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HEADER    DNA BINDING PROTEIN/DNA                 27-AUG-10   3ON0              
TITLE     CRYSTAL STRUCTURE OF THE PED208 TRAM-SBMA COMPLEX                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN TRAM;                                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: SBMA;                                                      
COMPND   7 CHAIN: P;                                                            
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: TRAM;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 OTHER_DETAILS: CHEMICALLY SYNTHESIZED OLIGO                          
KEYWDS    DNA BINDING PROTEIN, DNA PROTEIN-DNA COMPLEX, TETRAMER, COOPERATIVE   
KEYWDS   2 BINDING, UNWINDING OF DNA, KINKING OF DNA, PLASMID CONJUGATION,      
KEYWDS   3 BACTERIAL CONJUGATION, RIBBON-HELIX-HELIX, 4-HELIX BUNDLE,           
KEYWDS   4 TRANSCRIPTIONAL REPRESSOR, DNA, DNA BINDING PROTEIN-DNA COMPLEX      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.J.W.WONG,J.LU,R.A.EDWARDS,L.S.FROST,J.N.MARK GLOVER                 
REVDAT   2   07-SEP-11 3ON0    1       JRNL   VERSN                             
REVDAT   1   25-MAY-11 3ON0    0                                                
JRNL        AUTH   J.J.WONG,J.LU,R.A.EDWARDS,L.S.FROST,J.N.GLOVER               
JRNL        TITL   STRUCTURAL BASIS OF COOPERATIVE DNA RECOGNITION BY THE       
JRNL        TITL 2 PLASMID CONJUGATION FACTOR, TRAM.                            
JRNL        REF    NUCLEIC ACIDS RES.            V.  39  6775 2011              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   21565799                                                     
JRNL        DOI    10.1093/NAR/GKR296                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.87 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0066                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.87                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 83.78                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 26155                          
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) : 0.252                           
REMARK   3   R VALUE            (WORKING SET) : 0.250                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1383                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.87                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1655                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.29                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4090                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 73                           
REMARK   3   BIN FREE R VALUE                    : 0.5020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3737                                    
REMARK   3   NUCLEIC ACID ATOMS       : 489                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 78.07                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.32000                                              
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : -0.29000                                             
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): 0.497         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.328         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.293         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.321        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.909                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4326 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5916 ; 1.348 ; 2.111       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   457 ; 4.485 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   190 ;32.358 ;25.632       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   742 ;21.349 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;23.352 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   678 ; 0.064 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3014 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  2306 ; 0.697 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3736 ; 1.286 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2020 ; 1.305 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2180 ; 2.197 ; 4.500       
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 : 4                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     61       A      98      3                      
REMARK   3           1     B     61       B      98      3                      
REMARK   3           1     C     61       C      98      3                      
REMARK   3           1     D     61       D      98      3                      
REMARK   3           2     A    102       A     118      3                      
REMARK   3           2     B    102       B     118      3                      
REMARK   3           2     C    102       C     118      3                      
REMARK   3           2     D    102       D     118      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    220 ; 0.040 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    B    (A):    220 ; 0.040 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    C    (A):    220 ; 0.050 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    D    (A):    220 ; 0.030 ; 0.050           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    219 ; 0.060 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    B    (A):    219 ; 0.060 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    C    (A):    219 ; 0.070 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    D    (A):    219 ; 0.050 ; 5.000           
REMARK   3   TIGHT THERMAL      1    A (A**2):    220 ; 0.080 ; 0.500           
REMARK   3   TIGHT THERMAL      1    B (A**2):    220 ; 0.070 ; 0.500           
REMARK   3   TIGHT THERMAL      1    C (A**2):    220 ; 0.090 ; 0.500           
REMARK   3   TIGHT THERMAL      1    D (A**2):    220 ; 0.060 ; 0.500           
REMARK   3   LOOSE THERMAL      1    A (A**2):    219 ; 0.100 ;10.000           
REMARK   3   LOOSE THERMAL      1    B (A**2):    219 ; 0.090 ;10.000           
REMARK   3   LOOSE THERMAL      1    C (A**2):    219 ; 0.090 ;10.000           
REMARK   3   LOOSE THERMAL      1    D (A**2):    219 ; 0.080 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B C A D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      2       B      47      3                      
REMARK   3           1     C      2       C      47      3                      
REMARK   3           1     A      2       A      47      3                      
REMARK   3           1     D      2       D      47      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    B    (A):    184 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   2    C    (A):    184 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   2    A    (A):    184 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   2    D    (A):    184 ; 0.040 ; 0.050           
REMARK   3   LOOSE POSITIONAL   2    B    (A):    180 ; 0.090 ; 5.000           
REMARK   3   LOOSE POSITIONAL   2    C    (A):    180 ; 0.050 ; 5.000           
REMARK   3   LOOSE POSITIONAL   2    A    (A):    180 ; 0.040 ; 5.000           
REMARK   3   LOOSE POSITIONAL   2    D    (A):    180 ; 0.050 ; 5.000           
REMARK   3   TIGHT THERMAL      2    B (A**2):    184 ; 0.040 ; 0.500           
REMARK   3   TIGHT THERMAL      2    C (A**2):    184 ; 0.050 ; 0.500           
REMARK   3   TIGHT THERMAL      2    A (A**2):    184 ; 0.060 ; 0.500           
REMARK   3   TIGHT THERMAL      2    D (A**2):    184 ; 0.090 ; 0.500           
REMARK   3   LOOSE THERMAL      2    B (A**2):    180 ; 0.050 ;10.000           
REMARK   3   LOOSE THERMAL      2    C (A**2):    180 ; 0.060 ;10.000           
REMARK   3   LOOSE THERMAL      2    A (A**2):    180 ; 0.050 ;10.000           
REMARK   3   LOOSE THERMAL      2    D (A**2):    180 ; 0.080 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A B C                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     48       A      52      3                      
REMARK   3           1     B     48       B      52      3                      
REMARK   3           1     C     48       C      52      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    A    (A):     20 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   3    B    (A):     20 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   3    C    (A):     20 ; 0.040 ; 0.050           
REMARK   3   LOOSE POSITIONAL   3    A    (A):     26 ; 0.050 ; 5.000           
REMARK   3   LOOSE POSITIONAL   3    B    (A):     26 ; 0.050 ; 5.000           
REMARK   3   LOOSE POSITIONAL   3    C    (A):     26 ; 0.040 ; 5.000           
REMARK   3   TIGHT THERMAL      3    A (A**2):     20 ; 0.200 ; 0.500           
REMARK   3   TIGHT THERMAL      3    B (A**2):     20 ; 0.210 ; 0.500           
REMARK   3   TIGHT THERMAL      3    C (A**2):     20 ; 0.070 ; 0.500           
REMARK   3   LOOSE THERMAL      3    A (A**2):     26 ; 0.090 ;10.000           
REMARK   3   LOOSE THERMAL      3    B (A**2):     26 ; 0.120 ;10.000           
REMARK   3   LOOSE THERMAL      3    C (A**2):     26 ; 0.070 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : A B D                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     99       A     101      3                      
REMARK   3           1     B     99       B     101      3                      
REMARK   3           1     D     99       D     101      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    A    (A):     12 ; 0.040 ; 0.050           
REMARK   3   TIGHT POSITIONAL   4    B    (A):     12 ; 0.040 ; 0.050           
REMARK   3   TIGHT POSITIONAL   4    D    (A):     12 ; 0.020 ; 0.050           
REMARK   3   LOOSE POSITIONAL   4    A    (A):     13 ; 0.110 ; 5.000           
REMARK   3   LOOSE POSITIONAL   4    B    (A):     13 ; 0.120 ; 5.000           
REMARK   3   LOOSE POSITIONAL   4    D    (A):     13 ; 0.030 ; 5.000           
REMARK   3   TIGHT THERMAL      4    A (A**2):     12 ; 0.040 ; 0.500           
REMARK   3   TIGHT THERMAL      4    B (A**2):     12 ; 0.040 ; 0.500           
REMARK   3   TIGHT THERMAL      4    D (A**2):     12 ; 0.040 ; 0.500           
REMARK   3   LOOSE THERMAL      4    A (A**2):     13 ; 0.050 ;10.000           
REMARK   3   LOOSE THERMAL      4    B (A**2):     13 ; 0.070 ;10.000           
REMARK   3   LOOSE THERMAL      4    D (A**2):     13 ; 0.050 ;10.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
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    61        A   118                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.7840  12.8760  -1.8840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7139 T22:   0.1167                                     
REMARK   3      T33:   0.2248 T12:   0.0418                                     
REMARK   3      T13:  -0.1040 T23:   0.0719                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6449 L22:   2.0772                                     
REMARK   3      L33:   2.1212 L12:   0.8542                                     
REMARK   3      L13:  -0.4735 L23:  -0.0922                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0229 S12:   0.0089 S13:   0.2212                       
REMARK   3      S21:  -0.1509 S22:  -0.0588 S23:   0.4751                       
REMARK   3      S31:  -0.0270 S32:  -0.1991 S33:   0.0817                       
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 :   B    61        B   118                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.0510  18.6790 -10.3550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0465 T22:   0.1270                                     
REMARK   3      T33:   0.4437 T12:   0.0961                                     
REMARK   3      T13:   0.2479 T23:   0.1406                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6862 L22:   2.7371                                     
REMARK   3      L33:   5.4403 L12:   1.7495                                     
REMARK   3      L13:   1.0673 L23:   2.1580                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0031 S12:   0.4052 S13:   0.3121                       
REMARK   3      S21:  -0.8604 S22:   0.1561 S23:  -0.4873                       
REMARK   3      S31:  -0.1439 S32:   0.4651 S33:  -0.1591                       
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 :   C    61        C   118                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3020   9.3330  -5.7420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7347 T22:   0.1027                                     
REMARK   3      T33:   0.2188 T12:  -0.0292                                     
REMARK   3      T13:   0.0292 T23:   0.0111                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9089 L22:   4.4153                                     
REMARK   3      L33:   2.3097 L12:   0.0008                                     
REMARK   3      L13:   0.2377 L23:   1.6920                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0470 S12:   0.1294 S13:  -0.0343                       
REMARK   3      S21:  -0.3930 S22:   0.1523 S23:  -0.4272                       
REMARK   3      S31:   0.0712 S32:   0.1979 S33:  -0.1994                       
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 :   D    61        D   118                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.5290  22.1910  -6.6580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7455 T22:   0.1168                                     
REMARK   3      T33:   0.2342 T12:   0.0257                                     
REMARK   3      T13:  -0.0013 T23:   0.1505                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7833 L22:   4.5896                                     
REMARK   3      L33:   5.2033 L12:  -0.2760                                     
REMARK   3      L13:   2.1156 L23:   1.2767                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0883 S12:   0.2906 S13:   0.3293                       
REMARK   3      S21:  -0.3530 S22:  -0.0471 S23:   0.2393                       
REMARK   3      S31:  -0.3244 S32:  -0.1820 S33:  -0.0413                       
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 :   P     1        P    24                          
REMARK   3    ORIGIN FOR THE GROUP (A):  46.0100  30.3150  42.0870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9874 T22:   0.1111                                     
REMARK   3      T33:   0.2114 T12:   0.0609                                     
REMARK   3      T13:  -0.0937 T23:  -0.0296                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6147 L22:   2.1560                                     
REMARK   3      L33:   5.4844 L12:  -0.1880                                     
REMARK   3      L13:  -3.7455 L23:  -0.0427                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0841 S12:   0.0772 S13:   0.1209                       
REMARK   3      S21:  -0.0280 S22:  -0.4000 S23:   0.0213                       
REMARK   3      S31:  -0.1336 S32:  -0.3287 S33:   0.3159                       
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     2        A    47                          
REMARK   3    ORIGIN FOR THE GROUP (A):  58.4040  25.3940   9.0840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1534 T22:   0.6016                                     
REMARK   3      T33:   0.6108 T12:  -0.1840                                     
REMARK   3      T13:   0.2458 T23:  -0.2975                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2069 L22:  10.9812                                     
REMARK   3      L33:   8.4635 L12:  -5.5068                                     
REMARK   3      L13:   3.2199 L23:  -1.0684                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5683 S12:   0.6631 S13:  -0.6791                       
REMARK   3      S21:  -1.2429 S22:   0.2161 S23:  -0.1141                       
REMARK   3      S31:   1.4143 S32:   1.1153 S33:  -0.7844                       
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 :   B     2        B    47                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.6360  29.8460  38.5470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8827 T22:   0.4443                                     
REMARK   3      T33:   0.5990 T12:   0.0948                                     
REMARK   3      T13:  -0.0976 T23:  -0.0114                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7125 L22:  10.7212                                     
REMARK   3      L33:   4.4898 L12:  -0.0681                                     
REMARK   3      L13:   2.9368 L23:   2.3109                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4764 S12:  -0.2265 S13:   0.6743                       
REMARK   3      S21:  -0.6040 S22:  -0.1982 S23:   1.4255                       
REMARK   3      S31:  -0.8864 S32:  -0.6720 S33:   0.6746                       
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 :   C     2        C    47                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.4560  17.7500  37.1960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2176 T22:   0.1676                                     
REMARK   3      T33:   0.1741 T12:   0.0274                                     
REMARK   3      T13:  -0.0604 T23:  -0.1665                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.9270 L22:   5.7081                                     
REMARK   3      L33:   3.3968 L12:  -2.0735                                     
REMARK   3      L13:   5.5200 L23:  -0.1350                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4553 S12:   0.3393 S13:  -0.5600                       
REMARK   3      S21:  -0.4203 S22:  -0.1578 S23:   0.0842                       
REMARK   3      S31:   0.5718 S32:   0.1407 S33:  -0.2975                       
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 :   D     2        D    47                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.0280  36.9270  14.8810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5592 T22:   0.1755                                     
REMARK   3      T33:   0.2536 T12:  -0.0140                                     
REMARK   3      T13:  -0.0203 T23:   0.1294                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9351 L22:  13.1175                                     
REMARK   3      L33:   9.9923 L12:   0.9513                                     
REMARK   3      L13:  -0.6684 L23:  -0.5219                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2668 S12:  -0.0865 S13:   0.2799                       
REMARK   3      S21:  -0.1452 S22:   0.2025 S23:   1.0098                       
REMARK   3      S31:  -0.0296 S32:  -0.8172 S33:   0.0643                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3ON0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061320.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-APR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 12.3.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1158                             
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27538                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.870                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 83.789                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 81.0                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.87                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.43300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
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: PDB ENTRY 2G7O, C-TERMINAL DOMAIN WITH RESIDUES      
REMARK 200  MUTATED TO PED208                                                   
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 36% MPD, 5% PEG 2000, 100MM CACODYLIC    
REMARK 280  ACID, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
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                                         
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       83.78250            
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       83.78250            
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       46.51250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       77.34350            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       46.51250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       77.34350            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       83.78250            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       46.51250            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       77.34350            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       83.78250            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       46.51250            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       77.34350            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
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: DECAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 44630 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 51750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -420.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, B, C, P                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       93.02500            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       83.78250            
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     1                                                      
REMARK 465     ARG A    55                                                      
REMARK 465     GLU A    56                                                      
REMARK 465     GLY A    57                                                      
REMARK 465     GLY A    58                                                      
REMARK 465     GLU A   127                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B   120                                                      
REMARK 465     ASP B   121                                                      
REMARK 465     ASP B   122                                                      
REMARK 465     GLU B   123                                                      
REMARK 465     ASP B   124                                                      
REMARK 465     ASP B   125                                                      
REMARK 465     GLN B   126                                                      
REMARK 465     GLU B   127                                                      
REMARK 465     MET C     1                                                      
REMARK 465     PRO C   120                                                      
REMARK 465     ASP C   121                                                      
REMARK 465     ASP C   122                                                      
REMARK 465     GLU C   123                                                      
REMARK 465     ASP C   124                                                      
REMARK 465     ASP C   125                                                      
REMARK 465     GLN C   126                                                      
REMARK 465     GLU C   127                                                      
REMARK 465     MET D     1                                                      
REMARK 465     TYR D    48                                                      
REMARK 465     MET D    49                                                      
REMARK 465     ILE D    50                                                      
REMARK 465     GLN D    51                                                      
REMARK 465     GLN D    52                                                      
REMARK 465     GLU D    53                                                      
REMARK 465     LYS D    54                                                      
REMARK 465     ARG D    55                                                      
REMARK 465     GLU D    56                                                      
REMARK 465     GLY D    57                                                      
REMARK 465     GLY D    58                                                      
REMARK 465     PRO D   120                                                      
REMARK 465     ASP D   121                                                      
REMARK 465     ASP D   122                                                      
REMARK 465     GLU D   123                                                      
REMARK 465     ASP D   124                                                      
REMARK 465     ASP D   125                                                      
REMARK 465     GLN D   126                                                      
REMARK 465     GLU D   127                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLY D    27     N    GLU D    29              2.17            
REMARK 500   O    GLY B    27     N    GLU B    29              2.18            
REMARK 500   O    GLY A    27     N    GLU A    29              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   ND2  ASN A    97     NH1  ARG A   112     4555     1.92            
REMARK 500   NZ   LYS A   109     OE1  GLU C    81     4555     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE A 119   C     PRO A 120   N       0.252                       
REMARK 500     DT P   4   O3'    DT P   4   C3'    -0.047                       
REMARK 500     DC P  18   O3'    DC P  18   C3'    -0.061                       
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    ARG B  23   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG B  23   NE  -  CZ  -  NH2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500     DG P   2   C3' -  C2' -  C1' ANGL. DEV. =  -6.2 DEGREES          
REMARK 500     DG P   2   O4' -  C1' -  N9  ANGL. DEV. =   4.7 DEGREES          
REMARK 500     DT P   4   O4' -  C1' -  N1  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     DG P   7   C3' -  C2' -  C1' ANGL. DEV. =  -5.6 DEGREES          
REMARK 500     DA P   9   O4' -  C4' -  C3' ANGL. DEV. =  -3.3 DEGREES          
REMARK 500     DA P   9   C1' -  O4' -  C4' ANGL. DEV. =  -6.7 DEGREES          
REMARK 500     DA P   9   O4' -  C1' -  N9  ANGL. DEV. =  -6.7 DEGREES          
REMARK 500     DT P  10   C3' -  O3' -  P   ANGL. DEV. =   7.2 DEGREES          
REMARK 500     DA P  13   C1' -  O4' -  C4' ANGL. DEV. =  -6.3 DEGREES          
REMARK 500     DG P  14   C1' -  O4' -  C4' ANGL. DEV. =  -6.4 DEGREES          
REMARK 500     DG P  14   C3' -  C2' -  C1' ANGL. DEV. =  -6.9 DEGREES          
REMARK 500     DG P  14   O4' -  C1' -  N9  ANGL. DEV. =   6.2 DEGREES          
REMARK 500     DT P  16   O4' -  C1' -  N1  ANGL. DEV. =   4.6 DEGREES          
REMARK 500     DT P  16   N3  -  C4  -  O4  ANGL. DEV. =   5.2 DEGREES          
REMARK 500     DT P  16   C5  -  C4  -  O4  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DA P  15   C3' -  O3' -  P   ANGL. DEV. =   7.9 DEGREES          
REMARK 500     DT P  17   O4' -  C1' -  N1  ANGL. DEV. =  -7.4 DEGREES          
REMARK 500     DC P  18   O4' -  C1' -  N1  ANGL. DEV. =  -8.7 DEGREES          
REMARK 500     DG P  19   C3' -  C2' -  C1' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DG P  19   O4' -  C1' -  C2' ANGL. DEV. =  -5.4 DEGREES          
REMARK 500     DA P  21   O4' -  C1' -  N9  ANGL. DEV. =   2.7 DEGREES          
REMARK 500     DT P  22   C3' -  C2' -  C1' ANGL. DEV. =  -6.2 DEGREES          
REMARK 500     DC P  23   C3' -  C2' -  C1' ANGL. DEV. =  -5.6 DEGREES          
REMARK 500     DT P  24   C3' -  C2' -  C1' ANGL. DEV. =  -5.7 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    ILE A  28       57.72    -57.13                                   
REMARK 500    GLU A  29      -71.89    -17.22                                   
REMARK 500    ASN A  35      -59.82    -23.94                                   
REMARK 500    PHE A 119       47.31   -140.35                                   
REMARK 500    PRO A 120      128.41    -37.17                                   
REMARK 500    ASP A 125      -51.42     94.96                                   
REMARK 500    ILE B  28       56.60    -56.97                                   
REMARK 500    GLU B  29      -72.01    -16.15                                   
REMARK 500    ASN B  35      -59.89    -26.62                                   
REMARK 500    ARG B  55      110.67    160.52                                   
REMARK 500    GLU B  56        7.46     45.31                                   
REMARK 500    PHE B  59      154.20    -38.67                                   
REMARK 500    ILE C  28       56.06    -57.26                                   
REMARK 500    GLU C  29      -71.97    -15.82                                   
REMARK 500    ASN C  35      -56.05    -29.46                                   
REMARK 500    LYS C  54      -76.95    -55.88                                   
REMARK 500    GLU C  56     -128.99    -76.92                                   
REMARK 500    PHE C  59     -119.40    -88.00                                   
REMARK 500    ASN C  60       67.81    144.00                                   
REMARK 500    GLN C  61      -51.46    -28.42                                   
REMARK 500    VAL C 102      -58.40   -122.41                                   
REMARK 500    ILE D  28       57.20    -56.60                                   
REMARK 500    GLU D  29      -72.12    -17.06                                   
REMARK 500    ASN D  60       96.81    163.61                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    PHE A 119         10.48                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LYS B  54        24.7      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3ON0 A    1   127  UNP    P33788   TRAM8_ECOLX      1    127             
DBREF  3ON0 B    1   127  UNP    P33788   TRAM8_ECOLX      1    127             
DBREF  3ON0 C    1   127  UNP    P33788   TRAM8_ECOLX      1    127             
DBREF  3ON0 D    1   127  UNP    P33788   TRAM8_ECOLX      1    127             
DBREF  3ON0 P    1    24  PDB    3ON0     3ON0             1     24             
SEQRES   1 A  127  MET PRO LYS ILE GLN THR TYR VAL ASN ASN ASN VAL TYR          
SEQRES   2 A  127  GLU GLN ILE THR ASP LEU VAL THR ILE ARG LYS GLN GLU          
SEQRES   3 A  127  GLY ILE GLU GLU ALA SER LEU SER ASN VAL SER SER MET          
SEQRES   4 A  127  LEU LEU GLU LEU GLY LEU ARG VAL TYR MET ILE GLN GLN          
SEQRES   5 A  127  GLU LYS ARG GLU GLY GLY PHE ASN GLN MET GLU TYR ASN          
SEQRES   6 A  127  LYS LEU MET LEU GLU ASN VAL SER ARG VAL ARG ALA MET          
SEQRES   7 A  127  CYS THR GLU ILE LEU LYS MET SER VAL LEU ASN GLN GLU          
SEQRES   8 A  127  SER ILE ALA SER GLY ASN PHE ASP TYR ALA VAL ILE LYS          
SEQRES   9 A  127  PRO ALA ILE ASP LYS PHE ALA ARG GLU GLN VAL SER ILE          
SEQRES  10 A  127  PHE PHE PRO ASP ASP GLU ASP ASP GLN GLU                      
SEQRES   1 B  127  MET PRO LYS ILE GLN THR TYR VAL ASN ASN ASN VAL TYR          
SEQRES   2 B  127  GLU GLN ILE THR ASP LEU VAL THR ILE ARG LYS GLN GLU          
SEQRES   3 B  127  GLY ILE GLU GLU ALA SER LEU SER ASN VAL SER SER MET          
SEQRES   4 B  127  LEU LEU GLU LEU GLY LEU ARG VAL TYR MET ILE GLN GLN          
SEQRES   5 B  127  GLU LYS ARG GLU GLY GLY PHE ASN GLN MET GLU TYR ASN          
SEQRES   6 B  127  LYS LEU MET LEU GLU ASN VAL SER ARG VAL ARG ALA MET          
SEQRES   7 B  127  CYS THR GLU ILE LEU LYS MET SER VAL LEU ASN GLN GLU          
SEQRES   8 B  127  SER ILE ALA SER GLY ASN PHE ASP TYR ALA VAL ILE LYS          
SEQRES   9 B  127  PRO ALA ILE ASP LYS PHE ALA ARG GLU GLN VAL SER ILE          
SEQRES  10 B  127  PHE PHE PRO ASP ASP GLU ASP ASP GLN GLU                      
SEQRES   1 C  127  MET PRO LYS ILE GLN THR TYR VAL ASN ASN ASN VAL TYR          
SEQRES   2 C  127  GLU GLN ILE THR ASP LEU VAL THR ILE ARG LYS GLN GLU          
SEQRES   3 C  127  GLY ILE GLU GLU ALA SER LEU SER ASN VAL SER SER MET          
SEQRES   4 C  127  LEU LEU GLU LEU GLY LEU ARG VAL TYR MET ILE GLN GLN          
SEQRES   5 C  127  GLU LYS ARG GLU GLY GLY PHE ASN GLN MET GLU TYR ASN          
SEQRES   6 C  127  LYS LEU MET LEU GLU ASN VAL SER ARG VAL ARG ALA MET          
SEQRES   7 C  127  CYS THR GLU ILE LEU LYS MET SER VAL LEU ASN GLN GLU          
SEQRES   8 C  127  SER ILE ALA SER GLY ASN PHE ASP TYR ALA VAL ILE LYS          
SEQRES   9 C  127  PRO ALA ILE ASP LYS PHE ALA ARG GLU GLN VAL SER ILE          
SEQRES  10 C  127  PHE PHE PRO ASP ASP GLU ASP ASP GLN GLU                      
SEQRES   1 D  127  MET PRO LYS ILE GLN THR TYR VAL ASN ASN ASN VAL TYR          
SEQRES   2 D  127  GLU GLN ILE THR ASP LEU VAL THR ILE ARG LYS GLN GLU          
SEQRES   3 D  127  GLY ILE GLU GLU ALA SER LEU SER ASN VAL SER SER MET          
SEQRES   4 D  127  LEU LEU GLU LEU GLY LEU ARG VAL TYR MET ILE GLN GLN          
SEQRES   5 D  127  GLU LYS ARG GLU GLY GLY PHE ASN GLN MET GLU TYR ASN          
SEQRES   6 D  127  LYS LEU MET LEU GLU ASN VAL SER ARG VAL ARG ALA MET          
SEQRES   7 D  127  CYS THR GLU ILE LEU LYS MET SER VAL LEU ASN GLN GLU          
SEQRES   8 D  127  SER ILE ALA SER GLY ASN PHE ASP TYR ALA VAL ILE LYS          
SEQRES   9 D  127  PRO ALA ILE ASP LYS PHE ALA ARG GLU GLN VAL SER ILE          
SEQRES  10 D  127  PHE PHE PRO ASP ASP GLU ASP ASP GLN GLU                      
SEQRES   1 P   24   DA  DG  DA  DT  DT  DC  DG  DA  DA  DT  DC  DT  DA          
SEQRES   2 P   24   DG  DA  DT  DT  DC  DG  DA  DA  DT  DC  DT                  
HELIX    1   1 ASN A    9  GLN A   25  1                                  17    
HELIX    2   2 SER A   32  GLU A   53  1                                  22    
HELIX    3   3 ASN A   60  ASN A   89  1                                  30    
HELIX    4   4 ASN A   89  GLY A   96  1                                   8    
HELIX    5   5 ASP A   99  PHE A  119  1                                  21    
HELIX    6   6 PRO A  120  ASP A  124  5                                   5    
HELIX    7   7 ASN B    9  GLN B   25  1                                  17    
HELIX    8   8 SER B   32  ARG B   55  1                                  24    
HELIX    9   9 ASN B   60  ASN B   89  1                                  30    
HELIX   10  10 ASN B   89  GLY B   96  1                                   8    
HELIX   11  11 ASP B   99  PHE B  119  1                                  21    
HELIX   12  12 ASN C    9  GLN C   25  1                                  17    
HELIX   13  13 SER C   32  GLU C   56  1                                  25    
HELIX   14  14 ASN C   60  ASN C   89  1                                  30    
HELIX   15  15 ASN C   89  GLY C   96  1                                   8    
HELIX   16  16 ASP C   99  PHE C  119  1                                  21    
HELIX   17  17 ASN D    9  GLN D   25  1                                  17    
HELIX   18  18 SER D   32  VAL D   47  1                                  16    
HELIX   19  19 ASN D   60  ASN D   89  1                                  30    
HELIX   20  20 ASN D   89  GLY D   96  1                                   8    
HELIX   21  21 ASP D   99  PHE D  119  1                                  21    
SHEET    1   A 2 LYS A   3  TYR A   7  0                                        
SHEET    2   A 2 LYS D   3  TYR D   7 -1  O  ILE D   4   N  THR A   6           
SHEET    1   B 2 LYS B   3  TYR B   7  0                                        
SHEET    2   B 2 LYS C   3  TYR C   7 -1  O  THR C   6   N  ILE B   4           
CISPEP   1 GLY C   58    PHE C   59          0         5.69                     
CRYST1   93.025  154.687  167.565  90.00  90.00  90.00 C 2 2 21     32          
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      0.010750  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006465  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005968        0.00000                         
ATOM      1  N   PRO A   2      65.176  39.878  12.409  1.00 98.88           N  
ANISOU    1  N   PRO A   2    12137  11869  13562  -5136   3342  -1971       N  
ATOM      2  CA  PRO A   2      64.444  39.726  13.659  1.00 94.53           C  
ANISOU    2  CA  PRO A   2    12009  11088  12821  -4748   2740  -2165       C  
ATOM      3  C   PRO A   2      64.025  38.288  13.901  1.00 90.71           C  
ANISOU    3  C   PRO A   2    11663  10788  12013  -4217   2811  -2330       C  
ATOM      4  O   PRO A   2      63.656  37.572  12.968  1.00 88.98           O  
ANISOU    4  O   PRO A   2    11563  10756  11490  -4151   3257  -2254       O  
ATOM      5  CB  PRO A   2      63.191  40.594  13.454  1.00 91.19           C  
ANISOU    5  CB  PRO A   2    12271  10403  11973  -4858   2681  -1948       C  
ATOM      6  CG  PRO A   2      63.492  41.449  12.282  1.00 94.74           C  
ANISOU    6  CG  PRO A   2    12644  10838  12516  -5390   3089  -1672       C  
ATOM      7  CD  PRO A   2      64.406  40.646  11.423  1.00 98.15           C  
ANISOU    7  CD  PRO A   2    12524  11657  13111  -5435   3667  -1658       C  
ATOM      8  N   LYS A   3      64.060  37.882  15.161  1.00 89.88           N  
ANISOU    8  N   LYS A   3    11623  10576  11952  -3817   2330  -2549       N  
ATOM      9  CA  LYS A   3      63.790  36.505  15.520  1.00 87.49           C  
ANISOU    9  CA  LYS A   3    11450  10382  11409  -3328   2357  -2683       C  
ATOM     10  C   LYS A   3      62.475  36.378  16.256  1.00 82.97           C  
ANISOU   10  C   LYS A   3    11497   9608  10421  -3026   2164  -2571       C  
ATOM     11  O   LYS A   3      62.143  37.195  17.082  1.00 83.03           O  
ANISOU   11  O   LYS A   3    11769   9400  10379  -2942   1803  -2547       O  
ATOM     12  CB  LYS A   3      64.923  35.988  16.394  1.00 90.95           C  
ANISOU   12  CB  LYS A   3    11484  10874  12199  -3022   2009  -2997       C  
ATOM     13  CG  LYS A   3      64.636  34.668  17.044  1.00 89.09           C  
ANISOU   13  CG  LYS A   3    11517  10638  11696  -2461   1911  -3131       C  
ATOM     14  CD  LYS A   3      65.879  34.152  17.733  1.00 93.39           C  
ANISOU   14  CD  LYS A   3    11638  11262  12585  -2132   1576  -3473       C  
ATOM     15  CE  LYS A   3      65.555  33.011  18.668  1.00 91.63           C  
ANISOU   15  CE  LYS A   3    11844  10918  12054  -1517   1353  -3591       C  
ATOM     16  NZ  LYS A   3      66.541  32.979  19.766  1.00 96.54           N  
ANISOU   16  NZ  LYS A   3    12272  11465  12946  -1130    769  -3927       N  
ATOM     17  N   ILE A   4      61.721  35.342  15.961  1.00 80.34           N  
ANISOU   17  N   ILE A   4    11393   9333   9800  -2841   2401  -2488       N  
ATOM     18  CA  ILE A   4      60.464  35.146  16.648  1.00 77.42           C  
ANISOU   18  CA  ILE A   4    11489   8810   9119  -2580   2300  -2305       C  
ATOM     19  C   ILE A   4      60.442  33.828  17.385  1.00 77.32           C  
ANISOU   19  C   ILE A   4    11580   8763   9034  -2145   2232  -2370       C  
ATOM     20  O   ILE A   4      60.836  32.785  16.838  1.00 78.19           O  
ANISOU   20  O   ILE A   4    11553   8961   9194  -2109   2390  -2480       O  
ATOM     21  CB  ILE A   4      59.301  35.140  15.662  1.00 75.17           C  
ANISOU   21  CB  ILE A   4    11418   8538   8607  -2810   2590  -2056       C  
ATOM     22  CG1 ILE A   4      59.010  36.567  15.195  1.00 75.56           C  
ANISOU   22  CG1 ILE A   4    11564   8538   8608  -3131   2590  -1933       C  
ATOM     23  CG2 ILE A   4      58.062  34.512  16.291  1.00 72.72           C  
ANISOU   23  CG2 ILE A   4    11410   8127   8093  -2538   2568  -1837       C  
ATOM     24  CD1 ILE A   4      57.762  36.657  14.331  1.00 73.37           C  
ANISOU   24  CD1 ILE A   4    11545   8252   8081  -3275   2774  -1708       C  
ATOM     25  N   GLN A   5      59.963  33.874  18.621  1.00 76.89           N  
ANISOU   25  N   GLN A   5    11841   8560   8814  -1762   2006  -2284       N  
ATOM     26  CA  GLN A   5      59.757  32.671  19.404  1.00 77.02           C  
ANISOU   26  CA  GLN A   5    12075   8486   8701  -1333   1986  -2240       C  
ATOM     27  C   GLN A   5      58.259  32.434  19.529  1.00 75.30           C  
ANISOU   27  C   GLN A   5    12157   8195   8260  -1306   2215  -1824       C  
ATOM     28  O   GLN A   5      57.576  33.220  20.166  1.00 75.21           O  
ANISOU   28  O   GLN A   5    12365   8151   8061  -1141   2178  -1630       O  
ATOM     29  CB  GLN A   5      60.407  32.842  20.782  1.00 79.08           C  
ANISOU   29  CB  GLN A   5    12503   8632   8914   -825   1580  -2426       C  
ATOM     30  CG  GLN A   5      61.895  33.169  20.726  1.00 81.42           C  
ANISOU   30  CG  GLN A   5    12386   8994   9557   -878   1260  -2841       C  
ATOM     31  CD  GLN A   5      62.477  33.575  22.077  1.00 84.62           C  
ANISOU   31  CD  GLN A   5    12996   9221   9935   -383    696  -3069       C  
ATOM     32  OE1 GLN A   5      62.459  32.806  23.017  1.00 85.59           O  
ANISOU   32  OE1 GLN A   5    13466   9227   9828    172    551  -3097       O  
ATOM     33  NE2 GLN A   5      63.013  34.789  22.165  1.00 86.59           N  
ANISOU   33  NE2 GLN A   5    13080   9400  10419   -572    330  -3234       N  
ATOM     34  N   THR A   6      57.736  31.392  18.896  1.00 74.88           N  
ANISOU   34  N   THR A   6    12096   8107   8250  -1459   2426  -1683       N  
ATOM     35  CA  THR A   6      56.336  31.030  19.109  1.00 75.13           C  
ANISOU   35  CA  THR A   6    12301   8045   8199  -1456   2612  -1250       C  
ATOM     36  C   THR A   6      56.200  29.706  19.816  1.00 77.36           C  
ANISOU   36  C   THR A   6    12779   8136   8477  -1175   2648  -1093       C  
ATOM     37  O   THR A   6      56.892  28.736  19.494  1.00 78.49           O  
ANISOU   37  O   THR A   6    12919   8186   8718  -1163   2562  -1314       O  
ATOM     38  CB  THR A   6      55.567  30.814  17.822  1.00 74.08           C  
ANISOU   38  CB  THR A   6    12039   7914   8192  -1910   2745  -1132       C  
ATOM     39  OG1 THR A   6      56.497  30.573  16.769  1.00 74.74           O  
ANISOU   39  OG1 THR A   6    11989   8052   8358  -2108   2706  -1481       O  
ATOM     40  CG2 THR A   6      54.696  31.981  17.505  1.00 72.89           C  
ANISOU   40  CG2 THR A   6    11854   7873   7969  -2090   2809   -949       C  
ATOM     41  N   TYR A   7      55.259  29.651  20.746  1.00 78.60           N  
ANISOU   41  N   TYR A   7    13131   8228   8506   -929   2808   -671       N  
ATOM     42  CA  TYR A   7      54.961  28.416  21.408  1.00 81.19           C  
ANISOU   42  CA  TYR A   7    13677   8331   8842   -716   2918   -392       C  
ATOM     43  C   TYR A   7      53.730  27.833  20.768  1.00 81.81           C  
ANISOU   43  C   TYR A   7    13591   8301   9193  -1146   3115     18       C  
ATOM     44  O   TYR A   7      52.627  28.307  20.986  1.00 82.37           O  
ANISOU   44  O   TYR A   7    13547   8469   9280  -1191   3345    434       O  
ATOM     45  CB  TYR A   7      54.803  28.671  22.894  1.00 83.44           C  
ANISOU   45  CB  TYR A   7    14307   8602   8794   -107   3013   -149       C  
ATOM     46  CG  TYR A   7      56.082  29.241  23.446  1.00 84.57           C  
ANISOU   46  CG  TYR A   7    14607   8787   8737    296   2649   -641       C  
ATOM     47  CD1 TYR A   7      57.081  28.412  23.911  1.00 87.11           C  
ANISOU   47  CD1 TYR A   7    15127   8952   9017    628   2417   -915       C  
ATOM     48  CD2 TYR A   7      56.324  30.608  23.437  1.00 84.25           C  
ANISOU   48  CD2 TYR A   7    14499   8908   8605    316   2464   -858       C  
ATOM     49  CE1 TYR A   7      58.262  28.921  24.392  1.00 88.98           C  
ANISOU   49  CE1 TYR A   7    15420   9221   9167    978   2002  -1388       C  
ATOM     50  CE2 TYR A   7      57.512  31.127  23.919  1.00 85.54           C  
ANISOU   50  CE2 TYR A   7    14746   9051   8706    613   2033  -1313       C  
ATOM     51  CZ  TYR A   7      58.476  30.275  24.391  1.00 88.22           C  
ANISOU   51  CZ  TYR A   7    15203   9264   9053    937   1796  -1581       C  
ATOM     52  OH  TYR A   7      59.661  30.765  24.871  1.00 90.76           O  
ANISOU   52  OH  TYR A   7    15529   9559   9397   1228   1293  -2050       O  
ATOM     53  N   VAL A   8      53.942  26.815  19.939  1.00 82.56           N  
ANISOU   53  N   VAL A   8    13663   8186   9519  -1436   2972   -127       N  
ATOM     54  CA  VAL A   8      52.862  26.150  19.222  1.00 84.15           C  
ANISOU   54  CA  VAL A   8    13726   8184  10064  -1888   2991    185       C  
ATOM     55  C   VAL A   8      52.505  24.811  19.843  1.00 88.44           C  
ANISOU   55  C   VAL A   8    14481   8341  10782  -1846   3040    555       C  
ATOM     56  O   VAL A   8      53.218  24.307  20.711  1.00 89.83           O  
ANISOU   56  O   VAL A   8    14982   8400  10748  -1429   3044    499       O  
ATOM     57  CB  VAL A   8      53.273  25.888  17.795  1.00 82.93           C  
ANISOU   57  CB  VAL A   8    13521   7967  10023  -2212   2717   -234       C  
ATOM     58  CG1 VAL A   8      53.700  27.179  17.165  1.00 79.89           C  
ANISOU   58  CG1 VAL A   8    12969   7929   9458  -2268   2724   -547       C  
ATOM     59  CG2 VAL A   8      54.415  24.911  17.775  1.00 84.20           C  
ANISOU   59  CG2 VAL A   8    13944   7947  10101  -1976   2527   -598       C  
ATOM     60  N   ASN A   9      51.402  24.233  19.383  1.00 91.23           N  
ANISOU   60  N   ASN A   9    14657   8457  11548  -2288   3033    936       N  
ATOM     61  CA  ASN A   9      50.986  22.929  19.865  1.00 96.43           C  
ANISOU   61  CA  ASN A   9    15496   8661  12480  -2376   3054   1353       C  
ATOM     62  C   ASN A   9      51.688  21.796  19.126  1.00 97.67           C  
ANISOU   62  C   ASN A   9    15975   8405  12729  -2481   2608    950       C  
ATOM     63  O   ASN A   9      52.376  22.028  18.134  1.00 94.73           O  
ANISOU   63  O   ASN A   9    15620   8148  12224  -2500   2334    383       O  
ATOM     64  CB  ASN A   9      49.463  22.769  19.810  1.00100.33           C  
ANISOU   64  CB  ASN A   9    15588   9038  13493  -2835   3221   2014       C  
ATOM     65  CG  ASN A   9      48.923  22.776  18.400  1.00100.72           C  
ANISOU   65  CG  ASN A   9    15357   8982  13930  -3379   2813   1812       C  
ATOM     66  OD1 ASN A   9      49.520  22.208  17.484  1.00101.64           O  
ANISOU   66  OD1 ASN A   9    15731   8837  14050  -3495   2365   1332       O  
ATOM     67  ND2 ASN A   9      47.780  23.413  18.218  1.00101.55           N  
ANISOU   67  ND2 ASN A   9    14966   9291  14329  -3643   2946   2167       N  
ATOM     68  N   ASN A  10      51.515  20.573  19.623  1.00102.57           N  
ANISOU   68  N   ASN A  10    16893   8534  13544  -2505   2560   1268       N  
ATOM     69  CA  ASN A  10      52.236  19.436  19.077  1.00104.66           C  
ANISOU   69  CA  ASN A  10    17592   8356  13819  -2473   2107    878       C  
ATOM     70  C   ASN A  10      51.880  19.156  17.627  1.00105.49           C  
ANISOU   70  C   ASN A  10    17617   8237  14227  -2928   1644    610       C  
ATOM     71  O   ASN A  10      52.739  18.777  16.829  1.00104.85           O  
ANISOU   71  O   ASN A  10    17835   8068  13936  -2746   1289     31       O  
ATOM     72  CB  ASN A  10      52.032  18.199  19.944  1.00110.37           C  
ANISOU   72  CB  ASN A  10    18724   8515  14697  -2425   2129   1336       C  
ATOM     73  CG  ASN A  10      52.842  18.251  21.213  1.00110.12           C  
ANISOU   73  CG  ASN A  10    19044   8622  14174  -1755   2404   1339       C  
ATOM     74  OD1 ASN A  10      54.009  18.630  21.202  1.00106.50           O  
ANISOU   74  OD1 ASN A  10    18708   8458  13300  -1287   2277    744       O  
ATOM     75  ND2 ASN A  10      52.229  17.867  22.319  1.00115.05           N  
ANISOU   75  ND2 ASN A  10    19828   9028  14856  -1684   2776   2028       N  
ATOM     76  N   ASN A  11      50.614  19.349  17.286  1.00107.61           N  
ANISOU   76  N   ASN A  11    17491   8426  14970  -3454   1635   1024       N  
ATOM     77  CA  ASN A  11      50.185  19.234  15.901  1.00109.05           C  
ANISOU   77  CA  ASN A  11    17609   8407  15418  -3844   1127    750       C  
ATOM     78  C   ASN A  11      51.036  20.060  14.966  1.00104.04           C  
ANISOU   78  C   ASN A  11    17026   8203  14302  -3582   1052     83       C  
ATOM     79  O   ASN A  11      51.783  19.534  14.140  1.00104.76           O  
ANISOU   79  O   ASN A  11    17513   8115  14174  -3398    691   -433       O  
ATOM     80  CB  ASN A  11      48.770  19.738  15.765  1.00110.91           C  
ANISOU   80  CB  ASN A  11    17262   8709  16171  -4345   1196   1245       C  
ATOM     81  CG  ASN A  11      47.777  18.642  15.819  1.00120.07           C  
ANISOU   81  CG  ASN A  11    18344   9219  18057  -4865    901   1752       C  
ATOM     82  OD1 ASN A  11      48.114  17.487  16.101  1.00125.54           O  
ANISOU   82  OD1 ASN A  11    19491   9363  18845  -4853    687   1803       O  
ATOM     83  ND2 ASN A  11      46.528  18.979  15.543  1.00125.03           N  
ANISOU   83  ND2 ASN A  11    18383   9870  19254  -5341    848   2146       N  
ATOM     84  N   VAL A  12      50.880  21.372  15.094  1.00 99.65           N  
ANISOU   84  N   VAL A  12    16080   8205  13577  -3548   1418    135       N  
ATOM     85  CA  VAL A  12      51.638  22.318  14.308  1.00 95.31           C  
ANISOU   85  CA  VAL A  12    15525   8083  12605  -3354   1451   -378       C  
ATOM     86  C   VAL A  12      53.101  21.895  14.234  1.00 94.61           C  
ANISOU   86  C   VAL A  12    15789   8037  12123  -2906   1414   -881       C  
ATOM     87  O   VAL A  12      53.662  21.758  13.150  1.00 95.03           O  
ANISOU   87  O   VAL A  12    16051   8087  11969  -2802   1197  -1331       O  
ATOM     88  CB  VAL A  12      51.532  23.739  14.911  1.00 91.45           C  
ANISOU   88  CB  VAL A  12    14676   8140  11933  -3260   1898   -215       C  
ATOM     89  CG1 VAL A  12      52.422  24.709  14.165  1.00 87.39           C  
ANISOU   89  CG1 VAL A  12    14171   8011  11023  -3103   1955   -696       C  
ATOM     90  CG2 VAL A  12      50.083  24.216  14.914  1.00 92.54           C  
ANISOU   90  CG2 VAL A  12    14424   8309  12428  -3615   1951    256       C  
ATOM     91  N   TYR A  13      53.718  21.679  15.388  1.00 94.23           N  
ANISOU   91  N   TYR A  13    15817   8039  11949  -2577   1628   -802       N  
ATOM     92  CA  TYR A  13      55.127  21.321  15.434  1.00 94.12           C  
ANISOU   92  CA  TYR A  13    16040   8115  11605  -2100   1583  -1275       C  
ATOM     93  C   TYR A  13      55.443  20.108  14.560  1.00 98.11           C  
ANISOU   93  C   TYR A  13    16980   8201  12096  -2010   1162  -1596       C  
ATOM     94  O   TYR A  13      56.374  20.128  13.755  1.00 97.88           O  
ANISOU   94  O   TYR A  13    17043   8368  11779  -1723   1104  -2084       O  
ATOM     95  CB  TYR A  13      55.554  21.047  16.868  1.00 94.58           C  
ANISOU   95  CB  TYR A  13    16216   8145  11574  -1739   1742  -1104       C  
ATOM     96  CG  TYR A  13      57.044  21.036  17.037  1.00 93.82           C  
ANISOU   96  CG  TYR A  13    16190   8291  11166  -1213   1713  -1610       C  
ATOM     97  CD1 TYR A  13      57.748  19.849  17.139  1.00 96.87           C  
ANISOU   97  CD1 TYR A  13    16979   8372  11457   -844   1459  -1849       C  
ATOM     98  CD2 TYR A  13      57.751  22.217  17.086  1.00 90.80           C  
ANISOU   98  CD2 TYR A  13    15448   8424  10629  -1086   1902  -1845       C  
ATOM     99  CE1 TYR A  13      59.112  19.847  17.287  1.00 97.24           C  
ANISOU   99  CE1 TYR A  13    16995   8688  11264   -325   1419  -2320       C  
ATOM    100  CE2 TYR A  13      59.111  22.225  17.236  1.00 91.02           C  
ANISOU  100  CE2 TYR A  13    15406   8687  10489   -649   1850  -2285       C  
ATOM    101  CZ  TYR A  13      59.785  21.040  17.333  1.00 94.66           C  
ANISOU  101  CZ  TYR A  13    16198   8905  10863   -252   1620  -2526       C  
ATOM    102  OH  TYR A  13      61.144  21.064  17.481  1.00 96.65           O  
ANISOU  102  OH  TYR A  13    16289   9440  10992    220   1558  -2971       O  
ATOM    103  N   GLU A  14      54.672  19.043  14.728  1.00102.39           N  
ANISOU  103  N   GLU A  14    17802   8147  12952  -2232    870  -1299       N  
ATOM    104  CA  GLU A  14      54.896  17.860  13.928  1.00107.25           C  
ANISOU  104  CA  GLU A  14    18938   8256  13555  -2128    360  -1608       C  
ATOM    105  C   GLU A  14      54.868  18.229  12.458  1.00106.87           C  
ANISOU  105  C   GLU A  14    18921   8327  13358  -2186    151  -1988       C  
ATOM    106  O   GLU A  14      55.790  17.908  11.707  1.00108.57           O  
ANISOU  106  O   GLU A  14    19452   8604  13195  -1749     17  -2493       O  
ATOM    107  CB  GLU A  14      53.836  16.799  14.206  1.00112.49           C  
ANISOU  107  CB  GLU A  14    19844   8178  14719  -2537      5  -1155       C  
ATOM    108  CG  GLU A  14      54.285  15.699  15.127  1.00117.18           C  
ANISOU  108  CG  GLU A  14    20896   8341  15288  -2252    -81  -1046       C  
ATOM    109  CD  GLU A  14      53.748  14.372  14.666  1.00126.04           C  
ANISOU  109  CD  GLU A  14    22542   8594  16754  -2506   -723   -978       C  
ATOM    110  OE1 GLU A  14      52.896  14.383  13.753  1.00128.12           O  
ANISOU  110  OE1 GLU A  14    22716   8609  17354  -2962  -1093   -950       O  
ATOM    111  OE2 GLU A  14      54.175  13.317  15.189  1.00131.49           O  
ANISOU  111  OE2 GLU A  14    23775   8802  17383  -2239   -929   -974       O  
ATOM    112  N   GLN A  15      53.800  18.907  12.056  1.00105.37           N  
ANISOU  112  N   GLN A  15    18420   8182  13431  -2663    140  -1731       N  
ATOM    113  CA  GLN A  15      53.591  19.237  10.653  1.00105.44           C  
ANISOU  113  CA  GLN A  15    18551   8217  13292  -2719   -125  -2045       C  
ATOM    114  C   GLN A  15      54.800  19.924  10.057  1.00102.46           C  
ANISOU  114  C   GLN A  15    18183   8405  12342  -2258    214  -2501       C  
ATOM    115  O   GLN A  15      55.207  19.634   8.929  1.00104.84           O  
ANISOU  115  O   GLN A  15    18885   8639  12309  -1966     -9  -2908       O  
ATOM    116  CB  GLN A  15      52.382  20.144  10.501  1.00103.84           C  
ANISOU  116  CB  GLN A  15    17908   8139  13407  -3218    -79  -1696       C  
ATOM    117  CG  GLN A  15      51.148  19.623  11.186  1.00107.38           C  
ANISOU  117  CG  GLN A  15    18134   8153  14515  -3712   -270  -1133       C  
ATOM    118  CD  GLN A  15      49.891  20.072  10.481  1.00109.71           C  
ANISOU  118  CD  GLN A  15    18149   8352  15184  -4161   -576   -964       C  
ATOM    119  OE1 GLN A  15      49.005  20.674  11.085  1.00109.52           O  
ANISOU  119  OE1 GLN A  15    17575   8524  15514  -4472   -310   -484       O  
ATOM    120  NE2 GLN A  15      49.814  19.796   9.185  1.00112.78           N  
ANISOU  120  NE2 GLN A  15    18942   8451  15459  -4119  -1154  -1377       N  
ATOM    121  N   ILE A  16      55.371  20.839  10.826  1.00 97.69           N  
ANISOU  121  N   ILE A  16    17142   8341  11634  -2175    751  -2410       N  
ATOM    122  CA  ILE A  16      56.491  21.617  10.346  1.00 95.56           C  
ANISOU  122  CA  ILE A  16    16725   8625  10959  -1853   1123  -2744       C  
ATOM    123  C   ILE A  16      57.743  20.767  10.257  1.00 98.28           C  
ANISOU  123  C   ILE A  16    17328   8988  11026  -1281   1096  -3142       C  
ATOM    124  O   ILE A  16      58.368  20.696   9.203  1.00100.55           O  
ANISOU  124  O   ILE A  16    17819   9426  10960   -951   1131  -3489       O  
ATOM    125  CB  ILE A  16      56.748  22.837  11.242  1.00 91.21           C  
ANISOU  125  CB  ILE A  16    15638   8562  10455  -1957   1586  -2545       C  
ATOM    126  CG1 ILE A  16      55.443  23.610  11.438  1.00 89.04           C  
ANISOU  126  CG1 ILE A  16    15140   8259  10431  -2430   1603  -2134       C  
ATOM    127  CG2 ILE A  16      57.836  23.714  10.651  1.00 90.00           C  
ANISOU  127  CG2 ILE A  16    15262   8931  10004  -1756   1950  -2825       C  
ATOM    128  CD1 ILE A  16      55.635  25.005  11.880  1.00 85.20           C  
ANISOU  128  CD1 ILE A  16    14263   8232   9876  -2502   1982  -2026       C  
ATOM    129  N   THR A  17      58.112  20.119  11.357  1.00 98.54           N  
ANISOU  129  N   THR A  17    17385   8878  11179  -1093   1049  -3085       N  
ATOM    130  CA  THR A  17      59.317  19.298  11.349  1.00101.73           C  
ANISOU  130  CA  THR A  17    18018   9311  11324   -480    988  -3481       C  
ATOM    131  C   THR A  17      59.198  18.268  10.232  1.00106.50           C  
ANISOU  131  C   THR A  17    19262   9483  11719   -243    552  -3766       C  
ATOM    132  O   THR A  17      60.190  17.875   9.620  1.00109.68           O  
ANISOU  132  O   THR A  17    19861  10061  11749    340    584  -4179       O  
ATOM    133  CB  THR A  17      59.563  18.598  12.693  1.00102.34           C  
ANISOU  133  CB  THR A  17    18192   9153  11540   -285    877  -3365       C  
ATOM    134  OG1 THR A  17      58.436  17.781  13.008  1.00105.21           O  
ANISOU  134  OG1 THR A  17    18941   8851  12185   -620    519  -3018       O  
ATOM    135  CG2 THR A  17      59.757  19.615  13.805  1.00 97.87           C  
ANISOU  135  CG2 THR A  17    17101   8991  11092   -384   1235  -3149       C  
ATOM    136  N   ASP A  18      57.968  17.851   9.961  1.00107.68           N  
ANISOU  136  N   ASP A  18    19726   9065  12124   -669    120  -3544       N  
ATOM    137  CA  ASP A  18      57.696  16.963   8.840  1.00112.88           C  
ANISOU  137  CA  ASP A  18    21058   9215  12615   -492   -438  -3825       C  
ATOM    138  C   ASP A  18      58.056  17.638   7.528  1.00113.18           C  
ANISOU  138  C   ASP A  18    21147   9662  12196   -233   -237  -4133       C  
ATOM    139  O   ASP A  18      58.655  17.028   6.643  1.00117.69           O  
ANISOU  139  O   ASP A  18    22247  10155  12316    357   -416  -4548       O  
ATOM    140  CB  ASP A  18      56.222  16.554   8.817  1.00114.68           C  
ANISOU  140  CB  ASP A  18    21467   8761  13345  -1116   -985  -3484       C  
ATOM    141  CG  ASP A  18      55.949  15.300   9.626  1.00118.90           C  
ANISOU  141  CG  ASP A  18    22361   8598  14220  -1198  -1412  -3295       C  
ATOM    142  OD1 ASP A  18      54.785  14.855   9.652  1.00122.41           O  
ANISOU  142  OD1 ASP A  18    22900   8432  15177  -1747  -1871  -2968       O  
ATOM    143  OD2 ASP A  18      56.893  14.750  10.232  1.00120.22           O  
ANISOU  143  OD2 ASP A  18    22707   8803  14170   -718  -1306  -3456       O  
ATOM    144  N   LEU A  19      57.680  18.903   7.404  1.00108.98           N  
ANISOU  144  N   LEU A  19    20121   9551  11735   -623    150  -3911       N  
ATOM    145  CA  LEU A  19      57.972  19.650   6.196  1.00109.60           C  
ANISOU  145  CA  LEU A  19    20265  10008  11369   -416    414  -4115       C  
ATOM    146  C   LEU A  19      59.458  19.794   5.972  1.00111.01           C  
ANISOU  146  C   LEU A  19    20295  10764  11119    198    956  -4399       C  
ATOM    147  O   LEU A  19      59.931  19.634   4.853  1.00115.52           O  
ANISOU  147  O   LEU A  19    21266  11446  11182    705   1024  -4692       O  
ATOM    148  CB  LEU A  19      57.306  21.015   6.219  1.00104.93           C  
ANISOU  148  CB  LEU A  19    19190   9727  10950   -956    724  -3792       C  
ATOM    149  CG  LEU A  19      55.902  20.957   5.622  1.00106.13           C  
ANISOU  149  CG  LEU A  19    19637   9390  11296  -1344    160  -3675       C  
ATOM    150  CD1 LEU A  19      55.189  22.282   5.823  1.00101.24           C  
ANISOU  150  CD1 LEU A  19    18513   9073  10879  -1842    442  -3334       C  
ATOM    151  CD2 LEU A  19      55.972  20.580   4.142  1.00110.88           C  
ANISOU  151  CD2 LEU A  19    20965   9784  11381   -897   -174  -4066       C  
ATOM    152  N   VAL A  20      60.196  20.093   7.029  1.00108.14           N  
ANISOU  152  N   VAL A  20    19354  10774  10960    195   1332  -4306       N  
ATOM    153  CA  VAL A  20      61.634  20.196   6.904  1.00110.47           C  
ANISOU  153  CA  VAL A  20    19359  11630  10985    750   1810  -4557       C  
ATOM    154  C   VAL A  20      62.178  18.907   6.319  1.00117.14           C  
ANISOU  154  C   VAL A  20    20836  12238  11433   1494   1515  -4961       C  
ATOM    155  O   VAL A  20      62.911  18.919   5.331  1.00121.58           O  
ANISOU  155  O   VAL A  20    21533  13139  11524   2046   1824  -5204       O  
ATOM    156  CB  VAL A  20      62.293  20.439   8.246  1.00107.68           C  
ANISOU  156  CB  VAL A  20    18390  11549  10974    696   2010  -4465       C  
ATOM    157  CG1 VAL A  20      63.755  20.801   8.049  1.00110.16           C  
ANISOU  157  CG1 VAL A  20    18188  12526  11141   1155   2534  -4680       C  
ATOM    158  CG2 VAL A  20      61.567  21.545   8.977  1.00101.78           C  
ANISOU  158  CG2 VAL A  20    17202  10873  10598     16   2136  -4072       C  
ATOM    159  N   THR A  21      61.812  17.787   6.930  1.00118.74           N  
ANISOU  159  N   THR A  21    21473  11840  11803   1545    932  -5009       N  
ATOM    160  CA  THR A  21      62.199  16.484   6.408  1.00125.53           C  
ANISOU  160  CA  THR A  21    23085  12325  12286   2254    502  -5406       C  
ATOM    161  C   THR A  21      61.865  16.396   4.927  1.00130.05           C  
ANISOU  161  C   THR A  21    24293  12743  12377   2528    328  -5618       C  
ATOM    162  O   THR A  21      62.741  16.178   4.091  1.00135.00           O  
ANISOU  162  O   THR A  21    25170  13686  12439   3302    572  -5948       O  
ATOM    163  CB  THR A  21      61.465  15.352   7.135  1.00126.50           C  
ANISOU  163  CB  THR A  21    23733  11607  12726   2058   -228  -5324       C  
ATOM    164  OG1 THR A  21      61.786  15.399   8.530  1.00123.34           O  
ANISOU  164  OG1 THR A  21    22863  11329  12673   1912    -57  -5122       O  
ATOM    165  CG2 THR A  21      61.872  14.010   6.572  1.00133.53           C  
ANISOU  165  CG2 THR A  21    25502  12029  13203   2819   -758  -5764       C  
ATOM    166  N   ILE A  22      60.589  16.572   4.606  1.00129.16           N  
ANISOU  166  N   ILE A  22    24446  12154  12476   1945    -98  -5424       N  
ATOM    167  CA  ILE A  22      60.148  16.489   3.224  1.00134.10           C  
ANISOU  167  CA  ILE A  22    25769  12534  12649   2206   -410  -5644       C  
ATOM    168  C   ILE A  22      61.121  17.216   2.308  1.00136.65           C  
ANISOU  168  C   ILE A  22    25963  13613  12345   2786    354  -5794       C  
ATOM    169  O   ILE A  22      61.547  16.675   1.291  1.00143.13           O  
ANISOU  169  O   ILE A  22    27482  14386  12514   3583    260  -6153       O  
ATOM    170  CB  ILE A  22      58.746  17.102   3.027  1.00131.12           C  
ANISOU  170  CB  ILE A  22    25348  11830  12642   1419   -743  -5349       C  
ATOM    171  CG1 ILE A  22      57.707  16.371   3.877  1.00130.37           C  
ANISOU  171  CG1 ILE A  22    25308  10988  13239    806  -1448  -5114       C  
ATOM    172  CG2 ILE A  22      58.354  17.060   1.551  1.00135.83           C  
ANISOU  172  CG2 ILE A  22    26730  12176  12702   1789  -1119  -5630       C  
ATOM    173  CD1 ILE A  22      57.425  14.965   3.404  1.00136.56           C  
ANISOU  173  CD1 ILE A  22    27043  10906  13937   1138  -2383  -5433       C  
ATOM    174  N   ARG A  23      61.468  18.445   2.675  1.00132.42           N  
ANISOU  174  N   ARG A  23    24560  13752  12002   2402   1115  -5493       N  
ATOM    175  CA  ARG A  23      62.280  19.299   1.821  1.00135.28           C  
ANISOU  175  CA  ARG A  23    24698  14815  11887   2769   1916  -5496       C  
ATOM    176  C   ARG A  23      63.677  18.739   1.599  1.00141.16           C  
ANISOU  176  C   ARG A  23    25408  16011  12217   3679   2344  -5783       C  
ATOM    177  O   ARG A  23      64.045  18.420   0.469  1.00147.82           O  
ANISOU  177  O   ARG A  23    26855  16943  12366   4446   2476  -6025       O  
ATOM    178  CB  ARG A  23      62.364  20.699   2.401  1.00129.68           C  
ANISOU  178  CB  ARG A  23    23049  14632  11593   2085   2545  -5091       C  
ATOM    179  CG  ARG A  23      61.013  21.327   2.717  1.00125.99           C  
ANISOU  179  CG  ARG A  23    22532  13803  11537   1249   2184  -4791       C  
ATOM    180  CD  ARG A  23      60.421  22.015   1.499  1.00130.55           C  
ANISOU  180  CD  ARG A  23    23539  14360  11704   1224   2241  -4743       C  
ATOM    181  NE  ARG A  23      59.796  23.289   1.812  1.00127.09           N  
ANISOU  181  NE  ARG A  23    22619  14075  11593    506   2456  -4372       N  
ATOM    182  CZ  ARG A  23      58.902  23.937   1.066  1.00127.65           C  
ANISOU  182  CZ  ARG A  23    23024  13985  11495    284   2301  -4270       C  
ATOM    183  NH1 ARG A  23      58.448  23.445  -0.082  1.00132.33           N  
ANISOU  183  NH1 ARG A  23    24472  14214  11593    702   1867  -4518       N  
ATOM    184  NH2 ARG A  23      58.447  25.100   1.502  1.00123.44           N  
ANISOU  184  NH2 ARG A  23    22002  13625  11274   -319   2522  -3938       N  
ATOM    185  N   LYS A  24      64.464  18.622   2.661  1.00139.55           N  
ANISOU  185  N   LYS A  24    24515  16107  12400   3672   2558  -5766       N  
ATOM    186  CA  LYS A  24      65.795  18.040   2.522  1.00145.92           C  
ANISOU  186  CA  LYS A  24    25199  17363  12881   4574   2915  -6055       C  
ATOM    187  C   LYS A  24      65.730  16.853   1.576  1.00153.25           C  
ANISOU  187  C   LYS A  24    27255  17854  13118   5459   2433  -6471       C  
ATOM    188  O   LYS A  24      66.604  16.648   0.732  1.00160.18           O  
ANISOU  188  O   LYS A  24    28310  19167  13385   6358   2887  -6681       O  
ATOM    189  CB  LYS A  24      66.325  17.564   3.865  1.00143.89           C  
ANISOU  189  CB  LYS A  24    24449  17113  13111   4551   2729  -6117       C  
ATOM    190  CG  LYS A  24      66.392  18.639   4.902  1.00137.95           C  
ANISOU  190  CG  LYS A  24    22705  16695  13013   3774   3051  -5771       C  
ATOM    191  CD  LYS A  24      67.262  18.215   6.054  1.00138.86           C  
ANISOU  191  CD  LYS A  24    22318  16981  13462   4024   2979  -5909       C  
ATOM    192  CE  LYS A  24      66.912  19.020   7.281  1.00133.51           C  
ANISOU  192  CE  LYS A  24    21027  16287  13413   3227   2933  -5598       C  
ATOM    193  NZ  LYS A  24      67.929  18.870   8.346  1.00136.02           N  
ANISOU  193  NZ  LYS A  24    20740  16897  14047   3508   2938  -5739       N  
ATOM    194  N   GLN A  25      64.675  16.068   1.740  1.00152.44           N  
ANISOU  194  N   GLN A  25    27918  16867  13137   5209   1492  -6571       N  
ATOM    195  CA  GLN A  25      64.461  14.875   0.948  1.00159.58           C  
ANISOU  195  CA  GLN A  25    30008  17146  13478   5956    785  -6990       C  
ATOM    196  C   GLN A  25      64.201  15.235  -0.510  1.00164.05           C  
ANISOU  196  C   GLN A  25    31219  17763  13351   6358    913  -7084       C  
ATOM    197  O   GLN A  25      64.269  14.379  -1.390  1.00171.60           O  
ANISOU  197  O   GLN A  25    33206  18363  13632   7233    478  -7485       O  
ATOM    198  CB  GLN A  25      63.282  14.096   1.525  1.00157.56           C  
ANISOU  198  CB  GLN A  25    30289  15874  13703   5365   -272  -6969       C  
ATOM    199  CG  GLN A  25      63.320  12.622   1.246  1.00165.40           C  
ANISOU  199  CG  GLN A  25    32372  16130  14344   6098  -1121  -7414       C  
ATOM    200  CD  GLN A  25      62.608  11.815   2.313  1.00163.89           C  
ANISOU  200  CD  GLN A  25    32346  15106  14818   5492  -1914  -7286       C  
ATOM    201  OE1 GLN A  25      62.391  12.287   3.434  1.00156.54           O  
ANISOU  201  OE1 GLN A  25    30619  14321  14538   4725  -1663  -6890       O  
ATOM    202  NE2 GLN A  25      62.251  10.577   1.971  1.00170.95           N  
ANISOU  202  NE2 GLN A  25    34334  15087  15530   5872  -2884  -7607       N  
ATOM    203  N   GLU A  26      63.907  16.506  -0.762  1.00160.05           N  
ANISOU  203  N   GLU A  26    30185  17666  12961   5776   1478  -6725       N  
ATOM    204  CA  GLU A  26      63.695  16.991  -2.123  1.00164.42           C  
ANISOU  204  CA  GLU A  26    31335  18320  12816   6160   1701  -6757       C  
ATOM    205  C   GLU A  26      64.908  17.764  -2.633  1.00167.98           C  
ANISOU  205  C   GLU A  26    31223  19768  12835   6678   2941  -6599       C  
ATOM    206  O   GLU A  26      64.789  18.608  -3.523  1.00169.67           O  
ANISOU  206  O   GLU A  26    31579  20251  12635   6716   3439  -6408       O  
ATOM    207  CB  GLU A  26      62.455  17.883  -2.192  1.00158.63           C  
ANISOU  207  CB  GLU A  26    30536  17294  12444   5212   1441  -6452       C  
ATOM    208  CG  GLU A  26      61.143  17.146  -2.033  1.00157.93           C  
ANISOU  208  CG  GLU A  26    31088  16204  12712   4779    213  -6587       C  
ATOM    209  CD  GLU A  26      59.987  18.090  -1.781  1.00152.02           C  
ANISOU  209  CD  GLU A  26    29935  15302  12522   3753     52  -6218       C  
ATOM    210  OE1 GLU A  26      60.181  19.083  -1.060  1.00146.64           O  
ANISOU  210  OE1 GLU A  26    28288  15161  12266   3153    730  -5836       O  
ATOM    211  OE2 GLU A  26      58.881  17.845  -2.296  1.00153.97           O  
ANISOU  211  OE2 GLU A  26    30825  14875  12800   3572   -801  -6325       O  
ATOM    212  N   GLY A  27      66.073  17.475  -2.062  1.00169.81           N  
ANISOU  212  N   GLY A  27    30794  20535  13192   7073   3435  -6653       N  
ATOM    213  CA  GLY A  27      67.297  18.175  -2.432  1.00174.00           C  
ANISOU  213  CA  GLY A  27    30573  22049  13491   7497   4641  -6448       C  
ATOM    214  C   GLY A  27      67.452  19.505  -1.716  1.00167.46           C  
ANISOU  214  C   GLY A  27    28493  21717  13416   6476   5281  -5949       C  
ATOM    215  O   GLY A  27      68.571  19.991  -1.541  1.00170.09           O  
ANISOU  215  O   GLY A  27    27869  22820  13938   6599   6142  -5761       O  
ATOM    216  N   ILE A  28      66.330  20.094  -1.300  1.00159.56           N  
ANISOU  216  N   ILE A  28    27488  20264  12875   5486   4824  -5735       N  
ATOM    217  CA  ILE A  28      66.347  21.401  -0.637  1.00153.29           C  
ANISOU  217  CA  ILE A  28    25669  19832  12743   4530   5310  -5284       C  
ATOM    218  C   ILE A  28      67.233  21.374   0.605  1.00151.24           C  
ANISOU  218  C   ILE A  28    24364  19939  13160   4342   5482  -5262       C  
ATOM    219  O   ILE A  28      66.784  21.644   1.717  1.00144.10           O  
ANISOU  219  O   ILE A  28    23042  18803  12908   3604   5103  -5144       O  
ATOM    220  CB  ILE A  28      64.928  21.910  -0.281  1.00145.51           C  
ANISOU  220  CB  ILE A  28    24895  18262  12129   3600   4689  -5105       C  
ATOM    221  CG1 ILE A  28      63.997  21.774  -1.486  1.00148.21           C  
ANISOU  221  CG1 ILE A  28    26337  18144  11830   3859   4300  -5219       C  
ATOM    222  CG2 ILE A  28      64.977  23.359   0.184  1.00140.23           C  
ANISOU  222  CG2 ILE A  28    23338  17976  11966   2767   5237  -4655       C  
ATOM    223  CD1 ILE A  28      64.657  22.123  -2.811  1.00155.84           C  
ANISOU  223  CD1 ILE A  28    27660  19572  11980   4596   5076  -5180       C  
ATOM    224  N   GLU A  29      68.494  21.021   0.382  1.00158.31           N  
ANISOU  224  N   GLU A  29    24881  21415  13856   5104   6042  -5391       N  
ATOM    225  CA  GLU A  29      69.554  21.076   1.388  1.00158.65           C  
ANISOU  225  CA  GLU A  29    23835  21937  14510   5066   6297  -5388       C  
ATOM    226  C   GLU A  29      69.229  21.945   2.597  1.00150.33           C  
ANISOU  226  C   GLU A  29    22031  20790  14296   4019   6100  -5127       C  
ATOM    227  O   GLU A  29      68.992  21.435   3.693  1.00146.09           O  
ANISOU  227  O   GLU A  29    21470  19896  14140   3839   5462  -5283       O  
ATOM    228  CB  GLU A  29      70.829  21.614   0.733  1.00166.95           C  
ANISOU  228  CB  GLU A  29    24109  23875  15450   5504   7381  -5194       C  
ATOM    229  CG  GLU A  29      72.005  21.770   1.675  1.00169.57           C  
ANISOU  229  CG  GLU A  29    23172  24760  16496   5461   7652  -5183       C  
ATOM    230  CD  GLU A  29      72.974  20.613   1.580  1.00178.51           C  
ANISOU  230  CD  GLU A  29    24298  26206  17320   6597   7697  -5580       C  
ATOM    231  OE1 GLU A  29      73.362  20.250   0.448  1.00186.31           O  
ANISOU  231  OE1 GLU A  29    25700  27510  17579   7475   8227  -5635       O  
ATOM    232  OE2 GLU A  29      73.351  20.072   2.638  1.00177.45           O  
ANISOU  232  OE2 GLU A  29    23795  26003  17626   6680   7201  -5842       O  
ATOM    233  N   GLU A  30      69.228  23.259   2.375  1.00148.75           N  
ANISOU  233  N   GLU A  30    21298  20888  14331   3387   6655  -4718       N  
ATOM    234  CA  GLU A  30      69.175  24.267   3.444  1.00142.60           C  
ANISOU  234  CA  GLU A  30    19711  20140  14329   2491   6593  -4459       C  
ATOM    235  C   GLU A  30      67.835  24.395   4.164  1.00133.30           C  
ANISOU  235  C   GLU A  30    18991  18302  13354   1833   5857  -4408       C  
ATOM    236  O   GLU A  30      67.596  25.380   4.854  1.00128.69           O  
ANISOU  236  O   GLU A  30    17934  17703  13259   1122   5833  -4158       O  
ATOM    237  CB  GLU A  30      69.578  25.641   2.890  1.00145.20           C  
ANISOU  237  CB  GLU A  30    19428  20922  14819   2034   7395  -4018       C  
ATOM    238  CG  GLU A  30      68.641  26.175   1.810  1.00145.33           C  
ANISOU  238  CG  GLU A  30    20229  20701  14288   1850   7562  -3793       C  
ATOM    239  CD  GLU A  30      68.697  25.361   0.523  1.00153.68           C  
ANISOU  239  CD  GLU A  30    22122  21808  14462   2761   7797  -3975       C  
ATOM    240  OE1 GLU A  30      69.695  24.635   0.307  1.00160.46           O  
ANISOU  240  OE1 GLU A  30    22763  23073  15133   3535   8128  -4167       O  
ATOM    241  OE2 GLU A  30      67.739  25.453  -0.275  1.00153.50           O  
ANISOU  241  OE2 GLU A  30    23003  21411  13911   2762   7613  -3946       O  
ATOM    242  N   ALA A  31      66.962  23.411   4.006  1.00131.20           N  
ANISOU  242  N   ALA A  31    19633  17481  12737   2081   5249  -4629       N  
ATOM    243  CA  ALA A  31      65.686  23.449   4.696  1.00123.65           C  
ANISOU  243  CA  ALA A  31    19019  15931  12030   1482   4601  -4531       C  
ATOM    244  C   ALA A  31      65.933  23.403   6.194  1.00119.76           C  
ANISOU  244  C   ALA A  31    17983  15405  12117   1238   4320  -4534       C  
ATOM    245  O   ALA A  31      66.776  22.643   6.665  1.00122.76           O  
ANISOU  245  O   ALA A  31    18173  15912  12559   1734   4239  -4785       O  
ATOM    246  CB  ALA A  31      64.814  22.290   4.267  1.00124.39           C  
ANISOU  246  CB  ALA A  31    20101  15411  11752   1792   3964  -4760       C  
ATOM    247  N   SER A  32      65.208  24.221   6.945  1.00113.48           N  
ANISOU  247  N   SER A  32    16985  14436  11694    554   4157  -4268       N  
ATOM    248  CA  SER A  32      65.368  24.228   8.384  1.00110.13           C  
ANISOU  248  CA  SER A  32    16171  13942  11730    390   3870  -4259       C  
ATOM    249  C   SER A  32      64.067  24.586   9.066  1.00104.04           C  
ANISOU  249  C   SER A  32    15647  12743  11142   -165   3508  -3999       C  
ATOM    250  O   SER A  32      63.105  24.999   8.428  1.00102.10           O  
ANISOU  250  O   SER A  32    15719  12319  10753   -495   3501  -3817       O  
ATOM    251  CB  SER A  32      66.460  25.209   8.810  1.00111.52           C  
ANISOU  251  CB  SER A  32    15447  14633  12294    249   4245  -4203       C  
ATOM    252  OG  SER A  32      65.941  26.517   8.947  1.00107.80           O  
ANISOU  252  OG  SER A  32    14764  14160  12035   -406   4358  -3890       O  
ATOM    253  N   LEU A  33      64.056  24.431  10.379  1.00101.71           N  
ANISOU  253  N   LEU A  33    15202  12301  11142   -205   3216  -3976       N  
ATOM    254  CA  LEU A  33      62.881  24.697  11.167  1.00 97.01           C  
ANISOU  254  CA  LEU A  33    14804  11348  10705   -619   2941  -3694       C  
ATOM    255  C   LEU A  33      62.468  26.145  10.998  1.00 93.91           C  
ANISOU  255  C   LEU A  33    14137  11133  10412  -1129   3179  -3436       C  
ATOM    256  O   LEU A  33      61.377  26.432  10.513  1.00 91.77           O  
ANISOU  256  O   LEU A  33    14159  10665  10045  -1441   3132  -3236       O  
ATOM    257  CB  LEU A  33      63.179  24.409  12.629  1.00 96.36           C  
ANISOU  257  CB  LEU A  33    14601  11167  10845   -445   2689  -3714       C  
ATOM    258  CG  LEU A  33      62.105  23.557  13.285  1.00 95.76           C  
ANISOU  258  CG  LEU A  33    15051  10565  10770   -482   2342  -3520       C  
ATOM    259  CD1 LEU A  33      62.096  23.816  14.772  1.00 95.11           C  
ANISOU  259  CD1 LEU A  33    14863  10421  10852   -435   2216  -3378       C  
ATOM    260  CD2 LEU A  33      60.768  23.915  12.675  1.00 94.88           C  
ANISOU  260  CD2 LEU A  33    15156  10245  10648   -963   2345  -3224       C  
ATOM    261  N   SER A  34      63.354  27.055  11.390  1.00 94.25           N  
ANISOU  261  N   SER A  34    13620  11518  10675  -1206   3378  -3454       N  
ATOM    262  CA  SER A  34      63.058  28.478  11.330  1.00 92.06           C  
ANISOU  262  CA  SER A  34    13118  11348  10512  -1681   3545  -3217       C  
ATOM    263  C   SER A  34      62.767  28.828   9.890  1.00 93.20           C  
ANISOU  263  C   SER A  34    13454  11579  10379  -1841   3871  -3129       C  
ATOM    264  O   SER A  34      61.700  29.328   9.538  1.00 90.51           O  
ANISOU  264  O   SER A  34    13421  11056   9912  -2138   3819  -2927       O  
ATOM    265  CB  SER A  34      64.254  29.289  11.826  1.00 94.41           C  
ANISOU  265  CB  SER A  34    12765  11954  11152  -1731   3653  -3292       C  
ATOM    266  OG  SER A  34      64.822  30.061  10.792  1.00 97.05           O  
ANISOU  266  OG  SER A  34    12784  12588  11503  -1950   4107  -3211       O  
ATOM    267  N   ASN A  35      63.762  28.564   9.068  1.00 97.98           N  
ANISOU  267  N   ASN A  35    13873  12486  10868  -1572   4219  -3284       N  
ATOM    268  CA  ASN A  35      63.638  28.537   7.630  1.00100.75           C  
ANISOU  268  CA  ASN A  35    14553  12917  10810  -1479   4545  -3261       C  
ATOM    269  C   ASN A  35      62.226  28.268   7.086  1.00 98.25           C  
ANISOU  269  C   ASN A  35    14942  12195  10193  -1581   4240  -3190       C  
ATOM    270  O   ASN A  35      61.671  29.081   6.355  1.00 97.60           O  
ANISOU  270  O   ASN A  35    15060  12094   9928  -1839   4386  -3011       O  
ATOM    271  CB  ASN A  35      64.581  27.461   7.133  1.00106.08           C  
ANISOU  271  CB  ASN A  35    15228  13798  11280   -863   4712  -3542       C  
ATOM    272  CG  ASN A  35      64.696  27.457   5.668  1.00110.49           C  
ANISOU  272  CG  ASN A  35    16117  14513  11349   -617   5131  -3533       C  
ATOM    273  OD1 ASN A  35      64.640  28.515   5.048  1.00111.76           O  
ANISOU  273  OD1 ASN A  35    16201  14826  11438   -930   5522  -3280       O  
ATOM    274  ND2 ASN A  35      64.852  26.271   5.078  1.00115.20           N  
ANISOU  274  ND2 ASN A  35    17177  15042  11552      0   5041  -3805       N  
ATOM    275  N   VAL A  36      61.657  27.118   7.433  1.00 97.43           N  
ANISOU  275  N   VAL A  36    15210  11739  10071  -1380   3784  -3323       N  
ATOM    276  CA  VAL A  36      60.336  26.731   6.941  1.00 96.13           C  
ANISOU  276  CA  VAL A  36    15631  11147   9749  -1496   3396  -3268       C  
ATOM    277  C   VAL A  36      59.198  27.483   7.622  1.00 91.54           C  
ANISOU  277  C   VAL A  36    14959  10388   9435  -1994   3194  -2968       C  
ATOM    278  O   VAL A  36      58.222  27.848   6.977  1.00 91.21           O  
ANISOU  278  O   VAL A  36    15201  10177   9277  -2199   3056  -2853       O  
ATOM    279  CB  VAL A  36      60.076  25.224   7.112  1.00 97.77           C  
ANISOU  279  CB  VAL A  36    16250  10954   9943  -1186   2925  -3463       C  
ATOM    280  CG1 VAL A  36      58.587  24.942   7.044  1.00 95.92           C  
ANISOU  280  CG1 VAL A  36    16396  10224   9827  -1499   2427  -3307       C  
ATOM    281  CG2 VAL A  36      60.820  24.432   6.065  1.00102.89           C  
ANISOU  281  CG2 VAL A  36    17266  11665  10161   -606   3009  -3785       C  
ATOM    282  N   SER A  37      59.302  27.693   8.929  1.00 88.67           N  
ANISOU  282  N   SER A  37    14235  10059   9396  -2112   3151  -2854       N  
ATOM    283  CA  SER A  37      58.271  28.449   9.639  1.00 84.92           C  
ANISOU  283  CA  SER A  37    13678   9473   9116  -2469   3023  -2557       C  
ATOM    284  C   SER A  37      58.153  29.847   9.042  1.00 84.10           C  
ANISOU  284  C   SER A  37    13498   9563   8895  -2739   3268  -2429       C  
ATOM    285  O   SER A  37      57.061  30.384   8.895  1.00 82.44           O  
ANISOU  285  O   SER A  37    13432   9221   8669  -2968   3133  -2237       O  
ATOM    286  CB  SER A  37      58.586  28.568  11.138  1.00 82.97           C  
ANISOU  286  CB  SER A  37    13130   9270   9123  -2421   2983  -2480       C  
ATOM    287  OG  SER A  37      59.166  27.384  11.649  1.00 84.46           O  
ANISOU  287  OG  SER A  37    13371   9357   9364  -2082   2847  -2655       O  
ATOM    288  N   SER A  38      59.293  30.439   8.725  1.00 86.05           N  
ANISOU  288  N   SER A  38    13489  10115   9092  -2711   3626  -2514       N  
ATOM    289  CA  SER A  38      59.320  31.739   8.082  1.00 86.61           C  
ANISOU  289  CA  SER A  38    13534  10325   9047  -2980   3898  -2363       C  
ATOM    290  C   SER A  38      58.465  31.720   6.813  1.00 87.83           C  
ANISOU  290  C   SER A  38    14205  10333   8835  -2981   3862  -2332       C  
ATOM    291  O   SER A  38      57.553  32.534   6.643  1.00 85.98           O  
ANISOU  291  O   SER A  38    14149   9984   8536  -3211   3750  -2158       O  
ATOM    292  CB  SER A  38      60.760  32.097   7.740  1.00 90.28           C  
ANISOU  292  CB  SER A  38    13621  11125   9557  -2936   4343  -2428       C  
ATOM    293  OG  SER A  38      60.815  33.285   7.005  1.00 91.82           O  
ANISOU  293  OG  SER A  38    13850  11406   9631  -3216   4656  -2229       O  
ATOM    294  N   MET A  39      58.758  30.774   5.928  1.00 91.37           N  
ANISOU  294  N   MET A  39    14942  10763   9012  -2651   3900  -2533       N  
ATOM    295  CA  MET A  39      57.974  30.614   4.719  1.00 93.49           C  
ANISOU  295  CA  MET A  39    15800  10829   8891  -2546   3744  -2574       C  
ATOM    296  C   MET A  39      56.486  30.450   5.045  1.00 90.59           C  
ANISOU  296  C   MET A  39    15610  10104   8706  -2751   3180  -2485       C  
ATOM    297  O   MET A  39      55.629  31.021   4.376  1.00 90.82           O  
ANISOU  297  O   MET A  39    15940  10008   8560  -2859   3026  -2405       O  
ATOM    298  CB  MET A  39      58.512  29.451   3.880  1.00 98.15           C  
ANISOU  298  CB  MET A  39    16753  11393   9148  -2045   3753  -2857       C  
ATOM    299  CG  MET A  39      57.672  29.121   2.672  1.00102.09           C  
ANISOU  299  CG  MET A  39    17977  11587   9223  -1842   3423  -2973       C  
ATOM    300  SD  MET A  39      56.332  27.980   3.068  1.00104.61           S  
ANISOU  300  SD  MET A  39    18550  11333   9863  -1933   2535  -3075       S  
ATOM    301  CE  MET A  39      57.129  26.391   2.790  1.00108.04           C  
ANISOU  301  CE  MET A  39    19334  11620  10097  -1352   2373  -3444       C  
ATOM    302  N   LEU A  40      56.179  29.691   6.090  1.00 88.56           N  
ANISOU  302  N   LEU A  40    15140   9691   8818  -2793   2892  -2469       N  
ATOM    303  CA  LEU A  40      54.787  29.457   6.456  1.00 87.04           C  
ANISOU  303  CA  LEU A  40    14990   9190   8892  -3003   2432  -2309       C  
ATOM    304  C   LEU A  40      54.129  30.716   6.996  1.00 84.10           C  
ANISOU  304  C   LEU A  40    14371   8942   8642  -3281   2513  -2031       C  
ATOM    305  O   LEU A  40      52.952  30.960   6.756  1.00 84.06           O  
