CNRS Nantes University UFIP UFIP
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***  4ekw  ***

elNémo ID: 21031822363973522

Job options:

ID        	=	 21031822363973522
JOBID     	=	 4ekw
USERID    	=	 kaitlynbm
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 4ekw

HEADER    TRANSPORT PROTEIN                       10-APR-12   4EKW              
TITLE     CRYSTAL STRUCTURE OF THE NAVAB VOLTAGE-GATED SODIUM CHANNEL (WILD-    
TITLE    2 TYPE, 3.2 A)                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ION TRANSPORT PROTEIN;                                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARCOBACTER BUTZLERI;                            
SOURCE   3 ORGANISM_TAXID: 367737;                                              
SOURCE   4 STRAIN: RM4018;                                                      
SOURCE   5 GENE: ABU_1752;                                                      
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PFASTBAC DUAL                         
KEYWDS    VOLTAGE-GATED ION CHANNEL, TETRAMERIC ION CHANNEL SUPERFAMILY,        
KEYWDS   2 VOLTAGE-GATED SODIUM CHANNEL, MEMBRANE, TRANSPORT PROTEIN            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.PAYANDEH,T.M.GAMAL EL-DIN,T.SCHEUER,N.ZHENG,W.A.CATTERALL           
REVDAT   2   03-OCT-12 4EKW    1       JRNL                                     
REVDAT   1   16-MAY-12 4EKW    0                                                
JRNL        AUTH   J.PAYANDEH,T.M.GAMAL EL-DIN,T.SCHEUER,N.ZHENG,W.A.CATTERALL  
JRNL        TITL   CRYSTAL STRUCTURE OF A VOLTAGE-GATED SODIUM CHANNEL IN TWO   
JRNL        TITL 2 POTENTIALLY INACTIVATED STATES.                              
JRNL        REF    NATURE                        V. 486   135 2012              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   22678296                                                     
JRNL        DOI    10.1038/NATURE11077                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.21 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 3.21                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 44951                          
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) : 0.309                           
REMARK   3   R VALUE            (WORKING SET) : 0.308                           
REMARK   3   FREE R VALUE                     : 0.322                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2397                            
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) : 3.21                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.29                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3321                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.23                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 176                          
REMARK   3   BIN FREE R VALUE                    : 0.2430                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7138                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 77                                      
REMARK   3   SOLVENT ATOMS            : 3                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 102.72                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 53.81000                                             
REMARK   3    B22 (A**2) : 53.81000                                             
REMARK   3    B33 (A**2) : -107.63000                                           
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): 0.144         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.090         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.278         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 35.530        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.820                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.822                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7410 ; 0.009 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10076 ; 1.382 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   864 ; 5.699 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   282 ;28.968 ;21.489       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1111 ;18.899 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;16.323 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1201 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5312 ; 0.005 ; 0.021       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.496                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : K, H, -L                                        
REMARK   3      TWIN FRACTION : 0.504                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 16                                         
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  1001        A  1094                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.1017  38.3668  61.5445              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7721 T22:   0.8455                                     
REMARK   3      T33:   1.1958 T12:   0.2259                                     
REMARK   3      T13:   0.1066 T23:  -0.0976                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2161 L22:   0.3387                                     
REMARK   3      L33:   3.3358 L12:  -0.4631                                     
REMARK   3      L13:  -1.9486 L23:   0.9120                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0047 S12:  -0.0087 S13:  -0.3749                       
REMARK   3      S21:   0.0372 S22:  -0.1230 S23:  -0.2089                       
REMARK   3      S31:   0.0308 S32:   0.0372 S33:   0.1277                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1095        A  1159                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.5618  62.5316  65.1412              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3099 T22:   0.7032                                     
REMARK   3      T33:   1.1430 T12:   0.0561                                     
REMARK   3      T13:   0.1142 T23:  -0.0576                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1066 L22:   2.1514                                     
REMARK   3      L33:   3.5680 L12:  -0.0095                                     
REMARK   3      L13:  -0.0291 L23:   0.0599                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1168 S12:   0.1672 S13:  -0.1379                       
REMARK   3      S21:  -0.1867 S22:  -0.1688 S23:   0.1594                       
REMARK   3      S31:  -0.0695 S32:  -0.0631 S33:   0.0520                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1160        A  1181                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.6072  71.3772  73.8420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6531 T22:   0.6892                                     
REMARK   3      T33:   1.2535 T12:  -0.0299                                     
REMARK   3      T13:  -0.0135 T23:  -0.1474                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6981 L22:   6.6901                                     
REMARK   3      L33:   7.5889 L12:   4.2180                                     
REMARK   3      L13:  -2.3906 L23:  -6.3878                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1598 S12:  -0.0059 S13:   0.0999                       
REMARK   3      S21:  -0.1801 S22:  -0.0097 S23:  -0.1161                       
REMARK   3      S31:   0.5980 S32:  -0.1514 S33:  -0.1501                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1182        A  1219                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.8565  76.4977  67.0676              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3021 T22:   0.8512                                     
REMARK   3      T33:   1.2291 T12:   0.0430                                     
REMARK   3      T13:   0.0770 T23:   0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8201 L22:   3.8167                                     
REMARK   3      L33:  13.4178 L12:   0.4732                                     
REMARK   3      L13:  -2.9326 L23:   1.4401                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1577 S12:   0.1455 S13:   0.2295                       
REMARK   3      S21:  -0.1668 S22:   0.7447 S23:  -0.3011                       
REMARK   3      S31:  -0.6484 S32:   0.2451 S33:  -0.9023                       
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 :   B  1001        B  1049                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.0120  35.9182  61.0080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5423 T22:   0.7421                                     
REMARK   3      T33:   1.2574 T12:   0.0124                                     
REMARK   3      T13:  -0.1784 T23:   0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4354 L22:   4.0803                                     
REMARK   3      L33:  13.7510 L12:  -0.4319                                     
REMARK   3      L13:  -2.5411 L23:   5.7667                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0258 S12:   0.0291 S13:  -0.5303                       
REMARK   3      S21:  -0.2561 S22:   0.0568 S23:   0.2379                       
REMARK   3      S31:  -0.0426 S32:   0.4148 S33:  -0.0826                       
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 :   B  1050        B  1137                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.6977  35.1963  56.8852              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7118 T22:   0.4798                                     
REMARK   3      T33:   1.1089 T12:  -0.0766                                     
REMARK   3      T13:  -0.1385 T23:  -0.1848                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0896 L22:   1.9375                                     
REMARK   3      L33:   1.4434 L12:   1.0102                                     
REMARK   3      L13:  -1.2217 L23:  -1.4491                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0473 S12:   0.5289 S13:   0.0061                       
REMARK   3      S21:  -0.0873 S22:   0.1249 S23:   0.3275                       
REMARK   3      S31:   0.0945 S32:  -0.4276 S33:  -0.0775                       
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  1138        B  1193                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2364  52.8580  75.2797              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5451 T22:   0.6688                                     
REMARK   3      T33:   1.2684 T12:   0.2145                                     
REMARK   3      T13:   0.0579 T23:  -0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3120 L22:   1.3191                                     
REMARK   3      L33:   1.4697 L12:  -0.0176                                     
REMARK   3      L13:   0.6565 L23:  -0.2837                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0708 S12:   0.0732 S13:   0.0374                       
REMARK   3      S21:  -0.0754 S22:  -0.0695 S23:  -0.3666                       
REMARK   3      S31:   0.0647 S32:   0.0714 S33:  -0.0013                       
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 :   B  1194        B  1219                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9008  59.1027  60.2547              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9159 T22:   0.7171                                     
REMARK   3      T33:   1.3007 T12:  -0.2882                                     
REMARK   3      T13:  -0.0002 T23:   0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5780 L22:   2.7957                                     
REMARK   3      L33:   1.2561 L12:  -3.1456                                     
REMARK   3      L13:  -2.1109 L23:   1.8458                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1305 S12:  -0.2066 S13:  -0.1676                       
REMARK   3      S21:  -0.0483 S22:   0.1976 S23:   0.2826                       
REMARK   3      S31:   0.0211 S32:   0.1046 S33:  -0.0671                       
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 :   C  1001        C  1104                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.4542  85.3752 114.1325              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8896 T22:   0.9483                                     
REMARK   3      T33:   1.4332 T12:  -0.2117                                     
REMARK   3      T13:  -0.1983 T23:  -0.1497                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3008 L22:   1.3834                                     
REMARK   3      L33:   2.1865 L12:  -0.1807                                     
REMARK   3      L13:   0.5655 L23:  -1.3628                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1741 S12:  -0.0433 S13:   0.2627                       
REMARK   3      S21:  -0.2485 S22:  -0.3350 S23:  -0.4392                       
REMARK   3      S31:   0.7257 S32:   0.0942 S33:   0.1609                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C  1105        C  1150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.2128  63.8224 118.0449              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5567 T22:   0.7915                                     
REMARK   3      T33:   1.3479 T12:   0.0075                                     
REMARK   3      T13:  -0.2237 T23:  -0.1359                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0708 L22:   0.5071                                     
REMARK   3      L33:   3.2652 L12:   0.1356                                     
REMARK   3      L13:  -0.3956 L23:  -1.2619                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0866 S12:  -0.1004 S13:   0.0107                       
REMARK   3      S21:   0.1054 S22:  -0.0473 S23:  -0.1589                       
REMARK   3      S31:  -0.0810 S32:   0.3091 S33:   0.1339                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C  1151        C  1184                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0280  52.8727  99.1689              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6064 T22:   0.5460                                     
REMARK   3      T33:   1.1899 T12:  -0.0690                                     
REMARK   3      T13:  -0.0550 T23:  -0.0314                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6785 L22:   1.5832                                     
REMARK   3      L33:   3.1423 L12:  -1.0212                                     
REMARK   3      L13:   0.5370 L23:  -1.0329                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0380 S12:  -0.1859 S13:  -0.0658                       
REMARK   3      S21:   0.0554 S22:   0.2013 S23:   0.2220                       
REMARK   3      S31:   0.2583 S32:  -0.3595 S33:  -0.1633                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C  1185        C  1213                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.0172  48.5188 106.6970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5402 T22:   0.6034                                     
REMARK   3      T33:   1.1597 T12:  -0.0689                                     
REMARK   3      T13:   0.0303 T23:   0.0782                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8275 L22:   3.9009                                     
REMARK   3      L33:   0.2640 L12:  -0.7877                                     
REMARK   3      L13:  -0.5818 L23:  -0.2269                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1554 S12:  -0.2185 S13:  -0.0488                       
REMARK   3      S21:   0.2723 S22:   0.2470 S23:  -0.0366                       
REMARK   3      S31:   0.0516 S32:  -0.0066 S33:  -0.0915                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D  1001        D  1080                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.2592  94.0033 117.8833              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7806 T22:   0.7882                                     
REMARK   3      T33:   1.1190 T12:   0.1999                                     
REMARK   3      T13:   0.0801 T23:  -0.1117                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9671 L22:   1.6945                                     
REMARK   3      L33:   0.2884 L12:  -1.5373                                     
REMARK   3      L13:  -0.7470 L23:   0.5689                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0102 S12:  -0.2406 S13:   0.1215                       
REMARK   3      S21:  -0.1158 S22:   0.0228 S23:   0.3393                       
REMARK   3      S31:  -0.0440 S32:   0.0908 S33:  -0.0330                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D  1081        D  1155                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.3977  85.0965 112.4988              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6158 T22:   0.4618                                     
REMARK   3      T33:   1.2372 T12:  -0.1072                                     
REMARK   3      T13:  -0.0099 T23:  -0.2019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5174 L22:   0.2297                                     
REMARK   3      L33:   3.6211 L12:   0.2737                                     
REMARK   3      L13:  -1.3511 L23:  -0.8982                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0481 S12:  -0.3743 S13:  -0.1881                       
REMARK   3      S21:   0.0473 S22:   0.0968 S23:   0.0273                       
REMARK   3      S31:  -0.3117 S32:  -0.1781 S33:  -0.1449                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D  1156        D  1187                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.4009  72.2758  99.3869              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8330 T22:   0.5262                                     
REMARK   3      T33:   1.0693 T12:  -0.0510                                     
REMARK   3      T13:   0.1292 T23:  -0.0866                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1456 L22:   6.1593                                     
REMARK   3      L33:   4.8895 L12:   3.9090                                     
REMARK   3      L13:   4.4850 L23:   4.5084                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1623 S12:  -0.3186 S13:  -0.0032                       
REMARK   3      S21:   0.7060 S22:  -0.0110 S23:  -1.2838                       
REMARK   3      S31:   0.2127 S32:  -0.3606 S33:  -0.1513                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D  1188        D  1217                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.6361  67.5415 109.5248              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6102 T22:   0.7394                                     
REMARK   3      T33:   1.2560 T12:  -0.3000                                     
