1.00237.26           C  
ATOM   8232  CD  GLU D  92     126.059  21.080 -57.303  1.00238.35           C  
ATOM   8233  OE1 GLU D  92     124.884  21.074 -56.879  1.00238.37           O  
ATOM   8234  OE2 GLU D  92     126.901  21.929 -56.953  1.00240.17           O  
ATOM   8235  N   ILE D  93     126.528  16.820 -60.916  1.00235.53           N  
ATOM   8236  CA  ILE D  93     127.600  15.854 -61.242  1.00235.02           C  
ATOM   8237  C   ILE D  93     128.109  16.027 -62.682  1.00233.84           C  
ATOM   8238  O   ILE D  93     129.082  15.378 -63.076  1.00233.89           O  
ATOM   8239  CB  ILE D  93     127.194  14.361 -61.010  1.00235.30           C  
ATOM   8240  CG1 ILE D  93     126.193  13.875 -62.070  1.00235.15           C  
ATOM   8241  CG2 ILE D  93     126.672  14.159 -59.590  1.00235.86           C  
ATOM   8242  CD1 ILE D  93     125.589  12.510 -61.773  1.00234.77           C  
ATOM   8243  N   LEU D  94     127.432  16.876 -63.461  1.00232.77           N  
ATOM   8244  CA  LEU D  94     127.900  17.286 -64.789  1.00232.19           C  
ATOM   8245  C   LEU D  94     128.537  18.684 -64.786  1.00233.31           C  
ATOM   8246  O   LEU D  94     129.396  18.963 -65.620  1.00232.99           O  
ATOM   8247  CB  LEU D  94     126.752  17.240 -65.802  1.00231.15           C  
ATOM   8248  CG  LEU D  94     125.979  15.916 -65.882  1.00230.18           C  
ATOM   8249  CD1 LEU D  94     125.007  15.935 -67.054  1.00229.19           C  
ATOM   8250  CD2 LEU D  94     126.912  14.713 -65.969  1.00230.02           C  
ATOM   8251  N   ARG D  95     128.117  19.556 -63.865  1.00232.96           N  
ATOM   8252  CA  ARG D  95     128.758  20.872 -63.684  1.00231.75           C  
ATOM   8253  C   ARG D  95     130.174  20.731 -63.092  1.00231.70           C  
ATOM   8254  O   ARG D  95     131.018  21.620 -63.263  1.00230.52           O  
ATOM   8255  CB  ARG D  95     127.887  21.792 -62.814  1.00230.71           C  
ATOM   8256  CG  ARG D  95     128.317  23.257 -62.822  1.00229.53           C  
ATOM   8257  CD  ARG D  95     127.179  24.191 -62.417  1.00228.76           C  
ATOM   8258  NE  ARG D  95     126.643  23.896 -61.088  1.00228.21           N  
ATOM   8259  CZ  ARG D  95     127.227  24.221 -59.934  1.00228.28           C  
ATOM   8260  NH1 ARG D  95     128.398  24.854 -59.907  1.00228.14           N  
ATOM   8261  NH2 ARG D  95     126.638  23.904 -58.788  1.00228.20           N  
ATOM   8262  N   GLY D  96     130.419  19.615 -62.400  1.00231.94           N  
ATOM   8263  CA  GLY D  96     131.766  19.223 -61.967  1.00231.38           C  
ATOM   8264  C   GLY D  96     132.577  18.558 -63.076  1.00230.96           C  
ATOM   8265  O   GLY D  96     133.790  18.758 -63.164  1.00230.65           O  
ATOM   8266  N   ASP D  97     131.906  17.761 -63.915  1.00229.93           N  
ATOM   8267  CA  ASP D  97     132.516  17.165 -65.123  1.00228.11           C  
ATOM   8268  C   ASP D  97     132.505  18.125 -66.341  1.00229.46           C  
ATOM   8269  O   ASP D  97     132.901  17.728 -67.441  1.00228.86           O  
ATOM   8270  CB  ASP D  97     131.810  15.838 -65.498  1.00224.99           C  
ATOM   8271  CG  ASP D  97     132.397  14.616 -64.786  1.00222.00           C  
ATOM   8272  OD1 ASP D  97     132.954  14.755 -63.678  1.00219.09           O  
ATOM   8273  OD2 ASP D  97     132.285  13.501 -65.342  1.00220.04           O  
ATOM   8274  N   PHE D  98     132.055  19.372 -66.143  1.00232.17           N  
ATOM   8275  CA  PHE D  98     132.018  20.403 -67.204  1.00232.99           C  
ATOM   8276  C   PHE D  98     133.114  21.459 -67.029  1.00232.93           C  
ATOM   8277  O   PHE D  98     133.765  21.844 -68.003  1.00233.36           O  
ATOM   8278  CB  PHE D  98     130.647  21.096 -67.247  1.00233.81           C  
ATOM   8279  CG  PHE D  98     130.583  22.282 -68.187  1.00234.36           C  
ATOM   8280  CD1 PHE D  98     130.297  22.101 -69.536  1.00234.46           C  
ATOM   8281  CD2 PHE D  98     130.797  23.577 -67.719  1.00234.05           C  
ATOM   8282  CE1 PHE D  98     130.232  23.188 -70.405  1.00234.53           C  
ATOM   8283  CE2 PHE D  98     130.736  24.668 -68.582  1.00233.84           C  
ATOM   8284  CZ  PHE D  98     130.452  24.473 -69.927  1.00234.21           C  
ATOM   8285  N   SER D  99     133.297  21.940 -65.798  1.00231.22           N  
ATOM   8286  CA  SER D  99     134.420  22.828 -65.467  1.00230.50           C  
ATOM   8287  C   SER D  99     135.749  22.154 -65.811  1.00230.37           C  
ATOM   8288  O   SER D  99     136.762  22.819 -66.036  1.00230.15           O  
ATOM   8289  CB  SER D  99     134.396  23.193 -63.983  1.00230.13           C  
ATOM   8290  OG  SER D  99     133.160  23.790 -63.630  1.00229.86           O  
ATOM   8291  N   SER D 100     135.723  20.825 -65.827  1.00231.41           N  
ATOM   8292  CA  SER D 100     136.822  20.010 -66.320  1.00231.50           C  
ATOM   8293  C   SER D 100     137.066  20.162 -67.826  1.00232.40           C  
ATOM   8294  O   SER D 100     138.209  20.075 -68.281  1.00233.24           O  
ATOM   8295  CB  SER D 100     136.521  18.541 -66.028  1.00231.09           C  
ATOM   8296  OG  SER D 100     136.140  18.346 -64.677  1.00229.17           O  
ATOM   8297  N   ALA D 101     135.991  20.383 -68.584  1.00232.02           N  
ATOM   8298  CA  ALA D 101     136.017  20.332 -70.054  1.00230.86           C  
ATOM   8299  C   ALA D 101     137.098  21.188 -70.720  1.00229.92           C  
ATOM   8300  O   ALA D 101     137.693  20.760 -71.710  1.00229.50           O  
ATOM   8301  CB  ALA D 101     134.643  20.703 -70.616  1.00231.55           C  
ATOM   8302  N   ASN D 102     137.349  22.383 -70.181  1.00227.65           N  
ATOM   8303  CA  ASN D 102     138.249  23.355 -70.828  1.00225.77           C  
ATOM   8304  C   ASN D 102     139.496  23.766 -70.021  1.00224.97           C  
ATOM   8305  O   ASN D 102     140.594  23.828 -70.580  1.00223.90           O  
ATOM   8306  CB  ASN D 102     137.464  24.601 -71.273  1.00225.28           C  
ATOM   8307  CG  ASN D 102     136.749  25.298 -70.125  1.00224.91           C  
ATOM   8308  OD1 ASN D 102     136.987  25.003 -68.954  1.00223.64           O  
ATOM   8309  ND2 ASN D 102     135.867  26.233 -70.462  1.00225.64           N  