ANISOU  305  O   LEU A  40    14453   8781   8706  -3421   2223  -1902       O  
ATOM    306  CB  LEU A  40      54.674  28.335   7.481  1.00 86.59           C  
ANISOU  306  CB  LEU A  40    14777   8930   9191  -2974   2205  -2275       C  
ATOM    307  CG  LEU A  40      54.932  26.935   6.945  1.00 90.49           C  
ANISOU  307  CG  LEU A  40    15643   9132   9607  -2707   1912  -2539       C  
ATOM    308  CD1 LEU A  40      54.698  25.920   8.041  1.00 90.61           C  
ANISOU  308  CD1 LEU A  40    15541   8881  10007  -2743   1683  -2423       C  
ATOM    309  CD2 LEU A  40      54.031  26.665   5.747  1.00 92.90           C  
ANISOU  309  CD2 LEU A  40    16412   9107   9778  -2721   1461  -2643       C  
ATOM    310  N   LEU A  41      54.886  31.503   7.749  1.00 82.39           N  
ANISOU  310  N   LEU A  41    13847   8986   8472  -3327   2847  -1957       N  
ATOM    311  CA  LEU A  41      54.382  32.761   8.269  1.00 80.19           C  
ANISOU  311  CA  LEU A  41    13430   8797   8241  -3511   2896  -1733       C  
ATOM    312  C   LEU A  41      54.050  33.677   7.111  1.00 81.87           C  
ANISOU  312  C   LEU A  41    13958   9012   8139  -3599   2940  -1717       C  
ATOM    313  O   LEU A  41      52.965  34.254   7.044  1.00 81.17           O  
ANISOU  313  O   LEU A  41    13961   8840   8040  -3683   2729  -1573       O  
ATOM    314  CB  LEU A  41      55.434  33.431   9.146  1.00 78.84           C  
ANISOU  314  CB  LEU A  41    12963   8832   8162  -3520   3152  -1728       C  
ATOM    315  CG  LEU A  41      55.576  32.920  10.574  1.00 76.73           C  
ANISOU  315  CG  LEU A  41    12445   8553   8156  -3385   3058  -1689       C  
ATOM    316  CD1 LEU A  41      56.726  33.616  11.269  1.00 75.27           C  
ANISOU  316  CD1 LEU A  41    12013   8529   8056  -3365   3195  -1766       C  
ATOM    317  CD2 LEU A  41      54.272  33.104  11.340  1.00 73.72           C  
ANISOU  317  CD2 LEU A  41    12062   8070   7877  -3392   2878  -1417       C  
ATOM    318  N   GLU A  42      55.006  33.811   6.199  1.00 84.90           N  
ANISOU  318  N   GLU A  42    14510   9505   8245  -3533   3243  -1846       N  
ATOM    319  CA  GLU A  42      54.816  34.633   5.024  1.00 87.60           C  
ANISOU  319  CA  GLU A  42    15255   9829   8200  -3559   3354  -1807       C  
ATOM    320  C   GLU A  42      53.502  34.222   4.383  1.00 88.37           C  
ANISOU  320  C   GLU A  42    15716   9669   8193  -3475   2874  -1855       C  
ATOM    321  O   GLU A  42      52.652  35.052   4.087  1.00 88.03           O  
ANISOU  321  O   GLU A  42    15866   9548   8034  -3548   2704  -1746       O  
ATOM    322  CB  GLU A  42      55.978  34.416   4.056  1.00 91.89           C  
ANISOU  322  CB  GLU A  42    15962  10523   8430  -3382   3788  -1922       C  
ATOM    323  CG  GLU A  42      56.599  35.681   3.489  1.00 95.02           C  
ANISOU  323  CG  GLU A  42    16445  11057   8601  -3538   4257  -1736       C  
ATOM    324  CD  GLU A  42      58.105  35.554   3.335  1.00100.04           C  
ANISOU  324  CD  GLU A  42    16758  11982   9271  -3484   4826  -1738       C  
ATOM    325  OE1 GLU A  42      58.746  34.994   4.241  1.00 99.56           O  
ANISOU  325  OE1 GLU A  42    16197  12049   9584  -3468   4816  -1842       O  
ATOM    326  OE2 GLU A  42      58.657  36.009   2.314  1.00104.94           O  
ANISOU  326  OE2 GLU A  42    17611  12714   9548  -3427   5303  -1617       O  
ATOM    327  N   LEU A  43      53.334  32.920   4.203  1.00 90.17           N  
ANISOU  327  N   LEU A  43    16029   9729   8502  -3314   2589  -2032       N  
ATOM    328  CA  LEU A  43      52.157  32.386   3.540  1.00 92.61           C  
ANISOU  328  CA  LEU A  43    16660   9724   8805  -3254   2018  -2118       C  
ATOM    329  C   LEU A  43      50.888  32.744   4.296  1.00 91.08           C  
ANISOU  329  C   LEU A  43    16132   9461   9014  -3485   1695  -1890       C  
ATOM    330  O   LEU A  43      49.898  33.154   3.700  1.00 92.40           O  
ANISOU  330  O   LEU A  43    16496   9497   9115  -3490   1345  -1874       O  
ATOM    331  CB  LEU A  43      52.294  30.870   3.400  1.00 94.83           C  
ANISOU  331  CB  LEU A  43    17067   9767   9196  -3079   1714  -2338       C  
ATOM    332  CG  LEU A  43      51.589  30.126   2.263  1.00 98.78           C  
ANISOU  332  CG  LEU A  43    18132   9875   9525  -2880   1104  -2577       C  
ATOM    333  CD1 LEU A  43      50.364  29.381   2.753  1.00 98.90           C  
ANISOU  333  CD1 LEU A  43    17903   9538  10138  -3126    450  -2494       C  
ATOM    334  CD2 LEU A  43      51.241  31.076   1.133  1.00100.51           C  
ANISOU  334  CD2 LEU A  43    18842  10094   9251  -2744   1072  -2618       C  
ATOM    335  N   GLY A  44      50.928  32.593   5.616  1.00 89.16           N  
ANISOU  335  N   GLY A  44    15391   9325   9162  -3614   1823  -1708       N  
ATOM    336  CA  GLY A  44      49.766  32.846   6.463  1.00 89.12           C  
ANISOU  336  CA  GLY A  44    15014   9315   9533  -3752   1631  -1433       C  
ATOM    337  C   GLY A  44      49.337  34.293   6.443  1.00 88.92           C  
ANISOU  337  C   GLY A  44    15024   9452   9310  -3759   1724  -1299       C  
ATOM    338  O   GLY A  44      48.152  34.609   6.431  1.00 89.69           O  
ANISOU  338  O   GLY A  44    15009   9513   9557  -3776   1437  -1160       O  
ATOM    339  N   LEU A  45      50.317  35.180   6.447  1.00 88.95           N  
ANISOU  339  N   LEU A  45    15165   9620   9011  -3745   2104  -1333       N  
ATOM    340  CA  LEU A  45      50.048  36.601   6.348  1.00 89.83           C  
ANISOU  340  CA  LEU A  45    15439   9806   8884  -3751   2168  -1225       C  
ATOM    341  C   LEU A  45      49.297  36.919   5.062  1.00 93.75           C  
ANISOU  341  C   LEU A  45    16376  10152   9092  -3681   1875  -1308       C  
ATOM    342  O   LEU A  45      48.279  37.608   5.067  1.00 93.81           O  
ANISOU  342  O   LEU A  45    16405  10147   9093  -3625   1627  -1202       O  
ATOM    343  CB  LEU A  45      51.362  37.375   6.386  1.00 89.12           C  
ANISOU  343  CB  LEU A  45    15452   9826   8583  -3826   2586  -1249       C  
ATOM    344  CG  LEU A  45      51.911  37.676   7.772  1.00 86.19           C  
ANISOU  344  CG  LEU A  45    14723   9576   8448  -3854   2741  -1157       C  
ATOM    345  CD1 LEU A  45      53.308  38.247   7.660  1.00 86.72           C  
ANISOU  345  CD1 LEU A  45    14805   9706   8438  -3993   3072  -1212       C  
ATOM    346  CD2 LEU A  45      50.984  38.640   8.487  1.00 83.94           C  
ANISOU  346  CD2 LEU A  45    14434   9299   8161  -3765   2571   -975       C  
ATOM    347  N   ARG A  46      49.807  36.403   3.956  1.00 98.26           N  
ANISOU  347  N   ARG A  46    17338  10611   9384  -3606   1886  -1511       N  
ATOM    348  CA  ARG A  46      49.212  36.693   2.665  1.00103.86           C  
ANISOU  348  CA  ARG A  46    18609  11142   9712  -3448   1588  -1627       C  
ATOM    349  C   ARG A  46      47.717  36.387   2.683  1.00106.51           C  
ANISOU  349  C   ARG A  46    18775  11327  10367  -3421    952  -1622       C  
ATOM    350  O   ARG A  46      46.898  37.194   2.240  1.00107.96           O  
ANISOU  350  O   ARG A  46    19179  11460  10381  -3319    681  -1598       O  
ATOM    351  CB  ARG A  46      49.928  35.928   1.548  1.00107.04           C  
ANISOU  351  CB  ARG A  46    19492  11432   9748  -3251   1654  -1865       C  
ATOM    352  CG  ARG A  46      49.732  36.535   0.163  1.00112.21           C  
ANISOU  352  CG  ARG A  46    20914  11940   9781  -3002   1561  -1956       C  
ATOM    353  CD  ARG A  46      51.063  36.687  -0.576  1.00116.35           C  
ANISOU  353  CD  ARG A  46    21841  12580   9786  -2855   2201  -1960       C  
ATOM    354  NE  ARG A  46      51.922  35.524  -0.372  1.00117.47           N  
ANISOU  354  NE  ARG A  46    21752  12811  10069  -2777   2396  -2099       N  
ATOM    355  CZ  ARG A  46      52.059  34.535  -1.246  1.00121.70           C  
ANISOU  355  CZ  ARG A  46    22750  13194  10298  -2405   2206  -2361       C  
ATOM    356  NH1 ARG A  46      51.400  34.571  -2.397  1.00125.78           N  
ANISOU  356  NH1 ARG A  46    24003  13447  10341  -2076   1795  -2520       N  
ATOM    357  NH2 ARG A  46      52.859  33.512  -0.971  1.00121.66           N  
ANISOU  357  NH2 ARG A  46    22533  13274  10420  -2296   2376  -2490       N  
ATOM    358  N   VAL A  47      47.360  35.226   3.211  1.00108.80           N  
ANISOU  358  N   VAL A  47    18645  11536  11160  -3518    705  -1621       N  
ATOM    359  CA  VAL A  47      45.962  34.840   3.265  1.00113.45           C  
ANISOU  359  CA  VAL A  47    18923  11977  12205  -3569    113  -1558       C  
ATOM    360  C   VAL A  47      45.181  35.740   4.209  1.00114.04           C  
ANISOU  360  C   VAL A  47    18521  12297  12513  -3597    214  -1254       C  
ATOM    361  O   VAL A  47      44.169  36.333   3.838  1.00116.12           O  
ANISOU  361  O   VAL A  47    18790  12548  12783  -3490   -145  -1230       O  
ATOM    362  CB  VAL A  47      45.799  33.404   3.750  1.00114.11           C  
ANISOU  362  CB  VAL A  47    18619  11882  12854  -3740   -112  -1533       C  
ATOM    363  CG1 VAL A  47      44.331  33.062   3.832  1.00117.38           C  
ANISOU  363  CG1 VAL A  47    18585  12144  13870  -3874   -702  -1390       C  
ATOM    364  CG2 VAL A  47      46.518  32.453   2.821  1.00116.37           C  
ANISOU  364  CG2 VAL A  47    19445  11892  12880  -3618   -293  -1870       C  
ATOM    365  N   TYR A  48      45.649  35.807   5.447  1.00 57.52           N  
ATOM    366  CA  TYR A  48      45.039  36.629   6.477  1.00 61.40           C  
ATOM    367  C   TYR A  48      44.586  37.993   5.938  1.00 63.78           C  
ATOM    368  O   TYR A  48      43.436  38.401   6.156  1.00 63.98           O  
ATOM    369  CB  TYR A  48      46.040  36.809   7.606  1.00 61.71           C  
ATOM    370  CG  TYR A  48      45.489  37.548   8.799  1.00 64.00           C  
ATOM    371  CD1 TYR A  48      45.611  38.928   8.901  1.00 66.16           C  
ATOM    372  CD2 TYR A  48      44.847  36.868   9.826  1.00 65.93           C  
ATOM    373  CE1 TYR A  48      45.099  39.618   9.997  1.00 68.24           C  
ATOM    374  CE2 TYR A  48      44.339  37.543  10.931  1.00 67.77           C  
ATOM    375  CZ  TYR A  48      44.467  38.920  11.012  1.00 68.92           C  
ATOM    376  OH  TYR A  48      43.971  39.602  12.108  1.00 70.49           O  
ATOM    377  N   MET A  49      45.497  38.693   5.247  1.00 66.70           N  
ATOM    378  CA  MET A  49      45.175  39.951   4.541  1.00 69.63           C  
ATOM    379  C   MET A  49      43.923  39.802   3.679  1.00 70.67           C  
ATOM    380  O   MET A  49      42.935  40.538   3.866  1.00 70.77           O  
ATOM    381  CB  MET A  49      46.351  40.407   3.659  1.00 70.33           C  
ATOM    382  CG  MET A  49      47.031  41.718   4.092  1.00 74.91           C  
ATOM    383  SD  MET A  49      47.007  42.007   5.905  1.00 85.56           S  
ATOM    384  CE  MET A  49      47.968  43.541   6.062  1.00 83.48           C  
ATOM    385  N   ILE A  50      43.971  38.852   2.739  1.00 71.98           N  
ATOM    386  CA  ILE A  50      42.829  38.560   1.870  1.00 73.38           C  
ATOM    387  C   ILE A  50      41.520  38.456   2.671  1.00 74.60           C  
ATOM    388  O   ILE A  50      40.544  39.168   2.382  1.00 74.86           O  
ATOM    389  CB  ILE A  50      43.036  37.249   1.075  1.00 73.34           C  
ATOM    390  CG1 ILE A  50      44.383  37.253   0.322  1.00 73.74           C  
ATOM    391  CG2 ILE A  50      41.860  36.999   0.143  1.00 73.03           C  
ATOM    392  CD1 ILE A  50      44.422  38.125  -0.948  1.00 74.22           C  
ATOM    393  N   GLN A  51      41.499  37.576   3.675  1.00 75.84           N  
ATOM    394  CA  GLN A  51      40.310  37.414   4.529  1.00 77.28           C  
ATOM    395  C   GLN A  51      39.907  38.765   5.100  1.00 78.03           C  
ATOM    396  O   GLN A  51      38.732  39.145   5.090  1.00 78.02           O  
ATOM    397  CB  GLN A  51      40.590  36.438   5.682  1.00 77.45           C  
ATOM    398  CG  GLN A  51      40.795  34.995   5.234  1.00 78.88           C  
ATOM    399  CD  GLN A  51      39.579  34.462   4.478  1.00 80.79           C  
ATOM    400  OE1 GLN A  51      39.617  34.284   3.243  1.00 81.22           O  
ATOM    401  NE2 GLN A  51      38.479  34.235   5.212  1.00 80.90           N  
ATOM    402  N   GLN A  52      40.911  39.472   5.609  1.00 79.11           N  
ATOM    403  CA  GLN A  52      40.749  40.801   6.172  1.00 80.30           C  
ATOM    404  C   GLN A  52      39.954  41.681   5.220  1.00 80.91           C  
ATOM    405  O   GLN A  52      38.984  42.335   5.623  1.00 80.53           O  
ATOM    406  CB  GLN A  52      42.131  41.422   6.369  1.00 80.53           C  
ATOM    407  CG  GLN A  52      42.129  42.711   7.170  1.00 82.34           C  
ATOM    408  CD  GLN A  52      42.143  42.441   8.669  1.00 85.02           C  
ATOM    409  OE1 GLN A  52      41.551  41.457   9.142  1.00 85.84           O  
ATOM    410  NE2 GLN A  52      42.829  43.308   9.426  1.00 85.18           N  
ATOM    411  N   GLU A  53      40.384  41.679   3.956  1.00 83.72           N  
ATOM    412  CA  GLU A  53      39.794  42.503   2.894  1.00 86.33           C  
ATOM    413  C   GLU A  53      38.525  41.877   2.318  1.00 87.24           C  
ATOM    414  O   GLU A  53      38.530  41.412   1.172  1.00 87.63           O  
ATOM    415  CB  GLU A  53      40.804  42.688   1.751  1.00 86.71           C  
ATOM    416  CG  GLU A  53      42.102  43.394   2.149  1.00 89.63           C  
ATOM    417  CD  GLU A  53      41.974  44.916   2.136  1.00 93.14           C  
ATOM    418  OE1 GLU A  53      40.838  45.426   2.310  1.00 94.91           O  
ATOM    419  OE2 GLU A  53      43.010  45.599   1.949  1.00 93.73           O  
ATOM    420  N   LYS A  54      37.442  41.870   3.096  1.00 88.18           N  
ATOM    421  CA  LYS A  54      36.209  41.207   2.662  1.00 88.89           C  
ATOM    422  C   LYS A  54      35.132  41.260   3.740  1.00 89.00           C  
ATOM    423  O   LYS A  54      34.678  42.339   4.116  1.00 89.21           O  
ATOM    424  CB  LYS A  54      36.492  39.748   2.268  1.00 89.10           C  
ATOM    425  CG  LYS A  54      37.382  39.593   1.028  1.00 90.25           C  
ATOM    426  CD  LYS A  54      37.500  38.132   0.571  1.00 91.77           C  
ATOM    427  CE  LYS A  54      38.260  38.018  -0.762  1.00 91.87           C  
ATOM    428  NZ  LYS A  54      38.148  36.665  -1.392  1.00 91.39           N  
ATOM    429  N   PHE A  59      28.513  34.645   7.887  1.00 62.54           N  
ATOM    430  CA  PHE A  59      27.520  33.604   7.578  1.00 62.47           C  
ATOM    431  C   PHE A  59      26.281  33.714   8.454  1.00 60.97           C  
ATOM    432  O   PHE A  59      26.393  33.738   9.679  1.00 61.59           O  
ATOM    433  CB  PHE A  59      28.107  32.190   7.749  1.00 63.09           C  
ATOM    434  CG  PHE A  59      27.118  31.090   7.431  1.00 65.78           C  
ATOM    435  CD1 PHE A  59      26.420  30.441   8.452  1.00 67.59           C  
ATOM    436  CD2 PHE A  59      26.863  30.726   6.103  1.00 67.46           C  
ATOM    437  CE1 PHE A  59      25.499  29.436   8.154  1.00 68.47           C  
ATOM    438  CE2 PHE A  59      25.942  29.733   5.797  1.00 68.30           C  
ATOM    439  CZ  PHE A  59      25.257  29.086   6.827  1.00 69.06           C  
ATOM    440  N   ASN A  60      25.106  33.747   7.837  1.00 58.70           N  
ATOM    441  CA  ASN A  60      23.875  33.885   8.600  1.00 56.63           C  
ATOM    442  C   ASN A  60      23.087  32.561   8.685  1.00 54.30           C  
ATOM    443  O   ASN A  60      22.382  32.188   7.728  1.00 54.92           O  
ATOM    444  CB  ASN A  60      23.007  34.990   7.983  1.00 57.21           C  
ATOM    445  CG  ASN A  60      21.691  35.207   8.746  1.00 60.11           C  
ATOM    446  OD1 ASN A  60      21.117  36.302   8.722  1.00 62.29           O  
ATOM    447  ND2 ASN A  60      21.213  34.159   9.432  1.00 62.31           N  
ATOM    448  N   GLN A  61      23.191  31.864   9.816  1.00 95.47           N  
ANISOU  448  N   GLN A  61    16352   9547  10373  -1686   -135  -1002       N  
ATOM    449  CA  GLN A  61      22.442  30.624  10.031  1.00 89.74           C  
ANISOU  449  CA  GLN A  61    15561   8977   9561  -1513   -164   -918       C  
ATOM    450  C   GLN A  61      20.962  30.745   9.723  1.00 87.60           C  
ANISOU  450  C   GLN A  61    15330   8466   9490  -1310    -90   -942       C  
ATOM    451  O   GLN A  61      20.414  29.978   8.942  1.00 85.36           O  
ANISOU  451  O   GLN A  61    15008   8167   9258  -1121   -144   -765       O  
ATOM    452  CB  GLN A  61      22.573  30.151  11.473  1.00 90.19           C  
ANISOU  452  CB  GLN A  61    15577   9310   9380  -1638   -149  -1059       C  
ATOM    453  CG  GLN A  61      23.633  29.099  11.702  1.00 87.15           C  
ANISOU  453  CG  GLN A  61    15084   9270   8760  -1698   -274   -907       C  
ATOM    454  CD  GLN A  61      23.551  27.972  10.710  1.00 82.09           C  
ANISOU  454  CD  GLN A  61    14378   8667   8147  -1491   -356   -646       C  
ATOM    455  OE1 GLN A  61      22.474  27.593  10.274  1.00 79.53           O  
ANISOU  455  OE1 GLN A  61    14074   8210   7935  -1306   -326   -595       O  
ATOM    456  NE2 GLN A  61      24.696  27.435  10.337  1.00 81.05           N  
ANISOU  456  NE2 GLN A  61    14161   8715   7918  -1527   -455   -486       N  
ATOM    457  N   MET A  62      20.303  31.702  10.357  1.00 87.33           N  
ANISOU  457  N   MET A  62    15364   8245   9571  -1352     36  -1171       N  
ATOM    458  CA  MET A  62      18.855  31.767  10.283  1.00 85.36           C  
ANISOU  458  CA  MET A  62    15120   7805   9505  -1160    117  -1218       C  
ATOM    459  C   MET A  62      18.381  31.932   8.841  1.00 82.72           C  
ANISOU  459  C   MET A  62    14797   7232   9402   -968     60  -1016       C  
ATOM    460  O   MET A  62      17.486  31.231   8.379  1.00 80.79           O  
ANISOU  460  O   MET A  62    14498   6982   9217   -779     27   -900       O  
ATOM    461  CB  MET A  62      18.331  32.885  11.178  1.00 87.98           C  
ANISOU  461  CB  MET A  62    15525   7957   9947  -1241    282  -1516       C  
ATOM    462  CG  MET A  62      17.117  32.490  12.003  1.00 89.64           C  
ANISOU  462  CG  MET A  62    15695   8209  10156  -1145    391  -1655       C  
ATOM    463  SD  MET A  62      17.229  30.856  12.830  1.00 91.64           S  
ANISOU  463  SD  MET A  62    15853   8898  10067  -1175    328  -1579       S  
ATOM    464  CE  MET A  62      18.745  30.994  13.777  1.00 92.19           C  
ANISOU  464  CE  MET A  62    15952   9239   9835  -1481    286  -1681       C  
ATOM    465  N   GLU A  63      19.009  32.850   8.126  1.00 81.79           N  
ANISOU  465  N   GLU A  63    14750   6927   9399  -1033     43   -968       N  
ATOM    466  CA  GLU A  63      18.595  33.155   6.779  1.00 79.69           C  
ANISOU  466  CA  GLU A  63    14512   6426   9340   -874    -11   -774       C  
ATOM    467  C   GLU A  63      18.778  31.914   5.930  1.00 75.85           C  
ANISOU  467  C   GLU A  63    13955   6136   8727   -771   -143   -526       C  
ATOM    468  O   GLU A  63      17.991  31.632   5.026  1.00 75.14           O  
ANISOU  468  O   GLU A  63    13850   5948   8751   -590   -196   -376       O  
ATOM    469  CB  GLU A  63      19.420  34.312   6.235  1.00 81.22           C  
ANISOU  469  CB  GLU A  63    14804   6418   9640  -1004     -4   -754       C  
ATOM    470  CG  GLU A  63      18.668  35.132   5.228  1.00 83.15           C  
ANISOU  470  CG  GLU A  63    15111   6313  10169   -851     -1   -644       C  
ATOM    471  CD  GLU A  63      17.379  35.682   5.799  1.00 85.41           C  
ANISOU  471  CD  GLU A  63    15401   6378  10671   -724    112   -817       C  
ATOM    472  OE1 GLU A  63      17.447  36.387   6.816  1.00 88.02           O  
ANISOU  472  OE1 GLU A  63    15778   6634  11033   -849    240  -1074       O  
ATOM    473  OE2 GLU A  63      16.299  35.416   5.232  1.00 85.34           O  
ANISOU  473  OE2 GLU A  63    15343   6278  10803   -504     76   -703       O  
ATOM    474  N   TYR A  64      19.825  31.168   6.245  1.00 73.09           N  
ANISOU  474  N   TYR A  64    13559   6069   8143   -891   -194   -491       N  
ATOM    475  CA  TYR A  64      20.189  29.972   5.499  1.00 69.19           C  
ANISOU  475  CA  TYR A  64    13001   5765   7521   -813   -302   -277       C  
ATOM    476  C   TYR A  64      19.221  28.841   5.813  1.00 67.35           C  
ANISOU  476  C   TYR A  64    12700   5650   7240   -665   -313   -261       C  
ATOM    477  O   TYR A  64      18.697  28.192   4.914  1.00 65.91           O  
ANISOU  477  O   TYR A  64    12496   5448   7099   -515   -376   -106       O  
ATOM    478  CB  TYR A  64      21.614  29.578   5.864  1.00 68.62           C  
ANISOU  478  CB  TYR A  64    12883   5950   7240   -981   -342   -258       C  
ATOM    479  CG  TYR A  64      22.042  28.209   5.424  1.00 65.47           C  
ANISOU  479  CG  TYR A  64    12402   5781   6693   -905   -428    -80       C  
ATOM    480  CD1 TYR A  64      22.786  28.036   4.274  1.00 64.16           C  
ANISOU  480  CD1 TYR A  64    12232   5628   6520   -893   -485     96       C  
ATOM    481  CD2 TYR A  64      21.731  27.083   6.176  1.00 63.94           C  
ANISOU  481  CD2 TYR A  64    12139   5788   6369   -851   -442    -89       C  
ATOM    482  CE1 TYR A  64      23.195  26.778   3.867  1.00 62.31           C  
ANISOU  482  CE1 TYR A  64    11924   5589   6164   -818   -545    241       C  
ATOM    483  CE2 TYR A  64      22.137  25.820   5.783  1.00 60.73           C  
ANISOU  483  CE2 TYR A  64    11663   5563   5849   -775   -511     72       C  
ATOM    484  CZ  TYR A  64      22.870  25.676   4.624  1.00 60.78           C  
ANISOU  484  CZ  TYR A  64    11664   5567   5864   -755   -559    227       C  
ATOM    485  OH  TYR A  64      23.288  24.430   4.212  1.00 59.06           O  
ANISOU  485  OH  TYR A  64    11380   5512   5549   -674   -610    369       O  
ATOM    486  N   ASN A  65      18.979  28.593   7.094  1.00 67.07           N  
ANISOU  486  N   ASN A  65    12633   5744   7106   -723   -250   -423       N  
ATOM    487  CA  ASN A  65      17.967  27.623   7.479  1.00 65.38           C  
ANISOU  487  CA  ASN A  65    12360   5619   6862   -601   -237   -422       C  
ATOM    488  C   ASN A  65      16.660  27.875   6.748  1.00 65.04           C  
ANISOU  488  C   ASN A  65    12318   5348   7047   -419   -225   -387       C  
ATOM    489  O   ASN A  65      16.013  26.933   6.296  1.00 63.79           O  
ANISOU  489  O   ASN A  65    12107   5242   6889   -290   -276   -272       O  
ATOM    490  CB  ASN A  65      17.722  27.682   8.980  1.00 66.55           C  
ANISOU  490  CB  ASN A  65    12499   5882   6907   -703   -137   -633       C  
ATOM    491  CG  ASN A  65      18.894  27.169   9.769  1.00 66.62           C  
ANISOU  491  CG  ASN A  65    12481   6173   6658   -867   -178   -636       C  
ATOM    492  OD1 ASN A  65      19.013  27.424  10.962  1.00 69.38           O  
ANISOU  492  OD1 ASN A  65    12841   6632   6887  -1005   -112   -810       O  
ATOM    493  ND2 ASN A  65      19.781  26.453   9.101  1.00 64.67           N  
ANISOU  493  ND2 ASN A  65    12196   6050   6324   -854   -287   -443       N  
ATOM    494  N   LYS A  66      16.280  29.150   6.640  1.00 66.05           N  
ANISOU  494  N   LYS A  66    12501   5219   7375   -413   -161   -485       N  
ATOM    495  CA  LYS A  66      15.045  29.542   5.983  1.00 65.94           C  
ANISOU  495  CA  LYS A  66    12474   4974   7605   -234   -154   -448       C  
ATOM    496  C   LYS A  66      15.070  29.180   4.496  1.00 64.68           C  
ANISOU  496  C   LYS A  66    12317   4773   7485   -126   -290   -197       C  
ATOM    497  O   LYS A  66      14.159  28.515   3.989  1.00 63.92           O  
ANISOU  497  O   LYS A  66    12159   4686   7439     18   -344   -102       O  
ATOM    498  CB  LYS A  66      14.795  31.033   6.177  1.00 68.26           C  
ANISOU  498  CB  LYS A  66    12835   4985   8118   -253    -55   -594       C  
ATOM    499  CG  LYS A  66      13.507  31.523   5.579  1.00 68.82           C  
ANISOU  499  CG  LYS A  66    12875   4806   8468    -55    -47   -555       C  
ATOM    500  CD  LYS A  66      13.310  33.006   5.831  1.00 71.12           C  
ANISOU  500  CD  LYS A  66    13235   4790   8996    -66     65   -704       C  
ATOM    501  CE  LYS A  66      12.164  33.543   4.979  1.00 72.69           C  
ANISOU  501  CE  LYS A  66    13399   4721   9498    152     37   -596       C  
ATOM    502  NZ  LYS A  66      11.634  34.843   5.452  1.00 76.00           N  
ANISOU  502  NZ  LYS A  66    13854   4832  10192    190    182   -778       N  
ATOM    503  N   LEU A  67      16.122  29.576   3.793  1.00 64.21           N  
ANISOU  503  N   LEU A  67    12325   4684   7386   -210   -344    -92       N  
ATOM    504  CA  LEU A  67      16.217  29.221   2.382  1.00 63.16           C  
ANISOU  504  CA  LEU A  67    12208   4536   7255   -129   -462    139       C  
ATOM    505  C   LEU A  67      16.115  27.712   2.176  1.00 61.31           C  
ANISOU  505  C   LEU A  67    11903   4532   6859    -69   -529    234       C  
ATOM    506  O   LEU A  67      15.432  27.249   1.261  1.00 61.03           O  
ANISOU  506  O   LEU A  67    11849   4470   6869     54   -608    364       O  
ATOM    507  CB  LEU A  67      17.524  29.716   1.773  1.00 63.34           C  
ANISOU  507  CB  LEU A  67    12304   4550   7212   -259   -490    229       C  
ATOM    508  CG  LEU A  67      17.473  30.243   0.334  1.00 63.90           C  
ANISOU  508  CG  LEU A  67    12442   4450   7385   -200   -566    427       C  
ATOM    509  CD1 LEU A  67      18.771  29.944  -0.385  1.00 62.92           C  
ANISOU  509  CD1 LEU A  67    12349   4461   7096   -309   -608    557       C  
ATOM    510  CD2 LEU A  67      16.307  29.664  -0.430  1.00 64.12           C  
ANISOU  510  CD2 LEU A  67    12430   4454   7478    -17   -650    548       C  
ATOM    511  N   MET A  68      16.810  26.949   3.011  1.00 60.37           N  
ANISOU  511  N   MET A  68    11749   4636   6553   -161   -504    173       N  
ATOM    512  CA  MET A  68      16.841  25.509   2.844  1.00 58.79           C  
ANISOU  512  CA  MET A  68    11493   4634   6209   -111   -558    266       C  
ATOM    513  C   MET A  68      15.453  24.923   3.075  1.00 58.72           C  
ANISOU  513  C   MET A  68    11425   4613   6274     12   -549    235       C  
ATOM    514  O   MET A  68      14.990  24.073   2.320  1.00 58.05           O  
ANISOU  514  O   MET A  68    11315   4562   6180    103   -617    349       O  
ATOM    515  CB  MET A  68      17.860  24.886   3.787  1.00 58.40           C  
ANISOU  515  CB  MET A  68    11411   4813   5963   -228   -534    220       C  
ATOM    516  CG  MET A  68      19.291  25.257   3.446  1.00 58.50           C  
ANISOU  516  CG  MET A  68    11451   4881   5896   -346   -556    274       C  
ATOM    517  SD  MET A  68      19.912  24.322   2.024  1.00 59.21           S  
ANISOU  517  SD  MET A  68    11537   5049   5912   -280   -639    487       S  
ATOM    518  CE  MET A  68      20.114  22.700   2.750  1.00 55.09           C  
ANISOU  518  CE  MET A  68    10930   4773   5228   -248   -648    508       C  
ATOM    519  N   LEU A  69      14.769  25.405   4.100  1.00 59.55           N  
ANISOU  519  N   LEU A  69    11505   4668   6455      4   -456     71       N  
ATOM    520  CA  LEU A  69      13.449  24.894   4.381  1.00 59.13           C  
ANISOU  520  CA  LEU A  69    11377   4611   6480    109   -430     31       C  
ATOM    521  C   LEU A  69      12.538  25.136   3.193  1.00 59.58           C  
ANISOU  521  C   LEU A  69    11416   4504   6717    250   -508    142       C  
ATOM    522  O   LEU A  69      11.712  24.275   2.845  1.00 58.92           O  
ANISOU  522  O   LEU A  69    11267   4472   6647    335   -555    204       O  
ATOM    523  CB  LEU A  69      12.874  25.552   5.626  1.00 60.37           C  
ANISOU  523  CB  LEU A  69    11511   4721   6705     76   -295   -180       C  
ATOM    524  CG  LEU A  69      11.435  25.150   5.943  1.00 59.99           C  
ANISOU  524  CG  LEU A  69    11368   4662   6766    183   -245   -235       C  
ATOM    525  CD1 LEU A  69      11.295  23.653   6.079  1.00 57.07           C  
ANISOU  525  CD1 LEU A  69    10947   4495   6240    185   -281   -155       C  
ATOM    526  CD2 LEU A  69      10.933  25.859   7.188  1.00 61.20           C  
ANISOU  526  CD2 LEU A  69    11502   4772   6978    141    -84   -465       C  
ATOM    527  N   GLU A  70      12.678  26.316   2.579  1.00 60.91           N  
ANISOU  527  N   GLU A  70    11643   4477   7024    265   -526    173       N  
ATOM    528  CA  GLU A  70      11.843  26.665   1.431  1.00 61.54           C  
ANISOU  528  CA  GLU A  70    11709   4399   7275    397   -618    303       C  
ATOM    529  C   GLU A  70      12.128  25.728   0.267  1.00 59.97           C  
ANISOU  529  C   GLU A  70    11527   4312   6947    415   -746    489       C  
ATOM    530  O   GLU A  70      11.231  25.096  -0.271  1.00 59.50           O  
ANISOU  530  O   GLU A  70    11405   4280   6923    507   -819    558       O  
ATOM    531  CB  GLU A  70      12.068  28.099   0.987  1.00 63.24           C  
ANISOU  531  CB  GLU A  70    12001   4376   7652    399   -615    328       C  
ATOM    532  CG  GLU A  70      11.284  28.430  -0.271  1.00 65.33           C  
ANISOU  532  CG  GLU A  70    12255   4495   8072    536   -735    504       C  
ATOM    533  CD  GLU A  70      11.778  29.678  -0.939  1.00 69.49           C  
ANISOU  533  CD  GLU A  70    12886   4807   8709    517   -757    596       C  
ATOM    534  OE1 GLU A  70      11.438  29.911  -2.120  1.00 72.18           O  
ANISOU  534  OE1 GLU A  70    13247   5060   9118    598   -878    788       O  
ATOM    535  OE2 GLU A  70      12.512  30.440  -0.281  1.00 71.86           O  
ANISOU  535  OE2 GLU A  70    13253   5028   9022    410   -656    480       O  
ATOM    536  N   ASN A  71      13.388  25.644  -0.124  1.00 59.26           N  
ANISOU  536  N   ASN A  71    11516   4292   6708    319   -768    559       N  
ATOM    537  CA  ASN A  71      13.738  24.797  -1.233  1.00 58.26           C  
ANISOU  537  CA  ASN A  71    11415   4268   6454    328   -866    714       C  
ATOM    538  C   ASN A  71      13.264  23.364  -1.008  1.00 56.77           C  
ANISOU  538  C   ASN A  71    11157   4242   6171    363   -878    700       C  
ATOM    539  O   ASN A  71      12.601  22.781  -1.865  1.00 56.54           O  
ANISOU  539  O   ASN A  71    11109   4226   6146    431   -964    788       O  
ATOM    540  CB  ASN A  71      15.230  24.893  -1.542  1.00 58.02           C  
ANISOU  540  CB  ASN A  71    11461   4305   6280    213   -857    767       C  
ATOM    541  CG  ASN A  71      15.565  26.110  -2.429  1.00 61.76           C  
ANISOU  541  CG  ASN A  71    12021   4609   6837    190   -890    867       C  
ATOM    542  OD1 ASN A  71      14.708  26.645  -3.135  1.00 64.67           O  
ANISOU  542  OD1 ASN A  71    12403   4830   7340    279   -956    951       O  
ATOM    543  ND2 ASN A  71      16.819  26.540  -2.399  1.00 64.75           N  
ANISOU  543  ND2 ASN A  71    12453   5011   7137     67   -848    871       N  
ATOM    544  N   VAL A  72      13.565  22.802   0.155  1.00 55.72           N  
ANISOU  544  N   VAL A  72    10989   4231   5951    309   -796    592       N  
ATOM    545  CA  VAL A  72      13.127  21.452   0.451  1.00 54.19           C  
ANISOU  545  CA  VAL A  72    10739   4173   5680    334   -796    586       C  
ATOM    546  C   VAL A  72      11.610  21.312   0.405  1.00 54.79           C  
ANISOU  546  C   VAL A  72    10734   4188   5895    426   -815    562       C  
ATOM    547  O   VAL A  72      11.088  20.370  -0.187  1.00 54.11           O  
ANISOU  547  O   VAL A  72    10622   4155   5784    465   -877    626       O  
ATOM    548  CB  VAL A  72      13.608  21.019   1.821  1.00 53.91           C  
ANISOU  548  CB  VAL A  72    10677   4267   5537    259   -704    486       C  
ATOM    549  CG1 VAL A  72      12.783  19.864   2.324  1.00 53.43           C  
ANISOU  549  CG1 VAL A  72    10552   4296   5453    291   -683    464       C  
ATOM    550  CG2 VAL A  72      15.077  20.668   1.766  1.00 52.58           C  
ANISOU  550  CG2 VAL A  72    10552   4216   5210    181   -710    542       C  
ATOM    551  N   SER A  73      10.897  22.243   1.023  1.00 55.83           N  
ANISOU  551  N   SER A  73    10820   4209   6182    458   -756    462       N  
ATOM    552  CA  SER A  73       9.449  22.175   0.994  1.00 56.84           C  
ANISOU  552  CA  SER A  73    10845   4284   6467    554   -768    438       C  
ATOM    553  C   SER A  73       8.925  22.228  -0.431  1.00 57.16           C  
ANISOU  553  C   SER A  73    10880   4257   6582    634   -912    585       C  
ATOM    554  O   SER A  73       8.024  21.486  -0.816  1.00 57.17           O  
ANISOU  554  O   SER A  73    10805   4307   6610    680   -974    621       O  
ATOM    555  CB  SER A  73       8.856  23.305   1.820  1.00 58.53           C  
ANISOU  555  CB  SER A  73    11011   4368   6858    587   -666    302       C  
ATOM    556  OG  SER A  73       8.648  22.869   3.142  1.00 59.67           O  
ANISOU  556  OG  SER A  73    11107   4618   6946    535   -538    156       O  
ATOM    557  N   ARG A  74       9.510  23.121  -1.210  1.00 57.68           N  
ANISOU  557  N   ARG A  74    11030   4216   6670    636   -969    674       N  
ATOM    558  CA  ARG A  74       9.130  23.326  -2.584  1.00 58.22           C  
ANISOU  558  CA  ARG A  74    11114   4223   6784    698  -1113    832       C  
ATOM    559  C   ARG A  74       9.323  22.032  -3.362  1.00 56.60           C  
ANISOU  559  C   ARG A  74    10934   4174   6400    662  -1193    911       C  
ATOM    560  O   ARG A  74       8.415  21.541  -4.031  1.00 56.60           O  
ANISOU  560  O   ARG A  74    10875   4203   6429    709  -1293    969       O  
ATOM    561  CB  ARG A  74      10.019  24.421  -3.149  1.00 59.25           C  
ANISOU  561  CB  ARG A  74    11358   4233   6920    668  -1132    915       C  
ATOM    562  CG  ARG A  74       9.318  25.331  -4.074  1.00 62.59           C  
ANISOU  562  CG  ARG A  74    11776   4498   7507    762  -1240   1045       C  
ATOM    563  CD  ARG A  74       9.994  26.677  -4.191  1.00 65.80           C  
ANISOU  563  CD  ARG A  74    12281   4724   7998    738  -1209   1084       C  
ATOM    564  NE  ARG A  74       9.000  27.627  -4.670  1.00 69.09           N  
ANISOU  564  NE  ARG A  74    12653   4949   8650    866  -1285   1176       N  
ATOM    565  CZ  ARG A  74       8.723  28.753  -4.049  1.00 71.05           C  
ANISOU  565  CZ  ARG A  74    12886   4990   9121    920  -1202   1101       C  
ATOM    566  NH1 ARG A  74       9.405  29.081  -2.966  1.00 72.21           N  
ANISOU  566  NH1 ARG A  74    13073   5109   9256    833  -1046    925       N  
ATOM    567  NH2 ARG A  74       7.785  29.546  -4.515  1.00 73.57           N  
ANISOU  567  NH2 ARG A  74    13149   5130   9673   1059  -1276   1200       N  
ATOM    568  N   VAL A  75      10.523  21.478  -3.252  1.00 54.99           N  
ANISOU  568  N   VAL A  75    10811   4069   6015    573  -1145    906       N  
ATOM    569  CA  VAL A  75      10.847  20.202  -3.877  1.00 53.53           C  
ANISOU  569  CA  VAL A  75    10659   4018   5663    538  -1187    954       C  
ATOM    570  C   VAL A  75       9.847  19.116  -3.475  1.00 53.58           C  
ANISOU  570  C   VAL A  75    10572   4095   5690    561  -1184    895       C  
ATOM    571  O   VAL A  75       9.381  18.327  -4.305  1.00 53.57           O  
ANISOU  571  O   VAL A  75    10568   4144   5643    564  -1268    945       O  
ATOM    572  CB  VAL A  75      12.264  19.771  -3.509  1.00 52.16           C  
ANISOU  572  CB  VAL A  75    10552   3935   5331    458  -1106    935       C  
ATOM    573  CG1 VAL A  75      12.502  18.357  -3.900  1.00 50.66           C  
ANISOU  573  CG1 VAL A  75    10379   3863   5006    440  -1115    954       C  
ATOM    574  CG2 VAL A  75      13.270  20.680  -4.199  1.00 52.55           C  
ANISOU  574  CG2 VAL A  75    10693   3935   5340    417  -1121   1014       C  
ATOM    575  N   ARG A  76       9.484  19.080  -2.202  1.00 53.56           N  
ANISOU  575  N   ARG A  76    10496   4101   5752    562  -1084    783       N  
ATOM    576  CA  ARG A  76       8.518  18.081  -1.780  1.00 53.56           C  
ANISOU  576  CA  ARG A  76    10405   4167   5777    569  -1068    732       C  
ATOM    577  C   ARG A  76       7.155  18.233  -2.431  1.00 54.32           C  
ANISOU  577  C   ARG A  76    10404   4219   6018    636  -1167    762       C  
ATOM    578  O   ARG A  76       6.571  17.254  -2.877  1.00 54.28           O  
ANISOU  578  O   ARG A  76    10363   4278   5981    620  -1224    781       O  
ATOM    579  CB  ARG A  76       8.338  18.094  -0.276  1.00 54.04           C  
ANISOU  579  CB  ARG A  76    10406   4254   5871    549   -933    609       C  
ATOM    580  CG  ARG A  76       7.356  17.076   0.160  1.00 54.82           C  
ANISOU  580  CG  ARG A  76    10414   4421   5994    542   -905    567       C  
ATOM    581  CD  ARG A  76       6.733  17.462   1.438  1.00 58.22           C  
ANISOU  581  CD  ARG A  76    10756   4851   6513    543   -783    448       C  
ATOM    582  NE  ARG A  76       5.546  16.644   1.661  1.00 61.10           N  
ANISOU  582  NE  ARG A  76    11009   5265   6943    542   -766    418       N  
ATOM    583  CZ  ARG A  76       5.019  16.396   2.858  1.00 62.15           C  
ANISOU  583  CZ  ARG A  76    11069   5452   7092    508   -637    321       C  
ATOM    584  NH1 ARG A  76       5.574  16.907   3.945  1.00 62.71           N  
ANISOU  584  NH1 ARG A  76    11176   5544   7107    471   -520    237       N  
ATOM    585  NH2 ARG A  76       3.934  15.644   2.961  1.00 63.18           N  
ANISOU  585  NH2 ARG A  76    11091   5626   7287    496   -623    305       N  
ATOM    586  N   ALA A  77       6.629  19.451  -2.455  1.00 55.15           N  
ANISOU  586  N   ALA A  77    10456   4208   6289    709  -1187    766       N  
ATOM    587  CA  ALA A  77       5.384  19.695  -3.159  1.00 56.21           C  
ANISOU  587  CA  ALA A  77    10482   4302   6574    787  -1304    823       C  
ATOM    588  C   ALA A  77       5.509  19.278  -4.636  1.00 56.40           C  
ANISOU  588  C   ALA A  77    10573   4372   6484    766  -1467    960       C  
ATOM    589  O   ALA A  77       4.638  18.572  -5.183  1.00 56.91           O  
ANISOU  589  O   ALA A  77    10563   4506   6555    763  -1563    985       O  
ATOM    590  CB  ALA A  77       4.995  21.141  -3.052  1.00 57.50           C  
ANISOU  590  CB  ALA A  77    10597   4309   6942    884  -1302    830       C  
ATOM    591  N   MET A  78       6.590  19.708  -5.284  1.00 55.82           N  
ANISOU  591  N   MET A  78    10641   4271   6298    737  -1495   1041       N  
ATOM    592  CA  MET A  78       6.762  19.404  -6.696  1.00 55.76           C  
ANISOU  592  CA  MET A  78    10712   4314   6160    707  -1635   1166       C  
ATOM    593  C   MET A  78       6.768  17.886  -6.914  1.00 55.10           C  
ANISOU  593  C   MET A  78    10646   4365   5925    630  -1636   1120       C  
ATOM    594  O   MET A  78       6.067  17.369  -7.783  1.00 56.16           O  
ANISOU  594  O   MET A  78    10753   4559   6027    614  -1758   1163       O  
ATOM    595  CB  MET A  78       8.010  20.091  -7.279  1.00 55.28           C  
ANISOU  595  CB  MET A  78    10802   4211   5991    672  -1632   1252       C  
ATOM    596  CG  MET A  78       7.811  21.575  -7.601  1.00 56.26           C  
ANISOU  596  CG  MET A  78    10929   4185   6263    741  -1692   1354       C  
ATOM    597  SD  MET A  78       9.204  22.428  -8.399  1.00 57.39           S  
ANISOU  597  SD  MET A  78    11250   4272   6282    678  -1693   1478       S  
ATOM    598  CE  MET A  78      10.473  22.247  -7.157  1.00 55.44           C  
ANISOU  598  CE  MET A  78    11044   4049   5971    604  -1497   1330       C  
ATOM    599  N   CYS A  79       7.526  17.147  -6.115  1.00 53.75           N  
ANISOU  599  N   CYS A  79    10516   4239   5666    580  -1503   1033       N  
ATOM    600  CA  CYS A  79       7.584  15.693  -6.318  1.00 53.25           C  
ANISOU  600  CA  CYS A  79    10482   4270   5480    515  -1491    993       C  
ATOM    601  C   CYS A  79       6.254  15.014  -6.094  1.00 54.12           C  
ANISOU  601  C   CYS A  79    10466   4411   5684    512  -1525    942       C  
ATOM    602  O   CYS A  79       5.901  14.071  -6.800  1.00 54.82           O  
ANISOU  602  O   CYS A  79    10570   4559   5700    457  -1590    940       O  
ATOM    603  CB  CYS A  79       8.601  15.049  -5.409  1.00 51.57           C  
ANISOU  603  CB  CYS A  79    10321   4088   5185    480  -1346    930       C  
ATOM    604  SG  CYS A  79      10.216  15.506  -5.873  1.00 51.71           S  
ANISOU  604  SG  CYS A  79    10473   4109   5067    458  -1312    988       S  
ATOM    605  N   THR A  80       5.521  15.465  -5.092  1.00 54.25           N  
ANISOU  605  N   THR A  80    10358   4393   5862    560  -1469    887       N  
ATOM    606  CA  THR A  80       4.215  14.914  -4.874  1.00 55.07           C  
ANISOU  606  CA  THR A  80    10319   4533   6072    554  -1494    841       C  
ATOM    607  C   THR A  80       3.465  14.971  -6.186  1.00 56.65           C  
ANISOU  607  C   THR A  80    10482   4760   6283    556  -1681    922       C  
ATOM    608  O   THR A  80       2.908  13.964  -6.627  1.00 57.30           O  
ANISOU  608  O   THR A  80    10538   4914   6320    485  -1738    900       O  
ATOM    609  CB  THR A  80       3.454  15.704  -3.818  1.00 55.84           C  
ANISOU  609  CB  THR A  80    10272   4581   6363    624  -1418    781       C  
ATOM    610  OG1 THR A  80       4.154  15.634  -2.574  1.00 54.83           O  
ANISOU  610  OG1 THR A  80    10187   4452   6194    601  -1250    701       O  
ATOM    611  CG2 THR A  80       2.082  15.142  -3.634  1.00 56.64           C  
ANISOU  611  CG2 THR A  80    10203   4733   6583    613  -1439    736       C  
ATOM    612  N   GLU A  81       3.468  16.140  -6.830  1.00 57.71           N  
ANISOU  612  N   GLU A  81    10621   4838   6469    627  -1781   1020       N  
ATOM    613  CA  GLU A  81       2.740  16.311  -8.101  1.00 59.38           C  
ANISOU  613  CA  GLU A  81    10793   5088   6681    633  -1983   1126       C  
ATOM    614  C   GLU A  81       3.300  15.454  -9.231  1.00 58.92           C  
ANISOU  614  C   GLU A  81    10880   5117   6388    527  -2059   1157       C  
ATOM    615  O   GLU A  81       2.562  14.775  -9.941  1.00 59.96           O  
ANISOU  615  O   GLU A  81    10969   5338   6476    464  -2178   1160       O  
ATOM    616  CB  GLU A  81       2.713  17.775  -8.533  1.00 60.84           C  
ANISOU  616  CB  GLU A  81    10969   5177   6969    737  -2071   1252       C  
ATOM    617  CG  GLU A  81       1.900  18.670  -7.619  1.00 62.06           C  
ANISOU  617  CG  GLU A  81    10956   5233   7392    856  -2018   1220       C  
ATOM    618  CD  GLU A  81       0.486  18.177  -7.475  1.00 65.11           C  
ANISOU  618  CD  GLU A  81    11132   5691   7918    872  -2076   1180       C  
ATOM    619  OE1 GLU A  81      -0.186  17.976  -8.501  1.00 66.37           O  
ANISOU  619  OE1 GLU A  81    11233   5928   8058    857  -2264   1273       O  
ATOM    620  OE2 GLU A  81       0.052  17.965  -6.330  1.00 67.09           O  
ANISOU  620  OE2 GLU A  81    11271   5933   8285    885  -1933   1054       O  
ATOM    621  N   ILE A  82       4.612  15.490  -9.399  1.00 57.47           N  
ANISOU  621  N   ILE A  82    10867   4916   6055    499  -1984   1170       N  
ATOM    622  CA  ILE A  82       5.238  14.701 -10.442  1.00 57.01           C  
ANISOU  622  CA  ILE A  82    10953   4935   5773    403  -2022   1181       C  
ATOM    623  C   ILE A  82       4.891  13.242 -10.256  1.00 56.67           C  
ANISOU  623  C   ILE A  82    10895   4951   5684    319  -1978   1063       C  
ATOM    624  O   ILE A  82       4.583  12.540 -11.224  1.00 57.44           O  
ANISOU  624  O   ILE A  82    11034   5126   5665    233  -2074   1054       O  
ATOM    625  CB  ILE A  82       6.750  14.853 -10.400  1.00 55.89           C  
ANISOU  625  CB  ILE A  82    10965   4766   5505    391  -1903   1187       C  
ATOM    626  CG1 ILE A  82       7.135  16.310 -10.712  1.00 56.31           C  
ANISOU  626  CG1 ILE A  82    11052   4750   5594    449  -1949   1312       C  
ATOM    627  CG2 ILE A  82       7.386  13.862 -11.365  1.00 55.52           C  
ANISOU  627  CG2 ILE A  82    11056   4799   5239    295  -1901   1163       C  
ATOM    628  CD1 ILE A  82       8.562  16.649 -10.399  1.00 54.62           C  
ANISOU  628  CD1 ILE A  82    10947   4500   5305    439  -1816   1310       C  
ATOM    629  N   LEU A  83       4.945  12.790  -9.002  1.00 55.50           N  
ANISOU  629  N   LEU A  83    10696   4767   5624    333  -1830    974       N  
ATOM    630  CA  LEU A  83       4.615  11.413  -8.679  1.00 55.05           C  
ANISOU  630  CA  LEU A  83    10627   4739   5549    254  -1769    873       C  
ATOM    631  C   LEU A  83       3.224  11.121  -9.187  1.00 56.68           C  
ANISOU  631  C   LEU A  83    10710   5005   5822    206  -1909    864       C  
ATOM    632  O   LEU A  83       3.015  10.157  -9.910  1.00 57.58           O  
ANISOU  632  O   LEU A  83    10874   5170   5835    103  -1960    819       O  
ATOM    633  CB  LEU A  83       4.651  11.170  -7.182  1.00 53.99           C  
ANISOU  633  CB  LEU A  83    10429   4564   5519    281  -1609    809       C  
ATOM    634  CG  LEU A  83       4.331   9.727  -6.779  1.00 53.78           C  
ANISOU  634  CG  LEU A  83    10399   4549   5484    196  -1535    726       C  
ATOM    635  CD1 LEU A  83       5.504   8.804  -7.066  1.00 52.42           C  
ANISOU  635  CD1 LEU A  83    10396   4359   5163    156  -1454    706       C  
ATOM    636  CD2 LEU A  83       4.006   9.674  -5.305  1.00 53.05           C  
ANISOU  636  CD2 LEU A  83    10209   4438   5511    218  -1407    685       C  
ATOM    637  N   LYS A  84       2.258  11.956  -8.824  1.00 57.25           N  
ANISOU  637  N   LYS A  84    10612   5071   6070    277  -1970    900       N  
ATOM    638  CA  LYS A  84       0.896  11.681  -9.263  1.00 58.88           C  
ANISOU  638  CA  LYS A  84    10665   5351   6357    233  -2110    896       C  
ATOM    639  C   LYS A  84       0.795  11.559 -10.785  1.00 60.22           C  
ANISOU  639  C   LYS A  84    10905   5604   6371    161  -2301    957       C  
ATOM    640  O   LYS A  84       0.085  10.699 -11.310  1.00 61.67           O  
ANISOU  640  O   LYS A  84    11050   5870   6513     48  -2388    907       O  
ATOM    641  CB  LYS A  84      -0.048  12.747  -8.755  1.00 59.78           C  
ANISOU  641  CB  LYS A  84    10575   5441   6696    348  -2152    941       C  
ATOM    642  CG  LYS A  84      -0.237  12.727  -7.272  1.00 58.98           C  
ANISOU  642  CG  LYS A  84    10379   5289   6741    388  -1967    852       C  
ATOM    643  CD  LYS A  84      -1.365  13.664  -6.916  1.00 61.36           C  
ANISOU  643  CD  LYS A  84    10456   5579   7281    494  -2011    876       C  
ATOM    644  CE  LYS A  84      -1.203  14.203  -5.527  1.00 61.76           C  
ANISOU  644  CE  LYS A  84    10462   5552   7454    570  -1817    805       C  
ATOM    645  NZ  LYS A  84      -1.627  15.627  -5.471  1.00 63.03           N  
ANISOU  645  NZ  LYS A  84    10508   5635   7807    719  -1857    861       N  
ATOM    646  N   MET A  85       1.510  12.418 -11.499  1.00 60.14           N  
ANISOU  646  N   MET A  85    11005   5581   6264    209  -2365   1064       N  
ATOM    647  CA  MET A  85       1.481  12.349 -12.950  1.00 61.35           C  
ANISOU  647  CA  MET A  85    11244   5831   6236    131  -2541   1132       C  
ATOM    648  C   MET A  85       2.178  11.087 -13.481  1.00 60.87           C  
ANISOU  648  C   MET A  85    11361   5811   5957     -8  -2472   1023       C  
ATOM    649  O   MET A  85       1.688  10.471 -14.411  1.00 62.22           O  
ANISOU  649  O   MET A  85    11552   6082   6007   -126  -2596    995       O  
ATOM    650  CB  MET A  85       2.022  13.637 -13.587  1.00 61.53           C  
ANISOU  650  CB  MET A  85    11340   5828   6212    211  -2624   1294       C  
ATOM    651  CG  MET A  85       1.047  14.794 -13.475  1.00 62.78           C  
ANISOU  651  CG  MET A  85    11314   5957   6582    333  -2757   1418       C  
ATOM    652  SD  MET A  85       1.646  16.401 -14.074  1.00 66.29           S  
ANISOU  652  SD  MET A  85    11844   6321   7023    440  -2838   1627       S  
ATOM    653  CE  MET A  85       2.784  16.853 -12.761  1.00 60.71           C  
ANISOU  653  CE  MET A  85    11209   5453   6406    516  -2574   1548       C  
ATOM    654  N   SER A  86       3.295  10.682 -12.883  1.00 59.08           N  
ANISOU  654  N   SER A  86    11255   5508   5685      5  -2276    956       N  
ATOM    655  CA  SER A  86       3.977   9.505 -13.400  1.00 59.18           C  
ANISOU  655  CA  SER A  86    11431   5538   5518   -105  -2197    852       C  
ATOM    656  C   SER A  86       3.055   8.330 -13.293  1.00 60.32           C  
ANISOU  656  C   SER A  86    11509   5706   5703   -214  -2210    734       C  
ATOM    657  O   SER A  86       2.957   7.531 -14.208  1.00 61.74           O  
ANISOU  657  O   SER A  86    11778   5944   5736   -341  -2263    662       O  
ATOM    658  CB  SER A  86       5.240   9.213 -12.632  1.00 57.25           C  
ANISOU  658  CB  SER A  86    11285   5204   5263    -55  -1985    808       C  
ATOM    659  OG  SER A  86       6.124  10.300 -12.724  1.00 56.97           O  
ANISOU  659  OG  SER A  86    11306   5150   5191     26  -1968    909       O  
ATOM    660  N   VAL A  87       2.372   8.227 -12.164  1.00 60.19           N  
ANISOU  660  N   VAL A  87    11341   5645   5884   -176  -2154    708       N  
ATOM    661  CA  VAL A  87       1.384   7.179 -11.959  1.00 61.43           C  
ANISOU  661  CA  VAL A  87    11409   5821   6110   -287  -2162    606       C  
ATOM    662  C   VAL A  87       0.341   7.152 -13.082  1.00 64.13           C  
ANISOU  662  C   VAL A  87    11680   6291   6397   -393  -2385    614       C  
ATOM    663  O   VAL A  87      -0.177   6.083 -13.448  1.00 65.20           O  
ANISOU  663  O   VAL A  87    11825   6461   6487   -545  -2411    506       O  
ATOM    664  CB  VAL A  87       0.659   7.382 -10.639  1.00 60.93           C  
ANISOU  664  CB  VAL A  87    11160   5719   6270   -224  -2090    606       C  
ATOM    665  CG1 VAL A  87      -0.715   6.771 -10.702  1.00 62.87           C  
ANISOU  665  CG1 VAL A  87    11246   6032   6610   -335  -2179    548       C  
ATOM    666  CG2 VAL A  87       1.482   6.799  -9.505  1.00 59.09           C  
ANISOU  666  CG2 VAL A  87    11005   5382   6064   -195  -1868    557       C  
ATOM    667  N   LEU A  88       0.022   8.329 -13.628  1.00 65.16           N  
ANISOU  667  N   LEU A  88    11735   6490   6532   -319  -2553    748       N  
ATOM    668  CA  LEU A  88      -0.964   8.394 -14.689  1.00 67.50           C  
ANISOU  668  CA  LEU A  88    11947   6930   6771   -411  -2792    786       C  
ATOM    669  C   LEU A  88      -0.381   7.979 -16.028  1.00 68.48           C  
ANISOU  669  C   LEU A  88    12276   7133   6610   -536  -2866    761       C  
ATOM    670  O   LEU A  88      -1.116   7.775 -16.977  1.00 70.77           O  
ANISOU  670  O   LEU A  88    12531   7560   6797   -658  -3058    762       O  
ATOM    671  CB  LEU A  88      -1.574   9.788 -14.794  1.00 68.63           C  
ANISOU  671  CB  LEU A  88    11925   7111   7039   -276  -2956    959       C  
ATOM    672  CG  LEU A  88      -2.649  10.161 -13.777  1.00 68.93           C  
ANISOU  672  CG  LEU A  88    11697   7126   7366   -185  -2950    971       C  
ATOM    673  CD1 LEU A  88      -3.362  11.447 -14.195  1.00 70.50           C  
ANISOU  673  CD1 LEU A  88    11731   7375   7681    -63  -3152   1146       C  
ATOM    674  CD2 LEU A  88      -3.639   9.044 -13.636  1.00 69.80           C  
ANISOU  674  CD2 LEU A  88    11683   7308   7530   -333  -2969    847       C  
ATOM    675  N   ASN A  89       0.932   7.857 -16.124  1.00 67.19           N  
ANISOU  675  N   ASN A  89    12321   6899   6311   -515  -2714    735       N  
ATOM    676  CA  ASN A  89       1.512   7.515 -17.410  1.00 68.72           C  
ANISOU  676  CA  ASN A  89    12710   7174   6226   -633  -2762    702       C  
ATOM    677  C   ASN A  89       1.114   6.122 -17.832  1.00 70.47           C  
ANISOU  677  C   ASN A  89    12988   7432   6355   -823  -2754    517       C  
ATOM    678  O   ASN A  89       1.160   5.190 -17.046  1.00 69.73           O  
ANISOU  678  O   ASN A  89    12895   7228   6370   -846  -2593    391       O  
ATOM    679  CB  ASN A  89       3.025   7.619 -17.395  1.00 67.02           C  
ANISOU  679  CB  ASN A  89    12687   6877   5900   -571  -2578    698       C  
ATOM    680  CG  ASN A  89       3.596   7.758 -18.783  1.00 68.35           C  
ANISOU  680  CG  ASN A  89    13031   7155   5784   -660  -2649    722       C  
ATOM    681  OD1 ASN A  89       3.084   8.532 -19.582  1.00 70.85           O  
ANISOU  681  OD1 ASN A  89    13314   7592   6015   -681  -2857    854       O  
ATOM    682  ND2 ASN A  89       4.656   7.021 -19.082  1.00 67.36           N  
ANISOU  682  ND2 ASN A  89    13092   6991   5510   -711  -2476    602       N  
ATOM    683  N   GLN A  90       0.729   5.963 -19.083  1.00 73.35           N  
ANISOU  683  N   GLN A  90    13410   7948   6513   -972  -2929    501       N  
ATOM    684  CA  GLN A  90       0.227   4.666 -19.532  1.00 75.51           C  
ANISOU  684  CA  GLN A  90    13730   8261   6700  -1179  -2940    308       C  
ATOM    685  C   GLN A  90       1.177   3.517 -19.172  1.00 73.89           C  
ANISOU  685  C   GLN A  90    13705   7895   6477  -1210  -2669    127       C  
ATOM    686  O   GLN A  90       0.748   2.482 -18.666  1.00 74.00           O  
ANISOU  686  O   GLN A  90    13690   7824   6602  -1295  -2585    -11       O  
ATOM    687  CB  GLN A  90      -0.044   4.687 -21.037  1.00 78.68           C  
ANISOU  687  CB  GLN A  90    14219   8860   6814  -1347  -3147    305       C  
ATOM    688  CG  GLN A  90      -0.690   3.422 -21.573  1.00 83.19           C  
ANISOU  688  CG  GLN A  90    14829   9493   7288  -1589  -3188     96       C  
ATOM    689  CD  GLN A  90      -0.418   3.247 -23.069  1.00 89.06           C  
ANISOU  689  CD  GLN A  90    15764  10401   7673  -1766  -3294     34       C  
ATOM    690  OE1 GLN A  90      -1.260   2.743 -23.819  1.00 92.51           O  
ANISOU  690  OE1 GLN A  90    16179  10989   7981  -1974  -3467    -55       O  
ATOM    691  NE2 GLN A  90       0.767   3.674 -23.508  1.00 88.91           N  
ANISOU  691  NE2 GLN A  90    15931  10368   7481  -1697  -3188     80       N  
ATOM    692  N   GLU A  91       2.466   3.702 -19.436  1.00 72.41           N  
ANISOU  692  N   GLU A  91    13694   7659   6158  -1141  -2532    135       N  
ATOM    693  CA  GLU A  91       3.452   2.665 -19.174  1.00 70.97           C  
ANISOU  693  CA  GLU A  91    13675   7325   5964  -1147  -2278    -22       C  
ATOM    694  C   GLU A  91       3.434   2.262 -17.713  1.00 68.95           C  
ANISOU  694  C   GLU A  91    13321   6899   5978  -1043  -2122    -29       C  
ATOM    695  O   GLU A  91       3.625   1.098 -17.405  1.00 69.30           O  
ANISOU  695  O   GLU A  91    13441   6816   6073  -1100  -1968   -173       O  
ATOM    696  CB  GLU A  91       4.862   3.117 -19.559  1.00 70.12           C  
ANISOU  696  CB  GLU A  91    13726   7205   5711  -1057  -2153     20       C  
ATOM    697  CG  GLU A  91       5.145   3.204 -21.048  1.00 72.25           C  
ANISOU  697  CG  GLU A  91    14156   7626   5670  -1188  -2232    -18       C  
ATOM    698  CD  GLU A  91       4.647   4.485 -21.666  1.00 74.31           C  
ANISOU  698  CD  GLU A  91    14344   8060   5831  -1180  -2476    182       C  
ATOM    699  OE1 GLU A  91       5.350   5.026 -22.549  1.00 75.02           O  
ANISOU  699  OE1 GLU A  91    14563   8243   5698  -1197  -2487    243       O  
ATOM    700  OE2 GLU A  91       3.559   4.959 -21.273  1.00 75.87           O  
ANISOU  700  OE2 GLU A  91    14352   8298   6178  -1154  -2652    285       O  
ATOM    701  N   SER A  92       3.221   3.219 -16.811  1.00 67.07           N  
ANISOU  701  N   SER A  92    12923   6652   5908   -894  -2155    127       N  
ATOM    702  CA  SER A  92       3.092   2.921 -15.384  1.00 64.88           C  
ANISOU  702  CA  SER A  92    12541   6244   5868   -809  -2023    131       C  
ATOM    703  C   SER A  92       1.857   2.067 -15.104  1.00 66.12           C  
ANISOU  703  C   SER A  92    12588   6394   6140   -944  -2068     37       C  
ATOM    704  O   SER A  92       1.966   0.978 -14.531  1.00 66.16           O  
ANISOU  704  O   SER A  92    12643   6269   6227   -990  -1914    -65       O  
ATOM    705  CB  SER A  92       3.012   4.216 -14.590  1.00 63.38           C  
ANISOU  705  CB  SER A  92    12203   6069   5812   -644  -2062    297       C  
ATOM    706  OG  SER A  92       4.023   5.123 -14.994  1.00 62.27           O  
ANISOU  706  OG  SER A  92    12152   5950   5557   -548  -2054    392       O  
ATOM    707  N   ILE A  93       0.684   2.559 -15.507  1.00 67.24           N  
ANISOU  707  N   ILE A  93    12574   6676   6298  -1008  -2282     83       N  
ATOM    708  CA  ILE A  93      -0.548   1.775 -15.413  1.00 68.66           C  
ANISOU  708  CA  ILE A  93    12633   6884   6571  -1166  -2349    -11       C  
ATOM    709  C   ILE A  93      -0.295   0.336 -15.877  1.00 69.66           C  
ANISOU  709  C   ILE A  93    12941   6927   6602  -1341  -2245   -206       C  
ATOM    710  O   ILE A  93      -0.639  -0.636 -15.196  1.00 69.71           O  
ANISOU  710  O   ILE A  93    12928   6816   6742  -1416  -2129   -296       O  
ATOM    711  CB  ILE A  93      -1.677   2.334 -16.303  1.00 70.90           C  
ANISOU  711  CB  ILE A  93    12772   7370   6799  -1256  -2628     39       C  
ATOM    712  CG1 ILE A  93      -1.724   3.863 -16.277  1.00 70.01           C  
ANISOU  712  CG1 ILE A  93    12537   7337   6726  -1079  -2755    240       C  
ATOM    713  CG2 ILE A  93      -3.014   1.761 -15.865  1.00 72.02           C  
ANISOU  713  CG2 ILE A  93    12712   7544   7108  -1380  -2687    -23       C  
ATOM    714  CD1 ILE A  93      -2.894   4.413 -15.513  1.00 69.56           C  
ANISOU  714  CD1 ILE A  93    12197   7321   6910  -1015  -2840    321       C  
ATOM    715  N   ALA A  94       0.307   0.209 -17.049  1.00 70.39           N  
ANISOU  715  N   ALA A  94    13215   7071   6460  -1411  -2276   -272       N  
ATOM    716  CA  ALA A  94       0.570  -1.103 -17.632  1.00 71.66           C  
ANISOU  716  CA  ALA A  94    13563   7151   6515  -1581  -2173   -481       C  
ATOM    717  C   ALA A  94       1.347  -2.030 -16.693  1.00 70.40           C  
ANISOU  717  C   ALA A  94    13505   6749   6496  -1513  -1901   -547       C  
ATOM    718  O   ALA A  94       1.007  -3.194 -16.547  1.00 71.59           O  
ANISOU  718  O   ALA A  94    13703   6780   6717  -1648  -1815   -690       O  
ATOM    719  CB  ALA A  94       1.303  -0.953 -18.947  1.00 72.46           C  
ANISOU  719  CB  ALA A  94    13855   7343   6332  -1633  -2208   -534       C  
ATOM    720  N   SER A  95       2.389  -1.514 -16.054  1.00 68.34           N  
ANISOU  720  N   SER A  95    13273   6413   6280  -1308  -1771   -436       N  
ATOM    721  CA  SER A  95       3.256  -2.346 -15.216  1.00 67.48           C  
ANISOU  721  CA  SER A  95    13261   6089   6288  -1224  -1526   -473       C  
ATOM    722  C   SER A  95       2.530  -2.959 -14.023  1.00 67.49           C  
ANISOU  722  C   SER A  95    13148   5978   6517  -1248  -1461   -461       C  
ATOM    723  O   SER A  95       2.976  -3.954 -13.468  1.00 67.43           O  
ANISOU  723  O   SER A  95    13233   5782   6607  -1240  -1279   -514       O  
ATOM    724  CB  SER A  95       4.416  -1.518 -14.680  1.00 65.03           C  
ANISOU  724  CB  SER A  95    12960   5762   5988  -1003  -1435   -330       C  
ATOM    725  OG  SER A  95       3.968  -0.745 -13.588  1.00 63.26           O  
ANISOU  725  OG  SER A  95    12553   5566   5917   -899  -1477   -183       O  
ATOM    726  N   GLY A  96       1.430  -2.344 -13.605  1.00 67.93           N  
ANISOU  726  N   GLY A  96    12999   6147   6664  -1268  -1601   -380       N  
ATOM    727  CA  GLY A  96       0.701  -2.821 -12.437  1.00 68.11           C  
ANISOU  727  CA  GLY A  96    12897   6089   6894  -1296  -1533   -358       C  
ATOM    728  C   GLY A  96       1.485  -2.675 -11.140  1.00 66.40           C  
ANISOU  728  C   GLY A  96    12677   5760   6793  -1115  -1363   -240       C  
ATOM    729  O   GLY A  96       1.094  -3.213 -10.114  1.00 66.38           O  
ANISOU  729  O   GLY A  96    12613   5668   6941  -1136  -1266   -219       O  
ATOM    730  N   ASN A  97       2.585  -1.929 -11.171  1.00 65.07           N  
ANISOU  730  N   ASN A  97    12570   5608   6546   -947  -1330   -159       N  
ATOM    731  CA  ASN A  97       3.425  -1.789  -9.993  1.00 63.37           C  
ANISOU  731  CA  ASN A  97    12357   5306   6415   -786  -1181    -51       C  
ATOM    732  C   ASN A  97       3.386  -0.423  -9.361  1.00 61.99           C  
ANISOU  732  C   ASN A  97    12038   5244   6271   -653  -1244     85       C  
ATOM    733  O   ASN A  97       4.089  -0.171  -8.390  1.00 60.55           O  
ANISOU  733  O   ASN A  97    11851   5019   6137   -528  -1138    172       O  
ATOM    734  CB  ASN A  97       4.857  -2.094 -10.351  1.00 62.83           C  
ANISOU  734  CB  ASN A  97    12465   5150   6258   -695  -1062    -67       C  
ATOM    735  CG  ASN A  97       5.026  -3.496 -10.775  1.00 66.06           C  
ANISOU  735  CG  ASN A  97    13026   5402   6673   -797   -953   -203       C  
ATOM    736  OD1 ASN A  97       6.103  -3.902 -11.195  1.00 68.46           O  
ANISOU  736  OD1 ASN A  97    13473   5621   6917   -736   -844   -247       O  
ATOM    737  ND2 ASN A  97       3.944  -4.278 -10.680  1.00 68.65           N  
ANISOU  737  ND2 ASN A  97    13319   5680   7085   -959   -973   -281       N  
ATOM    738  N   PHE A  98       2.591   0.482  -9.911  1.00 62.37           N  
ANISOU  738  N   PHE A  98    11970   5435   6294   -677  -1418    104       N  
ATOM    739  CA  PHE A  98       2.602   1.833  -9.394  1.00 61.07           C  
ANISOU  739  CA  PHE A  98    11683   5352   6171   -541  -1468    223       C  
ATOM    740  C   PHE A  98       1.185   2.314  -9.136  1.00 62.28           C  
ANISOU  740  C   PHE A  98    11624   5597   6444   -584  -1584    240       C  
ATOM    741  O   PHE A  98       0.743   3.327  -9.678  1.00 62.99           O  
ANISOU  741  O   PHE A  98    11620   5793   6522   -547  -1738    293       O  
ATOM    742  CB  PHE A  98       3.369   2.763 -10.338  1.00 60.51           C  
ANISOU  742  CB  PHE A  98    11690   5349   5954   -468  -1551    271       C  
ATOM    743  CG  PHE A  98       4.760   2.289 -10.654  1.00 59.73           C  
ANISOU  743  CG  PHE A  98    11779   5174   5741   -429  -1427    244       C  
ATOM    744  CD1 PHE A  98       4.991   1.414 -11.715  1.00 59.92           C  
ANISOU  744  CD1 PHE A  98    11949   5176   5644   -534  -1420    132       C  
ATOM    745  CD2 PHE A  98       5.834   2.706  -9.890  1.00 57.55           C  
ANISOU  745  CD2 PHE A  98    11527   4856   5482   -293  -1313    322       C  
ATOM    746  CE1 PHE A  98       6.260   0.970 -12.004  1.00 59.47           C  
ANISOU  746  CE1 PHE A  98    12049   5046   5501   -487  -1287     98       C  
ATOM    747  CE2 PHE A  98       7.110   2.260 -10.175  1.00 56.78           C  
ANISOU  747  CE2 PHE A  98    11575   4699   5300   -249  -1197    301       C  
ATOM    748  CZ  PHE A  98       7.321   1.392 -11.236  1.00 58.34           C  
ANISOU  748  CZ  PHE A  98    11909   4866   5394   -338  -1177    189       C  
ATOM    749  N   ASP A  99       0.475   1.544  -8.319  1.00 63.08           N  
ANISOU  749  N   ASP A  99    11646   5652   6669   -662  -1505    201       N  
ATOM    750  CA  ASP A  99      -0.843   1.876  -7.824  1.00 64.41           C  
ANISOU  750  CA  ASP A  99    11592   5900   6983   -700  -1565    211       C  
ATOM    751  C   ASP A  99      -0.649   2.885  -6.706  1.00 63.09           C  
ANISOU  751  C   ASP A  99    11329   5743   6901   -545  -1491    299       C  
ATOM    752  O   ASP A  99      -0.084   2.568  -5.657  1.00 61.90           O  
ANISOU  752  O   ASP A  99    11229   5516   6773   -505  -1328    320       O  
ATOM    753  CB  ASP A  99      -1.522   0.606  -7.299  1.00 65.94           C  
ANISOU  753  CB  ASP A  99    11760   6028   7267   -855  -1471    136       C  
ATOM    754  CG  ASP A  99      -2.873   0.872  -6.649  1.00 68.30           C  
ANISOU  754  CG  ASP A  99    11810   6412   7728   -902  -1497    142       C  
ATOM    755  OD1 ASP A  99      -3.563  -0.111  -6.295  1.00 70.86           O  
ANISOU  755  OD1 ASP A  99    12092   6701   8132  -1052  -1433     83       O  
ATOM    756  OD2 ASP A  99      -3.254   2.052  -6.492  1.00 69.59           O  
ANISOU  756  OD2 ASP A  99    11816   6671   7953   -791  -1572    202       O  
ATOM    757  N   TYR A 100      -1.111   4.110  -6.938  1.00 63.34           N  
ANISOU  757  N   TYR A 100    11224   5866   6978   -460  -1614    352       N  
ATOM    758  CA  TYR A 100      -0.877   5.206  -6.003  1.00 62.15           C  
ANISOU  758  CA  TYR A 100    10997   5714   6903   -311  -1547    417       C  
ATOM    759  C   TYR A 100      -1.360   4.892  -4.580  1.00 61.93           C  
ANISOU  759  C   TYR A 100    10864   5669   6999   -328  -1387    395       C  
ATOM    760  O   TYR A 100      -0.817   5.396  -3.593  1.00 60.73           O  
ANISOU  760  O   TYR A 100    10723   5492   6859   -237  -1269    426       O  
ATOM    761  CB  TYR A 100      -1.531   6.476  -6.526  1.00 62.88           C  
ANISOU  761  CB  TYR A 100    10939   5886   7065   -228  -1707    471       C  
ATOM    762  CG  TYR A 100      -1.192   7.710  -5.739  1.00 62.61           C  
ANISOU  762  CG  TYR A 100    10855   5827   7105    -72  -1643    525       C  
ATOM    763  CD1 TYR A 100       0.016   8.360  -5.919  1.00 61.86           C  
ANISOU  763  CD1 TYR A 100    10910   5687   6907     19  -1628    578       C  
ATOM    764  CD2 TYR A 100      -2.081   8.230  -4.818  1.00 63.74           C  
ANISOU  764  CD2 TYR A 100    10800   5992   7425    -25  -1588    510       C  
ATOM    765  CE1 TYR A 100       0.325   9.495  -5.202  1.00 61.45           C  
ANISOU  765  CE1 TYR A 100    10820   5603   6925    142  -1568    612       C  
ATOM    766  CE2 TYR A 100      -1.776   9.360  -4.102  1.00 63.41           C  
ANISOU  766  CE2 TYR A 100    10725   5916   7452    108  -1517    534       C  
ATOM    767  CZ  TYR A 100      -0.574   9.991  -4.297  1.00 63.00           C  
ANISOU  767  CZ  TYR A 100    10833   5811   7294    186  -1512    584       C  
ATOM    768  OH  TYR A 100      -0.256  11.128  -3.581  1.00 64.98           O  
ANISOU  768  OH  TYR A 100    11059   6018   7614    299  -1439    594       O  
ATOM    769  N   ALA A 101      -2.379   4.048  -4.483  1.00 63.10           N  
ANISOU  769  N   ALA A 101    10911   5838   7225   -462  -1382    340       N  
ATOM    770  CA  ALA A 101      -2.967   3.709  -3.204  1.00 63.26           C  
ANISOU  770  CA  ALA A 101    10821   5859   7357   -504  -1230    322       C  
ATOM    771  C   ALA A 101      -1.998   2.872  -2.415  1.00 62.35           C  
ANISOU  771  C   ALA A 101    10884   5644   7160   -522  -1061    341       C  
ATOM    772  O   ALA A 101      -2.141   2.711  -1.209  1.00 62.53           O  
ANISOU  772  O   ALA A 101    10863   5665   7229   -534   -915    354       O  
ATOM    773  CB  ALA A 101      -4.259   2.953  -3.408  1.00 65.05           C  
ANISOU  773  CB  ALA A 101    10901   6133   7684   -666  -1271    261       C  
ATOM    774  N   VAL A 102      -1.005   2.326  -3.103  1.00 61.73           N  
ANISOU  774  N   VAL A 102    11006   5490   6960   -524  -1080    346       N  
ATOM    775  CA  VAL A 102      -0.032   1.484  -2.434  1.00 60.69           C  
ANISOU  775  CA  VAL A 102    11038   5255   6767   -524   -932    380       C  
ATOM    776  C   VAL A 102       1.234   2.269  -2.207  1.00 59.09           C  
ANISOU  776  C   VAL A 102    10928   5050   6474   -372   -907    444       C  
ATOM    777  O   VAL A 102       1.707   2.402  -1.090  1.00 58.39           O  
ANISOU  777  O   VAL A 102    10850   4960   6377   -322   -794    496       O  
ATOM    778  CB  VAL A 102       0.326   0.262  -3.268  1.00 61.18           C  
ANISOU  778  CB  VAL A 102    11261   5212   6773   -617   -938    336       C  
ATOM    779  CG1 VAL A 102       1.390  -0.536  -2.560  1.00 60.11           C  
ANISOU  779  CG1 VAL A 102    11282   4957   6598   -583   -788    393       C  
ATOM    780  CG2 VAL A 102      -0.899  -0.565  -3.511  1.00 62.50           C  
ANISOU  780  CG2 VAL A 102    11345   5376   7026   -794   -963    261       C  
ATOM    781  N   ILE A 103       1.786   2.771  -3.302  1.00 58.84           N  
ANISOU  781  N   ILE A 103    10965   5028   6364   -316  -1017    440       N  
ATOM    782  CA  ILE A 103       3.015   3.537  -3.291  1.00 57.42           C  
ANISOU  782  CA  ILE A 103    10872   4849   6096   -189  -1007    496       C  
ATOM    783  C   ILE A 103       2.963   4.641  -2.252  1.00 56.73           C  
ANISOU  783  C   ILE A 103    10680   4818   6057   -105   -964    532       C  
ATOM    784  O   ILE A 103       3.914   4.881  -1.511  1.00 55.70           O  
ANISOU  784  O   ILE A 103    10609   4681   5874    -40   -880    577       O  
ATOM    785  CB  ILE A 103       3.162   4.242  -4.613  1.00 57.53           C  
ANISOU  785  CB  ILE A 103    10912   4900   6045   -158  -1153    489       C  
ATOM    786  CG1 ILE A 103       3.638   3.288  -5.682  1.00 58.01           C  
ANISOU  786  CG1 ILE A 103    11125   4910   6008   -223  -1173    444       C  
ATOM    787  CG2 ILE A 103       4.162   5.348  -4.510  1.00 57.14           C  
ANISOU  787  CG2 ILE A 103    10901   4869   5939    -35  -1150    550       C  
ATOM    788  CD1 ILE A 103       3.839   4.037  -6.971  1.00 59.45           C  
ANISOU  788  CD1 ILE A 103    11345   5151   6093   -202  -1311    449       C  
ATOM    789  N   LYS A 104       1.841   5.337  -2.236  1.00 57.39           N  
ANISOU  789  N   LYS A 104    10601   4961   6244   -108  -1025    505       N  
ATOM    790  CA  LYS A 104       1.701   6.523  -1.435  1.00 57.10           C  
ANISOU  790  CA  LYS A 104    10461   4966   6269    -22   -990    513       C  
ATOM    791  C   LYS A 104       1.844   6.253   0.074  1.00 56.66           C  
ANISOU  791  C   LYS A 104    10395   4920   6214    -39   -821    515       C  
ATOM    792  O   LYS A 104       2.665   6.877   0.759  1.00 55.78           O  
ANISOU  792  O   LYS A 104    10328   4818   6047     27   -759    538       O  
ATOM    793  CB  LYS A 104       0.352   7.150  -1.730  1.00 58.73           C  
ANISOU  793  CB  LYS A 104    10475   5223   6617    -20  -1078    480       C  
ATOM    794  CG  LYS A 104       0.369   8.636  -1.578  1.00 60.10           C  
ANISOU  794  CG  LYS A 104    10574   5406   6855    103  -1104    493       C  
ATOM    795  CD  LYS A 104       1.211   8.981  -0.371  1.00 62.34           C  
ANISOU  795  CD  LYS A 104    10921   5677   7089    144   -954    490       C  
ATOM    796  CE  LYS A 104       1.711  10.411  -0.459  1.00 63.06           C  
ANISOU  796  CE  LYS A 104    11020   5743   7198    258   -987    506       C  
ATOM    797  NZ  LYS A 104       1.542  11.021   0.889  1.00 64.73           N  
ANISOU  797  NZ  LYS A 104    11157   5970   7468    283   -843    447       N  
ATOM    798  N   PRO A 105       1.027   5.338   0.611  1.00 57.29           N  
ANISOU  798  N   PRO A 105    10413   5006   6348   -141   -748    492       N  
ATOM    799  CA  PRO A 105       1.228   5.028   2.019  1.00 56.83           C  
ANISOU  799  CA  PRO A 105    10366   4967   6259   -169   -589    513       C  
ATOM    800  C   PRO A 105       2.619   4.440   2.250  1.00 55.69           C  
ANISOU  800  C   PRO A 105    10403   4775   5982   -146   -544    590       C  
ATOM    801  O   PRO A 105       3.232   4.716   3.277  1.00 55.35           O  
ANISOU  801  O   PRO A 105    10389   4771   5870   -118   -458    626       O  
ATOM    802  CB  PRO A 105       0.126   4.013   2.328  1.00 57.99           C  
ANISOU  802  CB  PRO A 105    10433   5115   6485   -302   -529    490       C  
ATOM    803  CG  PRO A 105      -0.451   3.595   1.010  1.00 58.91           C  
ANISOU  803  CG  PRO A 105    10527   5201   6656   -354   -664    454       C  
ATOM    804  CD  PRO A 105      -0.165   4.690   0.038  1.00 58.58           C  
ANISOU  804  CD  PRO A 105    10477   5176   6604   -244   -806    448       C  
ATOM    805  N   ALA A 106       3.117   3.651   1.301  1.00 55.24           N  
ANISOU  805  N   ALA A 106    10461   4640   5888   -159   -602    609       N  
ATOM    806  CA  ALA A 106       4.454   3.093   1.410  1.00 54.65           C  
ANISOU  806  CA  ALA A 106    10539   4512   5713   -116   -562    682       C  
ATOM    807  C   ALA A 106       5.461   4.221   1.643  1.00 53.73           C  
ANISOU  807  C   ALA A 106    10440   4452   5521    -10   -576    710       C  
ATOM    808  O   ALA A 106       6.349   4.136   2.495  1.00 53.37           O  
ANISOU  808  O   ALA A 106    10446   4430   5401     20   -508    776       O  
ATOM    809  CB  ALA A 106       4.804   2.285   0.148  1.00 54.36           C  
ANISOU  809  CB  ALA A 106    10612   4382   5661   -131   -621    666       C  
ATOM    810  N   ILE A 107       5.306   5.292   0.887  1.00 53.55           N  
ANISOU  810  N   ILE A 107    10372   4455   5520     40   -671    666       N  
ATOM    811  CA  ILE A 107       6.197   6.419   1.010  1.00 53.09           C  
ANISOU  811  CA  ILE A 107    10333   4434   5407    123   -686    683       C  
ATOM    812  C   ILE A 107       6.052   7.106   2.370  1.00 53.68           C  
ANISOU  812  C   ILE A 107    10335   4577   5484    125   -600    668       C  
ATOM    813  O   ILE A 107       7.044   7.479   3.014  1.00 53.29           O  
ANISOU  813  O   ILE A 107    10333   4567   5349    154   -560    701       O  
ATOM    814  CB  ILE A 107       5.952   7.404  -0.129  1.00 53.04           C  
ANISOU  814  CB  ILE A 107    10298   4421   5435    167   -807    653       C  
ATOM    815  CG1 ILE A 107       6.386   6.743  -1.457  1.00 52.89           C  
ANISOU  815  CG1 ILE A 107    10382   4355   5357    157   -881    666       C  
ATOM    816  CG2 ILE A 107       6.656   8.719   0.143  1.00 51.53           C  
ANISOU  816  CG2 ILE A 107    10107   4255   5218    238   -810    662       C  
ATOM    817  CD1 ILE A 107       6.158   7.569  -2.697  1.00 53.22           C  
ANISOU  817  CD1 ILE A 107    10416   4404   5402    182  -1012    659       C  
ATOM    818  N   ASP A 108       4.815   7.265   2.820  1.00 54.84           N  
ANISOU  818  N   ASP A 108    10362   4749   5725     84   -565    611       N  
ATOM    819  CA  ASP A 108       4.585   7.799   4.157  1.00 55.49           C  
ANISOU  819  CA  ASP A 108    10380   4902   5801     69   -456    576       C  
ATOM    820  C   ASP A 108       5.264   6.908   5.200  1.00 55.58           C  
ANISOU  820  C   ASP A 108    10472   4952   5692     16   -360    649       C  
ATOM    821  O   ASP A 108       5.915   7.392   6.128  1.00 55.63           O  
ANISOU  821  O   ASP A 108    10501   5029   5606     20   -304    657       O  
ATOM    822  CB  ASP A 108       3.096   7.844   4.443  1.00 56.83           C  
ANISOU  822  CB  ASP A 108    10400   5094   6100     23   -412    503       C  
ATOM    823  CG  ASP A 108       2.392   8.867   3.618  1.00 58.02           C  
ANISOU  823  CG  ASP A 108    10443   5219   6382     91   -505    446       C  
ATOM    824  OD1 ASP A 108       3.074   9.656   2.931  1.00 58.99           O  
ANISOU  824  OD1 ASP A 108    10621   5306   6487    169   -592    463       O  
ATOM    825  OD2 ASP A 108       1.152   8.880   3.647  1.00 60.09           O  
ANISOU  825  OD2 ASP A 108    10558   5500   6772     67   -493    393       O  
ATOM    826  N   LYS A 109       5.087   5.602   5.047  1.00 55.66           N  
ANISOU  826  N   LYS A 109    10526   4916   5707    -39   -346    705       N  
ATOM    827  CA  LYS A 109       5.721   4.659   5.920  1.00 55.79           C  
ANISOU  827  CA  LYS A 109    10624   4946   5626    -78   -270    806       C  
ATOM    828  C   LYS A 109       7.224   4.917   5.920  1.00 54.78           C  
ANISOU  828  C   LYS A 109    10588   4837   5391     -1   -306    874       C  
ATOM    829  O   LYS A 109       7.847   4.988   6.977  1.00 54.99           O  
ANISOU  829  O   LYS A 109    10635   4947   5310    -12   -255    932       O  
ATOM    830  CB  LYS A 109       5.410   3.229   5.455  1.00 56.46           C  
ANISOU  830  CB  LYS A 109    10763   4929   5762   -133   -264    856       C  
ATOM    831  CG  LYS A 109       5.720   2.180   6.470  1.00 57.33           C  
ANISOU  831  CG  LYS A 109    10939   5035   5809   -187   -171    974       C  
ATOM    832  CD  LYS A 109       6.023   0.855   5.829  1.00 59.00           C  
ANISOU  832  CD  LYS A 109    11254   5102   6062   -194   -180   1041       C  
ATOM    833  CE  LYS A 109       6.214  -0.202   6.914  1.00 62.09           C  
ANISOU  833  CE  LYS A 109    11707   5473   6410   -248    -84   1183       C  
ATOM    834  NZ  LYS A 109       7.332  -1.090   6.574  1.00 63.10           N  
ANISOU  834  NZ  LYS A 109    11956   5486   6532   -174    -99   1292       N  
ATOM    835  N   PHE A 110       7.809   5.063   4.734  1.00 53.91           N  
ANISOU  835  N   PHE A 110    10523   4662   5297     67   -395    869       N  
ATOM    836  CA  PHE A 110       9.265   5.223   4.634  1.00 53.18           C  
ANISOU  836  CA  PHE A 110    10503   4588   5116    136   -424    936       C  
ATOM    837  C   PHE A 110       9.740   6.434   5.409  1.00 53.22           C  
ANISOU  837  C   PHE A 110    10470   4701   5048    146   -415    910       C  
ATOM    838  O   PHE A 110      10.693   6.357   6.183  1.00 53.21           O  
ANISOU  838  O   PHE A 110    10497   4774   4945    150   -394    983       O  
ATOM    839  CB  PHE A 110       9.724   5.357   3.183  1.00 52.13           C  
ANISOU  839  CB  PHE A 110    10416   4384   5009    195   -507    914       C  
ATOM    840  CG  PHE A 110      11.197   5.609   3.045  1.00 50.84           C  
ANISOU  840  CG  PHE A 110    10301   4250   4765    262   -525    973       C  
ATOM    841  CD1 PHE A 110      11.685   6.915   2.954  1.00 50.45           C  
ANISOU  841  CD1 PHE A 110    10227   4259   4681    288   -564    938       C  
ATOM    842  CD2 PHE A 110      12.101   4.555   3.025  1.00 50.00           C  
ANISOU  842  CD2 PHE A 110    10259   4107   4632    300   -498   1064       C  
ATOM    843  CE1 PHE A 110      13.054   7.168   2.836  1.00 48.63           C  
ANISOU  843  CE1 PHE A 110    10026   4070   4382    334   -578    990       C  
ATOM    844  CE2 PHE A 110      13.462   4.779   2.911  1.00 49.41           C  
ANISOU  844  CE2 PHE A 110    10202   4074   4497    365   -511   1120       C  
ATOM    845  CZ  PHE A 110      13.946   6.086   2.815  1.00 49.37           C  
ANISOU  845  CZ  PHE A 110    10164   4148   4448    374   -552   1082       C  
ATOM    846  N   ALA A 111       9.074   7.560   5.179  1.00 53.44           N  
ANISOU  846  N   ALA A 111    10434   4734   5137    149   -436    806       N  
ATOM    847  CA  ALA A 111       9.364   8.798   5.889  1.00 53.72           C  
ANISOU  847  CA  ALA A 111    10437   4845   5128    147   -414    749       C  
ATOM    848  C   ALA A 111       9.305   8.630   7.402  1.00 54.99           C  
ANISOU  848  C   ALA A 111    10583   5116   5195     75   -317    756       C  
ATOM    849  O   ALA A 111      10.214   9.036   8.114  1.00 54.74           O  
ANISOU  849  O   ALA A 111    10577   5175   5047     59   -307    774       O  
ATOM    850  CB  ALA A 111       8.391   9.830   5.480  1.00 53.93           C  
ANISOU  850  CB  ALA A 111    10388   4829   5274    165   -431    640       C  
ATOM    851  N   ARG A 112       8.224   8.038   7.891  1.00 56.44           N  
ANISOU  851  N   ARG A 112    10722   5304   5417     19   -245    740       N  
ATOM    852  CA  ARG A 112       8.043   7.900   9.316  1.00 58.33           C  
ANISOU  852  CA  ARG A 112    10951   5660   5553    -65   -141    744       C  
ATOM    853  C   ARG A 112       9.172   7.101   9.964  1.00 58.45           C  
ANISOU  853  C   ARG A 112    11047   5746   5415    -83   -147    893       C  
ATOM    854  O   ARG A 112       9.732   7.537  10.978  1.00 58.93           O  
ANISOU  854  O   ARG A 112    11118   5936   5335   -129   -118    896       O  
ATOM    855  CB  ARG A 112       6.694   7.268   9.606  1.00 59.87           C  
ANISOU  855  CB  ARG A 112    11083   5842   5824   -130    -58    718       C  
ATOM    856  CG  ARG A 112       5.565   8.263   9.681  1.00 63.16           C  
ANISOU  856  CG  ARG A 112    11383   6263   6352   -134     -4    561       C  
ATOM    857  CD  ARG A 112       4.399   7.696  10.459  1.00 70.33           C  
ANISOU  857  CD  ARG A 112    12217   7221   7283   -229    121    536       C  
ATOM    858  NE  ARG A 112       3.331   7.278   9.566  1.00 74.69           N  
ANISOU  858  NE  ARG A 112    12686   7685   8009   -223     88    512       N  
ATOM    859  CZ  ARG A 112       3.302   6.118   8.916  1.00 76.25           C  
ANISOU  859  CZ  ARG A 112    12929   7806   8238   -244     35    606       C  
ATOM    860  NH1 ARG A 112       4.290   5.236   9.050  1.00 76.48           N  
ANISOU  860  NH1 ARG A 112    13087   7817   8155   -252     15    738       N  
ATOM    861  NH2 ARG A 112       2.279   5.836   8.122  1.00 77.31           N  
ANISOU  861  NH2 ARG A 112    12975   7878   8522   -257     -1    564       N  
ATOM    862  N   GLU A 113       9.506   5.950   9.371  1.00 57.99           N  
ANISOU  862  N   GLU A 113    11043   5602   5389    -47   -188   1012       N  
ATOM    863  CA  GLU A 113      10.561   5.095   9.882  1.00 58.37           C  
ANISOU  863  CA  GLU A 113    11156   5691   5330    -37   -201   1177       C  
ATOM    864  C   GLU A 113      11.879   5.829   9.907  1.00 57.81           C  
ANISOU  864  C   GLU A 113    11093   5702   5169     11   -268   1195       C  
ATOM    865  O   GLU A 113      12.600   5.790  10.887  1.00 58.70           O  
ANISOU  865  O   GLU A 113    11216   5945   5142    -22   -267   1278       O  
ATOM    866  CB  GLU A 113      10.668   3.816   9.063  1.00 58.17           C  
ANISOU  866  CB  GLU A 113    11187   5519   5397     12   -223   1274       C  
ATOM    867  CG  GLU A 113       9.340   3.092   8.946  1.00 60.46           C  
ANISOU  867  CG  GLU A 113    11464   5721   5787    -56   -162   1244       C  
ATOM    868  CD  GLU A 113       9.464   1.711   8.331  1.00 63.79           C  
ANISOU  868  CD  GLU A 113    11959   5989   6289    -33   -165   1340       C  
ATOM    869  OE1 GLU A 113      10.317   1.549   7.424  1.00 64.91           O  
ANISOU  869  OE1 GLU A 113    12146   6055   6463     60   -225   1358       O  
ATOM    870  OE2 GLU A 113       8.708   0.792   8.737  1.00 64.73           O  
ANISOU  870  OE2 GLU A 113    12094   6055   6444   -112    -97   1389       O  
ATOM    871  N   GLN A 114      12.192   6.516   8.830  1.00 57.01           N  
ANISOU  871  N   GLN A 114    10985   5535   5142     77   -329   1121       N  
ATOM    872  CA  GLN A 114      13.399   7.326   8.780  1.00 57.26           C  
ANISOU  872  CA  GLN A 114    11014   5640   5101    106   -386   1123       C  
ATOM    873  C   GLN A 114      13.480   8.410   9.854  1.00 58.06           C  
ANISOU  873  C   GLN A 114    11085   5882   5092     25   -359   1041       C  
ATOM    874  O   GLN A 114      14.510   8.577  10.481  1.00 58.39           O  
ANISOU  874  O   GLN A 114    11128   6049   5010      2   -389   1099       O  
ATOM    875  CB  GLN A 114      13.452   8.014   7.449  1.00 56.33           C  
ANISOU  875  CB  GLN A 114    10896   5422   5086    166   -439   1042       C  
ATOM    876  CG  GLN A 114      13.823   7.100   6.350  1.00 56.87           C  
ANISOU  876  CG  GLN A 114    11006   5385   5219    241   -473   1113       C  
ATOM    877  CD  GLN A 114      15.319   7.055   6.155  1.00 57.17           C  
ANISOU  877  CD  GLN A 114    11052   5470   5199    296   -513   1198       C  