REMARK   3      T13:  -0.0272 T23:  -0.0236                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3578 L22:   1.1388                                     
REMARK   3      L33:   0.8911 L12:  -1.2224                                     
REMARK   3      L13:   1.0985 L23:  -0.9836                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0636 S12:  -0.2343 S13:  -0.0959                       
REMARK   3      S21:   0.0532 S22:   0.0887 S23:   0.0580                       
REMARK   3      S31:  -0.0670 S32:  -0.2111 S33:  -0.0251                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4EKW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071746.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.75                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL, SI(111)            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44951                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.210                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.08600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.050                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3RVY                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 78.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CHAPSO:DMPC BICELLES, 2 M AMMONIUM       
REMARK 280  SULPHATE, 0.1 M NA-CITRATE, 28% GLUCOSE, NICOTINIC ACID, PH 4.75,   
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z+1/2                                              
REMARK 290       4555   Y,-X,Z+1/2                                              
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       96.32050            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       96.32050            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15060 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 47950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -151.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      125.85600            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14640 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 47140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -169.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      125.85600            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MSE A   983                                                      
REMARK 465     ASP A   984                                                      
REMARK 465     TYR A   985                                                      
REMARK 465     LYS A   986                                                      
REMARK 465     ASP A   987                                                      
REMARK 465     ASP A   988                                                      
REMARK 465     ASP A   989                                                      
REMARK 465     ASP A   990                                                      
REMARK 465     LYS A   991                                                      
REMARK 465     GLY A   992                                                      
REMARK 465     SER A   993                                                      
REMARK 465     LEU A   994                                                      
REMARK 465     VAL A   995                                                      
REMARK 465     PRO A   996                                                      
REMARK 465     ARG A   997                                                      
REMARK 465     GLY A   998                                                      
REMARK 465     SER A   999                                                      
REMARK 465     HIS A  1000                                                      
REMARK 465     ALA A  1220                                                      
REMARK 465     MSE A  1221                                                      
REMARK 465     ALA A  1222                                                      
REMARK 465     ILE A  1223                                                      
REMARK 465     LEU A  1224                                                      
REMARK 465     ASN A  1225                                                      
REMARK 465     GLN A  1226                                                      
REMARK 465     LYS A  1227                                                      
REMARK 465     GLU A  1228                                                      
REMARK 465     GLU A  1229                                                      
REMARK 465     GLN A  1230                                                      
REMARK 465     HIS A  1231                                                      
REMARK 465     ILE A  1232                                                      
REMARK 465     ILE A  1233                                                      
REMARK 465     ASP A  1234                                                      
REMARK 465     GLU A  1235                                                      
REMARK 465     VAL A  1236                                                      
REMARK 465     GLN A  1237                                                      
REMARK 465     SER A  1238                                                      
REMARK 465     HIS A  1239                                                      
REMARK 465     GLU A  1240                                                      
REMARK 465     ASP A  1241                                                      
REMARK 465     ASN A  1242                                                      
REMARK 465     ILE A  1243                                                      
REMARK 465     ASN A  1244                                                      
REMARK 465     ASN A  1245                                                      
REMARK 465     GLU A  1246                                                      
REMARK 465     ILE A  1247                                                      
REMARK 465     ILE A  1248                                                      
REMARK 465     LYS A  1249                                                      
REMARK 465     LEU A  1250                                                      
REMARK 465     ARG A  1251                                                      
REMARK 465     GLU A  1252                                                      
REMARK 465     GLU A  1253                                                      
REMARK 465     ILE A  1254                                                      
REMARK 465     VAL A  1255                                                      
REMARK 465     GLU A  1256                                                      
REMARK 465     LEU A  1257                                                      
REMARK 465     LYS A  1258                                                      
REMARK 465     GLU A  1259                                                      
REMARK 465     LEU A  1260                                                      
REMARK 465     ILE A  1261                                                      
REMARK 465     LYS A  1262                                                      
REMARK 465     THR A  1263                                                      
REMARK 465     SER A  1264                                                      
REMARK 465     LEU A  1265                                                      
REMARK 465     LYS A  1266                                                      
REMARK 465     ASN A  1267                                                      
REMARK 465     MSE B   983                                                      
REMARK 465     ASP B   984                                                      
REMARK 465     TYR B   985                                                      
REMARK 465     LYS B   986                                                      
REMARK 465     ASP B   987                                                      
REMARK 465     ASP B   988                                                      
REMARK 465     ASP B   989                                                      
REMARK 465     ASP B   990                                                      
REMARK 465     LYS B   991                                                      
REMARK 465     GLY B   992                                                      
REMARK 465     SER B   993                                                      
REMARK 465     LEU B   994                                                      
REMARK 465     VAL B   995                                                      
REMARK 465     PRO B   996                                                      
REMARK 465     ARG B   997                                                      
REMARK 465     GLY B   998                                                      
REMARK 465     SER B   999                                                      
REMARK 465     HIS B  1000                                                      
REMARK 465     ALA B  1220                                                      
REMARK 465     MSE B  1221                                                      
REMARK 465     ALA B  1222                                                      
REMARK 465     ILE B  1223                                                      
REMARK 465     LEU B  1224                                                      
REMARK 465     ASN B  1225                                                      
REMARK 465     GLN B  1226                                                      
REMARK 465     LYS B  1227                                                      
REMARK 465     GLU B  1228                                                      
REMARK 465     GLU B  1229                                                      
REMARK 465     GLN B  1230                                                      
REMARK 465     HIS B  1231                                                      
REMARK 465     ILE B  1232                                                      
REMARK 465     ILE B  1233                                                      
REMARK 465     ASP B  1234                                                      
REMARK 465     GLU B  1235                                                      
REMARK 465     VAL B  1236                                                      
REMARK 465     GLN B  1237                                                      
REMARK 465     SER B  1238                                                      
REMARK 465     HIS B  1239                                                      
REMARK 465     GLU B  1240                                                      
REMARK 465     ASP B  1241                                                      
REMARK 465     ASN B  1242                                                      
REMARK 465     ILE B  1243                                                      
REMARK 465     ASN B  1244                                                      
REMARK 465     ASN B  1245                                                      
REMARK 465     GLU B  1246                                                      
REMARK 465     ILE B  1247                                                      
REMARK 465     ILE B  1248                                                      
REMARK 465     LYS B  1249                                                      
REMARK 465     LEU B  1250                                                      
REMARK 465     ARG B  1251                                                      
REMARK 465     GLU B  1252                                                      
REMARK 465     GLU B  1253                                                      
REMARK 465     ILE B  1254                                                      
REMARK 465     VAL B  1255                                                      
REMARK 465     GLU B  1256                                                      
REMARK 465     LEU B  1257                                                      
REMARK 465     LYS B  1258                                                      
REMARK 465     GLU B  1259                                                      
REMARK 465     LEU B  1260                                                      
REMARK 465     ILE B  1261                                                      
REMARK 465     LYS B  1262                                                      
REMARK 465     THR B  1263                                                      
REMARK 465     SER B  1264                                                      
REMARK 465     LEU B  1265                                                      
REMARK 465     LYS B  1266                                                      
REMARK 465     ASN B  1267                                                      
REMARK 465     MSE C   983                                                      
REMARK 465     ASP C   984                                                      
REMARK 465     TYR C   985                                                      
REMARK 465     LYS C   986                                                      
REMARK 465     ASP C   987                                                      
REMARK 465     ASP C   988                                                      
REMARK 465     ASP C   989                                                      
REMARK 465     ASP C   990                                                      
REMARK 465     LYS C   991                                                      
REMARK 465     GLY C   992                                                      
REMARK 465     SER C   993                                                      
REMARK 465     LEU C   994                                                      
REMARK 465     VAL C   995                                                      
REMARK 465     PRO C   996                                                      
REMARK 465     ARG C   997                                                      
REMARK 465     GLY C   998                                                      
REMARK 465     SER C   999                                                      
REMARK 465     HIS C  1000                                                      
REMARK 465     VAL C  1214                                                      
REMARK 465     ALA C  1215                                                      
REMARK 465     ILE C  1216                                                      
REMARK 465     ILE C  1217                                                      
REMARK 465     VAL C  1218                                                      
REMARK 465     ASP C  1219                                                      
REMARK 465     ALA C  1220                                                      
REMARK 465     MSE C  1221                                                      
REMARK 465     ALA C  1222                                                      
REMARK 465     ILE C  1223                                                      
REMARK 465     LEU C  1224                                                      
REMARK 465     ASN C  1225                                                      
REMARK 465     GLN C  1226                                                      
REMARK 465     LYS C  1227                                                      
REMARK 465     GLU C  1228                                                      
REMARK 465     GLU C  1229                                                      
REMARK 465     GLN C  1230                                                      
REMARK 465     HIS C  1231                                                      
REMARK 465     ILE C  1232                                                      
REMARK 465     ILE C  1233                                                      
REMARK 465     ASP C  1234                                                      
REMARK 465     GLU C  1235                                                      
REMARK 465     VAL C  1236                                                      
REMARK 465     GLN C  1237                                                      
REMARK 465     SER C  1238                                                      
REMARK 465     HIS C  1239                                                      
REMARK 465     GLU C  1240                                                      
REMARK 465     ASP C  1241                                                      
REMARK 465     ASN C  1242                                                      
REMARK 465     ILE C  1243                                                      
REMARK 465     ASN C  1244                                                      
REMARK 465     ASN C  1245                                                      
REMARK 465     GLU C  1246                                                      
REMARK 465     ILE C  1247                                                      
REMARK 465     ILE C  1248                                                      
REMARK 465     LYS C  1249                                                      
REMARK 465     LEU C  1250                                                      
REMARK 465     ARG C  1251                                                      
REMARK 465     GLU C  1252                                                      
REMARK 465     GLU C  1253                                                      
REMARK 465     ILE C  1254                                                      
REMARK 465     VAL C  1255                                                      
REMARK 465     GLU C  1256                                                      
REMARK 465     LEU C  1257                                                      
REMARK 465     LYS C  1258                                                      
REMARK 465     GLU C  1259                                                      
REMARK 465     LEU C  1260                                                      
REMARK 465     ILE C  1261                                                      
REMARK 465     LYS C  1262                                                      
REMARK 465     THR C  1263                                                      
REMARK 465     SER C  1264                                                      
REMARK 465     LEU C  1265                                                      
REMARK 465     LYS C  1266                                                      
REMARK 465     ASN C  1267                                                      
REMARK 465     MSE D   983                                                      
REMARK 465     ASP D   984                                                      
REMARK 465     TYR D   985                                                      
REMARK 465     LYS D   986                                                      
REMARK 465     ASP D   987                                                      