ATOM   8310  N   ASN D 103     139.333  24.044 -68.725  1.00223.51           N  
ATOM   8311  CA  ASN D 103     140.443  24.546 -67.886  1.00222.40           C  
ATOM   8312  C   ASN D 103     141.618  23.576 -67.696  1.00222.57           C  
ATOM   8313  O   ASN D 103     142.743  24.013 -67.439  1.00222.09           O  
ATOM   8314  CB  ASN D 103     139.936  24.996 -66.505  1.00221.42           C  
ATOM   8315  CG  ASN D 103     139.467  26.443 -66.491  1.00220.24           C  
ATOM   8316  OD1 ASN D 103     139.809  27.208 -65.588  1.00219.99           O  
ATOM   8317  ND2 ASN D 103     138.684  26.824 -67.494  1.00221.40           N  
ATOM   8318  N   ARG D 104     141.354  22.275 -67.803  1.00223.78           N  
ATOM   8319  CA  ARG D 104     142.406  21.255 -67.699  1.00224.02           C  
ATOM   8320  C   ARG D 104     143.078  20.976 -69.043  1.00223.31           C  
ATOM   8321  O   ARG D 104     144.299  20.824 -69.107  1.00222.28           O  
ATOM   8322  CB  ARG D 104     141.854  19.950 -67.113  1.00225.12           C  
ATOM   8323  CG  ARG D 104     141.832  19.928 -65.593  1.00225.70           C  
ATOM   8324  CD  ARG D 104     141.568  18.532 -65.041  1.00225.98           C  
ATOM   8325  NE  ARG D 104     140.167  18.314 -64.682  1.00226.26           N  
ATOM   8326  CZ  ARG D 104     139.693  17.197 -64.130  1.00226.61           C  
ATOM   8327  NH1 ARG D 104     140.500  16.170 -63.871  1.00226.52           N  
ATOM   8328  NH2 ARG D 104     138.402  17.101 -63.836  1.00227.45           N  
ATOM   8329  N   ASP D 105     142.281  20.905 -70.106  1.00220.98           N  
ATOM   8330  CA  ASP D 105     142.805  20.662 -71.452  1.00219.12           C  
ATOM   8331  C   ASP D 105     143.778  21.752 -71.902  1.00220.10           C  
ATOM   8332  O   ASP D 105     144.754  21.457 -72.590  1.00217.85           O  
ATOM   8333  CB  ASP D 105     141.661  20.518 -72.461  1.00217.74           C  
ATOM   8334  CG  ASP D 105     140.865  19.237 -72.262  1.00216.52           C  
ATOM   8335  OD1 ASP D 105     141.252  18.407 -71.409  1.00216.49           O  
ATOM   8336  OD2 ASP D 105     139.846  19.061 -72.960  1.00217.34           O  
ATOM   8337  N   ASN D 106     143.516  22.999 -71.510  1.00220.97           N  
ATOM   8338  CA  ASN D 106     144.476  24.090 -71.727  1.00220.89           C  
ATOM   8339  C   ASN D 106     145.785  23.889 -70.947  1.00221.10           C  
ATOM   8340  O   ASN D 106     146.860  24.253 -71.432  1.00218.59           O  
ATOM   8341  CB  ASN D 106     143.855  25.452 -71.382  1.00221.33           C  
ATOM   8342  CG  ASN D 106     142.979  25.999 -72.500  1.00221.37           C  
ATOM   8343  OD1 ASN D 106     142.457  25.249 -73.327  1.00221.31           O  
ATOM   8344  ND2 ASN D 106     142.816  27.317 -72.528  1.00223.11           N  
ATOM   8345  N   THR D 107     145.687  23.305 -69.750  1.00221.50           N  
ATOM   8346  CA  THR D 107     146.859  22.994 -68.920  1.00221.31           C  
ATOM   8347  C   THR D 107     147.581  21.733 -69.420  1.00220.51           C  
ATOM   8348  O   THR D 107     148.728  21.472 -69.043  1.00221.02           O  
ATOM   8349  CB  THR D 107     146.459  22.803 -67.432  1.00221.90           C  
ATOM   8350  OG1 THR D 107     145.644  23.902 -67.002  1.00222.08           O  
ATOM   8351  CG2 THR D 107     147.693  22.714 -66.540  1.00223.03           C  
ATOM   8352  N   TYR D 108     146.897  20.956 -70.260  1.00218.85           N  
ATOM   8353  CA  TYR D 108     147.469  19.758 -70.883  1.00216.45           C  
ATOM   8354  C   TYR D 108     147.843  19.946 -72.352  1.00215.55           C  
ATOM   8355  O   TYR D 108     148.695  19.217 -72.859  1.00212.75           O  
ATOM   8356  CB  TYR D 108     146.499  18.583 -70.768  1.00215.48           C  
ATOM   8357  CG  TYR D 108     146.502  17.941 -69.407  1.00214.11           C  
ATOM   8358  CD1 TYR D 108     147.655  17.345 -68.904  1.00213.60           C  
ATOM   8359  CD2 TYR D 108     145.356  17.926 -68.620  1.00213.79           C  
ATOM   8360  CE1 TYR D 108     147.666  16.754 -67.651  1.00213.04           C  
ATOM   8361  CE2 TYR D 108     145.357  17.339 -67.367  1.00213.23           C  
ATOM   8362  CZ  TYR D 108     146.514  16.753 -66.887  1.00212.93           C  
ATOM   8363  OH  TYR D 108     146.521  16.165 -65.643  1.00212.20           O  
ATOM   8364  N   ASN D 109     147.199  20.895 -73.036  1.00215.87           N  
ATOM   8365  CA  ASN D 109     147.499  21.168 -74.449  1.00215.69           C  
ATOM   8366  C   ASN D 109     148.809  21.943 -74.640  1.00215.45           C  
ATOM   8367  O   ASN D 109     149.570  21.650 -75.566  1.00213.70           O  
ATOM   8368  CB  ASN D 109     146.331  21.880 -75.158  1.00216.60           C  
ATOM   8369  CG  ASN D 109     146.221  23.358 -74.803  1.00217.85           C  
ATOM   8370  OD1 ASN D 109     147.011  23.890 -74.023  1.00216.95           O  
ATOM   8371  ND2 ASN D 109     145.232  24.028 -75.384  1.00220.16           N  
ATOM   8372  N   ARG D 110     149.072  22.923 -73.771  1.00214.59           N  
ATOM   8373  CA  ARG D 110     150.372  23.612 -73.756  1.00211.49           C  
ATOM   8374  C   ARG D 110     151.454  22.726 -73.117  1.00210.80           C  
ATOM   8375  O   ARG D 110     152.648  22.991 -73.271  1.00208.85           O  
ATOM   8376  CB  ARG D 110     150.286  24.959 -73.024  1.00210.24           C  
ATOM   8377  CG  ARG D 110     150.254  24.848 -71.506  1.00208.97           C  
ATOM   8378  CD  ARG D 110     150.590  26.160 -70.825  1.00208.32           C  
ATOM   8379  NE  ARG D 110     150.764  25.971 -69.385  1.00207.76           N  
ATOM   8380  CZ  ARG D 110     151.835  25.426 -68.808  1.00207.22           C  
ATOM   8381  NH1 ARG D 110     152.866  25.000 -69.535  1.00207.02           N  
ATOM   8382  NH2 ARG D 110     151.877  25.302 -67.486  1.00207.55           N  
ATOM   8383  N   VAL D 111     151.021  21.701 -72.377  1.00210.56           N  
ATOM   8384  CA  VAL D 111     151.904  20.644 -71.869  1.00210.97           C  
ATOM   8385  C   VAL D 111     152.019  19.483 -72.878  1.00210.66           C  
ATOM   8386  O   VAL D 111     152.934  18.659 -72.784  1.00211.36           O  
ATOM   8387  CB  VAL D 111     151.416  20.121 -70.496  1.00211.36           C  
ATOM   8388  CG1 VAL D 111     152.046  18.794 -70.170  1.00211.64           C  