ATOM    878  OE1 GLN A 114      15.976   6.175   6.692  1.00 59.50           O  
ANISOU  878  OE1 GLN A 114    11352   5805   5449    319   -505   1322       O  
ATOM    879  NE2 GLN A 114      15.866   8.000   5.384  1.00 54.76           N  
ANISOU  879  NE2 GLN A 114    10741   5163   4904    317   -554   1143       N  
ATOM    880  N   VAL A 115      12.409   9.177  10.025  1.00 58.49           N  
ANISOU  880  N   VAL A 115    11107   5917   5199    -17   -302    896       N  
ATOM    881  CA  VAL A 115      12.386  10.191  11.044  1.00 59.58           C  
ANISOU  881  CA  VAL A 115    11226   6170   5242   -100   -251    787       C  
ATOM    882  C   VAL A 115      12.587   9.516  12.393  1.00 61.51           C  
ANISOU  882  C   VAL A 115    11487   6574   5309   -187   -206    875       C  
ATOM    883  O   VAL A 115      13.320  10.014  13.240  1.00 62.33           O  
ANISOU  883  O   VAL A 115    11598   6825   5258   -256   -214    864       O  
ATOM    884  CB  VAL A 115      11.059  10.974  11.025  1.00 59.81           C  
ANISOU  884  CB  VAL A 115    11205   6133   5387   -114   -173    618       C  
ATOM    885  CG1 VAL A 115      10.862  11.766  12.315  1.00 60.41           C  
ANISOU  885  CG1 VAL A 115    11268   6333   5352   -216    -76    493       C  
ATOM    886  CG2 VAL A 115      11.018  11.895   9.825  1.00 58.55           C  
ANISOU  886  CG2 VAL A 115    11032   5839   5378    -35   -233    543       C  
ATOM    887  N   SER A 116      11.952   8.369  12.595  1.00 62.64           N  
ANISOU  887  N   SER A 116    11641   6693   5466   -196   -164    970       N  
ATOM    888  CA  SER A 116      11.995   7.745  13.909  1.00 64.92           C  
ANISOU  888  CA  SER A 116    11952   7132   5581   -290   -113   1067       C  
ATOM    889  C   SER A 116      13.387   7.235  14.283  1.00 66.02           C  
ANISOU  889  C   SER A 116    12123   7378   5583   -275   -205   1248       C  
ATOM    890  O   SER A 116      13.680   7.060  15.460  1.00 67.22           O  
ANISOU  890  O   SER A 116    12291   7702   5547   -365   -191   1323       O  
ATOM    891  CB  SER A 116      10.976   6.630  14.014  1.00 65.21           C  
ANISOU  891  CB  SER A 116    11996   7102   5677   -314    -41   1137       C  
ATOM    892  OG  SER A 116      11.438   5.502  13.323  1.00 64.98           O  
ANISOU  892  OG  SER A 116    12006   6961   5721   -232   -106   1301       O  
ATOM    893  N   ILE A 117      14.246   7.010  13.295  1.00 66.15           N  
ANISOU  893  N   ILE A 117    12141   7306   5688   -165   -296   1321       N  
ATOM    894  CA  ILE A 117      15.640   6.717  13.590  1.00 67.90           C  
ANISOU  894  CA  ILE A 117    12358   7638   5803   -137   -386   1476       C  
ATOM    895  C   ILE A 117      16.231   7.791  14.495  1.00 69.95           C  
ANISOU  895  C   ILE A 117    12594   8099   5886   -240   -409   1399       C  
ATOM    896  O   ILE A 117      16.959   7.471  15.416  1.00 71.32           O  
ANISOU  896  O   ILE A 117    12762   8444   5891   -289   -457   1529       O  
ATOM    897  CB  ILE A 117      16.526   6.714  12.350  1.00 66.81           C  
ANISOU  897  CB  ILE A 117    12204   7395   5787    -14   -463   1504       C  
ATOM    898  CG1 ILE A 117      16.041   5.707  11.305  1.00 66.46           C  
ANISOU  898  CG1 ILE A 117    12193   7145   5915     83   -442   1551       C  
ATOM    899  CG2 ILE A 117      17.972   6.455  12.744  1.00 66.50           C  
ANISOU  899  CG2 ILE A 117    12130   7492   5646     15   -551   1662       C  
ATOM    900  CD1 ILE A 117      16.274   4.316  11.663  1.00 68.56           C  
ANISOU  900  CD1 ILE A 117    12488   7384   6177    123   -440   1750       C  
ATOM    901  N   PHE A 118      15.936   9.061  14.228  1.00 71.00           N  
ANISOU  901  N   PHE A 118    12712   8206   6057   -277   -381   1191       N  
ATOM    902  CA  PHE A 118      16.538  10.150  14.993  1.00 73.67           C  
ANISOU  902  CA  PHE A 118    13038   8711   6243   -386   -397   1089       C  
ATOM    903  C   PHE A 118      15.599  10.832  15.964  1.00 76.42           C  
ANISOU  903  C   PHE A 118    13403   9134   6499   -514   -284    915       C  
ATOM    904  O   PHE A 118      16.032  11.540  16.853  1.00 78.03           O  
ANISOU  904  O   PHE A 118    13612   9503   6533   -634   -282    835       O  
ATOM    905  CB  PHE A 118      17.102  11.187  14.048  1.00 72.33           C  
ANISOU  905  CB  PHE A 118    12845   8456   6179   -346   -443    980       C  
ATOM    906  CG  PHE A 118      18.329  10.731  13.321  1.00 70.98           C  
ANISOU  906  CG  PHE A 118    12644   8283   6044   -255   -549   1131       C  
ATOM    907  CD1 PHE A 118      18.227  10.055  12.129  1.00 69.20           C  
ANISOU  907  CD1 PHE A 118    12425   7885   5984   -122   -561   1202       C  
ATOM    908  CD2 PHE A 118      19.587  10.988  13.833  1.00 71.31           C  
ANISOU  908  CD2 PHE A 118    12641   8502   5950   -310   -631   1192       C  
ATOM    909  CE1 PHE A 118      19.356   9.639  11.459  1.00 68.57           C  
ANISOU  909  CE1 PHE A 118    12311   7802   5941    -35   -633   1324       C  
ATOM    910  CE2 PHE A 118      20.718  10.579  13.174  1.00 70.74           C  
ANISOU  910  CE2 PHE A 118    12518   8435   5926   -220   -715   1327       C  
ATOM    911  CZ  PHE A 118      20.602   9.902  11.983  1.00 69.74           C  
ANISOU  911  CZ  PHE A 118    12401   8126   5972    -77   -707   1389       C  
ATOM    912  N   PHE A 119      14.312  10.615  15.783  1.00 41.75           N  
ATOM    913  CA  PHE A 119      13.299  11.283  16.573  1.00 43.07           C  
ATOM    914  C   PHE A 119      12.196  10.315  16.901  1.00 43.24           C  
ATOM    915  O   PHE A 119      11.101  10.511  16.389  1.00 44.44           O  
ATOM    916  CB  PHE A 119      12.759  12.514  15.803  1.00 43.55           C  
ATOM    917  CG  PHE A 119      13.858  13.372  15.240  1.00 45.36           C  
ATOM    918  CD1 PHE A 119      14.204  13.291  13.902  1.00 48.23           C  
ATOM    919  CD2 PHE A 119      14.615  14.181  16.072  1.00 46.66           C  
ATOM    920  CE1 PHE A 119      15.269  14.051  13.382  1.00 49.29           C  
ATOM    921  CE2 PHE A 119      15.680  14.932  15.570  1.00 48.60           C  
ATOM    922  CZ  PHE A 119      16.005  14.866  14.221  1.00 49.10           C  
ATOM    923  N   PRO A 120      12.835   8.958  17.428  1.00 69.20           N  
ATOM    924  CA  PRO A 120      11.948   8.021  18.093  1.00 69.51           C  
ATOM    925  C   PRO A 120      10.922   8.765  18.939  1.00 70.43           C  
ATOM    926  O   PRO A 120      11.289   9.624  19.742  1.00 70.60           O  
ATOM    927  CB  PRO A 120      12.894   7.217  18.993  1.00 69.08           C  
ATOM    928  CG  PRO A 120      14.275   7.587  18.582  1.00 68.50           C  
ATOM    929  CD  PRO A 120      14.180   8.951  18.019  1.00 69.15           C  
ATOM    930  N   ASP A 121       9.646   8.444  18.750  1.00 71.43           N  
ATOM    931  CA  ASP A 121       8.570   9.081  19.496  1.00 72.60           C  
ATOM    932  C   ASP A 121       8.648   8.884  20.988  1.00 72.97           C  
ATOM    933  O   ASP A 121       8.195   9.730  21.752  1.00 73.24           O  
ATOM    934  CB  ASP A 121       7.226   8.556  19.031  1.00 72.87           C  
ATOM    935  CG  ASP A 121       6.662   9.370  17.911  1.00 75.51           C  
ATOM    936  OD1 ASP A 121       6.360   8.769  16.853  1.00 77.54           O  
ATOM    937  OD2 ASP A 121       6.545  10.615  18.086  1.00 78.05           O  
ATOM    938  N   ASP A 122       9.183   7.747  21.407  1.00 73.72           N  
ATOM    939  CA  ASP A 122       9.208   7.408  22.819  1.00 74.08           C  
ATOM    940  C   ASP A 122      10.417   8.059  23.497  1.00 75.10           C  
ATOM    941  O   ASP A 122      10.734   7.765  24.656  1.00 75.03           O  
ATOM    942  CB  ASP A 122       9.149   5.888  23.019  1.00 73.35           C  
ATOM    943  CG  ASP A 122      10.372   5.154  22.461  1.00 72.56           C  
ATOM    944  OD1 ASP A 122      11.254   5.777  21.824  1.00 70.60           O  
ATOM    945  OD2 ASP A 122      10.452   3.924  22.675  1.00 71.17           O  
ATOM    946  N   GLU A 123      11.068   8.964  22.765  1.00 76.34           N  
ATOM    947  CA  GLU A 123      12.181   9.741  23.301  1.00 77.86           C  
ATOM    948  C   GLU A 123      11.910  11.243  23.211  1.00 79.33           C  
ATOM    949  O   GLU A 123      12.837  12.050  23.168  1.00 79.62           O  
ATOM    950  CB  GLU A 123      13.505   9.360  22.626  1.00 77.26           C  
ATOM    951  CG  GLU A 123      13.936   7.937  22.951  1.00 76.85           C  
ATOM    952  CD  GLU A 123      15.318   7.544  22.409  1.00 76.75           C  
ATOM    953  OE1 GLU A 123      16.081   8.419  21.945  1.00 76.12           O  
ATOM    954  OE2 GLU A 123      15.644   6.337  22.448  1.00 76.28           O  
ATOM    955  N   ASP A 124      10.634  11.610  23.221  1.00 81.29           N  
ATOM    956  CA  ASP A 124      10.239  13.019  23.147  1.00 83.58           C  
ATOM    957  C   ASP A 124      10.262  13.793  24.470  1.00 85.10           C  
ATOM    958  O   ASP A 124      10.518  13.233  25.536  1.00 85.34           O  
ATOM    959  CB  ASP A 124       8.858  13.158  22.508  1.00 83.55           C  
ATOM    960  CG  ASP A 124       8.907  13.011  21.016  1.00 83.55           C  
ATOM    961  OD1 ASP A 124      10.035  12.863  20.498  1.00 84.62           O  
ATOM    962  OD2 ASP A 124       7.837  13.035  20.369  1.00 83.43           O  
ATOM    963  N   ASP A 125       9.962  15.090  24.366  1.00 87.02           N  
ATOM    964  CA  ASP A 125      10.082  16.067  25.461  1.00 88.53           C  
ATOM    965  C   ASP A 125      11.426  16.798  25.398  1.00 89.35           C  
ATOM    966  O   ASP A 125      11.468  18.028  25.400  1.00 89.37           O  
ATOM    967  CB  ASP A 125       9.847  15.425  26.828  1.00 88.70           C  
ATOM    968  CG  ASP A 125       8.439  14.871  26.965  1.00 89.87           C  
ATOM    969  OD1 ASP A 125       8.027  14.539  28.103  1.00 90.60           O  
ATOM    970  OD2 ASP A 125       7.748  14.768  25.921  1.00 90.33           O  
ATOM    971  N   GLN A 126      12.519  16.042  25.312  1.00 90.48           N  
ATOM    972  CA  GLN A 126      13.838  16.655  25.155  1.00 91.46           C  
ATOM    973  C   GLN A 126      13.830  17.660  24.007  1.00 91.70           C  
ATOM    974  O   GLN A 126      14.313  18.787  24.152  1.00 92.14           O  
ATOM    975  CB  GLN A 126      14.933  15.592  24.951  1.00 91.76           C  
ATOM    976  CG  GLN A 126      16.053  15.975  23.947  1.00 92.98           C  
ATOM    977  CD  GLN A 126      16.654  17.372  24.169  1.00 94.89           C  
ATOM    978  OE1 GLN A 126      17.162  17.987  23.227  1.00 95.63           O  
ATOM    979  NE2 GLN A 126      16.594  17.873  25.408  1.00 95.03           N  
TER     980      GLN A 126                                                      
ATOM    981  N   PRO B   2      28.574  19.912  50.465  1.00 72.91           N  
ANISOU  981  N   PRO B   2    14009   7794   5899   -347   1380    -16       N  
ATOM    982  CA  PRO B   2      29.860  19.928  49.787  1.00 69.86           C  
ANISOU  982  CA  PRO B   2    13532   7297   5714   -267    893    -15       C  
ATOM    983  C   PRO B   2      29.943  21.119  48.850  1.00 67.90           C  
ANISOU  983  C   PRO B   2    12839   7147   5814   -123    833    -64       C  
ATOM    984  O   PRO B   2      28.942  21.531  48.270  1.00 67.70           O  
ANISOU  984  O   PRO B   2    12466   7301   5955   -113   1076    -57       O  
ATOM    985  CB  PRO B   2      29.855  18.624  48.989  1.00 68.37           C  
ANISOU  985  CB  PRO B   2    13182   7173   5624   -437    818    106       C  
ATOM    986  CG  PRO B   2      28.776  17.796  49.576  1.00 70.97           C  
ANISOU  986  CG  PRO B   2    13692   7550   5722   -643   1172    194       C  
ATOM    987  CD  PRO B   2      27.757  18.762  50.057  1.00 73.41           C  
ANISOU  987  CD  PRO B   2    13898   7989   6006   -586   1605    113       C  
ATOM    988  N   LYS B   3      31.137  21.668  48.705  1.00 66.94           N  
ANISOU  988  N   LYS B   3    12736   6872   5824    -25    484   -118       N  
ATOM    989  CA  LYS B   3      31.313  22.866  47.911  1.00 66.03           C  
ANISOU  989  CA  LYS B   3    12306   6789   5995     69    418   -140       C  
ATOM    990  C   LYS B   3      32.093  22.591  46.631  1.00 63.87           C  
ANISOU  990  C   LYS B   3    11724   6560   5986     -9    261    -72       C  
ATOM    991  O   LYS B   3      33.095  21.904  46.644  1.00 63.81           O  
ANISOU  991  O   LYS B   3    11767   6455   6021    -49     50    -98       O  
ATOM    992  CB  LYS B   3      32.036  23.926  48.736  1.00 67.40           C  
ANISOU  992  CB  LYS B   3    12727   6731   6151    213    188   -260       C  
ATOM    993  CG  LYS B   3      32.558  25.073  47.923  1.00 66.66           C  
ANISOU  993  CG  LYS B   3    12364   6587   6375    252     30   -259       C  
ATOM    994  CD  LYS B   3      33.110  26.129  48.826  1.00 68.72           C  
ANISOU  994  CD  LYS B   3    12888   6592   6632    393   -217   -385       C  
ATOM    995  CE  LYS B   3      33.840  27.201  48.063  1.00 68.19           C  
ANISOU  995  CE  LYS B   3    12585   6412   6912    367   -420   -362       C  
ATOM    996  NZ  LYS B   3      34.951  27.738  48.878  1.00 70.74           N  
ANISOU  996  NZ  LYS B   3    13120   6417   7342    428   -810   -482       N  
ATOM    997  N   ILE B   4      31.646  23.145  45.521  1.00 62.98           N  
ANISOU  997  N   ILE B   4    11316   6568   6044    -19    355     -7       N  
ATOM    998  CA  ILE B   4      32.375  22.956  44.298  1.00 61.93           C  
ANISOU  998  CA  ILE B   4    10974   6471   6085   -103    279     54       C  
ATOM    999  C   ILE B   4      32.931  24.271  43.786  1.00 62.39           C  
ANISOU  999  C   ILE B   4    10947   6431   6327    -94    200     65       C  
ATOM   1000  O   ILE B   4      32.254  25.305  43.811  1.00 63.03           O  
ANISOU 1000  O   ILE B   4    11045   6480   6422    -16    218     74       O  
ATOM   1001  CB  ILE B   4      31.484  22.334  43.199  1.00 61.32           C  
ANISOU 1001  CB  ILE B   4    10726   6571   6003   -166    413    151       C  
ATOM   1002  CG1 ILE B   4      31.218  20.860  43.506  1.00 61.55           C  
ANISOU 1002  CG1 ILE B   4    10823   6660   5905   -235    442    159       C  
ATOM   1003  CG2 ILE B   4      32.131  22.479  41.824  1.00 60.39           C  
ANISOU 1003  CG2 ILE B   4    10476   6474   5995   -233    385    211       C  
ATOM   1004  CD1 ILE B   4      30.409  20.161  42.446  1.00 60.77           C  
ANISOU 1004  CD1 ILE B   4    10567   6690   5834   -298    498    239       C  
ATOM   1005  N   GLN B   5      34.167  24.208  43.307  1.00 62.40           N  
ANISOU 1005  N   GLN B   5    10845   6369   6496   -182    117     52       N  
ATOM   1006  CA  GLN B   5      34.776  25.317  42.609  1.00 63.19           C  
ANISOU 1006  CA  GLN B   5    10849   6377   6784   -262    106    102       C  
ATOM   1007  C   GLN B   5      34.940  24.916  41.125  1.00 63.39           C  
ANISOU 1007  C   GLN B   5    10743   6533   6812   -399    289    200       C  
ATOM   1008  O   GLN B   5      35.707  24.016  40.804  1.00 63.51           O  
ANISOU 1008  O   GLN B   5    10633   6606   6890   -456    343    137       O  
ATOM   1009  CB  GLN B   5      36.122  25.668  43.270  1.00 64.15           C  
ANISOU 1009  CB  GLN B   5    10928   6294   7152   -288    -91    -16       C  
ATOM   1010  CG  GLN B   5      36.014  25.926  44.796  1.00 64.18           C  
ANISOU 1010  CG  GLN B   5    11184   6125   7076   -126   -329   -135       C  
ATOM   1011  CD  GLN B   5      37.361  26.020  45.517  1.00 65.98           C  
ANISOU 1011  CD  GLN B   5    11396   6101   7571   -123   -646   -288       C  
ATOM   1012  OE1 GLN B   5      38.187  26.877  45.230  1.00 67.39           O  
ANISOU 1012  OE1 GLN B   5    11406   6132   8069   -220   -738   -300       O  
ATOM   1013  NE2 GLN B   5      37.566  25.148  46.476  1.00 66.22           N  
ANISOU 1013  NE2 GLN B   5    11626   6044   7490    -21   -849   -406       N  
ATOM   1014  N   THR B   6      34.197  25.553  40.224  1.00 63.81           N  
ANISOU 1014  N   THR B   6    10866   6605   6776   -427    356    332       N  
ATOM   1015  CA  THR B   6      34.438  25.361  38.793  1.00 65.20           C  
ANISOU 1015  CA  THR B   6    11046   6844   6883   -566    517    434       C  
ATOM   1016  C   THR B   6      34.951  26.609  38.137  1.00 67.57           C  
ANISOU 1016  C   THR B   6    11439   6989   7247   -722    565    547       C  
ATOM   1017  O   THR B   6      34.421  27.700  38.370  1.00 68.42           O  
ANISOU 1017  O   THR B   6    11681   6947   7368   -674    406    606       O  
ATOM   1018  CB  THR B   6      33.159  25.089  38.012  1.00 64.94           C  
ANISOU 1018  CB  THR B   6    11138   6887   6648   -503    495    524       C  
ATOM   1019  OG1 THR B   6      32.041  25.560  38.776  1.00 65.08           O  
ANISOU 1019  OG1 THR B   6    11167   6869   6690   -346    347    497       O  
ATOM   1020  CG2 THR B   6      33.011  23.618  37.674  1.00 63.84           C  
ANISOU 1020  CG2 THR B   6    10942   6909   6405   -485    554    479       C  
ATOM   1021  N   TYR B   7      35.938  26.436  37.266  1.00 69.33           N  
ANISOU 1021  N   TYR B   7    11606   7235   7500   -915    802    572       N  
ATOM   1022  CA  TYR B   7      36.451  27.538  36.491  1.00 72.27           C  
ANISOU 1022  CA  TYR B   7    12116   7453   7891  -1143    931    717       C  
ATOM   1023  C   TYR B   7      35.797  27.512  35.126  1.00 73.43           C  
ANISOU 1023  C   TYR B   7    12601   7615   7684  -1204   1032    881       C  
ATOM   1024  O   TYR B   7      36.129  26.693  34.285  1.00 74.37           O  
ANISOU 1024  O   TYR B   7    12744   7867   7648  -1274   1284    864       O  
ATOM   1025  CB  TYR B   7      37.967  27.455  36.419  1.00 74.60           C  
ANISOU 1025  CB  TYR B   7    12128   7742   8474  -1352   1188    626       C  
ATOM   1026  CG  TYR B   7      38.562  27.543  37.795  1.00 75.01           C  
ANISOU 1026  CG  TYR B   7    11906   7701   8893  -1261    950    451       C  
ATOM   1027  CD1 TYR B   7      38.940  28.764  38.325  1.00 77.15           C  
ANISOU 1027  CD1 TYR B   7    12183   7730   9402  -1353    783    488       C  
ATOM   1028  CD2 TYR B   7      38.682  26.410  38.594  1.00 74.08           C  
ANISOU 1028  CD2 TYR B   7    11606   7689   8852  -1070    819    253       C  
ATOM   1029  CE1 TYR B   7      39.456  28.855  39.594  1.00 78.13           C  
ANISOU 1029  CE1 TYR B   7    12134   7721   9830  -1243    491    315       C  
ATOM   1030  CE2 TYR B   7      39.200  26.490  39.875  1.00 74.33           C  
ANISOU 1030  CE2 TYR B   7    11505   7577   9160   -969    527     93       C  
ATOM   1031  CZ  TYR B   7      39.586  27.723  40.371  1.00 76.73           C  
ANISOU 1031  CZ  TYR B   7    11819   7641   9694  -1046    358    117       C  
ATOM   1032  OH  TYR B   7      40.100  27.856  41.651  1.00 77.85           O  
ANISOU 1032  OH  TYR B   7    11902   7588  10090   -927     -2    -53       O  
ATOM   1033  N   VAL B   8      34.838  28.403  34.925  1.00 74.04           N  
ANISOU 1033  N   VAL B   8    12974   7526   7631  -1145    785   1013       N  
ATOM   1034  CA  VAL B   8      34.078  28.447  33.698  1.00 75.62           C  
ANISOU 1034  CA  VAL B   8    13576   7662   7496  -1158    731   1159       C  
ATOM   1035  C   VAL B   8      34.541  29.589  32.814  1.00 79.77           C  
ANISOU 1035  C   VAL B   8    14498   7936   7874  -1429    820   1371       C  
ATOM   1036  O   VAL B   8      35.330  30.429  33.241  1.00 81.09           O  
ANISOU 1036  O   VAL B   8    14575   7975   8262  -1602    892   1406       O  
ATOM   1037  CB  VAL B   8      32.600  28.631  33.998  1.00 74.22           C  
ANISOU 1037  CB  VAL B   8    13467   7419   7314   -887    322   1135       C  
ATOM   1038  CG1 VAL B   8      32.133  27.512  34.897  1.00 71.22           C  
ANISOU 1038  CG1 VAL B   8    12723   7273   7066   -686    303    953       C  
ATOM   1039  CG2 VAL B   8      32.363  29.976  34.640  1.00 75.02           C  
ANISOU 1039  CG2 VAL B   8    13623   7291   7592   -833     67   1155       C  
ATOM   1040  N   ASN B   9      34.049  29.616  31.578  1.00 82.27           N  
ANISOU 1040  N   ASN B   9    15304   8147   7810  -1482    786   1519       N  
ATOM   1041  CA  ASN B   9      34.371  30.713  30.672  1.00 87.09           C  
ANISOU 1041  CA  ASN B   9    16445   8461   8184  -1764    843   1760       C  
ATOM   1042  C   ASN B   9      33.430  31.898  30.870  1.00 87.92           C  
ANISOU 1042  C   ASN B   9    16838   8237   8329  -1632    297   1851       C  
ATOM   1043  O   ASN B   9      32.408  31.791  31.558  1.00 85.09           O  
ANISOU 1043  O   ASN B   9    16264   7909   8158  -1297    -90   1704       O  
ATOM   1044  CB  ASN B   9      34.382  30.257  29.201  1.00 90.42           C  
ANISOU 1044  CB  ASN B   9    17409   8857   8090  -1904   1059   1886       C  
ATOM   1045  CG  ASN B   9      33.013  29.811  28.717  1.00 90.39           C  
ANISOU 1045  CG  ASN B   9    17706   8783   7854  -1605    582   1867       C  
ATOM   1046  OD1 ASN B   9      31.994  30.434  29.035  1.00 91.28           O  
ANISOU 1046  OD1 ASN B   9    17892   8695   8095  -1396     49   1870       O  
ATOM   1047  ND2 ASN B   9      32.980  28.719  27.957  1.00 90.54           N  
ANISOU 1047  ND2 ASN B   9    17869   8951   7579  -1566    744   1813       N  
ATOM   1048  N   ASN B  10      33.783  33.025  30.260  1.00 92.22           N  
ANISOU 1048  N   ASN B  10    17874   8452   8713  -1906    282   2080       N  
ATOM   1049  CA  ASN B  10      33.038  34.246  30.466  1.00 93.80           C  
ANISOU 1049  CA  ASN B  10    18367   8283   8988  -1788   -273   2153       C  
ATOM   1050  C   ASN B  10      31.584  34.144  30.048  1.00 94.12           C  
ANISOU 1050  C   ASN B  10    18686   8187   8887  -1445   -827   2104       C  
ATOM   1051  O   ASN B  10      30.712  34.699  30.702  1.00 93.33           O  
ANISOU 1051  O   ASN B  10    18453   7951   9057  -1147  -1305   1976       O  
ATOM   1052  CB  ASN B  10      33.733  35.403  29.777  1.00 98.99           C  
ANISOU 1052  CB  ASN B  10    19589   8568   9455  -2199   -189   2442       C  
ATOM   1053  CG  ASN B  10      34.975  35.838  30.514  1.00 99.30           C  
ANISOU 1053  CG  ASN B  10    19226   8645   9857  -2481    159   2441       C  
ATOM   1054  OD1 ASN B  10      34.979  35.954  31.739  1.00 95.89           O  
ANISOU 1054  OD1 ASN B  10    18289   8296   9850  -2275    -16   2247       O  
ATOM   1055  ND2 ASN B  10      36.041  36.085  29.773  1.00104.15           N  
ANISOU 1055  ND2 ASN B  10    20076   9179  10317  -2964    658   2646       N  
ATOM   1056  N   ASN B  11      31.327  33.427  28.961  1.00 95.95           N  
ANISOU 1056  N   ASN B  11    19289   8441   8728  -1471   -776   2173       N  
ATOM   1057  CA  ASN B  11      29.963  33.171  28.520  1.00 96.85           C  
ANISOU 1057  CA  ASN B  11    19611   8417   8769  -1139  -1344   2093       C  
ATOM   1058  C   ASN B  11      29.116  32.629  29.638  1.00 92.54           C  
ANISOU 1058  C   ASN B  11    18342   8122   8698   -764  -1536   1799       C  
ATOM   1059  O   ASN B  11      28.178  33.277  30.100  1.00 93.09           O  
ANISOU 1059  O   ASN B  11    18309   8008   9055   -490  -2025   1678       O  
ATOM   1060  CB  ASN B  11      29.962  32.129  27.416  1.00 98.18           C  
ANISOU 1060  CB  ASN B  11    20124   8678   8503  -1198  -1177   2141       C  
ATOM   1061  CG  ASN B  11      29.924  32.741  26.062  1.00105.81           C  
ANISOU 1061  CG  ASN B  11    22073   9218   8914  -1384  -1376   2398       C  
ATOM   1062  OD1 ASN B  11      30.036  33.960  25.920  1.00110.68           O  
ANISOU 1062  OD1 ASN B  11    23129   9464   9459  -1533  -1585   2578       O  
ATOM   1063  ND2 ASN B  11      29.761  31.906  25.039  1.00109.90           N  
ANISOU 1063  ND2 ASN B  11    23022   9740   8994  -1380  -1346   2423       N  
ATOM   1064  N   VAL B  12      29.449  31.408  30.041  1.00 88.83           N  
ANISOU 1064  N   VAL B  12    17394   8059   8300   -757  -1134   1674       N  
ATOM   1065  CA  VAL B  12      28.735  30.719  31.084  1.00 85.10           C  
ANISOU 1065  CA  VAL B  12    16282   7844   8206   -476  -1202   1425       C  
ATOM   1066  C   VAL B  12      28.533  31.683  32.253  1.00 84.47           C  
ANISOU 1066  C   VAL B  12    15913   7692   8489   -335  -1353   1314       C  
ATOM   1067  O   VAL B  12      27.409  31.892  32.724  1.00 84.65           O  
ANISOU 1067  O   VAL B  12    15713   7659   8790    -38  -1701   1137       O  
ATOM   1068  CB  VAL B  12      29.522  29.467  31.532  1.00 81.88           C  
ANISOU 1068  CB  VAL B  12    15468   7834   7811   -574   -694   1346       C  
ATOM   1069  CG1 VAL B  12      28.857  28.805  32.723  1.00 78.28           C  
ANISOU 1069  CG1 VAL B  12    14428   7613   7702   -343   -722   1124       C  
ATOM   1070  CG2 VAL B  12      29.663  28.486  30.378  1.00 82.88           C  
ANISOU 1070  CG2 VAL B  12    15888   8023   7580   -662   -568   1409       C  
ATOM   1071  N   TYR B  13      29.625  32.285  32.705  1.00 84.14           N  
ANISOU 1071  N   TYR B  13    15868   7633   8468   -543  -1093   1393       N  
ATOM   1072  CA  TYR B  13      29.562  33.166  33.854  1.00 83.70           C  
ANISOU 1072  CA  TYR B  13    15586   7494   8721   -407  -1234   1273       C  
ATOM   1073  C   TYR B  13      28.505  34.251  33.691  1.00 86.85           C  
ANISOU 1073  C   TYR B  13    16231   7540   9228   -171  -1802   1232       C  
ATOM   1074  O   TYR B  13      27.650  34.441  34.559  1.00 86.23           O  
ANISOU 1074  O   TYR B  13    15822   7491   9449    147  -2001    991       O  
ATOM   1075  CB  TYR B  13      30.918  33.803  34.107  1.00 84.20           C  
ANISOU 1075  CB  TYR B  13    15719   7476   8797   -705   -986   1398       C  
ATOM   1076  CG  TYR B  13      31.006  34.419  35.470  1.00 82.86           C  
ANISOU 1076  CG  TYR B  13    15264   7278   8940   -550  -1090   1230       C  
ATOM   1077  CD1 TYR B  13      30.892  35.787  35.639  1.00 85.23           C  
ANISOU 1077  CD1 TYR B  13    15819   7217   9345   -510  -1448   1261       C  
ATOM   1078  CD2 TYR B  13      31.175  33.627  36.594  1.00 79.71           C  
ANISOU 1078  CD2 TYR B  13    14414   7174   8696   -428   -872   1034       C  
ATOM   1079  CE1 TYR B  13      30.961  36.359  36.888  1.00 84.81           C  
ANISOU 1079  CE1 TYR B  13    15562   7115   9548   -336  -1569   1080       C  
ATOM   1080  CE2 TYR B  13      31.246  34.180  37.855  1.00 79.03           C  
ANISOU 1080  CE2 TYR B  13    14170   7035   8825   -269   -980    869       C  
ATOM   1081  CZ  TYR B  13      31.138  35.556  37.996  1.00 82.04           C  
ANISOU 1081  CZ  TYR B  13    14793   7069   9309   -213  -1324    882       C  
ATOM   1082  OH  TYR B  13      31.207  36.140  39.244  1.00 82.82           O  
ANISOU 1082  OH  TYR B  13    14792   7085   9592    -26  -1461    694       O  
ATOM   1083  N   GLU B  14      28.575  34.976  32.582  1.00 90.84           N  
ANISOU 1083  N   GLU B  14    17344   7687   9484   -324  -2059   1451       N  
ATOM   1084  CA  GLU B  14      27.588  36.005  32.307  1.00 94.77           C  
ANISOU 1084  CA  GLU B  14    18154   7773  10081    -86  -2704   1409       C  
ATOM   1085  C   GLU B  14      26.186  35.438  32.445  1.00 94.28           C  
ANISOU 1085  C   GLU B  14    17736   7805  10282    311  -3013   1138       C  
ATOM   1086  O   GLU B  14      25.351  35.984  33.164  1.00 95.52           O  
ANISOU 1086  O   GLU B  14    17605   7877  10810    643  -3322    887       O  
ATOM   1087  CB  GLU B  14      27.767  36.574  30.902  1.00 99.35           C  
ANISOU 1087  CB  GLU B  14    19561   7939  10249   -324  -2961   1709       C  
ATOM   1088  CG  GLU B  14      28.500  37.894  30.848  1.00103.75           C  
ANISOU 1088  CG  GLU B  14    20575   8117  10728   -575  -3063   1918       C  
ATOM   1089  CD  GLU B  14      27.892  38.832  29.818  1.00111.43           C  
ANISOU 1089  CD  GLU B  14    22356   8508  11473   -551  -3728   2077       C  
ATOM   1090  OE1 GLU B  14      27.037  38.380  29.026  1.00113.12           O  
ANISOU 1090  OE1 GLU B  14    22818   8622  11541   -373  -4073   2044       O  
ATOM   1091  OE2 GLU B  14      28.257  40.023  29.798  1.00116.09           O  
ANISOU 1091  OE2 GLU B  14    23373   8697  12041   -707  -3967   2232       O  
ATOM   1092  N   GLN B  15      25.936  34.338  31.748  1.00 93.09           N  
ANISOU 1092  N   GLN B  15    17584   7819   9965    274  -2918   1170       N  
ATOM   1093  CA  GLN B  15      24.604  33.779  31.681  1.00 93.17           C  
ANISOU 1093  CA  GLN B  15    17286   7857  10257    595  -3261    938       C  
ATOM   1094  C   GLN B  15      24.056  33.539  33.070  1.00 90.41           C  
ANISOU 1094  C   GLN B  15    16177   7805  10371    838  -3068    629       C  
ATOM   1095  O   GLN B  15      22.880  33.786  33.345  1.00 92.38           O  
ANISOU 1095  O   GLN B  15    16116   7958  11027   1165  -3425    365       O  
ATOM   1096  CB  GLN B  15      24.632  32.465  30.913  1.00 92.17           C  
ANISOU 1096  CB  GLN B  15    17211   7922   9887    474  -3087   1016       C  
ATOM   1097  CG  GLN B  15      25.274  32.560  29.544  1.00 95.17           C  
ANISOU 1097  CG  GLN B  15    18398   8059   9705    209  -3136   1314       C  
ATOM   1098  CD  GLN B  15      24.701  31.540  28.599  1.00 96.96           C  
ANISOU 1098  CD  GLN B  15    18802   8275   9765    269  -3343   1302       C  
ATOM   1099  OE1 GLN B  15      25.420  30.710  28.037  1.00 96.75           O  
ANISOU 1099  OE1 GLN B  15    18990   8419   9350     52  -2958   1431       O  
ATOM   1100  NE2 GLN B  15      23.385  31.577  28.433  1.00 99.53           N  
ANISOU 1100  NE2 GLN B  15    19004   8383  10430    587  -3976   1109       N  
ATOM   1101  N   ILE B  16      24.915  33.046  33.946  1.00 86.22           N  
ANISOU 1101  N   ILE B  16    15361   7617   9781    677  -2496    644       N  
ATOM   1102  CA  ILE B  16      24.484  32.703  35.282  1.00 84.01           C  
ANISOU 1102  CA  ILE B  16    14478   7621   9820    860  -2236    381       C  
ATOM   1103  C   ILE B  16      24.217  33.954  36.100  1.00 85.70           C  
ANISOU 1103  C   ILE B  16    14638   7649  10276   1090  -2434    202       C  
ATOM   1104  O   ILE B  16      23.128  34.128  36.635  1.00 87.44           O  
ANISOU 1104  O   ILE B  16    14489   7876  10858   1400  -2575    -89       O  
ATOM   1105  CB  ILE B  16      25.521  31.823  35.998  1.00 80.14           C  
ANISOU 1105  CB  ILE B  16    13807   7482   9162    636  -1659    446       C  
ATOM   1106  CG1 ILE B  16      25.906  30.638  35.117  1.00 78.77           C  
ANISOU 1106  CG1 ILE B  16    13738   7458   8733    422  -1487    608       C  
ATOM   1107  CG2 ILE B  16      24.979  31.337  37.334  1.00 78.54           C  
ANISOU 1107  CG2 ILE B  16    13097   7547   9199    801  -1388    195       C  
ATOM   1108  CD1 ILE B  16      26.516  29.501  35.884  1.00 75.24           C  
ANISOU 1108  CD1 ILE B  16    12993   7357   8238    302  -1023    578       C  
ATOM   1109  N   THR B  17      25.210  34.827  36.204  1.00 85.49           N  
ANISOU 1109  N   THR B  17    14957   7446  10080    938  -2438    354       N  
ATOM   1110  CA  THR B  17      25.017  36.053  36.951  1.00 87.65           C  
ANISOU 1110  CA  THR B  17    15248   7494  10562   1164  -2685    184       C  
ATOM   1111  C   THR B  17      23.772  36.780  36.428  1.00 91.87           C  
ANISOU 1111  C   THR B  17    15842   7698  11365   1492  -3293     12       C  
ATOM   1112  O   THR B  17      23.054  37.429  37.184  1.00 94.00           O  
ANISOU 1112  O   THR B  17    15865   7890  11961   1835  -3469   -299       O  
ATOM   1113  CB  THR B  17      26.251  36.970  36.878  1.00 88.06           C  
ANISOU 1113  CB  THR B  17    15740   7297  10420    907  -2725    417       C  
ATOM   1114  OG1 THR B  17      26.504  37.328  35.518  1.00 91.39           O  
ANISOU 1114  OG1 THR B  17    16705   7414  10604    679  -2992    707       O  
ATOM   1115  CG2 THR B  17      27.468  36.262  37.421  1.00 83.97           C  
ANISOU 1115  CG2 THR B  17    15083   7071   9750    622  -2194    526       C  
ATOM   1116  N   ASP B  18      23.515  36.656  35.130  1.00 93.49           N  
ANISOU 1116  N   ASP B  18    16397   7690  11436   1408  -3636    185       N  
ATOM   1117  CA  ASP B  18      22.301  37.193  34.539  1.00 97.91           C  
ANISOU 1117  CA  ASP B  18    17021   7899  12282   1733  -4310      6       C  
ATOM   1118  C   ASP B  18      21.071  36.542  35.139  1.00 98.29           C  
ANISOU 1118  C   ASP B  18    16328   8202  12817   2059  -4242   -382       C  
ATOM   1119  O   ASP B  18      20.086  37.216  35.438  1.00101.92           O  
ANISOU 1119  O   ASP B  18    16529   8470  13726   2443  -4630   -716       O  
ATOM   1120  CB  ASP B  18      22.300  36.969  33.036  1.00 99.86           C  
ANISOU 1120  CB  ASP B  18    17846   7879  12219   1560  -4672    275       C  
ATOM   1121  CG  ASP B  18      22.973  38.083  32.289  1.00103.20           C  
ANISOU 1121  CG  ASP B  18    19092   7823  12295   1364  -5028    569       C  
ATOM   1122  OD1 ASP B  18      22.984  38.042  31.050  1.00106.59           O  
ANISOU 1122  OD1 ASP B  18    20143   7966  12391   1216  -5342    801       O  
ATOM   1123  OD2 ASP B  18      23.486  39.007  32.933  1.00103.98           O  
ANISOU 1123  OD2 ASP B  18    19269   7802  12437   1344  -5006    574       O  
ATOM   1124  N   LEU B  19      21.125  35.225  35.302  1.00 95.02           N  
ANISOU 1124  N   LEU B  19    15559   8201  12343   1898  -3745   -350       N  
ATOM   1125  CA  LEU B  19      20.008  34.488  35.872  1.00 95.74           C  
ANISOU 1125  CA  LEU B  19    14934   8551  12892   2113  -3582   -678       C  
ATOM   1126  C   LEU B  19      19.727  34.897  37.305  1.00 96.27           C  
ANISOU 1126  C   LEU B  19    14545   8802  13231   2333  -3236   -996       C  
ATOM   1127  O   LEU B  19      18.572  35.035  37.701  1.00 99.97           O  
ANISOU 1127  O   LEU B  19    14497   9276  14213   2649  -3328  -1371       O  
ATOM   1128  CB  LEU B  19      20.269  32.995  35.807  1.00 92.20           C  
ANISOU 1128  CB  LEU B  19    14291   8478  12264   1840  -3108   -534       C  
ATOM   1129  CG  LEU B  19      19.741  32.401  34.513  1.00 93.75           C  
ANISOU 1129  CG  LEU B  19    14638   8503  12479   1812  -3543   -448       C  
ATOM   1130  CD1 LEU B  19      20.160  30.945  34.391  1.00 89.80           C  
ANISOU 1130  CD1 LEU B  19    14046   8337  11739   1530  -3106   -282       C  
ATOM   1131  CD2 LEU B  19      18.222  32.560  34.480  1.00 97.94           C  
ANISOU 1131  CD2 LEU B  19    14662   8876  13676   2167  -3990   -819       C  
ATOM   1132  N   VAL B  20      20.781  35.086  38.086  1.00 93.26           N  
ANISOU 1132  N   VAL B  20    14354   8558  12523   2174  -2838   -873       N  
ATOM   1133  CA  VAL B  20      20.607  35.536  39.450  1.00 94.15           C  
ANISOU 1133  CA  VAL B  20    14186   8798  12788   2390  -2536  -1167       C  
ATOM   1134  C   VAL B  20      19.815  36.836  39.411  1.00 99.54           C  
ANISOU 1134  C   VAL B  20    14858   9115  13848   2797  -3087  -1465       C  
ATOM   1135  O   VAL B  20      18.775  36.973  40.059  1.00103.00           O  
ANISOU 1135  O   VAL B  20    14786   9631  14718   3128  -3004  -1878       O  
ATOM   1136  CB  VAL B  20      21.954  35.771  40.135  1.00 90.90           C  
ANISOU 1136  CB  VAL B  20    14126   8441  11970   2182  -2247   -978       C  
ATOM   1137  CG1 VAL B  20      21.750  35.969  41.630  1.00 91.57           C  
ANISOU 1137  CG1 VAL B  20    13966   8698  12128   2395  -1869  -1289       C  
ATOM   1138  CG2 VAL B  20      22.894  34.602  39.874  1.00 86.18           C  
ANISOU 1138  CG2 VAL B  20    13632   8096  11017   1783  -1876   -659       C  
ATOM   1139  N   THR B  21      20.305  37.788  38.630  1.00100.95           N  
ANISOU 1139  N   THR B  21    15607   8874  13876   2765  -3644  -1265       N  
ATOM   1140  CA  THR B  21      19.605  39.044  38.472  1.00106.53           C  
ANISOU 1140  CA  THR B  21    16405   9148  14924   3150  -4295  -1523       C  
ATOM   1141  C   THR B  21      18.147  38.778  38.146  1.00110.97           C  
ANISOU 1141  C   THR B  21    16429   9680  16054   3479  -4579  -1878       C  
ATOM   1142  O   THR B  21      17.250  39.222  38.858  1.00114.83           O  
ANISOU 1142  O   THR B  21    16439  10172  17020   3882  -4599  -2340       O  
ATOM   1143  CB  THR B  21      20.195  39.888  37.339  1.00107.72           C  
ANISOU 1143  CB  THR B  21    17325   8793  14810   2993  -4935  -1186       C  
ATOM   1144  OG1 THR B  21      21.560  40.196  37.630  1.00104.71           O  
ANISOU 1144  OG1 THR B  21    17372   8413  14000   2661  -4672   -876       O  
ATOM   1145  CG2 THR B  21      19.420  41.178  37.196  1.00113.39           C  
ANISOU 1145  CG2 THR B  21    18174   9006  15902   3421  -5701  -1472       C  
ATOM   1146  N   ILE B  22      17.913  38.055  37.058  1.00111.22           N  
ANISOU 1146  N   ILE B  22    16531   9666  16061   3318  -4808  -1687       N  
ATOM   1147  CA  ILE B  22      16.551  37.763  36.629  1.00116.12           C  
ANISOU 1147  CA  ILE B  22    16641  10196  17282   3607  -5187  -2013       C  
ATOM   1148  C   ILE B  22      15.682  37.373  37.819  1.00118.28           C  
ANISOU 1148  C   ILE B  22    16018  10856  18068   3837  -4624  -2474       C  
ATOM   1149  O   ILE B  22      14.579  37.905  38.001  1.00123.74           O  
ANISOU 1149  O   ILE B  22    16223  11388  19406   4262  -4941  -2943       O  
ATOM   1150  CB  ILE B  22      16.504  36.619  35.593  1.00114.35           C  
ANISOU 1150  CB  ILE B  22    16500  10034  16914   3334  -5258  -1750       C  
ATOM   1151  CG1 ILE B  22      17.285  37.000  34.334  1.00113.82           C  
ANISOU 1151  CG1 ILE B  22    17379   9566  16302   3109  -5776  -1315       C  
ATOM   1152  CG2 ILE B  22      15.065  36.277  35.246  1.00118.77           C  
ANISOU 1152  CG2 ILE B  22    16442  10489  18195   3633  -5670  -2126       C  
ATOM   1153  CD1 ILE B  22      16.634  38.083  33.517  1.00118.77           C  
ANISOU 1153  CD1 ILE B  22    18396   9559  17173   3424  -6775  -1440       C  
ATOM   1154  N   ARG B  23      16.193  36.451  38.631  1.00114.60           N  
ANISOU 1154  N   ARG B  23    15356  10878  17311   3551  -3783  -2353       N  
ATOM   1155  CA  ARG B  23      15.417  35.881  39.726  1.00116.99           C  
ANISOU 1155  CA  ARG B  23    14890  11574  17988   3659  -3121  -2719       C  
ATOM   1156  C   ARG B  23      15.060  36.894  40.809  1.00120.80           C  
ANISOU 1156  C   ARG B  23    15158  12034  18708   4045  -2973  -3151       C  
ATOM   1157  O   ARG B  23      13.880  37.159  41.044  1.00126.53           O  
ANISOU 1157  O   ARG B  23    15251  12728  20096   4405  -3041  -3637       O  
ATOM   1158  CB  ARG B  23      16.130  34.666  40.314  1.00112.18           C  
ANISOU 1158  CB  ARG B  23    14287  11419  16918   3239  -2327  -2444       C  
ATOM   1159  CG  ARG B  23      16.614  33.704  39.240  1.00110.30           C  
ANISOU 1159  CG  ARG B  23    14332  11186  16390   2881  -2484  -2028       C  
ATOM   1160  CD  ARG B  23      16.398  32.247  39.593  1.00111.54           C  
ANISOU 1160  CD  ARG B  23    14082  11738  16561   2607  -1888  -1978       C  
ATOM   1161  NE  ARG B  23      15.442  31.556  38.793  1.00116.03           N  
ANISOU 1161  NE  ARG B  23    14249  12248  17590   2609  -2181  -2060       N  
ATOM   1162  CZ  ARG B  23      15.354  30.272  38.446  1.00115.20           C  
ANISOU 1162  CZ  ARG B  23    13995  12313  17463   2328  -2014  -1895       C  
ATOM   1163  NH1 ARG B  23      14.302  29.980  37.714  1.00118.80           N  
ANISOU 1163  NH1 ARG B  23    14047  12603  18490   2438  -2457  -2068       N  
ATOM   1164  NH2 ARG B  23      16.220  29.308  38.754  1.00111.17           N  
ANISOU 1164  NH2 ARG B  23    13718  12073  16448   1976  -1523  -1597       N  
ATOM   1165  N   LYS B  24      16.062  37.469  41.466  1.00118.28           N  
ANISOU 1165  N   LYS B  24    15338  11709  17891   3990  -2788  -3012       N  
ATOM   1166  CA  LYS B  24      15.784  38.504  42.453  1.00122.38           C  
ANISOU 1166  CA  LYS B  24    15769  12151  18579   4387  -2726  -3427       C  
ATOM   1167  C   LYS B  24      14.689  39.410  41.929  1.00128.94           C  
ANISOU 1167  C   LYS B  24    16303  12600  20088   4867  -3438  -3843       C  
ATOM   1168  O   LYS B  24      13.780  39.803  42.656  1.00134.26           O  
ANISOU 1168  O   LYS B  24    16432  13332  21248   5267  -3257  -4384       O  
ATOM   1169  CB  LYS B  24      17.027  39.341  42.719  1.00119.61           C  
ANISOU 1169  CB  LYS B  24    16163  11592  17693   4309  -2898  -3178       C  
ATOM   1170  CG  LYS B  24      18.199  38.538  43.205  1.00114.13           C  
ANISOU 1170  CG  LYS B  24    15781  11198  16386   3870  -2326  -2794       C  
ATOM   1171  CD  LYS B  24      19.241  39.423  43.823  1.00113.59           C  
ANISOU 1171  CD  LYS B  24    16273  10943  15945   3878  -2421  -2708       C  
ATOM   1172  CE  LYS B  24      20.563  38.705  43.812  1.00109.31           C  
ANISOU 1172  CE  LYS B  24    16105  10553  14875   3400  -2145  -2244       C  
ATOM   1173  NZ  LYS B  24      21.572  39.387  44.639  1.00110.15           N  
ANISOU 1173  NZ  LYS B  24    16659  10524  14671   3391  -2149  -2206       N  
ATOM   1174  N   GLN B  25      14.798  39.735  40.648  1.00129.20           N  
ANISOU 1174  N   GLN B  25    16733  12219  20138   4829  -4260  -3598       N  
ATOM   1175  CA  GLN B  25      13.861  40.613  39.980  1.00135.61           C  
ANISOU 1175  CA  GLN B  25    17421  12552  21552   5272  -5137  -3936       C  
ATOM   1176  C   GLN B  25      12.477  39.972  39.890  1.00140.27           C  
ANISOU 1176  C   GLN B  25    17081  13287  22927   5489  -5079  -4369       C  
ATOM   1177  O   GLN B  25      11.489  40.648  39.619  1.00146.81           O  
ANISOU 1177  O   GLN B  25    17555  13779  24447   5953  -5704  -4823       O  
ATOM   1178  CB  GLN B  25      14.392  40.946  38.589  1.00134.56           C  
ANISOU 1178  CB  GLN B  25    18077  11936  21114   5087  -5982  -3489       C  
ATOM   1179  CG  GLN B  25      13.907  42.265  38.039  1.00141.11           C  
ANISOU 1179  CG  GLN B  25    19206  12116  22292   5516  -7013  -3723       C  
ATOM   1180  CD  GLN B  25      14.877  42.863  37.044  1.00139.97           C  
ANISOU 1180  CD  GLN B  25    20125  11498  21558   5234  -7633  -3187       C  
ATOM   1181  OE1 GLN B  25      16.060  42.509  37.020  1.00133.75           O  
ANISOU 1181  OE1 GLN B  25    19813  10901  20105   4752  -7182  -2694       O  
ATOM   1182  NE2 GLN B  25      14.384  43.784  36.221  1.00146.00           N  
ANISOU 1182  NE2 GLN B  25    21277  11617  22578   5527  -8672  -3293       N  
ATOM   1183  N   GLU B  26      12.408  38.666  40.121  1.00137.48           N  
ANISOU 1183  N   GLU B  26    16316  13405  22515   5151  -4359  -4243       N  
ATOM   1184  CA  GLU B  26      11.130  37.960  40.137  1.00142.17           C  
ANISOU 1184  CA  GLU B  26    15958  14172  23887   5275  -4185  -4638       C  
ATOM   1185  C   GLU B  26      10.675  37.668  41.565  1.00144.57           C  
ANISOU 1185  C   GLU B  26    15577  14959  24394   5341  -3151  -5029       C  
ATOM   1186  O   GLU B  26       9.913  36.729  41.802  1.00146.78           O  
ANISOU 1186  O   GLU B  26    15115  15547  25107   5216  -2630  -5206       O  
ATOM   1187  CB  GLU B  26      11.233  36.650  39.360  1.00138.47           C  
ANISOU 1187  CB  GLU B  26    15482  13851  23279   4837  -4128  -4250       C  
ATOM   1188  CG  GLU B  26      11.375  36.823  37.864  1.00138.41           C  
ANISOU 1188  CG  GLU B  26    16054  13351  23185   4816  -5150  -3963       C  
ATOM   1189  CD  GLU B  26      11.805  35.540  37.173  1.00134.27           C  
ANISOU 1189  CD  GLU B  26    15742  12997  22276   4346  -5002  -3506       C  
ATOM   1190  OE1 GLU B  26      12.675  34.825  37.720  1.00129.47           O  
ANISOU 1190  OE1 GLU B  26    15319  12793  21080   3961  -4239  -3185       O  
ATOM   1191  OE2 GLU B  26      11.282  35.250  36.077  1.00136.69           O  
ANISOU 1191  OE2 GLU B  26    16068  12999  22869   4383  -5703  -3487       O  
ATOM   1192  N   GLY B  27      11.149  38.470  42.514  1.00144.60           N  
ANISOU 1192  N   GLY B  27    15877  15003  24064   5517  -2851  -5157       N  
ATOM   1193  CA  GLY B  27      10.824  38.265  43.920  1.00147.06           C  
ANISOU 1193  CA  GLY B  27    15730  15744  24404   5580  -1836  -5511       C  
ATOM   1194  C   GLY B  27      11.714  37.232  44.588  1.00141.03           C  
ANISOU 1194  C   GLY B  27    15305  15408  22874   5056   -979  -5075       C  
ATOM   1195  O   GLY B  27      11.906  37.268  45.802  1.00141.78           O  
ANISOU 1195  O   GLY B  27    15464  15763  22642   5070   -236  -5223       O  
ATOM   1196  N   ILE B  28      12.266  36.313  43.795  1.00135.38           N  
ANISOU 1196  N   ILE B  28    14858  14731  21850   4615  -1118  -4555       N  
ATOM   1197  CA  ILE B  28      13.100  35.235  44.334  1.00129.73           C  
ANISOU 1197  CA  ILE B  28    14447  14379  20464   4124   -404  -4147       C  
ATOM   1198  C   ILE B  28      14.281  35.781  45.134  1.00126.25           C  
ANISOU 1198  C   ILE B  28    14744  13937  19289   4096   -217  -3972       C  
ATOM   1199  O   ILE B  28      15.444  35.495  44.844  1.00120.13           O  
ANISOU 1199  O   ILE B  28    14579  13132  17933   3780   -342  -3496       O  
ATOM   1200  CB  ILE B  28      13.589  34.256  43.237  1.00124.49           C  
ANISOU 1200  CB  ILE B  28    14017  13697  19588   3711   -705  -3639       C  
ATOM   1201  CG1 ILE B  28      12.425  33.838  42.337  1.00128.30           C  
ANISOU 1201  CG1 ILE B  28    13842  14075  20831   3786  -1090  -3827       C  
ATOM   1202  CG2 ILE B  28      14.239  33.030  43.863  1.00119.73           C  
ANISOU 1202  CG2 ILE B  28    13583  13471  18439   3248     43  -3316       C  
ATOM   1203  CD1 ILE B  28      11.137  33.583  43.088  1.00134.90           C  
ANISOU 1203  CD1 ILE B  28    13738  15144  22374   3936   -518  -4346       C  
ATOM   1204  N   GLU B  29      13.951  36.585  46.138  1.00130.82           N  
ANISOU 1204  N   GLU B  29    15232  14527  19945   4450     63  -4401       N  
ATOM   1205  CA  GLU B  29      14.901  37.089  47.123  1.00129.12           C  
ANISOU 1205  CA  GLU B  29    15655  14312  19091   4474    301  -4341       C  
ATOM   1206  C   GLU B  29      16.232  36.332  47.162  1.00121.79           C  
ANISOU 1206  C   GLU B  29    15350  13485  17439   3996    441  -3776       C  
ATOM   1207  O   GLU B  29      17.267  36.846  46.737  1.00118.02           O  
ANISOU 1207  O   GLU B  29    15446  12753  16644   3921    -77  -3472       O  
ATOM   1208  CB  GLU B  29      14.257  37.014  48.508  1.00134.60           C  
ANISOU 1208  CB  GLU B  29    16056  15298  19787   4644   1177  -4790       C  
ATOM   1209  CG  GLU B  29      15.151  37.474  49.638  1.00134.59           C  
ANISOU 1209  CG  GLU B  29    16757  15281  19099   4699   1436  -4779       C  
ATOM   1210  CD  GLU B  29      14.854  38.900  50.062  1.00140.97           C  
ANISOU 1210  CD  GLU B  29    17635  15824  20105   5263   1132  -5260       C  
ATOM   1211  OE1 GLU B  29      13.663  39.224  50.283  1.00147.56           O  
ANISOU 1211  OE1 GLU B  29    17826  16723  21516   5629   1363  -5807       O  
ATOM   1212  OE2 GLU B  29      15.813  39.694  50.182  1.00138.99           O  
ANISOU 1212  OE2 GLU B  29    18057  15283  19470   5344    655  -5112       O  
ATOM   1213  N   GLU B  30      16.186  35.110  47.685  1.00120.37           N  
ANISOU 1213  N   GLU B  30    15036  13658  17040   3666   1144  -3657       N  
ATOM   1214  CA  GLU B  30      17.386  34.339  48.027  1.00114.53           C  
ANISOU 1214  CA  GLU B  30    14864  13029  15622   3269   1369  -3225       C  
ATOM   1215  C   GLU B  30      18.167  33.786  46.832  1.00108.14           C  
ANISOU 1215  C   GLU B  30    14258  12132  14699   2940    900  -2742       C  
ATOM   1216  O   GLU B  30      18.991  32.885  46.982  1.00104.00           O  
ANISOU 1216  O   GLU B  30    14032  11738  13746   2594   1115  -2416       O  
ATOM   1217  CB  GLU B  30      17.012  33.182  48.957  1.00116.23           C  
ANISOU 1217  CB  GLU B  30    14920  13602  15640   3019   2235  -3259       C  
ATOM   1218  CG  GLU B  30      16.060  32.170  48.326  1.00118.44           C  
ANISOU 1218  CG  GLU B  30    14537  14070  16394   2810   2434  -3245       C  
ATOM   1219  CD  GLU B  30      14.675  32.752  48.053  1.00126.61           C  
ANISOU 1219  CD  GLU B  30    14808  15074  18223   3159   2378  -3721       C  
ATOM   1220  OE1 GLU B  30      14.314  33.790  48.662  1.00131.07           O  
ANISOU 1220  OE1 GLU B  30    15318  15562  18919   3561   2439  -4131       O  
ATOM   1221  OE2 GLU B  30      13.944  32.163  47.226  1.00128.40           O  
ANISOU 1221  OE2 GLU B  30    14480  15330  18976   3051   2233  -3714       O  
ATOM   1222  N   ALA B  31      17.913  34.311  45.645  1.00107.63           N  
ANISOU 1222  N   ALA B  31    14071  11825  14999   3059    252  -2710       N  
ATOM   1223  CA  ALA B  31      18.673  33.876  44.493  1.00102.36           C  
ANISOU 1223  CA  ALA B  31    13680  11054  14158   2765   -157  -2273       C  
ATOM   1224  C   ALA B  31      20.135  34.232  44.693  1.00 98.14           C  
ANISOU 1224  C   ALA B  31    13789  10398  13100   2610   -280  -1986       C  
ATOM   1225  O   ALA B  31      20.456  35.329  45.146  1.00 99.65           O  
ANISOU 1225  O   ALA B  31    14252  10380  13230   2827   -485  -2114       O  
ATOM   1226  CB  ALA B  31      18.141  34.520  43.235  1.00104.19           C  
ANISOU 1226  CB  ALA B  31    13811  10977  14799   2944   -867  -2306       C  
ATOM   1227  N   SER B  32      21.023  33.307  44.358  1.00 93.28           N  
ANISOU 1227  N   SER B  32    13391   9894  12158   2244   -180  -1625       N  
ATOM   1228  CA  SER B  32      22.445  33.568  44.480  1.00 89.78           C  
ANISOU 1228  CA  SER B  32    13459   9331  11321   2073   -302  -1371       C  
ATOM   1229  C   SER B  32      23.242  32.842  43.416  1.00 85.83           C  
ANISOU 1229  C   SER B  32    13108   8842  10659   1735   -437   -997       C  
ATOM   1230  O   SER B  32      22.733  31.968  42.732  1.00 85.20           O  
ANISOU 1230  O   SER B  32    12794   8893  10686   1622   -388   -923       O  
ATOM   1231  CB  SER B  32      22.944  33.158  45.860  1.00 89.20           C  
ANISOU 1231  CB  SER B  32    13560   9417  10914   2022    151  -1434       C  
ATOM   1232  OG  SER B  32      23.276  31.794  45.880  1.00 86.37           O  
ANISOU 1232  OG  SER B  32    13179   9289  10351   1718    464  -1234       O  
ATOM   1233  N   LEU B  33      24.505  33.211  43.292  1.00 83.61           N  
ANISOU 1233  N   LEU B  33    13210   8414  10146   1575   -599   -785       N  
ATOM   1234  CA  LEU B  33      25.386  32.575  42.346  1.00 80.60           C  
ANISOU 1234  CA  LEU B  33    12973   8050   9601   1259   -647   -468       C  
ATOM   1235  C   LEU B  33      25.416  31.082  42.584  1.00 78.24           C  
ANISOU 1235  C   LEU B  33    12501   8054   9172   1082   -266   -412       C  
ATOM   1236  O   LEU B  33      25.008  30.312  41.722  1.00 77.60           O  
ANISOU 1236  O   LEU B  33    12276   8066   9143    982   -275   -318       O  
ATOM   1237  CB  LEU B  33      26.795  33.119  42.495  1.00 79.58           C  
ANISOU 1237  CB  LEU B  33    13178   7753   9304   1100   -751   -314       C  
ATOM   1238  CG  LEU B  33      27.418  33.506  41.160  1.00 80.25           C  
ANISOU 1238  CG  LEU B  33    13487   7645   9360    886  -1010    -48       C  
ATOM   1239  CD1 LEU B  33      28.932  33.478  41.233  1.00 79.62           C  
ANISOU 1239  CD1 LEU B  33    13578   7517   9157    611   -928    124       C  
ATOM   1240  CD2 LEU B  33      26.932  32.559  40.112  1.00 80.79           C  
ANISOU 1240  CD2 LEU B  33    13444   7857   9395    785   -956     64       C  
ATOM   1241  N   SER B  34      25.902  30.668  43.752  1.00 77.26           N  
ANISOU 1241  N   SER B  34    12451   8040   8864   1048     14   -471       N  
ATOM   1242  CA  SER B  34      26.063  29.246  44.038  1.00 75.35           C  
ANISOU 1242  CA  SER B  34    12144   8024   8461    859    319   -397       C  
ATOM   1243  C   SER B  34      24.695  28.596  43.933  1.00 76.89           C  
ANISOU 1243  C   SER B  34    11987   8392   8836    903    519   -502       C  
ATOM   1244  O   SER B  34      24.465  27.640  43.197  1.00 75.62           O  
ANISOU 1244  O   SER B  34    11679   8333   8718    752    531   -385       O  
ATOM   1245  CB  SER B  34      26.633  29.040  45.443  1.00 75.57           C  
ANISOU 1245  CB  SER B  34    12401   8069   8244    863    521   -480       C  
ATOM   1246  OG  SER B  34      25.702  28.395  46.305  1.00 77.18           O  
ANISOU 1246  OG  SER B  34    12500   8445   8380    900    902   -622       O  
ATOM   1247  N   ASN B  35      23.794  29.145  44.716  1.00 80.22           N  
ANISOU 1247  N   ASN B  35    12259   8830   9390   1118    680   -754       N  
ATOM   1248  CA  ASN B  35      22.381  28.890  44.622  1.00 83.24           C  
ANISOU 1248  CA  ASN B  35    12199   9329  10098   1211    846   -933       C  
ATOM   1249  C   ASN B  35      21.902  28.473  43.222  1.00 82.80           C  
ANISOU 1249  C   ASN B  35    11908   9248  10306   1140    546   -819       C  
ATOM   1250  O   ASN B  35      21.344  27.394  43.036  1.00 82.77           O  
ANISOU 1250  O   ASN B  35    11650   9390  10409    989    716   -788       O  
ATOM   1251  CB  ASN B  35      21.690  30.181  45.044  1.00 87.10           C  
ANISOU 1251  CB  ASN B  35    12571   9700  10822   1552    775  -1236       C  
ATOM   1252  CG  ASN B  35      20.235  30.022  45.184  1.00 91.22           C  
ANISOU 1252  CG  ASN B  35    12559  10345  11755   1686   1014  -1512       C  
ATOM   1253  OD1 ASN B  35      19.764  28.964  45.556  1.00 92.65           O  
ANISOU 1253  OD1 ASN B  35    12517  10741  11945   1501   1442  -1512       O  
ATOM   1254  ND2 ASN B  35      19.495  31.071  44.886  1.00 95.72           N  
ANISOU 1254  ND2 ASN B  35    12898  10756  12714   2003    725  -1764       N  
ATOM   1255  N   VAL B  36      22.114  29.342  42.240  1.00 82.68           N  
ANISOU 1255  N   VAL B  36    12035   9005  10375   1240     71   -753       N  
ATOM   1256  CA  VAL B  36      21.626  29.102  40.891  1.00 82.86           C  
ANISOU 1256  CA  VAL B  36    11958   8929  10596   1217   -295   -666       C  
ATOM   1257  C   VAL B  36      22.463  28.073  40.146  1.00 79.59           C  
ANISOU 1257  C   VAL B  36    11770   8581   9891    933   -297   -378       C  
ATOM   1258  O   VAL B  36      21.926  27.252  39.412  1.00 80.23           O  
ANISOU 1258  O   VAL B  36    11698   8694  10092    859   -400   -336       O  
ATOM   1259  CB  VAL B  36      21.593  30.393  40.056  1.00 84.56           C  
ANISOU 1259  CB  VAL B  36    12391   8819  10920   1403   -836   -670       C  
ATOM   1260  CG1 VAL B  36      21.609  30.063  38.581  1.00 83.91           C  
ANISOU 1260  CG1 VAL B  36    12498   8589  10795   1294  -1226   -468       C  
ATOM   1261  CG2 VAL B  36      20.376  31.233  40.405  1.00 88.71           C  
ANISOU 1261  CG2 VAL B  36    12568   9238  11900   1748   -988  -1019       C  
ATOM   1262  N   SER B  37      23.781  28.119  40.303  1.00 76.69           N  
ANISOU 1262  N   SER B  37    11749   8212   9179    787   -213   -208       N  
ATOM   1263  CA  SER B  37      24.636  27.126  39.649  1.00 73.82           C  
ANISOU 1263  CA  SER B  37    11558   7922   8567    546   -171      9       C  
ATOM   1264  C   SER B  37      24.253  25.730  40.131  1.00 73.23           C  
ANISOU 1264  C   SER B  37    11259   8066   8499    431    110    -15       C  
ATOM   1265  O   SER B  37      24.277  24.769  39.379  1.00 72.56           O  
ANISOU 1265  O   SER B  37    11179   8024   8365    304     48     89       O  
ATOM   1266  CB  SER B  37      26.117  27.372  39.950  1.00 71.60           C  
ANISOU 1266  CB  SER B  37    11566   7613   8025    420    -79    126       C  
ATOM   1267  OG  SER B  37      26.448  28.747  39.950  1.00 72.31           O  
ANISOU 1267  OG  SER B  37    11839   7493   8144    509   -271    121       O  
ATOM   1268  N   SER B  38      23.910  25.620  41.402  1.00 74.26           N  
ANISOU 1268  N   SER B  38    11248   8309   8659    464    421   -153       N  
ATOM   1269  CA  SER B  38      23.495  24.352  41.946  1.00 74.56           C  
ANISOU 1269  CA  SER B  38    11130   8516   8684    312    713   -157       C  
ATOM   1270  C   SER B  38      22.303  23.845  41.145  1.00 76.69           C  
ANISOU 1270  C   SER B  38    11048   8796   9293    305    586   -197       C  
ATOM   1271  O   SER B  38      22.310  22.732  40.619  1.00 75.60           O  
ANISOU 1271  O   SER B  38    10901   8698   9126    140    535    -84       O  
ATOM   1272  CB  SER B  38      23.124  24.533  43.414  1.00 76.47           C  
ANISOU 1272  CB  SER B  38    11330   8841   8886    359   1102   -318       C  
ATOM   1273  OG  SER B  38      22.542  23.365  43.939  1.00 77.94           O  
ANISOU 1273  OG  SER B  38    11376   9163   9073    174   1426   -314       O  
ATOM   1274  N   MET B  39      21.278  24.682  41.044  1.00 80.08           N  
ANISOU 1274  N   MET B  39    11184   9158  10086    506    476   -385       N  
ATOM   1275  CA  MET B  39      20.080  24.317  40.298  1.00 83.04           C  
ANISOU 1275  CA  MET B  39    11166   9489  10896    536    266   -475       C  
ATOM   1276  C   MET B  39      20.424  23.941  38.850  1.00 81.36           C  
ANISOU 1276  C   MET B  39    11195   9134  10585    485   -199   -293       C  
ATOM   1277  O   MET B  39      19.846  23.018  38.287  1.00 82.31           O  
ANISOU 1277  O   MET B  39    11139   9246  10889    390   -336   -275       O  
ATOM   1278  CB  MET B  39      19.038  25.440  40.360  1.00 87.21           C  
ANISOU 1278  CB  MET B  39    11346   9910  11879    824    118   -753       C  
ATOM   1279  CG  MET B  39      17.852  25.247  39.430  1.00 91.81           C  
ANISOU 1279  CG  MET B  39    11525  10360  12999    910   -276   -880       C  
ATOM   1280  SD  MET B  39      18.173  25.820  37.738  1.00 94.93           S  
ANISOU 1280  SD  MET B  39    12364  10410  13294   1041  -1080   -733       S  
ATOM   1281  CE  MET B  39      17.656  27.539  37.849  1.00 97.24           C  
ANISOU 1281  CE  MET B  39    12583  10466  13897   1424  -1404   -994       C  
ATOM   1282  N   LEU B  40      21.376  24.651  38.258  1.00 79.34           N  
ANISOU 1282  N   LEU B  40    11371   8749  10026    532   -423   -162       N  
ATOM   1283  CA  LEU B  40      21.788  24.361  36.897  1.00 78.43           C  
ANISOU 1283  CA  LEU B  40    11586   8496   9718    475   -779      7       C  
ATOM   1284  C   LEU B  40      22.552  23.056  36.810  1.00 75.93           C  
ANISOU 1284  C   LEU B  40    11413   8325   9111    254   -583    153       C  
ATOM   1285  O   LEU B  40      22.431  22.339  35.827  1.00 76.35           O  
ANISOU 1285  O   LEU B  40    11581   8311   9117    205   -823    221       O  
ATOM   1286  CB  LEU B  40      22.652  25.481  36.336  1.00 77.76           C  
ANISOU 1286  CB  LEU B  40    11948   8235   9364    525   -966    120       C  
ATOM   1287  CG  LEU B  40      21.911  26.770  35.999  1.00 81.21           C  
ANISOU 1287  CG  LEU B  40    12394   8412  10052    760  -1366      6       C  
ATOM   1288  CD1 LEU B  40      22.859  27.744  35.329  1.00 81.22           C  
ANISOU 1288  CD1 LEU B  40    12939   8200   9719    723  -1547    183       C  
ATOM   1289  CD2 LEU B  40      20.725  26.494  35.107  1.00 83.67           C  
ANISOU 1289  CD2 LEU B  40    12554   8550  10685    881  -1827    -90       C  
ATOM   1290  N   LEU B  41      23.358  22.754  37.818  1.00 73.84           N  
ANISOU 1290  N   LEU B  41    11188   8222   8647    145   -206    184       N  
ATOM   1291  CA  LEU B  41      24.058  21.485  37.842  1.00 72.01           C  
ANISOU 1291  CA  LEU B  41    11074   8096   8190    -33    -69    282       C  
ATOM   1292  C   LEU B  41      23.045  20.348  37.929  1.00 74.01           C  
ANISOU 1292  C   LEU B  41    11048   8400   8673   -126    -65    243       C  
ATOM   1293  O   LEU B  41      23.080  19.390  37.162  1.00 73.87           O  
ANISOU 1293  O   LEU B  41    11117   8350   8601   -204   -244    308       O  
ATOM   1294  CB  LEU B  41      24.984  21.423  39.042  1.00 69.91           C  
ANISOU 1294  CB  LEU B  41    10904   7931   7728   -102    246    286       C  
ATOM   1295  CG  LEU B  41      26.293  22.183  38.943  1.00 67.68           C  
ANISOU 1295  CG  LEU B  41    10887   7594   7236    -84    240    340       C  
ATOM   1296  CD1 LEU B  41      27.027  22.076  40.253  1.00 65.33           C  
ANISOU 1296  CD1 LEU B  41    10655   7344   6821   -122    455    301       C  
ATOM   1297  CD2 LEU B  41      27.140  21.643  37.820  1.00 65.39           C  
ANISOU 1297  CD2 LEU B  41    10798   7283   6763   -163    138    437       C  
ATOM   1298  N   GLU B  42      22.138  20.459  38.883  1.00 76.61           N  
ANISOU 1298  N   GLU B  42    11041   8798   9269   -129    163    126       N  
ATOM   1299  CA  GLU B  42      21.104  19.467  39.049  1.00 79.54           C  
ANISOU 1299  CA  GLU B  42    11082   9207   9935   -268    231     85       C  
ATOM   1300  C   GLU B  42      20.477  19.216  37.684  1.00 81.08           C  
ANISOU 1300  C   GLU B  42    11194   9243  10367   -210   -254     80       C  
ATOM   1301  O   GLU B  42      20.327  18.077  37.259  1.00 81.26           O  
ANISOU 1301  O   GLU B  42    11224   9236  10416   -350   -388    144       O  
ATOM   1302  CB  GLU B  42      20.055  20.002  40.022  1.00 83.21           C  
ANISOU 1302  CB  GLU B  42    11128   9744  10746   -230    548    -98       C  
ATOM   1303  CG  GLU B  42      19.623  19.034  41.107  1.00 85.98           C  
ANISOU 1303  CG  GLU B  42    11320  10221  11128   -487   1011    -94       C  
ATOM   1304  CD  GLU B  42      19.405  19.738  42.441  1.00 89.51           C  
ANISOU 1304  CD  GLU B  42    11696  10779  11533   -444   1511   -232       C  
ATOM   1305  OE1 GLU B  42      20.185  20.666  42.762  1.00 88.20           O  
ANISOU 1305  OE1 GLU B  42    11821  10601  11090   -268   1505   -251       O  
ATOM   1306  OE2 GLU B  42      18.462  19.363  43.168  1.00 93.81           O  
ANISOU 1306  OE2 GLU B  42    11910  11411  12321   -596   1924   -330       O  
ATOM   1307  N   LEU B  43      20.129  20.295  36.998  1.00 82.77           N  
ANISOU 1307  N   LEU B  43    11397   9315  10737      8   -573      1       N  
ATOM   1308  CA  LEU B  43      19.452  20.212  35.714  1.00 85.48           C  
ANISOU 1308  CA  LEU B  43    11736   9439  11305    106  -1126    -28       C  
ATOM   1309  C   LEU B  43      20.336  19.494  34.707  1.00 84.00           C  
ANISOU 1309  C   LEU B  43    12050   9186  10680     39  -1340    142       C  
ATOM   1310  O   LEU B  43      19.890  18.589  34.008  1.00 85.32           O  
ANISOU 1310  O   LEU B  43    12215   9248  10955     -9  -1641    147       O  
ATOM   1311  CB  LEU B  43      19.106  21.616  35.216  1.00 87.20           C  
ANISOU 1311  CB  LEU B  43    12002   9461  11668    366  -1471   -127       C  
ATOM   1312  CG  LEU B  43      17.913  21.838  34.292  1.00 90.93           C  
ANISOU 1312  CG  LEU B  43    12279   9655  12615    541  -2083   -276       C  
ATOM   1313  CD1 LEU B  43      18.382  22.113  32.891  1.00 90.61           C  
ANISOU 1313  CD1 LEU B  43    12880   9344  12203    631  -2612   -141       C  
ATOM   1314  CD2 LEU B  43      16.944  20.673  34.358  1.00 92.98           C  
ANISOU 1314  CD2 LEU B  43    12052   9935  13341    409  -2125   -367       C  
ATOM   1315  N   GLY B  44      21.600  19.887  34.651  1.00 81.91           N  
ANISOU 1315  N   GLY B  44    12198   8978   9947     35  -1171    258       N  
ATOM   1316  CA  GLY B  44      22.528  19.313  33.696  1.00 81.76           C  
ANISOU 1316  CA  GLY B  44    12641   8918   9507    -11  -1280    377       C  
ATOM   1317  C   GLY B  44      22.689  17.827  33.900  1.00 81.85           C  
ANISOU 1317  C   GLY B  44    12598   9025   9475   -161  -1185    397       C  
ATOM   1318  O   GLY B  44      22.742  17.063  32.950  1.00 82.60           O  
ANISOU 1318  O   GLY B  44    12930   9018   9435   -159  -1454    418       O  
ATOM   1319  N   LEU B  45      22.776  17.412  35.150  1.00 81.98           N  
ANISOU 1319  N   LEU B  45    12369   9205   9573   -288   -826    387       N  
ATOM   1320  CA  LEU B  45      22.891  16.009  35.455  1.00 82.93           C  
ANISOU 1320  CA  LEU B  45    12478   9371   9660   -450   -769    418       C  
ATOM   1321  C   LEU B  45      21.695  15.229  34.927  1.00 87.13           C  
ANISOU 1321  C   LEU B  45    12796   9769  10539   -504  -1097    383       C  
ATOM   1322  O   LEU B  45      21.848  14.176  34.317  1.00 87.18           O  
ANISOU 1322  O   LEU B  45    12988   9692  10444   -552  -1329    410       O  
ATOM   1323  CB  LEU B  45      22.996  15.823  36.959  1.00 82.10           C  
ANISOU 1323  CB  LEU B  45    12210   9405   9579   -591   -355    423       C  
ATOM   1324  CG  LEU B  45      24.389  15.971  37.552  1.00 78.80           C  
ANISOU 1324  CG  LEU B  45    12067   9069   8806   -583   -131    455       C  
ATOM   1325  CD1 LEU B  45      24.297  16.008  39.065  1.00 78.71           C  
ANISOU 1325  CD1 LEU B  45    11970   9136   8802   -689    215    447       C  
ATOM   1326  CD2 LEU B  45      25.279  14.832  37.089  1.00 76.50           C  
ANISOU 1326  CD2 LEU B  45    12038   8745   8284   -621   -266    481       C  
ATOM   1327  N   ARG B  46      20.499  15.743  35.170  1.00 91.80           N  
ANISOU 1327  N   ARG B  46    12970  10324  11587   -487  -1138    294       N  
ATOM   1328  CA  ARG B  46      19.304  15.035  34.772  1.00 97.50           C  
ANISOU 1328  CA  ARG B  46    13376  10900  12769   -561  -1453    232       C  
ATOM   1329  C   ARG B  46      19.338  14.709  33.284  1.00 99.85           C  
ANISOU 1329  C   ARG B  46    14026  10968  12946   -430  -2045    238       C  
ATOM   1330  O   ARG B  46      19.053  13.583  32.881  1.00101.17           O  
ANISOU 1330  O   ARG B  46    14218  11018  13205   -531  -2310    250       O  
ATOM   1331  CB  ARG B  46      18.068  15.849  35.126  1.00100.78           C  
ANISOU 1331  CB  ARG B  46    13238  11292  13763   -499  -1438     73       C  
ATOM   1332  CG  ARG B  46      16.803  15.017  35.195  1.00106.25           C  
ANISOU 1332  CG  ARG B  46    13408  11890  15071   -674  -1564    -12       C  
ATOM   1333  CD  ARG B  46      16.034  15.305  36.480  1.00110.47           C  
ANISOU 1333  CD  ARG B  46    13360  12595  16018   -813  -1003   -123       C  
ATOM   1334  NE  ARG B  46      16.020  16.734  36.795  1.00111.37           N  
ANISOU 1334  NE  ARG B  46    13377  12781  16159   -562   -856   -257       N  
ATOM   1335  CZ  ARG B  46      15.004  17.555  36.531  1.00115.55           C  
ANISOU 1335  CZ  ARG B  46    13444  13195  17263   -362  -1097   -490       C  
ATOM   1336  NH1 ARG B  46      13.900  17.086  35.949  1.00119.79           N  
ANISOU 1336  NH1 ARG B  46    13528  13542  18445   -392  -1500   -622       N  
ATOM   1337  NH2 ARG B  46      15.091  18.846  36.851  1.00114.98           N  
ANISOU 1337  NH2 ARG B  46    13357  13166  17166   -119   -987   -612       N  
ATOM   1338  N   VAL B  47      19.700  15.695  32.473  1.00101.74           N  
ANISOU 1338  N   VAL B  47    14601  11114  12940   -215  -2257    235       N  
ATOM   1339  CA  VAL B  47      19.744  15.504  31.040  1.00105.59           C  
ANISOU 1339  CA  VAL B  47    15553  11355  13211    -79  -2797    241       C  
ATOM   1340  C   VAL B  47      20.803  14.492  30.689  1.00105.86           C  
ANISOU 1340  C   VAL B  47    16017  11450  12755   -142  -2700    317       C  
ATOM   1341  O   VAL B  47      20.565  13.552  29.947  1.00107.51           O  
ANISOU 1341  O   VAL B  47    16413  11491  12946   -135  -3081    292       O  
ATOM   1342  CB  VAL B  47      20.056  16.802  30.308  1.00105.62           C  
ANISOU 1342  CB  VAL B  47    15955  11236  12941    116  -2962    259       C  
ATOM   1343  CG1 VAL B  47      20.199  16.534  28.828  1.00107.53           C  
ANISOU 1343  CG1 VAL B  47    16827  11208  12819    233  -3463    283       C  
ATOM   1344  CG2 VAL B  47      18.960  17.813  30.558  1.00108.09           C  
ANISOU 1344  CG2 VAL B  47    15861  11428  13780    239  -3178    137       C  
ATOM   1345  N   TYR B  48      21.987  14.687  31.227  1.00 57.43           N  
ATOM   1346  CA  TYR B  48      23.069  13.750  30.962  1.00 61.44           C  
ATOM   1347  C   TYR B  48      22.589  12.296  31.132  1.00 63.81           C  
ATOM   1348  O   TYR B  48      22.794  11.464  30.242  1.00 64.09           O  
ATOM   1349  CB  TYR B  48      24.237  14.033  31.880  1.00 61.60           C  
ATOM   1350  CG  TYR B  48      25.432  13.178  31.598  1.00 63.92           C  
ATOM   1351  CD1 TYR B  48      25.591  11.945  32.213  1.00 65.95           C  
ATOM   1352  CD2 TYR B  48      26.416  13.610  30.726  1.00 65.80           C  
ATOM   1353  CE1 TYR B  48      26.707  11.164  31.963  1.00 67.97           C  
ATOM   1354  CE2 TYR B  48      27.530  12.843  30.468  1.00 67.59           C  
ATOM   1355  CZ  TYR B  48      27.670  11.620  31.084  1.00 68.72           C  
ATOM   1356  OH  TYR B  48      28.787  10.859  30.817  1.00 70.53           O  
ATOM   1357  N   MET B  49      21.955  12.007  32.274  1.00 66.67           N  
ATOM   1358  CA  MET B  49      21.284  10.725  32.520  1.00 69.57           C  
ATOM   1359  C   MET B  49      20.351  10.342  31.377  1.00 70.51           C  
ATOM   1360  O   MET B  49      20.550   9.319  30.730  1.00 70.62           O  
ATOM   1361  CB  MET B  49      20.499  10.769  33.838  1.00 70.15           C  
ATOM   1362  CG  MET B  49      21.052   9.850  34.930  1.00 74.92           C  
ATOM   1363  SD  MET B  49      22.859   9.533  34.829  1.00 85.63           S  
ATOM   1364  CE  MET B  49      23.134   8.474  36.285  1.00 83.46           C  
ATOM   1365  N   ILE B  50      19.329  11.161  31.146  1.00 71.90           N  
ATOM   1366  CA  ILE B  50      18.418  10.960  30.024  1.00 73.35           C  
ATOM   1367  C   ILE B  50      19.132  10.626  28.686  1.00 74.56           C  
ATOM   1368  O   ILE B  50      18.795   9.634  28.031  1.00 74.77           O  
ATOM   1369  CB  ILE B  50      17.537  12.185  29.807  1.00 73.31           C  
ATOM   1370  CG1 ILE B  50      16.881  12.617  31.121  1.00 73.60           C  
ATOM   1371  CG2 ILE B  50      16.513  11.904  28.724  1.00 73.07           C  
ATOM   1372  CD1 ILE B  50      15.650  11.860  31.462  1.00 74.00           C  
ATOM   1373  N   GLN B  51      20.095  11.451  28.274  1.00 75.71           N  
ATOM   1374  CA  GLN B  51      20.862  11.150  27.071  1.00 77.18           C  
ATOM   1375  C   GLN B  51      21.486   9.767  27.178  1.00 77.88           C  
ATOM   1376  O   GLN B  51      21.410   8.959  26.257  1.00 77.90           O  
ATOM   1377  CB  GLN B  51      21.959  12.190  26.837  1.00 77.34           C  
ATOM   1378  CG  GLN B  51      21.427  13.561  26.465  1.00 78.77           C  
ATOM   1379  CD  GLN B  51      20.573  13.536  25.212  1.00 80.43           C  
ATOM   1380  OE1 GLN B  51      19.347  13.677  25.277  1.00 80.63           O  
ATOM   1381  NE2 GLN B  51      21.218  13.342  24.057  1.00 80.64           N  
ATOM   1382  N   GLN B  52      22.116   9.525  28.318  1.00 78.91           N  
ATOM   1383  CA  GLN B  52      22.743   8.259  28.644  1.00 79.66           C  
ATOM   1384  C   GLN B  52      21.823   7.094  28.304  1.00 79.47           C  
ATOM   1385  O   GLN B  52      22.225   6.132  27.653  1.00 79.75           O  
ATOM   1386  CB  GLN B  52      23.025   8.248  30.143  1.00 80.24           C  
ATOM   1387  CG  GLN B  52      23.889   7.116  30.626  1.00 82.22           C  
ATOM   1388  CD  GLN B  52      25.357   7.419  30.436  1.00 84.90           C  
ATOM   1389  OE1 GLN B  52      25.751   8.086  29.465  1.00 85.69           O  
ATOM   1390  NE2 GLN B  52      26.183   6.941  31.369  1.00 85.10           N  
ATOM   1391  N   GLU B  53      20.582   7.195  28.751  1.00 77.14           N  
ATOM   1392  CA  GLU B  53      19.623   6.126  28.610  1.00 75.63           C  
ATOM   1393  C   GLU B  53      19.249   5.873  27.142  1.00 74.10           C  
ATOM   1394  O   GLU B  53      19.230   4.718  26.677  1.00 73.96           O  
ATOM   1395  CB  GLU B  53      18.370   6.465  29.428  1.00 75.89           C  
ATOM   1396  CG  GLU B  53      17.105   5.701  28.997  1.00 78.07           C  
ATOM   1397  CD  GLU B  53      16.959   5.553  27.460  1.00 79.05           C  
ATOM   1398  OE1 GLU B  53      17.145   4.417  26.946  1.00 78.65           O  
ATOM   1399  OE2 GLU B  53      16.664   6.567  26.778  1.00 79.04           O  
ATOM   1400  N   LYS B  54      19.003   6.973  26.426  1.00 72.09           N  
ATOM   1401  CA  LYS B  54      18.253   7.017  25.152  1.00 69.85           C  
ATOM   1402  C   LYS B  54      18.378   5.872  24.097  1.00 68.60           C  
ATOM   1403  O   LYS B  54      17.392   5.148  23.827  1.00 68.84           O  
ATOM   1404  CB  LYS B  54      18.381   8.412  24.507  1.00 69.98           C  
ATOM   1405  CG  LYS B  54      17.150   9.275  24.744  1.00 68.90           C  
ATOM   1406  CD  LYS B  54      17.394  10.758  24.520  1.00 69.07           C  
ATOM   1407  CE  LYS B  54      16.071  11.534  24.734  1.00 70.80           C  
ATOM   1408  NZ  LYS B  54      16.195  13.010  25.011  1.00 71.20           N  
ATOM   1409  N   ARG B  55      19.549   5.725  23.487  1.00 65.93           N  
ATOM   1410  CA  ARG B  55      19.731   4.778  22.376  1.00 63.59           C  
ATOM   1411  C   ARG B  55      20.979   5.256  21.676  1.00 63.00           C  
ATOM   1412  O   ARG B  55      20.984   6.328  21.079  1.00 63.12           O  
ATOM   1413  CB  ARG B  55      18.524   4.755  21.404  1.00 62.71           C  
ATOM   1414  CG  ARG B  55      17.647   3.475  21.499  1.00 59.47           C  
ATOM   1415  CD  ARG B  55      16.538   3.319  20.423  1.00 51.28           C  
ATOM   1416  NE  ARG B  55      15.250   3.869  20.837  1.00 48.80           N  
ATOM   1417  CZ  ARG B  55      14.084   3.228  20.776  1.00 47.78           C  
ATOM   1418  NH1 ARG B  55      14.034   2.002  20.303  1.00 49.65           N  
ATOM   1419  NH2 ARG B  55      12.958   3.816  21.177  1.00 46.13           N  
ATOM   1420  N   GLU B  56      22.054   4.487  21.775  1.00 61.96           N  
ATOM   1421  CA  GLU B  56      23.355   5.014  21.394  1.00 61.25           C  
ATOM   1422  C   GLU B  56      23.486   6.409  21.999  1.00 61.08           C  
ATOM   1423  O   GLU B  56      24.430   7.142  21.731  1.00 61.07           O  
ATOM   1424  CB  GLU B  56      23.533   5.058  19.871  1.00 61.52           C  
ATOM   1425  CG  GLU B  56      23.651   3.687  19.208  1.00 60.05           C  
ATOM   1426  CD  GLU B  56      22.424   2.850  19.451  1.00 59.79           C  
ATOM   1427  OE1 GLU B  56      21.296   3.325  19.193  1.00 59.72           O  
ATOM   1428  OE2 GLU B  56      22.586   1.715  19.920  1.00 59.69           O  
ATOM   1429  N   GLY B  57      22.520   6.770  22.830  1.00 60.82           N  
ATOM   1430  CA  GLY B  57      22.647   7.949  23.665  1.00 60.23           C  
ATOM   1431  C   GLY B  57      22.087   9.216  23.054  1.00 59.91           C  
ATOM   1432  O   GLY B  57      22.765  10.238  23.033  1.00 60.39           O  
ATOM   1433  N   GLY B  58      20.849   9.160  22.563  1.00 59.08           N  
ATOM   1434  CA  GLY B  58      20.194  10.337  21.991  1.00 57.68           C  
ATOM   1435  C   GLY B  58      20.736  10.838  20.659  1.00 56.43           C  
ATOM   1436  O   GLY B  58      21.724  10.313  20.135  1.00 55.74           O  
ATOM   1437  N   PHE B  59      20.077  11.873  20.134  1.00 55.59           N  
ATOM   1438  CA  PHE B  59      20.373  12.437  18.815  1.00 54.97           C  
ATOM   1439  C   PHE B  59      21.854  12.481  18.501  1.00 54.02           C  
ATOM   1440  O   PHE B  59      22.651  12.548  19.393  1.00 54.90           O  
ATOM   1441  CB  PHE B  59      19.782  13.829  18.681  1.00 55.02           C  
ATOM   1442  CG  PHE B  59      19.988  14.428  17.324  1.00 57.02           C  
ATOM   1443  CD1 PHE B  59      21.102  15.230  17.066  1.00 57.85           C  
ATOM   1444  CD2 PHE B  59      19.091  14.164  16.292  1.00 57.30           C  
ATOM   1445  CE1 PHE B  59      21.320  15.772  15.816  1.00 57.29           C  
ATOM   1446  CE2 PHE B  59      19.290  14.706  15.045  1.00 58.77           C  
ATOM   1447  CZ  PHE B  59      20.414  15.522  14.806  1.00 59.32           C  
ATOM   1448  N   ASN B  60      22.232  12.463  17.233  1.00 53.14           N  
ATOM   1449  CA  ASN B  60      23.645  12.367  16.889  1.00 52.05           C  
ATOM   1450  C   ASN B  60      24.100  13.258  15.695  1.00 51.20           C  
ATOM   1451  O   ASN B  60      24.219  12.754  14.577  1.00 52.14           O  
ATOM   1452  CB  ASN B  60      23.928  10.895  16.601  1.00 51.95           C  
ATOM   1453  CG  ASN B  60      25.362  10.637  16.186  1.00 53.60           C  
ATOM   1454  OD1 ASN B  60      25.818   9.498  16.223  1.00 53.77           O  
ATOM   1455  ND2 ASN B  60      26.085  11.693  15.779  1.00 55.16           N  
ATOM   1456  N   GLN B  61      24.374  14.552  15.907  1.00 99.19           N  
ANISOU 1456  N   GLN B  61    16072   9868  11747   -881  -1015    765       N  
ATOM   1457  CA  GLN B  61      24.654  15.460  14.769  1.00 93.87           C  
ANISOU 1457  CA  GLN B  61    15068   9208  11390   -650   -664    649       C  
ATOM   1458  C   GLN B  61      25.333  14.784  13.585  1.00 92.61           C  
ANISOU 1458  C   GLN B  61    14931   8865  11391   -205   -685    706       C  
ATOM   1459  O   GLN B  61      24.856  14.853  12.453  1.00 90.29           O  
ANISOU 1459  O   GLN B  61    14673   8464  11168    -83   -460    700       O  
ATOM   1460  CB  GLN B  61      25.518  16.661  15.176  1.00 94.07           C  
ANISOU 1460  CB  GLN B  61    14665   9451  11628   -696   -529    501       C  
ATOM   1461  CG  GLN B  61      24.757  17.939  15.447  1.00 90.10           C  
ANISOU 1461  CG  GLN B  61    13996   9083  11155  -1005   -238    347       C  
ATOM   1462  CD  GLN B  61      23.694  18.195  14.426  1.00 85.06           C  
ANISOU 1462  CD  GLN B  61    13448   8321  10548   -973     16    329       C  
ATOM   1463  OE1 GLN B  61      23.876  17.942  13.244  1.00 82.96           O  
ANISOU 1463  OE1 GLN B  61    13210   7907  10403   -687    108    388       O  
ATOM   1464  NE2 GLN B  61      22.570  18.705  14.879  1.00 83.72           N  
ANISOU 1464  NE2 GLN B  61    13311   8233  10264  -1265    126    226       N  
ATOM   1465  N   MET B  62      26.469  14.154  13.848  1.00 93.05           N  
ANISOU 1465  N   MET B  62    14946   8903  11504     47   -961    742       N  
ATOM   1466  CA  MET B  62      27.321  13.705  12.774  1.00 92.03           C  
ANISOU 1466  CA  MET B  62    14716   8673  11578    489   -946    717       C  
ATOM   1467  C   MET B  62      26.636  12.613  11.959  1.00 89.92           C  
ANISOU 1467  C   MET B  62    14851   8124  11190    640  -1006    826       C  
ATOM   1468  O   MET B  62      26.674  12.608  10.728  1.00 88.49           O  
ANISOU 1468  O   MET B  62    14615   7868  11139    864   -787    780       O  
ATOM   1469  CB  MET B  62      28.659  13.246  13.333  1.00 95.63           C  
ANISOU 1469  CB  MET B  62    15014   9197  12123    746  -1269    692       C  
ATOM   1470  CG  MET B  62      29.853  13.633  12.473  1.00 97.97           C  
ANISOU 1470  CG  MET B  62    14874   9626  12724   1081  -1094    524       C  
ATOM   1471  SD  MET B  62      29.876  15.358  11.937  1.00 98.62           S  
ANISOU 1471  SD  MET B  62    14532   9943  12997    847   -564    366       S  
ATOM   1472  CE  MET B  62      29.716  16.216  13.507  1.00 98.63           C  
ANISOU 1472  CE  MET B  62    14430  10150  12895    413   -646    349       C  
ATOM   1473  N   GLU B  63      25.984  11.697  12.653  1.00 88.92           N  
ANISOU 1473  N   GLU B  63    15153   7847  10786    475  -1297    969       N  
ATOM   1474  CA  GLU B  63      25.302  10.606  11.986  1.00 87.19           C  
ANISOU 1474  CA  GLU B  63    15362   7348  10418    564  -1380   1073       C  
ATOM   1475  C   GLU B  63      24.163  11.153  11.137  1.00 82.55           C  
ANISOU 1475  C   GLU B  63    14775   6785   9804    390  -1009   1034       C  
ATOM   1476  O   GLU B  63      23.876  10.660  10.066  1.00 82.05           O  
ANISOU 1476  O   GLU B  63    14862   6560   9755    570   -918   1047       O  
ATOM   1477  CB  GLU B  63      24.768   9.624  13.021  1.00 89.09           C  
ANISOU 1477  CB  GLU B  63    16090   7438  10321    313  -1756   1239       C  
ATOM   1478  CG  GLU B  63      24.699   8.206  12.515  1.00 91.90           C  
ANISOU 1478  CG  GLU B  63    16914   7437  10567    543  -2013   1355       C  
ATOM   1479  CD  GLU B  63      26.049   7.693  12.063  1.00 95.40           C  
ANISOU 1479  CD  GLU B  63    17226   7757  11264   1102  -2206   1302       C  
ATOM   1480  OE1 GLU B  63      26.995   7.720  12.869  1.00 98.67           O  
ANISOU 1480  OE1 GLU B  63    17491   8252  11749   1225  -2471   1297       O  
ATOM   1481  OE2 GLU B  63      26.173   7.251  10.907  1.00 95.73           O  
ANISOU 1481  OE2 GLU B  63    17300   7641  11430   1423  -2100   1245       O  
ATOM   1482  N   TYR B  64      23.517  12.187  11.642  1.00 79.05           N  
ANISOU 1482  N   TYR B  64    14159   6551   9326     47   -813    970       N  
ATOM   1483  CA  TYR B  64      22.416  12.857  10.960  1.00 74.59           C  
ANISOU 1483  CA  TYR B  64    13549   6037   8753   -110   -492    908       C  
ATOM   1484  C   TYR B  64      22.891  13.650   9.743  1.00 72.69           C  
ANISOU 1484  C   TYR B  64    13009   5816   8795    156   -187    823       C  
ATOM   1485  O   TYR B  64      22.327  13.553   8.669  1.00 71.11           O  
ANISOU 1485  O   TYR B  64    12904   5521   8595    245    -27    832       O  
ATOM   1486  CB  TYR B  64      21.730  13.789  11.958  1.00 73.33           C  
ANISOU 1486  CB  TYR B  64    13251   6105   8507   -511   -399    819       C  
ATOM   1487  CG  TYR B  64      20.724  14.739  11.375  1.00 69.62           C  
ANISOU 1487  CG  TYR B  64    12640   5721   8092   -628    -83    706       C  
ATOM   1488  CD1 TYR B  64      19.370  14.463  11.433  1.00 68.15           C  
ANISOU 1488  CD1 TYR B  64    12653   5564   7675   -884    -60    687       C  
ATOM   1489  CD2 TYR B  64      21.125  15.938  10.791  1.00 68.04           C  
ANISOU 1489  CD2 TYR B  64    12108   5578   8166   -493    178    607       C  
ATOM   1490  CE1 TYR B  64      18.441  15.345  10.901  1.00 66.18           C  
ANISOU 1490  CE1 TYR B  64    12248   5403   7494   -943    193    561       C  
ATOM   1491  CE2 TYR B  64      20.200  16.835  10.260  1.00 64.53           C  
ANISOU 1491  CE2 TYR B  64    11567   5173   7780   -565    421    511       C  
ATOM   1492  CZ  TYR B  64      18.868  16.529  10.323  1.00 64.42           C  
ANISOU 1492  CZ  TYR B  64    11725   5192   7558   -762    414    482       C  
ATOM   1493  OH  TYR B  64      17.955  17.400   9.812  1.00 62.76           O  
ANISOU 1493  OH  TYR B  64    11399   5029   7418   -789    614    367       O  
ATOM   1494  N   ASN B  65      23.924  14.456   9.917  1.00 72.58           N  
ANISOU 1494  N   ASN B  65    12642   5938   8999    245   -106    739       N  
ATOM   1495  CA  ASN B  65      24.504  15.136   8.787  1.00 71.34           C  
ANISOU 1495  CA  ASN B  65    12233   5800   9075    456    170    666       C  
ATOM   1496  C   ASN B  65      24.809  14.146   7.679  1.00 71.68           C  
ANISOU 1496  C   ASN B  65    12432   5674   9130    782    142    706       C  
ATOM   1497  O   ASN B  65      24.547  14.400   6.509  1.00 70.68           O  
ANISOU 1497  O   ASN B  65    12304   5498   9054    869    377    692       O  
ATOM   1498  CB  ASN B  65      25.782  15.853   9.201  1.00 72.80           C  
ANISOU 1498  CB  ASN B  65    12038   6162   9461    506    204    565       C  
