HEADER    HYDROLASE                               10-AUG-17   5OPL              
TITLE     CRYSTAL STRUCTURE OF K25E CN-II MUTANT                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOSOLIC PURINE 5'-NUCLEOTIDASE;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CYTOSOLIC 5'-NUCLEOTIDASE II;                               
COMPND   5 EC: 3.1.3.5;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NT5C2, NT5B, NT5CP, PNT5;                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    NUCLEOTIDASE, RELAPSED LEUKEMIA, HYDROLASE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.KUGLER,A.HNIZDA,P.PACHL,P.REZACOVA                                  
REVDAT   2   20-JUN-18 5OPL    1       JRNL                                     
REVDAT   1   13-JUN-18 5OPL    0                                                
JRNL        AUTH   A.HNIZDA,M.FABRY,T.MORIYAMA,P.PACHL,M.KUGLER,V.BRINSA,       
JRNL        AUTH 2 D.B.ASCHER,W.L.CARROLL,P.NOVAK,M.ZALIOVA,J.TRKA,P.REZACOVA,  
JRNL        AUTH 3 J.J.YANG,V.VEVERKA                                           
JRNL        TITL   RELAPSED ACUTE LYMPHOBLASTIC LEUKEMIA-SPECIFIC MUTATIONS IN  
JRNL        TITL 2 NT5C2 CLUSTER INTO HOTSPOTS DRIVING INTERSUBUNIT             
JRNL        TITL 3 STIMULATION.                                                 
JRNL        REF    LEUKEMIA                      V.  32  1393 2018              
JRNL        REFN                   ESSN 1476-5551                               
JRNL        PMID   29535428                                                     
JRNL        DOI    10.1038/S41375-018-0073-5                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.05                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 65251                          
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1674                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2752                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 54.41                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5030                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 71                           
REMARK   3   BIN FREE R VALUE                    : 0.5440                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3828                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 55                                      
REMARK   3   SOLVENT ATOMS            : 364                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.64000                                              
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : -0.62000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.106         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.102         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.086         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.866         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4076 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3813 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5505 ; 1.529 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8792 ; 0.963 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   491 ; 5.993 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   197 ;30.760 ;23.249       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   697 ;12.876 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;17.137 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   586 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4563 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1001 ; 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):  1923 ; 0.738 ; 1.564       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1922 ; 0.732 ; 1.564       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2414 ; 1.242 ; 2.341       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2415 ; 1.242 ; 2.341       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2152 ; 1.006 ; 1.799       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2152 ; 0.998 ; 1.799       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3086 ; 1.658 ; 2.608       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4963 ; 6.908 ;14.382       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4964 ; 6.907 ;14.392       
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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
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     3        A    14                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.3300  35.8630 -30.6320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1781 T22:   0.2200                                     
REMARK   3      T33:   0.1505 T12:   0.0203                                     
REMARK   3      T13:  -0.0182 T23:   0.0375                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.4833 L22:   6.5972                                     
REMARK   3      L33:   6.3126 L12:   4.4589                                     
REMARK   3      L13:  -4.3274 L23:   0.0316                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2781 S12:   0.1724 S13:   0.5315                       
REMARK   3      S21:  -0.0495 S22:  -0.0833 S23:   0.0434                       
REMARK   3      S31:  -0.5372 S32:  -0.0373 S33:  -0.1948                       
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    15        A    28                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.2950  46.9640 -25.6920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3835 T22:   0.3664                                     
REMARK   3      T33:   0.3860 T12:   0.0085                                     
REMARK   3      T13:  -0.0020 T23:   0.0402                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9486 L22:  15.2383                                     
REMARK   3      L33:   6.5252 L12:   0.2811                                     
REMARK   3      L13:  -4.9368 L23:   4.6488                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1003 S12:  -0.1407 S13:   0.1243                       
REMARK   3      S21:   0.1671 S22:   0.0508 S23:  -0.0795                       
REMARK   3      S31:  -0.0857 S32:   0.1565 S33:  -0.1512                       
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 :   A    29        A    47                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9850  38.6640 -13.2970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1872 T22:   0.2277                                     
REMARK   3      T33:   0.2346 T12:  -0.1200                                     
REMARK   3      T13:   0.0063 T23:   0.0239                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8237 L22:   0.8565                                     
REMARK   3      L33:   3.3000 L12:  -0.9396                                     
REMARK   3      L13:  -1.0891 L23:   1.5733                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1646 S12:   0.1761 S13:   0.6246                       
REMARK   3      S21:  -0.2015 S22:  -0.0356 S23:  -0.1776                       
REMARK   3      S31:  -0.5668 S32:   0.1367 S33:  -0.1291                       
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 :   A    48        A   128                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.8530  20.3230 -22.5050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0177 T22:   0.1187                                     
REMARK   3      T33:   0.0444 T12:   0.0036                                     
REMARK   3      T13:  -0.0140 T23:   0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3828 L22:   0.5962                                     
REMARK   3      L33:   0.7605 L12:   0.4194                                     
REMARK   3      L13:   0.0751 L23:   0.0707                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0571 S12:   0.0898 S13:  -0.0537                       
REMARK   3      S21:  -0.0972 S22:   0.0359 S23:   0.0563                       
REMARK   3      S31:  -0.0048 S32:  -0.0595 S33:   0.0212                       
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 :   A   129        A   152                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.3020  20.1680  -5.5070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0853 T22:   0.1195                                     
REMARK   3      T33:   0.0380 T12:  -0.0055                                     
REMARK   3      T13:  -0.0026 T23:   0.0356                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4100 L22:   3.9291                                     
REMARK   3      L33:   8.1926 L12:   0.9542                                     
REMARK   3      L13:  -1.5024 L23:   2.8493                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0066 S12:  -0.1141 S13:   0.1240                       
REMARK   3      S21:   0.2979 S22:  -0.1271 S23:   0.1569                       
REMARK   3      S31:  -0.0807 S32:  -0.2861 S33:   0.1338                       
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 :   A   153        A   209                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.5150  11.8730 -21.6850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0290 T22:   0.1153                                     
REMARK   3      T33:   0.0729 T12:   0.0194                                     
REMARK   3      T13:  -0.0089 T23:  -0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9857 L22:   2.6233                                     
REMARK   3      L33:   1.3906 L12:   0.5685                                     
REMARK   3      L13:  -1.0061 L23:  -0.0648                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0653 S12:   0.1190 S13:  -0.3279                       
REMARK   3      S21:   0.0054 S22:   0.0227 S23:   0.1591                       
REMARK   3      S31:   0.1683 S32:  -0.0145 S33:   0.0425                       
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 :   A   210        A   225                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.0760  16.1290 -35.7110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0642 T22:   0.2324                                     
REMARK   3      T33:   0.1193 T12:  -0.0080                                     
REMARK   3      T13:   0.0199 T23:  -0.0436                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9901 L22:   9.8021                                     
REMARK   3      L33:   1.8478 L12:   1.7233                                     
REMARK   3      L13:  -0.5641 L23:  -1.8341                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1113 S12:   0.2998 S13:  -0.2521                       
REMARK   3      S21:  -0.1871 S22:   0.0722 S23:  -0.0354                       
REMARK   3      S31:   0.1065 S32:   0.0259 S33:   0.0391                       
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 :   A   226        A   289                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3990  25.0260 -29.3350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0400 T22:   0.1424                                     
REMARK   3      T33:   0.0795 T12:  -0.0192                                     
REMARK   3      T13:   0.0389 T23:   0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8757 L22:   0.9679                                     
REMARK   3      L33:   2.6266 L12:   0.2166                                     
REMARK   3      L13:  -0.6786 L23:  -1.2066                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0288 S12:  -0.0301 S13:   0.0500                       
REMARK   3      S21:  -0.0232 S22:   0.0275 S23:  -0.0143                       
REMARK   3      S31:  -0.1472 S32:   0.0194 S33:  -0.0564                       
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 :   A   290        A   307                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.2840   9.4050 -17.1970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1022 T22:   0.1390                                     
REMARK   3      T33:   0.1160 T12:  -0.0510                                     
REMARK   3      T13:   0.0239 T23:   0.0299                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5479 L22:   4.9016                                     
REMARK   3      L33:   6.9748 L12:  -1.7156                                     
REMARK   3      L13:  -3.2633 L23:   2.2493                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2085 S12:   0.1153 S13:  -0.2162                       
REMARK   3      S21:   0.3477 S22:   0.0734 S23:   0.1305                       
REMARK   3      S31:   0.6977 S32:  -0.4866 S33:   0.1351                       
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 :   A   308        A   332                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5960   8.0000 -23.9780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1309 T22:   0.1627                                     
REMARK   3      T33:   0.2011 T12:  -0.0206                                     
REMARK   3      T13:   0.0670 T23:   0.0323                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6710 L22:   5.0082                                     
REMARK   3      L33:   4.9408 L12:  -0.4474                                     
REMARK   3      L13:  -0.5050 L23:  -0.1126                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1524 S12:   0.3039 S13:   0.0687                       
REMARK   3      S21:  -0.3580 S22:   0.0075 S23:  -0.6873                       
REMARK   3      S31:   0.3098 S32:   0.1528 S33:   0.1448                       
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 :   A   333        A   421                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.0290  32.2060 -11.6200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0616 T22:   0.1590                                     
REMARK   3      T33:   0.0873 T12:  -0.0382                                     
REMARK   3      T13:   0.0371 T23:  -0.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4662 L22:   1.7464                                     
REMARK   3      L33:   2.0500 L12:  -0.5956                                     
REMARK   3      L13:   0.2049 L23:   0.0438                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0222 S12:  -0.1667 S13:   0.0767                       
REMARK   3      S21:   0.0668 S22:   0.0143 S23:   0.2815                       
REMARK   3      S31:  -0.2086 S32:  -0.1475 S33:   0.0078                       
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 :   A   422        A   455                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.1990  35.3610 -12.3360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0434 T22:   0.1831                                     
REMARK   3      T33:   0.1433 T12:   0.0525                                     
REMARK   3      T13:  -0.0103 T23:  -0.0291                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3107 L22:   2.3557                                     
REMARK   3      L33:   3.5319 L12:   0.3646                                     
REMARK   3      L13:   1.6461 L23:   0.7126                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0397 S12:  -0.3676 S13:   0.5207                       
REMARK   3      S21:  -0.0605 S22:  -0.1256 S23:   0.4489                       
REMARK   3      S31:  -0.3224 S32:  -0.5124 S33:   0.1653                       
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 :   A   456        A   477                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.7460  36.3430 -15.7690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0712 T22:   0.1256                                     
REMARK   3      T33:   0.0802 T12:  -0.0260                                     
REMARK   3      T13:   0.0403 T23:  -0.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2166 L22:   2.6774                                     
REMARK   3      L33:   6.5343 L12:   0.2262                                     
REMARK   3      L13:  -1.1545 L23:   1.4156                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0983 S12:   0.0042 S13:   0.1161                       
REMARK   3      S21:  -0.2259 S22:   0.0392 S23:  -0.3192                       
REMARK   3      S31:  -0.6229 S32:   0.3799 S33:  -0.1374                       
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 :   A   478        A   488                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.3340  40.9880   4.5960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1840 T22:   0.2126                                     
REMARK   3      T33:   0.2059 T12:  -0.0038                                     
REMARK   3      T13:   0.0456 T23:   0.0305                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0606 L22:   0.9914                                     
REMARK   3      L33:   7.9793 L12:   0.9091                                     
REMARK   3      L13:  -3.9105 L23:  -1.1545                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1539 S12:   0.0150 S13:   0.0150                       
REMARK   3      S21:  -0.0718 S22:  -0.0176 S23:  -0.1230                       
REMARK   3      S31:  -0.4004 S32:  -0.0559 S33:  -0.1363                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 5OPL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200006175.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-FEB-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 300K               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66924                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.050                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.05500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.91                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.46                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.65900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.840                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MOPS/HEPES-NA PH 7.5; 0.02 M OF    
REMARK 280  EACH CARBOXYLIC ACID ; 10% W/V PEG 8000, 20% V/V ETHYLENE GLYCOL    
REMARK 280  G6 MORPHEUS CONDITION, VAPOR DIFFUSION, TEMPERATURE 293K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       46.13100            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       63.78800            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       64.99400            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       46.13100            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       63.78800            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       64.99400            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       46.13100            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       63.78800            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       64.99400            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       46.13100            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       63.78800            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       64.99400            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 20450 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 75630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A1003  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -18                                                      
REMARK 465     GLY A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     GLY A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     VAL A    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     ARG A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLU A   401                                                      
REMARK 465     LEU A   402                                                      
REMARK 465     TYR A   403                                                      
REMARK 465     LYS A   404                                                      
REMARK 465     HIS A   405                                                      
REMARK 465     LEU A   406                                                      
REMARK 465     ASP A   407                                                      
REMARK 465     SER A   408                                                      
REMARK 465     SER A   409                                                      
REMARK 465     SER A   410                                                      
REMARK 465     ASN A   411                                                      
REMARK 465     GLU A   412                                                      
REMARK 465     ARG A   413                                                      
REMARK 465     PRO A   414                                                      
REMARK 465     ASP A   415                                                      
REMARK 465     ILE A   416                                                      
REMARK 465     THR A   489                                                      
REMARK 465     VAL A   490                                                      
REMARK 465     GLU A   491                                                      
REMARK 465     HIS A   492                                                      
REMARK 465     THR A   493                                                      
REMARK 465     HIS A   494                                                      
REMARK 465     VAL A   495                                                      
REMARK 465     ASP A   496                                                      
REMARK 465     ILE A   497                                                      
REMARK 465     ASN A   498                                                      
REMARK 465     GLU A   499                                                      
REMARK 465     MET A   500                                                      
REMARK 465     GLU A   501                                                      
REMARK 465     SER A   502                                                      
REMARK 465     PRO A   503                                                      
REMARK 465     LEU A   504                                                      
REMARK 465     ALA A   505                                                      
REMARK 465     THR A   506                                                      
REMARK 465     ARG A   507                                                      
REMARK 465     ASN A   508                                                      
REMARK 465     ARG A   509                                                      
REMARK 465     THR A   510                                                      
REMARK 465     SER A   511                                                      
REMARK 465     VAL A   512                                                      
REMARK 465     ASP A   513                                                      
REMARK 465     PHE A   514                                                      
REMARK 465     LYS A   515                                                      
REMARK 465     ASP A   516                                                      
REMARK 465     THR A   517                                                      
REMARK 465     ASP A   518                                                      
REMARK 465     TYR A   519                                                      
REMARK 465     LYS A   520                                                      
REMARK 465     ARG A   521                                                      
REMARK 465     HIS A   522                                                      
REMARK 465     GLN A   523                                                      
REMARK 465     LEU A   524                                                      
REMARK 465     THR A   525                                                      
REMARK 465     ARG A   526                                                      
REMARK 465     SER A   527                                                      
REMARK 465     ILE A   528                                                      
REMARK 465     SER A   529                                                      
REMARK 465     GLU A   530                                                      
REMARK 465     ILE A   531                                                      
REMARK 465     LYS A   532                                                      
REMARK 465     PRO A   533                                                      
REMARK 465     PRO A   534                                                      
REMARK 465     ASN A   535                                                      
REMARK 465     LEU A   536                                                      
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   OD2  ASP A    54     O3   GOL A   606              2.18            
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    ASP A  54   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A 277   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 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    MET A  53      -66.59    -91.78                                   
REMARK 500    THR A  56      -72.49   -132.59                                   
REMARK 500    PRO A 267       33.85    -84.43                                   
REMARK 500    PHE A 354      -76.18    -83.91                                   
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                              MG A 610  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  52   OD2                                                    
REMARK 620 2 ASP A  54   O   115.2                                              
REMARK 620 3 ASP A 351   OD1  90.6  78.7                                        
REMARK 620 4 HOH A 736   O    98.8 133.3 134.3                                  
REMARK 620 5 HOH A 770   O   153.0  90.0  84.6  67.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 610                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5OPL   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF K25E CN-II MUTANT                               
DBREF  5OPL A    1   536  UNP    P49902   5NTC_HUMAN       1    536             
SEQADV 5OPL MET A  -18  UNP  P49902              INITIATING METHIONINE          
SEQADV 5OPL GLY A  -17  UNP  P49902              EXPRESSION TAG                 
SEQADV 5OPL SER A  -16  UNP  P49902              EXPRESSION TAG                 
SEQADV 5OPL SER A  -15  UNP  P49902              EXPRESSION TAG                 
SEQADV 5OPL HIS A  -14  UNP  P49902              EXPRESSION TAG                 
SEQADV 5OPL HIS A  -13  UNP  P49902              EXPRESSION TAG                 
SEQADV 5OPL HIS A  -12  UNP  P49902              EXPRESSION TAG                 
SEQADV 5OPL HIS A  -11  UNP  P49902              EXPRESSION TAG                 
SEQADV 5OPL HIS A  -10  UNP  P49902              EXPRESSION TAG                 
SEQADV 5OPL HIS A   -9  UNP  P49902              EXPRESSION TAG                 
SEQADV 5OPL SER A   -8  UNP  P49902              EXPRESSION TAG                 
SEQADV 5OPL SER A   -7  UNP  P49902              EXPRESSION TAG                 
SEQADV 5OPL GLY A   -6  UNP  P49902              EXPRESSION TAG                 
SEQADV 5OPL LEU A   -5  UNP  P49902              EXPRESSION TAG                 
SEQADV 5OPL VAL A   -4  UNP  P49902              EXPRESSION TAG                 
SEQADV 5OPL PRO A   -3  UNP  P49902              EXPRESSION TAG                 
SEQADV 5OPL ARG A   -2  UNP  P49902              EXPRESSION TAG                 
SEQADV 5OPL GLY A   -1  UNP  P49902              EXPRESSION TAG                 
SEQADV 5OPL SER A    0  UNP  P49902              EXPRESSION TAG                 
SEQADV 5OPL GLU A   25  UNP  P49902    LYS    25 ENGINEERED MUTATION            
SEQRES   1 A  555  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  555  LEU VAL PRO ARG GLY SER MET SER THR SER TRP SER ASP          
SEQRES   3 A  555  ARG LEU GLN ASN ALA ALA ASP MET PRO ALA ASN MET ASP          
SEQRES   4 A  555  LYS HIS ALA LEU GLU LYS TYR ARG ARG GLU ALA TYR HIS          
SEQRES   5 A  555  ARG VAL PHE VAL ASN ARG SER LEU ALA MET GLU LYS ILE          
SEQRES   6 A  555  LYS CYS PHE GLY PHE ASP MET ASP TYR THR LEU ALA VAL          
SEQRES   7 A  555  TYR LYS SER PRO GLU TYR GLU SER LEU GLY PHE GLU LEU          
SEQRES   8 A  555  THR VAL GLU ARG LEU VAL SER ILE GLY TYR PRO GLN GLU          
SEQRES   9 A  555  LEU LEU SER PHE ALA TYR ASP SER THR PHE PRO THR ARG          
SEQRES  10 A  555  GLY LEU VAL PHE ASP THR LEU TYR GLY ASN LEU LEU LYS          
SEQRES  11 A  555  VAL ASP ALA TYR GLY ASN LEU LEU VAL CYS ALA HIS GLY          
SEQRES  12 A  555  PHE ASN PHE ILE ARG GLY PRO GLU THR ARG GLU GLN TYR          
SEQRES  13 A  555  PRO ASN LYS PHE ILE GLN ARG ASP ASP THR GLU ARG PHE          
SEQRES  14 A  555  TYR ILE LEU ASN THR LEU PHE ASN LEU PRO GLU THR TYR          
SEQRES  15 A  555  LEU LEU ALA CYS LEU VAL ASP PHE PHE THR ASN CYS PRO          
SEQRES  16 A  555  ARG TYR THR SER CYS GLU THR GLY PHE LYS ASP GLY ASP          
SEQRES  17 A  555  LEU PHE MET SER TYR ARG SER MET PHE GLN ASP VAL ARG          
SEQRES  18 A  555  ASP ALA VAL ASP TRP VAL HIS TYR LYS GLY SER LEU LYS          
SEQRES  19 A  555  GLU LYS THR VAL GLU ASN LEU GLU LYS TYR VAL VAL LYS          
SEQRES  20 A  555  ASP GLY LYS LEU PRO LEU LEU LEU SER ARG MET LYS GLU          
SEQRES  21 A  555  VAL GLY LYS VAL PHE LEU ALA THR ASN SER ASP TYR LYS          
SEQRES  22 A  555  TYR THR ASP LYS ILE MET THR TYR LEU PHE ASP PHE PRO          
SEQRES  23 A  555  HIS GLY PRO LYS PRO GLY SER SER HIS ARG PRO TRP GLN          
SEQRES  24 A  555  SER TYR PHE ASP LEU ILE LEU VAL ASP ALA ARG LYS PRO          
SEQRES  25 A  555  LEU PHE PHE GLY GLU GLY THR VAL LEU ARG GLN VAL ASP          
SEQRES  26 A  555  THR LYS THR GLY LYS LEU LYS ILE GLY THR TYR THR GLY          
SEQRES  27 A  555  PRO LEU GLN HIS GLY ILE VAL TYR SER GLY GLY SER SER          
SEQRES  28 A  555  ASP THR ILE CYS ASP LEU LEU GLY ALA LYS GLY LYS ASP          
SEQRES  29 A  555  ILE LEU TYR ILE GLY ASP HIS ILE PHE GLY ASP ILE LEU          
SEQRES  30 A  555  LYS SER LYS LYS ARG GLN GLY TRP ARG THR PHE LEU VAL          
SEQRES  31 A  555  ILE PRO GLU LEU ALA GLN GLU LEU HIS VAL TRP THR ASP          
SEQRES  32 A  555  LYS SER SER LEU PHE GLU GLU LEU GLN SER LEU ASP ILE          
SEQRES  33 A  555  PHE LEU ALA GLU LEU TYR LYS HIS LEU ASP SER SER SER          
SEQRES  34 A  555  ASN GLU ARG PRO ASP ILE SER SER ILE GLN ARG ARG ILE          
SEQRES  35 A  555  LYS LYS VAL THR HIS ASP MET ASP MET CYS TYR GLY MET          
SEQRES  36 A  555  MET GLY SER LEU PHE ARG SER GLY SER ARG GLN THR LEU          
SEQRES  37 A  555  PHE ALA SER GLN VAL MET ARG TYR ALA ASP LEU TYR ALA          
SEQRES  38 A  555  ALA SER PHE ILE ASN LEU LEU TYR TYR PRO PHE SER TYR          
SEQRES  39 A  555  LEU PHE ARG ALA ALA HIS VAL LEU MET PRO HIS GLU SER          
SEQRES  40 A  555  THR VAL GLU HIS THR HIS VAL ASP ILE ASN GLU MET GLU          
SEQRES  41 A  555  SER PRO LEU ALA THR ARG ASN ARG THR SER VAL ASP PHE          
SEQRES  42 A  555  LYS ASP THR ASP TYR LYS ARG HIS GLN LEU THR ARG SER          
SEQRES  43 A  555  ILE SER GLU ILE LYS PRO PRO ASN LEU                          
HET    GOL  A 601       6                                                       
HET    GOL  A 602       6                                                       
HET    GOL  A 603       6                                                       
HET    GOL  A 604       6                                                       
HET    GOL  A 605       6                                                       
HET    GOL  A 606       6                                                       
HET    GOL  A 607       6                                                       
HET    GOL  A 608       6                                                       
HET    GOL  A 609       6                                                       
HET     MG  A 610       1                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  GOL    9(C3 H8 O3)                                                  
FORMUL  11   MG    MG 2+                                                        
FORMUL  12  HOH   *364(H2 O)                                                    
HELIX    1 AA1 SER A    4  ASP A   14  1                                  11    
HELIX    2 AA2 ASP A   20  ARG A   28  1                                   9    
HELIX    3 AA3 ARG A   29  ARG A   34  5                                   6    
HELIX    4 AA4 GLU A   44  ILE A   46  5                                   3    
HELIX    5 AA5 PRO A   63  ILE A   80  1                                  18    
HELIX    6 AA6 PRO A   83  PHE A   89  5                                   7    
HELIX    7 AA7 ARG A  129  ARG A  134  1                                   6    
HELIX    8 AA8 THR A  155  PHE A  157  5                                   3    
HELIX    9 AA9 ASN A  158  CYS A  175  1                                  18    
HELIX   10 AB1 TYR A  194  LYS A  211  1                                  18    
HELIX   11 AB2 SER A  213  GLU A  220  1                                   8    
HELIX   12 AB3 ASN A  221  VAL A  226  1                                   6    
HELIX   13 AB4 GLY A  230  GLY A  243  1                                  14    
HELIX   14 AB5 ASP A  252  PHE A  264  1                                  13    
HELIX   15 AB6 PRO A  278  PHE A  283  5                                   6    
HELIX   16 AB7 PRO A  293  GLY A  297  5                                   5    
HELIX   17 AB8 SER A  331  GLY A  340  1                                  10    
HELIX   18 AB9 LYS A  342  LYS A  344  5                                   3    
HELIX   19 AC1 ASP A  356  GLY A  365  1                                  10    
HELIX   20 AC2 GLU A  374  LYS A  385  1                                  12    
HELIX   21 AC3 LYS A  385  ALA A  400  1                                  16    
HELIX   22 AC4 SER A  418  CYS A  433  1                                  16    
HELIX   23 AC5 THR A  448  ALA A  458  1                                  11    
HELIX   24 AC6 SER A  464  TYR A  471  5                                   8    
HELIX   25 AC7 MET A  484  SER A  488  5                                   5    
SHEET    1 AA110 PHE A  36  VAL A  37  0                                        
SHEET    2 AA110 LEU A 460  ALA A 462 -1  O  TYR A 461   N  PHE A  36           
SHEET    3 AA110 ARG A 367  VAL A 371  1  N  LEU A 370   O  LEU A 460           
SHEET    4 AA110 ILE A 346  GLY A 350  1  N  TYR A 348   O  ARG A 367           
SHEET    5 AA110 CYS A  48  PHE A  51  1  N  GLY A  50   O  ILE A 349           
SHEET    6 AA110 LYS A 244  ALA A 248  1  O  ALA A 248   N  PHE A  51           
SHEET    7 AA110 LEU A 285  VAL A 288  1  O  LEU A 285   N  LEU A 247           
SHEET    8 AA110 TYR A 327  GLY A 329  1  O  TYR A 327   N  ILE A 286           
SHEET    9 AA110 LEU A 302  ASP A 306 -1  N  ARG A 303   O  SER A 328           
SHEET   10 AA110 LYS A 311  LEU A 312 -1  O  LYS A 311   N  ASP A 306           
SHEET    1 AA2 2 LEU A  41  ALA A  42  0                                        
SHEET    2 AA2 2 LEU A 476  PHE A 477 -1  O  PHE A 477   N  LEU A  41           
SHEET    1 AA3 5 ASN A 126  ILE A 128  0                                        
SHEET    2 AA3 5 LEU A 118  HIS A 123 -1  N  CYS A 121   O  ILE A 128           
SHEET    3 AA3 5 ASN A 108  VAL A 112 -1  N  LYS A 111   O  LEU A 119           
SHEET    4 AA3 5 LEU A 100  ASP A 103 -1  N  VAL A 101   O  LEU A 110           
SHEET    5 AA3 5 PHE A 150  LEU A 153 -1  O  LEU A 153   N  LEU A 100           
SHEET    1 AA4 3 THR A 179  CYS A 181  0                                        
SHEET    2 AA4 3 GLY A 184  ASP A 187 -1  O  GLY A 184   N  CYS A 181           
SHEET    3 AA4 3 LEU A 190  SER A 193 -1  O  LEU A 190   N  ASP A 187           
SHEET    1 AA5 2 ARG A 442  SER A 443  0                                        
SHEET    2 AA5 2 ARG A 446  GLN A 447 -1  O  ARG A 446   N  SER A 443           
LINK         OD2 ASP A  52                MG    MG A 610     1555   1555  2.30  
LINK         O   ASP A  54                MG    MG A 610     1555   1555  2.37  
LINK         OD1 ASP A 351                MG    MG A 610     1555   1555  2.44  
LINK        MG    MG A 610                 O   HOH A 736     1555   1555  2.56  
LINK        MG    MG A 610                 O   HOH A 770     1555   1555  2.70  
CISPEP   1 SER A   62    PRO A   63          0         3.91                     
CISPEP   2 LYS A  292    PRO A  293          0        13.78                     
SITE     1 AC1  4 LEU A  41  ALA A  42  LYS A  45  ARG A 367                    
SITE     1 AC2  9 ASP A 284  LEU A 321  GLN A 322  HIS A 323                    
SITE     2 AC2  9 GLY A 324  ILE A 325  HOH A 715  HOH A 720                    
SITE     3 AC2  9 HOH A 730                                                     
SITE     1 AC3  4 ARG A 144  LYS A 362  GLN A 453  TYR A 457                    
SITE     1 AC4  9 PRO A  96  THR A  97  GLU A 378  TYR A 434                    
SITE     2 AC4  9 GLY A 438  HOH A 702  HOH A 779  HOH A 791                    
SITE     3 AC4  9 HOH A 835                                                     
SITE     1 AC5  6 PHE A 157  ARG A 202  VAL A 205  ASP A 206                    
SITE     2 AC5  6 TYR A 210  HOH A 745                                          
SITE     1 AC6  8 ASP A  54  TYR A  65  HIS A 209  LYS A 215                    
SITE     2 AC6  8 SER A 251  TYR A 255  HOH A 705  HOH A 711                    
SITE     1 AC7  4 ASN A 154  HIS A 352  HOH A 726  HOH A 797                    
SITE     1 AC8  8 PHE A 172  THR A 173  CYS A 175  PRO A 176                    
SITE     2 AC8  8 TYR A 178  THR A 179  SER A 180  HOH A 839                    
SITE     1 AC9  3 TYR A 151  GLN A 199  ARG A 202                               
SITE     1 AD1  6 ASP A  52  ASP A  54  ASP A 351  HIS A 352                    
SITE     2 AD1  6 HOH A 736  HOH A 770                                          
CRYST1   92.262  127.576  129.988  90.00  90.00  90.00 I 2 2 2       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      0.010839  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007838  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007693        0.00000                         
ATOM      1  N   THR A   3      -8.373  37.331 -32.035  1.00 51.30           N  
ATOM      2  CA  THR A   3      -6.931  37.330 -31.607  1.00 47.88           C  
ATOM      3  C   THR A   3      -6.699  36.369 -30.419  1.00 44.11           C  
ATOM      4  O   THR A   3      -7.038  36.670 -29.261  1.00 46.28           O  
ATOM      5  CB  THR A   3      -6.412  38.735 -31.221  1.00 50.28           C  
ATOM      6  OG1 THR A   3      -6.865  39.705 -32.168  1.00 55.76           O  
ATOM      7  CG2 THR A   3      -4.893  38.756 -31.212  1.00 48.50           C  
ATOM      8  N   SER A   4      -6.122  35.213 -30.712  1.00 38.81           N  
ATOM      9  CA  SER A   4      -5.804  34.255 -29.675  1.00 35.24           C  
ATOM     10  C   SER A   4      -4.523  34.659 -28.953  1.00 32.87           C  
ATOM     11  O   SER A   4      -3.770  35.532 -29.411  1.00 32.49           O  
ATOM     12  CB  SER A   4      -5.629  32.865 -30.279  1.00 33.94           C  
ATOM     13  OG  SER A   4      -4.330  32.711 -30.813  1.00 32.29           O  
ATOM     14  N   TRP A   5      -4.271  34.007 -27.825  1.00 31.20           N  
ATOM     15  CA  TRP A   5      -2.993  34.183 -27.124  1.00 30.33           C  
ATOM     16  C   TRP A   5      -1.780  33.837 -28.004  1.00 28.65           C  
ATOM     17  O   TRP A   5      -0.742  34.506 -27.916  1.00 28.73           O  
ATOM     18  CB  TRP A   5      -2.939  33.417 -25.778  1.00 31.00           C  
ATOM     19  CG  TRP A   5      -3.443  31.991 -25.767  1.00 30.52           C  
ATOM     20  CD1 TRP A   5      -4.694  31.575 -25.389  1.00 31.43           C  
ATOM     21  CD2 TRP A   5      -2.701  30.810 -26.078  1.00 30.55           C  
ATOM     22  NE1 TRP A   5      -4.780  30.204 -25.473  1.00 31.60           N  
ATOM     23  CE2 TRP A   5      -3.566  29.712 -25.886  1.00 31.28           C  
ATOM     24  CE3 TRP A   5      -1.383  30.568 -26.521  1.00 31.32           C  
ATOM     25  CZ2 TRP A   5      -3.163  28.385 -26.117  1.00 32.18           C  
ATOM     26  CZ3 TRP A   5      -0.979  29.231 -26.743  1.00 31.62           C  
ATOM     27  CH2 TRP A   5      -1.880  28.172 -26.539  1.00 32.22           C  
ATOM     28  N   SER A   6      -1.920  32.843 -28.880  1.00 27.51           N  
ATOM     29  CA  SER A   6      -0.783  32.440 -29.743  1.00 27.14           C  
ATOM     30  C   SER A   6      -0.548  33.448 -30.869  1.00 27.83           C  
ATOM     31  O   SER A   6       0.610  33.640 -31.261  1.00 27.74           O  
ATOM     32  CB  SER A   6      -0.951  31.024 -30.311  1.00 27.06           C  
ATOM     33  OG  SER A   6      -2.043  30.957 -31.193  1.00 26.27           O  
ATOM     34  N   ASP A   7      -1.628  34.093 -31.360  1.00 29.24           N  
ATOM     35  CA  ASP A   7      -1.518  35.269 -32.273  1.00 31.36           C  
ATOM     36  C   ASP A   7      -0.684  36.406 -31.648  1.00 31.96           C  
ATOM     37  O   ASP A   7       0.192  36.987 -32.296  1.00 33.40           O  
ATOM     38  CB  ASP A   7      -2.896  35.831 -32.653  1.00 33.36           C  
ATOM     39  CG  ASP A   7      -3.739  34.857 -33.454  1.00 34.17           C  
ATOM     40  OD1 ASP A   7      -3.199  33.909 -34.048  1.00 34.03           O  
ATOM     41  OD2 ASP A   7      -4.951  35.052 -33.492  1.00 35.82           O  
ATOM     42  N   ARG A   8      -0.940  36.709 -30.383  1.00 31.77           N  
ATOM     43  CA  ARG A   8      -0.144  37.710 -29.653  1.00 33.05           C  
ATOM     44  C   ARG A   8       1.324  37.280 -29.583  1.00 32.18           C  
ATOM     45  O   ARG A   8       2.223  38.063 -29.894  1.00 33.25           O  
ATOM     46  CB  ARG A   8      -0.652  37.888 -28.220  1.00 34.08           C  
ATOM     47  CG  ARG A   8      -2.120  38.292 -28.107  1.00 35.75           C  
ATOM     48  CD  ARG A   8      -2.312  39.636 -28.751  1.00 38.72           C  
ATOM     49  NE  ARG A   8      -3.583  40.218 -28.386  1.00 41.73           N  
ATOM     50  CZ  ARG A   8      -3.993  41.426 -28.770  1.00 45.27           C  
ATOM     51  NH1 ARG A   8      -3.220  42.195 -29.535  1.00 46.57           N  
ATOM     52  NH2 ARG A   8      -5.185  41.861 -28.385  1.00 48.14           N  
ATOM     53  N   LEU A   9       1.557  36.033 -29.188  1.00 30.45           N  
ATOM     54  CA  LEU A   9       2.932  35.522 -29.049  1.00 30.88           C  
ATOM     55  C   LEU A   9       3.670  35.500 -30.403  1.00 31.34           C  
ATOM     56  O   LEU A   9       4.831  35.948 -30.487  1.00 32.05           O  
ATOM     57  CB  LEU A   9       2.945  34.118 -28.416  1.00 30.24           C  
ATOM     58  CG  LEU A   9       2.518  33.993 -26.927  1.00 30.74           C  
ATOM     59  CD1 LEU A   9       2.405  32.530 -26.532  1.00 30.75           C  
ATOM     60  CD2 LEU A   9       3.469  34.734 -26.015  1.00 33.12           C  
ATOM     61  N   GLN A  10       3.009  34.978 -31.443  1.00 30.88           N  
ATOM     62  CA  GLN A  10       3.617  34.952 -32.806  1.00 32.33           C  
ATOM     63  C   GLN A  10       3.876  36.379 -33.338  1.00 34.16           C  
ATOM     64  O   GLN A  10       4.912  36.611 -33.966  1.00 34.95           O  
ATOM     65  CB  GLN A  10       2.781  34.126 -33.811  1.00 32.69           C  
ATOM     66  CG  GLN A  10       3.437  33.905 -35.183  1.00 34.72           C  
ATOM     67  CD  GLN A  10       4.749  33.139 -35.074  1.00 35.58           C  
ATOM     68  OE1 GLN A  10       4.746  31.941 -34.834  1.00 35.68           O  
ATOM     69  NE2 GLN A  10       5.881  33.841 -35.233  1.00 36.62           N  
ATOM     70  N   ASN A  11       2.961  37.326 -33.077  1.00 34.60           N  
ATOM     71  CA  ASN A  11       3.169  38.739 -33.442  1.00 37.05           C  
ATOM     72  C   ASN A  11       4.443  39.284 -32.790  1.00 37.40           C  
ATOM     73  O   ASN A  11       5.247  39.978 -33.427  1.00 38.93           O  
ATOM     74  CB  ASN A  11       1.983  39.640 -33.012  1.00 38.95           C  
ATOM     75  CG  ASN A  11       0.725  39.434 -33.857  1.00 40.68           C  
ATOM     76  OD1 ASN A  11       0.732  38.757 -34.895  1.00 41.02           O  
ATOM     77  ND2 ASN A  11      -0.382  40.016 -33.394  1.00 42.59           N  
ATOM     78  N   ALA A  12       4.615  38.984 -31.507  1.00 35.82           N  
ATOM     79  CA  ALA A  12       5.838  39.416 -30.796  1.00 37.00           C  
ATOM     80  C   ALA A  12       7.070  38.643 -31.314  1.00 36.42           C  
ATOM     81  O   ALA A  12       8.170  39.196 -31.380  1.00 37.97           O  
ATOM     82  CB  ALA A  12       5.676  39.269 -29.274  1.00 36.97           C  
ATOM     83  N   ALA A  13       6.876  37.367 -31.665  1.00 34.77           N  
ATOM     84  CA  ALA A  13       7.968  36.527 -32.214  1.00 35.65           C  
ATOM     85  C   ALA A  13       8.501  37.063 -33.548  1.00 37.26           C  
ATOM     86  O   ALA A  13       9.699  36.957 -33.832  1.00 39.03           O  
ATOM     87  CB  ALA A  13       7.520  35.088 -32.381  1.00 34.30           C  
ATOM     88  N   ASP A  14       7.626  37.649 -34.359  1.00 37.12           N  
ATOM     89  CA  ASP A  14       8.059  38.173 -35.669  1.00 39.83           C  
ATOM     90  C   ASP A  14       9.008  39.377 -35.580  1.00 41.57           C  
ATOM     91  O   ASP A  14       9.714  39.679 -36.546  1.00 43.72           O  
ATOM     92  CB  ASP A  14       6.835  38.525 -36.530  1.00 40.83           C  
ATOM     93  CG  ASP A  14       5.990  37.308 -36.842  1.00 40.09           C  
ATOM     94  OD1 ASP A  14       6.529  36.170 -36.895  1.00 39.68           O  
ATOM     95  OD2 ASP A  14       4.775  37.482 -37.006  1.00 41.30           O  
ATOM     96  N   MET A  15       9.021  40.071 -34.447  1.00 63.09           N  
ATOM     97  CA  MET A  15       9.910  41.226 -34.277  1.00 59.91           C  
ATOM     98  C   MET A  15      11.351  40.812 -33.936  1.00 55.47           C  
ATOM     99  O   MET A  15      11.559  39.982 -33.054  1.00 53.10           O  
ATOM    100  CB  MET A  15       9.361  42.157 -33.208  1.00 58.96           C  
ATOM    101  CG  MET A  15       8.005  42.737 -33.590  1.00 64.10           C  
ATOM    102  SD  MET A  15       7.083  43.260 -32.132  1.00 64.31           S  
ATOM    103  CE  MET A  15       8.017  44.716 -31.617  1.00 60.59           C  
ATOM    104  N   PRO A  16      12.352  41.405 -34.628  1.00 54.77           N  
ATOM    105  CA  PRO A  16      13.754  41.120 -34.294  1.00 51.75           C  
ATOM    106  C   PRO A  16      14.127  41.787 -32.974  1.00 48.14           C  
ATOM    107  O   PRO A  16      13.504  42.757 -32.571  1.00 47.56           O  
ATOM    108  CB  PRO A  16      14.516  41.758 -35.449  1.00 53.98           C  
ATOM    109  CG  PRO A  16      13.678  42.951 -35.816  1.00 56.07           C  
ATOM    110  CD  PRO A  16      12.245  42.501 -35.621  1.00 57.51           C  
ATOM    111  N   ALA A  17      15.120  41.248 -32.293  1.00 46.27           N  
ATOM    112  CA  ALA A  17      15.540  41.795 -31.016  1.00 44.38           C  
ATOM    113  C   ALA A  17      16.357  43.069 -31.231  1.00 44.36           C  
ATOM    114  O   ALA A  17      17.369  43.038 -31.925  1.00 45.55           O  
ATOM    115  CB  ALA A  17      16.370  40.774 -30.261  1.00 44.28           C  
ATOM    116  N   ASN A  18      15.924  44.175 -30.634  1.00 43.61           N  
ATOM    117  CA  ASN A  18      16.756  45.360 -30.515  1.00 43.82           C  
ATOM    118  C   ASN A  18      17.452  45.262 -29.172  1.00 42.90           C  
ATOM    119  O   ASN A  18      16.819  45.493 -28.136  1.00 42.18           O  
ATOM    120  CB  ASN A  18      15.910  46.628 -30.588  1.00 44.45           C  
ATOM    121  CG  ASN A  18      16.749  47.900 -30.447  1.00 45.63           C  
ATOM    122  OD1 ASN A  18      17.972  47.859 -30.160  1.00 46.15           O  
ATOM    123  ND2 ASN A  18      16.103  49.047 -30.662  1.00 46.93           N  
ATOM    124  N   MET A  19      18.743  44.926 -29.184  1.00 43.74           N  
ATOM    125  CA  MET A  19      19.504  44.689 -27.932  1.00 44.31           C  
ATOM    126  C   MET A  19      20.206  45.943 -27.363  1.00 45.58           C  
ATOM    127  O   MET A  19      20.926  45.854 -26.366  1.00 47.16           O  
ATOM    128  CB  MET A  19      20.489  43.508 -28.107  1.00 46.04           C  
ATOM    129  CG  MET A  19      19.814  42.166 -28.398  1.00 45.36           C  
ATOM    130  SD  MET A  19      18.590  41.706 -27.123  1.00 44.19           S  