ATOM   8389  CG2 VAL D 111     151.714  21.138 -69.402  1.00211.13           C  
ATOM   8390  N   SER D 112     151.081  19.419 -73.825  1.00210.23           N  
ATOM   8391  CA  SER D 112     151.214  18.568 -75.016  1.00209.44           C  
ATOM   8392  C   SER D 112     151.966  19.302 -76.139  1.00209.47           C  
ATOM   8393  O   SER D 112     152.355  18.678 -77.127  1.00208.71           O  
ATOM   8394  CB  SER D 112     149.844  18.092 -75.511  1.00208.95           C  
ATOM   8395  OG  SER D 112     149.264  17.166 -74.605  1.00208.79           O  
ATOM   8396  N   GLU D 113     152.135  20.622 -75.996  1.00210.63           N  
ATOM   8397  CA  GLU D 113     153.143  21.383 -76.759  1.00209.61           C  
ATOM   8398  C   GLU D 113     154.540  21.102 -76.200  1.00208.96           C  
ATOM   8399  O   GLU D 113     155.503  20.984 -76.955  1.00209.06           O  
ATOM   8400  CB  GLU D 113     152.907  22.902 -76.687  1.00209.93           C  
ATOM   8401  CG  GLU D 113     151.870  23.476 -77.646  1.00209.73           C  
ATOM   8402  CD  GLU D 113     151.900  25.005 -77.694  1.00208.86           C  
ATOM   8403  OE1 GLU D 113     152.626  25.627 -76.886  1.00207.73           O  
ATOM   8404  OE2 GLU D 113     151.195  25.589 -78.543  1.00210.22           O  
ATOM   8405  N   ASP D 114     154.640  21.011 -74.873  1.00207.20           N  
ATOM   8406  CA  ASP D 114     155.915  20.739 -74.195  1.00205.24           C  
ATOM   8407  C   ASP D 114     156.319  19.249 -74.207  1.00206.26           C  
ATOM   8408  O   ASP D 114     157.368  18.889 -73.669  1.00206.13           O  
ATOM   8409  CB  ASP D 114     155.882  21.281 -72.756  1.00202.98           C  
ATOM   8410  CG  ASP D 114     155.715  22.801 -72.698  1.00200.22           C  
ATOM   8411  OD1 ASP D 114     156.108  23.500 -73.659  1.00199.53           O  
ATOM   8412  OD2 ASP D 114     155.188  23.298 -71.680  1.00198.18           O  
ATOM   8413  N   LEU D 115     155.486  18.392 -74.803  1.00206.08           N  
ATOM   8414  CA  LEU D 115     155.892  17.028 -75.170  1.00207.16           C  
ATOM   8415  C   LEU D 115     156.112  16.887 -76.690  1.00207.42           C  
ATOM   8416  O   LEU D 115     156.815  15.973 -77.124  1.00207.88           O  
ATOM   8417  CB  LEU D 115     154.868  15.996 -74.670  1.00207.40           C  
ATOM   8418  CG  LEU D 115     155.157  14.524 -75.017  1.00207.36           C  
ATOM   8419  CD1 LEU D 115     154.878  13.591 -73.854  1.00207.84           C  
ATOM   8420  CD2 LEU D 115     154.377  14.085 -76.255  1.00206.78           C  
ATOM   8421  N   ARG D 116     155.531  17.790 -77.487  1.00207.24           N  
ATOM   8422  CA  ARG D 116     155.617  17.722 -78.960  1.00206.77           C  
ATOM   8423  C   ARG D 116     156.407  18.872 -79.618  1.00207.33           C  
ATOM   8424  O   ARG D 116     157.316  18.614 -80.412  1.00199.72           O  
ATOM   8425  CB  ARG D 116     154.210  17.650 -79.571  1.00207.04           C  
ATOM   8426  CG  ARG D 116     154.194  17.361 -81.074  1.00207.28           C  
ATOM   8427  CD  ARG D 116     152.824  16.899 -81.547  1.00207.55           C  
ATOM   8428  NE  ARG D 116     152.487  15.568 -81.036  1.00207.75           N  
ATOM   8429  CZ  ARG D 116     152.869  14.412 -81.583  1.00208.55           C  
ATOM   8430  NH1 ARG D 116     153.619  14.384 -82.684  1.00208.36           N  
ATOM   8431  NH2 ARG D 116     152.497  13.265 -81.021  1.00209.51           N  
ATOM   8432  N   SER D 117     156.058  20.123 -79.300  1.00209.38           N  
ATOM   8433  CA  SER D 117     156.673  21.314 -79.938  1.00211.12           C  
ATOM   8434  C   SER D 117     158.181  21.480 -79.666  1.00210.15           C  
ATOM   8435  O   SER D 117     158.874  22.175 -80.419  1.00210.98           O  
ATOM   8436  CB  SER D 117     155.936  22.599 -79.518  1.00213.01           C  
ATOM   8437  OG  SER D 117     156.385  23.728 -80.255  1.00216.18           O  
ATOM   8438  N   ARG D 118     158.674  20.862 -78.591  1.00205.01           N  
ATOM   8439  CA  ARG D 118     160.102  20.882 -78.254  1.00200.36           C  
ATOM   8440  C   ARG D 118     160.828  19.643 -78.802  1.00194.90           C  
ATOM   8441  O   ARG D 118     161.950  19.763 -79.295  1.00189.24           O  
ATOM   8442  CB  ARG D 118     160.296  21.002 -76.737  1.00201.62           C  
ATOM   8443  CG  ARG D 118     159.614  22.235 -76.114  1.00202.75           C  
ATOM   8444  CD  ARG D 118     159.869  22.355 -74.606  1.00203.23           C  
ATOM   8445  NE  ARG D 118     159.589  21.107 -73.893  1.00204.28           N  
ATOM   8446  CZ  ARG D 118     159.774  20.915 -72.588  1.00204.32           C  
ATOM   8447  NH1 ARG D 118     160.229  21.886 -71.802  1.00203.64           N  
ATOM   8448  NH2 ARG D 118     159.491  19.734 -72.066  1.00205.85           N  
ATOM   8449  N   ILE D 119     160.189  18.469 -78.725  1.00190.22           N  
ATOM   8450  CA  ILE D 119     160.709  17.239 -79.361  1.00187.29           C  
ATOM   8451  C   ILE D 119     160.949  17.443 -80.871  1.00186.92           C  
ATOM   8452  O   ILE D 119     161.803  16.777 -81.454  1.00181.02           O  
ATOM   8453  CB  ILE D 119     159.774  16.001 -79.115  1.00185.85           C  
ATOM   8454  CG1 ILE D 119     160.035  15.376 -77.739  1.00185.01           C  
ATOM   8455  CG2 ILE D 119     159.971  14.923 -80.184  1.00185.49           C  
ATOM   8456  CD1 ILE D 119     161.163  14.356 -77.724  1.00182.96           C  
ATOM   8457  N   GLU D 120     160.207  18.367 -81.488  1.00187.96           N  
ATOM   8458  CA  GLU D 120     160.411  18.745 -82.898  1.00185.71           C  
ATOM   8459  C   GLU D 120     161.515  19.806 -83.082  1.00184.88           C  
ATOM   8460  O   GLU D 120     162.255  19.763 -84.068  1.00185.34           O  
ATOM   8461  CB  GLU D 120     159.092  19.234 -83.513  1.00185.51           C  
ATOM   8462  CG  GLU D 120     159.098  19.379 -85.043  1.00185.77           C  
ATOM   8463  CD  GLU D 120     159.576  20.742 -85.535  1.00185.89           C  
ATOM   8464  OE1 GLU D 120     159.435  21.745 -84.804  1.00186.53           O  
ATOM   8465  OE2 GLU D 120     160.088  20.808 -86.671  1.00188.08           O  
ATOM   8466  N   VAL D 121     161.615  20.759 -82.152  1.00182.36           N  
ATOM   8467  CA  VAL D 121     162.725  21.728 -82.147  1.00181.30           C  