ATOM   1499  CG  ASN B  65      25.514  17.006  10.106  1.00 72.08           C  
ANISOU 1499  CG  ASN B  65    11769   6230   9387    187    297    493       C  
ATOM   1500  OD1 ASN B  65      26.399  17.471  10.814  1.00 74.96           O  
ANISOU 1500  OD1 ASN B  65    11879   6755   9848    138    252    418       O  
ATOM   1501  ND2 ASN B  65      24.282  17.477  10.101  1.00 69.49           N  
ANISOU 1501  ND2 ASN B  65    11562   5873   8968    -29    421    490       N  
ATOM   1502  N   LYS B  66      25.376  13.012   8.053  1.00 73.20           N  
ANISOU 1502  N   LYS B  66    12776   5767   9269    968   -164    749       N  
ATOM   1503  CA  LYS B  66      25.720  11.993   7.072  1.00 74.00           C  
ANISOU 1503  CA  LYS B  66    13036   5690   9391   1307   -219    752       C  
ATOM   1504  C   LYS B  66      24.494  11.483   6.292  1.00 72.26           C  
ANISOU 1504  C   LYS B  66    13172   5293   8992   1231   -143    832       C  
ATOM   1505  O   LYS B  66      24.493  11.470   5.061  1.00 71.65           O  
ANISOU 1505  O   LYS B  66    13082   5169   8973   1395     62    791       O  
ATOM   1506  CB  LYS B  66      26.448  10.840   7.757  1.00 77.03           C  
ANISOU 1506  CB  LYS B  66    13575   5952   9742   1527   -627    786       C  
ATOM   1507  CG  LYS B  66      26.882   9.743   6.824  1.00 78.60           C  
ANISOU 1507  CG  LYS B  66    13937   5946   9984   1921   -718    750       C  
ATOM   1508  CD  LYS B  66      27.700   8.690   7.545  1.00 81.85           C  
ANISOU 1508  CD  LYS B  66    14483   6217  10400   2193  -1163    764       C  
ATOM   1509  CE  LYS B  66      27.897   7.480   6.652  1.00 84.37           C  
ANISOU 1509  CE  LYS B  66    15064   6261  10731   2572  -1284    725       C  
ATOM   1510  NZ  LYS B  66      28.982   6.559   7.098  1.00 89.35           N  
ANISOU 1510  NZ  LYS B  66    15721   6765  11464   2984  -1698    667       N  
ATOM   1511  N   LEU B  67      23.448  11.076   7.008  1.00 71.24           N  
ANISOU 1511  N   LEU B  67    13351   5094   8622    951   -300    932       N  
ATOM   1512  CA  LEU B  67      22.222  10.631   6.363  1.00 69.71           C  
ANISOU 1512  CA  LEU B  67    13466   4783   8239    826   -232    986       C  
ATOM   1513  C   LEU B  67      21.678  11.689   5.419  1.00 67.55           C  
ANISOU 1513  C   LEU B  67    12988   4624   8053    776    121    926       C  
ATOM   1514  O   LEU B  67      21.296  11.399   4.297  1.00 67.42           O  
ANISOU 1514  O   LEU B  67    13097   4516   8003    883    241    931       O  
ATOM   1515  CB  LEU B  67      21.153  10.312   7.390  1.00 69.41           C  
ANISOU 1515  CB  LEU B  67    13696   4752   7924    437   -397   1059       C  
ATOM   1516  CG  LEU B  67      20.276   9.093   7.096  1.00 70.22           C  
ANISOU 1516  CG  LEU B  67    14273   4647   7760    343   -538   1145       C  
ATOM   1517  CD1 LEU B  67      18.878   9.348   7.601  1.00 68.67           C  
ANISOU 1517  CD1 LEU B  67    14173   4597   7322   -108   -478   1137       C  
ATOM   1518  CD2 LEU B  67      20.240   8.769   5.624  1.00 70.42           C  
ANISOU 1518  CD2 LEU B  67    14359   4545   7853    607   -381   1119       C  
ATOM   1519  N   MET B  68      21.633  12.929   5.868  1.00 66.33           N  
ANISOU 1519  N   MET B  68    12543   4656   8004    612    273    868       N  
ATOM   1520  CA  MET B  68      21.053  13.954   5.040  1.00 64.57           C  
ANISOU 1520  CA  MET B  68    12182   4498   7855    565    557    825       C  
ATOM   1521  C   MET B  68      21.882  14.126   3.786  1.00 65.26           C  
ANISOU 1521  C   MET B  68    12151   4543   8101    839    744    804       C  
ATOM   1522  O   MET B  68      21.345  14.315   2.703  1.00 64.81           O  
ANISOU 1522  O   MET B  68    12168   4441   8016    875    908    819       O  
ATOM   1523  CB  MET B  68      20.937  15.275   5.795  1.00 63.79           C  
ANISOU 1523  CB  MET B  68    11812   4566   7859    359    665    750       C  
ATOM   1524  CG  MET B  68      19.951  15.224   6.934  1.00 63.22           C  
ANISOU 1524  CG  MET B  68    11829   4584   7606     47    539    727       C  
ATOM   1525  SD  MET B  68      18.236  15.365   6.415  1.00 62.92           S  
ANISOU 1525  SD  MET B  68    11925   4572   7410   -116    636    689       S  
ATOM   1526  CE  MET B  68      18.168  17.046   5.887  1.00 59.80           C  
ANISOU 1526  CE  MET B  68    11233   4230   7258    -61    898    595       C  
ATOM   1527  N   LEU B  69      23.199  14.072   3.919  1.00 66.75           N  
ANISOU 1527  N   LEU B  69    12144   4775   8444   1018    719    753       N  
ATOM   1528  CA  LEU B  69      24.042  14.286   2.755  1.00 67.19           C  
ANISOU 1528  CA  LEU B  69    12045   4848   8635   1233    930    692       C  
ATOM   1529  C   LEU B  69      23.784  13.184   1.747  1.00 67.91           C  
ANISOU 1529  C   LEU B  69    12408   4781   8612   1422    904    715       C  
ATOM   1530  O   LEU B  69      23.765  13.417   0.540  1.00 67.84           O  
ANISOU 1530  O   LEU B  69    12398   4768   8609   1490   1124    697       O  
ATOM   1531  CB  LEU B  69      25.512  14.312   3.147  1.00 69.14           C  
ANISOU 1531  CB  LEU B  69    11995   5218   9058   1392    888    587       C  
ATOM   1532  CG  LEU B  69      26.478  14.407   1.977  1.00 69.99           C  
ANISOU 1532  CG  LEU B  69    11911   5396   9284   1597   1112    477       C  
ATOM   1533  CD1 LEU B  69      26.181  15.652   1.150  1.00 67.40           C  
ANISOU 1533  CD1 LEU B  69    11503   5124   8981   1413   1444    491       C  
ATOM   1534  CD2 LEU B  69      27.923  14.374   2.462  1.00 72.08           C  
ANISOU 1534  CD2 LEU B  69    11831   5836   9722   1755   1046    331       C  
ATOM   1535  N   GLU B  70      23.578  11.970   2.245  1.00 68.99           N  
ANISOU 1535  N   GLU B  70    12811   4777   8626   1486    625    758       N  
ATOM   1536  CA  GLU B  70      23.347  10.850   1.349  1.00 69.86           C  
ANISOU 1536  CA  GLU B  70    13213   4706   8623   1661    579    766       C  
ATOM   1537  C   GLU B  70      22.017  11.049   0.648  1.00 67.63           C  
ANISOU 1537  C   GLU B  70    13129   4393   8175   1471    715    833       C  
ATOM   1538  O   GLU B  70      21.942  11.060  -0.578  1.00 67.37           O  
ANISOU 1538  O   GLU B  70    13132   4341   8126   1567    900    809       O  
ATOM   1539  CB  GLU B  70      23.356   9.526   2.093  1.00 71.61           C  
ANISOU 1539  CB  GLU B  70    13744   4734   8731   1737    222    812       C  
ATOM   1540  CG  GLU B  70      22.983   8.366   1.222  1.00 73.66           C  
ANISOU 1540  CG  GLU B  70    14362   4770   8856   1877    165    816       C  
ATOM   1541  CD  GLU B  70      22.557   7.181   2.039  1.00 77.93           C  
ANISOU 1541  CD  GLU B  70    15324   5078   9208   1809   -191    911       C  
ATOM   1542  OE1 GLU B  70      21.920   6.280   1.447  1.00 80.32           O  
ANISOU 1542  OE1 GLU B  70    15992   5184   9342   1805   -241    937       O  
ATOM   1543  OE2 GLU B  70      22.856   7.143   3.271  1.00 80.22           O  
ANISOU 1543  OE2 GLU B  70    15607   5376   9498   1733   -426    963       O  
ATOM   1544  N   ASN B  71      20.961  11.217   1.426  1.00 66.12           N  
ANISOU 1544  N   ASN B  71    13049   4225   7848   1192    622    900       N  
ATOM   1545  CA  ASN B  71      19.670  11.380   0.813  1.00 64.66           C  
ANISOU 1545  CA  ASN B  71    13013   4047   7508   1027    721    934       C  
ATOM   1546  C   ASN B  71      19.690  12.472  -0.245  1.00 63.45           C  
ANISOU 1546  C   ASN B  71    12666   3978   7464   1078   1000    914       C  
ATOM   1547  O   ASN B  71      19.209  12.275  -1.342  1.00 63.43           O  
ANISOU 1547  O   ASN B  71    12805   3929   7365   1123   1095    930       O  
ATOM   1548  CB  ASN B  71      18.583  11.589   1.862  1.00 63.63           C  
ANISOU 1548  CB  ASN B  71    12932   4005   7239    705    613    953       C  
ATOM   1549  CG  ASN B  71      18.093  10.267   2.444  1.00 67.05           C  
ANISOU 1549  CG  ASN B  71    13728   4315   7434    572    360   1002       C  
ATOM   1550  OD1 ASN B  71      18.390   9.189   1.920  1.00 70.53           O  
ANISOU 1550  OD1 ASN B  71    14426   4563   7808    737    262   1030       O  
ATOM   1551  ND2 ASN B  71      17.341  10.339   3.524  1.00 69.49           N  
ANISOU 1551  ND2 ASN B  71    14077   4727   7598    256    254   1002       N  
ATOM   1552  N   VAL B  72      20.270  13.617   0.077  1.00 62.81           N  
ANISOU 1552  N   VAL B  72    12289   4010   7566   1054   1120    883       N  
ATOM   1553  CA  VAL B  72      20.270  14.729  -0.839  1.00 61.90           C  
ANISOU 1553  CA  VAL B  72    12045   3940   7534   1056   1361    885       C  
ATOM   1554  C   VAL B  72      21.083  14.413  -2.079  1.00 63.38           C  
ANISOU 1554  C   VAL B  72    12248   4095   7740   1252   1515    865       C  
ATOM   1555  O   VAL B  72      20.682  14.718  -3.201  1.00 63.13           O  
ANISOU 1555  O   VAL B  72    12309   4042   7634   1251   1662    902       O  
ATOM   1556  CB  VAL B  72      20.848  15.960  -0.194  1.00 61.76           C  
ANISOU 1556  CB  VAL B  72    11741   4022   7704    969   1452    848       C  
ATOM   1557  CG1 VAL B  72      21.311  16.933  -1.265  1.00 62.24           C  
ANISOU 1557  CG1 VAL B  72    11707   4090   7853    997   1704    856       C  
ATOM   1558  CG2 VAL B  72      19.822  16.571   0.716  1.00 59.83           C  
ANISOU 1558  CG2 VAL B  72    11474   3824   7434    762   1373    839       C  
ATOM   1559  N   SER B  73      22.243  13.811  -1.886  1.00 64.96           N  
ANISOU 1559  N   SER B  73    12346   4306   8030   1421   1476    789       N  
ATOM   1560  CA  SER B  73      23.050  13.461  -3.031  1.00 66.86           C  
ANISOU 1560  CA  SER B  73    12563   4556   8286   1608   1635    714       C  
ATOM   1561  C   SER B  73      22.325  12.448  -3.926  1.00 66.87           C  
ANISOU 1561  C   SER B  73    12889   4425   8093   1682   1598    738       C  
ATOM   1562  O   SER B  73      22.274  12.596  -5.142  1.00 67.39           O  
ANISOU 1562  O   SER B  73    13014   4505   8085   1700   1789    732       O  
ATOM   1563  CB  SER B  73      24.404  12.945  -2.570  1.00 69.25           C  
ANISOU 1563  CB  SER B  73    12656   4918   8738   1814   1564    581       C  
ATOM   1564  OG  SER B  73      25.321  14.030  -2.519  1.00 70.96           O  
ANISOU 1564  OG  SER B  73    12530   5317   9115   1751   1757    512       O  
ATOM   1565  N   ARG B  74      21.754  11.425  -3.307  1.00 66.63           N  
ANISOU 1565  N   ARG B  74    13093   4267   7958   1689   1349    768       N  
ATOM   1566  CA  ARG B  74      20.944  10.451  -3.998  1.00 66.51           C  
ANISOU 1566  CA  ARG B  74    13416   4117   7739   1703   1288    792       C  
ATOM   1567  C   ARG B  74      19.861  11.151  -4.818  1.00 64.65           C  
ANISOU 1567  C   ARG B  74    13253   3937   7375   1531   1433    868       C  
ATOM   1568  O   ARG B  74      19.756  10.972  -6.022  1.00 65.27           O  
ANISOU 1568  O   ARG B  74    13444   4001   7353   1586   1566    855       O  
ATOM   1569  CB  ARG B  74      20.307   9.555  -2.966  1.00 66.62           C  
ANISOU 1569  CB  ARG B  74    13672   4005   7637   1608    998    843       C  
ATOM   1570  CG  ARG B  74      20.250   8.147  -3.387  1.00 69.99           C  
ANISOU 1570  CG  ARG B  74    14434   4229   7931   1739    864    810       C  
ATOM   1571  CD  ARG B  74      20.208   7.201  -2.208  1.00 72.97           C  
ANISOU 1571  CD  ARG B  74    15039   4441   8245   1706    542    850       C  
ATOM   1572  NE  ARG B  74      20.800   5.939  -2.627  1.00 76.89           N  
ANISOU 1572  NE  ARG B  74    15779   4706   8731   1977    412    773       N  
ATOM   1573  CZ  ARG B  74      21.830   5.396  -2.013  1.00 79.71           C  
ANISOU 1573  CZ  ARG B  74    16114   4948   9225   2225    211    719       C  
ATOM   1574  NH1 ARG B  74      22.329   6.006  -0.936  1.00 80.86           N  
ANISOU 1574  NH1 ARG B  74    16010   5213   9501   2189    123    752       N  
ATOM   1575  NH2 ARG B  74      22.330   4.252  -2.447  1.00 82.85           N  
ANISOU 1575  NH2 ARG B  74    16742   5111   9626   2511     79    622       N  
ATOM   1576  N   VAL B  75      19.054  11.965  -4.163  1.00 62.50           N  
ANISOU 1576  N   VAL B  75    12908   3735   7102   1332   1394    934       N  
ATOM   1577  CA  VAL B  75      18.009  12.686  -4.844  1.00 61.03           C  
ANISOU 1577  CA  VAL B  75    12768   3602   6820   1210   1480    992       C  
ATOM   1578  C   VAL B  75      18.547  13.460  -6.047  1.00 62.11           C  
ANISOU 1578  C   VAL B  75    12830   3768   6999   1282   1716   1009       C  
ATOM   1579  O   VAL B  75      17.935  13.493  -7.108  1.00 62.31           O  
ANISOU 1579  O   VAL B  75    13011   3787   6878   1266   1780   1053       O  
ATOM   1580  CB  VAL B  75      17.310  13.620  -3.877  1.00 59.33           C  
ANISOU 1580  CB  VAL B  75    12405   3473   6665   1038   1417   1008       C  
ATOM   1581  CG1 VAL B  75      16.445  14.595  -4.616  1.00 58.27           C  
ANISOU 1581  CG1 VAL B  75    12263   3382   6496    985   1499   1050       C  
ATOM   1582  CG2 VAL B  75      16.489  12.804  -2.915  1.00 58.67           C  
ANISOU 1582  CG2 VAL B  75    12451   3395   6446    889   1208    988       C  
ATOM   1583  N   ARG B  76      19.701  14.085  -5.896  1.00 63.13           N  
ANISOU 1583  N   ARG B  76    12732   3948   7307   1333   1846    973       N  
ATOM   1584  CA  ARG B  76      20.230  14.885  -6.990  1.00 64.20           C  
ANISOU 1584  CA  ARG B  76    12816   4126   7452   1328   2085    991       C  
ATOM   1585  C   ARG B  76      20.617  14.001  -8.169  1.00 65.45           C  
ANISOU 1585  C   ARG B  76    13115   4277   7476   1445   2193    932       C  
ATOM   1586  O   ARG B  76      20.309  14.317  -9.308  1.00 65.90           O  
ANISOU 1586  O   ARG B  76    13305   4342   7392   1390   2322    987       O  
ATOM   1587  CB  ARG B  76      21.422  15.713  -6.540  1.00 65.40           C  
ANISOU 1587  CB  ARG B  76    12680   4363   7805   1306   2216    939       C  
ATOM   1588  CG  ARG B  76      22.060  16.422  -7.690  1.00 67.92           C  
ANISOU 1588  CG  ARG B  76    12974   4738   8093   1248   2480    946       C  
ATOM   1589  CD  ARG B  76      23.498  16.735  -7.429  1.00 72.25           C  
ANISOU 1589  CD  ARG B  76    13228   5422   8801   1250   2635    822       C  
ATOM   1590  NE  ARG B  76      24.146  17.127  -8.667  1.00 76.67           N  
ANISOU 1590  NE  ARG B  76    13792   6069   9268   1168   2911    795       N  
ATOM   1591  CZ  ARG B  76      25.269  17.825  -8.735  1.00 79.26           C  
ANISOU 1591  CZ  ARG B  76    13886   6545   9685   1053   3122    709       C  
ATOM   1592  NH1 ARG B  76      25.868  18.220  -7.624  1.00 79.65           N  
ANISOU 1592  NH1 ARG B  76    13667   6663   9932   1030   3074    644       N  
ATOM   1593  NH2 ARG B  76      25.783  18.130  -9.913  1.00 81.99           N  
ANISOU 1593  NH2 ARG B  76    14269   6988   9896    927   3385    681       N  
ATOM   1594  N   ALA B  77      21.291  12.886  -7.902  1.00 66.10           N  
ANISOU 1594  N   ALA B  77    13184   4337   7595   1613   2127    810       N  
ATOM   1595  CA  ALA B  77      21.614  11.957  -8.976  1.00 67.53           C  
ANISOU 1595  CA  ALA B  77    13505   4498   7654   1748   2217    710       C  
ATOM   1596  C   ALA B  77      20.322  11.497  -9.657  1.00 66.84           C  
ANISOU 1596  C   ALA B  77    13743   4326   7327   1669   2145    796       C  
ATOM   1597  O   ALA B  77      20.189  11.563 -10.882  1.00 67.85           O  
ANISOU 1597  O   ALA B  77    13991   4490   7300   1637   2300    800       O  
ATOM   1598  CB  ALA B  77      22.383  10.780  -8.453  1.00 68.66           C  
ANISOU 1598  CB  ALA B  77    13621   4577   7889   1979   2085    559       C  
ATOM   1599  N   MET B  78      19.357  11.048  -8.860  1.00 65.13           N  
ANISOU 1599  N   MET B  78    13664   4023   7058   1605   1912    856       N  
ATOM   1600  CA  MET B  78      18.092  10.595  -9.419  1.00 64.22           C  
ANISOU 1600  CA  MET B  78    13825   3867   6710   1503   1832    912       C  
ATOM   1601  C   MET B  78      17.454  11.644 -10.336  1.00 64.07           C  
ANISOU 1601  C   MET B  78    13814   3937   6592   1386   1951   1016       C  
ATOM   1602  O   MET B  78      17.057  11.321 -11.454  1.00 65.18           O  
ANISOU 1602  O   MET B  78    14146   4083   6535   1370   2010   1022       O  
ATOM   1603  CB  MET B  78      17.127  10.143  -8.317  1.00 62.48           C  
ANISOU 1603  CB  MET B  78    13703   3598   6440   1380   1586    948       C  
ATOM   1604  CG  MET B  78      17.441   8.766  -7.771  1.00 62.98           C  
ANISOU 1604  CG  MET B  78    13949   3505   6476   1464   1420    875       C  
ATOM   1605  SD  MET B  78      16.191   8.125  -6.644  1.00 62.89           S  
ANISOU 1605  SD  MET B  78    14143   3445   6306   1218   1151    923       S  
ATOM   1606  CE  MET B  78      16.393   9.157  -5.205  1.00 61.16           C  
ANISOU 1606  CE  MET B  78    13614   3338   6284   1128   1097    962       C  
ATOM   1607  N   CYS B  79      17.379  12.893  -9.882  1.00 63.02           N  
ANISOU 1607  N   CYS B  79    13497   3857   6589   1310   1971   1094       N  
ATOM   1608  CA  CYS B  79      16.728  13.931 -10.665  1.00 63.29           C  
ANISOU 1608  CA  CYS B  79    13579   3926   6541   1223   2023   1207       C  
ATOM   1609  C   CYS B  79      17.453  14.227 -11.950  1.00 65.38           C  
ANISOU 1609  C   CYS B  79    13909   4215   6720   1228   2248   1228       C  
ATOM   1610  O   CYS B  79      16.829  14.505 -12.960  1.00 66.33           O  
ANISOU 1610  O   CYS B  79    14205   4342   6654   1170   2263   1315       O  
ATOM   1611  CB  CYS B  79      16.593  15.213  -9.869  1.00 62.13           C  
ANISOU 1611  CB  CYS B  79    13244   3788   6575   1161   1988   1265       C  
ATOM   1612  SG  CYS B  79      15.435  15.025  -8.556  1.00 60.97           S  
ANISOU 1612  SG  CYS B  79    13034   3673   6460   1096   1742   1225       S  
ATOM   1613  N   THR B  80      18.772  14.207 -11.904  1.00 66.45           N  
ANISOU 1613  N   THR B  80    13888   4384   6975   1282   2419   1139       N  
ATOM   1614  CA  THR B  80      19.535  14.423 -13.101  1.00 68.72           C  
ANISOU 1614  CA  THR B  80    14214   4739   7156   1244   2666   1117       C  
ATOM   1615  C   THR B  80      19.068  13.422 -14.162  1.00 69.97           C  
ANISOU 1615  C   THR B  80    14627   4898   7062   1275   2673   1076       C  
ATOM   1616  O   THR B  80      18.843  13.788 -15.321  1.00 71.37           O  
ANISOU 1616  O   THR B  80    14972   5113   7033   1168   2781   1152       O  
ATOM   1617  CB  THR B  80      21.023  14.242 -12.832  1.00 70.21           C  
ANISOU 1617  CB  THR B  80    14151   5019   7508   1321   2838    949       C  
ATOM   1618  OG1 THR B  80      21.456  15.267 -11.942  1.00 69.57           O  
ANISOU 1618  OG1 THR B  80    13842   4956   7635   1250   2847    989       O  
ATOM   1619  CG2 THR B  80      21.814  14.349 -14.112  1.00 72.76           C  
ANISOU 1619  CG2 THR B  80    14496   5465   7685   1250   3125    875       C  
ATOM   1620  N   GLU B  81      18.915  12.160 -13.763  1.00 69.70           N  
ANISOU 1620  N   GLU B  81    14653   4805   7025   1401   2546    962       N  
ATOM   1621  CA  GLU B  81      18.494  11.120 -14.692  1.00 70.78           C  
ANISOU 1621  CA  GLU B  81    15044   4920   6928   1425   2547    895       C  
ATOM   1622  C   GLU B  81      17.061  11.363 -15.136  1.00 69.60           C  
ANISOU 1622  C   GLU B  81    15106   4769   6572   1290   2408   1044       C  
ATOM   1623  O   GLU B  81      16.766  11.318 -16.322  1.00 70.96           O  
ANISOU 1623  O   GLU B  81    15462   4990   6511   1221   2490   1070       O  
ATOM   1624  CB  GLU B  81      18.614   9.724 -14.069  1.00 70.97           C  
ANISOU 1624  CB  GLU B  81    15135   4828   7001   1580   2404    747       C  
ATOM   1625  CG  GLU B  81      20.031   9.262 -13.854  1.00 73.05           C  
ANISOU 1625  CG  GLU B  81    15216   5097   7444   1780   2512    552       C  
ATOM   1626  CD  GLU B  81      20.843   9.351 -15.108  1.00 77.68           C  
ANISOU 1626  CD  GLU B  81    15763   5818   7934   1791   2803    423       C  
ATOM   1627  OE1 GLU B  81      20.469   8.710 -16.116  1.00 78.89           O  
ANISOU 1627  OE1 GLU B  81    16152   5962   7862   1771   2858    364       O  
ATOM   1628  OE2 GLU B  81      21.857  10.078 -15.095  1.00 81.00           O  
ANISOU 1628  OE2 GLU B  81    15914   6377   8486   1787   2989    367       O  
ATOM   1629  N   ILE B  82      16.172  11.621 -14.184  1.00 67.23           N  
ANISOU 1629  N   ILE B  82    14761   4438   6346   1249   2196   1123       N  
ATOM   1630  CA  ILE B  82      14.771  11.840 -14.513  1.00 66.28           C  
ANISOU 1630  CA  ILE B  82    14778   4355   6050   1145   2040   1221       C  
ATOM   1631  C   ILE B  82      14.648  12.971 -15.511  1.00 67.32           C  
ANISOU 1631  C   ILE B  82    14960   4534   6085   1084   2122   1360       C  
ATOM   1632  O   ILE B  82      13.913  12.883 -16.490  1.00 68.14           O  
ANISOU 1632  O   ILE B  82    15259   4684   5949   1025   2078   1413       O  
ATOM   1633  CB  ILE B  82      13.961  12.182 -13.274  1.00 64.31           C  
ANISOU 1633  CB  ILE B  82    14393   4115   5928   1104   1836   1247       C  
ATOM   1634  CG1 ILE B  82      13.930  10.981 -12.321  1.00 63.65           C  
ANISOU 1634  CG1 ILE B  82    14341   3975   5868   1103   1722   1136       C  
ATOM   1635  CG2 ILE B  82      12.570  12.592 -13.658  1.00 63.86           C  
ANISOU 1635  CG2 ILE B  82    14404   4143   5716   1024   1682   1314       C  
ATOM   1636  CD1 ILE B  82      13.452  11.316 -10.921  1.00 61.42           C  
ANISOU 1636  CD1 ILE B  82    13890   3721   5727   1034   1568   1135       C  
ATOM   1637  N   LEU B  83      15.386  14.040 -15.244  1.00 67.51           N  
ANISOU 1637  N   LEU B  83    14828   4538   6285   1081   2226   1423       N  
ATOM   1638  CA  LEU B  83      15.411  15.202 -16.104  1.00 68.61           C  
ANISOU 1638  CA  LEU B  83    15057   4673   6340    998   2299   1576       C  
ATOM   1639  C   LEU B  83      15.792  14.799 -17.520  1.00 70.93           C  
ANISOU 1639  C   LEU B  83    15561   5025   6364    927   2477   1569       C  
ATOM   1640  O   LEU B  83      15.133  15.192 -18.488  1.00 72.37           O  
ANISOU 1640  O   LEU B  83    15958   5219   6318    848   2419   1699       O  
ATOM   1641  CB  LEU B  83      16.409  16.223 -15.575  1.00 68.70           C  
ANISOU 1641  CB  LEU B  83    14883   4644   6574    967   2433   1606       C  
ATOM   1642  CG  LEU B  83      16.471  17.494 -16.422  1.00 70.60           C  
ANISOU 1642  CG  LEU B  83    15276   4832   6716    839   2497   1785       C  
ATOM   1643  CD1 LEU B  83      15.255  18.364 -16.196  1.00 69.33           C  
ANISOU 1643  CD1 LEU B  83    15185   4573   6584    876   2229   1923       C  
ATOM   1644  CD2 LEU B  83      17.737  18.260 -16.113  1.00 71.17           C  
ANISOU 1644  CD2 LEU B  83    15195   4895   6951    746   2712   1773       C  
ATOM   1645  N   LYS B  84      16.862  14.028 -17.654  1.00 71.55           N  
ANISOU 1645  N   LYS B  84    15574   5152   6460    961   2684   1404       N  
ATOM   1646  CA  LYS B  84      17.269  13.603 -18.984  1.00 73.98           C  
ANISOU 1646  CA  LYS B  84    16057   5547   6506    884   2883   1347       C  
ATOM   1647  C   LYS B  84      16.157  12.827 -19.687  1.00 74.18           C  
ANISOU 1647  C   LYS B  84    16337   5583   6264    870   2738   1357       C  
ATOM   1648  O   LYS B  84      15.916  13.030 -20.879  1.00 76.55           O  
ANISOU 1648  O   LYS B  84    16855   5946   6285    744   2798   1435       O  
ATOM   1649  CB  LYS B  84      18.558  12.793 -18.946  1.00 75.09           C  
ANISOU 1649  CB  LYS B  84    16043   5754   6735    973   3110   1101       C  
ATOM   1650  CG  LYS B  84      19.774  13.602 -18.566  1.00 75.74           C  
ANISOU 1650  CG  LYS B  84    15868   5899   7012    934   3306   1066       C  
ATOM   1651  CD  LYS B  84      21.002  12.749 -18.741  1.00 78.80           C  
ANISOU 1651  CD  LYS B  84    16086   6403   7451   1041   3528    779       C  
ATOM   1652  CE  LYS B  84      22.097  13.134 -17.779  1.00 79.82           C  
ANISOU 1652  CE  LYS B  84    15863   6586   7879   1108   3608    677       C  
ATOM   1653  NZ  LYS B  84      22.818  11.900 -17.340  1.00 80.77           N  
ANISOU 1653  NZ  LYS B  84    15815   6722   8153   1374   3601    396       N  
ATOM   1654  N   MET B  85      15.466  11.957 -18.956  1.00 72.27           N  
ANISOU 1654  N   MET B  85    16085   5291   6084    964   2544   1281       N  
ATOM   1655  CA  MET B  85      14.391  11.180 -19.555  1.00 72.30           C  
ANISOU 1655  CA  MET B  85    16316   5323   5831    917   2406   1268       C  
ATOM   1656  C   MET B  85      13.169  12.033 -19.888  1.00 72.18           C  
ANISOU 1656  C   MET B  85    16388   5353   5683    836   2202   1459       C  
ATOM   1657  O   MET B  85      12.550  11.832 -20.923  1.00 73.80           O  
ANISOU 1657  O   MET B  85    16806   5631   5601    752   2161   1496       O  
ATOM   1658  CB  MET B  85      14.022   9.966 -18.704  1.00 70.65           C  
ANISOU 1658  CB  MET B  85    16110   5044   5690    987   2266   1126       C  
ATOM   1659  CG  MET B  85      15.064   8.894 -18.725  1.00 71.44           C  
ANISOU 1659  CG  MET B  85    16230   5075   5841   1098   2419    919       C  
ATOM   1660  SD  MET B  85      14.681   7.485 -17.660  1.00 73.06           S  
ANISOU 1660  SD  MET B  85    16523   5119   6117   1165   2211    787       S  
ATOM   1661  CE  MET B  85      15.099   8.153 -16.046  1.00 68.30           C  
ANISOU 1661  CE  MET B  85    15619   4466   5866   1243   2117    851       C  
ATOM   1662  N   SER B  86      12.825  12.992 -19.039  1.00 70.77           N  
ANISOU 1662  N   SER B  86    16044   5136   5710    874   2062   1564       N  
ATOM   1663  CA  SER B  86      11.724  13.905 -19.366  1.00 71.58           C  
ANISOU 1663  CA  SER B  86    16210   5269   5721    853   1845   1723       C  
ATOM   1664  C   SER B  86      11.996  14.631 -20.675  1.00 74.46           C  
ANISOU 1664  C   SER B  86    16796   5632   5865    765   1933   1882       C  
ATOM   1665  O   SER B  86      11.117  14.794 -21.518  1.00 75.99           O  
ANISOU 1665  O   SER B  86    17175   5881   5817    726   1773   1979       O  
ATOM   1666  CB  SER B  86      11.527  14.949 -18.272  1.00 70.08           C  
ANISOU 1666  CB  SER B  86    15799   5011   5816    930   1717   1782       C  
ATOM   1667  OG  SER B  86      11.217  14.367 -17.026  1.00 67.98           O  
ANISOU 1667  OG  SER B  86    15338   4768   5724    970   1627   1645       O  
ATOM   1668  N   VAL B  87      13.227  15.084 -20.833  1.00 75.69           N  
ANISOU 1668  N   VAL B  87    16933   5738   6087    711   2181   1905       N  
ATOM   1669  CA  VAL B  87      13.620  15.737 -22.063  1.00 78.92           C  
ANISOU 1669  CA  VAL B  87    17580   6154   6252    558   2306   2050       C  
ATOM   1670  C   VAL B  87      13.386  14.826 -23.265  1.00 80.97           C  
ANISOU 1670  C   VAL B  87    18073   6538   6152    464   2368   1991       C  
ATOM   1671  O   VAL B  87      13.072  15.291 -24.357  1.00 83.64           O  
ANISOU 1671  O   VAL B  87    18674   6905   6199    336   2327   2147       O  
ATOM   1672  CB  VAL B  87      15.090  16.173 -22.012  1.00 79.90           C  
ANISOU 1672  CB  VAL B  87    17610   6264   6483    462   2620   2018       C  
ATOM   1673  CG1 VAL B  87      15.674  16.260 -23.412  1.00 83.62           C  
ANISOU 1673  CG1 VAL B  87    18329   6827   6616    242   2849   2060       C  
ATOM   1674  CG2 VAL B  87      15.215  17.513 -21.308  1.00 79.20           C  
ANISOU 1674  CG2 VAL B  87    17433   6031   6626    464   2544   2168       C  
ATOM   1675  N   LEU B  88      13.538  13.526 -23.069  1.00 80.24           N  
ANISOU 1675  N   LEU B  88    17913   6506   6068    520   2452   1767       N  
ATOM   1676  CA  LEU B  88      13.350  12.586 -24.169  1.00 82.30           C  
ANISOU 1676  CA  LEU B  88    18396   6875   5997    429   2525   1671       C  
ATOM   1677  C   LEU B  88      11.887  12.300 -24.480  1.00 82.27           C  
ANISOU 1677  C   LEU B  88    18538   6928   5795    419   2229   1732       C  
ATOM   1678  O   LEU B  88      11.565  11.717 -25.509  1.00 84.10           O  
ANISOU 1678  O   LEU B  88    18989   7260   5705    311   2248   1693       O  
ATOM   1679  CB  LEU B  88      14.076  11.273 -23.890  1.00 82.00           C  
ANISOU 1679  CB  LEU B  88    18272   6843   6042    507   2710   1389       C  
ATOM   1680  CG  LEU B  88      15.586  11.277 -24.114  1.00 83.59           C  
ANISOU 1680  CG  LEU B  88    18366   7084   6309    492   3055   1248       C  
ATOM   1681  CD1 LEU B  88      16.094   9.852 -24.099  1.00 84.00           C  
ANISOU 1681  CD1 LEU B  88    18397   7137   6381    607   3180    944       C  
ATOM   1682  CD2 LEU B  88      15.939  11.965 -25.426  1.00 86.56           C  
ANISOU 1682  CD2 LEU B  88    18935   7580   6373    262   3242   1350       C  
ATOM   1683  N   ASN B  89      10.994  12.693 -23.588  1.00 80.56           N  
ANISOU 1683  N   ASN B  89    18176   6673   5759    522   1959   1797       N  
ATOM   1684  CA  ASN B  89       9.583  12.442 -23.818  1.00 81.03           C  
ANISOU 1684  CA  ASN B  89    18307   6837   5643    512   1672   1814       C  
ATOM   1685  C   ASN B  89       9.075  13.209 -25.019  1.00 84.18           C  
ANISOU 1685  C   ASN B  89    18940   7294   5749    436   1542   2013       C  
ATOM   1686  O   ASN B  89       9.321  14.409 -25.147  1.00 85.27           O  
ANISOU 1686  O   ASN B  89    19120   7337   5943    454   1505   2208       O  
ATOM   1687  CB  ASN B  89       8.764  12.828 -22.598  1.00 78.67           C  
ANISOU 1687  CB  ASN B  89    17758   6527   5605    632   1426   1810       C  
ATOM   1688  CG  ASN B  89       7.439  12.137 -22.570  1.00 78.57           C  
ANISOU 1688  CG  ASN B  89    17736   6674   5442    596   1192   1710       C  
ATOM   1689  OD1 ASN B  89       7.359  10.935 -22.805  1.00 79.54           O  
ANISOU 1689  OD1 ASN B  89    17966   6852   5402    495   1263   1562       O  
ATOM   1690  ND2 ASN B  89       6.384  12.881 -22.281  1.00 78.12           N  
ANISOU 1690  ND2 ASN B  89    17547   6698   5438    674    909   1766       N  
ATOM   1691  N   GLN B  90       8.347  12.526 -25.890  1.00 86.18           N  
ANISOU 1691  N   GLN B  90    19375   7692   5679    341   1451   1971       N  
ATOM   1692  CA  GLN B  90       7.901  13.153 -27.124  1.00 89.89           C  
ANISOU 1692  CA  GLN B  90    20107   8228   5819    253   1315   2163       C  
ATOM   1693  C   GLN B  90       7.269  14.537 -26.901  1.00 90.03           C  
ANISOU 1693  C   GLN B  90    20088   8166   5955    388   1005   2387       C  
ATOM   1694  O   GLN B  90       7.620  15.502 -27.602  1.00 92.20           O  
ANISOU 1694  O   GLN B  90    20585   8344   6104    332    993   2611       O  
ATOM   1695  CB  GLN B  90       6.941  12.236 -27.879  1.00 91.69           C  
ANISOU 1695  CB  GLN B  90    20474   8651   5712    153   1179   2068       C  
ATOM   1696  CG  GLN B  90       6.601  12.740 -29.289  1.00 97.87           C  
ANISOU 1696  CG  GLN B  90    21574   9522   6091     29   1057   2260       C  
ATOM   1697  CD  GLN B  90       5.251  12.233 -29.748  1.00102.44           C  
ANISOU 1697  CD  GLN B  90    22194  10314   6415      0    758   2206       C  
ATOM   1698  OE1 GLN B  90       5.001  12.087 -30.951  1.00106.12           O  
ANISOU 1698  OE1 GLN B  90    22933  10904   6485   -153    713   2269       O  
ATOM   1699  NE2 GLN B  90       4.368  11.941 -28.777  1.00101.02           N  
ANISOU 1699  NE2 GLN B  90    21733  10207   6444    118    559   2071       N  
ATOM   1700  N   GLU B  91       6.353  14.620 -25.928  1.00 87.62           N  
ANISOU 1700  N   GLU B  91    19517   7896   5879    552    755   2310       N  
ATOM   1701  CA  GLU B  91       5.649  15.862 -25.631  1.00 87.92           C  
ANISOU 1701  CA  GLU B  91    19476   7863   6064    735    431   2457       C  
ATOM   1702  C   GLU B  91       6.612  17.008 -25.325  1.00 87.82           C  
ANISOU 1702  C   GLU B  91    19503   7595   6270    776    545   2626       C  
ATOM   1703  O   GLU B  91       6.354  18.166 -25.690  1.00 90.14           O  
ANISOU 1703  O   GLU B  91    19952   7753   6544    856    323   2838       O  
ATOM   1704  CB  GLU B  91       4.659  15.687 -24.487  1.00 85.83           C  
ANISOU 1704  CB  GLU B  91    18855   7715   6043    884    219   2272       C  
ATOM   1705  CG  GLU B  91       3.420  14.915 -24.832  1.00 86.83           C  
ANISOU 1705  CG  GLU B  91    18934   8117   5939    845      1   2134       C  
ATOM   1706  CD  GLU B  91       3.642  13.423 -24.756  1.00 86.73           C  
ANISOU 1706  CD  GLU B  91    18936   8212   5804    648    237   1932       C  
ATOM   1707  OE1 GLU B  91       2.763  12.701 -24.223  1.00 85.64           O  
ANISOU 1707  OE1 GLU B  91    18613   8266   5659    601    126   1733       O  
ATOM   1708  OE2 GLU B  91       4.712  12.970 -25.221  1.00 88.10           O  
ANISOU 1708  OE2 GLU B  91    19312   8276   5886    530    536   1957       O  
ATOM   1709  N   SER B  92       7.719  16.682 -24.661  1.00 85.24           N  
ANISOU 1709  N   SER B  92    19050   7194   6145    719    874   2527       N  
ATOM   1710  CA  SER B  92       8.765  17.669 -24.381  1.00 84.91           C  
ANISOU 1710  CA  SER B  92    19031   6942   6290    701   1036   2656       C  
ATOM   1711  C   SER B  92       9.444  18.151 -25.677  1.00 88.11           C  
ANISOU 1711  C   SER B  92    19811   7286   6379    495   1173   2860       C  
ATOM   1712  O   SER B  92       9.470  19.356 -25.975  1.00 90.28           O  
ANISOU 1712  O   SER B  92    20285   7383   6634    486   1040   3091       O  
ATOM   1713  CB  SER B  92       9.799  17.094 -23.410  1.00 81.95           C  
ANISOU 1713  CB  SER B  92    18407   6553   6179    683   1347   2473       C  
ATOM   1714  OG  SER B  92       9.170  16.406 -22.342  1.00 78.76           O  
ANISOU 1714  OG  SER B  92    17722   6231   5971    803   1239   2281       O  
ATOM   1715  N   ILE B  93       9.985  17.204 -26.440  1.00 88.44           N  
ANISOU 1715  N   ILE B  93    19971   7472   6162    314   1435   2763       N  
ATOM   1716  CA  ILE B  93      10.544  17.516 -27.741  1.00 91.81           C  
ANISOU 1716  CA  ILE B  93    20755   7909   6222     68   1583   2918       C  
ATOM   1717  C   ILE B  93       9.616  18.461 -28.502  1.00 94.70           C  
ANISOU 1717  C   ILE B  93    21429   8192   6360     80   1206   3200       C  
ATOM   1718  O   ILE B  93      10.045  19.487 -29.048  1.00 97.40           O  
ANISOU 1718  O   ILE B  93    22061   8379   6570    -62   1205   3441       O  
ATOM   1719  CB  ILE B  93      10.715  16.264 -28.612  1.00 92.75           C  
ANISOU 1719  CB  ILE B  93    20976   8242   6022    -87   1791   2747       C  
ATOM   1720  CG1 ILE B  93      11.217  15.073 -27.800  1.00 89.47           C  
ANISOU 1720  CG1 ILE B  93    20259   7895   5839     -2   2023   2434       C  
ATOM   1721  CG2 ILE B  93      11.676  16.565 -29.749  1.00 95.94           C  
ANISOU 1721  CG2 ILE B  93    21674   8684   6095   -389   2075   2839       C  
ATOM   1722  CD1 ILE B  93      12.656  14.721 -28.072  1.00 89.58           C  
ANISOU 1722  CD1 ILE B  93    20252   7958   5828   -150   2458   2286       C  
ATOM   1723  N   ALA B  94       8.338  18.100 -28.541  1.00 94.23           N  
ANISOU 1723  N   ALA B  94    21319   8241   6242    241    872   3163       N  
ATOM   1724  CA  ALA B  94       7.340  18.867 -29.267  1.00 97.18           C  
ANISOU 1724  CA  ALA B  94    21952   8572   6401    310    454   3394       C  
ATOM   1725  C   ALA B  94       7.317  20.338 -28.848  1.00 98.41           C  
ANISOU 1725  C   ALA B  94    22183   8430   6780    454    227   3615       C  
ATOM   1726  O   ALA B  94       7.372  21.225 -29.683  1.00102.13           O  
ANISOU 1726  O   ALA B  94    23049   8740   7018    357     80   3894       O  
ATOM   1727  CB  ALA B  94       5.969  18.238 -29.089  1.00 96.13           C  
ANISOU 1727  CB  ALA B  94    21622   8642   6263    497    133   3247       C  
ATOM   1728  N   SER B  95       7.245  20.593 -27.550  1.00 95.71           N  
ANISOU 1728  N   SER B  95    21489   8000   6876    669    194   3489       N  
ATOM   1729  CA  SER B  95       7.127  21.956 -27.058  1.00 96.94           C  
ANISOU 1729  CA  SER B  95    21692   7862   7277    840    -42   3651       C  
ATOM   1730  C   SER B  95       8.260  22.867 -27.529  1.00 99.51           C  
ANISOU 1730  C   SER B  95    22376   7932   7501    595    155   3895       C  
ATOM   1731  O   SER B  95       8.100  24.078 -27.574  1.00102.14           O  
ANISOU 1731  O   SER B  95    22945   7975   7891    675    -99   4113       O  
ATOM   1732  CB  SER B  95       7.091  21.955 -25.532  1.00 93.12           C  
ANISOU 1732  CB  SER B  95    20751   7362   7269   1044     -4   3429       C  
ATOM   1733  OG  SER B  95       8.389  21.724 -25.011  1.00 90.74           O  
ANISOU 1733  OG  SER B  95    20339   7025   7112    866    426   3351       O  
ATOM   1734  N   GLY B  96       9.408  22.286 -27.851  1.00 99.39           N  
ANISOU 1734  N   GLY B  96    22396   8026   7340    292    607   3836       N  
ATOM   1735  CA  GLY B  96      10.594  23.062 -28.180  1.00101.92           C  
ANISOU 1735  CA  GLY B  96    22982   8172   7573      0    870   4004       C  
ATOM   1736  C   GLY B  96      11.147  23.881 -27.026  1.00100.83           C  
ANISOU 1736  C   GLY B  96    22651   7809   7852     77    938   3984       C  
ATOM   1737  O   GLY B  96      11.992  24.740 -27.236  1.00103.35           O  
ANISOU 1737  O   GLY B  96    23214   7939   8113   -163   1087   4148       O  
ATOM   1738  N   ASN B  97      10.693  23.619 -25.804  1.00 97.40           N  
ANISOU 1738  N   ASN B  97    21788   7406   7813    370    844   3776       N  
ATOM   1739  CA  ASN B  97      11.084  24.437 -24.665  1.00 96.26           C  
ANISOU 1739  CA  ASN B  97    21458   7053   8065    462    864   3746       C  
ATOM   1740  C   ASN B  97      12.015  23.755 -23.694  1.00 92.70           C  
ANISOU 1740  C   ASN B  97    20599   6753   7870    410   1239   3491       C  
ATOM   1741  O   ASN B  97      12.408  24.337 -22.685  1.00 91.29           O  
ANISOU 1741  O   ASN B  97    20230   6441   8016    464   1284   3438       O  
ATOM   1742  CB  ASN B  97       9.842  24.899 -23.925  1.00 95.68           C  
ANISOU 1742  CB  ASN B  97    21219   6874   8263    840    432   3705       C  
ATOM   1743  CG  ASN B  97       9.027  25.871 -24.743  1.00101.28           C  
ANISOU 1743  CG  ASN B  97    22340   7348   8793    948      5   3970       C  
ATOM   1744  OD1 ASN B  97       7.947  26.278 -24.345  1.00104.00           O  
ANISOU 1744  OD1 ASN B  97    22576   7622   9317   1280   -388   3929       O  
ATOM   1745  ND2 ASN B  97       9.550  26.259 -25.891  1.00105.63           N  
ANISOU 1745  ND2 ASN B  97    23371   7782   8983    664     70   4234       N  
ATOM   1746  N   PHE B  98      12.358  22.511 -23.993  1.00 91.40           N  
ANISOU 1746  N   PHE B  98    20310   6858   7558    318   1486   3324       N  
ATOM   1747  CA  PHE B  98      13.134  21.733 -23.067  1.00 88.11           C  
ANISOU 1747  CA  PHE B  98    19510   6582   7385    329   1775   3070       C  
ATOM   1748  C   PHE B  98      14.272  21.074 -23.793  1.00 89.52           C  
ANISOU 1748  C   PHE B  98    19742   6930   7341     73   2171   2989       C  
ATOM   1749  O   PHE B  98      14.443  19.871 -23.816  1.00 88.40           O  
ANISOU 1749  O   PHE B  98    19443   6987   7160    101   2322   2781       O  
ATOM   1750  CB  PHE B  98      12.238  20.741 -22.368  1.00 84.93           C  
ANISOU 1750  CB  PHE B  98    18822   6327   7120    565   1615   2869       C  
ATOM   1751  CG  PHE B  98      11.061  21.380 -21.707  1.00 84.09           C  
ANISOU 1751  CG  PHE B  98    18624   6117   7210    807   1236   2899       C  
ATOM   1752  CD1 PHE B  98       9.877  21.545 -22.395  1.00 84.88           C  
ANISOU 1752  CD1 PHE B  98    18905   6228   7119    914    902   3001       C  
ATOM   1753  CD2 PHE B  98      11.140  21.832 -20.391  1.00 81.51           C  
ANISOU 1753  CD2 PHE B  98    18010   5702   7256    931   1207   2800       C  
ATOM   1754  CE1 PHE B  98       8.785  22.137 -21.780  1.00 84.79           C  
ANISOU 1754  CE1 PHE B  98    18759   6154   7305   1168    546   2978       C  
ATOM   1755  CE2 PHE B  98      10.052  22.429 -19.771  1.00 80.75           C  
ANISOU 1755  CE2 PHE B  98    17798   5537   7345   1160    872   2778       C  
ATOM   1756  CZ  PHE B  98       8.874  22.583 -20.460  1.00 82.96           C  
ANISOU 1756  CZ  PHE B  98    18228   5839   7452   1292    542   2853       C  
ATOM   1757  N   ASP B  99      15.049  21.915 -24.422  1.00 92.97           N  
ANISOU 1757  N   ASP B  99    20427   7281   7618   -195   2335   3146       N  
ATOM   1758  CA  ASP B  99      16.267  21.487 -25.030  1.00 95.11           C  
ANISOU 1758  CA  ASP B  99    20700   7737   7700   -472   2751   3036       C  
ATOM   1759  C   ASP B  99      17.226  21.272 -23.878  1.00 92.60           C  
ANISOU 1759  C   ASP B  99    19957   7481   7745   -413   2983   2808       C  
ATOM   1760  O   ASP B  99      17.573  22.202 -23.153  1.00 92.23           O  
ANISOU 1760  O   ASP B  99    19835   7279   7930   -438   2973   2872       O  
ATOM   1761  CB  ASP B  99      16.750  22.590 -25.973  1.00 99.91           C  
ANISOU 1761  CB  ASP B  99    21718   8231   8012   -829   2838   3287       C  
ATOM   1762  CG  ASP B  99      18.076  22.275 -26.615  1.00103.43           C  
ANISOU 1762  CG  ASP B  99    22144   8915   8241  -1177   3308   3145       C  
ATOM   1763  OD1 ASP B  99      18.505  23.070 -27.484  1.00108.86           O  
ANISOU 1763  OD1 ASP B  99    23192   9556   8615  -1546   3421   3335       O  
ATOM   1764  OD2 ASP B  99      18.684  21.246 -26.249  1.00102.96           O  
ANISOU 1764  OD2 ASP B  99    21716   9087   8316  -1088   3555   2834       O  
ATOM   1765  N   TYR B 100      17.629  20.028 -23.688  1.00 91.04           N  
ANISOU 1765  N   TYR B 100    19493   7497   7601   -318   3165   2535       N  
ATOM   1766  CA  TYR B 100      18.448  19.684 -22.546  1.00 88.80           C  
ANISOU 1766  CA  TYR B 100    18798   7275   7666   -204   3320   2309       C  
ATOM   1767  C   TYR B 100      19.744  20.476 -22.483  1.00 90.73           C  
ANISOU 1767  C   TYR B 100    18957   7557   7961   -457   3617   2290       C  
ATOM   1768  O   TYR B 100      20.331  20.612 -21.407  1.00 89.10           O  
ANISOU 1768  O   TYR B 100    18432   7349   8072   -378   3674   2171       O  
ATOM   1769  CB  TYR B 100      18.777  18.204 -22.554  1.00 87.86           C  
ANISOU 1769  CB  TYR B 100    18480   7355   7547    -74   3465   2022       C  
ATOM   1770  CG  TYR B 100      19.531  17.790 -21.316  1.00 86.39           C  
ANISOU 1770  CG  TYR B 100    17889   7210   7725     92   3549   1803       C  
ATOM   1771  CD1 TYR B 100      18.860  17.554 -20.122  1.00 83.71           C  
ANISOU 1771  CD1 TYR B 100    17384   6760   7661    332   3289   1789       C  
ATOM   1772  CD2 TYR B 100      20.908  17.641 -21.331  1.00 88.57           C  
ANISOU 1772  CD2 TYR B 100    17939   7657   8055     -2   3876   1598       C  
ATOM   1773  CE1 TYR B 100      19.530  17.186 -18.984  1.00 82.06           C  
ANISOU 1773  CE1 TYR B 100    16843   6581   7756    469   3334   1613       C  
ATOM   1774  CE2 TYR B 100      21.590  17.261 -20.193  1.00 87.22           C  
ANISOU 1774  CE2 TYR B 100    17397   7527   8215    175   3909   1401       C  
ATOM   1775  CZ  TYR B 100      20.891  17.041 -19.026  1.00 84.67           C  
ANISOU 1775  CZ  TYR B 100    16963   7062   8146    407   3627   1428       C  
ATOM   1776  OH  TYR B 100      21.555  16.678 -17.889  1.00 85.63           O  
ANISOU 1776  OH  TYR B 100    16752   7216   8566    565   3631   1256       O  
ATOM   1777  N   ALA B 101      20.190  20.982 -23.632  1.00 94.18           N  
ANISOU 1777  N   ALA B 101    19679   8046   8059   -791   3808   2399       N  
ATOM   1778  CA  ALA B 101      21.431  21.741 -23.706  1.00 96.76           C  
ANISOU 1778  CA  ALA B 101    19951   8447   8365  -1116   4123   2370       C  
ATOM   1779  C   ALA B 101      21.280  23.172 -23.188  1.00 97.30           C  
ANISOU 1779  C   ALA B 101    20174   8227   8569  -1222   3964   2619       C  
ATOM   1780  O   ALA B 101      22.275  23.818 -22.881  1.00 98.95           O  
ANISOU 1780  O   ALA B 101    20265   8472   8859  -1457   4191   2571       O  
ATOM   1781  CB  ALA B 101      21.953  21.760 -25.124  1.00101.01           C  
ANISOU 1781  CB  ALA B 101    20762   9165   8451  -1497   4401   2386       C  
ATOM   1782  N   VAL B 102      20.047  23.681 -23.141  1.00 96.50           N  
ANISOU 1782  N   VAL B 102    20342   7845   8479  -1057   3574   2867       N  
ATOM   1783  CA  VAL B 102      19.757  25.027 -22.627  1.00 96.83           C  
ANISOU 1783  CA  VAL B 102    20558   7558   8676  -1087   3364   3087       C  
ATOM   1784  C   VAL B 102      19.411  24.930 -21.153  1.00 92.89           C  
ANISOU 1784  C   VAL B 102    19680   6988   8627   -747   3189   2955       C  
ATOM   1785  O   VAL B 102      19.998  25.604 -20.307  1.00 92.64           O  
ANISOU 1785  O   VAL B 102    19485   6874   8839   -813   3262   2915       O  
ATOM   1786  CB  VAL B 102      18.538  25.646 -23.319  1.00 98.27           C  
ANISOU 1786  CB  VAL B 102    21212   7467   8657  -1024   2984   3394       C  
ATOM   1787  CG1 VAL B 102      18.178  26.971 -22.664  1.00 98.45           C  
ANISOU 1787  CG1 VAL B 102    21388   7117   8903   -968   2725   3575       C  
ATOM   1788  CG2 VAL B 102      18.802  25.801 -24.784  1.00102.10           C  
ANISOU 1788  CG2 VAL B 102    22135   8003   8656  -1387   3116   3563       C  
ATOM   1789  N   ILE B 103      18.425  24.093 -20.870  1.00 90.09           N  
ANISOU 1789  N   ILE B 103    19203   6676   8352   -418   2957   2883       N  
ATOM   1790  CA  ILE B 103      17.964  23.854 -19.519  1.00 86.58           C  
ANISOU 1790  CA  ILE B 103    18416   6203   8276   -120   2782   2746       C  
ATOM   1791  C   ILE B 103      19.130  23.585 -18.583  1.00 85.12           C  
ANISOU 1791  C   ILE B 103    17838   6166   8339   -162   3044   2525       C  
ATOM   1792  O   ILE B 103      19.217  24.119 -17.476  1.00 83.58           O  
ANISOU 1792  O   ILE B 103    17445   5873   8437    -94   2977   2483       O  
ATOM   1793  CB  ILE B 103      17.116  22.583 -19.481  1.00 84.23           C  
ANISOU 1793  CB  ILE B 103    17998   6056   7950    131   2639   2622       C  
ATOM   1794  CG1 ILE B 103      15.733  22.833 -20.064  1.00 84.95           C  
ANISOU 1794  CG1 ILE B 103    18369   6027   7883    255   2294   2796       C  
ATOM   1795  CG2 ILE B 103      16.994  22.057 -18.064  1.00 81.06           C  
ANISOU 1795  CG2 ILE B 103    17205   5708   7886    351   2568   2425       C  
ATOM   1796  CD1 ILE B 103      14.899  21.581 -20.022  1.00 83.91           C  
ANISOU 1796  CD1 ILE B 103    18115   6066   7701    446   2169   2657       C  
ATOM   1797  N   LYS B 104      20.022  22.725 -19.047  1.00 85.75           N  
ANISOU 1797  N   LYS B 104    17792   6496   8293   -261   3334   2362       N  
ATOM   1798  CA  LYS B 104      21.079  22.193 -18.216  1.00 84.59           C  
ANISOU 1798  CA  LYS B 104    17233   6536   8371   -227   3544   2108       C  
ATOM   1799  C   LYS B 104      21.997  23.274 -17.678  1.00 85.46           C  
ANISOU 1799  C   LYS B 104    17231   6604   8636   -443   3695   2115       C  
ATOM   1800  O   LYS B 104      22.186  23.383 -16.484  1.00 83.38           O  
ANISOU 1800  O   LYS B 104    16684   6324   8671   -328   3636   2017       O  
ATOM   1801  CB  LYS B 104      21.887  21.174 -19.010  1.00 86.44           C  
ANISOU 1801  CB  LYS B 104    17384   7043   8417   -292   3827   1914       C  
ATOM   1802  CG  LYS B 104      22.491  20.111 -18.155  1.00 86.17           C  
ANISOU 1802  CG  LYS B 104    16945   7178   8619    -68   3889   1630       C  
ATOM   1803  CD  LYS B 104      22.950  20.699 -16.853  1.00 87.86           C  
ANISOU 1803  CD  LYS B 104    16874   7348   9161    -39   3854   1586       C  
ATOM   1804  CE  LYS B 104      22.965  19.644 -15.751  1.00 86.34           C  
ANISOU 1804  CE  LYS B 104    16376   7213   9218    267   3723   1394       C  
ATOM   1805  NZ  LYS B 104      24.232  19.789 -14.989  1.00 88.60           N  
ANISOU 1805  NZ  LYS B 104    16289   7653   9722    233   3889   1208       N  
ATOM   1806  N   PRO B 105      22.598  24.069 -18.569  1.00 88.90           N  
ANISOU 1806  N   PRO B 105    17904   7033   8841   -797   3901   2226       N  
ATOM   1807  CA  PRO B 105      23.410  25.181 -18.074  1.00 90.20           C  
ANISOU 1807  CA  PRO B 105    18009   7133   9131  -1054   4036   2245       C  
ATOM   1808  C   PRO B 105      22.592  26.170 -17.243  1.00 88.54           C  
ANISOU 1808  C   PRO B 105    17919   6579   9142   -940   3729   2412       C  
ATOM   1809  O   PRO B 105      23.095  26.710 -16.266  1.00 87.83           O  
ANISOU 1809  O   PRO B 105    17612   6459   9302   -986   3766   2333       O  
ATOM   1810  CB  PRO B 105      23.925  25.851 -19.352  1.00 94.50           C  
ANISOU 1810  CB  PRO B 105    18915   7687   9306  -1493   4263   2387       C  
ATOM   1811  CG  PRO B 105      23.111  25.294 -20.465  1.00 95.15           C  
ANISOU 1811  CG  PRO B 105    19313   7759   9081  -1425   4156   2509       C  
ATOM   1812  CD  PRO B 105      22.639  23.948 -20.037  1.00 91.94           C  
ANISOU 1812  CD  PRO B 105    18616   7494   8821  -1022   4042   2318       C  
ATOM   1813  N   ALA B 106      21.342  26.393 -17.632  1.00 88.05           N  
ANISOU 1813  N   ALA B 106    18184   6280   8990   -784   3423   2615       N  
ATOM   1814  CA  ALA B 106      20.448  27.246 -16.863  1.00 87.10           C  
ANISOU 1814  CA  ALA B 106    18149   5852   9094   -608   3104   2723       C  
ATOM   1815  C   ALA B 106      20.374  26.738 -15.426  1.00 83.65           C  
ANISOU 1815  C   ALA B 106    17255   5520   9007   -353   3034   2501       C  
ATOM   1816  O   ALA B 106      20.446  27.500 -14.472  1.00 83.33           O  
ANISOU 1816  O   ALA B 106    17108   5342   9212   -350   2971   2471       O  
ATOM   1817  CB  ALA B 106      19.060  27.279 -17.494  1.00 86.86           C  
ANISOU 1817  CB  ALA B 106    18441   5641   8922   -401   2764   2905       C  
ATOM   1818  N   ILE B 107      20.231  25.439 -15.266  1.00 81.39           N  
ANISOU 1818  N   ILE B 107    16728   5468   8728   -155   3041   2344       N  
ATOM   1819  CA  ILE B 107      20.150  24.878 -13.935  1.00 78.55           C  
ANISOU 1819  CA  ILE B 107    15987   5206   8652     55   2958   2154       C  
ATOM   1820  C   ILE B 107      21.460  25.097 -13.180  1.00 79.28           C  
ANISOU 1820  C   ILE B 107    15778   5421   8921    -98   3191   2005       C  
ATOM   1821  O   ILE B 107      21.465  25.436 -12.005  1.00 78.17           O  
ANISOU 1821  O   ILE B 107    15426   5241   9033    -39   3106   1926       O  
ATOM   1822  CB  ILE B 107      19.789  23.379 -13.994  1.00 76.35           C  
ANISOU 1822  CB  ILE B 107    15579   5123   8307    262   2915   2029       C  
ATOM   1823  CG1 ILE B 107      18.339  23.223 -14.441  1.00 75.72           C  
ANISOU 1823  CG1 ILE B 107    15729   4941   8101    424   2637   2143       C  
ATOM   1824  CG2 ILE B 107      19.983  22.739 -12.675  1.00 72.98           C  
ANISOU 1824  CG2 ILE B 107    14794   4808   8126    410   2870   1840       C  
ATOM   1825  CD1 ILE B 107      17.893  21.816 -14.579  1.00 74.09           C  
ANISOU 1825  CD1 ILE B 107    15459   4897   7794    577   2586   2036       C  
ATOM   1826  N   ASP B 108      22.576  24.914 -13.864  1.00 81.78           N  
ANISOU 1826  N   ASP B 108    16060   5919   9096   -310   3488   1947       N  
ATOM   1827  CA  ASP B 108      23.873  25.122 -13.243  1.00 82.91           C  
ANISOU 1827  CA  ASP B 108    15884   6231   9387   -472   3717   1780       C  
ATOM   1828  C   ASP B 108      23.973  26.563 -12.787  1.00 84.19           C  
ANISOU 1828  C   ASP B 108    16154   6172   9661   -683   3699   1885       C  
ATOM   1829  O   ASP B 108      24.394  26.854 -11.666  1.00 83.40           O  
ANISOU 1829  O   ASP B 108    15781   6104   9804   -686   3695   1766       O  
ATOM   1830  CB  ASP B 108      24.997  24.817 -14.234  1.00 86.07           C  
ANISOU 1830  CB  ASP B 108    16243   6885   9573   -704   4058   1682       C  
ATOM   1831  CG  ASP B 108      25.101  23.343 -14.555  1.00 85.92           C  
ANISOU 1831  CG  ASP B 108    16059   7096   9490   -474   4099   1508       C  
ATOM   1832  OD1 ASP B 108      24.450  22.527 -13.861  1.00 84.75           O  
ANISOU 1832  OD1 ASP B 108    15803   6916   9484   -159   3871   1458       O  
ATOM   1833  OD2 ASP B 108      25.832  23.000 -15.497  1.00 89.18           O  
ANISOU 1833  OD2 ASP B 108    16464   7719   9701   -625   4361   1408       O  
ATOM   1834  N   LYS B 109      23.579  27.465 -13.678  1.00 86.49           N  
ANISOU 1834  N   LYS B 109    16879   6223   9762   -867   3671   2113       N  
ATOM   1835  CA  LYS B 109      23.568  28.887 -13.389  1.00 88.03           C  
ANISOU 1835  CA  LYS B 109    17288   6123  10037  -1066   3618   2241       C  
ATOM   1836  C   LYS B 109      22.740  29.175 -12.142  1.00 85.27           C  
ANISOU 1836  C   LYS B 109    16809   5598   9992   -794   3333   2197       C  
ATOM   1837  O   LYS B 109      23.134  29.988 -11.305  1.00 85.62           O  
ANISOU 1837  O   LYS B 109    16757   5546  10227   -915   3356   2141       O  
ATOM   1838  CB  LYS B 109      22.984  29.650 -14.571  1.00 90.92           C  
ANISOU 1838  CB  LYS B 109    18215   6196  10137  -1210   3523   2524       C  
ATOM   1839  CG  LYS B 109      23.298  31.112 -14.547  1.00 94.50           C  
ANISOU 1839  CG  LYS B 109    18970   6339  10595  -1522   3540   2665       C  
ATOM   1840  CD  LYS B 109      22.269  31.895 -15.327  1.00 98.05           C  
ANISOU 1840  CD  LYS B 109    19990   6377  10890  -1481   3254   2957       C  
ATOM   1841  CE  LYS B 109      22.603  33.377 -15.330  1.00103.50           C  
ANISOU 1841  CE  LYS B 109    21060   6691  11574  -1805   3250   3112       C  
ATOM   1842  NZ  LYS B 109      21.377  34.215 -15.198  1.00105.20           N  
ANISOU 1842  NZ  LYS B 109    21631   6434  11907  -1530   2826   3278       N  
ATOM   1843  N   PHE B 110      21.591  28.511 -12.019  1.00 82.66           N  
ANISOU 1843  N   PHE B 110    16470   5246   9690   -455   3078   2202       N  
ATOM   1844  CA  PHE B 110      20.696  28.772 -10.895  1.00 80.38           C  
ANISOU 1844  CA  PHE B 110    16058   4828   9657   -214   2814   2135       C  
ATOM   1845  C   PHE B 110      21.394  28.413  -9.608  1.00 78.69           C  
ANISOU 1845  C   PHE B 110    15404   4824   9669   -214   2909   1913       C  
ATOM   1846  O   PHE B 110      21.450  29.217  -8.665  1.00 78.34           O  
ANISOU 1846  O   PHE B 110    15269   4665   9833   -259   2860   1847       O  
ATOM   1847  CB  PHE B 110      19.403  27.975 -11.012  1.00 77.88           C  
ANISOU 1847  CB  PHE B 110    15757   4539   9295    102   2561   2138       C  
ATOM   1848  CG  PHE B 110      18.501  28.116  -9.821  1.00 75.04           C  
ANISOU 1848  CG  PHE B 110    15206   4130   9174    322   2324   2013       C  
ATOM   1849  CD1 PHE B 110      18.501  27.152  -8.815  1.00 72.14           C  
ANISOU 1849  CD1 PHE B 110    14482   4008   8922    430   2318   1823       C  
ATOM   1850  CD2 PHE B 110      17.652  29.203  -9.703  1.00 75.31           C  
ANISOU 1850  CD2 PHE B 110    15430   3876   9309    417   2099   2070       C  
ATOM   1851  CE1 PHE B 110      17.671  27.264  -7.733  1.00 69.08           C  
ANISOU 1851  CE1 PHE B 110    13921   3616   8712    578   2124   1692       C  
ATOM   1852  CE2 PHE B 110      16.824  29.331  -8.614  1.00 73.58           C  
ANISOU 1852  CE2 PHE B 110    15000   3655   9302    611   1904   1905       C  
ATOM   1853  CZ  PHE B 110      16.830  28.348  -7.628  1.00 70.91           C  
ANISOU 1853  CZ  PHE B 110    14294   3603   9045    667   1933   1713       C  
ATOM   1854  N   ALA B 111      21.929  27.194  -9.592  1.00 77.67           N  
ANISOU 1854  N   ALA B 111    15023   4996   9494   -156   3029   1792       N  
ATOM   1855  CA  ALA B 111      22.669  26.684  -8.453  1.00 76.52           C  
ANISOU 1855  CA  ALA B 111    14471   5073   9532   -133   3093   1590       C  
ATOM   1856  C   ALA B 111      23.763  27.661  -8.025  1.00 79.00           C  
ANISOU 1856  C   ALA B 111    14668   5391   9956   -414   3279   1534       C  
ATOM   1857  O   ALA B 111      23.885  28.014  -6.853  1.00 77.85           O  
ANISOU 1857  O   ALA B 111    14312   5250  10016   -420   3218   1425       O  
ATOM   1858  CB  ALA B 111      23.278  25.367  -8.797  1.00 76.01           C  
ANISOU 1858  CB  ALA B 111    14229   5280   9370    -51   3212   1486       C  
ATOM   1859  N   ARG B 112      24.572  28.097  -8.975  1.00 82.55           N  
ANISOU 1859  N   ARG B 112    15257   5861  10246   -685   3516   1596       N  
ATOM   1860  CA  ARG B 112      25.702  28.935  -8.625  1.00 85.73           C  
ANISOU 1860  CA  ARG B 112    15529   6321  10722  -1005   3726   1518       C  
ATOM   1861  C   ARG B 112      25.275  30.221  -7.949  1.00 86.09           C  
ANISOU 1861  C   ARG B 112    15734   6053  10921  -1101   3598   1580       C  
ATOM   1862  O   ARG B 112      25.839  30.617  -6.932  1.00 85.99           O  
ANISOU 1862  O   ARG B 112    15472   6110  11092  -1207   3639   1440       O  
ATOM   1863  CB  ARG B 112      26.542  29.250  -9.853  1.00 89.85           C  
ANISOU 1863  CB  ARG B 112    16225   6918  10997  -1344   4015   1579       C  
ATOM   1864  CG  ARG B 112      27.591  28.187 -10.145  1.00 93.54           C  
ANISOU 1864  CG  ARG B 112    16338   7810  11394  -1347   4248   1375       C  
ATOM   1865  CD  ARG B 112      28.683  28.744 -11.052  1.00103.34           C  
ANISOU 1865  CD  ARG B 112    17639   9201  12425  -1793   4596   1353       C  
ATOM   1866  NE  ARG B 112      28.546  28.263 -12.427  1.00109.12           N  
ANISOU 1866  NE  ARG B 112    18615   9989  12856  -1836   4710   1435       N  
ATOM   1867  CZ  ARG B 112      27.724  28.782 -13.338  1.00111.68           C  
ANISOU 1867  CZ  ARG B 112    19455  10012  12966  -1924   4620   1705       C  
ATOM   1868  NH1 ARG B 112      26.943  29.810 -13.034  1.00112.09           N  
ANISOU 1868  NH1 ARG B 112    19837   9662  13092  -1942   4399   1912       N  
ATOM   1869  NH2 ARG B 112      27.679  28.264 -14.557  1.00113.79           N  
ANISOU 1869  NH2 ARG B 112    19911  10382  12943  -1980   4736   1754       N  
ATOM   1870  N   GLU B 113      24.284  30.881  -8.530  1.00 86.84           N  
ANISOU 1870  N   GLU B 113    16252   5800  10942  -1053   3430   1778       N  
ATOM   1871  CA  GLU B 113      23.793  32.141  -7.998  1.00 87.74           C  
ANISOU 1871  CA  GLU B 113    16573   5559  11207  -1099   3278   1828       C  
ATOM   1872  C   GLU B 113      23.248  31.926  -6.606  1.00 84.77           C  
ANISOU 1872  C   GLU B 113    15884   5233  11091   -851   3094   1650       C  
ATOM   1873  O   GLU B 113      23.434  32.751  -5.723  1.00 85.38           O  
ANISOU 1873  O   GLU B 113    15894   5198  11348   -959   3081   1557       O  
ATOM   1874  CB  GLU B 113      22.709  32.712  -8.900  1.00 88.99           C  
ANISOU 1874  CB  GLU B 113    17226   5343  11244   -992   3063   2058       C  
ATOM   1875  CG  GLU B 113      23.114  32.719 -10.346  1.00 93.47           C  
ANISOU 1875  CG  GLU B 113    18126   5895  11493  -1225   3220   2251       C  
ATOM   1876  CD  GLU B 113      22.139  33.478 -11.216  1.00 98.59           C  
ANISOU 1876  CD  GLU B 113    19322   6126  12011  -1161   2978   2506       C  
ATOM   1877  OE1 GLU B 113      20.924  33.337 -10.962  1.00 98.21           O  
ANISOU 1877  OE1 GLU B 113    19289   5954  12072   -785   2671   2506       O  
ATOM   1878  OE2 GLU B 113      22.586  34.211 -12.144  1.00102.52           O  
ANISOU 1878  OE2 GLU B 113    20234   6433  12285  -1495   3083   2697       O  
ATOM   1879  N   GLN B 114      22.566  30.811  -6.405  1.00 82.06           N  
ANISOU 1879  N   GLN B 114    15367   5064  10749   -549   2956   1595       N  
ATOM   1880  CA  GLN B 114      21.999  30.514  -5.103  1.00 79.98           C  
ANISOU 1880  CA  GLN B 114    14824   4883  10683   -355   2786   1425       C  
ATOM   1881  C   GLN B 114      23.068  30.291  -4.040  1.00 79.60           C  
ANISOU 1881  C   GLN B 114    14390   5093  10761   -494   2921   1243       C  
ATOM   1882  O   GLN B 114      23.011  30.858  -2.957  1.00 79.27           O  
ANISOU 1882  O   GLN B 114    14212   5011  10895   -535   2860   1119       O  
ATOM   1883  CB  GLN B 114      21.136  29.279  -5.214  1.00 77.54           C  
ANISOU 1883  CB  GLN B 114    14444   4725  10291    -74   2636   1415       C  
ATOM   1884  CG  GLN B 114      19.840  29.555  -5.895  1.00 78.63           C  
ANISOU 1884  CG  GLN B 114    14880   4637  10357    110   2427   1534       C  
ATOM   1885  CD  GLN B 114      18.775  29.882  -4.906  1.00 77.93           C  
ANISOU 1885  CD  GLN B 114    14688   4480  10443    286   2201   1399       C  
ATOM   1886  OE1 GLN B 114      18.421  31.041  -4.757  1.00 81.20           O  
ANISOU 1886  OE1 GLN B 114    15252   4625  10976    287   2108   1397       O  
ATOM   1887  NE2 GLN B 114      18.263  28.858  -4.194  1.00 73.94           N  
ANISOU 1887  NE2 GLN B 114    13931   4219   9946    422   2110   1264       N  
ATOM   1888  N   VAL B 115      24.034  29.440  -4.347  1.00 79.97           N  
ANISOU 1888  N   VAL B 115    14249   5419  10718   -551   3092   1207       N  
ATOM   1889  CA  VAL B 115      25.129  29.211  -3.435  1.00 80.24           C  
ANISOU 1889  CA  VAL B 115    13906   5719  10863   -664   3199   1033       C  
ATOM   1890  C   VAL B 115      25.803  30.541  -3.114  1.00 83.39           C  
ANISOU 1890  C   VAL B 115    14324   6007  11354   -984   3332    997       C  
ATOM   1891  O   VAL B 115      26.155  30.809  -1.969  1.00 83.11           O  
ANISOU 1891  O   VAL B 115    14043   6061  11473  -1059   3309    850       O  
ATOM   1892  CB  VAL B 115      26.148  28.243  -4.042  1.00 80.75           C  
ANISOU 1892  CB  VAL B 115    13787   6082  10814   -671   3376    982       C  
ATOM   1893  CG1 VAL B 115      27.430  28.245  -3.242  1.00 81.16           C  
ANISOU 1893  CG1 VAL B 115    13449   6410  10980   -821   3498    794       C  
ATOM   1894  CG2 VAL B 115      25.565  26.856  -4.098  1.00 78.20           C  
ANISOU 1894  CG2 VAL B 115    13420   5863  10431   -356   3222    978       C  
ATOM   1895  N   SER B 116      25.980  31.381  -4.126  1.00 86.76           N  
ANISOU 1895  N   SER B 116    15071   6228  11664  -1202   3465   1137       N  
ATOM   1896  CA  SER B 116      26.756  32.592  -3.938  1.00 90.55           C  
ANISOU 1896  CA  SER B 116    15607   6606  12193  -1571   3623   1108       C  
ATOM   1897  C   SER B 116      26.042  33.564  -3.012  1.00 91.01           C  
ANISOU 1897  C   SER B 116    15774   6366  12441  -1546   3444   1070       C  
ATOM   1898  O   SER B 116      26.678  34.422  -2.421  1.00 92.73           O  
ANISOU 1898  O   SER B 116    15935   6544  12755  -1818   3540    976       O  
ATOM   1899  CB  SER B 116      27.079  33.261  -5.277  1.00 93.87           C  
ANISOU 1899  CB  SER B 116    16417   6848  12400  -1857   3798   1287       C  
ATOM   1900  OG  SER B 116      25.973  34.014  -5.740  1.00 94.65           O  
ANISOU 1900  OG  SER B 116    16991   6499  12475  -1767   3604   1480       O  
ATOM   1901  N   ILE B 117      24.726  33.431  -2.881  1.00 90.27           N  
ANISOU 1901  N   ILE B 117    15817   6082  12399  -1227   3190   1114       N  
ATOM   1902  CA  ILE B 117      23.993  34.210  -1.878  1.00 91.26           C  
ANISOU 1902  CA  ILE B 117    15961   5990  12725  -1149   3013   1006       C  
ATOM   1903  C   ILE B 117      24.658  34.088  -0.513  1.00 91.50           C  
ANISOU 1903  C   ILE B 117    15577   6289  12899  -1260   3064    779       C  
ATOM   1904  O   ILE B 117      24.769  35.055   0.216  1.00 92.89           O  
ANISOU 1904  O   ILE B 117    15763   6317  13213  -1417   3064    669       O  
ATOM   1905  CB  ILE B 117      22.535  33.720  -1.684  1.00 88.83           C  
ANISOU 1905  CB  ILE B 117    15671   5623  12456   -762   2743    990       C  
ATOM   1906  CG1 ILE B 117      21.719  33.838  -2.976  1.00 90.12           C  
ANISOU 1906  CG1 ILE B 117    16233   5526  12482   -607   2632   1204       C  
ATOM   1907  CG2 ILE B 117      21.878  34.475  -0.542  1.00 87.71           C  
ANISOU 1907  CG2 ILE B 117    15465   5335  12525   -697   2593    805       C  
ATOM   1908  CD1 ILE B 117      21.515  35.290  -3.447  1.00 94.96           C  
ANISOU 1908  CD1 ILE B 117    17280   5667  13132   -712   2573   1314       C  
ATOM   1909  N   PHE B 118      25.085  32.886  -0.159  1.00 91.21           N  
ANISOU 1909  N   PHE B 118    15196   6634  12825  -1171   3086    705       N  
ATOM   1910  CA  PHE B 118      25.611  32.642   1.175  1.00 92.31           C  
ANISOU 1910  CA  PHE B 118    14953   7040  13079  -1235   3074    505       C  
ATOM   1911  C   PHE B 118      27.110  32.417   1.217  1.00 95.87           C  
ANISOU 1911  C   PHE B 118    15125   7799  13502  -1466   3278    433       C  
ATOM   1912  O   PHE B 118      27.699  32.406   2.286  1.00 95.72           O  
ANISOU 1912  O   PHE B 118    14803   7993  13575  -1569   3272    269       O  
ATOM   1913  CB  PHE B 118      24.898  31.453   1.819  1.00 88.68           C  
ANISOU 1913  CB  PHE B 118    14308   6776  12610   -952   2879    450       C  
ATOM   1914  CG  PHE B 118      23.493  31.753   2.222  1.00 86.76           C  
ANISOU 1914  CG  PHE B 118    14200   6336  12427   -780   2683    412       C  
ATOM   1915  CD1 PHE B 118      22.446  31.533   1.346  1.00 85.63           C  
ANISOU 1915  CD1 PHE B 118    14305   6026  12204   -558   2578    538       C  
ATOM   1916  CD2 PHE B 118      23.218  32.283   3.469  1.00 85.99           C  
ANISOU 1916  CD2 PHE B 118    13963   6247  12461   -847   2607    224       C  
ATOM   1917  CE1 PHE B 118      21.138  31.824   1.712  1.00 84.74           C  
ANISOU 1917  CE1 PHE B 118    14267   5775  12155   -386   2392    460       C  
ATOM   1918  CE2 PHE B 118      21.919  32.579   3.847  1.00 85.15           C  
ANISOU 1918  CE2 PHE B 118    13938   6001  12416   -686   2442    135       C  
ATOM   1919  CZ  PHE B 118      20.873  32.347   2.965  1.00 84.89           C  
ANISOU 1919  CZ  PHE B 118    14120   5818  12314   -445   2331    246       C  
ATOM   1920  N   PHE B 119      27.750  32.249   0.070  1.00 45.59           N  
ATOM   1921  CA  PHE B 119      29.185  31.881   0.119  1.00 48.91           C  
ATOM   1922  C   PHE B 119      30.118  32.738  -0.776  1.00 49.71           C  
ATOM   1923  O   PHE B 119      29.906  32.813  -1.984  1.00 50.88           O  
ATOM   1924  CB  PHE B 119      29.367  30.356  -0.123  1.00 49.41           C  
ATOM   1925  CG  PHE B 119      28.683  29.490   0.924  1.00 51.90           C  
ATOM   1926  CD1 PHE B 119      27.352  29.109   0.779  1.00 53.18           C  
ATOM   1927  CD2 PHE B 119      29.365  29.077   2.074  1.00 54.33           C  
ATOM   1928  CE1 PHE B 119      26.720  28.326   1.759  1.00 52.97           C  
ATOM   1929  CE2 PHE B 119      28.726  28.299   3.061  1.00 52.97           C  
ATOM   1930  CZ  PHE B 119      27.410  27.929   2.896  1.00 52.46           C  
TER    1931      PHE B 119                                                      
ATOM   1932  N   PRO C   2      36.709  32.968  35.001  1.00 82.59           N  
ANISOU 1932  N   PRO C   2    15030   6130  10221   -694  -1767   1332       N  
ATOM   1933  CA  PRO C   2      35.970  33.245  36.225  1.00 80.34           C  
ANISOU 1933  CA  PRO C   2    14826   5511  10189   -521  -2146    715       C  
ATOM   1934  C   PRO C   2      35.706  31.949  36.970  1.00 76.28           C  
ANISOU 1934  C   PRO C   2    14585   5258   9139   -304  -1808    175       C  
ATOM   1935  O   PRO C   2      35.465  30.915  36.362  1.00 74.25           O  
ANISOU 1935  O   PRO C   2    14546   5350   8316   -285  -1401    183       O  
ATOM   1936  CB  PRO C   2      34.648  33.838  35.723  1.00 80.69           C  
ANISOU 1936  CB  PRO C   2    14974   5433  10252   -559  -2419    680       C  
ATOM   1937  CG  PRO C   2      34.914  34.256  34.328  1.00 84.26           C  
ANISOU 1937  CG  PRO C   2    15331   5997  10686   -810  -2357   1407       C  
ATOM   1938  CD  PRO C   2      35.914  33.275  33.805  1.00 84.39           C  
ANISOU 1938  CD  PRO C   2    15357   6490  10216   -822  -1773   1674       C  
ATOM   1939  N   LYS C   3      35.754  32.016  38.292  1.00 75.57           N  
ANISOU 1939  N   LYS C   3    14475   4994   9244   -131  -2026   -282       N  
ATOM   1940  CA  LYS C   3      35.593  30.836  39.123  1.00 72.42           C  
ANISOU 1940  CA  LYS C   3    14300   4833   8382     43  -1752   -698       C  
ATOM   1941  C   LYS C   3      34.271  30.886  39.854  1.00 71.11           C  
ANISOU 1941  C   LYS C   3    14255   4697   8067    194  -1900  -1174       C  
ATOM   1942  O   LYS C   3      33.854  31.925  40.312  1.00 73.22           O  
ANISOU 1942  O   LYS C   3    14379   4732   8711    281  -2321  -1388       O  
ATOM   1943  CB  LYS C   3      36.716  30.811  40.138  1.00 73.05           C  
ANISOU 1943  CB  LYS C   3    14257   4786   8713    147  -1867   -825       C  
ATOM   1944  CG  LYS C   3      36.531  29.793  41.221  1.00 70.92           C  
ANISOU 1944  CG  LYS C   3    14198   4712   8038    331  -1715  -1239       C  
ATOM   1945  CD  LYS C   3      37.795  29.691  42.038  1.00 71.76           C  
ANISOU 1945  CD  LYS C   3    14199   4693   8374    420  -1827  -1292       C  
ATOM   1946  CE  LYS C   3      37.532  28.966  43.310  1.00 70.45           C  
ANISOU 1946  CE  LYS C   3    14225   4690   7853    619  -1817  -1699       C  
ATOM   1947  NZ  LYS C   3      38.507  29.400  44.321  1.00 73.48           N  
ANISOU 1947  NZ  LYS C   3    14480   4858   8582    775  -2165  -1876       N  
ATOM   1948  N   ILE C   4      33.604  29.761  39.969  1.00 68.84           N  
ANISOU 1948  N   ILE C   4    14192   4699   7265    236  -1578  -1344       N  
ATOM   1949  CA  ILE C   4      32.350  29.728  40.684  1.00 68.43           C  
ANISOU 1949  CA  ILE C   4    14189   4763   7046    363  -1648  -1739       C  
ATOM   1950  C   ILE C   4      32.422  28.769  41.853  1.00 67.51           C  
ANISOU 1950  C   ILE C   4    14173   4890   6585    489  -1465  -1982       C  
ATOM   1951  O   ILE C   4      32.982  27.678  41.765  1.00 66.37           O  
ANISOU 1951  O   ILE C   4    14169   4855   6192    429  -1192  -1828       O  
ATOM   1952  CB  ILE C   4      31.201  29.279  39.794  1.00 67.72           C  
ANISOU 1952  CB  ILE C   4    14231   4802   6698    264  -1481  -1673       C  
ATOM   1953  CG1 ILE C   4      30.825  30.378  38.809  1.00 69.86           C  
ANISOU 1953  CG1 ILE C   4    14405   4845   7293    170  -1757  -1487       C  
ATOM   1954  CG2 ILE C   4      30.006  28.891  40.644  1.00 67.04           C  
ANISOU 1954  CG2 ILE C   4    14158   4935   6381    377  -1432  -2034       C  
ATOM   1955  CD1 ILE C   4      29.615  30.057  37.992  1.00 69.12           C  
ANISOU 1955  CD1 ILE C   4    14435   4841   6988    107  -1684  -1480       C  
ATOM   1956  N   GLN C   5      31.843  29.193  42.961  1.00 68.85           N  
ANISOU 1956  N   GLN C   5    14258   5168   6735    687  -1646  -2368       N  
ATOM   1957  CA  GLN C   5      31.739  28.364  44.142  1.00 68.73           C  
ANISOU 1957  CA  GLN C   5    14319   5477   6320    811  -1482  -2556       C  
ATOM   1958  C   GLN C   5      30.255  28.037  44.355  1.00 69.30           C  
ANISOU 1958  C   GLN C   5    14370   5874   6086    829  -1325  -2707       C  
ATOM   1959  O   GLN C   5      29.471  28.921  44.682  1.00 71.37           O  
ANISOU 1959  O   GLN C   5    14459   6203   6454    996  -1531  -3030       O  
ATOM   1960  CB  GLN C   5      32.339  29.097  45.355  1.00 70.51           C  
ANISOU 1960  CB  GLN C   5    14430   5682   6680   1081  -1808  -2893       C  
ATOM   1961  CG  GLN C   5      33.798  29.539  45.171  1.00 70.23           C  
ANISOU 1961  CG  GLN C   5    14340   5265   7081   1054  -2033  -2739       C  
ATOM   1962  CD  GLN C   5      34.297  30.503  46.286  1.00 73.50           C  
ANISOU 1962  CD  GLN C   5    14606   5547   7775   1357  -2517  -3147       C  
ATOM   1963  OE1 GLN C   5      34.354  30.155  47.468  1.00 74.35           O  
ANISOU 1963  OE1 GLN C   5    14778   5932   7538   1584  -2535  -3430       O  
ATOM   1964  NE2 GLN C   5      34.685  31.698  45.889  1.00 74.89           N  
ANISOU 1964  NE2 GLN C   5    14578   5289   8587   1362  -2950  -3150       N  
ATOM   1965  N   THR C   6      29.856  26.787  44.140  1.00 68.22           N  
ANISOU 1965  N   THR C   6    14370   5915   5634    663  -1002  -2482       N  
ATOM   1966  CA  THR C   6      28.489  26.388  44.470  1.00 69.77           C  
ANISOU 1966  CA  THR C   6    14485   6442   5582    652   -846  -2561       C  
ATOM   1967  C   THR C   6      28.481  25.414  45.604  1.00 71.17           C  
ANISOU 1967  C   THR C   6    14689   6991   5359    665   -642  -2487       C  
ATOM   1968  O   THR C   6      29.308  24.514  45.667  1.00 70.34           O  
ANISOU 1968  O   THR C   6    14757   6802   5168    562   -557  -2244       O  
ATOM   1969  CB  THR C   6      27.792  25.657  43.341  1.00 68.41           C  
ANISOU 1969  CB  THR C   6    14401   6168   5422    421   -698  -2316       C  
ATOM   1970  OG1 THR C   6      28.780  25.116  42.465  1.00 67.06           O  
ANISOU 1970  OG1 THR C   6    14431   5730   5318    300   -659  -2062       O  
ATOM   1971  CG2 THR C   6      26.872  26.580  42.585  1.00 68.94           C  
ANISOU 1971  CG2 THR C   6    14347   6112   5734    436   -866  -2458       C  
ATOM   1972  N   TYR C   7      27.511  25.585  46.487  1.00 74.15           N  
ANISOU 1972  N   TYR C   7    14872   7813   5489    798   -569  -2680       N  
ATOM   1973  CA  TYR C   7      27.312  24.668  47.588  1.00 76.42           C  
ANISOU 1973  CA  TYR C   7    15137   8568   5329    784   -345  -2516       C  
ATOM   1974  C   TYR C   7      26.157  23.761  47.244  1.00 76.99           C  
ANISOU 1974  C   TYR C   7    15118   8797   5338    527   -105  -2212       C  
ATOM   1975  O   TYR C   7      25.002  24.172  47.285  1.00 78.98           O  
ANISOU 1975  O   TYR C   7    15116   9315   5576    581    -39  -2369       O  
ATOM   1976  CB  TYR C   7      27.050  25.466  48.854  1.00 80.30           C  
ANISOU 1976  CB  TYR C   7    15426   9564   5518   1141   -404  -2921       C  
ATOM   1977  CG  TYR C   7      28.246  26.323  49.167  1.00 81.07           C  
ANISOU 1977  CG  TYR C   7    15616   9403   5784   1394   -742  -3228       C  
ATOM   1978  CD1 TYR C   7      29.264  25.845  49.974  1.00 82.29           C  
ANISOU 1978  CD1 TYR C   7    15932   9628   5708   1455   -774  -3131       C  
ATOM   1979  CD2 TYR C   7      28.395  27.581  48.597  1.00 81.36           C  
ANISOU 1979  CD2 TYR C   7    15570   9053   6291   1539  -1083  -3565       C  
ATOM   1980  CE1 TYR C   7      30.368  26.598  50.234  1.00 83.31           C  
ANISOU 1980  CE1 TYR C   7    16117   9467   6069   1672  -1124  -3400       C  
ATOM   1981  CE2 TYR C   7      29.507  28.344  48.855  1.00 81.95           C  
ANISOU 1981  CE2 TYR C   7    15685   8820   6634   1730  -1447  -3788       C  
ATOM   1982  CZ  TYR C   7      30.490  27.843  49.671  1.00 83.12           C  
ANISOU 1982  CZ  TYR C   7    15977   9054   6552   1801  -1460  -3719       C  
ATOM   1983  OH  TYR C   7      31.607  28.587  49.951  1.00 84.64           O  
ANISOU 1983  OH  TYR C   7    16180   8908   7071   1992  -1864  -3945       O  
ATOM   1984  N   VAL C   8      26.482  22.533  46.861  1.00 75.87           N  
ANISOU 1984  N   VAL C   8    15157   8439   5229    259    -29  -1800       N  
ATOM   1985  CA  VAL C   8      25.485  21.587  46.373  1.00 76.57           C  
ANISOU 1985  CA  VAL C   8    15172   8517   5405    -14     89  -1485       C  
ATOM   1986  C   VAL C   8      25.218  20.535  47.427  1.00 80.17           C  
ANISOU 1986  C   VAL C   8    15535   9364   5563   -165    261  -1083       C  
ATOM   1987  O   VAL C   8      25.920  20.474  48.443  1.00 81.58           O  
ANISOU 1987  O   VAL C   8    15773   9797   5427    -53    284  -1044       O  
ATOM   1988  CB  VAL C   8      25.979  20.891  45.124  1.00 73.60           C  
ANISOU 1988  CB  VAL C   8    15046   7584   5336   -186    -38  -1326       C  
ATOM   1989  CG1 VAL C   8      26.316  21.920  44.068  1.00 71.04           C  
ANISOU 1989  CG1 VAL C   8    14808   6946   5239    -60   -183  -1614       C  
ATOM   1990  CG2 VAL C   8      27.204  20.041  45.461  1.00 73.16           C  
ANISOU 1990  CG2 VAL C   8    15211   7370   5216   -226    -86  -1125       C  
ATOM   1991  N   ASN C   9      24.202  19.710  47.199  1.00 82.21           N  
ANISOU 1991  N   ASN C   9    15631   9664   5941   -430    348   -746       N  
ATOM   1992  CA  ASN C   9      23.902  18.651  48.151  1.00 86.50           C  
ANISOU 1992  CA  ASN C   9    16041  10559   6266   -646    487   -223       C  
ATOM   1993  C   ASN C   9      24.745  17.424  47.872  1.00 85.61           C  
ANISOU 1993  C   ASN C   9    16206   9955   6367   -862    283    136       C  
ATOM   1994  O   ASN C   9      25.417  17.337  46.837  1.00 81.91           O  
ANISOU 1994  O   ASN C   9    15995   8920   6206   -832     74    -55       O  
ATOM   1995  CB  ASN C   9      22.413  18.309  48.163  1.00 90.17           C  
ANISOU 1995  CB  ASN C   9    16118  11314   6828   -860    650     50       C  
ATOM   1996  CG  ASN C   9      21.928  17.799  46.834  1.00 89.06           C  
ANISOU 1996  CG  ASN C   9    16029  10565   7246  -1072    439    107       C  
ATOM   1997  OD1 ASN C   9      22.592  16.983  46.180  1.00 88.56           O  
ANISOU 1997  OD1 ASN C   9    16250   9943   7456  -1197    193    242       O  
ATOM   1998  ND2 ASN C   9      20.757  18.271  46.418  1.00 90.02           N  
ANISOU 1998  ND2 ASN C   9    15866  10794   7543  -1077    498    -41       N  
ATOM   1999  N   ASN C  10      24.717  16.479  48.803  1.00 89.63           N  
ANISOU 1999  N   ASN C  10    16642  10712   6702  -1063    328    661       N  
ATOM   2000  CA  ASN C  10      25.525  15.277  48.670  1.00 89.80           C  
ANISOU 2000  CA  ASN C  10    16903  10247   6969  -1254     58   1004       C  
ATOM   2001  C   ASN C  10      25.249  14.459  47.408  1.00 88.83           C  
ANISOU 2001  C   ASN C  10    16850   9463   7439  -1449   -218   1066       C  
ATOM   2002  O   ASN C  10      26.173  13.917  46.804  1.00 86.71           O  
ANISOU 2002  O   ASN C  10    16855   8663   7428  -1412   -494    962       O  
ATOM   2003  CB  ASN C  10      25.393  14.426  49.919  1.00 95.11           C  
ANISOU 2003  CB  ASN C  10    17445  11319   7375  -1476    116   1650       C  
ATOM   2004  CG  ASN C  10      26.112  15.034  51.085  1.00 96.17           C  
ANISOU 2004  CG  ASN C  10    17658  11971   6910  -1214    250   1527       C  
ATOM   2005  OD1 ASN C  10      27.221  15.534  50.937  1.00 92.37           O  
ANISOU 2005  OD1 ASN C  10    17450  11231   6416   -957    114   1104       O  
ATOM   2006  ND2 ASN C  10      25.489  15.006  52.251  1.00102.09           N  
ANISOU 2006  ND2 ASN C  10    18146  13489   7153  -1261    509   1896       N  
ATOM   2007  N   ASN C  11      23.980  14.378  47.017  1.00 90.94           N  
ANISOU 2007  N   ASN C  11    16847   9781   7926  -1618   -167   1190       N  
ATOM   2008  CA  ASN C  11      23.605  13.726  45.765  1.00 90.76           C  
ANISOU 2008  CA  ASN C  11    16882   9140   8463  -1743   -480   1150       C  
ATOM   2009  C   ASN C  11      24.406  14.239  44.600  1.00 85.77           C  
ANISOU 2009  C   ASN C  11    16575   8105   7909  -1461   -619    575       C  
ATOM   2010  O   ASN C  11      25.215  13.528  44.010  1.00 85.05           O  
ANISOU 2010  O   ASN C  11    16730   7542   8041  -1420   -906    501       O  
ATOM   2011  CB  ASN C  11      22.140  13.982  45.449  1.00 92.82           C  
ANISOU 2011  CB  ASN C  11    16798   9560   8909  -1871   -381   1198       C  
ATOM   2012  CG  ASN C  11      21.251  12.857  45.894  1.00100.20           C  
ANISOU 2012  CG  ASN C  11    17408  10499  10166  -2273   -479   1874       C  
ATOM   2013  OD1 ASN C  11      21.690  11.936  46.591  1.00104.71           O  
ANISOU 2013  OD1 ASN C  11    17997  11025  10762  -2474   -598   2372       O  
ATOM   2014  ND2 ASN C  11      19.985  12.919  45.500  1.00104.46           N  
ANISOU 2014  ND2 ASN C  11    17618  11068  11005  -2414   -464   1941       N  
ATOM   2015  N   VAL C  12      24.135  15.487  44.255  1.00 83.13           N  
ANISOU 2015  N   VAL C  12    16203   7984   7399  -1260   -428    180       N  
ATOM   2016  CA  VAL C  12      24.830  16.144  43.172  1.00 79.15           C  
ANISOU 2016  CA  VAL C  12    15953   7202   6919  -1017   -512   -277       C  
ATOM   2017  C   VAL C  12      26.332  15.871  43.258  1.00 77.53           C  
ANISOU 2017  C   VAL C  12    16012   6818   6628   -886   -589   -346       C  
ATOM   2018  O   VAL C  12      26.943  15.393  42.306  1.00 76.50           O  
ANISOU 2018  O   VAL C  12    16083   6309   6675   -803   -790   -498       O  
ATOM   2019  CB  VAL C  12      24.562  17.655  43.212  1.00 77.51           C  
ANISOU 2019  CB  VAL C  12    15643   7308   6499   -826   -309   -605       C  
ATOM   2020  CG1 VAL C  12      25.372  18.367  42.152  1.00 73.88           C  
ANISOU 2020  CG1 VAL C  12    15417   6588   6065   -621   -396   -946       C  
ATOM   2021  CG2 VAL C  12      23.067  17.929  43.041  1.00 79.26           C  
ANISOU 2021  CG2 VAL C  12    15577   7681   6858   -924   -264   -597       C  
ATOM   2022  N   TYR C  13      26.922  16.161  44.411  1.00 77.79           N  
ANISOU 2022  N   TYR C  13    16024   7154   6378   -837   -444   -260       N  
ATOM   2023  CA  TYR C  13      28.352  15.950  44.599  1.00 76.54           C  
ANISOU 2023  CA  TYR C  13    16079   6830   6174   -710   -532   -326       C  
ATOM   2024  C   TYR C  13      28.809  14.537  44.201  1.00 78.07           C  
ANISOU 2024  C   TYR C  13    16414   6579   6671   -810   -830   -162       C  
ATOM   2025  O   TYR C  13      29.747  14.358  43.415  1.00 76.43           O  
ANISOU 2025  O   TYR C  13    16376   6074   6588   -645   -961   -413       O  
ATOM   2026  CB  TYR C  13      28.740  16.231  46.042  1.00 77.68           C  
ANISOU 2026  CB  TYR C  13    16171   7361   5984   -671   -411   -194       C  
ATOM   2027  CG  TYR C  13      30.218  16.448  46.200  1.00 75.76           C  
ANISOU 2027  CG  TYR C  13    16109   6968   5707   -478   -495   -379       C  
ATOM   2028  CD1 TYR C  13      31.024  15.471  46.747  1.00 76.91           C  
ANISOU 2028  CD1 TYR C  13    16376   6947   5897   -533   -673   -155       C  
ATOM   2029  CD2 TYR C  13      30.811  17.640  45.791  1.00 73.19           C  
ANISOU 2029  CD2 TYR C  13    15804   6634   5373   -255   -437   -751       C  
ATOM   2030  CE1 TYR C  13      32.375  15.665  46.887  1.00 75.76           C  
ANISOU 2030  CE1 TYR C  13    16361   6652   5773   -350   -768   -341       C  
ATOM   2031  CE2 TYR C  13      32.162  17.846  45.921  1.00 71.73           C  
ANISOU 2031  CE2 TYR C  13    15722   6298   5232   -100   -524   -887       C  
ATOM   2032  CZ  TYR C  13      32.939  16.850  46.465  1.00 73.44           C  
ANISOU 2032  CZ  TYR C  13    16053   6371   5481   -137   -677   -705       C  
ATOM   2033  OH  TYR C  13      34.287  17.043  46.598  1.00 73.44           O  
ANISOU 2033  OH  TYR C  13    16122   6210   5573     24   -779   -854       O  
ATOM   2034  N   GLU C  14      28.155  13.529  44.761  1.00 81.85           N  
ANISOU 2034  N   GLU C  14    16785   7025   7291  -1071   -959    267       N  
ATOM   2035  CA  GLU C  14      28.508  12.155  44.440  1.00 84.41           C  
ANISOU 2035  CA  GLU C  14    17214   6849   8008  -1170  -1355    425       C  