REMARK 465     ASP D   988                                                      
REMARK 465     ASP D   989                                                      
REMARK 465     ASP D   990                                                      
REMARK 465     LYS D   991                                                      
REMARK 465     GLY D   992                                                      
REMARK 465     SER D   993                                                      
REMARK 465     LEU D   994                                                      
REMARK 465     VAL D   995                                                      
REMARK 465     PRO D   996                                                      
REMARK 465     ARG D   997                                                      
REMARK 465     GLY D   998                                                      
REMARK 465     SER D   999                                                      
REMARK 465     HIS D  1000                                                      
REMARK 465     VAL D  1218                                                      
REMARK 465     ASP D  1219                                                      
REMARK 465     ALA D  1220                                                      
REMARK 465     MSE D  1221                                                      
REMARK 465     ALA D  1222                                                      
REMARK 465     ILE D  1223                                                      
REMARK 465     LEU D  1224                                                      
REMARK 465     ASN D  1225                                                      
REMARK 465     GLN D  1226                                                      
REMARK 465     LYS D  1227                                                      
REMARK 465     GLU D  1228                                                      
REMARK 465     GLU D  1229                                                      
REMARK 465     GLN D  1230                                                      
REMARK 465     HIS D  1231                                                      
REMARK 465     ILE D  1232                                                      
REMARK 465     ILE D  1233                                                      
REMARK 465     ASP D  1234                                                      
REMARK 465     GLU D  1235                                                      
REMARK 465     VAL D  1236                                                      
REMARK 465     GLN D  1237                                                      
REMARK 465     SER D  1238                                                      
REMARK 465     HIS D  1239                                                      
REMARK 465     GLU D  1240                                                      
REMARK 465     ASP D  1241                                                      
REMARK 465     ASN D  1242                                                      
REMARK 465     ILE D  1243                                                      
REMARK 465     ASN D  1244                                                      
REMARK 465     ASN D  1245                                                      
REMARK 465     GLU D  1246                                                      
REMARK 465     ILE D  1247                                                      
REMARK 465     ILE D  1248                                                      
REMARK 465     LYS D  1249                                                      
REMARK 465     LEU D  1250                                                      
REMARK 465     ARG D  1251                                                      
REMARK 465     GLU D  1252                                                      
REMARK 465     GLU D  1253                                                      
REMARK 465     ILE D  1254                                                      
REMARK 465     VAL D  1255                                                      
REMARK 465     GLU D  1256                                                      
REMARK 465     LEU D  1257                                                      
REMARK 465     LYS D  1258                                                      
REMARK 465     GLU D  1259                                                      
REMARK 465     LEU D  1260                                                      
REMARK 465     ILE D  1261                                                      
REMARK 465     LYS D  1262                                                      
REMARK 465     THR D  1263                                                      
REMARK 465     SER D  1264                                                      
REMARK 465     LEU D  1265                                                      
REMARK 465     LYS D  1266                                                      
REMARK 465     ASN D  1267                                                      
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   OG   SER A  1180     OE2  GLU B  1177     2565     2.09            
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 A1008      -64.24   -103.26                                   
REMARK 500    SER A1040      -36.40   -147.32                                   
REMARK 500    ARG A1068      -91.93     42.53                                   
REMARK 500    PHE A1071      -60.02    -94.61                                   
REMARK 500    PHE A1072       15.66    -68.02                                   
REMARK 500    LYS A1073       25.91   -140.02                                   
REMARK 500    THR A1091        5.52    -61.08                                   
REMARK 500    SER A1092     -144.18   -143.48                                   
REMARK 500    SER A1093      132.65     64.99                                   
REMARK 500    SER A1132      -19.25    -49.66                                   
REMARK 500    PHE A1141      -70.00    -51.99                                   
REMARK 500    ALA A1148       39.64    -79.60                                   
REMARK 500    LEU A1176       -3.52     71.41                                   
REMARK 500    SER A1178       53.05     71.23                                   
REMARK 500    SER A1180      -96.20    -75.32                                   
REMARK 500    MSE A1181      -15.42    -48.02                                   
REMARK 500    GLU A1189      -18.57    -49.91                                   
REMARK 500    PHE A1203      -70.46    -52.10                                   
REMARK 500    SER B1034      132.46    -39.92                                   
REMARK 500    LYS B1035       40.70    -93.13                                   
REMARK 500    THR B1036      -40.40   -148.14                                   
REMARK 500    SER B1040      -69.33   -133.30                                   
REMARK 500    PHE B1041       49.19    -76.79                                   
REMARK 500    TYR B1065       26.36    -71.85                                   
REMARK 500    PHE B1072       32.27    -73.92                                   
REMARK 500    SER B1077      -71.42    -79.98                                   
REMARK 500    PHE B1079      -71.50    -60.21                                   
REMARK 500    PHE B1081      -75.03    -46.26                                   
REMARK 500    PRO B1090      176.00    -53.55                                   
REMARK 500    PHE B1107       24.79    -69.36                                   
REMARK 500    SER B1125        0.89    -67.19                                   
REMARK 500    LEU B1151      -71.15    -99.81                                   
REMARK 500    PHE B1152      -77.80    -61.09                                   
REMARK 500    PRO B1157      -71.62    -68.95                                   
REMARK 500    PHE B1160       26.90   -143.68                                   
REMARK 500    ILE B1183      -77.70   -137.05                                   
REMARK 500    VAL B1190      -74.30   -100.00                                   
REMARK 500    PRO B1192       25.77    -78.64                                   
REMARK 500    VAL B1205      -73.25    -62.97                                   
REMARK 500    VAL C1009      -78.70   -103.73                                   
REMARK 500    GLU C1010      -19.10    -45.87                                   
REMARK 500    GLU C1032       -8.19    -54.66                                   
REMARK 500    ARG C1068      -89.84     57.02                                   
REMARK 500    SER C1093      138.02     72.09                                   
REMARK 500    LEU C1109        1.34    -68.34                                   
REMARK 500    ILE C1124      -70.38    -58.91                                   
REMARK 500    SER C1125       27.18    -64.66                                   
REMARK 500    ALA C1148      -83.18    -53.44                                   
REMARK 500    LEU C1163      -42.63    -29.03                                   
REMARK 500    PHE C1167      -76.30    -56.75                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      64 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PX4 A 1301                                                       
REMARK 610     PX4 B 1301                                                       
REMARK 610     PX4 B 1302                                                       
REMARK 610     PX4 C 1301                                                       
REMARK 610     PX4 D 1301                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PX4 A 1301                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1302                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PX4 B 1301                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PX4 B 1302                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1303                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PX4 C 1301                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 1302                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PX4 D 1301                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 1302                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3RVY   RELATED DB: PDB                                   
REMARK 900 NAVAB, I217C                                                         
REMARK 900 RELATED ID: 3RVZ   RELATED DB: PDB                                   
REMARK 900 NAVAB, I217C                                                         
REMARK 900 RELATED ID: 3RW0   RELATED DB: PDB                                   
REMARK 900 NAVAB, M221C                                                         
DBREF  4EKW A 1001  1267  UNP    A8EVM5   A8EVM5_ARCB4     1    267             
DBREF  4EKW B 1001  1267  UNP    A8EVM5   A8EVM5_ARCB4     1    267             
DBREF  4EKW C 1001  1267  UNP    A8EVM5   A8EVM5_ARCB4     1    267             
DBREF  4EKW D 1001  1267  UNP    A8EVM5   A8EVM5_ARCB4     1    267             
SEQADV 4EKW MSE A  983  UNP  A8EVM5              INITIATING METHIONINE          
SEQADV 4EKW ASP A  984  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW TYR A  985  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW LYS A  986  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ASP A  987  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ASP A  988  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ASP A  989  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ASP A  990  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW LYS A  991  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW GLY A  992  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW SER A  993  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW LEU A  994  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW VAL A  995  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW PRO A  996  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ARG A  997  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW GLY A  998  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW SER A  999  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW HIS A 1000  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW MSE B  983  UNP  A8EVM5              INITIATING METHIONINE          
SEQADV 4EKW ASP B  984  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW TYR B  985  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW LYS B  986  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ASP B  987  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ASP B  988  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ASP B  989  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ASP B  990  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW LYS B  991  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW GLY B  992  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW SER B  993  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW LEU B  994  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW VAL B  995  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW PRO B  996  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ARG B  997  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW GLY B  998  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW SER B  999  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW HIS B 1000  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW MSE C  983  UNP  A8EVM5              INITIATING METHIONINE          
SEQADV 4EKW ASP C  984  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW TYR C  985  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW LYS C  986  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ASP C  987  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ASP C  988  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ASP C  989  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ASP C  990  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW LYS C  991  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW GLY C  992  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW SER C  993  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW LEU C  994  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW VAL C  995  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW PRO C  996  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ARG C  997  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW GLY C  998  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW SER C  999  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW HIS C 1000  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW MSE D  983  UNP  A8EVM5              INITIATING METHIONINE          
SEQADV 4EKW ASP D  984  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW TYR D  985  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW LYS D  986  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ASP D  987  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ASP D  988  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ASP D  989  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ASP D  990  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW LYS D  991  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW GLY D  992  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW SER D  993  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW LEU D  994  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW VAL D  995  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW PRO D  996  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW ARG D  997  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW GLY D  998  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW SER D  999  UNP  A8EVM5              EXPRESSION TAG                 
SEQADV 4EKW HIS D 1000  UNP  A8EVM5              EXPRESSION TAG                 
SEQRES   1 A  285  MSE ASP TYR LYS ASP ASP ASP ASP LYS GLY SER LEU VAL          
SEQRES   2 A  285  PRO ARG GLY SER HIS MSE TYR LEU ARG ILE THR ASN ILE          
SEQRES   3 A  285  VAL GLU SER SER PHE PHE THR LYS PHE ILE ILE TYR LEU          
SEQRES   4 A  285  ILE VAL LEU ASN GLY ILE THR MSE GLY LEU GLU THR SER          
SEQRES   5 A  285  LYS THR PHE MSE GLN SER PHE GLY VAL TYR THR THR LEU          
SEQRES   6 A  285  PHE ASN GLN ILE VAL ILE THR ILE PHE THR ILE GLU ILE          
SEQRES   7 A  285  ILE LEU ARG ILE TYR VAL HIS ARG ILE SER PHE PHE LYS          
SEQRES   8 A  285  ASP PRO TRP SER LEU PHE ASP PHE PHE VAL VAL ALA ILE          
SEQRES   9 A  285  SER LEU VAL PRO THR SER SER GLY PHE GLU ILE LEU ARG          
SEQRES  10 A  285  VAL LEU ARG VAL LEU ARG LEU PHE ARG LEU VAL THR ALA          
SEQRES  11 A  285  VAL PRO GLN MSE ARG LYS ILE VAL SER ALA LEU ILE SER          
SEQRES  12 A  285  VAL ILE PRO GLY MSE LEU SER VAL ILE ALA LEU MSE THR          
SEQRES  13 A  285  LEU PHE PHE TYR ILE PHE ALA ILE MSE ALA THR GLN LEU          
SEQRES  14 A  285  PHE GLY GLU ARG PHE PRO GLU TRP PHE GLY THR LEU GLY          
SEQRES  15 A  285  GLU SER PHE TYR THR LEU PHE GLN VAL MSE THR LEU GLU          
SEQRES  16 A  285  SER TRP SER MSE GLY ILE VAL ARG PRO LEU MSE GLU VAL          
SEQRES  17 A  285  TYR PRO TYR ALA TRP VAL PHE PHE ILE PRO PHE ILE PHE          
SEQRES  18 A  285  VAL VAL THR PHE VAL MSE ILE ASN LEU VAL VAL ALA ILE          
SEQRES  19 A  285  ILE VAL ASP ALA MSE ALA ILE LEU ASN GLN LYS GLU GLU          
SEQRES  20 A  285  GLN HIS ILE ILE ASP GLU VAL GLN SER HIS GLU ASP ASN          
SEQRES  21 A  285  ILE ASN ASN GLU ILE ILE LYS LEU ARG GLU GLU ILE VAL          
SEQRES  22 A  285  GLU LEU LYS GLU LEU ILE LYS THR SER LEU LYS ASN              
SEQRES   1 B  285  MSE ASP TYR LYS ASP ASP ASP ASP LYS GLY SER LEU VAL          
SEQRES   2 B  285  PRO ARG GLY SER HIS MSE TYR LEU ARG ILE THR ASN ILE          
SEQRES   3 B  285  VAL GLU SER SER PHE PHE THR LYS PHE ILE ILE TYR LEU          
SEQRES   4 B  285  ILE VAL LEU ASN GLY ILE THR MSE GLY LEU GLU THR SER          
SEQRES   5 B  285  LYS THR PHE MSE GLN SER PHE GLY VAL TYR THR THR LEU          
SEQRES   6 B  285  PHE ASN GLN ILE VAL ILE THR ILE PHE THR ILE GLU ILE          
SEQRES   7 B  285  ILE LEU ARG ILE TYR VAL HIS ARG ILE SER PHE PHE LYS          
SEQRES   8 B  285  ASP PRO TRP SER LEU PHE ASP PHE PHE VAL VAL ALA ILE          
SEQRES   9 B  285  SER LEU VAL PRO THR SER SER GLY PHE GLU ILE LEU ARG          
SEQRES  10 B  285  VAL LEU ARG VAL LEU ARG LEU PHE ARG LEU VAL THR ALA          
SEQRES  11 B  285  VAL PRO GLN MSE ARG LYS ILE VAL SER ALA LEU ILE SER          
SEQRES  12 B  285  VAL ILE PRO GLY MSE LEU SER VAL ILE ALA LEU MSE THR          
SEQRES  13 B  285  LEU PHE PHE TYR ILE PHE ALA ILE MSE ALA THR GLN LEU          
SEQRES  14 B  285  PHE GLY GLU ARG PHE PRO GLU TRP PHE GLY THR LEU GLY          
SEQRES  15 B  285  GLU SER PHE TYR THR LEU PHE GLN VAL MSE THR LEU GLU          
SEQRES  16 B  285  SER TRP SER MSE GLY ILE VAL ARG PRO LEU MSE GLU VAL          