ATOM   8468  C   VAL D 121     164.058  21.029 -81.835  1.00180.15           C  
ATOM   8469  O   VAL D 121     165.126  21.506 -82.228  1.00181.96           O  
ATOM   8470  CB  VAL D 121     162.483  22.884 -81.129  1.00180.48           C  
ATOM   8471  CG1 VAL D 121     163.736  23.734 -80.943  1.00179.42           C  
ATOM   8472  CG2 VAL D 121     161.327  23.759 -81.578  1.00180.56           C  
ATOM   8473  N   LEU D 122     163.979  19.894 -81.140  1.00179.69           N  
ATOM   8474  CA  LEU D 122     165.156  19.123 -80.735  1.00175.07           C  
ATOM   8475  C   LEU D 122     165.592  18.108 -81.796  1.00172.97           C  
ATOM   8476  O   LEU D 122     166.731  18.157 -82.255  1.00165.71           O  
ATOM   8477  CB  LEU D 122     164.882  18.409 -79.404  1.00175.30           C  
ATOM   8478  CG  LEU D 122     166.066  17.897 -78.574  1.00175.18           C  
ATOM   8479  CD1 LEU D 122     166.686  16.654 -79.190  1.00175.11           C  
ATOM   8480  CD2 LEU D 122     167.117  18.984 -78.372  1.00174.79           C  
ATOM   8481  N   LYS D 123     164.699  17.191 -82.179  1.00170.16           N  
ATOM   8482  CA  LYS D 123     165.042  16.136 -83.154  1.00167.56           C  
ATOM   8483  C   LYS D 123     165.590  16.682 -84.478  1.00166.08           C  
ATOM   8484  O   LYS D 123     166.354  15.992 -85.151  1.00162.94           O  
ATOM   8485  CB  LYS D 123     163.857  15.192 -83.433  1.00166.87           C  
ATOM   8486  CG  LYS D 123     163.969  13.796 -82.803  1.00165.80           C  
ATOM   8487  CD  LYS D 123     163.689  13.782 -81.301  1.00164.75           C  
ATOM   8488  CE  LYS D 123     164.923  14.117 -80.472  1.00163.78           C  
ATOM   8489  NZ  LYS D 123     164.721  13.897 -79.012  1.00162.47           N  
ATOM   8490  N   ARG D 124     165.196  17.900 -84.853  1.00164.78           N  
ATOM   8491  CA  ARG D 124     165.806  18.599 -85.994  1.00163.22           C  
ATOM   8492  C   ARG D 124     167.261  18.964 -85.678  1.00162.88           C  
ATOM   8493  O   ARG D 124     168.141  18.885 -86.543  1.00163.01           O  
ATOM   8494  CB  ARG D 124     165.020  19.871 -86.337  1.00162.27           C  
ATOM   8495  CG  ARG D 124     165.417  20.513 -87.666  1.00160.85           C  
ATOM   8496  CD  ARG D 124     164.992  21.970 -87.741  1.00158.58           C  
ATOM   8497  NE  ARG D 124     165.815  22.834 -86.890  1.00155.95           N  
ATOM   8498  CZ  ARG D 124     166.937  23.455 -87.264  1.00154.19           C  
ATOM   8499  NH1 ARG D 124     167.422  23.331 -88.496  1.00153.74           N  
ATOM   8500  NH2 ARG D 124     167.588  24.213 -86.388  1.00153.81           N  
ATOM   8501  N   LYS D 125     167.497  19.366 -84.432  1.00160.73           N  
ATOM   8502  CA  LYS D 125     168.837  19.668 -83.951  1.00159.18           C  
ATOM   8503  C   LYS D 125     169.673  18.385 -83.828  1.00157.59           C  
ATOM   8504  O   LYS D 125     170.821  18.364 -84.261  1.00156.73           O  
ATOM   8505  CB  LYS D 125     168.756  20.406 -82.609  1.00159.43           C  
ATOM   8506  CG  LYS D 125     169.971  21.245 -82.266  1.00160.13           C  
ATOM   8507  CD  LYS D 125     171.168  20.386 -81.879  1.00160.39           C  
ATOM   8508  CE  LYS D 125     172.106  21.112 -80.925  1.00160.19           C  
ATOM   8509  NZ  LYS D 125     172.634  22.378 -81.500  1.00158.79           N  
ATOM   8510  N   VAL D 126     169.096  17.321 -83.263  1.00157.15           N  
ATOM   8511  CA  VAL D 126     169.812  16.037 -83.074  1.00154.59           C  
ATOM   8512  C   VAL D 126     170.113  15.284 -84.387  1.00155.49           C  
ATOM   8513  O   VAL D 126     171.130  14.589 -84.472  1.00152.02           O  
ATOM   8514  CB  VAL D 126     169.075  15.092 -82.063  1.00153.44           C  
ATOM   8515  CG1 VAL D 126     169.395  13.617 -82.321  1.00151.19           C  
ATOM   8516  CG2 VAL D 126     169.443  15.463 -80.636  1.00153.06           C  
ATOM   8517  N   ILE D 127     169.251  15.422 -85.397  1.00157.69           N  
ATOM   8518  CA  ILE D 127     169.502  14.817 -86.724  1.00157.40           C  
ATOM   8519  C   ILE D 127     170.613  15.559 -87.489  1.00158.40           C  
ATOM   8520  O   ILE D 127     171.321  14.953 -88.300  1.00152.67           O  
ATOM   8521  CB  ILE D 127     168.205  14.715 -87.592  1.00157.38           C  
ATOM   8522  CG1 ILE D 127     167.503  13.366 -87.371  1.00156.12           C  
ATOM   8523  CG2 ILE D 127     168.518  14.853 -89.082  1.00159.49           C  
ATOM   8524  CD1 ILE D 127     167.273  12.988 -85.909  1.00154.21           C  
ATOM   8525  N   GLU D 128     170.765  16.859 -87.221  1.00157.27           N  
ATOM   8526  CA  GLU D 128     171.897  17.644 -87.741  1.00154.33           C  
ATOM   8527  C   GLU D 128     173.239  17.228 -87.103  1.00149.33           C  
ATOM   8528  O   GLU D 128     174.307  17.512 -87.655  1.00144.57           O  
ATOM   8529  CB  GLU D 128     171.643  19.143 -87.521  1.00156.74           C  
ATOM   8530  CG  GLU D 128     172.630  20.080 -88.217  1.00158.30           C  
ATOM   8531  CD  GLU D 128     172.256  21.549 -88.071  1.00159.67           C  
ATOM   8532  OE1 GLU D 128     171.296  21.861 -87.332  1.00160.06           O  
ATOM   8533  OE2 GLU D 128     172.928  22.397 -88.695  1.00162.25           O  
ATOM   8534  N   LYS D 129     173.172  16.560 -85.948  1.00145.46           N  
ATOM   8535  CA  LYS D 129     174.357  16.054 -85.243  1.00144.13           C  
ATOM   8536  C   LYS D 129     174.638  14.580 -85.550  1.00143.65           C  
ATOM   8537  O   LYS D 129     175.802  14.189 -85.667  1.00134.70           O  
ATOM   8538  CB  LYS D 129     174.206  16.257 -83.730  1.00145.36           C  
ATOM   8539  CG  LYS D 129     173.915  17.703 -83.309  1.00146.03           C  
ATOM   8540  CD  LYS D 129     175.089  18.649 -83.566  1.00146.32           C  
ATOM   8541  CE  LYS D 129     174.628  20.095 -83.720  1.00146.55           C  
ATOM   8542  NZ  LYS D 129     173.909  20.322 -85.010  1.00145.92           N  
ATOM   8543  N   VAL D 130     173.586  13.768 -85.673  1.00145.19           N  
ATOM   8544  CA  VAL D 130     173.724  12.378 -86.148  1.00145.57           C  
ATOM   8545  C   VAL D 130     174.246  12.356 -87.592  1.00143.74           C  
ATOM   8546  O   VAL D 130     174.897  11.394 -88.018  1.00136.44           O  