ATOM   2036  C   GLU C  14      28.509  11.957  42.933  1.00 83.06           C  
ANISOU 2036  C   GLU C  14    17160   6282   8118  -1012  -1564     27       C  
ATOM   2037  O   GLU C  14      29.481  11.469  42.352  1.00 83.07           O  
ANISOU 2037  O   GLU C  14    17333   5971   8260   -821  -1785   -231       O  
ATOM   2038  CB  GLU C  14      27.526  11.177  45.075  1.00 89.06           C  
ANISOU 2038  CB  GLU C  14    17600   7413   8827  -1533  -1512   1014       C  
ATOM   2039  CG  GLU C  14      28.018  10.548  46.345  1.00 93.46           C  
ANISOU 2039  CG  GLU C  14    18153   8079   9281  -1694  -1587   1499       C  
ATOM   2040  CD  GLU C  14      27.641   9.075  46.415  1.00100.54           C  
ANISOU 2040  CD  GLU C  14    18966   8520  10716  -2016  -2051   2018       C  
ATOM   2041  OE1 GLU C  14      26.843   8.611  45.564  1.00101.90           O  
ANISOU 2041  OE1 GLU C  14    19038   8341  11338  -2121  -2288   1998       O  
ATOM   2042  OE2 GLU C  14      28.147   8.371  47.312  1.00105.06           O  
ANISOU 2042  OE2 GLU C  14    19569   9042  11308  -2165  -2241   2456       O  
ATOM   2043  N   GLN C  15      27.403  12.341  42.306  1.00 82.48           N  
ANISOU 2043  N   GLN C  15    16975   6263   8100  -1063  -1503    -45       N  
ATOM   2044  CA  GLN C  15      27.206  12.117  40.886  1.00 81.58           C  
ANISOU 2044  CA  GLN C  15    16971   5820   8207   -911  -1741   -397       C  
ATOM   2045  C   GLN C  15      28.356  12.680  40.077  1.00 78.37           C  
ANISOU 2045  C   GLN C  15    16768   5438   7571   -571  -1646   -842       C  
ATOM   2046  O   GLN C  15      28.811  12.070  39.101  1.00 79.10           O  
ANISOU 2046  O   GLN C  15    17001   5255   7799   -367  -1909  -1136       O  
ATOM   2047  CB  GLN C  15      25.917  12.775  40.432  1.00 81.30           C  
ANISOU 2047  CB  GLN C  15    16788   5927   8175   -985  -1631   -432       C  
ATOM   2048  CG  GLN C  15      24.712  12.398  41.247  1.00 84.85           C  
ANISOU 2048  CG  GLN C  15    16940   6477   8824  -1324  -1627     32       C  
ATOM   2049  CD  GLN C  15      23.467  12.486  40.416  1.00 86.73           C  
ANISOU 2049  CD  GLN C  15    17047   6581   9324  -1383  -1763    -59       C  
ATOM   2050  OE1 GLN C  15      22.532  13.216  40.736  1.00 87.55           O  
ANISOU 2050  OE1 GLN C  15    16910   7015   9338  -1480  -1514     28       O  
ATOM   2051  NE2 GLN C  15      23.460  11.763  39.308  1.00 88.21           N  
ANISOU 2051  NE2 GLN C  15    17390   6288   9837  -1276  -2195   -298       N  
ATOM   2052  N   ILE C  16      28.823  13.851  40.481  1.00 75.14           N  
ANISOU 2052  N   ILE C  16    16342   5381   6825   -494  -1290   -893       N  
ATOM   2053  CA  ILE C  16      29.874  14.513  39.744  1.00 72.67           C  
ANISOU 2053  CA  ILE C  16    16146   5137   6328   -226  -1164  -1207       C  
ATOM   2054  C   ILE C  16      31.213  13.864  40.002  1.00 73.08           C  
ANISOU 2054  C   ILE C  16    16282   5051   6435    -98  -1265  -1265       C  
ATOM   2055  O   ILE C  16      31.937  13.552  39.065  1.00 73.60           O  
ANISOU 2055  O   ILE C  16    16434   5014   6516    136  -1354  -1545       O  
ATOM   2056  CB  ILE C  16      29.980  15.974  40.105  1.00 70.32           C  
ANISOU 2056  CB  ILE C  16    15766   5169   5785   -200   -850  -1222       C  
ATOM   2057  CG1 ILE C  16      28.609  16.640  39.985  1.00 70.38           C  
ANISOU 2057  CG1 ILE C  16    15652   5310   5778   -314   -782  -1188       C  
ATOM   2058  CG2 ILE C  16      31.022  16.643  39.230  1.00 68.69           C  
ANISOU 2058  CG2 ILE C  16    15625   5014   5460     24   -743  -1439       C  
ATOM   2059  CD1 ILE C  16      28.670  18.166  39.894  1.00 68.42           C  
ANISOU 2059  CD1 ILE C  16    15336   5282   5377   -223   -593  -1311       C  
ATOM   2060  N   THR C  17      31.559  13.661  41.266  1.00 73.18           N  
ANISOU 2060  N   THR C  17    16256   5099   6451   -222  -1257  -1018       N  
ATOM   2061  CA  THR C  17      32.843  13.048  41.540  1.00 74.03           C  
ANISOU 2061  CA  THR C  17    16436   5036   6657    -96  -1401  -1082       C  
ATOM   2062  C   THR C  17      32.869  11.673  40.865  1.00 76.82           C  
ANISOU 2062  C   THR C  17    16863   4979   7345    -32  -1812  -1203       C  
ATOM   2063  O   THR C  17      33.921  11.208  40.419  1.00 77.75           O  
ANISOU 2063  O   THR C  17    17035   4945   7563    210  -1953  -1479       O  
ATOM   2064  CB  THR C  17      33.116  12.924  43.025  1.00 74.59           C  
ANISOU 2064  CB  THR C  17    16481   5186   6675   -245  -1410   -766       C  
ATOM   2065  OG1 THR C  17      32.039  12.210  43.612  1.00 78.40           O  
ANISOU 2065  OG1 THR C  17    16903   5626   7259   -524  -1550   -383       O  
ATOM   2066  CG2 THR C  17      33.181  14.258  43.657  1.00 71.87           C  
ANISOU 2066  CG2 THR C  17    16064   5219   6023   -217  -1095   -771       C  
ATOM   2067  N   ASP C  18      31.700  11.040  40.773  1.00 78.66           N  
ANISOU 2067  N   ASP C  18    17065   5028   7793   -226  -2035  -1026       N  
ATOM   2068  CA  ASP C  18      31.558   9.776  40.051  1.00 81.96           C  
ANISOU 2068  CA  ASP C  18    17537   4987   8616   -149  -2532  -1188       C  
ATOM   2069  C   ASP C  18      31.918   9.954  38.580  1.00 81.57           C  
ANISOU 2069  C   ASP C  18    17579   4970   8444    231  -2538  -1741       C  
ATOM   2070  O   ASP C  18      32.625   9.136  37.992  1.00 83.82           O  
ANISOU 2070  O   ASP C  18    17927   5016   8906    510  -2855  -2093       O  
ATOM   2071  CB  ASP C  18      30.126   9.243  40.170  1.00 84.35           C  
ANISOU 2071  CB  ASP C  18    17735   5093   9221   -453  -2769   -865       C  
ATOM   2072  CG  ASP C  18      29.930   8.363  41.388  1.00 88.05           C  
ANISOU 2072  CG  ASP C  18    18104   5359   9991   -793  -3015   -302       C  
ATOM   2073  OD1 ASP C  18      28.817   7.818  41.549  1.00 91.69           O  
ANISOU 2073  OD1 ASP C  18    18416   5644  10777  -1085  -3235     60       O  
ATOM   2074  OD2 ASP C  18      30.891   8.203  42.179  1.00 88.63           O  
ANISOU 2074  OD2 ASP C  18    18229   5449   9996   -779  -3012   -182       O  
ATOM   2075  N   LEU C  19      31.424  11.036  37.990  1.00 79.21           N  
ANISOU 2075  N   LEU C  19    17273   5001   7821    263  -2201  -1819       N  
ATOM   2076  CA  LEU C  19      31.683  11.320  36.587  1.00 79.49           C  
ANISOU 2076  CA  LEU C  19    17392   5181   7630    603  -2158  -2253       C  
ATOM   2077  C   LEU C  19      33.152  11.539  36.294  1.00 79.25           C  
ANISOU 2077  C   LEU C  19    17361   5367   7384    901  -1962  -2498       C  
ATOM   2078  O   LEU C  19      33.661  11.095  35.276  1.00 81.93           O  
ANISOU 2078  O   LEU C  19    17745   5742   7641   1255  -2091  -2905       O  
ATOM   2079  CB  LEU C  19      30.881  12.526  36.137  1.00 77.25           C  
ANISOU 2079  CB  LEU C  19    17091   5201   7059    527  -1854  -2184       C  
ATOM   2080  CG  LEU C  19      29.519  12.128  35.579  1.00 78.89           C  
ANISOU 2080  CG  LEU C  19    17321   5191   7461    447  -2156  -2219       C  
ATOM   2081  CD1 LEU C  19      28.689  13.362  35.276  1.00 76.29           C  
ANISOU 2081  CD1 LEU C  19    16955   5131   6900    348  -1886  -2126       C  
ATOM   2082  CD2 LEU C  19      29.712  11.275  34.346  1.00 81.65           C  
ANISOU 2082  CD2 LEU C  19    17806   5367   7851    807  -2537  -2683       C  
ATOM   2083  N   VAL C  20      33.830  12.235  37.188  1.00 76.89           N  
ANISOU 2083  N   VAL C  20    16982   5242   6991    783  -1661  -2269       N  
ATOM   2084  CA  VAL C  20      35.256  12.437  37.045  1.00 77.11           C  
ANISOU 2084  CA  VAL C  20    16945   5443   6911   1023  -1487  -2441       C  
ATOM   2085  C   VAL C  20      35.932  11.080  36.993  1.00 80.85           C  
ANISOU 2085  C   VAL C  20    17443   5603   7673   1239  -1884  -2718       C  
ATOM   2086  O   VAL C  20      36.699  10.792  36.069  1.00 83.36           O  
ANISOU 2086  O   VAL C  20    17725   6054   7893   1608  -1896  -3117       O  
ATOM   2087  CB  VAL C  20      35.819  13.250  38.212  1.00 74.37           C  
ANISOU 2087  CB  VAL C  20    16506   5207   6545    842  -1241  -2151       C  
ATOM   2088  CG1 VAL C  20      37.244  13.681  37.911  1.00 74.37           C  
ANISOU 2088  CG1 VAL C  20    16377   5414   6468   1071  -1026  -2298       C  
ATOM   2089  CG2 VAL C  20      34.934  14.444  38.461  1.00 71.40           C  
ANISOU 2089  CG2 VAL C  20    16101   5036   5994    624   -994  -1912       C  
ATOM   2090  N   THR C  21      35.637  10.241  37.981  1.00 82.05           N  
ANISOU 2090  N   THR C  21    17632   5360   8181   1020  -2227  -2498       N  
ATOM   2091  CA  THR C  21      36.174   8.899  37.994  1.00 86.25           C  
ANISOU 2091  CA  THR C  21    18185   5480   9105   1193  -2730  -2729       C  
ATOM   2092  C   THR C  21      35.918   8.253  36.639  1.00 89.93           C  
ANISOU 2092  C   THR C  21    18700   5863   9608   1543  -3022  -3239       C  
ATOM   2093  O   THR C  21      36.848   7.836  35.954  1.00 92.54           O  
ANISOU 2093  O   THR C  21    18987   6256   9919   1961  -3121  -3722       O  
ATOM   2094  CB  THR C  21      35.509   8.039  39.068  1.00 87.68           C  
ANISOU 2094  CB  THR C  21    18401   5214   9700    837  -3142  -2309       C  
ATOM   2095  OG1 THR C  21      35.766   8.590  40.359  1.00 85.24           O  
ANISOU 2095  OG1 THR C  21    18063   5054   9271    570  -2894  -1870       O  
ATOM   2096  CG2 THR C  21      36.049   6.624  39.015  1.00 92.07           C  
ANISOU 2096  CG2 THR C  21    18972   5244  10766   1017  -3780  -2549       C  
ATOM   2097  N   ILE C  22      34.647   8.180  36.258  1.00 90.76           N  
ANISOU 2097  N   ILE C  22    18872   5854   9757   1402  -3173  -3163       N  
ATOM   2098  CA  ILE C  22      34.265   7.524  35.012  1.00 95.10           C  
ANISOU 2098  CA  ILE C  22    19492   6277  10366   1745  -3555  -3669       C  
ATOM   2099  C   ILE C  22      35.187   7.952  33.880  1.00 96.65           C  
ANISOU 2099  C   ILE C  22    19669   6985  10070   2241  -3256  -4174       C  
ATOM   2100  O   ILE C  22      35.695   7.113  33.126  1.00100.86           O  
ANISOU 2100  O   ILE C  22    20203   7445  10672   2700  -3608  -4747       O  
ATOM   2101  CB  ILE C  22      32.821   7.872  34.595  1.00 94.29           C  
ANISOU 2101  CB  ILE C  22    19448   6165  10215   1547  -3576  -3518       C  
ATOM   2102  CG1 ILE C  22      31.813   7.384  35.637  1.00 94.30           C  
ANISOU 2102  CG1 ILE C  22    19393   5723  10713   1057  -3860  -2987       C  
ATOM   2103  CG2 ILE C  22      32.515   7.267  33.248  1.00 97.94           C  
ANISOU 2103  CG2 ILE C  22    20004   6534  10676   1971  -3994  -4109       C  
ATOM   2104  CD1 ILE C  22      31.697   5.902  35.709  1.00 98.12           C  
ANISOU 2104  CD1 ILE C  22    19869   5548  11864   1088  -4629  -3096       C  
ATOM   2105  N   ARG C  23      35.395   9.263  33.770  1.00 93.74           N  
ANISOU 2105  N   ARG C  23    19252   7150   9216   2157  -2627  -3948       N  
ATOM   2106  CA  ARG C  23      36.160   9.829  32.671  1.00 95.83           C  
ANISOU 2106  CA  ARG C  23    19451   8003   8958   2548  -2262  -4258       C  
ATOM   2107  C   ARG C  23      37.617   9.367  32.676  1.00 98.54           C  
ANISOU 2107  C   ARG C  23    19633   8468   9338   2890  -2235  -4576       C  
ATOM   2108  O   ARG C  23      38.058   8.685  31.739  1.00103.25           O  
ANISOU 2108  O   ARG C  23    20202   9217   9813   3393  -2434  -5153       O  
ATOM   2109  CB  ARG C  23      36.095  11.347  32.716  1.00 92.38           C  
ANISOU 2109  CB  ARG C  23    18953   8008   8140   2299  -1668  -3822       C  
ATOM   2110  CG  ARG C  23      34.685  11.928  32.792  1.00 91.66           C  
ANISOU 2110  CG  ARG C  23    18977   7812   8036   1964  -1674  -3516       C  
ATOM   2111  CD  ARG C  23      34.062  12.034  31.408  1.00 97.13           C  
ANISOU 2111  CD  ARG C  23    19785   8751   8371   2222  -1739  -3786       C  
ATOM   2112  NE  ARG C  23      33.315  13.267  31.224  1.00 96.45           N  
ANISOU 2112  NE  ARG C  23    19717   8883   8046   1975  -1455  -3438       N  
ATOM   2113  CZ  ARG C  23      32.394  13.498  30.289  1.00 98.38           C  
ANISOU 2113  CZ  ARG C  23    20090   9221   8068   2050  -1571  -3529       C  
ATOM   2114  NH1 ARG C  23      32.029  12.568  29.422  1.00101.89           N  
ANISOU 2114  NH1 ARG C  23    20672   9565   8477   2382  -1984  -3986       N  
ATOM   2115  NH2 ARG C  23      31.819  14.690  30.249  1.00 96.62           N  
ANISOU 2115  NH2 ARG C  23    19856   9159   7696   1804  -1329  -3180       N  
ATOM   2116  N   LYS C  24      38.368   9.730  33.715  1.00 95.99           N  
ANISOU 2116  N   LYS C  24    19189   8100   9183   2663  -2019  -4253       N  
ATOM   2117  CA  LYS C  24      39.753   9.277  33.805  1.00 98.89           C  
ANISOU 2117  CA  LYS C  24    19370   8530   9672   2968  -2029  -4545       C  
ATOM   2118  C   LYS C  24      39.842   7.828  33.354  1.00104.23           C  
ANISOU 2118  C   LYS C  24    20091   8865  10647   3374  -2651  -5152       C  
ATOM   2119  O   LYS C  24      40.763   7.425  32.648  1.00108.40           O  
ANISOU 2119  O   LYS C  24    20460   9671  11056   3875  -2658  -5681       O  
ATOM   2120  CB  LYS C  24      40.257   9.374  35.234  1.00 96.17           C  
ANISOU 2120  CB  LYS C  24    18976   7873   9691   2638  -2041  -4163       C  
ATOM   2121  CG  LYS C  24      40.201  10.764  35.802  1.00 92.03           C  
ANISOU 2121  CG  LYS C  24    18399   7608   8960   2281  -1546  -3641       C  
ATOM   2122  CD  LYS C  24      41.093  10.884  37.010  1.00 91.26           C  
ANISOU 2122  CD  LYS C  24    18201   7331   9142   2131  -1544  -3426       C  
ATOM   2123  CE  LYS C  24      40.616  12.020  37.859  1.00 88.66           C  
ANISOU 2123  CE  LYS C  24    17904   7062   8718   1737  -1287  -2934       C  
ATOM   2124  NZ  LYS C  24      41.592  12.356  38.915  1.00 89.43           N  
ANISOU 2124  NZ  LYS C  24    17887   7078   9015   1655  -1255  -2770       N  
ATOM   2125  N   GLN C  25      38.858   7.054  33.783  1.00104.68           N  
ANISOU 2125  N   GLN C  25    20330   8315  11129   3158  -3199  -5066       N  
ATOM   2126  CA  GLN C  25      38.785   5.643  33.490  1.00110.06           C  
ANISOU 2126  CA  GLN C  25    21059   8490  12268   3470  -3951  -5578       C  
ATOM   2127  C   GLN C  25      38.555   5.406  31.999  1.00114.37           C  
ANISOU 2127  C   GLN C  25    21639   9357  12460   4013  -4071  -6237       C  
ATOM   2128  O   GLN C  25      38.736   4.295  31.502  1.00119.82           O  
ANISOU 2128  O   GLN C  25    22325   9758  13443   4464  -4688  -6876       O  
ATOM   2129  CB  GLN C  25      37.660   5.023  34.319  1.00109.53           C  
ANISOU 2129  CB  GLN C  25    21135   7717  12763   3006  -4475  -5157       C  
ATOM   2130  CG  GLN C  25      37.842   3.558  34.605  1.00115.18           C  
ANISOU 2130  CG  GLN C  25    21847   7706  14210   3142  -5332  -5429       C  
ATOM   2131  CD  GLN C  25      37.192   3.127  35.910  1.00114.64           C  
ANISOU 2131  CD  GLN C  25    21827   7036  14697   2541  -5675  -4715       C  
ATOM   2132  OE1 GLN C  25      36.901   3.947  36.781  1.00109.19           O  
ANISOU 2132  OE1 GLN C  25    21148   6558  13783   2077  -5194  -4066       O  
ATOM   2133  NE2 GLN C  25      36.970   1.818  36.050  1.00120.43           N  
ANISOU 2133  NE2 GLN C  25    22565   7026  16165   2565  -6547  -4832       N  
ATOM   2134  N   GLU C  26      38.156   6.455  31.286  1.00112.44           N  
ANISOU 2134  N   GLU C  26    21430   9708  11585   3995  -3531  -6097       N  
ATOM   2135  CA  GLU C  26      37.959   6.359  29.840  1.00116.83           C  
ANISOU 2135  CA  GLU C  26    22034  10702  11653   4527  -3581  -6677       C  
ATOM   2136  C   GLU C  26      39.115   7.010  29.084  1.00118.94           C  
ANISOU 2136  C   GLU C  26    22082  11862  11247   4927  -2948  -6882       C  
ATOM   2137  O   GLU C  26      38.953   7.451  27.945  1.00121.36           O  
ANISOU 2137  O   GLU C  26    22411  12800  10901   5235  -2691  -7080       O  
ATOM   2138  CB  GLU C  26      36.645   7.024  29.432  1.00114.28           C  
ANISOU 2138  CB  GLU C  26    21903  10447  11069   4260  -3484  -6374       C  
ATOM   2139  CG  GLU C  26      35.408   6.279  29.867  1.00114.34           C  
ANISOU 2139  CG  GLU C  26    22071   9664  11711   3968  -4150  -6272       C  
ATOM   2140  CD  GLU C  26      34.162   7.132  29.767  1.00111.36           C  
ANISOU 2140  CD  GLU C  26    21815   9349  11150   3580  -3942  -5824       C  
ATOM   2141  OE1 GLU C  26      34.232   8.337  30.080  1.00107.83           O  
ANISOU 2141  OE1 GLU C  26    21319   9299  10351   3268  -3300  -5323       O  
ATOM   2142  OE2 GLU C  26      33.103   6.602  29.394  1.00113.59           O  
ANISOU 2142  OE2 GLU C  26    22218   9239  11702   3589  -4471  -5984       O  
ATOM   2143  N   GLY C  27      40.279   7.074  29.725  1.00118.50           N  
ANISOU 2143  N   GLY C  27    21793  11879  11353   4912  -2705  -6790       N  
ATOM   2144  CA  GLY C  27      41.443   7.734  29.139  1.00120.56           C  
ANISOU 2144  CA  GLY C  27    21752  12984  11071   5214  -2062  -6862       C  
ATOM   2145  C   GLY C  27      41.450   9.244  29.341  1.00115.73           C  
ANISOU 2145  C   GLY C  27    21061  12794  10119   4746  -1343  -6093       C  
ATOM   2146  O   GLY C  27      42.515   9.864  29.338  1.00116.33           O  
ANISOU 2146  O   GLY C  27    20825  13359  10017   4782   -835  -5911       O  
ATOM   2147  N   ILE C  28      40.266   9.836  29.515  1.00111.33           N  
ANISOU 2147  N   ILE C  28    20747  12022   9532   4314  -1342  -5650       N  
ATOM   2148  CA  ILE C  28      40.141  11.295  29.657  1.00107.18           C  
ANISOU 2148  CA  ILE C  28    20159  11825   8740   3890   -772  -4966       C  
ATOM   2149  C   ILE C  28      40.977  11.824  30.825  1.00103.73           C  
ANISOU 2149  C   ILE C  28    19517  11227   8669   3551   -529  -4541       C  
ATOM   2150  O   ILE C  28      40.470  12.460  31.739  1.00 98.62           O  
ANISOU 2150  O   ILE C  28    18957  10254   8260   3075   -496  -4062       O  
ATOM   2151  CB  ILE C  28      38.666  11.763  29.792  1.00103.25           C  
ANISOU 2151  CB  ILE C  28    19942  11022   8266   3493   -907  -4627       C  
ATOM   2152  CG1 ILE C  28      37.806  11.121  28.707  1.00106.80           C  
ANISOU 2152  CG1 ILE C  28    20608  11512   8458   3838  -1274  -5095       C  
ATOM   2153  CG2 ILE C  28      38.572  13.271  29.700  1.00 99.98           C  
ANISOU 2153  CG2 ILE C  28    19444  10992   7554   3167   -389  -4030       C  
ATOM   2154  CD1 ILE C  28      38.502  11.008  27.360  1.00112.89           C  
ANISOU 2154  CD1 ILE C  28    21264  13049   8582   4441  -1076  -5543       C  
ATOM   2155  N   GLU C  29      42.267  11.518  30.771  1.00107.10           N  
ANISOU 2155  N   GLU C  29    19655  11902   9137   3853   -395  -4783       N  
ATOM   2156  CA  GLU C  29      43.273  12.043  31.680  1.00105.28           C  
ANISOU 2156  CA  GLU C  29    19165  11616   9219   3630   -153  -4447       C  
ATOM   2157  C   GLU C  29      42.829  13.262  32.475  1.00 99.62           C  
ANISOU 2157  C   GLU C  29    18499  10733   8619   3072     53  -3776       C  
ATOM   2158  O   GLU C  29      42.606  13.179  33.679  1.00 96.00           O  
ANISOU 2158  O   GLU C  29    18166   9737   8574   2767   -188  -3596       O  
ATOM   2159  CB  GLU C  29      44.507  12.433  30.866  1.00110.25           C  
ANISOU 2159  CB  GLU C  29    19366  13002   9520   3955    339  -4509       C  
ATOM   2160  CG  GLU C  29      45.632  13.036  31.685  1.00110.01           C  
ANISOU 2160  CG  GLU C  29    18997  12942   9860   3746    584  -4162       C  
ATOM   2161  CD  GLU C  29      46.707  12.017  32.022  1.00114.56           C  
ANISOU 2161  CD  GLU C  29    19364  13362  10801   4095    353  -4655       C  
ATOM   2162  OE1 GLU C  29      47.179  11.299  31.092  1.00120.10           O  
ANISOU 2162  OE1 GLU C  29    19891  14505  11237   4641    374  -5215       O  
ATOM   2163  OE2 GLU C  29      47.076  11.947  33.216  1.00112.02           O  
ANISOU 2163  OE2 GLU C  29    19048  12496  11019   3853    127  -4508       O  
ATOM   2164  N   GLU C  30      42.721  14.394  31.780  1.00 99.46           N  
ANISOU 2164  N   GLU C  30    18365  11206   8219   2967    474  -3416       N  
ATOM   2165  CA  GLU C  30      42.543  15.707  32.399  1.00 95.17           C  
ANISOU 2165  CA  GLU C  30    17766  10573   7819   2510    672  -2816       C  
ATOM   2166  C   GLU C  30      41.176  15.942  33.038  1.00 90.03           C  
ANISOU 2166  C   GLU C  30    17449   9467   7290   2167    418  -2644       C  
ATOM   2167  O   GLU C  30      40.832  17.074  33.372  1.00 87.54           O  
ANISOU 2167  O   GLU C  30    17107   9121   7034   1852    541  -2230       O  
ATOM   2168  CB  GLU C  30      42.816  16.813  31.375  1.00 97.84           C  
ANISOU 2168  CB  GLU C  30    17860  11547   7766   2497   1126  -2440       C  
ATOM   2169  CG  GLU C  30      41.864  16.799  30.189  1.00100.69           C  
ANISOU 2169  CG  GLU C  30    18433  12246   7578   2640   1146  -2523       C  
ATOM   2170  CD  GLU C  30      42.064  15.565  29.280  1.00107.52           C  
ANISOU 2170  CD  GLU C  30    19342  13433   8080   3194   1051  -3163       C  
ATOM   2171  OE1 GLU C  30      43.121  14.899  29.380  1.00110.40           O  
ANISOU 2171  OE1 GLU C  30    19473  13912   8563   3487   1084  -3483       O  
ATOM   2172  OE2 GLU C  30      41.168  15.259  28.455  1.00109.74           O  
ANISOU 2172  OE2 GLU C  30    19878  13841   7976   3374    897  -3394       O  
ATOM   2173  N   ALA C  31      40.393  14.891  33.224  1.00 88.91           N  
ANISOU 2173  N   ALA C  31    17581   8966   7234   2231     36  -2956       N  
ATOM   2174  CA  ALA C  31      39.098  15.070  33.855  1.00 84.72           C  
ANISOU 2174  CA  ALA C  31    17294   8065   6831   1903   -170  -2766       C  
ATOM   2175  C   ALA C  31      39.281  15.617  35.273  1.00 81.10           C  
ANISOU 2175  C   ALA C  31    16784   7325   6705   1584   -172  -2455       C  
ATOM   2176  O   ALA C  31      40.165  15.185  36.024  1.00 81.37           O  
ANISOU 2176  O   ALA C  31    16731   7189   6999   1626   -262  -2515       O  
ATOM   2177  CB  ALA C  31      38.318  13.774  33.865  1.00 85.63           C  
ANISOU 2177  CB  ALA C  31    17639   7812   7082   1997   -613  -3089       C  
ATOM   2178  N   SER C  32      38.453  16.581  35.639  1.00 77.81           N  
ANISOU 2178  N   SER C  32    16418   6873   6275   1303   -109  -2161       N  
ATOM   2179  CA  SER C  32      38.542  17.126  36.979  1.00 75.14           C  
ANISOU 2179  CA  SER C  32    16039   6324   6186   1069   -148  -1944       C  
ATOM   2180  C   SER C  32      37.193  17.581  37.484  1.00 72.68           C  
ANISOU 2180  C   SER C  32    15859   5901   5856    829   -230  -1798       C  
ATOM   2181  O   SER C  32      36.236  17.693  36.723  1.00 72.69           O  
ANISOU 2181  O   SER C  32    15950   5975   5695    809   -229  -1813       O  
ATOM   2182  CB  SER C  32      39.522  18.296  37.040  1.00 75.26           C  
ANISOU 2182  CB  SER C  32    15794   6508   6294   1036     73  -1733       C  
ATOM   2183  OG  SER C  32      38.865  19.522  36.772  1.00 74.10           O  
ANISOU 2183  OG  SER C  32    15611   6461   6084    869    167  -1496       O  
ATOM   2184  N   LEU C  33      37.129  17.833  38.783  1.00 71.06           N  
ANISOU 2184  N   LEU C  33    15649   5551   5802    678   -311  -1683       N  
ATOM   2185  CA  LEU C  33      35.915  18.303  39.413  1.00 69.61           C  
ANISOU 2185  CA  LEU C  33    15522   5346   5580    490   -357  -1574       C  
ATOM   2186  C   LEU C  33      35.389  19.555  38.709  1.00 68.81           C  
ANISOU 2186  C   LEU C  33    15345   5395   5405    445   -235  -1501       C  
ATOM   2187  O   LEU C  33      34.307  19.550  38.123  1.00 68.75           O  
ANISOU 2187  O   LEU C  33    15415   5412   5294    394   -258  -1515       O  
ATOM   2188  CB  LEU C  33      36.195  18.637  40.869  1.00 68.98           C  
ANISOU 2188  CB  LEU C  33    15399   5222   5589    421   -424  -1498       C  
ATOM   2189  CG  LEU C  33      35.151  17.994  41.765  1.00 70.11           C  
ANISOU 2189  CG  LEU C  33    15641   5341   5655    282   -536  -1414       C  
ATOM   2190  CD1 LEU C  33      35.051  18.745  43.080  1.00 70.80           C  
ANISOU 2190  CD1 LEU C  33    15666   5560   5676    250   -546  -1364       C  
ATOM   2191  CD2 LEU C  33      33.823  17.983  41.049  1.00 71.30           C  
ANISOU 2191  CD2 LEU C  33    15823   5536   5732    192   -509  -1406       C  
ATOM   2192  N   SER C  34      36.169  20.625  38.757  1.00 68.51           N  
ANISOU 2192  N   SER C  34    15138   5412   5481    454   -158  -1402       N  
ATOM   2193  CA  SER C  34      35.735  21.877  38.179  1.00 68.39           C  
ANISOU 2193  CA  SER C  34    15028   5470   5488    384   -126  -1274       C  
ATOM   2194  C   SER C  34      35.458  21.631  36.721  1.00 69.55           C  
ANISOU 2194  C   SER C  34    15241   5777   5407    439    -22  -1244       C  
ATOM   2195  O   SER C  34      34.374  21.875  36.209  1.00 69.15           O  
ANISOU 2195  O   SER C  34    15278   5741   5254    384    -78  -1241       O  
ATOM   2196  CB  SER C  34      36.816  22.952  38.360  1.00 69.36           C  
ANISOU 2196  CB  SER C  34    14913   5567   5874    376   -123  -1116       C  
ATOM   2197  OG  SER C  34      37.398  23.352  37.136  1.00 71.08           O  
ANISOU 2197  OG  SER C  34    14994   5956   6058    386     34   -897       O  
ATOM   2198  N   ASN C  35      36.496  21.146  36.072  1.00 71.61           N  
ANISOU 2198  N   ASN C  35    15442   6189   5577    583    117  -1247       N  
ATOM   2199  CA  ASN C  35      36.463  20.638  34.724  1.00 73.85           C  
ANISOU 2199  CA  ASN C  35    15794   6720   5545    741    221  -1310       C  
ATOM   2200  C   ASN C  35      35.121  20.028  34.287  1.00 73.61           C  
ANISOU 2200  C   ASN C  35    16006   6617   5347    755     58  -1490       C  
ATOM   2201  O   ASN C  35      34.538  20.443  33.292  1.00 74.45           O  
ANISOU 2201  O   ASN C  35    16169   6880   5239    772     69  -1425       O  
ATOM   2202  CB  ASN C  35      37.540  19.584  34.674  1.00 75.72           C  
ANISOU 2202  CB  ASN C  35    15986   7029   5754    959    281  -1512       C  
ATOM   2203  CG  ASN C  35      37.708  19.048  33.369  1.00 78.64           C  
ANISOU 2203  CG  ASN C  35    16383   7724   5773   1210    385  -1661       C  
ATOM   2204  OD1 ASN C  35      37.617  19.780  32.410  1.00 81.16           O  
ANISOU 2204  OD1 ASN C  35    16641   8357   5841   1215    544  -1457       O  
ATOM   2205  ND2 ASN C  35      37.954  17.757  33.283  1.00 81.27           N  
ANISOU 2205  ND2 ASN C  35    16804   8003   6073   1447    258  -2026       N  
ATOM   2206  N   VAL C  36      34.636  19.040  35.041  1.00 72.68           N  
ANISOU 2206  N   VAL C  36    16013   6246   5356    733   -126  -1676       N  
ATOM   2207  CA  VAL C  36      33.373  18.369  34.732  1.00 72.60           C  
ANISOU 2207  CA  VAL C  36    16177   6098   5309    716   -333  -1818       C  
ATOM   2208  C   VAL C  36      32.149  19.193  35.082  1.00 70.92           C  
ANISOU 2208  C   VAL C  36    15955   5810   5183    501   -385  -1685       C  
ATOM   2209  O   VAL C  36      31.174  19.195  34.332  1.00 71.96           O  
ANISOU 2209  O   VAL C  36    16177   5931   5235    503   -500  -1739       O  
ATOM   2210  CB  VAL C  36      33.238  17.025  35.460  1.00 72.86           C  
ANISOU 2210  CB  VAL C  36    16289   5852   5540    710   -557  -1960       C  
ATOM   2211  CG1 VAL C  36      31.785  16.586  35.487  1.00 72.49           C  
ANISOU 2211  CG1 VAL C  36    16331   5609   5603    574   -783  -1972       C  
ATOM   2212  CG2 VAL C  36      34.089  15.973  34.793  1.00 75.10           C  
ANISOU 2212  CG2 VAL C  36    16619   6148   5767    997   -648  -2234       C  
ATOM   2213  N   SER C  37      32.187  19.884  36.212  1.00 68.94           N  
ANISOU 2213  N   SER C  37    15584   5515   5096    355   -336  -1558       N  
ATOM   2214  CA  SER C  37      31.065  20.736  36.590  1.00 67.84           C  
ANISOU 2214  CA  SER C  37    15383   5350   5043    210   -391  -1504       C  
ATOM   2215  C   SER C  37      30.840  21.810  35.541  1.00 68.51           C  
ANISOU 2215  C   SER C  37    15447   5520   5065    220   -391  -1416       C  
ATOM   2216  O   SER C  37      29.714  22.202  35.275  1.00 68.65           O  
ANISOU 2216  O   SER C  37    15474   5491   5119    155   -509  -1438       O  
ATOM   2217  CB  SER C  37      31.308  21.397  37.941  1.00 66.58           C  
ANISOU 2217  CB  SER C  37    15081   5194   5021    145   -363  -1463       C  
ATOM   2218  OG  SER C  37      31.914  20.500  38.845  1.00 66.13           O  
ANISOU 2218  OG  SER C  37    15052   5100   4976    156   -354  -1473       O  
ATOM   2219  N   SER C  38      31.924  22.300  34.961  1.00 69.68           N  
ANISOU 2219  N   SER C  38    15535   5798   5141    287   -271  -1275       N  
ATOM   2220  CA  SER C  38      31.827  23.330  33.944  1.00 71.23           C  
ANISOU 2220  CA  SER C  38    15692   6103   5271    263   -280  -1070       C  
ATOM   2221  C   SER C  38      31.026  22.752  32.788  1.00 73.02           C  
ANISOU 2221  C   SER C  38    16113   6412   5218    353   -357  -1170       C  
ATOM   2222  O   SER C  38      30.028  23.329  32.344  1.00 73.27           O  
ANISOU 2222  O   SER C  38    16185   6383   5270    287   -517  -1132       O  
ATOM   2223  CB  SER C  38      33.224  23.740  33.488  1.00 72.96           C  
ANISOU 2223  CB  SER C  38    15764   6518   5439    307    -95   -823       C  
ATOM   2224  OG  SER C  38      33.163  24.568  32.349  1.00 75.61           O  
ANISOU 2224  OG  SER C  38    16064   7028   5637    271    -88   -528       O  
ATOM   2225  N   MET C  39      31.449  21.587  32.312  1.00 74.50           N  
ANISOU 2225  N   MET C  39    16417   6713   5175    538   -302  -1349       N  
ATOM   2226  CA  MET C  39      30.751  20.947  31.229  1.00 76.62           C  
ANISOU 2226  CA  MET C  39    16882   7047   5185    689   -447  -1529       C  
ATOM   2227  C   MET C  39      29.281  20.758  31.592  1.00 75.26           C  
ANISOU 2227  C   MET C  39    16778   6576   5244    560   -706  -1657       C  
ATOM   2228  O   MET C  39      28.407  20.925  30.743  1.00 76.80           O  
ANISOU 2228  O   MET C  39    17081   6765   5335    593   -884  -1697       O  
ATOM   2229  CB  MET C  39      31.418  19.620  30.870  1.00 78.74           C  
ANISOU 2229  CB  MET C  39    17239   7411   5267    956   -442  -1817       C  
ATOM   2230  CG  MET C  39      30.621  18.755  29.895  1.00 82.39           C  
ANISOU 2230  CG  MET C  39    17915   7851   5539   1167   -717  -2129       C  
ATOM   2231  SD  MET C  39      29.397  17.689  30.734  1.00 84.74           S  
ANISOU 2231  SD  MET C  39    18278   7614   6304   1025  -1092  -2342       S  
ATOM   2232  CE  MET C  39      30.367  16.209  31.014  1.00 85.09           C  
ANISOU 2232  CE  MET C  39    18340   7549   6441   1246  -1195  -2636       C  
ATOM   2233  N   LEU C  40      29.001  20.418  32.844  1.00 72.98           N  
ANISOU 2233  N   LEU C  40    16401   6073   5255    417   -727  -1697       N  
ATOM   2234  CA  LEU C  40      27.625  20.188  33.251  1.00 72.44           C  
ANISOU 2234  CA  LEU C  40    16315   5792   5416    281   -921  -1768       C  
ATOM   2235  C   LEU C  40      26.824  21.478  33.281  1.00 72.06           C  
ANISOU 2235  C   LEU C  40    16159   5742   5478    162   -961  -1669       C  
ATOM   2236  O   LEU C  40      25.637  21.479  32.966  1.00 72.81           O  
ANISOU 2236  O   LEU C  40    16260   5720   5684    117  -1156  -1745       O  
ATOM   2237  CB  LEU C  40      27.570  19.518  34.610  1.00 71.24           C  
ANISOU 2237  CB  LEU C  40    16057   5522   5490    152   -890  -1753       C  
ATOM   2238  CG  LEU C  40      27.959  18.047  34.640  1.00 72.85           C  
ANISOU 2238  CG  LEU C  40    16357   5582   5739    227  -1011  -1858       C  
ATOM   2239  CD1 LEU C  40      27.772  17.499  36.049  1.00 72.54           C  
ANISOU 2239  CD1 LEU C  40    16194   5445   5923     37  -1001  -1716       C  
ATOM   2240  CD2 LEU C  40      27.149  17.239  33.629  1.00 74.50           C  
ANISOU 2240  CD2 LEU C  40    16696   5616   5995    320  -1323  -2046       C  
ATOM   2241  N   LEU C  41      27.468  22.571  33.679  1.00 71.41           N  
ANISOU 2241  N   LEU C  41    15953   5745   5434    120   -834  -1519       N  
ATOM   2242  CA  LEU C  41      26.823  23.877  33.719  1.00 71.51           C  
ANISOU 2242  CA  LEU C  41    15841   5703   5626     38   -955  -1455       C  
ATOM   2243  C   LEU C  41      26.473  24.291  32.300  1.00 74.03           C  
ANISOU 2243  C   LEU C  41    16292   6043   5793     80  -1110  -1358       C  
ATOM   2244  O   LEU C  41      25.355  24.722  32.006  1.00 74.69           O  
ANISOU 2244  O   LEU C  41    16363   6001   6013     38  -1334  -1416       O  
ATOM   2245  CB  LEU C  41      27.765  24.912  34.311  1.00 70.64           C  
ANISOU 2245  CB  LEU C  41    15575   5617   5650     13   -882  -1314       C  
ATOM   2246  CG  LEU C  41      27.903  24.944  35.827  1.00 68.74           C  
ANISOU 2246  CG  LEU C  41    15178   5364   5577     -2   -822  -1444       C  
ATOM   2247  CD1 LEU C  41      28.920  26.005  36.250  1.00 67.51           C  
ANISOU 2247  CD1 LEU C  41    14876   5171   5604      9   -849  -1335       C  
ATOM   2248  CD2 LEU C  41      26.562  25.218  36.466  1.00 67.46           C  
ANISOU 2248  CD2 LEU C  41    14883   5174   5575    -31   -943  -1637       C  
ATOM   2249  N   GLU C  42      27.451  24.163  31.417  1.00 76.03           N  
ANISOU 2249  N   GLU C  42    16655   6496   5738    179   -989  -1203       N  
ATOM   2250  CA  GLU C  42      27.249  24.493  30.032  1.00 79.39           C  
ANISOU 2250  CA  GLU C  42    17220   7056   5887    248  -1104  -1063       C  
ATOM   2251  C   GLU C  42      26.004  23.750  29.576  1.00 80.12           C  
ANISOU 2251  C   GLU C  42    17476   7012   5956    317  -1353  -1339       C  
ATOM   2252  O   GLU C  42      25.107  24.330  28.965  1.00 81.29           O  
ANISOU 2252  O   GLU C  42    17673   7069   6145    288  -1604  -1303       O  
ATOM   2253  CB  GLU C  42      28.458  24.031  29.230  1.00 81.90           C  
ANISOU 2253  CB  GLU C  42    17616   7735   5767    417   -871   -949       C  
ATOM   2254  CG  GLU C  42      28.975  25.031  28.224  1.00 86.09           C  
ANISOU 2254  CG  GLU C  42    18113   8546   6052    395   -820   -517       C  
ATOM   2255  CD  GLU C  42      30.493  25.044  28.176  1.00 89.06           C  
ANISOU 2255  CD  GLU C  42    18332   9252   6257    441   -476   -274       C  
ATOM   2256  OE1 GLU C  42      31.112  24.916  29.259  1.00 87.23           O  
ANISOU 2256  OE1 GLU C  42    17946   8869   6330    379   -355   -347       O  
ATOM   2257  OE2 GLU C  42      31.064  25.182  27.068  1.00 93.47           O  
ANISOU 2257  OE2 GLU C  42    18898  10253   6362    547   -326     -3       O  
ATOM   2258  N   LEU C  43      25.952  22.463  29.898  1.00 80.01           N  
ANISOU 2258  N   LEU C  43    17524   6934   5943    400  -1340  -1602       N  
ATOM   2259  CA  LEU C  43      24.862  21.599  29.458  1.00 81.73           C  
ANISOU 2259  CA  LEU C  43    17867   6967   6220    468  -1633  -1863       C  
ATOM   2260  C   LEU C  43      23.537  22.084  30.031  1.00 81.33           C  
ANISOU 2260  C   LEU C  43    17656   6662   6584    278  -1813  -1886       C  
ATOM   2261  O   LEU C  43      22.544  22.202  29.308  1.00 82.87           O  
ANISOU 2261  O   LEU C  43    17923   6732   6832    303  -2106  -1972       O  
ATOM   2262  CB  LEU C  43      25.138  20.152  29.874  1.00 81.46           C  
ANISOU 2262  CB  LEU C  43    17867   6830   6253    549  -1644  -2083       C  
ATOM   2263  CG  LEU C  43      24.517  18.995  29.082  1.00 83.73           C  
ANISOU 2263  CG  LEU C  43    18328   6950   6534    731  -2006  -2391       C  
ATOM   2264  CD1 LEU C  43      23.349  18.346  29.804  1.00 82.99           C  
ANISOU 2264  CD1 LEU C  43    18096   6475   6960    538  -2247  -2454       C  
ATOM   2265  CD2 LEU C  43      24.118  19.437  27.678  1.00 86.22           C  
ANISOU 2265  CD2 LEU C  43    18843   7407   6509    920  -2216  -2458       C  
ATOM   2266  N   GLY C  44      23.536  22.381  31.327  1.00 79.82           N  
ANISOU 2266  N   GLY C  44    17233   6431   6666    119  -1645  -1834       N  
ATOM   2267  CA  GLY C  44      22.329  22.816  32.006  1.00 80.76           C  
ANISOU 2267  CA  GLY C  44    17126   6413   7147    -19  -1754  -1897       C  
ATOM   2268  C   GLY C  44      21.777  24.105  31.440  1.00 82.68           C  
ANISOU 2268  C   GLY C  44    17336   6600   7477    -24  -1955  -1857       C  
ATOM   2269  O   GLY C  44      20.569  24.253  31.287  1.00 83.76           O  
ANISOU 2269  O   GLY C  44    17382   6584   7859    -59  -2193  -1978       O  
ATOM   2270  N   LEU C  45      22.665  25.045  31.139  1.00 83.98           N  
ANISOU 2270  N   LEU C  45    17544   6864   7500     -4  -1895  -1657       N  
ATOM   2271  CA  LEU C  45      22.265  26.304  30.528  1.00 86.83           C  
ANISOU 2271  CA  LEU C  45    17885   7127   7982    -30  -2156  -1536       C  
ATOM   2272  C   LEU C  45      21.541  26.079  29.212  1.00 90.56           C  
ANISOU 2272  C   LEU C  45    18578   7539   8290     41  -2443  -1548       C  
ATOM   2273  O   LEU C  45      20.471  26.637  28.971  1.00 91.50           O  
ANISOU 2273  O   LEU C  45    18635   7459   8673     11  -2760  -1627       O  
ATOM   2274  CB  LEU C  45      23.493  27.171  30.284  1.00 87.13           C  
ANISOU 2274  CB  LEU C  45    17931   7279   7898    -52  -2059  -1202       C  
ATOM   2275  CG  LEU C  45      23.948  28.030  31.454  1.00 85.28           C  
ANISOU 2275  CG  LEU C  45    17434   6967   8002   -117  -2010  -1196       C  
ATOM   2276  CD1 LEU C  45      25.284  28.667  31.144  1.00 85.93           C  
ANISOU 2276  CD1 LEU C  45    17505   7139   8007   -160  -1920   -815       C  
ATOM   2277  CD2 LEU C  45      22.908  29.086  31.744  1.00 85.06           C  
ANISOU 2277  CD2 LEU C  45    17213   6693   8412   -142  -2363  -1343       C  
ATOM   2278  N   ARG C  46      22.137  25.255  28.360  1.00 93.77           N  
ANISOU 2278  N   ARG C  46    19239   8134   8256    173  -2363  -1512       N  
ATOM   2279  CA  ARG C  46      21.574  24.980  27.054  1.00 98.95           C  
ANISOU 2279  CA  ARG C  46    20146   8799   8651    310  -2657  -1564       C  
ATOM   2280  C   ARG C  46      20.128  24.537  27.162  1.00100.68           C  
ANISOU 2280  C   ARG C  46    20308   8702   9244    290  -2980  -1866       C  
ATOM   2281  O   ARG C  46      19.267  25.049  26.461  1.00102.72           O  
ANISOU 2281  O   ARG C  46    20628   8814   9587    304  -3336  -1877       O  
ATOM   2282  CB  ARG C  46      22.405  23.936  26.332  1.00100.34           C  
ANISOU 2282  CB  ARG C  46    20560   9260   8304    536  -2521  -1636       C  
ATOM   2283  CG  ARG C  46      22.227  23.975  24.853  1.00105.72           C  
ANISOU 2283  CG  ARG C  46    21522  10133   8513    739  -2768  -1605       C  
ATOM   2284  CD  ARG C  46      23.572  23.980  24.159  1.00109.69           C  
ANISOU 2284  CD  ARG C  46    22134  11157   8387    903  -2462  -1372       C  
ATOM   2285  NE  ARG C  46      24.500  23.027  24.763  1.00108.88           N  
ANISOU 2285  NE  ARG C  46    21967  11172   8232    998  -2146  -1558       N  
ATOM   2286  CZ  ARG C  46      24.750  21.811  24.278  1.00111.26           C  
ANISOU 2286  CZ  ARG C  46    22432  11617   8223   1305  -2193  -1924       C  
ATOM   2287  NH1 ARG C  46      24.142  21.376  23.169  1.00114.92           N  
ANISOU 2287  NH1 ARG C  46    23148  12154   8362   1576  -2543  -2177       N  
ATOM   2288  NH2 ARG C  46      25.616  21.029  24.905  1.00109.50           N  
ANISOU 2288  NH2 ARG C  46    22122  11444   8040   1371  -1949  -2072       N  
ATOM   2289  N   VAL C  47      19.857  23.596  28.054  1.00101.36           N  
ANISOU 2289  N   VAL C  47    20247   8676   9589    238  -2874  -2068       N  
ATOM   2290  CA  VAL C  47      18.495  23.125  28.240  1.00104.62           C  
ANISOU 2290  CA  VAL C  47    20515   8804  10430    177  -3152  -2286       C  
ATOM   2291  C   VAL C  47      17.628  24.243  28.770  1.00106.65           C  
ANISOU 2291  C   VAL C  47    20487   8947  11089     46  -3241  -2280       C  
ATOM   2292  O   VAL C  47      16.528  24.478  28.275  1.00108.54           O  
ANISOU 2292  O   VAL C  47    20685   8974  11580     52  -3603  -2398       O  
ATOM   2293  CB  VAL C  47      18.422  21.956  29.211  1.00103.22           C  
ANISOU 2293  CB  VAL C  47    20165   8561  10492     87  -2997  -2372       C  
ATOM   2294  CG1 VAL C  47      16.983  21.539  29.407  1.00104.65           C  
ANISOU 2294  CG1 VAL C  47    20112   8469  11180    -22  -3275  -2505       C  
ATOM   2295  CG2 VAL C  47      19.244  20.807  28.699  1.00103.77           C  
ANISOU 2295  CG2 VAL C  47    20496   8672  10259    252  -3005  -2453       C  
ATOM   2296  N   TYR C  48      18.130  24.949  29.774  1.00 57.50           N  
ATOM   2297  CA  TYR C  48      17.370  26.074  30.314  1.00 61.55           C  
ATOM   2298  C   TYR C  48      16.927  27.019  29.189  1.00 63.72           C  
ATOM   2299  O   TYR C  48      15.731  27.308  29.045  1.00 63.93           O  
ATOM   2300  CB  TYR C  48      18.167  26.838  31.392  1.00 61.83           C  
ATOM   2301  CG  TYR C  48      17.332  27.901  32.085  1.00 64.07           C  
ATOM   2302  CD1 TYR C  48      17.300  29.209  31.601  1.00 66.10           C  
ATOM   2303  CD2 TYR C  48      16.552  27.589  33.200  1.00 65.85           C  
ATOM   2304  CE1 TYR C  48      16.521  30.180  32.215  1.00 68.24           C  
ATOM   2305  CE2 TYR C  48      15.778  28.558  33.830  1.00 67.70           C  
ATOM   2306  CZ  TYR C  48      15.764  29.850  33.333  1.00 68.84           C  
ATOM   2307  OH  TYR C  48      14.997  30.819  33.945  1.00 70.45           O  
ATOM   2308  N   MET C  49      17.902  27.495  28.413  1.00 66.38           N  
ATOM   2309  CA  MET C  49      17.630  28.274  27.220  1.00 69.40           C  
ATOM   2310  C   MET C  49      16.577  27.590  26.354  1.00 70.53           C  
ATOM   2311  O   MET C  49      15.497  28.139  26.124  1.00 70.80           O  
ATOM   2312  CB  MET C  49      18.922  28.482  26.427  1.00 70.15           C  
ATOM   2313  CG  MET C  49      19.417  29.940  26.357  1.00 74.98           C  
ATOM   2314  SD  MET C  49      18.961  30.982  27.799  1.00 85.46           S  
ATOM   2315  CE  MET C  49      19.754  32.558  27.389  1.00 83.43           C  
ATOM   2316  N   ILE C  50      16.889  26.388  25.875  1.00 71.91           N  
ATOM   2317  CA  ILE C  50      15.950  25.626  25.061  1.00 73.32           C  
ATOM   2318  C   ILE C  50      14.550  25.638  25.669  1.00 74.46           C  
ATOM   2319  O   ILE C  50      13.588  25.981  24.990  1.00 74.78           O  
ATOM   2320  CB  ILE C  50      16.403  24.155  24.870  1.00 73.39           C  
ATOM   2321  CG1 ILE C  50      17.863  24.069  24.375  1.00 73.77           C  
ATOM   2322  CG2 ILE C  50      15.449  23.407  23.960  1.00 72.82           C  
ATOM   2323  CD1 ILE C  50      18.067  24.294  22.902  1.00 74.00           C  
ATOM   2324  N   GLN C  51      14.425  25.262  26.939  1.00 75.75           N  
ATOM   2325  CA  GLN C  51      13.103  25.242  27.582  1.00 77.24           C  
ATOM   2326  C   GLN C  51      12.458  26.612  27.476  1.00 77.93           C  
ATOM   2327  O   GLN C  51      11.269  26.744  27.180  1.00 77.85           O  
ATOM   2328  CB  GLN C  51      13.215  24.851  29.058  1.00 77.48           C  
ATOM   2329  CG  GLN C  51      13.575  23.379  29.304  1.00 78.85           C  
ATOM   2330  CD  GLN C  51      12.555  22.423  28.694  1.00 80.67           C  
ATOM   2331  OE1 GLN C  51      12.817  21.794  27.662  1.00 81.17           O  
ATOM   2332  NE2 GLN C  51      11.379  22.324  29.317  1.00 80.71           N  
ATOM   2333  N   GLN C  52      13.277  27.625  27.742  1.00 79.02           N  
ATOM   2334  CA  GLN C  52      12.897  29.030  27.668  1.00 80.02           C  
ATOM   2335  C   GLN C  52      12.274  29.352  26.333  1.00 80.30           C  
ATOM   2336  O   GLN C  52      11.122  29.800  26.248  1.00 80.15           O  
ATOM   2337  CB  GLN C  52      14.163  29.880  27.782  1.00 80.41           C  
ATOM   2338  CG  GLN C  52      13.921  31.371  27.928  1.00 82.18           C  
ATOM   2339  CD  GLN C  52      13.654  31.757  29.369  1.00 84.93           C  
ATOM   2340  OE1 GLN C  52      12.974  31.028  30.112  1.00 85.88           O  
ATOM   2341  NE2 GLN C  52      14.201  32.899  29.783  1.00 85.17           N  
ATOM   2342  N   GLU C  53      13.100  29.159  25.304  1.00 80.99           N  
ATOM   2343  CA  GLU C  53      12.756  29.425  23.922  1.00 81.87           C  
ATOM   2344  C   GLU C  53      11.472  28.724  23.552  1.00 82.11           C  
ATOM   2345  O   GLU C  53      10.651  29.251  22.808  1.00 81.65           O  
ATOM   2346  CB  GLU C  53      13.899  28.979  23.009  1.00 82.09           C  
ATOM   2347  CG  GLU C  53      14.917  30.075  22.746  1.00 84.22           C  
ATOM   2348  CD  GLU C  53      14.233  31.350  22.244  1.00 88.01           C  
ATOM   2349  OE1 GLU C  53      13.165  31.225  21.599  1.00 88.87           O  
ATOM   2350  OE2 GLU C  53      14.741  32.472  22.495  1.00 89.16           O  
ATOM   2351  N   LYS C  54      11.303  27.530  24.097  1.00 83.08           N  
ATOM   2352  CA  LYS C  54      10.103  26.750  23.871  1.00 84.30           C  
ATOM   2353  C   LYS C  54       8.875  27.570  24.274  1.00 84.76           C  
ATOM   2354  O   LYS C  54       8.191  28.128  23.425  1.00 84.76           O  
ATOM   2355  CB  LYS C  54      10.171  25.434  24.658  1.00 84.71           C  
ATOM   2356  CG  LYS C  54       9.573  24.223  23.948  1.00 85.76           C  
ATOM   2357  CD  LYS C  54       8.210  24.561  23.335  1.00 88.38           C  
ATOM   2358  CE  LYS C  54       7.944  23.708  22.082  1.00 89.25           C  
ATOM   2359  NZ  LYS C  54       7.505  24.541  20.919  1.00 88.89           N  
ATOM   2360  N   ARG C  55       8.619  27.678  25.574  1.00 85.67           N  
ATOM   2361  CA  ARG C  55       7.410  28.348  26.060  1.00 86.18           C  
ATOM   2362  C   ARG C  55       7.214  29.772  25.533  1.00 85.87           C  
ATOM   2363  O   ARG C  55       6.110  30.295  25.623  1.00 86.15           O  
ATOM   2364  CB  ARG C  55       7.347  28.343  27.586  1.00 86.60           C  
ATOM   2365  CG  ARG C  55       8.172  29.438  28.233  1.00 88.93           C  
ATOM   2366  CD  ARG C  55       8.204  29.283  29.760  1.00 92.45           C  
ATOM   2367  NE  ARG C  55       9.488  29.728  30.300  1.00 94.90           N  
ATOM   2368  CZ  ARG C  55      10.509  28.918  30.571  1.00 95.60           C  
ATOM   2369  NH1 ARG C  55      10.396  27.610  30.379  1.00 96.30           N  
ATOM   2370  NH2 ARG C  55      11.643  29.416  31.046  1.00 96.25           N  
ATOM   2371  N   GLU C  56       8.264  30.398  24.997  1.00 85.46           N  
ATOM   2372  CA  GLU C  56       8.118  31.686  24.273  1.00 84.82           C  
ATOM   2373  C   GLU C  56       7.549  31.483  22.862  1.00 83.67           C  
ATOM   2374  O   GLU C  56       6.518  30.834  22.692  1.00 83.32           O  
ATOM   2375  CB  GLU C  56       9.457  32.434  24.184  1.00 85.13           C  
ATOM   2376  CG  GLU C  56       9.840  33.206  25.451  1.00 87.05           C  
ATOM   2377  CD  GLU C  56      11.335  33.528  25.523  1.00 89.78           C  
ATOM   2378  OE1 GLU C  56      11.787  34.028  26.580  1.00 90.23           O  
ATOM   2379  OE2 GLU C  56      12.059  33.271  24.526  1.00 91.11           O  
ATOM   2380  N   GLY C  57       8.217  32.053  21.857  1.00 82.49           N  
ATOM   2381  CA  GLY C  57       7.906  31.733  20.449  1.00 80.93           C  
ATOM   2382  C   GLY C  57       8.580  30.410  20.097  1.00 79.42           C  
ATOM   2383  O   GLY C  57       8.778  29.580  20.997  1.00 79.68           O  
ATOM   2384  N   GLY C  58       8.910  30.201  18.811  1.00 77.46           N  
ATOM   2385  CA  GLY C  58       9.940  29.210  18.395  1.00 74.30           C  
ATOM   2386  C   GLY C  58      11.251  29.849  18.834  1.00 72.22           C  
ATOM   2387  O   GLY C  58      11.212  30.706  19.718  1.00 72.45           O  
ATOM   2388  N   PHE C  59      12.408  29.532  18.246  1.00 69.62           N  
ATOM   2389  CA  PHE C  59      12.616  28.677  17.085  1.00 66.85           C  
ATOM   2390  C   PHE C  59      12.758  27.248  17.596  1.00 65.00           C  
ATOM   2391  O   PHE C  59      11.821  26.751  18.220  1.00 66.01           O  
ATOM   2392  CB  PHE C  59      13.852  29.194  16.337  1.00 66.87           C  
ATOM   2393  CG  PHE C  59      14.496  28.217  15.403  1.00 66.30           C  
ATOM   2394  CD1 PHE C  59      15.751  27.690  15.695  1.00 66.03           C  
ATOM   2395  CD2 PHE C  59      13.902  27.877  14.202  1.00 65.72           C  
ATOM   2396  CE1 PHE C  59      16.386  26.798  14.821  1.00 65.18           C  
ATOM   2397  CE2 PHE C  59      14.537  26.990  13.321  1.00 65.35           C  
ATOM   2398  CZ  PHE C  59      15.784  26.453  13.637  1.00 64.37           C  
ATOM   2399  N   ASN C  60      13.877  26.567  17.374  1.00 61.39           N  
ATOM   2400  CA  ASN C  60      13.906  25.168  17.821  1.00 57.83           C  
ATOM   2401  C   ASN C  60      14.662  24.136  16.965  1.00 54.77           C  
ATOM   2402  O   ASN C  60      14.050  23.233  16.407  1.00 55.02           O  
ATOM   2403  CB  ASN C  60      12.465  24.674  17.987  1.00 57.82           C  
ATOM   2404  CG  ASN C  60      12.391  23.369  18.752  1.00 59.53           C  
ATOM   2405  OD1 ASN C  60      13.415  22.843  19.226  1.00 61.23           O  
ATOM   2406  ND2 ASN C  60      11.180  22.832  18.884  1.00 60.46           N  
ATOM   2407  N   GLN C  61      15.981  24.243  16.899  1.00 83.50           N  
ANISOU 2407  N   GLN C  61    15195   7733   8797   -180   -705   -294       N  
ATOM   2408  CA  GLN C  61      16.796  23.345  16.085  1.00 78.88           C  
ANISOU 2408  CA  GLN C  61    14473   7175   8324   -168   -797   -264       C  
ATOM   2409  C   GLN C  61      16.211  21.971  15.889  1.00 76.62           C  
ANISOU 2409  C   GLN C  61    14265   6913   7933   -172   -721   -180       C  
ATOM   2410  O   GLN C  61      16.119  21.473  14.768  1.00 75.00           O  
ANISOU 2410  O   GLN C  61    13898   6767   7832   -194   -650   -126       O  
ATOM   2411  CB  GLN C  61      18.172  23.169  16.698  1.00 79.79           C  
ANISOU 2411  CB  GLN C  61    14623   7224   8471   -107  -1065   -350       C  
ATOM   2412  CG  GLN C  61      19.216  24.073  16.133  1.00 77.79           C  
ANISOU 2412  CG  GLN C  61    14130   6970   8457   -126  -1148   -434       C  
ATOM   2413  CD  GLN C  61      19.172  24.092  14.642  1.00 73.96           C  
ANISOU 2413  CD  GLN C  61    13404   6556   8140   -185   -992   -379       C  
ATOM   2414  OE1 GLN C  61      18.887  23.074  14.006  1.00 71.61           O  
ANISOU 2414  OE1 GLN C  61    13081   6304   7824   -180   -926   -306       O  
ATOM   2415  NE2 GLN C  61      19.437  25.263  14.057  1.00 73.43           N  
ANISOU 2415  NE2 GLN C  61    13189   6483   8226   -246   -929   -414       N  
ATOM   2416  N   MET C  62      15.837  21.336  16.985  1.00 75.45           N  
ANISOU 2416  N   MET C  62    14394   6707   7568   -159   -733   -171       N  
ATOM   2417  CA  MET C  62      15.513  19.929  16.917  1.00 73.56           C  
ANISOU 2417  CA  MET C  62    14269   6456   7222   -167   -698    -99       C  
ATOM   2418  C   MET C  62      14.262  19.709  16.082  1.00 70.66           C  
ANISOU 2418  C   MET C  62    13784   6171   6893   -244   -445    -35       C  
ATOM   2419  O   MET C  62      14.215  18.825  15.232  1.00 69.31           O  
ANISOU 2419  O   MET C  62    13521   6034   6780   -257   -420     19       O  
ATOM   2420  CB  MET C  62      15.357  19.341  18.317  1.00 75.48           C  
ANISOU 2420  CB  MET C  62    14893   6590   7194   -151   -748   -100       C  
ATOM   2421  CG  MET C  62      15.940  17.933  18.471  1.00 77.50           C  
ANISOU 2421  CG  MET C  62    15318   6770   7359    -99   -907    -61       C  
ATOM   2422  SD  MET C  62      17.657  17.706  17.880  1.00 80.97           S  
ANISOU 2422  SD  MET C  62    15542   7202   8021     22  -1233   -126       S  
ATOM   2423  CE  MET C  62      18.500  19.117  18.629  1.00 81.63           C  
ANISOU 2423  CE  MET C  62    15597   7253   8166     72  -1423   -255       C  
ATOM   2424  N   GLU C  63      13.250  20.529  16.321  1.00 68.79           N  
ANISOU 2424  N   GLU C  63    13542   5961   6636   -288   -271    -57       N  
ATOM   2425  CA  GLU C  63      12.001  20.386  15.604  1.00 66.35           C  
ANISOU 2425  CA  GLU C  63    13102   5722   6384   -349    -56    -27       C  
ATOM   2426  C   GLU C  63      12.228  20.574  14.101  1.00 63.57           C  
ANISOU 2426  C   GLU C  63    12475   5441   6237   -336    -83      3       C  
ATOM   2427  O   GLU C  63      11.602  19.899  13.275  1.00 62.96           O  
ANISOU 2427  O   GLU C  63    12303   5410   6207   -369      5     46       O  
ATOM   2428  CB  GLU C  63      10.997  21.401  16.140  1.00 66.91           C  
ANISOU 2428  CB  GLU C  63    13183   5803   6436   -371    106    -90       C  
ATOM   2429  CG  GLU C  63       9.568  20.935  16.039  1.00 68.24           C  
ANISOU 2429  CG  GLU C  63    13319   6012   6599   -444    343    -95       C  
ATOM   2430  CD  GLU C  63       9.327  19.629  16.778  1.00 70.14           C  
ANISOU 2430  CD  GLU C  63    13804   6196   6650   -514    425    -62       C  
ATOM   2431  OE1 GLU C  63       9.579  19.594  18.002  1.00 72.28           O  
ANISOU 2431  OE1 GLU C  63    14361   6381   6722   -519    415    -81       O  
ATOM   2432  OE2 GLU C  63       8.885  18.641  16.145  1.00 70.12           O  
ANISOU 2432  OE2 GLU C  63    13737   6219   6685   -568    495    -17       O  
ATOM   2433  N   TYR C  64      13.135  21.496  13.777  1.00 61.42           N  
ANISOU 2433  N   TYR C  64    12097   5165   6077   -297   -200    -25       N  
ATOM   2434  CA  TYR C  64      13.509  21.853  12.428  1.00 58.50           C  
ANISOU 2434  CA  TYR C  64    11517   4835   5876   -295   -215     -3       C  
ATOM   2435  C   TYR C  64      14.307  20.738  11.780  1.00 57.63           C  
ANISOU 2435  C   TYR C  64    11360   4734   5802   -287   -293     33       C  
ATOM   2436  O   TYR C  64      14.036  20.345  10.654  1.00 56.59           O  
ANISOU 2436  O   TYR C  64    11120   4646   5737   -304   -233     77       O  
ATOM   2437  CB  TYR C  64      14.347  23.133  12.476  1.00 58.59           C  
ANISOU 2437  CB  TYR C  64    11470   4811   5980   -280   -299    -58       C  
ATOM   2438  CG  TYR C  64      15.022  23.524  11.171  1.00 56.70           C  
ANISOU 2438  CG  TYR C  64    11059   4584   5900   -298   -308    -42       C  
ATOM   2439  CD1 TYR C  64      14.422  24.409  10.292  1.00 55.45           C  
ANISOU 2439  CD1 TYR C  64    10828   4431   5810   -312   -219    -19       C  
ATOM   2440  CD2 TYR C  64      16.278  23.020  10.835  1.00 56.11           C  
ANISOU 2440  CD2 TYR C  64    10910   4502   5906   -298   -405    -62       C  
ATOM   2441  CE1 TYR C  64      15.046  24.755   9.096  1.00 54.98           C  
ANISOU 2441  CE1 TYR C  64    10669   4360   5859   -343   -207      2       C  
ATOM   2442  CE2 TYR C  64      16.905  23.358   9.656  1.00 54.11           C  
ANISOU 2442  CE2 TYR C  64    10516   4253   5790   -335   -369    -58       C  
ATOM   2443  CZ  TYR C  64      16.285  24.217   8.786  1.00 54.43           C  
ANISOU 2443  CZ  TYR C  64    10529   4290   5862   -365   -260    -18       C  
ATOM   2444  OH  TYR C  64      16.913  24.572   7.615  1.00 53.92           O  
ANISOU 2444  OH  TYR C  64    10379   4207   5901   -416   -204    -10       O  
ATOM   2445  N   ASN C  65      15.314  20.228  12.481  1.00 57.77           N  
ANISOU 2445  N   ASN C  65    11467   4702   5779   -249   -444      2       N  
ATOM   2446  CA  ASN C  65      16.075  19.097  11.960  1.00 56.85           C  
ANISOU 2446  CA  ASN C  65    11312   4585   5705   -222   -530     18       C  
ATOM   2447  C   ASN C  65      15.153  17.955  11.611  1.00 56.11           C  
ANISOU 2447  C   ASN C  65    11280   4512   5529   -252   -426     90       C  
ATOM   2448  O   ASN C  65      15.330  17.283  10.581  1.00 55.76           O  
ANISOU 2448  O   ASN C  65    11132   4496   5557   -253   -412    119       O  
ATOM   2449  CB  ASN C  65      17.087  18.611  12.969  1.00 58.02           C  
ANISOU 2449  CB  ASN C  65    11589   4657   5798   -153   -737    -37       C  
ATOM   2450  CG  ASN C  65      18.203  19.586  13.167  1.00 59.03           C  
ANISOU 2450  CG  ASN C  65    11606   4764   6059   -125   -872   -134       C  
ATOM   2451  OD1 ASN C  65      18.842  19.616  14.215  1.00 61.95           O  
ANISOU 2451  OD1 ASN C  65    12097   5065   6377    -67  -1056   -201       O  
ATOM   2452  ND2 ASN C  65      18.448  20.401  12.167  1.00 57.69           N  
ANISOU 2452  ND2 ASN C  65    11223   4640   6058   -172   -788   -148       N  
ATOM   2453  N   LYS C  66      14.166  17.725  12.464  1.00 55.79           N  
ANISOU 2453  N   LYS C  66    11411   4449   5339   -286   -338    109       N  
ATOM   2454  CA  LYS C  66      13.222  16.657  12.225  1.00 55.15           C  
ANISOU 2454  CA  LYS C  66    11389   4377   5190   -339   -219    162       C  
ATOM   2455  C   LYS C  66      12.402  16.910  10.930  1.00 54.19           C  
ANISOU 2455  C   LYS C  66    11058   4338   5195   -377    -95    182       C  
ATOM   2456  O   LYS C  66      12.293  16.025  10.058  1.00 53.47           O  
ANISOU 2456  O   LYS C  66    10912   4265   5138   -391    -82    218       O  
ATOM   2457  CB  LYS C  66      12.335  16.481  13.445  1.00 56.14           C  
ANISOU 2457  CB  LYS C  66    11739   4452   5140   -391   -110    159       C  
ATOM   2458  CG  LYS C  66      11.288  15.433  13.315  1.00 55.99           C  
ANISOU 2458  CG  LYS C  66    11783   4430   5061   -477     47    197       C  
ATOM   2459  CD  LYS C  66      10.454  15.325  14.568  1.00 57.14           C  
ANISOU 2459  CD  LYS C  66    12164   4516   5031   -552    199    180       C  
ATOM   2460  CE  LYS C  66       9.259  14.440  14.306  1.00 58.05           C  
ANISOU 2460  CE  LYS C  66    12275   4639   5141   -669    404    193       C  
ATOM   2461  NZ  LYS C  66       8.719  13.819  15.540  1.00 60.68           N  
ANISOU 2461  NZ  LYS C  66    12925   4870   5261   -765    553    194       N  
ATOM   2462  N   LEU C  67      11.849  18.115  10.781  1.00 53.40           N  
ANISOU 2462  N   LEU C  67    10856   4275   5159   -382    -27    153       N  
ATOM   2463  CA  LEU C  67      11.050  18.402   9.601  1.00 52.60           C  
ANISOU 2463  CA  LEU C  67    10591   4232   5165   -396     48    163       C  
ATOM   2464  C   LEU C  67      11.885  18.278   8.317  1.00 52.12           C  
ANISOU 2464  C   LEU C  67    10424   4185   5193   -371    -26    195       C  
ATOM   2465  O   LEU C  67      11.384  17.862   7.254  1.00 52.13           O  
ANISOU 2465  O   LEU C  67    10353   4217   5236   -383      6    221       O  
ATOM   2466  CB  LEU C  67      10.483  19.809   9.671  1.00 52.69           C  
ANISOU 2466  CB  LEU C  67    10533   4254   5233   -378     92    120       C  
ATOM   2467  CG  LEU C  67       9.117  20.059   9.039  1.00 52.88           C  
ANISOU 2467  CG  LEU C  67    10440   4319   5333   -384    182     96       C  
ATOM   2468  CD1 LEU C  67       9.104  21.438   8.403  1.00 52.39           C  
ANISOU 2468  CD1 LEU C  67    10295   4249   5363   -328    138     80       C  
ATOM   2469  CD2 LEU C  67       8.783  18.987   8.010  1.00 53.13           C  
ANISOU 2469  CD2 LEU C  67    10410   4380   5395   -408    182    133       C  
ATOM   2470  N   MET C  68      13.149  18.665   8.388  1.00 51.88           N  
ANISOU 2470  N   MET C  68    10384   4130   5199   -341   -118    179       N  
ATOM   2471  CA  MET C  68      13.956  18.625   7.191  1.00 51.52           C  
ANISOU 2471  CA  MET C  68    10237   4093   5244   -335   -143    191       C  
ATOM   2472  C   MET C  68      14.245  17.174   6.853  1.00 51.76           C  
ANISOU 2472  C   MET C  68    10289   4125   5251   -328   -170    212       C  
ATOM   2473  O   MET C  68      14.190  16.775   5.682  1.00 51.70           O  
ANISOU 2473  O   MET C  68    10225   4138   5280   -337   -134    236       O  
ATOM   2474  CB  MET C  68      15.250  19.415   7.374  1.00 52.11           C  
ANISOU 2474  CB  MET C  68    10262   4137   5399   -323   -211    140       C  
ATOM   2475  CG  MET C  68      15.050  20.924   7.545  1.00 51.93           C  
ANISOU 2475  CG  MET C  68    10225   4095   5410   -336   -184    119       C  
ATOM   2476  SD  MET C  68      14.719  21.712   5.965  1.00 53.44           S  
ANISOU 2476  SD  MET C  68    10357   4286   5664   -363    -94    160       S  
ATOM   2477  CE  MET C  68      16.339  21.570   5.191  1.00 51.47           C  
ANISOU 2477  CE  MET C  68    10021   4015   5520   -400    -90    128       C  
ATOM   2478  N   LEU C  69      14.522  16.367   7.876  1.00 52.15           N  
ANISOU 2478  N   LEU C  69    10453   4137   5224   -308   -239    203       N  
ATOM   2479  CA  LEU C  69      14.810  14.959   7.630  1.00 51.78           C  
ANISOU 2479  CA  LEU C  69    10456   4069   5151   -291   -281    221       C  
ATOM   2480  C   LEU C  69      13.602  14.291   7.013  1.00 51.59           C  
ANISOU 2480  C   LEU C  69    10443   4070   5089   -344   -177    267       C  
ATOM   2481  O   LEU C  69      13.741  13.414   6.157  1.00 51.86           O  
ANISOU 2481  O   LEU C  69    10454   4106   5144   -340   -181    283       O  
ATOM   2482  CB  LEU C  69      15.202  14.236   8.907  1.00 52.49           C  
ANISOU 2482  CB  LEU C  69    10725   4084   5136   -253   -390    209       C  
ATOM   2483  CG  LEU C  69      15.410  12.726   8.758  1.00 52.13           C  
ANISOU 2483  CG  LEU C  69    10774   3988   5044   -227   -445    231       C  
ATOM   2484  CD1 LEU C  69      16.492  12.408   7.754  1.00 50.72           C  
ANISOU 2484  CD1 LEU C  69    10445   3823   5002   -169   -510    191       C  
ATOM   2485  CD2 LEU C  69      15.733  12.083  10.115  1.00 52.89           C  
ANISOU 2485  CD2 LEU C  69    11116   3979   5002   -182   -573    228       C  
ATOM   2486  N   GLU C  70      12.410  14.700   7.427  1.00 51.60           N  
ANISOU 2486  N   GLU C  70    10467   4090   5050   -393    -84    273       N  
ATOM   2487  CA  GLU C  70      11.219  14.095   6.876  1.00 51.73           C  
ANISOU 2487  CA  GLU C  70    10459   4129   5065   -449      6    289       C  
ATOM   2488  C   GLU C  70      11.083  14.450   5.402  1.00 51.11           C  
ANISOU 2488  C   GLU C  70    10244   4097   5079   -434      4    295       C  
ATOM   2489  O   GLU C  70      10.995  13.590   4.514  1.00 50.74           O  
ANISOU 2489  O   GLU C  70    10185   4052   5041   -442     -4    310       O  
ATOM   2490  CB  GLU C  70       9.989  14.582   7.607  1.00 52.30           C  
ANISOU 2490  CB  GLU C  70    10539   4215   5116   -502    116    261       C  
ATOM   2491  CG  GLU C  70       8.720  13.997   7.038  1.00 54.00           C  
ANISOU 2491  CG  GLU C  70    10685   4458   5375   -566    204    246       C  
ATOM   2492  CD  GLU C  70       7.481  14.712   7.522  1.00 57.05           C  
ANISOU 2492  CD  GLU C  70    10997   4873   5806   -605    320    182       C  
ATOM   2493  OE1 GLU C  70       6.420  14.604   6.884  1.00 59.16           O  
ANISOU 2493  OE1 GLU C  70    11135   5176   6169   -634    363    137       O  
ATOM   2494  OE2 GLU C  70       7.567  15.393   8.548  1.00 59.15           O  
ANISOU 2494  OE2 GLU C  70    11329   5123   6021   -599    360    160       O  
ATOM   2495  N   ASN C  71      11.050  15.745   5.143  1.00 51.03           N  
ANISOU 2495  N   ASN C  71    10161   4108   5122   -410      6    281       N  
ATOM   2496  CA  ASN C  71      10.920  16.214   3.779  1.00 50.73           C  
ANISOU 2496  CA  ASN C  71    10051   4086   5137   -391     -3    292       C  
ATOM   2497  C   ASN C  71      11.967  15.588   2.884  1.00 50.19           C  
ANISOU 2497  C   ASN C  71     9992   4006   5073   -379    -29    311       C  
ATOM   2498  O   ASN C  71      11.642  15.068   1.812  1.00 50.45           O  
ANISOU 2498  O   ASN C  71    10024   4043   5100   -382    -29    325       O  
ATOM   2499  CB  ASN C  71      10.956  17.740   3.706  1.00 50.82           C  
ANISOU 2499  CB  ASN C  71    10032   4090   5189   -364     -6    281       C  
ATOM   2500  CG  ASN C  71       9.593  18.362   3.988  1.00 53.43           C  
ANISOU 2500  CG  ASN C  71    10320   4434   5546   -354     17    246       C  
ATOM   2501  OD1 ASN C  71       8.566  17.678   3.978  1.00 55.75           O  
ANISOU 2501  OD1 ASN C  71    10577   4752   5851   -376     43    223       O  
ATOM   2502  ND2 ASN C  71       9.577  19.660   4.239  1.00 56.22           N  
ANISOU 2502  ND2 ASN C  71    10666   4767   5928   -323     11    227       N  
ATOM   2503  N   VAL C  72      13.220  15.605   3.319  1.00 49.79           N  
ANISOU 2503  N   VAL C  72     9945   3936   5039   -362    -57    296       N  
ATOM   2504  CA  VAL C  72      14.260  14.987   2.509  1.00 49.43           C  
ANISOU 2504  CA  VAL C  72     9879   3879   5024   -348    -63    285       C  
ATOM   2505  C   VAL C  72      13.998  13.498   2.293  1.00 49.48           C  
ANISOU 2505  C   VAL C  72     9934   3877   4988   -345    -81    297       C  
ATOM   2506  O   VAL C  72      14.098  12.985   1.177  1.00 49.43           O  
ANISOU 2506  O   VAL C  72     9927   3872   4984   -345    -58    300       O  
ATOM   2507  CB  VAL C  72      15.628  15.170   3.118  1.00 49.53           C  
ANISOU 2507  CB  VAL C  72     9849   3870   5101   -322   -108    234       C  
ATOM   2508  CG1 VAL C  72      16.577  14.192   2.495  1.00 50.05           C  
ANISOU 2508  CG1 VAL C  72     9881   3923   5212   -295   -118    198       C  
ATOM   2509  CG2 VAL C  72      16.094  16.573   2.889  1.00 49.08           C  
ANISOU 2509  CG2 VAL C  72     9732   3807   5108   -346    -66    213       C  
ATOM   2510  N   SER C  73      13.648  12.800   3.358  1.00 49.52           N  
ANISOU 2510  N   SER C  73    10013   3862   4942   -350   -115    303       N  
ATOM   2511  CA  SER C  73      13.406  11.376   3.211  1.00 50.13           C  
ANISOU 2511  CA  SER C  73    10163   3909   4975   -357   -130    315       C  
ATOM   2512  C   SER C  73      12.258  11.110   2.240  1.00 49.76           C  
ANISOU 2512  C   SER C  73    10097   3888   4922   -404    -80    332       C  
ATOM   2513  O   SER C  73      12.323  10.256   1.363  1.00 49.91           O  
ANISOU 2513  O   SER C  73    10133   3894   4937   -401    -88    331       O  
ATOM   2514  CB  SER C  73      13.143  10.736   4.571  1.00 50.64           C  
ANISOU 2514  CB  SER C  73    10361   3921   4958   -372   -156    326       C  
ATOM   2515  OG  SER C  73      14.351  10.191   5.077  1.00 52.37           O  
ANISOU 2515  OG  SER C  73    10642   4083   5174   -300   -264    304       O  
ATOM   2516  N   ARG C  74      11.205  11.880   2.410  1.00 49.65           N  
ANISOU 2516  N   ARG C  74    10042   3906   4917   -438    -41    331       N  
ATOM   2517  CA  ARG C  74      10.034  11.776   1.588  1.00 49.66           C  
ANISOU 2517  CA  ARG C  74     9999   3930   4940   -469    -27    321       C  
ATOM   2518  C   ARG C  74      10.388  11.990   0.113  1.00 49.28           C  
ANISOU 2518  C   ARG C  74     9939   3885   4898   -430    -60    328       C  
ATOM   2519  O   ARG C  74      10.070  11.172  -0.763  1.00 49.39           O  
ANISOU 2519  O   ARG C  74     9979   3889   4898   -439    -83    322       O  
ATOM   2520  CB  ARG C  74       9.094  12.871   2.038  1.00 50.16           C  
ANISOU 2520  CB  ARG C  74     9992   4024   5044   -478      1    297       C  
ATOM   2521  CG  ARG C  74       7.671  12.457   2.031  1.00 52.73           C  
ANISOU 2521  CG  ARG C  74    10259   4364   5414   -533     31    252       C  
ATOM   2522  CD  ARG C  74       6.833  13.254   3.052  1.00 55.05           C  
ANISOU 2522  CD  ARG C  74    10489   4678   5749   -557    102    205       C  
ATOM   2523  NE  ARG C  74       5.668  12.442   3.391  1.00 57.25           N  
ANISOU 2523  NE  ARG C  74    10724   4958   6073   -649    182    147       N  
ATOM   2524  CZ  ARG C  74       5.331  12.148   4.627  1.00 58.41           C  
ANISOU 2524  CZ  ARG C  74    10922   5084   6185   -729    309    127       C  
ATOM   2525  NH1 ARG C  74       6.062  12.644   5.607  1.00 59.50           N  
ANISOU 2525  NH1 ARG C  74    11165   5203   6237   -706    333    161       N  
ATOM   2526  NH2 ARG C  74       4.273  11.382   4.880  1.00 60.19           N  
ANISOU 2526  NH2 ARG C  74    11108   5301   6462   -839    415     66       N  
ATOM   2527  N   VAL C  75      11.051  13.101  -0.162  1.00 48.47           N  
ANISOU 2527  N   VAL C  75     9822   3787   4808   -396    -53    336       N  
ATOM   2528  CA  VAL C  75      11.500  13.386  -1.496  1.00 48.14           C  
ANISOU 2528  CA  VAL C  75     9817   3729   4745   -375    -50    346       C  
ATOM   2529  C   VAL C  75      12.281  12.211  -2.069  1.00 48.63           C  
ANISOU 2529  C   VAL C  75     9919   3773   4784   -372    -35    336       C  
ATOM   2530  O   VAL C  75      12.083  11.817  -3.223  1.00 49.07           O  
ANISOU 2530  O   VAL C  75    10036   3813   4796   -368    -41    335       O  
ATOM   2531  CB  VAL C  75      12.357  14.654  -1.498  1.00 48.05           C  
ANISOU 2531  CB  VAL C  75     9800   3705   4753   -366     -9    352       C  
ATOM   2532  CG1 VAL C  75      13.095  14.806  -2.823  1.00 47.85           C  
ANISOU 2532  CG1 VAL C  75     9845   3644   4690   -369     46    358       C  
ATOM   2533  CG2 VAL C  75      11.480  15.865  -1.219  1.00 47.70           C  
ANISOU 2533  CG2 VAL C  75     9742   3660   4722   -354    -36    359       C  
ATOM   2534  N   ARG C  76      13.157  11.630  -1.260  1.00 48.80           N  
ANISOU 2534  N   ARG C  76     9921   3786   4833   -362    -31    320       N  
ATOM   2535  CA  ARG C  76      13.986  10.547  -1.755  1.00 49.27           C  
ANISOU 2535  CA  ARG C  76    10007   3821   4893   -338    -24    293       C  
ATOM   2536  C   ARG C  76      13.178   9.323  -2.144  1.00 49.01           C  
ANISOU 2536  C   ARG C  76    10040   3768   4814   -354    -60    298       C  
ATOM   2537  O   ARG C  76      13.455   8.693  -3.174  1.00 49.55           O  
ANISOU 2537  O   ARG C  76    10154   3817   4857   -340    -46    278       O  
ATOM   2538  CB  ARG C  76      15.058  10.139  -0.764  1.00 49.76           C  
ANISOU 2538  CB  ARG C  76    10036   3863   5009   -298    -58    258       C  
ATOM   2539  CG  ARG C  76      15.834   8.956  -1.293  1.00 51.34           C  
ANISOU 2539  CG  ARG C  76    10254   4027   5226   -254    -66    213       C  
ATOM   2540  CD  ARG C  76      16.432   8.147  -0.181  1.00 54.40           C  
ANISOU 2540  CD  ARG C  76    10661   4368   5640   -197   -164    186       C  
ATOM   2541  NE  ARG C  76      16.868   6.838  -0.652  1.00 57.03           N  
ANISOU 2541  NE  ARG C  76    11040   4649   5979   -146   -194    147       N  
ATOM   2542  CZ  ARG C  76      17.845   6.155  -0.077  1.00 58.62           C  
ANISOU 2542  CZ  ARG C  76    11238   4796   6240    -56   -287     87       C  
ATOM   2543  NH1 ARG C  76      18.482   6.663   0.969  1.00 59.59           N  
ANISOU 2543  NH1 ARG C  76    11315   4910   6416    -12   -370     59       N  
ATOM   2544  NH2 ARG C  76      18.189   4.972  -0.543  1.00 59.96           N  
ANISOU 2544  NH2 ARG C  76    11455   4909   6418      0   -318     45       N  
ATOM   2545  N   ALA C  77      12.193   8.974  -1.327  1.00 48.33           N  
ANISOU 2545  N   ALA C  77     9965   3681   4718   -392    -90    314       N  
ATOM   2546  CA  ALA C  77      11.332   7.843  -1.645  1.00 48.32           C  
ANISOU 2546  CA  ALA C  77    10016   3652   4691   -433   -114    308       C  
ATOM   2547  C   ALA C  77      10.592   8.152  -2.933  1.00 48.77           C  
ANISOU 2547  C   ALA C  77    10067   3728   4737   -438   -135    296       C  
ATOM   2548  O   ALA C  77      10.541   7.332  -3.865  1.00 49.39           O  
ANISOU 2548  O   ALA C  77    10206   3777   4782   -436   -160    277       O  
ATOM   2549  CB  ALA C  77      10.362   7.612  -0.553  1.00 48.14           C  
ANISOU 2549  CB  ALA C  77     9996   3622   4673   -500   -101    314       C  
ATOM   2550  N   MET C  78      10.039   9.361  -3.006  1.00 48.62           N  
ANISOU 2550  N   MET C  78     9993   3744   4736   -434   -143    302       N  
ATOM   2551  CA  MET C  78       9.259   9.758  -4.166  1.00 48.57           C  
ANISOU 2551  CA  MET C  78    10005   3738   4711   -418   -206    286       C  
ATOM   2552  C   MET C  78      10.088   9.691  -5.445  1.00 49.08           C  
ANISOU 2552  C   MET C  78    10183   3770   4693   -381   -194    293       C  
ATOM   2553  O   MET C  78       9.628   9.139  -6.449  1.00 50.01           O  
ANISOU 2553  O   MET C  78    10379   3861   4763   -376   -255    271       O  
ATOM   2554  CB  MET C  78       8.646  11.139  -3.968  1.00 48.19           C  
ANISOU 2554  CB  MET C  78     9898   3714   4699   -396   -233    287       C  
ATOM   2555  CG  MET C  78       7.395  11.142  -3.118  1.00 47.86           C  
ANISOU 2555  CG  MET C  78     9738   3701   4748   -434   -250    244       C  
ATOM   2556  SD  MET C  78       6.536  12.756  -3.052  1.00 49.90           S  
ANISOU 2556  SD  MET C  78     9915   3976   5070   -378   -309    216       S  
ATOM   2557  CE  MET C  78       7.651  13.797  -2.095  1.00 47.85           C  
ANISOU 2557  CE  MET C  78     9671   3722   4787   -366   -213    270       C  
ATOM   2558  N   CYS C  79      11.301  10.237  -5.419  1.00 48.71           N  
ANISOU 2558  N   CYS C  79    10150   3720   4635   -363   -107    311       N  
ATOM   2559  CA  CYS C  79      12.138  10.194  -6.616  1.00 49.67           C  
ANISOU 2559  CA  CYS C  79    10383   3807   4683   -348    -44    304       C  
ATOM   2560  C   CYS C  79      12.486   8.757  -7.041  1.00 50.41           C  
ANISOU 2560  C   CYS C  79    10522   3877   4754   -343    -36    266       C  
ATOM   2561  O   CYS C  79      12.520   8.429  -8.246  1.00 51.27           O  
ANISOU 2561  O   CYS C  79    10757   3948   4773   -333    -28    248       O  
ATOM   2562  CB  CYS C  79      13.412  10.984  -6.410  1.00 49.36           C  
ANISOU 2562  CB  CYS C  79    10310   3769   4676   -352     76    303       C  
ATOM   2563  SG  CYS C  79      13.114  12.747  -6.214  1.00 50.40           S  
ANISOU 2563  SG  CYS C  79    10445   3897   4808   -361     78    346       S  
ATOM   2564  N   THR C  80      12.764   7.907  -6.056  1.00 49.76           N  
ANISOU 2564  N   THR C  80    10366   3800   4740   -343    -44    253       N  
ATOM   2565  CA  THR C  80      13.054   6.536  -6.366  1.00 50.30           C  
ANISOU 2565  CA  THR C  80    10488   3829   4796   -328    -53    216       C  
ATOM   2566  C   THR C  80      11.946   6.016  -7.265  1.00 50.97           C  
ANISOU 2566  C   THR C  80    10662   3890   4813   -351   -131    207       C  
ATOM   2567  O   THR C  80      12.208   5.355  -8.282  1.00 51.78           O  
ANISOU 2567  O   THR C  80    10870   3953   4850   -333   -120    172       O  
ATOM   2568  CB  THR C  80      13.118   5.680  -5.094  1.00 50.04           C  
ANISOU 2568  CB  THR C  80    10414   3778   4821   -329    -95    217       C  
ATOM   2569  OG1 THR C  80      14.197   6.135  -4.291  1.00 50.09           O  
ANISOU 2569  OG1 THR C  80    10344   3796   4890   -290    -62    208       O  
ATOM   2570  CG2 THR C  80      13.370   4.248  -5.436  1.00 50.43           C  
ANISOU 2570  CG2 THR C  80    10542   3764   4854   -308   -119    178       C  
ATOM   2571  N   GLU C  81      10.705   6.313  -6.883  1.00 50.83           N  
ANISOU 2571  N   GLU C  81    10597   3894   4823   -390   -210    222       N  
ATOM   2572  CA  GLU C  81       9.551   5.767  -7.592  1.00 51.54           C  
ANISOU 2572  CA  GLU C  81    10731   3960   4892   -415   -315    187       C  
ATOM   2573  C   GLU C  81       9.408   6.417  -8.934  1.00 52.02           C  
ANISOU 2573  C   GLU C  81    10907   4004   4856   -373   -363    180       C  
ATOM   2574  O   GLU C  81       9.181   5.748  -9.946  1.00 52.95           O  
ANISOU 2574  O   GLU C  81    11143   4077   4900   -364   -424    143       O  
ATOM   2575  CB  GLU C  81       8.270   5.958  -6.796  1.00 51.79           C  
ANISOU 2575  CB  GLU C  81    10641   4021   5017   -470   -373    175       C  
ATOM   2576  CG  GLU C  81       8.170   5.088  -5.560  1.00 51.76           C  
ANISOU 2576  CG  GLU C  81    10588   4003   5074   -537   -321    177       C  
ATOM   2577  CD  GLU C  81       8.321   3.649  -5.913  1.00 54.45           C  
ANISOU 2577  CD  GLU C  81    11026   4276   5388   -561   -337    151       C  
ATOM   2578  OE1 GLU C  81       7.636   3.213  -6.849  1.00 55.19           O  
ANISOU 2578  OE1 GLU C  81    11153   4346   5472   -577   -418    102       O  
ATOM   2579  OE2 GLU C  81       9.138   2.951  -5.279  1.00 56.65           O  
ANISOU 2579  OE2 GLU C  81    11359   4514   5653   -553   -287    173       O  
ATOM   2580  N   ILE C  82       9.558   7.736  -8.955  1.00 51.66           N  
ANISOU 2580  N   ILE C  82    10858   3979   4793   -347   -341    217       N  
ATOM   2581  CA  ILE C  82       9.468   8.473 -10.219  1.00 52.15           C  
ANISOU 2581  CA  ILE C  82    11089   3996   4729   -306   -386    224       C  
ATOM   2582  C   ILE C  82      10.526   7.984 -11.204  1.00 52.72           C  
ANISOU 2582  C   ILE C  82    11332   4021   4680   -298   -276    213       C  
ATOM   2583  O   ILE C  82      10.250   7.776 -12.383  1.00 53.87           O  
ANISOU 2583  O   ILE C  82    11665   4109   4695   -276   -339    192       O  
ATOM   2584  CB  ILE C  82       9.658   9.934  -9.991  1.00 51.89           C  
ANISOU 2584  CB  ILE C  82    11051   3970   4693   -288   -350    271       C  
ATOM   2585  CG1 ILE C  82       8.531  10.469  -9.108  1.00 51.55           C  
ANISOU 2585  CG1 ILE C  82    10848   3969   4771   -283   -459    262       C  
ATOM   2586  CG2 ILE C  82       9.713  10.668 -11.320  1.00 53.03           C  
ANISOU 2586  CG2 ILE C  82    11439   4037   4672   -251   -378    290       C  
ATOM   2587  CD1 ILE C  82       8.783  11.884  -8.604  1.00 50.61           C  
ANISOU 2587  CD1 ILE C  82    10699   3857   4673   -265   -414    305       C  
ATOM   2588  N   LEU C  83      11.738   7.793 -10.704  1.00 52.13           N  
ANISOU 2588  N   LEU C  83    11189   3966   4653   -312   -115    214       N  
ATOM   2589  CA  LEU C  83      12.808   7.231 -11.505  1.00 52.76           C  
ANISOU 2589  CA  LEU C  83    11377   4008   4661   -305     20    174       C  
ATOM   2590  C   LEU C  83      12.381   5.925 -12.137  1.00 53.30           C  
ANISOU 2590  C   LEU C  83    11539   4037   4676   -293    -60    125       C  
ATOM   2591  O   LEU C  83      12.515   5.729 -13.354  1.00 54.79           O  
ANISOU 2591  O   LEU C  83    11929   4169   4721   -281    -34     96       O  
ATOM   2592  CB  LEU C  83      14.041   6.980 -10.649  1.00 52.24           C  
ANISOU 2592  CB  LEU C  83    11154   3974   4720   -305    153    147       C  
ATOM   2593  CG  LEU C  83      15.237   6.468 -11.451  1.00 53.25           C  
ANISOU 2593  CG  LEU C  83    11351   4067   4816   -293    319     76       C  
ATOM   2594  CD1 LEU C  83      15.801   7.587 -12.320  1.00 53.66           C  
ANISOU 2594  CD1 LEU C  83    11526   4090   4772   -331    483     83       C  
ATOM   2595  CD2 LEU C  83      16.311   5.912 -10.538  1.00 52.42           C  
ANISOU 2595  CD2 LEU C  83    11058   3985   4873   -262    380     18       C  
ATOM   2596  N   LYS C  84      11.865   5.019 -11.327  1.00 52.40           N  
ANISOU 2596  N   LYS C  84    11308   3939   4663   -304   -151    112       N  
ATOM   2597  CA  LYS C  84      11.479   3.731 -11.883  1.00 53.10           C  
ANISOU 2597  CA  LYS C  84    11486   3977   4713   -304   -226     59       C  
ATOM   2598  C   LYS C  84      10.430   3.879 -12.988  1.00 54.18           C  
ANISOU 2598  C   LYS C  84    11775   4075   4736   -301   -372     41       C  
ATOM   2599  O   LYS C  84      10.472   3.173 -13.997  1.00 55.58           O  
ANISOU 2599  O   LYS C  84    12121   4193   4805   -285   -395     -9       O  
ATOM   2600  CB  LYS C  84      10.995   2.782 -10.803  1.00 52.35           C  
ANISOU 2600  CB  LYS C  84    11269   3884   4739   -339   -292     53       C  
ATOM   2601  CG  LYS C  84      12.083   2.295  -9.871  1.00 51.76           C  
ANISOU 2601  CG  LYS C  84    11114   3808   4744   -316   -197     53       C  
ATOM   2602  CD  LYS C  84      11.512   1.222  -8.975  1.00 52.69           C  
ANISOU 2602  CD  LYS C  84    11201   3887   4931   -358   -270     53       C  
ATOM   2603  CE  LYS C  84      12.093   1.281  -7.598  1.00 53.26           C  
ANISOU 2603  CE  LYS C  84    11182   3969   5084   -347   -234     87       C  
ATOM   2604  NZ  LYS C  84      11.042   0.938  -6.630  1.00 53.08           N  
ANISOU 2604  NZ  LYS C  84    11134   3931   5104   -432   -287    116       N  
ATOM   2605  N   MET C  85       9.495   4.809 -12.815  1.00 54.02           N  
ANISOU 2605  N   MET C  85    11703   4081   4741   -304   -486     69       N  
ATOM   2606  CA  MET C  85       8.473   4.998 -13.835  1.00 54.86           C  
ANISOU 2606  CA  MET C  85    11948   4141   4755   -276   -674     36       C  
ATOM   2607  C   MET C  85       9.033   5.634 -15.100  1.00 56.05           C  
ANISOU 2607  C   MET C  85    12377   4227   4694   -230   -629     53       C  
ATOM   2608  O   MET C  85       8.654   5.235 -16.214  1.00 57.48           O  
ANISOU 2608  O   MET C  85    12771   4336   4734   -202   -744      8       O  
ATOM   2609  CB  MET C  85       7.275   5.764 -13.301  1.00 54.37           C  
ANISOU 2609  CB  MET C  85    11736   4115   4807   -274   -830     34       C  
ATOM   2610  CG  MET C  85       6.371   4.936 -12.451  1.00 54.12           C  
ANISOU 2610  CG  MET C  85    11495   4115   4952   -338   -899    -20       C  
ATOM   2611  SD  MET C  85       5.027   5.878 -11.681  1.00 57.08           S  
ANISOU 2611  SD  MET C  85    11639   4544   5503   -342  -1026    -52       S  
ATOM   2612  CE  MET C  85       5.894   6.745 -10.374  1.00 52.03           C  
ANISOU 2612  CE  MET C  85    10884   3972   4912   -356   -820     43       C  
ATOM   2613  N   SER C  86       9.941   6.595 -14.945  1.00 55.62           N  
ANISOU 2613  N   SER C  86    12343   4185   4606   -233   -457    112       N  
ATOM   2614  CA  SER C  86      10.549   7.236 -16.118  1.00 57.52           C  
ANISOU 2614  CA  SER C  86    12877   4347   4632   -217   -360    131       C  
ATOM   2615  C   SER C  86      11.260   6.185 -16.966  1.00 58.91           C  
ANISOU 2615  C   SER C  86    13216   4475   4694   -224   -242     72       C  
ATOM   2616  O   SER C  86      11.153   6.162 -18.201  1.00 60.64           O  
ANISOU 2616  O   SER C  86    13740   4603   4699   -202   -274     52       O  
ATOM   2617  CB  SER C  86      11.552   8.311 -15.707  1.00 56.98           C  
ANISOU 2617  CB  SER C  86    12770   4297   4583   -250   -144    187       C  
ATOM   2618  OG  SER C  86      10.948   9.271 -14.875  1.00 56.25           O  
ANISOU 2618  OG  SER C  86    12530   4244   4597   -240   -244    236       O  
ATOM   2619  N   VAL C  87      11.989   5.309 -16.281  1.00 58.29           N  
ANISOU 2619  N   VAL C  87    12949   4446   4753   -244   -114     36       N  
ATOM   2620  CA  VAL C  87      12.649   4.200 -16.933  1.00 59.49           C  
ANISOU 2620  CA  VAL C  87    13208   4555   4840   -237    -10    -40       C  
ATOM   2621  C   VAL C  87      11.673   3.389 -17.769  1.00 60.77           C  
ANISOU 2621  C   VAL C  87    13548   4653   4890   -213   -216    -87       C  
ATOM   2622  O   VAL C  87      12.049   2.858 -18.818  1.00 62.48           O  