ATOM    131  CE  MET A  19      19.670  41.115 -25.814  1.00 47.24           C  
ATOM    132  N   ASP A  20      19.962  47.112 -27.955  1.00 45.58           N  
ATOM    133  CA  ASP A  20      20.327  48.378 -27.313  1.00 47.13           C  
ATOM    134  C   ASP A  20      19.727  48.394 -25.903  1.00 47.05           C  
ATOM    135  O   ASP A  20      18.548  48.142 -25.757  1.00 44.87           O  
ATOM    136  CB  ASP A  20      19.790  49.566 -28.115  1.00 46.97           C  
ATOM    137  CG  ASP A  20      20.018  50.896 -27.415  1.00 48.37           C  
ATOM    138  OD1 ASP A  20      21.117  51.466 -27.546  1.00 50.98           O  
ATOM    139  OD2 ASP A  20      19.088  51.379 -26.725  1.00 47.42           O  
ATOM    140  N   LYS A  21      20.536  48.703 -24.888  1.00 50.39           N  
ATOM    141  CA  LYS A  21      20.088  48.651 -23.474  1.00 51.91           C  
ATOM    142  C   LYS A  21      18.863  49.490 -23.148  1.00 50.72           C  
ATOM    143  O   LYS A  21      18.067  49.080 -22.332  1.00 50.60           O  
ATOM    144  CB  LYS A  21      21.217  49.027 -22.491  1.00 56.49           C  
ATOM    145  CG  LYS A  21      22.194  47.879 -22.226  1.00 59.79           C  
ATOM    146  CD  LYS A  21      23.338  48.267 -21.293  1.00 65.59           C  
ATOM    147  CE  LYS A  21      24.205  47.066 -20.915  1.00 69.84           C  
ATOM    148  NZ  LYS A  21      24.880  46.412 -22.077  1.00 69.92           N  
ATOM    149  N   HIS A  22      18.719  50.655 -23.769  1.00 51.15           N  
ATOM    150  CA  HIS A  22      17.546  51.504 -23.520  1.00 50.95           C  
ATOM    151  C   HIS A  22      16.304  50.999 -24.220  1.00 48.85           C  
ATOM    152  O   HIS A  22      15.195  51.186 -23.716  1.00 48.80           O  
ATOM    153  CB  HIS A  22      17.815  52.945 -23.907  1.00 52.77           C  
ATOM    154  CG  HIS A  22      18.899  53.578 -23.096  1.00 56.54           C  
ATOM    155  ND1 HIS A  22      19.969  54.240 -23.663  1.00 59.33           N  
ATOM    156  CD2 HIS A  22      19.089  53.633 -21.756  1.00 58.86           C  
ATOM    157  CE1 HIS A  22      20.760  54.695 -22.708  1.00 62.71           C  
ATOM    158  NE2 HIS A  22      20.250  54.337 -21.542  1.00 62.63           N  
ATOM    159  N   ALA A  23      16.478  50.384 -25.386  1.00 48.18           N  
ATOM    160  CA  ALA A  23      15.372  49.741 -26.074  1.00 47.51           C  
ATOM    161  C   ALA A  23      14.787  48.630 -25.154  1.00 47.48           C  
ATOM    162  O   ALA A  23      13.569  48.598 -24.905  1.00 47.56           O  
ATOM    163  CB  ALA A  23      15.821  49.192 -27.422  1.00 47.22           C  
ATOM    164  N   LEU A  24      15.666  47.796 -24.590  1.00 48.07           N  
ATOM    165  CA  LEU A  24      15.252  46.728 -23.647  1.00 49.21           C  
ATOM    166  C   LEU A  24      14.489  47.255 -22.421  1.00 51.27           C  
ATOM    167  O   LEU A  24      13.412  46.753 -22.110  1.00 51.22           O  
ATOM    168  CB  LEU A  24      16.471  45.928 -23.163  1.00 50.47           C  
ATOM    169  CG  LEU A  24      17.318  45.211 -24.226  1.00 50.05           C  
ATOM    170  CD1 LEU A  24      18.488  44.496 -23.562  1.00 52.61           C  
ATOM    171  CD2 LEU A  24      16.497  44.264 -25.095  1.00 48.62           C  
ATOM    172  N   GLU A  25      15.072  48.249 -21.740  1.00 53.59           N  
ATOM    173  CA  GLU A  25      14.454  48.939 -20.591  1.00 56.74           C  
ATOM    174  C   GLU A  25      13.025  49.377 -20.889  1.00 56.36           C  
ATOM    175  O   GLU A  25      12.125  49.136 -20.081  1.00 58.24           O  
ATOM    176  CB  GLU A  25      15.243  50.201 -20.193  1.00 59.04           C  
ATOM    177  CG  GLU A  25      16.520  49.957 -19.406  1.00 62.63           C  
ATOM    178  CD  GLU A  25      17.361  51.227 -19.247  1.00 65.70           C  
ATOM    179  OE1 GLU A  25      16.809  52.291 -18.857  1.00 66.90           O  
ATOM    180  OE2 GLU A  25      18.583  51.163 -19.525  1.00 68.10           O  
ATOM    181  N   LYS A  26      12.833  50.029 -22.037  1.00 54.76           N  
ATOM    182  CA  LYS A  26      11.509  50.527 -22.437  1.00 55.47           C  
ATOM    183  C   LYS A  26      10.543  49.363 -22.729  1.00 54.80           C  
ATOM    184  O   LYS A  26       9.381  49.393 -22.310  1.00 55.87           O  
ATOM    185  CB  LYS A  26      11.629  51.439 -23.658  1.00 56.44           C  
ATOM    186  CG  LYS A  26      10.429  52.347 -23.865  1.00 59.93           C  
ATOM    187  CD  LYS A  26      10.711  53.440 -24.902  1.00 61.47           C  
ATOM    188  CE  LYS A  26       9.452  54.217 -25.287  1.00 64.98           C  
ATOM    189  NZ  LYS A  26       8.487  53.381 -26.059  1.00 66.37           N  
ATOM    190  N   TYR A  27      11.053  48.331 -23.411  1.00 52.12           N  
ATOM    191  CA  TYR A  27      10.220  47.199 -23.860  1.00 52.04           C  
ATOM    192  C   TYR A  27       9.567  46.388 -22.719  1.00 53.24           C  
ATOM    193  O   TYR A  27       8.400  46.018 -22.806  1.00 53.89           O  
ATOM    194  CB  TYR A  27      11.049  46.243 -24.719  1.00 49.95           C  
ATOM    195  CG  TYR A  27      10.269  45.484 -25.751  1.00 50.60           C  
ATOM    196  CD1 TYR A  27       9.489  46.164 -26.701  1.00 52.31           C  
ATOM    197  CD2 TYR A  27      10.370  44.102 -25.854  1.00 50.36           C  
ATOM    198  CE1 TYR A  27       8.799  45.483 -27.694  1.00 54.07           C  
ATOM    199  CE2 TYR A  27       9.690  43.405 -26.846  1.00 52.01           C  
ATOM    200  CZ  TYR A  27       8.911  44.097 -27.767  1.00 54.00           C  
ATOM    201  OH  TYR A  27       8.218  43.423 -28.744  1.00 56.54           O  
ATOM    202  N   ARG A  28      10.361  46.113 -21.679  1.00 53.91           N  
ATOM    203  CA  ARG A  28       9.936  45.314 -20.509  1.00 56.83           C  
ATOM    204  C   ARG A  28       9.125  46.102 -19.477  1.00 60.92           C  
ATOM    205  O   ARG A  28       8.792  45.567 -18.423  1.00 63.89           O  
ATOM    206  CB  ARG A  28      11.152  44.675 -19.816  1.00 56.24           C  
ATOM    207  CG  ARG A  28      11.854  45.557 -18.784  1.00 57.11           C  
ATOM    208  CD  ARG A  28      13.314  45.215 -18.675  1.00 56.90           C  
ATOM    209  NE  ARG A  28      14.018  46.047 -17.716  1.00 59.03           N  
ATOM    210  CZ  ARG A  28      15.310  46.394 -17.790  1.00 59.53           C  
ATOM    211  NH1 ARG A  28      16.113  45.986 -18.782  1.00 57.83           N  
ATOM    212  NH2 ARG A  28      15.817  47.181 -16.861  1.00 62.45           N  
ATOM    213  N   ARG A  29       8.858  47.378 -19.728  1.00 60.85           N  
ATOM    214  CA  ARG A  29       7.869  48.108 -18.923  1.00 63.38           C  
ATOM    215  C   ARG A  29       6.470  47.653 -19.352  1.00 62.14           C  
ATOM    216  O   ARG A  29       5.572  47.518 -18.500  1.00 61.81           O  
ATOM    217  CB  ARG A  29       8.012  49.627 -19.072  1.00 69.67           C  
ATOM    218  CG  ARG A  29       9.374  50.172 -18.662  1.00 72.73           C  
ATOM    219  CD  ARG A  29       9.676  50.098 -17.163  1.00 72.03           C  
ATOM    220  NE  ARG A  29      10.922  50.839 -16.907  1.00 76.00           N  
ATOM    221  CZ  ARG A  29      11.086  51.894 -16.094  1.00 79.71           C  
ATOM    222  NH1 ARG A  29      10.095  52.370 -15.328  1.00 80.42           N  
ATOM    223  NH2 ARG A  29      12.294  52.469 -16.020  1.00 82.34           N  
ATOM    224  N   GLU A  30       6.291  47.394 -20.652  1.00 61.91           N  
ATOM    225  CA  GLU A  30       4.996  46.951 -21.151  1.00 61.19           C  
ATOM    226  C   GLU A  30       4.629  45.616 -20.532  1.00 55.31           C  
ATOM    227  O   GLU A  30       5.486  44.723 -20.412  1.00 52.24           O  
ATOM    228  CB  GLU A  30       4.991  46.811 -22.659  1.00 64.46           C  
ATOM    229  CG  GLU A  30       5.167  48.108 -23.381  1.00 70.34           C  
ATOM    230  CD  GLU A  30       5.028  47.903 -24.871  1.00 74.48           C  
ATOM    231  OE1 GLU A  30       3.910  47.515 -25.308  1.00 75.69           O  
ATOM    232  OE2 GLU A  30       6.035  48.120 -25.595  1.00 77.17           O  
ATOM    233  N   ALA A  31       3.358  45.484 -20.154  1.00 52.62           N  
ATOM    234  CA  ALA A  31       2.873  44.302 -19.436  1.00 47.84           C  
ATOM    235  C   ALA A  31       3.141  43.005 -20.216  1.00 44.92           C  
ATOM    236  O   ALA A  31       3.525  42.003 -19.640  1.00 41.45           O  
ATOM    237  CB  ALA A  31       1.380  44.457 -19.131  1.00 48.14           C  
ATOM    238  N   TYR A  32       3.022  43.103 -21.543  1.00 46.75           N  
ATOM    239  CA  TYR A  32       3.095  41.964 -22.482  1.00 45.61           C  
ATOM    240  C   TYR A  32       4.472  41.326 -22.546  1.00 43.17           C  
ATOM    241  O   TYR A  32       4.586  40.119 -22.655  1.00 41.56           O  
ATOM    242  CB  TYR A  32       2.601  42.417 -23.892  1.00 49.47           C  
ATOM    243  CG  TYR A  32       1.322  43.205 -23.747  1.00 51.80           C  
ATOM    244  CD1 TYR A  32       0.253  42.658 -23.026  1.00 50.27           C  
ATOM    245  CD2 TYR A  32       1.208  44.523 -24.193  1.00 55.68           C  
ATOM    246  CE1 TYR A  32      -0.906  43.354 -22.808  1.00 52.03           C  
ATOM    247  CE2 TYR A  32       0.022  45.232 -23.993  1.00 57.81           C  
ATOM    248  CZ  TYR A  32      -1.029  44.631 -23.279  1.00 55.98           C  
ATOM    249  OH  TYR A  32      -2.234  45.249 -23.011  1.00 58.00           O  
ATOM    250  N   HIS A  33       5.502  42.133 -22.381  1.00 43.10           N  
ATOM    251  CA  HIS A  33       6.866  41.682 -22.463  1.00 41.68           C  
ATOM    252  C   HIS A  33       7.541  41.628 -21.117  1.00 39.23           C  
ATOM    253  O   HIS A  33       8.759  41.587 -21.070  1.00 38.70           O  
ATOM    254  CB  HIS A  33       7.613  42.636 -23.386  1.00 44.58           C  
ATOM    255  CG  HIS A  33       6.926  42.847 -24.692  1.00 47.40           C  
ATOM    256  ND1 HIS A  33       6.500  41.803 -25.483  1.00 47.00           N  
ATOM    257  CD2 HIS A  33       6.584  43.979 -25.350  1.00 51.09           C  
ATOM    258  CE1 HIS A  33       5.933  42.279 -26.575  1.00 50.20           C  
ATOM    259  NE2 HIS A  33       5.977  43.597 -26.522  1.00 52.81           N  
ATOM    260  N   ARG A  34       6.762  41.639 -20.028  1.00 37.80           N  
ATOM    261  CA  ARG A  34       7.313  41.645 -18.673  1.00 36.19           C  
ATOM    262  C   ARG A  34       7.477  40.266 -18.117  1.00 32.00           C  
ATOM    263  O   ARG A  34       6.768  39.369 -18.487  1.00 30.66           O  
ATOM    264  CB  ARG A  34       6.399  42.385 -17.694  1.00 38.16           C  
ATOM    265  CG  ARG A  34       6.697  43.854 -17.639  1.00 42.82           C  
ATOM    266  CD  ARG A  34       5.805  44.577 -16.646  1.00 45.17           C  
ATOM    267  NE  ARG A  34       6.181  44.244 -15.266  1.00 45.17           N  
ATOM    268  CZ  ARG A  34       5.467  44.589 -14.184  1.00 47.06           C  
ATOM    269  NH1 ARG A  34       4.320  45.256 -14.310  1.00 48.94           N  
ATOM    270  NH2 ARG A  34       5.893  44.257 -12.968  1.00 46.28           N  
ATOM    271  N   VAL A  35       8.400  40.132 -17.187  1.00 29.88           N  
ATOM    272  CA  VAL A  35       8.477  38.959 -16.341  1.00 27.15           C  
ATOM    273  C   VAL A  35       7.873  39.384 -14.984  1.00 26.35           C  
ATOM    274  O   VAL A  35       8.321  40.365 -14.394  1.00 27.08           O  
ATOM    275  CB  VAL A  35       9.928  38.490 -16.154  1.00 26.58           C  
ATOM    276  CG1 VAL A  35      10.043  37.451 -15.022  1.00 24.73           C  
ATOM    277  CG2 VAL A  35      10.481  37.942 -17.473  1.00 26.93           C  
ATOM    278  N   PHE A  36       6.887  38.624 -14.522  1.00 24.72           N  
ATOM    279  CA  PHE A  36       6.211  38.883 -13.251  1.00 24.25           C  
ATOM    280  C   PHE A  36       6.867  38.082 -12.122  1.00 23.24           C  
ATOM    281  O   PHE A  36       7.312  36.954 -12.337  1.00 22.38           O  
ATOM    282  CB  PHE A  36       4.723  38.592 -13.419  1.00 23.87           C  
ATOM    283  CG  PHE A  36       4.058  39.512 -14.411  1.00 25.31           C  
ATOM    284  CD1 PHE A  36       3.870  40.865 -14.100  1.00 26.70           C  
ATOM    285  CD2 PHE A  36       3.745  39.072 -15.689  1.00 25.68           C  
ATOM    286  CE1 PHE A  36       3.293  41.726 -15.004  1.00 28.65           C  
ATOM    287  CE2 PHE A  36       3.173  39.934 -16.608  1.00 27.71           C  
ATOM    288  CZ  PHE A  36       2.945  41.270 -16.267  1.00 29.24           C  
ATOM    289  N   VAL A  37       6.933  38.678 -10.923  1.00 23.78           N  
ATOM    290  CA  VAL A  37       7.738  38.168  -9.815  1.00 23.26           C  
ATOM    291  C   VAL A  37       6.843  37.863  -8.597  1.00 23.30           C  
ATOM    292  O   VAL A  37       6.261  38.775  -8.014  1.00 23.88           O  
ATOM    293  CB  VAL A  37       8.782  39.213  -9.441  1.00 24.44           C  
ATOM    294  CG1 VAL A  37       9.808  38.674  -8.442  1.00 24.54           C  
ATOM    295  CG2 VAL A  37       9.511  39.746 -10.680  1.00 25.22           C  
ATOM    296  N   ASN A  38       6.765  36.590  -8.220  1.00 22.41           N  
ATOM    297  CA  ASN A  38       6.160  36.199  -6.955  1.00 22.81           C  
ATOM    298  C   ASN A  38       7.120  36.201  -5.790  1.00 23.59           C  
ATOM    299  O   ASN A  38       6.711  36.557  -4.684  1.00 24.12           O  
ATOM    300  CB  ASN A  38       5.492  34.827  -7.077  1.00 22.37           C  
ATOM    301  CG  ASN A  38       4.292  34.872  -7.988  1.00 22.49           C  
ATOM    302  OD1 ASN A  38       3.400  35.681  -7.777  1.00 23.34           O  
ATOM    303  ND2 ASN A  38       4.225  33.985  -8.957  1.00 22.08           N  
ATOM    304  N   ARG A  39       8.383  35.802  -6.020  1.00 23.54           N  
ATOM    305  CA  ARG A  39       9.409  35.847  -4.991  1.00 24.87           C  
ATOM    306  C   ARG A  39      10.662  36.371  -5.647  1.00 25.30           C  
ATOM    307  O   ARG A  39      10.913  36.052  -6.800  1.00 24.51           O  
ATOM    308  CB  ARG A  39       9.667  34.455  -4.372  1.00 25.23           C  
ATOM    309  CG  ARG A  39       8.633  34.027  -3.307  1.00 26.21           C  
ATOM    310  CD  ARG A  39       8.624  32.518  -3.036  1.00 26.68           C  
ATOM    311  NE  ARG A  39       8.280  31.797  -4.254  1.00 25.77           N  
ATOM    312  CZ  ARG A  39       7.056  31.725  -4.781  1.00 25.85           C  
ATOM    313  NH1 ARG A  39       5.984  32.258  -4.167  1.00 26.28           N  
ATOM    314  NH2 ARG A  39       6.869  31.085  -5.934  1.00 25.50           N  
ATOM    315  N   SER A  40      11.421  37.163  -4.903  1.00 26.74           N  
ATOM    316  CA  SER A  40      12.620  37.791  -5.410  1.00 27.51           C  
ATOM    317  C   SER A  40      13.598  36.719  -5.944  1.00 26.99           C  
ATOM    318  O   SER A  40      13.700  35.615  -5.408  1.00 26.22           O  
ATOM    319  CB  SER A  40      13.274  38.640  -4.321  1.00 29.55           C  
ATOM    320  OG  SER A  40      12.414  39.721  -3.971  1.00 31.00           O  
ATOM    321  N   LEU A  41      14.291  37.058  -7.029  1.00 27.27           N  
ATOM    322  CA  LEU A  41      15.202  36.109  -7.670  1.00 27.25           C  
ATOM    323  C   LEU A  41      16.360  36.912  -8.251  1.00 28.61           C  
ATOM    324  O   LEU A  41      16.160  37.785  -9.088  1.00 28.91           O  
ATOM    325  CB  LEU A  41      14.477  35.285  -8.744  1.00 25.98           C  
ATOM    326  CG  LEU A  41      15.269  34.072  -9.290  1.00 25.71           C  
ATOM    327  CD1 LEU A  41      14.338  32.981  -9.737  1.00 25.00           C  
ATOM    328  CD2 LEU A  41      16.214  34.455 -10.441  1.00 26.17           C  
ATOM    329  N   ALA A  42      17.549  36.638  -7.747  1.00 29.95           N  
ATOM    330  CA  ALA A  42      18.781  37.300  -8.187  1.00 31.63           C  
ATOM    331  C   ALA A  42      19.356  36.451  -9.342  1.00 31.65           C  
ATOM    332  O   ALA A  42      19.939  35.348  -9.136  1.00 31.72           O  
ATOM    333  CB  ALA A  42      19.757  37.362  -7.030  1.00 33.09           C  
ATOM    334  N   MET A  43      19.203  36.959 -10.569  1.00 32.77           N  
ATOM    335  CA  MET A  43      19.599  36.188 -11.764  1.00 33.13           C  
ATOM    336  C   MET A  43      21.082  35.862 -11.772  1.00 34.04           C  
ATOM    337  O   MET A  43      21.465  34.859 -12.331  1.00 33.42           O  
ATOM    338  CB  MET A  43      19.251  36.907 -13.065  1.00 34.63           C  
ATOM    339  CG  MET A  43      17.803  36.888 -13.421  1.00 34.39           C  
ATOM    340  SD  MET A  43      17.221  35.256 -13.932  1.00 35.05           S  
ATOM    341  CE  MET A  43      17.900  35.225 -15.590  1.00 35.42           C  
ATOM    342  N   GLU A  44      21.881  36.679 -11.108  1.00 35.57           N  
ATOM    343  CA  GLU A  44      23.312  36.443 -10.946  1.00 38.26           C  
ATOM    344  C   GLU A  44      23.622  35.108 -10.265  1.00 36.99           C  
ATOM    345  O   GLU A  44      24.643  34.519 -10.523  1.00 37.04           O  
ATOM    346  CB  GLU A  44      23.894  37.588 -10.127  1.00 41.63           C  
ATOM    347  CG  GLU A  44      25.385  37.613  -9.978  1.00 46.11           C  
ATOM    348  CD  GLU A  44      25.856  38.899  -9.307  1.00 50.34           C  
ATOM    349  OE1 GLU A  44      25.076  39.467  -8.492  1.00 53.28           O  
ATOM    350  OE2 GLU A  44      26.995  39.330  -9.571  1.00 54.39           O  
ATOM    351  N   LYS A  45      22.740  34.634  -9.392  1.00 35.44           N  
ATOM    352  CA  LYS A  45      22.938  33.329  -8.740  1.00 35.06           C  
ATOM    353  C   LYS A  45      22.537  32.128  -9.599  1.00 32.73           C  
ATOM    354  O   LYS A  45      22.817  30.987  -9.237  1.00 32.52           O  
ATOM    355  CB  LYS A  45      22.180  33.293  -7.404  1.00 35.90           C  
ATOM    356  CG  LYS A  45      22.745  34.256  -6.380  1.00 38.68           C  
ATOM    357  CD  LYS A  45      21.976  34.174  -5.076  1.00 40.04           C  
ATOM    358  CE  LYS A  45      22.310  35.348  -4.174  1.00 43.02           C  
ATOM    359  NZ  LYS A  45      21.300  35.467  -3.089  1.00 43.72           N  
ATOM    360  N   ILE A  46      21.874  32.355 -10.731  1.00 30.69           N  
ATOM    361  CA  ILE A  46      21.465  31.236 -11.560  1.00 29.87           C  
ATOM    362  C   ILE A  46      22.655  30.794 -12.397  1.00 30.83           C  
ATOM    363  O   ILE A  46      23.235  31.607 -13.090  1.00 31.20           O  
ATOM    364  CB  ILE A  46      20.273  31.624 -12.439  1.00 28.70           C  
ATOM    365  CG1 ILE A  46      19.090  32.045 -11.543  1.00 27.80           C  
ATOM    366  CG2 ILE A  46      19.871  30.483 -13.384  1.00 28.34           C  
ATOM    367  CD1 ILE A  46      18.605  30.990 -10.577  1.00 27.85           C  
ATOM    368  N   LYS A  47      23.050  29.534 -12.249  1.00 31.36           N  
ATOM    369  CA  LYS A  47      24.145  28.934 -13.020  1.00 32.63           C  
ATOM    370  C   LYS A  47      23.679  27.997 -14.118  1.00 31.82           C  
ATOM    371  O   LYS A  47      24.467  27.645 -14.982  1.00 32.15           O  
ATOM    372  CB  LYS A  47      25.077  28.146 -12.095  1.00 34.83           C  
ATOM    373  CG  LYS A  47      25.492  28.891 -10.827  1.00 36.46           C  
ATOM    374  CD  LYS A  47      26.091  30.255 -11.115  1.00 37.73           C  
ATOM    375  CE  LYS A  47      26.398  30.967  -9.799  1.00 39.64           C  
ATOM    376  NZ  LYS A  47      26.902  32.329 -10.101  1.00 40.88           N  
ATOM    377  N  ACYS A  48      22.445  27.480 -14.007  0.70 22.21           N  
ATOM    378  N  BCYS A  48      22.377  27.729 -14.163  0.30 22.63           N  
ATOM    379  CA ACYS A  48      21.864  26.633 -15.028  0.70 21.79           C  
ATOM    380  CA BCYS A  48      21.860  26.645 -14.940  0.30 22.43           C  
ATOM    381  C  ACYS A  48      20.462  27.049 -15.375  0.70 21.30           C  
ATOM    382  C  BCYS A  48      20.411  26.917 -15.355  0.30 21.63           C  
ATOM    383  O  ACYS A  48      19.666  27.377 -14.483  0.70 20.90           O  
ATOM    384  O  BCYS A  48      19.539  27.062 -14.491  0.30 21.18           O  
ATOM    385  CB ACYS A  48      21.786  25.183 -14.573  0.70 21.78           C  
ATOM    386  CB BCYS A  48      21.970  25.403 -14.070  0.30 22.78           C  
ATOM    387  SG ACYS A  48      23.316  24.404 -14.052  0.70 22.45           S  
ATOM    388  SG BCYS A  48      21.749  23.854 -14.933  0.30 23.15           S  
ATOM    389  N   PHE A  49      20.149  26.987 -16.667  1.00 21.32           N  
ATOM    390  CA  PHE A  49      18.833  27.227 -17.163  1.00 21.10           C  
ATOM    391  C   PHE A  49      18.284  25.920 -17.753  1.00 20.69           C  
ATOM    392  O   PHE A  49      18.881  25.347 -18.669  1.00 21.27           O  
ATOM    393  CB  PHE A  49      18.871  28.322 -18.221  1.00 21.70           C  
ATOM    394  CG  PHE A  49      19.423  29.631 -17.722  1.00 22.30           C  
ATOM    395  CD1 PHE A  49      20.772  29.904 -17.837  1.00 22.93           C  
ATOM    396  CD2 PHE A  49      18.579  30.621 -17.199  1.00 22.37           C  
ATOM    397  CE1 PHE A  49      21.294  31.116 -17.420  1.00 23.58           C  
ATOM    398  CE2 PHE A  49      19.104  31.851 -16.770  1.00 22.62           C  
ATOM    399  CZ  PHE A  49      20.459  32.088 -16.869  1.00 23.48           C  
ATOM    400  N   GLY A  50      17.156  25.447 -17.232  1.00 19.49           N  
ATOM    401  CA  GLY A  50      16.571  24.216 -17.681  1.00 19.29           C  
ATOM    402  C   GLY A  50      15.216  24.470 -18.320  1.00 18.73           C  
ATOM    403  O   GLY A  50      14.514  25.373 -17.898  1.00 18.32           O  
ATOM    404  N   PHE A  51      14.869  23.627 -19.291  1.00 18.87           N  
ATOM    405  CA  PHE A  51      13.634  23.721 -20.072  1.00 18.61           C  
ATOM    406  C   PHE A  51      12.854  22.424 -20.232  1.00 18.83           C  
ATOM    407  O   PHE A  51      13.426  21.323 -20.374  1.00 18.09           O  
ATOM    408  CB  PHE A  51      13.943  24.193 -21.480  1.00 19.09           C  
ATOM    409  CG  PHE A  51      14.489  25.577 -21.576  1.00 19.38           C  
ATOM    410  CD1 PHE A  51      15.842  25.812 -21.449  1.00 19.93           C  
ATOM    411  CD2 PHE A  51      13.639  26.656 -21.792  1.00 19.10           C  
ATOM    412  CE1 PHE A  51      16.338  27.117 -21.551  1.00 20.29           C  
ATOM    413  CE2 PHE A  51      14.136  27.952 -21.907  1.00 19.33           C  
ATOM    414  CZ  PHE A  51      15.484  28.179 -21.794  1.00 19.76           C  
ATOM    415  N   ASP A  52      11.517  22.590 -20.242  1.00 19.32           N  
ATOM    416  CA  ASP A  52      10.620  21.671 -20.882  1.00 20.70           C  
ATOM    417  C   ASP A  52      10.440  22.091 -22.344  1.00 21.02           C  
ATOM    418  O   ASP A  52      10.768  23.220 -22.719  1.00 21.89           O  
ATOM    419  CB  ASP A  52       9.294  21.699 -20.125  1.00 21.22           C  
ATOM    420  CG  ASP A  52       8.390  20.541 -20.438  1.00 22.76           C  
ATOM    421  OD1 ASP A  52       8.819  19.481 -20.953  1.00 23.23           O  
ATOM    422  OD2 ASP A  52       7.188  20.705 -20.069  1.00 24.39           O  
ATOM    423  N   MET A  53       9.984  21.175 -23.189  1.00 20.94           N  
ATOM    424  CA  MET A  53       9.759  21.490 -24.584  1.00 21.32           C  
ATOM    425  C   MET A  53       8.308  21.964 -24.847  1.00 20.77           C  
ATOM    426  O   MET A  53       8.082  23.110 -25.205  1.00 20.01           O  
ATOM    427  CB  MET A  53      10.068  20.315 -25.488  1.00 22.29           C  
ATOM    428  CG  MET A  53      10.059  20.737 -26.942  1.00 23.03           C  
ATOM    429  SD  MET A  53      10.487  19.433 -28.078  1.00 25.06           S  
ATOM    430  CE  MET A  53       9.097  18.309 -27.819  1.00 24.88           C  
ATOM    431  N   ASP A  54       7.360  21.065 -24.673  1.00 21.14           N  
ATOM    432  CA  ASP A  54       5.977  21.310 -25.093  1.00 21.26           C  
ATOM    433  C   ASP A  54       5.378  22.480 -24.338  1.00 20.36           C  
ATOM    434  O   ASP A  54       5.481  22.555 -23.111  1.00 20.78           O  
ATOM    435  CB  ASP A  54       5.141  20.060 -24.896  1.00 22.15           C  
ATOM    436  CG  ASP A  54       5.292  19.069 -26.011  1.00 23.13           C  
ATOM    437  OD1 ASP A  54       5.697  19.360 -27.141  1.00 24.62           O  
ATOM    438  OD2 ASP A  54       4.972  17.928 -25.747  1.00 25.15           O  
ATOM    439  N   TYR A  55       4.794  23.414 -25.075  1.00 19.74           N  
ATOM    440  CA  TYR A  55       4.227  24.647 -24.540  1.00 19.72           C  
ATOM    441  C   TYR A  55       5.189  25.530 -23.741  1.00 20.05           C  
ATOM    442  O   TYR A  55       4.753  26.339 -22.909  1.00 19.70           O  
ATOM    443  CB  TYR A  55       2.966  24.349 -23.729  1.00 19.69           C  
ATOM    444  CG  TYR A  55       1.749  24.088 -24.598  1.00 19.95           C  
ATOM    445  CD1 TYR A  55       1.180  25.115 -25.373  1.00 20.59           C  
ATOM    446  CD2 TYR A  55       1.146  22.842 -24.639  1.00 20.26           C  
ATOM    447  CE1 TYR A  55       0.044  24.898 -26.169  1.00 20.33           C  
ATOM    448  CE2 TYR A  55      -0.001  22.624 -25.428  1.00 20.36           C  
ATOM    449  CZ  TYR A  55      -0.554  23.653 -26.177  1.00 20.37           C  
ATOM    450  OH  TYR A  55      -1.732  23.430 -26.940  1.00 20.42           O  
ATOM    451  N   THR A  56       6.495  25.374 -24.011  1.00 19.70           N  
ATOM    452  CA  THR A  56       7.523  26.141 -23.336  1.00 20.00           C  
ATOM    453  C   THR A  56       8.435  26.645 -24.428  1.00 19.73           C  
ATOM    454  O   THR A  56       8.387  27.823 -24.769  1.00 20.25           O  
ATOM    455  CB  THR A  56       8.243  25.283 -22.275  1.00 20.17           C  
ATOM    456  OG1 THR A  56       7.295  24.833 -21.319  1.00 20.45           O  
ATOM    457  CG2 THR A  56       9.333  26.096 -21.563  1.00 20.15           C  
ATOM    458  N   LEU A  57       9.226  25.753 -25.009  1.00 19.84           N  
ATOM    459  CA  LEU A  57       9.991  26.049 -26.231  1.00 19.92           C  
ATOM    460  C   LEU A  57       9.090  25.938 -27.487  1.00 20.02           C  
ATOM    461  O   LEU A  57       9.194  26.746 -28.406  1.00 20.16           O  
ATOM    462  CB  LEU A  57      11.154  25.082 -26.368  1.00 20.53           C  
ATOM    463  CG  LEU A  57      12.275  25.231 -25.316  1.00 20.67           C  
ATOM    464  CD1 LEU A  57      13.194  24.041 -25.358  1.00 21.18           C  
ATOM    465  CD2 LEU A  57      13.062  26.504 -25.532  1.00 21.33           C  
ATOM    466  N   ALA A  58       8.229  24.933 -27.519  1.00 19.64           N  
ATOM    467  CA  ALA A  58       7.368  24.682 -28.667  1.00 20.18           C  
ATOM    468  C   ALA A  58       5.940  25.053 -28.249  1.00 20.01           C  
ATOM    469  O   ALA A  58       5.261  24.266 -27.617  1.00 18.67           O  
ATOM    470  CB  ALA A  58       7.431  23.232 -29.061  1.00 20.40           C  
ATOM    471  N   VAL A  59       5.520  26.273 -28.586  1.00 20.95           N  
ATOM    472  CA  VAL A  59       4.197  26.752 -28.159  1.00 21.24           C  
ATOM    473  C   VAL A  59       3.236  26.493 -29.299  1.00 21.23           C  
ATOM    474  O   VAL A  59       3.446  26.992 -30.425  1.00 21.74           O  
ATOM    475  CB  VAL A  59       4.230  28.215 -27.705  1.00 22.20           C  
ATOM    476  CG1 VAL A  59       2.826  28.669 -27.287  1.00 22.30           C  
ATOM    477  CG2 VAL A  59       5.164  28.329 -26.494  1.00 22.41           C  
ATOM    478  N   TYR A  60       2.243  25.648 -29.037  1.00 20.20           N  
ATOM    479  CA  TYR A  60       1.346  25.204 -30.105  1.00 21.03           C  
ATOM    480  C   TYR A  60       0.280  26.265 -30.328  1.00 21.01           C  
ATOM    481  O   TYR A  60      -0.286  26.809 -29.352  1.00 20.97           O  
ATOM    482  CB  TYR A  60       0.736  23.826 -29.781  1.00 20.77           C  
ATOM    483  CG  TYR A  60       1.801  22.747 -29.672  1.00 20.60           C  
ATOM    484  CD1 TYR A  60       2.430  22.244 -30.815  1.00 21.34           C  
ATOM    485  CD2 TYR A  60       2.209  22.263 -28.429  1.00 20.26           C  
ATOM    486  CE1 TYR A  60       3.392  21.250 -30.731  1.00 21.40           C  
ATOM    487  CE2 TYR A  60       3.211  21.295 -28.330  1.00 20.72           C  
ATOM    488  CZ  TYR A  60       3.821  20.800 -29.479  1.00 21.25           C  
ATOM    489  OH  TYR A  60       4.815  19.820 -29.372  1.00 20.80           O  
ATOM    490  N   LYS A  61       0.040  26.568 -31.583  1.00 21.82           N  
ATOM    491  CA  LYS A  61      -0.869  27.657 -31.969  1.00 23.08           C  
ATOM    492  C   LYS A  61      -2.344  27.309 -31.658  1.00 22.69           C  
ATOM    493  O   LYS A  61      -2.764  26.158 -31.863  1.00 22.80           O  
ATOM    494  CB  LYS A  61      -0.712  27.991 -33.434  1.00 24.00           C  
ATOM    495  CG  LYS A  61       0.639  28.633 -33.727  1.00 25.09           C  
ATOM    496  CD  LYS A  61       0.827  29.007 -35.188  1.00 26.68           C  
ATOM    497  CE  LYS A  61       2.144  29.756 -35.308  1.00 27.44           C  
ATOM    498  NZ  LYS A  61       2.301  30.278 -36.667  1.00 29.73           N  
ATOM    499  N   SER A  62      -3.070  28.321 -31.175  1.00 22.80           N  
ATOM    500  CA  SER A  62      -4.463  28.239 -30.727  1.00 22.75           C  
ATOM    501  C   SER A  62      -5.385  29.077 -31.610  1.00 23.00           C  
ATOM    502  O   SER A  62      -5.011  30.211 -31.928  1.00 22.53           O  
ATOM    503  CB  SER A  62      -4.545  28.760 -29.303  1.00 23.01           C  
ATOM    504  OG  SER A  62      -5.860  28.664 -28.759  1.00 23.19           O  
ATOM    505  N   PRO A  63      -6.591  28.587 -31.965  1.00 22.96           N  
ATOM    506  CA  PRO A  63      -7.154  27.321 -31.508  1.00 22.66           C  
ATOM    507  C   PRO A  63      -6.826  26.114 -32.380  1.00 22.60           C  
ATOM    508  O   PRO A  63      -7.367  25.039 -32.138  1.00 22.66           O  
ATOM    509  CB  PRO A  63      -8.678  27.595 -31.579  1.00 23.15           C  
ATOM    510  CG  PRO A  63      -8.811  28.460 -32.800  1.00 24.01           C  
ATOM    511  CD  PRO A  63      -7.590  29.373 -32.714  1.00 23.85           C  
ATOM    512  N   GLU A  64      -5.949  26.274 -33.373  1.00 23.39           N  
ATOM    513  CA  GLU A  64      -5.702  25.231 -34.358  1.00 24.12           C  
ATOM    514  C   GLU A  64      -5.260  23.914 -33.719  1.00 22.93           C  
ATOM    515  O   GLU A  64      -5.754  22.849 -34.084  1.00 22.53           O  
ATOM    516  CB  GLU A  64      -4.665  25.697 -35.384  1.00 25.57           C  
ATOM    517  CG  GLU A  64      -5.224  26.609 -36.460  1.00 27.84           C  
ATOM    518  CD  GLU A  64      -5.408  28.054 -35.993  1.00 28.74           C  
ATOM    519  OE1 GLU A  64      -4.933  28.441 -34.889  1.00 27.38           O  
ATOM    520  OE2 GLU A  64      -6.070  28.798 -36.742  1.00 30.86           O  
ATOM    521  N   TYR A  65      -4.356  23.974 -32.738  1.00 21.64           N  
ATOM    522  CA  TYR A  65      -3.819  22.729 -32.182  1.00 21.28           C  
ATOM    523  C   TYR A  65      -4.824  22.017 -31.276  1.00 20.85           C  
ATOM    524  O   TYR A  65      -4.997  20.798 -31.358  1.00 20.76           O  
ATOM    525  CB  TYR A  65      -2.533  22.998 -31.423  1.00 21.19           C  
ATOM    526  CG  TYR A  65      -1.816  21.759 -30.964  1.00 20.88           C  
ATOM    527  CD1 TYR A  65      -1.074  20.977 -31.861  1.00 21.61           C  
ATOM    528  CD2 TYR A  65      -1.835  21.389 -29.632  1.00 20.90           C  
ATOM    529  CE1 TYR A  65      -0.387  19.864 -31.433  1.00 21.57           C  
ATOM    530  CE2 TYR A  65      -1.157  20.264 -29.203  1.00 20.76           C  
ATOM    531  CZ  TYR A  65      -0.438  19.512 -30.107  1.00 21.31           C  
ATOM    532  OH  TYR A  65       0.224  18.396 -29.635  1.00 21.95           O  
ATOM    533  N   GLU A  66      -5.512  22.783 -30.444  1.00 20.30           N  
ATOM    534  CA  GLU A  66      -6.618  22.228 -29.651  1.00 20.15           C  
ATOM    535  C   GLU A  66      -7.666  21.585 -30.551  1.00 20.49           C  
ATOM    536  O   GLU A  66      -8.159  20.494 -30.259  1.00 20.22           O  
ATOM    537  CB  GLU A  66      -7.300  23.306 -28.777  1.00 20.17           C  
ATOM    538  CG  GLU A  66      -6.438  24.052 -27.773  1.00 19.84           C  
ATOM    539  CD  GLU A  66      -5.932  25.387 -28.290  1.00 20.14           C  
ATOM    540  OE1 GLU A  66      -5.220  25.399 -29.304  1.00 20.16           O  
ATOM    541  OE2 GLU A  66      -6.262  26.436 -27.685  1.00 21.02           O  
ATOM    542  N   SER A  67      -7.978  22.254 -31.653  1.00 21.29           N  
ATOM    543  CA  SER A  67      -9.009  21.768 -32.570  1.00 22.46           C  
ATOM    544  C   SER A  67      -8.585  20.441 -33.248  1.00 22.42           C  
ATOM    545  O   SER A  67      -9.373  19.502 -33.332  1.00 21.88           O  
ATOM    546  CB  SER A  67      -9.378  22.829 -33.583  1.00 23.42           C  
ATOM    547  OG  SER A  67     -10.410  22.308 -34.394  1.00 26.54           O  
ATOM    548  N   LEU A  68      -7.308  20.328 -33.611  1.00 22.38           N  
ATOM    549  CA  LEU A  68      -6.763  19.071 -34.104  1.00 22.63           C  
ATOM    550  C   LEU A  68      -6.834  17.966 -33.038  1.00 21.81           C  
ATOM    551  O   LEU A  68      -7.311  16.868 -33.330  1.00 22.55           O  
ATOM    552  CB  LEU A  68      -5.323  19.255 -34.597  1.00 23.33           C  
ATOM    553  CG  LEU A  68      -4.617  17.977 -35.053  1.00 24.22           C  
ATOM    554  CD1 LEU A  68      -5.296  17.359 -36.275  1.00 25.33           C  
ATOM    555  CD2 LEU A  68      -3.155  18.286 -35.335  1.00 24.71           C  
ATOM    556  N   GLY A  69      -6.382  18.252 -31.818  1.00 20.66           N  
ATOM    557  CA  GLY A  69      -6.509  17.290 -30.698  1.00 19.97           C  
ATOM    558  C   GLY A  69      -7.949  16.800 -30.521  1.00 19.80           C  
ATOM    559  O   GLY A  69      -8.234  15.598 -30.356  1.00 19.92           O  
ATOM    560  N   PHE A  70      -8.842  17.766 -30.501  1.00 19.66           N  
ATOM    561  CA  PHE A  70     -10.287  17.505 -30.372  1.00 19.85           C  
ATOM    562  C   PHE A  70     -10.817  16.581 -31.455  1.00 20.86           C  
ATOM    563  O   PHE A  70     -11.439  15.566 -31.169  1.00 20.96           O  
ATOM    564  CB  PHE A  70     -11.039  18.829 -30.380  1.00 19.30           C  
ATOM    565  CG  PHE A  70     -12.513  18.698 -30.191  1.00 19.11           C  
ATOM    566  CD1 PHE A  70     -13.069  18.693 -28.909  1.00 18.97           C  
ATOM    567  CD2 PHE A  70     -13.366  18.647 -31.308  1.00 20.15           C  
ATOM    568  CE1 PHE A  70     -14.446  18.599 -28.735  1.00 18.91           C  
ATOM    569  CE2 PHE A  70     -14.753  18.559 -31.136  1.00 20.19           C  
ATOM    570  CZ  PHE A  70     -15.268  18.518 -29.845  1.00 19.71           C  
ATOM    571  N  AGLU A  71     -10.549  16.934 -32.702  0.50 21.95           N  
ATOM    572  N  BGLU A  71     -10.553  16.936 -32.700  0.50 22.06           N  
ATOM    573  CA AGLU A  71     -11.004  16.157 -33.855  0.50 23.31           C  
ATOM    574  CA BGLU A  71     -10.996  16.150 -33.845  0.50 23.42           C  
ATOM    575  C  AGLU A  71     -10.492  14.712 -33.810  0.50 22.98           C  
ATOM    576  C  BGLU A  71     -10.505  14.707 -33.760  0.50 23.02           C  
ATOM    577  O  AGLU A  71     -11.249  13.767 -34.050  0.50 23.00           O  
ATOM    578  O  BGLU A  71     -11.287  13.760 -33.915  0.50 22.95           O  
ATOM    579  CB AGLU A  71     -10.569  16.848 -35.156  0.50 24.92           C  
ATOM    580  CB BGLU A  71     -10.490  16.793 -35.133  0.50 25.08           C  
ATOM    581  CG AGLU A  71     -10.551  15.933 -36.374  0.50 26.84           C  
ATOM    582  CG BGLU A  71     -11.247  18.035 -35.555  0.50 26.39           C  
ATOM    583  CD AGLU A  71     -10.142  16.651 -37.660  0.50 28.46           C  
ATOM    584  CD BGLU A  71     -10.691  18.618 -36.842  0.50 27.95           C  
ATOM    585  OE1AGLU A  71     -11.010  17.297 -38.284  0.50 29.67           O  
ATOM    586  OE1BGLU A  71      -9.464  18.509 -37.056  0.50 29.72           O  
ATOM    587  OE2AGLU A  71      -8.958  16.562 -38.057  0.50 29.61           O  
ATOM    588  OE2BGLU A  71     -11.470  19.161 -37.651  0.50 29.27           O  
ATOM    589  N   LEU A  72      -9.217  14.535 -33.462  1.00 22.49           N  
ATOM    590  CA  LEU A  72      -8.634  13.183 -33.386  1.00 22.38           C  
ATOM    591  C   LEU A  72      -9.185  12.374 -32.206  1.00 21.69           C  
ATOM    592  O   LEU A  72      -9.375  11.164 -32.320  1.00 21.65           O  
ATOM    593  CB  LEU A  72      -7.104  13.252 -33.356  1.00 22.59           C  
ATOM    594  CG  LEU A  72      -6.461  13.827 -34.637  1.00 23.31           C  
ATOM    595  CD1 LEU A  72      -4.962  13.927 -34.456  1.00 23.52           C  
ATOM    596  CD2 LEU A  72      -6.776  13.017 -35.887  1.00 24.65           C  
ATOM    597  N   THR A  73      -9.445  13.042 -31.081  1.00 20.98           N  
ATOM    598  CA  THR A  73     -10.020  12.381 -29.894  1.00 20.76           C  
ATOM    599  C   THR A  73     -11.431  11.903 -30.224  1.00 21.11           C  
ATOM    600  O   THR A  73     -11.771  10.741 -29.979  1.00 21.75           O  
ATOM    601  CB  THR A  73      -9.981  13.323 -28.701  1.00 19.92           C  
ATOM    602  OG1 THR A  73      -8.597  13.693 -28.463  1.00 20.11           O  
ATOM    603  CG2 THR A  73     -10.563  12.665 -27.449  1.00 19.81           C  
ATOM    604  N   VAL A  74     -12.209  12.777 -30.849  1.00 21.26           N  
ATOM    605  CA  VAL A  74     -13.579  12.420 -31.309  1.00 21.69           C  
ATOM    606  C   VAL A  74     -13.565  11.213 -32.233  1.00 22.33           C  
ATOM    607  O   VAL A  74     -14.336  10.262 -32.054  1.00 22.54           O  
ATOM    608  CB  VAL A  74     -14.268  13.624 -32.003  1.00 22.03           C  
ATOM    609  CG1 VAL A  74     -15.487  13.187 -32.788  1.00 22.91           C  
ATOM    610  CG2 VAL A  74     -14.664  14.652 -30.956  1.00 21.74           C  
ATOM    611  N   GLU A  75     -12.652  11.237 -33.195  1.00 22.83           N  
ATOM    612  CA AGLU A  75     -12.599  10.176 -34.172  0.50 23.85           C  
ATOM    613  CA BGLU A  75     -12.519  10.181 -34.193  0.50 23.59           C  
ATOM    614  C   GLU A  75     -12.225   8.872 -33.494  1.00 23.72           C  
ATOM    615  O   GLU A  75     -12.771   7.831 -33.844  1.00 24.02           O  
ATOM    616  CB AGLU A  75     -11.682  10.536 -35.346  0.50 24.69           C  
ATOM    617  CB BGLU A  75     -11.402  10.518 -35.209  0.50 24.01           C  
ATOM    618  CG AGLU A  75     -12.331  11.554 -36.264  0.50 25.38           C  
ATOM    619  CG BGLU A  75     -11.046   9.402 -36.202  0.50 24.96           C  
ATOM    620  CD AGLU A  75     -11.437  12.086 -37.362  0.50 26.19           C  
ATOM    621  CD BGLU A  75      -9.899   9.754 -37.158  0.50 25.27           C  
ATOM    622  OE1AGLU A  75     -10.236  11.749 -37.420  0.50 26.64           O  
ATOM    623  OE1BGLU A  75      -8.776  10.111 -36.757  0.50 23.88           O  
ATOM    624  OE2AGLU A  75     -11.964  12.850 -38.185  0.50 27.32           O  
ATOM    625  OE2BGLU A  75     -10.145   9.619 -38.359  0.50 26.79           O  
ATOM    626  N   ARG A  76     -11.339   8.934 -32.501  1.00 23.18           N  
ATOM    627  CA  ARG A  76     -10.982   7.735 -31.723  1.00 23.21           C  
ATOM    628  C   ARG A  76     -12.195   7.175 -30.955  1.00 22.80           C  
ATOM    629  O   ARG A  76     -12.439   5.996 -30.962  1.00 22.83           O  
ATOM    630  CB  ARG A  76      -9.851   8.050 -30.749  1.00 23.01           C  
ATOM    631  CG  ARG A  76      -9.512   6.956 -29.751  1.00 23.46           C  
ATOM    632  CD  ARG A  76      -9.135   5.656 -30.437  1.00 25.28           C  
ATOM    633  NE  ARG A  76      -8.737   4.644 -29.452  1.00 26.06           N  
ATOM    634  CZ  ARG A  76      -8.397   3.384 -29.742  1.00 27.69           C  
ATOM    635  NH1 ARG A  76      -8.380   2.945 -30.998  1.00 28.11           N  
ATOM    636  NH2 ARG A  76      -8.051   2.557 -28.757  1.00 28.29           N  
ATOM    637  N   LEU A  77     -12.951   8.048 -30.295  1.00 22.24           N  
ATOM    638  CA  LEU A  77     -14.146   7.585 -29.578  1.00 22.38           C  
ATOM    639  C   LEU A  77     -15.187   6.957 -30.513  1.00 23.03           C  
ATOM    640  O   LEU A  77     -15.764   5.916 -30.206  1.00 23.52           O  
ATOM    641  CB  LEU A  77     -14.786   8.739 -28.821  1.00 21.66           C  
ATOM    642  CG  LEU A  77     -13.989   9.294 -27.657  1.00 20.89           C  
ATOM    643  CD1 LEU A  77     -14.639  10.579 -27.191  1.00 20.31           C  
ATOM    644  CD2 LEU A  77     -13.904   8.264 -26.556  1.00 21.25           C  
ATOM    645  N   VAL A  78     -15.416   7.575 -31.660  1.00 23.49           N  
ATOM    646  CA  VAL A  78     -16.325   6.998 -32.642  1.00 24.40           C  
ATOM    647  C   VAL A  78     -15.807   5.640 -33.100  1.00 25.65           C  
ATOM    648  O   VAL A  78     -16.542   4.687 -33.198  1.00 25.86           O  
ATOM    649  CB  VAL A  78     -16.567   7.914 -33.858  1.00 24.61           C  
ATOM    650  CG1 VAL A  78     -17.397   7.196 -34.930  1.00 26.15           C  
ATOM    651  CG2 VAL A  78     -17.313   9.148 -33.421  1.00 24.11           C  
ATOM    652  N   SER A  79     -14.525   5.573 -33.367  1.00 26.30           N  
ATOM    653  CA  SER A  79     -13.856   4.332 -33.750  1.00 28.24           C  
ATOM    654  C   SER A  79     -14.075   3.162 -32.759  1.00 28.67           C  
ATOM    655  O   SER A  79     -14.230   2.015 -33.179  1.00 28.96           O  
ATOM    656  CB  SER A  79     -12.365   4.657 -33.905  1.00 28.80           C  
ATOM    657  OG  SER A  79     -11.606   3.522 -33.964  1.00 31.48           O  
ATOM    658  N   ILE A  80     -14.122   3.449 -31.458  1.00 28.85           N  
ATOM    659  CA  ILE A  80     -14.392   2.406 -30.451  1.00 29.78           C  
ATOM    660  C   ILE A  80     -15.873   2.214 -30.109  1.00 30.26           C  
ATOM    661  O   ILE A  80     -16.197   1.432 -29.223  1.00 30.91           O  
ATOM    662  CB  ILE A  80     -13.596   2.617 -29.135  1.00 30.58           C  
ATOM    663  CG1 ILE A  80     -14.043   3.885 -28.391  1.00 30.24           C  
ATOM    664  CG2 ILE A  80     -12.107   2.641 -29.426  1.00 30.80           C  
ATOM    665  CD1 ILE A  80     -13.730   3.868 -26.918  1.00 30.54           C  
ATOM    666  N   GLY A  81     -16.773   2.914 -30.799  1.00 29.76           N  
ATOM    667  CA  GLY A  81     -18.185   2.642 -30.695  1.00 29.88           C  
ATOM    668  C   GLY A  81     -19.080   3.735 -30.159  1.00 29.00           C  
ATOM    669  O   GLY A  81     -20.282   3.494 -30.013  1.00 28.83           O  
ATOM    670  N   TYR A  82     -18.539   4.920 -29.868  1.00 27.71           N  
ATOM    671  CA  TYR A  82     -19.401   6.065 -29.547  1.00 27.21           C  
ATOM    672  C   TYR A  82     -20.272   6.454 -30.768  1.00 28.18           C  
ATOM    673  O   TYR A  82     -19.873   6.239 -31.905  1.00 27.79           O  
ATOM    674  CB  TYR A  82     -18.600   7.260 -29.050  1.00 26.17           C  
ATOM    675  CG  TYR A  82     -18.313   7.183 -27.558  1.00 26.03           C  
ATOM    676  CD1 TYR A  82     -17.474   6.189 -27.028  1.00 26.40           C  
ATOM    677  CD2 TYR A  82     -18.894   8.082 -26.671  1.00 25.91           C  
ATOM    678  CE1 TYR A  82     -17.239   6.098 -25.652  1.00 26.03           C  
ATOM    679  CE2 TYR A  82     -18.654   8.007 -25.292  1.00 25.66           C  
ATOM    680  CZ  TYR A  82     -17.836   7.014 -24.786  1.00 25.91           C  
ATOM    681  OH  TYR A  82     -17.614   6.952 -23.417  1.00 26.44           O  
ATOM    682  N   PRO A  83     -21.441   7.061 -30.523  1.00 29.00           N  
ATOM    683  CA  PRO A  83     -22.354   7.353 -31.623  1.00 29.99           C  
ATOM    684  C   PRO A  83     -21.796   8.330 -32.657  1.00 30.46           C  
ATOM    685  O   PRO A  83     -20.983   9.215 -32.340  1.00 28.70           O  
ATOM    686  CB  PRO A  83     -23.591   7.958 -30.944  1.00 29.81           C  
ATOM    687  CG  PRO A  83     -23.344   7.990 -29.497  1.00 29.26           C  
ATOM    688  CD  PRO A  83     -22.003   7.395 -29.200  1.00 29.11           C  
ATOM    689  N   GLN A  84     -22.275   8.170 -33.884  1.00 31.74           N  
ATOM    690  CA  GLN A  84     -21.831   8.955 -35.023  1.00 33.13           C  
ATOM    691  C   GLN A  84     -22.033  10.444 -34.844  1.00 30.63           C  
ATOM    692  O   GLN A  84     -21.299  11.206 -35.418  1.00 29.63           O  
ATOM    693  CB  GLN A  84     -22.607   8.515 -36.299  1.00 37.21           C  
ATOM    694  CG  GLN A  84     -22.271   7.107 -36.776  1.00 40.34           C  
ATOM    695  CD  GLN A  84     -20.876   7.023 -37.345  1.00 43.04           C  
ATOM    696  OE1 GLN A  84     -20.535   7.788 -38.250  1.00 47.89           O  
ATOM    697  NE2 GLN A  84     -20.055   6.082 -36.840  1.00 43.59           N  
ATOM    698  N   GLU A  85     -23.019  10.841 -34.044  1.00 29.89           N  
ATOM    699  CA  GLU A  85     -23.318  12.241 -33.796  1.00 30.03           C  
ATOM    700  C   GLU A  85     -22.136  13.033 -33.269  1.00 28.41           C  
ATOM    701  O   GLU A  85     -22.075  14.218 -33.494  1.00 28.01           O  
ATOM    702  CB  GLU A  85     -24.484  12.429 -32.844  1.00 31.22           C  
ATOM    703  CG  GLU A  85     -25.847  12.054 -33.435  1.00 33.28           C  
ATOM    704  CD  GLU A  85     -26.304  10.664 -33.043  1.00 34.96           C  
ATOM    705  OE1 GLU A  85     -25.435   9.801 -32.742  1.00 34.45           O  
ATOM    706  OE2 GLU A  85     -27.550  10.436 -33.035  1.00 36.83           O  
ATOM    707  N   LEU A  86     -21.204  12.376 -32.578  1.00 27.21           N  
ATOM    708  CA  LEU A  86     -19.992  13.025 -32.116  1.00 25.75           C  
ATOM    709  C   LEU A  86     -19.274  13.755 -33.235  1.00 26.01           C  
ATOM    710  O   LEU A  86     -18.671  14.797 -32.986  1.00 24.57           O  
ATOM    711  CB  LEU A  86     -19.034  12.021 -31.469  1.00 25.49           C  
ATOM    712  CG  LEU A  86     -19.188  11.735 -29.988  1.00 24.99           C  
ATOM    713  CD1 LEU A  86     -20.511  11.084 -29.646  1.00 25.10           C  
ATOM    714  CD2 LEU A  86     -18.030  10.849 -29.511  1.00 25.11           C  
ATOM    715  N   LEU A  87     -19.342  13.216 -34.454  1.00 26.61           N  
ATOM    716  CA  LEU A  87     -18.699  13.836 -35.620  1.00 27.62           C  
ATOM    717  C   LEU A  87     -19.234  15.218 -35.987  1.00 28.09           C  
ATOM    718  O   LEU A  87     -18.587  15.947 -36.698  1.00 28.94           O  
ATOM    719  CB  LEU A  87     -18.768  12.910 -36.841  1.00 28.82           C  
ATOM    720  CG  LEU A  87     -18.071  11.524 -36.726  1.00 29.04           C  
ATOM    721  CD1 LEU A  87     -18.284  10.648 -37.978  1.00 30.45           C  
ATOM    722  CD2 LEU A  87     -16.611  11.673 -36.396  1.00 28.34           C  
ATOM    723  N   SER A  88     -20.394  15.590 -35.485  1.00 28.34           N  
ATOM    724  CA  SER A  88     -20.926  16.902 -35.736  1.00 28.55           C  
ATOM    725  C   SER A  88     -20.481  17.903 -34.668  1.00 27.58           C  
ATOM    726  O   SER A  88     -20.870  19.063 -34.767  1.00 28.22           O  
ATOM    727  CB  SER A  88     -22.448  16.821 -35.840  1.00 29.62           C  
ATOM    728  OG  SER A  88     -22.962  16.659 -34.539  1.00 30.26           O  
ATOM    729  N   PHE A  89     -19.704  17.495 -33.643  1.00 25.32           N  
ATOM    730  CA  PHE A  89     -19.139  18.463 -32.699  1.00 24.14           C  
ATOM    731  C   PHE A  89     -18.072  19.270 -33.432  1.00 23.46           C  
ATOM    732  O   PHE A  89     -17.462  18.772 -34.357  1.00 23.85           O  
ATOM    733  CB  PHE A  89     -18.466  17.835 -31.465  1.00 23.18           C  
ATOM    734  CG  PHE A  89     -19.350  16.952 -30.607  1.00 23.52           C  
ATOM    735  CD1 PHE A  89     -20.752  16.977 -30.675  1.00 24.29           C  
ATOM    736  CD2 PHE A  89     -18.741  16.083 -29.687  1.00 23.18           C  
ATOM    737  CE1 PHE A  89     -21.522  16.129 -29.862  1.00 24.46           C  
ATOM    738  CE2 PHE A  89     -19.497  15.250 -28.866  1.00 23.77           C  
ATOM    739  CZ  PHE A  89     -20.895  15.262 -28.954  1.00 24.07           C  
ATOM    740  N   ALA A  90     -17.867  20.515 -33.039  1.00 22.87           N  
ATOM    741  CA  ALA A  90     -16.724  21.298 -33.533  1.00 23.00           C  