ATOM   8547  CB  VAL D 130     172.389  11.601 -86.069  1.00147.71           C  
ATOM   8548  CG1 VAL D 130     172.527  10.211 -86.693  1.00149.27           C  
ATOM   8549  CG2 VAL D 130     171.927  11.491 -84.625  1.00150.01           C  
ATOM   8550  N   GLN D 131     173.938  13.418 -88.337  1.00142.75           N  
ATOM   8551  CA  GLN D 131     174.576  13.706 -89.624  1.00137.66           C  
ATOM   8552  C   GLN D 131     176.102  13.682 -89.484  1.00133.71           C  
ATOM   8553  O   GLN D 131     176.789  12.928 -90.180  1.00128.46           O  
ATOM   8554  CB  GLN D 131     174.133  15.092 -90.118  1.00137.75           C  
ATOM   8555  CG  GLN D 131     174.580  15.462 -91.529  1.00138.06           C  
ATOM   8556  CD  GLN D 131     173.634  14.969 -92.611  1.00137.52           C  
ATOM   8557  OE1 GLN D 131     173.804  15.293 -93.787  1.00137.43           O  
ATOM   8558  NE2 GLN D 131     172.633  14.184 -92.223  1.00141.52           N  
ATOM   8559  N   HIS D 132     176.612  14.496 -88.559  1.00130.99           N  
ATOM   8560  CA  HIS D 132     178.051  14.680 -88.381  1.00128.13           C  
ATOM   8561  C   HIS D 132     178.738  13.469 -87.771  1.00125.79           C  
ATOM   8562  O   HIS D 132     179.952  13.336 -87.881  1.00121.99           O  
ATOM   8563  CB  HIS D 132     178.333  15.933 -87.555  1.00128.45           C  
ATOM   8564  CG  HIS D 132     178.035  17.201 -88.288  1.00129.44           C  
ATOM   8565  ND1 HIS D 132     176.755  17.686 -88.443  1.00133.23           N  
ATOM   8566  CD2 HIS D 132     178.848  18.070 -88.934  1.00129.84           C  
ATOM   8567  CE1 HIS D 132     176.793  18.807 -89.140  1.00130.84           C  
ATOM   8568  NE2 HIS D 132     178.051  19.063 -89.450  1.00130.34           N  
ATOM   8569  N   ILE D 133     177.971  12.591 -87.130  1.00126.31           N  
ATOM   8570  CA  ILE D 133     178.492  11.279 -86.737  1.00122.88           C  
ATOM   8571  C   ILE D 133     178.802  10.490 -88.000  1.00124.59           C  
ATOM   8572  O   ILE D 133     179.929  10.039 -88.199  1.00120.10           O  
ATOM   8573  CB  ILE D 133     177.507  10.467 -85.843  1.00121.66           C  
ATOM   8574  CG1 ILE D 133     177.769  10.738 -84.362  1.00121.60           C  
ATOM   8575  CG2 ILE D 133     177.661   8.971 -86.073  1.00122.71           C  
ATOM   8576  CD1 ILE D 133     177.495  12.164 -83.937  1.00117.02           C  
ATOM   8577  N   GLN D 134     177.799  10.351 -88.862  1.00125.73           N  
ATOM   8578  CA  GLN D 134     177.954   9.576 -90.089  1.00123.82           C  
ATOM   8579  C   GLN D 134     178.876  10.266 -91.104  1.00123.12           C  
ATOM   8580  O   GLN D 134     179.612   9.592 -91.829  1.00121.56           O  
ATOM   8581  CB  GLN D 134     176.583   9.231 -90.685  1.00124.50           C  
ATOM   8582  CG  GLN D 134     175.915   8.034 -89.990  1.00124.17           C  
ATOM   8583  CD  GLN D 134     174.427   8.224 -89.775  1.00123.27           C  
ATOM   8584  OE1 GLN D 134     173.929   8.081 -88.656  1.00121.98           O  
ATOM   8585  NE2 GLN D 134     173.710   8.558 -90.842  1.00125.64           N  
ATOM   8586  N   LEU D 135     178.855  11.599 -91.141  1.00119.75           N  
ATOM   8587  CA  LEU D 135     179.811  12.363 -91.951  1.00116.16           C  
ATOM   8588  C   LEU D 135     181.231  11.975 -91.555  1.00112.64           C  
ATOM   8589  O   LEU D 135     182.016  11.486 -92.372  1.00111.55           O  
ATOM   8590  CB  LEU D 135     179.612  13.872 -91.742  1.00117.66           C  
ATOM   8591  CG  LEU D 135     180.501  14.889 -92.479  1.00118.67           C  
ATOM   8592  CD1 LEU D 135     180.100  16.297 -92.068  1.00117.55           C  
ATOM   8593  CD2 LEU D 135     181.988  14.696 -92.230  1.00119.44           C  
ATOM   8594  N   LEU D 136     181.551  12.186 -90.286  1.00112.58           N  
ATOM   8595  CA  LEU D 136     182.887  11.912 -89.792  1.00109.77           C  
ATOM   8596  C   LEU D 136     183.182  10.414 -89.942  1.00111.43           C  
ATOM   8597  O   LEU D 136     184.266  10.052 -90.394  1.00107.71           O  
ATOM   8598  CB  LEU D 136     183.051  12.404 -88.344  1.00107.70           C  
ATOM   8599  CG  LEU D 136     183.188  13.926 -88.084  1.00104.98           C  
ATOM   8600  CD1 LEU D 136     184.639  14.374 -88.091  1.00102.11           C  
ATOM   8601  CD2 LEU D 136     182.385  14.795 -89.054  1.00102.01           C  
ATOM   8602  N   GLN D 137     182.213   9.557 -89.609  1.00111.93           N  
ATOM   8603  CA  GLN D 137     182.322   8.102 -89.850  1.00113.66           C  
ATOM   8604  C   GLN D 137     182.920   7.764 -91.214  1.00111.91           C  
ATOM   8605  O   GLN D 137     183.678   6.802 -91.353  1.00108.77           O  
ATOM   8606  CB  GLN D 137     180.950   7.424 -89.780  1.00115.01           C  
ATOM   8607  CG  GLN D 137     180.493   6.982 -88.401  1.00116.31           C  
ATOM   8608  CD  GLN D 137     179.075   6.422 -88.402  1.00117.18           C  
ATOM   8609  OE1 GLN D 137     178.424   6.358 -87.363  1.00117.53           O  
ATOM   8610  NE2 GLN D 137     178.593   6.017 -89.573  1.00122.52           N  
ATOM   8611  N   LYS D 138     182.543   8.537 -92.227  1.00115.32           N  
ATOM   8612  CA  LYS D 138     183.050   8.319 -93.575  1.00114.49           C  
ATOM   8613  C   LYS D 138     184.478   8.838 -93.701  1.00110.75           C  
ATOM   8614  O   LYS D 138     185.342   8.167 -94.272  1.00108.93           O  
ATOM   8615  CB  LYS D 138     182.136   8.995 -94.608  1.00118.16           C  
ATOM   8616  CG  LYS D 138     182.441   8.653 -96.073  1.00121.61           C  
ATOM   8617  CD  LYS D 138     182.485   7.145 -96.364  1.00123.46           C  
ATOM   8618  CE  LYS D 138     181.170   6.441 -96.019  1.00124.47           C  
ATOM   8619  NZ  LYS D 138     181.008   6.099 -94.566  1.00126.79           N  
ATOM   8620  N   ASN D 139     184.721  10.030 -93.159  1.00106.36           N  
ATOM   8621  CA  ASN D 139     186.054  10.623 -93.187  1.00103.66           C  
ATOM   8622  C   ASN D 139     187.076   9.761 -92.484  1.00101.23           C  
ATOM   8623  O   ASN D 139     188.261   9.834 -92.793  1.00 97.54           O  
ATOM   8624  CB  ASN D 139     186.045  12.010 -92.555  1.00102.67           C  
ATOM   8625  CG  ASN D 139     185.621  13.081 -93.527  1.00101.70           C  