ANISOU 2622  O   VAL C  87    13999   4798   4944   -198   -150   -143       O  
ATOM   2623  CB  VAL C  87      13.314   3.280 -15.897  1.00 58.25           C  
ANISOU 2623  CB  VAL C  87    12802   4449   4881   -236     69    -76       C  
ATOM   2624  CG1 VAL C  87      13.451   1.900 -16.441  1.00 59.47           C  
ANISOU 2624  CG1 VAL C  87    13050   4548   4997   -211     59   -160       C  
ATOM   2625  CG2 VAL C  87      14.662   3.817 -15.505  1.00 57.86           C  
ANISOU 2625  CG2 VAL C  87    12638   4435   4912   -245    308    -84       C  
ATOM   2626  N   LEU C  88      10.430   3.282 -17.306  1.00 60.38           N  
ANISOU 2626  N   LEU C  88    13381   4624   4934   -214   -458    -80       N  
ATOM   2627  CA  LEU C  88       9.431   2.470 -18.012  1.00 61.82           C  
ANISOU 2627  CA  LEU C  88    13686   4747   5056   -200   -683   -147       C  
ATOM   2628  C   LEU C  88       8.822   3.216 -19.197  1.00 63.68           C  
ANISOU 2628  C   LEU C  88    14209   4905   5082   -151   -844   -148       C  
ATOM   2629  O   LEU C  88       8.137   2.625 -20.047  1.00 65.01           O  
ANISOU 2629  O   LEU C  88    14550   5002   5150   -125  -1037   -217       O  
ATOM   2630  CB  LEU C  88       8.316   2.016 -17.068  1.00 61.05           C  
ANISOU 2630  CB  LEU C  88    13331   4694   5170   -237   -863   -168       C  
ATOM   2631  CG  LEU C  88       8.617   0.860 -16.126  1.00 59.97           C  
ANISOU 2631  CG  LEU C  88    13014   4579   5191   -288   -779   -188       C  
ATOM   2632  CD1 LEU C  88       7.336   0.333 -15.514  1.00 59.91           C  
ANISOU 2632  CD1 LEU C  88    12836   4580   5347   -350   -956   -229       C  
ATOM   2633  CD2 LEU C  88       9.303  -0.241 -16.897  1.00 60.98           C  
ANISOU 2633  CD2 LEU C  88    13323   4634   5214   -268   -708   -251       C  
ATOM   2634  N   ASN C  89       9.067   4.520 -19.261  1.00 63.86           N  
ANISOU 2634  N   ASN C  89    14307   4927   5029   -135   -782    -74       N  
ATOM   2635  CA  ASN C  89       8.520   5.274 -20.377  1.00 66.12           C  
ANISOU 2635  CA  ASN C  89    14920   5111   5090    -76   -950    -65       C  
ATOM   2636  C   ASN C  89       9.076   4.771 -21.706  1.00 68.39           C  
ANISOU 2636  C   ASN C  89    15593   5291   5103    -65   -866   -106       C  
ATOM   2637  O   ASN C  89      10.275   4.569 -21.853  1.00 68.37           O  
ANISOU 2637  O   ASN C  89    15651   5287   5040   -108   -560   -104       O  
ATOM   2638  CB  ASN C  89       8.744   6.771 -20.218  1.00 65.69           C  
ANISOU 2638  CB  ASN C  89    14922   5049   4989    -65   -884     28       C  
ATOM   2639  CG  ASN C  89       7.755   7.557 -20.996  1.00 67.47           C  
ANISOU 2639  CG  ASN C  89    15398   5173   5062     21  -1175     33       C  
ATOM   2640  OD1 ASN C  89       6.562   7.260 -20.948  1.00 68.55           O  
ANISOU 2640  OD1 ASN C  89    15428   5315   5303     74  -1485    -33       O  
ATOM   2641  ND2 ASN C  89       8.227   8.558 -21.739  1.00 68.34           N  
ANISOU 2641  ND2 ASN C  89    15857   5178   4931     35  -1088    101       N  
ATOM   2642  N   GLN C  90       8.195   4.554 -22.670  1.00 70.87           N  
ANISOU 2642  N   GLN C  90    16161   5508   5257     -5  -1142   -159       N  
ATOM   2643  CA  GLN C  90       8.628   4.059 -23.966  1.00 73.49           C  
ANISOU 2643  CA  GLN C  90    16902   5723   5299      9  -1081   -205       C  
ATOM   2644  C   GLN C  90       9.828   4.863 -24.489  1.00 73.90           C  
ANISOU 2644  C   GLN C  90    17230   5717   5130    -28   -742   -139       C  
ATOM   2645  O   GLN C  90      10.840   4.275 -24.863  1.00 74.28           O  
ANISOU 2645  O   GLN C  90    17375   5750   5096    -73   -455   -180       O  
ATOM   2646  CB  GLN C  90       7.464   4.075 -24.963  1.00 76.26           C  
ANISOU 2646  CB  GLN C  90    17547   5956   5473     97  -1472   -260       C  
ATOM   2647  CG  GLN C  90       7.745   3.357 -26.264  1.00 81.02           C  
ANISOU 2647  CG  GLN C  90    18576   6432   5775    115  -1459   -329       C  
ATOM   2648  CD  GLN C  90       6.928   3.922 -27.450  1.00 87.39           C  
ANISOU 2648  CD  GLN C  90    19843   7077   6284    217  -1794   -343       C  
ATOM   2649  OE1 GLN C  90       6.610   3.188 -28.399  1.00 90.26           O  
ANISOU 2649  OE1 GLN C  90    20494   7338   6461    257  -1963   -434       O  
ATOM   2650  NE2 GLN C  90       6.594   5.223 -27.398  1.00 88.25           N  
ANISOU 2650  NE2 GLN C  90    20041   7147   6342    268  -1909   -259       N  
ATOM   2651  N   GLU C  91       9.727   6.195 -24.499  1.00 73.66           N  
ANISOU 2651  N   GLU C  91    17318   5649   5021    -16   -759    -48       N  
ATOM   2652  CA  GLU C  91      10.816   7.027 -25.030  1.00 74.39           C  
ANISOU 2652  CA  GLU C  91    17702   5664   4898    -77   -423     13       C  
ATOM   2653  C   GLU C  91      12.158   6.701 -24.357  1.00 72.69           C  
ANISOU 2653  C   GLU C  91    17204   5553   4861   -174     -9     -6       C  
ATOM   2654  O   GLU C  91      13.197   6.681 -24.997  1.00 74.31           O  
ANISOU 2654  O   GLU C  91    17621   5701   4911   -238    320    -32       O  
ATOM   2655  CB  GLU C  91      10.501   8.528 -24.937  1.00 74.66           C  
ANISOU 2655  CB  GLU C  91    17861   5641   4867    -57   -506    118       C  
ATOM   2656  CG  GLU C  91       9.415   9.020 -25.881  1.00 77.10           C  
ANISOU 2656  CG  GLU C  91    18578   5792   4923     56   -885    132       C  
ATOM   2657  CD  GLU C  91       8.018   8.778 -25.343  1.00 77.39           C  
ANISOU 2657  CD  GLU C  91    18324   5895   5187    160  -1328     81       C  
ATOM   2658  OE1 GLU C  91       7.168   9.692 -25.434  1.00 78.07           O  
ANISOU 2658  OE1 GLU C  91    18514   5909   5239    256  -1622    111       O  
ATOM   2659  OE2 GLU C  91       7.773   7.670 -24.807  1.00 77.57           O  
ANISOU 2659  OE2 GLU C  91    18005   6032   5435    144  -1375      0       O  
ATOM   2660  N   SER C  92      12.136   6.440 -23.059  1.00 69.89           N  
ANISOU 2660  N   SER C  92    16373   5344   4837   -183    -28     -6       N  
ATOM   2661  CA  SER C  92      13.356   6.043 -22.336  1.00 68.12           C  
ANISOU 2661  CA  SER C  92    15855   5214   4812   -247    296    -42       C  
ATOM   2662  C   SER C  92      13.880   4.700 -22.829  1.00 68.87           C  
ANISOU 2662  C   SER C  92    15995   5295   4877   -242    412   -154       C  
ATOM   2663  O   SER C  92      15.040   4.583 -23.211  1.00 70.12           O  
ANISOU 2663  O   SER C  92    16219   5433   4989   -290    743   -210       O  
ATOM   2664  CB  SER C  92      13.089   5.960 -20.849  1.00 65.13           C  
ANISOU 2664  CB  SER C  92    15016   4972   4759   -241    193    -19       C  
ATOM   2665  OG  SER C  92      12.301   7.058 -20.463  1.00 64.41           O  
ANISOU 2665  OG  SER C  92    14899   4886   4690   -223     14     65       O  
ATOM   2666  N   ILE C  93      13.030   3.682 -22.812  1.00 68.12           N  
ANISOU 2666  N   ILE C  93    15851   5205   4825   -188    149   -200       N  
ATOM   2667  CA  ILE C  93      13.427   2.390 -23.337  1.00 68.89           C  
ANISOU 2667  CA  ILE C  93    16028   5269   4879   -174    227   -309       C  
ATOM   2668  C   ILE C  93      14.107   2.580 -24.682  1.00 71.40           C  
ANISOU 2668  C   ILE C  93    16771   5470   4887   -195    459   -350       C  
ATOM   2669  O   ILE C  93      15.187   2.043 -24.914  1.00 72.04           O  
ANISOU 2669  O   ILE C  93    16846   5548   4978   -218    759   -437       O  
ATOM   2670  CB  ILE C  93      12.215   1.460 -23.552  1.00 69.28           C  
ANISOU 2670  CB  ILE C  93    16119   5285   4919   -125   -124   -354       C  
ATOM   2671  CG1 ILE C  93      11.218   1.573 -22.392  1.00 66.91           C  
ANISOU 2671  CG1 ILE C  93    15478   5073   4871   -123   -380   -305       C  
ATOM   2672  CG2 ILE C  93      12.676   0.015 -23.716  1.00 69.24           C  
ANISOU 2672  CG2 ILE C  93    16092   5262   4956   -112    -44   -466       C  
ATOM   2673  CD1 ILE C  93      11.123   0.342 -21.584  1.00 64.71           C  
ANISOU 2673  CD1 ILE C  93    14926   4844   4818   -133   -426   -358       C  
ATOM   2674  N   ALA C  94      13.462   3.360 -25.553  1.00 72.86           N  
ANISOU 2674  N   ALA C  94    17336   5550   4797   -182    318   -294       N  
ATOM   2675  CA  ALA C  94      13.927   3.576 -26.914  1.00 75.41           C  
ANISOU 2675  CA  ALA C  94    18162   5730   4761   -205    507   -321       C  
ATOM   2676  C   ALA C  94      15.363   4.067 -26.933  1.00 76.11           C  
ANISOU 2676  C   ALA C  94    18236   5827   4855   -304    993   -337       C  
ATOM   2677  O   ALA C  94      16.177   3.549 -27.680  1.00 78.12           O  
ANISOU 2677  O   ALA C  94    18679   6025   4978   -337   1279   -435       O  
ATOM   2678  CB  ALA C  94      13.001   4.542 -27.647  1.00 76.81           C  
ANISOU 2678  CB  ALA C  94    18745   5782   4657   -167    247   -235       C  
ATOM   2679  N   SER C  95      15.680   5.047 -26.094  1.00 74.84           N  
ANISOU 2679  N   SER C  95    17832   5737   4869   -355   1093   -258       N  
ATOM   2680  CA  SER C  95      16.991   5.689 -26.135  1.00 76.07           C  
ANISOU 2680  CA  SER C  95    17974   5888   5041   -467   1546   -280       C  
ATOM   2681  C   SER C  95      18.108   4.728 -25.813  1.00 76.12           C  
ANISOU 2681  C   SER C  95    17673   5976   5274   -483   1829   -425       C  
ATOM   2682  O   SER C  95      19.253   4.953 -26.163  1.00 77.90           O  
ANISOU 2682  O   SER C  95    17932   6177   5489   -573   2238   -503       O  
ATOM   2683  CB  SER C  95      17.060   6.824 -25.129  1.00 74.33           C  
ANISOU 2683  CB  SER C  95    17485   5738   5018   -510   1549   -181       C  
ATOM   2684  OG  SER C  95      17.312   6.298 -23.850  1.00 71.36           O  
ANISOU 2684  OG  SER C  95    16580   5519   5016   -482   1508   -219       O  
ATOM   2685  N   GLY C  96      17.775   3.659 -25.114  1.00 74.80           N  
ANISOU 2685  N   GLY C  96    17196   5898   5328   -396   1611   -470       N  
ATOM   2686  CA  GLY C  96      18.779   2.698 -24.691  1.00 75.04           C  
ANISOU 2686  CA  GLY C  96    16916   5996   5600   -378   1815   -609       C  
ATOM   2687  C   GLY C  96      19.789   3.265 -23.710  1.00 74.54           C  
ANISOU 2687  C   GLY C  96    16458   6031   5835   -428   2038   -631       C  
ATOM   2688  O   GLY C  96      20.821   2.657 -23.454  1.00 75.16           O  
ANISOU 2688  O   GLY C  96    16290   6149   6116   -414   2252   -770       O  
ATOM   2689  N   ASN C  97      19.499   4.429 -23.145  1.00 73.67           N  
ANISOU 2689  N   ASN C  97    16277   5950   5763   -475   1971   -508       N  
ATOM   2690  CA  ASN C  97      20.440   5.068 -22.224  1.00 73.13           C  
ANISOU 2690  CA  ASN C  97    15851   5965   5970   -531   2166   -532       C  
ATOM   2691  C   ASN C  97      20.007   5.053 -20.763  1.00 70.27           C  
ANISOU 2691  C   ASN C  97    15104   5716   5881   -469   1887   -466       C  
ATOM   2692  O   ASN C  97      20.692   5.616 -19.906  1.00 69.37           O  
ANISOU 2692  O   ASN C  97    14696   5668   5992   -503   1992   -480       O  
ATOM   2693  CB  ASN C  97      20.677   6.505 -22.648  1.00 74.38           C  
ANISOU 2693  CB  ASN C  97    16223   6057   5979   -656   2375   -459       C  
ATOM   2694  CG  ASN C  97      21.327   6.591 -23.982  1.00 78.85           C  
ANISOU 2694  CG  ASN C  97    17163   6504   6293   -748   2735   -537       C  
ATOM   2695  OD1 ASN C  97      21.494   7.666 -24.548  1.00 82.71           O  
ANISOU 2695  OD1 ASN C  97    17936   6898   6592   -863   2932   -479       O  
ATOM   2696  ND2 ASN C  97      21.698   5.449 -24.510  1.00 81.17           N  
ANISOU 2696  ND2 ASN C  97    17487   6786   6568   -701   2837   -673       N  
ATOM   2697  N   PHE C  98      18.871   4.422 -20.476  1.00 68.76           N  
ANISOU 2697  N   PHE C  98    14920   5539   5667   -387   1541   -403       N  
ATOM   2698  CA  PHE C  98      18.317   4.512 -19.130  1.00 66.16           C  
ANISOU 2698  CA  PHE C  98    14287   5300   5550   -348   1293   -328       C  
ATOM   2699  C   PHE C  98      17.850   3.152 -18.663  1.00 65.56           C  
ANISOU 2699  C   PHE C  98    14087   5246   5577   -264   1077   -365       C  
ATOM   2700  O   PHE C  98      16.700   2.967 -18.282  1.00 64.33           O  
ANISOU 2700  O   PHE C  98    13926   5102   5415   -241    801   -291       O  
ATOM   2701  CB  PHE C  98      17.186   5.529 -19.081  1.00 65.09           C  
ANISOU 2701  CB  PHE C  98    14283   5152   5296   -366   1086   -188       C  
ATOM   2702  CG  PHE C  98      17.579   6.879 -19.604  1.00 66.19           C  
ANISOU 2702  CG  PHE C  98    14611   5236   5302   -449   1283   -139       C  
ATOM   2703  CD1 PHE C  98      17.455   7.186 -20.957  1.00 67.31           C  
ANISOU 2703  CD1 PHE C  98    15183   5256   5136   -482   1371   -129       C  
ATOM   2704  CD2 PHE C  98      18.100   7.842 -18.746  1.00 64.84           C  
ANISOU 2704  CD2 PHE C  98    14218   5117   5299   -501   1384   -107       C  
ATOM   2705  CE1 PHE C  98      17.834   8.437 -21.439  1.00 68.62           C  
ANISOU 2705  CE1 PHE C  98    15571   5343   5158   -573   1570    -77       C  
ATOM   2706  CE2 PHE C  98      18.473   9.094 -19.215  1.00 65.61           C  
ANISOU 2706  CE2 PHE C  98    14504   5146   5278   -594   1577    -63       C  
ATOM   2707  CZ  PHE C  98      18.338   9.393 -20.568  1.00 68.10           C  
ANISOU 2707  CZ  PHE C  98    15267   5328   5278   -634   1678    -43       C  
ATOM   2708  N   ASP C  99      18.758   2.190 -18.724  1.00 67.04           N  
ANISOU 2708  N   ASP C  99    14180   5427   5865   -223   1217   -493       N  
ATOM   2709  CA  ASP C  99      18.517   0.898 -18.137  1.00 66.61           C  
ANISOU 2709  CA  ASP C  99    13995   5377   5936   -144   1035   -533       C  
ATOM   2710  C   ASP C  99      18.716   1.011 -16.636  1.00 64.98           C  
ANISOU 2710  C   ASP C  99    13461   5246   5981   -118    940   -499       C  
ATOM   2711  O   ASP C  99      19.730   1.539 -16.161  1.00 64.57           O  
ANISOU 2711  O   ASP C  99    13213   5237   6084   -123   1099   -545       O  
ATOM   2712  CB  ASP C  99      19.450  -0.136 -18.749  1.00 68.34           C  
ANISOU 2712  CB  ASP C  99    14246   5547   6174    -89   1208   -692       C  
ATOM   2713  CG  ASP C  99      19.133  -0.377 -20.190  1.00 70.90           C  
ANISOU 2713  CG  ASP C  99    14934   5784   6222   -110   1274   -726       C  
ATOM   2714  OD1 ASP C  99      19.864  -1.116 -20.893  1.00 72.10           O  
ANISOU 2714  OD1 ASP C  99    15166   5884   6343    -75   1453   -865       O  
ATOM   2715  OD2 ASP C  99      18.114   0.199 -20.614  1.00 72.48           O  
ANISOU 2715  OD2 ASP C  99    15347   5961   6230   -152   1128   -619       O  
ATOM   2716  N   TYR C 100      17.729   0.521 -15.893  1.00 63.72           N  
ANISOU 2716  N   TYR C 100    13255   5094   5861   -100    682   -426       N  
ATOM   2717  CA  TYR C 100      17.800   0.586 -14.454  1.00 62.29           C  
ANISOU 2717  CA  TYR C 100    12826   4966   5875    -81    580   -385       C  
ATOM   2718  C   TYR C 100      19.076  -0.114 -13.989  1.00 62.76           C  
ANISOU 2718  C   TYR C 100    12714   5015   6116      4    668   -505       C  
ATOM   2719  O   TYR C 100      19.769   0.366 -13.090  1.00 62.09           O  
ANISOU 2719  O   TYR C 100    12419   4976   6196     23    695   -517       O  
ATOM   2720  CB  TYR C 100      16.554  -0.039 -13.827  1.00 61.44           C  
ANISOU 2720  CB  TYR C 100    12732   4844   5766    -90    332   -311       C  
ATOM   2721  CG  TYR C 100      16.515   0.111 -12.325  1.00 61.81           C  
ANISOU 2721  CG  TYR C 100    12581   4933   5971    -85    239   -254       C  
ATOM   2722  CD1 TYR C 100      16.046   1.286 -11.733  1.00 60.49           C  
ANISOU 2722  CD1 TYR C 100    12332   4833   5820   -137    211   -164       C  
ATOM   2723  CD2 TYR C 100      16.966  -0.915 -11.493  1.00 63.82           C  
ANISOU 2723  CD2 TYR C 100    12759   5145   6345    -20    173   -296       C  
ATOM   2724  CE1 TYR C 100      16.025   1.434 -10.368  1.00 60.65           C  
ANISOU 2724  CE1 TYR C 100    12201   4883   5960   -134    137   -119       C  
ATOM   2725  CE2 TYR C 100      16.946  -0.774 -10.106  1.00 63.85           C  
ANISOU 2725  CE2 TYR C 100    12634   5168   6458    -13     82   -242       C  
ATOM   2726  CZ  TYR C 100      16.473   0.400  -9.558  1.00 63.16           C  
ANISOU 2726  CZ  TYR C 100    12470   5154   6373    -75     73   -155       C  
ATOM   2727  OH  TYR C 100      16.456   0.537  -8.187  1.00 66.19           O  
ANISOU 2727  OH  TYR C 100    12756   5549   6843    -70     -7   -108       O  
ATOM   2728  N   ALA C 101      19.401  -1.236 -14.630  1.00 63.85           N  
ANISOU 2728  N   ALA C 101    12944   5085   6231     64    700   -609       N  
ATOM   2729  CA  ALA C 101      20.563  -2.021 -14.229  1.00 64.35           C  
ANISOU 2729  CA  ALA C 101    12847   5121   6482    172    748   -745       C  
ATOM   2730  C   ALA C 101      21.875  -1.246 -14.377  1.00 65.34           C  
ANISOU 2730  C   ALA C 101    12794   5295   6739    174    995   -856       C  
ATOM   2731  O   ALA C 101      22.946  -1.746 -14.059  1.00 66.45           O  
ANISOU 2731  O   ALA C 101    12752   5421   7076    273   1043  -1000       O  
ATOM   2732  CB  ALA C 101      20.614  -3.307 -14.999  1.00 65.29           C  
ANISOU 2732  CB  ALA C 101    13118   5150   6540    237    747   -844       C  
ATOM   2733  N   VAL C 102      21.800  -0.020 -14.859  1.00 65.31           N  
ANISOU 2733  N   VAL C 102    12839   5336   6640     66   1150   -802       N  
ATOM   2734  CA  VAL C 102      23.019   0.758 -14.982  1.00 66.50           C  
ANISOU 2734  CA  VAL C 102    12818   5523   6928     35   1409   -912       C  
ATOM   2735  C   VAL C 102      22.933   2.046 -14.216  1.00 65.37           C  
ANISOU 2735  C   VAL C 102    12548   5445   6844    -39   1389   -814       C  
ATOM   2736  O   VAL C 102      23.749   2.325 -13.342  1.00 65.78           O  
ANISOU 2736  O   VAL C 102    12334   5536   7125     -6   1390   -883       O  
ATOM   2737  CB  VAL C 102      23.298   1.145 -16.417  1.00 68.31           C  
ANISOU 2737  CB  VAL C 102    13253   5719   6984    -52   1707   -969       C  
ATOM   2738  CG1 VAL C 102      24.538   2.014 -16.451  1.00 69.41           C  
ANISOU 2738  CG1 VAL C 102    13192   5891   7290   -116   2003  -1088       C  
ATOM   2739  CG2 VAL C 102      23.457  -0.087 -17.277  1.00 69.08           C  
ANISOU 2739  CG2 VAL C 102    13492   5746   7009     18   1761  -1087       C  
ATOM   2740  N   ILE C 103      21.939   2.839 -14.574  1.00 64.47           N  
ANISOU 2740  N   ILE C 103    12636   5334   6525   -130   1355   -665       N  
ATOM   2741  CA  ILE C 103      21.647   4.065 -13.874  1.00 63.22           C  
ANISOU 2741  CA  ILE C 103    12400   5225   6394   -196   1307   -556       C  
ATOM   2742  C   ILE C 103      21.698   3.879 -12.371  1.00 61.75           C  
ANISOU 2742  C   ILE C 103    11973   5084   6405   -126   1100   -539       C  
ATOM   2743  O   ILE C 103      22.291   4.693 -11.664  1.00 61.82           O  
ANISOU 2743  O   ILE C 103    11794   5133   6561   -148   1139   -557       O  
ATOM   2744  CB  ILE C 103      20.235   4.493 -14.169  1.00 62.03           C  
ANISOU 2744  CB  ILE C 103    12483   5063   6024   -241   1156   -396       C  
ATOM   2745  CG1 ILE C 103      20.127   5.032 -15.556  1.00 63.36           C  
ANISOU 2745  CG1 ILE C 103    12935   5173   5964   -316   1330   -385       C  
ATOM   2746  CG2 ILE C 103      19.805   5.598 -13.237  1.00 61.44           C  
ANISOU 2746  CG2 ILE C 103    12306   5038   6002   -280   1056   -288       C  
ATOM   2747  CD1 ILE C 103      18.741   5.509 -15.776  1.00 63.73           C  
ANISOU 2747  CD1 ILE C 103    13188   5202   5825   -335   1130   -245       C  
ATOM   2748  N   LYS C 104      21.036   2.833 -11.892  1.00 60.66           N  
ANISOU 2748  N   LYS C 104    11872   4925   6253    -53    880   -502       N  
ATOM   2749  CA  LYS C 104      20.781   2.677 -10.469  1.00 59.57           C  
ANISOU 2749  CA  LYS C 104    11602   4805   6226     -5    667   -447       C  
ATOM   2750  C   LYS C 104      22.083   2.592  -9.693  1.00 60.06           C  
ANISOU 2750  C   LYS C 104    11421   4876   6524     76    680   -573       C  
ATOM   2751  O   LYS C 104      22.312   3.351  -8.739  1.00 59.53           O  
ANISOU 2751  O   LYS C 104    11211   4849   6560     68    623   -550       O  
ATOM   2752  CB  LYS C 104      19.934   1.432 -10.212  1.00 59.27           C  
ANISOU 2752  CB  LYS C 104    11683   4715   6124     43    472   -404       C  
ATOM   2753  CG  LYS C 104      19.058   1.543  -9.004  1.00 59.44           C  
ANISOU 2753  CG  LYS C 104    11689   4748   6146     24    283   -288       C  
ATOM   2754  CD  LYS C 104      19.785   2.262  -7.892  1.00 62.14           C  
ANISOU 2754  CD  LYS C 104    11845   5130   6635     51    264   -301       C  
ATOM   2755  CE  LYS C 104      18.806   2.871  -6.918  1.00 61.70           C  
ANISOU 2755  CE  LYS C 104    11803   5106   6535     -7    148   -174       C  
ATOM   2756  NZ  LYS C 104      19.279   2.427  -5.589  1.00 63.61           N  
ANISOU 2756  NZ  LYS C 104    11975   5314   6880     71     10   -193       N  
ATOM   2757  N   PRO C 105      22.960   1.676 -10.107  1.00 61.37           N  
ANISOU 2757  N   PRO C 105    11532   5000   6788    164    743   -724       N  
ATOM   2758  CA  PRO C 105      24.214   1.584  -9.381  1.00 62.45           C  
ANISOU 2758  CA  PRO C 105    11409   5138   7180    262    723   -873       C  
ATOM   2759  C   PRO C 105      25.033   2.858  -9.548  1.00 62.91           C  
ANISOU 2759  C   PRO C 105    11286   5257   7359    176    935   -945       C  
ATOM   2760  O   PRO C 105      25.681   3.311  -8.602  1.00 63.21           O  
ANISOU 2760  O   PRO C 105    11110   5320   7588    212    857  -1003       O  
ATOM   2761  CB  PRO C 105      24.915   0.361 -10.007  1.00 63.97           C  
ANISOU 2761  CB  PRO C 105    11588   5268   7450    375    773  -1039       C  
ATOM   2762  CG  PRO C 105      24.153   0.030 -11.221  1.00 63.80           C  
ANISOU 2762  CG  PRO C 105    11823   5221   7198    306    884   -982       C  
ATOM   2763  CD  PRO C 105      22.774   0.565 -11.051  1.00 62.29           C  
ANISOU 2763  CD  PRO C 105    11811   5053   6802    203    774   -773       C  
ATOM   2764  N   ALA C 106      24.993   3.431 -10.742  1.00 63.17           N  
ANISOU 2764  N   ALA C 106    11431   5299   7272     58   1197   -944       N  
ATOM   2765  CA  ALA C 106      25.624   4.723 -10.991  1.00 64.18           C  
ANISOU 2765  CA  ALA C 106    11450   5464   7473    -64   1430   -987       C  
ATOM   2766  C   ALA C 106      25.191   5.797  -9.958  1.00 62.94           C  
ANISOU 2766  C   ALA C 106    11238   5349   7330   -114   1290   -861       C  
ATOM   2767  O   ALA C 106      25.998   6.604  -9.458  1.00 63.59           O  
ANISOU 2767  O   ALA C 106    11103   5457   7600   -150   1355   -942       O  
ATOM   2768  CB  ALA C 106      25.273   5.184 -12.377  1.00 64.25           C  
ANISOU 2768  CB  ALA C 106    11713   5446   7252   -192   1683   -939       C  
ATOM   2769  N   ILE C 107      23.900   5.813  -9.655  1.00 61.05           N  
ANISOU 2769  N   ILE C 107    11187   5111   6899   -120   1104   -676       N  
ATOM   2770  CA  ILE C 107      23.382   6.730  -8.688  1.00 59.83           C  
ANISOU 2770  CA  ILE C 107    11002   4991   6742   -156    971   -562       C  
ATOM   2771  C   ILE C 107      23.926   6.411  -7.302  1.00 60.20           C  
ANISOU 2771  C   ILE C 107    10841   5047   6986    -51    770   -624       C  
ATOM   2772  O   ILE C 107      24.312   7.305  -6.550  1.00 60.38           O  
ANISOU 2772  O   ILE C 107    10722   5096   7123    -78    746   -638       O  
ATOM   2773  CB  ILE C 107      21.871   6.668  -8.699  1.00 58.04           C  
ANISOU 2773  CB  ILE C 107    10998   4760   6295   -176    825   -386       C  
ATOM   2774  CG1 ILE C 107      21.386   7.218 -10.039  1.00 58.38           C  
ANISOU 2774  CG1 ILE C 107    11259   4781   6143   -270    990   -331       C  
ATOM   2775  CG2 ILE C 107      21.298   7.463  -7.513  1.00 55.96           C  
ANISOU 2775  CG2 ILE C 107    10685   4530   6046   -192    672   -284       C  
ATOM   2776  CD1 ILE C 107      19.901   7.268 -10.189  1.00 57.25           C  
ANISOU 2776  CD1 ILE C 107    11314   4631   5807   -285    838   -186       C  
ATOM   2777  N   ASP C 108      23.965   5.127  -6.975  1.00 60.66           N  
ANISOU 2777  N   ASP C 108    10908   5067   7074     72    613   -664       N  
ATOM   2778  CA  ASP C 108      24.502   4.685  -5.707  1.00 61.17           C  
ANISOU 2778  CA  ASP C 108    10835   5110   7298    195    392   -727       C  
ATOM   2779  C   ASP C 108      25.940   5.127  -5.578  1.00 63.01           C  
ANISOU 2779  C   ASP C 108    10782   5360   7800    226    472   -922       C  
ATOM   2780  O   ASP C 108      26.373   5.652  -4.541  1.00 63.52           O  
ANISOU 2780  O   ASP C 108    10703   5435   7998    258    338   -958       O  
ATOM   2781  CB  ASP C 108      24.388   3.173  -5.636  1.00 61.63           C  
ANISOU 2781  CB  ASP C 108    10990   5095   7330    321    243   -751       C  
ATOM   2782  CG  ASP C 108      22.958   2.734  -5.495  1.00 60.79           C  
ANISOU 2782  CG  ASP C 108    11136   4965   6996    279    135   -571       C  
ATOM   2783  OD1 ASP C 108      22.095   3.637  -5.314  1.00 61.36           O  
ANISOU 2783  OD1 ASP C 108    11272   5085   6957    173    152   -441       O  
ATOM   2784  OD2 ASP C 108      22.691   1.526  -5.541  1.00 61.60           O  
ANISOU 2784  OD2 ASP C 108    11362   4996   7048    349     35   -571       O  
ATOM   2785  N   LYS C 109      26.670   4.931  -6.660  1.00 64.47           N  
ANISOU 2785  N   LYS C 109    10884   5543   8067    208    703  -1062       N  
ATOM   2786  CA  LYS C 109      28.059   5.313  -6.728  1.00 66.63           C  
ANISOU 2786  CA  LYS C 109    10855   5833   8628    215    839  -1285       C  
ATOM   2787  C   LYS C 109      28.238   6.805  -6.493  1.00 66.34           C  
ANISOU 2787  C   LYS C 109    10717   5843   8647     71    953  -1264       C  
ATOM   2788  O   LYS C 109      29.117   7.233  -5.744  1.00 67.39           O  
ANISOU 2788  O   LYS C 109    10592   5987   9026    102    881  -1399       O  
ATOM   2789  CB  LYS C 109      28.619   4.951  -8.094  1.00 68.50           C  
ANISOU 2789  CB  LYS C 109    11072   6060   8894    176   1144  -1421       C  
ATOM   2790  CG  LYS C 109      30.120   4.938  -8.118  1.00 71.69           C  
ANISOU 2790  CG  LYS C 109    11120   6469   9649    222   1265  -1706       C  
ATOM   2791  CD  LYS C 109      30.620   5.158  -9.503  1.00 74.83           C  
ANISOU 2791  CD  LYS C 109    11511   6870  10051     93   1681  -1821       C  
ATOM   2792  CE  LYS C 109      32.130   5.059  -9.530  1.00 79.85           C  
ANISOU 2792  CE  LYS C 109    11748   7511  11079    138   1823  -2142       C  
ATOM   2793  NZ  LYS C 109      32.707   6.095 -10.432  1.00 82.74           N  
ANISOU 2793  NZ  LYS C 109    12040   7895  11502    -85   2266  -2237       N  
ATOM   2794  N   PHE C 110      27.398   7.599  -7.144  1.00 65.11           N  
ANISOU 2794  N   PHE C 110    10775   5701   8264    -80   1112  -1101       N  
ATOM   2795  CA  PHE C 110      27.469   9.042  -6.980  1.00 64.86           C  
ANISOU 2795  CA  PHE C 110    10698   5691   8254   -222   1223  -1063       C  
ATOM   2796  C   PHE C 110      27.285   9.450  -5.529  1.00 63.97           C  
ANISOU 2796  C   PHE C 110    10506   5596   8206   -165    943  -1011       C  
ATOM   2797  O   PHE C 110      28.033  10.282  -5.016  1.00 64.80           O  
ANISOU 2797  O   PHE C 110    10405   5711   8503   -209    962  -1110       O  
ATOM   2798  CB  PHE C 110      26.416   9.747  -7.824  1.00 63.39           C  
ANISOU 2798  CB  PHE C 110    10811   5495   7780   -356   1365   -875       C  
ATOM   2799  CG  PHE C 110      26.402  11.247  -7.637  1.00 62.49           C  
ANISOU 2799  CG  PHE C 110    10694   5382   7669   -494   1459   -820       C  
ATOM   2800  CD1 PHE C 110      25.512  11.859  -6.752  1.00 60.64           C  
ANISOU 2800  CD1 PHE C 110    10540   5161   7338   -486   1253   -667       C  
ATOM   2801  CD2 PHE C 110      27.290  12.046  -8.323  1.00 63.50           C  
ANISOU 2801  CD2 PHE C 110    10741   5485   7901   -638   1767   -932       C  
ATOM   2802  CE1 PHE C 110      25.505  13.247  -6.582  1.00 59.06           C  
ANISOU 2802  CE1 PHE C 110    10348   4949   7144   -604   1333   -624       C  
ATOM   2803  CE2 PHE C 110      27.292  13.423  -8.148  1.00 63.34           C  
ANISOU 2803  CE2 PHE C 110    10739   5445   7883   -772   1854   -882       C  
ATOM   2804  CZ  PHE C 110      26.392  14.021  -7.273  1.00 61.42           C  
ANISOU 2804  CZ  PHE C 110    10582   5213   7541   -746   1622   -725       C  
ATOM   2805  N   ALA C 111      26.275   8.867  -4.886  1.00 62.44           N  
ANISOU 2805  N   ALA C 111    10486   5395   7845    -80    699   -862       N  
ATOM   2806  CA  ALA C 111      25.957   9.164  -3.502  1.00 61.88           C  
ANISOU 2806  CA  ALA C 111    10406   5327   7779    -28    443   -797       C  
ATOM   2807  C   ALA C 111      27.146   8.866  -2.611  1.00 64.03           C  
ANISOU 2807  C   ALA C 111    10430   5582   8318     94    275   -984       C  
ATOM   2808  O   ALA C 111      27.539   9.695  -1.773  1.00 64.12           O  
ANISOU 2808  O   ALA C 111    10316   5602   8445     80    186  -1027       O  
ATOM   2809  CB  ALA C 111      24.776   8.351  -3.062  1.00 60.07           C  
ANISOU 2809  CB  ALA C 111    10406   5078   7340     37    255   -640       C  
ATOM   2810  N   ARG C 112      27.724   7.684  -2.795  1.00 65.76           N  
ANISOU 2810  N   ARG C 112    10579   5767   8640    224    213  -1107       N  
ATOM   2811  CA  ARG C 112      28.813   7.271  -1.939  1.00 68.58           C  
ANISOU 2811  CA  ARG C 112    10713   6090   9254    379     -5  -1298       C  
ATOM   2812  C   ARG C 112      30.007   8.208  -2.032  1.00 70.47           C  
ANISOU 2812  C   ARG C 112    10623   6362   9790    313    130  -1503       C  
ATOM   2813  O   ARG C 112      30.553   8.648  -1.016  1.00 71.32           O  
ANISOU 2813  O   ARG C 112    10577   6460  10060    367    -70  -1592       O  
ATOM   2814  CB  ARG C 112      29.228   5.851  -2.276  1.00 70.41           C  
ANISOU 2814  CB  ARG C 112    10929   6268   9554    537    -77  -1409       C  
ATOM   2815  CG  ARG C 112      28.428   4.812  -1.517  1.00 72.45           C  
ANISOU 2815  CG  ARG C 112    11456   6453   9619    662   -361  -1270       C  
ATOM   2816  CD  ARG C 112      29.160   3.467  -1.476  1.00 79.89           C  
ANISOU 2816  CD  ARG C 112    12342   7310  10703    868   -529  -1430       C  
ATOM   2817  NE  ARG C 112      28.584   2.520  -2.431  1.00 83.72           N  
ANISOU 2817  NE  ARG C 112    13008   7768  11032    861   -406  -1365       N  
ATOM   2818  CZ  ARG C 112      28.858   2.490  -3.740  1.00 85.92           C  
ANISOU 2818  CZ  ARG C 112    13203   8088  11355    790   -112  -1448       C  
ATOM   2819  NH1 ARG C 112      29.713   3.351  -4.278  1.00 87.73           N  
ANISOU 2819  NH1 ARG C 112    13167   8383  11783    705    124  -1601       N  
ATOM   2820  NH2 ARG C 112      28.274   1.591  -4.517  1.00 85.98           N  
ANISOU 2820  NH2 ARG C 112    13409   8059  11200    794    -42  -1386       N  
ATOM   2821  N   GLU C 113      30.412   8.514  -3.254  1.00 71.32           N  
ANISOU 2821  N   GLU C 113    10634   6499   9966    187    476  -1585       N  
ATOM   2822  CA  GLU C 113      31.538   9.413  -3.462  1.00 73.69           C  
ANISOU 2822  CA  GLU C 113    10621   6822  10557     83    671  -1792       C  
ATOM   2823  C   GLU C 113      31.297  10.777  -2.810  1.00 72.74           C  
ANISOU 2823  C   GLU C 113    10509   6717  10411    -42    646  -1704       C  
ATOM   2824  O   GLU C 113      32.193  11.373  -2.210  1.00 74.36           O  
ANISOU 2824  O   GLU C 113    10443   6923  10886    -50    584  -1877       O  
ATOM   2825  CB  GLU C 113      31.804   9.572  -4.959  1.00 74.69           C  
ANISOU 2825  CB  GLU C 113    10741   6959  10677    -71   1104  -1851       C  
ATOM   2826  CG  GLU C 113      31.900   8.239  -5.649  1.00 77.07           C  
ANISOU 2826  CG  GLU C 113    11083   7241  10960     48   1138  -1919       C  
ATOM   2827  CD  GLU C 113      32.353   8.346  -7.089  1.00 81.61           C  
ANISOU 2827  CD  GLU C 113    11636   7817  11556    -95   1578  -2025       C  
ATOM   2828  OE1 GLU C 113      31.990   9.353  -7.737  1.00 82.56           O  
ANISOU 2828  OE1 GLU C 113    11912   7941  11517   -300   1845  -1914       O  
ATOM   2829  OE2 GLU C 113      33.057   7.415  -7.568  1.00 83.70           O  
ANISOU 2829  OE2 GLU C 113    11753   8068  11982      3   1655  -2221       O  
ATOM   2830  N   GLN C 114      30.075  11.262  -2.934  1.00 70.47           N  
ANISOU 2830  N   GLN C 114    10528   6438   9812   -133    684  -1451       N  
ATOM   2831  CA  GLN C 114      29.700  12.545  -2.378  1.00 70.12           C  
ANISOU 2831  CA  GLN C 114    10534   6399   9709   -244    667  -1351       C  
ATOM   2832  C   GLN C 114      29.771  12.556  -0.863  1.00 70.08           C  
ANISOU 2832  C   GLN C 114    10473   6383   9772   -117    304  -1368       C  
ATOM   2833  O   GLN C 114      30.298  13.487  -0.251  1.00 70.97           O  
ANISOU 2833  O   GLN C 114    10430   6493  10043   -169    259  -1454       O  
ATOM   2834  CB  GLN C 114      28.280  12.863  -2.792  1.00 67.68           C  
ANISOU 2834  CB  GLN C 114    10568   6093   9054   -322    732  -1087       C  
ATOM   2835  CG  GLN C 114      28.174  13.296  -4.212  1.00 69.04           C  
ANISOU 2835  CG  GLN C 114    10851   6255   9127   -479   1081  -1052       C  
ATOM   2836  CD  GLN C 114      28.349  14.771  -4.345  1.00 69.94           C  
ANISOU 2836  CD  GLN C 114    10955   6348   9272   -655   1260  -1042       C  
ATOM   2837  OE1 GLN C 114      29.439  15.234  -4.688  1.00 73.85           O  
ANISOU 2837  OE1 GLN C 114    11240   6827   9993   -759   1472  -1219       O  
ATOM   2838  NE2 GLN C 114      27.282  15.532  -4.054  1.00 66.39           N  
ANISOU 2838  NE2 GLN C 114    10726   5888   8612   -692   1182   -849       N  
ATOM   2839  N   VAL C 115      29.210  11.522  -0.259  1.00 69.34           N  
ANISOU 2839  N   VAL C 115    10537   6270   9540     43     47  -1283       N  
ATOM   2840  CA  VAL C 115      29.261  11.378   1.173  1.00 69.67           C  
ANISOU 2840  CA  VAL C 115    10593   6278   9600    177   -305  -1294       C  
ATOM   2841  C   VAL C 115      30.715  11.314   1.631  1.00 73.14           C  
ANISOU 2841  C   VAL C 115    10697   6696  10397    275   -448  -1572       C  
ATOM   2842  O   VAL C 115      31.092  11.923   2.645  1.00 73.94           O  
ANISOU 2842  O   VAL C 115    10714   6778  10602    304   -652  -1641       O  
ATOM   2843  CB  VAL C 115      28.509  10.102   1.620  1.00 68.39           C  
ANISOU 2843  CB  VAL C 115    10682   6072   9230    325   -521  -1172       C  
ATOM   2844  CG1 VAL C 115      28.852   9.746   3.056  1.00 68.73           C  
ANISOU 2844  CG1 VAL C 115    10751   6049   9316    492   -896  -1230       C  
ATOM   2845  CG2 VAL C 115      27.005  10.286   1.457  1.00 65.45           C  
ANISOU 2845  CG2 VAL C 115    10612   5721   8536    228   -431   -917       C  
ATOM   2846  N   SER C 116      31.536  10.592   0.876  1.00 75.55           N  
ANISOU 2846  N   SER C 116    10802   7001  10904    328   -347  -1749       N  
ATOM   2847  CA  SER C 116      32.907  10.353   1.298  1.00 79.44           C  
ANISOU 2847  CA  SER C 116    10945   7468  11770    455   -515  -2045       C  
ATOM   2848  C   SER C 116      33.754  11.602   1.230  1.00 81.81           C  
ANISOU 2848  C   SER C 116    10939   7800  12347    302   -356  -2217       C  
ATOM   2849  O   SER C 116      34.783  11.666   1.884  1.00 84.17           O  
ANISOU 2849  O   SER C 116    10947   8075  12959    398   -564  -2458       O  
ATOM   2850  CB  SER C 116      33.551   9.257   0.466  1.00 81.05           C  
ANISOU 2850  CB  SER C 116    10995   7662  12137    555   -423  -2211       C  
ATOM   2851  OG  SER C 116      33.917   9.769  -0.796  1.00 82.01           O  
ANISOU 2851  OG  SER C 116    10959   7836  12367    364     14  -2293       O  
ATOM   2852  N   ILE C 117      33.327  12.587   0.441  1.00 81.98           N  
ANISOU 2852  N   ILE C 117    11034   7859  12257     67     -1  -2103       N  
ATOM   2853  CA  ILE C 117      33.942  13.919   0.495  1.00 84.65           C  
ANISOU 2853  CA  ILE C 117    11157   8204  12800   -110    148  -2220       C  
ATOM   2854  C   ILE C 117      34.031  14.415   1.931  1.00 85.82           C  
ANISOU 2854  C   ILE C 117    11283   8325  13000    -27   -221  -2244       C  
ATOM   2855  O   ILE C 117      35.063  14.914   2.357  1.00 88.35           O  
ANISOU 2855  O   ILE C 117    11285   8633  13650    -39   -300  -2484       O  
ATOM   2856  CB  ILE C 117      33.150  15.000  -0.291  1.00 82.90           C  
ANISOU 2856  CB  ILE C 117    11160   7995  12345   -355    494  -2016       C  
ATOM   2857  CG1 ILE C 117      33.015  14.641  -1.775  1.00 83.36           C  
ANISOU 2857  CG1 ILE C 117    11304   8064  12306   -458    873  -1980       C  
ATOM   2858  CG2 ILE C 117      33.829  16.349  -0.141  1.00 83.48           C  
ANISOU 2858  CG2 ILE C 117    11028   8051  12638   -536    627  -2144       C  
ATOM   2859  CD1 ILE C 117      34.337  14.680  -2.567  1.00 87.94           C  
ANISOU 2859  CD1 ILE C 117    11533   8644  13238   -556   1175  -2271       C  
ATOM   2860  N   PHE C 118      32.942  14.283   2.674  1.00 84.99           N  
ANISOU 2860  N   PHE C 118    11517   8206  12570     50   -439  -2007       N  
ATOM   2861  CA  PHE C 118      32.896  14.829   4.022  1.00 87.24           C  
ANISOU 2861  CA  PHE C 118    11851   8456  12840    112   -758  -2003       C  
ATOM   2862  C   PHE C 118      33.032  13.785   5.131  1.00 90.01           C  
ANISOU 2862  C   PHE C 118    12282   8750  13170    373  -1202  -2047       C  
ATOM   2863  O   PHE C 118      33.207  14.116   6.301  1.00 90.59           O  
ANISOU 2863  O   PHE C 118    12384   8776  13258    455  -1510  -2093       O  
ATOM   2864  CB  PHE C 118      31.628  15.662   4.211  1.00 83.99           C  
ANISOU 2864  CB  PHE C 118    11764   8054  12094     -7   -675  -1732       C  
ATOM   2865  CG  PHE C 118      31.634  16.957   3.446  1.00 83.08           C  
ANISOU 2865  CG  PHE C 118    11587   7957  12024   -248   -332  -1715       C  
ATOM   2866  CD1 PHE C 118      31.158  17.010   2.150  1.00 81.62           C  
ANISOU 2866  CD1 PHE C 118    11505   7796  11711   -381     19  -1599       C  
ATOM   2867  CD2 PHE C 118      32.118  18.114   4.023  1.00 83.46           C  
ANISOU 2867  CD2 PHE C 118    11503   7981  12230   -340   -373  -1816       C  
ATOM   2868  CE1 PHE C 118      31.158  18.191   1.447  1.00 81.51           C  
ANISOU 2868  CE1 PHE C 118    11492   7770  11708   -598    324  -1573       C  
ATOM   2869  CE2 PHE C 118      32.120  19.301   3.326  1.00 83.53           C  
ANISOU 2869  CE2 PHE C 118    11489   7980  12267   -567    -57  -1794       C  
ATOM   2870  CZ  PHE C 118      31.642  19.342   2.036  1.00 82.83           C  
ANISOU 2870  CZ  PHE C 118    11532   7904  12034   -695    293  -1668       C  
ATOM   2871  N   PHE C 119      32.954  12.517   4.743  1.00 46.16           N  
ATOM   2872  CA  PHE C 119      33.162  11.382   5.659  1.00 49.06           C  
ATOM   2873  C   PHE C 119      34.285  10.432   5.159  1.00 50.28           C  
ATOM   2874  O   PHE C 119      34.017   9.309   4.710  1.00 51.70           O  
ATOM   2875  CB  PHE C 119      31.829  10.644   5.882  1.00 48.92           C  
ATOM   2876  CG  PHE C 119      30.812  11.500   6.560  1.00 52.07           C  
ATOM   2877  CD1 PHE C 119      30.045  12.401   5.832  1.00 55.98           C  
ATOM   2878  CD2 PHE C 119      30.669  11.478   7.939  1.00 54.80           C  
ATOM   2879  CE1 PHE C 119      29.102  13.250   6.472  1.00 56.90           C  
ATOM   2880  CE2 PHE C 119      29.733  12.323   8.588  1.00 56.59           C  
ATOM   2881  CZ  PHE C 119      28.953  13.211   7.853  1.00 56.31           C  
TER    2882      PHE C 119                                                      
ATOM   2883  N   PRO D   2      55.587  22.898  22.137  1.00 74.08           N  
ANISOU 2883  N   PRO D   2    15981   5372   6796    -32   1130   2792       N  
ATOM   2884  CA  PRO D   2      56.883  22.965  21.497  1.00 72.75           C  
ANISOU 2884  CA  PRO D   2    15614   5189   6839    459    846   2722       C  
ATOM   2885  C   PRO D   2      57.106  24.367  21.001  1.00 67.96           C  
ANISOU 2885  C   PRO D   2    14325   5085   6410    484    688   2479       C  
ATOM   2886  O   PRO D   2      56.178  24.991  20.507  1.00 64.93           O  
ANISOU 2886  O   PRO D   2    13651   4916   6104    113    825   2305       O  
ATOM   2887  CB  PRO D   2      56.725  22.043  20.294  1.00 73.57           C  
ANISOU 2887  CB  PRO D   2    15919   4892   7141    323   1043   2603       C  
ATOM   2888  CG  PRO D   2      55.580  21.178  20.614  1.00 76.84           C  
ANISOU 2888  CG  PRO D   2    16815   4976   7403   -176   1326   2716       C  
ATOM   2889  CD  PRO D   2      54.663  22.023  21.401  1.00 75.79           C  
ANISOU 2889  CD  PRO D   2    16399   5262   7136   -503   1421   2739       C  
ATOM   2890  N   LYS D   3      58.343  24.833  21.108  1.00 67.87           N  
ANISOU 2890  N   LYS D   3    14051   5236   6501    916    383   2485       N  
ATOM   2891  CA  LYS D   3      58.672  26.203  20.819  1.00 64.43           C  
ANISOU 2891  CA  LYS D   3    13043   5230   6208    916    218   2292       C  
ATOM   2892  C   LYS D   3      59.407  26.284  19.511  1.00 63.39           C  
ANISOU 2892  C   LYS D   3    12579   5093   6413   1057    263   2137       C  
ATOM   2893  O   LYS D   3      60.256  25.450  19.231  1.00 66.43           O  
ANISOU 2893  O   LYS D   3    13061   5232   6949   1401    279   2210       O  
ATOM   2894  CB  LYS D   3      59.558  26.762  21.926  1.00 66.29           C  
ANISOU 2894  CB  LYS D   3    13197   5674   6318   1196   -178   2398       C  
ATOM   2895  CG  LYS D   3      60.253  28.051  21.582  1.00 64.17           C  
ANISOU 2895  CG  LYS D   3    12353   5759   6269   1226   -399   2212       C  
ATOM   2896  CD  LYS D   3      60.788  28.688  22.834  1.00 66.61           C  
ANISOU 2896  CD  LYS D   3    12691   6268   6350   1327   -824   2274       C  
ATOM   2897  CE  LYS D   3      61.672  29.843  22.525  1.00 65.51           C  
ANISOU 2897  CE  LYS D   3    11993   6416   6483   1329  -1094   2110       C  
ATOM   2898  NZ  LYS D   3      62.737  29.927  23.534  1.00 71.10           N  
ANISOU 2898  NZ  LYS D   3    12657   7240   7116   1556  -1661   2233       N  
ATOM   2899  N   ILE D   4      59.087  27.300  18.708  1.00 59.96           N  
ANISOU 2899  N   ILE D   4    11789   4906   6087    822    317   1932       N  
ATOM   2900  CA  ILE D   4      59.794  27.505  17.458  1.00 59.37           C  
ANISOU 2900  CA  ILE D   4    11462   4843   6255    913    419   1791       C  
ATOM   2901  C   ILE D   4      60.539  28.832  17.445  1.00 58.09           C  
ANISOU 2901  C   ILE D   4    10797   5024   6251    957    243   1716       C  
ATOM   2902  O   ILE D   4      60.026  29.872  17.875  1.00 56.22           O  
ANISOU 2902  O   ILE D   4    10435   5005   5920    754    108   1665       O  
ATOM   2903  CB  ILE D   4      58.844  27.453  16.288  1.00 57.79           C  
ANISOU 2903  CB  ILE D   4    11406   4550   6002    560    629   1637       C  
ATOM   2904  CG1 ILE D   4      58.448  26.000  16.029  1.00 61.25           C  
ANISOU 2904  CG1 ILE D   4    12363   4558   6349    508    817   1666       C  
ATOM   2905  CG2 ILE D   4      59.503  28.032  15.071  1.00 57.05           C  
ANISOU 2905  CG2 ILE D   4    11097   4537   6041    593    739   1492       C  
ATOM   2906  CD1 ILE D   4      57.680  25.799  14.747  1.00 60.80           C  
ANISOU 2906  CD1 ILE D   4    12517   4367   6218    145    946   1486       C  
ATOM   2907  N   GLN D   5      61.769  28.795  16.967  1.00 60.06           N  
ANISOU 2907  N   GLN D   5    10755   5295   6772   1221    281   1706       N  
ATOM   2908  CA  GLN D   5      62.503  30.016  16.746  1.00 59.50           C  
ANISOU 2908  CA  GLN D   5    10192   5509   6905   1162    185   1627       C  
ATOM   2909  C   GLN D   5      62.657  30.206  15.221  1.00 59.47           C  
ANISOU 2909  C   GLN D   5    10141   5452   7004   1047    569   1492       C  
ATOM   2910  O   GLN D   5      63.343  29.419  14.571  1.00 62.66           O  
ANISOU 2910  O   GLN D   5    10550   5695   7563   1292    860   1481       O  
ATOM   2911  CB  GLN D   5      63.858  29.930  17.458  1.00 63.06           C  
ANISOU 2911  CB  GLN D   5    10235   6089   7638   1501    -84   1739       C  
ATOM   2912  CG  GLN D   5      63.738  29.631  18.941  1.00 63.95           C  
ANISOU 2912  CG  GLN D   5    10555   6212   7530   1629   -510   1898       C  
ATOM   2913  CD  GLN D   5      65.074  29.291  19.607  1.00 69.73           C  
ANISOU 2913  CD  GLN D   5    10919   7036   8539   2034   -889   2058       C  
ATOM   2914  OE1 GLN D   5      65.997  30.109  19.635  1.00 71.55           O  
ANISOU 2914  OE1 GLN D   5    10573   7541   9072   1999  -1119   2012       O  
ATOM   2915  NE2 GLN D   5      65.174  28.079  20.155  1.00 72.79           N  
ANISOU 2915  NE2 GLN D   5    11632   7177   8847   2407   -990   2267       N  
ATOM   2916  N   THR D   6      61.993  31.201  14.641  1.00 56.67           N  
ANISOU 2916  N   THR D   6     9819   5188   6524    710    595   1398       N  
ATOM   2917  CA  THR D   6      62.246  31.521  13.234  1.00 57.96           C  
ANISOU 2917  CA  THR D   6    10012   5307   6704    583    924   1305       C  
ATOM   2918  C   THR D   6      62.929  32.849  13.081  1.00 58.68           C  
ANISOU 2918  C   THR D   6     9722   5599   6973    435    902   1293       C  
ATOM   2919  O   THR D   6      62.555  33.854  13.723  1.00 56.92           O  
ANISOU 2919  O   THR D   6     9409   5498   6720    265    605   1296       O  
ATOM   2920  CB  THR D   6      60.970  31.708  12.416  1.00 55.89           C  
ANISOU 2920  CB  THR D   6    10157   4947   6131    279    938   1242       C  
ATOM   2921  OG1 THR D   6      59.891  32.059  13.295  1.00 53.83           O  
ANISOU 2921  OG1 THR D   6     9907   4772   5776    157    628   1279       O  
ATOM   2922  CG2 THR D   6      60.642  30.455  11.614  1.00 57.92           C  
ANISOU 2922  CG2 THR D   6    10879   4923   6205    293   1173   1176       C  
ATOM   2923  N   TYR D   7      63.895  32.883  12.177  1.00 61.92           N  
ANISOU 2923  N   TYR D   7     9962   6004   7559    469   1278   1265       N  
ATOM   2924  CA  TYR D   7      64.521  34.151  11.841  1.00 63.09           C  
ANISOU 2924  CA  TYR D   7     9806   6292   7872    223   1351   1265       C  
ATOM   2925  C   TYR D   7      63.882  34.688  10.581  1.00 62.17           C  
ANISOU 2925  C   TYR D   7    10155   6037   7429    -57   1586   1237       C  
ATOM   2926  O   TYR D   7      64.097  34.150   9.502  1.00 64.63           O  
ANISOU 2926  O   TYR D   7    10737   6217   7604    -30   2022   1195       O  
ATOM   2927  CB  TYR D   7      66.018  33.952  11.701  1.00 68.16           C  
ANISOU 2927  CB  TYR D   7     9881   7052   8964    392   1652   1282       C  
ATOM   2928  CG  TYR D   7      66.572  33.445  12.993  1.00 70.63           C  
ANISOU 2928  CG  TYR D   7     9759   7505   9573    695   1256   1349       C  
ATOM   2929  CD1 TYR D   7      67.053  34.331  13.949  1.00 72.05           C  
ANISOU 2929  CD1 TYR D   7     9497   7906   9972    538    806   1378       C  
ATOM   2930  CD2 TYR D   7      66.551  32.080  13.296  1.00 72.67           C  
ANISOU 2930  CD2 TYR D   7    10158   7624   9828   1120   1268   1391       C  
ATOM   2931  CE1 TYR D   7      67.552  33.877  15.157  1.00 75.40           C  
ANISOU 2931  CE1 TYR D   7     9603   8462  10583    803    336   1457       C  
ATOM   2932  CE2 TYR D   7      67.046  31.610  14.511  1.00 75.17           C  
ANISOU 2932  CE2 TYR D   7    10163   8039  10358   1429    832   1506       C  
ATOM   2933  CZ  TYR D   7      67.549  32.517  15.437  1.00 76.86           C  
ANISOU 2933  CZ  TYR D   7     9922   8524  10756   1270    340   1543       C  
ATOM   2934  OH  TYR D   7      68.039  32.080  16.648  1.00 80.54           O  
ANISOU 2934  OH  TYR D   7    10153   9094  11353   1556   -190   1671       O  
ATOM   2935  N   VAL D   8      63.053  35.716  10.738  1.00 59.56           N  
ANISOU 2935  N   VAL D   8     9986   5707   6938   -290   1280   1261       N  
ATOM   2936  CA  VAL D   8      62.316  36.279   9.615  1.00 59.47           C  
ANISOU 2936  CA  VAL D   8    10454   5549   6591   -515   1353   1286       C  
ATOM   2937  C   VAL D   8      62.918  37.601   9.199  1.00 61.71           C  
ANISOU 2937  C   VAL D   8    10673   5814   6961   -776   1483   1351       C  
ATOM   2938  O   VAL D   8      63.779  38.136   9.894  1.00 62.95           O  
ANISOU 2938  O   VAL D   8    10371   6085   7464   -836   1451   1347       O  
ATOM   2939  CB  VAL D   8      60.859  36.505   9.975  1.00 56.04           C  
ANISOU 2939  CB  VAL D   8    10247   5084   5960   -539    924   1302       C  
ATOM   2940  CG1 VAL D   8      60.270  35.218  10.442  1.00 55.00           C  
ANISOU 2940  CG1 VAL D   8    10170   4955   5774   -376    835   1254       C  
ATOM   2941  CG2 VAL D   8      60.758  37.542  11.065  1.00 54.71           C  
ANISOU 2941  CG2 VAL D   8     9818   4992   5979   -558    627   1310       C  
ATOM   2942  N   ASN D   9      62.470  38.127   8.062  1.00 63.15           N  
ANISOU 2942  N   ASN D   9    11357   5829   6810   -968   1595   1422       N  
ATOM   2943  CA  ASN D   9      62.944  39.433   7.604  1.00 65.88           C  
ANISOU 2943  CA  ASN D   9    11783   6069   7178  -1258   1737   1526       C  
ATOM   2944  C   ASN D   9      62.134  40.552   8.238  1.00 63.87           C  
ANISOU 2944  C   ASN D   9    11603   5720   6944  -1307   1254   1575       C  
ATOM   2945  O   ASN D   9      61.109  40.313   8.889  1.00 60.53           O  
ANISOU 2945  O   ASN D   9    11177   5339   6482  -1107    865   1532       O  
ATOM   2946  CB  ASN D   9      62.919  39.533   6.077  1.00 69.37           C  
ANISOU 2946  CB  ASN D   9    12851   6323   7184  -1435   2104   1620       C  
ATOM   2947  CG  ASN D   9      61.515  39.451   5.512  1.00 68.86           C  
ANISOU 2947  CG  ASN D   9    13382   6126   6655  -1390   1698   1677       C  
ATOM   2948  OD1 ASN D   9      60.561  40.002   6.083  1.00 67.67           O  
ANISOU 2948  OD1 ASN D   9    13194   5959   6558  -1315   1184   1723       O  
ATOM   2949  ND2 ASN D   9      61.376  38.761   4.386  1.00 71.26           N  
ANISOU 2949  ND2 ASN D   9    14232   6334   6509  -1432   1922   1663       N  
ATOM   2950  N   ASN D  10      62.606  41.779   8.059  1.00 66.63           N  
ANISOU 2950  N   ASN D  10    12028   5912   7378  -1576   1336   1661       N  
ATOM   2951  CA  ASN D  10      62.000  42.907   8.731  1.00 65.80           C  
ANISOU 2951  CA  ASN D  10    12019   5641   7341  -1595    942   1675       C  
ATOM   2952  C   ASN D  10      60.558  43.140   8.320  1.00 64.91           C  
ANISOU 2952  C   ASN D  10    12365   5368   6928  -1401    610   1773       C  
ATOM   2953  O   ASN D  10      59.749  43.578   9.127  1.00 63.21           O  
ANISOU 2953  O   ASN D  10    12098   5108   6812  -1213    267   1725       O  
ATOM   2954  CB  ASN D  10      62.832  44.148   8.513  1.00 69.96           C  
ANISOU 2954  CB  ASN D  10    12630   5942   8008  -1977   1129   1754       C  
ATOM   2955  CG  ASN D  10      64.082  44.163   9.364  1.00 71.58           C  
ANISOU 2955  CG  ASN D  10    12205   6335   8657  -2178   1222   1624       C  
ATOM   2956  OD1 ASN D  10      64.032  43.889  10.556  1.00 68.84           O  
ANISOU 2956  OD1 ASN D  10    11511   6157   8488  -2017    890   1472       O  
ATOM   2957  ND2 ASN D  10      65.210  44.517   8.757  1.00 76.98           N  
ANISOU 2957  ND2 ASN D  10    12742   6990   9517  -2558   1662   1698       N  
ATOM   2958  N   ASN D  11      60.238  42.841   7.066  1.00 67.05           N  
ANISOU 2958  N   ASN D  11    13083   5561   6833  -1438    710   1906       N  
ATOM   2959  CA  ASN D  11      58.870  42.943   6.582  1.00 67.51           C  
ANISOU 2959  CA  ASN D  11    13507   5519   6626  -1258    293   2020       C  
ATOM   2960  C   ASN D  11      57.920  42.131   7.400  1.00 63.98           C  
ANISOU 2960  C   ASN D  11    12694   5299   6317   -987    -18   1889       C  
ATOM   2961  O   ASN D  11      57.027  42.657   8.060  1.00 63.60           O  
ANISOU 2961  O   ASN D  11    12508   5221   6437   -780   -339   1890       O  
ATOM   2962  CB  ASN D  11      58.785  42.390   5.191  1.00 70.36           C  
ANISOU 2962  CB  ASN D  11    14393   5831   6509  -1373    410   2125       C  
ATOM   2963  CG  ASN D  11      58.799  43.442   4.182  1.00 76.92           C  
ANISOU 2963  CG  ASN D  11    15866   6342   7020  -1539    415   2376       C  
ATOM   2964  OD1 ASN D  11      59.015  44.636   4.495  1.00 79.86           O  
ANISOU 2964  OD1 ASN D  11    16283   6480   7578  -1601    401   2478       O  
ATOM   2965  ND2 ASN D  11      58.571  43.043   2.925  1.00 82.63           N  
ANISOU 2965  ND2 ASN D  11    17208   6990   7197  -1640    429   2487       N  
ATOM   2966  N   VAL D  12      58.093  40.824   7.307  1.00 62.40           N  
ANISOU 2966  N   VAL D  12    12378   5292   6041   -988    134   1780       N  
ATOM   2967  CA  VAL D  12      57.301  39.907   8.086  1.00 59.67           C  
ANISOU 2967  CA  VAL D  12    11715   5137   5819   -813    -73   1667       C  
ATOM   2968  C   VAL D  12      57.207  40.405   9.534  1.00 57.49           C  
ANISOU 2968  C   VAL D  12    11032   4931   5881   -658   -166   1583       C  
ATOM   2969  O   VAL D  12      56.105  40.541  10.076  1.00 56.98           O  
ANISOU 2969  O   VAL D  12    10826   4908   5915   -488   -420   1577       O  
ATOM   2970  CB  VAL D  12      57.926  38.496   8.029  1.00 59.22           C  
ANISOU 2970  CB  VAL D  12    11598   5192   5710   -840    222   1544       C  
ATOM   2971  CG1 VAL D  12      57.208  37.517   8.978  1.00 56.33           C  
ANISOU 2971  CG1 VAL D  12    10946   4972   5484   -704     61   1449       C  
ATOM   2972  CG2 VAL D  12      57.972  38.003   6.573  1.00 62.01           C  
ANISOU 2972  CG2 VAL D  12    12494   5425   5643   -996    361   1575       C  
ATOM   2973  N   TYR D  13      58.352  40.697  10.147  1.00 56.94           N  
ANISOU 2973  N   TYR D  13    10777   4875   5984   -729     41   1512       N  
ATOM   2974  CA  TYR D  13      58.354  41.074  11.552  1.00 55.89           C  
ANISOU 2974  CA  TYR D  13    10374   4796   6064   -623    -74   1398       C  
ATOM   2975  C   TYR D  13      57.408  42.240  11.824  1.00 57.07           C  
ANISOU 2975  C   TYR D  13    10665   4764   6256   -498   -290   1418       C  
ATOM   2976  O   TYR D  13      56.582  42.214  12.752  1.00 56.10           O  
ANISOU 2976  O   TYR D  13    10403   4704   6209   -291   -395   1333       O  
ATOM   2977  CB  TYR D  13      59.759  41.441  11.999  1.00 56.90           C  
ANISOU 2977  CB  TYR D  13    10316   4937   6365   -797     63   1335       C  
ATOM   2978  CG  TYR D  13      59.893  41.488  13.495  1.00 56.07           C  
ANISOU 2978  CG  TYR D  13     9994   4931   6380   -711   -109   1192       C  
ATOM   2979  CD1 TYR D  13      59.988  42.693  14.162  1.00 57.33           C  
ANISOU 2979  CD1 TYR D  13    10254   4922   6605   -799   -250   1103       C  
ATOM   2980  CD2 TYR D  13      59.921  40.309  14.251  1.00 54.64           C  
ANISOU 2980  CD2 TYR D  13     9612   4962   6187   -551   -136   1146       C  
ATOM   2981  CE1 TYR D  13      60.104  42.729  15.545  1.00 57.74           C  
ANISOU 2981  CE1 TYR D  13    10234   5046   6658   -744   -426    945       C  
ATOM   2982  CE2 TYR D  13      60.044  40.338  15.621  1.00 54.36           C  
ANISOU 2982  CE2 TYR D  13     9499   5004   6152   -483   -316   1039       C  
ATOM   2983  CZ  TYR D  13      60.128  41.541  16.260  1.00 56.41           C  
ANISOU 2983  CZ  TYR D  13     9883   5126   6426   -585   -465    927       C  
ATOM   2984  OH  TYR D  13      60.240  41.558  17.621  1.00 58.31           O  
ANISOU 2984  OH  TYR D  13    10167   5425   6563   -538   -659    796       O  
ATOM   2985  N   GLU D  14      57.543  43.279  11.010  1.00 59.86           N  
ANISOU 2985  N   GLU D  14    11330   4856   6559   -605   -304   1539       N  
ATOM   2986  CA  GLU D  14      56.718  44.458  11.183  1.00 62.21           C  
ANISOU 2986  CA  GLU D  14    11822   4891   6926   -423   -499   1579       C  
ATOM   2987  C   GLU D  14      55.266  44.055  11.138  1.00 62.04           C  
ANISOU 2987  C   GLU D  14    11662   4984   6926   -116   -719   1627       C  
ATOM   2988  O   GLU D  14      54.491  44.400  12.045  1.00 62.98           O  
ANISOU 2988  O   GLU D  14    11616   5093   7222    152   -770   1531       O  
ATOM   2989  CB  GLU D  14      56.974  45.478  10.098  1.00 65.67           C  
ANISOU 2989  CB  GLU D  14    12722   4981   7249   -570   -506   1778       C  
ATOM   2990  CG  GLU D  14      57.808  46.618  10.545  1.00 69.19           C  
ANISOU 2990  CG  GLU D  14    13342   5127   7822   -777   -399   1718       C  
ATOM   2991  CD  GLU D  14      57.355  47.911   9.911  1.00 75.34           C  
ANISOU 2991  CD  GLU D  14    14653   5423   8550   -707   -526   1912       C  
ATOM   2992  OE1 GLU D  14      56.476  47.858   9.038  1.00 76.55           O  
ANISOU 2992  OE1 GLU D  14    15008   5528   8550   -490   -732   2124       O  
ATOM   2993  OE2 GLU D  14      57.863  48.980  10.301  1.00 79.70           O  
ANISOU 2993  OE2 GLU D  14    15453   5615   9214   -873   -467   1858       O  
ATOM   2994  N   GLN D  15      54.902  43.321  10.086  1.00 61.71           N  
ANISOU 2994  N   GLN D  15    11688   5052   6707   -177   -829   1759       N  
ATOM   2995  CA  GLN D  15      53.513  42.957   9.865  1.00 62.31           C  
ANISOU 2995  CA  GLN D  15    11581   5251   6841     29  -1128   1831       C  
ATOM   2996  C   GLN D  15      52.926  42.280  11.082  1.00 60.00           C  
ANISOU 2996  C   GLN D  15    10818   5206   6772    166  -1031   1664       C  
ATOM   2997  O   GLN D  15      51.776  42.512  11.449  1.00 61.74           O  
ANISOU 2997  O   GLN D  15    10756   5479   7223    423  -1161   1677       O  
ATOM   2998  CB  GLN D  15      53.401  42.007   8.703  1.00 62.95           C  
ANISOU 2998  CB  GLN D  15    11836   5441   6639   -174  -1261   1922       C  
ATOM   2999  CG  GLN D  15      54.119  42.434   7.478  1.00 65.56           C  
ANISOU 2999  CG  GLN D  15    12731   5552   6624   -373  -1229   2074       C  
ATOM   3000  CD  GLN D  15      53.451  41.860   6.258  1.00 69.16           C  
ANISOU 3000  CD  GLN D  15    13484   6046   6750   -473  -1566   2199       C  
ATOM   3001  OE1 GLN D  15      54.093  41.247   5.410  1.00 70.32           O  
ANISOU 3001  OE1 GLN D  15    14030   6169   6520   -727  -1383   2189       O  
ATOM   3002  NE2 GLN D  15      52.134  42.030   6.181  1.00 71.96           N  
ANISOU 3002  NE2 GLN D  15    13627   6462   7251   -269  -2068   2303       N  
ATOM   3003  N   ILE D  16      53.727  41.437  11.713  1.00 56.65           N  
ANISOU 3003  N   ILE D  16    10309   4926   6289     10   -776   1528       N  
ATOM   3004  CA  ILE D  16      53.235  40.681  12.847  1.00 55.15           C  
ANISOU 3004  CA  ILE D  16     9798   4940   6215     92   -650   1408       C  
ATOM   3005  C   ILE D  16      53.099  41.578  14.063  1.00 55.75           C  
ANISOU 3005  C   ILE D  16     9824   4935   6424    306   -529   1284       C  
ATOM   3006  O   ILE D  16      52.014  41.678  14.654  1.00 57.39           O  
ANISOU 3006  O   ILE D  16     9795   5209   6801    523   -475   1250       O  
ATOM   3007  CB  ILE D  16      54.140  39.502  13.172  1.00 52.74           C  
ANISOU 3007  CB  ILE D  16     9502   4758   5781    -83   -463   1339       C  
ATOM   3008  CG1 ILE D  16      54.397  38.675  11.906  1.00 53.03           C  
ANISOU 3008  CG1 ILE D  16     9716   4789   5643   -277   -502   1414       C  
ATOM   3009  CG2 ILE D  16      53.513  38.661  14.251  1.00 52.10           C  
ANISOU 3009  CG2 ILE D  16     9202   4838   5757    -28   -340   1275       C  
ATOM   3010  CD1 ILE D  16      54.867  37.281  12.166  1.00 51.67           C  
ANISOU 3010  CD1 ILE D  16     9538   4697   5398   -364   -326   1356       C  
ATOM   3011  N   THR D  17      54.185  42.247  14.429  1.00 54.88           N  
ANISOU 3011  N   THR D  17     9936   4671   6245    227   -464   1201       N  
ATOM   3012  CA  THR D  17      54.124  43.073  15.603  1.00 56.39           C  
ANISOU 3012  CA  THR D  17    10213   4736   6476    380   -369   1034       C  
ATOM   3013  C   THR D  17      52.973  44.055  15.417  1.00 59.63           C  
ANISOU 3013  C   THR D  17    10627   4954   7078    701   -413   1069       C  
ATOM   3014  O   THR D  17      52.317  44.457  16.389  1.00 61.90           O  
ANISOU 3014  O   THR D  17    10881   5191   7448    959   -238    926       O  
ATOM   3015  CB  THR D  17      55.437  43.808  15.846  1.00 56.80           C  
ANISOU 3015  CB  THR D  17    10523   4602   6456    167   -397    941       C  
ATOM   3016  OG1 THR D  17      55.738  44.614  14.701  1.00 59.42           O  
ANISOU 3016  OG1 THR D  17    11056   4688   6833     58   -487   1080       O  
ATOM   3017  CG2 THR D  17      56.565  42.819  16.052  1.00 54.11           C  
ANISOU 3017  CG2 THR D  17    10049   4487   6024    -67   -386    928       C  
ATOM   3018  N   ASP D  18      52.724  44.431  14.165  1.00 60.57           N  
ANISOU 3018  N   ASP D  18    10815   4947   7251    719   -635   1268       N  
ATOM   3019  CA  ASP D  18      51.602  45.290  13.842  1.00 64.58           C  
ANISOU 3019  CA  ASP D  18    11279   5272   7986   1092   -775   1368       C  
ATOM   3020  C   ASP D  18      50.287  44.608  14.208  1.00 65.83           C  
ANISOU 3020  C   ASP D  18    10900   5732   8382   1324   -730   1366       C  
ATOM   3021  O   ASP D  18      49.383  45.212  14.787  1.00 69.31           O  
ANISOU 3021  O   ASP D  18    11146   6097   9093   1716   -603   1305       O  
ATOM   3022  CB  ASP D  18      51.611  45.634  12.348  1.00 66.29           C  
ANISOU 3022  CB  ASP D  18    11730   5329   8127   1032  -1109   1639       C  
ATOM   3023  CG  ASP D  18      52.357  46.941  12.038  1.00 68.88           C  
ANISOU 3023  CG  ASP D  18    12611   5183   8378    989  -1121   1693       C  
ATOM   3024  OD1 ASP D  18      52.343  47.357  10.865  1.00 71.81           O  
ANISOU 3024  OD1 ASP D  18    13296   5355   8635    958  -1360   1945       O  
ATOM   3025  OD2 ASP D  18      52.943  47.559  12.956  1.00 69.49           O  
ANISOU 3025  OD2 ASP D  18    12871   5057   8476    952   -908   1490       O  
ATOM   3026  N   LEU D  19      50.188  43.333  13.865  1.00 63.72           N  
ANISOU 3026  N   LEU D  19    10388   5784   8039   1066   -790   1424       N  
ATOM   3027  CA  LEU D  19      48.988  42.570  14.167  1.00 65.59           C  
ANISOU 3027  CA  LEU D  19    10082   6317   8525   1148   -738   1433       C  
ATOM   3028  C   LEU D  19      48.732  42.469  15.665  1.00 66.13           C  
ANISOU 3028  C   LEU D  19    10001   6467   8659   1281   -261   1233       C  
ATOM   3029  O   LEU D  19      47.583  42.596  16.117  1.00 70.34           O  
ANISOU 3029  O   LEU D  19    10096   7108   9522   1550    -80   1217       O  
ATOM   3030  CB  LEU D  19      49.072  41.173  13.559  1.00 63.48           C  
ANISOU 3030  CB  LEU D  19     9724   6287   8107    755   -872   1501       C  
ATOM   3031  CG  LEU D  19      48.505  41.168  12.140  1.00 65.95           C  
ANISOU 3031  CG  LEU D  19     9992   6614   8452    700  -1380   1702       C  
ATOM   3032  CD1 LEU D  19      48.775  39.830  11.483  1.00 63.86           C  
ANISOU 3032  CD1 LEU D  19     9845   6485   7934    269  -1490   1711       C  
ATOM   3033  CD2 LEU D  19      47.008  41.480  12.165  1.00 70.78           C  
ANISOU 3033  CD2 LEU D  19     9993   7368   9531    991  -1574   1791       C  
ATOM   3034  N   VAL D  20      49.795  42.244  16.431  1.00 62.74           N  
ANISOU 3034  N   VAL D  20     9930   5992   7915   1100    -55   1090       N  
ATOM   3035  CA  VAL D  20      49.654  42.170  17.864  1.00 63.89           C  
ANISOU 3035  CA  VAL D  20    10119   6180   7977   1197    364    905       C  
ATOM   3036  C   VAL D  20      49.013  43.454  18.355  1.00 68.84           C  
ANISOU 3036  C   VAL D  20    10778   6579   8798   1626    558    782       C  
ATOM   3037  O   VAL D  20      47.985  43.427  19.041  1.00 72.80           O  
ANISOU 3037  O   VAL D  20    10974   7186   9499   1870    930    714       O  
ATOM   3038  CB  VAL D  20      50.994  41.987  18.559  1.00 60.98           C  
ANISOU 3038  CB  VAL D  20    10203   5748   7219    977    393    784       C  
ATOM   3039  CG1 VAL D  20      50.764  41.691  20.021  1.00 62.57           C  
ANISOU 3039  CG1 VAL D  20    10536   6021   7218   1034    782    629       C  
ATOM   3040  CG2 VAL D  20      51.794  40.863  17.910  1.00 56.91           C  
ANISOU 3040  CG2 VAL D  20     9680   5375   6568    649    193    913       C  
ATOM   3041  N   THR D  21      49.622  44.582  17.999  1.00 69.57           N  
ANISOU 3041  N   THR D  21    11259   6325   8849   1715    361    750       N  
ATOM   3042  CA  THR D  21      49.046  45.889  18.302  1.00 74.95           C  
ANISOU 3042  CA  THR D  21    12075   6668   9734   2167    509    642       C  
ATOM   3043  C   THR D  21      47.568  45.959  17.913  1.00 79.84           C  
ANISOU 3043  C   THR D  21    12074   7412  10850   2585    546    780       C  
ATOM   3044  O   THR D  21      46.710  46.286  18.738  1.00 84.51           O  
ANISOU 3044  O   THR D  21    12465   7986  11657   2969    983    637       O  
ATOM   3045  CB  THR D  21      49.776  47.009  17.554  1.00 75.17           C  
ANISOU 3045  CB  THR D  21    12573   6263   9725   2154    190    697       C  
ATOM   3046  OG1 THR D  21      51.160  47.012  17.923  1.00 72.06           O  
ANISOU 3046  OG1 THR D  21    12636   5777   8968   1733    144    564       O  
ATOM   3047  CG2 THR D  21      49.163  48.345  17.901  1.00 80.88           C  
ANISOU 3047  CG2 THR D  21    13525   6541  10665   2664    360    579       C  
ATOM   3048  N   ILE D  22      47.277  45.662  16.651  1.00 79.81           N  
ANISOU 3048  N   ILE D  22    11762   7536  11026   2511     86   1054       N  
ATOM   3049  CA  ILE D  22      45.907  45.722  16.171  1.00 85.73           C  
ANISOU 3049  CA  ILE D  22    11841   8440  12291   2875    -48   1222       C  
ATOM   3050  C   ILE D  22      44.972  45.024  17.141  1.00 89.00           C  
ANISOU 3050  C   ILE D  22    11657   9201  12958   2949    463   1106       C  
ATOM   3051  O   ILE D  22      43.933  45.574  17.528  1.00 95.24           O  
ANISOU 3051  O   ILE D  22    11999   9980  14206   3450    745   1070       O  
ATOM   3052  CB  ILE D  22      45.748  45.057  14.793  1.00 84.66           C  
ANISOU 3052  CB  ILE D  22    11463   8520  12182   2599   -656   1506       C  
ATOM   3053  CG1 ILE D  22      46.593  45.782  13.740  1.00 83.14           C  
ANISOU 3053  CG1 ILE D  22    11906   7973  11713   2529  -1094   1662       C  
ATOM   3054  CG2 ILE D  22      44.268  45.050  14.377  1.00 90.85           C  
ANISOU 3054  CG2 ILE D  22    11433   9532  13554   2937   -891   1680       C  
ATOM   3055  CD1 ILE D  22      46.088  47.158  13.410  1.00 87.79           C  
ANISOU 3055  CD1 ILE D  22    12613   8163  12581   3090  -1287   1786       C  
ATOM   3056  N   ARG D  23      45.351  43.806  17.523  1.00 85.54           N  
ANISOU 3056  N   ARG D  23    11221   9044  12235   2461    623   1062       N  
ATOM   3057  CA  ARG D  23      44.515  42.960  18.361  1.00 88.87           C  
ANISOU 3057  CA  ARG D  23    11135   9795  12837   2388   1123   1005       C  
ATOM   3058  C   ARG D  23      44.261  43.558  19.746  1.00 92.79           C  
ANISOU 3058  C   ARG D  23    11803  10158  13294   2738   1849    750       C  
ATOM   3059  O   ARG D  23      43.114  43.856  20.096  1.00 99.46           O  
ANISOU 3059  O   ARG D  23    12071  11102  14618   3123   2248    724       O  
ATOM   3060  CB  ARG D  23      45.144  41.586  18.484  1.00 84.24           C  
ANISOU 3060  CB  ARG D  23    10733   9407  11866   1799   1123   1030       C  
ATOM   3061  CG  ARG D  23      45.504  40.953  17.145  1.00 82.65           C  
ANISOU 3061  CG  ARG D  23    10524   9275  11604   1443    489   1221       C  
ATOM   3062  CD  ARG D  23      44.324  40.208  16.564  1.00 89.57           C  
ANISOU 3062  CD  ARG D  23    10660  10461  12913   1276    305   1373       C  
ATOM   3063  NE  ARG D  23      44.682  38.895  16.055  1.00 88.51           N  
ANISOU 3063  NE  ARG D  23    10655  10436  12538    720     86   1440       N  
ATOM   3064  CZ  ARG D  23      43.973  38.160  15.198  1.00 91.91           C  
ANISOU 3064  CZ  ARG D  23    10668  11056  13197    409   -300   1564       C  
ATOM   3065  NH1 ARG D  23      42.821  38.591  14.676  1.00 97.66           N  
ANISOU 3065  NH1 ARG D  23    10697  11956  14454    592   -615   1678       N  
ATOM   3066  NH2 ARG D  23      44.448  36.972  14.851  1.00 89.71           N  
ANISOU 3066  NH2 ARG D  23    10699  10771  12615    -87   -412   1570       N  
ATOM   3067  N   LYS D  24      45.314  43.740  20.537  1.00 89.61           N  
ANISOU 3067  N   LYS D  24    12185   9535  12328   2611   2026    552       N  
ATOM   3068  CA  LYS D  24      45.136  44.372  21.838  1.00 94.34           C  
ANISOU 3068  CA  LYS D  24    13140   9947  12759   2920   2679    270       C  
ATOM   3069  C   LYS D  24      44.148  45.518  21.721  1.00101.44           C  
ANISOU 3069  C   LYS D  24    13699  10645  14198   3577   2888    217       C  
ATOM   3070  O   LYS D  24      43.287  45.729  22.575  1.00107.83           O  
ANISOU 3070  O   LYS D  24    14290  11480  15199   3930   3586     61       O  
ATOM   3071  CB  LYS D  24      46.452  44.923  22.357  1.00 91.20           C  
ANISOU 3071  CB  LYS D  24    13683   9206  11762   2781   2551     63       C  
ATOM   3072  CG  LYS D  24      47.492  43.888  22.517  1.00 85.92           C  
ANISOU 3072  CG  LYS D  24    13319   8709  10617   2241   2312    123       C  
ATOM   3073  CD  LYS D  24      48.577  44.355  23.441  1.00 86.18           C  
ANISOU 3073  CD  LYS D  24    14186   8483  10074   2124   2307   -123       C  
ATOM   3074  CE  LYS D  24      49.834  43.555  23.159  1.00 82.03           C  
ANISOU 3074  CE  LYS D  24    13840   8083   9243   1656   1815      2       C  
ATOM   3075  NZ  LYS D  24      50.866  43.718  24.208  1.00 84.09           N  
ANISOU 3075  NZ  LYS D  24    14806   8208   8937   1475   1742   -202       N  
ATOM   3076  N   GLN D  25      44.301  46.268  20.643  1.00101.13           N  
ANISOU 3076  N   GLN D  25    13656  10374  14394   3766   2304    362       N  
ATOM   3077  CA  GLN D  25      43.474  47.421  20.381  1.00108.16           C  
ANISOU 3077  CA  GLN D  25    14300  10985  15810   4453   2357    368       C  
ATOM   3078  C   GLN D  25      42.033  46.996  20.102  1.00114.03           C  
ANISOU 3078  C   GLN D  25    13910  12138  17279   4736   2486    550       C  
ATOM   3079  O   GLN D  25      41.121  47.812  20.148  1.00121.73           O  
ANISOU 3079  O   GLN D  25    14475  12970  18807   5408   2711    538       O  
ATOM   3080  CB  GLN D  25      44.051  48.187  19.192  1.00106.21           C  
ANISOU 3080  CB  GLN D  25    14398  10389  15569   4496   1620    560       C  
ATOM   3081  CG  GLN D  25      43.703  49.671  19.158  1.00113.31           C  
ANISOU 3081  CG  GLN D  25    15575  10718  16761   5193   1683    497       C  
ATOM   3082  CD  GLN D  25      44.756  50.497  18.435  1.00111.02           C  
ANISOU 3082  CD  GLN D  25    16101   9917  16164   5034   1159    576       C  
ATOM   3083  OE1 GLN D  25      45.908  50.070  18.272  1.00103.74           O  
ANISOU 3083  OE1 GLN D  25    15626   9043  14748   4401    918    571       O  
ATOM   3084  NE2 GLN D  25      44.371  51.688  18.006  1.00117.39           N  
ANISOU 3084  NE2 GLN D  25    17098  10210  17293   5617   1014    664       N  
ATOM   3085  N   GLU D  26      41.829  45.715  19.816  1.00111.31           N  
ANISOU 3085  N   GLU D  26    13038  12285  16971   4220   2337    716       N  
ATOM   3086  CA  GLU D  26      40.479  45.191  19.612  1.00117.65           C  
ANISOU 3086  CA  GLU D  26    12694  13525  18483   4333   2448    877       C  
ATOM   3087  C   GLU D  26      39.967  44.444  20.843  1.00120.87           C  
ANISOU 3087  C   GLU D  26    12823  14218  18882   4162   3370    714       C  
ATOM   3088  O   GLU D  26      39.116  43.555  20.728  1.00124.09           O  
ANISOU 3088  O   GLU D  26    12360  15065  19722   3898   3472    858       O  
ATOM   3089  CB  GLU D  26      40.439  44.257  18.409  1.00114.25           C  
ANISOU 3089  CB  GLU D  26    11845  13418  18145   3816   1655   1170       C  
ATOM   3090  CG  GLU D  26      40.623  44.955  17.093  1.00114.08           C  
ANISOU 3090  CG  GLU D  26    11952  13181  18213   4022    770   1393       C  
ATOM   3091  CD  GLU D  26      40.935  43.984  15.977  1.00110.22           C  
ANISOU 3091  CD  GLU D  26    11451  12920  17508   3397     35   1605       C  
ATOM   3092  OE1 GLU D  26      41.702  43.022  16.213  1.00104.71           O  
ANISOU 3092  OE1 GLU D  26    11168  12310  16308   2808    167   1522       O  
ATOM   3093  OE2 GLU D  26      40.421  44.188  14.858  1.00113.91           O  
ANISOU 3093  OE2 GLU D  26    11552  13447  18281   3519   -691   1855       O  
ATOM   3094  N   GLY D  27      40.489  44.804  22.014  1.00120.68           N  
ANISOU 3094  N   GLY D  27    13593  13925  18334   4263   4029    419       N  
ATOM   3095  CA  GLY D  27      40.127  44.131  23.259  1.00123.81           C  
ANISOU 3095  CA  GLY D  27    13981  14526  18534   4077   4957    266       C  
ATOM   3096  C   GLY D  27      40.890  42.830  23.478  1.00117.06           C  
ANISOU 3096  C   GLY D  27    13558  13855  17066   3300   4837    344       C  
ATOM   3097  O   GLY D  27      41.072  42.400  24.624  1.00118.10           O  
ANISOU 3097  O   GLY D  27    14195  13986  16692   3106   5496    202       O  
ATOM   3098  N   ILE D  28      41.341  42.201  22.389  1.00110.74           N  
ANISOU 3098  N   ILE D  28    12635  13171  16271   2882   4012    574       N  
ATOM   3099  CA  ILE D  28      42.043  40.918  22.481  1.00104.80           C  
ANISOU 3099  CA  ILE D  28    12256  12545  15018   2208   3869    667       C  
ATOM   3100  C   ILE D  28      43.265  41.015  23.392  1.00100.70           C  
ANISOU 3100  C   ILE D  28    12837  11754  13671   2114   4011    484       C  
ATOM   3101  O   ILE D  28      44.390  40.748  22.986  1.00 93.95           O  
ANISOU 3101  O   ILE D  28    12487  10788  12420   1842   3451    532       O  
ATOM   3102  CB  ILE D  28      42.444  40.369  21.097  1.00 99.34           C  
ANISOU 3102  CB  ILE D  28    11405  11931  14410   1853   2970    888       C  
ATOM   3103  CG1 ILE D  28      41.257  40.447  20.140  1.00104.31           C  
ANISOU 3103  CG1 ILE D  28    11006  12806  15822   1975   2650   1063       C  
ATOM   3104  CG2 ILE D  28      42.951  38.932  21.209  1.00 94.89           C  
ANISOU 3104  CG2 ILE D  28    11120  11477  13455   1215   2935    984       C  
ATOM   3105  CD1 ILE D  28      39.939  40.110  20.793  1.00112.48           C  
ANISOU 3105  CD1 ILE D  28    11177  14152  17410   2006   3341   1069       C  
ATOM   3106  N   GLU D  29      43.010  41.424  24.629  1.00105.86           N  
ANISOU 3106  N   GLU D  29    13835  12307  14082   2356   4772    266       N  
ATOM   3107  CA  GLU D  29      43.994  41.440  25.703  1.00104.34           C  
ANISOU 3107  CA  GLU D  29    14695  11895  13055   2235   4955     81       C  
ATOM   3108  C   GLU D  29      45.224  40.582  25.433  1.00 96.65           C  
ANISOU 3108  C   GLU D  29    14192  10924  11605   1751   4320    224       C  
ATOM   3109  O   GLU D  29      46.311  41.101  25.188  1.00 92.44           O  
ANISOU 3109  O   GLU D  29    14152  10177  10793   1754   3780    148       O  
ATOM   3110  CB  GLU D  29      43.326  40.930  26.977  1.00111.06           C  
ANISOU 3110  CB  GLU D  29    15690  12860  13645   2172   5911     11       C  
ATOM   3111  CG  GLU D  29      44.242  40.857  28.183  1.00111.87           C  
ANISOU 3111  CG  GLU D  29    16960  12756  12791   2027   6087   -155       C  
ATOM   3112  CD  GLU D  29      44.082  42.059  29.107  1.00119.38           C  
ANISOU 3112  CD  GLU D  29    18500  13411  13449   2484   6653   -528       C  
ATOM   3113  OE1 GLU D  29      42.927  42.391  29.477  1.00126.69           O  
ANISOU 3113  OE1 GLU D  29    19001  14392  14742   2827   7502   -633       O  
ATOM   3114  OE2 GLU D  29      45.114  42.667  29.468  1.00117.85           O  
ANISOU 3114  OE2 GLU D  29    19188  12916  12674   2490   6264   -733       O  
ATOM   3115  N   GLU D  30      45.033  39.266  25.491  1.00 95.70           N  
ANISOU 3115  N   GLU D  30    13898  11026  11438   1338   4429    432       N  
ATOM   3116  CA  GLU D  30      46.129  38.289  25.490  1.00 90.12           C  
ANISOU 3116  CA  GLU D  30    13703  10290  10248    942   3998    571       C  
ATOM   3117  C   GLU D  30      46.869  38.130  24.165  1.00 83.03           C  
ANISOU 3117  C   GLU D  30    12617   9377   9552    811   3192    695       C  
ATOM   3118  O   GLU D  30      47.565  37.144  23.954  1.00 79.54           O  
ANISOU 3118  O   GLU D  30    12391   8940   8892    508   2896    842       O  
ATOM   3119  CB  GLU D  30      45.610  36.914  25.931  1.00 92.77           C  
ANISOU 3119  CB  GLU D  30    13968  10778  10500    553   4416    771       C  
ATOM   3120  CG  GLU D  30      44.572  36.312  24.987  1.00 94.97           C  
ANISOU 3120  CG  GLU D  30    13322  11283  11480    335   4411    944       C  
ATOM   3121  CD  GLU D  30      43.269  37.101  24.974  1.00103.09           C  
ANISOU 3121  CD  GLU D  30    13569  12475  13125    645   4884    852       C  
ATOM   3122  OE1 GLU D  30      43.020  37.876  25.930  1.00107.73           O  
ANISOU 3122  OE1 GLU D  30    14408  12986  13537    990   5484    658       O  
ATOM   3123  OE2 GLU D  30      42.490  36.945  24.007  1.00105.15           O  
ANISOU 3123  OE2 GLU D  30    12972  12932  14050    561   4642    968       O  
ATOM   3124  N   ALA D  31      46.718  39.084  23.265  1.00 81.57           N  
ANISOU 3124  N   ALA D  31    12083   9142   9767   1061   2874    647       N  
ATOM   3125  CA  ALA D  31      47.444  39.001  22.016  1.00 75.81           C  
ANISOU 3125  CA  ALA D  31    11290   8376   9140    928   2192    760       C  
ATOM   3126  C   ALA D  31      48.938  39.109  22.303  1.00 71.66           C  
ANISOU 3126  C   ALA D  31    11428   7678   8122    844   1884    692       C  
ATOM   3127  O   ALA D  31      49.367  39.925  23.130  1.00 73.14           O  
ANISOU 3127  O   ALA D  31    12067   7703   8022   1007   1990    502       O  
ATOM   3128  CB  ALA D  31      46.993  40.089  21.056  1.00 76.67           C  
ANISOU 3128  CB  ALA D  31    11022   8416   9695   1227   1920    755       C  
ATOM   3129  N   SER D  32      49.727  38.279  21.631  1.00 67.13           N  
ANISOU 3129  N   SER D  32    10903   7132   7470    586   1506    832       N  
ATOM   3130  CA  SER D  32      51.164  38.323  21.803  1.00 64.02           C  
ANISOU 3130  CA  SER D  32    10957   6626   6740    518   1187    797       C  
ATOM   3131  C   SER D  32      51.874  37.890  20.548  1.00 60.19           C  
ANISOU 3131  C   SER D  32    10335   6142   6392    364    789    922       C  
ATOM   3132  O   SER D  32      51.280  37.285  19.652  1.00 59.54           O  
ANISOU 3132  O   SER D  32     9951   6135   6538    250    746   1039       O  
ATOM   3133  CB  SER D  32      51.585  37.385  22.918  1.00 65.15           C  
ANISOU 3133  CB  SER D  32    11498   6796   6459    403   1329    840       C  
ATOM   3134  OG  SER D  32      51.764  36.070  22.420  1.00 63.44           O  
ANISOU 3134  OG  SER D  32    11196   6629   6280    201   1230   1036       O  
ATOM   3135  N   LEU D  33      53.167  38.172  20.512  1.00 58.40           N  
ANISOU 3135  N   LEU D  33    10345   5832   6012    333    511    885       N  
ATOM   3136  CA  LEU D  33      53.999  37.834  19.368  1.00 55.65           C  
ANISOU 3136  CA  LEU D  33     9902   5471   5773    212    243    981       C  
ATOM   3137  C   LEU D  33      53.841  36.367  19.020  1.00 54.74           C  
ANISOU 3137  C   LEU D  33     9730   5418   5651     84    300   1120       C  
ATOM   3138  O   LEU D  33      53.386  36.012  17.929  1.00 53.93           O  
ANISOU 3138  O   LEU D  33     9463   5320   5709    -18    252   1186       O  
ATOM   3139  CB  LEU D  33      55.457  38.109  19.700  1.00 55.35           C  
ANISOU 3139  CB  LEU D  33    10040   5389   5602    177     18    931       C  
ATOM   3140  CG  LEU D  33      56.148  38.880  18.596  1.00 55.39           C  
ANISOU 3140  CG  LEU D  33     9944   5308   5793     98   -152    930       C  
ATOM   3141  CD1 LEU D  33      57.655  38.685  18.652  1.00 56.20           C  
ANISOU 3141  CD1 LEU D  33    10017   5442   5893      1   -335    940       C  
ATOM   3142  CD2 LEU D  33      55.581  38.413  17.271  1.00 55.48           C  
ANISOU 3142  CD2 LEU D  33     9804   5329   5947     51   -111   1050       C  
ATOM   3143  N   SER D  34      54.213  35.512  19.971  1.00 55.48           N  
ANISOU 3143  N   SER D  34    10044   5517   5518     80    375   1168       N  
ATOM   3144  CA  SER D  34      54.260  34.086  19.722  1.00 55.24           C  
ANISOU 3144  CA  SER D  34    10087   5444   5460    -24    426   1305       C  
ATOM   3145  C   SER D  34      52.837  33.654  19.438  1.00 56.43           C  
ANISOU 3145  C   SER D  34    10057   5630   5755   -193    645   1343       C  
ATOM   3146  O   SER D  34      52.516  33.016  18.441  1.00 56.04           O  
ANISOU 3146  O   SER D  34     9910   5539   5843   -362    587   1386       O  
ATOM   3147  CB  SER D  34      54.790  33.371  20.958  1.00 57.21           C  
ANISOU 3147  CB  SER D  34    10680   5648   5408     46    452   1390       C  
ATOM   3148  OG  SER D  34      53.794  32.528  21.520  1.00 59.18           O  
ANISOU 3148  OG  SER D  34    11073   5863   5550    -83    765   1487       O  
ATOM   3149  N   ASN D  35      51.991  34.014  20.375  1.00 58.98           N  
ANISOU 3149  N   ASN D  35    10342   6029   6036   -163    912   1310       N  
ATOM   3150  CA  ASN D  35      50.563  33.927  20.244  1.00 61.50           C  
ANISOU 3150  CA  ASN D  35    10311   6451   6605   -293   1157   1326       C  
ATOM   3151  C   ASN D  35      50.048  34.119  18.799  1.00 61.03           C  
ANISOU 3151  C   ASN D  35     9865   6438   6884   -388    885   1331       C  
ATOM   3152  O   ASN D  35      49.376  33.244  18.247  1.00 62.18           O  
ANISOU 3152  O   ASN D  35     9848   6600   7178   -667    869   1401       O  
ATOM   3153  CB  ASN D  35      50.016  35.018  21.140  1.00 63.98           C  
ANISOU 3153  CB  ASN D  35    10555   6840   6914    -75   1429   1207       C  
ATOM   3154  CG  ASN D  35      48.563  35.012  21.191  1.00 67.90           C  
ANISOU 3154  CG  ASN D  35    10586   7478   7736   -136   1768   1222       C  
ATOM   3155  OD1 ASN D  35      47.960  33.956  21.158  1.00 70.44           O  
ANISOU 3155  OD1 ASN D  35    10772   7842   8149   -432   1937   1338       O  
ATOM   3156  ND2 ASN D  35      47.959  36.190  21.260  1.00 71.12           N  
ANISOU 3156  ND2 ASN D  35    10710   7939   8372    140   1881   1107       N  
ATOM   3157  N   VAL D  36      50.358  35.277  18.202  1.00 59.63           N  
ANISOU 3157  N   VAL D  36     9607   6254   6794   -191    642   1262       N  
ATOM   3158  CA  VAL D  36      49.910  35.601  16.841  1.00 59.54           C  
ANISOU 3158  CA  VAL D  36     9347   6265   7012   -242    323   1298       C  
ATOM   3159  C   VAL D  36      50.648  34.831  15.746  1.00 57.61           C  