ATOM    742  C   ALA A  90     -16.123  22.058 -32.372  1.00 22.17           C  
ATOM    743  O   ALA A  90     -16.844  22.619 -31.539  1.00 21.31           O  
ATOM    744  CB  ALA A  90     -17.144  22.243 -34.666  1.00 23.94           C  
ATOM    745  N   TYR A  91     -14.800  22.064 -32.300  1.00 22.29           N  
ATOM    746  CA  TYR A  91     -14.099  22.676 -31.177  1.00 21.90           C  
ATOM    747  C   TYR A  91     -14.445  24.144 -31.059  1.00 22.04           C  
ATOM    748  O   TYR A  91     -14.454  24.839 -32.041  1.00 21.74           O  
ATOM    749  CB  TYR A  91     -12.579  22.522 -31.270  1.00 21.95           C  
ATOM    750  CG  TYR A  91     -11.879  23.048 -30.041  1.00 21.22           C  
ATOM    751  CD1 TYR A  91     -11.950  22.377 -28.832  1.00 20.66           C  
ATOM    752  CD2 TYR A  91     -11.177  24.246 -30.079  1.00 21.47           C  
ATOM    753  CE1 TYR A  91     -11.323  22.864 -27.709  1.00 20.58           C  
ATOM    754  CE2 TYR A  91     -10.540  24.750 -28.963  1.00 20.97           C  
ATOM    755  CZ  TYR A  91     -10.621  24.055 -27.774  1.00 20.79           C  
ATOM    756  OH  TYR A  91      -9.988  24.557 -26.677  1.00 20.84           O  
ATOM    757  N   ASP A  92     -14.705  24.594 -29.831  1.00 21.84           N  
ATOM    758  CA  ASP A  92     -15.074  25.979 -29.582  1.00 23.04           C  
ATOM    759  C   ASP A  92     -14.166  26.522 -28.511  1.00 22.17           C  
ATOM    760  O   ASP A  92     -14.342  26.211 -27.317  1.00 21.28           O  
ATOM    761  CB  ASP A  92     -16.527  26.018 -29.133  1.00 24.98           C  
ATOM    762  CG  ASP A  92     -16.994  27.383 -28.723  1.00 27.52           C  
ATOM    763  OD1 ASP A  92     -16.288  28.411 -28.888  1.00 27.13           O  
ATOM    764  OD2 ASP A  92     -18.139  27.398 -28.164  1.00 33.09           O  
ATOM    765  N   SER A  93     -13.202  27.345 -28.930  1.00 21.85           N  
ATOM    766  CA  SER A  93     -12.233  27.911 -28.027  1.00 21.85           C  
ATOM    767  C   SER A  93     -12.863  28.869 -26.998  1.00 21.57           C  
ATOM    768  O   SER A  93     -12.235  29.147 -25.961  1.00 20.72           O  
ATOM    769  CB  SER A  93     -11.143  28.646 -28.817  1.00 22.63           C  
ATOM    770  OG  SER A  93     -11.723  29.789 -29.444  1.00 23.89           O  
ATOM    771  N   THR A  94     -14.096  29.340 -27.235  1.00 21.58           N  
ATOM    772  CA  THR A  94     -14.716  30.258 -26.295  1.00 22.14           C  
ATOM    773  C   THR A  94     -15.231  29.573 -25.019  1.00 21.96           C  
ATOM    774  O   THR A  94     -15.473  30.270 -24.027  1.00 24.08           O  
ATOM    775  CB  THR A  94     -15.812  31.137 -26.906  1.00 23.12           C  
ATOM    776  OG1 THR A  94     -17.017  30.393 -27.144  1.00 23.06           O  
ATOM    777  CG2 THR A  94     -15.321  31.819 -28.216  1.00 24.09           C  
ATOM    778  N   PHE A  95     -15.363  28.242 -25.014  1.00 20.51           N  
ATOM    779  CA  PHE A  95     -15.910  27.542 -23.866  1.00 20.01           C  
ATOM    780  C   PHE A  95     -14.842  27.242 -22.780  1.00 19.64           C  
ATOM    781  O   PHE A  95     -14.984  27.682 -21.652  1.00 19.63           O  
ATOM    782  CB  PHE A  95     -16.673  26.257 -24.256  1.00 19.31           C  
ATOM    783  CG  PHE A  95     -17.176  25.486 -23.052  1.00 18.62           C  
ATOM    784  CD1 PHE A  95     -18.362  25.820 -22.451  1.00 18.95           C  
ATOM    785  CD2 PHE A  95     -16.420  24.448 -22.494  1.00 18.17           C  
ATOM    786  CE1 PHE A  95     -18.802  25.123 -21.312  1.00 18.88           C  
ATOM    787  CE2 PHE A  95     -16.841  23.776 -21.365  1.00 17.77           C  
ATOM    788  CZ  PHE A  95     -18.041  24.110 -20.779  1.00 18.21           C  
ATOM    789  N   PRO A  96     -13.789  26.492 -23.123  1.00 19.69           N  
ATOM    790  CA  PRO A  96     -12.939  26.012 -22.051  1.00 19.64           C  
ATOM    791  C   PRO A  96     -11.953  27.068 -21.537  1.00 20.07           C  
ATOM    792  O   PRO A  96     -11.449  27.894 -22.305  1.00 20.01           O  
ATOM    793  CB  PRO A  96     -12.188  24.850 -22.691  1.00 19.51           C  
ATOM    794  CG  PRO A  96     -12.126  25.173 -24.142  1.00 19.80           C  
ATOM    795  CD  PRO A  96     -13.326  26.023 -24.442  1.00 20.02           C  
ATOM    796  N   THR A  97     -11.766  27.052 -20.224  1.00 19.74           N  
ATOM    797  CA  THR A  97     -10.640  27.700 -19.560  1.00 18.89           C  
ATOM    798  C   THR A  97      -9.885  26.589 -18.889  1.00 17.74           C  
ATOM    799  O   THR A  97     -10.482  25.635 -18.440  1.00 16.83           O  
ATOM    800  CB  THR A  97     -11.163  28.675 -18.511  1.00 19.56           C  
ATOM    801  OG1 THR A  97     -11.900  29.691 -19.175  1.00 20.24           O  
ATOM    802  CG2 THR A  97     -10.008  29.384 -17.765  1.00 19.42           C  
ATOM    803  N   ARG A  98      -8.558  26.717 -18.826  1.00 17.50           N  
ATOM    804  CA  ARG A  98      -7.717  25.718 -18.194  1.00 17.23           C  
ATOM    805  C   ARG A  98      -7.904  25.697 -16.664  1.00 17.20           C  
ATOM    806  O   ARG A  98      -8.230  26.715 -16.073  1.00 18.07           O  
ATOM    807  CB  ARG A  98      -6.274  26.006 -18.533  1.00 17.43           C  
ATOM    808  CG  ARG A  98      -5.319  24.938 -18.076  1.00 17.85           C  
ATOM    809  CD  ARG A  98      -4.087  24.940 -18.948  1.00 18.03           C  
ATOM    810  NE  ARG A  98      -3.312  26.176 -18.962  1.00 18.60           N  
ATOM    811  CZ  ARG A  98      -2.091  26.326 -18.450  1.00 19.34           C  
ATOM    812  NH1 ARG A  98      -1.488  25.343 -17.754  1.00 19.84           N  
ATOM    813  NH2 ARG A  98      -1.451  27.470 -18.626  1.00 19.58           N  
ATOM    814  N   GLY A  99      -7.718  24.525 -16.076  1.00 16.66           N  
ATOM    815  CA  GLY A  99      -7.756  24.278 -14.618  1.00 16.90           C  
ATOM    816  C   GLY A  99      -9.088  23.902 -14.032  1.00 16.92           C  
ATOM    817  O   GLY A  99      -9.247  23.858 -12.805  1.00 17.52           O  
ATOM    818  N   LEU A 100     -10.079  23.647 -14.891  1.00 17.05           N  
ATOM    819  CA  LEU A 100     -11.371  23.179 -14.418  1.00 16.89           C  
ATOM    820  C   LEU A 100     -11.270  21.762 -13.860  1.00 16.99           C  
ATOM    821  O   LEU A 100     -10.370  20.996 -14.223  1.00 16.88           O  
ATOM    822  CB  LEU A 100     -12.421  23.261 -15.524  1.00 16.83           C  
ATOM    823  CG  LEU A 100     -12.614  24.699 -16.034  1.00 17.17           C  
ATOM    824  CD1 LEU A 100     -13.509  24.676 -17.269  1.00 17.64           C  
ATOM    825  CD2 LEU A 100     -13.164  25.675 -15.015  1.00 17.24           C  
ATOM    826  N   VAL A 101     -12.185  21.440 -12.965  1.00 16.98           N  
ATOM    827  CA  VAL A 101     -12.272  20.136 -12.351  1.00 17.66           C  
ATOM    828  C   VAL A 101     -13.446  19.384 -12.953  1.00 18.18           C  
ATOM    829  O   VAL A 101     -14.582  19.909 -12.958  1.00 18.51           O  
ATOM    830  CB  VAL A 101     -12.507  20.289 -10.830  1.00 18.23           C  
ATOM    831  CG1 VAL A 101     -12.560  18.935 -10.128  1.00 18.70           C  
ATOM    832  CG2 VAL A 101     -11.425  21.175 -10.215  1.00 18.45           C  
ATOM    833  N   PHE A 102     -13.219  18.181 -13.460  1.00 17.67           N  
ATOM    834  CA  PHE A 102     -14.344  17.333 -13.825  1.00 18.02           C  
ATOM    835  C   PHE A 102     -14.746  16.496 -12.653  1.00 18.73           C  
ATOM    836  O   PHE A 102     -13.930  15.695 -12.110  1.00 18.88           O  
ATOM    837  CB  PHE A 102     -14.089  16.443 -15.040  1.00 18.02           C  
ATOM    838  CG  PHE A 102     -15.339  15.819 -15.614  1.00 17.89           C  
ATOM    839  CD1 PHE A 102     -16.272  16.608 -16.293  1.00 18.00           C  
ATOM    840  CD2 PHE A 102     -15.606  14.466 -15.456  1.00 18.13           C  
ATOM    841  CE1 PHE A 102     -17.417  16.053 -16.815  1.00 18.04           C  
ATOM    842  CE2 PHE A 102     -16.755  13.897 -15.980  1.00 18.71           C  
ATOM    843  CZ  PHE A 102     -17.657  14.694 -16.683  1.00 18.35           C  
ATOM    844  N   ASP A 103     -16.010  16.666 -12.251  1.00 18.52           N  
ATOM    845  CA  ASP A 103     -16.573  15.857 -11.208  1.00 19.57           C  
ATOM    846  C   ASP A 103     -17.152  14.615 -11.842  1.00 19.80           C  
ATOM    847  O   ASP A 103     -18.185  14.709 -12.490  1.00 20.28           O  
ATOM    848  CB  ASP A 103     -17.667  16.621 -10.449  1.00 19.99           C  
ATOM    849  CG  ASP A 103     -18.333  15.779  -9.367  1.00 20.99           C  
ATOM    850  OD1 ASP A 103     -18.081  14.556  -9.281  1.00 20.77           O  
ATOM    851  OD2 ASP A 103     -19.129  16.355  -8.597  1.00 21.35           O  
ATOM    852  N   THR A 104     -16.502  13.465 -11.661  1.00 20.06           N  
ATOM    853  CA  THR A 104     -16.924  12.238 -12.344  1.00 20.82           C  
ATOM    854  C   THR A 104     -18.187  11.609 -11.758  1.00 21.64           C  
ATOM    855  O   THR A 104     -18.755  10.695 -12.383  1.00 22.17           O  
ATOM    856  CB  THR A 104     -15.853  11.147 -12.323  1.00 21.48           C  
ATOM    857  OG1 THR A 104     -15.575  10.810 -10.968  1.00 22.26           O  
ATOM    858  CG2 THR A 104     -14.596  11.595 -13.027  1.00 21.42           C  
ATOM    859  N   LEU A 105     -18.610  12.041 -10.562  1.00 21.39           N  
ATOM    860  CA  LEU A 105     -19.821  11.501  -9.990  1.00 22.44           C  
ATOM    861  C   LEU A 105     -21.022  12.104 -10.674  1.00 22.08           C  
ATOM    862  O   LEU A 105     -21.908  11.381 -11.120  1.00 22.30           O  
ATOM    863  CB  LEU A 105     -19.886  11.801  -8.481  1.00 23.42           C  
ATOM    864  CG  LEU A 105     -21.056  11.218  -7.720  1.00 24.51           C  
ATOM    865  CD1 LEU A 105     -21.151   9.692  -7.898  1.00 25.52           C  
ATOM    866  CD2 LEU A 105     -20.946  11.580  -6.244  1.00 24.85           C  
ATOM    867  N   TYR A 106     -21.064  13.434 -10.759  1.00 21.66           N  
ATOM    868  CA  TYR A 106     -22.248  14.119 -11.308  1.00 22.22           C  
ATOM    869  C   TYR A 106     -22.093  14.684 -12.725  1.00 21.45           C  
ATOM    870  O   TYR A 106     -23.044  15.255 -13.263  1.00 20.94           O  
ATOM    871  CB  TYR A 106     -22.659  15.227 -10.334  1.00 23.26           C  
ATOM    872  CG  TYR A 106     -23.071  14.734  -8.974  1.00 24.33           C  
ATOM    873  CD1 TYR A 106     -24.056  13.779  -8.840  1.00 26.13           C  
ATOM    874  CD2 TYR A 106     -22.515  15.265  -7.819  1.00 25.59           C  
ATOM    875  CE1 TYR A 106     -24.478  13.337  -7.593  1.00 27.13           C  
ATOM    876  CE2 TYR A 106     -22.909  14.823  -6.560  1.00 26.32           C  
ATOM    877  CZ  TYR A 106     -23.880  13.853  -6.471  1.00 27.31           C  
ATOM    878  OH  TYR A 106     -24.278  13.408  -5.263  1.00 29.20           O  
ATOM    879  N   GLY A 107     -20.905  14.540 -13.339  1.00 20.37           N  
ATOM    880  CA  GLY A 107     -20.731  14.937 -14.722  1.00 19.95           C  
ATOM    881  C   GLY A 107     -20.706  16.456 -14.929  1.00 19.78           C  
ATOM    882  O   GLY A 107     -21.164  16.921 -15.969  1.00 19.73           O  
ATOM    883  N   ASN A 108     -20.141  17.195 -13.962  1.00 18.99           N  
ATOM    884  CA  ASN A 108     -20.059  18.654 -14.004  1.00 18.77           C  
ATOM    885  C   ASN A 108     -18.620  19.106 -14.180  1.00 18.00           C  
ATOM    886  O   ASN A 108     -17.703  18.471 -13.673  1.00 18.09           O  
ATOM    887  CB  ASN A 108     -20.589  19.258 -12.714  1.00 18.82           C  
ATOM    888  CG  ASN A 108     -22.030  18.945 -12.490  1.00 19.72           C  
ATOM    889  OD1 ASN A 108     -22.805  18.909 -13.445  1.00 19.61           O  
ATOM    890  ND2 ASN A 108     -22.399  18.670 -11.243  1.00 19.89           N  
ATOM    891  N   LEU A 109     -18.440  20.237 -14.850  1.00 17.69           N  
ATOM    892  CA  LEU A 109     -17.176  20.972 -14.850  1.00 17.19           C  
ATOM    893  C   LEU A 109     -17.265  22.083 -13.827  1.00 17.92           C  
ATOM    894  O   LEU A 109     -18.249  22.848 -13.786  1.00 18.51           O  
ATOM    895  CB  LEU A 109     -16.858  21.578 -16.211  1.00 17.08           C  
ATOM    896  CG  LEU A 109     -16.336  20.620 -17.268  1.00 17.18           C  
ATOM    897  CD1 LEU A 109     -16.325  21.261 -18.648  1.00 17.22           C  
ATOM    898  CD2 LEU A 109     -14.923  20.143 -16.921  1.00 17.01           C  
ATOM    899  N   LEU A 110     -16.244  22.173 -12.995  1.00 17.71           N  
ATOM    900  CA  LEU A 110     -16.240  23.073 -11.864  1.00 18.49           C  
ATOM    901  C   LEU A 110     -15.021  23.962 -11.910  1.00 18.16           C  
ATOM    902  O   LEU A 110     -13.902  23.490 -12.168  1.00 18.38           O  
ATOM    903  CB  LEU A 110     -16.217  22.271 -10.579  1.00 19.01           C  
ATOM    904  CG  LEU A 110     -17.261  21.164 -10.423  1.00 19.56           C  
ATOM    905  CD1 LEU A 110     -16.956  20.418  -9.142  1.00 20.02           C  
ATOM    906  CD2 LEU A 110     -18.673  21.726 -10.362  1.00 19.74           C  
ATOM    907  N   LYS A 111     -15.229  25.251 -11.660  1.00 18.09           N  
ATOM    908  CA  LYS A 111     -14.136  26.184 -11.493  1.00 18.19           C  
ATOM    909  C   LYS A 111     -14.118  26.456 -10.000  1.00 18.37           C  
ATOM    910  O   LYS A 111     -15.152  26.827  -9.422  1.00 17.97           O  
ATOM    911  CB  LYS A 111     -14.379  27.452 -12.264  1.00 19.14           C  
ATOM    912  CG  LYS A 111     -13.165  28.385 -12.335  1.00 19.85           C  
ATOM    913  CD  LYS A 111     -13.608  29.594 -13.156  1.00 20.64           C  
ATOM    914  CE  LYS A 111     -12.535  30.612 -13.301  1.00 21.50           C  
ATOM    915  NZ  LYS A 111     -13.006  31.688 -14.220  1.00 21.85           N  
ATOM    916  N   VAL A 112     -12.969  26.200  -9.369  1.00 17.90           N  
ATOM    917  CA  VAL A 112     -12.851  26.278  -7.902  1.00 18.82           C  
ATOM    918  C   VAL A 112     -11.751  27.233  -7.460  1.00 18.79           C  
ATOM    919  O   VAL A 112     -10.836  27.547  -8.262  1.00 17.27           O  
ATOM    920  CB  VAL A 112     -12.635  24.896  -7.251  1.00 19.35           C  
ATOM    921  CG1 VAL A 112     -13.782  23.969  -7.590  1.00 19.57           C  
ATOM    922  CG2 VAL A 112     -11.297  24.272  -7.617  1.00 19.15           C  
ATOM    923  N   ASP A 113     -11.859  27.726  -6.218  1.00 19.22           N  
ATOM    924  CA  ASP A 113     -10.750  28.475  -5.612  1.00 20.08           C  
ATOM    925  C   ASP A 113      -9.761  27.533  -4.931  1.00 20.52           C  
ATOM    926  O   ASP A 113      -9.912  26.304  -4.995  1.00 19.14           O  
ATOM    927  CB  ASP A 113     -11.229  29.594  -4.689  1.00 20.97           C  
ATOM    928  CG  ASP A 113     -11.809  29.101  -3.389  1.00 21.45           C  
ATOM    929  OD1 ASP A 113     -11.711  27.880  -3.056  1.00 20.76           O  
ATOM    930  OD2 ASP A 113     -12.376  29.980  -2.713  1.00 22.02           O  
ATOM    931  N   ALA A 114      -8.742  28.116  -4.276  1.00 21.95           N  
ATOM    932  CA  ALA A 114      -7.694  27.321  -3.614  1.00 22.45           C  
ATOM    933  C   ALA A 114      -8.209  26.449  -2.483  1.00 23.21           C  
ATOM    934  O   ALA A 114      -7.507  25.521  -2.063  1.00 24.25           O  
ATOM    935  CB  ALA A 114      -6.614  28.248  -3.057  1.00 23.81           C  
ATOM    936  N   TYR A 115      -9.393  26.765  -1.955  1.00 22.42           N  
ATOM    937  CA  TYR A 115      -9.975  26.055  -0.821  1.00 23.10           C  
ATOM    938  C   TYR A 115     -11.087  25.100  -1.221  1.00 23.42           C  
ATOM    939  O   TYR A 115     -11.823  24.660  -0.371  1.00 25.07           O  
ATOM    940  CB  TYR A 115     -10.461  27.093   0.197  1.00 23.33           C  
ATOM    941  CG  TYR A 115      -9.289  27.902   0.672  1.00 23.12           C  
ATOM    942  CD1 TYR A 115      -8.425  27.378   1.622  1.00 23.57           C  
ATOM    943  CD2 TYR A 115      -9.019  29.158   0.150  1.00 23.08           C  
ATOM    944  CE1 TYR A 115      -7.320  28.076   2.062  1.00 23.63           C  
ATOM    945  CE2 TYR A 115      -7.900  29.877   0.561  1.00 23.86           C  
ATOM    946  CZ  TYR A 115      -7.050  29.333   1.538  1.00 24.05           C  
ATOM    947  OH  TYR A 115      -5.940  30.038   1.951  1.00 23.94           O  
ATOM    948  N   GLY A 116     -11.235  24.824  -2.518  1.00 22.81           N  
ATOM    949  CA  GLY A 116     -12.284  23.947  -3.025  1.00 22.55           C  
ATOM    950  C   GLY A 116     -13.670  24.569  -3.091  1.00 22.38           C  
ATOM    951  O   GLY A 116     -14.632  23.836  -3.283  1.00 22.46           O  
ATOM    952  N   ASN A 117     -13.791  25.891  -2.932  1.00 22.20           N  
ATOM    953  CA  ASN A 117     -15.100  26.542  -2.999  1.00 22.59           C  
ATOM    954  C   ASN A 117     -15.490  26.693  -4.469  1.00 22.02           C  
ATOM    955  O   ASN A 117     -14.657  27.009  -5.324  1.00 20.78           O  
ATOM    956  CB  ASN A 117     -15.120  27.918  -2.349  1.00 23.03           C  
ATOM    957  CG  ASN A 117     -14.736  27.865  -0.911  1.00 23.73           C  
ATOM    958  OD1 ASN A 117     -15.293  27.080  -0.158  1.00 23.77           O  
ATOM    959  ND2 ASN A 117     -13.767  28.679  -0.517  1.00 23.62           N  
ATOM    960  N   LEU A 118     -16.754  26.447  -4.750  1.00 22.42           N  
ATOM    961  CA  LEU A 118     -17.226  26.462  -6.112  1.00 22.78           C  
ATOM    962  C   LEU A 118     -17.371  27.889  -6.565  1.00 22.46           C  
ATOM    963  O   LEU A 118     -18.028  28.660  -5.907  1.00 23.13           O  
ATOM    964  CB  LEU A 118     -18.582  25.771  -6.203  1.00 24.56           C  
ATOM    965  CG  LEU A 118     -18.605  24.349  -6.708  1.00 26.42           C  
ATOM    966  CD1 LEU A 118     -17.670  23.475  -5.926  1.00 28.33           C  
ATOM    967  CD2 LEU A 118     -20.038  23.821  -6.650  1.00 27.69           C  
ATOM    968  N   LEU A 119     -16.779  28.234  -7.697  1.00 21.46           N  
ATOM    969  CA  LEU A 119     -16.986  29.510  -8.336  1.00 21.61           C  
ATOM    970  C   LEU A 119     -17.963  29.408  -9.532  1.00 21.99           C  
ATOM    971  O   LEU A 119     -18.749  30.335  -9.755  1.00 22.01           O  
ATOM    972  CB  LEU A 119     -15.655  30.055  -8.807  1.00 21.72           C  
ATOM    973  CG  LEU A 119     -14.573  30.189  -7.703  1.00 22.07           C  
ATOM    974  CD1 LEU A 119     -13.259  30.651  -8.272  1.00 21.93           C  
ATOM    975  CD2 LEU A 119     -15.078  31.169  -6.640  1.00 23.27           C  
ATOM    976  N   VAL A 120     -17.859  28.319 -10.307  1.00 21.20           N  
ATOM    977  CA  VAL A 120     -18.682  28.092 -11.503  1.00 21.23           C  
ATOM    978  C   VAL A 120     -18.971  26.608 -11.588  1.00 20.78           C  
ATOM    979  O   VAL A 120     -18.090  25.811 -11.331  1.00 18.90           O  
ATOM    980  CB  VAL A 120     -17.976  28.488 -12.813  1.00 20.88           C  
ATOM    981  CG1 VAL A 120     -18.941  28.328 -14.003  1.00 21.40           C  
ATOM    982  CG2 VAL A 120     -17.473  29.921 -12.731  1.00 21.67           C  
ATOM    983  N   CYS A 121     -20.195  26.253 -11.973  1.00 20.99           N  
ATOM    984  CA  CYS A 121     -20.539  24.855 -12.201  1.00 21.62           C  
ATOM    985  C   CYS A 121     -21.361  24.753 -13.479  1.00 21.37           C  
ATOM    986  O   CYS A 121     -22.428  25.366 -13.579  1.00 21.93           O  
ATOM    987  CB  CYS A 121     -21.379  24.332 -11.044  1.00 22.58           C  
ATOM    988  SG  CYS A 121     -22.062  22.647 -11.238  1.00 24.26           S  
ATOM    989  N   ALA A 122     -20.911  23.932 -14.412  1.00 20.40           N  
ATOM    990  CA  ALA A 122     -21.663  23.712 -15.648  1.00 20.43           C  
ATOM    991  C   ALA A 122     -21.898  22.229 -15.862  1.00 19.98           C  
ATOM    992  O   ALA A 122     -20.967  21.419 -15.761  1.00 19.14           O  
ATOM    993  CB  ALA A 122     -20.930  24.306 -16.838  1.00 20.37           C  
ATOM    994  N   HIS A 123     -23.151  21.891 -16.147  1.00 20.10           N  
ATOM    995  CA  HIS A 123     -23.529  20.549 -16.528  1.00 20.02           C  
ATOM    996  C   HIS A 123     -23.821  20.557 -18.033  1.00 20.36           C  
ATOM    997  O   HIS A 123     -24.798  21.151 -18.477  1.00 19.72           O  
ATOM    998  CB  HIS A 123     -24.740  20.101 -15.736  1.00 20.64           C  
ATOM    999  CG  HIS A 123     -25.022  18.653 -15.890  1.00 20.82           C  
ATOM   1000  ND1 HIS A 123     -24.251  17.688 -15.282  1.00 20.72           N  
ATOM   1001  CD2 HIS A 123     -25.949  17.997 -16.616  1.00 21.37           C  
ATOM   1002  CE1 HIS A 123     -24.697  16.492 -15.620  1.00 21.09           C  
ATOM   1003  NE2 HIS A 123     -25.728  16.650 -16.429  1.00 21.79           N  
ATOM   1004  N   GLY A 124     -22.919  19.954 -18.806  1.00 19.75           N  
ATOM   1005  CA  GLY A 124     -22.927  20.129 -20.252  1.00 20.30           C  
ATOM   1006  C   GLY A 124     -22.682  21.603 -20.537  1.00 20.38           C  
ATOM   1007  O   GLY A 124     -21.704  22.171 -20.060  1.00 19.43           O  
ATOM   1008  N   PHE A 125     -23.607  22.240 -21.254  1.00 20.65           N  
ATOM   1009  CA  PHE A 125     -23.520  23.674 -21.478  1.00 21.60           C  
ATOM   1010  C   PHE A 125     -24.479  24.511 -20.603  1.00 23.34           C  
ATOM   1011  O   PHE A 125     -24.667  25.698 -20.859  1.00 24.34           O  
ATOM   1012  CB  PHE A 125     -23.736  23.974 -22.975  1.00 21.78           C  
ATOM   1013  CG  PHE A 125     -22.759  23.259 -23.893  1.00 21.22           C  
ATOM   1014  CD1 PHE A 125     -21.380  23.345 -23.679  1.00 20.90           C  
ATOM   1015  CD2 PHE A 125     -23.209  22.526 -24.962  1.00 21.57           C  
ATOM   1016  CE1 PHE A 125     -20.489  22.686 -24.514  1.00 20.66           C  
ATOM   1017  CE2 PHE A 125     -22.317  21.882 -25.814  1.00 21.89           C  
ATOM   1018  CZ  PHE A 125     -20.963  21.951 -25.579  1.00 21.08           C  
ATOM   1019  N  AASN A 126     -25.099  23.893 -19.594  0.50 23.80           N  
ATOM   1020  N  BASN A 126     -25.066  23.898 -19.585  0.50 24.10           N  
ATOM   1021  CA AASN A 126     -26.014  24.580 -18.669  0.50 24.75           C  
ATOM   1022  CA BASN A 126     -25.963  24.600 -18.694  0.50 25.20           C  
ATOM   1023  C  AASN A 126     -25.193  25.035 -17.473  0.50 24.73           C  
ATOM   1024  C  BASN A 126     -25.179  25.037 -17.476  0.50 25.01           C  
ATOM   1025  O  AASN A 126     -24.665  24.196 -16.733  0.50 23.82           O  
ATOM   1026  O  BASN A 126     -24.672  24.195 -16.726  0.50 24.10           O  
ATOM   1027  CB AASN A 126     -27.128  23.628 -18.196  0.50 25.44           C  
ATOM   1028  CB BASN A 126     -27.101  23.692 -18.281  0.50 26.32           C  
ATOM   1029  CG AASN A 126     -28.194  24.315 -17.320  0.50 26.40           C  
ATOM   1030  CG BASN A 126     -28.088  23.466 -19.400  0.50 27.46           C  
ATOM   1031  OD1AASN A 126     -28.376  25.539 -17.354  0.50 26.64           O  
ATOM   1032  OD1BASN A 126     -28.163  24.244 -20.355  0.50 28.25           O  
ATOM   1033  ND2AASN A 126     -28.925  23.504 -16.543  0.50 26.69           N  
ATOM   1034  ND2BASN A 126     -28.877  22.412 -19.275  0.50 28.38           N  
ATOM   1035  N   PHE A 127     -25.072  26.355 -17.317  1.00 25.35           N  
ATOM   1036  CA  PHE A 127     -24.416  26.968 -16.181  1.00 26.33           C  
ATOM   1037  C   PHE A 127     -25.362  27.021 -14.998  1.00 27.70           C  
ATOM   1038  O   PHE A 127     -26.419  27.583 -15.079  1.00 27.68           O  
ATOM   1039  CB  PHE A 127     -23.813  28.326 -16.581  1.00 26.88           C  
ATOM   1040  CG  PHE A 127     -22.545  28.160 -17.408  1.00 26.36           C  
ATOM   1041  CD1 PHE A 127     -22.628  27.751 -18.767  1.00 26.75           C  
ATOM   1042  CD2 PHE A 127     -21.301  28.327 -16.840  1.00 25.81           C  
ATOM   1043  CE1 PHE A 127     -21.498  27.566 -19.551  1.00 26.24           C  
ATOM   1044  CE2 PHE A 127     -20.154  28.145 -17.602  1.00 25.81           C  
ATOM   1045  CZ  PHE A 127     -20.243  27.750 -18.950  1.00 25.93           C  
ATOM   1046  N   ILE A 128     -24.992  26.328 -13.934  1.00 28.61           N  
ATOM   1047  CA  ILE A 128     -25.871  26.091 -12.804  1.00 31.55           C  
ATOM   1048  C   ILE A 128     -25.632  27.210 -11.786  1.00 32.86           C  
ATOM   1049  O   ILE A 128     -24.478  27.476 -11.406  1.00 30.99           O  
ATOM   1050  CB  ILE A 128     -25.596  24.715 -12.131  1.00 32.40           C  
ATOM   1051  CG1 ILE A 128     -25.627  23.558 -13.155  1.00 32.58           C  
ATOM   1052  CG2 ILE A 128     -26.605  24.458 -11.009  1.00 34.13           C  
ATOM   1053  CD1 ILE A 128     -26.921  23.414 -13.938  1.00 33.18           C  
ATOM   1054  N   ARG A 129     -26.727  27.829 -11.360  1.00 52.93           N  
ATOM   1055  CA  ARG A 129     -26.708  28.996 -10.484  1.00 56.54           C  
ATOM   1056  C   ARG A 129     -26.527  28.561  -9.047  1.00 53.63           C  
ATOM   1057  O   ARG A 129     -26.674  27.379  -8.742  1.00 50.68           O  
ATOM   1058  CB  ARG A 129     -28.025  29.747 -10.585  1.00 63.03           C  
ATOM   1059  CG  ARG A 129     -28.316  30.296 -11.959  1.00 68.64           C  
ATOM   1060  CD  ARG A 129     -29.411  31.347 -11.883  1.00 76.32           C  
ATOM   1061  NE  ARG A 129     -29.576  32.043 -13.154  1.00 82.61           N  
ATOM   1062  CZ  ARG A 129     -30.334  33.119 -13.334  1.00 90.58           C  
ATOM   1063  NH1 ARG A 129     -31.022  33.648 -12.319  1.00 94.28           N  
ATOM   1064  NH2 ARG A 129     -30.413  33.681 -14.542  1.00 96.06           N  
ATOM   1065  N   GLY A 130     -26.253  29.527  -8.170  1.00 54.80           N  
ATOM   1066  CA  GLY A 130     -25.932  29.261  -6.758  1.00 52.64           C  
ATOM   1067  C   GLY A 130     -26.826  28.244  -6.048  1.00 51.79           C  
ATOM   1068  O   GLY A 130     -26.325  27.190  -5.598  1.00 49.16           O  
ATOM   1069  N   PRO A 131     -28.142  28.533  -5.946  1.00 54.30           N  
ATOM   1070  CA  PRO A 131     -29.096  27.640  -5.249  1.00 54.28           C  
ATOM   1071  C   PRO A 131     -29.224  26.221  -5.788  1.00 51.48           C  
ATOM   1072  O   PRO A 131     -29.228  25.267  -5.005  1.00 48.96           O  
ATOM   1073  CB  PRO A 131     -30.432  28.402  -5.366  1.00 59.77           C  
ATOM   1074  CG  PRO A 131     -30.022  29.832  -5.393  1.00 61.81           C  
ATOM   1075  CD  PRO A 131     -28.740  29.867  -6.186  1.00 59.21           C  
ATOM   1076  N   GLU A 132     -29.296  26.066  -7.106  1.00 51.74           N  
ATOM   1077  CA  GLU A 132     -29.321  24.724  -7.701  1.00 50.28           C  
ATOM   1078  C   GLU A 132     -28.004  23.932  -7.490  1.00 45.52           C  
ATOM   1079  O   GLU A 132     -28.029  22.688  -7.473  1.00 44.18           O  
ATOM   1080  CB  GLU A 132     -29.675  24.787  -9.193  1.00 53.25           C  
ATOM   1081  CG  GLU A 132     -29.734  23.411  -9.890  1.00 53.02           C  
ATOM   1082  CD  GLU A 132     -30.134  23.475 -11.372  1.00 56.47           C  
ATOM   1083  OE1 GLU A 132     -30.686  24.529 -11.801  1.00 58.92           O  
ATOM   1084  OE2 GLU A 132     -29.866  22.467 -12.099  1.00 55.43           O  
ATOM   1085  N   THR A 133     -26.863  24.604  -7.302  1.00 42.90           N  
ATOM   1086  CA  THR A 133     -25.610  23.835  -7.060  1.00 39.18           C  
ATOM   1087  C   THR A 133     -25.627  23.181  -5.669  1.00 37.10           C  
ATOM   1088  O   THR A 133     -25.004  22.152  -5.473  1.00 33.74           O  
ATOM   1089  CB  THR A 133     -24.299  24.646  -7.197  1.00 38.66           C  
ATOM   1090  OG1 THR A 133     -24.150  25.518  -6.077  1.00 41.41           O  
ATOM   1091  CG2 THR A 133     -24.266  25.449  -8.487  1.00 40.08           C  
ATOM   1092  N   ARG A 134     -26.360  23.768  -4.722  1.00 38.92           N  
ATOM   1093  CA  ARG A 134     -26.448  23.205  -3.365  1.00 38.61           C  
ATOM   1094  C   ARG A 134     -27.057  21.832  -3.270  1.00 37.90           C  
ATOM   1095  O   ARG A 134     -26.720  21.089  -2.376  1.00 37.07           O  
ATOM   1096  CB  ARG A 134     -27.133  24.177  -2.403  1.00 41.85           C  
ATOM   1097  CG  ARG A 134     -26.216  25.338  -2.104  1.00 42.18           C  
ATOM   1098  CD  ARG A 134     -26.577  26.037  -0.830  1.00 45.28           C  
ATOM   1099  NE  ARG A 134     -25.702  27.189  -0.640  1.00 46.05           N  
ATOM   1100  CZ  ARG A 134     -24.550  27.215   0.048  1.00 43.97           C  
ATOM   1101  NH1 ARG A 134     -24.050  26.137   0.662  1.00 41.59           N  
ATOM   1102  NH2 ARG A 134     -23.899  28.373   0.132  1.00 45.04           N  
ATOM   1103  N   GLU A 135     -27.886  21.456  -4.230  1.00 39.06           N  
ATOM   1104  CA  GLU A 135     -28.465  20.104  -4.237  1.00 39.89           C  
ATOM   1105  C   GLU A 135     -27.344  19.044  -4.286  1.00 35.60           C  
ATOM   1106  O   GLU A 135     -27.335  18.138  -3.480  1.00 36.25           O  
ATOM   1107  CB  GLU A 135     -29.482  19.939  -5.386  1.00 43.40           C  
ATOM   1108  CG  GLU A 135     -30.607  20.993  -5.360  1.00 48.68           C  
ATOM   1109  CD  GLU A 135     -31.461  21.044  -6.642  1.00 53.14           C  
ATOM   1110  OE1 GLU A 135     -30.923  20.826  -7.758  1.00 54.59           O  
ATOM   1111  OE2 GLU A 135     -32.672  21.331  -6.540  1.00 58.05           O  
ATOM   1112  N   GLN A 136     -26.376  19.203  -5.193  1.00 31.61           N  
ATOM   1113  CA  GLN A 136     -25.225  18.275  -5.325  1.00 28.66           C  
ATOM   1114  C   GLN A 136     -24.001  18.654  -4.480  1.00 26.46           C  
ATOM   1115  O   GLN A 136     -23.179  17.810  -4.176  1.00 26.44           O  
ATOM   1116  CB  GLN A 136     -24.791  18.166  -6.808  1.00 26.99           C  
ATOM   1117  CG  GLN A 136     -25.864  17.534  -7.673  1.00 29.00           C  
ATOM   1118  CD  GLN A 136     -25.511  17.383  -9.138  1.00 28.28           C  
ATOM   1119  OE1 GLN A 136     -24.724  18.144  -9.695  1.00 26.34           O  
ATOM   1120  NE2 GLN A 136     -26.115  16.411  -9.765  1.00 29.36           N  
ATOM   1121  N   TYR A 137     -23.855  19.928  -4.153  1.00 25.95           N  
ATOM   1122  CA  TYR A 137     -22.710  20.429  -3.400  1.00 24.81           C  
ATOM   1123  C   TYR A 137     -23.270  21.238  -2.235  1.00 26.32           C  
ATOM   1124  O   TYR A 137     -23.319  22.468  -2.307  1.00 26.19           O  
ATOM   1125  CB  TYR A 137     -21.826  21.302  -4.314  1.00 23.48           C  
ATOM   1126  CG  TYR A 137     -21.415  20.609  -5.586  1.00 21.80           C  
ATOM   1127  CD1 TYR A 137     -20.306  19.776  -5.612  1.00 20.34           C  
ATOM   1128  CD2 TYR A 137     -22.156  20.775  -6.765  1.00 22.30           C  
ATOM   1129  CE1 TYR A 137     -19.942  19.110  -6.759  1.00 19.50           C  
ATOM   1130  CE2 TYR A 137     -21.788  20.135  -7.927  1.00 21.74           C  
ATOM   1131  CZ  TYR A 137     -20.668  19.305  -7.929  1.00 20.19           C  
ATOM   1132  OH  TYR A 137     -20.300  18.661  -9.088  1.00 19.61           O  
ATOM   1133  N   PRO A 138     -23.721  20.546  -1.161  1.00 28.22           N  
ATOM   1134  CA  PRO A 138     -24.416  21.241  -0.063  1.00 30.12           C  
ATOM   1135  C   PRO A 138     -23.599  22.351   0.603  1.00 30.01           C  
ATOM   1136  O   PRO A 138     -24.181  23.317   1.121  1.00 32.13           O  
ATOM   1137  CB  PRO A 138     -24.710  20.120   0.934  1.00 32.01           C  
ATOM   1138  CG  PRO A 138     -24.699  18.862   0.131  1.00 31.28           C  
ATOM   1139  CD  PRO A 138     -23.687  19.081  -0.958  1.00 28.51           C  
ATOM   1140  N   ASN A 139     -22.264  22.239   0.561  1.00 27.65           N  
ATOM   1141  CA  ASN A 139     -21.399  23.240   1.157  1.00 27.58           C  
ATOM   1142  C   ASN A 139     -20.696  24.104   0.093  1.00 26.12           C  
ATOM   1143  O   ASN A 139     -19.770  24.851   0.413  1.00 25.85           O  
ATOM   1144  CB  ASN A 139     -20.419  22.528   2.102  1.00 27.55           C  
ATOM   1145  CG  ASN A 139     -19.672  23.479   3.011  1.00 28.99           C  
ATOM   1146  OD1 ASN A 139     -20.202  24.497   3.511  1.00 30.04           O  
ATOM   1147  ND2 ASN A 139     -18.370  23.174   3.205  1.00 29.17           N  
ATOM   1148  N   LYS A 140     -21.173  24.050  -1.152  1.00 25.20           N  
ATOM   1149  CA  LYS A 140     -20.520  24.732  -2.266  1.00 24.83           C  
ATOM   1150  C   LYS A 140     -18.973  24.491  -2.236  1.00 22.69           C  
ATOM   1151  O   LYS A 140     -18.202  25.400  -2.361  1.00 22.77           O  
ATOM   1152  CB  LYS A 140     -20.880  26.236  -2.261  1.00 28.04           C  
ATOM   1153  CG  LYS A 140     -22.076  26.592  -3.163  1.00 30.97           C  
ATOM   1154  CD  LYS A 140     -22.342  28.094  -3.171  1.00 34.87           C  
ATOM   1155  CE  LYS A 140     -23.636  28.403  -3.908  1.00 38.10           C  
ATOM   1156  NZ  LYS A 140     -24.227  29.746  -3.579  1.00 42.65           N  
ATOM   1157  N   PHE A 141     -18.602  23.234  -2.113  1.00 21.31           N  
ATOM   1158  CA  PHE A 141     -17.252  22.806  -1.781  1.00 21.22           C  
ATOM   1159  C   PHE A 141     -17.006  21.418  -2.320  1.00 20.37           C  
ATOM   1160  O   PHE A 141     -17.892  20.566  -2.270  1.00 20.00           O  
ATOM   1161  CB  PHE A 141     -17.097  22.822  -0.247  1.00 22.53           C  
ATOM   1162  CG  PHE A 141     -15.883  22.115   0.270  1.00 22.91           C  
ATOM   1163  CD1 PHE A 141     -14.663  22.764   0.334  1.00 23.37           C  
ATOM   1164  CD2 PHE A 141     -15.957  20.801   0.702  1.00 23.23           C  
ATOM   1165  CE1 PHE A 141     -13.545  22.121   0.848  1.00 24.38           C  
ATOM   1166  CE2 PHE A 141     -14.838  20.159   1.230  1.00 24.44           C  
ATOM   1167  CZ  PHE A 141     -13.631  20.822   1.287  1.00 24.78           C  
ATOM   1168  N   ILE A 142     -15.788  21.187  -2.803  1.00 20.32           N  
ATOM   1169  CA  ILE A 142     -15.350  19.844  -3.136  1.00 21.18           C  
ATOM   1170  C   ILE A 142     -14.024  19.584  -2.426  1.00 23.12           C  
ATOM   1171  O   ILE A 142     -13.259  20.520  -2.209  1.00 22.58           O  
ATOM   1172  CB  ILE A 142     -15.144  19.641  -4.646  1.00 20.45           C  
ATOM   1173  CG1 ILE A 142     -14.143  20.642  -5.213  1.00 21.39           C  
ATOM   1174  CG2 ILE A 142     -16.461  19.809  -5.404  1.00 20.62           C  
ATOM   1175  CD1 ILE A 142     -13.447  20.178  -6.498  1.00 21.75           C  
ATOM   1176  N   GLN A 143     -13.779  18.319  -2.110  1.00 25.74           N  
ATOM   1177  CA  GLN A 143     -12.502  17.886  -1.518  1.00 29.48           C  
ATOM   1178  C   GLN A 143     -11.610  17.558  -2.683  1.00 29.71           C  
ATOM   1179  O   GLN A 143     -11.718  16.462  -3.230  1.00 29.08           O  
ATOM   1180  CB  GLN A 143     -12.674  16.626  -0.682  1.00 32.99           C  
ATOM   1181  CG  GLN A 143     -13.801  16.608   0.330  1.00 35.65           C  
ATOM   1182  CD  GLN A 143     -13.874  15.260   1.081  1.00 40.32           C  
ATOM   1183  OE1 GLN A 143     -13.812  14.166   0.467  1.00 41.54           O  
ATOM   1184  NE2 GLN A 143     -13.982  15.328   2.409  1.00 42.42           N  
ATOM   1185  N   ARG A 144     -10.770  18.485  -3.113  1.00 31.63           N  
ATOM   1186  CA  ARG A 144     -10.039  18.264  -4.377  1.00 34.53           C  
ATOM   1187  C   ARG A 144      -9.008  17.129  -4.305  1.00 37.35           C  
ATOM   1188  O   ARG A 144      -8.700  16.559  -5.325  1.00 41.40           O  
ATOM   1189  CB  ARG A 144      -9.408  19.553  -4.948  1.00 36.04           C  
ATOM   1190  CG  ARG A 144      -8.161  20.049  -4.242  1.00 38.89           C  
ATOM   1191  CD  ARG A 144      -7.512  21.201  -5.011  1.00 40.05           C  
ATOM   1192  NE  ARG A 144      -6.379  21.746  -4.280  1.00 43.46           N  
ATOM   1193  CZ  ARG A 144      -6.484  22.548  -3.222  1.00 45.05           C  
ATOM   1194  NH1 ARG A 144      -7.685  22.940  -2.771  1.00 44.65           N  
ATOM   1195  NH2 ARG A 144      -5.389  22.968  -2.616  1.00 48.01           N  
ATOM   1196  N   ASP A 145      -8.537  16.791  -3.115  1.00 39.83           N  
ATOM   1197  CA  ASP A 145      -7.693  15.598  -2.885  1.00 43.86           C  
ATOM   1198  C   ASP A 145      -8.392  14.247  -3.158  1.00 40.72           C  
ATOM   1199  O   ASP A 145      -7.719  13.237  -3.174  1.00 41.02           O  
ATOM   1200  CB  ASP A 145      -7.121  15.581  -1.437  1.00 49.21           C  
ATOM   1201  CG  ASP A 145      -8.229  15.632  -0.329  1.00 52.87           C  
ATOM   1202  OD1 ASP A 145      -9.434  15.952  -0.633  1.00 53.90           O  
ATOM   1203  OD2 ASP A 145      -7.873  15.405   0.862  1.00 58.17           O  
ATOM   1204  N   ASP A 146      -9.719  14.236  -3.340  1.00 35.44           N  
ATOM   1205  CA  ASP A 146     -10.457  13.026  -3.705  1.00 34.00           C  
ATOM   1206  C   ASP A 146     -10.270  12.807  -5.208  1.00 32.55           C  
ATOM   1207  O   ASP A 146     -11.131  13.161  -6.058  1.00 28.96           O  
ATOM   1208  CB  ASP A 146     -11.931  13.144  -3.295  1.00 32.10           C  
ATOM   1209  CG  ASP A 146     -12.753  11.911  -3.639  1.00 32.64           C  
ATOM   1210  OD1 ASP A 146     -12.222  10.914  -4.149  1.00 33.88           O  
ATOM   1211  OD2 ASP A 146     -13.970  11.967  -3.434  1.00 32.10           O  
ATOM   1212  N   THR A 147      -9.129  12.210  -5.526  1.00 34.18           N  
ATOM   1213  CA  THR A 147      -8.684  12.088  -6.907  1.00 34.31           C  
ATOM   1214  C   THR A 147      -9.400  10.962  -7.676  1.00 35.24           C  
ATOM   1215  O   THR A 147      -9.376  10.976  -8.900  1.00 35.00           O  
ATOM   1216  CB  THR A 147      -7.161  11.892  -6.988  1.00 36.97           C  
ATOM   1217  OG1 THR A 147      -6.819  10.694  -6.308  1.00 39.99           O  
ATOM   1218  CG2 THR A 147      -6.428  13.062  -6.334  1.00 37.05           C  
ATOM   1219  N   GLU A 148     -10.044  10.015  -6.992  1.00 36.69           N  
ATOM   1220  CA  GLU A 148     -10.923   9.053  -7.671  1.00 37.99           C  
ATOM   1221  C   GLU A 148     -12.159   9.754  -8.253  1.00 33.78           C  
ATOM   1222  O   GLU A 148     -12.645   9.355  -9.311  1.00 34.83           O  
ATOM   1223  CB  GLU A 148     -11.420   7.934  -6.745  1.00 42.53           C  
ATOM   1224  CG  GLU A 148     -10.345   7.153  -5.980  1.00 48.70           C  
ATOM   1225  CD  GLU A 148      -9.567   6.165  -6.832  1.00 53.04           C  
ATOM   1226  OE1 GLU A 148      -9.441   5.002  -6.403  1.00 59.64           O  
ATOM   1227  OE2 GLU A 148      -9.049   6.550  -7.911  1.00 53.30           O  
ATOM   1228  N   ARG A 149     -12.662  10.789  -7.579  1.00 29.79           N  
ATOM   1229  CA  ARG A 149     -13.844  11.501  -8.040  1.00 26.72           C  
ATOM   1230  C   ARG A 149     -13.565  12.723  -8.933  1.00 24.25           C  
ATOM   1231  O   ARG A 149     -14.295  12.963  -9.905  1.00 22.94           O  
ATOM   1232  CB  ARG A 149     -14.702  11.935  -6.848  1.00 26.19           C  
ATOM   1233  CG  ARG A 149     -15.891  12.785  -7.206  1.00 24.41           C  
ATOM   1234  CD  ARG A 149     -16.860  12.955  -6.049  1.00 25.32           C  
ATOM   1235  NE  ARG A 149     -17.846  13.978  -6.385  1.00 23.94           N  
ATOM   1236  CZ  ARG A 149     -18.686  14.540  -5.518  1.00 24.61           C  
ATOM   1237  NH1 ARG A 149     -18.669  14.198  -4.237  1.00 26.11           N  
ATOM   1238  NH2 ARG A 149     -19.532  15.476  -5.929  1.00 23.83           N  
ATOM   1239  N   PHE A 150     -12.549  13.503  -8.587  1.00 23.45           N  
ATOM   1240  CA  PHE A 150     -12.290  14.785  -9.227  1.00 22.20           C  
ATOM   1241  C   PHE A 150     -11.013  14.722 -10.062  1.00 23.35           C  
ATOM   1242  O   PHE A 150      -9.960  14.318  -9.559  1.00 24.77           O  
ATOM   1243  CB  PHE A 150     -12.180  15.892  -8.167  1.00 22.22           C  
ATOM   1244  CG  PHE A 150     -13.433  16.078  -7.349  1.00 21.70           C  
ATOM   1245  CD1 PHE A 150     -14.578  16.616  -7.926  1.00 21.12           C  
ATOM   1246  CD2 PHE A 150     -13.469  15.728  -5.994  1.00 23.17           C  
ATOM   1247  CE1 PHE A 150     -15.743  16.784  -7.176  1.00 21.10           C  
ATOM   1248  CE2 PHE A 150     -14.647  15.879  -5.248  1.00 23.07           C  
ATOM   1249  CZ  PHE A 150     -15.768  16.418  -5.843  1.00 21.83           C  
ATOM   1250  N   TYR A 151     -11.092  15.118 -11.332  1.00 22.04           N  
ATOM   1251  CA  TYR A 151      -9.906  15.226 -12.152  1.00 23.05           C  
ATOM   1252  C   TYR A 151      -9.715  16.693 -12.547  1.00 22.23           C  
ATOM   1253  O   TYR A 151     -10.607  17.302 -13.165  1.00 21.10           O  
ATOM   1254  CB  TYR A 151     -10.034  14.334 -13.384  1.00 23.95           C  
ATOM   1255  CG  TYR A 151      -8.745  14.197 -14.164  1.00 26.09           C  
ATOM   1256  CD1 TYR A 151      -8.432  15.076 -15.178  1.00 26.68           C  
ATOM   1257  CD2 TYR A 151      -7.868  13.130 -13.930  1.00 28.65           C  
ATOM   1258  CE1 TYR A 151      -7.259  14.944 -15.927  1.00 29.27           C  
ATOM   1259  CE2 TYR A 151      -6.668  12.993 -14.651  1.00 31.15           C  
ATOM   1260  CZ  TYR A 151      -6.369  13.901 -15.647  1.00 31.44           C  
ATOM   1261  OH  TYR A 151      -5.211  13.782 -16.380  1.00 34.96           O  
ATOM   1262  N   ILE A 152      -8.549  17.238 -12.236  1.00 22.49           N  
ATOM   1263  CA  ILE A 152      -8.233  18.631 -12.528  1.00 23.06           C  
ATOM   1264  C   ILE A 152      -7.508  18.726 -13.877  1.00 24.62           C  
ATOM   1265  O   ILE A 152      -6.423  18.165 -14.079  1.00 25.73           O  
ATOM   1266  CB  ILE A 152      -7.433  19.288 -11.384  1.00 24.53           C  
ATOM   1267  CG1 ILE A 152      -8.198  19.118 -10.057  1.00 23.74           C  
ATOM   1268  CG2 ILE A 152      -7.223  20.783 -11.655  1.00 25.48           C  
ATOM   1269  CD1 ILE A 152      -7.414  19.572  -8.839  1.00 25.54           C  
ATOM   1270  N   LEU A 153      -8.127  19.477 -14.782  1.00 19.68           N  
ATOM   1271  CA  LEU A 153      -7.717  19.578 -16.173  1.00 19.95           C  
ATOM   1272  C   LEU A 153      -6.747  20.769 -16.294  1.00 20.31           C  
ATOM   1273  O   LEU A 153      -7.065  21.800 -16.879  1.00 20.24           O  
ATOM   1274  CB  LEU A 153      -8.963  19.742 -17.062  1.00 19.66           C  
ATOM   1275  CG  LEU A 153      -9.909  18.519 -17.033  1.00 19.96           C  
ATOM   1276  CD1 LEU A 153     -11.359  18.910 -17.264  1.00 19.83           C  
ATOM   1277  CD2 LEU A 153      -9.504  17.441 -18.046  1.00 20.62           C  
ATOM   1278  N  AASN A 154      -5.535  20.535 -15.799  0.50 21.41           N  
ATOM   1279  N  BASN A 154      -5.555  20.667 -15.726  0.50 21.51           N  
ATOM   1280  CA AASN A 154      -4.553  21.584 -15.552  0.50 22.08           C  
ATOM   1281  CA BASN A 154      -4.706  21.862 -15.657  0.50 22.06           C  
ATOM   1282  C  AASN A 154      -3.575  21.941 -16.665  0.50 21.79           C  
ATOM   1283  C  BASN A 154      -3.566  21.980 -16.679  0.50 21.85           C  
ATOM   1284  O  AASN A 154      -2.868  22.944 -16.558  0.50 22.02           O  
ATOM   1285  O  BASN A 154      -2.747  22.884 -16.535  0.50 22.11           O  
ATOM   1286  CB AASN A 154      -3.757  21.220 -14.316  0.50 23.77           C  
ATOM   1287  CB BASN A 154      -4.187  22.064 -14.237  0.50 23.75           C  
ATOM   1288  CG AASN A 154      -4.338  21.834 -13.071  0.50 24.80           C  
ATOM   1289  CG BASN A 154      -3.352  20.919 -13.783  0.50 24.88           C  
ATOM   1290  OD1AASN A 154      -4.978  22.892 -13.112  0.50 24.65           O  
ATOM   1291  OD1BASN A 154      -2.996  20.083 -14.592  0.50 24.90           O  
ATOM   1292  ND2AASN A 154      -4.144  21.165 -11.958  0.50 26.27           N  
ATOM   1293  ND2BASN A 154      -3.013  20.877 -12.494  0.50 26.54           N  
ATOM   1294  N   THR A 155      -3.509  21.120 -17.701  1.00 21.09           N  
ATOM   1295  CA  THR A 155      -2.574  21.354 -18.816  1.00 21.78           C  
ATOM   1296  C   THR A 155      -3.270  21.899 -20.049  1.00 20.37           C  
ATOM   1297  O   THR A 155      -4.488  21.720 -20.256  1.00 18.54           O  
ATOM   1298  CB  THR A 155      -1.782  20.092 -19.218  1.00 22.73           C  
ATOM   1299  OG1 THR A 155      -2.592  19.270 -20.060  1.00 22.59           O  
ATOM   1300  CG2 THR A 155      -1.341  19.302 -17.960  1.00 24.33           C  
ATOM   1301  N   LEU A 156      -2.475  22.542 -20.902  1.00 20.99           N  
ATOM   1302  CA  LEU A 156      -2.984  23.018 -22.181  1.00 21.31           C  
ATOM   1303  C   LEU A 156      -3.425  21.836 -23.072  1.00 20.25           C  
ATOM   1304  O   LEU A 156      -4.388  21.970 -23.821  1.00 19.38           O  
ATOM   1305  CB  LEU A 156      -1.972  23.921 -22.858  1.00 23.36           C  
ATOM   1306  CG  LEU A 156      -1.806  25.240 -22.082  1.00 24.96           C  
ATOM   1307  CD1 LEU A 156      -0.375  25.687 -22.111  1.00 27.60           C  
ATOM   1308  CD2 LEU A 156      -2.734  26.293 -22.616  1.00 25.09           C  
ATOM   1309  N   PHE A 157      -2.778  20.678 -22.950  1.00 20.16           N  
ATOM   1310  CA  PHE A 157      -3.252  19.481 -23.648  1.00 20.64           C  
ATOM   1311  C   PHE A 157      -4.652  19.016 -23.223  1.00 19.98           C  
ATOM   1312  O   PHE A 157      -5.309  18.281 -23.984  1.00 20.83           O  
ATOM   1313  CB  PHE A 157      -2.312  18.313 -23.461  1.00 21.69           C  
ATOM   1314  CG  PHE A 157      -0.979  18.493 -24.117  1.00 23.30           C  
ATOM   1315  CD1 PHE A 157      -0.873  18.787 -25.462  1.00 23.97           C  
ATOM   1316  CD2 PHE A 157       0.190  18.358 -23.379  1.00 25.55           C  
ATOM   1317  CE1 PHE A 157       0.367  18.947 -26.070  1.00 25.33           C  
ATOM   1318  CE2 PHE A 157       1.452  18.531 -23.980  1.00 26.68           C  
ATOM   1319  CZ  PHE A 157       1.535  18.815 -25.331  1.00 26.54           C  
ATOM   1320  N   ASN A 158      -5.087  19.406 -22.030  1.00 18.92           N  
ATOM   1321  CA  ASN A 158      -6.437  19.090 -21.532  1.00 18.11           C  
ATOM   1322  C   ASN A 158      -7.550  20.017 -22.044  1.00 17.81           C  
ATOM   1323  O   ASN A 158      -8.721  19.765 -21.734  1.00 16.89           O  
ATOM   1324  CB  ASN A 158      -6.499  19.160 -20.011  1.00 18.48           C  
ATOM   1325  CG  ASN A 158      -5.684  18.086 -19.278  1.00 19.73           C  
ATOM   1326  OD1 ASN A 158      -5.094  18.412 -18.244  1.00 21.13           O  
ATOM   1327  ND2 ASN A 158      -5.712  16.821 -19.723  1.00 19.48           N  
ATOM   1328  N   LEU A 159      -7.228  21.089 -22.764  1.00 18.24           N  
ATOM   1329  CA  LEU A 159      -8.263  21.991 -23.278  1.00 18.77           C  
ATOM   1330  C   LEU A 159      -9.267  21.299 -24.212  1.00 18.68           C  
ATOM   1331  O   LEU A 159     -10.457  21.472 -23.992  1.00 18.45           O  
ATOM   1332  CB  LEU A 159      -7.694  23.227 -23.954  1.00 19.67           C  
ATOM   1333  CG  LEU A 159      -7.131  24.318 -23.009  1.00 20.32           C  
ATOM   1334  CD1 LEU A 159      -6.344  25.328 -23.812  1.00 21.31           C  
ATOM   1335  CD2 LEU A 159      -8.187  25.020 -22.190  1.00 20.56           C  
ATOM   1336  N   PRO A 160      -8.808  20.502 -25.204  1.00 19.62           N  
ATOM   1337  CA  PRO A 160      -9.812  19.814 -26.023  1.00 19.85           C  
ATOM   1338  C   PRO A 160     -10.781  18.894 -25.244  1.00 19.70           C  
ATOM   1339  O   PRO A 160     -11.985  18.947 -25.506  1.00 20.08           O  
ATOM   1340  CB  PRO A 160      -8.998  19.028 -27.040  1.00 20.64           C  
ATOM   1341  CG  PRO A 160      -7.589  19.396 -26.869  1.00 20.81           C  
ATOM   1342  CD  PRO A 160      -7.441  20.320 -25.730  1.00 20.40           C  
ATOM   1343  N   GLU A 161     -10.268  18.082 -24.318  1.00 19.49           N  
ATOM   1344  CA  GLU A 161     -11.120  17.233 -23.510  1.00 19.41           C  
ATOM   1345  C   GLU A 161     -11.996  18.013 -22.541  1.00 18.51           C  
ATOM   1346  O   GLU A 161     -13.082  17.562 -22.255  1.00 18.65           O  
ATOM   1347  CB  GLU A 161     -10.357  16.113 -22.821  1.00 20.33           C  
ATOM   1348  CG  GLU A 161      -9.765  16.456 -21.466  1.00 20.63           C  
ATOM   1349  CD  GLU A 161      -8.691  15.459 -21.055  1.00 22.04           C  
ATOM   1350  OE1 GLU A 161      -8.983  14.573 -20.215  1.00 22.66           O  
ATOM   1351  OE2 GLU A 161      -7.554  15.566 -21.596  1.00 22.21           O  
ATOM   1352  N   THR A 162     -11.572  19.194 -22.076  1.00 17.74           N  