ATOM   8626  OD1 ASN D 139     185.644  12.877 -94.738  1.00104.18           O  
ATOM   8627  ND2 ASN D 139     185.232  14.235 -93.004  1.00 99.75           N  
ATOM   8628  N   VAL D 140     186.607   8.952 -91.538  1.00103.36           N  
ATOM   8629  CA  VAL D 140     187.469   7.993 -90.854  1.00104.14           C  
ATOM   8630  C   VAL D 140     187.631   6.715 -91.664  1.00106.72           C  
ATOM   8631  O   VAL D 140     188.727   6.157 -91.713  1.00102.26           O  
ATOM   8632  CB  VAL D 140     186.967   7.641 -89.436  1.00104.56           C  
ATOM   8633  CG1 VAL D 140     186.775   8.910 -88.624  1.00105.22           C  
ATOM   8634  CG2 VAL D 140     185.688   6.804 -89.483  1.00105.20           C  
ATOM   8635  N   ARG D 141     186.559   6.243 -92.297  1.00104.06           N  
ATOM   8636  CA  ARG D 141     186.682   5.099 -93.195  1.00101.46           C  
ATOM   8637  C   ARG D 141     187.696   5.443 -94.290  1.00 98.70           C  
ATOM   8638  O   ARG D 141     188.508   4.600 -94.662  1.00 96.48           O  
ATOM   8639  CB  ARG D 141     185.332   4.728 -93.810  1.00102.27           C  
ATOM   8640  CG  ARG D 141     185.377   3.492 -94.712  1.00103.07           C  
ATOM   8641  CD  ARG D 141     184.504   3.662 -95.948  1.00105.00           C  
ATOM   8642  NE  ARG D 141     183.086   3.493 -95.638  1.00108.00           N  
ATOM   8643  CZ  ARG D 141     182.451   2.322 -95.583  1.00111.94           C  
ATOM   8644  NH1 ARG D 141     183.094   1.180 -95.813  1.00113.05           N  
ATOM   8645  NH2 ARG D 141     181.155   2.289 -95.290  1.00113.47           N  
ATOM   8646  N   ALA D 142     187.652   6.686 -94.777  1.00100.69           N  
ATOM   8647  CA  ALA D 142     188.595   7.181 -95.794  1.00 97.45           C  
ATOM   8648  C   ALA D 142     190.045   7.351 -95.278  1.00 91.85           C  
ATOM   8649  O   ALA D 142     191.010   7.163 -96.030  1.00 94.91           O  
ATOM   8650  CB  ALA D 142     188.082   8.498 -96.381  1.00103.12           C  
ATOM   8651  N   GLN D 143     190.187   7.710 -94.005  1.00 87.04           N  
ATOM   8652  CA  GLN D 143     191.501   7.868 -93.375  1.00 85.10           C  
ATOM   8653  C   GLN D 143     192.070   6.552 -92.842  1.00 85.88           C  
ATOM   8654  O   GLN D 143     193.266   6.329 -92.947  1.00 84.76           O  
ATOM   8655  CB  GLN D 143     191.437   8.909 -92.248  1.00 82.92           C  
ATOM   8656  CG  GLN D 143     192.591   8.849 -91.239  1.00 80.75           C  
ATOM   8657  CD  GLN D 143     192.578   9.997 -90.238  1.00 78.20           C  
ATOM   8658  OE1 GLN D 143     193.058   9.861 -89.107  1.00 76.68           O  
ATOM   8659  NE2 GLN D 143     192.033  11.134 -90.649  1.00 78.77           N  
ATOM   8660  N   LEU D 144     191.231   5.692 -92.266  1.00 88.92           N  
ATOM   8661  CA  LEU D 144     191.704   4.437 -91.636  1.00 86.74           C  
ATOM   8662  C   LEU D 144     192.499   3.528 -92.580  1.00 88.03           C  
ATOM   8663  O   LEU D 144     193.512   2.945 -92.180  1.00 84.70           O  
ATOM   8664  CB  LEU D 144     190.529   3.643 -91.038  1.00 86.38           C  
ATOM   8665  CG  LEU D 144     190.766   2.188 -90.591  1.00 86.74           C  
ATOM   8666  CD1 LEU D 144     191.968   2.056 -89.661  1.00 85.46           C  
ATOM   8667  CD2 LEU D 144     189.504   1.624 -89.935  1.00 88.66           C  
ATOM   8668  N   VAL D 145     192.028   3.396 -93.818  1.00 89.47           N  
ATOM   8669  CA  VAL D 145     192.694   2.552 -94.818  1.00 86.70           C  
ATOM   8670  C   VAL D 145     193.915   3.253 -95.419  1.00 85.03           C  
ATOM   8671  O   VAL D 145     194.921   2.609 -95.709  1.00 82.11           O  
ATOM   8672  CB  VAL D 145     191.725   2.133 -95.951  1.00 86.73           C  
ATOM   8673  CG1 VAL D 145     191.479   3.295 -96.928  1.00 88.19           C  
ATOM   8674  CG2 VAL D 145     192.265   0.904 -96.674  1.00 88.11           C  
ATOM   8675  N   ASP D 146     193.812   4.568 -95.608  1.00 82.02           N  
ATOM   8676  CA  ASP D 146     194.922   5.381 -96.100  1.00 81.70           C  
ATOM   8677  C   ASP D 146     196.165   5.211 -95.217  1.00 77.49           C  
ATOM   8678  O   ASP D 146     197.272   5.010 -95.729  1.00 75.12           O  
ATOM   8679  CB  ASP D 146     194.497   6.852 -96.165  1.00 84.33           C  
ATOM   8680  CG  ASP D 146     195.655   7.792 -96.423  1.00 88.52           C  
ATOM   8681  OD1 ASP D 146     196.575   7.433 -97.197  1.00 92.04           O  
ATOM   8682  OD2 ASP D 146     195.637   8.900 -95.849  1.00 85.41           O  
ATOM   8683  N   MET D 147     195.972   5.286 -93.900  1.00 76.36           N  
ATOM   8684  CA  MET D 147     197.056   5.055 -92.939  1.00 76.08           C  
ATOM   8685  C   MET D 147     197.530   3.615 -93.015  1.00 76.93           C  
ATOM   8686  O   MET D 147     198.722   3.353 -92.893  1.00 78.57           O  
ATOM   8687  CB  MET D 147     196.627   5.378 -91.501  1.00 75.25           C  
ATOM   8688  CG  MET D 147     196.621   6.872 -91.150  1.00 73.46           C  
ATOM   8689  SD  MET D 147     198.248   7.619 -90.899  1.00 71.38           S  
ATOM   8690  CE  MET D 147     198.911   6.599 -89.575  1.00 67.95           C  
ATOM   8691  N   LYS D 148     196.601   2.683 -93.211  1.00 77.64           N  
ATOM   8692  CA  LYS D 148     196.977   1.301 -93.500  1.00 75.69           C  
ATOM   8693  C   LYS D 148     197.892   1.298 -94.723  1.00 74.57           C  
ATOM   8694  O   LYS D 148     198.980   0.711 -94.703  1.00 72.45           O  
ATOM   8695  CB  LYS D 148     195.741   0.439 -93.765  1.00 74.57           C  
ATOM   8696  CG  LYS D 148     195.969  -1.046 -93.593  1.00 73.61           C  
ATOM   8697  CD  LYS D 148     194.748  -1.829 -94.050  1.00 73.77           C  
ATOM   8698  CE  LYS D 148     194.644  -3.177 -93.349  1.00 74.49           C  
ATOM   8699  NZ  LYS D 148     195.831  -4.041 -93.578  1.00 75.57           N  
ATOM   8700  N   ARG D 149     197.448   1.988 -95.772  1.00 77.38           N  
ATOM   8701  CA  ARG D 149     198.181   2.050 -97.039  1.00 74.14           C  
ATOM   8702  C   ARG D 149     199.532   2.753 -96.932  1.00 70.25           C  
ATOM   8703  O   ARG D 149     200.499   2.319 -97.565  1.00 69.61           O  