SEQRES  17 B  285  TYR PRO TYR ALA TRP VAL PHE PHE ILE PRO PHE ILE PHE          
SEQRES  18 B  285  VAL VAL THR PHE VAL MSE ILE ASN LEU VAL VAL ALA ILE          
SEQRES  19 B  285  ILE VAL ASP ALA MSE ALA ILE LEU ASN GLN LYS GLU GLU          
SEQRES  20 B  285  GLN HIS ILE ILE ASP GLU VAL GLN SER HIS GLU ASP ASN          
SEQRES  21 B  285  ILE ASN ASN GLU ILE ILE LYS LEU ARG GLU GLU ILE VAL          
SEQRES  22 B  285  GLU LEU LYS GLU LEU ILE LYS THR SER LEU LYS ASN              
SEQRES   1 C  285  MSE ASP TYR LYS ASP ASP ASP ASP LYS GLY SER LEU VAL          
SEQRES   2 C  285  PRO ARG GLY SER HIS MSE TYR LEU ARG ILE THR ASN ILE          
SEQRES   3 C  285  VAL GLU SER SER PHE PHE THR LYS PHE ILE ILE TYR LEU          
SEQRES   4 C  285  ILE VAL LEU ASN GLY ILE THR MSE GLY LEU GLU THR SER          
SEQRES   5 C  285  LYS THR PHE MSE GLN SER PHE GLY VAL TYR THR THR LEU          
SEQRES   6 C  285  PHE ASN GLN ILE VAL ILE THR ILE PHE THR ILE GLU ILE          
SEQRES   7 C  285  ILE LEU ARG ILE TYR VAL HIS ARG ILE SER PHE PHE LYS          
SEQRES   8 C  285  ASP PRO TRP SER LEU PHE ASP PHE PHE VAL VAL ALA ILE          
SEQRES   9 C  285  SER LEU VAL PRO THR SER SER GLY PHE GLU ILE LEU ARG          
SEQRES  10 C  285  VAL LEU ARG VAL LEU ARG LEU PHE ARG LEU VAL THR ALA          
SEQRES  11 C  285  VAL PRO GLN MSE ARG LYS ILE VAL SER ALA LEU ILE SER          
SEQRES  12 C  285  VAL ILE PRO GLY MSE LEU SER VAL ILE ALA LEU MSE THR          
SEQRES  13 C  285  LEU PHE PHE TYR ILE PHE ALA ILE MSE ALA THR GLN LEU          
SEQRES  14 C  285  PHE GLY GLU ARG PHE PRO GLU TRP PHE GLY THR LEU GLY          
SEQRES  15 C  285  GLU SER PHE TYR THR LEU PHE GLN VAL MSE THR LEU GLU          
SEQRES  16 C  285  SER TRP SER MSE GLY ILE VAL ARG PRO LEU MSE GLU VAL          
SEQRES  17 C  285  TYR PRO TYR ALA TRP VAL PHE PHE ILE PRO PHE ILE PHE          
SEQRES  18 C  285  VAL VAL THR PHE VAL MSE ILE ASN LEU VAL VAL ALA ILE          
SEQRES  19 C  285  ILE VAL ASP ALA MSE ALA ILE LEU ASN GLN LYS GLU GLU          
SEQRES  20 C  285  GLN HIS ILE ILE ASP GLU VAL GLN SER HIS GLU ASP ASN          
SEQRES  21 C  285  ILE ASN ASN GLU ILE ILE LYS LEU ARG GLU GLU ILE VAL          
SEQRES  22 C  285  GLU LEU LYS GLU LEU ILE LYS THR SER LEU LYS ASN              
SEQRES   1 D  285  MSE ASP TYR LYS ASP ASP ASP ASP LYS GLY SER LEU VAL          
SEQRES   2 D  285  PRO ARG GLY SER HIS MSE TYR LEU ARG ILE THR ASN ILE          
SEQRES   3 D  285  VAL GLU SER SER PHE PHE THR LYS PHE ILE ILE TYR LEU          
SEQRES   4 D  285  ILE VAL LEU ASN GLY ILE THR MSE GLY LEU GLU THR SER          
SEQRES   5 D  285  LYS THR PHE MSE GLN SER PHE GLY VAL TYR THR THR LEU          
SEQRES   6 D  285  PHE ASN GLN ILE VAL ILE THR ILE PHE THR ILE GLU ILE          
SEQRES   7 D  285  ILE LEU ARG ILE TYR VAL HIS ARG ILE SER PHE PHE LYS          
SEQRES   8 D  285  ASP PRO TRP SER LEU PHE ASP PHE PHE VAL VAL ALA ILE          
SEQRES   9 D  285  SER LEU VAL PRO THR SER SER GLY PHE GLU ILE LEU ARG          
SEQRES  10 D  285  VAL LEU ARG VAL LEU ARG LEU PHE ARG LEU VAL THR ALA          
SEQRES  11 D  285  VAL PRO GLN MSE ARG LYS ILE VAL SER ALA LEU ILE SER          
SEQRES  12 D  285  VAL ILE PRO GLY MSE LEU SER VAL ILE ALA LEU MSE THR          
SEQRES  13 D  285  LEU PHE PHE TYR ILE PHE ALA ILE MSE ALA THR GLN LEU          
SEQRES  14 D  285  PHE GLY GLU ARG PHE PRO GLU TRP PHE GLY THR LEU GLY          
SEQRES  15 D  285  GLU SER PHE TYR THR LEU PHE GLN VAL MSE THR LEU GLU          
SEQRES  16 D  285  SER TRP SER MSE GLY ILE VAL ARG PRO LEU MSE GLU VAL          
SEQRES  17 D  285  TYR PRO TYR ALA TRP VAL PHE PHE ILE PRO PHE ILE PHE          
SEQRES  18 D  285  VAL VAL THR PHE VAL MSE ILE ASN LEU VAL VAL ALA ILE          
SEQRES  19 D  285  ILE VAL ASP ALA MSE ALA ILE LEU ASN GLN LYS GLU GLU          
SEQRES  20 D  285  GLN HIS ILE ILE ASP GLU VAL GLN SER HIS GLU ASP ASN          
SEQRES  21 D  285  ILE ASN ASN GLU ILE ILE LYS LEU ARG GLU GLU ILE VAL          
SEQRES  22 D  285  GLU LEU LYS GLU LEU ILE LYS THR SER LEU LYS ASN              
MODRES 4EKW MSE A 1001  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE A 1029  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE A 1038  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE A 1116  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE A 1130  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE A 1137  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE A 1147  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE A 1174  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE A 1181  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE A 1188  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE A 1209  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE B 1001  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE B 1029  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE B 1038  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE B 1116  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE B 1130  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE B 1137  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE B 1147  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE B 1174  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE B 1181  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE B 1188  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE B 1209  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE C 1001  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE C 1029  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE C 1038  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE C 1116  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE C 1130  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE C 1137  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE C 1147  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE C 1174  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE C 1181  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE C 1188  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE C 1209  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE D 1001  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE D 1029  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE D 1038  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE D 1116  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE D 1130  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE D 1137  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE D 1147  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE D 1174  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE D 1181  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE D 1188  MET  SELENOMETHIONINE                                   
MODRES 4EKW MSE D 1209  MET  SELENOMETHIONINE                                   
HET    MSE  A1001       8                                                       
HET    MSE  A1029       8                                                       
HET    MSE  A1038       8                                                       
HET    MSE  A1116       8                                                       
HET    MSE  A1130       8                                                       
HET    MSE  A1137       8                                                       
HET    MSE  A1147       8                                                       
HET    MSE  A1174       8                                                       
HET    MSE  A1181       8                                                       
HET    MSE  A1188       8                                                       
HET    MSE  A1209       8                                                       
HET    MSE  B1001       8                                                       
HET    MSE  B1029       8                                                       
HET    MSE  B1038       8                                                       
HET    MSE  B1116       8                                                       
HET    MSE  B1130       8                                                       
HET    MSE  B1137       8                                                       
HET    MSE  B1147       8                                                       
HET    MSE  B1174       8                                                       
HET    MSE  B1181       8                                                       
HET    MSE  B1188       8                                                       
HET    MSE  B1209       8                                                       
HET    MSE  C1001       8                                                       
HET    MSE  C1029       8                                                       
HET    MSE  C1038       8                                                       
HET    MSE  C1116       8                                                       
HET    MSE  C1130       8                                                       
HET    MSE  C1137       8                                                       
HET    MSE  C1147       8                                                       
HET    MSE  C1174       8                                                       
HET    MSE  C1181       8                                                       
HET    MSE  C1188       8                                                       
HET    MSE  C1209       8                                                       
HET    MSE  D1001       8                                                       
HET    MSE  D1029       8                                                       
HET    MSE  D1038       8                                                       
HET    MSE  D1116       8                                                       
HET    MSE  D1130       8                                                       
HET    MSE  D1137       8                                                       
HET    MSE  D1147       8                                                       
HET    MSE  D1174       8                                                       
HET    MSE  D1181       8                                                       
HET    MSE  D1188       8                                                       
HET    MSE  D1209       8                                                       
HET    PX4  A1301      14                                                       
HET    PO4  A1302       5                                                       
HET    PX4  B1301       9                                                       
HET    PX4  B1302       6                                                       
HET    PO4  B1303       5                                                       
HET    PX4  C1301      20                                                       
HET    PO4  C1302       5                                                       
HET    PX4  D1301       8                                                       
HET    PO4  D1302       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     PX4 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE                      
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   1  MSE    44(C5 H11 N O2 SE)                                           
FORMUL   5  PX4    5(C36 H73 N O8 P 1+)                                         
FORMUL   6  PO4    4(O4 P 3-)                                                   
FORMUL  14  HOH   *3(H2 O)                                                      
HELIX    1   1 MSE A 1001  GLU A 1010  1                                  10    
HELIX    2   2 SER A 1011  LEU A 1031  1                                  21    
HELIX    3   3 PHE A 1041  TYR A 1065  1                                  25    
HELIX    4   4 HIS A 1067  PHE A 1071  5                                   5    
HELIX    5   5 ASP A 1074  ILE A 1086  1                                  13    
HELIX    6   6 VAL A 1100  LEU A 1104  5                                   5    
HELIX    7   7 PHE A 1107  ALA A 1112  1                                   6    
HELIX    8   8 VAL A 1113  SER A 1125  1                                  13    
HELIX    9   9 VAL A 1126  LEU A 1151  1                                  26    
HELIX   10  10 THR A 1162  THR A 1175  1                                  14    
HELIX   11  11 ILE A 1183  GLU A 1189  1                                   7    
HELIX   12  12 TYR A 1193  ASP A 1219  1                                  27    
HELIX   13  13 ILE B 1005  GLU B 1010  1                                   6    
HELIX   14  14 SER B 1011  GLY B 1030  1                                  20    
HELIX   15  15 THR B 1036  SER B 1040  5                                   5    
HELIX   16  16 PHE B 1041  TYR B 1065  1                                  25    
HELIX   17  17 HIS B 1067  PHE B 1072  1                                   6    
HELIX   18  18 TRP B 1076  VAL B 1089  1                                  14    
HELIX   19  19 PHE B 1095  LEU B 1101  1                                   7    
HELIX   20  20 ARG B 1102  LEU B 1106  5                                   5    
HELIX   21  21 PHE B 1107  ALA B 1112  1                                   6    
HELIX   22  22 VAL B 1113  SER B 1125  1                                  13    
HELIX   23  23 VAL B 1126  GLY B 1129  5                                   4    
HELIX   24  24 MSE B 1130  TYR B 1142  1                                  13    
HELIX   25  25 TYR B 1142  LEU B 1151  1                                  10    
HELIX   26  26 PHE B 1156  GLY B 1161  1                                   6    
HELIX   27  27 THR B 1162  LEU B 1176  1                                  15    
HELIX   28  28 ILE B 1183  GLU B 1189  1                                   7    
HELIX   29  29 TYR B 1193  VAL B 1214  1                                  22    
HELIX   30  30 VAL B 1214  ASP B 1219  1                                   6    
HELIX   31  31 TYR C 1002  ASN C 1007  1                                   6    
HELIX   32  32 SER C 1011  GLY C 1030  1                                  20    
HELIX   33  33 THR C 1036  PHE C 1041  1                                   6    
HELIX   34  34 PHE C 1041  ARG C 1068  1                                  28    
HELIX   35  35 ILE C 1069  PHE C 1071  5                                   3    
HELIX   36  36 ASP C 1074  VAL C 1089  1                                  16    
HELIX   37  37 GLU C 1096  LEU C 1101  1                                   6    
HELIX   38  38 ARG C 1102  LEU C 1104  5                                   3    
HELIX   39  39 ARG C 1105  LEU C 1106  5                                   2    
HELIX   40  40 PHE C 1107  ALA C 1112  1                                   6    
HELIX   41  41 PRO C 1114  SER C 1125  1                                  12    
HELIX   42  42 VAL C 1126  LEU C 1131  1                                   6    
HELIX   43  43 ALA C 1135  GLY C 1153  1                                  19    
HELIX   44  44 PHE C 1156  GLY C 1161  1                                   6    
HELIX   45  45 THR C 1162  THR C 1175  1                                  14    
HELIX   46  46 ILE C 1183  GLU C 1189  1                                   7    
HELIX   47  47 ALA C 1194  VAL C 1213  1                                  20    
HELIX   48  48 ILE D 1005  GLU D 1010  1                                   6    
HELIX   49  49 SER D 1011  GLU D 1032  1                                  22    
HELIX   50  50 SER D 1034  SER D 1040  1                                   7    
HELIX   51  51 PHE D 1041  TYR D 1065  1                                  25    
HELIX   52  52 HIS D 1067  PHE D 1072  1                                   6    
HELIX   53  53 SER D 1077  PHE D 1082  1                                   6    
HELIX   54  54 VAL D 1083  VAL D 1089  1                                   7    
HELIX   55  55 GLU D 1096  LEU D 1101  1                                   6    
HELIX   56  56 VAL D 1103  LEU D 1106  5                                   4    
HELIX   57  57 PHE D 1107  VAL D 1113  1                                   7    
HELIX   58  58 GLN D 1115  GLY D 1153  1                                  39    
HELIX   59  59 THR D 1162  THR D 1175  1                                  14    
HELIX   60  60 TRP D 1179  VAL D 1184  1                                   6    
HELIX   61  61 VAL D 1184  GLU D 1189  1                                   6    
HELIX   62  62 ILE D 1199  ALA D 1215  1                                  17    
LINK         C   MSE A1001                 N   TYR A1002     1555   1555  1.34  
LINK         C   THR A1028                 N   MSE A1029     1555   1555  1.34  
LINK         C   MSE A1029                 N   GLY A1030     1555   1555  1.33  
LINK         C   PHE A1037                 N   MSE A1038     1555   1555  1.33  
LINK         C   MSE A1038                 N   GLN A1039     1555   1555  1.33  
LINK         C   GLN A1115                 N   MSE A1116     1555   1555  1.33  
LINK         C   MSE A1116                 N   ARG A1117     1555   1555  1.34  
LINK         C   GLY A1129                 N   MSE A1130     1555   1555  1.33  
LINK         C   MSE A1130                 N   LEU A1131     1555   1555  1.33  
LINK         C   LEU A1136                 N   MSE A1137     1555   1555  1.34  
LINK         C   MSE A1137                 N   THR A1138     1555   1555  1.34  
LINK         C   ILE A1146                 N   MSE A1147     1555   1555  1.34  
LINK         C   MSE A1147                 N   ALA A1148     1555   1555  1.33  
LINK         C   VAL A1173                 N   MSE A1174     1555   1555  1.33  
LINK         C   MSE A1174                 N   THR A1175     1555   1555  1.34  
LINK         C   SER A1180                 N   MSE A1181     1555   1555  1.34  
LINK         C   MSE A1181                 N   GLY A1182     1555   1555  1.34  
LINK         C   LEU A1187                 N   MSE A1188     1555   1555  1.33  
LINK         C   MSE A1188                 N   GLU A1189     1555   1555  1.33  
LINK         C   VAL A1208                 N   MSE A1209     1555   1555  1.34  
LINK         C   MSE A1209                 N   ILE A1210     1555   1555  1.33  
LINK         C   MSE B1001                 N   TYR B1002     1555   1555  1.34  
LINK         C   THR B1028                 N   MSE B1029     1555   1555  1.33  
LINK         C   MSE B1029                 N   GLY B1030     1555   1555  1.33  
LINK         C   PHE B1037                 N   MSE B1038     1555   1555  1.34  
LINK         C   MSE B1038                 N   GLN B1039     1555   1555  1.33  
LINK         C   GLN B1115                 N   MSE B1116     1555   1555  1.34  
LINK         C   MSE B1116                 N   ARG B1117     1555   1555  1.34  
LINK         C   GLY B1129                 N   MSE B1130     1555   1555  1.33  
LINK         C   MSE B1130                 N   LEU B1131     1555   1555  1.34  
LINK         C   LEU B1136                 N   MSE B1137     1555   1555  1.33  
LINK         C   MSE B1137                 N   THR B1138     1555   1555  1.34  