ATOM   1353  CA  THR A 162     -12.453  20.039 -21.279  1.00 17.43           C  
ATOM   1354  C   THR A 162     -13.734  20.325 -22.101  1.00 17.43           C  
ATOM   1355  O   THR A 162     -14.865  20.119 -21.624  1.00 17.40           O  
ATOM   1356  CB  THR A 162     -11.754  21.330 -20.839  1.00 17.57           C  
ATOM   1357  OG1 THR A 162     -10.573  21.024 -20.074  1.00 17.32           O  
ATOM   1358  CG2 THR A 162     -12.652  22.141 -19.989  1.00 17.88           C  
ATOM   1359  N   TYR A 163     -13.565  20.730 -23.346  1.00 17.22           N  
ATOM   1360  CA  TYR A 163     -14.731  21.027 -24.192  1.00 17.68           C  
ATOM   1361  C   TYR A 163     -15.467  19.745 -24.561  1.00 17.76           C  
ATOM   1362  O   TYR A 163     -16.706  19.724 -24.511  1.00 18.07           O  
ATOM   1363  CB  TYR A 163     -14.325  21.818 -25.433  1.00 18.08           C  
ATOM   1364  CG  TYR A 163     -15.465  22.167 -26.328  1.00 18.14           C  
ATOM   1365  CD1 TYR A 163     -16.481  23.015 -25.886  1.00 18.56           C  
ATOM   1366  CD2 TYR A 163     -15.543  21.658 -27.607  1.00 18.66           C  
ATOM   1367  CE1 TYR A 163     -17.564  23.325 -26.703  1.00 19.13           C  
ATOM   1368  CE2 TYR A 163     -16.605  21.965 -28.440  1.00 19.31           C  
ATOM   1369  CZ  TYR A 163     -17.623  22.796 -27.981  1.00 19.60           C  
ATOM   1370  OH  TYR A 163     -18.702  23.122 -28.789  1.00 20.28           O  
ATOM   1371  N   LEU A 164     -14.732  18.695 -24.920  1.00 17.61           N  
ATOM   1372  CA  LEU A 164     -15.378  17.429 -25.285  1.00 17.91           C  
ATOM   1373  C   LEU A 164     -16.268  16.866 -24.165  1.00 17.94           C  
ATOM   1374  O   LEU A 164     -17.402  16.387 -24.419  1.00 17.75           O  
ATOM   1375  CB  LEU A 164     -14.354  16.393 -25.724  1.00 18.34           C  
ATOM   1376  CG  LEU A 164     -14.846  15.072 -26.315  1.00 19.20           C  
ATOM   1377  CD1 LEU A 164     -15.898  15.229 -27.412  1.00 20.03           C  
ATOM   1378  CD2 LEU A 164     -13.657  14.270 -26.833  1.00 19.88           C  
ATOM   1379  N   LEU A 165     -15.796  16.934 -22.916  1.00 17.26           N  
ATOM   1380  CA  LEU A 165     -16.606  16.423 -21.811  1.00 17.36           C  
ATOM   1381  C   LEU A 165     -17.956  17.140 -21.772  1.00 17.69           C  
ATOM   1382  O   LEU A 165     -19.011  16.487 -21.679  1.00 18.38           O  
ATOM   1383  CB  LEU A 165     -15.853  16.552 -20.480  1.00 17.45           C  
ATOM   1384  CG  LEU A 165     -14.680  15.581 -20.379  1.00 17.41           C  
ATOM   1385  CD1 LEU A 165     -13.676  16.078 -19.344  1.00 17.75           C  
ATOM   1386  CD2 LEU A 165     -15.156  14.180 -20.070  1.00 17.90           C  
ATOM   1387  N   ALA A 166     -17.934  18.466 -21.886  1.00 17.64           N  
ATOM   1388  CA  ALA A 166     -19.162  19.244 -21.923  1.00 18.09           C  
ATOM   1389  C   ALA A 166     -20.052  18.893 -23.138  1.00 18.42           C  
ATOM   1390  O   ALA A 166     -21.269  18.734 -22.982  1.00 18.82           O  
ATOM   1391  CB  ALA A 166     -18.860  20.722 -21.854  1.00 18.15           C  
ATOM   1392  N   CYS A 167     -19.448  18.747 -24.312  1.00 18.36           N  
ATOM   1393  CA  CYS A 167     -20.166  18.313 -25.512  1.00 19.23           C  
ATOM   1394  C   CYS A 167     -20.893  16.992 -25.287  1.00 19.46           C  
ATOM   1395  O   CYS A 167     -22.022  16.823 -25.728  1.00 19.03           O  
ATOM   1396  CB  CYS A 167     -19.219  18.150 -26.701  1.00 19.90           C  
ATOM   1397  SG  CYS A 167     -18.586  19.688 -27.411  1.00 21.21           S  
ATOM   1398  N   LEU A 168     -20.209  16.044 -24.658  1.00 18.91           N  
ATOM   1399  CA  LEU A 168     -20.733  14.690 -24.468  1.00 19.48           C  
ATOM   1400  C   LEU A 168     -21.887  14.700 -23.483  1.00 19.62           C  
ATOM   1401  O   LEU A 168     -22.964  14.180 -23.785  1.00 20.17           O  
ATOM   1402  CB  LEU A 168     -19.608  13.734 -23.987  1.00 19.66           C  
ATOM   1403  CG  LEU A 168     -18.575  13.400 -25.069  1.00 19.82           C  
ATOM   1404  CD1 LEU A 168     -17.412  12.641 -24.444  1.00 19.81           C  
ATOM   1405  CD2 LEU A 168     -19.156  12.571 -26.185  1.00 21.38           C  
ATOM   1406  N   VAL A 169     -21.700  15.338 -22.334  1.00 18.53           N  
ATOM   1407  CA  VAL A 169     -22.792  15.465 -21.371  1.00 18.79           C  
ATOM   1408  C   VAL A 169     -24.024  16.134 -22.009  1.00 19.57           C  
ATOM   1409  O   VAL A 169     -25.177  15.658 -21.872  1.00 20.12           O  
ATOM   1410  CB  VAL A 169     -22.350  16.214 -20.094  1.00 18.13           C  
ATOM   1411  CG1 VAL A 169     -23.533  16.443 -19.162  1.00 18.71           C  
ATOM   1412  CG2 VAL A 169     -21.258  15.435 -19.349  1.00 18.41           C  
ATOM   1413  N   ASP A 170     -23.782  17.213 -22.757  1.00 19.66           N  
ATOM   1414  CA  ASP A 170     -24.861  17.860 -23.491  1.00 20.23           C  
ATOM   1415  C   ASP A 170     -25.546  16.896 -24.472  1.00 21.22           C  
ATOM   1416  O   ASP A 170     -26.782  16.833 -24.530  1.00 21.77           O  
ATOM   1417  CB  ASP A 170     -24.365  19.119 -24.220  1.00 20.04           C  
ATOM   1418  CG  ASP A 170     -25.432  19.731 -25.129  1.00 21.58           C  
ATOM   1419  OD1 ASP A 170     -26.428  20.239 -24.618  1.00 22.52           O  
ATOM   1420  OD2 ASP A 170     -25.275  19.681 -26.347  1.00 21.81           O  
ATOM   1421  N   PHE A 171     -24.752  16.159 -25.237  1.00 21.40           N  
ATOM   1422  CA  PHE A 171     -25.287  15.315 -26.286  1.00 22.93           C  
ATOM   1423  C   PHE A 171     -26.156  14.214 -25.676  1.00 23.66           C  
ATOM   1424  O   PHE A 171     -27.317  14.051 -26.063  1.00 24.96           O  
ATOM   1425  CB  PHE A 171     -24.181  14.661 -27.142  1.00 23.10           C  
ATOM   1426  CG  PHE A 171     -24.723  13.586 -28.028  1.00 24.45           C  
ATOM   1427  CD1 PHE A 171     -25.504  13.932 -29.147  1.00 25.96           C  
ATOM   1428  CD2 PHE A 171     -24.563  12.245 -27.703  1.00 24.45           C  
ATOM   1429  CE1 PHE A 171     -26.078  12.942 -29.933  1.00 27.83           C  
ATOM   1430  CE2 PHE A 171     -25.113  11.257 -28.501  1.00 26.00           C  
ATOM   1431  CZ  PHE A 171     -25.877  11.600 -29.606  1.00 27.71           C  
ATOM   1432  N   PHE A 172     -25.588  13.463 -24.740  1.00 22.52           N  
ATOM   1433  CA  PHE A 172     -26.308  12.376 -24.096  1.00 23.58           C  
ATOM   1434  C   PHE A 172     -27.575  12.860 -23.356  1.00 24.09           C  
ATOM   1435  O   PHE A 172     -28.591  12.207 -23.390  1.00 24.52           O  
ATOM   1436  CB  PHE A 172     -25.386  11.555 -23.194  1.00 22.94           C  
ATOM   1437  CG  PHE A 172     -24.388  10.729 -23.956  1.00 23.49           C  
ATOM   1438  CD1 PHE A 172     -24.801   9.735 -24.808  1.00 25.23           C  
ATOM   1439  CD2 PHE A 172     -23.036  10.944 -23.831  1.00 23.37           C  
ATOM   1440  CE1 PHE A 172     -23.887   8.948 -25.502  1.00 25.92           C  
ATOM   1441  CE2 PHE A 172     -22.119  10.191 -24.559  1.00 23.35           C  
ATOM   1442  CZ  PHE A 172     -22.537   9.188 -25.371  1.00 24.64           C  
ATOM   1443  N   THR A 173     -27.498  14.013 -22.713  1.00 24.10           N  
ATOM   1444  CA  THR A 173     -28.651  14.593 -22.035  1.00 25.09           C  
ATOM   1445  C   THR A 173     -29.786  14.874 -23.015  1.00 27.63           C  
ATOM   1446  O   THR A 173     -30.957  14.669 -22.675  1.00 28.53           O  
ATOM   1447  CB  THR A 173     -28.278  15.903 -21.334  1.00 24.12           C  
ATOM   1448  OG1 THR A 173     -27.309  15.629 -20.329  1.00 22.74           O  
ATOM   1449  CG2 THR A 173     -29.518  16.563 -20.661  1.00 24.91           C  
ATOM   1450  N   ASN A 174     -29.469  15.385 -24.195  1.00 28.42           N  
ATOM   1451  CA  ASN A 174     -30.533  15.832 -25.121  1.00 31.48           C  
ATOM   1452  C   ASN A 174     -30.884  14.833 -26.217  1.00 32.76           C  
ATOM   1453  O   ASN A 174     -31.744  15.106 -27.030  1.00 34.68           O  
ATOM   1454  CB  ASN A 174     -30.217  17.219 -25.642  1.00 31.92           C  
ATOM   1455  CG  ASN A 174     -30.209  18.233 -24.527  1.00 31.98           C  
ATOM   1456  OD1 ASN A 174     -29.186  18.777 -24.162  1.00 32.84           O  
ATOM   1457  ND2 ASN A 174     -31.332  18.439 -23.945  1.00 33.67           N  
ATOM   1458  N   CYS A 175     -30.271  13.652 -26.183  1.00 32.02           N  
ATOM   1459  CA  CYS A 175     -30.544  12.627 -27.160  1.00 33.66           C  
ATOM   1460  C   CYS A 175     -31.588  11.663 -26.588  1.00 34.07           C  
ATOM   1461  O   CYS A 175     -31.311  11.004 -25.576  1.00 32.68           O  
ATOM   1462  CB  CYS A 175     -29.265  11.878 -27.477  1.00 33.61           C  
ATOM   1463  SG  CYS A 175     -29.570  10.542 -28.620  1.00 36.66           S  
ATOM   1464  N   PRO A 176     -32.769  11.556 -27.239  1.00 36.17           N  
ATOM   1465  CA  PRO A 176     -33.883  10.739 -26.701  1.00 37.61           C  
ATOM   1466  C   PRO A 176     -33.583   9.265 -26.474  1.00 37.59           C  
ATOM   1467  O   PRO A 176     -34.259   8.652 -25.689  1.00 38.19           O  
ATOM   1468  CB  PRO A 176     -35.022  10.890 -27.743  1.00 39.97           C  
ATOM   1469  CG  PRO A 176     -34.571  11.871 -28.752  1.00 39.92           C  
ATOM   1470  CD  PRO A 176     -33.095  12.142 -28.561  1.00 37.54           C  
ATOM   1471  N   ARG A 177     -32.570   8.709 -27.128  1.00 37.66           N  
ATOM   1472  CA  ARG A 177     -32.192   7.304 -26.919  1.00 38.40           C  
ATOM   1473  C   ARG A 177     -31.694   7.010 -25.483  1.00 37.27           C  
ATOM   1474  O   ARG A 177     -31.772   5.887 -25.032  1.00 38.38           O  
ATOM   1475  CB  ARG A 177     -31.092   6.884 -27.909  1.00 38.90           C  
ATOM   1476  CG  ARG A 177     -31.371   7.203 -29.383  1.00 40.83           C  
ATOM   1477  CD  ARG A 177     -30.447   6.423 -30.328  1.00 41.93           C  
ATOM   1478  NE  ARG A 177     -29.007   6.787 -30.256  1.00 40.22           N  
ATOM   1479  CZ  ARG A 177     -28.413   7.805 -30.900  1.00 39.81           C  
ATOM   1480  NH1 ARG A 177     -29.112   8.661 -31.646  1.00 41.43           N  
ATOM   1481  NH2 ARG A 177     -27.093   7.979 -30.798  1.00 38.58           N  
ATOM   1482  N   TYR A 178     -31.193   8.013 -24.772  1.00 35.48           N  
ATOM   1483  CA  TYR A 178     -30.642   7.816 -23.435  1.00 34.89           C  
ATOM   1484  C   TYR A 178     -31.543   8.408 -22.371  1.00 34.73           C  
ATOM   1485  O   TYR A 178     -32.217   9.381 -22.636  1.00 35.64           O  
ATOM   1486  CB  TYR A 178     -29.297   8.505 -23.363  1.00 33.94           C  
ATOM   1487  CG  TYR A 178     -28.393   8.035 -24.449  1.00 35.50           C  
ATOM   1488  CD1 TYR A 178     -27.613   6.903 -24.282  1.00 36.64           C  
ATOM   1489  CD2 TYR A 178     -28.380   8.678 -25.682  1.00 37.09           C  
ATOM   1490  CE1 TYR A 178     -26.799   6.440 -25.317  1.00 38.52           C  
ATOM   1491  CE2 TYR A 178     -27.588   8.234 -26.715  1.00 38.44           C  
ATOM   1492  CZ  TYR A 178     -26.789   7.127 -26.530  1.00 39.08           C  
ATOM   1493  OH  TYR A 178     -25.989   6.723 -27.572  1.00 42.66           O  
ATOM   1494  N   THR A 179     -31.557   7.834 -21.176  1.00 33.71           N  
ATOM   1495  CA  THR A 179     -32.222   8.422 -20.024  1.00 33.07           C  
ATOM   1496  C   THR A 179     -31.170   8.996 -19.081  1.00 31.63           C  
ATOM   1497  O   THR A 179     -30.231   8.274 -18.645  1.00 31.01           O  
ATOM   1498  CB  THR A 179     -33.049   7.369 -19.308  1.00 34.43           C  
ATOM   1499  OG1 THR A 179     -33.963   6.819 -20.246  1.00 36.23           O  
ATOM   1500  CG2 THR A 179     -33.815   7.945 -18.155  1.00 34.88           C  
ATOM   1501  N   SER A 180     -31.325  10.274 -18.752  1.00 30.60           N  
ATOM   1502  CA  SER A 180     -30.391  10.971 -17.883  1.00 30.07           C  
ATOM   1503  C   SER A 180     -30.631  10.508 -16.463  1.00 30.25           C  
ATOM   1504  O   SER A 180     -31.749  10.506 -16.017  1.00 31.03           O  
ATOM   1505  CB  SER A 180     -30.597  12.473 -17.971  1.00 30.59           C  
ATOM   1506  OG  SER A 180     -30.287  12.927 -19.267  1.00 31.22           O  
ATOM   1507  N   CYS A 181     -29.582  10.077 -15.781  1.00 29.48           N  
ATOM   1508  CA  CYS A 181     -29.655   9.705 -14.375  1.00 30.79           C  
ATOM   1509  C   CYS A 181     -28.697  10.598 -13.595  1.00 28.92           C  
ATOM   1510  O   CYS A 181     -27.865  11.311 -14.147  1.00 26.50           O  
ATOM   1511  CB  CYS A 181     -29.312   8.209 -14.199  1.00 32.63           C  
ATOM   1512  SG  CYS A 181     -30.405   7.067 -15.118  1.00 36.25           S  
ATOM   1513  N   GLU A 182     -28.808  10.541 -12.294  1.00 29.71           N  
ATOM   1514  CA  GLU A 182     -27.953  11.332 -11.437  1.00 29.93           C  
ATOM   1515  C   GLU A 182     -26.442  11.142 -11.762  1.00 27.03           C  
ATOM   1516  O   GLU A 182     -25.704  12.113 -11.830  1.00 26.20           O  
ATOM   1517  CB  GLU A 182     -28.245  10.957  -9.980  1.00 33.60           C  
ATOM   1518  CG  GLU A 182     -27.678  11.952  -8.979  1.00 36.38           C  
ATOM   1519  CD  GLU A 182     -27.822  11.507  -7.513  1.00 40.06           C  
ATOM   1520  OE1 GLU A 182     -27.631  10.288  -7.183  1.00 42.68           O  
ATOM   1521  OE2 GLU A 182     -28.067  12.412  -6.685  1.00 42.72           O  
ATOM   1522  N   THR A 183     -26.003   9.904 -11.992  1.00 25.74           N  
ATOM   1523  CA  THR A 183     -24.556   9.589 -12.145  1.00 24.34           C  
ATOM   1524  C   THR A 183     -24.130   9.146 -13.549  1.00 23.51           C  
ATOM   1525  O   THR A 183     -22.976   8.722 -13.765  1.00 23.03           O  
ATOM   1526  CB  THR A 183     -24.104   8.547 -11.112  1.00 25.17           C  
ATOM   1527  OG1 THR A 183     -24.673   7.268 -11.420  1.00 25.66           O  
ATOM   1528  CG2 THR A 183     -24.491   8.986  -9.658  1.00 26.03           C  
ATOM   1529  N   GLY A 184     -25.040   9.251 -14.507  1.00 23.28           N  
ATOM   1530  CA  GLY A 184     -24.749   8.919 -15.901  1.00 23.58           C  
ATOM   1531  C   GLY A 184     -26.020   8.720 -16.727  1.00 24.63           C  
ATOM   1532  O   GLY A 184     -27.047   9.300 -16.410  1.00 24.67           O  
ATOM   1533  N   PHE A 185     -25.927   7.863 -17.744  1.00 25.00           N  
ATOM   1534  CA  PHE A 185     -26.961   7.702 -18.763  1.00 26.11           C  
ATOM   1535  C   PHE A 185     -27.317   6.233 -18.976  1.00 28.49           C  
ATOM   1536  O   PHE A 185     -26.451   5.373 -19.037  1.00 28.54           O  
ATOM   1537  CB  PHE A 185     -26.503   8.296 -20.093  1.00 24.92           C  
ATOM   1538  CG  PHE A 185     -26.171   9.756 -20.014  1.00 23.96           C  
ATOM   1539  CD1 PHE A 185     -27.191  10.716 -20.018  1.00 24.40           C  
ATOM   1540  CD2 PHE A 185     -24.851  10.186 -19.950  1.00 23.14           C  
ATOM   1541  CE1 PHE A 185     -26.918  12.066 -19.950  1.00 23.54           C  
ATOM   1542  CE2 PHE A 185     -24.559  11.551 -19.871  1.00 22.61           C  
ATOM   1543  CZ  PHE A 185     -25.611  12.493 -19.878  1.00 22.84           C  
ATOM   1544  N   LYS A 186     -28.595   5.971 -19.103  1.00 30.83           N  
ATOM   1545  CA  LYS A 186     -29.115   4.635 -19.346  1.00 34.72           C  
ATOM   1546  C   LYS A 186     -29.492   4.535 -20.837  1.00 36.00           C  
ATOM   1547  O   LYS A 186     -30.199   5.402 -21.367  1.00 34.89           O  
ATOM   1548  CB  LYS A 186     -30.339   4.420 -18.470  1.00 36.33           C  
ATOM   1549  CG  LYS A 186     -30.769   2.986 -18.273  1.00 39.50           C  
ATOM   1550  CD  LYS A 186     -32.097   2.953 -17.513  1.00 41.44           C  
ATOM   1551  CE  LYS A 186     -32.548   1.548 -17.079  1.00 44.63           C  
ATOM   1552  NZ  LYS A 186     -32.605   0.562 -18.199  1.00 46.31           N  
ATOM   1553  N   ASP A 187     -29.005   3.482 -21.489  1.00 37.69           N  
ATOM   1554  CA  ASP A 187     -29.301   3.149 -22.907  1.00 39.40           C  
ATOM   1555  C   ASP A 187     -29.765   1.691 -22.874  1.00 41.94           C  
ATOM   1556  O   ASP A 187     -28.976   0.761 -23.079  1.00 41.67           O  
ATOM   1557  CB  ASP A 187     -28.003   3.348 -23.715  1.00 40.04           C  
ATOM   1558  CG  ASP A 187     -28.070   2.874 -25.177  1.00 41.86           C  
ATOM   1559  OD1 ASP A 187     -29.133   2.744 -25.787  1.00 43.46           O  
ATOM   1560  OD2 ASP A 187     -26.968   2.638 -25.713  1.00 44.90           O  
ATOM   1561  N   GLY A 188     -31.027   1.503 -22.517  1.00 43.20           N  
ATOM   1562  CA  GLY A 188     -31.589   0.174 -22.308  1.00 45.49           C  
ATOM   1563  C   GLY A 188     -30.886  -0.576 -21.183  1.00 45.48           C  
ATOM   1564  O   GLY A 188     -30.955  -0.167 -20.018  1.00 45.75           O  
ATOM   1565  N   ASP A 189     -30.216  -1.672 -21.550  1.00 45.35           N  
ATOM   1566  CA  ASP A 189     -29.479  -2.551 -20.624  1.00 44.63           C  
ATOM   1567  C   ASP A 189     -27.982  -2.184 -20.488  1.00 41.70           C  
ATOM   1568  O   ASP A 189     -27.171  -2.993 -19.990  1.00 41.40           O  
ATOM   1569  CB  ASP A 189     -29.578  -4.019 -21.095  1.00 46.77           C  
ATOM   1570  CG  ASP A 189     -30.951  -4.619 -20.893  1.00 49.21           C  
ATOM   1571  OD1 ASP A 189     -31.679  -4.230 -19.954  1.00 49.57           O  
ATOM   1572  OD2 ASP A 189     -31.278  -5.527 -21.668  1.00 51.06           O  
ATOM   1573  N   LEU A 190     -27.616  -1.003 -20.968  1.00 38.43           N  
ATOM   1574  CA  LEU A 190     -26.296  -0.483 -20.790  1.00 36.58           C  
ATOM   1575  C   LEU A 190     -26.413   0.794 -19.959  1.00 34.68           C  
ATOM   1576  O   LEU A 190     -27.317   1.619 -20.208  1.00 33.50           O  
ATOM   1577  CB  LEU A 190     -25.673  -0.192 -22.144  1.00 36.61           C  
ATOM   1578  CG  LEU A 190     -25.513  -1.442 -23.038  1.00 39.18           C  
ATOM   1579  CD1 LEU A 190     -25.796  -1.137 -24.509  1.00 39.84           C  
ATOM   1580  CD2 LEU A 190     -24.120  -2.013 -22.860  1.00 39.13           C  
ATOM   1581  N   PHE A 191     -25.506   0.945 -18.982  1.00 32.85           N  
ATOM   1582  CA  PHE A 191     -25.416   2.156 -18.198  1.00 31.08           C  
ATOM   1583  C   PHE A 191     -24.034   2.732 -18.324  1.00 29.85           C  
ATOM   1584  O   PHE A 191     -23.034   2.043 -18.031  1.00 29.65           O  
ATOM   1585  CB  PHE A 191     -25.718   1.905 -16.733  1.00 31.82           C  
ATOM   1586  CG  PHE A 191     -25.710   3.151 -15.914  1.00 30.38           C  
ATOM   1587  CD1 PHE A 191     -26.821   3.987 -15.917  1.00 30.92           C  
ATOM   1588  CD2 PHE A 191     -24.612   3.496 -15.160  1.00 30.12           C  
ATOM   1589  CE1 PHE A 191     -26.842   5.151 -15.170  1.00 30.18           C  
ATOM   1590  CE2 PHE A 191     -24.602   4.670 -14.415  1.00 29.68           C  
ATOM   1591  CZ  PHE A 191     -25.716   5.506 -14.419  1.00 29.47           C  
ATOM   1592  N   MET A 192     -23.975   3.981 -18.772  1.00 28.24           N  
ATOM   1593  CA  MET A 192     -22.713   4.674 -18.949  1.00 28.18           C  
ATOM   1594  C   MET A 192     -22.625   5.757 -17.877  1.00 26.01           C  
ATOM   1595  O   MET A 192     -23.259   6.809 -17.982  1.00 24.95           O  
ATOM   1596  CB  MET A 192     -22.621   5.312 -20.342  1.00 29.70           C  
ATOM   1597  CG  MET A 192     -21.265   5.952 -20.585  1.00 31.63           C  
ATOM   1598  SD  MET A 192     -21.088   6.981 -22.054  1.00 35.69           S  
ATOM   1599  CE  MET A 192     -22.431   8.122 -21.824  1.00 34.34           C  
ATOM   1600  N   SER A 193     -21.822   5.494 -16.858  1.00 24.71           N  
ATOM   1601  CA  SER A 193     -21.575   6.468 -15.803  1.00 23.45           C  
ATOM   1602  C   SER A 193     -20.751   7.600 -16.341  1.00 22.22           C  
ATOM   1603  O   SER A 193     -19.967   7.419 -17.287  1.00 21.56           O  
ATOM   1604  CB  SER A 193     -20.882   5.771 -14.614  1.00 24.21           C  
ATOM   1605  OG  SER A 193     -19.542   5.457 -14.929  1.00 23.22           O  
ATOM   1606  N   TYR A 194     -20.925   8.795 -15.775  1.00 22.07           N  
ATOM   1607  CA  TYR A 194     -20.021   9.890 -16.097  1.00 21.31           C  
ATOM   1608  C   TYR A 194     -18.549   9.482 -15.865  1.00 21.83           C  
ATOM   1609  O   TYR A 194     -17.678   9.930 -16.603  1.00 21.89           O  
ATOM   1610  CB  TYR A 194     -20.323  11.129 -15.294  1.00 21.10           C  
ATOM   1611  CG  TYR A 194     -21.657  11.759 -15.587  1.00 21.34           C  
ATOM   1612  CD1 TYR A 194     -21.936  12.276 -16.835  1.00 21.36           C  
ATOM   1613  CD2 TYR A 194     -22.637  11.855 -14.604  1.00 22.47           C  
ATOM   1614  CE1 TYR A 194     -23.169  12.893 -17.096  1.00 22.22           C  
ATOM   1615  CE2 TYR A 194     -23.860  12.464 -14.859  1.00 22.90           C  
ATOM   1616  CZ  TYR A 194     -24.113  12.968 -16.116  1.00 22.66           C  
ATOM   1617  OH  TYR A 194     -25.296  13.552 -16.421  1.00 23.65           O  
ATOM   1618  N   ARG A 195     -18.286   8.660 -14.850  1.00 23.43           N  
ATOM   1619  CA  ARG A 195     -16.918   8.200 -14.551  1.00 25.29           C  
ATOM   1620  C   ARG A 195     -16.358   7.362 -15.703  1.00 24.58           C  
ATOM   1621  O   ARG A 195     -15.213   7.575 -16.080  1.00 22.81           O  
ATOM   1622  CB  ARG A 195     -16.870   7.423 -13.227  1.00 28.53           C  
ATOM   1623  CG  ARG A 195     -15.524   6.789 -12.841  1.00 32.68           C  
ATOM   1624  CD  ARG A 195     -14.475   7.825 -12.511  1.00 34.74           C  
ATOM   1625  NE  ARG A 195     -13.142   7.262 -12.193  1.00 39.30           N  
ATOM   1626  CZ  ARG A 195     -12.205   6.903 -13.092  1.00 41.16           C  
ATOM   1627  NH1 ARG A 195     -12.405   7.020 -14.412  1.00 40.96           N  
ATOM   1628  NH2 ARG A 195     -11.040   6.424 -12.669  1.00 43.85           N  
ATOM   1629  N   SER A 196     -17.139   6.399 -16.223  1.00 24.77           N  
ATOM   1630  CA  SER A 196     -16.625   5.540 -17.306  1.00 25.86           C  
ATOM   1631  C   SER A 196     -16.509   6.349 -18.595  1.00 24.42           C  
ATOM   1632  O   SER A 196     -15.553   6.165 -19.367  1.00 23.67           O  
ATOM   1633  CB  SER A 196     -17.456   4.266 -17.537  1.00 27.26           C  
ATOM   1634  OG  SER A 196     -18.699   4.637 -18.088  1.00 29.56           O  
ATOM   1635  N   MET A 197     -17.432   7.279 -18.794  1.00 23.07           N  
ATOM   1636  CA  MET A 197     -17.361   8.168 -19.957  1.00 22.76           C  
ATOM   1637  C   MET A 197     -16.082   9.030 -19.919  1.00 21.57           C  
ATOM   1638  O   MET A 197     -15.366   9.143 -20.916  1.00 20.80           O  
ATOM   1639  CB  MET A 197     -18.591   9.088 -20.001  1.00 22.69           C  
ATOM   1640  CG  MET A 197     -18.715   9.886 -21.279  1.00 23.04           C  
ATOM   1641  SD  MET A 197     -19.922  11.211 -21.187  1.00 23.91           S  
ATOM   1642  CE  MET A 197     -19.038  12.448 -20.275  1.00 23.51           C  
ATOM   1643  N   PHE A 198     -15.840   9.633 -18.757  1.00 20.87           N  
ATOM   1644  CA  PHE A 198     -14.608  10.373 -18.511  1.00 21.08           C  
ATOM   1645  C   PHE A 198     -13.354   9.531 -18.803  1.00 21.77           C  
ATOM   1646  O   PHE A 198     -12.395  10.038 -19.408  1.00 21.33           O  
ATOM   1647  CB  PHE A 198     -14.568  10.895 -17.067  1.00 21.63           C  
ATOM   1648  CG  PHE A 198     -13.226  11.404 -16.678  1.00 21.77           C  
ATOM   1649  CD1 PHE A 198     -12.816  12.661 -17.093  1.00 21.39           C  
ATOM   1650  CD2 PHE A 198     -12.354  10.590 -15.993  1.00 22.94           C  
ATOM   1651  CE1 PHE A 198     -11.530  13.089 -16.796  1.00 22.36           C  
ATOM   1652  CE2 PHE A 198     -11.090  11.029 -15.659  1.00 23.56           C  
ATOM   1653  CZ  PHE A 198     -10.685  12.271 -16.065  1.00 23.01           C  
ATOM   1654  N   GLN A 199     -13.346   8.277 -18.330  1.00 22.89           N  
ATOM   1655  CA  GLN A 199     -12.210   7.386 -18.547  1.00 24.32           C  
ATOM   1656  C   GLN A 199     -11.993   7.122 -20.029  1.00 23.68           C  
ATOM   1657  O   GLN A 199     -10.851   7.137 -20.500  1.00 23.41           O  
ATOM   1658  CB  GLN A 199     -12.314   6.078 -17.773  1.00 26.68           C  
ATOM   1659  CG  GLN A 199     -10.987   5.339 -17.623  1.00 29.41           C  
ATOM   1660  CD  GLN A 199      -9.898   6.189 -16.937  1.00 30.78           C  
ATOM   1661  OE1 GLN A 199     -10.098   6.721 -15.836  1.00 31.65           O  
ATOM   1662  NE2 GLN A 199      -8.774   6.364 -17.610  1.00 31.52           N  
ATOM   1663  N   ASP A 200     -13.072   6.916 -20.766  1.00 22.91           N  
ATOM   1664  CA  ASP A 200     -12.963   6.735 -22.223  1.00 22.87           C  
ATOM   1665  C   ASP A 200     -12.327   7.965 -22.883  1.00 21.56           C  
ATOM   1666  O   ASP A 200     -11.480   7.830 -23.750  1.00 21.85           O  
ATOM   1667  CB  ASP A 200     -14.321   6.465 -22.866  1.00 23.09           C  
ATOM   1668  CG  ASP A 200     -14.851   5.086 -22.574  1.00 24.54           C  
ATOM   1669  OD1 ASP A 200     -14.093   4.188 -22.219  1.00 25.38           O  
ATOM   1670  OD2 ASP A 200     -16.074   4.905 -22.723  1.00 25.43           O  
ATOM   1671  N   VAL A 201     -12.719   9.152 -22.459  1.00 20.14           N  
ATOM   1672  CA  VAL A 201     -12.211  10.373 -23.035  1.00 19.82           C  
ATOM   1673  C   VAL A 201     -10.700  10.490 -22.753  1.00 20.77           C  
ATOM   1674  O   VAL A 201      -9.862  10.727 -23.665  1.00 20.55           O  
ATOM   1675  CB  VAL A 201     -12.998  11.588 -22.525  1.00 19.01           C  
ATOM   1676  CG1 VAL A 201     -12.324  12.886 -22.934  1.00 18.88           C  
ATOM   1677  CG2 VAL A 201     -14.393  11.589 -23.073  1.00 19.26           C  
ATOM   1678  N   ARG A 202     -10.363  10.272 -21.491  1.00 21.46           N  
ATOM   1679  CA  ARG A 202      -8.992  10.374 -21.015  1.00 23.01           C  
ATOM   1680  C   ARG A 202      -8.113   9.342 -21.782  1.00 23.66           C  
ATOM   1681  O   ARG A 202      -7.028   9.667 -22.295  1.00 23.41           O  
ATOM   1682  CB  ARG A 202      -9.045  10.147 -19.483  1.00 24.46           C  
ATOM   1683  CG  ARG A 202      -7.807  10.413 -18.705  1.00 27.32           C  
ATOM   1684  CD  ARG A 202      -7.616  11.892 -18.329  1.00 26.39           C  
ATOM   1685  NE  ARG A 202      -7.187  12.683 -19.449  1.00 25.27           N  
ATOM   1686  CZ  ARG A 202      -6.057  12.527 -20.111  1.00 25.94           C  
ATOM   1687  NH1 ARG A 202      -5.154  11.655 -19.743  1.00 28.08           N  
ATOM   1688  NH2 ARG A 202      -5.778  13.326 -21.120  1.00 25.93           N  
ATOM   1689  N   ASP A 203      -8.600   8.103 -21.890  1.00 24.19           N  
ATOM   1690  CA  ASP A 203      -7.908   7.068 -22.656  1.00 25.32           C  
ATOM   1691  C   ASP A 203      -7.729   7.451 -24.121  1.00 24.50           C  
ATOM   1692  O   ASP A 203      -6.693   7.181 -24.701  1.00 24.55           O  
ATOM   1693  CB  ASP A 203      -8.652   5.724 -22.568  1.00 27.07           C  
ATOM   1694  CG  ASP A 203      -8.597   5.084 -21.165  1.00 28.01           C  
ATOM   1695  OD1 ASP A 203      -7.866   5.557 -20.287  1.00 28.03           O  
ATOM   1696  OD2 ASP A 203      -9.319   4.107 -20.955  1.00 29.15           O  
ATOM   1697  N   ALA A 204      -8.745   8.087 -24.705  1.00 23.19           N  
ATOM   1698  CA  ALA A 204      -8.710   8.475 -26.107  1.00 23.24           C  
ATOM   1699  C   ALA A 204      -7.688   9.592 -26.371  1.00 22.93           C  
ATOM   1700  O   ALA A 204      -6.973   9.547 -27.353  1.00 23.18           O  
ATOM   1701  CB  ALA A 204     -10.088   8.872 -26.599  1.00 22.20           C  
ATOM   1702  N   VAL A 205      -7.633  10.569 -25.479  1.00 22.95           N  
ATOM   1703  CA  VAL A 205      -6.631  11.648 -25.559  1.00 23.17           C  
ATOM   1704  C   VAL A 205      -5.236  11.040 -25.480  1.00 24.16           C  
ATOM   1705  O   VAL A 205      -4.390  11.291 -26.339  1.00 24.57           O  
ATOM   1706  CB  VAL A 205      -6.843  12.719 -24.471  1.00 22.13           C  
ATOM   1707  CG1 VAL A 205      -5.698  13.736 -24.479  1.00 22.49           C  
ATOM   1708  CG2 VAL A 205      -8.150  13.470 -24.706  1.00 21.28           C  
ATOM   1709  N   ASP A 206      -5.016  10.207 -24.469  1.00 24.95           N  
ATOM   1710  CA  ASP A 206      -3.737   9.483 -24.350  1.00 26.56           C  
ATOM   1711  C   ASP A 206      -3.375   8.737 -25.641  1.00 26.80           C  
ATOM   1712  O   ASP A 206      -2.237   8.831 -26.131  1.00 26.86           O  
ATOM   1713  CB  ASP A 206      -3.789   8.474 -23.209  1.00 28.69           C  
ATOM   1714  CG  ASP A 206      -3.708   9.110 -21.823  1.00 29.50           C  
ATOM   1715  OD1 ASP A 206      -3.449  10.344 -21.691  1.00 30.64           O  
ATOM   1716  OD2 ASP A 206      -3.906   8.338 -20.861  1.00 30.98           O  
ATOM   1717  N   TRP A 207      -4.345   7.999 -26.176  1.00 25.98           N  
ATOM   1718  CA  TRP A 207      -4.159   7.232 -27.393  1.00 27.10           C  
ATOM   1719  C   TRP A 207      -3.756   8.140 -28.558  1.00 26.94           C  
ATOM   1720  O   TRP A 207      -2.826   7.825 -29.288  1.00 27.55           O  
ATOM   1721  CB  TRP A 207      -5.428   6.443 -27.738  1.00 27.07           C  
ATOM   1722  CG  TRP A 207      -5.296   5.566 -28.910  1.00 28.51           C  
ATOM   1723  CD1 TRP A 207      -4.949   4.258 -28.904  1.00 30.25           C  
ATOM   1724  CD2 TRP A 207      -5.523   5.915 -30.280  1.00 28.76           C  
ATOM   1725  NE1 TRP A 207      -4.919   3.772 -30.177  1.00 31.42           N  
ATOM   1726  CE2 TRP A 207      -5.274   4.766 -31.044  1.00 30.74           C  
ATOM   1727  CE3 TRP A 207      -5.901   7.091 -30.934  1.00 27.87           C  
ATOM   1728  CZ2 TRP A 207      -5.401   4.748 -32.441  1.00 31.98           C  
ATOM   1729  CZ3 TRP A 207      -6.029   7.068 -32.320  1.00 28.92           C  
ATOM   1730  CH2 TRP A 207      -5.778   5.920 -33.053  1.00 30.86           C  
ATOM   1731  N   VAL A 208      -4.463   9.255 -28.719  1.00 25.83           N  
ATOM   1732  CA  VAL A 208      -4.177  10.195 -29.811  1.00 26.42           C  
ATOM   1733  C   VAL A 208      -2.708  10.681 -29.764  1.00 27.06           C  
ATOM   1734  O   VAL A 208      -2.036  10.786 -30.796  1.00 27.22           O  
ATOM   1735  CB  VAL A 208      -5.192  11.360 -29.766  1.00 25.49           C  
ATOM   1736  CG1 VAL A 208      -4.669  12.572 -30.504  1.00 25.95           C  
ATOM   1737  CG2 VAL A 208      -6.537  10.905 -30.354  1.00 25.54           C  
ATOM   1738  N   HIS A 209      -2.235  10.965 -28.560  1.00 27.71           N  
ATOM   1739  CA  HIS A 209      -0.842  11.433 -28.348  1.00 29.63           C  
ATOM   1740  C   HIS A 209       0.208  10.344 -28.545  1.00 32.59           C  
ATOM   1741  O   HIS A 209       1.256  10.596 -29.143  1.00 33.10           O  
ATOM   1742  CB  HIS A 209      -0.684  12.019 -26.942  1.00 28.57           C  
ATOM   1743  CG  HIS A 209      -1.239  13.390 -26.815  1.00 27.79           C  
ATOM   1744  ND1 HIS A 209      -0.452  14.515 -26.903  1.00 28.10           N  
ATOM   1745  CD2 HIS A 209      -2.505  13.835 -26.676  1.00 25.83           C  
ATOM   1746  CE1 HIS A 209      -1.196  15.590 -26.749  1.00 26.70           C  
ATOM   1747  NE2 HIS A 209      -2.451  15.206 -26.638  1.00 25.39           N  
ATOM   1748  N   TYR A 210      -0.080   9.149 -28.049  1.00 35.57           N  
ATOM   1749  CA  TYR A 210       0.908   8.071 -28.011  1.00 39.35           C  
ATOM   1750  C   TYR A 210       0.849   7.071 -29.171  1.00 38.91           C  
ATOM   1751  O   TYR A 210       1.881   6.586 -29.574  1.00 39.55           O  
ATOM   1752  CB  TYR A 210       0.862   7.350 -26.662  1.00 43.61           C  
ATOM   1753  CG  TYR A 210       1.081   8.314 -25.490  1.00 48.49           C  
ATOM   1754  CD1 TYR A 210       2.073   9.324 -25.538  1.00 50.45           C  
ATOM   1755  CD2 TYR A 210       0.281   8.244 -24.342  1.00 52.42           C  
ATOM   1756  CE1 TYR A 210       2.248  10.217 -24.480  1.00 53.43           C  
ATOM   1757  CE2 TYR A 210       0.458   9.124 -23.274  1.00 55.96           C  
ATOM   1758  CZ  TYR A 210       1.439  10.107 -23.346  1.00 56.58           C  
ATOM   1759  OH  TYR A 210       1.611  10.969 -22.270  1.00 61.06           O  
ATOM   1760  N   LYS A 211      -0.328   6.778 -29.696  1.00 37.27           N  
ATOM   1761  CA  LYS A 211      -0.494   5.794 -30.775  1.00 37.69           C  
ATOM   1762  C   LYS A 211      -1.173   6.344 -32.022  1.00 35.57           C  
ATOM   1763  O   LYS A 211      -1.113   5.723 -33.054  1.00 35.82           O  
ATOM   1764  CB  LYS A 211      -1.345   4.647 -30.263  1.00 40.63           C  
ATOM   1765  CG  LYS A 211      -0.701   3.841 -29.147  1.00 44.37           C  
ATOM   1766  CD  LYS A 211      -1.770   3.317 -28.211  1.00 47.43           C  
ATOM   1767  CE  LYS A 211      -1.200   2.471 -27.081  1.00 51.29           C  
ATOM   1768  NZ  LYS A 211      -1.233   1.012 -27.417  1.00 53.80           N  
ATOM   1769  N   GLY A 212      -1.843   7.489 -31.932  1.00 32.90           N  
ATOM   1770  CA  GLY A 212      -2.572   8.011 -33.055  1.00 32.44           C  
ATOM   1771  C   GLY A 212      -1.759   9.010 -33.838  1.00 31.22           C  
ATOM   1772  O   GLY A 212      -0.535   9.048 -33.755  1.00 30.38           O  
ATOM   1773  N   SER A 213      -2.456   9.868 -34.563  1.00 30.36           N  
ATOM   1774  CA  SER A 213      -1.810  10.625 -35.628  1.00 29.88           C  
ATOM   1775  C   SER A 213      -1.503  12.064 -35.259  1.00 27.82           C  
ATOM   1776  O   SER A 213      -1.140  12.829 -36.145  1.00 27.85           O  
ATOM   1777  CB  SER A 213      -2.702  10.556 -36.889  1.00 31.60           C  
ATOM   1778  OG  SER A 213      -3.930  11.231 -36.678  1.00 32.12           O  
ATOM   1779  N   LEU A 214      -1.591  12.432 -33.973  1.00 26.35           N  
ATOM   1780  CA  LEU A 214      -1.427  13.825 -33.587  1.00 25.91           C  
ATOM   1781  C   LEU A 214      -0.007  14.354 -33.897  1.00 25.31           C  
ATOM   1782  O   LEU A 214       0.152  15.399 -34.505  1.00 24.81           O  
ATOM   1783  CB  LEU A 214      -1.743  14.062 -32.099  1.00 25.95           C  
ATOM   1784  CG  LEU A 214      -1.535  15.499 -31.577  1.00 26.01           C  
ATOM   1785  CD1 LEU A 214      -2.390  16.511 -32.310  1.00 26.36           C  
ATOM   1786  CD2 LEU A 214      -1.842  15.626 -30.095  1.00 27.35           C  
ATOM   1787  N   LYS A 215       0.990  13.623 -33.453  1.00 26.05           N  
ATOM   1788  CA  LYS A 215       2.401  14.006 -33.719  1.00 27.42           C  
ATOM   1789  C   LYS A 215       2.699  14.130 -35.211  1.00 28.08           C  
ATOM   1790  O   LYS A 215       3.278  15.109 -35.649  1.00 28.44           O  
ATOM   1791  CB  LYS A 215       3.324  12.996 -33.093  1.00 28.69           C  
ATOM   1792  CG  LYS A 215       3.419  13.110 -31.579  1.00 29.73           C  
ATOM   1793  CD  LYS A 215       4.518  12.161 -31.086  1.00 32.16           C  
ATOM   1794  CE  LYS A 215       4.921  12.431 -29.661  1.00 34.16           C  
ATOM   1795  NZ  LYS A 215       3.836  11.925 -28.754  1.00 35.68           N  
ATOM   1796  N   GLU A 216       2.260  13.141 -35.976  1.00 30.00           N  
ATOM   1797  CA  GLU A 216       2.460  13.101 -37.446  1.00 32.36           C  
ATOM   1798  C   GLU A 216       1.826  14.306 -38.157  1.00 31.20           C  
ATOM   1799  O   GLU A 216       2.448  14.971 -38.988  1.00 30.78           O  
ATOM   1800  CB  GLU A 216       1.908  11.775 -37.971  1.00 36.42           C  
ATOM   1801  CG  GLU A 216       1.848  11.635 -39.475  1.00 41.33           C  
ATOM   1802  CD  GLU A 216       1.549  10.209 -39.908  1.00 45.64           C  
ATOM   1803  OE1 GLU A 216       0.454   9.683 -39.573  1.00 47.34           O  
ATOM   1804  OE2 GLU A 216       2.412   9.635 -40.611  1.00 50.52           O  
ATOM   1805  N   LYS A 217       0.583  14.601 -37.810  1.00 29.92           N  
ATOM   1806  CA  LYS A 217      -0.102  15.754 -38.369  1.00 29.96           C  
ATOM   1807  C   LYS A 217       0.520  17.075 -37.946  1.00 27.90           C  
ATOM   1808  O   LYS A 217       0.542  18.026 -38.723  1.00 28.02           O  
ATOM   1809  CB  LYS A 217      -1.590  15.703 -38.027  1.00 31.39           C  
ATOM   1810  CG  LYS A 217      -2.289  14.582 -38.771  1.00 34.77           C  
ATOM   1811  CD  LYS A 217      -3.786  14.569 -38.512  1.00 36.93           C  
ATOM   1812  CE  LYS A 217      -4.446  13.346 -39.140  1.00 40.20           C  
ATOM   1813  NZ  LYS A 217      -3.973  13.154 -40.527  1.00 43.56           N  
ATOM   1814  N   THR A 218       1.077  17.128 -36.734  1.00 25.79           N  
ATOM   1815  CA  THR A 218       1.718  18.342 -36.269  1.00 24.61           C  
ATOM   1816  C   THR A 218       2.966  18.577 -37.106  1.00 25.71           C  
ATOM   1817  O   THR A 218       3.166  19.658 -37.612  1.00 26.38           O  
ATOM   1818  CB  THR A 218       2.100  18.236 -34.769  1.00 23.82           C  
ATOM   1819  OG1 THR A 218       0.924  17.946 -33.977  1.00 22.81           O  
ATOM   1820  CG2 THR A 218       2.775  19.517 -34.281  1.00 23.54           C  
ATOM   1821  N   VAL A 219       3.783  17.554 -37.222  1.00 26.58           N  
ATOM   1822  CA  VAL A 219       5.048  17.632 -37.908  1.00 29.52           C  
ATOM   1823  C   VAL A 219       4.906  17.908 -39.416  1.00 31.70           C  
ATOM   1824  O   VAL A 219       5.785  18.531 -40.015  1.00 32.55           O  
ATOM   1825  CB  VAL A 219       5.836  16.340 -37.624  1.00 30.76           C  
ATOM   1826  CG1 VAL A 219       6.881  16.063 -38.662  1.00 34.19           C  
ATOM   1827  CG2 VAL A 219       6.427  16.426 -36.225  1.00 30.36           C  
ATOM   1828  N   GLU A 220       3.801  17.473 -40.021  1.00 32.97           N  
ATOM   1829  CA  GLU A 220       3.630  17.701 -41.442  1.00 36.24           C  
ATOM   1830  C   GLU A 220       3.171  19.136 -41.698  1.00 35.22           C  
ATOM   1831  O   GLU A 220       3.166  19.579 -42.828  1.00 37.15           O  
ATOM   1832  CB  GLU A 220       2.748  16.634 -42.089  1.00 39.88           C  
ATOM   1833  CG  GLU A 220       1.276  16.938 -42.023  1.00 42.03           C  
ATOM   1834  CD  GLU A 220       0.374  15.748 -42.356  1.00 45.35           C  
ATOM   1835  OE1 GLU A 220       0.884  14.641 -42.659  1.00 48.98           O  
ATOM   1836  OE2 GLU A 220      -0.862  15.952 -42.310  1.00 46.26           O  
ATOM   1837  N   ASN A 221       2.826  19.886 -40.662  1.00 32.49           N  
ATOM   1838  CA  ASN A 221       2.542  21.296 -40.862  1.00 32.09           C  
ATOM   1839  C   ASN A 221       2.934  22.161 -39.681  1.00 29.81           C  
ATOM   1840  O   ASN A 221       2.092  22.778 -39.004  1.00 28.64           O  
ATOM   1841  CB  ASN A 221       1.074  21.487 -41.236  1.00 32.80           C  
ATOM   1842  CG  ASN A 221       0.834  22.806 -41.917  1.00 34.09           C  
ATOM   1843  OD1 ASN A 221       1.677  23.754 -41.867  1.00 33.06           O  
ATOM   1844  ND2 ASN A 221      -0.310  22.900 -42.567  1.00 35.50           N  
ATOM   1845  N   LEU A 222       4.237  22.247 -39.465  1.00 29.48           N  
ATOM   1846  CA  LEU A 222       4.751  22.930 -38.285  1.00 28.84           C  
ATOM   1847  C   LEU A 222       4.417  24.418 -38.245  1.00 28.83           C  
ATOM   1848  O   LEU A 222       4.164  24.958 -37.163  1.00 27.23           O  
ATOM   1849  CB  LEU A 222       6.241  22.667 -38.126  1.00 30.11           C  
ATOM   1850  CG  LEU A 222       6.483  21.212 -37.723  1.00 30.57           C  
ATOM   1851  CD1 LEU A 222       7.883  20.750 -38.073  1.00 32.86           C  
ATOM   1852  CD2 LEU A 222       6.167  20.969 -36.260  1.00 30.12           C  
ATOM   1853  N   GLU A 223       4.329  25.070 -39.407  1.00 29.76           N  
ATOM   1854  CA  GLU A 223       3.994  26.509 -39.432  1.00 30.83           C  
ATOM   1855  C   GLU A 223       2.582  26.769 -38.960  1.00 28.89           C  
ATOM   1856  O   GLU A 223       2.283  27.781 -38.338  1.00 28.90           O  
ATOM   1857  CB  GLU A 223       4.163  27.099 -40.836  1.00 34.10           C  
ATOM   1858  CG  GLU A 223       5.624  27.182 -41.270  1.00 37.67           C  
ATOM   1859  CD  GLU A 223       6.214  25.865 -41.806  1.00 40.66           C  
ATOM   1860  OE1 GLU A 223       5.476  24.824 -41.921  1.00 41.49           O  
ATOM   1861  OE2 GLU A 223       7.446  25.891 -42.125  1.00 45.97           O  
ATOM   1862  N   LYS A 224       1.703  25.849 -39.283  1.00 28.50           N  
ATOM   1863  CA  LYS A 224       0.304  25.939 -38.841  1.00 28.17           C  
ATOM   1864  C   LYS A 224       0.157  25.747 -37.327  1.00 26.30           C  
ATOM   1865  O   LYS A 224      -0.715  26.359 -36.690  1.00 26.66           O  
ATOM   1866  CB  LYS A 224      -0.528  24.878 -39.550  1.00 29.27           C  
ATOM   1867  CG  LYS A 224      -2.009  24.977 -39.241  1.00 30.59           C  
ATOM   1868  CD  LYS A 224      -2.868  24.061 -40.091  1.00 32.21           C  
ATOM   1869  CE  LYS A 224      -4.274  24.144 -39.549  1.00 33.68           C  
ATOM   1870  NZ  LYS A 224      -5.164  23.269 -40.313  1.00 36.34           N  
ATOM   1871  N   TYR A 225       0.985  24.865 -36.780  1.00 24.58           N  
ATOM   1872  CA  TYR A 225       0.825  24.386 -35.416  1.00 23.62           C  
ATOM   1873  C   TYR A 225       1.812  24.886 -34.375  1.00 23.35           C  
ATOM   1874  O   TYR A 225       1.543  24.725 -33.213  1.00 22.58           O  
ATOM   1875  CB  TYR A 225       0.806  22.859 -35.426  1.00 23.21           C  
ATOM   1876  CG  TYR A 225      -0.429  22.325 -36.099  1.00 23.83           C  
ATOM   1877  CD1 TYR A 225      -1.691  22.652 -35.609  1.00 24.62           C  
ATOM   1878  CD2 TYR A 225      -0.356  21.490 -37.220  1.00 24.18           C  
ATOM   1879  CE1 TYR A 225      -2.851  22.190 -36.227  1.00 25.65           C  
ATOM   1880  CE2 TYR A 225      -1.534  21.013 -37.830  1.00 25.44           C  
ATOM   1881  CZ  TYR A 225      -2.756  21.391 -37.327  1.00 25.91           C  
ATOM   1882  OH  TYR A 225      -3.914  20.928 -37.886  1.00 28.09           O  
ATOM   1883  N   VAL A 226       2.930  25.501 -34.761  1.00 26.59           N  
ATOM   1884  CA  VAL A 226       3.997  25.799 -33.773  1.00 25.68           C  
ATOM   1885  C   VAL A 226       4.557  27.230 -33.951  1.00 25.88           C  
ATOM   1886  O   VAL A 226       5.018  27.606 -35.025  1.00 25.40           O  
ATOM   1887  CB  VAL A 226       5.143  24.753 -33.816  1.00 24.77           C  
ATOM   1888  CG1 VAL A 226       6.176  25.016 -32.726  1.00 23.54           C  
ATOM   1889  CG2 VAL A 226       4.599  23.355 -33.624  1.00 25.07           C  
ATOM   1890  N   VAL A 227       4.520  28.000 -32.865  1.00 26.26           N  
ATOM   1891  CA  VAL A 227       5.097  29.353 -32.815  1.00 26.66           C  
ATOM   1892  C   VAL A 227       6.604  29.244 -33.073  1.00 26.01           C  
ATOM   1893  O   VAL A 227       7.279  28.358 -32.550  1.00 24.89           O  
ATOM   1894  CB  VAL A 227       4.770  30.057 -31.453  1.00 27.39           C  
ATOM   1895  CG1 VAL A 227       5.513  31.408 -31.298  1.00 27.87           C  
ATOM   1896  CG2 VAL A 227       3.266  30.301 -31.359  1.00 28.30           C  
ATOM   1897  N   LYS A 228       7.099  30.100 -33.947  1.00 26.87           N  
ATOM   1898  CA  LYS A 228       8.520  30.146 -34.272  1.00 26.18           C  
ATOM   1899  C   LYS A 228       9.035  31.575 -34.126  1.00 26.27           C  
ATOM   1900  O   LYS A 228       8.387  32.526 -34.560  1.00 26.61           O  
ATOM   1901  CB  LYS A 228       8.713  29.680 -35.683  1.00 27.08           C  
ATOM   1902  CG  LYS A 228      10.178  29.528 -36.044  1.00 26.82           C  
ATOM   1903  CD  LYS A 228      10.275  28.665 -37.268  1.00 27.89           C  
ATOM   1904  CE  LYS A 228      11.641  28.668 -37.855  1.00 27.67           C  
ATOM   1905  NZ  LYS A 228      11.662  27.697 -38.957  1.00 28.15           N  
ATOM   1906  N   ASP A 229      10.204  31.717 -33.517  1.00 25.39           N  
ATOM   1907  CA  ASP A 229      10.693  33.013 -33.109  1.00 26.70           C  
ATOM   1908  C   ASP A 229      12.199  33.001 -33.229  1.00 25.83           C  
ATOM   1909  O   ASP A 229      12.868  32.204 -32.584  1.00 24.86           O  
ATOM   1910  CB  ASP A 229      10.294  33.251 -31.642  1.00 27.88           C  
ATOM   1911  CG  ASP A 229      10.726  34.643 -31.112  1.00 30.09           C  
ATOM   1912  OD1 ASP A 229      11.384  35.448 -31.835  1.00 29.17           O  
ATOM   1913  OD2 ASP A 229      10.408  34.928 -29.931  1.00 31.33           O  
ATOM   1914  N   GLY A 230      12.723  33.881 -34.058  1.00 26.79           N  
ATOM   1915  CA  GLY A 230      14.158  34.017 -34.241  1.00 26.60           C  
ATOM   1916  C   GLY A 230      14.879  34.451 -32.974  1.00 27.05           C  
ATOM   1917  O   GLY A 230      16.084  34.252 -32.871  1.00 27.18           O  
ATOM   1918  N   LYS A 231      14.174  35.063 -32.037  1.00 27.86           N  
ATOM   1919  CA  LYS A 231      14.776  35.445 -30.748  1.00 29.09           C  
ATOM   1920  C   LYS A 231      15.077  34.275 -29.799  1.00 28.86           C  
ATOM   1921  O   LYS A 231      15.887  34.445 -28.895  1.00 29.93           O  
ATOM   1922  CB  LYS A 231      13.933  36.488 -30.045  1.00 30.11           C  
ATOM   1923  CG  LYS A 231      13.861  37.798 -30.825  1.00 31.35           C  
ATOM   1924  CD  LYS A 231      13.066  38.893 -30.150  1.00 32.59           C  
ATOM   1925  CE  LYS A 231      11.626  38.480 -29.896  1.00 32.46           C  
ATOM   1926  NZ  LYS A 231      10.881  38.138 -31.131  1.00 32.08           N  
ATOM   1927  N   LEU A 232      14.472  33.102 -30.033  1.00 28.07           N  
ATOM   1928  CA  LEU A 232      14.769  31.904 -29.273  1.00 27.58           C  
ATOM   1929  C   LEU A 232      16.243  31.539 -29.295  1.00 26.66           C  
ATOM   1930  O   LEU A 232      16.874  31.487 -28.247  1.00 25.76           O  
ATOM   1931  CB  LEU A 232      13.851  30.719 -29.648  1.00 28.31           C  
ATOM   1932  CG  LEU A 232      14.396  29.405 -29.041  1.00 28.41           C  
ATOM   1933  CD1 LEU A 232      13.971  29.402 -27.612  1.00 29.71           C  
ATOM   1934  CD2 LEU A 232      14.001  28.116 -29.673  1.00 28.83           C  
ATOM   1935  N   PRO A 233      16.854  31.375 -30.489  1.00 27.12           N  
ATOM   1936  CA  PRO A 233      18.263  31.069 -30.433  1.00 25.87           C  
ATOM   1937  C   PRO A 233      19.111  32.126 -29.775  1.00 25.84           C  
ATOM   1938  O   PRO A 233      20.145  31.799 -29.178  1.00 25.65           O  
ATOM   1939  CB  PRO A 233      18.669  30.919 -31.918  1.00 26.66           C  
ATOM   1940  CG  PRO A 233      17.408  30.686 -32.643  1.00 27.12           C  
ATOM   1941  CD  PRO A 233      16.252  31.042 -31.795  1.00 27.18           C  
ATOM   1942  N   LEU A 234      18.741  33.399 -29.947  1.00 26.01           N  
ATOM   1943  CA  LEU A 234      19.522  34.476 -29.355  1.00 26.40           C  
ATOM   1944  C   LEU A 234      19.472  34.362 -27.835  1.00 25.98           C  
ATOM   1945  O   LEU A 234      20.501  34.478 -27.183  1.00 26.53           O  
ATOM   1946  CB  LEU A 234      19.012  35.850 -29.815  1.00 28.23           C  
ATOM   1947  CG  LEU A 234      19.633  37.084 -29.174  1.00 30.22           C  
ATOM   1948  CD1 LEU A 234      21.143  37.126 -29.369  1.00 30.97           C  
ATOM   1949  CD2 LEU A 234      18.984  38.369 -29.688  1.00 31.72           C  
ATOM   1950  N   LEU A 235      18.285  34.135 -27.264  1.00 24.85           N  
ATOM   1951  CA  LEU A 235      18.192  34.082 -25.785  1.00 24.84           C  
ATOM   1952  C   LEU A 235      18.975  32.891 -25.211  1.00 23.92           C  
ATOM   1953  O   LEU A 235      19.713  33.035 -24.255  1.00 23.68           O  
ATOM   1954  CB  LEU A 235      16.738  34.022 -25.333  1.00 24.74           C  
ATOM   1955  CG  LEU A 235      16.571  33.894 -23.818  1.00 25.27           C  
ATOM   1956  CD1 LEU A 235      17.274  35.029 -23.063  1.00 26.56           C  
ATOM   1957  CD2 LEU A 235      15.067  33.925 -23.546  1.00 25.86           C  
ATOM   1958  N   LEU A 236      18.788  31.722 -25.814  1.00 23.58           N  
ATOM   1959  CA  LEU A 236      19.524  30.538 -25.406  1.00 23.72           C  
ATOM   1960  C   LEU A 236      21.034  30.700 -25.508  1.00 24.28           C  
ATOM   1961  O   LEU A 236      21.760  30.312 -24.559  1.00 24.38           O  
ATOM   1962  CB  LEU A 236      19.012  29.285 -26.113  1.00 23.66           C  