ATOM   8704  CB  ARG D 149     197.317   2.667 -98.156  1.00 73.55           C  
ATOM   8705  CG  ARG D 149     196.730   1.602 -99.078  1.00 72.44           C  
ATOM   8706  CD  ARG D 149     195.460   2.027 -99.785  1.00 71.99           C  
ATOM   8707  NE  ARG D 149     194.869   0.882-100.484  1.00 70.49           N  
ATOM   8708  CZ  ARG D 149     193.697   0.895-101.115  1.00 71.85           C  
ATOM   8709  NH1 ARG D 149     192.964   2.004-101.149  1.00 70.90           N  
ATOM   8710  NH2 ARG D 149     193.254  -0.205-101.720  1.00 66.16           N  
ATOM   8711  N   LEU D 150     199.604   3.819 -96.136  1.00 69.80           N  
ATOM   8712  CA  LEU D 150     200.885   4.489 -95.896  1.00 69.62           C  
ATOM   8713  C   LEU D 150     201.797   3.701 -94.966  1.00 68.52           C  
ATOM   8714  O   LEU D 150     203.015   3.881 -95.005  1.00 62.83           O  
ATOM   8715  CB  LEU D 150     200.707   5.913 -95.362  1.00 71.55           C  
ATOM   8716  CG  LEU D 150     200.942   6.963 -96.442  1.00 73.54           C  
ATOM   8717  CD1 LEU D 150     199.824   6.873 -97.494  1.00 74.82           C  
ATOM   8718  CD2 LEU D 150     201.042   8.349 -95.828  1.00 69.43           C  
ATOM   8719  N   GLU D 151     201.213   2.831 -94.143  1.00 74.08           N  
ATOM   8720  CA  GLU D 151     201.995   2.011 -93.218  1.00 78.10           C  
ATOM   8721  C   GLU D 151     202.831   0.973 -93.964  1.00 77.12           C  
ATOM   8722  O   GLU D 151     204.010   0.792 -93.651  1.00 74.38           O  
ATOM   8723  CB  GLU D 151     201.087   1.311 -92.200  1.00 82.88           C  
ATOM   8724  CG  GLU D 151     201.817   0.558 -91.074  1.00 86.34           C  
ATOM   8725  CD  GLU D 151     202.065   1.414 -89.844  1.00 91.42           C  
ATOM   8726  OE1 GLU D 151     203.010   2.234 -89.864  1.00 93.66           O  
ATOM   8727  OE2 GLU D 151     201.319   1.254 -88.853  1.00 92.28           O  
ATOM   8728  N   VAL D 152     202.233   0.282 -94.934  1.00 75.21           N  
ATOM   8729  CA  VAL D 152     203.000  -0.691 -95.722  1.00 71.80           C  
ATOM   8730  C   VAL D 152     203.733  -0.018 -96.889  1.00 69.74           C  
ATOM   8731  O   VAL D 152     204.873  -0.379 -97.169  1.00 68.63           O  
ATOM   8732  CB  VAL D 152     202.150  -1.886 -96.210  1.00 72.86           C  
ATOM   8733  CG1 VAL D 152     201.211  -1.470 -97.321  1.00 72.13           C  
ATOM   8734  CG2 VAL D 152     203.066  -3.030 -96.658  1.00 70.47           C  
ATOM   8735  N   ASP D 153     203.094   0.952 -97.551  1.00 65.24           N  
ATOM   8736  CA  ASP D 153     203.783   1.823 -98.513  1.00 69.18           C  
ATOM   8737  C   ASP D 153     205.174   2.165 -98.007  1.00 70.11           C  
ATOM   8738  O   ASP D 153     206.136   2.167 -98.772  1.00 74.29           O  
ATOM   8739  CB  ASP D 153     202.984   3.124 -98.737  1.00 71.89           C  
ATOM   8740  CG  ASP D 153     203.843   4.299 -99.267  1.00 76.45           C  
ATOM   8741  OD1 ASP D 153     203.553   4.786-100.382  1.00 80.29           O  
ATOM   8742  OD2 ASP D 153     204.779   4.762 -98.567  1.00 71.29           O  
ATOM   8743  N   ILE D 154     205.273   2.467 -96.718  1.00 62.65           N  
ATOM   8744  CA  ILE D 154     206.550   2.820 -96.106  1.00 60.78           C  
ATOM   8745  C   ILE D 154     207.428   1.611 -95.754  1.00 60.45           C  
ATOM   8746  O   ILE D 154     208.645   1.682 -95.889  1.00 64.96           O  
ATOM   8747  CB  ILE D 154     206.326   3.735 -94.889  1.00 60.76           C  
ATOM   8748  CG1 ILE D 154     206.446   5.192 -95.335  1.00 61.70           C  
ATOM   8749  CG2 ILE D 154     207.306   3.430 -93.774  1.00 58.20           C  
ATOM   8750  CD1 ILE D 154     205.667   6.148 -94.482  1.00 63.02           C  
ATOM   8751  N   ASP D 155     206.827   0.507 -95.322  1.00 64.31           N  
ATOM   8752  CA  ASP D 155     207.584  -0.727 -95.095  1.00 67.87           C  
ATOM   8753  C   ASP D 155     208.407  -1.078 -96.351  1.00 71.48           C  
ATOM   8754  O   ASP D 155     209.573  -1.504 -96.270  1.00 71.88           O  
ATOM   8755  CB  ASP D 155     206.632  -1.872 -94.730  1.00 70.91           C  
ATOM   8756  CG  ASP D 155     207.356  -3.099 -94.185  1.00 74.61           C  
ATOM   8757  OD1 ASP D 155     206.801  -4.215 -94.300  1.00 76.20           O  
ATOM   8758  OD2 ASP D 155     208.471  -2.963 -93.643  1.00 84.31           O  
ATOM   8759  N   ILE D 156     207.783  -0.883 -97.511  1.00 74.44           N  
ATOM   8760  CA  ILE D 156     208.478  -0.937 -98.790  1.00 72.93           C  
ATOM   8761  C   ILE D 156     209.594   0.089 -98.783  1.00 71.72           C  
ATOM   8762  O   ILE D 156     210.772  -0.263 -98.731  1.00 73.92           O  
ATOM   8763  CB  ILE D 156     207.535  -0.582 -99.959  1.00 72.77           C  
ATOM   8764  CG1 ILE D 156     206.604  -1.748-100.268  1.00 73.17           C  
ATOM   8765  CG2 ILE D 156     208.328  -0.175-101.205  1.00 74.88           C  
ATOM   8766  CD1 ILE D 156     205.372  -1.331-101.057  1.00 75.09           C  
ATOM   8767  N   LYS D 157     209.198   1.360 -98.780  1.00 74.97           N  
ATOM   8768  CA  LYS D 157     210.112   2.472 -99.024  1.00 79.06           C  
ATOM   8769  C   LYS D 157     211.252   2.644 -98.010  1.00 78.85           C  
ATOM   8770  O   LYS D 157     212.098   3.516 -98.205  1.00 79.18           O  
ATOM   8771  CB  LYS D 157     209.337   3.782 -99.123  1.00 81.88           C  
ATOM   8772  CG  LYS D 157     208.559   3.952-100.409  1.00 84.75           C  
ATOM   8773  CD  LYS D 157     208.293   5.425-100.632  1.00 89.78           C  
ATOM   8774  CE  LYS D 157     207.188   5.670-101.629  1.00 92.36           C  
ATOM   8775  NZ  LYS D 157     207.029   7.135-101.881  1.00100.85           N  
ATOM   8776  N   ILE D 158     211.270   1.858 -96.930  1.00 75.75           N  
ATOM   8777  CA  ILE D 158     212.455   1.778 -96.071  1.00 77.33           C  
ATOM   8778  C   ILE D 158     213.257   0.577 -96.493  1.00 75.57           C  
ATOM   8779  O   ILE D 158     214.420   0.709 -96.846  1.00 79.05           O  
ATOM   8780  CB  ILE D 158     212.129   1.661 -94.570  1.00 78.04           C  
ATOM   8781  CG1 ILE D 158     211.443   2.942 -94.082  1.00 79.23           C  
ATOM   8782  CG2 ILE D 158     213.416   1.411 -93.756  1.00 73.70           C  