LINK         C   ILE B1146                 N   MSE B1147     1555   1555  1.34  
LINK         C   MSE B1147                 N   ALA B1148     1555   1555  1.33  
LINK         C   VAL B1173                 N   MSE B1174     1555   1555  1.34  
LINK         C   MSE B1174                 N   THR B1175     1555   1555  1.34  
LINK         C   SER B1180                 N   MSE B1181     1555   1555  1.34  
LINK         C   MSE B1181                 N   GLY B1182     1555   1555  1.34  
LINK         C   LEU B1187                 N   MSE B1188     1555   1555  1.33  
LINK         C   MSE B1188                 N   GLU B1189     1555   1555  1.33  
LINK         C   VAL B1208                 N   MSE B1209     1555   1555  1.33  
LINK         C   MSE B1209                 N   ILE B1210     1555   1555  1.33  
LINK         C   MSE C1001                 N   TYR C1002     1555   1555  1.34  
LINK         C   THR C1028                 N   MSE C1029     1555   1555  1.34  
LINK         C   MSE C1029                 N   GLY C1030     1555   1555  1.34  
LINK         C   PHE C1037                 N   MSE C1038     1555   1555  1.33  
LINK         C   MSE C1038                 N   GLN C1039     1555   1555  1.33  
LINK         C   GLN C1115                 N   MSE C1116     1555   1555  1.33  
LINK         C   MSE C1116                 N   ARG C1117     1555   1555  1.34  
LINK         C   GLY C1129                 N   MSE C1130     1555   1555  1.33  
LINK         C   MSE C1130                 N   LEU C1131     1555   1555  1.34  
LINK         C   LEU C1136                 N   MSE C1137     1555   1555  1.33  
LINK         C   MSE C1137                 N   THR C1138     1555   1555  1.33  
LINK         C   ILE C1146                 N   MSE C1147     1555   1555  1.33  
LINK         C   MSE C1147                 N   ALA C1148     1555   1555  1.33  
LINK         C   VAL C1173                 N   MSE C1174     1555   1555  1.33  
LINK         C   MSE C1174                 N   THR C1175     1555   1555  1.33  
LINK         C   SER C1180                 N   MSE C1181     1555   1555  1.34  
LINK         C   MSE C1181                 N   GLY C1182     1555   1555  1.34  
LINK         C   LEU C1187                 N   MSE C1188     1555   1555  1.34  
LINK         C   MSE C1188                 N   GLU C1189     1555   1555  1.34  
LINK         C   VAL C1208                 N   MSE C1209     1555   1555  1.34  
LINK         C   MSE C1209                 N   ILE C1210     1555   1555  1.34  
LINK         C   MSE D1001                 N   TYR D1002     1555   1555  1.34  
LINK         C   THR D1028                 N   MSE D1029     1555   1555  1.34  
LINK         C   MSE D1029                 N   GLY D1030     1555   1555  1.33  
LINK         C   PHE D1037                 N   MSE D1038     1555   1555  1.33  
LINK         C   MSE D1038                 N   GLN D1039     1555   1555  1.34  
LINK         C   GLN D1115                 N   MSE D1116     1555   1555  1.33  
LINK         C   MSE D1116                 N   ARG D1117     1555   1555  1.34  
LINK         C   GLY D1129                 N   MSE D1130     1555   1555  1.34  
LINK         C   MSE D1130                 N   LEU D1131     1555   1555  1.33  
LINK         C   LEU D1136                 N   MSE D1137     1555   1555  1.33  
LINK         C   MSE D1137                 N   THR D1138     1555   1555  1.34  
LINK         C   ILE D1146                 N   MSE D1147     1555   1555  1.34  
LINK         C   MSE D1147                 N   ALA D1148     1555   1555  1.34  
LINK         C   VAL D1173                 N   MSE D1174     1555   1555  1.34  
LINK         C   MSE D1174                 N   THR D1175     1555   1555  1.34  
LINK         C   SER D1180                 N   MSE D1181     1555   1555  1.35  
LINK         C   MSE D1181                 N   GLY D1182     1555   1555  1.33  
LINK         C   LEU D1187                 N   MSE D1188     1555   1555  1.32  
LINK         C   MSE D1188                 N   GLU D1189     1555   1555  1.33  
LINK         C   VAL D1208                 N   MSE D1209     1555   1555  1.34  
LINK         C   MSE D1209                 N   ILE D1210     1555   1555  1.34  
SITE     1 AC1  4 GLY A1164  GLU A1165  TRP B1195  ILE B1199                    
SITE     1 AC2  1 SER A1034                                                     
SITE     1 AC3  2 TRP A1195  GLY B1164                                          
SITE     1 AC4  1 TYR A1191                                                     
SITE     1 AC5  1 TYR B1193                                                     
SITE     1 AC6  4 GLY C1164  PHE C1167  TYR C1168  TRP D1195                    
SITE     1 AC7  2 ILE C1097  LEU D1151                                          
SITE     1 AC8  3 VAL C1190  TYR C1191  PRO C1192                               
SITE     1 AC9  2 TRP C1195  GLY D1164                                          
CRYST1  125.856  125.856  192.641  90.00  90.00  90.00 P 42         16          
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      0.007946  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007946  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005191        0.00000                         
HETATM    1  N   MSE A1001      49.228  34.775  45.936  1.00122.09           N  
ANISOU    1  N   MSE A1001    12817  14528  19043   2590   1709  -1523       N  
HETATM    2  CA  MSE A1001      48.048  33.940  46.313  1.00123.98           C  
ANISOU    2  CA  MSE A1001    13121  14662  19322   2658   1696  -1463       C  
HETATM    3  C   MSE A1001      46.777  34.674  45.964  1.00121.88           C  
ANISOU    3  C   MSE A1001    12988  14331  18991   2600   1709  -1515       C  
HETATM    4  O   MSE A1001      45.686  34.232  46.329  1.00122.74           O  
ANISOU    4  O   MSE A1001    13149  14382  19103   2623   1698  -1492       O  
HETATM    5  CB  MSE A1001      48.109  33.640  47.820  1.00126.88           C  
ANISOU    5  CB  MSE A1001    13443  15103  19665   2698   1629  -1360       C  
HETATM    6  CG  MSE A1001      47.455  32.317  48.238  1.00128.35           C  
ANISOU    6  CG  MSE A1001    13661  15180  19926   2804   1648  -1279       C  
HETATM    7 SE   MSE A1001      46.680  32.426  50.059  1.00133.56          SE  
ANISOU    7 SE   MSE A1001    14359  15877  20512   2809   1573  -1173      SE  
HETATM    8  CE  MSE A1001      45.342  33.842  49.745  1.00126.03           C  
ANISOU    8  CE  MSE A1001    13530  14892  19462   2657   1556  -1271       C  
ATOM      9  N   TYR A1002      46.910  35.791  45.246  1.00119.77           N  
ANISOU    9  N   TYR A1002    12778  14078  18651   2534   1747  -1588       N  
ATOM     10  CA  TYR A1002      45.780  36.692  44.964  1.00119.39           C  
ANISOU   10  CA  TYR A1002    12868  13996  18500   2511   1768  -1627       C  
ATOM     11  C   TYR A1002      44.646  36.004  44.188  1.00119.95           C  
ANISOU   11  C   TYR A1002    12974  14008  18594   2578   1790  -1665       C  
ATOM     12  O   TYR A1002      43.462  36.258  44.448  1.00118.21           O  
ANISOU   12  O   TYR A1002    12823  13794  18299   2589   1774  -1670       O  
ATOM     13  CB  TYR A1002      46.266  37.961  44.235  1.00118.52           C  
ANISOU   13  CB  TYR A1002    12840  13892  18303   2453   1843  -1692       C  
ATOM     14  CG  TYR A1002      45.170  38.851  43.654  1.00116.61           C  
ANISOU   14  CG  TYR A1002    12759  13611  17938   2485   1895  -1726       C  
ATOM     15  CD1 TYR A1002      44.324  39.586  44.485  1.00116.37           C  
ANISOU   15  CD1 TYR A1002    12825  13590  17799   2472   1875  -1692       C  
ATOM     16  CD2 TYR A1002      44.998  38.966  42.271  1.00114.95           C  
ANISOU   16  CD2 TYR A1002    12604  13368  17703   2546   1967  -1788       C  
ATOM     17  CE1 TYR A1002      43.326  40.401  43.959  1.00115.32           C  
ANISOU   17  CE1 TYR A1002    12842  13441  17531   2537   1929  -1713       C  
ATOM     18  CE2 TYR A1002      44.007  39.777  41.735  1.00114.82           C  
ANISOU   18  CE2 TYR A1002    12733  13347  17546   2616   2020  -1811       C  
ATOM     19  CZ  TYR A1002      43.171  40.493  42.582  1.00114.59           C  
ANISOU   19  CZ  TYR A1002    12800  13334  17404   2620   2002  -1770       C  
ATOM     20  OH  TYR A1002      42.182  41.303  42.056  1.00111.83           O  
ANISOU   20  OH  TYR A1002    12598  12998  16893   2725   2060  -1783       O  
ATOM     21  N   LEU A1003      45.018  35.130  43.251  1.00119.80           N  
ANISOU   21  N   LEU A1003    12896  13952  18671   2616   1830  -1704       N  
ATOM     22  CA  LEU A1003      44.043  34.417  42.424  1.00119.37           C  
ANISOU   22  CA  LEU A1003    12852  13865  18638   2656   1867  -1772       C  
ATOM     23  C   LEU A1003      43.278  33.348  43.219  1.00118.75           C  
ANISOU   23  C   LEU A1003    12753  13751  18618   2659   1853  -1744       C  
ATOM     24  O   LEU A1003      42.182  32.935  42.823  1.00118.62           O  
ANISOU   24  O   LEU A1003    12751  13738  18582   2658   1883  -1819       O  
ATOM     25  CB  LEU A1003      44.731  33.785  41.198  1.00119.14           C  
ANISOU   25  CB  LEU A1003    12769  13802  18698   2681   1929  -1830       C  
ATOM     26  CG  LEU A1003      45.535  34.658  40.219  1.00119.13           C  
ANISOU   26  CG  LEU A1003    12789  13818  18655   2678   1969  -1872       C  
ATOM     27  CD1 LEU A1003      46.223  33.791  39.179  1.00119.26           C  
ANISOU   27  CD1 LEU A1003    12735  13796  18783   2704   2022  -1919       C  
ATOM     28  CD2 LEU A1003      44.688  35.719  39.528  1.00118.65           C  
ANISOU   28  CD2 LEU A1003    12839  13795  18446   2705   2001  -1929       C  
ATOM     29  N   ARG A1004      43.863  32.922  44.341  1.00116.97           N  
ANISOU   29  N   ARG A1004    12491  13504  18448   2663   1817  -1644       N  
ATOM     30  CA  ARG A1004      43.376  31.774  45.110  1.00116.23           C  
ANISOU   30  CA  ARG A1004    12396  13343  18424   2680   1834  -1600       C  
ATOM     31  C   ARG A1004      42.217  32.136  46.026  1.00114.87           C  
ANISOU   31  C   ARG A1004    12280  13195  18170   2644   1791  -1586       C  
ATOM     32  O   ARG A1004      41.332  31.313  46.282  1.00115.28           O  
ANISOU   32  O   ARG A1004    12355  13194  18252   2629   1833  -1610       O  
ATOM     33  CB  ARG A1004      44.521  31.164  45.925  1.00117.23           C  
ANISOU   33  CB  ARG A1004    12466  13454  18622   2741   1822  -1484       C  
ATOM     34  CG  ARG A1004      44.197  29.827  46.575  1.00118.06           C  
ANISOU   34  CG  ARG A1004    12599  13453  18806   2792   1883  -1425       C  
ATOM     35  CD  ARG A1004      45.435  29.177  47.164  1.00119.08           C  
ANISOU   35  CD  ARG A1004    12674  13585  18987   2907   1888  -1305       C  
ATOM     36  NE  ARG A1004      45.098  28.381  48.340  1.00120.12           N  
ANISOU   36  NE  ARG A1004    12859  13650  19132   2972   1916  -1201       N  
ATOM     37  CZ  ARG A1004      45.838  27.381  48.812  1.00123.04           C  
ANISOU   37  CZ  ARG A1004    13227  13973  19550   3113   1975  -1091       C  
ATOM     38  NH1 ARG A1004      46.976  27.027  48.208  1.00123.26           N  
ANISOU   38  NH1 ARG A1004    13186  14026  19621   3204   2004  -1074       N  
ATOM     39  NH2 ARG A1004      45.429  26.721  49.893  1.00125.05           N  
ANISOU   39  NH2 ARG A1004    13558  14156  19801   3179   2016   -993       N  
ATOM     40  N   ILE A1005      42.235  33.374  46.508  1.00112.90           N  
ANISOU   40  N   ILE A1005    12059  13023  17816   2620   1723  -1557       N  
ATOM     41  CA  ILE A1005      41.259  33.861  47.479  1.00110.92           C  
ANISOU   41  CA  ILE A1005    11863  12805  17478   2592   1673  -1530       C  
ATOM     42  C   ILE A1005      39.970  34.405  46.818  1.00110.70           C  
ANISOU   42  C   ILE A1005    11889  12827  17342   2586   1687  -1629       C  
ATOM     43  O   ILE A1005      38.888  34.310  47.402  1.00110.76           O  
ANISOU   43  O   ILE A1005    11924  12858  17303   2569   1671  -1640       O  
ATOM     44  CB  ILE A1005      41.916  34.877  48.458  1.00109.70           C  
ANISOU   44  CB  ILE A1005    11713  12709  17256   2566   1605  -1450       C  
ATOM     45  CG1 ILE A1005      41.138  34.952  49.780  1.00109.80           C  
ANISOU   45  CG1 ILE A1005    11762  12736  17223   2548   1552  -1388       C  
ATOM     46  CG2 ILE A1005      42.116  36.239  47.801  1.00108.46           C  
ANISOU   46  CG2 ILE A1005    11614  12599  16997   2537   1620  -1500       C  
ATOM     47  CD1 ILE A1005      41.911  35.554  50.936  1.00110.18           C  
ANISOU   47  CD1 ILE A1005    11783  12848  17231   2522   1490  -1304       C  
ATOM     48  N   THR A1006      40.088  34.945  45.601  1.00110.10           N  
ANISOU   48  N   THR A1006    11827  12787  17219   2612   1722  -1702       N  
ATOM     49  CA  THR A1006      38.936  35.425  44.817  1.00109.45           C  
ANISOU   49  CA  THR A1006    11784  12792  17010   2650   1744  -1798       C  
ATOM     50  C   THR A1006      37.903  34.310  44.596  1.00110.31           C  
ANISOU   50  C   THR A1006    11835  12926  17150   2630   1777  -1895       C  
ATOM     51  O   THR A1006      36.691  34.575  44.478  1.00109.09           O  
ANISOU   51  O   THR A1006    11688  12886  16875   2647   1773  -1971       O  
ATOM     52  CB  THR A1006      39.384  36.002  43.450  1.00109.53           C  
ANISOU   52  CB  THR A1006    11815  12829  16972   2704   1794  -1855       C  
ATOM     53  OG1 THR A1006      40.330  37.056  43.662  1.00110.35           O  
ANISOU   53  OG1 THR A1006    11987  12900  17042   2694   1794  -1787       O  
ATOM     54  CG2 THR A1006      38.202  36.568  42.666  1.00109.70           C  
ANISOU   54  CG2 THR A1006    11876  12977  16827   2786   1816  -1943       C  
ATOM     55  N   ASN A1007      38.394  33.068  44.547  1.00110.46           N  
ANISOU   55  N   ASN A1007    11801  12848  17322   2593   1825  -1900       N  
ATOM     56  CA  ASN A1007      37.545  31.887  44.395  1.00110.80           C  
ANISOU   56  CA  ASN A1007    11804  12880  17413   2539   1896  -2003       C  
ATOM     57  C   ASN A1007      36.730  31.585  45.654  1.00111.76           C  
ANISOU   57  C   ASN A1007    11954  12985  17525   2487   1882  -1972       C  
ATOM     58  O   ASN A1007      35.755  30.823  45.601  1.00113.44           O  
ANISOU   58  O   ASN A1007    12146  13218  17737   2420   1950  -2085       O  
ATOM     59  CB  ASN A1007      38.382  30.668  43.992  1.00110.35           C  
ANISOU   59  CB  ASN A1007    11718  12690  17520   2523   1984  -2006       C  
ATOM     60  CG  ASN A1007      38.909  30.761  42.569  1.00109.22           C  
ANISOU   60  CG  ASN A1007    11535  12578  17387   2555   2019  -2082       C  
ATOM     61  OD1 ASN A1007      38.151  30.681  41.602  1.00108.88           O  
ANISOU   61  OD1 ASN A1007    11454  12636  17280   2542   2061  -2228       O  
ATOM     62  ND2 ASN A1007      40.219  30.914  42.438  1.00108.69           N  
ANISOU   62  ND2 ASN A1007    11464  12445  17390   2599   2003  -1992       N  
ATOM     63  N   ILE A1008      37.132  32.187  46.775  1.00110.82           N  
ANISOU   63  N   ILE A1008    11879  12836  17390   2507   1803  -1832       N  
ATOM     64  CA  ILE A1008      36.450  32.005  48.058  1.00111.01           C  
ANISOU   64  CA  ILE A1008    11938  12841  17400   2468   1779  -1782       C  
ATOM     65  C   ILE A1008      35.578  33.228  48.400  1.00110.80           C  
ANISOU   65  C   ILE A1008    11942  12946  17210   2480   1700  -1789       C  
ATOM     66  O   ILE A1008      34.351  33.120  48.464  1.00110.58           O  
ANISOU   66  O   ILE A1008    11906  13004  17106   2447   1714  -1882       O  
ATOM     67  CB  ILE A1008      37.450  31.730  49.217  1.00110.51           C  
ANISOU   67  CB  ILE A1008    11896  12672  17423   2492   1750  -1617       C  
ATOM     68  CG1 ILE A1008      38.643  30.893  48.744  1.00110.32           C  
ANISOU   68  CG1 ILE A1008    11841  12550  17527   2534   1810  -1581       C  
ATOM     69  CG2 ILE A1008      36.741  31.089  50.411  1.00110.80           C  
ANISOU   69  CG2 ILE A1008    11974  12650  17475   2455   1770  -1577       C  
ATOM     70  CD1 ILE A1008      39.912  31.125  49.548  1.00110.74           C  
ANISOU   70  CD1 ILE A1008    11876  12594  17607   2597   1748  -1432       C  
ATOM     71  N   VAL A1009      36.223  34.384  48.597  1.00110.24           N  
ANISOU   71  N   VAL A1009    11911  12897  17078   2523   1634  -1702       N  
ATOM     72  CA  VAL A1009      35.575  35.624  49.085  1.00109.17           C  
ANISOU   72  CA  VAL A1009    11840  12851  16788   2545   1576  -1678       C  
ATOM     73  C   VAL A1009      34.346  36.051  48.266  1.00108.18           C  
ANISOU   73  C   VAL A1009    11717  12873  16513   2596   1594  -1798       C  
ATOM     74  O   VAL A1009      33.501  36.811  48.752  1.00107.24           O  
ANISOU   74  O   VAL A1009    11647  12840  16261   2626   1558  -1790       O  
ATOM     75  CB  VAL A1009      36.585  36.811  49.177  1.00108.52           C  
ANISOU   75  CB  VAL A1009    11817  12753  16663   2567   1549  -1594       C  
ATOM     76  CG1 VAL A1009      36.014  37.952  50.009  1.00108.39           C  
ANISOU   76  CG1 VAL A1009    11889  12785  16510   2571   1507  -1546       C  
ATOM     77  CG2 VAL A1009      37.898  36.368  49.794  1.00107.69           C  
ANISOU   77  CG2 VAL A1009    11669  12565  16685   2530   1532  -1504       C  
ATOM     78  N   GLU A1010      34.258  35.548  47.035  1.00107.87           N  
ANISOU   78  N   GLU A1010    11619  12880  16487   2618   1651  -1911       N  
ATOM     79  CA  GLU A1010      33.191  35.896  46.094  1.00107.69           C  
ANISOU   79  CA  GLU A1010    11569  13045  16303   2691   1672  -2041       C  
ATOM     80  C   GLU A1010      32.258  34.712  45.822  1.00108.73           C  
ANISOU   80  C   GLU A1010    11592  13260  16460   2615   1722  -2198       C  
ATOM     81  O   GLU A1010      31.286  34.845  45.074  1.00109.54           O  
ANISOU   81  O   GLU A1010    11632  13569  16418   2664   1739  -2337       O  
ATOM     82  CB  GLU A1010      33.803  36.360  44.767  1.00107.42           C  
ANISOU   82  CB  GLU A1010    11547  13038  16231   2780   1709  -2069       C  
ATOM     83  CG  GLU A1010      34.648  37.626  44.841  1.00105.33           C  
ANISOU   83  CG  GLU A1010    11406  12701  15913   2843   1700  -1949       C  
ATOM     84  CD  GLU A1010      34.031  38.798  44.093  1.00104.08           C  
ANISOU   84  CD  GLU A1010    11333  12679  15535   2999   1729  -1974       C  
ATOM     85  OE1 GLU A1010      32.958  38.628  43.464  1.00103.65           O  
ANISOU   85  OE1 GLU A1010    11214  12812  15354   3079   1737  -2086       O  
ATOM     86  OE2 GLU A1010      34.633  39.893  44.126  1.00102.68           O  
ANISOU   86  OE2 GLU A1010    11290  12428  15296   3046   1757  -1887       O  