ATOM   1963  CG  LEU A 236      17.881  28.533 -25.400  1.00 24.21           C  
ATOM   1964  CD1 LEU A 236      16.668  29.399 -25.179  1.00 25.57           C  
ATOM   1965  CD2 LEU A 236      17.474  27.334 -26.216  1.00 24.40           C  
ATOM   1966  N   SER A 237      21.511  31.360 -26.569  1.00 24.56           N  
ATOM   1967  CA  SER A 237      22.938  31.667 -26.688  1.00 25.80           C  
ATOM   1968  C   SER A 237      23.392  32.555 -25.554  1.00 26.85           C  
ATOM   1969  O   SER A 237      24.478  32.362 -25.005  1.00 27.73           O  
ATOM   1970  CB  SER A 237      23.306  32.310 -28.076  1.00 26.00           C  
ATOM   1971  OG  SER A 237      22.755  33.621 -28.246  1.00 26.60           O  
ATOM   1972  N   ARG A 238      22.566  33.525 -25.181  1.00 27.89           N  
ATOM   1973  CA  ARG A 238      22.931  34.443 -24.080  1.00 29.50           C  
ATOM   1974  C   ARG A 238      22.957  33.722 -22.729  1.00 29.37           C  
ATOM   1975  O   ARG A 238      23.819  33.984 -21.913  1.00 29.73           O  
ATOM   1976  CB  ARG A 238      22.019  35.672 -24.061  1.00 31.51           C  
ATOM   1977  CG  ARG A 238      22.254  36.606 -25.257  1.00 33.58           C  
ATOM   1978  CD  ARG A 238      21.189  37.687 -25.370  1.00 35.72           C  
ATOM   1979  NE  ARG A 238      21.251  38.540 -24.199  1.00 38.26           N  
ATOM   1980  CZ  ARG A 238      22.074  39.575 -24.067  1.00 41.57           C  
ATOM   1981  NH1 ARG A 238      22.896  39.931 -25.062  1.00 42.01           N  
ATOM   1982  NH2 ARG A 238      22.071  40.257 -22.932  1.00 43.48           N  
ATOM   1983  N   MET A 239      22.019  32.796 -22.516  1.00 27.90           N  
ATOM   1984  CA  MET A 239      22.019  31.980 -21.304  1.00 28.08           C  
ATOM   1985  C   MET A 239      23.299  31.190 -21.220  1.00 29.45           C  
ATOM   1986  O   MET A 239      23.933  31.110 -20.171  1.00 30.07           O  
ATOM   1987  CB  MET A 239      20.809  31.032 -21.284  1.00 26.14           C  
ATOM   1988  CG  MET A 239      19.519  31.785 -20.998  1.00 25.90           C  
ATOM   1989  SD  MET A 239      18.107  30.686 -21.275  1.00 24.56           S  
ATOM   1990  CE  MET A 239      16.835  31.668 -20.503  1.00 25.17           C  
ATOM   1991  N   LYS A 240      23.687  30.621 -22.350  1.00 30.62           N  
ATOM   1992  CA  LYS A 240      24.868  29.755 -22.396  1.00 33.04           C  
ATOM   1993  C   LYS A 240      26.192  30.482 -22.156  1.00 34.46           C  
ATOM   1994  O   LYS A 240      27.156  29.865 -21.714  1.00 35.02           O  
ATOM   1995  CB  LYS A 240      24.893  28.946 -23.711  1.00 33.98           C  
ATOM   1996  CG  LYS A 240      25.859  27.792 -23.633  1.00 36.83           C  
ATOM   1997  CD  LYS A 240      25.503  26.545 -24.427  1.00 37.67           C  
ATOM   1998  CE  LYS A 240      26.674  25.584 -24.260  1.00 40.70           C  
ATOM   1999  NZ  LYS A 240      26.652  24.508 -25.261  1.00 42.78           N  
ATOM   2000  N   GLU A 241      26.216  31.794 -22.390  1.00 35.97           N  
ATOM   2001  CA  GLU A 241      27.374  32.648 -22.078  1.00 37.66           C  
ATOM   2002  C   GLU A 241      27.581  32.831 -20.584  1.00 37.60           C  
ATOM   2003  O   GLU A 241      28.676  33.058 -20.153  1.00 37.47           O  
ATOM   2004  CB  GLU A 241      27.217  34.042 -22.704  1.00 40.26           C  
ATOM   2005  CG  GLU A 241      27.318  34.054 -24.222  1.00 41.32           C  
ATOM   2006  CD  GLU A 241      26.822  35.356 -24.871  1.00 43.76           C  
ATOM   2007  OE1 GLU A 241      26.749  36.391 -24.152  1.00 46.17           O  
ATOM   2008  OE2 GLU A 241      26.524  35.346 -26.110  1.00 43.30           O  
ATOM   2009  N   VAL A 242      26.518  32.760 -19.789  1.00 36.17           N  
ATOM   2010  CA  VAL A 242      26.635  32.957 -18.341  1.00 36.96           C  
ATOM   2011  C   VAL A 242      26.350  31.707 -17.545  1.00 35.35           C  
ATOM   2012  O   VAL A 242      26.437  31.741 -16.356  1.00 36.70           O  
ATOM   2013  CB  VAL A 242      25.743  34.121 -17.833  1.00 38.34           C  
ATOM   2014  CG1 VAL A 242      26.102  35.407 -18.588  1.00 39.90           C  
ATOM   2015  CG2 VAL A 242      24.249  33.820 -17.971  1.00 36.79           C  
ATOM   2016  N   GLY A 243      25.988  30.607 -18.185  1.00 32.93           N  
ATOM   2017  CA  GLY A 243      25.642  29.410 -17.434  1.00 32.21           C  
ATOM   2018  C   GLY A 243      25.461  28.214 -18.332  1.00 30.31           C  
ATOM   2019  O   GLY A 243      25.724  28.287 -19.550  1.00 30.54           O  
ATOM   2020  N   LYS A 244      25.033  27.117 -17.731  1.00 28.27           N  
ATOM   2021  CA  LYS A 244      24.732  25.927 -18.481  1.00 26.71           C  
ATOM   2022  C   LYS A 244      23.236  25.905 -18.870  1.00 24.93           C  
ATOM   2023  O   LYS A 244      22.417  26.562 -18.212  1.00 24.61           O  
ATOM   2024  CB  LYS A 244      25.139  24.714 -17.664  1.00 27.79           C  
ATOM   2025  CG  LYS A 244      26.669  24.649 -17.588  1.00 30.36           C  
ATOM   2026  CD  LYS A 244      27.109  23.540 -16.706  1.00 32.11           C  
ATOM   2027  CE  LYS A 244      28.617  23.594 -16.603  1.00 34.61           C  
ATOM   2028  NZ  LYS A 244      28.928  22.756 -15.420  1.00 36.58           N  
ATOM   2029  N   VAL A 245      22.920  25.192 -19.946  1.00 22.96           N  
ATOM   2030  CA  VAL A 245      21.555  25.104 -20.471  1.00 21.86           C  
ATOM   2031  C   VAL A 245      21.200  23.643 -20.633  1.00 21.07           C  
ATOM   2032  O   VAL A 245      21.984  22.895 -21.210  1.00 21.46           O  
ATOM   2033  CB  VAL A 245      21.450  25.869 -21.788  1.00 21.44           C  
ATOM   2034  CG1 VAL A 245      20.034  25.833 -22.323  1.00 20.95           C  
ATOM   2035  CG2 VAL A 245      21.891  27.315 -21.587  1.00 22.63           C  
ATOM   2036  N   PHE A 246      20.038  23.210 -20.140  1.00 20.02           N  
ATOM   2037  CA  PHE A 246      19.613  21.866 -20.383  1.00 19.45           C  
ATOM   2038  C   PHE A 246      18.147  21.734 -20.801  1.00 19.07           C  
ATOM   2039  O   PHE A 246      17.324  22.622 -20.552  1.00 18.97           O  
ATOM   2040  CB  PHE A 246      19.909  20.960 -19.183  1.00 20.14           C  
ATOM   2041  CG  PHE A 246      19.094  21.236 -17.964  1.00 20.28           C  
ATOM   2042  CD1 PHE A 246      19.540  22.143 -16.975  1.00 21.13           C  
ATOM   2043  CD2 PHE A 246      17.906  20.543 -17.745  1.00 20.22           C  
ATOM   2044  CE1 PHE A 246      18.789  22.357 -15.810  1.00 21.55           C  
ATOM   2045  CE2 PHE A 246      17.161  20.764 -16.583  1.00 20.59           C  
ATOM   2046  CZ  PHE A 246      17.612  21.664 -15.620  1.00 21.22           C  
ATOM   2047  N   LEU A 247      17.859  20.612 -21.426  1.00 19.02           N  
ATOM   2048  CA  LEU A 247      16.497  20.253 -21.817  1.00 19.67           C  
ATOM   2049  C   LEU A 247      16.137  18.996 -21.029  1.00 20.02           C  
ATOM   2050  O   LEU A 247      16.911  18.036 -21.008  1.00 19.98           O  
ATOM   2051  CB  LEU A 247      16.420  19.969 -23.325  1.00 19.67           C  
ATOM   2052  CG  LEU A 247      15.056  19.566 -23.911  1.00 19.67           C  
ATOM   2053  CD1 LEU A 247      14.134  20.737 -23.758  1.00 20.02           C  
ATOM   2054  CD2 LEU A 247      15.151  19.155 -25.390  1.00 19.98           C  
ATOM   2055  N   ALA A 248      14.978  19.005 -20.382  1.00 20.13           N  
ATOM   2056  CA  ALA A 248      14.444  17.793 -19.754  1.00 21.00           C  
ATOM   2057  C   ALA A 248      12.968  17.702 -20.140  1.00 20.96           C  
ATOM   2058  O   ALA A 248      12.153  18.422 -19.598  1.00 21.74           O  
ATOM   2059  CB  ALA A 248      14.601  17.843 -18.250  1.00 21.39           C  
ATOM   2060  N   THR A 249      12.662  16.844 -21.093  1.00 21.29           N  
ATOM   2061  CA  THR A 249      11.328  16.736 -21.676  1.00 22.02           C  
ATOM   2062  C   THR A 249      10.779  15.322 -21.549  1.00 22.95           C  
ATOM   2063  O   THR A 249      11.502  14.328 -21.648  1.00 21.63           O  
ATOM   2064  CB  THR A 249      11.299  17.156 -23.164  1.00 21.97           C  
ATOM   2065  OG1 THR A 249       9.987  16.966 -23.698  1.00 23.56           O  
ATOM   2066  CG2 THR A 249      12.258  16.350 -24.018  1.00 22.05           C  
ATOM   2067  N   ASN A 250       9.464  15.243 -21.339  1.00 24.19           N  
ATOM   2068  CA  ASN A 250       8.785  13.974 -21.348  1.00 25.75           C  
ATOM   2069  C   ASN A 250       8.731  13.394 -22.761  1.00 25.93           C  
ATOM   2070  O   ASN A 250       8.602  12.205 -22.907  1.00 26.26           O  
ATOM   2071  CB  ASN A 250       7.350  14.096 -20.747  1.00 27.06           C  
ATOM   2072  CG  ASN A 250       7.362  14.143 -19.213  1.00 27.74           C  
ATOM   2073  OD1 ASN A 250       8.427  14.057 -18.572  1.00 27.35           O  
ATOM   2074  ND2 ASN A 250       6.161  14.280 -18.610  1.00 28.72           N  
ATOM   2075  N   SER A 251       8.854  14.226 -23.794  1.00 26.49           N  
ATOM   2076  CA  SER A 251       8.789  13.706 -25.171  1.00 27.46           C  
ATOM   2077  C   SER A 251       9.956  12.806 -25.532  1.00 27.17           C  
ATOM   2078  O   SER A 251      11.006  12.841 -24.892  1.00 27.49           O  
ATOM   2079  CB  SER A 251       8.770  14.825 -26.168  1.00 28.33           C  
ATOM   2080  OG  SER A 251       7.583  15.535 -26.046  1.00 31.26           O  
ATOM   2081  N   ASP A 252       9.749  12.004 -26.566  1.00 26.81           N  
ATOM   2082  CA  ASP A 252      10.765  11.105 -27.084  1.00 27.01           C  
ATOM   2083  C   ASP A 252      11.738  11.872 -28.005  1.00 24.74           C  
ATOM   2084  O   ASP A 252      11.509  13.031 -28.406  1.00 23.55           O  
ATOM   2085  CB  ASP A 252      10.116   9.954 -27.857  1.00 29.47           C  
ATOM   2086  CG  ASP A 252       9.241  10.476 -28.998  1.00 31.69           C  
ATOM   2087  OD1 ASP A 252       9.754  10.677 -30.119  1.00 31.99           O  
ATOM   2088  OD2 ASP A 252       8.047  10.828 -28.704  1.00 35.46           O  
ATOM   2089  N   TYR A 253      12.827  11.213 -28.327  1.00 24.51           N  
ATOM   2090  CA  TYR A 253      13.893  11.857 -29.098  1.00 23.80           C  
ATOM   2091  C   TYR A 253      13.459  12.232 -30.497  1.00 23.40           C  
ATOM   2092  O   TYR A 253      13.734  13.347 -30.947  1.00 22.22           O  
ATOM   2093  CB  TYR A 253      15.150  11.014 -29.188  1.00 24.60           C  
ATOM   2094  CG  TYR A 253      16.263  11.814 -29.893  1.00 24.50           C  
ATOM   2095  CD1 TYR A 253      16.842  12.920 -29.277  1.00 23.77           C  
ATOM   2096  CD2 TYR A 253      16.659  11.510 -31.192  1.00 25.33           C  
ATOM   2097  CE1 TYR A 253      17.830  13.667 -29.901  1.00 23.49           C  
ATOM   2098  CE2 TYR A 253      17.653  12.256 -31.828  1.00 25.37           C  
ATOM   2099  CZ  TYR A 253      18.223  13.332 -31.166  1.00 24.44           C  
ATOM   2100  OH  TYR A 253      19.194  14.080 -31.798  1.00 24.94           O  
ATOM   2101  N   LYS A 254      12.791  11.323 -31.193  1.00 24.66           N  
ATOM   2102  CA  LYS A 254      12.432  11.588 -32.595  1.00 25.63           C  
ATOM   2103  C   LYS A 254      11.534  12.811 -32.728  1.00 24.38           C  
ATOM   2104  O   LYS A 254      11.763  13.648 -33.571  1.00 23.17           O  
ATOM   2105  CB  LYS A 254      11.772  10.386 -33.253  1.00 28.56           C  
ATOM   2106  CG  LYS A 254      12.789   9.397 -33.793  1.00 31.50           C  
ATOM   2107  CD  LYS A 254      12.108   8.171 -34.389  1.00 34.94           C  
ATOM   2108  CE  LYS A 254      13.120   7.308 -35.106  1.00 37.52           C  
ATOM   2109  NZ  LYS A 254      12.819   5.864 -34.891  1.00 40.45           N  
ATOM   2110  N   TYR A 255      10.503  12.901 -31.887  1.00 24.09           N  
ATOM   2111  CA  TYR A 255       9.606  14.062 -31.907  1.00 23.42           C  
ATOM   2112  C   TYR A 255      10.361  15.327 -31.468  1.00 22.13           C  
ATOM   2113  O   TYR A 255      10.261  16.389 -32.090  1.00 21.30           O  
ATOM   2114  CB  TYR A 255       8.411  13.819 -30.989  1.00 23.78           C  
ATOM   2115  CG  TYR A 255       7.380  14.928 -31.046  1.00 23.90           C  
ATOM   2116  CD1 TYR A 255       6.568  15.089 -32.164  1.00 24.42           C  
ATOM   2117  CD2 TYR A 255       7.185  15.788 -29.952  1.00 23.17           C  
ATOM   2118  CE1 TYR A 255       5.632  16.090 -32.229  1.00 24.69           C  
ATOM   2119  CE2 TYR A 255       6.251  16.799 -29.995  1.00 23.28           C  
ATOM   2120  CZ  TYR A 255       5.464  16.954 -31.132  1.00 24.15           C  
ATOM   2121  OH  TYR A 255       4.494  17.941 -31.203  1.00 23.85           O  
ATOM   2122  N   THR A 256      11.123  15.211 -30.395  1.00 21.67           N  
ATOM   2123  CA  THR A 256      11.924  16.347 -29.909  1.00 21.32           C  
ATOM   2124  C   THR A 256      12.813  16.899 -31.024  1.00 21.09           C  
ATOM   2125  O   THR A 256      12.869  18.097 -31.270  1.00 21.18           O  
ATOM   2126  CB  THR A 256      12.773  15.930 -28.690  1.00 21.15           C  
ATOM   2127  OG1 THR A 256      11.913  15.502 -27.624  1.00 21.61           O  
ATOM   2128  CG2 THR A 256      13.699  17.070 -28.199  1.00 20.63           C  
ATOM   2129  N   ASP A 257      13.486  16.017 -31.722  1.00 21.95           N  
ATOM   2130  CA  ASP A 257      14.380  16.433 -32.811  1.00 22.09           C  
ATOM   2131  C   ASP A 257      13.621  17.146 -33.951  1.00 22.38           C  
ATOM   2132  O   ASP A 257      14.050  18.199 -34.410  1.00 21.01           O  
ATOM   2133  CB  ASP A 257      15.111  15.219 -33.336  1.00 23.46           C  
ATOM   2134  CG  ASP A 257      16.288  15.564 -34.259  1.00 24.04           C  
ATOM   2135  OD1 ASP A 257      16.785  16.690 -34.285  1.00 22.78           O  
ATOM   2136  OD2 ASP A 257      16.715  14.620 -34.933  1.00 26.43           O  
ATOM   2137  N   LYS A 258      12.458  16.617 -34.333  1.00 23.40           N  
ATOM   2138  CA  LYS A 258      11.661  17.262 -35.366  1.00 24.79           C  
ATOM   2139  C   LYS A 258      11.238  18.663 -34.962  1.00 23.16           C  
ATOM   2140  O   LYS A 258      11.370  19.611 -35.740  1.00 22.34           O  
ATOM   2141  CB  LYS A 258      10.432  16.408 -35.741  1.00 27.87           C  
ATOM   2142  CG  LYS A 258      10.824  15.187 -36.554  1.00 31.98           C  
ATOM   2143  CD  LYS A 258       9.639  14.517 -37.235  1.00 36.28           C  
ATOM   2144  CE  LYS A 258      10.023  13.169 -37.858  1.00 39.33           C  
ATOM   2145  NZ  LYS A 258       9.863  12.112 -36.803  1.00 41.32           N  
ATOM   2146  N   ILE A 259      10.738  18.785 -33.735  1.00 21.97           N  
ATOM   2147  CA  ILE A 259      10.211  20.059 -33.249  1.00 21.66           C  
ATOM   2148  C   ILE A 259      11.345  21.073 -33.056  1.00 21.07           C  
ATOM   2149  O   ILE A 259      11.261  22.201 -33.548  1.00 21.15           O  
ATOM   2150  CB  ILE A 259       9.448  19.882 -31.917  1.00 21.33           C  
ATOM   2151  CG1 ILE A 259       8.157  19.049 -32.127  1.00 22.13           C  
ATOM   2152  CG2 ILE A 259       9.113  21.228 -31.324  1.00 21.26           C  
ATOM   2153  CD1 ILE A 259       7.189  19.578 -33.150  1.00 22.87           C  
ATOM   2154  N   MET A 260      12.414  20.640 -32.396  1.00 20.94           N  
ATOM   2155  CA  MET A 260      13.533  21.525 -32.123  1.00 20.52           C  
ATOM   2156  C   MET A 260      14.240  21.963 -33.413  1.00 20.56           C  
ATOM   2157  O   MET A 260      14.605  23.141 -33.548  1.00 20.37           O  
ATOM   2158  CB  MET A 260      14.496  20.871 -31.127  1.00 20.62           C  
ATOM   2159  CG  MET A 260      13.929  20.637 -29.712  1.00 20.80           C  
ATOM   2160  SD  MET A 260      13.500  22.143 -28.819  1.00 20.75           S  
ATOM   2161  CE  MET A 260      15.173  22.693 -28.375  1.00 20.82           C  
ATOM   2162  N   THR A 261      14.380  21.059 -34.382  1.00 20.74           N  
ATOM   2163  CA  THR A 261      14.969  21.433 -35.662  1.00 20.93           C  
ATOM   2164  C   THR A 261      14.166  22.552 -36.286  1.00 21.29           C  
ATOM   2165  O   THR A 261      14.739  23.539 -36.758  1.00 21.40           O  
ATOM   2166  CB  THR A 261      15.122  20.233 -36.600  1.00 21.59           C  
ATOM   2167  OG1 THR A 261      15.950  19.251 -35.967  1.00 20.87           O  
ATOM   2168  CG2 THR A 261      15.691  20.622 -37.969  1.00 22.34           C  
ATOM   2169  N   TYR A 262      12.839  22.412 -36.306  1.00 21.82           N  
ATOM   2170  CA  TYR A 262      11.983  23.479 -36.807  1.00 22.75           C  
ATOM   2171  C   TYR A 262      12.172  24.801 -36.032  1.00 22.29           C  
ATOM   2172  O   TYR A 262      12.323  25.836 -36.662  1.00 22.81           O  
ATOM   2173  CB  TYR A 262      10.510  23.045 -36.769  1.00 23.97           C  
ATOM   2174  CG  TYR A 262       9.503  24.144 -36.951  1.00 25.45           C  
ATOM   2175  CD1 TYR A 262       9.151  24.611 -38.223  1.00 27.03           C  
ATOM   2176  CD2 TYR A 262       8.865  24.689 -35.849  1.00 25.94           C  
ATOM   2177  CE1 TYR A 262       8.190  25.612 -38.375  1.00 28.20           C  
ATOM   2178  CE2 TYR A 262       7.941  25.684 -35.993  1.00 26.98           C  
ATOM   2179  CZ  TYR A 262       7.603  26.132 -37.236  1.00 27.83           C  
ATOM   2180  OH  TYR A 262       6.641  27.101 -37.275  1.00 29.81           O  
ATOM   2181  N   LEU A 263      12.197  24.751 -34.696  1.00 21.44           N  
ATOM   2182  CA  LEU A 263      12.342  25.959 -33.879  1.00 21.35           C  
ATOM   2183  C   LEU A 263      13.658  26.736 -34.176  1.00 21.27           C  
ATOM   2184  O   LEU A 263      13.733  27.950 -34.008  1.00 21.22           O  
ATOM   2185  CB  LEU A 263      12.250  25.618 -32.391  1.00 21.02           C  
ATOM   2186  CG  LEU A 263      10.868  25.179 -31.849  1.00 21.57           C  
ATOM   2187  CD1 LEU A 263      10.941  24.760 -30.394  1.00 21.31           C  
ATOM   2188  CD2 LEU A 263       9.848  26.295 -32.028  1.00 22.23           C  
ATOM   2189  N   PHE A 264      14.671  26.022 -34.615  1.00 20.86           N  
ATOM   2190  CA  PHE A 264      15.971  26.624 -34.915  1.00 21.09           C  
ATOM   2191  C   PHE A 264      16.240  26.789 -36.417  1.00 21.92           C  
ATOM   2192  O   PHE A 264      17.383  27.168 -36.811  1.00 21.91           O  
ATOM   2193  CB  PHE A 264      17.087  25.788 -34.274  1.00 20.24           C  
ATOM   2194  CG  PHE A 264      17.195  25.986 -32.802  1.00 20.49           C  
ATOM   2195  CD1 PHE A 264      16.288  25.353 -31.940  1.00 20.47           C  
ATOM   2196  CD2 PHE A 264      18.181  26.812 -32.253  1.00 20.27           C  
ATOM   2197  CE1 PHE A 264      16.379  25.527 -30.571  1.00 20.40           C  
ATOM   2198  CE2 PHE A 264      18.252  27.003 -30.878  1.00 20.58           C  
ATOM   2199  CZ  PHE A 264      17.352  26.369 -30.045  1.00 20.57           C  
ATOM   2200  N   ASP A 265      15.244  26.521 -37.263  1.00 22.02           N  
ATOM   2201  CA  ASP A 265      15.478  26.555 -38.707  1.00 23.16           C  
ATOM   2202  C   ASP A 265      15.313  27.974 -39.237  1.00 24.03           C  
ATOM   2203  O   ASP A 265      14.216  28.405 -39.616  1.00 24.17           O  
ATOM   2204  CB  ASP A 265      14.555  25.585 -39.425  1.00 24.54           C  
ATOM   2205  CG  ASP A 265      14.753  25.581 -40.949  1.00 26.04           C  
ATOM   2206  OD1 ASP A 265      15.776  26.042 -41.429  1.00 26.20           O  
ATOM   2207  OD2 ASP A 265      13.845  25.144 -41.651  1.00 28.02           O  
ATOM   2208  N   PHE A 266      16.404  28.709 -39.187  1.00 23.53           N  
ATOM   2209  CA  PHE A 266      16.520  30.029 -39.735  1.00 24.64           C  
ATOM   2210  C   PHE A 266      17.822  30.000 -40.535  1.00 24.81           C  
ATOM   2211  O   PHE A 266      18.658  29.132 -40.295  1.00 23.74           O  
ATOM   2212  CB  PHE A 266      16.672  31.054 -38.605  1.00 25.15           C  
ATOM   2213  CG  PHE A 266      15.432  31.233 -37.791  1.00 25.76           C  
ATOM   2214  CD1 PHE A 266      14.446  32.120 -38.208  1.00 26.71           C  
ATOM   2215  CD2 PHE A 266      15.247  30.532 -36.622  1.00 25.26           C  
ATOM   2216  CE1 PHE A 266      13.302  32.279 -37.477  1.00 27.12           C  
ATOM   2217  CE2 PHE A 266      14.068  30.689 -35.906  1.00 25.88           C  
ATOM   2218  CZ  PHE A 266      13.107  31.558 -36.346  1.00 26.11           C  
ATOM   2219  N   PRO A 267      18.013  30.951 -41.457  1.00 25.98           N  
ATOM   2220  CA  PRO A 267      19.239  30.909 -42.252  1.00 27.17           C  
ATOM   2221  C   PRO A 267      20.400  31.590 -41.510  1.00 27.38           C  
ATOM   2222  O   PRO A 267      21.222  32.243 -42.148  1.00 29.76           O  
ATOM   2223  CB  PRO A 267      18.848  31.689 -43.517  1.00 28.08           C  
ATOM   2224  CG  PRO A 267      17.873  32.703 -43.021  1.00 28.30           C  
ATOM   2225  CD  PRO A 267      17.116  32.036 -41.900  1.00 27.12           C  
ATOM   2226  N   HIS A 268      20.428  31.485 -40.184  1.00 26.15           N  
ATOM   2227  CA  HIS A 268      21.428  32.096 -39.336  1.00 26.10           C  
ATOM   2228  C   HIS A 268      21.426  31.432 -37.991  1.00 25.00           C  
ATOM   2229  O   HIS A 268      20.526  30.646 -37.670  1.00 23.13           O  
ATOM   2230  CB  HIS A 268      21.218  33.605 -39.179  1.00 27.59           C  
ATOM   2231  CG  HIS A 268      19.872  33.999 -38.664  1.00 28.01           C  
ATOM   2232  ND1 HIS A 268      19.501  33.861 -37.346  1.00 28.46           N  
ATOM   2233  CD2 HIS A 268      18.817  34.574 -39.294  1.00 29.05           C  
ATOM   2234  CE1 HIS A 268      18.264  34.311 -37.189  1.00 28.55           C  
ATOM   2235  NE2 HIS A 268      17.832  34.742 -38.354  1.00 29.08           N  
ATOM   2236  N   GLY A 269      22.434  31.744 -37.192  1.00 24.57           N  
ATOM   2237  CA  GLY A 269      22.509  31.205 -35.849  1.00 24.78           C  
ATOM   2238  C   GLY A 269      21.797  32.172 -34.886  1.00 25.47           C  
ATOM   2239  O   GLY A 269      20.788  32.758 -35.272  1.00 26.47           O  
ATOM   2240  N   PRO A 270      22.392  32.448 -33.713  1.00 25.52           N  
ATOM   2241  CA  PRO A 270      21.779  33.322 -32.684  1.00 26.46           C  
ATOM   2242  C   PRO A 270      21.332  34.660 -33.205  1.00 27.22           C  
ATOM   2243  O   PRO A 270      20.179  35.050 -32.961  1.00 28.19           O  
ATOM   2244  CB  PRO A 270      22.863  33.464 -31.621  1.00 26.89           C  
ATOM   2245  CG  PRO A 270      23.631  32.201 -31.720  1.00 26.80           C  
ATOM   2246  CD  PRO A 270      23.664  31.889 -33.245  1.00 26.00           C  
ATOM   2247  N   LYS A 271      22.203  35.327 -33.964  1.00 26.98           N  
ATOM   2248  CA  LYS A 271      21.870  36.602 -34.604  1.00 27.63           C  
ATOM   2249  C   LYS A 271      21.889  36.504 -36.109  1.00 26.55           C  
ATOM   2250  O   LYS A 271      22.674  35.732 -36.675  1.00 25.34           O  
ATOM   2251  CB  LYS A 271      22.861  37.678 -34.189  1.00 29.69           C  
ATOM   2252  CG  LYS A 271      22.774  38.025 -32.711  1.00 31.07           C  
ATOM   2253  CD  LYS A 271      24.012  38.818 -32.231  1.00 32.93           C  
ATOM   2254  CE  LYS A 271      23.990  40.238 -32.706  1.00 34.56           C  
ATOM   2255  NZ  LYS A 271      24.909  41.107 -31.932  1.00 36.91           N  
ATOM   2256  N   PRO A 272      21.071  37.332 -36.782  1.00 26.44           N  
ATOM   2257  CA  PRO A 272      21.260  37.443 -38.229  1.00 26.08           C  
ATOM   2258  C   PRO A 272      22.740  37.711 -38.607  1.00 25.65           C  
ATOM   2259  O   PRO A 272      23.402  38.509 -37.962  1.00 25.94           O  
ATOM   2260  CB  PRO A 272      20.379  38.655 -38.603  1.00 27.48           C  
ATOM   2261  CG  PRO A 272      19.304  38.643 -37.565  1.00 27.58           C  
ATOM   2262  CD  PRO A 272      20.013  38.253 -36.296  1.00 27.37           C  
ATOM   2263  N   GLY A 273      23.205  37.032 -39.651  1.00 24.88           N  
ATOM   2264  CA  GLY A 273      24.605  37.143 -40.140  1.00 25.02           C  
ATOM   2265  C   GLY A 273      25.531  36.055 -39.620  1.00 23.99           C  
ATOM   2266  O   GLY A 273      26.562  35.791 -40.221  1.00 23.68           O  
ATOM   2267  N   SER A 274      25.137  35.398 -38.523  1.00 23.11           N  
ATOM   2268  CA  SER A 274      25.885  34.299 -37.933  1.00 22.79           C  
ATOM   2269  C   SER A 274      25.567  32.966 -38.595  1.00 22.50           C  
ATOM   2270  O   SER A 274      24.428  32.721 -39.016  1.00 22.48           O  
ATOM   2271  CB  SER A 274      25.636  34.231 -36.412  1.00 22.49           C  
ATOM   2272  OG  SER A 274      24.350  33.703 -36.080  1.00 21.78           O  
ATOM   2273  N   SER A 275      26.560  32.072 -38.642  1.00 22.68           N  
ATOM   2274  CA  SER A 275      26.343  30.704 -39.132  1.00 22.19           C  
ATOM   2275  C   SER A 275      25.250  29.998 -38.333  1.00 21.84           C  
ATOM   2276  O   SER A 275      25.196  30.068 -37.101  1.00 21.49           O  
ATOM   2277  CB  SER A 275      27.643  29.894 -39.057  1.00 22.46           C  
ATOM   2278  OG  SER A 275      28.612  30.367 -39.980  1.00 22.76           O  
ATOM   2279  N   HIS A 276      24.372  29.302 -39.032  1.00 22.17           N  
ATOM   2280  CA  HIS A 276      23.406  28.435 -38.369  1.00 22.17           C  
ATOM   2281  C   HIS A 276      24.152  27.316 -37.593  1.00 22.48           C  
ATOM   2282  O   HIS A 276      25.140  26.803 -38.081  1.00 22.61           O  
ATOM   2283  CB  HIS A 276      22.457  27.813 -39.394  1.00 22.45           C  
ATOM   2284  CG  HIS A 276      21.431  26.903 -38.784  1.00 21.98           C  
ATOM   2285  ND1 HIS A 276      21.639  25.549 -38.624  1.00 21.84           N  
ATOM   2286  CD2 HIS A 276      20.199  27.158 -38.278  1.00 21.69           C  
ATOM   2287  CE1 HIS A 276      20.577  25.007 -38.043  1.00 21.65           C  
ATOM   2288  NE2 HIS A 276      19.691  25.962 -37.823  1.00 21.31           N  
ATOM   2289  N   ARG A 277      23.678  26.982 -36.397  1.00 22.37           N  
ATOM   2290  CA  ARG A 277      24.219  25.906 -35.536  1.00 23.48           C  
ATOM   2291  C   ARG A 277      23.036  24.909 -35.247  1.00 22.32           C  
ATOM   2292  O   ARG A 277      21.898  25.356 -35.062  1.00 21.31           O  
ATOM   2293  CB  ARG A 277      24.722  26.504 -34.181  1.00 25.18           C  
ATOM   2294  CG  ARG A 277      25.782  27.605 -34.286  1.00 28.39           C  
ATOM   2295  CD  ARG A 277      26.092  28.434 -33.014  1.00 29.69           C  
ATOM   2296  NE  ARG A 277      25.833  27.600 -31.905  1.00 31.54           N  
ATOM   2297  CZ  ARG A 277      25.455  27.982 -30.683  1.00 32.46           C  
ATOM   2298  NH1 ARG A 277      25.454  29.282 -30.297  1.00 32.93           N  
ATOM   2299  NH2 ARG A 277      25.171  27.011 -29.820  1.00 30.42           N  
ATOM   2300  N   PRO A 278      23.303  23.597 -35.168  1.00 22.09           N  
ATOM   2301  CA  PRO A 278      22.223  22.662 -34.831  1.00 22.09           C  
ATOM   2302  C   PRO A 278      21.630  22.978 -33.437  1.00 20.68           C  
ATOM   2303  O   PRO A 278      22.345  23.474 -32.548  1.00 20.23           O  
ATOM   2304  CB  PRO A 278      22.903  21.296 -34.851  1.00 22.69           C  
ATOM   2305  CG  PRO A 278      24.213  21.480 -35.455  1.00 23.74           C  
ATOM   2306  CD  PRO A 278      24.602  22.916 -35.309  1.00 23.69           C  
ATOM   2307  N   TRP A 279      20.339  22.743 -33.273  1.00 20.09           N  
ATOM   2308  CA  TRP A 279      19.679  22.937 -31.969  1.00 19.58           C  
ATOM   2309  C   TRP A 279      20.402  22.312 -30.775  1.00 19.53           C  
ATOM   2310  O   TRP A 279      20.475  22.937 -29.708  1.00 18.93           O  
ATOM   2311  CB  TRP A 279      18.214  22.479 -32.007  1.00 19.52           C  
ATOM   2312  CG  TRP A 279      17.947  21.036 -32.024  1.00 19.61           C  
ATOM   2313  CD1 TRP A 279      17.680  20.285 -33.094  1.00 20.46           C  
ATOM   2314  CD2 TRP A 279      17.847  20.166 -30.892  1.00 19.80           C  
ATOM   2315  NE1 TRP A 279      17.432  18.981 -32.733  1.00 20.74           N  
ATOM   2316  CE2 TRP A 279      17.503  18.887 -31.378  1.00 20.16           C  
ATOM   2317  CE3 TRP A 279      17.973  20.352 -29.524  1.00 19.14           C  
ATOM   2318  CZ2 TRP A 279      17.295  17.795 -30.546  1.00 20.43           C  
ATOM   2319  CZ3 TRP A 279      17.750  19.277 -28.699  1.00 19.56           C  
ATOM   2320  CH2 TRP A 279      17.432  18.010 -29.207  1.00 20.02           C  
ATOM   2321  N   GLN A 280      20.966  21.109 -30.974  1.00 19.90           N  
ATOM   2322  CA  GLN A 280      21.625  20.394 -29.884  1.00 20.42           C  
ATOM   2323  C   GLN A 280      22.848  21.160 -29.317  1.00 20.53           C  
ATOM   2324  O   GLN A 280      23.163  21.022 -28.125  1.00 20.46           O  
ATOM   2325  CB  GLN A 280      22.076  18.978 -30.282  1.00 20.88           C  
ATOM   2326  CG  GLN A 280      20.980  18.045 -30.746  1.00 20.93           C  
ATOM   2327  CD  GLN A 280      20.760  18.057 -32.260  1.00 21.61           C  
ATOM   2328  OE1 GLN A 280      21.002  19.066 -32.933  1.00 21.28           O  
ATOM   2329  NE2 GLN A 280      20.248  16.953 -32.788  1.00 22.70           N  
ATOM   2330  N   SER A 281      23.490  21.985 -30.140  1.00 20.60           N  
ATOM   2331  CA  SER A 281      24.658  22.748 -29.718  1.00 21.33           C  
ATOM   2332  C   SER A 281      24.310  23.835 -28.705  1.00 21.16           C  
ATOM   2333  O   SER A 281      25.209  24.400 -28.068  1.00 21.19           O  
ATOM   2334  CB  SER A 281      25.376  23.382 -30.920  1.00 22.06           C  
ATOM   2335  OG  SER A 281      24.605  24.479 -31.450  1.00 21.97           O  
ATOM   2336  N   TYR A 282      23.011  24.117 -28.530  1.00 20.49           N  
ATOM   2337  CA  TYR A 282      22.576  25.112 -27.554  1.00 20.82           C  
ATOM   2338  C   TYR A 282      22.460  24.559 -26.140  1.00 20.76           C  
ATOM   2339  O   TYR A 282      22.263  25.339 -25.171  1.00 21.84           O  
ATOM   2340  CB  TYR A 282      21.262  25.776 -28.001  1.00 20.59           C  
ATOM   2341  CG  TYR A 282      21.449  26.664 -29.187  1.00 21.14           C  
ATOM   2342  CD1 TYR A 282      21.504  26.123 -30.478  1.00 21.27           C  
ATOM   2343  CD2 TYR A 282      21.579  28.052 -29.046  1.00 21.85           C  
ATOM   2344  CE1 TYR A 282      21.695  26.928 -31.593  1.00 21.38           C  
ATOM   2345  CE2 TYR A 282      21.718  28.864 -30.162  1.00 22.32           C  
ATOM   2346  CZ  TYR A 282      21.796  28.288 -31.440  1.00 21.88           C  
ATOM   2347  OH  TYR A 282      22.002  29.052 -32.565  1.00 21.87           O  
ATOM   2348  N   PHE A 283      22.613  23.242 -26.006  1.00 20.35           N  
ATOM   2349  CA  PHE A 283      22.387  22.523 -24.750  1.00 20.31           C  
ATOM   2350  C   PHE A 283      23.618  21.780 -24.230  1.00 21.26           C  
ATOM   2351  O   PHE A 283      24.284  21.037 -24.979  1.00 21.82           O  
ATOM   2352  CB  PHE A 283      21.230  21.548 -24.927  1.00 19.68           C  
ATOM   2353  CG  PHE A 283      19.930  22.243 -25.192  1.00 19.16           C  
ATOM   2354  CD1 PHE A 283      19.119  22.664 -24.149  1.00 19.26           C  
ATOM   2355  CD2 PHE A 283      19.541  22.526 -26.490  1.00 19.05           C  
ATOM   2356  CE1 PHE A 283      17.950  23.346 -24.419  1.00 19.28           C  
ATOM   2357  CE2 PHE A 283      18.365  23.214 -26.758  1.00 18.76           C  
ATOM   2358  CZ  PHE A 283      17.582  23.634 -25.734  1.00 18.90           C  
ATOM   2359  N   ASP A 284      23.919  21.996 -22.955  1.00 21.82           N  
ATOM   2360  CA  ASP A 284      24.985  21.260 -22.287  1.00 22.89           C  
ATOM   2361  C   ASP A 284      24.523  19.853 -21.960  1.00 22.90           C  
ATOM   2362  O   ASP A 284      25.350  18.968 -21.806  1.00 23.32           O  
ATOM   2363  CB  ASP A 284      25.430  21.959 -21.022  1.00 23.71           C  
ATOM   2364  CG  ASP A 284      26.052  23.302 -21.300  1.00 24.60           C  
ATOM   2365  OD1 ASP A 284      27.212  23.323 -21.700  1.00 25.38           O  
ATOM   2366  OD2 ASP A 284      25.392  24.348 -21.167  1.00 24.24           O  
ATOM   2367  N   LEU A 285      23.210  19.648 -21.841  1.00 21.86           N  
ATOM   2368  CA  LEU A 285      22.672  18.347 -21.500  1.00 22.29           C  
ATOM   2369  C   LEU A 285      21.297  18.253 -22.077  1.00 20.90           C  
ATOM   2370  O   LEU A 285      20.534  19.179 -21.918  1.00 20.48           O  
ATOM   2371  CB  LEU A 285      22.636  18.172 -19.957  1.00 23.57           C  
ATOM   2372  CG  LEU A 285      22.103  16.862 -19.344  1.00 24.75           C  
ATOM   2373  CD1 LEU A 285      22.657  16.680 -17.933  1.00 26.56           C  
ATOM   2374  CD2 LEU A 285      20.598  16.814 -19.243  1.00 24.63           C  
ATOM   2375  N   ILE A 286      20.988  17.143 -22.733  1.00 20.52           N  
ATOM   2376  CA  ILE A 286      19.681  16.915 -23.363  1.00 20.36           C  
ATOM   2377  C   ILE A 286      19.138  15.591 -22.813  1.00 20.95           C  
ATOM   2378  O   ILE A 286      19.801  14.538 -22.863  1.00 21.53           O  
ATOM   2379  CB  ILE A 286      19.780  16.861 -24.903  1.00 20.25           C  
ATOM   2380  CG1 ILE A 286      20.376  18.170 -25.457  1.00 20.04           C  
ATOM   2381  CG2 ILE A 286      18.409  16.574 -25.520  1.00 20.14           C  
ATOM   2382  CD1 ILE A 286      20.766  18.106 -26.929  1.00 20.22           C  
ATOM   2383  N   LEU A 287      17.945  15.636 -22.266  1.00 20.80           N  
ATOM   2384  CA  LEU A 287      17.347  14.452 -21.649  1.00 21.40           C  
ATOM   2385  C   LEU A 287      15.899  14.366 -22.129  1.00 21.03           C  
ATOM   2386  O   LEU A 287      15.145  15.336 -22.019  1.00 20.69           O  
ATOM   2387  CB  LEU A 287      17.464  14.560 -20.136  1.00 22.24           C  
ATOM   2388  CG  LEU A 287      17.003  13.377 -19.300  1.00 23.63           C  
ATOM   2389  CD1 LEU A 287      17.805  13.270 -18.005  1.00 24.77           C  
ATOM   2390  CD2 LEU A 287      15.519  13.494 -19.012  1.00 23.79           C  
ATOM   2391  N   VAL A 288      15.555  13.226 -22.703  1.00 21.27           N  
ATOM   2392  CA  VAL A 288      14.221  12.960 -23.217  1.00 21.81           C  
ATOM   2393  C   VAL A 288      13.607  11.825 -22.383  1.00 22.57           C  
ATOM   2394  O   VAL A 288      14.274  11.244 -21.525  1.00 22.90           O  
ATOM   2395  CB  VAL A 288      14.257  12.620 -24.744  1.00 22.00           C  
ATOM   2396  CG1 VAL A 288      14.750  13.827 -25.558  1.00 21.57           C  
ATOM   2397  CG2 VAL A 288      15.126  11.414 -25.067  1.00 22.70           C  
ATOM   2398  N   ASP A 289      12.342  11.494 -22.649  1.00 23.52           N  
ATOM   2399  CA  ASP A 289      11.638  10.448 -21.915  1.00 24.35           C  
ATOM   2400  C   ASP A 289      11.792  10.666 -20.392  1.00 24.94           C  
ATOM   2401  O   ASP A 289      11.995   9.712 -19.652  1.00 25.15           O  
ATOM   2402  CB  ASP A 289      12.164   9.061 -22.288  1.00 24.98           C  
ATOM   2403  CG  ASP A 289      12.226   8.827 -23.786  1.00 25.59           C  
ATOM   2404  OD1 ASP A 289      11.197   9.080 -24.478  1.00 25.94           O  
ATOM   2405  OD2 ASP A 289      13.281   8.360 -24.269  1.00 25.49           O  
ATOM   2406  N   ALA A 290      11.720  11.918 -19.943  1.00 24.96           N  
ATOM   2407  CA  ALA A 290      12.012  12.253 -18.550  1.00 25.20           C  
ATOM   2408  C   ALA A 290      11.063  11.634 -17.522  1.00 27.50           C  
ATOM   2409  O   ALA A 290      11.476  11.445 -16.360  1.00 27.95           O  
ATOM   2410  CB  ALA A 290      12.063  13.763 -18.354  1.00 25.27           C  
ATOM   2411  N   ARG A 291       9.821  11.347 -17.914  1.00 29.91           N  
ATOM   2412  CA  ARG A 291       8.774  10.884 -16.968  1.00 33.02           C  
ATOM   2413  C   ARG A 291       8.662  11.759 -15.694  1.00 31.74           C  
ATOM   2414  O   ARG A 291       8.719  11.265 -14.549  1.00 31.80           O  
ATOM   2415  CB  ARG A 291       8.986   9.418 -16.565  1.00 36.28           C  
ATOM   2416  CG  ARG A 291       9.146   8.404 -17.701  1.00 39.61           C  
ATOM   2417  CD  ARG A 291       7.924   7.553 -17.953  1.00 46.12           C  
ATOM   2418  NE  ARG A 291       7.279   7.057 -16.714  1.00 50.93           N  
ATOM   2419  CZ  ARG A 291       7.390   5.828 -16.194  1.00 55.52           C  
ATOM   2420  NH1 ARG A 291       8.115   4.867 -16.781  1.00 57.10           N  
ATOM   2421  NH2 ARG A 291       6.746   5.550 -15.060  1.00 58.66           N  
ATOM   2422  N   LYS A 292       8.518  13.060 -15.897  1.00 30.64           N  
ATOM   2423  CA  LYS A 292       8.144  13.983 -14.821  1.00 30.73           C  
ATOM   2424  C   LYS A 292       6.659  13.714 -14.575  1.00 33.03           C  
ATOM   2425  O   LYS A 292       5.953  13.557 -15.562  1.00 34.36           O  
ATOM   2426  CB  LYS A 292       8.357  15.424 -15.256  1.00 30.05           C  
ATOM   2427  CG  LYS A 292       9.839  15.726 -15.517  1.00 28.60           C  
ATOM   2428  CD  LYS A 292      10.069  17.078 -16.170  1.00 28.45           C  
ATOM   2429  CE  LYS A 292       9.721  17.056 -17.626  1.00 29.07           C  
ATOM   2430  NZ  LYS A 292       9.602  18.432 -18.102  1.00 30.06           N  
ATOM   2431  N   PRO A 293       6.164  13.706 -13.327  1.00 33.82           N  
ATOM   2432  CA  PRO A 293       6.863  14.216 -12.143  1.00 32.98           C  
ATOM   2433  C   PRO A 293       7.801  13.252 -11.410  1.00 31.91           C  
ATOM   2434  O   PRO A 293       8.546  13.711 -10.535  1.00 31.91           O  
ATOM   2435  CB  PRO A 293       5.700  14.570 -11.183  1.00 35.46           C  
ATOM   2436  CG  PRO A 293       4.587  13.671 -11.570  1.00 37.74           C  
ATOM   2437  CD  PRO A 293       4.710  13.571 -13.077  1.00 37.35           C  
ATOM   2438  N   LEU A 294       7.714  11.951 -11.702  1.00 32.14           N  
ATOM   2439  CA  LEU A 294       8.537  10.917 -11.062  1.00 32.19           C  
ATOM   2440  C   LEU A 294      10.033  11.245 -11.149  1.00 29.52           C  
ATOM   2441  O   LEU A 294      10.830  10.902 -10.287  1.00 29.61           O  
ATOM   2442  CB  LEU A 294       8.242   9.569 -11.735  1.00 34.43           C  
ATOM   2443  CG  LEU A 294       9.094   8.338 -11.409  1.00 36.03           C  
ATOM   2444  CD1 LEU A 294       8.960   8.017  -9.935  1.00 38.35           C  
ATOM   2445  CD2 LEU A 294       8.722   7.118 -12.265  1.00 38.19           C  
ATOM   2446  N   PHE A 295      10.401  11.862 -12.248  1.00 27.37           N  
ATOM   2447  CA  PHE A 295      11.740  12.411 -12.476  1.00 25.58           C  
ATOM   2448  C   PHE A 295      12.315  13.170 -11.278  1.00 25.70           C  
ATOM   2449  O   PHE A 295      13.507  13.066 -10.985  1.00 24.92           O  
ATOM   2450  CB  PHE A 295      11.630  13.364 -13.650  1.00 24.40           C  
ATOM   2451  CG  PHE A 295      12.935  13.923 -14.120  1.00 23.05           C  
ATOM   2452  CD1 PHE A 295      13.811  13.141 -14.823  1.00 22.61           C  
ATOM   2453  CD2 PHE A 295      13.259  15.256 -13.885  1.00 23.05           C  
ATOM   2454  CE1 PHE A 295      15.008  13.670 -15.280  1.00 21.87           C  
ATOM   2455  CE2 PHE A 295      14.445  15.801 -14.343  1.00 22.14           C  
ATOM   2456  CZ  PHE A 295      15.318  15.008 -15.030  1.00 21.88           C  
ATOM   2457  N   PHE A 296      11.460  13.924 -10.586  1.00 26.63           N  
ATOM   2458  CA  PHE A 296      11.897  14.676  -9.398  1.00 27.58           C  
ATOM   2459  C   PHE A 296      12.035  13.889  -8.105  1.00 30.08           C  
ATOM   2460  O   PHE A 296      12.524  14.440  -7.116  1.00 31.58           O  
ATOM   2461  CB  PHE A 296      11.032  15.915  -9.204  1.00 27.59           C  
ATOM   2462  CG  PHE A 296      11.114  16.857 -10.367  1.00 26.09           C  
ATOM   2463  CD1 PHE A 296      12.276  17.596 -10.580  1.00 25.00           C  
ATOM   2464  CD2 PHE A 296      10.079  16.963 -11.277  1.00 26.02           C  
ATOM   2465  CE1 PHE A 296      12.385  18.458 -11.657  1.00 24.60           C  
ATOM   2466  CE2 PHE A 296      10.163  17.859 -12.342  1.00 25.73           C  
ATOM   2467  CZ  PHE A 296      11.335  18.595 -12.545  1.00 24.97           C  
ATOM   2468  N   GLY A 297      11.687  12.604  -8.128  1.00 31.31           N  
ATOM   2469  CA  GLY A 297      12.001  11.679  -7.041  1.00 33.98           C  
ATOM   2470  C   GLY A 297      12.984  10.638  -7.519  1.00 34.20           C  
ATOM   2471  O   GLY A 297      14.074  10.980  -7.987  1.00 34.49           O  
ATOM   2472  N   GLU A 298      12.585   9.371  -7.431  1.00 35.34           N  
ATOM   2473  CA AGLU A 298      13.423   8.241  -7.807  0.50 36.09           C  
ATOM   2474  CA BGLU A 298      13.463   8.252  -7.815  0.50 36.03           C  
ATOM   2475  C   GLU A 298      13.754   8.213  -9.326  1.00 33.54           C  
ATOM   2476  O   GLU A 298      14.797   7.720  -9.750  1.00 32.98           O  
ATOM   2477  CB AGLU A 298      12.735   6.932  -7.342  0.50 39.34           C  
ATOM   2478  CB BGLU A 298      12.874   6.895  -7.383  0.50 39.23           C  
ATOM   2479  CG AGLU A 298      11.302   6.720  -7.859  0.50 39.76           C  
ATOM   2480  CG BGLU A 298      12.680   6.706  -5.883  0.50 42.38           C  
ATOM   2481  CD AGLU A 298      10.160   7.104  -6.890  0.50 41.45           C  
ATOM   2482  CD BGLU A 298      13.957   6.347  -5.156  0.50 44.39           C  
ATOM   2483  OE1AGLU A 298       9.264   6.255  -6.687  0.50 43.93           O  
ATOM   2484  OE1BGLU A 298      15.037   6.468  -5.750  0.50 43.08           O  
ATOM   2485  OE2AGLU A 298      10.119   8.251  -6.361  0.50 40.18           O  
ATOM   2486  OE2BGLU A 298      13.879   5.939  -3.979  0.50 48.21           O  
ATOM   2487  N   GLY A 299      12.848   8.743 -10.143  1.00 31.76           N  
ATOM   2488  CA  GLY A 299      13.017   8.694 -11.588  1.00 30.18           C  
ATOM   2489  C   GLY A 299      13.036   7.271 -12.104  1.00 31.29           C  
ATOM   2490  O   GLY A 299      12.435   6.396 -11.504  1.00 32.94           O  
ATOM   2491  N   THR A 300      13.721   7.076 -13.238  1.00 29.99           N  
ATOM   2492  CA  THR A 300      13.930   5.762 -13.870  1.00 31.36           C  
ATOM   2493  C   THR A 300      15.397   5.606 -14.230  1.00 30.56           C  
ATOM   2494  O   THR A 300      16.180   6.571 -14.089  1.00 28.81           O  
ATOM   2495  CB  THR A 300      13.098   5.631 -15.164  1.00 31.61           C  
ATOM   2496  OG1 THR A 300      13.476   6.644 -16.110  1.00 29.15           O  
ATOM   2497  CG2 THR A 300      11.614   5.745 -14.818  1.00 33.03           C  
ATOM   2498  N   VAL A 301      15.796   4.434 -14.712  1.00 31.76           N  
ATOM   2499  CA  VAL A 301      17.215   4.262 -14.989  1.00 31.80           C  
ATOM   2500  C   VAL A 301      17.661   5.215 -16.120  1.00 29.35           C  
ATOM   2501  O   VAL A 301      16.890   5.556 -17.037  1.00 28.43           O  
ATOM   2502  CB  VAL A 301      17.640   2.791 -15.217  1.00 34.84           C  
ATOM   2503  CG1 VAL A 301      17.240   1.929 -14.013  1.00 37.93           C  
ATOM   2504  CG2 VAL A 301      17.076   2.222 -16.503  1.00 35.11           C  
ATOM   2505  N   LEU A 302      18.894   5.688 -16.011  1.00 28.56           N  
ATOM   2506  CA  LEU A 302      19.483   6.517 -17.043  1.00 27.20           C  
ATOM   2507  C   LEU A 302      19.863   5.657 -18.279  1.00 27.69           C  
ATOM   2508  O   LEU A 302      20.519   4.639 -18.165  1.00 29.11           O  
ATOM   2509  CB  LEU A 302      20.694   7.247 -16.488  1.00 27.65           C  
ATOM   2510  CG  LEU A 302      21.242   8.334 -17.392  1.00 26.86           C  
ATOM   2511  CD1 LEU A 302      20.254   9.484 -17.484  1.00 26.02           C  
ATOM   2512  CD2 LEU A 302      22.618   8.771 -16.877  1.00 28.37           C  
ATOM   2513  N   ARG A 303      19.398   6.081 -19.447  1.00 26.27           N  
ATOM   2514  CA  ARG A 303      19.626   5.395 -20.703  1.00 27.07           C  
ATOM   2515  C   ARG A 303      20.256   6.390 -21.626  1.00 26.05           C  
ATOM   2516  O   ARG A 303      20.167   7.600 -21.397  1.00 25.17           O  
ATOM   2517  CB  ARG A 303      18.303   4.933 -21.347  1.00 27.78           C  
ATOM   2518  CG  ARG A 303      17.416   4.022 -20.512  1.00 29.47           C  
ATOM   2519  CD  ARG A 303      18.007   2.645 -20.308  1.00 31.94           C  
ATOM   2520  NE  ARG A 303      18.022   1.870 -21.534  1.00 33.75           N  
ATOM   2521  CZ  ARG A 303      16.963   1.268 -22.079  1.00 35.85           C  
ATOM   2522  NH1 ARG A 303      15.750   1.310 -21.511  1.00 36.58           N  
ATOM   2523  NH2 ARG A 303      17.117   0.602 -23.212  1.00 37.57           N  
ATOM   2524  N   GLN A 304      20.861   5.867 -22.686  1.00 26.83           N  
ATOM   2525  CA  GLN A 304      21.466   6.645 -23.717  1.00 26.61           C  
ATOM   2526  C   GLN A 304      20.711   6.452 -25.038  1.00 27.02           C  
ATOM   2527  O   GLN A 304      20.378   5.330 -25.424  1.00 27.66           O  
ATOM   2528  CB  GLN A 304      22.895   6.196 -23.889  1.00 28.65           C  
ATOM   2529  CG  GLN A 304      23.641   6.999 -24.932  1.00 29.50           C  
ATOM   2530  CD  GLN A 304      25.058   6.536 -25.112  1.00 31.60           C  
ATOM   2531  OE1 GLN A 304      25.470   5.533 -24.556  1.00 33.35           O  
ATOM   2532  NE2 GLN A 304      25.809   7.266 -25.905  1.00 32.88           N  
ATOM   2533  N   VAL A 305      20.437   7.562 -25.718  1.00 26.46           N  
ATOM   2534  CA  VAL A 305      19.741   7.532 -26.997  1.00 27.86           C  
ATOM   2535  C   VAL A 305      20.767   7.325 -28.084  1.00 29.21           C  
ATOM   2536  O   VAL A 305      21.775   8.007 -28.133  1.00 29.98           O  
ATOM   2537  CB  VAL A 305      19.009   8.844 -27.283  1.00 27.69           C  
ATOM   2538  CG1 VAL A 305      18.383   8.838 -28.683  1.00 29.71           C  
ATOM   2539  CG2 VAL A 305      17.958   9.123 -26.220  1.00 27.16           C  
ATOM   2540  N   ASP A 306      20.525   6.372 -28.968  1.00 31.43           N  
ATOM   2541  CA  ASP A 306      21.303   6.293 -30.214  1.00 33.40           C  
ATOM   2542  C   ASP A 306      20.674   7.315 -31.174  1.00 34.89           C  
ATOM   2543  O   ASP A 306      19.591   7.071 -31.749  1.00 35.81           O  
ATOM   2544  CB  ASP A 306      21.237   4.894 -30.795  1.00 35.27           C  
ATOM   2545  CG  ASP A 306      21.954   4.767 -32.125  1.00 37.23           C  
ATOM   2546  OD1 ASP A 306      22.007   5.746 -32.889  1.00 37.24           O  
ATOM   2547  OD2 ASP A 306      22.412   3.651 -32.409  1.00 38.28           O  
ATOM   2548  N   THR A 307      21.334   8.464 -31.338  1.00 35.29           N  
ATOM   2549  CA  THR A 307      20.732   9.572 -32.113  1.00 37.03           C  
ATOM   2550  C   THR A 307      20.594   9.367 -33.636  1.00 40.69           C  
ATOM   2551  O   THR A 307      19.815  10.096 -34.267  1.00 43.05           O  
ATOM   2552  CB  THR A 307      21.413  10.920 -31.820  1.00 36.46           C  
ATOM   2553  OG1 THR A 307      22.790  10.845 -32.150  1.00 36.46           O  
ATOM   2554  CG2 THR A 307      21.241  11.289 -30.350  1.00 33.96           C  
ATOM   2555  N   LYS A 308      21.297   8.387 -34.212  1.00 44.71           N  
ATOM   2556  CA  LYS A 308      21.067   7.963 -35.613  1.00 48.28           C  
ATOM   2557  C   LYS A 308      19.693   7.294 -35.824  1.00 47.69           C  
ATOM   2558  O   LYS A 308      18.970   7.607 -36.771  1.00 49.37           O  
ATOM   2559  CB  LYS A 308      22.094   6.910 -36.093  1.00 51.35           C  
ATOM   2560  CG  LYS A 308      23.567   7.191 -35.888  1.00 53.17           C  
ATOM   2561  CD  LYS A 308      24.103   8.312 -36.764  1.00 56.35           C  
ATOM   2562  CE  LYS A 308      25.599   8.138 -36.998  1.00 59.14           C  
ATOM   2563  NZ  LYS A 308      26.146   9.227 -37.850  1.00 62.13           N  
ATOM   2564  N   THR A 309      19.376   6.327 -34.961  1.00 45.92           N  
ATOM   2565  CA  THR A 309      18.202   5.472 -35.113  1.00 45.64           C  
ATOM   2566  C   THR A 309      16.996   6.019 -34.349  1.00 44.01           C  
ATOM   2567  O   THR A 309      15.861   5.668 -34.656  1.00 45.71           O  
ATOM   2568  CB  THR A 309      18.512   4.039 -34.655  1.00 45.29           C  
ATOM   2569  OG1 THR A 309      18.811   4.024 -33.249  1.00 42.58           O  
ATOM   2570  CG2 THR A 309      19.707   3.473 -35.434  1.00 47.19           C  
ATOM   2571  N   GLY A 310      17.245   6.855 -33.350  1.00 41.01           N  
ATOM   2572  CA  GLY A 310      16.197   7.305 -32.439  1.00 39.65           C  
ATOM   2573  C   GLY A 310      15.816   6.283 -31.382  1.00 38.01           C  