ATOM   8783  CD1 ILE D 158     211.185   2.994 -92.576  1.00 77.40           C  
ATOM   8784  N   ARG D 159     212.637  -0.598 -96.479  1.00 73.36           N  
ATOM   8785  CA  ARG D 159     213.326  -1.785 -96.954  1.00 76.41           C  
ATOM   8786  C   ARG D 159     213.832  -1.547 -98.379  1.00 80.00           C  
ATOM   8787  O   ARG D 159     214.733  -2.241 -98.842  1.00 81.49           O  
ATOM   8788  CB  ARG D 159     212.428  -3.011 -96.907  1.00 77.71           C  
ATOM   8789  CG  ARG D 159     213.215  -4.296 -96.918  1.00 78.42           C  
ATOM   8790  CD  ARG D 159     212.325  -5.518 -96.920  1.00 80.42           C  
ATOM   8791  NE  ARG D 159     211.626  -5.715 -95.645  1.00 85.57           N  
ATOM   8792  CZ  ARG D 159     210.403  -5.261 -95.349  1.00 90.14           C  
ATOM   8793  NH1 ARG D 159     209.694  -4.559 -96.237  1.00 89.80           N  
ATOM   8794  NH2 ARG D 159     209.883  -5.508 -94.146  1.00 89.18           N  
ATOM   8795  N   SER D 160     213.249  -0.552 -99.054  1.00 80.46           N  
ATOM   8796  CA  SER D 160     213.700  -0.083-100.370  1.00 83.29           C  
ATOM   8797  C   SER D 160     215.129   0.489-100.394  1.00 84.72           C  
ATOM   8798  O   SER D 160     215.748   0.555-101.461  1.00 82.70           O  
ATOM   8799  CB  SER D 160     212.715   0.971-100.893  1.00 82.64           C  
ATOM   8800  OG  SER D 160     213.097   1.475-102.156  1.00 81.98           O  
ATOM   8801  N   CYS D 161     215.638   0.897 -99.228  1.00 88.12           N  
ATOM   8802  CA  CYS D 161     216.941   1.585 -99.100  1.00 91.03           C  
ATOM   8803  C   CYS D 161     218.038   0.733 -98.497  1.00 87.90           C  
ATOM   8804  O   CYS D 161     219.147   1.215 -98.259  1.00 89.19           O  
ATOM   8805  CB  CYS D 161     216.789   2.799 -98.209  1.00 94.74           C  
ATOM   8806  SG  CYS D 161     215.307   3.674 -98.548  1.00101.06           S  
ATOM   8807  N   ARG D 162     217.715  -0.526 -98.233  1.00 87.63           N  
ATOM   8808  CA  ARG D 162     218.703  -1.516 -97.839  1.00 87.08           C  
ATOM   8809  C   ARG D 162     219.806  -1.650 -98.912  1.00 87.10           C  
ATOM   8810  O   ARG D 162     220.884  -2.183 -98.629  1.00 89.57           O  
ATOM   8811  CB  ARG D 162     218.000  -2.856 -97.606  1.00 89.23           C  
ATOM   8812  CG  ARG D 162     218.782  -3.844 -96.799  1.00 91.24           C  
ATOM   8813  CD  ARG D 162     218.017  -5.145 -96.672  1.00 93.55           C  
ATOM   8814  NE  ARG D 162     218.835  -6.165 -96.021  1.00 97.53           N  
ATOM   8815  CZ  ARG D 162     219.814  -6.850 -96.614  1.00102.52           C  
ATOM   8816  NH1 ARG D 162     220.116  -6.649 -97.896  1.00103.30           N  
ATOM   8817  NH2 ARG D 162     220.501  -7.750 -95.915  1.00103.62           N  
ATOM   8818  N   GLY D 163     219.530  -1.168-100.132  1.00 80.49           N  
ATOM   8819  CA  GLY D 163     220.498  -1.170-101.224  1.00 85.16           C  
ATOM   8820  C   GLY D 163     220.885   0.205-101.735  1.00 86.34           C  
ATOM   8821  O   GLY D 163     221.510   0.312-102.790  1.00 86.48           O  
ATOM   8822  N   SER D 164     220.508   1.259-101.015  1.00 86.66           N  
ATOM   8823  CA  SER D 164     221.008   2.605-101.306  1.00 89.79           C  
ATOM   8824  C   SER D 164     221.681   3.204-100.080  1.00 92.17           C  
ATOM   8825  O   SER D 164     222.374   4.222-100.193  1.00 93.50           O  
ATOM   8826  CB  SER D 164     219.877   3.525-101.775  1.00 91.37           C  
ATOM   8827  OG  SER D 164     219.352   3.112-103.028  1.00 97.46           O  
ATOM   8828  N   CYS D 165     221.500   2.551 -98.926  1.00 97.54           N  
ATOM   8829  CA  CYS D 165     221.928   3.090 -97.627  1.00103.52           C  
ATOM   8830  C   CYS D 165     222.733   2.085 -96.790  1.00101.69           C  
ATOM   8831  O   CYS D 165     222.577   0.868 -96.929  1.00100.43           O  
ATOM   8832  CB  CYS D 165     220.709   3.565 -96.815  1.00108.08           C  
ATOM   8833  SG  CYS D 165     219.781   4.973 -97.534  1.00113.55           S  
ATOM   8834  N   SER D 166     223.578   2.629 -95.912  1.00105.06           N  
ATOM   8835  CA  SER D 166     224.438   1.851 -95.017  1.00104.97           C  
ATOM   8836  C   SER D 166     223.644   0.818 -94.236  1.00104.67           C  
ATOM   8837  O   SER D 166     223.942  -0.378 -94.263  1.00103.17           O  
ATOM   8838  CB  SER D 166     225.131   2.793 -94.025  1.00104.40           C  
ATOM   8839  OG  SER D 166     224.180   3.577 -93.317  1.00102.68           O  
ATOM   8840  N   ARG D 167     222.622   1.302 -93.544  1.00107.69           N  
ATOM   8841  CA  ARG D 167     221.835   0.476 -92.660  1.00110.94           C  
ATOM   8842  C   ARG D 167     220.360   0.701 -92.942  1.00108.77           C  
ATOM   8843  O   ARG D 167     219.915   1.844 -93.068  1.00106.83           O  
ATOM   8844  CB  ARG D 167     222.160   0.842 -91.221  1.00116.55           C  
ATOM   8845  CG  ARG D 167     221.805  -0.227 -90.225  1.00120.25           C  
ATOM   8846  CD  ARG D 167     222.098   0.228 -88.800  1.00122.65           C  
ATOM   8847  NE  ARG D 167     221.201  -0.413 -87.842  1.00124.84           N  
ATOM   8848  CZ  ARG D 167     219.911  -0.109 -87.684  1.00127.30           C  
ATOM   8849  NH1 ARG D 167     219.331   0.840 -88.421  1.00127.55           N  
ATOM   8850  NH2 ARG D 167     219.188  -0.763 -86.781  1.00128.64           N  
ATOM   8851  N   ALA D 168     219.617  -0.396 -93.057  1.00110.03           N  
ATOM   8852  CA  ALA D 168     218.181  -0.351 -93.311  1.00108.96           C  
ATOM   8853  C   ALA D 168     217.468  -0.801 -92.059  1.00109.21           C  
ATOM   8854  O   ALA D 168     217.795  -1.857 -91.517  1.00109.81           O  
ATOM   8855  CB  ALA D 168     217.821  -1.257 -94.464  1.00110.75           C  
ATOM   8856  N   LEU D 169     216.490  -0.017 -91.609  1.00106.49           N  
ATOM   8857  CA  LEU D 169     215.817  -0.288 -90.338  1.00104.91           C  
ATOM   8858  C   LEU D 169     214.905  -1.513 -90.475  1.00108.99           C  
ATOM   8859  O   LEU D 169     213.971  -1.505 -91.284  1.00110.16           O  
ATOM   8860  CB  LEU D 169     215.035   0.945 -89.865  1.00101.54           C  
ATOM   8861  CG  LEU D 169     214.792   1.060 -88.356  1.00100.59           C  
ATOM   8