ATOM     87  N   SER A1011      32.556  33.561  46.425  1.00109.31           N  
ANISOU   87  N   SER A1011    11645  13185  16702   2499   1761  -2185       N  
ATOM     88  CA  SER A1011      31.835  32.316  46.130  1.00110.63           C  
ANISOU   88  CA  SER A1011    11733  13382  16918   2392   1856  -2348       C  
ATOM     89  C   SER A1011      30.405  32.365  46.642  1.00110.54           C  
ANISOU   89  C   SER A1011    11685  13534  16779   2346   1849  -2452       C  
ATOM     90  O   SER A1011      30.072  33.230  47.453  1.00110.57           O  
ANISOU   90  O   SER A1011    11741  13580  16691   2396   1766  -2361       O  
ATOM     91  CB  SER A1011      32.577  31.095  46.695  1.00111.15           C  
ANISOU   91  CB  SER A1011    11830  13211  17190   2301   1932  -2286       C  
ATOM     92  OG  SER A1011      32.604  31.107  48.111  1.00110.34           O  
ANISOU   92  OG  SER A1011    11797  13004  17122   2280   1892  -2153       O  
ATOM     93  N   SER A1012      29.568  31.452  46.150  1.00111.65           N  
ANISOU   93  N   SER A1012    11733  13780  16910   2241   1946  -2655       N  
ATOM     94  CA  SER A1012      28.159  31.389  46.542  1.00114.29           C  
ANISOU   94  CA  SER A1012    12003  14309  17114   2174   1957  -2797       C  
ATOM     95  C   SER A1012      27.989  30.987  48.009  1.00114.70           C  
ANISOU   95  C   SER A1012    12135  14195  17251   2076   1966  -2706       C  
ATOM     96  O   SER A1012      27.219  31.613  48.742  1.00114.35           O  
ANISOU   96  O   SER A1012    12097  14262  17090   2097   1896  -2688       O  
ATOM     97  CB  SER A1012      27.385  30.437  45.631  1.00116.56           C  
ANISOU   97  CB  SER A1012    12157  14759  17371   2050   2082  -3069       C  
ATOM     98  OG  SER A1012      27.935  29.132  45.676  1.00119.44           O  
ANISOU   98  OG  SER A1012    12561  14881  17939   1902   2223  -3095       O  
ATOM     99  N   PHE A1013      28.728  29.958  48.424  1.00115.47           N  
ANISOU   99  N   PHE A1013    12301  14027  17543   1989   2058  -2641       N  
ATOM    100  CA  PHE A1013      28.742  29.473  49.812  1.00116.11           C  
ANISOU  100  CA  PHE A1013    12481  13919  17716   1922   2086  -2528       C  
ATOM    101  C   PHE A1013      29.065  30.568  50.821  1.00115.17           C  
ANISOU  101  C   PHE A1013    12429  13780  17550   2030   1932  -2321       C  
ATOM    102  O   PHE A1013      28.455  30.628  51.893  1.00114.27           O  
ANISOU  102  O   PHE A1013    12353  13661  17405   1988   1913  -2286       O  
ATOM    103  CB  PHE A1013      29.752  28.324  49.952  1.00115.88           C  
ANISOU  103  CB  PHE A1013    12535  13607  17887   1885   2208  -2447       C  
ATOM    104  CG  PHE A1013      30.234  28.087  51.364  1.00115.25           C  
ANISOU  104  CG  PHE A1013    12576  13322  17893   1909   2200  -2246       C  
ATOM    105  CD1 PHE A1013      29.439  27.410  52.291  1.00116.22           C  
ANISOU  105  CD1 PHE A1013    12760  13370  18028   1798   2299  -2285       C  
ATOM    106  CD2 PHE A1013      31.498  28.518  51.761  1.00113.61           C  
ANISOU  106  CD2 PHE A1013    12413  13010  17744   2041   2104  -2029       C  
ATOM    107  CE1 PHE A1013      29.897  27.176  53.583  1.00115.44           C  
ANISOU  107  CE1 PHE A1013    12776  13089  17995   1843   2297  -2091       C  
ATOM    108  CE2 PHE A1013      31.961  28.284  53.048  1.00113.02           C  
ANISOU  108  CE2 PHE A1013    12429  12787  17726   2081   2095  -1850       C  
ATOM    109  CZ  PHE A1013      31.159  27.613  53.960  1.00114.24           C  
ANISOU  109  CZ  PHE A1013    12655  12862  17890   1994   2189  -1872       C  
ATOM    110  N   PHE A1014      30.039  31.407  50.461  1.00115.39           N  
ANISOU  110  N   PHE A1014    12474  13796  17574   2155   1839  -2196       N  
ATOM    111  CA  PHE A1014      30.556  32.484  51.304  1.00114.75           C  
ANISOU  111  CA  PHE A1014    12459  13687  17454   2242   1715  -2011       C  
ATOM    112  C   PHE A1014      29.436  33.347  51.878  1.00114.90           C  
ANISOU  112  C   PHE A1014    12482  13865  17308   2256   1643  -2033       C  
ATOM    113  O   PHE A1014      29.366  33.537  53.097  1.00114.17           O  
ANISOU  113  O   PHE A1014    12447  13709  17222   2238   1597  -1924       O  
ATOM    114  CB  PHE A1014      31.530  33.352  50.500  1.00114.82           C  
ANISOU  114  CB  PHE A1014    12472  13711  17441   2348   1661  -1948       C  
ATOM    115  CG  PHE A1014      32.601  34.008  51.329  1.00115.92           C  
ANISOU  115  CG  PHE A1014    12677  13748  17618   2392   1585  -1761       C  
ATOM    116  CD1 PHE A1014      33.858  33.400  51.486  1.00117.10           C  
ANISOU  116  CD1 PHE A1014    12829  13752  17914   2394   1606  -1667       C  
ATOM    117  CD2 PHE A1014      32.372  35.241  51.939  1.00114.67           C  
ANISOU  117  CD2 PHE A1014    12574  13658  17337   2432   1503  -1691       C  
ATOM    118  CE1 PHE A1014      34.856  34.006  52.244  1.00116.36           C  
ANISOU  118  CE1 PHE A1014    12764  13616  17834   2426   1537  -1521       C  
ATOM    119  CE2 PHE A1014      33.366  35.848  52.701  1.00115.01           C  
ANISOU  119  CE2 PHE A1014    12665  13628  17406   2444   1447  -1548       C  
ATOM    120  CZ  PHE A1014      34.609  35.233  52.851  1.00115.25           C  
ANISOU  120  CZ  PHE A1014    12670  13548  17573   2436   1460  -1471       C  
ATOM    121  N   THR A1015      28.557  33.847  51.001  1.00114.93           N  
ANISOU  121  N   THR A1015    12421  14091  17155   2302   1638  -2173       N  
ATOM    122  CA  THR A1015      27.450  34.727  51.406  1.00114.45           C  
ANISOU  122  CA  THR A1015    12359  14219  16909   2352   1575  -2201       C  
ATOM    123  C   THR A1015      26.521  34.030  52.394  1.00114.59           C  
ANISOU  123  C   THR A1015    12358  14240  16941   2225   1606  -2262       C  
ATOM    124  O   THR A1015      26.279  34.543  53.487  1.00115.72           O  
ANISOU  124  O   THR A1015    12563  14358  17047   2232   1543  -2159       O  
ATOM    125  CB  THR A1015      26.650  35.259  50.193  1.00115.48           C  
ANISOU  125  CB  THR A1015    12405  14627  16845   2456   1578  -2354       C  
ATOM    126  OG1 THR A1015      27.373  36.333  49.578  1.00116.65           O  
ANISOU  126  OG1 THR A1015    12624  14769  16927   2611   1539  -2252       O  
ATOM    127  CG2 THR A1015      25.291  35.793  50.624  1.00115.94           C  
ANISOU  127  CG2 THR A1015    12428  14917  16707   2494   1539  -2427       C  
ATOM    128  N   LYS A1016      26.037  32.850  52.011  1.00114.42           N  
ANISOU  128  N   LYS A1016    12261  14238  16976   2096   1720  -2434       N  
ATOM    129  CA  LYS A1016      25.133  32.040  52.834  1.00113.71           C  
ANISOU  129  CA  LYS A1016    12160  14138  16905   1943   1795  -2528       C  
ATOM    130  C   LYS A1016      25.757  31.629  54.178  1.00113.56           C  
ANISOU  130  C   LYS A1016    12268  13844  17036   1898   1801  -2341       C  
ATOM    131  O   LYS A1016      25.046  31.500  55.178  1.00112.79           O  
ANISOU  131  O   LYS A1016    12199  13742  16914   1827   1809  -2342       O  
ATOM    132  CB  LYS A1016      24.652  30.815  52.042  1.00113.98           C  
ANISOU  132  CB  LYS A1016    12104  14220  16982   1791   1956  -2766       C  
ATOM    133  CG  LYS A1016      23.976  31.168  50.720  1.00113.09           C  
ANISOU  133  CG  LYS A1016    11838  14431  16698   1838   1949  -2972       C  
ATOM    134  CD  LYS A1016      23.571  29.936  49.936  1.00114.44           C  
ANISOU  134  CD  LYS A1016    11912  14657  16914   1661   2121  -3227       C  
ATOM    135  CE  LYS A1016      22.928  30.319  48.611  1.00115.72           C  
ANISOU  135  CE  LYS A1016    11898  15186  16883   1726   2103  -3436       C  
ATOM    136  NZ  LYS A1016      22.654  29.145  47.728  1.00117.00           N  
ANISOU  136  NZ  LYS A1016    11953  15413  17088   1544   2277  -3701       N  
ATOM    137  N   PHE A1017      27.082  31.451  54.191  1.00113.69           N  
ANISOU  137  N   PHE A1017    12351  13654  17190   1953   1797  -2183       N  
ATOM    138  CA  PHE A1017      27.834  31.158  55.418  1.00113.13           C  
ANISOU  138  CA  PHE A1017    12387  13362  17235   1960   1788  -1986       C  
ATOM    139  C   PHE A1017      27.886  32.353  56.367  1.00111.01           C  
ANISOU  139  C   PHE A1017    12158  13141  16879   2038   1640  -1836       C  
ATOM    140  O   PHE A1017      28.072  32.178  57.574  1.00110.18           O  
ANISOU  140  O   PHE A1017    12122  12921  16821   2027   1625  -1709       O  
ATOM    141  CB  PHE A1017      29.261  30.677  55.102  1.00114.35           C  
ANISOU  141  CB  PHE A1017    12576  13339  17533   2020   1820  -1872       C  
ATOM    142  CG  PHE A1017      30.011  30.155  56.307  1.00115.65           C  
ANISOU  142  CG  PHE A1017    12834  13306  17801   2049   1836  -1687       C  
ATOM    143  CD1 PHE A1017      29.666  28.928  56.888  1.00117.53           C  
ANISOU  143  CD1 PHE A1017    13148  13387  18119   1971   1989  -1705       C  
ATOM    144  CD2 PHE A1017      31.055  30.884  56.865  1.00114.75           C  
ANISOU  144  CD2 PHE A1017    12735  13175  17689   2156   1716  -1503       C  
ATOM    145  CE1 PHE A1017      30.345  28.447  58.000  1.00117.60           C  
ANISOU  145  CE1 PHE A1017    13255  13229  18201   2036   2012  -1521       C  
ATOM    146  CE2 PHE A1017      31.740  30.405  57.978  1.00116.29           C  
ANISOU  146  CE2 PHE A1017    12995  13239  17952   2206   1725  -1338       C  
ATOM    147  CZ  PHE A1017      31.383  29.186  58.547  1.00117.00           C  
ANISOU  147  CZ  PHE A1017    13167  13174  18112   2165   1870  -1335       C  
ATOM    148  N   ILE A1018      27.749  33.560  55.817  1.00109.40           N  
ANISOU  148  N   ILE A1018    11924  13101  16544   2125   1545  -1848       N  
ATOM    149  CA  ILE A1018      27.612  34.763  56.634  1.00108.95           C  
ANISOU  149  CA  ILE A1018    11916  13099  16379   2185   1432  -1737       C  
ATOM    150  C   ILE A1018      26.169  34.831  57.132  1.00110.04           C  
ANISOU  150  C   ILE A1018    12033  13376  16401   2136   1431  -1836       C  
ATOM    151  O   ILE A1018      25.920  35.031  58.330  1.00108.72           O  
ANISOU  151  O   ILE A1018    11920  13168  16223   2110   1388  -1748       O  
ATOM    152  CB  ILE A1018      27.978  36.057  55.861  1.00107.75           C  
ANISOU  152  CB  ILE A1018    11779  13047  16116   2305   1369  -1710       C  
ATOM    153  CG1 ILE A1018      29.483  36.120  55.569  1.00106.74           C  
ANISOU  153  CG1 ILE A1018    11674  12784  16097   2337   1364  -1604       C  
ATOM    154  CG2 ILE A1018      27.551  37.299  56.646  1.00107.65           C  
ANISOU  154  CG2 ILE A1018    11834  13103  15963   2358   1289  -1631       C  
ATOM    155  CD1 ILE A1018      29.886  37.215  54.591  1.00105.56           C  
ANISOU  155  CD1 ILE A1018    11550  12705  15853   2436   1348  -1606       C  
ATOM    156  N   ILE A1019      25.227  34.638  56.205  1.00111.89           N  
ANISOU  156  N   ILE A1019    12176  13795  16541   2120   1479  -2030       N  
ATOM    157  CA  ILE A1019      23.791  34.721  56.514  1.00113.28           C  
ANISOU  157  CA  ILE A1019    12297  14167  16578   2077   1482  -2162       C  
ATOM    158  C   ILE A1019      23.382  33.654  57.527  1.00114.46           C  
ANISOU  158  C   ILE A1019    12469  14190  16828   1916   1561  -2188       C  
ATOM    159  O   ILE A1019      22.396  33.822  58.248  1.00116.71           O  
ANISOU  159  O   ILE A1019    12745  14576  17023   1871   1545  -2234       O  
ATOM    160  CB  ILE A1019      22.887  34.609  55.258  1.00113.51           C  
ANISOU  160  CB  ILE A1019    12188  14469  16471   2088   1529  -2395       C  
ATOM    161  CG1 ILE A1019      23.557  35.218  54.013  1.00113.65           C  
ANISOU  161  CG1 ILE A1019    12193  14546  16444   2234   1503  -2379       C  
ATOM    162  CG2 ILE A1019      21.509  35.221  55.523  1.00112.82           C  
ANISOU  162  CG2 ILE A1019    12037  14659  16171   2124   1486  -2498       C  
ATOM    163  CD1 ILE A1019      23.824  36.714  54.054  1.00112.65           C  
ANISOU  163  CD1 ILE A1019    12154  14461  16186   2419   1404  -2231       C  
ATOM    164  N   TYR A1020      24.142  32.565  57.588  1.00113.18           N  
ANISOU  164  N   TYR A1020    12352  13805  16847   1840   1659  -2154       N  
ATOM    165  CA  TYR A1020      23.895  31.548  58.591  1.00113.52           C  
ANISOU  165  CA  TYR A1020    12462  13680  16988   1712   1763  -2146       C  
ATOM    166  C   TYR A1020      24.311  32.057  59.959  1.00112.35           C  
ANISOU  166  C   TYR A1020    12413  13415  16858   1770   1666  -1926       C  
ATOM    167  O   TYR A1020      23.689  31.716  60.966  1.00113.65           O  
ANISOU  167  O   TYR A1020    12626  13535  17022   1691   1703  -1922       O  
ATOM    168  CB  TYR A1020      24.657  30.265  58.264  1.00115.13           C  
ANISOU  168  CB  TYR A1020    12716  13661  17366   1652   1916  -2149       C  
ATOM    169  CG  TYR A1020      24.248  29.072  59.099  1.00116.89           C  
ANISOU  169  CG  TYR A1020    13030  13706  17675   1513   2085  -2181       C  
ATOM    170  CD1 TYR A1020      22.966  28.518  58.984  1.00118.67           C  
ANISOU  170  CD1 TYR A1020    13208  14041  17842   1337   2212  -2421       C  
ATOM    171  CD2 TYR A1020      25.145  28.484  59.992  1.00117.45           C  
ANISOU  171  CD2 TYR A1020    13241  13513  17874   1562   2134  -1982       C  
ATOM    172  CE1 TYR A1020      22.586  27.421  59.745  1.00121.14           C  
ANISOU  172  CE1 TYR A1020    13631  14165  18232   1193   2401  -2460       C  
ATOM    173  CE2 TYR A1020      24.778  27.379  60.755  1.00119.77           C  
ANISOU  173  CE2 TYR A1020    13653  13618  18236   1455   2318  -1998       C  
ATOM    174  CZ  TYR A1020      23.499  26.852  60.629  1.00121.65           C  
ANISOU  174  CZ  TYR A1020    13864  13931  18426   1260   2461  -2239       C  
ATOM    175  OH  TYR A1020      23.124  25.759  61.383  1.00123.49           O  
ANISOU  175  OH  TYR A1020    14240  13955  18726   1138   2675  -2266       O  
ATOM    176  N   LEU A1021      25.345  32.894  59.987  1.00110.21           N  
ANISOU  176  N   LEU A1021    12170  13111  16594   1897   1551  -1758       N  
ATOM    177  CA  LEU A1021      26.000  33.245  61.246  1.00109.59           C  
ANISOU  177  CA  LEU A1021    12173  12918  16550   1944   1473  -1552       C  
ATOM    178  C   LEU A1021      25.334  34.396  61.995  1.00109.03           C  
ANISOU  178  C   LEU A1021    12114  12973  16340   1968   1359  -1512       C  
ATOM    179  O   LEU A1021      25.035  34.253  63.182  1.00108.64           O  
ANISOU  179  O   LEU A1021    12116  12866  16295   1930   1350  -1442       O  
ATOM    180  CB  LEU A1021      27.492  33.508  61.028  1.00108.72           C  
ANISOU  180  CB  LEU A1021    12075  12721  16512   2041   1423  -1409       C  
ATOM    181  CG  LEU A1021      28.432  33.126  62.171  1.00108.97           C  
ANISOU  181  CG  LEU A1021    12168  12605  16631   2079   1412  -1224       C  
ATOM    182  CD1 LEU A1021      28.362  31.638  62.490  1.00110.31           C  
ANISOU  182  CD1 LEU A1021    12395  12606  16912   2037   1563  -1227       C  
ATOM    183  CD2 LEU A1021      29.855  33.525  61.823  1.00109.01           C  
ANISOU  183  CD2 LEU A1021    12148  12596  16676   2168   1354  -1121       C  
ATOM    184  N   ILE A1022      25.096  35.517  61.304  1.00108.62           N  
ANISOU  184  N   ILE A1022    12028  13083  16158   2043   1287  -1554       N  
ATOM    185  CA  ILE A1022      24.407  36.686  61.890  1.00107.34           C  
ANISOU  185  CA  ILE A1022    11894  13045  15844   2086   1198  -1523       C  
ATOM    186  C   ILE A1022      23.057  36.340  62.509  1.00107.74           C  
ANISOU  186  C   ILE A1022    11923  13185  15829   2006   1223  -1622       C  
ATOM    187  O   ILE A1022      22.723  36.863  63.563  1.00108.76           O  
ANISOU  187  O   ILE A1022    12102  13318  15905   2004   1164  -1542       O  
ATOM    188  CB  ILE A1022      24.193  37.849  60.887  1.00106.27           C  
ANISOU  188  CB  ILE A1022    11747  13077  15554   2205   1160  -1571       C  
ATOM    189  CG1 ILE A1022      23.513  37.345  59.607  1.00107.86           C  
ANISOU  189  CG1 ILE A1022    11844  13433  15704   2210   1227  -1765       C  
ATOM    190  CG2 ILE A1022      25.509  38.556  60.594  1.00105.96           C  
ANISOU  190  CG2 ILE A1022    11766  12943  15551   2274   1130  -1448       C  
ATOM    191  CD1 ILE A1022      23.030  38.434  58.679  1.00108.00           C  
ANISOU  191  CD1 ILE A1022    11848  13659  15526   2360   1200  -1822       C  
ATOM    192  N   VAL A1023      22.291  35.470  61.849  1.00107.97           N  
ANISOU  192  N   VAL A1023    11871  13296  15857   1927   1319  -1810       N  
ATOM    193  CA  VAL A1023      20.990  35.029  62.355  1.00108.75           C  
ANISOU  193  CA  VAL A1023    11930  13497  15892   1819   1368  -1945       C  
ATOM    194  C   VAL A1023      21.155  34.180  63.626  1.00109.52           C  
ANISOU  194  C   VAL A1023    12117  13376  16119   1713   1425  -1853       C  
ATOM    195  O   VAL A1023      20.469  34.404  64.625  1.00108.63           O  
ANISOU  195  O   VAL A1023    12034  13291  15950   1676   1396  -1831       O  
ATOM    196  CB  VAL A1023      20.180  34.268  61.273  1.00109.90           C  
ANISOU  196  CB  VAL A1023    11951  13807  15997   1733   1479  -2203       C  
ATOM    197  CG1 VAL A1023      18.811  33.855  61.805  1.00110.62           C  
ANISOU  197  CG1 VAL A1023    11986  14037  16006   1600   1540  -2371       C  
ATOM    198  CG2 VAL A1023      20.023  35.121  60.018  1.00109.03           C  
ANISOU  198  CG2 VAL A1023    11752  13937  15736   1873   1421  -2282       C  
ATOM    199  N   LEU A1024      22.074  33.217  63.591  1.00110.90           N  
ANISOU  199  N   LEU A1024    12345  13335  16458   1683   1512  -1791       N  
ATOM    200  CA  LEU A1024      22.327  32.372  64.760  1.00112.13           C  
ANISOU  200  CA  LEU A1024    12607  13271  16724   1625   1587  -1682       C  
ATOM    201  C   LEU A1024      22.877  33.164  65.940  1.00111.63           C  
ANISOU  201  C   LEU A1024    12612  13159  16645   1715   1454  -1463       C  
ATOM    202  O   LEU A1024      22.423  32.996  67.078  1.00111.88           O  
ANISOU  202  O   LEU A1024    12704  13139  16668   1670   1464  -1412       O  
ATOM    203  CB  LEU A1024      23.247  31.192  64.424  1.00112.20           C  
ANISOU  203  CB  LEU A1024    12673  13064  16893   1616   1722  -1647       C  
ATOM    204  CG  LEU A1024      22.529  29.842  64.466  1.00113.49           C  
ANISOU  204  CG  LEU A1024    12884  13118  17117   1455   1941  -1798       C  
ATOM    205  CD1 LEU A1024      22.046  29.436  63.081  1.00114.76           C  