ANISOU 3159  C   VAL D  36     9359   5913   6617   -446     82   1338       C  
ATOM   3160  O   VAL D  36      50.040  34.431  14.743  1.00 59.44           O  
ANISOU 3160  O   VAL D  36     9486   6161   6937   -649   -139   1378       O  
ATOM   3161  CB  VAL D  36      50.046  37.117  16.512  1.00 59.27           C  
ANISOU 3161  CB  VAL D  36     9277   6174   7071     39    154   1252       C  
ATOM   3162  CG1 VAL D  36      50.074  37.313  15.024  1.00 58.64           C  
ANISOU 3162  CG1 VAL D  36     9205   6043   7032    -40   -237   1334       C  
ATOM   3163  CG2 VAL D  36      48.908  37.925  17.128  1.00 62.56           C  
ANISOU 3163  CG2 VAL D  36     9337   6666   7765    289    350   1212       C  
ATOM   3164  N   SER D  37      51.955  34.650  15.901  1.00 54.81           N  
ANISOU 3164  N   SER D  37     9335   5448   6042   -384    113   1315       N  
ATOM   3165  CA  SER D  37      52.688  33.878  14.897  1.00 53.89           C  
ANISOU 3165  CA  SER D  37     9469   5207   5800   -516     14   1329       C  
ATOM   3166  C   SER D  37      52.124  32.447  14.817  1.00 55.80           C  
ANISOU 3166  C   SER D  37     9810   5375   6018   -772     90   1359       C  
ATOM   3167  O   SER D  37      52.031  31.826  13.743  1.00 56.86           O  
ANISOU 3167  O   SER D  37    10118   5398   6087   -976    -39   1339       O  
ATOM   3168  CB  SER D  37      54.174  33.821  15.226  1.00 52.00           C  
ANISOU 3168  CB  SER D  37     9431   4891   5437   -362     89   1311       C  
ATOM   3169  OG  SER D  37      54.596  34.996  15.875  1.00 51.27           O  
ANISOU 3169  OG  SER D  37     9249   4859   5371   -199     57   1269       O  
ATOM   3170  N   SER D  38      51.746  31.924  15.972  1.00 57.02           N  
ANISOU 3170  N   SER D  38     9939   5549   6179   -798    316   1401       N  
ATOM   3171  CA  SER D  38      51.185  30.597  16.028  1.00 59.56           C  
ANISOU 3171  CA  SER D  38    10394   5744   6491  -1094    434   1450       C  
ATOM   3172  C   SER D  38      49.943  30.557  15.149  1.00 62.27           C  
ANISOU 3172  C   SER D  38    10436   6180   7046  -1416    238   1431       C  
ATOM   3173  O   SER D  38      49.809  29.698  14.284  1.00 63.91           O  
ANISOU 3173  O   SER D  38    10861   6225   7196  -1709     94   1400       O  
ATOM   3174  CB  SER D  38      50.850  30.246  17.471  1.00 61.14           C  
ANISOU 3174  CB  SER D  38    10626   5963   6642  -1094    760   1534       C  
ATOM   3175  OG  SER D  38      50.086  29.063  17.538  1.00 64.66           O  
ANISOU 3175  OG  SER D  38    11161   6276   7131  -1469    918   1604       O  
ATOM   3176  N   MET D  39      49.050  31.512  15.360  1.00 63.74           N  
ANISOU 3176  N   MET D  39    10127   6609   7481  -1342    202   1440       N  
ATOM   3177  CA  MET D  39      47.837  31.591  14.571  1.00 67.59           C  
ANISOU 3177  CA  MET D  39    10187   7242   8251  -1591    -80   1452       C  
ATOM   3178  C   MET D  39      48.178  31.703  13.081  1.00 67.11           C  
ANISOU 3178  C   MET D  39    10381   7089   8030  -1664   -542   1415       C  
ATOM   3179  O   MET D  39      47.526  31.078  12.232  1.00 70.53           O  
ANISOU 3179  O   MET D  39    10806   7499   8492  -2040   -850   1401       O  
ATOM   3180  CB  MET D  39      46.960  32.752  15.049  1.00 69.57           C  
ANISOU 3180  CB  MET D  39     9836   7751   8847  -1337    -27   1477       C  
ATOM   3181  CG  MET D  39      45.758  33.034  14.170  1.00 75.29           C  
ANISOU 3181  CG  MET D  39     9998   8664   9943  -1478   -440   1523       C  
ATOM   3182  SD  MET D  39      46.204  34.161  12.826  1.00 77.93           S  
ANISOU 3182  SD  MET D  39    10530   8942  10139  -1206  -1025   1547       S  
ATOM   3183  CE  MET D  39      45.888  35.754  13.577  1.00 77.08           C  
ANISOU 3183  CE  MET D  39    10021   8933  10332   -622   -845   1569       C  
ATOM   3184  N   LEU D  40      49.217  32.472  12.768  1.00 63.56           N  
ANISOU 3184  N   LEU D  40    10208   6567   7376  -1357   -579   1395       N  
ATOM   3185  CA  LEU D  40      49.621  32.666  11.375  1.00 63.71           C  
ANISOU 3185  CA  LEU D  40    10566   6480   7162  -1414   -909   1376       C  
ATOM   3186  C   LEU D  40      50.221  31.419  10.759  1.00 64.25           C  
ANISOU 3186  C   LEU D  40    11185   6298   6930  -1664   -843   1287       C  
ATOM   3187  O   LEU D  40      50.007  31.149   9.574  1.00 66.72           O  
ANISOU 3187  O   LEU D  40    11796   6518   7036  -1905  -1146   1242       O  
ATOM   3188  CB  LEU D  40      50.627  33.803  11.258  1.00 60.66           C  
ANISOU 3188  CB  LEU D  40    10335   6057   6658  -1077   -854   1391       C  
ATOM   3189  CG  LEU D  40      50.027  35.197  11.414  1.00 61.63           C  
ANISOU 3189  CG  LEU D  40    10096   6307   7012   -824  -1024   1467       C  
ATOM   3190  CD1 LEU D  40      51.091  36.242  11.153  1.00 59.74           C  
ANISOU 3190  CD1 LEU D  40    10135   5943   6621   -609   -976   1481       C  
ATOM   3191  CD2 LEU D  40      48.848  35.388  10.478  1.00 65.17           C  
ANISOU 3191  CD2 LEU D  40    10332   6849   7582   -945  -1513   1554       C  
ATOM   3192  N   LEU D  41      50.994  30.680  11.558  1.00 62.63           N  
ANISOU 3192  N   LEU D  41    11178   5949   6669  -1574   -462   1262       N  
ATOM   3193  CA  LEU D  41      51.527  29.381  11.129  1.00 64.10           C  
ANISOU 3193  CA  LEU D  41    11901   5822   6630  -1738   -324   1176       C  
ATOM   3194  C   LEU D  41      50.376  28.434  10.830  1.00 68.75           C  
ANISOU 3194  C   LEU D  41    12533   6324   7263  -2230   -511   1138       C  
ATOM   3195  O   LEU D  41      50.305  27.827   9.768  1.00 71.69           O  
ANISOU 3195  O   LEU D  41    13347   6488   7404  -2510   -695   1022       O  
ATOM   3196  CB  LEU D  41      52.409  28.767  12.215  1.00 62.16           C  
ANISOU 3196  CB  LEU D  41    11787   5437   6393  -1493     52   1215       C  
ATOM   3197  CG  LEU D  41      53.796  29.383  12.374  1.00 58.74           C  
ANISOU 3197  CG  LEU D  41    11369   5031   5918  -1074    205   1223       C  
ATOM   3198  CD1 LEU D  41      54.498  28.783  13.594  1.00 56.76           C  
ANISOU 3198  CD1 LEU D  41    11171   4688   5706   -829    428   1304       C  
ATOM   3199  CD2 LEU D  41      54.612  29.203  11.081  1.00 58.07           C  
ANISOU 3199  CD2 LEU D  41    11671   4764   5630  -1045    270   1115       C  
ATOM   3200  N   GLU D  42      49.465  28.327  11.782  1.00 70.45           N  
ANISOU 3200  N   GLU D  42    12305   6694   7771  -2373   -442   1225       N  
ATOM   3201  CA  GLU D  42      48.311  27.479  11.614  1.00 76.17           C  
ANISOU 3201  CA  GLU D  42    12928   7373   8640  -2918   -597   1208       C  
ATOM   3202  C   GLU D  42      47.679  27.782  10.263  1.00 79.39           C  
ANISOU 3202  C   GLU D  42    13300   7871   8994  -3190  -1172   1135       C  
ATOM   3203  O   GLU D  42      47.389  26.885   9.467  1.00 83.32           O  
ANISOU 3203  O   GLU D  42    14200   8137   9320  -3645  -1409   1017       O  
ATOM   3204  CB  GLU D  42      47.318  27.745  12.747  1.00 77.87           C  
ANISOU 3204  CB  GLU D  42    12466   7869   9253  -2986   -410   1332       C  
ATOM   3205  CG  GLU D  42      46.730  26.489  13.369  1.00 82.92           C  
ANISOU 3205  CG  GLU D  42    13193   8316   9997  -3460   -141   1371       C  
ATOM   3206  CD  GLU D  42      46.620  26.605  14.883  1.00 84.02           C  
ANISOU 3206  CD  GLU D  42    13104   8564  10256  -3283    385   1513       C  
ATOM   3207  OE1 GLU D  42      47.516  27.231  15.492  1.00 80.30           O  
ANISOU 3207  OE1 GLU D  42    12774   8130   9608  -2766    566   1544       O  
ATOM   3208  OE2 GLU D  42      45.648  26.068  15.466  1.00 89.05           O  
ANISOU 3208  OE2 GLU D  42    13453   9242  11142  -3699    627   1592       O  
ATOM   3209  N   LEU D  43      47.490  29.069  10.014  1.00 78.63           N  
ANISOU 3209  N   LEU D  43    12800   8070   9007  -2903  -1424   1209       N  
ATOM   3210  CA  LEU D  43      46.835  29.554   8.806  1.00 82.71           C  
ANISOU 3210  CA  LEU D  43    13247   8709   9471  -3076  -2060   1210       C  
ATOM   3211  C   LEU D  43      47.632  29.179   7.567  1.00 83.72           C  
ANISOU 3211  C   LEU D  43    14249   8533   9027  -3180  -2208   1077       C  
ATOM   3212  O   LEU D  43      47.083  28.664   6.594  1.00 88.66           O  
ANISOU 3212  O   LEU D  43    15174   9066   9446  -3619  -2676    988       O  
ATOM   3213  CB  LEU D  43      46.664  31.066   8.904  1.00 80.90           C  
ANISOU 3213  CB  LEU D  43    12530   8759   9449  -2621  -2213   1352       C  
ATOM   3214  CG  LEU D  43      45.494  31.709   8.170  1.00 85.83           C  
ANISOU 3214  CG  LEU D  43    12676   9629  10305  -2709  -2899   1457       C  
ATOM   3215  CD1 LEU D  43      45.983  32.460   6.925  1.00 85.93           C  
ANISOU 3215  CD1 LEU D  43    13238   9538   9873  -2552  -3321   1504       C  
ATOM   3216  CD2 LEU D  43      44.405  30.684   7.833  1.00 91.89           C  
ANISOU 3216  CD2 LEU D  43    13203  10458  11252  -3336  -3293   1406       C  
ATOM   3217  N   GLY D  44      48.937  29.413   7.628  1.00 80.09           N  
ANISOU 3217  N   GLY D  44    14201   7916   8312  -2796  -1785   1050       N  
ATOM   3218  CA  GLY D  44      49.830  29.082   6.527  1.00 82.25           C  
ANISOU 3218  CA  GLY D  44    15300   7896   8057  -2822  -1724    914       C  
ATOM   3219  C   GLY D  44      49.808  27.608   6.167  1.00 86.98           C  
ANISOU 3219  C   GLY D  44    16504   8126   8421  -3217  -1650    715       C  
ATOM   3220  O   GLY D  44      49.765  27.239   4.994  1.00 91.28           O  
ANISOU 3220  O   GLY D  44    17703   8462   8519  -3501  -1903    566       O  
ATOM   3221  N   LEU D  45      49.845  26.754   7.177  1.00 87.35           N  
ANISOU 3221  N   LEU D  45    16436   8038   8716  -3245  -1298    709       N  
ATOM   3222  CA  LEU D  45      49.780  25.323   6.942  1.00 92.83           C  
ANISOU 3222  CA  LEU D  45    17747   8293   9232  -3626  -1202    533       C  
ATOM   3223  C   LEU D  45      48.523  24.956   6.171  1.00100.43           C  
ANISOU 3223  C   LEU D  45    18764   9260  10133  -4301  -1828    440       C  
ATOM   3224  O   LEU D  45      48.577  24.246   5.173  1.00104.96           O  
ANISOU 3224  O   LEU D  45    20126   9483  10274  -4635  -1993    219       O  
ATOM   3225  CB  LEU D  45      49.809  24.574   8.267  1.00 91.42           C  
ANISOU 3225  CB  LEU D  45    17380   7984   9371  -3583   -794    623       C  
ATOM   3226  CG  LEU D  45      51.199  24.346   8.848  1.00 87.35           C  
ANISOU 3226  CG  LEU D  45    17136   7252   8800  -3010   -234    652       C  
ATOM   3227  CD1 LEU D  45      51.089  23.851  10.271  1.00 86.08           C  
ANISOU 3227  CD1 LEU D  45    16736   7048   8924  -2943     47    822       C  
ATOM   3228  CD2 LEU D  45      51.948  23.345   7.976  1.00 89.65           C  
ANISOU 3228  CD2 LEU D  45    18336   7005   8721  -3005    -14    428       C  
ATOM   3229  N   ARG D  46      47.385  25.451   6.633  1.00103.45           N  
ANISOU 3229  N   ARG D  46    18298  10044  10963  -4501  -2184    596       N  
ATOM   3230  CA  ARG D  46      46.127  25.088   6.017  1.00112.70           C  
ANISOU 3230  CA  ARG D  46    19320  11286  12214  -5175  -2842    535       C  
ATOM   3231  C   ARG D  46      46.171  25.335   4.515  1.00117.95           C  
ANISOU 3231  C   ARG D  46    20620  11876  12322  -5331  -3421    402       C  
ATOM   3232  O   ARG D  46      45.778  24.482   3.723  1.00124.42           O  
ANISOU 3232  O   ARG D  46    22029  12415  12831  -5919  -3801    196       O  
ATOM   3233  CB  ARG D  46      44.977  25.848   6.666  1.00113.56           C  
ANISOU 3233  CB  ARG D  46    18260  11926  12962  -5207  -3114    752       C  
ATOM   3234  CG  ARG D  46      43.616  25.198   6.455  1.00122.83           C  
ANISOU 3234  CG  ARG D  46    19018  13192  14461  -5982  -3646    717       C  
ATOM   3235  CD  ARG D  46      42.849  25.083   7.773  1.00125.16           C  
ANISOU 3235  CD  ARG D  46    18373  13735  15447  -6095  -3254    878       C  
ATOM   3236  NE  ARG D  46      43.004  26.282   8.599  1.00120.82           N  
ANISOU 3236  NE  ARG D  46    17155  13558  15193  -5391  -2917   1072       N  
ATOM   3237  CZ  ARG D  46      42.101  27.256   8.686  1.00123.49           C  
ANISOU 3237  CZ  ARG D  46    16523  14373  16024  -5229  -3233   1221       C  
ATOM   3238  NH1 ARG D  46      40.963  27.167   8.003  1.00131.18           N  
ANISOU 3238  NH1 ARG D  46    16965  15574  17303  -5720  -3956   1230       N  
ATOM   3239  NH2 ARG D  46      42.336  28.312   9.461  1.00118.45           N  
ANISOU 3239  NH2 ARG D  46    15452  13964  15589  -4568  -2851   1352       N  
ATOM   3240  N   VAL D  47      46.663  26.500   4.121  1.00116.85           N  
ANISOU 3240  N   VAL D  47    20453  11943  12000  -4839  -3482    519       N  
ATOM   3241  CA  VAL D  47      46.756  26.819   2.713  1.00122.83           C  
ANISOU 3241  CA  VAL D  47    21915  12618  12138  -4955  -3981    441       C  
ATOM   3242  C   VAL D  47      47.764  25.909   2.055  1.00125.73           C  
ANISOU 3242  C   VAL D  47    23462  12450  11858  -5021  -3538    157       C  
ATOM   3243  O   VAL D  47      47.466  25.304   1.038  1.00133.00           O  
ANISOU 3243  O   VAL D  47    25157  13112  12266  -5505  -3953    -55       O  
ATOM   3244  CB  VAL D  47      47.190  28.264   2.483  1.00119.27           C  
ANISOU 3244  CB  VAL D  47    21291  12420  11608  -4401  -4009    658       C  
ATOM   3245  CG1 VAL D  47      47.290  28.544   0.999  1.00124.25           C  
ANISOU 3245  CG1 VAL D  47    22800  12918  11492  -4557  -4496    609       C  
ATOM   3246  CG2 VAL D  47      46.209  29.224   3.136  1.00118.69           C  
ANISOU 3246  CG2 VAL D  47    20087  12816  12193  -4228  -4394    925       C  
ATOM   3247  N   PHE D  59      35.434  16.517   7.302  1.00 65.04           N  
ATOM   3248  CA  PHE D  59      34.338  17.431   7.669  1.00 65.17           C  
ATOM   3249  C   PHE D  59      34.673  18.956   7.701  1.00 64.01           C  
ATOM   3250  O   PHE D  59      35.837  19.374   7.559  1.00 64.38           O  
ATOM   3251  CB  PHE D  59      33.663  17.011   8.992  1.00 65.80           C  
ATOM   3252  CG  PHE D  59      32.258  17.548   9.138  1.00 67.21           C  
ATOM   3253  CD1 PHE D  59      31.952  18.489  10.108  1.00 68.70           C  
ATOM   3254  CD2 PHE D  59      31.254  17.142   8.263  1.00 67.47           C  
ATOM   3255  CE1 PHE D  59      30.648  18.999  10.220  1.00 69.00           C  
ATOM   3256  CE2 PHE D  59      29.958  17.652   8.367  1.00 68.07           C  
ATOM   3257  CZ  PHE D  59      29.657  18.581   9.347  1.00 68.16           C  
ATOM   3258  N   ASN D  60      33.637  19.775   7.903  1.00 61.62           N  
ATOM   3259  CA  ASN D  60      33.758  21.211   7.685  1.00 58.70           C  
ATOM   3260  C   ASN D  60      32.375  21.869   7.585  1.00 55.31           C  
ATOM   3261  O   ASN D  60      31.775  21.840   6.517  1.00 55.67           O  
ATOM   3262  CB  ASN D  60      34.516  21.423   6.373  1.00 59.28           C  
ATOM   3263  CG  ASN D  60      34.925  22.871   6.160  1.00 61.83           C  
ATOM   3264  OD1 ASN D  60      34.290  23.614   5.393  1.00 64.68           O  
ATOM   3265  ND2 ASN D  60      35.986  23.282   6.838  1.00 62.92           N  
ATOM   3266  N   GLN D  61      31.851  22.442   8.663  1.00102.82           N  
ANISOU 3266  N   GLN D  61    15202  10030  13837    102  -2755  -1562       N  
ATOM   3267  CA  GLN D  61      30.494  22.971   8.571  1.00 95.59           C  
ANISOU 3267  CA  GLN D  61    14669   8952  12700    -11  -2482  -1283       C  
ATOM   3268  C   GLN D  61      30.265  23.759   7.296  1.00 93.10           C  
ANISOU 3268  C   GLN D  61    14111   8779  12484   -282  -2070  -1088       C  
ATOM   3269  O   GLN D  61      29.342  23.475   6.537  1.00 90.04           O  
ANISOU 3269  O   GLN D  61    13847   8443  11923   -267  -1793   -894       O  
ATOM   3270  CB  GLN D  61      30.147  23.862   9.755  1.00 95.59           C  
ANISOU 3270  CB  GLN D  61    15022   8657  12640    -72  -2658  -1281       C  
ATOM   3271  CG  GLN D  61      29.334  23.174  10.820  1.00 91.87           C  
ANISOU 3271  CG  GLN D  61    15076   7993  11836    159  -2825  -1266       C  
ATOM   3272  CD  GLN D  61      28.221  22.344  10.238  1.00 86.28           C  
ANISOU 3272  CD  GLN D  61    14555   7347  10881    244  -2559  -1067       C  
ATOM   3273  OE1 GLN D  61      27.641  22.690   9.214  1.00 83.21           O  
ANISOU 3273  OE1 GLN D  61    14043   7061  10513    110  -2215   -890       O  
ATOM   3274  NE2 GLN D  61      27.919  21.232  10.884  1.00 85.49           N  
ANISOU 3274  NE2 GLN D  61    14771   7170  10540    455  -2740  -1091       N  
ATOM   3275  N   MET D  62      31.099  24.764   7.070  1.00 93.57           N  
ANISOU 3275  N   MET D  62    13847   8888  12817   -549  -2049  -1132       N  
ATOM   3276  CA  MET D  62      30.847  25.718   6.005  1.00 91.50           C  
ANISOU 3276  CA  MET D  62    13458   8685  12625   -856  -1690   -911       C  
ATOM   3277  C   MET D  62      30.880  25.030   4.639  1.00 89.23           C  
ANISOU 3277  C   MET D  62    12902   8719  12283   -837  -1377   -836       C  
ATOM   3278  O   MET D  62      29.996  25.219   3.806  1.00 86.72           O  
ANISOU 3278  O   MET D  62    12731   8406  11811   -906  -1085   -601       O  
ATOM   3279  CB  MET D  62      31.852  26.869   6.081  1.00 95.37           C  
ANISOU 3279  CB  MET D  62    13654   9153  13429  -1188  -1761   -977       C  
ATOM   3280  CG  MET D  62      31.232  28.236   5.847  1.00 96.57           C  
ANISOU 3280  CG  MET D  62    14030   9068  13593  -1481  -1600   -741       C  
ATOM   3281  SD  MET D  62      29.676  28.478   6.763  1.00 96.68           S  
ANISOU 3281  SD  MET D  62    14710   8711  13313  -1262  -1682   -632       S  
ATOM   3282  CE  MET D  62      30.194  28.210   8.461  1.00 97.45           C  
ANISOU 3282  CE  MET D  62    14968   8633  13427  -1057  -2167   -931       C  
ATOM   3283  N   GLU D  63      31.896  24.212   4.423  1.00 89.36           N  
ANISOU 3283  N   GLU D  63    12532   9005  12417   -712  -1461  -1059       N  
ATOM   3284  CA  GLU D  63      32.038  23.538   3.158  1.00 87.85           C  
ANISOU 3284  CA  GLU D  63    12071   9142  12166   -662  -1180  -1041       C  
ATOM   3285  C   GLU D  63      30.830  22.632   2.919  1.00 82.84           C  
ANISOU 3285  C   GLU D  63    11824   8430  11221   -413  -1111   -913       C  
ATOM   3286  O   GLU D  63      30.355  22.476   1.786  1.00 81.86           O  
ANISOU 3286  O   GLU D  63    11682   8456  10965   -447   -809   -762       O  
ATOM   3287  CB  GLU D  63      33.325  22.727   3.154  1.00 91.10           C  
ANISOU 3287  CB  GLU D  63    12016   9843  12756   -484  -1346  -1369       C  
ATOM   3288  CG  GLU D  63      33.933  22.591   1.782  1.00 94.34           C  
ANISOU 3288  CG  GLU D  63    11955  10673  13216   -584   -993  -1390       C  
ATOM   3289  CD  GLU D  63      34.223  23.940   1.158  1.00 97.27           C  
ANISOU 3289  CD  GLU D  63    12108  11123  13726  -1065   -687  -1202       C  
ATOM   3290  OE1 GLU D  63      34.949  24.738   1.782  1.00100.57           O  
ANISOU 3290  OE1 GLU D  63    12331  11474  14406  -1294   -844  -1284       O  
ATOM   3291  OE2 GLU D  63      33.721  24.207   0.048  1.00 96.98           O  
ANISOU 3291  OE2 GLU D  63    12123  11196  13530  -1224   -313   -966       O  
ATOM   3292  N   TYR D  64      30.341  22.044   4.006  1.00 79.39           N  
ANISOU 3292  N   TYR D  64    11749   7755  10660   -181  -1402   -972       N  
ATOM   3293  CA  TYR D  64      29.198  21.143   3.991  1.00 74.43           C  
ANISOU 3293  CA  TYR D  64    11504   7023   9753     23  -1386   -859       C  
ATOM   3294  C   TYR D  64      27.898  21.895   3.733  1.00 71.16           C  
ANISOU 3294  C   TYR D  64    11386   6460   9192   -139  -1142   -570       C  
ATOM   3295  O   TYR D  64      27.107  21.510   2.880  1.00 69.01           O  
ANISOU 3295  O   TYR D  64    11198   6257   8764   -109   -935   -425       O  
ATOM   3296  CB  TYR D  64      29.133  20.408   5.334  1.00 73.94           C  
ANISOU 3296  CB  TYR D  64    11757   6741   9595    258  -1770   -991       C  
ATOM   3297  CG  TYR D  64      27.862  19.626   5.582  1.00 69.84           C  
ANISOU 3297  CG  TYR D  64    11692   6060   8784    390  -1766   -843       C  
ATOM   3298  CD1 TYR D  64      27.795  18.267   5.309  1.00 68.83           C  
ANISOU 3298  CD1 TYR D  64    11643   5974   8535    619  -1871   -908       C  
ATOM   3299  CD2 TYR D  64      26.728  20.247   6.097  1.00 67.16           C  
ANISOU 3299  CD2 TYR D  64    11695   5526   8298    280  -1665   -649       C  
ATOM   3300  CE1 TYR D  64      26.631  17.547   5.533  1.00 66.34           C  
ANISOU 3300  CE1 TYR D  64    11736   5502   7967    683  -1870   -758       C  
ATOM   3301  CE2 TYR D  64      25.562  19.541   6.324  1.00 63.43           C  
ANISOU 3301  CE2 TYR D  64    11583   4946   7573    361  -1634   -516       C  
ATOM   3302  CZ  TYR D  64      25.522  18.190   6.043  1.00 63.95           C  
ANISOU 3302  CZ  TYR D  64    11722   5048   7531    537  -1737   -559       C  
ATOM   3303  OH  TYR D  64      24.370  17.478   6.266  1.00 61.93           O  
ANISOU 3303  OH  TYR D  64    11817   4676   7038    564  -1711   -414       O  
ATOM   3304  N   ASN D  65      27.667  22.964   4.483  1.00 70.50           N  
ANISOU 3304  N   ASN D  65    11463   6164   9160   -285  -1194   -510       N  
ATOM   3305  CA  ASN D  65      26.519  23.812   4.212  1.00 68.09           C  
ANISOU 3305  CA  ASN D  65    11396   5723   8753   -416   -982   -270       C  
ATOM   3306  C   ASN D  65      26.468  24.196   2.741  1.00 67.94           C  
ANISOU 3306  C   ASN D  65    11174   5881   8758   -584   -667   -107       C  
ATOM   3307  O   ASN D  65      25.402  24.174   2.112  1.00 66.04           O  
ANISOU 3307  O   ASN D  65    11107   5627   8358   -567   -488     76       O  
ATOM   3308  CB  ASN D  65      26.572  25.075   5.063  1.00 69.25           C  
ANISOU 3308  CB  ASN D  65    11671   5634   9008   -562  -1092   -273       C  
ATOM   3309  CG  ASN D  65      26.387  24.788   6.545  1.00 69.17           C  
ANISOU 3309  CG  ASN D  65    11957   5429   8894   -388  -1378   -406       C  
ATOM   3310  OD1 ASN D  65      26.792  25.573   7.401  1.00 72.23           O  
ANISOU 3310  OD1 ASN D  65    12413   5649   9383   -454  -1566   -504       O  
ATOM   3311  ND2 ASN D  65      25.777  23.664   6.850  1.00 66.77           N  
ANISOU 3311  ND2 ASN D  65    11858   5138   8374   -180  -1421   -406       N  
ATOM   3312  N   LYS D  66      27.628  24.544   2.191  1.00 69.92           N  
ANISOU 3312  N   LYS D  66    11052   6313   9199   -754   -602   -177       N  
ATOM   3313  CA  LYS D  66      27.700  24.940   0.798  1.00 70.31           C  
ANISOU 3313  CA  LYS D  66    10921   6552   9240   -947   -286    -16       C  
ATOM   3314  C   LYS D  66      27.211  23.821  -0.138  1.00 68.66           C  
ANISOU 3314  C   LYS D  66    10720   6543   8824   -751   -140     14       C  
ATOM   3315  O   LYS D  66      26.318  24.033  -0.969  1.00 67.17           O  
ANISOU 3315  O   LYS D  66    10695   6343   8481   -793     55    222       O  
ATOM   3316  CB  LYS D  66      29.121  25.383   0.462  1.00 74.09           C  
ANISOU 3316  CB  LYS D  66    10956   7240   9954  -1179   -228   -122       C  
ATOM   3317  CG  LYS D  66      29.286  25.913  -0.940  1.00 75.52           C  
ANISOU 3317  CG  LYS D  66    10967   7625  10102  -1440    127     66       C  
ATOM   3318  CD  LYS D  66      30.672  26.503  -1.151  1.00 79.58           C  
ANISOU 3318  CD  LYS D  66    11031   8340  10864  -1747    204    -22       C  
ATOM   3319  CE  LYS D  66      30.925  26.678  -2.640  1.00 82.19           C  
ANISOU 3319  CE  LYS D  66    11162   8975  11092  -1964    601    137       C  
ATOM   3320  NZ  LYS D  66      32.108  27.519  -2.922  1.00 87.47           N  
ANISOU 3320  NZ  LYS D  66    11436   9814  11986  -2379    743    136       N  
ATOM   3321  N   LEU D  67      27.782  22.627   0.015  1.00 68.74           N  
ANISOU 3321  N   LEU D  67    10575   6710   8831   -517   -275   -209       N  
ATOM   3322  CA  LEU D  67      27.423  21.496  -0.834  1.00 67.50           C  
ANISOU 3322  CA  LEU D  67    10435   6722   8490   -311   -188   -226       C  
ATOM   3323  C   LEU D  67      25.934  21.190  -0.753  1.00 64.36           C  
ANISOU 3323  C   LEU D  67    10447   6124   7884   -215   -198    -52       C  
ATOM   3324  O   LEU D  67      25.289  20.907  -1.758  1.00 63.88           O  
ANISOU 3324  O   LEU D  67    10453   6151   7666   -191    -30     66       O  
ATOM   3325  CB  LEU D  67      28.198  20.252  -0.429  1.00 68.48           C  
ANISOU 3325  CB  LEU D  67    10412   6953   8652    -28   -427   -517       C  
ATOM   3326  CG  LEU D  67      28.592  19.278  -1.543  1.00 69.90           C  
ANISOU 3326  CG  LEU D  67    10381   7433   8744    150   -312   -644       C  
ATOM   3327  CD1 LEU D  67      28.520  17.861  -1.026  1.00 68.92           C  
ANISOU 3327  CD1 LEU D  67    10423   7219   8543    500   -621   -835       C  
ATOM   3328  CD2 LEU D  67      27.738  19.430  -2.795  1.00 69.27           C  
ANISOU 3328  CD2 LEU D  67    10421   7437   8462     61    -11   -421       C  
ATOM   3329  N   MET D  68      25.383  21.228   0.449  1.00 62.87           N  
ANISOU 3329  N   MET D  68    10525   5680   7684   -161   -396    -49       N  
ATOM   3330  CA  MET D  68      23.973  20.942   0.621  1.00 60.19           C  
ANISOU 3330  CA  MET D  68    10523   5183   7162    -92   -390     99       C  
ATOM   3331  C   MET D  68      23.125  21.994  -0.069  1.00 59.70           C  
ANISOU 3331  C   MET D  68    10539   5080   7064   -256   -167    330       C  
ATOM   3332  O   MET D  68      22.138  21.657  -0.714  1.00 58.73           O  
ANISOU 3332  O   MET D  68    10543   4975   6799   -207    -73    451       O  
ATOM   3333  CB  MET D  68      23.622  20.865   2.096  1.00 59.52           C  
ANISOU 3333  CB  MET D  68    10693   4870   7050    -24   -608     51       C  
ATOM   3334  CG  MET D  68      24.285  19.712   2.804  1.00 60.14           C  
ANISOU 3334  CG  MET D  68    10796   4938   7115    166   -879   -151       C  
ATOM   3335  SD  MET D  68      23.485  18.159   2.374  1.00 60.37           S  
ANISOU 3335  SD  MET D  68    11025   4977   6937    341   -922   -122       S  
ATOM   3336  CE  MET D  68      21.940  18.348   3.253  1.00 56.31           C  
ANISOU 3336  CE  MET D  68    10891   4252   6251    270   -890     66       C  
ATOM   3337  N   LEU D  69      23.506  23.265   0.049  1.00 60.78           N  
ANISOU 3337  N   LEU D  69    10614   5142   7337   -448   -113    385       N  
ATOM   3338  CA  LEU D  69      22.752  24.312  -0.611  1.00 60.23           C  
ANISOU 3338  CA  LEU D  69    10657   4990   7236   -587     54    603       C  
ATOM   3339  C   LEU D  69      22.781  24.129  -2.129  1.00 61.16           C  
ANISOU 3339  C   LEU D  69    10663   5319   7257   -639    266    714       C  
ATOM   3340  O   LEU D  69      21.777  24.347  -2.826  1.00 60.47           O  
ANISOU 3340  O   LEU D  69    10737   5194   7043   -629    360    884       O  
ATOM   3341  CB  LEU D  69      23.294  25.680  -0.248  1.00 61.94           C  
ANISOU 3341  CB  LEU D  69    10853   5057   7625   -802     38    636       C  
ATOM   3342  CG  LEU D  69      22.596  26.840  -0.961  1.00 61.60           C  
ANISOU 3342  CG  LEU D  69    10969   4881   7557   -945    169    867       C  
ATOM   3343  CD1 LEU D  69      21.120  26.867  -0.655  1.00 58.06           C  
ANISOU 3343  CD1 LEU D  69    10796   4280   6985   -770    131    939       C  
ATOM   3344  CD2 LEU D  69      23.243  28.152  -0.580  1.00 63.50           C  
ANISOU 3344  CD2 LEU D  69    11212   4933   7983  -1181    114    890       C  
ATOM   3345  N   GLU D  70      23.928  23.725  -2.654  1.00 63.10           N  
ANISOU 3345  N   GLU D  70    10625   5803   7548   -677    336    603       N  
ATOM   3346  CA  GLU D  70      24.015  23.497  -4.081  1.00 64.25           C  
ANISOU 3346  CA  GLU D  70    10673   6182   7556   -710    555    684       C  
ATOM   3347  C   GLU D  70      23.105  22.360  -4.490  1.00 62.12           C  
ANISOU 3347  C   GLU D  70    10556   5953   7094   -473    515    673       C  
ATOM   3348  O   GLU D  70      22.247  22.511  -5.359  1.00 61.55           O  
ANISOU 3348  O   GLU D  70    10638   5879   6871   -480    616    839       O  
ATOM   3349  CB  GLU D  70      25.433  23.158  -4.498  1.00 67.18           C  
ANISOU 3349  CB  GLU D  70    10670   6853   8003   -757    651    515       C  
ATOM   3350  CG  GLU D  70      25.537  22.861  -5.972  1.00 69.83           C  
ANISOU 3350  CG  GLU D  70    10918   7467   8148   -768    902    575       C  
ATOM   3351  CD  GLU D  70      26.849  22.233  -6.335  1.00 75.22           C  
ANISOU 3351  CD  GLU D  70    11203   8500   8877   -720    993    339       C  
ATOM   3352  OE1 GLU D  70      26.940  21.628  -7.426  1.00 78.22           O  
ANISOU 3352  OE1 GLU D  70    11514   9141   9066   -622   1161    304       O  
ATOM   3353  OE2 GLU D  70      27.788  22.340  -5.521  1.00 78.18           O  
ANISOU 3353  OE2 GLU D  70    11327   8898   9478   -759    883    168       O  
ATOM   3354  N   ASN D  71      23.299  21.209  -3.868  1.00 61.30           N  
ANISOU 3354  N   ASN D  71    10427   5868   6997   -267    336    475       N  
ATOM   3355  CA  ASN D  71      22.495  20.062  -4.209  1.00 59.80           C  
ANISOU 3355  CA  ASN D  71    10394   5687   6642    -70    264    455       C  
ATOM   3356  C   ASN D  71      21.006  20.370  -4.136  1.00 57.33           C  
ANISOU 3356  C   ASN D  71    10351   5188   6244    -91    255    647       C  
ATOM   3357  O   ASN D  71      20.255  20.068  -5.064  1.00 57.00           O  
ANISOU 3357  O   ASN D  71    10400   5198   6059    -48    313    737       O  
ATOM   3358  CB  ASN D  71      22.893  18.870  -3.350  1.00 59.65           C  
ANISOU 3358  CB  ASN D  71    10379   5631   6654    130     21    235       C  
ATOM   3359  CG  ASN D  71      24.100  18.155  -3.904  1.00 64.12           C  
ANISOU 3359  CG  ASN D  71    10680   6446   7239    262     23     13       C  
ATOM   3360  OD1 ASN D  71      24.504  18.395  -5.044  1.00 67.82           O  
ANISOU 3360  OD1 ASN D  71    10970   7149   7648    208    244     28       O  
ATOM   3361  ND2 ASN D  71      24.676  17.258  -3.115  1.00 67.53           N  
ANISOU 3361  ND2 ASN D  71    11092   6833   7733    450   -226   -204       N  
ATOM   3362  N   VAL D  72      20.579  21.001  -3.052  1.00 55.93           N  
ANISOU 3362  N   VAL D  72    10289   4807   6154   -145    178    692       N  
ATOM   3363  CA  VAL D  72      19.169  21.312  -2.906  1.00 54.04           C  
ANISOU 3363  CA  VAL D  72    10254   4427   5853   -140    177    836       C  
ATOM   3364  C   VAL D  72      18.703  22.288  -3.993  1.00 54.93           C  
ANISOU 3364  C   VAL D  72    10394   4553   5924   -234    327   1022       C  
ATOM   3365  O   VAL D  72      17.644  22.118  -4.611  1.00 54.13           O  
ANISOU 3365  O   VAL D  72    10397   4452   5718   -177    336   1119       O  
ATOM   3366  CB  VAL D  72      18.880  21.913  -1.547  1.00 53.40           C  
ANISOU 3366  CB  VAL D  72    10279   4155   5856   -162     93    822       C  
ATOM   3367  CG1 VAL D  72      17.556  22.634  -1.584  1.00 52.88           C  
ANISOU 3367  CG1 VAL D  72    10351   3984   5757   -165    145    963       C  
ATOM   3368  CG2 VAL D  72      18.893  20.850  -0.478  1.00 52.04           C  
ANISOU 3368  CG2 VAL D  72    10190   3936   5648    -59    -71    691       C  
ATOM   3369  N   SER D  73      19.497  23.323  -4.235  1.00 56.45           N  
ANISOU 3369  N   SER D  73    10507   4743   6199   -391    424   1076       N  
ATOM   3370  CA  SER D  73      19.118  24.288  -5.233  1.00 57.67           C  
ANISOU 3370  CA  SER D  73    10748   4869   6295   -498    541   1274       C  
ATOM   3371  C   SER D  73      19.019  23.622  -6.601  1.00 58.19           C  
ANISOU 3371  C   SER D  73    10801   5139   6172   -449    638   1320       C  
ATOM   3372  O   SER D  73      18.102  23.885  -7.401  1.00 58.45           O  
ANISOU 3372  O   SER D  73    10988   5137   6083   -420    651   1466       O  
ATOM   3373  CB  SER D  73      20.124  25.433  -5.250  1.00 60.05           C  
ANISOU 3373  CB  SER D  73    10976   5125   6715   -729    625   1333       C  
ATOM   3374  OG  SER D  73      19.682  26.505  -4.437  1.00 60.90           O  
ANISOU 3374  OG  SER D  73    11237   4960   6940   -774    530   1388       O  
ATOM   3375  N   ARG D  74      19.978  22.758  -6.872  1.00 58.76           N  
ANISOU 3375  N   ARG D  74    10691   5424   6212   -415    687   1173       N  
ATOM   3376  CA  ARG D  74      20.009  22.027  -8.115  1.00 59.64           C  
ANISOU 3376  CA  ARG D  74    10788   5749   6124   -336    775   1164       C  
ATOM   3377  C   ARG D  74      18.757  21.179  -8.281  1.00 57.37           C  
ANISOU 3377  C   ARG D  74    10670   5401   5727   -157    630   1164       C  
ATOM   3378  O   ARG D  74      18.089  21.217  -9.317  1.00 57.60           O  
ANISOU 3378  O   ARG D  74    10825   5467   5592   -129    659   1276       O  
ATOM   3379  CB  ARG D  74      21.225  21.126  -8.095  1.00 61.19           C  
ANISOU 3379  CB  ARG D  74    10742   6169   6339   -261    801    934       C  
ATOM   3380  CG  ARG D  74      21.912  21.069  -9.407  1.00 65.44           C  
ANISOU 3380  CG  ARG D  74    11166   6991   6708   -301   1021    935       C  
ATOM   3381  CD  ARG D  74      23.362  20.752  -9.239  1.00 69.49           C  
ANISOU 3381  CD  ARG D  74    11346   7739   7319   -305   1104    720       C  
ATOM   3382  NE  ARG D  74      24.051  21.213 -10.425  1.00 74.17           N  
ANISOU 3382  NE  ARG D  74    11808   8610   7764   -459   1403    790       N  
ATOM   3383  CZ  ARG D  74      25.129  21.970 -10.390  1.00 77.20           C  
ANISOU 3383  CZ  ARG D  74    11933   9135   8264   -700   1587    797       C  
ATOM   3384  NH1 ARG D  74      25.641  22.294  -9.219  1.00 78.04           N  
ANISOU 3384  NH1 ARG D  74    11886   9116   8650   -774   1459    712       N  
ATOM   3385  NH2 ARG D  74      25.701  22.364 -11.515  1.00 81.02           N  
ANISOU 3385  NH2 ARG D  74    12313   9894   8576   -874   1894    883       N  
ATOM   3386  N   VAL D  75      18.446  20.421  -7.235  1.00 55.16           N  
ANISOU 3386  N   VAL D  75    10403   5020   5536    -53    462   1042       N  
ATOM   3387  CA  VAL D  75      17.280  19.550  -7.223  1.00 53.37           C  
ANISOU 3387  CA  VAL D  75    10312   4727   5238     65    317   1037       C  
ATOM   3388  C   VAL D  75      16.012  20.353  -7.464  1.00 53.28           C  
ANISOU 3388  C   VAL D  75    10426   4605   5214     29    315   1216       C  
ATOM   3389  O   VAL D  75      15.145  19.960  -8.251  1.00 53.43           O  
ANISOU 3389  O   VAL D  75    10528   4652   5121     95    257   1263       O  
ATOM   3390  CB  VAL D  75      17.178  18.798  -5.897  1.00 51.71           C  
ANISOU 3390  CB  VAL D  75    10125   4399   5122    116    159    919       C  
ATOM   3391  CG1 VAL D  75      15.814  18.185  -5.745  1.00 50.00           C  
ANISOU 3391  CG1 VAL D  75    10042   4094   4861    151     43    966       C  
ATOM   3392  CG2 VAL D  75      18.264  17.745  -5.820  1.00 52.22           C  
ANISOU 3392  CG2 VAL D  75    10107   4556   5177    222     82    719       C  
ATOM   3393  N   ARG D  76      15.908  21.498  -6.804  1.00 53.41           N  
ANISOU 3393  N   ARG D  76    10455   4488   5349    -56    351   1298       N  
ATOM   3394  CA  ARG D  76      14.753  22.360  -7.019  1.00 53.58           C  
ANISOU 3394  CA  ARG D  76    10588   4397   5375    -46    327   1441       C  
ATOM   3395  C   ARG D  76      14.605  22.840  -8.470  1.00 54.65           C  
ANISOU 3395  C   ARG D  76    10815   4586   5364    -60    378   1586       C  
ATOM   3396  O   ARG D  76      13.507  22.805  -9.032  1.00 54.77           O  
ANISOU 3396  O   ARG D  76    10917   4581   5313     27    287   1651       O  
ATOM   3397  CB  ARG D  76      14.782  23.559  -6.084  1.00 54.02           C  
ANISOU 3397  CB  ARG D  76    10669   4279   5576   -107    339   1477       C  
ATOM   3398  CG  ARG D  76      13.579  24.424  -6.284  1.00 55.40           C  
ANISOU 3398  CG  ARG D  76    10953   4331   5764    -42    284   1587       C  
ATOM   3399  CD  ARG D  76      13.892  25.847  -5.974  1.00 59.39           C  
ANISOU 3399  CD  ARG D  76    11546   4651   6367   -115    299   1661       C  
ATOM   3400  NE  ARG D  76      12.892  26.735  -6.545  1.00 62.54           N  
ANISOU 3400  NE  ARG D  76    12087   4926   6751    -29    222   1782       N  
ATOM   3401  CZ  ARG D  76      12.583  27.909  -6.017  1.00 64.30           C  
ANISOU 3401  CZ  ARG D  76    12417   4933   7079      5    158   1805       C  
ATOM   3402  NH1 ARG D  76      13.195  28.328  -4.921  1.00 64.80           N  
ANISOU 3402  NH1 ARG D  76    12468   4891   7262    -57    171   1717       N  
ATOM   3403  NH2 ARG D  76      11.656  28.655  -6.577  1.00 66.41           N  
ANISOU 3403  NH2 ARG D  76    12821   5080   7334    126     49   1897       N  
ATOM   3404  N   ALA D  77      15.695  23.292  -9.075  1.00 55.72           N  
ANISOU 3404  N   ALA D  77    10932   4799   5440   -178    520   1637       N  
ATOM   3405  CA  ALA D  77      15.619  23.699 -10.473  1.00 57.50           C  
ANISOU 3405  CA  ALA D  77    11289   5088   5469   -211    588   1790       C  
ATOM   3406  C   ALA D  77      15.154  22.531 -11.321  1.00 57.29           C  
ANISOU 3406  C   ALA D  77    11292   5213   5263    -65    521   1721       C  
ATOM   3407  O   ALA D  77      14.223  22.649 -12.116  1.00 57.91           O  
ANISOU 3407  O   ALA D  77    11523   5260   5220     10    426   1818       O  
ATOM   3408  CB  ALA D  77      16.955  24.197 -10.951  1.00 59.41           C  
ANISOU 3408  CB  ALA D  77    11472   5445   5655   -398    796   1842       C  
ATOM   3409  N   MET D  78      15.801  21.390 -11.124  1.00 56.70           N  
ANISOU 3409  N   MET D  78    11082   5283   5180     -7    534   1535       N  
ATOM   3410  CA  MET D  78      15.488  20.203 -11.908  1.00 56.56           C  
ANISOU 3410  CA  MET D  78    11110   5388   4992    137    447   1435       C  
ATOM   3411  C   MET D  78      14.008  19.845 -11.786  1.00 55.57           C  
ANISOU 3411  C   MET D  78    11077   5135   4902    227    230   1457       C  
ATOM   3412  O   MET D  78      13.336  19.651 -12.800  1.00 56.94           O  
ANISOU 3412  O   MET D  78    11376   5343   4916    301    142   1502       O  
ATOM   3413  CB  MET D  78      16.402  19.028 -11.542  1.00 55.93           C  
ANISOU 3413  CB  MET D  78    10890   5430   4932    216    442   1206       C  
ATOM   3414  CG  MET D  78      17.794  19.115 -12.146  1.00 57.49           C  
ANISOU 3414  CG  MET D  78    10958   5858   5026    182    658   1138       C  
ATOM   3415  SD  MET D  78      18.818  17.657 -11.862  1.00 59.36           S  
ANISOU 3415  SD  MET D  78    11027   6249   5278    364    599    817       S  
ATOM   3416  CE  MET D  78      19.042  17.685 -10.079  1.00 56.25           C  
ANISOU 3416  CE  MET D  78    10526   5658   5189    318    473    751       C  
ATOM   3417  N   CYS D  79      13.482  19.796 -10.566  1.00 53.78           N  
ANISOU 3417  N   CYS D  79    10783   4776   4874    213    147   1424       N  
ATOM   3418  CA  CYS D  79      12.083  19.411 -10.385  1.00 53.31           C  
ANISOU 3418  CA  CYS D  79    10749   4641   4867    266    -27   1430       C  
ATOM   3419  C   CYS D  79      11.123  20.385 -11.031  1.00 54.71           C  
ANISOU 3419  C   CYS D  79    11007   4762   5019    298    -80   1577       C  
ATOM   3420  O   CYS D  79      10.097  19.972 -11.594  1.00 55.58           O  
ANISOU 3420  O   CYS D  79    11148   4883   5087    371   -241   1577       O  
ATOM   3421  CB  CYS D  79      11.742  19.282  -8.917  1.00 51.69           C  
ANISOU 3421  CB  CYS D  79    10454   4337   4847    222    -52   1377       C  
ATOM   3422  SG  CYS D  79      12.559  17.877  -8.141  1.00 51.27           S  
ANISOU 3422  SG  CYS D  79    10375   4298   4807    216    -99   1204       S  
ATOM   3423  N   THR D  80      11.439  21.676 -10.939  1.00 55.23           N  
ANISOU 3423  N   THR D  80    11115   4747   5122    247     21   1695       N  
ATOM   3424  CA  THR D  80      10.632  22.664 -11.615  1.00 56.67           C  
ANISOU 3424  CA  THR D  80    11427   4841   5266    303    -62   1838       C  
ATOM   3425  C   THR D  80      10.463  22.232 -13.060  1.00 58.39           C  
ANISOU 3425  C   THR D  80    11785   5158   5242    366   -138   1880       C  
ATOM   3426  O   THR D  80       9.339  22.182 -13.572  1.00 59.31           O  
ANISOU 3426  O   THR D  80    11951   5248   5335    477   -332   1900       O  
ATOM   3427  CB  THR D  80      11.272  24.052 -11.579  1.00 57.76           C  
ANISOU 3427  CB  THR D  80    11670   4854   5421    210     49   1978       C  
ATOM   3428  OG1 THR D  80      11.453  24.455 -10.222  1.00 56.64           O  
ANISOU 3428  OG1 THR D  80    11419   4609   5491    167     94   1914       O  
ATOM   3429  CG2 THR D  80      10.373  25.038 -12.257  1.00 59.25           C  
ANISOU 3429  CG2 THR D  80    12042   4904   5565    299    -94   2124       C  
ATOM   3430  N   GLU D  81      11.577  21.912 -13.716  1.00 59.29           N  
ANISOU 3430  N   GLU D  81    11951   5404   5172    306     10   1874       N  
ATOM   3431  CA  GLU D  81      11.535  21.555 -15.144  1.00 61.39           C  
ANISOU 3431  CA  GLU D  81    12390   5785   5149    373    -32   1907       C  
ATOM   3432  C   GLU D  81      10.783  20.249 -15.362  1.00 60.65           C  
ANISOU 3432  C   GLU D  81    12264   5748   5033    499   -239   1752       C  
ATOM   3433  O   GLU D  81       9.946  20.157 -16.263  1.00 62.00           O  
ANISOU 3433  O   GLU D  81    12573   5914   5071    597   -425   1786       O  
ATOM   3434  CB  GLU D  81      12.938  21.407 -15.723  1.00 62.92           C  
ANISOU 3434  CB  GLU D  81    12600   6163   5143    290    212   1893       C  
ATOM   3435  CG  GLU D  81      13.701  22.689 -15.838  1.00 64.78           C  
ANISOU 3435  CG  GLU D  81    12905   6363   5344    113    418   2079       C  
ATOM   3436  CD  GLU D  81      12.967  23.708 -16.654  1.00 68.95           C  
ANISOU 3436  CD  GLU D  81    13718   6749   5731    117    314   2305       C  
ATOM   3437  OE1 GLU D  81      12.658  23.435 -17.837  1.00 70.81           O  
ANISOU 3437  OE1 GLU D  81    14154   7069   5681    201    247   2348       O  
ATOM   3438  OE2 GLU D  81      12.708  24.802 -16.109  1.00 71.35           O  
ANISOU 3438  OE2 GLU D  81    14072   6838   6198     51    276   2432       O  
ATOM   3439  N   ILE D  82      11.086  19.246 -14.540  1.00 58.45           N  
ANISOU 3439  N   ILE D  82    11826   5500   4881    488   -235   1585       N  
ATOM   3440  CA  ILE D  82      10.416  17.964 -14.643  1.00 57.88           C  
ANISOU 3440  CA  ILE D  82    11744   5437   4809    564   -447   1443       C  
ATOM   3441  C   ILE D  82       8.925  18.160 -14.507  1.00 57.80           C  
ANISOU 3441  C   ILE D  82    11697   5328   4935    584   -657   1493       C  
ATOM   3442  O   ILE D  82       8.132  17.607 -15.287  1.00 58.95           O  
ANISOU 3442  O   ILE D  82    11914   5487   4996    657   -875   1455       O  
ATOM   3443  CB  ILE D  82      10.899  16.983 -13.568  1.00 56.19           C  
ANISOU 3443  CB  ILE D  82    11402   5206   4741    526   -435   1289       C  
ATOM   3444  CG1 ILE D  82      12.366  16.637 -13.803  1.00 56.70           C  
ANISOU 3444  CG1 ILE D  82    11465   5399   4679    558   -272   1185       C  
ATOM   3445  CG2 ILE D  82      10.068  15.708 -13.595  1.00 55.98           C  
ANISOU 3445  CG2 ILE D  82    11398   5131   4739    556   -686   1174       C  
ATOM   3446  CD1 ILE D  82      13.029  15.955 -12.636  1.00 54.80           C  
ANISOU 3446  CD1 ILE D  82    11109   5117   4595    537   -262   1049       C  
ATOM   3447  N   LEU D  83       8.550  18.958 -13.515  1.00 56.69           N  
ANISOU 3447  N   LEU D  83    11432   5100   5007    530   -600   1557       N  
ATOM   3448  CA  LEU D  83       7.147  19.291 -13.293  1.00 57.06           C  
ANISOU 3448  CA  LEU D  83    11382   5090   5208    570   -767   1583       C  
ATOM   3449  C   LEU D  83       6.500  19.806 -14.556  1.00 59.19           C  
ANISOU 3449  C   LEU D  83    11799   5353   5335    692   -942   1666       C  
ATOM   3450  O   LEU D  83       5.443  19.337 -14.966  1.00 60.46           O  
ANISOU 3450  O   LEU D  83    11914   5531   5526    752  -1178   1614       O  
ATOM   3451  CB  LEU D  83       7.000  20.355 -12.214  1.00 56.25           C  
ANISOU 3451  CB  LEU D  83    11168   4905   5299    546   -651   1635       C  
ATOM   3452  CG  LEU D  83       5.543  20.674 -11.882  1.00 56.92           C  
ANISOU 3452  CG  LEU D  83    11091   4974   5560    617   -800   1617       C  
ATOM   3453  CD1 LEU D  83       4.872  19.511 -11.143  1.00 55.89           C  
ANISOU 3453  CD1 LEU D  83    10758   4916   5560    519   -848   1499       C  
ATOM   3454  CD2 LEU D  83       5.488  21.925 -11.043  1.00 56.33           C  
ANISOU 3454  CD2 LEU D  83    10971   4808   5624    657   -696   1658       C  
ATOM   3455  N   LYS D  84       7.137  20.785 -15.181  1.00 60.12           N  
ANISOU 3455  N   LYS D  84    12110   5439   5293    713   -843   1802       N  
ATOM   3456  CA  LYS D  84       6.564  21.366 -16.382  1.00 62.46           C  
ANISOU 3456  CA  LYS D  84    12618   5700   5415    833  -1025   1908       C  
ATOM   3457  C   LYS D  84       6.376  20.320 -17.462  1.00 63.69           C  
ANISOU 3457  C   LYS D  84    12890   5957   5354    899  -1194   1827       C  
ATOM   3458  O   LYS D  84       5.354  20.296 -18.141  1.00 65.88           O  
ANISOU 3458  O   LYS D  84    13224   6211   5597   1017  -1474   1823       O  
ATOM   3459  CB  LYS D  84       7.417  22.512 -16.887  1.00 63.71           C  
ANISOU 3459  CB  LYS D  84    13018   5795   5394    790   -866   2095       C  
ATOM   3460  CG  LYS D  84       7.426  23.703 -15.957  1.00 63.19           C  
ANISOU 3460  CG  LYS D  84    12900   5570   5541    752   -785   2179       C  
ATOM   3461  CD  LYS D  84       8.107  24.871 -16.627  1.00 66.33           C  
ANISOU 3461  CD  LYS D  84    13594   5858   5748    685   -693   2395       C  
ATOM   3462  CE  LYS D  84       8.719  25.815 -15.615  1.00 66.50           C  
ANISOU 3462  CE  LYS D  84    13568   5742   5959    563   -525   2450       C  
ATOM   3463  NZ  LYS D  84       9.966  26.406 -16.153  1.00 68.37           N  
ANISOU 3463  NZ  LYS D  84    14007   5975   5997    363   -303   2619       N  
ATOM   3464  N   MET D  85       7.347  19.440 -17.629  1.00 63.02           N  
ANISOU 3464  N   MET D  85    12838   5982   5124    846  -1053   1738       N  
ATOM   3465  CA  MET D  85       7.202  18.407 -18.651  1.00 64.22           C  
ANISOU 3465  CA  MET D  85    13129   6217   5053    934  -1229   1627       C  
ATOM   3466  C   MET D  85       6.131  17.373 -18.295  1.00 63.84           C  
ANISOU 3466  C   MET D  85    12917   6134   5206    941  -1503   1478       C  
ATOM   3467  O   MET D  85       5.385  16.937 -19.174  1.00 65.65           O  
ANISOU 3467  O   MET D  85    13252   6366   5328   1033  -1784   1426       O  
ATOM   3468  CB  MET D  85       8.548  17.769 -18.989  1.00 64.08           C  
ANISOU 3468  CB  MET D  85    13196   6340   4813    921  -1013   1540       C  
ATOM   3469  CG  MET D  85       9.441  18.727 -19.742  1.00 65.42           C  
ANISOU 3469  CG  MET D  85    13559   6591   4707    897   -774   1698       C  
ATOM   3470  SD  MET D  85      11.092  18.139 -20.069  1.00 68.52           S  
ANISOU 3470  SD  MET D  85    13956   7218   4863    877   -452   1578       S  
ATOM   3471  CE  MET D  85      11.836  18.192 -18.433  1.00 63.03           C  
ANISOU 3471  CE  MET D  85    12932   6479   4537    738   -252   1525       C  
ATOM   3472  N   SER D  86       6.029  16.996 -17.021  1.00 61.64           N  
ANISOU 3472  N   SER D  86    12394   5818   5207    825  -1435   1416       N  
ATOM   3473  CA  SER D  86       4.974  16.066 -16.635  1.00 62.15           C  
ANISOU 3473  CA  SER D  86    12296   5850   5467    768  -1669   1306       C  
ATOM   3474  C   SER D  86       3.620  16.638 -16.996  1.00 64.22           C  
ANISOU 3474  C   SER D  86    12470   6097   5835    837  -1908   1349       C  
ATOM   3475  O   SER D  86       2.760  15.949 -17.539  1.00 66.19           O  
ANISOU 3475  O   SER D  86    12701   6350   6099    853  -2199   1263       O  
ATOM   3476  CB  SER D  86       5.005  15.767 -15.145  1.00 59.95           C  
ANISOU 3476  CB  SER D  86    11792   5538   5448    610  -1527   1276       C  
ATOM   3477  OG  SER D  86       6.270  15.284 -14.772  1.00 58.86           O  
ANISOU 3477  OG  SER D  86    11731   5402   5229    576  -1346   1224       O  
ATOM   3478  N   VAL D  87       3.427  17.902 -16.669  1.00 64.34           N  
ANISOU 3478  N   VAL D  87    12423   6085   5940    887  -1811   1465       N  
ATOM   3479  CA  VAL D  87       2.210  18.588 -17.042  1.00 66.92           C  
ANISOU 3479  CA  VAL D  87    12671   6392   6364   1012  -2054   1492       C  
ATOM   3480  C   VAL D  87       1.908  18.464 -18.543  1.00 69.87           C  
ANISOU 3480  C   VAL D  87    13303   6763   6482   1157  -2346   1497       C  
ATOM   3481  O   VAL D  87       0.741  18.378 -18.943  1.00 72.15           O  
ANISOU 3481  O   VAL D  87    13486   7057   6870   1241  -2666   1436       O  
ATOM   3482  CB  VAL D  87       2.294  20.075 -16.686  1.00 66.85           C  
ANISOU 3482  CB  VAL D  87    12678   6308   6414   1097  -1927   1621       C  
ATOM   3483  CG1 VAL D  87       1.384  20.875 -17.600  1.00 70.10           C  
ANISOU 3483  CG1 VAL D  87    13192   6662   6780   1305  -2229   1673       C  
ATOM   3484  CG2 VAL D  87       1.948  20.287 -15.232  1.00 65.00           C  
ANISOU 3484  CG2 VAL D  87    12125   6087   6486   1019  -1771   1570       C  
ATOM   3485  N   LEU D  88       2.953  18.459 -19.369  1.00 70.29           N  
ANISOU 3485  N   LEU D  88    13682   6826   6199   1189  -2236   1557       N  
ATOM   3486  CA  LEU D  88       2.763  18.335 -20.817  1.00 73.29           C  
ANISOU 3486  CA  LEU D  88    14367   7215   6264   1332  -2488   1563       C  
ATOM   3487  C   LEU D  88       2.446  16.926 -21.279  1.00 74.15           C  
ANISOU 3487  C   LEU D  88    14484   7368   6322   1324  -2725   1377       C  
ATOM   3488  O   LEU D  88       2.064  16.737 -22.419  1.00 76.75           O  
ANISOU 3488  O   LEU D  88    15040   7699   6424   1454  -3005   1345       O  
ATOM   3489  CB  LEU D  88       3.986  18.833 -21.581  1.00 74.02           C  
ANISOU 3489  CB  LEU D  88    14813   7339   5972   1354  -2253   1693       C  
ATOM   3490  CG  LEU D  88       4.172  20.344 -21.667  1.00 74.85           C  
ANISOU 3490  CG  LEU D  88    15075   7351   6015   1380  -2143   1918       C  
ATOM   3491  CD1 LEU D  88       5.253  20.662 -22.663  1.00 76.45           C  
ANISOU 3491  CD1 LEU D  88    15653   7614   5781   1364  -1947   2049       C  
ATOM   3492  CD2 LEU D  88       2.876  21.011 -22.051  1.00 77.02           C  
ANISOU 3492  CD2 LEU D  88    15379   7510   6373   1550  -2518   1961       C  
ATOM   3493  N   ASN D  89       2.620  15.933 -20.409  1.00 72.44           N  
ANISOU 3493  N   ASN D  89    14063   7164   6299   1172  -2639   1254       N  
ATOM   3494  CA  ASN D  89       2.355  14.551 -20.799  1.00 73.74           C  
ANISOU 3494  CA  ASN D  89    14270   7319   6427   1145  -2891   1075       C  
ATOM   3495  C   ASN D  89       0.884  14.343 -21.097  1.00 76.49           C  
ANISOU 3495  C   ASN D  89    14468   7638   6956   1154  -3300   1009       C  
ATOM   3496  O   ASN D  89       0.027  14.736 -20.310  1.00 76.42           O  
ANISOU 3496  O   ASN D  89    14128   7635   7271   1075  -3319   1035       O  
ATOM   3497  CB  ASN D  89       2.802  13.576 -19.722  1.00 71.41           C  
ANISOU 3497  CB  ASN D  89    13820   6996   6316    965  -2744    981       C  
ATOM   3498  CG  ASN D  89       3.054  12.174 -20.273  1.00 72.65           C  
ANISOU 3498  CG  ASN D  89    14168   7109   6326    977  -2949    797       C  
ATOM   3499  OD1 ASN D  89       3.740  12.016 -21.278  1.00 74.52           O  
ANISOU 3499  OD1 ASN D  89    14698   7393   6223   1141  -2957    740       O  
ATOM   3500  ND2 ASN D  89       2.512  11.150 -19.604  1.00 71.98           N  
ANISOU 3500  ND2 ASN D  89    13936   6930   6484    797  -3110    702       N  
ATOM   3501  N   GLN D  90       0.587  13.729 -22.235  1.00 79.64           N  
ANISOU 3501  N   GLN D  90    15095   8022   7145   1258  -3631    904       N  
ATOM   3502  CA  GLN D  90      -0.797  13.556 -22.645  1.00 82.96           C  
ANISOU 3502  CA  GLN D  90    15373   8420   7730   1278  -4070    826       C  
ATOM   3503  C   GLN D  90      -1.694  13.059 -21.510  1.00 82.04           C  
ANISOU 3503  C   GLN D  90    14800   8304   8068   1037  -4115    765       C  
ATOM   3504  O   GLN D  90      -2.752  13.646 -21.252  1.00 83.23           O  
ANISOU 3504  O   GLN D  90    14640   8504   8479   1042  -4245    780       O  
ATOM   3505  CB  GLN D  90      -0.891  12.609 -23.831  1.00 86.21           C  
ANISOU 3505  CB  GLN D  90    16088   8790   7878   1370  -4432    671       C  
ATOM   3506  CG  GLN D  90      -2.273  12.566 -24.475  1.00 92.15           C  
ANISOU 3506  CG  GLN D  90    16740   9521   8752   1430  -4941    589       C  
ATOM   3507  CD  GLN D  90      -2.501  11.262 -25.231  1.00 98.10           C  
ANISOU 3507  CD  GLN D  90    17686  10198   9390   1413  -5330    382       C  
ATOM   3508  OE1 GLN D  90      -3.229  11.222 -26.230  1.00102.43           O  
ANISOU 3508  OE1 GLN D  90    18368  10724   9828   1552  -5767    299       O  
ATOM   3509  NE2 GLN D  90      -1.864  10.184 -24.762  1.00 97.22           N  
ANISOU 3509  NE2 GLN D  90    17619  10022   9297   1259  -5206    285       N  
ATOM   3510  N   GLU D  91      -1.276  11.980 -20.845  1.00 80.03           N  
ANISOU 3510  N   GLU D  91    14511   7999   7897    830  -4010    691       N  
ATOM   3511  CA  GLU D  91      -2.059  11.393 -19.763  1.00 79.40           C  
ANISOU 3511  CA  GLU D  91    14052   7917   8201    543  -4025    656       C  
ATOM   3512  C   GLU D  91      -2.404  12.423 -18.686  1.00 77.84           C  
ANISOU 3512  C   GLU D  91    13496   7823   8255    496  -3739    769       C  
ATOM   3513  O   GLU D  91      -3.489  12.375 -18.105  1.00 79.35           O  
ANISOU 3513  O   GLU D  91    13298   8091   8761    341  -3817    738       O  
ATOM   3514  CB  GLU D  91      -1.317  10.219 -19.132  1.00 77.99           C  
ANISOU 3514  CB  GLU D  91    13988   7629   8016    347  -3909    603       C  
ATOM   3515  CG  GLU D  91      -1.247   8.959 -19.984  1.00 80.20           C  
ANISOU 3515  CG  GLU D  91    14558   7772   8141    346  -4262    440       C  
ATOM   3516  CD  GLU D  91      -0.113   8.987 -20.989  1.00 81.14           C  
ANISOU 3516  CD  GLU D  91    15106   7885   7839    634  -4224    388       C  
ATOM   3517  OE1 GLU D  91       0.549   7.943 -21.182  1.00 81.23           O  
ANISOU 3517  OE1 GLU D  91    15375   7784   7705    646  -4303    255       O  
ATOM   3518  OE2 GLU D  91       0.116  10.058 -21.589  1.00 82.51           O  
ANISOU 3518  OE2 GLU D  91    15366   8168   7817    849  -4113    476       O  
ATOM   3519  N   SER D  92      -1.486  13.353 -18.422  1.00 74.94           N  
ANISOU 3519  N   SER D  92    13252   7471   7752    625  -3407    887       N  
ATOM   3520  CA  SER D  92      -1.743  14.420 -17.470  1.00 73.27           C  
ANISOU 3520  CA  SER D  92    12763   7333   7744    629  -3158    976       C  
ATOM   3521  C   SER D  92      -2.832  15.350 -18.003  1.00 75.90           C  
ANISOU 3521  C   SER D  92    12933   7726   8180    821  -3402    972       C  
ATOM   3522  O   SER D  92      -3.859  15.570 -17.363  1.00 77.38           O  
ANISOU 3522  O   SER D  92    12715   8014   8671    763  -3436    924       O  
ATOM   3523  CB  SER D  92      -0.464  15.213 -17.188  1.00 70.50           C  
ANISOU 3523  CB  SER D  92    12625   6949   7213    721  -2802   1096       C  
ATOM   3524  OG  SER D  92       0.637  14.370 -16.903  1.00 68.05           O  
ANISOU 3524  OG  SER D  92    12493   6588   6774    611  -2630   1073       O  
ATOM   3525  N   ILE D  93      -2.608  15.904 -19.182  1.00 76.83           N  
ANISOU 3525  N   ILE D  93    13369   7791   8032   1061  -3575   1017       N  
ATOM   3526  CA  ILE D  93      -3.633  16.722 -19.809  1.00 79.77           C  
ANISOU 3526  CA  ILE D  93    13652   8183   8473   1280  -3890   1005       C  
ATOM   3527  C   ILE D  93      -4.996  16.048 -19.665  1.00 82.19           C  
ANISOU 3527  C   ILE D  93    13539   8588   9103   1169  -4195    845       C  
ATOM   3528  O   ILE D  93      -5.976  16.669 -19.253  1.00 83.86           O  
ANISOU 3528  O   ILE D  93    13370   8897   9594   1241  -4271    796       O  
ATOM   3529  CB  ILE D  93      -3.376  16.918 -21.322  1.00 81.81           C  
ANISOU 3529  CB  ILE D  93    14371   8360   8353   1503  -4165   1043       C  
ATOM   3530  CG1 ILE D  93      -1.888  17.149 -21.611  1.00 79.38           C  
ANISOU 3530  CG1 ILE D  93    14492   7995   7674   1522  -3845   1178       C  
ATOM   3531  CG2 ILE D  93      -4.216  18.050 -21.833  1.00 84.28           C  
ANISOU 3531  CG2 ILE D  93    14668   8648   8706   1770  -4445   1077       C  
ATOM   3532  CD1 ILE D  93      -1.535  18.572 -21.904  1.00 78.92           C  
ANISOU 3532  CD1 ILE D  93    14665   7867   7453   1701  -3747   1359       C  
ATOM   3533  N   ALA D  94      -5.046  14.770 -20.021  1.00 82.63           N  
ANISOU 3533  N   ALA D  94    13656   8617   9122    995  -4378    748       N  
ATOM   3534  CA  ALA D  94      -6.291  14.024 -20.008  1.00 85.45           C  
ANISOU 3534  CA  ALA D  94    13643   9050   9774    835  -4702    599       C  
ATOM   3535  C   ALA D  94      -6.978  14.062 -18.648  1.00 85.39           C  
ANISOU 3535  C   ALA D  94    13089   9197  10159    609  -4468    577       C  
ATOM   3536  O   ALA D  94      -8.171  14.290 -18.564  1.00 88.59           O  
ANISOU 3536  O   ALA D  94    13062   9747  10852    618  -4663    479       O  
ATOM   3537  CB  ALA D  94      -6.054  12.603 -20.440  1.00 85.70           C  
ANISOU 3537  CB  ALA D  94    13884   8979   9699    639  -4891    513       C  
ATOM   3538  N   SER D  95      -6.232  13.851 -17.578  1.00 82.26           N  
ANISOU 3538  N   SER D  95    12700   8790   9766    416  -4049    658       N  
ATOM   3539  CA  SER D  95      -6.846  13.789 -16.269  1.00 82.70           C  
ANISOU 3539  CA  SER D  95    12284   9002  10137    174  -3801    642       C  
ATOM   3540  C   SER D  95      -7.561  15.080 -15.893  1.00 84.22           C  
ANISOU 3540  C   SER D  95    12122   9360  10519    399  -3727    616       C  
ATOM   3541  O   SER D  95      -8.473  15.073 -15.074  1.00 86.19           O  
ANISOU 3541  O   SER D  95    11874   9811  11064    253  -3631    540       O  
ATOM   3542  CB  SER D  95      -5.794  13.477 -15.209  1.00 79.04           C  
ANISOU 3542  CB  SER D  95    11979   8472   9582    -15  -3376    744       C  
ATOM   3543  OG  SER D  95      -5.068  14.638 -14.864  1.00 76.34           O  
ANISOU 3543  OG  SER D  95    11761   8118   9127    212  -3092    834       O  
ATOM   3544  N   GLY D  96      -7.131  16.193 -16.472  1.00 83.91           N  
ANISOU 3544  N   GLY D  96    12347   9233  10301    754  -3764    676       N  
ATOM   3545  CA  GLY D  96      -7.677  17.492 -16.103  1.00 85.55           C  
ANISOU 3545  CA  GLY D  96    12302   9537  10665   1017  -3711    649       C  
ATOM   3546  C   GLY D  96      -7.345  17.922 -14.678  1.00 83.77           C  
ANISOU 3546  C   GLY D  96    11902   9388  10538    926  -3242    685       C  
ATOM   3547  O   GLY D  96      -7.921  18.887 -14.163  1.00 85.25           O  
ANISOU 3547  O   GLY D  96    11805   9686  10899   1120  -3174    618       O  
ATOM   3548  N   ASN D  97      -6.411  17.226 -14.039  1.00 80.71           N  
ANISOU 3548  N   ASN D  97    11702   8934  10029    661  -2942    774       N  
ATOM   3549  CA  ASN D  97      -6.080  17.530 -12.664  1.00 79.07           C  
ANISOU 3549  CA  ASN D  97    11363   8793   9888    557  -2522    803       C  
ATOM   3550  C   ASN D  97      -4.731  18.182 -12.487  1.00 75.67           C  
ANISOU 3550  C   ASN D  97    11345   8183   9225    671  -2289    932       C  
ATOM   3551  O   ASN D  97      -4.304  18.443 -11.354  1.00 73.99           O  
ANISOU 3551  O   ASN D  97    11089   7991   9033    595  -1958    957       O  
ATOM   3552  CB  ASN D  97      -6.107  16.261 -11.837  1.00 78.82           C  
ANISOU 3552  CB  ASN D  97    11198   8828   9921    142  -2351    804       C  
ATOM   3553  CG  ASN D  97      -7.473  15.678 -11.749  1.00 83.96           C  
ANISOU 3553  CG  ASN D  97    11364   9693  10843    -50  -2501    686       C  
ATOM   3554  OD1 ASN D  97      -7.661  14.602 -11.192  1.00 86.69           O  
ANISOU 3554  OD1 ASN D  97    11598  10084  11255   -429  -2415    698       O  
ATOM   3555  ND2 ASN D  97      -8.452  16.382 -12.305  1.00 87.94           N  
ANISOU 3555  ND2 ASN D  97    11575  10326  11514    202  -2746    569       N  
ATOM   3556  N   PHE D  98      -4.040  18.423 -13.589  1.00 74.81           N  
ANISOU 3556  N   PHE D  98    11636   7906   8883    833  -2453   1011       N  
ATOM   3557  CA  PHE D  98      -2.689  18.922 -13.475  1.00 71.92           C  
ANISOU 3557  CA  PHE D  98    11638   7390   8299    880  -2221   1137       C  
ATOM   3558  C   PHE D  98      -2.505  20.100 -14.379  1.00 73.17           C  
ANISOU 3558  C   PHE D  98    12055   7427   8319   1171  -2367   1214       C  
ATOM   3559  O   PHE D  98      -1.633  20.135 -15.241  1.00 72.63           O  
ANISOU 3559  O   PHE D  98    12369   7242   7984   1211  -2398   1316       O  
ATOM   3560  CB  PHE D  98      -1.677  17.812 -13.734  1.00 69.76           C  
ANISOU 3560  CB  PHE D  98    11642   7039   7824    692  -2165   1177       C  
ATOM   3561  CG  PHE D  98      -1.881  16.619 -12.849  1.00 69.18           C  
ANISOU 3561  CG  PHE D  98    11379   7031   7877    394  -2070   1118       C  
ATOM   3562  CD1 PHE D  98      -2.746  15.606 -13.233  1.00 70.28           C  
ANISOU 3562  CD1 PHE D  98    11367   7222   8113    246  -2323   1036       C  
ATOM   3563  CD2 PHE D  98      -1.249  16.530 -11.607  1.00 66.37           C  
ANISOU 3563  CD2 PHE D  98    11008   6668   7542    246  -1750   1150       C  
ATOM   3564  CE1 PHE D  98      -2.956  14.517 -12.413  1.00 70.26           C  
ANISOU 3564  CE1 PHE D  98    11227   7249   8221    -71  -2245   1010       C  
ATOM   3565  CE2 PHE D  98      -1.452  15.442 -10.786  1.00 65.81           C  
ANISOU 3565  CE2 PHE D  98    10818   6631   7555    -43  -1677   1123       C  
ATOM   3566  CZ  PHE D  98      -2.304  14.435 -11.188  1.00 68.41           C  
ANISOU 3566  CZ  PHE D  98    11018   6997   7976   -215  -1916   1064       C  
ATOM   3567  N   ASP D  99      -3.371  21.070 -14.148  1.00 75.56           N  
ANISOU 3567  N   ASP D  99    12141   7766   8803   1377  -2456   1159       N  
ATOM   3568  CA  ASP D  99      -3.334  22.331 -14.820  1.00 77.51           C  
ANISOU 3568  CA  ASP D  99    12632   7862   8957   1668  -2617   1235       C  
ATOM   3569  C   ASP D  99      -2.260  23.167 -14.121  1.00 75.22           C  
ANISOU 3569  C   ASP D  99    12555   7435   8590   1656  -2304   1345       C  
ATOM   3570  O   ASP D  99      -2.383  23.512 -12.933  1.00 74.43           O  
ANISOU 3570  O   ASP D  99    12226   7386   8667   1641  -2090   1275       O  
ATOM   3571  CB  ASP D  99      -4.717  22.965 -14.707  1.00 81.37           C  
ANISOU 3571  CB  ASP D  99    12763   8443   9710   1913  -2854   1089       C  
ATOM   3572  CG  ASP D  99      -4.778  24.341 -15.293  1.00 84.72           C  
ANISOU 3572  CG  ASP D  99    13455   8669  10066   2250  -3067   1155       C  
ATOM   3573  OD1 ASP D  99      -5.886  24.920 -15.298  1.00 89.45           O  
ANISOU 3573  OD1 ASP D  99    13790   9322  10874   2516  -3316   1017       O  
ATOM   3574  OD2 ASP D  99      -3.726  24.847 -15.744  1.00 84.94           O  
ANISOU 3574  OD2 ASP D  99    13953   8488   9835   2247  -2995   1342       O  
ATOM   3575  N   TYR D 100      -1.190  23.466 -14.855  1.00 74.29           N  
ANISOU 3575  N   TYR D 100    12873   7156   8198   1646  -2270   1510       N  
ATOM   3576  CA  TYR D 100      -0.051  24.177 -14.285  1.00 72.24           C  
ANISOU 3576  CA  TYR D 100    12821   6764   7863   1580  -1985   1622       C  
ATOM   3577  C   TYR D 100      -0.424  25.514 -13.642  1.00 73.33           C  
ANISOU 3577  C   TYR D 100    12916   6783   8165   1777  -1995   1605       C  
ATOM   3578  O   TYR D 100       0.237  25.969 -12.719  1.00 71.74           O  
ANISOU 3578  O   TYR D 100    12735   6515   8009   1705  -1750   1620       O  
ATOM   3579  CB  TYR D 100       1.023  24.396 -15.343  1.00 72.15           C  
ANISOU 3579  CB  TYR D 100    13258   6627   7530   1538  -1971   1805       C  
ATOM   3580  CG  TYR D 100       2.300  24.978 -14.783  1.00 70.98           C  
ANISOU 3580  CG  TYR D 100    13282   6370   7317   1404  -1665   1916       C  
ATOM   3581  CD1 TYR D 100       3.237  24.160 -14.156  1.00 68.79           C  
ANISOU 3581  CD1 TYR D 100    12927   6187   7022   1185  -1390   1881       C  
ATOM   3582  CD2 TYR D 100       2.571  26.341 -14.875  1.00 72.83           C  
ANISOU 3582  CD2 TYR D 100    13763   6390   7518   1494  -1685   2047       C  
ATOM   3583  CE1 TYR D 100       4.405  24.677 -13.636  1.00 67.60           C  
ANISOU 3583  CE1 TYR D 100    12894   5954   6838   1061  -1139   1960       C  
ATOM   3584  CE2 TYR D 100       3.736  26.872 -14.365  1.00 71.77           C  
ANISOU 3584  CE2 TYR D 100    13768   6153   7349   1337  -1426   2143       C  
ATOM   3585  CZ  TYR D 100       4.647  26.034 -13.749  1.00 70.09           C  
ANISOU 3585  CZ  TYR D 100    13428   6070   7133   1122  -1152   2091       C  
ATOM   3586  OH  TYR D 100       5.807  26.552 -13.238  1.00 71.31           O  
ANISOU 3586  OH  TYR D 100    13683   6136   7275    966   -922   2165       O  
ATOM   3587  N   ALA D 101      -1.481  26.139 -14.138  1.00 76.25           N  
ANISOU 3587  N   ALA D 101    13236   7114   8623   2049  -2310   1554       N  
ATOM   3588  CA  ALA D 101      -1.937  27.402 -13.589  1.00 78.02           C  
ANISOU 3588  CA  ALA D 101    13426   7210   9010   2299  -2379   1499       C  
ATOM   3589  C   ALA D 101      -2.522  27.221 -12.192  1.00 77.66           C  
ANISOU 3589  C   ALA D 101    12915   7359   9232   2296  -2181   1290       C  
ATOM   3590  O   ALA D 101      -2.766  28.199 -11.479  1.00 78.99           O  
ANISOU 3590  O   ALA D 101    13032   7447   9535   2492  -2160   1206       O  
ATOM   3591  CB  ALA D 101      -2.956  28.026 -14.506  1.00 81.90           C  
ANISOU 3591  CB  ALA D 101    13969   7617   9531   2627  -2812   1470       C  
ATOM   3592  N   VAL D 102      -2.737  25.968 -11.795  1.00 76.23           N  
ANISOU 3592  N   VAL D 102    12425   7428   9111   2069  -2035   1207       N  
ATOM   3593  CA  VAL D 102      -3.316  25.687 -10.489  1.00 75.97           C  
ANISOU 3593  CA  VAL D 102    11962   7614   9288   2015  -1815   1031       C  
ATOM   3594  C   VAL D 102      -2.295  25.094  -9.566  1.00 72.66           C  
ANISOU 3594  C   VAL D 102    11612   7211   8784   1718  -1459   1085       C  
ATOM   3595  O   VAL D 102      -2.057  25.601  -8.471  1.00 72.22           O  
ANISOU 3595  O   VAL D 102    11514   7144   8782   1735  -1242   1029       O  
ATOM   3596  CB  VAL D 102      -4.428  24.666 -10.579  1.00 77.47           C  
ANISOU 3596  CB  VAL D 102    11724   8083   9628   1929  -1911    898       C  
ATOM   3597  CG1 VAL D 102      -4.938  24.362  -9.186  1.00 77.28           C  
ANISOU 3597  CG1 VAL D 102    11282   8306   9776   1815  -1620    745       C  
ATOM   3598  CG2 VAL D 102      -5.529  25.174 -11.480  1.00 80.82           C  
ANISOU 3598  CG2 VAL D 102    12019   8523  10166   2239  -2310    808       C  
ATOM   3599  N   ILE D 103      -1.714  23.991 -10.018  1.00 70.80           N  
ANISOU 3599  N   ILE D 103    11492   6998   8411   1468  -1428   1176       N  
ATOM   3600  CA  ILE D 103      -0.696  23.275  -9.272  1.00 67.78           C  
ANISOU 3600  CA  ILE D 103    11200   6617   7937   1199  -1150   1223       C  
ATOM   3601  C   ILE D 103       0.387  24.209  -8.785  1.00 66.24           C  
ANISOU 3601  C   ILE D 103    11265   6236   7668   1233   -986   1296       C  
ATOM   3602  O   ILE D 103       0.804  24.163  -7.627  1.00 64.97           O  
ANISOU 3602  O   ILE D 103    11056   6095   7535   1131   -755   1254       O  
ATOM   3603  CB  ILE D 103       0.012  22.306 -10.183  1.00 66.47           C  
ANISOU 3603  CB  ILE D 103    11253   6413   7589   1038  -1217   1320       C  
ATOM   3604  CG1 ILE D 103      -0.862  21.110 -10.489  1.00 67.43           C  
ANISOU 3604  CG1 ILE D 103    11150   6693   7778    917  -1362   1244       C  
ATOM   3605  CG2 ILE D 103       1.289  21.836  -9.549  1.00 64.28           C  
ANISOU 3605  CG2 ILE D 103    11139   6082   7202    840   -973   1371       C  
ATOM   3606  CD1 ILE D 103      -0.144  20.165 -11.386  1.00 67.55           C  
ANISOU 3606  CD1 ILE D 103    11417   6651   7599    800  -1450   1307       C  
ATOM   3607  N   LYS D 104       0.861  25.044  -9.696  1.00 66.69           N  
ANISOU 3607  N   LYS D 104    11623   6101   7617   1356  -1119   1415       N  
ATOM   3608  CA  LYS D 104       2.026  25.856  -9.440  1.00 65.52           C  
ANISOU 3608  CA  LYS D 104    11753   5755   7384   1322   -985   1516       C  
ATOM   3609  C   LYS D 104       1.822  26.810  -8.262  1.00 65.79           C  
ANISOU 3609  C   LYS D 104    11707   5723   7567   1445   -893   1416       C  
ATOM   3610  O   LYS D 104       2.608  26.819  -7.324  1.00 64.04           O  
ANISOU 3610  O   LYS D 104    11522   5470   7341   1318   -687   1401       O  
ATOM   3611  CB  LYS D 104       2.373  26.623 -10.697  1.00 67.34           C  
ANISOU 3611  CB  LYS D 104    12321   5798   7466   1412  -1161   1679       C  
ATOM   3612  CG  LYS D 104       3.834  26.844 -10.833  1.00 67.58           C  
ANISOU 3612  CG  LYS D 104    12631   5705   7342   1228   -992   1823       C  
ATOM   3613  CD  LYS D 104       4.453  27.090  -9.472  1.00 68.91           C  
ANISOU 3613  CD  LYS D 104    12725   5838   7621   1134   -772   1754       C  
ATOM   3614  CE  LYS D 104       5.947  26.892  -9.528  1.00 68.04           C  
ANISOU 3614  CE  LYS D 104    12775   5692   7384    904   -588   1852       C  
ATOM   3615  NZ  LYS D 104       6.621  28.026  -8.895  1.00 70.16           N  
ANISOU 3615  NZ  LYS D 104    13186   5756   7717    874   -519   1890       N  
ATOM   3616  N   PRO D 105       0.774  27.641  -8.315  1.00 68.33           N  
ANISOU 3616  N   PRO D 105    11930   6017   8017   1722  -1071   1327       N  
ATOM   3617  CA  PRO D 105       0.577  28.490  -7.151  1.00 68.93           C  
ANISOU 3617  CA  PRO D 105    11928   6044   8218   1867   -977   1191       C  
ATOM   3618  C   PRO D 105       0.317  27.647  -5.914  1.00 67.53           C  
ANISOU 3618  C   PRO D 105    11436   6123   8100   1731   -721   1047       C  
ATOM   3619  O   PRO D 105       0.738  28.017  -4.830  1.00 66.98           O  
ANISOU 3619  O   PRO D 105    11401   6011   8037   1717   -549    979       O  
ATOM   3620  CB  PRO D 105      -0.646  29.344  -7.523  1.00 72.29           C  
ANISOU 3620  CB  PRO D 105    12247   6441   8778   2229  -1245   1081       C  
ATOM   3621  CG  PRO D 105      -1.216  28.733  -8.753  1.00 73.28           C  
ANISOU 3621  CG  PRO D 105    12317   6657   8867   2240  -1467   1142       C  
ATOM   3622  CD  PRO D 105      -0.121  27.998  -9.430  1.00 70.96           C  
ANISOU 3622  CD  PRO D 105    12279   6316   8367   1948  -1388   1340       C  
ATOM   3623  N   ALA D 106      -0.359  26.514  -6.078  1.00 67.34           N  
ANISOU 3623  N   ALA D 106    11137   6346   8101   1612   -709   1009       N  
ATOM   3624  CA  ALA D 106      -0.600  25.605  -4.953  1.00 66.84           C  
ANISOU 3624  CA  ALA D 106    10817   6517   8061   1420   -462    913       C  
ATOM   3625  C   ALA D 106       0.712  25.218  -4.282  1.00 64.12           C  
ANISOU 3625  C   ALA D 106    10709   6073   7582   1189   -265    995       C  
ATOM   3626  O   ALA D 106       0.838  25.241  -3.057  1.00 63.96           O  
ANISOU 3626  O   ALA D 106    10642   6108   7551   1141    -64    913       O  
ATOM   3627  CB  ALA D 106      -1.329  24.361  -5.419  1.00 66.80           C  
ANISOU 3627  CB  ALA D 106    10564   6728   8088   1251   -517    911       C  
ATOM   3628  N   ILE D 107       1.688  24.857  -5.099  1.00 62.33           N  
ANISOU 3628  N   ILE D 107    10730   5712   7239   1061   -330   1144       N  
ATOM   3629  CA  ILE D 107       3.005  24.535  -4.604  1.00 60.28           C  
ANISOU 3629  CA  ILE D 107    10675   5356   6871    877   -188   1206       C  
ATOM   3630  C   ILE D 107       3.673  25.720  -3.887  1.00 60.80           C  
ANISOU 3630  C   ILE D 107    10907   5242   6952    969   -120   1183       C  
ATOM   3631  O   ILE D 107       4.259  25.566  -2.819  1.00 60.09           O  
ANISOU 3631  O   ILE D 107    10855   5145   6831    871     28   1135       O  
ATOM   3632  CB  ILE D 107       3.876  24.060  -5.754  1.00 58.90           C  
ANISOU 3632  CB  ILE D 107    10698   5104   6577    774   -275   1340       C  
ATOM   3633  CG1 ILE D 107       3.302  22.756  -6.301  1.00 58.91           C  
ANISOU 3633  CG1 ILE D 107    10568   5259   6554    668   -354   1334       C  
ATOM   3634  CG2 ILE D 107       5.307  23.889  -5.302  1.00 56.16           C  
ANISOU 3634  CG2 ILE D 107    10528   4665   6145    626   -146   1379       C  
ATOM   3635  CD1 ILE D 107       4.114  22.128  -7.415  1.00 57.99           C  
ANISOU 3635  CD1 ILE D 107    10643   5100   6292    591   -436   1424       C  
ATOM   3636  N   ASP D 108       3.585  26.903  -4.474  1.00 62.55           N  
ANISOU 3636  N   ASP D 108    11259   5292   7216   1155   -261   1218       N  
ATOM   3637  CA  ASP D 108       4.113  28.096  -3.837  1.00 63.40           C  
ANISOU 3637  CA  ASP D 108    11543   5187   7357   1246   -245   1188       C  
ATOM   3638  C   ASP D 108       3.473  28.272  -2.472  1.00 64.24           C  
ANISOU 3638  C   ASP D 108    11478   5402   7528   1358   -122    992       C  
ATOM   3639  O   ASP D 108       4.149  28.529  -1.485  1.00 63.74           O  
ANISOU 3639  O   ASP D 108    11521   5259   7437   1307    -15    937       O  
ATOM   3640  CB  ASP D 108       3.834  29.327  -4.717  1.00 65.76           C  
ANISOU 3640  CB  ASP D 108    12021   5266   7700   1454   -465   1253       C  
ATOM   3641  CG  ASP D 108       4.627  29.303  -6.004  1.00 65.97           C  
ANISOU 3641  CG  ASP D 108    12285   5172   7609   1315   -547   1468       C  
ATOM   3642  OD1 ASP D 108       5.517  28.434  -6.119  1.00 65.54           O  
ANISOU 3642  OD1 ASP D 108    12241   5204   7458   1080   -418   1536       O  
ATOM   3643  OD2 ASP D 108       4.371  30.143  -6.894  1.00 68.87           O  
ANISOU 3643  OD2 ASP D 108    12840   5363   7963   1450   -743   1564       O  
ATOM   3644  N   LYS D 109       2.153  28.141  -2.439  1.00 66.08           N  
ANISOU 3644  N   LYS D 109    11434   5834   7840   1515   -142    876       N  
ATOM   3645  CA  LYS D 109       1.393  28.287  -1.216  1.00 67.58           C  
ANISOU 3645  CA  LYS D 109    11411   6195   8071   1635     10    672       C  
ATOM   3646  C   LYS D 109       1.907  27.280  -0.187  1.00 65.66           C  
ANISOU 3646  C   LYS D 109    11153   6086   7709   1368    247    670       C  
ATOM   3647  O   LYS D 109       2.111  27.629   0.965  1.00 66.06           O  
ANISOU 3647  O   LYS D 109    11260   6130   7709   1405    380    557       O  
ATOM   3648  CB  LYS D 109      -0.090  28.059  -1.504  1.00 70.16           C  
ANISOU 3648  CB  LYS D 109    11364   6785   8509   1785    -31    558       C  
ATOM   3649  CG  LYS D 109      -1.028  28.544  -0.418  1.00 73.31           C  
ANISOU 3649  CG  LYS D 109    11508   7378   8969   2004    108    312       C  
ATOM   3650  CD  LYS D 109      -2.329  27.745  -0.440  1.00 76.80           C  
ANISOU 3650  CD  LYS D 109    11484   8203   9493   1970    189    215       C  
ATOM   3651  CE  LYS D 109      -3.281  28.203   0.653  1.00 82.02           C  
ANISOU 3651  CE  LYS D 109    11838   9126  10199   2185    379    -52       C  
ATOM   3652  NZ  LYS D 109      -3.959  27.040   1.318  1.00 84.08           N  
ANISOU 3652  NZ  LYS D 109    11743   9786  10419   1907    664    -88       N  
ATOM   3653  N   PHE D 110       2.129  26.035  -0.603  1.00 63.83           N  
ANISOU 3653  N   PHE D 110    10883   5953   7418   1112    272    789       N  
ATOM   3654  CA  PHE D 110       2.599  25.020   0.328  1.00 62.36           C  
ANISOU 3654  CA  PHE D 110    10727   5856   7110    865    448    800       C  
ATOM   3655  C   PHE D 110       3.914  25.437   0.951  1.00 61.15           C  
ANISOU 3655  C   PHE D 110    10865   5490   6879    829    470    813       C  
ATOM   3656  O   PHE D 110       4.078  25.385   2.168  1.00 61.39           O  
ANISOU 3656  O   PHE D 110    10946   5556   6822    795    607    728       O  
ATOM   3657  CB  PHE D 110       2.794  23.683  -0.358  1.00 60.53           C  
ANISOU 3657  CB  PHE D 110    10485   5680   6833    625    401    927       C  
ATOM   3658  CG  PHE D 110       3.366  22.631   0.545  1.00 58.46           C  
ANISOU 3658  CG  PHE D 110    10325   5447   6440    384    524    952       C  
ATOM   3659  CD1 PHE D 110       4.719  22.344   0.531  1.00 56.32           C  
ANISOU 3659  CD1 PHE D 110    10308   5002   6090    292    474   1020       C  
ATOM   3660  CD2 PHE D 110       2.554  21.934   1.410  1.00 59.10           C  
ANISOU 3660  CD2 PHE D 110    10252   5734   6472    247    683    908       C  
ATOM   3661  CE1 PHE D 110       5.256  21.379   1.362  1.00 54.33           C  
ANISOU 3661  CE1 PHE D 110    10180   4747   5717    107    534   1034       C  
ATOM   3662  CE2 PHE D 110       3.080  20.955   2.257  1.00 58.33           C  
ANISOU 3662  CE2 PHE D 110    10315   5625   6224     18    768    955       C  
ATOM   3663  CZ  PHE D 110       4.436  20.678   2.228  1.00 56.29           C  
ANISOU 3663  CZ  PHE D 110    10338   5158   5893    -31    669   1013       C  
ATOM   3664  N   ALA D 111       4.853  25.839   0.104  1.00 60.17           N  
ANISOU 3664  N   ALA D 111    10929   5157   6778    823    333    919       N  
ATOM   3665  CA  ALA D 111       6.168  26.262   0.557  1.00 59.40           C  
ANISOU 3665  CA  ALA D 111    11067   4860   6644    762    328    933       C  
ATOM   3666  C   ALA D 111       6.068  27.386   1.572  1.00 61.38           C  
ANISOU 3666  C   ALA D 111    11395   5008   6918    930    353    791       C  
ATOM   3667  O   ALA D 111       6.714  27.350   2.609  1.00 60.80           O  
ANISOU 3667  O   ALA D 111    11440   4888   6774    870    414    723       O  
ATOM   3668  CB  ALA D 111       7.005  26.688  -0.608  1.00 58.65           C  
ANISOU 3668  CB  ALA D 111    11110   4593   6581    726    202   1067       C  
ATOM   3669  N   ARG D 112       5.253  28.386   1.273  1.00 64.16           N  
ANISOU 3669  N   ARG D 112    11702   5312   7365   1166    277    729       N  
ATOM   3670  CA  ARG D 112       5.145  29.540   2.161  1.00 67.09           C  
ANISOU 3670  CA  ARG D 112    12177   5552   7763   1374    264    567       C  
ATOM   3671  C   ARG D 112       4.629  29.152   3.542  1.00 67.93           C  
ANISOU 3671  C   ARG D 112    12178   5872   7762   1406    463    394       C  
ATOM   3672  O   ARG D 112       5.180  29.572   4.557  1.00 68.43           O  
ANISOU 3672  O   ARG D 112    12415   5830   7755   1431    491    289       O  
ATOM   3673  CB  ARG D 112       4.258  30.611   1.553  1.00 69.97           C  
ANISOU 3673  CB  ARG D 112    12511   5825   8251   1666    113    511       C  
ATOM   3674  CG  ARG D 112       5.005  31.566   0.682  1.00 73.20           C  
ANISOU 3674  CG  ARG D 112    13194   5891   8728   1669    -98    646       C  
ATOM   3675  CD  ARG D 112       4.168  32.828   0.469  1.00 82.14           C  
ANISOU 3675  CD  ARG D 112    14386   6855   9969   2017   -286    540       C  
ATOM   3676  NE  ARG D 112       3.525  32.838  -0.849  1.00 87.19           N  
ANISOU 3676  NE  ARG D 112    14967   7502  10659   2102   -443    658       N  
ATOM   3677  CZ  ARG D 112       2.367  32.244  -1.140  1.00 89.49           C  
ANISOU 3677  CZ  ARG D 112    14943   8077  10982   2222   -422    590       C  
ATOM   3678  NH1 ARG D 112       1.703  31.575  -0.207  1.00 90.32           N  
ANISOU 3678  NH1 ARG D 112    14746   8502  11071   2239   -212    420       N  
ATOM   3679  NH2 ARG D 112       1.874  32.314  -2.368  1.00 90.96           N  
ANISOU 3679  NH2 ARG D 112    15121   8232  11207   2306   -616    696       N  
ATOM   3680  N   GLU D 113       3.582  28.339   3.575  1.00 68.47           N  
ANISOU 3680  N   GLU D 113    11968   6245   7803   1383    599    367       N  
ATOM   3681  CA  GLU D 113       2.995  27.914   4.826  1.00 70.01           C  
ANISOU 3681  CA  GLU D 113    12048   6688   7866   1373    831    227       C  
ATOM   3682  C   GLU D 113       4.009  27.143   5.633  1.00 68.14           C  
ANISOU 3682  C   GLU D 113    12025   6407   7457   1125    905    291       C  
ATOM   3683  O   GLU D 113       4.110  27.295   6.841  1.00 69.34           O  
ANISOU 3683  O   GLU D 113    12291   6593   7463   1158   1022    167       O  
ATOM   3684  CB  GLU D 113       1.762  27.068   4.555  1.00 71.12           C  
ANISOU 3684  CB  GLU D 113    11831   7164   8028   1307    958    231       C  
ATOM   3685  CG  GLU D 113       0.759  27.788   3.676  1.00 74.79           C  
ANISOU 3685  CG  GLU D 113    12061   7675   8682   1575    831    156       C  
ATOM   3686  CD  GLU D 113      -0.566  27.059   3.552  1.00 79.59           C  
ANISOU 3686  CD  GLU D 113    12247   8654   9341   1528    957    107       C  
ATOM   3687  OE1 GLU D 113      -0.569  25.805   3.547  1.00 79.86           O  
ANISOU 3687  OE1 GLU D 113    12211   8829   9304   1205   1056    234       O  
ATOM   3688  OE2 GLU D 113      -1.604  27.754   3.454  1.00 82.78           O  
ANISOU 3688  OE2 GLU D 113    12387   9198   9868   1817    936    -69       O  
ATOM   3689  N   GLN D 114       4.777  26.319   4.948  1.00 65.90           N  
ANISOU 3689  N   GLN D 114    11814   6045   7182    901    817    468       N  
ATOM   3690  CA  GLN D 114       5.790  25.501   5.599  1.00 64.98           C  
ANISOU 3690  CA  GLN D 114    11898   5868   6922    690    831    525       C  
ATOM   3691  C   GLN D 114       6.891  26.345   6.218  1.00 64.97           C  
ANISOU 3691  C   GLN D 114    12155   5624   6906    760    732    450       C  
ATOM   3692  O   GLN D 114       7.271  26.159   7.365  1.00 65.39           O  
ANISOU 3692  O   GLN D 114    12370   5672   6804    722    783    375       O  
ATOM   3693  CB  GLN D 114       6.389  24.553   4.577  1.00 62.63           C  
ANISOU 3693  CB  GLN D 114    11603   5527   6667    502    722    694       C  
ATOM   3694  CG  GLN D 114       5.495  23.397   4.286  1.00 63.71           C  
ANISOU 3694  CG  GLN D 114    11559   5878   6770    356    801    764       C  
ATOM   3695  CD  GLN D 114       5.758  22.283   5.229  1.00 64.02           C  
ANISOU 3695  CD  GLN D 114    11731   5966   6629    150    878    794       C  
ATOM   3696  OE1 GLN D 114       5.054  22.132   6.216  1.00 67.60           O  
ANISOU 3696  OE1 GLN D 114    12152   6578   6956    110   1055    736       O  
ATOM   3697  NE2 GLN D 114       6.808  21.505   4.958  1.00 60.76           N  
ANISOU 3697  NE2 GLN D 114    11486   5416   6185     24    742    877       N  
ATOM   3698  N   VAL D 115       7.417  27.270   5.432  1.00 64.93           N  
ANISOU 3698  N   VAL D 115    12207   5407   7057    842    574    480       N  
ATOM   3699  CA  VAL D 115       8.430  28.176   5.923  1.00 65.46           C  
ANISOU 3699  CA  VAL D 115    12498   5222   7152    881    454    411       C  