ATOM   2574  O   GLY A 310      14.894   6.526 -30.577  1.00 37.84           O  
ATOM   2575  N   LYS A 311      16.538   5.169 -31.344  1.00 37.56           N  
ATOM   2576  CA  LYS A 311      16.260   4.101 -30.403  1.00 37.00           C  
ATOM   2577  C   LYS A 311      17.214   4.185 -29.224  1.00 34.69           C  
ATOM   2578  O   LYS A 311      18.334   4.641 -29.358  1.00 34.88           O  
ATOM   2579  CB  LYS A 311      16.440   2.751 -31.065  1.00 39.10           C  
ATOM   2580  CG  LYS A 311      15.559   2.571 -32.284  1.00 41.90           C  
ATOM   2581  CD  LYS A 311      15.754   1.194 -32.870  1.00 44.33           C  
ATOM   2582  CE  LYS A 311      14.910   1.036 -34.121  1.00 47.14           C  
ATOM   2583  NZ  LYS A 311      15.345  -0.198 -34.810  1.00 50.01           N  
ATOM   2584  N   LEU A 312      16.764   3.706 -28.084  1.00 33.53           N  
ATOM   2585  CA  LEU A 312      17.629   3.594 -26.896  1.00 32.22           C  
ATOM   2586  C   LEU A 312      18.651   2.498 -27.098  1.00 32.92           C  
ATOM   2587  O   LEU A 312      18.326   1.463 -27.649  1.00 34.45           O  
ATOM   2588  CB  LEU A 312      16.798   3.333 -25.652  1.00 31.19           C  
ATOM   2589  CG  LEU A 312      15.731   4.400 -25.362  1.00 30.94           C  
ATOM   2590  CD1 LEU A 312      15.033   4.046 -24.052  1.00 30.86           C  
ATOM   2591  CD2 LEU A 312      16.248   5.839 -25.327  1.00 29.46           C  
ATOM   2592  N   LYS A 313      19.886   2.754 -26.682  1.00 32.66           N  
ATOM   2593  CA  LYS A 313      20.894   1.708 -26.533  1.00 34.42           C  
ATOM   2594  C   LYS A 313      20.458   0.763 -25.422  1.00 33.98           C  
ATOM   2595  O   LYS A 313      19.720   1.157 -24.502  1.00 32.67           O  
ATOM   2596  CB  LYS A 313      22.265   2.293 -26.183  1.00 35.60           C  
ATOM   2597  CG  LYS A 313      22.725   3.334 -27.189  1.00 37.71           C  
ATOM   2598  CD  LYS A 313      24.219   3.459 -27.286  1.00 40.68           C  
ATOM   2599  CE  LYS A 313      24.525   4.691 -28.120  1.00 42.99           C  
ATOM   2600  NZ  LYS A 313      25.986   4.924 -28.276  1.00 45.97           N  
ATOM   2601  N   ILE A 314      20.878  -0.489 -25.518  1.00 35.67           N  
ATOM   2602  CA  ILE A 314      20.456  -1.487 -24.540  1.00 35.83           C  
ATOM   2603  C   ILE A 314      21.357  -1.328 -23.306  1.00 34.98           C  
ATOM   2604  O   ILE A 314      22.578  -1.261 -23.406  1.00 34.56           O  
ATOM   2605  CB  ILE A 314      20.427  -2.930 -25.108  1.00 38.37           C  
ATOM   2606  CG1 ILE A 314      19.560  -3.012 -26.385  1.00 39.47           C  
ATOM   2607  CG2 ILE A 314      19.870  -3.904 -24.061  1.00 39.28           C  
ATOM   2608  CD1 ILE A 314      18.153  -2.428 -26.311  1.00 38.20           C  
ATOM   2609  N   GLY A 315      20.704  -1.169 -22.157  1.00 34.25           N  
ATOM   2610  CA  GLY A 315      21.393  -1.111 -20.866  1.00 34.46           C  
ATOM   2611  C   GLY A 315      21.348   0.266 -20.222  1.00 32.26           C  
ATOM   2612  O   GLY A 315      20.940   1.221 -20.844  1.00 30.94           O  
ATOM   2613  N   THR A 316      21.776   0.319 -18.959  1.00 31.88           N  
ATOM   2614  CA  THR A 316      21.880   1.544 -18.197  1.00 30.46           C  
ATOM   2615  C   THR A 316      23.187   2.220 -18.511  1.00 30.65           C  
ATOM   2616  O   THR A 316      24.235   1.567 -18.548  1.00 31.70           O  
ATOM   2617  CB  THR A 316      21.799   1.269 -16.677  1.00 30.75           C  
ATOM   2618  OG1 THR A 316      20.512   0.744 -16.392  1.00 30.95           O  
ATOM   2619  CG2 THR A 316      21.997   2.532 -15.854  1.00 30.31           C  
ATOM   2620  N   TYR A 317      23.113   3.532 -18.701  1.00 29.95           N  
ATOM   2621  CA  TYR A 317      24.291   4.345 -19.029  1.00 31.45           C  
ATOM   2622  C   TYR A 317      25.016   4.767 -17.756  1.00 32.19           C  
ATOM   2623  O   TYR A 317      24.430   5.403 -16.868  1.00 30.99           O  
ATOM   2624  CB  TYR A 317      23.910   5.585 -19.847  1.00 30.90           C  
ATOM   2625  CG  TYR A 317      25.123   6.375 -20.253  1.00 32.12           C  
ATOM   2626  CD1 TYR A 317      25.991   5.897 -21.243  1.00 33.97           C  
ATOM   2627  CD2 TYR A 317      25.438   7.574 -19.616  1.00 32.23           C  
ATOM   2628  CE1 TYR A 317      27.125   6.605 -21.601  1.00 35.77           C  
ATOM   2629  CE2 TYR A 317      26.553   8.305 -19.987  1.00 33.57           C  
ATOM   2630  CZ  TYR A 317      27.393   7.823 -20.962  1.00 35.60           C  
ATOM   2631  OH  TYR A 317      28.503   8.540 -21.279  1.00 37.22           O  
ATOM   2632  N   THR A 318      26.283   4.391 -17.690  1.00 35.08           N  
ATOM   2633  CA  THR A 318      27.151   4.529 -16.516  1.00 37.25           C  
ATOM   2634  C   THR A 318      28.285   5.553 -16.757  1.00 39.25           C  
ATOM   2635  O   THR A 318      29.051   5.857 -15.848  1.00 40.86           O  
ATOM   2636  CB  THR A 318      27.800   3.151 -16.197  1.00 39.38           C  
ATOM   2637  OG1 THR A 318      28.521   2.679 -17.346  1.00 40.78           O  
ATOM   2638  CG2 THR A 318      26.722   2.067 -15.826  1.00 38.90           C  
ATOM   2639  N   GLY A 319      28.375   6.079 -17.980  1.00 39.58           N  
ATOM   2640  CA  GLY A 319      29.468   6.952 -18.399  1.00 41.27           C  
ATOM   2641  C   GLY A 319      29.243   8.421 -18.069  1.00 40.30           C  
ATOM   2642  O   GLY A 319      28.231   8.772 -17.458  1.00 38.52           O  
ATOM   2643  N   PRO A 320      30.210   9.280 -18.441  1.00 41.82           N  
ATOM   2644  CA  PRO A 320      30.198  10.696 -18.045  1.00 42.02           C  
ATOM   2645  C   PRO A 320      29.329  11.541 -18.965  1.00 40.14           C  
ATOM   2646  O   PRO A 320      28.839  11.048 -19.981  1.00 39.29           O  
ATOM   2647  CB  PRO A 320      31.671  11.107 -18.205  1.00 45.12           C  
ATOM   2648  CG  PRO A 320      32.149  10.278 -19.361  1.00 46.16           C  
ATOM   2649  CD  PRO A 320      31.412   8.949 -19.247  1.00 44.52           C  
ATOM   2650  N   LEU A 321      29.152  12.810 -18.633  1.00 40.46           N  
ATOM   2651  CA  LEU A 321      28.583  13.743 -19.590  1.00 39.56           C  
ATOM   2652  C   LEU A 321      29.606  13.939 -20.663  1.00 42.10           C  
ATOM   2653  O   LEU A 321      30.745  14.300 -20.355  1.00 44.18           O  
ATOM   2654  CB  LEU A 321      28.265  15.106 -18.947  1.00 40.00           C  
ATOM   2655  CG  LEU A 321      27.630  16.171 -19.871  1.00 39.43           C  
ATOM   2656  CD1 LEU A 321      26.321  15.700 -20.442  1.00 36.97           C  
ATOM   2657  CD2 LEU A 321      27.389  17.455 -19.125  1.00 40.76           C  
ATOM   2658  N   GLN A 322      29.230  13.709 -21.916  1.00 42.37           N  
ATOM   2659  CA  GLN A 322      30.115  14.093 -23.040  1.00 46.28           C  
ATOM   2660  C   GLN A 322      29.360  14.777 -24.132  1.00 45.10           C  
ATOM   2661  O   GLN A 322      28.148  14.671 -24.227  1.00 41.76           O  
ATOM   2662  CB  GLN A 322      30.917  12.910 -23.614  1.00 49.14           C  
ATOM   2663  CG  GLN A 322      30.132  11.614 -23.714  1.00 48.54           C  
ATOM   2664  CD  GLN A 322      31.013  10.409 -23.999  1.00 52.03           C  
ATOM   2665  OE1 GLN A 322      32.153  10.539 -24.452  1.00 56.23           O  
ATOM   2666  NE2 GLN A 322      30.481   9.217 -23.721  1.00 52.37           N  
ATOM   2667  N   HIS A 323      30.113  15.472 -24.962  1.00 47.99           N  
ATOM   2668  CA  HIS A 323      29.561  16.205 -26.073  1.00 49.42           C  
ATOM   2669  C   HIS A 323      28.819  15.254 -26.997  1.00 46.28           C  
ATOM   2670  O   HIS A 323      29.283  14.150 -27.275  1.00 45.06           O  
ATOM   2671  CB  HIS A 323      30.663  16.918 -26.833  1.00 55.28           C  
ATOM   2672  CG  HIS A 323      30.154  17.806 -27.917  1.00 59.80           C  
ATOM   2673  ND1 HIS A 323      29.897  17.347 -29.195  1.00 62.25           N  
ATOM   2674  CD2 HIS A 323      29.840  19.124 -27.916  1.00 62.67           C  
ATOM   2675  CE1 HIS A 323      29.455  18.348 -29.938  1.00 64.68           C  
ATOM   2676  NE2 HIS A 323      29.423  19.440 -29.189  1.00 65.27           N  
ATOM   2677  N   GLY A 324      27.658  15.693 -27.462  1.00 43.74           N  
ATOM   2678  CA  GLY A 324      26.805  14.872 -28.313  1.00 42.54           C  
ATOM   2679  C   GLY A 324      25.999  13.753 -27.682  1.00 39.61           C  
ATOM   2680  O   GLY A 324      25.213  13.137 -28.360  1.00 40.83           O  
ATOM   2681  N   ILE A 325      26.156  13.459 -26.405  1.00 37.73           N  
ATOM   2682  CA  ILE A 325      25.338  12.416 -25.817  1.00 35.36           C  
ATOM   2683  C   ILE A 325      23.915  12.942 -25.529  1.00 32.30           C  
ATOM   2684  O   ILE A 325      23.725  14.088 -25.158  1.00 31.41           O  
ATOM   2685  CB  ILE A 325      25.961  11.823 -24.552  1.00 36.44           C  
ATOM   2686  CG1 ILE A 325      25.240  10.538 -24.205  1.00 36.14           C  
ATOM   2687  CG2 ILE A 325      25.851  12.781 -23.379  1.00 36.79           C  
ATOM   2688  CD1 ILE A 325      25.731   9.884 -22.950  1.00 37.38           C  
ATOM   2689  N   VAL A 326      22.930  12.078 -25.749  1.00 30.13           N  
ATOM   2690  CA  VAL A 326      21.557  12.364 -25.436  1.00 28.39           C  
ATOM   2691  C   VAL A 326      21.075  11.291 -24.475  1.00 27.41           C  
ATOM   2692  O   VAL A 326      21.196  10.066 -24.734  1.00 27.63           O  
ATOM   2693  CB  VAL A 326      20.705  12.435 -26.702  1.00 28.77           C  
ATOM   2694  CG1 VAL A 326      19.232  12.623 -26.341  1.00 27.90           C  
ATOM   2695  CG2 VAL A 326      21.165  13.584 -27.566  1.00 30.38           C  
ATOM   2696  N   TYR A 327      20.546  11.752 -23.352  1.00 26.18           N  
ATOM   2697  CA  TYR A 327      20.027  10.867 -22.334  1.00 25.16           C  
ATOM   2698  C   TYR A 327      18.504  10.647 -22.437  1.00 23.94           C  
ATOM   2699  O   TYR A 327      17.766  11.482 -22.963  1.00 23.40           O  
ATOM   2700  CB  TYR A 327      20.293  11.458 -20.964  1.00 25.62           C  
ATOM   2701  CG  TYR A 327      21.736  11.685 -20.623  1.00 27.63           C  
ATOM   2702  CD1 TYR A 327      22.551  10.631 -20.274  1.00 28.05           C  
ATOM   2703  CD2 TYR A 327      22.271  12.981 -20.567  1.00 29.08           C  
ATOM   2704  CE1 TYR A 327      23.868  10.831 -19.913  1.00 30.11           C  
ATOM   2705  CE2 TYR A 327      23.599  13.194 -20.199  1.00 30.69           C  
ATOM   2706  CZ  TYR A 327      24.392  12.108 -19.879  1.00 31.12           C  
ATOM   2707  OH  TYR A 327      25.710  12.286 -19.494  1.00 33.37           O  
ATOM   2708  N   SER A 328      18.072   9.538 -21.838  1.00 23.21           N  
ATOM   2709  CA  SER A 328      16.680   9.194 -21.703  1.00 23.21           C  
ATOM   2710  C   SER A 328      16.412   8.695 -20.280  1.00 23.20           C  
ATOM   2711  O   SER A 328      17.186   7.907 -19.736  1.00 23.54           O  
ATOM   2712  CB  SER A 328      16.322   8.140 -22.745  1.00 23.65           C  
ATOM   2713  OG  SER A 328      15.076   7.541 -22.473  1.00 23.70           O  
ATOM   2714  N   GLY A 329      15.330   9.175 -19.663  1.00 24.16           N  
ATOM   2715  CA  GLY A 329      14.928   8.736 -18.319  1.00 24.46           C  
ATOM   2716  C   GLY A 329      15.714   9.458 -17.243  1.00 24.58           C  
ATOM   2717  O   GLY A 329      15.800  10.675 -17.245  1.00 25.69           O  
ATOM   2718  N   GLY A 330      16.314   8.723 -16.328  1.00 24.49           N  
ATOM   2719  CA  GLY A 330      17.101   9.347 -15.277  1.00 24.61           C  
ATOM   2720  C   GLY A 330      16.241  10.035 -14.225  1.00 25.16           C  
ATOM   2721  O   GLY A 330      15.052   9.727 -14.078  1.00 25.77           O  
ATOM   2722  N   SER A 331      16.839  11.005 -13.545  1.00 25.23           N  
ATOM   2723  CA  SER A 331      16.182  11.762 -12.479  1.00 25.58           C  
ATOM   2724  C   SER A 331      16.735  13.165 -12.435  1.00 26.04           C  
ATOM   2725  O   SER A 331      17.767  13.476 -13.073  1.00 25.59           O  
ATOM   2726  CB  SER A 331      16.404  11.066 -11.131  1.00 26.39           C  
ATOM   2727  OG  SER A 331      17.701  11.330 -10.638  1.00 26.86           O  
ATOM   2728  N   SER A 332      16.068  14.028 -11.685  1.00 26.65           N  
ATOM   2729  CA  SER A 332      16.568  15.374 -11.486  1.00 27.74           C  
ATOM   2730  C   SER A 332      17.983  15.391 -10.867  1.00 28.89           C  
ATOM   2731  O   SER A 332      18.779  16.266 -11.218  1.00 28.80           O  
ATOM   2732  CB  SER A 332      15.571  16.225 -10.695  1.00 29.21           C  
ATOM   2733  OG  SER A 332      15.406  15.759  -9.364  1.00 30.19           O  
ATOM   2734  N   ASP A 333      18.312  14.430  -9.989  1.00 32.02           N  
ATOM   2735  CA  ASP A 333      19.696  14.326  -9.459  1.00 34.30           C  
ATOM   2736  C   ASP A 333      20.773  14.073 -10.516  1.00 35.69           C  
ATOM   2737  O   ASP A 333      21.867  14.567 -10.367  1.00 35.44           O  
ATOM   2738  CB  ASP A 333      19.857  13.227  -8.392  1.00 37.04           C  
ATOM   2739  CG  ASP A 333      19.093  13.513  -7.123  1.00 37.25           C  
ATOM   2740  OD1 ASP A 333      18.775  14.667  -6.819  1.00 36.89           O  
ATOM   2741  OD2 ASP A 333      18.774  12.553  -6.430  1.00 39.87           O  
ATOM   2742  N   THR A 334      20.461  13.282 -11.549  1.00 37.28           N  
ATOM   2743  CA  THR A 334      21.340  13.082 -12.706  1.00 38.61           C  
ATOM   2744  C   THR A 334      21.794  14.417 -13.234  1.00 37.39           C  
ATOM   2745  O   THR A 334      22.983  14.650 -13.454  1.00 37.42           O  
ATOM   2746  CB  THR A 334      20.587  12.417 -13.898  1.00 39.98           C  
ATOM   2747  OG1 THR A 334      20.085  11.124 -13.524  1.00 42.34           O  
ATOM   2748  CG2 THR A 334      21.510  12.260 -15.118  1.00 41.27           C  
ATOM   2749  N   ILE A 335      20.824  15.289 -13.464  1.00 35.71           N  
ATOM   2750  CA  ILE A 335      21.119  16.587 -14.026  1.00 35.46           C  
ATOM   2751  C   ILE A 335      22.010  17.412 -13.107  1.00 34.68           C  
ATOM   2752  O   ILE A 335      23.041  17.976 -13.554  1.00 33.46           O  
ATOM   2753  CB  ILE A 335      19.809  17.342 -14.378  1.00 35.63           C  
ATOM   2754  CG1 ILE A 335      19.130  16.566 -15.514  1.00 36.50           C  
ATOM   2755  CG2 ILE A 335      20.118  18.801 -14.719  1.00 35.30           C  
ATOM   2756  CD1 ILE A 335      17.967  17.242 -16.176  1.00 36.43           C  
ATOM   2757  N   CYS A 336      21.624  17.470 -11.829  1.00 33.59           N  
ATOM   2758  CA  CYS A 336      22.411  18.201 -10.839  1.00 33.82           C  
ATOM   2759  C   CYS A 336      23.810  17.708 -10.754  1.00 34.58           C  
ATOM   2760  O   CYS A 336      24.775  18.517 -10.726  1.00 35.31           O  
ATOM   2761  CB  CYS A 336      21.791  18.076  -9.453  1.00 35.06           C  
ATOM   2762  SG  CYS A 336      20.319  19.065  -9.458  1.00 35.88           S  
ATOM   2763  N  AASP A 337      23.961  16.392 -10.695  0.50 35.14           N  
ATOM   2764  N  BASP A 337      23.944  16.385 -10.687  0.50 35.23           N  
ATOM   2765  CA AASP A 337      25.275  15.820 -10.527  0.50 36.94           C  
ATOM   2766  CA BASP A 337      25.246  15.763 -10.598  0.50 37.15           C  
ATOM   2767  C  AASP A 337      26.149  15.994 -11.794  0.50 36.85           C  
ATOM   2768  C  BASP A 337      26.107  16.099 -11.805  0.50 36.78           C  
ATOM   2769  O  AASP A 337      27.319  16.337 -11.677  0.50 37.54           O  
ATOM   2770  O  BASP A 337      27.201  16.640 -11.663  0.50 37.13           O  
ATOM   2771  CB AASP A 337      25.158  14.361 -10.067  0.50 38.55           C  
ATOM   2772  CB BASP A 337      25.122  14.245 -10.512  0.50 38.87           C  
ATOM   2773  CG AASP A 337      24.642  14.235  -8.624  0.50 38.67           C  
ATOM   2774  CG BASP A 337      26.457  13.560 -10.673  0.50 40.95           C  
ATOM   2775  OD1AASP A 337      24.326  15.255  -7.965  0.50 37.64           O  
ATOM   2776  OD1BASP A 337      27.383  13.874  -9.892  0.50 42.08           O  
ATOM   2777  OD2AASP A 337      24.547  13.098  -8.146  0.50 40.29           O  
ATOM   2778  OD2BASP A 337      26.590  12.712 -11.575  0.50 42.31           O  
ATOM   2779  N   LEU A 338      25.575  15.808 -12.988  1.00 36.21           N  
ATOM   2780  CA  LEU A 338      26.329  15.987 -14.256  1.00 36.46           C  
ATOM   2781  C   LEU A 338      26.640  17.430 -14.577  1.00 34.81           C  
ATOM   2782  O   LEU A 338      27.668  17.700 -15.165  1.00 35.37           O  
ATOM   2783  CB  LEU A 338      25.576  15.356 -15.420  1.00 36.51           C  
ATOM   2784  CG  LEU A 338      25.498  13.827 -15.354  1.00 38.31           C  
ATOM   2785  CD1 LEU A 338      24.544  13.350 -16.431  1.00 38.52           C  
ATOM   2786  CD2 LEU A 338      26.869  13.167 -15.514  1.00 40.34           C  
ATOM   2787  N   LEU A 339      25.771  18.361 -14.184  1.00 32.28           N  
ATOM   2788  CA  LEU A 339      26.067  19.783 -14.367  1.00 31.59           C  
ATOM   2789  C   LEU A 339      26.767  20.438 -13.170  1.00 31.90           C  
ATOM   2790  O   LEU A 339      27.103  21.612 -13.236  1.00 31.21           O  
ATOM   2791  CB  LEU A 339      24.771  20.545 -14.692  1.00 30.45           C  
ATOM   2792  CG  LEU A 339      24.048  20.064 -15.959  1.00 30.44           C  
ATOM   2793  CD1 LEU A 339      22.805  20.885 -16.129  1.00 29.53           C  
ATOM   2794  CD2 LEU A 339      24.906  20.157 -17.192  1.00 32.24           C  
ATOM   2795  N   GLY A 340      26.966  19.707 -12.071  1.00 33.00           N  
ATOM   2796  CA  GLY A 340      27.620  20.264 -10.876  1.00 33.91           C  
ATOM   2797  C   GLY A 340      26.813  21.401 -10.269  1.00 33.33           C  
ATOM   2798  O   GLY A 340      27.386  22.394  -9.857  1.00 33.61           O  
ATOM   2799  N   ALA A 341      25.485  21.253 -10.241  1.00 32.13           N  
ATOM   2800  CA  ALA A 341      24.562  22.282  -9.753  1.00 32.07           C  
ATOM   2801  C   ALA A 341      23.854  21.825  -8.450  1.00 33.13           C  
ATOM   2802  O   ALA A 341      23.658  20.623  -8.235  1.00 34.57           O  
ATOM   2803  CB  ALA A 341      23.501  22.594 -10.801  1.00 30.54           C  
ATOM   2804  N   LYS A 342      23.567  22.786  -7.580  1.00 33.52           N  
ATOM   2805  CA  LYS A 342      22.632  22.619  -6.471  1.00 34.61           C  
ATOM   2806  C   LYS A 342      21.314  23.186  -6.995  1.00 31.94           C  
ATOM   2807  O   LYS A 342      21.299  24.012  -7.937  1.00 33.17           O  
ATOM   2808  CB  LYS A 342      23.022  23.411  -5.214  1.00 36.90           C  
ATOM   2809  CG  LYS A 342      24.487  23.673  -4.917  1.00 40.09           C  
ATOM   2810  CD  LYS A 342      25.415  22.495  -5.096  1.00 42.78           C  
ATOM   2811  CE  LYS A 342      24.946  21.232  -4.414  1.00 44.65           C  
ATOM   2812  NZ  LYS A 342      25.995  20.192  -4.584  1.00 47.47           N  
ATOM   2813  N   GLY A 343      20.229  22.788  -6.369  1.00 30.71           N  
ATOM   2814  CA  GLY A 343      18.887  23.193  -6.767  1.00 27.83           C  
ATOM   2815  C   GLY A 343      18.695  24.670  -7.016  1.00 26.61           C  
ATOM   2816  O   GLY A 343      18.190  25.078  -8.069  1.00 24.16           O  
ATOM   2817  N   LYS A 344      19.118  25.480  -6.056  1.00 26.92           N  
ATOM   2818  CA  LYS A 344      18.926  26.922  -6.143  1.00 27.23           C  
ATOM   2819  C   LYS A 344      19.784  27.616  -7.189  1.00 27.59           C  
ATOM   2820  O   LYS A 344      19.547  28.798  -7.453  1.00 28.53           O  
ATOM   2821  CB  LYS A 344      19.133  27.592  -4.790  1.00 28.66           C  
ATOM   2822  CG  LYS A 344      17.992  27.395  -3.840  1.00 28.99           C  
ATOM   2823  CD  LYS A 344      18.517  27.570  -2.411  1.00 30.53           C  
ATOM   2824  CE  LYS A 344      17.579  26.920  -1.467  1.00 30.98           C  
ATOM   2825  NZ  LYS A 344      18.026  26.999  -0.064  1.00 32.28           N  
ATOM   2826  N   ASP A 345      20.738  26.894  -7.780  1.00 27.94           N  
ATOM   2827  CA  ASP A 345      21.495  27.357  -8.909  1.00 28.68           C  
ATOM   2828  C   ASP A 345      20.701  27.225 -10.224  1.00 26.13           C  
ATOM   2829  O   ASP A 345      21.181  27.678 -11.251  1.00 25.36           O  
ATOM   2830  CB  ASP A 345      22.717  26.438  -9.190  1.00 31.48           C  
ATOM   2831  CG  ASP A 345      23.743  26.426  -8.145  1.00 34.36           C  
ATOM   2832  OD1 ASP A 345      23.870  27.415  -7.368  1.00 38.07           O  
ATOM   2833  OD2 ASP A 345      24.471  25.389  -8.132  1.00 35.20           O  
ATOM   2834  N   ILE A 346      19.566  26.515 -10.209  1.00 24.53           N  
ATOM   2835  CA  ILE A 346      18.844  26.141 -11.414  1.00 23.17           C  
ATOM   2836  C   ILE A 346      17.571  26.982 -11.528  1.00 22.61           C  
ATOM   2837  O   ILE A 346      16.784  27.048 -10.572  1.00 21.85           O  
ATOM   2838  CB  ILE A 346      18.434  24.655 -11.378  1.00 22.76           C  
ATOM   2839  CG1 ILE A 346      19.686  23.770 -11.443  1.00 23.84           C  
ATOM   2840  CG2 ILE A 346      17.499  24.321 -12.561  1.00 22.20           C  
ATOM   2841  CD1 ILE A 346      19.469  22.302 -11.098  1.00 24.32           C  
ATOM   2842  N   LEU A 347      17.374  27.592 -12.698  1.00 22.58           N  
ATOM   2843  CA  LEU A 347      16.069  28.135 -13.065  1.00 21.64           C  
ATOM   2844  C   LEU A 347      15.436  27.204 -14.064  1.00 20.95           C  
ATOM   2845  O   LEU A 347      15.910  27.095 -15.194  1.00 20.89           O  
ATOM   2846  CB  LEU A 347      16.200  29.555 -13.625  1.00 22.30           C  
ATOM   2847  CG  LEU A 347      14.893  30.237 -14.035  1.00 22.23           C  
ATOM   2848  CD1 LEU A 347      14.009  30.485 -12.837  1.00 22.28           C  
ATOM   2849  CD2 LEU A 347      15.206  31.538 -14.770  1.00 23.25           C  
ATOM   2850  N   TYR A 348      14.367  26.527 -13.640  1.00 20.25           N  
ATOM   2851  CA  TYR A 348      13.658  25.595 -14.482  1.00 20.16           C  
ATOM   2852  C   TYR A 348      12.416  26.277 -15.055  1.00 19.22           C  
ATOM   2853  O   TYR A 348      11.622  26.894 -14.325  1.00 18.29           O  
ATOM   2854  CB  TYR A 348      13.273  24.287 -13.786  1.00 21.10           C  
ATOM   2855  CG  TYR A 348      12.767  23.238 -14.767  1.00 22.73           C  
ATOM   2856  CD1 TYR A 348      13.614  22.672 -15.675  1.00 23.82           C  
ATOM   2857  CD2 TYR A 348      11.411  22.867 -14.822  1.00 24.44           C  
ATOM   2858  CE1 TYR A 348      13.188  21.752 -16.597  1.00 25.08           C  
ATOM   2859  CE2 TYR A 348      10.963  21.931 -15.772  1.00 25.45           C  
ATOM   2860  CZ  TYR A 348      11.869  21.377 -16.640  1.00 26.25           C  
ATOM   2861  OH  TYR A 348      11.495  20.480 -17.626  1.00 28.47           O  
ATOM   2862  N   ILE A 349      12.349  26.197 -16.375  1.00 19.14           N  
ATOM   2863  CA  ILE A 349      11.417  26.962 -17.212  1.00 18.97           C  
ATOM   2864  C   ILE A 349      10.453  25.972 -17.837  1.00 18.91           C  
ATOM   2865  O   ILE A 349      10.856  25.119 -18.651  1.00 19.41           O  
ATOM   2866  CB  ILE A 349      12.195  27.753 -18.299  1.00 18.99           C  
ATOM   2867  CG1 ILE A 349      13.190  28.706 -17.634  1.00 19.04           C  
ATOM   2868  CG2 ILE A 349      11.229  28.502 -19.195  1.00 19.14           C  
ATOM   2869  CD1 ILE A 349      14.173  29.345 -18.572  1.00 19.95           C  
ATOM   2870  N   GLY A 350       9.173  26.088 -17.482  1.00 18.93           N  
ATOM   2871  CA  GLY A 350       8.161  25.195 -18.018  1.00 19.56           C  
ATOM   2872  C   GLY A 350       6.727  25.720 -17.873  1.00 19.93           C  
ATOM   2873  O   GLY A 350       6.507  26.741 -17.296  1.00 18.92           O  
ATOM   2874  N   ASP A 351       5.789  25.001 -18.442  1.00 22.11           N  
ATOM   2875  CA  ASP A 351       4.339  25.371 -18.416  1.00 23.61           C  
ATOM   2876  C   ASP A 351       3.464  24.515 -17.472  1.00 25.22           C  
ATOM   2877  O   ASP A 351       2.274  24.868 -17.228  1.00 24.59           O  
ATOM   2878  CB  ASP A 351       3.732  25.194 -19.794  1.00 24.14           C  
ATOM   2879  CG  ASP A 351       3.692  23.727 -20.212  1.00 25.67           C  
ATOM   2880  OD1 ASP A 351       4.759  23.046 -20.185  1.00 28.08           O  
ATOM   2881  OD2 ASP A 351       2.633  23.202 -20.555  1.00 26.53           O  
ATOM   2882  N  AHIS A 352       3.986  23.373 -17.013  0.50 26.39           N  
ATOM   2883  N  BHIS A 352       4.014  23.405 -16.994  0.50 25.99           N  
ATOM   2884  CA AHIS A 352       3.212  22.425 -16.186  0.50 28.32           C  
ATOM   2885  CA BHIS A 352       3.227  22.513 -16.177  0.50 27.69           C  
ATOM   2886  C  AHIS A 352       3.294  22.866 -14.729  0.50 29.14           C  
ATOM   2887  C  BHIS A 352       3.315  22.911 -14.729  0.50 28.74           C  
ATOM   2888  O  AHIS A 352       4.262  22.528 -14.039  0.50 28.54           O  
ATOM   2889  O  BHIS A 352       4.287  22.579 -14.044  0.50 28.20           O  
ATOM   2890  CB AHIS A 352       3.745  20.983 -16.316  0.50 29.11           C  
ATOM   2891  CB BHIS A 352       3.638  21.064 -16.283  0.50 28.09           C  
ATOM   2892  CG AHIS A 352       3.213  20.231 -17.502  0.50 30.45           C  
ATOM   2893  CG BHIS A 352       2.580  20.170 -15.745  0.50 28.86           C  
ATOM   2894  ND1AHIS A 352       2.401  19.120 -17.387  0.50 31.89           N  
ATOM   2895  ND1BHIS A 352       2.603  18.799 -15.856  0.50 30.20           N  
ATOM   2896  CD2AHIS A 352       3.402  20.416 -18.827  0.50 30.98           C  
ATOM   2897  CD2BHIS A 352       1.406  20.487 -15.148  0.50 28.98           C  
ATOM   2898  CE1AHIS A 352       2.092  18.672 -18.594  0.50 32.89           C  
ATOM   2899  CE1BHIS A 352       1.498  18.307 -15.320  0.50 30.85           C  
ATOM   2900  NE2AHIS A 352       2.687  19.440 -19.488  0.50 32.43           N  
ATOM   2901  NE2BHIS A 352       0.763  19.316 -14.878  0.50 30.43           N  
ATOM   2902  N   ILE A 353       2.280  23.598 -14.268  1.00 30.51           N  
ATOM   2903  CA  ILE A 353       2.269  24.194 -12.921  1.00 33.46           C  
ATOM   2904  C   ILE A 353       2.308  23.161 -11.823  1.00 36.60           C  
ATOM   2905  O   ILE A 353       2.928  23.418 -10.787  1.00 36.25           O  
ATOM   2906  CB  ILE A 353       1.100  25.213 -12.709  1.00 34.79           C  
ATOM   2907  CG1 ILE A 353       1.150  25.900 -11.340  1.00 35.14           C  
ATOM   2908  CG2 ILE A 353      -0.244  24.533 -12.830  1.00 36.42           C  
ATOM   2909  CD1 ILE A 353       2.445  26.557 -10.951  1.00 35.47           C  
ATOM   2910  N   PHE A 354       1.674  22.004 -12.038  1.00 39.59           N  
ATOM   2911  CA  PHE A 354       1.858  20.885 -11.125  1.00 44.35           C  
ATOM   2912  C   PHE A 354       3.115  20.062 -11.446  1.00 45.72           C  
ATOM   2913  O   PHE A 354       4.193  20.154 -10.771  1.00 47.68           O  
ATOM   2914  CB  PHE A 354       0.608  20.023 -11.074  1.00 49.58           C  
ATOM   2915  CG  PHE A 354       0.675  18.929 -10.043  1.00 54.48           C  
ATOM   2916  CD1 PHE A 354       1.199  17.667 -10.361  1.00 57.92           C  
ATOM   2917  CD2 PHE A 354       0.186  19.146  -8.734  1.00 56.73           C  
ATOM   2918  CE1 PHE A 354       1.251  16.650  -9.393  1.00 59.69           C  
ATOM   2919  CE2 PHE A 354       0.239  18.138  -7.773  1.00 58.33           C  
ATOM   2920  CZ  PHE A 354       0.775  16.891  -8.101  1.00 60.14           C  
ATOM   2921  N   GLY A 355       3.013  19.257 -12.485  1.00 44.29           N  
ATOM   2922  CA  GLY A 355       4.020  18.243 -12.785  1.00 44.38           C  
ATOM   2923  C   GLY A 355       5.487  18.620 -12.872  1.00 42.49           C  
ATOM   2924  O   GLY A 355       6.364  17.746 -12.754  1.00 47.41           O  
ATOM   2925  N   ASP A 356       5.756  19.874 -13.172  1.00 37.50           N  
ATOM   2926  CA  ASP A 356       7.109  20.363 -13.259  1.00 35.06           C  
ATOM   2927  C   ASP A 356       7.469  21.427 -12.252  1.00 31.88           C  
ATOM   2928  O   ASP A 356       8.508  21.296 -11.582  1.00 32.16           O  
ATOM   2929  CB  ASP A 356       7.388  20.955 -14.650  1.00 35.68           C  
ATOM   2930  CG  ASP A 356       7.542  19.900 -15.707  1.00 36.09           C  
ATOM   2931  OD1 ASP A 356       7.270  18.710 -15.419  1.00 40.50           O  
ATOM   2932  OD2 ASP A 356       7.893  20.255 -16.827  1.00 33.62           O  
ATOM   2933  N   ILE A 357       6.696  22.507 -12.222  1.00 27.53           N  
ATOM   2934  CA  ILE A 357       7.055  23.672 -11.466  1.00 26.75           C  
ATOM   2935  C   ILE A 357       6.865  23.391  -9.961  1.00 25.92           C  
ATOM   2936  O   ILE A 357       7.813  23.532  -9.173  1.00 24.10           O  
ATOM   2937  CB  ILE A 357       6.267  24.902 -11.920  1.00 27.43           C  
ATOM   2938  CG1 ILE A 357       6.662  25.324 -13.347  1.00 28.84           C  
ATOM   2939  CG2 ILE A 357       6.409  26.052 -10.917  1.00 28.11           C  
ATOM   2940  CD1 ILE A 357       8.127  25.485 -13.638  1.00 29.54           C  
ATOM   2941  N   LEU A 358       5.662  22.958  -9.588  1.00 25.07           N  
ATOM   2942  CA  LEU A 358       5.387  22.573  -8.205  1.00 25.70           C  
ATOM   2943  C   LEU A 358       6.372  21.514  -7.681  1.00 25.50           C  
ATOM   2944  O   LEU A 358       6.989  21.689  -6.636  1.00 24.69           O  
ATOM   2945  CB  LEU A 358       3.957  22.083  -8.055  1.00 27.08           C  
ATOM   2946  CG  LEU A 358       3.462  21.740  -6.653  1.00 28.63           C  
ATOM   2947  CD1 LEU A 358       1.946  21.893  -6.616  1.00 29.84           C  
ATOM   2948  CD2 LEU A 358       3.840  20.329  -6.219  1.00 30.00           C  
ATOM   2949  N   LYS A 359       6.561  20.453  -8.432  1.00 25.18           N  
ATOM   2950  CA  LYS A 359       7.379  19.361  -7.969  1.00 26.49           C  
ATOM   2951  C   LYS A 359       8.881  19.663  -7.911  1.00 25.56           C  
ATOM   2952  O   LYS A 359       9.546  19.231  -6.993  1.00 26.44           O  
ATOM   2953  CB  LYS A 359       7.124  18.117  -8.800  1.00 28.39           C  
ATOM   2954  CG  LYS A 359       5.727  17.566  -8.620  1.00 30.51           C  
ATOM   2955  CD  LYS A 359       5.637  16.719  -7.386  1.00 33.29           C  
ATOM   2956  CE  LYS A 359       4.180  16.469  -7.067  1.00 35.63           C  
ATOM   2957  NZ  LYS A 359       4.125  15.626  -5.851  1.00 38.40           N  
ATOM   2958  N   SER A 360       9.403  20.395  -8.875  1.00 23.89           N  
ATOM   2959  CA  SER A 360      10.820  20.783  -8.853  1.00 23.31           C  
ATOM   2960  C   SER A 360      11.063  21.731  -7.648  1.00 23.52           C  
ATOM   2961  O   SER A 360      12.080  21.625  -6.939  1.00 23.74           O  
ATOM   2962  CB  SER A 360      11.238  21.418 -10.168  1.00 21.91           C  
ATOM   2963  OG  SER A 360      10.701  22.728 -10.343  1.00 20.90           O  
ATOM   2964  N   LYS A 361      10.117  22.641  -7.405  1.00 23.03           N  
ATOM   2965  CA  LYS A 361      10.192  23.509  -6.234  1.00 23.79           C  
ATOM   2966  C   LYS A 361      10.126  22.682  -4.928  1.00 25.18           C  
ATOM   2967  O   LYS A 361      11.069  22.725  -4.148  1.00 24.63           O  
ATOM   2968  CB  LYS A 361       9.104  24.579  -6.282  1.00 23.79           C  
ATOM   2969  CG  LYS A 361       8.994  25.474  -5.057  1.00 24.67           C  
ATOM   2970  CD  LYS A 361      10.173  26.371  -4.825  1.00 24.84           C  
ATOM   2971  CE  LYS A 361      10.381  27.410  -5.918  1.00 24.48           C  
ATOM   2972  NZ  LYS A 361      11.530  28.277  -5.504  1.00 25.30           N  
ATOM   2973  N   LYS A 362       9.063  21.909  -4.717  1.00 26.11           N  
ATOM   2974  CA  LYS A 362       8.879  21.200  -3.431  1.00 28.90           C  
ATOM   2975  C   LYS A 362       9.865  20.078  -3.199  1.00 28.83           C  
ATOM   2976  O   LYS A 362      10.288  19.860  -2.096  1.00 28.94           O  
ATOM   2977  CB  LYS A 362       7.480  20.591  -3.259  1.00 31.31           C  
ATOM   2978  CG  LYS A 362       6.353  21.591  -3.358  1.00 32.95           C  
ATOM   2979  CD  LYS A 362       5.009  20.924  -2.997  1.00 35.57           C  
ATOM   2980  CE  LYS A 362       4.961  20.565  -1.527  1.00 38.59           C  
ATOM   2981  NZ  LYS A 362       3.620  20.808  -0.948  1.00 41.43           N  
ATOM   2982  N   ARG A 363      10.210  19.335  -4.233  1.00 28.50           N  
ATOM   2983  CA  ARG A 363      11.042  18.153  -4.026  1.00 30.36           C  
ATOM   2984  C   ARG A 363      12.530  18.474  -4.059  1.00 28.53           C  
ATOM   2985  O   ARG A 363      13.321  17.731  -3.521  1.00 28.81           O  
ATOM   2986  CB  ARG A 363      10.742  17.095  -5.068  1.00 32.70           C  
ATOM   2987  CG  ARG A 363       9.270  16.671  -5.164  1.00 35.05           C  
ATOM   2988  CD  ARG A 363       8.915  15.627  -4.177  1.00 40.47           C  
ATOM   2989  NE  ARG A 363       9.848  14.505  -4.190  1.00 45.69           N  
ATOM   2990  CZ  ARG A 363       9.760  13.454  -3.384  1.00 51.96           C  
ATOM   2991  NH1 ARG A 363       8.769  13.351  -2.510  1.00 55.42           N  
ATOM   2992  NH2 ARG A 363      10.672  12.485  -3.457  1.00 56.09           N  
ATOM   2993  N   GLN A 364      12.906  19.551  -4.739  1.00 26.18           N  
ATOM   2994  CA  GLN A 364      14.321  19.830  -4.984  1.00 25.81           C  
ATOM   2995  C   GLN A 364      14.776  21.248  -4.699  1.00 24.77           C  
ATOM   2996  O   GLN A 364      15.966  21.517  -4.735  1.00 24.78           O  
ATOM   2997  CB  GLN A 364      14.666  19.475  -6.460  1.00 25.64           C  
ATOM   2998  CG  GLN A 364      14.443  18.008  -6.815  1.00 26.97           C  
ATOM   2999  CD  GLN A 364      15.293  17.053  -5.986  1.00 29.13           C  
ATOM   3000  OE1 GLN A 364      16.329  17.431  -5.435  1.00 28.97           O  
ATOM   3001  NE2 GLN A 364      14.824  15.801  -5.856  1.00 30.96           N  
ATOM   3002  N   GLY A 365      13.868  22.170  -4.461  1.00 23.62           N  
ATOM   3003  CA  GLY A 365      14.241  23.549  -4.248  1.00 23.53           C  
ATOM   3004  C   GLY A 365      14.783  24.263  -5.479  1.00 22.58           C  
ATOM   3005  O   GLY A 365      15.621  25.166  -5.346  1.00 23.45           O  
ATOM   3006  N   TRP A 366      14.365  23.844  -6.670  1.00 21.54           N  
ATOM   3007  CA  TRP A 366      14.758  24.533  -7.877  1.00 21.04           C  
ATOM   3008  C   TRP A 366      14.066  25.900  -7.930  1.00 20.67           C  
ATOM   3009  O   TRP A 366      13.012  26.093  -7.323  1.00 20.55           O  
ATOM   3010  CB  TRP A 366      14.424  23.701  -9.118  1.00 21.02           C  
ATOM   3011  CG  TRP A 366      15.286  22.470  -9.307  1.00 21.76           C  
ATOM   3012  CD1 TRP A 366      16.162  21.914  -8.404  1.00 22.88           C  
ATOM   3013  CD2 TRP A 366      15.355  21.658 -10.474  1.00 21.85           C  
ATOM   3014  NE1 TRP A 366      16.794  20.827  -8.965  1.00 23.36           N  
ATOM   3015  CE2 TRP A 366      16.323  20.652 -10.236  1.00 22.74           C  
ATOM   3016  CE3 TRP A 366      14.718  21.701 -11.729  1.00 21.27           C  
ATOM   3017  CZ2 TRP A 366      16.644  19.682 -11.195  1.00 23.22           C  
ATOM   3018  CZ3 TRP A 366      15.034  20.738 -12.663  1.00 21.82           C  
ATOM   3019  CH2 TRP A 366      15.988  19.745 -12.398  1.00 22.62           C  
ATOM   3020  N   ARG A 367      14.704  26.871  -8.578  1.00 20.72           N  
ATOM   3021  CA  ARG A 367      13.996  28.099  -8.918  1.00 20.52           C  
ATOM   3022  C   ARG A 367      13.148  27.818 -10.163  1.00 19.74           C  
ATOM   3023  O   ARG A 367      13.486  26.953 -11.004  1.00 18.97           O  
ATOM   3024  CB  ARG A 367      14.927  29.282  -9.092  1.00 21.20           C  
ATOM   3025  CG  ARG A 367      15.896  29.503  -7.950  1.00 22.69           C  
ATOM   3026  CD  ARG A 367      15.272  29.608  -6.553  1.00 23.63           C  
ATOM   3027  NE  ARG A 367      14.310  30.710  -6.380  1.00 24.01           N  
ATOM   3028  CZ  ARG A 367      14.620  31.969  -6.068  1.00 25.76           C  
ATOM   3029  NH1 ARG A 367      15.912  32.363  -5.947  1.00 26.79           N  
ATOM   3030  NH2 ARG A 367      13.658  32.875  -5.910  1.00 25.64           N  
ATOM   3031  N   THR A 368      12.019  28.517 -10.230  1.00 18.86           N  
ATOM   3032  CA  THR A 368      10.982  28.212 -11.186  1.00 18.26           C  
ATOM   3033  C   THR A 368      10.543  29.447 -11.995  1.00 18.33           C  
ATOM   3034  O   THR A 368      10.365  30.559 -11.453  1.00 18.37           O  
ATOM   3035  CB  THR A 368       9.766  27.625 -10.473  1.00 18.33           C  
ATOM   3036  OG1 THR A 368       9.352  28.515  -9.417  1.00 18.13           O  
ATOM   3037  CG2 THR A 368      10.076  26.249  -9.921  1.00 18.66           C  
ATOM   3038  N   PHE A 369      10.340  29.202 -13.287  1.00 18.22           N  
ATOM   3039  CA  PHE A 369       9.750  30.159 -14.217  1.00 18.35           C  
ATOM   3040  C   PHE A 369       8.614  29.442 -14.908  1.00 18.40           C  
ATOM   3041  O   PHE A 369       8.834  28.496 -15.677  1.00 18.73           O  
ATOM   3042  CB  PHE A 369      10.781  30.645 -15.252  1.00 18.68           C  
ATOM   3043  CG  PHE A 369      10.300  31.779 -16.152  1.00 18.88           C  
ATOM   3044  CD1 PHE A 369       9.278  31.595 -17.078  1.00 19.09           C  
ATOM   3045  CD2 PHE A 369      10.889  33.008 -16.081  1.00 19.47           C  
ATOM   3046  CE1 PHE A 369       8.869  32.632 -17.926  1.00 19.69           C  
ATOM   3047  CE2 PHE A 369      10.472  34.054 -16.905  1.00 20.29           C  
ATOM   3048  CZ  PHE A 369       9.453  33.870 -17.817  1.00 20.02           C  
ATOM   3049  N   LEU A 370       7.385  29.923 -14.674  1.00 18.05           N  
ATOM   3050  CA  LEU A 370       6.224  29.350 -15.291  1.00 17.59           C  
ATOM   3051  C   LEU A 370       5.822  30.165 -16.526  1.00 17.78           C  
ATOM   3052  O   LEU A 370       5.560  31.377 -16.453  1.00 17.54           O  
ATOM   3053  CB  LEU A 370       5.069  29.291 -14.327  1.00 17.93           C  
ATOM   3054  CG  LEU A 370       3.793  28.646 -14.842  1.00 18.30           C  
ATOM   3055  CD1 LEU A 370       3.999  27.148 -14.946  1.00 18.59           C  
ATOM   3056  CD2 LEU A 370       2.635  28.943 -13.884  1.00 18.99           C  
ATOM   3057  N   VAL A 371       5.737  29.452 -17.637  1.00 17.39           N  
ATOM   3058  CA  VAL A 371       5.207  29.980 -18.882  1.00 18.15           C  
ATOM   3059  C   VAL A 371       3.708  29.748 -18.840  1.00 18.13           C  
ATOM   3060  O   VAL A 371       3.256  28.611 -18.630  1.00 18.25           O  
ATOM   3061  CB  VAL A 371       5.815  29.242 -20.081  1.00 18.55           C  
ATOM   3062  CG1 VAL A 371       5.189  29.687 -21.390  1.00 19.55           C  
ATOM   3063  CG2 VAL A 371       7.336  29.474 -20.088  1.00 18.60           C  
ATOM   3064  N   ILE A 372       2.938  30.825 -19.023  1.00 18.36           N  
ATOM   3065  CA  ILE A 372       1.469  30.731 -19.075  1.00 18.73           C  
ATOM   3066  C   ILE A 372       1.006  31.334 -20.396  1.00 19.66           C  
ATOM   3067  O   ILE A 372       0.822  32.564 -20.489  1.00 20.12           O  
ATOM   3068  CB  ILE A 372       0.787  31.460 -17.901  1.00 18.64           C  
ATOM   3069  CG1 ILE A 372       1.430  31.090 -16.566  1.00 18.01           C  
ATOM   3070  CG2 ILE A 372      -0.711  31.135 -17.915  1.00 19.58           C  
ATOM   3071  CD1 ILE A 372       0.902  31.919 -15.406  1.00 18.37           C  
ATOM   3072  N   PRO A 373       0.880  30.504 -21.434  1.00 20.31           N  
ATOM   3073  CA  PRO A 373       0.637  31.054 -22.793  1.00 21.35           C  
ATOM   3074  C   PRO A 373      -0.580  31.947 -22.860  1.00 22.01           C  
ATOM   3075  O   PRO A 373      -0.544  32.966 -23.541  1.00 22.38           O  
ATOM   3076  CB  PRO A 373       0.440  29.811 -23.654  1.00 22.09           C  
ATOM   3077  CG  PRO A 373       1.253  28.771 -22.937  1.00 21.61           C  
ATOM   3078  CD  PRO A 373       1.140  29.050 -21.473  1.00 20.23           C  
ATOM   3079  N   GLU A 374      -1.632  31.595 -22.116  1.00 21.77           N  
ATOM   3080  CA  GLU A 374      -2.899  32.349 -22.177  1.00 22.51           C  
ATOM   3081  C   GLU A 374      -2.759  33.745 -21.652  1.00 22.83           C  
ATOM   3082  O   GLU A 374      -3.590  34.606 -21.968  1.00 23.72           O  
ATOM   3083  CB  GLU A 374      -4.057  31.670 -21.400  1.00 22.35           C  
ATOM   3084  CG  GLU A 374      -4.312  30.233 -21.786  1.00 22.33           C  
ATOM   3085  CD  GLU A 374      -3.678  29.236 -20.816  1.00 21.03           C  
ATOM   3086  OE1 GLU A 374      -2.475  29.332 -20.602  1.00 19.48           O  
ATOM   3087  OE2 GLU A 374      -4.397  28.330 -20.306  1.00 20.95           O  
ATOM   3088  N   LEU A 375      -1.758  33.981 -20.816  1.00 22.43           N  
ATOM   3089  CA  LEU A 375      -1.537  35.295 -20.287  1.00 23.62           C  
ATOM   3090  C   LEU A 375      -1.381  36.348 -21.387  1.00 26.15           C  
ATOM   3091  O   LEU A 375      -1.743  37.488 -21.173  1.00 27.04           O  
ATOM   3092  CB  LEU A 375      -0.323  35.303 -19.349  1.00 22.86           C  
ATOM   3093  CG  LEU A 375      -0.066  36.524 -18.472  1.00 23.05           C  
ATOM   3094  CD1 LEU A 375      -1.254  36.848 -17.571  1.00 23.24           C  
ATOM   3095  CD2 LEU A 375       1.203  36.257 -17.666  1.00 22.35           C  
ATOM   3096  N   ALA A 376      -0.837  35.940 -22.542  1.00 27.46           N  
ATOM   3097  CA  ALA A 376      -0.527  36.836 -23.636  1.00 29.78           C  
ATOM   3098  C   ALA A 376      -1.767  37.515 -24.131  1.00 31.55           C  
ATOM   3099  O   ALA A 376      -1.643  38.603 -24.646  1.00 33.71           O  
ATOM   3100  CB  ALA A 376       0.149  36.092 -24.787  1.00 30.59           C  
ATOM   3101  N   GLN A 377      -2.940  36.880 -23.964  1.00 31.58           N  
ATOM   3102  CA  GLN A 377      -4.219  37.480 -24.261  1.00 33.17           C  
ATOM   3103  C   GLN A 377      -5.031  37.899 -23.025  1.00 32.40           C  
ATOM   3104  O   GLN A 377      -5.762  38.906 -23.113  1.00 33.32           O  
ATOM   3105  CB  GLN A 377      -5.055  36.582 -25.194  1.00 34.71           C  
ATOM   3106  CG  GLN A 377      -6.446  37.128 -25.615  1.00 37.02           C  
ATOM   3107  CD  GLN A 377      -6.436  38.523 -26.261  1.00 39.06           C  
ATOM   3108  OE1 GLN A 377      -5.410  39.040 -26.739  1.00 39.56           O  
ATOM   3109  NE2 GLN A 377      -7.605  39.139 -26.288  1.00 41.14           N  
ATOM   3110  N   GLU A 378      -4.937  37.158 -21.917  1.00 29.76           N  
ATOM   3111  CA  GLU A 378      -5.602  37.546 -20.663  1.00 29.48           C  
ATOM   3112  C   GLU A 378      -5.193  38.954 -20.220  1.00 30.34           C  
ATOM   3113  O   GLU A 378      -6.003  39.640 -19.645  1.00 31.32           O  
ATOM   3114  CB  GLU A 378      -5.300  36.581 -19.499  1.00 27.69           C  
ATOM   3115  CG  GLU A 378      -5.894  35.168 -19.635  1.00 27.07           C  
ATOM   3116  CD  GLU A 378      -6.924  34.818 -18.566  1.00 26.76           C  
ATOM   3117  OE1 GLU A 378      -7.071  35.594 -17.619  1.00 27.10           O  
ATOM   3118  OE2 GLU A 378      -7.630  33.801 -18.680  1.00 26.42           O  
ATOM   3119  N   LEU A 379      -3.929  39.333 -20.448  1.00 30.81           N  
ATOM   3120  CA  LEU A 379      -3.431  40.664 -20.116  1.00 32.60           C  
ATOM   3121  C   LEU A 379      -4.093  41.740 -20.937  1.00 35.35           C  
ATOM   3122  O   LEU A 379      -4.361  42.817 -20.394  1.00 37.11           O  
ATOM   3123  CB  LEU A 379      -1.933  40.795 -20.348  1.00 32.51           C  
ATOM   3124  CG  LEU A 379      -1.093  40.273 -19.221  1.00 31.52           C  
ATOM   3125  CD1 LEU A 379       0.342  40.198 -19.699  1.00 31.69           C  
ATOM   3126  CD2 LEU A 379      -1.261  41.164 -17.993  1.00 32.22           C  
ATOM   3127  N   HIS A 380      -4.334  41.481 -22.229  1.00 35.97           N  
ATOM   3128  CA  HIS A 380      -5.089  42.442 -23.045  1.00 38.67           C  
ATOM   3129  C   HIS A 380      -6.518  42.646 -22.521  1.00 38.66           C  
ATOM   3130  O   HIS A 380      -6.975  43.778 -22.432  1.00 39.63           O  
ATOM   3131  CB  HIS A 380      -5.085  42.074 -24.534  1.00 40.26           C  
ATOM   3132  CG  HIS A 380      -3.782  42.372 -25.221  1.00 41.57           C  
ATOM   3133  ND1 HIS A 380      -3.485  43.610 -25.759  1.00 44.12           N  
ATOM   3134  CD2 HIS A 380      -2.681  41.604 -25.427  1.00 41.31           C  
ATOM   3135  CE1 HIS A 380      -2.270  43.587 -26.286  1.00 44.25           C  
ATOM   3136  NE2 HIS A 380      -1.759  42.380 -26.100  1.00 42.42           N  
ATOM   3137  N   VAL A 381      -7.212  41.567 -22.162  1.00 37.03           N  
ATOM   3138  CA  VAL A 381      -8.558  41.684 -21.571  1.00 37.60           C  
ATOM   3139  C   VAL A 381      -8.512  42.442 -20.232  1.00 37.91           C  
ATOM   3140  O   VAL A 381      -9.326  43.338 -19.992  1.00 39.12           O  
ATOM   3141  CB  VAL A 381      -9.265  40.308 -21.381  1.00 36.50           C  
ATOM   3142  CG1 VAL A 381     -10.633  40.457 -20.728  1.00 37.23           C  
ATOM   3143  CG2 VAL A 381      -9.457  39.603 -22.727  1.00 37.02           C  
ATOM   3144  N   TRP A 382      -7.581  42.067 -19.365  1.00 36.94           N  
ATOM   3145  CA  TRP A 382      -7.434  42.691 -18.035  1.00 37.72           C  
ATOM   3146  C   TRP A 382      -7.291  44.216 -18.113  1.00 40.27           C  
ATOM   3147  O   TRP A 382      -7.957  44.946 -17.385  1.00 40.62           O  
ATOM   3148  CB  TRP A 382      -6.219  42.095 -17.318  1.00 36.05           C  
ATOM   3149  CG  TRP A 382      -5.951  42.715 -15.981  1.00 35.94           C  
ATOM   3150  CD1 TRP A 382      -5.024  43.674 -15.693  1.00 36.12           C  
ATOM   3151  CD2 TRP A 382      -6.619  42.425 -14.764  1.00 35.87           C  
ATOM   3152  NE1 TRP A 382      -5.079  43.998 -14.371  1.00 36.26           N  
ATOM   3153  CE2 TRP A 382      -6.048  43.252 -13.768  1.00 36.22           C  
ATOM   3154  CE3 TRP A 382      -7.666  41.562 -14.410  1.00 35.99           C  
ATOM   3155  CZ2 TRP A 382      -6.491  43.249 -12.442  1.00 36.50           C  
ATOM   3156  CZ3 TRP A 382      -8.096  41.548 -13.083  1.00 36.29           C  
ATOM   3157  CH2 TRP A 382      -7.502  42.388 -12.115  1.00 36.39           C  
ATOM   3158  N   THR A 383      -6.415  44.668 -19.009  1.00 42.65           N  
ATOM   3159  CA  THR A 383      -6.171  46.093 -19.226  1.00 46.55           C  
ATOM   3160  C   THR A 383      -7.330  46.779 -19.961  1.00 49.68           C  
ATOM   3161  O   THR A 383      -7.746  47.842 -19.543  1.00 52.29           O  
ATOM   3162  CB  THR A 383      -4.783  46.360 -19.895  1.00 47.36           C  
ATOM   3163  OG1 THR A 383      -4.481  47.754 -19.829  1.00 49.83           O  
ATOM   3164  CG2 THR A 383      -4.752  45.997 -21.359  1.00 48.34           C  
ATOM   3165  N   ASP A 384      -7.879  46.166 -21.009  1.00 50.99           N  
ATOM   3166  CA  ASP A 384      -9.020  46.756 -21.749  1.00 54.88           C  
ATOM   3167  C   ASP A 384     -10.331  46.858 -20.945  1.00 55.56           C  
ATOM   3168  O   ASP A 384     -11.111  47.786 -21.146  1.00 57.50           O  
ATOM   3169  CB  ASP A 384      -9.315  45.992 -23.057  1.00 56.39           C  
ATOM   3170  CG  ASP A 384      -8.179  46.074 -24.081  1.00 57.85           C  
ATOM   3171  OD1 ASP A 384      -7.450  47.085 -24.133  1.00 60.01           O  
ATOM   3172  OD2 ASP A 384      -8.021  45.099 -24.854  1.00 59.81           O  
ATOM   3173  N   LYS A 385     -10.578  45.907 -20.053  1.00 54.08           N  
ATOM   3174  CA  LYS A 385     -11.801  45.897 -19.244  1.00 55.22           C  
ATOM   3175  C   LYS A 385     -11.490  46.182 -17.766  1.00 54.81           C  
ATOM   3176  O   LYS A 385     -12.235  45.759 -16.880  1.00 54.77           O  
ATOM   3177  CB  LYS A 385     -12.513  44.543 -19.379  1.00 54.83           C  
ATOM   3178  CG  LYS A 385     -12.773  44.075 -20.806  1.00 55.70           C  
ATOM   3179  CD  LYS A 385     -13.907  44.844 -21.481  1.00 58.76           C  
ATOM   3180  CE  LYS A 385     -13.781  44.734 -22.997  1.00 60.02           C  
ATOM   3181  NZ  LYS A 385     -14.984  45.201 -23.744  1.00 62.95           N  
ATOM   3182  N   SER A 386     -10.395  46.899 -17.497  1.00 54.75           N  
ATOM   3183  CA  SER A 386     -10.021  47.277 -16.121  1.00 54.60           C  
ATOM   3184  C   SER A 386     -11.137  48.044 -15.380  1.00 56.15           C  