ANISOU  205  CD1 LEU A1024    12942  13398  17263   1360   2040  -2043       C  
ATOM    206  CD2 LEU A1024      23.431  28.775  65.067  1.00114.59           C  
ANISOU  206  CD2 LEU A1024    13172  12967  17401   1490   2072  -1645       C  
ATOM    207  N   ASN A1025      23.851  34.025  65.653  1.00110.56           N  
ANISOU  207  N   ASN A1025    12463  13046  16500   1829   1342  -1349       N  
ATOM    208  CA  ASN A1025      24.380  34.958  66.633  1.00108.47           C  
ANISOU  208  CA  ASN A1025    12239  12780  16194   1897   1216  -1178       C  
ATOM    209  C   ASN A1025      23.282  35.919  67.025  1.00108.20           C  
ANISOU  209  C   ASN A1025    12199  12899  16012   1883   1144  -1226       C  
ATOM    210  O   ASN A1025      23.206  36.336  68.179  1.00109.57           O  
ANISOU  210  O   ASN A1025    12421  13056  16153   1882   1083  -1122       O  
ATOM    211  CB  ASN A1025      25.562  35.725  66.050  1.00107.78           C  
ANISOU  211  CB  ASN A1025    12132  12709  16111   1990   1142  -1099       C  
ATOM    212  CG  ASN A1025      26.238  36.637  67.058  1.00107.82           C  
ANISOU  212  CG  ASN A1025    12171  12719  16077   2031   1036   -944       C  
ATOM    213  OD1 ASN A1025      27.114  37.422  66.685  1.00107.59           O  
ANISOU  213  OD1 ASN A1025    12129  12720  16028   2079    984   -899       O  
ATOM    214  ND2 ASN A1025      25.849  36.542  68.337  1.00107.17           N  
ANISOU  214  ND2 ASN A1025    12131  12610  15977   2002   1014   -873       N  
ATOM    215  N   GLY A1026      22.425  36.245  66.058  1.00107.49           N  
ANISOU  215  N   GLY A1026    12045  12974  15824   1883   1156  -1386       N  
ATOM    216  CA  GLY A1026      21.301  37.158  66.255  1.00105.59           C  
ANISOU  216  CA  GLY A1026    11788  12916  15415   1903   1098  -1447       C  
ATOM    217  C   GLY A1026      20.294  36.649  67.256  1.00105.39           C  
ANISOU  217  C   GLY A1026    11772  12896  15374   1800   1131  -1493       C  
ATOM    218  O   GLY A1026      19.712  37.445  67.995  1.00106.91           O  
ANISOU  218  O   GLY A1026    11990  13170  15460   1821   1060  -1454       O  
ATOM    219  N   ILE A1027      20.093  35.329  67.287  1.00104.89           N  
ANISOU  219  N   ILE A1027    11703  12735  15416   1683   1257  -1576       N  
ATOM    220  CA  ILE A1027      19.176  34.697  68.254  1.00104.41           C  
ANISOU  220  CA  ILE A1027    11671  12646  15355   1561   1326  -1629       C  
ATOM    221  C   ILE A1027      19.805  34.617  69.651  1.00103.05           C  
ANISOU  221  C   ILE A1027    11614  12284  15258   1577   1294  -1418       C  
ATOM    222  O   ILE A1027      19.097  34.572  70.655  1.00102.51           O  
ANISOU  222  O   ILE A1027    11583  12212  15152   1517   1300  -1411       O  
ATOM    223  CB  ILE A1027      18.704  33.287  67.800  1.00105.05           C  
ANISOU  223  CB  ILE A1027    11732  12670  15514   1410   1516  -1812       C  
ATOM    224  CG1 ILE A1027      18.161  33.322  66.366  1.00105.86           C  
ANISOU  224  CG1 ILE A1027    11695  12991  15535   1393   1547  -2035       C  
ATOM    225  CG2 ILE A1027      17.633  32.739  68.738  1.00104.38           C  
ANISOU  225  CG2 ILE A1027    11678  12575  15406   1266   1606  -1898       C  
ATOM    226  CD1 ILE A1027      18.198  31.988  65.640  1.00106.43           C  
ANISOU  226  CD1 ILE A1027    11753  12972  15714   1260   1738  -2193       C  
ATOM    227  N   THR A1028      21.132  34.625  69.712  1.00102.67           N  
ANISOU  227  N   THR A1028    11608  12104  15300   1665   1259  -1254       N  
ATOM    228  CA  THR A1028      21.831  34.437  70.985  1.00103.68           C  
ANISOU  228  CA  THR A1028    11824  12084  15486   1701   1235  -1060       C  
ATOM    229  C   THR A1028      22.190  35.746  71.725  1.00103.56           C  
ANISOU  229  C   THR A1028    11813  12149  15385   1773   1074   -925       C  
ATOM    230  O   THR A1028      23.004  35.752  72.660  1.00102.11           O  
ANISOU  230  O   THR A1028    11673  11890  15235   1822   1032   -764       O  
ATOM    231  CB  THR A1028      23.045  33.492  70.832  1.00104.07           C  
ANISOU  231  CB  THR A1028    11913  11957  15670   1758   1313   -961       C  
ATOM    232  OG1 THR A1028      23.324  32.883  72.096  1.00105.23           O  
ANISOU  232  OG1 THR A1028    12156  11966  15859   1784   1354   -816       O  
ATOM    233  CG2 THR A1028      24.287  34.230  70.317  1.00103.27           C  
ANISOU  233  CG2 THR A1028    11763  11900  15576   1868   1206   -868       C  
HETATM  234  N   MSE A1029      21.564  36.845  71.293  1.00102.86           N  
ANISOU  234  N   MSE A1029    11684  12225  15173   1785    999  -1001       N  
HETATM  235  CA  MSE A1029      21.628  38.131  71.992  1.00101.16           C  
ANISOU  235  CA  MSE A1029    11497  12082  14856   1828    882   -906       C  
HETATM  236  C   MSE A1029      20.353  38.321  72.770  1.00100.56           C  
ANISOU  236  C   MSE A1029    11439  12079  14690   1773    872   -954       C  
HETATM  237  O   MSE A1029      20.375  38.767  73.916  1.00 98.73           O  
ANISOU  237  O   MSE A1029    11257  11830  14427   1769    812   -848       O  
HETATM  238  CB  MSE A1029      21.747  39.291  71.010  1.00100.77           C  
ANISOU  238  CB  MSE A1029    11429  12150  14711   1901    834   -946       C  
HETATM  239  CG  MSE A1029      22.360  38.883  69.684  1.00102.41           C  
ANISOU  239  CG  MSE A1029    11587  12340  14983   1935    884  -1008       C  
HETATM  240 SE   MSE A1029      23.530  40.323  69.040  1.00105.16          SE  
ANISOU  240 SE   MSE A1029    11968  12714  15275   2030    825   -932      SE  
HETATM  241  CE  MSE A1029      24.756  40.400  70.592  1.00104.16           C  
ANISOU  241  CE  MSE A1029    11875  12483  15219   1993    762   -744       C  
ATOM    242  N   GLY A1030      19.228  37.999  72.133  1.00101.56           N  
ANISOU  242  N   GLY A1030    11512  12312  14763   1728    932  -1128       N  
ATOM    243  CA  GLY A1030      17.921  38.061  72.775  1.00103.36           C  
ANISOU  243  CA  GLY A1030    11735  12640  14899   1665    937  -1208       C  
ATOM    244  C   GLY A1030      17.799  36.955  73.796  1.00106.03           C  
ANISOU  244  C   GLY A1030    12128  12823  15337   1561   1018  -1175       C  
ATOM    245  O   GLY A1030      17.141  37.113  74.829  1.00105.98           O  
ANISOU  245  O   GLY A1030    12158  12830  15281   1517    998  -1151       O  
ATOM    246  N   LEU A1031      18.447  35.831  73.491  1.00108.60           N  
ANISOU  246  N   LEU A1031    12474  12990  15798   1531   1123  -1169       N  
ATOM    247  CA  LEU A1031      18.555  34.701  74.404  1.00109.39           C  
ANISOU  247  CA  LEU A1031    12667  12898  16000   1469   1234  -1106       C  
ATOM    248  C   LEU A1031      19.558  35.015  75.514  1.00110.40           C  
ANISOU  248  C   LEU A1031    12865  12927  16155   1564   1146   -872       C  
ATOM    249  O   LEU A1031      19.389  34.560  76.647  1.00112.51           O  
ANISOU  249  O   LEU A1031    13213  13097  16439   1541   1186   -791       O  
ATOM    250  CB  LEU A1031      18.985  33.456  73.636  1.00109.86           C  
ANISOU  250  CB  LEU A1031    12745  12817  16181   1434   1393  -1168       C  
ATOM    251  CG  LEU A1031      18.284  32.143  73.977  1.00111.94           C  
ANISOU  251  CG  LEU A1031    13088  12942  16503   1295   1602  -1270       C  
ATOM    252  CD1 LEU A1031      16.775  32.289  73.822  1.00111.77           C  
ANISOU  252  CD1 LEU A1031    12990  13103  16376   1149   1636  -1498       C  
ATOM    253  CD2 LEU A1031      18.806  31.008  73.102  1.00112.73           C  
ANISOU  253  CD2 LEU A1031    13219  12893  16719   1269   1773  -1330       C  
ATOM    254  N   GLU A1032      20.591  35.797  75.184  1.00109.91           N  
ANISOU  254  N   GLU A1032    12767  12906  16087   1666   1036   -776       N  
ATOM    255  CA  GLU A1032      21.593  36.257  76.165  1.00109.17           C  
ANISOU  255  CA  GLU A1032    12702  12784  15992   1747    940   -583       C  
ATOM    256  C   GLU A1032      21.024  37.116  77.290  1.00106.54           C  
ANISOU  256  C   GLU A1032    12393  12527  15559   1724    848   -533       C  
ATOM    257  O   GLU A1032      21.589  37.141  78.381  1.00108.31           O  
ANISOU  257  O   GLU A1032    12651  12717  15784   1763    805   -390       O  
ATOM    258  CB  GLU A1032      22.738  37.029  75.486  1.00109.25           C  
ANISOU  258  CB  GLU A1032    12656  12855  16000   1824    856   -536       C  
ATOM    259  CG  GLU A1032      24.103  36.350  75.546  1.00109.74           C  
ANISOU  259  CG  GLU A1032    12714  12829  16154   1909    878   -418       C  
ATOM    260  CD  GLU A1032      25.183  37.115  74.796  1.00109.18           C  
ANISOU  260  CD  GLU A1032    12574  12832  16075   1960    808   -403       C  
ATOM    261  OE1 GLU A1032      24.923  38.240  74.329  1.00109.23           O  
ANISOU  261  OE1 GLU A1032    12562  12936  16003   1933    749   -466       O  
ATOM    262  OE2 GLU A1032      26.303  36.592  74.665  1.00109.63           O  
ANISOU  262  OE2 GLU A1032    12605  12851  16198   2034    825   -329       O  
ATOM    263  N   THR A1033      19.927  37.821  77.030  1.00103.64           N  
ANISOU  263  N   THR A1033    12005  12280  15094   1675    820   -649       N  
ATOM    264  CA  THR A1033      19.359  38.726  78.028  1.00103.16           C  
ANISOU  264  CA  THR A1033    11972  12294  14929   1659    736   -605       C  
ATOM    265  C   THR A1033      18.844  37.976  79.271  1.00104.24           C  
ANISOU  265  C   THR A1033    12170  12347  15089   1603    782   -557       C  
ATOM    266  O   THR A1033      18.770  38.546  80.368  1.00104.02           O  
ANISOU  266  O   THR A1033    12176  12344  15005   1604    710   -466       O  
ATOM    267  CB  THR A1033      18.254  39.621  77.425  1.00101.77           C  
ANISOU  267  CB  THR A1033    11764  12280  14623   1652    708   -738       C  
ATOM    268  OG1 THR A1033      18.790  40.354  76.319  1.00101.28           O  
ANISOU  268  OG1 THR A1033    11673  12281  14529   1726    679   -761       O  
ATOM    269  CG2 THR A1033      17.726  40.608  78.454  1.00100.93           C  
ANISOU  269  CG2 THR A1033    11701  12242  14406   1648    629   -682       C  
ATOM    270  N   SER A1034      18.519  36.697  79.107  1.00104.03           N  
ANISOU  270  N   SER A1034    12171  12212  15145   1550    920   -621       N  
ATOM    271  CA  SER A1034      17.902  35.958  80.189  1.00105.35           C  
ANISOU  271  CA  SER A1034    12419  12284  15327   1487   1000   -597       C  
ATOM    272  C   SER A1034      18.895  35.476  81.246  1.00106.88           C  
ANISOU  272  C   SER A1034    12690  12345  15573   1575   1005   -393       C  
ATOM    273  O   SER A1034      19.851  34.764  80.943  1.00107.32           O  
ANISOU  273  O   SER A1034    12767  12299  15710   1653   1065   -322       O  
ATOM    274  CB  SER A1034      17.076  34.800  79.652  1.00107.19           C  
ANISOU  274  CB  SER A1034    12671  12444  15611   1373   1182   -765       C  
ATOM    275  OG  SER A1034      16.450  34.117  80.723  1.00109.09           O  
ANISOU  275  OG  SER A1034    13011  12578  15860   1299   1283   -750       O  
ATOM    276  N   LYS A1035      18.642  35.874  82.491  1.00107.41           N  
ANISOU  276  N   LYS A1035    12798  12435  15579   1575    942   -302       N  
ATOM    277  CA  LYS A1035      19.457  35.479  83.635  1.00108.70           C  
ANISOU  277  CA  LYS A1035    13026  12518  15757   1674    939   -110       C  
ATOM    278  C   LYS A1035      19.226  34.017  84.051  1.00112.66           C  
ANISOU  278  C   LYS A1035    13659  12817  16328   1675   1135    -82       C  
ATOM    279  O   LYS A1035      19.961  33.477  84.890  1.00114.54           O  
ANISOU  279  O   LYS A1035    13971  12975  16575   1799   1167     89       O  
ATOM    280  CB  LYS A1035      19.233  36.433  84.812  1.00107.56           C  
ANISOU  280  CB  LYS A1035    12876  12478  15513   1668    810    -32       C  
ATOM    281  CG  LYS A1035      17.772  36.621  85.214  1.00107.76           C  
ANISOU  281  CG  LYS A1035    12935  12525  15484   1544    832   -139       C  
ATOM    282  CD  LYS A1035      17.619  37.395  86.524  1.00106.57           C  
ANISOU  282  CD  LYS A1035    12801  12447  15245   1548    724    -40       C  
ATOM    283  CE  LYS A1035      17.839  36.499  87.734  1.00107.75           C  
ANISOU  283  CE  LYS A1035    13050  12477  15414   1603    796    101       C  
ATOM    284  NZ  LYS A1035      17.109  37.013  88.931  1.00107.80           N  
ANISOU  284  NZ  LYS A1035    13089  12531  15338   1553    739    134       N  
ATOM    285  N   THR A1036      18.209  33.379  83.468  1.00113.74           N  
ANISOU  285  N   THR A1036    13832  12883  16501   1541   1281   -255       N  
ATOM    286  CA  THR A1036      18.015  31.941  83.634  1.00116.23           C  
ANISOU  286  CA  THR A1036    14295  12975  16891   1516   1518   -261       C  
ATOM    287  C   THR A1036      18.895  31.233  82.599  1.00118.39           C  
ANISOU  287  C   THR A1036    14573  13153  17255   1587   1612   -260       C  
ATOM    288  O   THR A1036      19.206  30.037  82.725  1.00120.26           O  
ANISOU  288  O   THR A1036    14953  13180  17558   1636   1811   -202       O  
ATOM    289  CB  THR A1036      16.545  31.512  83.431  1.00116.93           C  
ANISOU  289  CB  THR A1036    14413  13040  16974   1305   1666   -483       C  
ATOM    290  OG1 THR A1036      15.680  32.649  83.495  1.00117.86           O  
ANISOU  290  OG1 THR A1036    14415  13375  16993   1224   1508   -583       O  
ATOM    291  CG2 THR A1036      16.120  30.507  84.500  1.00118.72           C  
ANISOU  291  CG2 THR A1036    14828  13060  17219   1269   1863   -431       C  
ATOM    292  N   PHE A1037      19.295  31.999  81.581  1.00116.76           N  
ANISOU  292  N   PHE A1037    14223  13095  17045   1600   1478   -321       N  
ATOM    293  CA  PHE A1037      20.113  31.512  80.471  1.00116.40           C  
ANISOU  293  CA  PHE A1037    14153  12995  17079   1658   1537   -338       C  
ATOM    294  C   PHE A1037      21.607  31.724  80.742  1.00116.08           C  
ANISOU  294  C   PHE A1037    14085  12976  17042   1858   1431   -132       C  
ATOM    295  O   PHE A1037      22.441  30.965  80.254  1.00117.37           O  
ANISOU  295  O   PHE A1037    14283  13038  17275   1956   1523    -79       O  
ATOM    296  CB  PHE A1037      19.681  32.218  79.174  1.00114.69           C  
ANISOU  296  CB  PHE A1037    13795  12939  16844   1566   1461   -528       C  
ATOM    297  CG  PHE A1037      20.288  31.647  77.925  1.00115.09           C  
ANISOU  297  CG  PHE A1037    13819  12932  16977   1589   1544   -589       C  
ATOM    298  CD1 PHE A1037      19.767  30.492  77.340  1.00116.84           C  
ANISOU  298  CD1 PHE A1037    14107  13018  17268   1480   1767   -734       C  
ATOM    299  CD2 PHE A1037      21.363  32.275  77.316  1.00114.15           C  
ANISOU  299  CD2 PHE A1037    13611  12898  16865   1701   1414   -518       C  
ATOM    300  CE1 PHE A1037      20.318  29.969  76.183  1.00116.55           C  
ANISOU  300  CE1 PHE A1037    14047  12929  17307   1495   1848   -795       C  
ATOM    301  CE2 PHE A1037      21.923  31.757  76.157  1.00115.40           C  
ANISOU  301  CE2 PHE A1037    13742  13005  17099   1723   1488   -575       C  
ATOM    302  CZ  PHE A1037      21.401  30.602  75.590  1.00116.32           C  
ANISOU  302  CZ  PHE A1037    13926  12985  17286   1626   1700   -709       C  
HETATM  303  N   MSE A1038      21.938  32.743  81.534  1.00115.12           N  
ANISOU  303  N   MSE A1038    13899  13002  16838   1914   1248    -27       N  
HETATM  304  CA  MSE A1038      23.344  33.110  81.796  1.00114.70           C  
ANISOU  304  CA  MSE A1038    13779  13039  16762   2078   1131    132       C  
HETATM  305  C   MSE A1038      24.009  32.280  82.878  1.00114.85           C  
ANISOU  305  C   MSE A1038    13892  12977  16769   2247   1199    325       C  
HETATM  306  O   MSE A1038      25.230  32.331  83.052  1.00113.64           O  
ANISOU  306  O   MSE A1038    13677  12913  16590   2408   1133    452       O  
HETATM  307  CB  MSE A1038      23.433  34.603  82.140  1.00112.53           C  
ANISOU  307  CB  MSE A1038    13393  12972  16392   2043    927    135       C  
HETATM  308  CG  MSE A1038      23.163  35.499  80.929  1.00111.62           C  
ANISOU  308  CG  MSE A1038    13189  12950  16272   1948    861    -18       C  
HETATM  309 SE   MSE A1038      24.654  35.464  79.634  1.00112.77          SE  
ANISOU  309 SE   MSE A1038    13239  13126  16481   2044    845    -12      SE  
HETATM  310  CE  MSE A1038      23.893  34.102  78.436  1.00113.31           C  
ANISOU  310  CE  MSE A1038    13378  13008  16666   1983   1052   -156       C  
ATOM    311  N   GLN A1039      23.210  31.505  83.602  1.00115.64           N  
ANISOU  311  N   GLN A1039    14142  12923  16875   2220   1343    344       N  
ATOM    312  CA  GLN A1039      23.697  30.732  84.742  1.00117.98           C  
ANISOU  312  CA  GLN A1039    14557  13134  17135   2401   1427    540       C  
ATOM    313  C   GLN A1039      23.603  29.215  84.489  1.00120.74           C  
ANISOU  313  C   GLN A1039    15102  13207  17564   2456   1707    558       C  
ATOM    314  O   GLN A1039      23.742  28.406  85.414  1.00122.61           O  
ANISOU  314  O   GLN A1039    15499  13315  17771   2600   1842    709       O  
ATOM    315  CB  GLN A1039      22.932  31.139  86.015  1.00117.70           C  
ANISOU  315  CB  GLN A1039    14565  13137  17020   2349   1376    580       C  
ATOM    316  CG  GLN A1039      22.884  32.649  86.267  1.00115.11           C  
ANISOU  316  CG  GLN A1039    14072  13053  16612   2269   1132    543       C  
ATOM    317  CD  GLN A1039      21.994  33.046  87.440  1.00114.88           C  
ANISOU  317  CD  GLN A1039    14091  13049  16511   2195   1092    561       C  
ATOM    318  OE1 GLN A1039      21.964  32.377  88.484  1.00115.63           O  
ANISOU  318  OE1 GLN A1039    14306  13056  16573   2293   1179    689       O  
ATOM    319  NE2 GLN A1039      21.269  34.152  87.278  1.00112.31           N  
ANISOU  319  NE2 GLN A1039    13681  12842  16149   2036    968    438       N  
ATOM    320  N   SER A1040      23.373  28.841  83.229  1.00120.81           N  
ANISOU  320  N   SER A1040    15109  13126  17667   2345   1809    402       N  
ATOM    321  CA  SER A1040      23.270  27.438  82.823  1.00122.40           C  
ANISOU  321  CA  SER A1040    15499  13055  17951   2359   2099    383       C  
ATOM    322  C   SER A1040      23.797  27.235  81.404  1.00123.13           C  
ANISOU  322  C   SER A1040    15520  13138  18127   2348   2128    288       C  
ATOM    323  O   SER A1040      24.404  26.203  81.098  1.00127.76           O  
ANISOU  323  O   SER A1040    16228  13549  18765   2474   2313    358       O  
ATOM    324  CB  SER A1040      21.822  26.961  82.911  1.00122.54           C  