ATOM   3700  C   VAL D 115       7.904  28.949   7.120  1.00 68.54           C  
ANISOU 3700  C   VAL D 115    12973   5611   7457   1085    513    203       C  
ATOM   3701  O   VAL D 115       8.618  29.175   8.096  1.00 69.08           O  
ANISOU 3701  O   VAL D 115    13245   5563   7437   1077    467    104       O  
ATOM   3702  CB  VAL D 115       8.854  29.153   4.826  1.00 65.18           C  
ANISOU 3702  CB  VAL D 115    12508   4961   7297    915    293    494       C  
ATOM   3703  CG1 VAL D 115       9.635  30.309   5.408  1.00 65.70           C  
ANISOU 3703  CG1 VAL D 115    12797   4747   7418    969    160    397       C  
ATOM   3704  CG2 VAL D 115       9.670  28.406   3.762  1.00 62.73           C  
ANISOU 3704  CG2 VAL D 115    12153   4655   7025    701    251    677       C  
ATOM   3705  N   SER D 116       6.645  29.349   7.056  1.00 71.11           N  
ANISOU 3705  N   SER D 116    13136   6078   7804   1288    604    113       N  
ATOM   3706  CA  SER D 116       6.101  30.189   8.113  1.00 74.90           C  
ANISOU 3706  CA  SER D 116    13682   6572   8204   1539    663   -123       C  
ATOM   3707  C   SER D 116       5.945  29.447   9.439  1.00 76.50           C  
ANISOU 3707  C   SER D 116    13929   6994   8145   1468    871   -215       C  
ATOM   3708  O   SER D 116       5.867  30.079  10.487  1.00 78.63           O  
ANISOU 3708  O   SER D 116    14346   7242   8288   1642    907   -416       O  
ATOM   3709  CB  SER D 116       4.774  30.814   7.692  1.00 77.07           C  
ANISOU 3709  CB  SER D 116    13731   6971   8581   1816    700   -231       C  
ATOM   3710  OG  SER D 116       3.733  29.870   7.816  1.00 77.83           O  
ANISOU 3710  OG  SER D 116    13530   7447   8593   1759    934   -233       O  
ATOM   3711  N   ILE D 117       5.891  28.113   9.395  1.00 76.25           N  
ANISOU 3711  N   ILE D 117    13805   7156   8011   1215    994    -68       N  
ATOM   3712  CA  ILE D 117       5.908  27.316  10.620  1.00 78.35           C  
ANISOU 3712  CA  ILE D 117    14195   7578   7996   1089   1160   -101       C  
ATOM   3713  C   ILE D 117       7.098  27.733  11.479  1.00 79.50           C  
ANISOU 3713  C   ILE D 117    14691   7473   8042   1108   1002   -184       C  
ATOM   3714  O   ILE D 117       6.974  27.888  12.680  1.00 81.78           O  
ANISOU 3714  O   ILE D 117    15149   7825   8098   1189   1098   -332       O  
ATOM   3715  CB  ILE D 117       6.067  25.799  10.356  1.00 76.60           C  
ANISOU 3715  CB  ILE D 117    13940   7463   7700    773   1205    109       C  
ATOM   3716  CG1 ILE D 117       4.926  25.230   9.494  1.00 77.16           C  
ANISOU 3716  CG1 ILE D 117    13668   7775   7874    701   1331    200       C  
ATOM   3717  CG2 ILE D 117       6.199  25.046  11.664  1.00 76.81           C  
ANISOU 3717  CG2 ILE D 117    14190   7584   7411    636   1331     97       C  
ATOM   3718  CD1 ILE D 117       3.563  25.243  10.148  1.00 81.64           C  
ANISOU 3718  CD1 ILE D 117    14015   8681   8324    761   1618     82       C  
ATOM   3719  N   PHE D 118       8.256  27.907  10.862  1.00 78.98           N  
ANISOU 3719  N   PHE D 118    14726   7139   8145   1029    758    -97       N  
ATOM   3720  CA  PHE D 118       9.463  28.205  11.609  1.00 81.08           C  
ANISOU 3720  CA  PHE D 118    15278   7173   8354   1010    572   -173       C  
ATOM   3721  C   PHE D 118       9.939  29.659  11.506  1.00 84.25           C  
ANISOU 3721  C   PHE D 118    15789   7289   8932   1174    374   -297       C  
ATOM   3722  O   PHE D 118      10.810  30.073  12.261  1.00 84.97           O  
ANISOU 3722  O   PHE D 118    16118   7188   8980   1184    209   -407       O  
ATOM   3723  CB  PHE D 118      10.576  27.261  11.177  1.00 78.15           C  
ANISOU 3723  CB  PHE D 118    14937   6721   8034    776    429    -14       C  
ATOM   3724  CG  PHE D 118      10.368  25.836  11.615  1.00 77.14           C  
ANISOU 3724  CG  PHE D 118    14847   6775   7688    615    540     80       C  
ATOM   3725  CD1 PHE D 118       9.655  24.946  10.826  1.00 75.53           C  
ANISOU 3725  CD1 PHE D 118    14433   6751   7515    495    668    232       C  
ATOM   3726  CD2 PHE D 118      10.883  25.386  12.819  1.00 77.49           C  
ANISOU 3726  CD2 PHE D 118    15170   6784   7488    576    486     20       C  
ATOM   3727  CE1 PHE D 118       9.463  23.634  11.232  1.00 75.35           C  
ANISOU 3727  CE1 PHE D 118    14484   6850   7294    316    744    331       C  
ATOM   3728  CE2 PHE D 118      10.690  24.076  13.234  1.00 77.44           C  
ANISOU 3728  CE2 PHE D 118    15261   6902   7261    411    563    130       C  
ATOM   3729  CZ  PHE D 118       9.984  23.201  12.441  1.00 76.67           C  
ANISOU 3729  CZ  PHE D 118    14959   6963   7210    269    693    290       C  
ATOM   3730  N   PHE D 119       9.378  30.428  10.569  1.00 45.43           N  
ATOM   3731  CA  PHE D 119       9.708  31.862  10.396  1.00 47.86           C  
ATOM   3732  C   PHE D 119       8.520  32.672   9.801  1.00 48.89           C  
ATOM   3733  O   PHE D 119       7.742  33.351  10.520  1.00 50.82           O  
ATOM   3734  CB  PHE D 119      10.902  32.064   9.458  1.00 48.44           C  
ATOM   3735  CG  PHE D 119      11.963  30.995   9.523  1.00 49.98           C  
ATOM   3736  CD1 PHE D 119      11.701  29.699   9.088  1.00 52.97           C  
ATOM   3737  CD2 PHE D 119      13.261  31.315   9.925  1.00 51.83           C  
ATOM   3738  CE1 PHE D 119      12.725  28.702   9.105  1.00 54.62           C  
ATOM   3739  CE2 PHE D 119      14.295  30.338   9.958  1.00 53.41           C  
ATOM   3740  CZ  PHE D 119      14.028  29.035   9.544  1.00 54.31           C  
TER    3741      PHE D 119                                                      
ATOM   3742  O5'  DA P   1      69.554  29.220  11.635  1.00100.20           O  
ANISOU 3742  O5'  DA P   1    19012  10763   8297   3245   3816   3480       O  
ATOM   3743  C5'  DA P   1      69.878  28.037  10.926  1.00102.21           C  
ANISOU 3743  C5'  DA P   1    19323  11134   8377   3306   4066   3219       C  
ATOM   3744  C4'  DA P   1      69.543  26.837  11.787  1.00100.36           C  
ANISOU 3744  C4'  DA P   1    19071  10715   8347   3204   3977   2849       C  
ATOM   3745  O4'  DA P   1      70.568  26.656  12.795  1.00100.04           O  
ANISOU 3745  O4'  DA P   1    18827  10369   8815   3165   4050   3024       O  
ATOM   3746  C3'  DA P   1      68.221  26.941  12.537  1.00 97.01           C  
ANISOU 3746  C3'  DA P   1    18686  10288   7885   3094   3591   2647       C  
ATOM   3747  O3'  DA P   1      67.379  25.939  12.027  1.00 96.67           O  
ANISOU 3747  O3'  DA P   1    18783  10425   7520   3062   3607   2194       O  
ATOM   3748  C2'  DA P   1      68.579  26.664  13.998  1.00 95.44           C  
ANISOU 3748  C2'  DA P   1    18331   9738   8193   2987   3484   2683       C  
ATOM   3749  C1'  DA P   1      70.054  27.039  14.047  1.00 96.91           C  
ANISOU 3749  C1'  DA P   1    18344   9810   8668   3035   3717   3045       C  
ATOM   3750  N9   DA P   1      70.297  28.468  14.156  1.00 97.21           N  
ANISOU 3750  N9   DA P   1    18305   9845   8786   2992   3623   3398       N  
ATOM   3751  C8   DA P   1      69.799  29.475  13.353  1.00 99.17           C  
ANISOU 3751  C8   DA P   1    18683  10261   8735   3054   3593   3552       C  
ATOM   3752  N7   DA P   1      70.195  30.690  13.682  1.00 98.20           N  
ANISOU 3752  N7   DA P   1    18482  10011   8819   2988   3579   3879       N  
ATOM   3753  C5   DA P   1      71.013  30.446  14.779  1.00 97.14           C  
ANISOU 3753  C5   DA P   1    18119   9671   9118   2843   3564   3902       C  
ATOM   3754  C6   DA P   1      71.745  31.317  15.599  1.00 96.21           C  
ANISOU 3754  C6   DA P   1    17803   9387   9367   2667   3550   4128       C  
ATOM   3755  N6   DA P   1      71.753  32.638  15.407  1.00 96.94           N  
ANISOU 3755  N6   DA P   1    17944   9402   9486   2601   3596   4372       N  
ATOM   3756  N1   DA P   1      72.459  30.756  16.603  1.00 95.34           N  
ANISOU 3756  N1   DA P   1    17440   9208   9578   2564   3514   4089       N  
ATOM   3757  C2   DA P   1      72.444  29.415  16.767  1.00 94.33           C  
ANISOU 3757  C2   DA P   1    17293   9110   9439   2672   3529   3885       C  
ATOM   3758  N3   DA P   1      71.790  28.488  16.065  1.00 93.81           N  
ANISOU 3758  N3   DA P   1    17439   9111   9093   2821   3589   3645       N  
ATOM   3759  C4   DA P   1      71.091  29.084  15.084  1.00 95.96           C  
ANISOU 3759  C4   DA P   1    17928   9511   9022   2877   3585   3644       C  
ATOM   3760  P    DG P   2      66.427  25.135  13.010  1.00 93.04           P  
ANISOU 3760  P    DG P   2    18339   9812   7201   2902   3397   1824       P  
ATOM   3761  OP1  DG P   2      65.840  24.012  12.263  1.00 95.55           O  
ANISOU 3761  OP1  DG P   2    18803  10304   7197   2835   3550   1327       O  
ATOM   3762  OP2  DG P   2      65.550  26.120  13.672  1.00 92.37           O  
ANISOU 3762  OP2  DG P   2    18202   9771   7124   2858   3012   1953       O  
ATOM   3763  O5'  DG P   2      67.391  24.547  14.132  1.00 91.15           O  
ANISOU 3763  O5'  DG P   2    17978   9145   7511   2887   3526   1939       O  
ATOM   3764  C5'  DG P   2      66.788  23.757  15.124  1.00 88.91           C  
ANISOU 3764  C5'  DG P   2    17704   8649   7431   2775   3416   1688       C  
ATOM   3765  C4'  DG P   2      67.431  24.016  16.464  1.00 87.68           C  
ANISOU 3765  C4'  DG P   2    17356   8223   7736   2773   3310   1989       C  
ATOM   3766  O4'  DG P   2      68.181  25.255  16.442  1.00 87.68           O  
ANISOU 3766  O4'  DG P   2    17211   8286   7815   2813   3247   2397       O  
ATOM   3767  C3'  DG P   2      66.441  24.147  17.618  1.00 86.08           C  
ANISOU 3767  C3'  DG P   2    17130   7930   7647   2637   2969   1887       C  
ATOM   3768  O3'  DG P   2      66.964  23.466  18.709  1.00 87.89           O  
ANISOU 3768  O3'  DG P   2    17253   7896   8246   2650   3035   1960       O  
ATOM   3769  C2'  DG P   2      66.430  25.630  17.942  1.00 84.15           C  
ANISOU 3769  C2'  DG P   2    16777   7766   7430   2610   2699   2195       C  
ATOM   3770  C1'  DG P   2      67.911  25.863  17.697  1.00 85.71           C  
ANISOU 3770  C1'  DG P   2    16838   7921   7808   2704   2944   2519       C  
ATOM   3771  N9   DG P   2      68.294  27.270  17.742  1.00 85.73           N  
ANISOU 3771  N9   DG P   2    16741   7968   7866   2669   2840   2843       N  
ATOM   3772  C8   DG P   2      67.765  28.354  17.075  1.00 85.19           C  
ANISOU 3772  C8   DG P   2    16774   8040   7556   2685   2751   2945       C  
ATOM   3773  N7   DG P   2      68.368  29.476  17.380  1.00 84.58           N  
ANISOU 3773  N7   DG P   2    16586   7882   7670   2625   2741   3248       N  
ATOM   3774  C5   DG P   2      69.346  29.110  18.304  1.00 85.15           C  
ANISOU 3774  C5   DG P   2    16435   7820   8097   2544   2786   3325       C  
ATOM   3775  C6   DG P   2      70.321  29.866  19.004  1.00 85.25           C  
ANISOU 3775  C6   DG P   2    16216   7757   8419   2409   2797   3568       C  
ATOM   3776  O6   DG P   2      70.550  31.073  18.961  1.00 87.14           O  
ANISOU 3776  O6   DG P   2    16429   7953   8726   2304   2808   3759       O  
ATOM   3777  N1   DG P   2      71.114  29.089  19.831  1.00 84.92           N  
ANISOU 3777  N1   DG P   2    15940   7702   8625   2393   2827   3580       N  
ATOM   3778  C2   DG P   2      70.982  27.735  19.982  1.00 85.60           C  
ANISOU 3778  C2   DG P   2    16053   7769   8703   2524   2884   3413       C  
ATOM   3779  N2   DG P   2      71.834  27.151  20.839  1.00 86.92           N  
ANISOU 3779  N2   DG P   2    15961   7940   9123   2549   2928   3520       N  
ATOM   3780  N3   DG P   2      70.078  27.003  19.344  1.00 85.14           N  
ANISOU 3780  N3   DG P   2    16247   7701   8401   2619   2917   3157       N  
ATOM   3781  C4   DG P   2      69.304  27.755  18.531  1.00 85.16           C  
ANISOU 3781  C4   DG P   2    16439   7793   8125   2607   2845   3111       C  
ATOM   3782  P    DA P   3      66.150  22.192  19.202  1.00 91.21           P  
ANISOU 3782  P    DA P   3    17805   8129   8722   2579   3100   1598       P  
ATOM   3783  OP1  DA P   3      66.403  21.124  18.200  1.00 93.63           O  
ANISOU 3783  OP1  DA P   3    18274   8385   8915   2641   3507   1349       O  
ATOM   3784  OP2  DA P   3      64.761  22.661  19.417  1.00 88.85           O  
ANISOU 3784  OP2  DA P   3    17567   7964   8228   2416   2759   1381       O  
ATOM   3785  O5'  DA P   3      66.814  21.800  20.623  1.00 89.81           O  
ANISOU 3785  O5'  DA P   3    17454   7706   8963   2645   3108   1849       O  
ATOM   3786  C5'  DA P   3      68.228  21.564  20.748  1.00 92.31           C  
ANISOU 3786  C5'  DA P   3    17599   7959   9514   2832   3352   2173       C  
ATOM   3787  C4'  DA P   3      68.769  22.106  22.061  1.00 91.28           C  
ANISOU 3787  C4'  DA P   3    17190   7852   9639   2834   3124   2508       C  
ATOM   3788  O4'  DA P   3      69.328  23.426  21.869  1.00 91.22           O  
ANISOU 3788  O4'  DA P   3    17014   8048   9599   2768   2959   2743       O  
ATOM   3789  C3'  DA P   3      67.701  22.290  23.121  1.00 88.86           C  
ANISOU 3789  C3'  DA P   3    16908   7504   9351   2676   2795   2386       C  
ATOM   3790  O3'  DA P   3      67.669  21.132  23.903  1.00 88.90           O  
ANISOU 3790  O3'  DA P   3    16930   7304   9544   2772   2952   2370       O  
ATOM   3791  C2'  DA P   3      68.131  23.504  23.937  1.00 88.00           C  
ANISOU 3791  C2'  DA P   3    16546   7551   9338   2584   2494   2657       C  
ATOM   3792  C1'  DA P   3      69.115  24.220  23.025  1.00 89.67           C  
ANISOU 3792  C1'  DA P   3    16658   7902   9510   2624   2620   2852       C  
ATOM   3793  N9   DA P   3      68.633  25.509  22.553  1.00 89.31           N  
ANISOU 3793  N9   DA P   3    16680   7957   9297   2478   2422   2833       N  
ATOM   3794  C8   DA P   3      67.552  25.729  21.747  1.00 89.15           C  
ANISOU 3794  C8   DA P   3    16902   7968   9005   2442   2355   2606       C  
ATOM   3795  N7   DA P   3      67.366  26.997  21.454  1.00 88.38           N  
ANISOU 3795  N7   DA P   3    16812   7956   8811   2368   2214   2712       N  
ATOM   3796  C5   DA P   3      68.396  27.641  22.112  1.00 87.84           C  
ANISOU 3796  C5   DA P   3    16507   7882   8988   2299   2202   2977       C  
ATOM   3797  C6   DA P   3      68.750  28.991  22.201  1.00 87.93           C  
ANISOU 3797  C6   DA P   3    16429   7911   9070   2171   2133   3167       C  
ATOM   3798  N6   DA P   3      68.058  29.956  21.588  1.00 87.64           N  
ANISOU 3798  N6   DA P   3    16564   7871   8863   2154   2076   3173       N  
ATOM   3799  N1   DA P   3      69.832  29.306  22.942  1.00 88.37           N  
ANISOU 3799  N1   DA P   3    16205   7998   9373   2064   2148   3350       N  
ATOM   3800  C2   DA P   3      70.514  28.334  23.546  1.00 88.29           C  
ANISOU 3800  C2   DA P   3    15998   8045   9505   2138   2208   3394       C  
ATOM   3801  N3   DA P   3      70.270  27.030  23.537  1.00 89.15           N  
ANISOU 3801  N3   DA P   3    16187   8105   9582   2314   2300   3284       N  
ATOM   3802  C4   DA P   3      69.190  26.747  22.794  1.00 88.73           C  
ANISOU 3802  C4   DA P   3    16434   7972   9306   2362   2303   3052       C  
ATOM   3803  P    DT P   4      68.071  21.101  25.451  1.00 88.60           P  
ANISOU 3803  P    DT P   4    16646   7280   9740   2825   2799   2658       P  
ATOM   3804  OP1  DT P   4      69.386  20.443  25.490  1.00 92.93           O  
ANISOU 3804  OP1  DT P   4    17014   7821  10473   3094   3111   2966       O  
ATOM   3805  OP2  DT P   4      66.919  20.576  26.214  1.00 86.74           O  
ANISOU 3805  OP2  DT P   4    16560   6885   9514   2730   2700   2447       O  
ATOM   3806  O5'  DT P   4      68.326  22.579  25.975  1.00 87.03           O  
ANISOU 3806  O5'  DT P   4    16209   7341   9519   2664   2420   2837       O  
ATOM   3807  C5'  DT P   4      69.643  22.898  26.385  1.00 86.63           C  
ANISOU 3807  C5'  DT P   4    15827   7479   9610   2748   2441   3181       C  
ATOM   3808  C4'  DT P   4      69.574  24.168  27.191  1.00 84.20           C  
ANISOU 3808  C4'  DT P   4    15336   7361   9297   2513   2074   3240       C  
ATOM   3809  O4'  DT P   4      69.292  25.357  26.380  1.00 83.92           O  
ANISOU 3809  O4'  DT P   4    15403   7349   9135   2338   1972   3143       O  
ATOM   3810  C3'  DT P   4      68.490  24.097  28.237  1.00 81.04           C  
ANISOU 3810  C3'  DT P   4    15019   6895   8876   2401   1828   3087       C  
ATOM   3811  O3'  DT P   4      69.167  24.566  29.334  1.00 82.19           O  
ANISOU 3811  O3'  DT P   4    14845   7275   9109   2336   1653   3293       O  
ATOM   3812  C2'  DT P   4      67.458  25.120  27.796  1.00 79.11           C  
ANISOU 3812  C2'  DT P   4    14971   6607   8478   2190   1618   2852       C  
ATOM   3813  C1'  DT P   4      68.330  26.149  27.058  1.00 80.37           C  
ANISOU 3813  C1'  DT P   4    15016   6886   8634   2131   1662   3001       C  
ATOM   3814  N1   DT P   4      67.552  27.024  26.085  1.00 77.96           N  
ANISOU 3814  N1   DT P   4    14941   6525   8155   2045   1608   2855       N  
ATOM   3815  C2   DT P   4      67.746  28.387  26.025  1.00 77.70           C  
ANISOU 3815  C2   DT P   4    14852   6535   8135   1889   1511   2943       C  
ATOM   3816  O2   DT P   4      68.543  28.994  26.706  1.00 79.47           O  
ANISOU 3816  O2   DT P   4    14839   6848   8509   1753   1458   3083       O  
ATOM   3817  N3   DT P   4      66.966  29.047  25.115  1.00 76.38           N  
ANISOU 3817  N3   DT P   4    14912   6318   7793   1891   1499   2859       N  
ATOM   3818  C4   DT P   4      66.020  28.500  24.274  1.00 75.23           C  
ANISOU 3818  C4   DT P   4    14998   6165   7421   2009   1533   2673       C  
ATOM   3819  O4   DT P   4      65.379  29.195  23.493  1.00 74.77           O  
ANISOU 3819  O4   DT P   4    15092   6144   7175   2034   1504   2648       O  
ATOM   3820  C5   DT P   4      65.858  27.073  24.387  1.00 74.45           C  
ANISOU 3820  C5   DT P   4    14939   6029   7318   2101   1628   2519       C  
ATOM   3821  C7   DT P   4      64.874  26.328  23.545  1.00 74.10           C  
ANISOU 3821  C7   DT P   4    15120   5998   7036   2162   1694   2239       C  
ATOM   3822  C6   DT P   4      66.620  26.426  25.264  1.00 76.20           C  
ANISOU 3822  C6   DT P   4    14982   6221   7750   2126   1681   2631       C  
ATOM   3823  P    DT P   5      68.588  24.456  30.807  1.00 80.46           P  
ANISOU 3823  P    DT P   5    14553   7121   8898   2261   1412   3275       P  
ATOM   3824  OP1  DT P   5      69.623  23.764  31.606  1.00 83.63           O  
ANISOU 3824  OP1  DT P   5    14639   7743   9393   2464   1500   3592       O  
ATOM   3825  OP2  DT P   5      67.229  23.867  30.744  1.00 79.33           O  
ANISOU 3825  OP2  DT P   5    14740   6709   8692   2259   1416   3014       O  
ATOM   3826  O5'  DT P   5      68.540  26.017  31.207  1.00 77.33           O  
ANISOU 3826  O5'  DT P   5    14034   6887   8460   1940   1113   3202       O  
ATOM   3827  C5'  DT P   5      69.560  26.844  30.693  1.00 75.41           C  
ANISOU 3827  C5'  DT P   5    13601   6792   8260   1847   1164   3322       C  
ATOM   3828  C4'  DT P   5      69.757  28.108  31.498  1.00 74.26           C  
ANISOU 3828  C4'  DT P   5    13257   6831   8130   1529    929   3280       C  
ATOM   3829  O4'  DT P   5      69.205  29.235  30.758  1.00 73.82           O  
ANISOU 3829  O4'  DT P   5    13428   6570   8049   1350    913   3124       O  
ATOM   3830  C3'  DT P   5      69.085  28.218  32.845  1.00 71.50           C  
ANISOU 3830  C3'  DT P   5    12868   6564   7733   1395    672   3166       C  
ATOM   3831  O3'  DT P   5      69.741  29.290  33.498  1.00 71.77           O  
ANISOU 3831  O3'  DT P   5    12626   6850   7794   1097    537   3154       O  
ATOM   3832  C2'  DT P   5      67.680  28.621  32.405  1.00 69.36           C  
ANISOU 3832  C2'  DT P   5    12983   5972   7398   1332    607   2913       C  
ATOM   3833  C1'  DT P   5      67.970  29.643  31.310  1.00 69.74           C  
ANISOU 3833  C1'  DT P   5    13111   5916   7472   1230    715   2909       C  
ATOM   3834  N1   DT P   5      67.007  29.736  30.145  1.00 67.67           N  
ANISOU 3834  N1   DT P   5    13200   5399   7113   1334    793   2793       N  
ATOM   3835  C2   DT P   5      66.771  30.974  29.594  1.00 67.59           C  
ANISOU 3835  C2   DT P   5    13313   5273   7097   1207    803   2760       C  
ATOM   3836  O2   DT P   5      67.287  31.982  30.030  1.00 69.37           O  
ANISOU 3836  O2   DT P   5    13404   5528   7425    981    778   2784       O  
ATOM   3837  N3   DT P   5      65.908  31.000  28.520  1.00 66.61           N  
ANISOU 3837  N3   DT P   5    13467   5010   6833   1349    864   2695       N  
ATOM   3838  C4   DT P   5      65.252  29.925  27.942  1.00 65.19           C  
ANISOU 3838  C4   DT P   5    13444   4813   6512   1545    907   2597       C  
ATOM   3839  O4   DT P   5      64.483  30.047  26.981  1.00 62.92           O  
ANISOU 3839  O4   DT P   5    13363   4488   6055   1643    940   2519       O  
ATOM   3840  C5   DT P   5      65.548  28.650  28.566  1.00 64.35           C  
ANISOU 3840  C5   DT P   5    13229   4758   6464   1626    934   2595       C  
ATOM   3841  C7   DT P   5      64.922  27.407  28.030  1.00 62.81           C  
ANISOU 3841  C7   DT P   5    13209   4492   6165   1789   1047   2452       C  
ATOM   3842  C6   DT P   5      66.399  28.612  29.608  1.00 65.93           C  
ANISOU 3842  C6   DT P   5    13165   5083   6803   1550    882   2724       C  
ATOM   3843  P    DC P   6      69.587  29.585  35.066  1.00 71.00           P  
ANISOU 3843  P    DC P   6    12322   7027   7628    889    274   3064       P  
ATOM   3844  OP1  DC P   6      70.869  30.137  35.546  1.00 73.46           O  
ANISOU 3844  OP1  DC P   6    12192   7761   7957    678    236   3150       O  
ATOM   3845  OP2  DC P   6      68.982  28.405  35.724  1.00 70.60           O  
ANISOU 3845  OP2  DC P   6    12339   6982   7502   1138    229   3128       O  
ATOM   3846  O5'  DC P   6      68.485  30.732  35.081  1.00 68.32           O  
ANISOU 3846  O5'  DC P   6    12276   6396   7285    626    166   2765       O  
ATOM   3847  C5'  DC P   6      68.801  31.966  34.492  1.00 68.12           C  
ANISOU 3847  C5'  DC P   6    12282   6250   7351    384    250   2686       C  
ATOM   3848  C4'  DC P   6      67.533  32.769  34.308  1.00 66.12           C  
ANISOU 3848  C4'  DC P   6    12390   5637   7096    297    212   2470       C  
ATOM   3849  O4'  DC P   6      66.775  32.278  33.183  1.00 65.47           O  
ANISOU 3849  O4'  DC P   6    12615   5291   6969    578    315   2509       O  
ATOM   3850  C3'  DC P   6      66.537  32.744  35.456  1.00 63.94           C  
ANISOU 3850  C3'  DC P   6    12186   5370   6740    224      4   2281       C  
ATOM   3851  O3'  DC P   6      66.857  33.851  36.239  1.00 65.26           O  
ANISOU 3851  O3'  DC P   6    12215   5631   6952   -140    -54   2119       O  
ATOM   3852  C2'  DC P   6      65.161  32.880  34.781  1.00 61.96           C  
ANISOU 3852  C2'  DC P   6    12323   4760   6460    369     24   2173       C  
ATOM   3853  C1'  DC P   6      65.503  32.882  33.286  1.00 64.33           C  
ANISOU 3853  C1'  DC P   6    12738   4915   6788    534    230   2323       C  
ATOM   3854  N1   DC P   6      64.639  32.127  32.352  1.00 65.15           N  
ANISOU 3854  N1   DC P   6    13088   4878   6788    816    279   2327       N  
ATOM   3855  C2   DC P   6      63.789  32.800  31.477  1.00 65.68           C  
ANISOU 3855  C2   DC P   6    13412   4741   6801    885    329   2279       C  
ATOM   3856  O2   DC P   6      63.738  34.029  31.512  1.00 67.17           O  
ANISOU 3856  O2   DC P   6    13657   4799   7066    739    363   2261       O  
ATOM   3857  N3   DC P   6      63.028  32.078  30.618  1.00 66.83           N  
ANISOU 3857  N3   DC P   6    13732   4855   6805   1113    357   2249       N  
ATOM   3858  C4   DC P   6      63.109  30.739  30.618  1.00 67.87           C  
ANISOU 3858  C4   DC P   6    13825   5071   6890   1239    379   2239       C  
ATOM   3859  N4   DC P   6      62.343  30.060  29.758  1.00 68.74           N  
ANISOU 3859  N4   DC P   6    14107   5155   6855   1402    429   2145       N  
ATOM   3860  C5   DC P   6      63.977  30.029  31.499  1.00 66.84           C  
ANISOU 3860  C5   DC P   6    13471   5073   6853   1208    372   2326       C  
ATOM   3861  C6   DC P   6      64.717  30.761  32.339  1.00 67.04           C  
ANISOU 3861  C6   DC P   6    13287   5209   6976   1010    301   2382       C  
ATOM   3862  P    DG P   7      66.422  33.972  37.764  1.00 67.47           P  
ANISOU 3862  P    DG P   7    12391   6114   7129   -336   -270   1918       P  
ATOM   3863  OP1  DG P   7      67.363  34.886  38.422  1.00 72.13           O  
ANISOU 3863  OP1  DG P   7    12695   6960   7751   -739   -282   1788       O  
ATOM   3864  OP2  DG P   7      66.225  32.634  38.360  1.00 68.03           O  
ANISOU 3864  OP2  DG P   7    12372   6412   7066    -81   -391   2049       O  
ATOM   3865  O5'  DG P   7      65.001  34.693  37.645  1.00 66.58           O  
ANISOU 3865  O5'  DG P   7    12664   5587   7047   -352   -265   1709       O  
ATOM   3866  C5'  DG P   7      64.902  36.063  37.328  1.00 68.30           C  
ANISOU 3866  C5'  DG P   7    13031   5519   7399   -577   -126   1569       C  
ATOM   3867  C4'  DG P   7      63.500  36.305  36.833  1.00 67.45           C  
ANISOU 3867  C4'  DG P   7    13290   5044   7292   -375    -96   1516       C  
ATOM   3868  O4'  DG P   7      63.249  35.319  35.819  1.00 66.36           O  
ANISOU 3868  O4'  DG P   7    13246   4882   7085    -23    -76   1710       O  
ATOM   3869  C3'  DG P   7      62.366  36.099  37.829  1.00 67.20           C  
ANISOU 3869  C3'  DG P   7    13344   5027   7161   -361   -266   1332       C  
ATOM   3870  O3'  DG P   7      61.432  37.125  37.625  1.00 69.29           O  
ANISOU 3870  O3'  DG P   7    13875   4947   7504   -370   -169   1209       O  
ATOM   3871  C2'  DG P   7      61.709  34.803  37.395  1.00 64.33           C  
ANISOU 3871  C2'  DG P   7    13058   4703   6684    -18   -343   1456       C  
ATOM   3872  C1'  DG P   7      61.886  35.003  35.902  1.00 65.23           C  
ANISOU 3872  C1'  DG P   7    13307   4624   6853    152   -170   1617       C  
ATOM   3873  N9   DG P   7      61.657  33.820  35.087  1.00 64.88           N  
ANISOU 3873  N9   DG P   7    13315   4622   6715    443   -162   1742       N  
ATOM   3874  C8   DG P   7      62.050  32.535  35.378  1.00 64.90           C  
ANISOU 3874  C8   DG P   7    13176   4822   6662    544   -206   1823       C  
ATOM   3875  N7   DG P   7      61.713  31.662  34.464  1.00 64.34           N  
ANISOU 3875  N7   DG P   7    13221   4697   6529    777   -133   1880       N  
ATOM   3876  C5   DG P   7      61.056  32.417  33.509  1.00 64.84           C  
ANISOU 3876  C5   DG P   7    13485   4587   6566    840    -76   1844       C  
ATOM   3877  C6   DG P   7      60.475  31.996  32.297  1.00 64.55           C  
ANISOU 3877  C6   DG P   7    13607   4505   6414   1050     -2   1853       C  
ATOM   3878  O6   DG P   7      60.441  30.849  31.858  1.00 65.07           O  
ANISOU 3878  O6   DG P   7    13687   4629   6409   1180     49   1847       O  
ATOM   3879  N1   DG P   7      59.909  33.056  31.597  1.00 64.89           N  
ANISOU 3879  N1   DG P   7    13799   4435   6421   1102     36   1865       N  
ATOM   3880  C2   DG P   7      59.915  34.365  32.047  1.00 65.44           C  
ANISOU 3880  C2   DG P   7    13896   4364   6606    964     50   1866       C  
ATOM   3881  N2   DG P   7      59.315  35.254  31.256  1.00 65.25           N  
ANISOU 3881  N2   DG P   7    14036   4214   6541   1096    135   1932       N  
ATOM   3882  N3   DG P   7      60.454  34.783  33.187  1.00 65.01           N  
ANISOU 3882  N3   DG P   7    13715   4303   6683    718      6   1801       N  
ATOM   3883  C4   DG P   7      61.010  33.752  33.868  1.00 64.90           C  
ANISOU 3883  C4   DG P   7    13519   4484   6657    667    -79   1793       C  
ATOM   3884  P    DA P   8      60.643  37.709  38.887  1.00 71.00           P  
ANISOU 3884  P    DA P   8    14148   5125   7706   -563   -246    924       P  
ATOM   3885  OP1  DA P   8      61.537  38.621  39.621  1.00 72.66           O  
ANISOU 3885  OP1  DA P   8    14213   5395   8001   -981   -173    740       O  
ATOM   3886  OP2  DA P   8      60.008  36.557  39.575  1.00 68.87           O  
ANISOU 3886  OP2  DA P   8    13815   5089   7264   -420   -457    907       O  
ATOM   3887  O5'  DA P   8      59.527  38.586  38.167  1.00 72.03           O  
ANISOU 3887  O5'  DA P   8    14601   4839   7928   -383    -88    920       O  
ATOM   3888  C5'  DA P   8      59.926  39.375  37.066  1.00 76.08           C  
ANISOU 3888  C5'  DA P   8    15238   5089   8581   -335    151   1076       C  
ATOM   3889  C4'  DA P   8      58.775  39.378  36.094  1.00 76.50           C  
ANISOU 3889  C4'  DA P   8    15520   4969   8579     55    192   1222       C  
ATOM   3890  O4'  DA P   8      58.783  38.157  35.313  1.00 74.00           O  
ANISOU 3890  O4'  DA P   8    15135   4879   8103    304     70   1385       O  
ATOM   3891  C3'  DA P   8      57.439  39.425  36.815  1.00 76.57           C  
ANISOU 3891  C3'  DA P   8    15624   4942   8527    143     87   1051       C  
ATOM   3892  O3'  DA P   8      56.597  40.328  36.131  1.00 81.38           O  
ANISOU 3892  O3'  DA P   8    16458   5264   9197    378    266   1149       O  
ATOM   3893  C2'  DA P   8      56.920  38.004  36.695  1.00 72.67           C  
ANISOU 3893  C2'  DA P   8    15041   4736   7834    347   -141   1086       C  
ATOM   3894  C1'  DA P   8      57.488  37.609  35.343  1.00 71.89           C  
ANISOU 3894  C1'  DA P   8    14943   4676   7696    528    -68   1326       C  
ATOM   3895  N9   DA P   8      57.629  36.172  35.234  1.00 69.75           N  
ANISOU 3895  N9   DA P   8    14548   4667   7289    611   -214   1353       N  
ATOM   3896  C8   DA P   8      58.247  35.371  36.140  1.00 68.52           C  
ANISOU 3896  C8   DA P   8    14211   4705   7120    455   -325   1296       C  
ATOM   3897  N7   DA P   8      58.228  34.111  35.799  1.00 67.21           N  
ANISOU 3897  N7   DA P   8    13997   4686   6854    603   -378   1357       N  
ATOM   3898  C5   DA P   8      57.558  34.079  34.594  1.00 66.75           C  
ANISOU 3898  C5   DA P   8    14082   4563   6716    828   -320   1409       C  
ATOM   3899  C6   DA P   8      57.205  33.035  33.717  1.00 66.25           C  
ANISOU 3899  C6   DA P   8    14052   4598   6522   1015   -315   1428       C  
ATOM   3900  N6   DA P   8      57.503  31.742  33.922  1.00 64.05           N  
ANISOU 3900  N6   DA P   8    13696   4425   6217   1022   -325   1415       N  
ATOM   3901  N1   DA P   8      56.536  33.376  32.595  1.00 67.07           N  
ANISOU 3901  N1   DA P   8    14275   4696   6514   1199   -269   1462       N  
ATOM   3902  C2   DA P   8      56.238  34.645  32.371  1.00 66.23           C  
ANISOU 3902  C2   DA P   8    14259   4460   6445   1247   -213   1530       C  
ATOM   3903  N3   DA P   8      56.517  35.692  33.122  1.00 68.55           N  
ANISOU 3903  N3   DA P   8    14568   4574   6905   1094   -168   1527       N  
ATOM   3904  C4   DA P   8      57.183  35.346  34.227  1.00 68.32           C  
ANISOU 3904  C4   DA P   8    14409   4585   6966    860   -234   1435       C  
ATOM   3905  P    DA P   9      55.073  40.479  36.593  1.00 82.95           P  
ANISOU 3905  P    DA P   9    16761   5421   9337    567    201   1033       P  
ATOM   3906  OP1  DA P   9      54.498  41.666  35.908  1.00 83.77           O  
ANISOU 3906  OP1  DA P   9    17081   5196   9550    804    464   1188       O  
ATOM   3907  OP2  DA P   9      55.022  40.341  38.065  1.00 81.84           O  
ANISOU 3907  OP2  DA P   9    16529   5365   9200    278     83    740       O  
ATOM   3908  O5'  DA P   9      54.433  39.156  35.973  1.00 80.70           O  
ANISOU 3908  O5'  DA P   9    16386   5461   8815    837    -25   1118       O  
ATOM   3909  C5'  DA P   9      54.076  39.247  34.615  1.00 81.98           C  
ANISOU 3909  C5'  DA P   9    16627   5634   8886   1162     48   1352       C  
ATOM   3910  C4'  DA P   9      53.178  38.085  34.308  1.00 80.56           C  
ANISOU 3910  C4'  DA P   9    16357   5774   8477   1346   -163   1305       C  
ATOM   3911  O4'  DA P   9      53.917  36.884  34.530  1.00 77.24           O  
ANISOU 3911  O4'  DA P   9    15806   5533   8009   1179   -286   1239       O  
ATOM   3912  C3'  DA P   9      52.020  37.898  35.262  1.00 80.50           C  
ANISOU 3912  C3'  DA P   9    16316   5838   8431   1342   -291   1095       C  
ATOM   3913  O3'  DA P   9      50.961  38.726  34.779  1.00 85.79           O  
ANISOU 3913  O3'  DA P   9    17072   6455   9069   1634   -206   1190       O  
ATOM   3914  C2'  DA P   9      51.731  36.397  35.132  1.00 75.84           C  
ANISOU 3914  C2'  DA P   9    15597   5555   7662   1346   -478   1001       C  
ATOM   3915  C1'  DA P   9      52.960  35.885  34.387  1.00 74.91           C  
ANISOU 3915  C1'  DA P   9    15455   5470   7539   1301   -432   1139       C  
ATOM   3916  N9   DA P   9      53.635  34.760  34.979  1.00 74.24           N  
ANISOU 3916  N9   DA P   9    15263   5484   7462   1117   -511   1059       N  
ATOM   3917  C8   DA P   9      54.414  34.743  36.110  1.00 73.18           C  
ANISOU 3917  C8   DA P   9    15054   5312   7440    879   -533   1006       C  
ATOM   3918  N7   DA P   9      54.895  33.561  36.390  1.00 71.73           N  
ANISOU 3918  N7   DA P   9    14768   5266   7219    824   -587   1005       N  
ATOM   3919  C5   DA P   9      54.394  32.763  35.371  1.00 71.91           C  
ANISOU 3919  C5   DA P   9    14827   5372   7123    999   -575   1015       C  
ATOM   3920  C6   DA P   9      54.521  31.406  35.078  1.00 71.15           C  
ANISOU 3920  C6   DA P   9    14696   5374   6965   1033   -557    998       C  
ATOM   3921  N6   DA P   9      55.237  30.564  35.812  1.00 71.45           N  
ANISOU 3921  N6   DA P   9    14648   5438   7060    948   -544   1037       N  
ATOM   3922  N1   DA P   9      53.893  30.939  33.989  1.00 72.69           N  
ANISOU 3922  N1   DA P   9    14942   5652   7026   1167   -528    943       N  
ATOM   3923  C2   DA P   9      53.174  31.770  33.232  1.00 72.91           C  
ANISOU 3923  C2   DA P   9    15022   5725   6954   1300   -547    950       C  
ATOM   3924  N3   DA P   9      52.977  33.069  33.404  1.00 73.22           N  
ANISOU 3924  N3   DA P   9    15104   5667   7050   1342   -552   1026       N  
ATOM   3925  C4   DA P   9      53.625  33.491  34.492  1.00 73.04           C  
ANISOU 3925  C4   DA P   9    15059   5499   7194   1167   -551   1036       C  
ATOM   3926  P    DT P  10      49.458  38.210  34.967  1.00 87.94           P  
ANISOU 3926  P    DT P  10    17249   6990   9175   1802   -365   1058       P  
ATOM   3927  OP1  DT P  10      48.578  39.319  35.400  1.00 89.60           O  
ANISOU 3927  OP1  DT P  10    17539   7027   9479   1959   -244   1064       O  
ATOM   3928  OP2  DT P  10      49.593  37.004  35.840  1.00 84.56           O  
ANISOU 3928  OP2  DT P  10    16707   6707   8714   1539   -535    829       O  
ATOM   3929  O5'  DT P  10      49.007  37.852  33.457  1.00 87.28           O  
ANISOU 3929  O5'  DT P  10    17109   7211   8844   2111   -407   1233       O  
ATOM   3930  C5'  DT P  10      49.493  36.675  32.809  1.00 84.46           C  
ANISOU 3930  C5'  DT P  10    16671   7083   8337   2033   -507   1197       C  
ATOM   3931  C4'  DT P  10      48.470  35.555  32.643  1.00 81.55           C  
ANISOU 3931  C4'  DT P  10    16150   7087   7749   2054   -680    995       C  
ATOM   3932  O4'  DT P  10      49.101  34.295  32.998  1.00 78.40           O  
ANISOU 3932  O4'  DT P  10    15713   6700   7374   1791   -732    831       O  
ATOM   3933  C3'  DT P  10      47.157  35.598  33.419  1.00 80.29           C  
ANISOU 3933  C3'  DT P  10    15900   7040   7568   2083   -768    821       C  
ATOM   3934  O3'  DT P  10      46.175  35.142  32.499  1.00 83.32           O  
ANISOU 3934  O3'  DT P  10    16133   7847   7676   2260   -864    775       O  
ATOM   3935  C2'  DT P  10      47.396  34.608  34.557  1.00 77.64           C  
ANISOU 3935  C2'  DT P  10    15534   6633   7333   1762   -835    585       C  
ATOM   3936  C1'  DT P  10      48.297  33.562  33.902  1.00 75.66           C  
ANISOU 3936  C1'  DT P  10    15282   6442   7024   1653   -830    587       C  
ATOM   3937  N1   DT P  10      49.248  32.824  34.795  1.00 71.16           N  
ANISOU 3937  N1   DT P  10    14733   5703   6603   1400   -813    531       N  
ATOM   3938  C2   DT P  10      49.517  31.498  34.577  1.00 69.17           C  
ANISOU 3938  C2   DT P  10    14447   5533   6300   1297   -802    438       C  
ATOM   3939  O2   DT P  10      49.008  30.842  33.703  1.00 69.21           O  
ANISOU 3939  O2   DT P  10    14412   5738   6146   1345   -804    336       O  
ATOM   3940  N3   DT P  10      50.415  30.945  35.438  1.00 67.96           N  
ANISOU 3940  N3   DT P  10    14303   5236   6284   1135   -767    462       N  
ATOM   3941  C4   DT P  10      51.064  31.574  36.473  1.00 67.38           C  
ANISOU 3941  C4   DT P  10    14235   5017   6348   1034   -776    539       C  
ATOM   3942  O4   DT P  10      51.855  30.997  37.199  1.00 69.16           O  
ANISOU 3942  O4   DT P  10    14426   5208   6645    914   -760    579       O  
ATOM   3943  C5   DT P  10      50.753  32.953  36.660  1.00 67.28           C  
ANISOU 3943  C5   DT P  10    14266   4915   6381   1083   -786    566       C  
ATOM   3944  C7   DT P  10      51.411  33.726  37.756  1.00 64.72           C  
ANISOU 3944  C7   DT P  10    13952   4445   6192    919   -772    576       C  
ATOM   3945  C6   DT P  10      49.875  33.501  35.817  1.00 70.33           C  
ANISOU 3945  C6   DT P  10    14675   5374   6674   1279   -786    579       C  
ATOM   3946  P    DC P  11      44.674  34.672  32.841  1.00 84.78           P  
ANISOU 3946  P    DC P  11    16119   8371   7721   2276   -995    539       P  
ATOM   3947  OP1  DC P  11      43.889  34.812  31.595  1.00 87.88           O  
ANISOU 3947  OP1  DC P  11    16358   9226   7807   2561  -1055    625       O  
ATOM   3948  OP2  DC P  11      44.227  35.329  34.090  1.00 83.63           O  
ANISOU 3948  OP2  DC P  11    16008   7996   7772   2256   -961    498       O  
ATOM   3949  O5'  DC P  11      44.823  33.098  33.098  1.00 82.29           O  
ANISOU 3949  O5'  DC P  11    15747   8140   7380   1941  -1056    242       O  
ATOM   3950  C5'  DC P  11      44.583  32.175  32.048  1.00 80.45           C  
ANISOU 3950  C5'  DC P  11    15404   8260   6903   1910  -1100    104       C  
ATOM   3951  C4'  DC P  11      44.590  30.786  32.654  1.00 77.40           C  
ANISOU 3951  C4'  DC P  11    15003   7817   6588   1577  -1081   -192       C  
ATOM   3952  O4'  DC P  11      45.786  30.616  33.440  1.00 74.38           O  
ANISOU 3952  O4'  DC P  11    14788   7017   6454   1435   -993    -93       O  
ATOM   3953  C3'  DC P  11      43.437  30.464  33.597  1.00 76.51           C  
ANISOU 3953  C3'  DC P  11    14761   7801   6507   1454  -1130   -422       C  
ATOM   3954  O3'  DC P  11      42.710  29.420  33.022  1.00 78.37           O  
ANISOU 3954  O3'  DC P  11    14846   8373   6559   1302  -1143   -717       O  
ATOM   3955  C2'  DC P  11      44.079  29.928  34.866  1.00 74.36           C  
ANISOU 3955  C2'  DC P  11    14619   7146   6487   1226  -1049   -454       C  
ATOM   3956  C1'  DC P  11      45.520  29.672  34.448  1.00 73.28           C  
ANISOU 3956  C1'  DC P  11    14634   6784   6423   1201   -964   -294       C  
ATOM   3957  N1   DC P  11      46.476  29.924  35.556  1.00 70.59           N  
ANISOU 3957  N1   DC P  11    14410   6105   6305   1126   -923   -145       N  
ATOM   3958  C2   DC P  11      47.359  28.929  35.943  1.00 68.63           C  
ANISOU 3958  C2   DC P  11    14227   5684   6164    974   -825   -136       C  
ATOM   3959  O2   DC P  11      47.311  27.861  35.342  1.00 69.43           O  
ANISOU 3959  O2   DC P  11    14326   5847   6208    899   -739   -266       O  
ATOM   3960  N3   DC P  11      48.231  29.159  36.948  1.00 67.46           N  
ANISOU 3960  N3   DC P  11    14133   5334   6167    917   -811      9       N  
ATOM   3961  C4   DC P  11      48.223  30.342  37.550  1.00 67.91           C  
ANISOU 3961  C4   DC P  11    14199   5328   6275    956   -878     84       C  
ATOM   3962  N4   DC P  11      49.086  30.561  38.545  1.00 67.18           N  
ANISOU 3962  N4   DC P  11    14130   5104   6292    857   -872    180       N  
ATOM   3963  C5   DC P  11      47.325  31.374  37.161  1.00 69.30           C  
ANISOU 3963  C5   DC P  11    14352   5593   6385   1106   -934     64       C  
ATOM   3964  C6   DC P  11      46.475  31.132  36.169  1.00 69.95           C  
ANISOU 3964  C6   DC P  11    14360   5907   6309   1214   -961    -22       C  
ATOM   3965  P    DT P  12      41.205  29.138  33.464  1.00 79.88           P  
ANISOU 3965  P    DT P  12    14802   8882   6667   1209  -1208   -989       P  
ATOM   3966  OP1  DT P  12      40.427  29.003  32.209  1.00 81.95           O  
ANISOU 3966  OP1  DT P  12    14831   9715   6592   1277  -1299  -1136       O  
ATOM   3967  OP2  DT P  12      40.827  30.077  34.555  1.00 76.92           O  
ANISOU 3967  OP2  DT P  12    14436   8344   6446   1339  -1238   -851       O  
ATOM   3968  O5'  DT P  12      41.286  27.671  34.064  1.00 76.81           O  
ANISOU 3968  O5'  DT P  12    14469   8302   6413    827  -1066  -1277       O  
ATOM   3969  C5'  DT P  12      41.623  26.668  33.170  1.00 75.08           C  
ANISOU 3969  C5'  DT P  12    14274   8159   6095    658   -970  -1464       C  
ATOM   3970  C4'  DT P  12      42.185  25.565  34.014  1.00 72.57           C  
ANISOU 3970  C4'  DT P  12    14131   7415   6029    400   -763  -1547       C  
ATOM   3971  O4'  DT P  12      43.169  26.125  34.916  1.00 70.46           O  
ANISOU 3971  O4'  DT P  12    14038   6760   5975    526   -760  -1216       O  
ATOM   3972  C3'  DT P  12      41.119  24.961  34.904  1.00 72.43           C  
ANISOU 3972  C3'  DT P  12    14004   7431   6083    172   -700  -1801       C  
ATOM   3973  O3'  DT P  12      41.305  23.564  34.814  1.00 72.15           O  
ANISOU 3973  O3'  DT P  12    14064   7214   6137   -119   -451  -2040       O  
ATOM   3974  C2'  DT P  12      41.395  25.542  36.300  1.00 69.26           C  
ANISOU 3974  C2'  DT P  12    13704   6722   5890    264   -722  -1551       C  
ATOM   3975  C1'  DT P  12      42.911  25.632  36.221  1.00 67.79           C  
ANISOU 3975  C1'  DT P  12    13733   6209   5815    370   -671  -1267       C  
ATOM   3976  N1   DT P  12      43.639  26.535  37.133  1.00 64.31           N  
ANISOU 3976  N1   DT P  12    13392   5539   5505    515   -740   -967       N  
ATOM   3977  C2   DT P  12      44.654  25.995  37.854  1.00 63.32           C  
ANISOU 3977  C2   DT P  12    13409   5110   5541    453   -621   -817       C  
ATOM   3978  O2   DT P  12      44.911  24.822  37.785  1.00 66.94           O  
ANISOU 3978  O2   DT P  12    13933   5439   6062    322   -437   -892       O  
ATOM   3979  N3   DT P  12      45.341  26.839  38.668  1.00 61.63           N  
ANISOU 3979  N3   DT P  12    13249   4762   5407    546   -697   -585       N  
ATOM   3980  C4   DT P  12      45.112  28.187  38.814  1.00 62.14           C  
ANISOU 3980  C4   DT P  12    13279   4891   5440    679   -839   -510       C  
ATOM   3981  O4   DT P  12      45.788  28.873  39.577  1.00 61.74           O  
ANISOU 3981  O4   DT P  12    13286   4703   5469    700   -871   -356       O  
ATOM   3982  C5   DT P  12      44.033  28.712  38.008  1.00 62.96           C  
ANISOU 3982  C5   DT P  12    13264   5253   5406    789   -925   -631       C  
ATOM   3983  C7   DT P  12      43.671  30.156  38.066  1.00 61.52           C  
ANISOU 3983  C7   DT P  12    13056   5114   5205    989  -1019   -525       C  
ATOM   3984  C6   DT P  12      43.361  27.874  37.207  1.00 65.09           C  
ANISOU 3984  C6   DT P  12    13437   5736   5556    711   -894   -841       C  
ATOM   3985  P    DA P  13      40.216  22.641  35.502  1.00 73.35           P  
ANISOU 3985  P    DA P  13    14118   7383   6368   -439   -293  -2373       P  
ATOM   3986  OP1  DA P  13      40.243  21.255  34.986  1.00 76.78           O  
ANISOU 3986  OP1  DA P  13    14627   7703   6843   -760     -1  -2704       O  
ATOM   3987  OP2  DA P  13      38.958  23.414  35.467  1.00 75.00           O  
ANISOU 3987  OP2  DA P  13    14036   8068   6395   -378   -513  -2487       O  
ATOM   3988  O5'  DA P  13      40.837  22.584  36.975  1.00 72.36           O  
ANISOU 3988  O5'  DA P  13    14190   6786   6516   -389   -188  -2083       O  
ATOM   3989  C5'  DA P  13      41.826  21.588  37.264  1.00 70.76           C  
ANISOU 3989  C5'  DA P  13    14225   6147   6511   -466     85  -1980       C  
ATOM   3990  C4'  DA P  13      42.135  21.608  38.750  1.00 68.40           C  
ANISOU 3990  C4'  DA P  13    14031   5565   6392   -409    143  -1714       C  
ATOM   3991  O4'  DA P  13      42.725  22.882  39.075  1.00 65.76           O  
ANISOU 3991  O4'  DA P  13    13693   5278   6016   -146   -114  -1409       O  
ATOM   3992  C3'  DA P  13      40.919  21.514  39.662  1.00 67.56           C  
ANISOU 3992  C3'  DA P  13    13806   5556   6307   -563    170  -1879       C  
ATOM   3993  O3'  DA P  13      40.861  20.233  40.224  1.00 66.97           O  
ANISOU 3993  O3'  DA P  13    13857   5182   6408   -773    518  -1951       O  
ATOM   3994  C2'  DA P  13      41.169  22.566  40.738  1.00 67.04           C  
ANISOU 3994  C2'  DA P  13    13747   5477   6250   -354    -21  -1584       C  
ATOM   3995  C1'  DA P  13      42.616  22.954  40.464  1.00 65.97           C  
ANISOU 3995  C1'  DA P  13    13747   5183   6135   -150    -90  -1276       C  
ATOM   3996  N9   DA P  13      43.000  24.301  40.833  1.00 65.14           N  
ANISOU 3996  N9   DA P  13    13619   5151   5978     52   -332  -1063       N  
ATOM   3997  C8   DA P  13      42.513  25.466  40.314  1.00 66.44           C  
ANISOU 3997  C8   DA P  13    13670   5549   6027    182   -544  -1103       C  
ATOM   3998  N7   DA P  13      43.064  26.537  40.835  1.00 65.45           N  
ANISOU 3998  N7   DA P  13    13586   5365   5916    327   -669   -897       N  
ATOM   3999  C5   DA P  13      43.962  26.029  41.751  1.00 63.12           C  
ANISOU 3999  C5   DA P  13    13404   4861   5718    276   -572   -727       C  
ATOM   4000  C6   DA P  13      44.852  26.656  42.620  1.00 62.62           C  
ANISOU 4000  C6   DA P  13    13395   4714   5682    333   -635   -516       C  
ATOM   4001  N6   DA P  13      44.962  27.980  42.697  1.00 60.87           N  
ANISOU 4001  N6   DA P  13    13160   4533   5435    424   -778   -474       N  
ATOM   4002  N1   DA P  13      45.610  25.872  43.414  1.00 63.74           N  
ANISOU 4002  N1   DA P  13    13598   4746   5875    290   -522   -353       N  
ATOM   4003  C2   DA P  13      45.479  24.545  43.313  1.00 64.96           C  
ANISOU 4003  C2   DA P  13    13797   4794   6089    217   -314   -380       C  
ATOM   4004  N3   DA P  13      44.678  23.837  42.518  1.00 65.54           N  
ANISOU 4004  N3   DA P  13    13860   4863   6180    120   -197   -609       N  
ATOM   4005  C4   DA P  13      43.939  24.657  41.762  1.00 64.24           C  
ANISOU 4005  C4   DA P  13    13594   4891   5925    143   -361   -789       C  
ATOM   4006  P    DG P  14      39.498  19.708  40.871  1.00 68.02           P  
ANISOU 4006  P    DG P  14    13870   5392   6583  -1046    671  -2235       P  
ATOM   4007  OP1  DG P  14      39.467  18.236  40.782  1.00 70.95           O  
ANISOU 4007  OP1  DG P  14    14385   5445   7129  -1321   1104  -2419       O  
ATOM   4008  OP2  DG P  14      38.383  20.493  40.320  1.00 68.17           O  
ANISOU 4008  OP2  DG P  14    13600   5897   6405  -1077    409  -2496       O  
ATOM   4009  O5'  DG P  14      39.725  20.115  42.399  1.00 67.41           O  
ANISOU 4009  O5'  DG P  14    13865   5172   6574   -890    640  -1896       O  
ATOM   4010  C5'  DG P  14      40.791  19.503  43.108  1.00 67.20           C  
ANISOU 4010  C5'  DG P  14    14065   4782   6688   -791    846  -1564       C  
ATOM   4011  C4'  DG P  14      41.093  20.309  44.345  1.00 66.43           C  
ANISOU 4011  C4'  DG P  14    13968   4735   6538   -601    674  -1258       C  
ATOM   4012  O4'  DG P  14      41.590  21.628  43.957  1.00 65.19           O  
ANISOU 4012  O4'  DG P  14    13741   4776   6254   -397    319  -1158       O  
ATOM   4013  C3'  DG P  14      39.881  20.568  45.241  1.00 67.68           C  
ANISOU 4013  C3'  DG P  14    14003   5056   6658   -713    660  -1400       C  
ATOM   4014  O3'  DG P  14      40.259  20.599  46.621  1.00 67.37           O  
ANISOU 4014  O3'  DG P  14    14051   4932   6616   -613    711  -1106       O  
ATOM   4015  C2'  DG P  14      39.539  21.995  44.854  1.00 67.05           C  
ANISOU 4015  C2'  DG P  14    13754   5295   6426   -581    292  -1480       C  
ATOM   4016  C1'  DG P  14      40.974  22.499  44.876  1.00 65.58           C  
ANISOU 4016  C1'  DG P  14    13696   4997   6225   -360    162  -1154       C  
ATOM   4017  N9   DG P  14      41.032  23.893  44.510  1.00 65.16           N  
ANISOU 4017  N9   DG P  14    13555   5136   6065   -200   -138  -1144       N  
ATOM   4018  C8   DG P  14      40.203  24.507  43.616  1.00 66.36           C  
ANISOU 4018  C8   DG P  14    13553   5525   6137   -178   -281  -1356       C  
ATOM   4019  N7   DG P  14      40.445  25.774  43.475  1.00 65.72           N  
ANISOU 4019  N7   DG P  14    13448   5530   5992     13   -489  -1254       N  
ATOM   4020  C5   DG P  14      41.496  26.013  44.346  1.00 65.64           C  
ANISOU 4020  C5   DG P  14    13574   5346   6022     67   -495  -1013       C  
ATOM   4021  C6   DG P  14      42.167  27.217  44.640  1.00 66.11           C  
ANISOU 4021  C6   DG P  14    13675   5387   6056    202   -644   -865       C  
ATOM   4022  O6   DG P  14      41.975  28.337  44.157  1.00 68.54           O  
ANISOU 4022  O6   DG P  14    13945   5764   6334    332   -768   -885       O  
ATOM   4023  N1   DG P  14      43.166  27.055  45.583  1.00 66.05           N  
ANISOU 4023  N1   DG P  14    13759   5276   6059    176   -614   -673       N  
ATOM   4024  C2   DG P  14      43.482  25.862  46.174  1.00 66.72           C  
ANISOU 4024  C2   DG P  14    13896   5281   6173     98   -451   -569       C  
ATOM   4025  N2   DG P  14      44.490  25.919  47.068  1.00 66.49           N  
ANISOU 4025  N2   DG P  14    13910   5251   6103    125   -466   -347       N  
ATOM   4026  N3   DG P  14      42.853  24.713  45.907  1.00 66.84           N  
ANISOU 4026  N3   DG P  14    13914   5235   6247     -3   -264   -674       N  
ATOM   4027  C4   DG P  14      41.871  24.865  44.992  1.00 65.31           C  
ANISOU 4027  C4   DG P  14    13623   5148   6045    -42   -302   -925       C  
ATOM   4028  P    DA P  15      39.806  19.443  47.624  1.00 68.37           P  
ANISOU 4028  P    DA P  15    14271   4855   6851   -756   1093  -1050       P  
ATOM   4029  OP1  DA P  15      40.420  18.198  47.121  1.00 71.12           O  
ANISOU 4029  OP1  DA P  15    14794   4861   7369   -799   1431   -973       O  
ATOM   4030  OP2  DA P  15      38.343  19.511  47.827  1.00 67.56           O  
ANISOU 4030  OP2  DA P  15    14010   4923   6738   -969   1130  -1372       O  
ATOM   4031  O5'  DA P  15      40.582  19.878  48.945  1.00 67.28           O  
ANISOU 4031  O5'  DA P  15    14198   4764   6603   -541   1005   -657       O  
ATOM   4032  C5'  DA P  15      41.970  20.134  48.874  1.00 65.35           C  
ANISOU 4032  C5'  DA P  15    14020   4498   6313   -323    877   -351       C  
ATOM   4033  C4'  DA P  15      42.426  21.051  50.000  1.00 64.54           C  
ANISOU 4033  C4'  DA P  15    13872   4629   6021   -186    653   -143       C  
ATOM   4034  O4'  DA P  15      42.616  22.386  49.452  1.00 62.51           O  
ANISOU 4034  O4'  DA P  15    13520   4548   5683   -138    306   -275       O  
ATOM   4035  C3'  DA P  15      41.506  21.179  51.222  1.00 63.47           C  
ANISOU 4035  C3'  DA P  15    13698   4628   5789   -264    710   -191       C  
ATOM   4036  O3'  DA P  15      42.335  21.264  52.375  1.00 63.19           O  
ANISOU 4036  O3'  DA P  15    13692   4730   5589   -122    681    142       O  
ATOM   4037  C2'  DA P  15      40.793  22.489  50.946  1.00 63.30           C  
ANISOU 4037  C2'  DA P  15    13543   4813   5696   -307    424   -490       C  
ATOM   4038  C1'  DA P  15      41.881  23.304  50.238  1.00 62.85           C  
ANISOU 4038  C1'  DA P  15    13482   4791   5607   -175    168   -410       C  
ATOM   4039  N9   DA P  15      41.356  24.362  49.367  1.00 60.98           N  
ANISOU 4039  N9   DA P  15    13152   4642   5375   -173    -44   -664       N  
ATOM   4040  C8   DA P  15      40.400  24.226  48.412  1.00 61.11           C  
ANISOU 4040  C8   DA P  15    13085   4670   5464   -248    -21   -919       C  
ATOM   4041  N7   DA P  15      40.092  25.332  47.781  1.00 59.15           N  
ANISOU 4041  N7   DA P  15    12748   4549   5178   -166   -226  -1050       N  
ATOM   4042  C5   DA P  15      40.919  26.255  48.358  1.00 60.20           C  
ANISOU 4042  C5   DA P  15    12938   4691   5244    -63   -365   -898       C  
ATOM   4043  C6   DA P  15      41.062  27.631  48.122  1.00 60.94           C  
ANISOU 4043  C6   DA P  15    13014   4835   5305     48   -544   -932       C  
ATOM   4044  N6   DA P  15      40.349  28.256  47.187  1.00 61.70           N  
ANISOU 4044  N6   DA P  15    13022   4999   5420    136   -620  -1071       N  
ATOM   4045  N1   DA P  15      41.949  28.313  48.875  1.00 60.45           N  
ANISOU 4045  N1   DA P  15    13019   4767   5184     65   -617   -816       N  
ATOM   4046  C2   DA P  15      42.640  27.625  49.792  1.00 60.75           C  
ANISOU 4046  C2   DA P  15    13100   4824   5156      5   -552   -648       C  
ATOM   4047  N3   DA P  15      42.587  26.327  50.108  1.00 61.24           N  
ANISOU 4047  N3   DA P  15    13185   4852   5231    -40   -384   -538       N  
ATOM   4048  C4   DA P  15      41.697  25.688  49.341  1.00 60.43           C  
ANISOU 4048  C4   DA P  15    13052   4677   5232    -85   -278   -684       C  
ATOM   4049  P    DT P  16      41.868  21.306  53.929  1.00 64.71           P  
ANISOU 4049  P    DT P  16    13873   5119   5594   -131    756    244       P  
ATOM   4050  OP1  DT P  16      43.022  20.847  54.730  1.00 64.67           O  
ANISOU 4050  OP1  DT P  16    13909   5218   5444     57    814    684       O  
ATOM   4051  OP2  DT P  16      40.537  20.697  54.174  1.00 64.11           O  
ANISOU 4051  OP2  DT P  16    13811   4932   5617   -297   1020     65       O  
ATOM   4052  O5'  DT P  16      41.766  22.889  54.133  1.00 62.76           O  
ANISOU 4052  O5'  DT P  16    13517   5145   5185   -152    400     21       O  
ATOM   4053  C5'  DT P  16      42.966  23.623  54.302  1.00 61.53           C  
ANISOU 4053  C5'  DT P  16    13328   5168   4883    -53    164    164       C  
ATOM   4054  C4'  DT P  16      42.588  25.074  54.371  1.00 60.24           C  
ANISOU 4054  C4'  DT P  16    13100   5147   4642   -123    -72   -131       C  
ATOM   4055  O4'  DT P  16      41.967  25.446  53.128  1.00 60.41           O  
ANISOU 4055  O4'  DT P  16    13101   4997   4854   -149   -127   -377       O  
ATOM   4056  C3'  DT P  16      41.509  25.319  55.406  1.00 62.27           C  
ANISOU 4056  C3'  DT P  16    13339   5536   4786   -205      6   -288       C  
ATOM   4057  O3'  DT P  16      42.068  26.037  56.504  1.00 65.48           O  
ANISOU 4057  O3'  DT P  16    13723   6227   4931   -214   -114   -253       O  
ATOM   4058  C2'  DT P  16      40.425  26.113  54.681  1.00 59.64           C  
ANISOU 4058  C2'  DT P  16    12955   5118   4589   -254    -57   -635       C  
ATOM   4059  C1'  DT P  16      41.159  26.560  53.436  1.00 59.06           C  
ANISOU 4059  C1'  DT P  16    12882   4926   4632   -189   -222   -637       C  
ATOM   4060  N1   DT P  16      40.225  26.937  52.313  1.00 57.84           N  
ANISOU 4060  N1   DT P  16    12666   4678   4633   -179   -255   -874       N  
ATOM   4061  C2   DT P  16      40.223  28.247  51.899  1.00 57.48           C  
ANISOU 4061  C2   DT P  16    12600   4641   4597   -110   -413  -1007       C  
ATOM   4062  O2   DT P  16      40.962  29.119  52.388  1.00 58.39           O  
ANISOU 4062  O2   DT P  16    12763   4794   4628   -105   -511   -985       O  
ATOM   4063  N3   DT P  16      39.327  28.490  50.886  1.00 55.86           N  
ANISOU 4063  N3   DT P  16    12310   4416   4498    -52   -431  -1166       N  
ATOM   4064  C4   DT P  16      38.458  27.610  50.279  1.00 55.57           C  
ANISOU 4064  C4   DT P  16    12179   4400   4533   -104   -334  -1260       C  
ATOM   4065  O4   DT P  16      37.676  27.898  49.370  1.00 54.66           O  
ANISOU 4065  O4   DT P  16    11941   4363   4463    -48   -380  -1409       O  
ATOM   4066  C5   DT P  16      38.518  26.279  50.770  1.00 56.53           C  
ANISOU 4066  C5   DT P  16    12345   4465   4667   -235   -149  -1171       C  
ATOM   4067  C7   DT P  16      37.596  25.286  50.134  1.00 57.29           C  
ANISOU 4067  C7   DT P  16    12350   4556   4862   -363      6  -1328       C  
ATOM   4068  C6   DT P  16      39.387  25.997  51.744  1.00 57.26           C  
ANISOU 4068  C6   DT P  16    12547   4535   4676   -241   -106   -956       C  
ATOM   4069  P    DT P  17      41.081  26.626  57.603  1.00 67.13           P  
ANISOU 4069  P    DT P  17    13916   6609   4980   -302    -66   -471       P  
ATOM   4070  OP1  DT P  17      41.172  25.840  58.834  1.00 70.02           O  
ANISOU 4070  OP1  DT P  17    14296   7191   5119   -285     83   -230       O  
ATOM   4071  OP2  DT P  17      39.740  26.825  57.038  1.00 69.41           O  
ANISOU 4071  OP2  DT P  17    14182   6727   5463   -338     11   -740       O  
ATOM   4072  O5'  DT P  17      41.655  28.107  57.772  1.00 67.59           O  
ANISOU 4072  O5'  DT P  17    13955   6803   4922   -357   -288   -677       O  
ATOM   4073  C5'  DT P  17      42.187  28.796  56.683  1.00 63.49           C  
ANISOU 4073  C5'  DT P  17    13439   6118   4567   -337   -435   -755       C  
ATOM   4074  C4'  DT P  17      41.722  30.237  56.634  1.00 63.68           C  
ANISOU 4074  C4'  DT P  17    13485   6081   4631   -388   -490  -1086       C  
ATOM   4075  O4'  DT P  17      40.865  30.328  55.481  1.00 62.19           O  
ANISOU 4075  O4'  DT P  17    13289   5646   4694   -291   -460  -1181       O  
ATOM   4076  C3'  DT P  17      40.939  30.821  57.813  1.00 65.59           C  
ANISOU 4076  C3'  DT P  17    13739   6473   4708   -468   -401  -1312       C  
ATOM   4077  O3'  DT P  17      41.623  32.000  58.242  1.00 64.90           O  
ANISOU 4077  O3'  DT P  17    13685   6468   4506   -585   -483  -1500       O  
ATOM   4078  C2'  DT P  17      39.562  31.139  57.217  1.00 66.43           C  
ANISOU 4078  C2'  DT P  17    13835   6379   5027   -381   -304  -1501       C  
ATOM   4079  C1'  DT P  17      39.841  31.247  55.717  1.00 63.45           C  
ANISOU 4079  C1'  DT P  17    13450   5774   4885   -277   -399  -1440       C  
ATOM   4080  N1   DT P  17      38.829  30.787  54.729  1.00 62.02           N  
ANISOU 4080  N1   DT P  17    13192   5482   4890   -173   -348  -1458       N  
ATOM   4081  C2   DT P  17      38.442  31.646  53.731  1.00 62.03           C  
ANISOU 4081  C2   DT P  17    13169   5353   5044    -41   -393  -1562       C  
ATOM   4082  O2   DT P  17      38.858  32.786  53.654  1.00 63.12           O  
ANISOU 4082  O2   DT P  17    13382   5393   5209     -3   -430  -1634       O  
ATOM   4083  N3   DT P  17      37.538  31.150  52.834  1.00 61.79           N  
ANISOU 4083  N3   DT P  17    13020   5330   5127     40   -371  -1581       N  
ATOM   4084  C4   DT P  17      37.001  29.884  52.811  1.00 63.08           C  
ANISOU 4084  C4   DT P  17    13101   5569   5299    -45   -285  -1553       C  
ATOM   4085  O4   DT P  17      36.186  29.520  51.950  1.00 60.72           O  
ANISOU 4085  O4   DT P  17    12668   5317   5087    -14   -269  -1629       O  
ATOM   4086  C5   DT P  17      37.469  29.034  53.891  1.00 63.80           C  
ANISOU 4086  C5   DT P  17    13267   5703   5272   -180   -195  -1429       C  
ATOM   4087  C7   DT P  17      36.969  27.632  54.004  1.00 64.78           C  
ANISOU 4087  C7   DT P  17    13349   5836   5428   -286    -23  -1371       C  
ATOM   4088  C6   DT P  17      38.353  29.509  54.780  1.00 62.74           C  
ANISOU 4088  C6   DT P  17    13231   5617   4992   -213   -244  -1364       C  
ATOM   4089  P    DC P  18      41.214  32.903  59.512  1.00 66.82           P  
ANISOU 4089  P    DC P  18    13967   6887   4535   -725   -399  -1807       P  
ATOM   4090  OP1  DC P  18      42.211  33.993  59.705  1.00 68.00           O  
ANISOU 4090  OP1  DC P  18    14148   7088   4601   -899   -480  -2002       O  
ATOM   4091  OP2  DC P  18      40.865  32.055  60.667  1.00 67.26           O  
ANISOU 4091  OP2  DC P  18    13983   7249   4324   -750   -318  -1700       O  
ATOM   4092  O5'  DC P  18      39.920  33.616  58.925  1.00 64.96           O  
ANISOU 4092  O5'  DC P  18    13779   6342   4562   -605   -269  -2025       O  
ATOM   4093  C5'  DC P  18      40.149  34.721  58.084  1.00 60.16           C  
ANISOU 4093  C5'  DC P  18    13238   5455   4163   -567   -284  -2159       C  
ATOM   4094  C4'  DC P  18      38.831  35.328  57.688  1.00 57.63           C  
ANISOU 4094  C4'  DC P  18    12932   4921   4044   -391   -135  -2311       C  
ATOM   4095  O4'  DC P  18      38.102  34.455  56.803  1.00 56.10           O  
ANISOU 4095  O4'  DC P  18    12627   4694   3993   -221   -159  -2133       O  
ATOM   4096  C3'  DC P  18      37.912  35.581  58.853  1.00 56.53           C  
ANISOU 4096  C3'  DC P  18    12804   4909   3768   -433     36  -2528       C  
ATOM   4097  O3'  DC P  18      38.066  36.912  59.077  1.00 57.30           O  
ANISOU 4097  O3'  DC P  18    13027   4836   3910   -483    146  -2792       O  
ATOM   4098  C2'  DC P  18      36.511  35.312  58.328  1.00 57.66           C  
ANISOU 4098  C2'  DC P  18    12841   4984   4083   -217    133  -2505       C  
ATOM   4099  C1'  DC P  18      36.753  34.862  56.885  1.00 57.46           C  
ANISOU 4099  C1'  DC P  18    12749   4832   4250    -86     -9  -2285       C  
ATOM   4100  N1   DC P  18      36.112  33.659  56.367  1.00 57.03           N  
ANISOU 4100  N1   DC P  18    12547   4879   4244    -32    -35  -2134       N  
ATOM   4101  C2   DC P  18      35.371  33.778  55.194  1.00 58.83           C  
ANISOU 4101  C2   DC P  18    12659   5037   4656    162    -49  -2117       C  
ATOM   4102  O2   DC P  18      35.254  34.898  54.722  1.00 58.83           O  
ANISOU 4102  O2   DC P  18    12698   4886   4770    327    -23  -2180       O  
ATOM   4103  N3   DC P  18      34.813  32.667  54.615  1.00 60.26           N  
ANISOU 4103  N3   DC P  18    12687   5331   4879    158    -69  -2035       N  
ATOM   4104  C4   DC P  18      35.000  31.481  55.205  1.00 57.81           C  
ANISOU 4104  C4   DC P  18    12379   5116   4472    -18    -32  -1949       C  
ATOM   4105  N4   DC P  18      34.423  30.439  54.633  1.00 56.55           N  
ANISOU 4105  N4   DC P  18    12087   5016   4381    -58      2  -1916       N  
ATOM   4106  C5   DC P  18      35.762  31.336  56.413  1.00 57.88           C  
ANISOU 4106  C5   DC P  18    12516   5181   4294   -159     -6  -1898       C  
ATOM   4107  C6   DC P  18      36.317  32.438  56.952  1.00 57.74           C  
ANISOU 4107  C6   DC P  18    12611   5132   4195   -170    -33  -2002       C  
ATOM   4108  P    DG P  19      37.545  37.533  60.428  1.00 59.68           P  
ANISOU 4108  P    DG P  19    13399   5249   4027   -606    344  -3112       P  
ATOM   4109  OP1  DG P  19      38.485  38.615  60.715  1.00 62.48           O  
ANISOU 4109  OP1  DG P  19    13895   5500   4345   -817    386  -3362       O  
ATOM   4110  OP2  DG P  19      37.343  36.459  61.455  1.00 60.77           O  
ANISOU 4110  OP2  DG P  19    13447   5775   3867   -704    316  -3027       O  
ATOM   4111  O5'  DG P  19      36.100  38.043  59.987  1.00 60.24           O  
ANISOU 4111  O5'  DG P  19    13451   5092   4346   -321    546  -3186       O  
ATOM   4112  C5'  DG P  19      35.884  39.023  59.037  1.00 60.58           C  
ANISOU 4112  C5'  DG P  19    13560   4780   4679   -112    644  -3208       C  
ATOM   4113  C4'  DG P  19      34.440  38.900  58.610  1.00 63.57           C  
ANISOU 4113  C4'  DG P  19    13792   5155   5206    197    749  -3141       C  
ATOM   4114  O4'  DG P  19      34.213  37.588  58.022  1.00 64.52           O  
ANISOU 4114  O4'  DG P  19    13717   5491   5307    236    553  -2886       O  
ATOM   4115  C3'  DG P  19      33.384  39.000  59.689  1.00 67.40           C  
ANISOU 4115  C3'  DG P  19    14243   5778   5588    209    962  -3344       C  
ATOM   4116  O3'  DG P  19      32.348  39.757  59.132  1.00 72.03           O  
ANISOU 4116  O3'  DG P  19    14778   6183   6407    545   1149  -3359       O  
ATOM   4117  C2'  DG P  19      32.928  37.558  59.865  1.00 67.73           C  
ANISOU 4117  C2'  DG P  19    14088   6155   5494    153    837  -3174       C  
ATOM   4118  C1'  DG P  19      32.921  37.174  58.401  1.00 66.78           C  
ANISOU 4118  C1'  DG P  19    13842   5960   5573    333    669  -2928       C  
ATOM   4119  N9   DG P  19      32.789  35.760  58.083  1.00 66.88           N  
ANISOU 4119  N9   DG P  19    13690   6187   5535    261    524  -2737       N  
ATOM   4120  C8   DG P  19      33.327  34.704  58.771  1.00 68.09           C  
ANISOU 4120  C8   DG P  19    13863   6514   5494     28    460  -2649       C  
ATOM   4121  N7   DG P  19      33.060  33.537  58.216  1.00 67.45           N  
ANISOU 4121  N7   DG P  19    13643   6528   5458     13    395  -2482       N  
ATOM   4122  C5   DG P  19      32.299  33.835  57.101  1.00 65.86           C  
ANISOU 4122  C5   DG P  19    13292   6278   5455    221    379  -2489       C  
ATOM   4123  C6   DG P  19      31.714  32.980  56.145  1.00 65.75           C  
ANISOU 4123  C6   DG P  19    13074   6368   5540    256    322  -2407       C  
ATOM   4124  O6   DG P  19      31.741  31.744  56.050  1.00 65.86           O  
ANISOU 4124  O6   DG P  19    13027   6465   5533     95    310  -2322       O  
ATOM   4125  N1   DG P  19      31.023  33.701  55.195  1.00 66.36           N  
ANISOU 4125  N1   DG P  19    13006   6456   5752    511    304  -2438       N  
ATOM   4126  C2   DG P  19      30.913  35.058  55.169  1.00 66.53           C  
ANISOU 4126  C2   DG P  19    13101   6336   5843    740    374  -2496       C  
ATOM   4127  N2   DG P  19      30.196  35.544  54.154  1.00 67.90           N  
ANISOU 4127  N2   DG P  19    13092   6577   6131   1028    359  -2450       N  
ATOM   4128  N3   DG P  19      31.447  35.873  56.058  1.00 67.70           N  
ANISOU 4128  N3   DG P  19    13474   6303   5944    692    474  -2596       N  
ATOM   4129  C4   DG P  19      32.129  35.198  57.002  1.00 66.96           C  
ANISOU 4129  C4   DG P  19    13497   6264   5682    408    452  -2608       C  
ATOM   4130  P    DA P  20      31.441  40.720  60.043  1.00 79.89           P  
ANISOU 4130  P    DA P  20    15849   7081   7424    648   1504  -3644       P  
ATOM   4131  OP1  DA P  20      32.252  41.896  60.457  1.00 79.04           O  
ANISOU 4131  OP1  DA P  20    16035   6649   7348    503   1684  -3898       O  
ATOM   4132  OP2  DA P  20      30.821  39.820  61.062  1.00 79.28           O  
ANISOU 4132  OP2  DA P  20    15642   7368   7113    503   1514  -3709       O  
ATOM   4133  O5'  DA P  20      30.307  41.226  59.025  1.00 80.77           O  
ANISOU 4133  O5'  DA P  20    15800   7075   7812   1123   1629  -3490       O  
ATOM   4134  C5'  DA P  20      30.513  41.108  57.618  1.00 83.01           C  
ANISOU 4134  C5'  DA P  20    15987   7303   8250   1329   1444  -3204       C  
ATOM   4135  C4'  DA P  20      29.230  40.673  56.934  1.00 84.96           C  
ANISOU 4135  C4'  DA P  20    15893   7827   8562   1648   1412  -3034       C  
ATOM   4136  O4'  DA P  20      29.257  39.249  56.603  1.00 82.34           O  
ANISOU 4136  O4'  DA P  20    15349   7835   8102   1459   1127  -2910       O  
ATOM   4137  C3'  DA P  20      28.012  40.901  57.816  1.00 88.59           C  
ANISOU 4137  C3'  DA P  20    16238   8419   9004   1769   1672  -3204       C  
ATOM   4138  O3'  DA P  20      26.935  41.348  57.017  1.00 93.53           O  
ANISOU 4138  O3'  DA P  20    16620   9127   9789   2227   1771  -3051       O  
ATOM   4139  C2'  DA P  20      27.747  39.522  58.393  1.00 86.19           C  
ANISOU 4139  C2'  DA P  20    15754   8500   8495   1473   1521  -3233       C  
ATOM   4140  C1'  DA P  20      28.122  38.651  57.195  1.00 83.55           C  
ANISOU 4140  C1'  DA P  20    15267   8299   8178   1448   1209  -2994       C  
ATOM   4141  N9   DA P  20      28.451  37.299  57.612  1.00 81.43           N  
ANISOU 4141  N9   DA P  20    14956   8242   7740   1093   1053  -2983       N  
ATOM   4142  C8   DA P  20      29.141  36.947  58.744  1.00 81.30           C  
ANISOU 4142  C8   DA P  20    15135   8215   7542    780   1073  -3081       C  
ATOM   4143  N7   DA P  20      29.285  35.655  58.901  1.00 79.76           N  
ANISOU 4143  N7   DA P  20    14861   8214   7232    551    960  -2988       N  
ATOM   4144  C5   DA P  20      28.635  35.125  57.783  1.00 78.74           C  
ANISOU 4144  C5   DA P  20    14470   8217   7230    675    865  -2876       C  
ATOM   4145  C6   DA P  20      28.422  33.805  57.340  1.00 75.70           C  
ANISOU 4145  C6   DA P  20    13908   8018   6836    517    771  -2785       C  
ATOM   4146  N6   DA P  20      28.866  32.749  58.008  1.00 73.45           N  
ANISOU 4146  N6   DA P  20    13708   7769   6430    239    783  -2733       N  
ATOM   4147  N1   DA P  20      27.740  33.612  56.195  1.00 76.13           N  
ANISOU 4147  N1   DA P  20    13695   8230   7002    655    691  -2749       N  
ATOM   4148  C2   DA P  20      27.290  34.675  55.524  1.00 78.04           C  
ANISOU 4148  C2   DA P  20    13837   8472   7343    992    691  -2741       C  
ATOM   4149  N3   DA P  20      27.420  35.967  55.836  1.00 80.80           N  
ANISOU 4149  N3   DA P  20    14354   8604   7742   1215    807  -2772       N  
ATOM   4150  C4   DA P  20      28.109  36.125  56.984  1.00 80.21           C  
ANISOU 4150  C4   DA P  20    14560   8344   7572   1013    896  -2868       C  
ATOM   4151  P    DA P  21      25.481  41.482  57.681  1.00 99.46           P  
ANISOU 4151  P    DA P  21    17137  10110  10545   2435   2024  -3164       P  
ATOM   4152  OP1  DA P  21      24.709  42.529  56.971  1.00101.85           O  
ANISOU 4152  OP1  DA P  21    17325  10321  11053   2989   2234  -3007       O  
ATOM   4153  OP2  DA P  21      25.648  41.570  59.150  1.00100.11           O  
ANISOU 4153  OP2  DA P  21    17441  10096  10498   2137   2219  -3466       O  
ATOM   4154  O5'  DA P  21      24.872  40.032  57.342  1.00 98.00           O  
ANISOU 4154  O5'  DA P  21    16557  10447  10230   2286   1760  -3077       O  
ATOM   4155  C5'  DA P  21      24.387  39.711  56.031  1.00 97.25           C  
ANISOU 4155  C5'  DA P  21    16127  10638  10184   2524   1568  -2855       C  
ATOM   4156  C4'  DA P  21      23.620  38.402  56.084  1.00 96.52           C  
ANISOU 4156  C4'  DA P  21    15672  11026   9974   2299   1442  -2905       C  
ATOM   4157  O4'  DA P  21      24.549  37.354  56.444  1.00 92.37           O  
ANISOU 4157  O4'  DA P  21    15330  10436   9330   1829   1277  -2954       O  
ATOM   4158  C3'  DA P  21      22.502  38.357  57.131  1.00 99.63           C  
ANISOU 4158  C3'  DA P  21    15891  11626  10338   2301   1695  -3080       C  
ATOM   4159  O3'  DA P  21      21.198  38.423  56.542  1.00104.16           O  
ANISOU 4159  O3'  DA P  21    15993  12625  10959   2621   1732  -3016       O  
ATOM   4160  C2'  DA P  21      22.669  37.025  57.850  1.00 96.77           C  
ANISOU 4160  C2'  DA P  21    15532  11408   9827   1806   1626  -3195       C  
ATOM   4161  C1'  DA P  21      23.823  36.355  57.120  1.00 92.59           C  
ANISOU 4161  C1'  DA P  21    15156  10759   9267   1578   1338  -3073       C  
ATOM   4162  N9   DA P  21      24.664  35.656  58.077  1.00 89.74           N  
ANISOU 4162  N9   DA P  21    15070  10252   8774   1183   1335  -3134       N  
ATOM   4163  C8   DA P  21      25.374  36.164  59.126  1.00 88.75           C  
ANISOU 4163  C8   DA P  21    15285   9876   8558   1077   1447  -3226       C  
ATOM   4164  N7   DA P  21      26.020  35.253  59.811  1.00 87.00           N  
ANISOU 4164  N7   DA P  21    15204   9671   8179    737   1399  -3217       N  
ATOM   4165  C5   DA P  21      25.693  34.072  59.165  1.00 86.15           C  
ANISOU 4165  C5   DA P  21    14866   9764   8104    611   1288  -3118       C  
ATOM   4166  C6   DA P  21      26.044  32.738  59.388  1.00 84.21           C  
ANISOU 4166  C6   DA P  21    14640   9580   7775    298   1250  -3038       C  
ATOM   4167  N6   DA P  21      26.850  32.346  60.364  1.00 82.47           N  
ANISOU 4167  N6   DA P  21    14669   9279   7386     91   1286  -2991       N  
ATOM   4168  N1   DA P  21      25.539  31.809  58.554  1.00 86.43           N  
ANISOU 4168  N1   DA P  21    14668  10024   8146    210   1193  -3005       N  
ATOM   4169  C2   DA P  21      24.736  32.181  57.545  1.00 87.72           C  
ANISOU 4169  C2   DA P  21    14534  10368   8426    420   1129  -3048       C  
ATOM   4170  N3   DA P  21      24.333  33.408  57.229  1.00 88.71           N  
ANISOU 4170  N3   DA P  21    14584  10508   8614    772   1135  -3069       N  
ATOM   4171  C4   DA P  21      24.856  34.303  58.094  1.00 88.22           C  
ANISOU 4171  C4   DA P  21    14822  10192   8507    850   1238  -3100       C  
ATOM   4172  P    DT P  22      19.890  38.185  57.442  1.00108.29           P  
ANISOU 4172  P    DT P  22    16213  13480  11452   2615   1972  -3181       P  
ATOM   4173  OP1  DT P  22      19.068  39.408  57.383  1.00112.46           O  
ANISOU 4173  OP1  DT P  22    16607  14019  12103   3160   2222  -3116       O  
ATOM   4174  OP2  DT P  22      20.282  37.630  58.760  1.00106.47           O  
ANISOU 4174  OP2  DT P  22    16254  13088  11111   2187   2086  -3371       O  
ATOM   4175  O5'  DT P  22      19.113  37.051  56.627  1.00110.04           O  
ANISOU 4175  O5'  DT P  22    15915  14280  11615   2475   1767  -3163       O  
ATOM   4176  C5'  DT P  22      19.777  36.166  55.754  1.00108.87           C  
ANISOU 4176  C5'  DT P  22    15761  14192  11414   2207   1468  -3105       C  
ATOM   4177  C4'  DT P  22      19.196  34.782  55.965  1.00110.73           C  
ANISOU 4177  C4'  DT P  22    15713  14780  11580   1770   1455  -3266       C  
ATOM   4178  O4'  DT P  22      20.203  33.977  56.624  1.00107.27           O  
ANISOU 4178  O4'  DT P  22    15666  13998  11093   1334   1441  -3309       O  
ATOM   4179  C3'  DT P  22      17.956  34.715  56.868  1.00115.16           C  
ANISOU 4179  C3'  DT P  22    15984  15629  12141   1766   1726  -3418       C  
ATOM   4180  O3'  DT P  22      17.110  33.587  56.520  1.00119.19           O  
ANISOU 4180  O3'  DT P  22    16037  16629  12619   1466   1690  -3549       O  
ATOM   4181  C2'  DT P  22      18.612  34.529  58.228  1.00112.53           C  
ANISOU 4181  C2'  DT P  22    16104  14891  11763   1485   1902  -3498       C  
ATOM   4182  C1'  DT P  22      19.601  33.463  57.789  1.00108.55           C  
ANISOU 4182  C1'  DT P  22    15784  14243  11217   1099   1684  -3453       C  
ATOM   4183  N1   DT P  22      20.647  33.141  58.759  1.00105.56           N  
ANISOU 4183  N1   DT P  22    15871  13480  10758    828   1737  -3441       N  
ATOM   4184  C2   DT P  22      21.105  31.848  58.766  1.00103.74           C  
ANISOU 4184  C2   DT P  22    15711  13216  10489    428   1687  -3422       C  
ATOM   4185  O2   DT P  22      20.674  30.998  58.008  1.00103.90           O  
ANISOU 4185  O2   DT P  22    15449  13468  10559    256   1621  -3462       O  
ATOM   4186  N3   DT P  22      22.082  31.598  59.693  1.00101.84           N  
ANISOU 4186  N3   DT P  22    15874  12678  10142    240   1736  -3360       N  
ATOM   4187  C4   DT P  22      22.620  32.506  60.584  1.00101.54           C  
ANISOU 4187  C4   DT P  22    16145  12428  10009    363   1808  -3369       C  
ATOM   4188  O4   DT P  22      23.491  32.187  61.381  1.00100.17           O  
ANISOU 4188  O4   DT P  22    16276  12090   9693    173   1827  -3314       O  
ATOM   4189  C5   DT P  22      22.089  33.846  60.514  1.00103.69           C  
ANISOU 4189  C5   DT P  22    16348  12702  10349    733   1883  -3448       C  
ATOM   4190  C7   DT P  22      22.604  34.908  61.439  1.00104.23           C  
ANISOU 4190  C7   DT P  22    16753  12516  10336    838   2013  -3530       C  
ATOM   4191  C6   DT P  22      21.135  34.104  59.612  1.00105.34           C  
ANISOU 4191  C6   DT P  22    16179  13161  10685    975   1854  -3453       C  
ATOM   4192  P    DC P  23      15.777  33.216  57.347  1.00124.53           P  
ANISOU 4192  P    DC P  23    16333  17685  13299   1345   1967  -3730       P  
ATOM   4193  OP1  DC P  23      14.666  34.001  56.768  1.00128.40           O  
ANISOU 4193  OP1  DC P  23    16312  18664  13808   1807   1976  -3689       O  
ATOM   4194  OP2  DC P  23      16.082  33.355  58.791  1.00124.33           O  
ANISOU 4194  OP2  DC P  23    16707  17278  13256   1235   2227  -3775       O  
ATOM   4195  O5'  DC P  23      15.536  31.653  57.059  1.00125.65           O  
ANISOU 4195  O5'  DC P  23    16238  18082  13421    772   1926  -3897       O  
ATOM   4196  C5'  DC P  23      16.622  30.713  57.053  1.00124.22           C  
ANISOU 4196  C5'  DC P  23    16442  17523  13231    366   1847  -3883       C  
ATOM   4197  C4'  DC P  23      16.494  29.559  58.054  1.00125.89           C  
ANISOU 4197  C4'  DC P  23    16758  17622  13453   -123   2114  -3996       C  
ATOM   4198  O4'  DC P  23      17.637  29.571  58.955  1.00122.34           O  
ANISOU 4198  O4'  DC P  23    16887  16645  12953   -182   2171  -3855       O  
ATOM   4199  C3'  DC P  23      15.283  29.491  58.993  1.00130.77           C  
ANISOU 4199  C3'  DC P  23    17086  18520  14080   -183   2433  -4133       C  
ATOM   4200  O3'  DC P  23      15.059  28.114  59.389  1.00133.91           O  
ANISOU 4200  O3'  DC P  23    17451  18912  14516   -720   2650  -4253       O  
ATOM   4201  C2'  DC P  23      15.781  30.323  60.166  1.00128.38           C  
ANISOU 4201  C2'  DC P  23    17217  17850  13713     47   2571  -4022       C  
ATOM   4202  C1'  DC P  23      17.152  29.670  60.280  1.00123.68           C  
ANISOU 4202  C1'  DC P  23    17119  16800  13074   -211   2473  -3897       C  
ATOM   4203  N1   DC P  23      18.135  30.407  61.095  1.00120.50           N  
ANISOU 4203  N1   DC P  23    17208  16009  12567    -43   2473  -3775       N  
ATOM   4204  C2   DC P  23      19.087  29.666  61.787  1.00117.99           C  
ANISOU 4204  C2   DC P  23    17284  15394  12154   -320   2524  -3667       C  
ATOM   4205  O2   DC P  23      19.063  28.437  61.683  1.00117.83           O  
ANISOU 4205  O2   DC P  23    17218  15376  12174   -663   2603  -3653       O  
ATOM   4206  N3   DC P  23      20.001  30.312  62.547  1.00116.34           N  
ANISOU 4206  N3   DC P  23    17479  14918  11806   -205   2507  -3585       N  
ATOM   4207  C4   DC P  23      19.972  31.641  62.619  1.00116.59           C  
ANISOU 4207  C4   DC P  23    17563  14906  11830    135   2478  -3642       C  
ATOM   4208  N4   DC P  23      20.894  32.230  63.377  1.00115.22           N  
ANISOU 4208  N4   DC P  23    17781  14486  11509    173   2478  -3618       N  
ATOM   4209  C5   DC P  23      19.003  32.419  61.918  1.00118.96           C  
ANISOU 4209  C5   DC P  23    17507  15427  12265    452   2471  -3724       C  
ATOM   4210  C6   DC P  23      18.107  31.766  61.170  1.00120.79           C  
ANISOU 4210  C6   DC P  23    17301  15995  12597    369   2449  -3771       C  
ATOM   4211  P    DT P  24      14.113  27.670  60.622  1.00138.55           P  
ANISOU 4211  P    DT P  24    17904  19628  15112   -942   3063  -4361       P  
ATOM   4212  OP1  DT P  24      13.237  26.610  60.075  1.00141.25           O  
ANISOU 4212  OP1  DT P  24    17783  20333  15550  -1365   3170  -4589       O  
ATOM   4213  OP2  DT P  24      13.539  28.879  61.263  1.00139.36           O  
ANISOU 4213  OP2  DT P  24    17917  19870  15163   -510   3156  -4344       O  
ATOM   4214  O5'  DT P  24      15.106  26.988  61.685  1.00136.51           O  
ANISOU 4214  O5'  DT P  24    18229  18844  14794  -1192   3247  -4203       O  
ATOM   4215  C5'  DT P  24      15.664  25.690  61.419  1.00135.43           C  
ANISOU 4215  C5'  DT P  24    18264  18468  14725  -1616   3304  -4174       C  
ATOM   4216  C4'  DT P  24      16.254  25.047  62.670  1.00134.82           C  
ANISOU 4216  C4'  DT P  24    18633  18021  14570  -1798   3588  -3987       C  
ATOM   4217  O4'  DT P  24      17.617  25.509  62.909  1.00130.65           O  
ANISOU 4217  O4'  DT P  24    18594  17140  13908  -1577   3382  -3750       O  
ATOM   4218  C3'  DT P  24      15.553  25.336  63.996  1.00137.04           C  
ANISOU 4218  C3'  DT P  24    18894  18424  14749  -1745   3905  -3993       C  
ATOM   4219  O3'  DT P  24      14.405  24.531  64.157  1.00140.91           O  
ANISOU 4219  O3'  DT P  24    19025  19156  15359  -2078   4237  -4162       O  
ATOM   4220  C2'  DT P  24      16.665  24.915  64.949  1.00134.84           C  
ANISOU 4220  C2'  DT P  24    19162  17754  14315  -1800   4012  -3718       C  
ATOM   4221  C1'  DT P  24      17.772  25.729  64.301  1.00130.22           C  
ANISOU 4221  C1'  DT P  24    18807  16998  13673  -1510   3594  -3627       C  
ATOM   4222  N1   DT P  24      17.512  27.147  64.549  1.00128.85           N  
ANISOU 4222  N1   DT P  24    18576  16973  13408  -1130   3483  -3714       N  
ATOM   4223  C2   DT P  24      18.395  27.891  65.291  1.00126.54           C  
ANISOU 4223  C2   DT P  24    18668  16496  12917   -932   3411  -3604       C  
ATOM   4224  O2   DT P  24      19.420  27.436  65.758  1.00124.42           O  
ANISOU 4224  O2   DT P  24    18758  16005  12512  -1035   3395  -3412       O  
ATOM   4225  N3   DT P  24      18.026  29.199  65.457  1.00127.06           N  
ANISOU 4225  N3   DT P  24    18666  16664  12946   -603   3378  -3735       N  
ATOM   4226  C4   DT P  24      16.882  29.803  64.965  1.00129.62           C  
ANISOU 4226  C4   DT P  24    18573  17265  13411   -403   3411  -3903       C  
ATOM   4227  O4   DT P  24      16.637  30.984  65.165  1.00129.98           O  
ANISOU 4227  O4   DT P  24    18612  17337  13435    -72   3429  -3983       O  
ATOM   4228  C5   DT P  24      15.999  28.953  64.201  1.00131.72           C  
ANISOU 4228  C5   DT P  24    18402  17798  13846   -611   3445  -3985       C  
ATOM   4229  C7   DT P  24      14.724  29.488  63.617  1.00135.10           C  
ANISOU 4229  C7   DT P  24    18291  18645  14396   -404   3462  -4148       C  
ATOM   4230  C6   DT P  24      16.352  27.678  64.035  1.00130.81           C  
ANISOU 4230  C6   DT P  24    18364  17565  13771   -991   3484  -3916       C  
TER    4231       DT P  24                                                      
MASTER      734    0    0   21    4    0    0    6 4226    5    0   42          
END

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Related entries of code: 3on0

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
No similar entries are found!
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
No complexes with the same small molecule ligand are found!

Entry Information

PDB ID	3on0
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	pED208 protein TraM
Ligand Name	cognate sbmA DNA
EC.Number	E.C.-.-.-.-
Resolution	2.87(Å)
Affinity (Kd/Ki/IC50)	Kd=4.8nM
Release Year	2011
Protein/NA Sequence	Check fasta file
Primary Reference	(2011) Nucleic Acids Res. Vol. 39: pp. 6775-6788

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): P33788
Entrez Gene ID	No matched NCBI Entrez Gene ID found!
ASD	Information of known allosteric effects of PDB entries

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