ATOM   3185  O   SER A 386     -11.251  47.925 -14.163  1.00 55.67           O  
ATOM   3186  CB  SER A 386      -8.719  48.098 -16.110  1.00 54.97           C  
ATOM   3187  OG  SER A 386      -8.910  49.355 -16.749  1.00 57.75           O  
ATOM   3188  N   SER A 387     -11.955  48.803 -16.117  1.00 57.90           N  
ATOM   3189  CA  SER A 387     -13.084  49.537 -15.529  1.00 59.87           C  
ATOM   3190  C   SER A 387     -14.161  48.627 -14.887  1.00 58.72           C  
ATOM   3191  O   SER A 387     -14.779  49.011 -13.889  1.00 59.93           O  
ATOM   3192  CB  SER A 387     -13.718  50.491 -16.560  1.00 62.69           C  
ATOM   3193  OG  SER A 387     -14.521  49.783 -17.491  1.00 63.02           O  
ATOM   3194  N   LEU A 388     -14.391  47.439 -15.450  1.00 56.51           N  
ATOM   3195  CA  LEU A 388     -15.261  46.432 -14.793  1.00 55.68           C  
ATOM   3196  C   LEU A 388     -14.688  45.950 -13.447  1.00 53.42           C  
ATOM   3197  O   LEU A 388     -15.388  45.965 -12.434  1.00 53.45           O  
ATOM   3198  CB  LEU A 388     -15.517  45.226 -15.704  1.00 54.73           C  
ATOM   3199  CG  LEU A 388     -16.478  45.434 -16.879  1.00 56.42           C  
ATOM   3200  CD1 LEU A 388     -16.380  44.267 -17.842  1.00 55.69           C  
ATOM   3201  CD2 LEU A 388     -17.903  45.551 -16.411  1.00 58.46           C  
ATOM   3202  N   PHE A 389     -13.422  45.529 -13.443  1.00 51.19           N  
ATOM   3203  CA  PHE A 389     -12.771  45.098 -12.197  1.00 50.13           C  
ATOM   3204  C   PHE A 389     -12.746  46.211 -11.155  1.00 52.01           C  
ATOM   3205  O   PHE A 389     -13.010  45.975  -9.984  1.00 51.54           O  
ATOM   3206  CB  PHE A 389     -11.344  44.610 -12.424  1.00 48.12           C  
ATOM   3207  CG  PHE A 389     -10.732  43.977 -11.199  1.00 47.29           C  
ATOM   3208  CD1 PHE A 389     -11.195  42.737 -10.729  1.00 46.73           C  
ATOM   3209  CD2 PHE A 389      -9.733  44.621 -10.485  1.00 47.16           C  
ATOM   3210  CE1 PHE A 389     -10.649  42.151  -9.592  1.00 45.99           C  
ATOM   3211  CE2 PHE A 389      -9.182  44.033  -9.351  1.00 46.67           C  
ATOM   3212  CZ  PHE A 389      -9.646  42.804  -8.897  1.00 46.02           C  
ATOM   3213  N   GLU A 390     -12.414  47.418 -11.606  1.00 54.19           N  
ATOM   3214  CA  GLU A 390     -12.384  48.589 -10.740  1.00 56.91           C  
ATOM   3215  C   GLU A 390     -13.733  48.849 -10.128  1.00 58.23           C  
ATOM   3216  O   GLU A 390     -13.803  49.133  -8.950  1.00 59.46           O  
ATOM   3217  CB  GLU A 390     -11.894  49.824 -11.489  1.00 59.41           C  
ATOM   3218  CG  GLU A 390     -10.377  49.892 -11.511  1.00 60.19           C  
ATOM   3219  CD  GLU A 390      -9.819  50.644 -12.704  1.00 62.40           C  
ATOM   3220  OE1 GLU A 390     -10.510  51.539 -13.247  1.00 65.78           O  
ATOM   3221  OE2 GLU A 390      -8.678  50.323 -13.097  1.00 62.85           O  
ATOM   3222  N   GLU A 391     -14.794  48.739 -10.923  1.00 58.63           N  
ATOM   3223  CA  GLU A 391     -16.160  48.885 -10.410  1.00 60.72           C  
ATOM   3224  C   GLU A 391     -16.486  47.801  -9.377  1.00 59.60           C  
ATOM   3225  O   GLU A 391     -17.086  48.094  -8.337  1.00 60.11           O  
ATOM   3226  CB  GLU A 391     -17.177  48.851 -11.560  1.00 62.01           C  
ATOM   3227  CG  GLU A 391     -18.629  49.047 -11.136  1.00 64.58           C  
ATOM   3228  CD  GLU A 391     -19.617  48.913 -12.286  1.00 65.99           C  
ATOM   3229  OE1 GLU A 391     -19.194  48.850 -13.454  1.00 65.62           O  
ATOM   3230  OE2 GLU A 391     -20.835  48.870 -12.021  1.00 67.80           O  
ATOM   3231  N   LEU A 392     -16.081  46.554  -9.670  1.00 57.59           N  
ATOM   3232  CA  LEU A 392     -16.294  45.441  -8.735  1.00 56.85           C  
ATOM   3233  C   LEU A 392     -15.592  45.696  -7.398  1.00 56.82           C  
ATOM   3234  O   LEU A 392     -16.198  45.552  -6.335  1.00 57.27           O  
ATOM   3235  CB  LEU A 392     -15.841  44.102  -9.334  1.00 54.51           C  
ATOM   3236  CG  LEU A 392     -16.108  42.866  -8.463  1.00 54.14           C  
ATOM   3237  CD1 LEU A 392     -17.592  42.643  -8.270  1.00 56.19           C  
ATOM   3238  CD2 LEU A 392     -15.483  41.606  -9.053  1.00 52.07           C  
ATOM   3239  N   GLN A 393     -14.327  46.089  -7.470  1.00 55.93           N  
ATOM   3240  CA  GLN A 393     -13.589  46.511  -6.274  1.00 57.76           C  
ATOM   3241  C   GLN A 393     -14.347  47.579  -5.456  1.00 60.65           C  
ATOM   3242  O   GLN A 393     -14.468  47.455  -4.231  1.00 62.05           O  
ATOM   3243  CB  GLN A 393     -12.212  47.058  -6.658  1.00 57.56           C  
ATOM   3244  CG  GLN A 393     -11.123  46.018  -6.755  1.00 55.81           C  
ATOM   3245  CD  GLN A 393      -9.823  46.619  -7.283  1.00 56.56           C  
ATOM   3246  OE1 GLN A 393      -9.846  47.551  -8.105  1.00 58.91           O  
ATOM   3247  NE2 GLN A 393      -8.685  46.102  -6.813  1.00 54.86           N  
ATOM   3248  N   SER A 394     -14.877  48.595  -6.144  1.00 61.79           N  
ATOM   3249  CA  SER A 394     -15.617  49.695  -5.486  1.00 65.33           C  
ATOM   3250  C   SER A 394     -16.889  49.215  -4.812  1.00 66.50           C  
ATOM   3251  O   SER A 394     -17.207  49.655  -3.720  1.00 68.37           O  
ATOM   3252  CB  SER A 394     -15.957  50.812  -6.481  1.00 66.66           C  
ATOM   3253  OG  SER A 394     -14.765  51.357  -7.019  1.00 65.68           O  
ATOM   3254  N   LEU A 395     -17.590  48.292  -5.464  1.00 65.98           N  
ATOM   3255  CA  LEU A 395     -18.805  47.699  -4.912  1.00 67.61           C  
ATOM   3256  C   LEU A 395     -18.545  46.837  -3.659  1.00 67.66           C  
ATOM   3257  O   LEU A 395     -19.271  46.958  -2.668  1.00 69.37           O  
ATOM   3258  CB  LEU A 395     -19.527  46.891  -5.992  1.00 66.78           C  
ATOM   3259  CG  LEU A 395     -20.202  47.774  -7.043  1.00 68.51           C  
ATOM   3260  CD1 LEU A 395     -20.349  47.042  -8.365  1.00 67.33           C  
ATOM   3261  CD2 LEU A 395     -21.552  48.276  -6.551  1.00 71.52           C  
ATOM   3262  N   ASP A 396     -17.521  45.977  -3.710  1.00 65.42           N  
ATOM   3263  CA  ASP A 396     -17.101  45.174  -2.532  1.00 65.65           C  
ATOM   3264  C   ASP A 396     -16.731  46.092  -1.344  1.00 68.05           C  
ATOM   3265  O   ASP A 396     -17.045  45.791  -0.195  1.00 68.68           O  
ATOM   3266  CB  ASP A 396     -15.910  44.241  -2.882  1.00 61.84           C  
ATOM   3267  CG  ASP A 396     -16.268  43.151  -3.929  1.00 60.14           C  
ATOM   3268  OD1 ASP A 396     -17.458  42.883  -4.158  1.00 60.85           O  
ATOM   3269  OD2 ASP A 396     -15.342  42.556  -4.536  1.00 58.17           O  
ATOM   3270  N   ILE A 397     -16.058  47.199  -1.665  1.00 70.07           N  
ATOM   3271  CA  ILE A 397     -15.675  48.252  -0.706  1.00 73.12           C  
ATOM   3272  C   ILE A 397     -16.887  48.954  -0.106  1.00 76.76           C  
ATOM   3273  O   ILE A 397     -16.963  49.132   1.111  1.00 79.64           O  
ATOM   3274  CB  ILE A 397     -14.721  49.293  -1.377  1.00 73.24           C  
ATOM   3275  CG1 ILE A 397     -13.319  48.685  -1.560  1.00 70.98           C  
ATOM   3276  CG2 ILE A 397     -14.617  50.589  -0.578  1.00 76.20           C  
ATOM   3277  CD1 ILE A 397     -12.449  49.395  -2.587  1.00 70.21           C  
ATOM   3278  N   PHE A 398     -17.811  49.379  -0.962  1.00 78.03           N  
ATOM   3279  CA  PHE A 398     -19.029  50.083  -0.528  1.00 81.14           C  
ATOM   3280  C   PHE A 398     -19.916  49.212   0.369  1.00 82.48           C  
ATOM   3281  O   PHE A 398     -20.477  49.693   1.364  1.00 85.20           O  
ATOM   3282  CB  PHE A 398     -19.827  50.553  -1.752  1.00 81.65           C  
ATOM   3283  CG  PHE A 398     -20.987  51.447  -1.418  1.00 84.95           C  
ATOM   3284  CD1 PHE A 398     -20.768  52.740  -0.955  1.00 87.56           C  
ATOM   3285  CD2 PHE A 398     -22.305  51.004  -1.574  1.00 86.23           C  
ATOM   3286  CE1 PHE A 398     -21.840  53.573  -0.643  1.00 91.10           C  
ATOM   3287  CE2 PHE A 398     -23.379  51.834  -1.268  1.00 89.47           C  
ATOM   3288  CZ  PHE A 398     -23.146  53.118  -0.799  1.00 92.11           C  
ATOM   3289  N   LEU A 399     -20.038  47.935   0.001  1.00 80.76           N  
ATOM   3290  CA  LEU A 399     -20.766  46.935   0.801  1.00 81.66           C  
ATOM   3291  C   LEU A 399     -20.069  46.757   2.164  1.00 81.84           C  
ATOM   3292  O   LEU A 399     -20.705  46.798   3.218  1.00 83.33           O  
ATOM   3293  CB  LEU A 399     -20.833  45.596   0.040  1.00 78.89           C  
ATOM   3294  CG  LEU A 399     -21.844  44.559   0.543  1.00 79.87           C  
ATOM   3295  CD1 LEU A 399     -23.266  44.942   0.145  1.00 82.04           C  
ATOM   3296  CD2 LEU A 399     -21.494  43.171   0.026  1.00 76.97           C  
ATOM   3297  N   ALA A 400     -18.752  46.573   2.111  1.00 79.51           N  
ATOM   3298  CA  ALA A 400     -17.913  46.524   3.309  1.00 79.78           C  
ATOM   3299  C   ALA A 400     -17.681  47.930   3.885  1.00 81.63           C  
ATOM   3300  O   ALA A 400     -18.445  48.416   4.710  1.00 83.97           O  
ATOM   3301  CB  ALA A 400     -16.589  45.861   2.973  1.00 76.12           C  
ATOM   3302  N   SER A 417     -28.960  43.299  -0.321  1.00 90.30           N  
ATOM   3303  CA  SER A 417     -29.679  44.316  -1.080  1.00 92.25           C  
ATOM   3304  C   SER A 417     -29.136  44.405  -2.513  1.00 89.46           C  
ATOM   3305  O   SER A 417     -28.240  43.646  -2.876  1.00 86.74           O  
ATOM   3306  CB  SER A 417     -29.591  45.665  -0.348  1.00 94.65           C  
ATOM   3307  OG  SER A 417     -28.249  46.104  -0.245  1.00 92.21           O  
ATOM   3308  N   SER A 418     -29.663  45.338  -3.310  1.00 91.02           N  
ATOM   3309  CA  SER A 418     -29.364  45.431  -4.760  1.00 89.50           C  
ATOM   3310  C   SER A 418     -27.889  45.650  -5.133  1.00 86.55           C  
ATOM   3311  O   SER A 418     -27.527  45.543  -6.311  1.00 84.89           O  
ATOM   3312  CB  SER A 418     -30.223  46.518  -5.439  1.00 92.10           C  
ATOM   3313  OG  SER A 418     -29.635  47.798  -5.335  1.00 92.45           O  
ATOM   3314  N   ILE A 419     -27.058  45.987  -4.147  1.00 86.15           N  
ATOM   3315  CA  ILE A 419     -25.599  46.002  -4.319  1.00 83.09           C  
ATOM   3316  C   ILE A 419     -25.063  44.581  -4.625  1.00 79.96           C  
ATOM   3317  O   ILE A 419     -24.164  44.435  -5.460  1.00 77.53           O  
ATOM   3318  CB  ILE A 419     -24.897  46.641  -3.083  1.00 83.65           C  
ATOM   3319  CG1 ILE A 419     -25.340  48.107  -2.880  1.00 86.78           C  
ATOM   3320  CG2 ILE A 419     -23.380  46.589  -3.194  1.00 80.87           C  
ATOM   3321  CD1 ILE A 419     -25.024  49.063  -4.020  1.00 86.51           C  
ATOM   3322  N   GLN A 420     -25.616  43.552  -3.973  1.00 80.41           N  
ATOM   3323  CA  GLN A 420     -25.212  42.153  -4.222  1.00 78.19           C  
ATOM   3324  C   GLN A 420     -25.554  41.688  -5.640  1.00 76.87           C  
ATOM   3325  O   GLN A 420     -24.709  41.105  -6.327  1.00 74.29           O  
ATOM   3326  CB  GLN A 420     -25.857  41.211  -3.211  1.00 79.84           C  
ATOM   3327  CG  GLN A 420     -25.314  41.370  -1.803  1.00 80.76           C  
ATOM   3328  CD  GLN A 420     -26.244  40.805  -0.735  1.00 83.84           C  
ATOM   3329  OE1 GLN A 420     -27.472  41.014  -0.770  1.00 85.95           O  
ATOM   3330  NE2 GLN A 420     -25.663  40.105   0.241  1.00 83.42           N  
ATOM   3331  N   ARG A 421     -26.799  41.932  -6.043  1.00 78.37           N  
ATOM   3332  CA  ARG A 421     -27.275  41.746  -7.432  1.00 78.37           C  
ATOM   3333  C   ARG A 421     -26.334  42.365  -8.457  1.00 75.94           C  
ATOM   3334  O   ARG A 421     -26.009  41.745  -9.468  1.00 73.54           O  
ATOM   3335  CB  ARG A 421     -28.663  42.396  -7.636  1.00 81.77           C  
ATOM   3336  CG  ARG A 421     -29.791  41.462  -8.054  1.00 83.23           C  
ATOM   3337  CD  ARG A 421     -31.096  42.247  -8.171  1.00 86.65           C  
ATOM   3338  NE  ARG A 421     -31.495  42.763  -6.861  1.00 88.79           N  
ATOM   3339  CZ  ARG A 421     -32.134  43.912  -6.611  1.00 91.56           C  
ATOM   3340  NH1 ARG A 421     -32.500  44.756  -7.579  1.00 92.92           N  
ATOM   3341  NH2 ARG A 421     -32.408  44.225  -5.350  1.00 93.18           N  
ATOM   3342  N   ARG A 422     -25.953  43.612  -8.198  1.00 71.54           N  
ATOM   3343  CA  ARG A 422     -25.042  44.339  -9.069  1.00 70.16           C  
ATOM   3344  C   ARG A 422     -23.617  43.733  -9.019  1.00 65.03           C  
ATOM   3345  O   ARG A 422     -22.950  43.680 -10.056  1.00 61.15           O  
ATOM   3346  CB  ARG A 422     -25.061  45.832  -8.721  1.00 74.62           C  
ATOM   3347  CG  ARG A 422     -23.910  46.661  -9.267  1.00 75.01           C  
ATOM   3348  CD  ARG A 422     -24.055  47.127 -10.717  1.00 76.04           C  
ATOM   3349  NE  ARG A 422     -23.144  48.260 -10.885  1.00 78.16           N  
ATOM   3350  CZ  ARG A 422     -23.354  49.499 -10.409  1.00 83.87           C  
ATOM   3351  NH1 ARG A 422     -24.491  49.834  -9.780  1.00 88.16           N  
ATOM   3352  NH2 ARG A 422     -22.423  50.439 -10.584  1.00 85.35           N  
ATOM   3353  N   ILE A 423     -23.176  43.284  -7.837  1.00 63.56           N  
ATOM   3354  CA  ILE A 423     -21.905  42.545  -7.705  1.00 60.44           C  
ATOM   3355  C   ILE A 423     -21.915  41.256  -8.554  1.00 57.83           C  
ATOM   3356  O   ILE A 423     -20.952  40.989  -9.274  1.00 54.89           O  
ATOM   3357  CB  ILE A 423     -21.529  42.271  -6.226  1.00 60.55           C  
ATOM   3358  CG1 ILE A 423     -20.971  43.568  -5.610  1.00 63.18           C  
ATOM   3359  CG2 ILE A 423     -20.479  41.160  -6.085  1.00 56.79           C  
ATOM   3360  CD1 ILE A 423     -20.828  43.581  -4.095  1.00 65.03           C  
ATOM   3361  N   LYS A 424     -23.000  40.483  -8.475  1.00 59.40           N  
ATOM   3362  CA  LYS A 424     -23.177  39.300  -9.338  1.00 57.49           C  
ATOM   3363  C   LYS A 424     -23.169  39.661 -10.824  1.00 55.17           C  
ATOM   3364  O   LYS A 424     -22.528  38.976 -11.622  1.00 51.32           O  
ATOM   3365  CB  LYS A 424     -24.475  38.570  -9.013  1.00 61.41           C  
ATOM   3366  CG  LYS A 424     -24.412  37.686  -7.772  1.00 63.25           C  
ATOM   3367  CD  LYS A 424     -25.824  37.482  -7.192  1.00 68.42           C  
ATOM   3368  CE  LYS A 424     -26.128  36.028  -6.841  1.00 69.56           C  
ATOM   3369  NZ  LYS A 424     -25.103  35.399  -5.954  1.00 68.91           N  
ATOM   3370  N   LYS A 425     -23.875  40.730 -11.190  1.00 56.71           N  
ATOM   3371  CA  LYS A 425     -24.000  41.099 -12.610  1.00 56.15           C  
ATOM   3372  C   LYS A 425     -22.651  41.526 -13.186  1.00 52.09           C  
ATOM   3373  O   LYS A 425     -22.287  41.096 -14.284  1.00 49.86           O  
ATOM   3374  CB  LYS A 425     -25.038  42.202 -12.839  1.00 60.76           C  
ATOM   3375  CG  LYS A 425     -25.279  42.559 -14.308  1.00 62.43           C  
ATOM   3376  CD  LYS A 425     -25.947  43.932 -14.442  1.00 67.81           C  
ATOM   3377  CE  LYS A 425     -26.480  44.211 -15.853  1.00 69.96           C  
ATOM   3378  NZ  LYS A 425     -25.505  43.826 -16.926  1.00 67.99           N  
ATOM   3379  N   VAL A 426     -21.950  42.396 -12.459  1.00 50.50           N  
ATOM   3380  CA  VAL A 426     -20.633  42.885 -12.877  1.00 48.05           C  
ATOM   3381  C   VAL A 426     -19.619  41.716 -12.928  1.00 43.35           C  
ATOM   3382  O   VAL A 426     -18.759  41.677 -13.825  1.00 41.06           O  
ATOM   3383  CB  VAL A 426     -20.151  44.054 -11.968  1.00 50.17           C  
ATOM   3384  CG1 VAL A 426     -18.679  44.371 -12.176  1.00 48.84           C  
ATOM   3385  CG2 VAL A 426     -20.986  45.316 -12.218  1.00 54.40           C  
ATOM   3386  N   THR A 427     -19.726  40.794 -11.965  1.00 41.30           N  
ATOM   3387  CA  THR A 427     -18.901  39.594 -11.931  1.00 38.82           C  
ATOM   3388  C   THR A 427     -19.115  38.790 -13.233  1.00 37.77           C  
ATOM   3389  O   THR A 427     -18.146  38.407 -13.915  1.00 34.42           O  
ATOM   3390  CB  THR A 427     -19.186  38.748 -10.659  1.00 38.74           C  
ATOM   3391  OG1 THR A 427     -18.740  39.461  -9.484  1.00 39.64           O  
ATOM   3392  CG2 THR A 427     -18.503  37.378 -10.711  1.00 35.88           C  
ATOM   3393  N   HIS A 428     -20.387  38.614 -13.603  1.00 40.09           N  
ATOM   3394  CA  HIS A 428     -20.715  37.902 -14.830  1.00 40.37           C  
ATOM   3395  C   HIS A 428     -20.114  38.571 -16.051  1.00 39.57           C  
ATOM   3396  O   HIS A 428     -19.404  37.912 -16.803  1.00 36.61           O  
ATOM   3397  CB  HIS A 428     -22.209  37.762 -15.033  1.00 43.54           C  
ATOM   3398  CG  HIS A 428     -22.566  36.849 -16.163  1.00 44.25           C  
ATOM   3399  ND1 HIS A 428     -23.131  37.297 -17.339  1.00 47.15           N  
ATOM   3400  CD2 HIS A 428     -22.428  35.512 -16.297  1.00 43.68           C  
ATOM   3401  CE1 HIS A 428     -23.338  36.274 -18.146  1.00 46.29           C  
ATOM   3402  NE2 HIS A 428     -22.907  35.181 -17.540  1.00 44.74           N  
ATOM   3403  N   ASP A 429     -20.382  39.865 -16.213  1.00 41.58           N  
ATOM   3404  CA  ASP A 429     -19.926  40.629 -17.390  1.00 42.84           C  
ATOM   3405  C   ASP A 429     -18.392  40.608 -17.510  1.00 40.77           C  
ATOM   3406  O   ASP A 429     -17.838  40.435 -18.606  1.00 40.22           O  
ATOM   3407  CB  ASP A 429     -20.402  42.086 -17.333  1.00 46.20           C  
ATOM   3408  CG  ASP A 429     -21.920  42.237 -17.460  1.00 49.40           C  
ATOM   3409  OD1 ASP A 429     -22.616  41.332 -17.977  1.00 49.52           O  
ATOM   3410  OD2 ASP A 429     -22.422  43.300 -17.047  1.00 52.55           O  
ATOM   3411  N   MET A 430     -17.714  40.776 -16.382  1.00 39.81           N  
ATOM   3412  CA  MET A 430     -16.254  40.713 -16.352  1.00 38.42           C  
ATOM   3413  C   MET A 430     -15.795  39.365 -16.889  1.00 34.98           C  
ATOM   3414  O   MET A 430     -14.978  39.298 -17.826  1.00 33.29           O  
ATOM   3415  CB  MET A 430     -15.729  40.898 -14.925  1.00 39.26           C  
ATOM   3416  CG  MET A 430     -14.216  41.124 -14.853  1.00 39.92           C  
ATOM   3417  SD  MET A 430     -13.461  40.900 -13.224  1.00 41.40           S  
ATOM   3418  CE  MET A 430     -14.649  41.723 -12.196  1.00 44.99           C  
ATOM   3419  N   ASP A 431     -16.332  38.303 -16.279  1.00 33.40           N  
ATOM   3420  CA  ASP A 431     -15.909  36.926 -16.571  1.00 31.28           C  
ATOM   3421  C   ASP A 431     -16.162  36.539 -18.049  1.00 31.27           C  
ATOM   3422  O   ASP A 431     -15.304  35.888 -18.694  1.00 29.20           O  
ATOM   3423  CB  ASP A 431     -16.618  35.935 -15.660  1.00 31.25           C  
ATOM   3424  CG  ASP A 431     -16.131  35.976 -14.211  1.00 31.37           C  
ATOM   3425  OD1 ASP A 431     -15.219  36.774 -13.799  1.00 30.93           O  
ATOM   3426  OD2 ASP A 431     -16.704  35.159 -13.475  1.00 31.96           O  
ATOM   3427  N   MET A 432     -17.292  36.997 -18.601  1.00 32.55           N  
ATOM   3428  CA  MET A 432     -17.630  36.679 -19.982  1.00 33.59           C  
ATOM   3429  C   MET A 432     -16.650  37.256 -21.013  1.00 34.18           C  
ATOM   3430  O   MET A 432     -16.524  36.711 -22.107  1.00 34.06           O  
ATOM   3431  CB  MET A 432     -19.067  37.093 -20.305  1.00 36.33           C  
ATOM   3432  CG  MET A 432     -20.119  36.255 -19.586  1.00 37.33           C  
ATOM   3433  SD  MET A 432     -19.962  34.440 -19.749  1.00 36.11           S  
ATOM   3434  CE  MET A 432     -18.988  33.983 -18.291  1.00 34.01           C  
ATOM   3435  N   CYS A 433     -15.942  38.329 -20.664  1.00 34.99           N  
ATOM   3436  CA  CYS A 433     -14.892  38.859 -21.530  1.00 35.78           C  
ATOM   3437  C   CYS A 433     -13.784  37.846 -21.812  1.00 32.43           C  
ATOM   3438  O   CYS A 433     -13.136  37.925 -22.844  1.00 32.82           O  
ATOM   3439  CB  CYS A 433     -14.267  40.117 -20.921  1.00 37.16           C  
ATOM   3440  SG  CYS A 433     -15.461  41.447 -20.768  1.00 42.09           S  
ATOM   3441  N   TYR A 434     -13.580  36.911 -20.900  1.00 29.97           N  
ATOM   3442  CA  TYR A 434     -12.538  35.893 -21.020  1.00 28.33           C  
ATOM   3443  C   TYR A 434     -13.022  34.626 -21.702  1.00 27.84           C  
ATOM   3444  O   TYR A 434     -12.196  33.842 -22.148  1.00 28.12           O  
ATOM   3445  CB  TYR A 434     -12.002  35.513 -19.629  1.00 26.24           C  
ATOM   3446  CG  TYR A 434     -11.326  36.645 -18.947  1.00 26.54           C  
ATOM   3447  CD1 TYR A 434     -12.039  37.522 -18.147  1.00 27.59           C  
ATOM   3448  CD2 TYR A 434      -9.935  36.836 -19.076  1.00 26.41           C  
ATOM   3449  CE1 TYR A 434     -11.402  38.580 -17.500  1.00 28.42           C  
ATOM   3450  CE2 TYR A 434      -9.301  37.912 -18.494  1.00 26.87           C  
ATOM   3451  CZ  TYR A 434     -10.022  38.773 -17.687  1.00 28.43           C  
ATOM   3452  OH  TYR A 434      -9.381  39.813 -17.067  1.00 29.30           O  
ATOM   3453  N   GLY A 435     -14.341  34.405 -21.761  1.00 27.25           N  
ATOM   3454  CA  GLY A 435     -14.911  33.158 -22.275  1.00 26.44           C  
ATOM   3455  C   GLY A 435     -15.988  32.676 -21.318  1.00 25.97           C  
ATOM   3456  O   GLY A 435     -16.205  33.280 -20.255  1.00 26.14           O  
ATOM   3457  N   MET A 436     -16.634  31.575 -21.656  1.00 25.47           N  
ATOM   3458  CA  MET A 436     -17.776  31.082 -20.877  1.00 25.85           C  
ATOM   3459  C   MET A 436     -17.376  30.565 -19.492  1.00 24.83           C  
ATOM   3460  O   MET A 436     -18.180  30.549 -18.577  1.00 24.80           O  
ATOM   3461  CB  MET A 436     -18.475  29.984 -21.640  1.00 26.76           C  
ATOM   3462  CG  MET A 436     -19.146  30.493 -22.924  1.00 28.58           C  
ATOM   3463  SD  MET A 436     -20.541  31.578 -22.533  1.00 30.42           S  
ATOM   3464  CE  MET A 436     -21.887  30.381 -22.607  1.00 31.83           C  
ATOM   3465  N   MET A 437     -16.120  30.150 -19.377  1.00 24.21           N  
ATOM   3466  CA  MET A 437     -15.590  29.692 -18.109  1.00 23.77           C  
ATOM   3467  C   MET A 437     -14.680  30.725 -17.500  1.00 22.97           C  
ATOM   3468  O   MET A 437     -13.967  30.419 -16.569  1.00 23.22           O  
ATOM   3469  CB  MET A 437     -14.910  28.350 -18.312  1.00 23.50           C  
ATOM   3470  CG  MET A 437     -15.911  27.244 -18.413  1.00 25.19           C  
ATOM   3471  SD  MET A 437     -16.562  26.924 -16.770  1.00 27.34           S  
ATOM   3472  CE  MET A 437     -17.754  25.724 -17.262  1.00 27.59           C  
ATOM   3473  N   GLY A 438     -14.726  31.959 -17.992  1.00 23.36           N  
ATOM   3474  CA  GLY A 438     -14.021  33.063 -17.347  1.00 23.17           C  
ATOM   3475  C   GLY A 438     -12.506  32.965 -17.373  1.00 22.22           C  
ATOM   3476  O   GLY A 438     -11.921  32.125 -18.080  1.00 22.23           O  
ATOM   3477  N   SER A 439     -11.890  33.878 -16.625  1.00 21.26           N  
ATOM   3478  CA  SER A 439     -10.465  34.008 -16.562  1.00 20.79           C  
ATOM   3479  C   SER A 439      -9.824  32.770 -15.950  1.00 19.28           C  
ATOM   3480  O   SER A 439     -10.360  32.142 -15.021  1.00 19.58           O  
ATOM   3481  CB  SER A 439     -10.052  35.242 -15.733  1.00 21.17           C  
ATOM   3482  OG  SER A 439      -8.635  35.288 -15.605  1.00 20.38           O  
ATOM   3483  N   LEU A 440      -8.651  32.445 -16.456  1.00 18.67           N  
ATOM   3484  CA  LEU A 440      -7.822  31.416 -15.852  1.00 18.33           C  
ATOM   3485  C   LEU A 440      -7.553  31.685 -14.354  1.00 18.01           C  
ATOM   3486  O   LEU A 440      -7.437  30.759 -13.559  1.00 18.42           O  
ATOM   3487  CB  LEU A 440      -6.509  31.376 -16.633  1.00 18.61           C  
ATOM   3488  CG  LEU A 440      -5.390  30.423 -16.208  1.00 18.15           C  
ATOM   3489  CD1 LEU A 440      -5.867  28.999 -16.188  1.00 18.35           C  
ATOM   3490  CD2 LEU A 440      -4.255  30.571 -17.171  1.00 18.99           C  
ATOM   3491  N   PHE A 441      -7.506  32.964 -13.975  1.00 18.75           N  
ATOM   3492  CA  PHE A 441      -6.991  33.404 -12.677  1.00 19.15           C  
ATOM   3493  C   PHE A 441      -8.012  33.791 -11.662  1.00 19.54           C  
ATOM   3494  O   PHE A 441      -7.680  33.923 -10.495  1.00 19.24           O  
ATOM   3495  CB  PHE A 441      -6.040  34.588 -12.878  1.00 19.79           C  
ATOM   3496  CG  PHE A 441      -4.885  34.284 -13.804  1.00 20.00           C  
ATOM   3497  CD1 PHE A 441      -3.867  33.435 -13.402  1.00 20.11           C  
ATOM   3498  CD2 PHE A 441      -4.843  34.835 -15.080  1.00 20.75           C  
ATOM   3499  CE1 PHE A 441      -2.796  33.163 -14.253  1.00 20.45           C  
ATOM   3500  CE2 PHE A 441      -3.778  34.580 -15.932  1.00 21.41           C  
ATOM   3501  CZ  PHE A 441      -2.758  33.726 -15.520  1.00 21.11           C  
ATOM   3502  N   ARG A 442      -9.264  33.985 -12.072  1.00 20.14           N  
ATOM   3503  CA  ARG A 442     -10.274  34.422 -11.125  1.00 21.08           C  
ATOM   3504  C   ARG A 442     -11.684  34.304 -11.701  1.00 22.12           C  
ATOM   3505  O   ARG A 442     -11.852  34.177 -12.891  1.00 21.77           O  
ATOM   3506  CB  ARG A 442     -10.028  35.870 -10.678  1.00 22.05           C  
ATOM   3507  CG  ARG A 442      -9.776  36.872 -11.792  1.00 22.46           C  
ATOM   3508  CD  ARG A 442      -9.599  38.321 -11.337  1.00 23.86           C  
ATOM   3509  NE  ARG A 442      -8.498  38.497 -10.367  1.00 23.29           N  
ATOM   3510  CZ  ARG A 442      -8.632  38.645  -9.052  1.00 24.06           C  
ATOM   3511  NH1 ARG A 442      -7.534  38.818  -8.305  1.00 24.15           N  
ATOM   3512  NH2 ARG A 442      -9.840  38.656  -8.456  1.00 25.33           N  
ATOM   3513  N   SER A 443     -12.661  34.343 -10.814  1.00 23.29           N  
ATOM   3514  CA  SER A 443     -14.037  34.671 -11.180  1.00 25.01           C  
ATOM   3515  C   SER A 443     -14.396  35.876 -10.321  1.00 26.29           C  
ATOM   3516  O   SER A 443     -14.431  35.775  -9.104  1.00 26.41           O  
ATOM   3517  CB  SER A 443     -14.949  33.474 -10.931  1.00 25.82           C  
ATOM   3518  OG  SER A 443     -16.294  33.918 -10.863  1.00 28.92           O  
ATOM   3519  N   GLY A 444     -14.589  37.031 -10.957  1.00 27.44           N  
ATOM   3520  CA  GLY A 444     -14.774  38.302 -10.242  1.00 29.53           C  
ATOM   3521  C   GLY A 444     -13.631  38.532  -9.263  1.00 29.37           C  
ATOM   3522  O   GLY A 444     -12.466  38.410  -9.622  1.00 28.63           O  
ATOM   3523  N   SER A 445     -13.950  38.778  -8.004  1.00 30.68           N  
ATOM   3524  CA  SER A 445     -12.926  39.046  -7.007  1.00 31.35           C  
ATOM   3525  C   SER A 445     -12.345  37.787  -6.359  1.00 30.25           C  
ATOM   3526  O   SER A 445     -11.545  37.905  -5.455  1.00 30.47           O  
ATOM   3527  CB  SER A 445     -13.484  39.968  -5.922  1.00 34.21           C  
ATOM   3528  OG  SER A 445     -14.561  39.325  -5.278  1.00 35.13           O  
ATOM   3529  N   ARG A 446     -12.737  36.596  -6.807  1.00 29.26           N  
ATOM   3530  CA  ARG A 446     -12.279  35.353  -6.184  1.00 28.90           C  
ATOM   3531  C   ARG A 446     -11.234  34.697  -7.064  1.00 25.48           C  
ATOM   3532  O   ARG A 446     -11.505  34.372  -8.226  1.00 24.65           O  
ATOM   3533  CB  ARG A 446     -13.463  34.417  -5.976  1.00 31.47           C  
ATOM   3534  CG  ARG A 446     -14.553  35.095  -5.159  1.00 36.34           C  
ATOM   3535  CD  ARG A 446     -15.673  34.148  -4.781  1.00 40.58           C  
ATOM   3536  NE  ARG A 446     -15.174  33.179  -3.799  1.00 44.61           N  
ATOM   3537  CZ  ARG A 446     -15.888  32.196  -3.222  1.00 47.52           C  
ATOM   3538  NH1 ARG A 446     -17.167  31.968  -3.540  1.00 49.25           N  
ATOM   3539  NH2 ARG A 446     -15.278  31.395  -2.350  1.00 48.07           N  
ATOM   3540  N   GLN A 447     -10.048  34.489  -6.515  1.00 23.41           N  
ATOM   3541  CA  GLN A 447      -8.991  33.825  -7.231  1.00 21.47           C  
ATOM   3542  C   GLN A 447      -9.214  32.328  -7.396  1.00 19.92           C  
ATOM   3543  O   GLN A 447      -9.693  31.658  -6.493  1.00 20.39           O  
ATOM   3544  CB  GLN A 447      -7.667  34.037  -6.539  1.00 21.93           C  
ATOM   3545  CG  GLN A 447      -7.249  35.493  -6.493  1.00 23.68           C  
ATOM   3546  CD  GLN A 447      -5.818  35.606  -6.007  1.00 24.41           C  
ATOM   3547  OE1 GLN A 447      -5.546  35.338  -4.846  1.00 26.49           O  
ATOM   3548  NE2 GLN A 447      -4.909  35.976  -6.881  1.00 24.36           N  
ATOM   3549  N   THR A 448      -8.807  31.807  -8.542  1.00 18.26           N  
ATOM   3550  CA  THR A 448      -8.878  30.360  -8.795  1.00 17.90           C  
ATOM   3551  C   THR A 448      -7.745  29.588  -8.084  1.00 18.15           C  
ATOM   3552  O   THR A 448      -6.713  30.155  -7.681  1.00 18.23           O  
ATOM   3553  CB  THR A 448      -8.756  30.037 -10.266  1.00 17.15           C  
ATOM   3554  OG1 THR A 448      -7.539  30.582 -10.796  1.00 16.21           O  
ATOM   3555  CG2 THR A 448      -9.964  30.546 -11.081  1.00 17.28           C  
ATOM   3556  N   LEU A 449      -7.952  28.293  -7.966  1.00 18.44           N  
ATOM   3557  CA  LEU A 449      -6.929  27.368  -7.526  1.00 18.50           C  
ATOM   3558  C   LEU A 449      -5.671  27.575  -8.348  1.00 17.70           C  
ATOM   3559  O   LEU A 449      -4.558  27.685  -7.786  1.00 16.85           O  
ATOM   3560  CB  LEU A 449      -7.454  25.939  -7.652  1.00 19.11           C  
ATOM   3561  CG  LEU A 449      -6.450  24.782  -7.526  1.00 19.51           C  
ATOM   3562  CD1 LEU A 449      -5.815  24.742  -6.104  1.00 20.73           C  
ATOM   3563  CD2 LEU A 449      -7.135  23.484  -7.841  1.00 20.21           C  
ATOM   3564  N   PHE A 450      -5.844  27.675  -9.675  1.00 17.16           N  
ATOM   3565  CA  PHE A 450      -4.699  27.864 -10.573  1.00 17.19           C  
ATOM   3566  C   PHE A 450      -3.874  29.120 -10.217  1.00 17.48           C  
ATOM   3567  O   PHE A 450      -2.654  29.053 -10.110  1.00 16.70           O  
ATOM   3568  CB  PHE A 450      -5.151  27.894 -12.033  1.00 17.79           C  
ATOM   3569  CG  PHE A 450      -4.009  27.840 -13.029  1.00 17.96           C  
ATOM   3570  CD1 PHE A 450      -3.372  28.996 -13.429  1.00 18.09           C  
ATOM   3571  CD2 PHE A 450      -3.664  26.648 -13.610  1.00 19.25           C  
ATOM   3572  CE1 PHE A 450      -2.321  28.961 -14.345  1.00 18.50           C  
ATOM   3573  CE2 PHE A 450      -2.620  26.599 -14.537  1.00 20.30           C  
ATOM   3574  CZ  PHE A 450      -1.939  27.763 -14.874  1.00 19.27           C  
ATOM   3575  N   ALA A 451      -4.539  30.260 -10.032  1.00 17.33           N  
ATOM   3576  CA  ALA A 451      -3.871  31.465  -9.609  1.00 17.83           C  
ATOM   3577  C   ALA A 451      -3.091  31.293  -8.308  1.00 18.64           C  
ATOM   3578  O   ALA A 451      -1.944  31.740  -8.224  1.00 18.57           O  
ATOM   3579  CB  ALA A 451      -4.866  32.603  -9.443  1.00 18.49           C  
ATOM   3580  N   SER A 452      -3.691  30.628  -7.321  1.00 19.92           N  
ATOM   3581  CA ASER A 452      -3.030  30.406  -6.041  0.50 20.97           C  
ATOM   3582  CA BSER A 452      -3.024  30.413  -6.045  0.50 20.94           C  
ATOM   3583  C   SER A 452      -1.784  29.536  -6.201  1.00 21.03           C  
ATOM   3584  O   SER A 452      -0.751  29.809  -5.564  1.00 20.39           O  
ATOM   3585  CB ASER A 452      -3.977  29.791  -5.003  0.50 22.68           C  
ATOM   3586  CB BSER A 452      -3.974  29.803  -5.018  0.50 22.53           C  
ATOM   3587  OG ASER A 452      -4.384  28.481  -5.367  0.50 23.33           O  
ATOM   3588  OG BSER A 452      -5.092  30.646  -4.819  0.50 23.29           O  
ATOM   3589  N  AGLN A 453      -1.875  28.507  -7.042  0.50 20.15           N  
ATOM   3590  N  BGLN A 453      -1.891  28.502  -7.040  0.50 20.91           N  
ATOM   3591  CA AGLN A 453      -0.715  27.650  -7.323  0.50 20.69           C  
ATOM   3592  CA BGLN A 453      -0.750  27.619  -7.342  0.50 21.99           C  
ATOM   3593  C  AGLN A 453       0.418  28.386  -8.037  0.50 19.97           C  
ATOM   3594  C  BGLN A 453       0.401  28.350  -8.061  0.50 20.68           C  
ATOM   3595  O  AGLN A 453       1.590  28.204  -7.694  0.50 20.56           O  
ATOM   3596  O  BGLN A 453       1.570  28.128  -7.741  0.50 21.26           O  
ATOM   3597  CB AGLN A 453      -1.116  26.443  -8.140  0.50 20.64           C  
ATOM   3598  CB BGLN A 453      -1.188  26.398  -8.151  0.50 22.94           C  
ATOM   3599  CG AGLN A 453      -1.999  25.483  -7.382  0.50 21.74           C  
ATOM   3600  CG BGLN A 453      -2.089  25.436  -7.386  0.50 25.05           C  
ATOM   3601  CD AGLN A 453      -2.520  24.409  -8.296  0.50 22.09           C  
ATOM   3602  CD BGLN A 453      -1.456  24.922  -6.119  0.50 27.77           C  
ATOM   3603  OE1AGLN A 453      -2.779  24.644  -9.485  0.50 21.23           O  
ATOM   3604  OE1BGLN A 453      -0.990  25.696  -5.278  0.50 30.56           O  
ATOM   3605  NE2AGLN A 453      -2.636  23.227  -7.774  0.50 23.61           N  
ATOM   3606  NE2BGLN A 453      -1.448  23.615  -5.957  0.50 29.82           N  
ATOM   3607  N   VAL A 454       0.063  29.236  -8.988  1.00 19.07           N  
ATOM   3608  CA  VAL A 454       1.070  30.062  -9.680  1.00 18.85           C  
ATOM   3609  C   VAL A 454       1.796  30.918  -8.639  1.00 19.26           C  
ATOM   3610  O   VAL A 454       3.038  30.934  -8.575  1.00 18.72           O  
ATOM   3611  CB  VAL A 454       0.432  30.991 -10.735  1.00 17.90           C  
ATOM   3612  CG1 VAL A 454       1.427  31.995 -11.271  1.00 18.26           C  
ATOM   3613  CG2 VAL A 454      -0.128  30.190 -11.901  1.00 17.39           C  
ATOM   3614  N   MET A 455       1.025  31.609  -7.811  1.00 19.74           N  
ATOM   3615  CA  MET A 455       1.623  32.499  -6.812  1.00 21.56           C  
ATOM   3616  C   MET A 455       2.565  31.755  -5.862  1.00 22.01           C  
ATOM   3617  O   MET A 455       3.641  32.262  -5.536  1.00 21.40           O  
ATOM   3618  CB  MET A 455       0.544  33.259  -6.015  1.00 23.04           C  
ATOM   3619  CG  MET A 455      -0.216  34.299  -6.823  1.00 23.79           C  
ATOM   3620  SD  MET A 455      -1.489  35.115  -5.843  1.00 27.45           S  
ATOM   3621  CE  MET A 455      -0.500  36.223  -4.928  1.00 29.62           C  
ATOM   3622  N   ARG A 456       2.145  30.557  -5.455  1.00 22.98           N  
ATOM   3623  CA  ARG A 456       2.840  29.792  -4.442  1.00 24.89           C  
ATOM   3624  C   ARG A 456       4.090  29.091  -4.955  1.00 23.52           C  
ATOM   3625  O   ARG A 456       5.049  28.942  -4.197  1.00 23.71           O  
ATOM   3626  CB  ARG A 456       1.900  28.743  -3.828  1.00 28.61           C  
ATOM   3627  CG  ARG A 456       2.443  27.915  -2.675  1.00 33.14           C  
ATOM   3628  CD  ARG A 456       1.330  27.126  -1.952  1.00 38.11           C  
ATOM   3629  NE  ARG A 456       0.391  28.101  -1.383  1.00 41.86           N  
ATOM   3630  CZ  ARG A 456      -0.921  28.250  -1.648  1.00 52.67           C  
ATOM   3631  NH1 ARG A 456      -1.586  27.444  -2.487  1.00 54.46           N  
ATOM   3632  NH2 ARG A 456      -1.592  29.231  -1.008  1.00 52.75           N  
ATOM   3633  N   TYR A 457       4.065  28.625  -6.208  1.00 21.73           N  
ATOM   3634  CA  TYR A 457       5.132  27.778  -6.712  1.00 21.17           C  
ATOM   3635  C   TYR A 457       5.963  28.347  -7.884  1.00 19.51           C  
ATOM   3636  O   TYR A 457       7.061  27.854  -8.086  1.00 19.48           O  
ATOM   3637  CB  TYR A 457       4.617  26.376  -7.044  1.00 22.15           C  
ATOM   3638  CG  TYR A 457       4.041  25.670  -5.849  1.00 24.22           C  
ATOM   3639  CD1 TYR A 457       4.863  25.212  -4.831  1.00 25.58           C  
ATOM   3640  CD2 TYR A 457       2.656  25.463  -5.726  1.00 25.28           C  
ATOM   3641  CE1 TYR A 457       4.345  24.605  -3.686  1.00 28.24           C  
ATOM   3642  CE2 TYR A 457       2.130  24.815  -4.606  1.00 27.87           C  
ATOM   3643  CZ  TYR A 457       2.978  24.401  -3.589  1.00 29.23           C  
ATOM   3644  OH  TYR A 457       2.489  23.757  -2.505  1.00 32.89           O  
ATOM   3645  N   ALA A 458       5.488  29.369  -8.593  1.00 18.26           N  
ATOM   3646  CA  ALA A 458       6.251  29.981  -9.666  1.00 18.05           C  
ATOM   3647  C   ALA A 458       6.953  31.194  -9.133  1.00 18.09           C  
ATOM   3648  O   ALA A 458       6.316  32.171  -8.771  1.00 18.57           O  
ATOM   3649  CB  ALA A 458       5.355  30.357 -10.832  1.00 17.92           C  
ATOM   3650  N   ASP A 459       8.275  31.169  -9.086  1.00 18.64           N  
ATOM   3651  CA  ASP A 459       9.004  32.336  -8.586  1.00 19.03           C  
ATOM   3652  C   ASP A 459       8.835  33.475  -9.519  1.00 19.14           C  
ATOM   3653  O   ASP A 459       8.611  34.614  -9.076  1.00 19.88           O  
ATOM   3654  CB  ASP A 459      10.462  32.034  -8.391  1.00 19.89           C  
ATOM   3655  CG  ASP A 459      10.705  30.950  -7.362  1.00 21.11           C  
ATOM   3656  OD1 ASP A 459       9.859  30.785  -6.441  1.00 22.66           O  
ATOM   3657  OD2 ASP A 459      11.709  30.217  -7.465  1.00 21.10           O  
ATOM   3658  N   LEU A 460       8.906  33.162 -10.815  1.00 18.94           N  
ATOM   3659  CA  LEU A 460       8.677  34.104 -11.887  1.00 19.12           C  
ATOM   3660  C   LEU A 460       7.677  33.479 -12.830  1.00 18.55           C  
ATOM   3661  O   LEU A 460       7.528  32.246 -12.895  1.00 18.28           O  
ATOM   3662  CB  LEU A 460       9.976  34.378 -12.672  1.00 20.15           C  
ATOM   3663  CG  LEU A 460      11.252  34.714 -11.872  1.00 21.31           C  
ATOM   3664  CD1 LEU A 460      12.491  34.717 -12.792  1.00 22.15           C  
ATOM   3665  CD2 LEU A 460      11.098  36.062 -11.215  1.00 22.11           C  
ATOM   3666  N   TYR A 461       6.971  34.342 -13.559  1.00 18.86           N  
ATOM   3667  CA  TYR A 461       6.062  33.879 -14.593  1.00 18.00           C  
ATOM   3668  C   TYR A 461       5.870  34.902 -15.682  1.00 18.88           C  
ATOM   3669  O   TYR A 461       6.079  36.120 -15.471  1.00 19.20           O  
ATOM   3670  CB  TYR A 461       4.706  33.442 -14.020  1.00 17.79           C  
ATOM   3671  CG  TYR A 461       3.761  34.515 -13.516  1.00 18.03           C  
ATOM   3672  CD1 TYR A 461       3.812  34.954 -12.201  1.00 18.08           C  
ATOM   3673  CD2 TYR A 461       2.771  35.031 -14.321  1.00 18.78           C  
ATOM   3674  CE1 TYR A 461       2.920  35.909 -11.716  1.00 18.76           C  
ATOM   3675  CE2 TYR A 461       1.879  35.990 -13.868  1.00 19.61           C  
ATOM   3676  CZ  TYR A 461       1.954  36.427 -12.555  1.00 19.65           C  
ATOM   3677  OH  TYR A 461       1.049  37.336 -12.099  1.00 20.38           O  
ATOM   3678  N   ALA A 462       5.445  34.397 -16.845  1.00 19.51           N  
ATOM   3679  CA  ALA A 462       5.173  35.252 -18.008  1.00 20.79           C  
ATOM   3680  C   ALA A 462       4.439  34.498 -19.056  1.00 20.84           C  
ATOM   3681  O   ALA A 462       4.338  33.286 -18.980  1.00 20.17           O  
ATOM   3682  CB  ALA A 462       6.498  35.784 -18.580  1.00 21.67           C  
ATOM   3683  N   ALA A 463       3.954  35.220 -20.067  1.00 22.45           N  
ATOM   3684  CA  ALA A 463       3.350  34.595 -21.225  1.00 23.35           C  
ATOM   3685  C   ALA A 463       4.339  33.786 -22.021  1.00 22.92           C  
ATOM   3686  O   ALA A 463       3.960  32.843 -22.709  1.00 24.04           O  
ATOM   3687  CB  ALA A 463       2.679  35.620 -22.113  1.00 25.57           C  
ATOM   3688  N   SER A 464       5.608  34.165 -21.939  1.00 22.15           N  
ATOM   3689  CA  SER A 464       6.678  33.510 -22.671  1.00 21.99           C  
ATOM   3690  C   SER A 464       7.983  33.690 -21.915  1.00 20.94           C  
ATOM   3691  O   SER A 464       8.237  34.743 -21.380  1.00 20.78           O  
ATOM   3692  CB  SER A 464       6.830  34.114 -24.057  1.00 23.57           C  
ATOM   3693  OG  SER A 464       7.927  33.501 -24.732  1.00 23.77           O  
ATOM   3694  N   PHE A 465       8.813  32.672 -21.897  1.00 20.56           N  
ATOM   3695  CA  PHE A 465      10.124  32.838 -21.303  1.00 21.16           C  
ATOM   3696  C   PHE A 465      11.020  33.755 -22.147  1.00 22.09           C  
ATOM   3697  O   PHE A 465      12.054  34.218 -21.658  1.00 21.84           O  
ATOM   3698  CB  PHE A 465      10.809  31.494 -21.086  1.00 21.43           C  
ATOM   3699  CG  PHE A 465      11.411  30.934 -22.296  1.00 23.07           C  
ATOM   3700  CD1 PHE A 465      12.665  31.343 -22.714  1.00 24.34           C  
ATOM   3701  CD2 PHE A 465      10.752  29.985 -23.012  1.00 24.53           C  
ATOM   3702  CE1 PHE A 465      13.225  30.839 -23.860  1.00 26.09           C  
ATOM   3703  CE2 PHE A 465      11.313  29.465 -24.156  1.00 26.92           C  
ATOM   3704  CZ  PHE A 465      12.556  29.901 -24.576  1.00 27.20           C  
ATOM   3705  N   ILE A 466      10.641  34.010 -23.398  1.00 23.12           N  
ATOM   3706  CA  ILE A 466      11.415  34.958 -24.214  1.00 25.36           C  
ATOM   3707  C   ILE A 466      11.568  36.331 -23.540  1.00 25.43           C  
ATOM   3708  O   ILE A 466      12.520  37.048 -23.819  1.00 26.22           O  
ATOM   3709  CB  ILE A 466      10.844  35.093 -25.652  1.00 27.31           C  
ATOM   3710  CG1 ILE A 466      11.904  35.614 -26.604  1.00 29.56           C  
ATOM   3711  CG2 ILE A 466       9.628  36.006 -25.688  1.00 28.56           C  
ATOM   3712  CD1 ILE A 466      12.948  34.539 -26.931  1.00 30.20           C  
ATOM   3713  N   ASN A 467      10.632  36.682 -22.643  1.00 24.41           N  
ATOM   3714  CA  ASN A 467      10.659  37.953 -21.940  1.00 25.40           C  
ATOM   3715  C   ASN A 467      11.912  38.171 -21.105  1.00 25.57           C  
ATOM   3716  O   ASN A 467      12.275  39.328 -20.866  1.00 26.81           O  
ATOM   3717  CB  ASN A 467       9.396  38.100 -21.073  1.00 25.20           C  
ATOM   3718  CG  ASN A 467       8.146  38.314 -21.909  1.00 26.34           C  
ATOM   3719  OD1 ASN A 467       8.232  38.392 -23.116  1.00 28.08           O  
ATOM   3720  ND2 ASN A 467       6.998  38.520 -21.252  1.00 26.25           N  
ATOM   3721  N   LEU A 468      12.590  37.079 -20.718  1.00 24.28           N  
ATOM   3722  CA  LEU A 468      13.909  37.141 -20.070  1.00 25.08           C  
ATOM   3723  C   LEU A 468      14.956  37.855 -20.897  1.00 27.24           C  
ATOM   3724  O   LEU A 468      15.890  38.407 -20.332  1.00 28.87           O  
ATOM   3725  CB  LEU A 468      14.463  35.756 -19.667  1.00 23.97           C  
ATOM   3726  CG  LEU A 468      13.677  35.026 -18.583  1.00 22.24           C  
ATOM   3727  CD1 LEU A 468      14.049  33.560 -18.551  1.00 21.74           C  
ATOM   3728  CD2 LEU A 468      13.857  35.631 -17.212  1.00 22.88           C  
ATOM   3729  N   LEU A 469      14.791  37.867 -22.212  1.00 28.17           N  
ATOM   3730  CA  LEU A 469      15.725  38.542 -23.132  1.00 30.94           C  
ATOM   3731  C   LEU A 469      15.819  40.041 -22.898  1.00 33.11           C  
ATOM   3732  O   LEU A 469      16.824  40.674 -23.247  1.00 35.58           O  
ATOM   3733  CB  LEU A 469      15.286  38.289 -24.578  1.00 31.62           C  
ATOM   3734  CG  LEU A 469      16.147  38.805 -25.729  1.00 34.37           C  
ATOM   3735  CD1 LEU A 469      17.551  38.236 -25.707  1.00 35.40           C  
ATOM   3736  CD2 LEU A 469      15.479  38.523 -27.064  1.00 35.38           C  
ATOM   3737  N   TYR A 470      14.762  40.603 -22.317  1.00 33.28           N  
ATOM   3738  CA  TYR A 470      14.674  42.021 -22.094  1.00 35.94           C  
ATOM   3739  C   TYR A 470      15.202  42.441 -20.743  1.00 36.44           C  
ATOM   3740  O   TYR A 470      15.119  43.613 -20.431  1.00 38.78           O  
ATOM   3741  CB  TYR A 470      13.243  42.513 -22.321  1.00 35.90           C  
ATOM   3742  CG  TYR A 470      12.672  41.916 -23.580  1.00 35.80           C  
ATOM   3743  CD1 TYR A 470      13.399  41.955 -24.768  1.00 37.86           C  
ATOM   3744  CD2 TYR A 470      11.429  41.287 -23.587  1.00 34.07           C  
ATOM   3745  CE1 TYR A 470      12.922  41.377 -25.921  1.00 38.08           C  
ATOM   3746  CE2 TYR A 470      10.940  40.724 -24.749  1.00 34.63           C  
ATOM   3747  CZ  TYR A 470      11.706  40.767 -25.912  1.00 36.28           C  
ATOM   3748  OH  TYR A 470      11.264  40.215 -27.088  1.00 37.11           O  
ATOM   3749  N   TYR A 471      15.782  41.536 -19.972  1.00 35.07           N  
ATOM   3750  CA  TYR A 471      16.357  41.912 -18.683  1.00 36.50           C  
ATOM   3751  C   TYR A 471      17.843  41.667 -18.718  1.00 39.40           C  
ATOM   3752  O   TYR A 471      18.281  40.679 -19.280  1.00 39.54           O  
ATOM   3753  CB  TYR A 471      15.719  41.149 -17.535  1.00 33.30           C  
ATOM   3754  CG  TYR A 471      14.271  41.503 -17.357  1.00 32.12           C  
ATOM   3755  CD1 TYR A 471      13.290  40.919 -18.153  1.00 30.46           C  
ATOM   3756  CD2 TYR A 471      13.870  42.433 -16.384  1.00 32.69           C  
ATOM   3757  CE1 TYR A 471      11.958  41.257 -18.002  1.00 29.66           C  
ATOM   3758  CE2 TYR A 471      12.536  42.778 -16.223  1.00 31.83           C  
ATOM   3759  CZ  TYR A 471      11.588  42.186 -17.024  1.00 30.67           C  
ATOM   3760  OH  TYR A 471      10.274  42.514 -16.855  1.00 29.78           O  
ATOM   3761  N   PRO A 472      18.620  42.563 -18.095  1.00 43.09           N  
ATOM   3762  CA  PRO A 472      20.051  42.376 -18.126  1.00 45.94           C  
ATOM   3763  C   PRO A 472      20.498  41.123 -17.407  1.00 45.65           C  
ATOM   3764  O   PRO A 472      19.797  40.562 -16.565  1.00 42.35           O  
ATOM   3765  CB  PRO A 472      20.611  43.621 -17.444  1.00 48.79           C  
ATOM   3766  CG  PRO A 472      19.502  44.176 -16.642  1.00 47.41           C  
ATOM   3767  CD  PRO A 472      18.213  43.691 -17.237  1.00 44.40           C  
ATOM   3768  N   PHE A 473      21.707  40.748 -17.788  1.00 49.50           N  
ATOM   3769  CA APHE A 473      22.320  39.488 -17.357  0.25 49.03           C  
ATOM   3770  CA BPHE A 473      22.324  39.490 -17.356  0.25 49.05           C  
ATOM   3771  CA CPHE A 473      22.350  39.512 -17.357  0.50 49.83           C  
ATOM   3772  C   PHE A 473      22.082  39.136 -15.878  1.00 48.02           C  
ATOM   3773  O   PHE A 473      21.686  38.004 -15.572  1.00 48.07           O  
ATOM   3774  CB APHE A 473      23.824  39.486 -17.684  0.25 52.41           C  
ATOM   3775  CB BPHE A 473      23.831  39.498 -17.672  0.25 52.43           C  
ATOM   3776  CB CPHE A 473      23.869  39.531 -17.748  0.50 53.69           C  
ATOM   3777  CG APHE A 473      24.143  39.043 -19.092  0.25 52.89           C  
ATOM   3778  CG BPHE A 473      24.165  39.063 -19.079  0.25 52.97           C  
ATOM   3779  CG CPHE A 473      24.719  40.594 -17.052  0.50 57.50           C  
ATOM   3780  CD1APHE A 473      23.459  37.985 -19.674  0.25 50.38           C  
ATOM   3781  CD1BPHE A 473      23.478  38.017 -19.679  0.25 50.46           C  
ATOM   3782  CD1CPHE A 473      24.591  41.958 -17.340  0.50 59.37           C  
ATOM   3783  CD2APHE A 473      25.158  39.656 -19.817  0.25 56.41           C  
ATOM   3784  CD2BPHE A 473      25.197  39.670 -19.783  0.25 56.53           C  
ATOM   3785  CD2CPHE A 473      25.716  40.211 -16.160  0.50 59.66           C  
ATOM   3786  CE1APHE A 473      23.761  37.568 -20.959  0.25 51.15           C  
ATOM   3787  CE1BPHE A 473      23.795  37.608 -20.964  0.25 51.28           C  
ATOM   3788  CE1CPHE A 473      25.378  42.899 -16.701  0.50 62.58           C  
ATOM   3789  CE2APHE A 473      25.464  39.240 -21.101  0.25 57.04           C  
ATOM   3790  CE2BPHE A 473      25.517  39.262 -21.066  0.25 57.20           C  
ATOM   3791  CE2CPHE A 473      26.508  41.155 -15.519  0.50 62.81           C  
ATOM   3792  CZ APHE A 473      24.764  38.195 -21.671  0.25 54.42           C  
ATOM   3793  CZ BPHE A 473      24.816  38.230 -21.656  0.25 54.59           C  
ATOM   3794  CZ CPHE A 473      26.340  42.498 -15.795  0.50 64.51           C  
ATOM   3795  N   SER A 474      22.300  40.091 -14.974  1.00 47.39           N  
ATOM   3796  CA  SER A 474      22.225  39.856 -13.538  1.00 45.87           C  
ATOM   3797  C   SER A 474      21.154  40.718 -12.841  1.00 43.04           C  
ATOM   3798  O   SER A 474      21.341  41.172 -11.712  1.00 42.42           O  
ATOM   3799  CB  SER A 474      23.577  40.180 -12.913  1.00 50.29           C  
ATOM   3800  OG  SER A 474      24.611  39.465 -13.556  1.00 53.04           O  
ATOM   3801  N   TYR A 475      20.022  40.891 -13.519  1.00 39.86           N  
ATOM   3802  CA  TYR A 475      18.887  41.608 -12.963  1.00 38.40           C  
ATOM   3803  C   TYR A 475      18.448  40.997 -11.629  1.00 36.66           C  
ATOM   3804  O   TYR A 475      18.508  39.780 -11.431  1.00 34.63           O  
ATOM   3805  CB  TYR A 475      17.734  41.559 -13.946  1.00 36.28           C  
ATOM   3806  CG  TYR A 475      16.623  42.514 -13.623  1.00 36.47           C  
ATOM   3807  CD1 TYR A 475      16.796  43.894 -13.781  1.00 39.44           C  
ATOM   3808  CD2 TYR A 475      15.386  42.053 -13.173  1.00 34.43           C  
ATOM   3809  CE1 TYR A 475      15.770  44.785 -13.504  1.00 39.69           C  
ATOM   3810  CE2 TYR A 475      14.360  42.944 -12.883  1.00 34.83           C  
ATOM   3811  CZ  TYR A 475      14.567  44.293 -13.056  1.00 37.47           C  
ATOM   3812  OH  TYR A 475      13.564  45.148 -12.779  1.00 39.25           O  
ATOM   3813  N   LEU A 476      18.020  41.844 -10.707  1.00 37.72           N  
ATOM   3814  CA  LEU A 476      17.444  41.357  -9.453  1.00 36.85           C  
ATOM   3815  C   LEU A 476      15.942  41.508  -9.558  1.00 34.85           C  
ATOM   3816  O   LEU A 476      15.424  42.617  -9.468  1.00 36.90           O  
ATOM   3817  CB  LEU A 476      18.000  42.102  -8.239  1.00 39.03           C  
ATOM   3818  CG  LEU A 476      17.405  41.714  -6.868  1.00 38.90           C  
ATOM   3819  CD1 LEU A 476      17.219  40.215  -6.637  1.00 36.74           C  
ATOM   3820  CD2 LEU A 476      18.247  42.303  -5.745  1.00 42.33           C  
ATOM   3821  N   PHE A 477      15.241  40.410  -9.807  1.00 31.89           N  
ATOM   3822  CA  PHE A 477      13.768  40.443  -9.800  1.00 30.31           C  
ATOM   3823  C   PHE A 477      13.298  40.599  -8.345  1.00 30.34           C  
ATOM   3824  O   PHE A 477      13.724  39.840  -7.499  1.00 29.45           O  
ATOM   3825  CB  PHE A 477      13.169  39.187 -10.431  1.00 27.90           C  
ATOM   3826  CG  PHE A 477      13.396  39.072 -11.913  1.00 27.58           C  
ATOM   3827  CD1 PHE A 477      12.575  39.737 -12.801  1.00 27.43           C  
ATOM   3828  CD2 PHE A 477      14.432  38.284 -12.430  1.00 28.31           C  
ATOM   3829  CE1 PHE A 477      12.758  39.625 -14.163  1.00 27.32           C  
ATOM   3830  CE2 PHE A 477      14.614  38.171 -13.810  1.00 27.84           C  
ATOM   3831  CZ  PHE A 477      13.770  38.830 -14.669  1.00 27.31           C  
ATOM   3832  N   ARG A 478      12.435  41.578  -8.081  1.00 37.56           N  
ATOM   3833  CA  ARG A 478      12.031  41.952  -6.726  1.00 38.87           C  
ATOM   3834  C   ARG A 478      10.547  41.725  -6.460  1.00 36.55           C  
ATOM   3835  O   ARG A 478       9.714  42.121  -7.264  1.00 35.90           O  
ATOM   3836  CB  ARG A 478      12.265  43.451  -6.533  1.00 42.89           C  
ATOM   3837  CG  ARG A 478      13.720  43.882  -6.533  1.00 47.43           C  
ATOM   3838  CD  ARG A 478      14.375  43.501  -5.212  1.00 52.75           C  
ATOM   3839  NE  ARG A 478      13.731  44.119  -4.033  1.00 57.09           N  
ATOM   3840  CZ  ARG A 478      13.953  43.765  -2.759  1.00 61.36           C  
ATOM   3841  NH1 ARG A 478      13.306  44.400  -1.782  1.00 63.17           N  
ATOM   3842  NH2 ARG A 478      14.810  42.781  -2.442  1.00 62.63           N  
ATOM   3843  N   ALA A 479      10.225  41.122  -5.318  1.00 34.92           N  
ATOM   3844  CA  ALA A 479       8.862  41.118  -4.806  1.00 34.48           C  
ATOM   3845  C   ALA A 479       8.923  41.633  -3.376  1.00 33.85           C  
ATOM   3846  O   ALA A 479       9.881  41.356  -2.668  1.00 32.67           O  
ATOM   3847  CB  ALA A 479       8.273  39.717  -4.845  1.00 34.07           C  
ATOM   3848  N   ALA A 480       7.899  42.364  -2.961  1.00 34.77           N  
ATOM   3849  CA  ALA A 480       7.827  42.869  -1.583  1.00 36.22           C  
ATOM   3850  C   ALA A 480       7.813  41.738  -0.535  1.00 36.72           C  
ATOM   3851  O   ALA A 480       7.273  40.652  -0.764  1.00 35.77           O  
ATOM   3852  CB  ALA A 480       6.610  43.753  -1.398  1.00 37.21           C  
ATOM   3853  N   HIS A 481       8.462  41.996   0.598  1.00 39.07           N  
ATOM   3854  CA  HIS A 481       8.410  41.075   1.747  1.00 40.22           C  
ATOM   3855  C   HIS A 481       6.977  40.910   2.221  1.00 38.02           C  
ATOM   3856  O   HIS A 481       6.181  41.828   2.181  1.00 38.51           O  
ATOM   3857  CB  HIS A 481       9.303  41.547   2.901  1.00 42.92           C  
ATOM   3858  CG  HIS A 481      10.771  41.372   2.648  1.00 46.26           C  
ATOM   3859  ND1 HIS A 481      11.334  40.148   2.348  1.00 48.66           N  
ATOM   3860  CD2 HIS A 481      11.796  42.258   2.684  1.00 48.95           C  
ATOM   3861  CE1 HIS A 481      12.637  40.293   2.173  1.00 49.77           C  
ATOM   3862  NE2 HIS A 481      12.945  41.563   2.383  1.00 51.39           N  
ATOM   3863  N   VAL A 482       6.653  39.691   2.602  1.00 36.58           N  
ATOM   3864  CA  VAL A 482       5.310  39.329   3.059  1.00 35.21           C  
ATOM   3865  C   VAL A 482       5.289  39.543   4.585  1.00 32.83           C  
ATOM   3866  O   VAL A 482       6.245  39.126   5.293  1.00 32.67           O  
ATOM   3867  CB  VAL A 482       5.025  37.860   2.680  1.00 35.48           C  
ATOM   3868  CG1 VAL A 482       3.647  37.420   3.141  1.00 35.52           C  
ATOM   3869  CG2 VAL A 482       5.185  37.659   1.175  1.00 36.51           C  
ATOM   3870  N   LEU A 483       4.263  40.247   5.064  1.00 31.20           N  
ATOM   3871  CA  LEU A 483       3.983  40.394   6.510  1.00 29.75           C  
ATOM   3872  C   LEU A 483       2.673  39.729   6.905  1.00 28.10           C  
ATOM   3873  O   LEU A 483       1.667  39.854   6.205  1.00 27.83           O  
ATOM   3874  CB  LEU A 483       3.865  41.860   6.913  1.00 30.97           C  
ATOM   3875  CG  LEU A 483       5.105  42.722   6.707  1.00 32.31           C  
ATOM   3876  CD1 LEU A 483       4.871  44.091   7.303  1.00 33.94           C  
ATOM   3877  CD2 LEU A 483       6.350  42.115   7.318  1.00 32.70           C  
ATOM   3878  N   MET A 484       2.675  39.088   8.064  1.00 26.09           N  
ATOM   3879  CA  MET A 484       1.445  38.539   8.609  1.00 25.42           C  
ATOM   3880  C   MET A 484       0.560  39.677   9.076  1.00 25.04           C  
ATOM   3881  O   MET A 484       1.057  40.760   9.345  1.00 25.18           O  
ATOM   3882  CB  MET A 484       1.727  37.577   9.756  1.00 25.02           C  
ATOM   3883  CG  MET A 484       2.489  36.337   9.345  1.00 25.06           C  
ATOM   3884  SD  MET A 484       2.690  35.195  10.708  1.00 24.91           S  
ATOM   3885  CE  MET A 484       1.008  34.662  10.957  1.00 25.27           C  
ATOM   3886  N   PRO A 485      -0.754  39.432   9.205  1.00 25.01           N  
ATOM   3887  CA  PRO A 485      -1.622  40.481   9.711  1.00 25.68           C  
ATOM   3888  C   PRO A 485      -1.201  41.126  11.042  1.00 25.50           C  
ATOM   3889  O   PRO A 485      -1.294  42.334  11.171  1.00 26.06           O  
ATOM   3890  CB  PRO A 485      -2.975  39.781   9.834  1.00 26.30           C  
ATOM   3891  CG  PRO A 485      -2.926  38.737   8.766  1.00 26.28           C  
ATOM   3892  CD  PRO A 485      -1.519  38.238   8.790  1.00 25.20           C  
ATOM   3893  N   HIS A 486      -0.681  40.358  11.990  1.00 24.93           N  
ATOM   3894  CA  HIS A 486      -0.308  40.940  13.287  1.00 25.40           C  
ATOM   3895  C   HIS A 486       1.012  41.738  13.199  1.00 26.62           C  
ATOM   3896  O   HIS A 486       1.322  42.504  14.099  1.00 27.11           O  
ATOM   3897  CB  HIS A 486      -0.228  39.877  14.377  1.00 24.36           C  
ATOM   3898  CG  HIS A 486       1.020  39.053  14.316  1.00 23.66           C  
ATOM   3899  ND1 HIS A 486       1.092  37.869  13.622  1.00 23.05           N  
ATOM   3900  CD2 HIS A 486       2.248  39.249  14.851  1.00 23.84           C  
ATOM   3901  CE1 HIS A 486       2.311  37.371  13.725  1.00 23.22           C  
ATOM   3902  NE2 HIS A 486       3.037  38.197  14.449  1.00 23.64           N  
ATOM   3903  N   GLU A 487       1.751  41.557  12.114  1.00 27.45           N  
ATOM   3904  CA  GLU A 487       2.987  42.271  11.896  1.00 29.70           C  
ATOM   3905  C   GLU A 487       2.756  43.597  11.179  1.00 33.49           C  
ATOM   3906  O   GLU A 487       3.678  44.325  11.031  1.00 34.80           O  
ATOM   3907  CB  GLU A 487       3.945  41.415  11.061  1.00 28.24           C  
ATOM   3908  CG  GLU A 487       4.311  40.118  11.742  1.00 27.18           C  
ATOM   3909  CD  GLU A 487       5.124  39.167  10.877  1.00 26.55           C  
ATOM   3910  OE1 GLU A 487       5.009  39.226   9.631  1.00 25.67           O  
ATOM   3911  OE2 GLU A 487       5.863  38.329  11.450  1.00 26.33           O  
ATOM   3912  N   SER A 488       1.529  43.866  10.704  1.00 37.42           N  
ATOM   3913  CA  SER A 488       1.240  44.952   9.716  1.00 41.15           C  
ATOM   3914  C   SER A 488       0.815  46.248  10.397  1.00 44.51           C  
ATOM   3915  O   SER A 488       0.757  46.294  11.643  1.00 48.54           O  
ATOM   3916  CB  SER A 488       0.140  44.496   8.735  1.00 41.66           C  
ATOM   3917  OG  SER A 488       0.574  43.391   7.922  1.00 40.86           O  
TER    3918      SER A 488                                                      
HETATM 3919  C1  GOL A 601      17.631  37.397  -3.421  1.00 55.06           C  
HETATM 3920  O1  GOL A 601      19.059  37.390  -3.347  1.00 55.59           O  
HETATM 3921  C2  GOL A 601      17.134  36.071  -2.861  1.00 54.35           C  
HETATM 3922  O2  GOL A 601      17.545  36.023  -1.479  1.00 52.34           O  
HETATM 3923  C3  GOL A 601      17.674  34.850  -3.643  1.00 49.92           C  
HETATM 3924  O3  GOL A 601      17.564  34.990  -5.068  1.00 42.61           O  
HETATM 3925  C1  GOL A 602      24.259  17.250 -25.840  1.00 49.82           C  
HETATM 3926  O1  GOL A 602      24.035  16.312 -26.913  1.00 48.00           O  
HETATM 3927  C2  GOL A 602      25.699  17.058 -25.351  1.00 53.32           C  
HETATM 3928  O2  GOL A 602      26.559  18.075 -25.910  1.00 49.48           O  
HETATM 3929  C3  GOL A 602      25.814  16.988 -23.833  1.00 54.49           C  
HETATM 3930  O3  GOL A 602      27.029  17.587 -23.337  1.00 59.53           O  
HETATM 3931  C1  GOL A 603      -0.329  21.292   2.150  1.00 80.15           C  
HETATM 3932  O1  GOL A 603       0.354  20.150   2.678  1.00 79.12           O  
HETATM 3933  C2  GOL A 603       0.539  22.528   2.373  1.00 80.04           C  
HETATM 3934  O2  GOL A 603       0.932  22.580   3.747  1.00 78.02           O  
HETATM 3935  C3  GOL A 603       1.775  22.528   1.465  1.00 79.98           C  
HETATM 3936  O3  GOL A 603       2.536  21.314   1.540  1.00 79.08           O  
HETATM 3937  C1  GOL A 604      -8.720  33.249 -21.984  1.00 64.81           C  
HETATM 3938  O1  GOL A 604      -9.657  34.257 -22.346  1.00 61.66           O  
HETATM 3939  C2  GOL A 604      -9.039  31.884 -22.621  1.00 65.47           C  
HETATM 3940  O2  GOL A 604      -9.796  32.040 -23.825  1.00 68.38           O  
HETATM 3941  C3  GOL A 604      -9.812  30.950 -21.681  1.00 63.95           C  
HETATM 3942  O3  GOL A 604     -10.624  31.640 -20.721  1.00 64.14           O  
HETATM 3943  C1  GOL A 605      -1.812  12.733 -22.801  1.00 56.52           C  
HETATM 3944  O1  GOL A 605      -3.138  12.820 -22.273  1.00 49.92           O  
HETATM 3945  C2  GOL A 605      -1.305  14.141 -23.069  1.00 59.80           C  
HETATM 3946  O2  GOL A 605      -1.819  15.013 -22.064  1.00 60.34           O  
HETATM 3947  C3  GOL A 605       0.228  14.171 -23.071  1.00 64.42           C  
HETATM 3948  O3  GOL A 605       0.773  14.044 -21.749  1.00 67.06           O  
HETATM 3949  C1  GOL A 606       2.506  14.543 -27.618  1.00 50.10           C  
HETATM 3950  O1  GOL A 606       1.581  13.716 -28.299  1.00 51.88           O  
HETATM 3951  C2  GOL A 606       2.935  15.562 -28.635  1.00 51.29           C  
HETATM 3952  O2  GOL A 606       1.820  15.955 -29.440  1.00 58.25           O  
HETATM 3953  C3  GOL A 606       3.489  16.710 -27.839  1.00 49.51           C  
HETATM 3954  O3  GOL A 606       4.461  16.172 -26.939  1.00 47.94           O  
HETATM 3955  C1  GOL A 607      -1.375  16.092 -15.533  1.00 81.61           C  
HETATM 3956  O1  GOL A 607      -0.177  15.559 -16.101  1.00 83.40           O  
HETATM 3957  C2  GOL A 607      -1.384  16.067 -13.991  1.00 83.12           C  
HETATM 3958  O2  GOL A 607      -0.215  15.403 -13.486  1.00 86.60           O  
HETATM 3959  C3  GOL A 607      -1.437  17.477 -13.381  1.00 81.47           C  
HETATM 3960  O3  GOL A 607      -2.424  17.702 -12.358  1.00 80.35           O  
HETATM 3961  C1  GOL A 608     -34.299  11.601 -22.315  1.00 55.66           C  
HETATM 3962  O1  GOL A 608     -35.325  10.818 -22.950  1.00 55.29           O  
HETATM 3963  C2  GOL A 608     -33.224  12.012 -23.331  1.00 54.11           C  
HETATM 3964  O2  GOL A 608     -33.625  13.230 -23.990  1.00 58.08           O  
HETATM 3965  C3  GOL A 608     -31.824  12.276 -22.773  1.00 53.77           C  
HETATM 3966  O3  GOL A 608     -31.051  11.249 -22.122  1.00 52.39           O  
HETATM 3967  C1  GOL A 609      -7.289   9.371 -14.889  1.00 65.99           C  
HETATM 3968  O1  GOL A 609      -8.431   8.522 -14.671  1.00 59.81           O  
HETATM 3969  C2  GOL A 609      -6.022   8.692 -15.458  1.00 66.74           C  
HETATM 3970  O2  GOL A 609      -5.573   9.437 -16.602  1.00 66.45           O  
HETATM 3971  C3  GOL A 609      -6.173   7.224 -15.897  1.00 67.53           C  
HETATM 3972  O3  GOL A 609      -5.053   6.388 -15.552  1.00 73.95           O  
HETATM 3973 MG    MG A 610       5.296  20.969 -21.355  1.00 43.14          MG  
HETATM 3974  O   HOH A 701     -26.992  20.679  -7.415  1.00 41.35           O  
HETATM 3975  O   HOH A 702      -8.191  36.004 -23.034  1.00 44.02           O  
HETATM 3976  O   HOH A 703      -6.887   8.758  -7.715  1.00 51.61           O  
HETATM 3977  O   HOH A 704      19.908   2.027 -32.488  1.00 41.05           O  
HETATM 3978  O   HOH A 705       1.787  17.308 -31.446  1.00 22.21           O  
HETATM 3979  O   HOH A 706      -4.039  14.966 -18.148  1.00 40.56           O  
HETATM 3980  O   HOH A 707       9.450  46.458 -16.242  1.00 51.95           O  
HETATM 3981  O   HOH A 708     -15.763  -0.347 -27.594  1.00 37.84           O  
HETATM 3982  O   HOH A 709       6.613  22.178 -17.675  1.00 24.84           O  
HETATM 3983  O   HOH A 710      -4.587  23.209 -10.368  1.00 40.04           O  
HETATM 3984  O   HOH A 711       5.607  13.953 -26.802  1.00 33.25           O  
HETATM 3985  O   HOH A 712      -8.825  26.773 -26.875  1.00 22.56           O  
HETATM 3986  O   HOH A 713      20.389  20.647  -5.042  1.00 36.11           O  
HETATM 3987  O   HOH A 714      19.515  13.597 -34.264  1.00 33.48           O  
HETATM 3988  O   HOH A 715      23.668  16.170 -29.425  1.00 38.96           O  
HETATM 3989  O   HOH A 716      30.305  13.532 -16.484  1.00 45.96           O  
HETATM 3990  O   HOH A 717       7.785  17.240 -20.288  1.00 31.03           O  
HETATM 3991  O   HOH A 718      -1.710  31.730 -33.608  1.00 29.40           O  
HETATM 3992  O   HOH A 719     -18.422  33.073  -9.721  1.00 38.66           O  
HETATM 3993  O   HOH A 720      25.699  20.008 -27.361  1.00 41.80           O  
HETATM 3994  O   HOH A 721       8.722   9.679 -24.073  1.00 31.38           O  
HETATM 3995  O   HOH A 722     -18.352   4.035 -13.135  1.00 40.85           O  
HETATM 3996  O   HOH A 723      -3.442  25.950  -3.484  1.00 55.79           O  
HETATM 3997  O   HOH A 724       7.837  18.389 -23.486  1.00 24.52           O  
HETATM 3998  O   HOH A 725     -18.398  29.543  -3.503  1.00 42.52           O  
HETATM 3999  O   HOH A 726      -4.645  16.471 -12.856  1.00 36.19           O  
HETATM 4000  O   HOH A 727       4.791  31.189 -24.520  1.00 24.90           O  
HETATM 4001  O   HOH A 728      -2.532  25.471 -28.321  1.00 19.04           O  
HETATM 4002  O   HOH A 729     -22.171  28.320 -12.234  1.00 30.84           O  
HETATM 4003  O   HOH A 730      28.057  19.406 -21.801  1.00 45.06           O  
HETATM 4004  O   HOH A 731      12.856   9.340 -15.402  1.00 27.94           O  
HETATM 4005  O   HOH A 732       7.889  42.595 -12.905  1.00 43.26           O  
HETATM 4006  O   HOH A 733     -26.988  44.857   1.656  1.00 49.82           O  
HETATM 4007  O   HOH A 734       7.353  27.941 -29.981  1.00 20.13           O  
HETATM 4008  O   HOH A 735      26.288  10.588 -17.604  1.00 40.21           O  
HETATM 4009  O   HOH A 736       4.407  18.567 -21.241  1.00 56.85           O  
HETATM 4010  O   HOH A 737      -7.534  30.634 -28.380  1.00 30.02           O  
HETATM 4011  O   HOH A 738      -3.728  18.847 -39.458  1.00 38.80           O  
HETATM 4012  O   HOH A 739     -23.049   5.330 -10.751  1.00 40.78           O  
HETATM 4013  O   HOH A 740      23.212  15.438 -22.976  1.00 31.35           O  
HETATM 4014  O   HOH A 741      -0.144  23.068 -16.338  1.00 40.04           O  
HETATM 4015  O   HOH A 742     -20.819  16.821  -3.624  1.00 26.35           O  
HETATM 4016  O   HOH A 743     -25.537  15.177 -12.461  1.00 32.62           O  
HETATM 4017  O   HOH A 744      -6.662  31.284 -36.149  1.00 33.56           O  
HETATM 4018  O   HOH A 745      -1.873  16.744 -20.079  1.00 29.56           O  
HETATM 4019  O   HOH A 746     -19.972  25.240 -27.895  1.00 22.46           O  
HETATM 4020  O   HOH A 747      -8.413  15.915  -7.858  1.00 35.44           O  
HETATM 4021  O   HOH A 748      15.552  13.302  -8.437  1.00 27.14           O  
HETATM 4022  O   HOH A 749       9.086  41.047 -29.472  1.00 31.68           O  
HETATM 4023  O   HOH A 750       5.893  42.808  -4.610  1.00 44.42           O  
HETATM 4024  O   HOH A 751     -27.700  12.497 -16.667  1.00 39.21           O  
HETATM 4025  O   HOH A 752     -19.797   4.233 -33.623  1.00 46.41           O  
HETATM 4026  O   HOH A 753     -20.418   8.644 -12.540  1.00 20.27           O  
HETATM 4027  O   HOH A 754      14.024   5.851 -20.729  1.00 23.21           O  
HETATM 4028  O   HOH A 755      -5.959   7.246 -19.569  1.00 39.05           O  
HETATM 4029  O   HOH A 756      27.865  29.321 -42.296  1.00 26.52           O  
HETATM 4030  O  AHOH A 757       7.342  39.288 -25.544  0.50 16.40           O  
HETATM 4031  O  BHOH A 757       9.018  39.209 -27.398  0.50 19.32           O  
HETATM 4032  O   HOH A 758      -6.517  22.442 -36.594  1.00 27.70           O  
HETATM 4033  O   HOH A 759       9.393  44.161 -14.964  1.00 43.83           O  
HETATM 4034  O   HOH A 760      21.292  27.966 -34.886  1.00 18.57           O  
HETATM 4035  O   HOH A 761      19.415   0.731 -29.962  1.00 39.83           O  
HETATM 4036  O   HOH A 762       9.809  33.004 -28.195  1.00 43.24           O  
HETATM 4037  O   HOH A 763      18.548  31.076  -6.509  1.00 29.21           O  
HETATM 4038  O   HOH A 764      22.466  27.912 -25.822  1.00 27.05           O  
HETATM 4039  O   HOH A 765      31.073   3.438 -17.405  1.00 47.67           O  
HETATM 4040  O   HOH A 766      14.587   4.870 -18.186  1.00 30.92           O  
HETATM 4041  O   HOH A 767      19.161  16.593 -35.487  1.00 29.76           O  
HETATM 4042  O   HOH A 768      11.771  19.542 -38.376  1.00 26.50           O  
HETATM 4043  O   HOH A 769       0.170  22.768 -19.622  1.00 34.43           O  
HETATM 4044  O   HOH A 770       2.630  20.816 -21.776  1.00 35.55           O  
HETATM 4045  O   HOH A 771      -5.127   5.063 -24.250  1.00 31.14           O  
HETATM 4046  O   HOH A 772     -10.876  41.786 -16.054  1.00 39.38           O  
HETATM 4047  O   HOH A 773     -27.336   7.455 -11.247  1.00 29.13           O  
HETATM 4048  O   HOH A 774      -9.947   9.521  -3.947  1.00 40.06           O  
HETATM 4049  O   HOH A 775     -22.874   4.063 -29.652  1.00 42.34           O  
HETATM 4050  O   HOH A 776      18.053  20.384  -3.493  1.00 36.30           O  
HETATM 4051  O   HOH A 777     -11.877   3.526 -23.573  1.00 32.37           O  
HETATM 4052  O   HOH A 778      -7.631  16.949 -24.132  1.00 21.81           O  
HETATM 4053  O   HOH A 779      -9.275  30.777 -26.132  1.00 44.56           O  
HETATM 4054  O   HOH A 780       2.577  36.898  -5.534  1.00 31.38           O  
HETATM 4055  O   HOH A 781      11.755   7.061 -19.280  1.00 33.79           O  
HETATM 4056  O   HOH A 782      -2.982  30.229 -35.359  1.00 26.62           O  
HETATM 4057  O   HOH A 783      18.014  36.582 -33.400  1.00 45.53           O  
HETATM 4058  O   HOH A 784     -15.203  13.907  -2.034  1.00 28.51           O  
HETATM 4059  O   HOH A 785     -12.923  35.895 -14.895  1.00 28.23           O  
HETATM 4060  O   HOH A 786     -16.214  29.943 -31.107  1.00 36.28           O  
HETATM 4061  O   HOH A 787      -7.279  35.081  -2.794  1.00 35.05           O  
HETATM 4062  O   HOH A 788      13.347  34.893  -2.832  1.00 32.24           O  
HETATM 4063  O   HOH A 789      23.653   9.628 -27.071  1.00 25.67           O  
HETATM 4064  O   HOH A 790       5.708  37.976  14.129  1.00 22.30           O  
HETATM 4065  O   HOH A 791     -12.193  30.800 -23.662  1.00 25.68           O  
HETATM 4066  O   HOH A 792      18.895  -0.986 -17.699  1.00 46.25           O  
HETATM 4067  O   HOH A 793      -8.868   5.037 -26.779  1.00 25.10           O  
HETATM 4068  O   HOH A 794      30.979  29.185 -39.413  1.00 22.08           O  
HETATM 4069  O   HOH A 795      -7.043  28.868 -20.105  1.00 18.81           O  
HETATM 4070  O   HOH A 796     -13.656   7.299 -36.349  1.00 27.75           O  
HETATM 4071  O   HOH A 797      -4.126  17.208 -16.015  1.00 34.95           O  
HETATM 4072  O   HOH A 798      17.588  16.809  -8.142  1.00 30.13           O  
HETATM 4073  O   HOH A 799      24.519  28.499 -27.647  1.00 25.99           O  
HETATM 4074  O   HOH A 800       8.902  37.035 -29.121  1.00 37.77           O  
HETATM 4075  O   HOH A 801      20.963   3.054 -22.846  1.00 26.69           O  
HETATM 4076  O   HOH A 802      -8.151  30.863  -4.405  1.00 31.32           O  
HETATM 4077  O   HOH A 803      -2.005  28.629 -37.436  1.00 30.51           O  
HETATM 4078  O   HOH A 804      -6.963  24.418 -11.443  1.00 20.24           O  
HETATM 4079  O   HOH A 805      12.047  29.509 -32.552  1.00 23.56           O  
HETATM 4080  O   HOH A 806      -1.318  18.323 -40.687  1.00 32.45           O  
HETATM 4081  O   HOH A 807       3.819  42.464   0.988  1.00 47.94           O  
HETATM 4082  O   HOH A 808     -27.702  15.072 -17.692  1.00 20.04           O  
HETATM 4083  O   HOH A 809      18.526  29.556   0.744  1.00 45.65           O  
HETATM 4084  O   HOH A 810     -24.135  27.555 -22.786  1.00 34.94           O  
HETATM 4085  O   HOH A 811     -23.165  18.577 -27.679  1.00 20.46           O  
HETATM 4086  O   HOH A 812     -13.694  30.176 -21.174  1.00 20.03           O  
HETATM 4087  O   HOH A 813      24.582  35.650 -28.197  1.00 34.77           O  
HETATM 4088  O   HOH A 814       1.169  27.375 -17.373  1.00 18.24           O  
HETATM 4089  O   HOH A 815      17.249  53.008 -27.924  1.00 47.47           O  
HETATM 4090  O   HOH A 816       0.789  41.705 -26.829  1.00 39.20           O  
HETATM 4091  O   HOH A 817      10.325  24.147  -1.933  1.00 33.74           O  
HETATM 4092  O   HOH A 818      11.079   6.846 -26.056  1.00 36.11           O  
HETATM 4093  O   HOH A 819      -8.994   4.261 -33.603  1.00 27.83           O  
HETATM 4094  O   HOH A 820     -13.650  26.050   1.776  1.00 23.96           O  
HETATM 4095  O   HOH A 821     -17.031   9.139  -9.357  1.00 31.96           O  
HETATM 4096  O   HOH A 822      13.386  48.731 -30.827  1.00 47.26           O  
HETATM 4097  O   HOH A 823     -19.638  21.413 -30.718  1.00 22.63           O  
HETATM 4098  O   HOH A 824     -27.837  22.316 -25.722  1.00 42.96           O  
HETATM 4099  O   HOH A 825      -9.272  44.164 -15.107  1.00 39.12           O  
HETATM 4100  O   HOH A 826      18.847  28.929 -35.298  1.00 21.95           O  
HETATM 4101  O   HOH A 827      19.327  48.232 -32.518  1.00 39.69           O  
HETATM 4102  O   HOH A 828      -0.329  41.465 -31.063  1.00 38.92           O  
HETATM 4103  O   HOH A 829      27.123  30.670 -35.240  1.00 29.93           O  
HETATM 4104  O   HOH A 830      23.743  43.388 -32.925  1.00 42.90           O  
HETATM 4105  O   HOH A 831     -22.173  26.279   2.808  1.00 29.82           O  
HETATM 4106  O   HOH A 832     -11.108   5.608 -25.327  1.00 28.46           O  
HETATM 4107  O   HOH A 833       7.988  10.331 -32.203  1.00 35.22           O  
HETATM 4108  O   HOH A 834     -24.293  15.557  -3.049  1.00 49.33           O  
HETATM 4109  O   HOH A 835      -7.368  31.579 -20.287  1.00 24.56           O  
HETATM 4110  O   HOH A 836       8.042  38.020  -1.055  1.00 35.08           O  
HETATM 4111  O   HOH A 837     -21.223   0.934 -29.599  1.00 44.04           O  
HETATM 4112  O   HOH A 838      -9.954  22.984 -17.885  1.00 17.31           O  
HETATM 4113  O   HOH A 839     -33.534  11.710 -19.573  1.00 38.02           O  
HETATM 4114  O   HOH A 840       0.972   8.747 -37.029  1.00 43.57           O  
HETATM 4115  O   HOH A 841     -28.187  20.867 -16.195  1.00 37.63           O  
HETATM 4116  O   HOH A 842      22.773  34.343 -14.709  1.00 35.56           O  
HETATM 4117  O   HOH A 843     -33.571   5.705 -22.744  1.00 52.01           O  
HETATM 4118  O   HOH A 844      -3.775  21.622 -26.497  1.00 18.54           O  
HETATM 4119  O   HOH A 845       1.762  40.757 -29.483  1.00 41.83           O  
HETATM 4120  O   HOH A 846     -28.405  15.471 -28.172  1.00 31.47           O  
HETATM 4121  O   HOH A 847      -8.036   9.452 -34.033  1.00 27.07           O  
HETATM 4122  O   HOH A 848     -19.718  21.210 -18.389  1.00 18.14           O  
HETATM 4123  O   HOH A 849      17.024   7.473 -11.602  1.00 46.52           O  
HETATM 4124  O   HOH A 850       4.435  13.583 -40.354  1.00 44.15           O  
HETATM 4125  O   HOH A 851     -10.763  20.864  -1.019  1.00 41.22           O  
HETATM 4126  O   HOH A 852      14.663   2.250 -19.119  1.00 37.95           O  
HETATM 4127  O   HOH A 853       1.555  10.514 -34.882  1.00 29.89           O  
HETATM 4128  O   HOH A 854      18.345  15.900  -4.260  1.00 42.49           O  
HETATM 4129  O   HOH A 855      23.207   5.313 -14.360  1.00 40.16           O  
HETATM 4130  O   HOH A 856       9.016  39.244   5.624  1.00 32.67           O  
HETATM 4131  O   HOH A 857      14.289   2.408 -28.096  1.00 44.15           O  
HETATM 4132  O   HOH A 858      20.450   5.147 -13.752  1.00 33.24           O  
HETATM 4133  O   HOH A 859      11.553  49.456 -26.642  1.00 42.12           O  
HETATM 4134  O   HOH A 860      28.862  20.314 -16.781  1.00 44.90           O  
HETATM 4135  O   HOH A 861      10.521  29.644  -3.282  1.00 32.05           O  
HETATM 4136  O   HOH A 862      25.876  19.018  -7.655  1.00 45.91           O  
HETATM 4137  O   HOH A 863      18.649  33.412  -7.580  1.00 31.14           O  
HETATM 4138  O   HOH A 864     -15.623  32.686 -14.254  1.00 22.86           O  
HETATM 4139  O   HOH A 865      23.781  23.852 -39.240  1.00 31.39           O  
HETATM 4140  O   HOH A 866     -16.809  38.803  -7.563  1.00 29.38           O  
HETATM 4141  O   HOH A 867      27.131  31.249 -31.380  1.00 30.71           O  
HETATM 4142  O   HOH A 868      13.764   2.513 -14.504  1.00 36.56           O  
HETATM 4143  O   HOH A 869     -30.824   8.928 -11.194  1.00 34.59           O  
HETATM 4144  O   HOH A 870      -0.099  44.050  15.961  1.00 46.28           O  
HETATM 4145  O   HOH A 871      -0.951  31.239  -3.155  1.00 26.37           O  
HETATM 4146  O   HOH A 872      11.202  35.426 -35.845  1.00 34.11           O  
HETATM 4147  O   HOH A 873       5.255  11.095 -16.722  1.00 50.91           O  
HETATM 4148  O   HOH A 874      17.469  23.936 -37.304  1.00 19.46           O  
HETATM 4149  O   HOH A 875     -20.358  20.524  -0.918  1.00 24.98           O  
HETATM 4150  O   HOH A 876      18.489  44.610 -10.955  1.00 37.15           O  
HETATM 4151  O   HOH A 877     -19.424  34.464 -13.706  1.00 38.97           O  
HETATM 4152  O   HOH A 878      27.435  26.473 -20.861  1.00 42.76           O  
HETATM 4153  O   HOH A 879      17.003  51.676 -30.198  1.00 37.09           O  
HETATM 4154  O   HOH A 880       2.136  36.712 -36.374  1.00 52.34           O  
HETATM 4155  O   HOH A 881       5.224  40.936  -6.525  1.00 46.77           O  
HETATM 4156  O   HOH A 882     -32.507  14.392 -20.214  1.00 40.88           O  
HETATM 4157  O   HOH A 883      28.875  -0.077 -17.848  1.00 44.40           O  
HETATM 4158  O   HOH A 884      18.854  22.220 -35.618  1.00 23.66           O  
HETATM 4159  O   HOH A 885      23.580  50.205 -28.132  1.00 43.97           O  
HETATM 4160  O   HOH A 886     -26.131  21.151 -21.924  1.00 20.33           O  
HETATM 4161  O   HOH A 887     -12.681  27.622 -31.698  1.00 27.95           O  
HETATM 4162  O   HOH A 888     -25.076  20.950  -9.546  1.00 36.85           O  
HETATM 4163  O   HOH A 889      13.635   8.702 -27.059  1.00 26.04           O  
HETATM 4164  O   HOH A 890      24.976  28.845 -41.762  1.00 26.94           O  
HETATM 4165  O   HOH A 891     -21.100  49.405   4.817  1.00 56.73           O  
HETATM 4166  O   HOH A 892     -20.509  18.557 -18.191  1.00 17.56           O  
HETATM 4167  O   HOH A 893      22.904  -1.072 -27.416  1.00 38.03           O  
HETATM 4168  O   HOH A 894     -19.236  40.679 -21.065  1.00 41.98           O  
HETATM 4169  O   HOH A 895      27.852  26.426 -37.328  1.00 38.63           O  
HETATM 4170  O   HOH A 896       8.480  37.592   2.036  1.00 38.81           O  
HETATM 4171  O   HOH A 897      13.353  12.853 -35.786  1.00 35.97           O  
HETATM 4172  O   HOH A 898      26.384  25.761 -10.202  1.00 58.05           O  
HETATM 4173  O   HOH A 899      16.091  28.601 -42.634  1.00 31.97           O  
HETATM 4174  O   HOH A 900     -20.965  31.088 -18.809  1.00 40.38           O  
HETATM 4175  O   HOH A 901      18.004  -1.493 -21.314  1.00 46.24           O  
HETATM 4176  O   HOH A 902     -10.770  25.538 -11.052  1.00 15.95           O  
HETATM 4177  O   HOH A 903     -18.311  17.871  -3.092  1.00 31.47           O  
HETATM 4178  O   HOH A 904      -5.845  32.126 -33.866  1.00 31.45           O  
HETATM 4179  O   HOH A 905       7.605  30.393 -23.819  1.00 21.31           O  
HETATM 4180  O   HOH A 906      -4.503  17.277 -26.527  1.00 24.25           O  
HETATM 4181  O   HOH A 907      15.682  11.962 -35.010  1.00 35.93           O  
HETATM 4182  O   HOH A 908      14.117  45.749 -27.255  1.00 45.35           O  
HETATM 4183  O   HOH A 909     -25.866  21.902 -28.043  1.00 35.82           O  
HETATM 4184  O   HOH A 910     -15.933   9.915  -3.775  1.00 43.84           O  
HETATM 4185  O   HOH A 911      -7.649  12.886 -10.450  1.00 40.77           O  
HETATM 4186  O   HOH A 912       6.029  17.939 -17.880  1.00 46.48           O  
HETATM 4187  O   HOH A 913     -18.170   4.201 -20.904  1.00 35.56           O  
HETATM 4188  O   HOH A 914     -24.369   6.225 -34.064  1.00 39.58           O  
HETATM 4189  O   HOH A 915       5.868  21.022 -41.475  1.00 37.27           O  
HETATM 4190  O   HOH A 916     -26.998  14.042 -14.110  1.00 45.17           O  
HETATM 4191  O   HOH A 917      -1.009  39.212   5.398  1.00 40.69           O  
HETATM 4192  O   HOH A 918     -18.113  11.586  -3.187  1.00 44.65           O  
HETATM 4193  O   HOH A 919       9.579  27.994 -40.910  1.00 45.07           O  
HETATM 4194  O   HOH A 920      -9.966  34.550  -3.646  1.00 27.91           O  
HETATM 4195  O   HOH A 921      21.601  34.301 -44.118  1.00 41.37           O  
HETATM 4196  O  AHOH A 922     -18.898  24.580 -31.996  0.50 16.59           O  
HETATM 4197  O  BHOH A 922     -19.738  26.370 -30.483  0.50 11.80           O  
HETATM 4198  O   HOH A 923      -9.761  28.232 -24.812  1.00 32.02           O  
HETATM 4199  O   HOH A 924      -5.947  36.048  -9.623  1.00 19.19           O  
HETATM 4200  O   HOH A 925      -8.574  28.105 -13.577  1.00 16.49           O  
HETATM 4201  O   HOH A 926     -16.049  16.550  -2.158  1.00 21.86           O  
HETATM 4202  O   HOH A 927       0.549  11.157 -32.007  1.00 26.63           O  
HETATM 4203  O   HOH A 928       7.876  13.690  -7.730  1.00 41.31           O  
HETATM 4204  O   HOH A 929      19.466  37.987 -21.999  1.00 49.95           O  
HETATM 4205  O   HOH A 930     -26.405  28.294 -18.990  1.00 26.76           O  
HETATM 4206  O   HOH A 931       3.237  45.609 -27.371  1.00 57.54           O  
HETATM 4207  O   HOH A 932      -4.100  20.932  -8.750  1.00 48.26           O  
HETATM 4208  O   HOH A 933     -27.986  14.901  -8.156  1.00 41.42           O  
HETATM 4209  O   HOH A 934      -6.533  15.611 -10.948  1.00 29.40           O  
HETATM 4210  O   HOH A 935      -6.880  33.225 -26.846  1.00 33.72           O  
HETATM 4211  O   HOH A 936       4.744  18.622 -45.062  1.00 50.57           O  
HETATM 4212  O   HOH A 937      -5.336   9.520 -34.809  1.00 31.19           O  
HETATM 4213  O   HOH A 938     -12.968  20.853 -34.198  1.00 28.13           O  
HETATM 4214  O   HOH A 939     -26.596  30.479 -14.987  1.00 55.85           O  
HETATM 4215  O   HOH A 940      18.796  19.428 -36.523  1.00 48.41           O  
HETATM 4216  O   HOH A 941       6.179  41.485 -10.875  1.00 24.93           O  
HETATM 4217  O   HOH A 942      -0.075  30.636 -38.307  1.00 44.10           O  
HETATM 4218  O   HOH A 943       6.577  36.071 -28.161  1.00 34.87           O  
HETATM 4219  O   HOH A 944       6.091  36.649  -1.841  1.00 36.37           O  
HETATM 4220  O   HOH A 945      10.369  37.711  -2.244  1.00 27.71           O  
HETATM 4221  O   HOH A 946      22.928  40.725 -36.133  1.00 25.55           O  
HETATM 4222  O   HOH A 947     -20.712   2.800 -16.437  1.00 25.55           O  
HETATM 4223  O   HOH A 948       5.587  33.724  -1.672  1.00 32.03           O  
HETATM 4224  O   HOH A 949     -14.426   3.470 -19.276  1.00 47.05           O  
HETATM 4225  O   HOH A 950      27.201  21.652 -25.561  1.00 47.65           O  
HETATM 4226  O   HOH A 951      13.962  27.292  -4.204  1.00 24.51           O  
HETATM 4227  O  AHOH A 952      18.258  31.385 -35.822  0.50 20.41           O  
HETATM 4228  O  BHOH A 952      17.880  33.582 -34.301  0.50 28.50           O  
HETATM 4229  O  AHOH A 953       8.352  10.726 -20.375  0.50 10.15           O  
HETATM 4230  O  BHOH A 953       8.254   8.529 -21.344  0.50 26.79           O  
HETATM 4231  O   HOH A 954      25.692  26.442 -40.939  1.00 43.10           O  
HETATM 4232  O   HOH A 955      21.098  39.149  -9.600  1.00 34.25           O  
HETATM 4233  O   HOH A 956     -17.579  31.564 -15.881  1.00 23.30           O  
HETATM 4234  O   HOH A 957      -7.291  22.502 -19.786  1.00 23.03           O  
HETATM 4235  O   HOH A 958       8.080  12.134 -34.449  1.00 37.41           O  
HETATM 4236  O   HOH A 959      18.293  19.217  -6.991  1.00 29.23           O  
HETATM 4237  O   HOH A 960       1.090  39.704 -24.957  1.00 39.83           O  
HETATM 4238  O   HOH A 961      -8.352  38.139 -14.808  1.00 36.86           O  
HETATM 4239  O   HOH A 962      -9.369  31.359 -30.372  1.00 41.46           O  
HETATM 4240  O   HOH A 963      23.399  49.272 -25.481  1.00 49.62           O  
HETATM 4241  O   HOH A 964     -27.428  18.197 -27.786  1.00 40.17           O  
HETATM 4242  O   HOH A 965      12.591   8.404 -30.235  1.00 33.78           O  
HETATM 4243  O   HOH A 966     -27.870   7.580  -8.435  1.00 46.59           O  
HETATM 4244  O   HOH A 967     -16.467  37.081 -25.082  1.00 41.75           O  
HETATM 4245  O   HOH A 968     -28.434   4.461 -28.442  1.00 52.10           O  
HETATM 4246  O   HOH A 969      -8.291  26.837 -11.212  1.00 16.01           O  
HETATM 4247  O   HOH A 970      24.324  26.742  -4.462  1.00 45.41           O  
HETATM 4248  O   HOH A 971      20.202  27.245 -42.095  1.00 48.37           O  
HETATM 4249  O   HOH A 972       4.649  38.775  -4.803  1.00 46.87           O  
HETATM 4250  O   HOH A 973     -13.723  12.797   4.069  1.00 52.30           O  
HETATM 4251  O   HOH A 974      28.893  28.792 -19.462  1.00 53.20           O  
HETATM 4252  O   HOH A 975       6.948  50.997 -23.201  1.00 52.19           O  
HETATM 4253  O   HOH A 976      24.287   8.228 -30.588  1.00 43.18           O  
HETATM 4254  O   HOH A 977      14.904  -0.511 -25.016  1.00 32.93           O  
HETATM 4255  O   HOH A 978     -12.788  33.191 -25.088  1.00 30.28           O  
HETATM 4256  O   HOH A 979      23.956  38.511 -27.580  1.00 40.64           O  
HETATM 4257  O   HOH A 980     -11.512  32.140 -27.457  1.00 34.50           O  
HETATM 4258  O   HOH A 981       4.128  38.364 -19.741  1.00 36.17           O  
HETATM 4259  O   HOH A 982      -6.435  31.719  -2.248  1.00 43.89           O  
HETATM 4260  O   HOH A 983       5.653  10.402 -13.437  1.00 42.70           O  
HETATM 4261  O   HOH A 984     -26.759  19.286 -20.023  1.00 42.11           O  
HETATM 4262  O   HOH A 985      13.388   6.440 -27.849  1.00 54.39           O  
HETATM 4263  O   HOH A 986      -4.762   0.658 -30.033  1.00 57.71           O  
HETATM 4264  O   HOH A 987      11.281  43.308 -10.411  1.00 42.06           O  
HETATM 4265  O   HOH A 988     -28.769  19.452 -18.247  1.00 44.41           O  
HETATM 4266  O   HOH A 989      25.279  35.056 -33.308  1.00 34.33           O  
HETATM 4267  O   HOH A 990      -5.364  24.837   0.155  1.00 45.65           O  
HETATM 4268  O   HOH A 991      15.659  16.633 -37.742  1.00 52.71           O  
HETATM 4269  O   HOH A 992      11.368  42.658 -30.215  1.00 43.48           O  
HETATM 4270  O   HOH A 993      -4.406   1.251 -27.110  1.00 52.62           O  
HETATM 4271  O   HOH A 994      -7.788  23.501   0.473  1.00 44.32           O  
HETATM 4272  O   HOH A 995       1.570  29.790 -40.813  1.00 56.54           O  
HETATM 4273  O   HOH A 996     -11.246  44.571 -24.991  1.00 60.00           O  
HETATM 4274  O   HOH A 997      12.923  10.105  -3.744  1.00 50.88           O  
HETATM 4275  O   HOH A 998     -12.189  30.693   1.588  1.00 45.09           O  
HETATM 4276  O   HOH A 999      22.776  17.766 -35.441  1.00 44.18           O  
HETATM 4277  O   HOH A1000      25.254  20.017 -32.241  1.00 34.61           O  
HETATM 4278  O   HOH A1001      13.125  43.981 -28.748  1.00 52.34           O  
HETATM 4279  O   HOH A1002      24.152  37.850  -5.658  1.00 62.99           O  
HETATM 4280  O   HOH A1003       0.000  25.011   0.000  0.50 66.88           O  
HETATM 4281  O   HOH A1004      26.602  30.298 -26.725  1.00 49.24           O  
HETATM 4282  O   HOH A1005       0.226  32.656 -35.323  1.00 37.30           O  
HETATM 4283  O   HOH A1006     -31.157  12.857 -13.586  1.00 47.10           O  
HETATM 4284  O   HOH A1007      -4.493  19.438 -28.238  1.00 22.83           O  
HETATM 4285  O   HOH A1008      -4.273  27.060  -0.350  1.00 46.05           O  
HETATM 4286  O   HOH A1009      18.662  31.733  -3.835  1.00 41.71           O  
HETATM 4287  O   HOH A1010     -14.404  29.527   2.844  1.00 36.06           O  
HETATM 4288  O   HOH A1011      15.278  37.156 -34.701  1.00 40.20           O  
HETATM 4289  O   HOH A1012     -11.405  25.876 -33.524  1.00 37.27           O  
HETATM 4290  O   HOH A1013      25.984  18.715 -29.838  1.00 43.61           O  
HETATM 4291  O   HOH A1014      -2.494   5.014 -25.369  1.00 38.90           O  
HETATM 4292  O   HOH A1015      -7.928  28.673 -22.803  1.00 37.81           O  
HETATM 4293  O   HOH A1016       1.433  32.310  -2.340  1.00 40.99           O  
HETATM 4294  O   HOH A1017       2.435  34.963  -3.398  1.00 40.64           O  
HETATM 4295  O   HOH A1018      -8.964   6.886 -34.399  1.00 28.17           O  
HETATM 4296  O   HOH A1019      12.385  21.923 -39.923  1.00 40.35           O  
HETATM 4297  O   HOH A1020       5.160  13.831 -23.818  1.00 44.79           O  
HETATM 4298  O   HOH A1021      15.689  21.951 -41.122  1.00 43.27           O  
HETATM 4299  O   HOH A1022      21.874  -1.792 -14.013  1.00 48.98           O  
HETATM 4300  O   HOH A1023      -5.817  17.091 -40.041  1.00 46.44           O  
HETATM 4301  O   HOH A1024      17.816  23.249 -39.883  1.00 29.70           O  
HETATM 4302  O   HOH A1025      15.844  45.892 -34.054  1.00 42.02           O  
HETATM 4303  O   HOH A1026      -3.701  28.299 -39.725  1.00 39.14           O  
HETATM 4304  O   HOH A1027      27.274  33.017 -33.641  1.00 32.56           O  
HETATM 4305  O   HOH A1028      16.491  31.036  -2.299  1.00 38.27           O  
HETATM 4306  O   HOH A1029     -17.202  16.567   0.531  1.00 39.65           O  
HETATM 4307  O   HOH A1030       5.823  10.439 -19.378  1.00 41.23           O  
HETATM 4308  O   HOH A1031      25.359   9.778 -14.944  1.00 41.12           O  
HETATM 4309  O   HOH A1032     -23.188  47.921   6.077  1.00 57.21           O  
HETATM 4310  O   HOH A1033     -24.786  17.636 -29.714  1.00 31.10           O  
HETATM 4311  O   HOH A1034      24.707  17.887 -33.768  1.00 41.87           O  
HETATM 4312  O  AHOH A1035       5.632  31.695 -27.439  0.50 25.01           O  
HETATM 4313  O  BHOH A1035       7.115  33.466 -27.240  0.50 24.48           O  
HETATM 4314  O   HOH A1036      -9.148  25.875 -35.758  1.00 51.04           O  
HETATM 4315  O   HOH A1037      -4.916   7.294 -36.520  1.00 40.23           O  
HETATM 4316  O   HOH A1038      28.981  -0.819 -15.331  1.00 47.80           O  
HETATM 4317  O   HOH A1039     -29.782  16.547 -16.924  1.00 33.98           O  
HETATM 4318  O   HOH A1040     -19.286   7.233 -10.277  1.00 36.56           O  
HETATM 4319  O   HOH A1041       5.512  37.470 -26.034  1.00 31.85           O  
HETATM 4320  O   HOH A1042       7.723  30.565 -28.885  1.00 41.55           O  
HETATM 4321  O   HOH A1043      -6.147  10.813 -11.495  1.00 51.40           O  
HETATM 4322  O   HOH A1044       4.246   9.741 -34.645  1.00 39.80           O  
HETATM 4323  O   HOH A1045      11.308  35.472  -1.081  1.00 42.16           O  
HETATM 4324  O   HOH A1046     -22.003  20.576 -29.327  1.00 24.75           O  
HETATM 4325  O   HOH A1047      29.060  27.817 -16.701  1.00 51.35           O  
HETATM 4326  O   HOH A1048       5.943  12.181 -38.488  1.00 44.66           O  
HETATM 4327  O   HOH A1049      13.576  17.655 -39.185  1.00 34.05           O  
HETATM 4328  O   HOH A1050      29.003  28.450 -35.556  1.00 39.31           O  
HETATM 4329  O   HOH A1051     -20.064  32.078 -14.839  1.00 30.56           O  
HETATM 4330  O   HOH A1052     -18.137  26.068 -34.257  1.00 43.94           O  
HETATM 4331  O   HOH A1053      25.991  35.699 -30.583  1.00 33.70           O  
HETATM 4332  O   HOH A1054      -7.436  33.597  -0.364  1.00 36.15           O  
HETATM 4333  O   HOH A1055     -17.136   9.463  -6.496  1.00 49.55           O  
HETATM 4334  O   HOH A1056      29.598  25.923 -18.781  1.00 59.62           O  
HETATM 4335  O   HOH A1057      24.466   0.286 -14.087  1.00 41.69           O  
HETATM 4336  O   HOH A1058     -21.299  47.521   8.270  1.00 50.75           O  
HETATM 4337  O   HOH A1059     -21.986  30.813 -13.498  1.00 37.11           O  
HETATM 4338  O   HOH A1060      10.199  33.124  -0.122  1.00 44.04           O  
HETATM 4339  O   HOH A1061     -26.994   3.103 -11.814  1.00 48.76           O  
HETATM 4340  O   HOH A1062       5.537   9.107 -32.452  1.00 44.55           O  
HETATM 4341  O   HOH A1063     -28.961   5.152 -12.219  1.00 45.91           O  
HETATM 4342  O   HOH A1064      26.790  -0.902 -13.346  1.00 42.69           O  
CONECT  422 3973                                                                
CONECT  434 3973                                                                
CONECT 2880 3973                                                                
CONECT 3919 3920 3921                                                           
CONECT 3920 3919                                                                
CONECT 3921 3919 3922 3923                                                      
CONECT 3922 3921                                                                
CONECT 3923 3921 3924                                                           
CONECT 3924 3923                                                                
CONECT 3925 3926 3927                                                           
CONECT 3926 3925                                                                
CONECT 3927 3925 3928 3929                                                      
CONECT 3928 3927                                                                
CONECT 3929 3927 3930                                                           
CONECT 3930 3929                                                                
CONECT 3931 3932 3933                                                           
CONECT 3932 3931                                                                
CONECT 3933 3931 3934 3935                                                      
CONECT 3934 3933                                                                
CONECT 3935 3933 3936                                                           
CONECT 3936 3935                                                                
CONECT 3937 3938 3939                                                           
CONECT 3938 3937                                                                
CONECT 3939 3937 3940 3941                                                      
CONECT 3940 3939                                                                
CONECT 3941 3939 3942                                                           
CONECT 3942 3941                                                                
CONECT 3943 3944 3945                                                           
CONECT 3944 3943                                                                
CONECT 3945 3943 3946 3947                                                      
CONECT 3946 3945                                                                
CONECT 3947 3945 3948                                                           
CONECT 3948 3947                                                                
CONECT 3949 3950 3951                                                           
CONECT 3950 3949                                                                
CONECT 3951 3949 3952 3953                                                      
CONECT 3952 3951                                                                
CONECT 3953 3951 3954                                                           
CONECT 3954 3953                                                                
CONECT 3955 3956 3957                                                           
CONECT 3956 3955                                                                
CONECT 3957 3955 3958 3959                                                      
CONECT 3958 3957                                                                
CONECT 3959 3957 3960                                                           
CONECT 3960 3959                                                                
CONECT 3961 3962 3963                                                           
CONECT 3962 3961                                                                
CONECT 3963 3961 3964 3965                                                      
CONECT 3964 3963                                                                
CONECT 3965 3963 3966                                                           
CONECT 3966 3965                                                                
CONECT 3967 3968 3969                                                           
CONECT 3968 3967                                                                
CONECT 3969 3967 3970 3971                                                      
CONECT 3970 3969                                                                
CONECT 3971 3969 3972                                                           
CONECT 3972 3971                                                                
CONECT 3973  422  434 2880 4009                                                 
CONECT 3973 4044                                                                
CONECT 4009 3973                                                                
CONECT 4044 3973                                                                
MASTER      727    0   10   25   22    0   18    6 4247    1   61   43          
END                                                                             