ANISOU  324  CB  SER A1040    15643  12918  17997   2126   2286    213       C  
ATOM    325  OG  SER A1040      21.296  27.178  84.208  1.00122.39           O  
ANISOU  325  OG  SER A1040    15691  12910  17904   2126   2258    294       O  
ATOM    326  N   PHE A1041      23.551  28.218  80.543  1.00119.91           N  
ANISOU  326  N   PHE A1041    14925  12911  17723   2207   1955    134       N  
ATOM    327  CA  PHE A1041      24.097  28.229  79.189  1.00119.65           C  
ANISOU  327  CA  PHE A1041    14797  12911  17755   2201   1943     46       C  
ATOM    328  C   PHE A1041      24.997  29.459  78.997  1.00118.29           C  
ANISOU  328  C   PHE A1041    14429  12986  17531   2283   1676    104       C  
ATOM    329  O   PHE A1041      25.070  30.034  77.897  1.00116.41           O  
ANISOU  329  O   PHE A1041    14068  12847  17315   2209   1594    -19       O  
ATOM    330  CB  PHE A1041      22.966  28.218  78.151  1.00119.19           C  
ANISOU  330  CB  PHE A1041    14703  12845  17739   1959   2018   -218       C  
ATOM    331  CG  PHE A1041      22.240  26.902  78.045  1.00121.13           C  
ANISOU  331  CG  PHE A1041    15130  12846  18049   1846   2322   -321       C  
ATOM    332  CD1 PHE A1041      21.357  26.488  79.046  1.00121.90           C  
ANISOU  332  CD1 PHE A1041    15368  12831  18118   1764   2452   -326       C  
ATOM    333  CD2 PHE A1041      22.419  26.084  76.928  1.00121.28           C  
ANISOU  333  CD2 PHE A1041    15185  12742  18155   1802   2498   -431       C  
ATOM    334  CE1 PHE A1041      20.686  25.277  78.941  1.00123.74           C  
ANISOU  334  CE1 PHE A1041    15783  12824  18406   1632   2767   -443       C  
ATOM    335  CE2 PHE A1041      21.747  24.875  76.818  1.00122.90           C  
ANISOU  335  CE2 PHE A1041    15568  12711  18416   1669   2811   -550       C  
ATOM    336  CZ  PHE A1041      20.881  24.470  77.826  1.00124.03           C  
ANISOU  336  CZ  PHE A1041    15860  12736  18528   1578   2954   -560       C  
ATOM    337  N   GLY A1042      25.676  29.850  80.078  1.00117.39           N  
ANISOU  337  N   GLY A1042    14290  12974  17338   2432   1557    282       N  
ATOM    338  CA  GLY A1042      26.590  30.996  80.069  1.00116.37           C  
ANISOU  338  CA  GLY A1042    13984  13086  17146   2493   1330    330       C  
ATOM    339  C   GLY A1042      27.876  30.757  79.292  1.00116.20           C  
ANISOU  339  C   GLY A1042    13888  13103  17160   2630   1323    378       C  
ATOM    340  O   GLY A1042      28.136  31.426  78.287  1.00114.54           O  
ANISOU  340  O   GLY A1042    13560  12987  16972   2558   1237    274       O  
ATOM    341  N   VAL A1043      28.674  29.795  79.757  1.00117.76           N  
ANISOU  341  N   VAL A1043    14161  13228  17352   2843   1425    538       N  
ATOM    342  CA  VAL A1043      29.953  29.445  79.121  1.00119.06           C  
ANISOU  342  CA  VAL A1043    14260  13440  17539   3009   1431    601       C  
ATOM    343  C   VAL A1043      29.817  29.052  77.635  1.00120.20           C  
ANISOU  343  C   VAL A1043    14415  13454  17801   2911   1533    457       C  
ATOM    344  O   VAL A1043      30.716  29.330  76.830  1.00121.23           O  
ANISOU  344  O   VAL A1043    14425  13687  17949   2958   1463    439       O  
ATOM    345  CB  VAL A1043      30.736  28.371  79.937  1.00120.41           C  
ANISOU  345  CB  VAL A1043    14538  13552  17662   3297   1552    813       C  
ATOM    346  CG1 VAL A1043      30.085  26.992  79.836  1.00122.01           C  
ANISOU  346  CG1 VAL A1043    14993  13423  17944   3316   1838    825       C  
ATOM    347  CG2 VAL A1043      32.198  28.317  79.511  1.00120.25           C  
ANISOU  347  CG2 VAL A1043    14387  13689  17613   3496   1492    891       C  
ATOM    348  N   TYR A1044      28.697  28.420  77.278  1.00120.15           N  
ANISOU  348  N   TYR A1044    14545  13240  17868   2766   1702    342       N  
ATOM    349  CA  TYR A1044      28.408  28.070  75.886  1.00120.29           C  
ANISOU  349  CA  TYR A1044    14562  13156  17984   2643   1803    175       C  
ATOM    350  C   TYR A1044      28.481  29.312  74.992  1.00120.53           C  
ANISOU  350  C   TYR A1044    14405  13389  18004   2530   1608     48       C  
ATOM    351  O   TYR A1044      29.246  29.346  74.016  1.00121.29           O  
ANISOU  351  O   TYR A1044    14422  13521  18142   2571   1588     20       O  
ATOM    352  CB  TYR A1044      27.019  27.428  75.766  1.00119.05           C  
ANISOU  352  CB  TYR A1044    14542  12816  17876   2452   1992     25       C  
ATOM    353  CG  TYR A1044      26.903  26.023  76.333  1.00120.41           C  
ANISOU  353  CG  TYR A1044    14949  12719  18083   2532   2265    112       C  
ATOM    354  CD1 TYR A1044      26.983  25.795  77.707  1.00121.05           C  
ANISOU  354  CD1 TYR A1044    15140  12759  18093   2670   2289    291       C  
ATOM    355  CD2 TYR A1044      26.683  24.924  75.496  1.00119.85           C  
ANISOU  355  CD2 TYR A1044    15004  12427  18105   2467   2521      8       C  
ATOM    356  CE1 TYR A1044      26.869  24.515  78.226  1.00122.72           C  
ANISOU  356  CE1 TYR A1044    15599  12703  18325   2761   2568    380       C  
ATOM    357  CE2 TYR A1044      26.564  23.645  76.009  1.00121.08           C  
ANISOU  357  CE2 TYR A1044    15411  12305  18288   2534   2811     83       C  
ATOM    358  CZ  TYR A1044      26.658  23.446  77.374  1.00122.58           C  
ANISOU  358  CZ  TYR A1044    15726  12445  18404   2690   2838    276       C  
ATOM    359  OH  TYR A1044      26.540  22.182  77.909  1.00124.54           O  
ANISOU  359  OH  TYR A1044    16256  12397  18666   2779   3152    365       O  
ATOM    360  N   THR A1045      27.700  30.332  75.360  1.00119.48           N  
ANISOU  360  N   THR A1045    14214  13379  17804   2402   1477    -19       N  
ATOM    361  CA  THR A1045      27.540  31.553  74.574  1.00116.75           C  
ANISOU  361  CA  THR A1045    13733  13199  17427   2295   1327   -142       C  
ATOM    362  C   THR A1045      28.815  32.396  74.532  1.00117.46           C  
ANISOU  362  C   THR A1045    13698  13457  17476   2392   1171    -60       C  
ATOM    363  O   THR A1045      29.211  32.869  73.469  1.00116.63           O  
ANISOU  363  O   THR A1045    13510  13413  17389   2365   1129   -140       O  
ATOM    364  CB  THR A1045      26.384  32.418  75.115  1.00114.05           C  
ANISOU  364  CB  THR A1045    13386  12942  17007   2164   1244   -213       C  
ATOM    365  OG1 THR A1045      25.293  31.582  75.507  1.00113.94           O  
ANISOU  365  OG1 THR A1045    13487  12790  17014   2082   1391   -268       O  
ATOM    366  CG2 THR A1045      25.903  33.371  74.057  1.00112.58           C  
ANISOU  366  CG2 THR A1045    13111  12873  16791   2062   1168   -370       C  
ATOM    367  N   THR A1046      29.451  32.582  75.687  1.00119.65           N  
ANISOU  367  N   THR A1046    13957  13820  17685   2498   1097     88       N  
ATOM    368  CA  THR A1046      30.659  33.405  75.787  1.00122.22           C  
ANISOU  368  CA  THR A1046    14146  14343  17950   2565    958    143       C  
ATOM    369  C   THR A1046      31.819  32.848  74.933  1.00124.35           C  
ANISOU  369  C   THR A1046    14358  14611  18276   2682   1000    166       C  
ATOM    370  O   THR A1046      32.780  33.568  74.615  1.00123.41           O  
ANISOU  370  O   THR A1046    14112  14657  18123   2695    903    154       O  
ATOM    371  CB  THR A1046      31.096  33.580  77.258  1.00125.39           C  
ANISOU  371  CB  THR A1046    14523  14868  18252   2662    882    285       C  
ATOM    372  OG1 THR A1046      29.942  33.799  78.080  1.00126.37           O  
ANISOU  372  OG1 THR A1046    14730  14945  18339   2570    877    277       O  
ATOM    373  CG2 THR A1046      32.045  34.772  77.410  1.00126.27           C  
ANISOU  373  CG2 THR A1046    14476  15226  18275   2644    730    276       C  
ATOM    374  N   LEU A1047      31.717  31.570  74.563  1.00124.90           N  
ANISOU  374  N   LEU A1047    14532  14493  18431   2756   1162    188       N  
ATOM    375  CA  LEU A1047      32.661  30.951  73.633  1.00123.80           C  
ANISOU  375  CA  LEU A1047    14361  14319  18357   2860   1227    197       C  
ATOM    376  C   LEU A1047      32.109  30.937  72.197  1.00122.35           C  
ANISOU  376  C   LEU A1047    14186  14038  18265   2718   1288     26       C  
ATOM    377  O   LEU A1047      32.859  30.749  71.232  1.00121.45           O  
ANISOU  377  O   LEU A1047    14017  13926  18201   2762   1309     -2       O  
ATOM    378  CB  LEU A1047      33.045  29.544  74.106  1.00125.88           C  
ANISOU  378  CB  LEU A1047    14746  14437  18645   3060   1389    341       C  
ATOM    379  CG  LEU A1047      33.802  29.437  75.442  1.00128.31           C  
ANISOU  379  CG  LEU A1047    15031  14879  18841   3268   1336    530       C  
ATOM    380  CD1 LEU A1047      34.043  27.970  75.793  1.00131.47           C  
ANISOU  380  CD1 LEU A1047    15600  15093  19259   3490   1540    676       C  
ATOM    381  CD2 LEU A1047      35.130  30.186  75.401  1.00128.36           C  
ANISOU  381  CD2 LEU A1047    14830  15172  18770   3354   1175    558       C  
ATOM    382  N   PHE A1048      30.800  31.141  72.065  1.00120.27           N  
ANISOU  382  N   PHE A1048    13979  13711  18007   2555   1315    -93       N  
ATOM    383  CA  PHE A1048      30.170  31.336  70.765  1.00119.34           C  
ANISOU  383  CA  PHE A1048    13839  13572  17935   2421   1346   -272       C  
ATOM    384  C   PHE A1048      30.575  32.732  70.271  1.00116.44           C  
ANISOU  384  C   PHE A1048    13348  13388  17507   2382   1183   -320       C  
ATOM    385  O   PHE A1048      30.907  32.926  69.094  1.00114.45           O  
ANISOU  385  O   PHE A1048    13041  13157  17288   2365   1185   -404       O  
ATOM    386  CB  PHE A1048      28.647  31.228  70.919  1.00121.41           C  
ANISOU  386  CB  PHE A1048    14172  13773  18184   2274   1410   -389       C  
ATOM    387  CG  PHE A1048      27.902  30.963  69.634  1.00123.45           C  
ANISOU  387  CG  PHE A1048    14419  14000  18486   2155   1501   -583       C  
ATOM    388  CD1 PHE A1048      27.414  29.685  69.350  1.00126.26           C  
ANISOU  388  CD1 PHE A1048    14871  14182  18919   2102   1706   -657       C  
ATOM    389  CD2 PHE A1048      27.652  31.992  68.725  1.00122.87           C  
ANISOU  389  CD2 PHE A1048    14247  14076  18362   2096   1398   -700       C  
ATOM    390  CE1 PHE A1048      26.709  29.435  68.175  1.00126.97           C  
ANISOU  390  CE1 PHE A1048    14928  14279  19035   1976   1793   -861       C  
ATOM    391  CE2 PHE A1048      26.953  31.745  67.546  1.00124.68           C  
ANISOU  391  CE2 PHE A1048    14448  14316  18609   2005   1477   -884       C  
ATOM    392  CZ  PHE A1048      26.478  30.465  67.272  1.00125.56           C  
ANISOU  392  CZ  PHE A1048    14625  14285  18796   1936   1667   -974       C  
ATOM    393  N   ASN A1049      30.566  33.685  71.204  1.00114.08           N  
ANISOU  393  N   ASN A1049    13020  13211  17116   2367   1061   -265       N  
ATOM    394  CA  ASN A1049      30.907  35.085  70.949  1.00111.93           C  
ANISOU  394  CA  ASN A1049    12667  13093  16769   2317    937   -305       C  
ATOM    395  C   ASN A1049      32.378  35.315  70.672  1.00111.54           C  
ANISOU  395  C   ASN A1049    12520  13138  16722   2390    892   -258       C  
ATOM    396  O   ASN A1049      32.758  36.306  70.039  1.00110.48           O  
ANISOU  396  O   ASN A1049    12333  13092  16552   2335    840   -324       O  
ATOM    397  CB  ASN A1049      30.475  35.942  72.132  1.00111.10           C  
ANISOU  397  CB  ASN A1049    12575  13076  16564   2270    846   -262       C  
ATOM    398  CG  ASN A1049      28.987  36.192  72.138  1.00110.08           C  
ANISOU  398  CG  ASN A1049    12514  12910  16402   2172    864   -351       C  
ATOM    399  OD1 ASN A1049      28.466  36.884  71.258  1.00109.88           O  
ANISOU  399  OD1 ASN A1049    12483  12922  16344   2114    855   -463       O  
ATOM    400  ND2 ASN A1049      28.289  35.622  73.119  1.00108.56           N  
ANISOU  400  ND2 ASN A1049    12387  12655  16206   2166    896   -304       N  
ATOM    401  N   GLN A1050      33.195  34.396  71.173  1.00113.18           N  
ANISOU  401  N   GLN A1050    12711  13333  16959   2523    924   -143       N  
ATOM    402  CA  GLN A1050      34.620  34.375  70.900  1.00112.78           C  
ANISOU  402  CA  GLN A1050    12553  13392  16909   2618    896   -100       C  
ATOM    403  C   GLN A1050      34.892  33.615  69.602  1.00112.31           C  
ANISOU  403  C   GLN A1050    12502  13218  16954   2655    992   -152       C  
ATOM    404  O   GLN A1050      35.917  33.827  68.957  1.00112.36           O  
ANISOU  404  O   GLN A1050    12414  13309  16967   2688    968   -170       O  
ATOM    405  CB  GLN A1050      35.371  33.767  72.084  1.00114.23           C  
ANISOU  405  CB  GLN A1050    12704  13656  17043   2782    883     54       C  
ATOM    406  CG  GLN A1050      36.867  34.041  72.082  1.00116.61           C  
ANISOU  406  CG  GLN A1050    12846  14170  17290   2871    817     86       C  
ATOM    407  CD  GLN A1050      37.207  35.510  71.909  1.00115.28           C  
ANISOU  407  CD  GLN A1050    12576  14175  17052   2714    716    -21       C  
ATOM    408  OE1 GLN A1050      36.543  36.384  72.469  1.00113.94           O  
ANISOU  408  OE1 GLN A1050    12437  14034  16821   2591    664    -55       O  
ATOM    409  NE2 GLN A1050      38.257  35.789  71.135  1.00115.47           N  
ANISOU  409  NE2 GLN A1050    12488  14306  17078   2713    705    -78       N  
ATOM    410  N   ILE A1051      33.956  32.749  69.218  1.00112.67           N  
ANISOU  410  N   ILE A1051    12656  13079  17074   2631   1109   -192       N  
ATOM    411  CA  ILE A1051      33.981  32.110  67.897  1.00113.28           C  
ANISOU  411  CA  ILE A1051    12750  13045  17248   2624   1210   -278       C  
ATOM    412  C   ILE A1051      33.557  33.098  66.795  1.00110.95           C  
ANISOU  412  C   ILE A1051    12411  12805  16938   2495   1161   -429       C  
ATOM    413  O   ILE A1051      34.248  33.232  65.777  1.00109.16           O  
ANISOU  413  O   ILE A1051    12127  12605  16746   2508   1164   -477       O  
ATOM    414  CB  ILE A1051      33.160  30.781  67.874  1.00114.37           C  
ANISOU  414  CB  ILE A1051    13022  12971  17464   2625   1384   -291       C  
ATOM    415  CG1 ILE A1051      34.021  29.621  68.394  1.00115.85           C  
ANISOU  415  CG1 ILE A1051    13264  13069  17683   2814   1484   -138       C  
ATOM    416  CG2 ILE A1051      32.647  30.452  66.475  1.00113.46           C  
ANISOU  416  CG2 ILE A1051    12917  12770  17422   2529   1478   -452       C  
ATOM    417  CD1 ILE A1051      33.288  28.307  68.586  1.00116.79           C  
ANISOU  417  CD1 ILE A1051    13557  12952  17867   2820   1693   -130       C  
ATOM    418  N   VAL A1052      32.447  33.805  67.020  1.00110.35           N  
ANISOU  418  N   VAL A1052    12370  12759  16801   2389   1122   -497       N  
ATOM    419  CA  VAL A1052      31.891  34.731  66.016  1.00110.84           C  
ANISOU  419  CA  VAL A1052    12414  12880  16820   2303   1093   -630       C  
ATOM    420  C   VAL A1052      32.832  35.890  65.657  1.00109.77           C  
ANISOU  420  C   VAL A1052    12216  12859  16632   2305   1011   -628       C  
ATOM    421  O   VAL A1052      33.015  36.207  64.477  1.00107.59           O  
ANISOU  421  O   VAL A1052    11920  12594  16366   2295   1031   -712       O  
ATOM    422  CB  VAL A1052      30.484  35.237  66.418  1.00111.22           C  
ANISOU  422  CB  VAL A1052    12513  12956  16789   2221   1073   -693       C  
ATOM    423  CG1 VAL A1052      30.137  36.526  65.687  1.00110.93           C  
ANISOU  423  CG1 VAL A1052    12465  13024  16658   2185   1020   -781       C  
ATOM    424  CG2 VAL A1052      29.436  34.164  66.129  1.00111.79           C  
ANISOU  424  CG2 VAL A1052    12629  12934  16913   2174   1189   -784       C  
ATOM    425  N   ILE A1053      33.432  36.510  66.670  1.00110.58           N  
ANISOU  425  N   ILE A1053    12291  13052  16674   2310    933   -544       N  
ATOM    426  CA  ILE A1053      34.449  37.540  66.436  1.00111.47           C  
ANISOU  426  CA  ILE A1053    12342  13276  16735   2285    884   -557       C  
ATOM    427  C   ILE A1053      35.634  37.018  65.603  1.00113.33           C  
ANISOU  427  C   ILE A1053    12500  13517  17044   2347    917   -560       C  
ATOM    428  O   ILE A1053      36.075  37.687  64.666  1.00113.84           O  
ANISOU  428  O   ILE A1053    12546  13611  17098   2309    928   -634       O  
ATOM    429  CB  ILE A1053      34.925  38.213  67.753  1.00110.97           C  
ANISOU  429  CB  ILE A1053    12242  13336  16585   2260    807   -487       C  
ATOM    430  CG1 ILE A1053      35.723  39.484  67.447  1.00111.38           C  
ANISOU  430  CG1 ILE A1053    12258  13497  16566   2178    789   -548       C  
ATOM    431  CG2 ILE A1053      35.734  37.255  68.620  1.00111.43           C  
ANISOU  431  CG2 ILE A1053    12226  13442  16669   2369    791   -372       C  
ATOM    432  CD1 ILE A1053      35.750  40.484  68.581  1.00112.60           C  
ANISOU  432  CD1 ILE A1053    12415  13759  16610   2094    737   -533       C  
ATOM    433  N   THR A1054      36.119  35.817  65.929  1.00115.09           N  
ANISOU  433  N   THR A1054    12691  13703  17334   2453    947   -477       N  
ATOM    434  CA  THR A1054      37.287  35.229  65.258  1.00116.08           C  
ANISOU  434  CA  THR A1054    12739  13844  17522   2538    979   -463       C  
ATOM    435  C   THR A1054      37.029  34.929  63.780  1.00116.15           C  
ANISOU  435  C   THR A1054    12777  13743  17610   2517   1055   -563       C  
ATOM    436  O   THR A1054      37.861  35.250  62.927  1.00116.57           O  
ANISOU  436  O   THR A1054    12769  13845  17678   2514   1056   -610       O  
ATOM    437  CB  THR A1054      37.789  33.964  65.985  1.00116.59           C  
ANISOU  437  CB  THR A1054    12791  13883  17623   2695   1016   -334       C  
ATOM    438  OG1 THR A1054      38.115  34.296  67.342  1.00117.12           O  
ANISOU  438  OG1 THR A1054    12811  14093  17596   2731    937   -244       O  
ATOM    439  CG2 THR A1054      39.030  33.403  65.303  1.00117.32           C  
ANISOU  439  CG2 THR A1054    12799  14013  17764   2803   1049   -316       C  
ATOM    440  N   ILE A1055      35.875  34.325  63.491  1.00115.71           N  
ANISOU  440  N   ILE A1055    12807  13560  17598   2493   1122   -608       N  
ATOM    441  CA  ILE A1055      35.468  34.017  62.116  1.00114.11           C  
ANISOU  441  CA  ILE A1055    12622  13280  17454   2463   1197   -723       C  
ATOM    442  C   ILE A1055      35.301  35.302  61.296  1.00112.97           C  
ANISOU  442  C   ILE A1055    12469  13217  17237   2394   1153   -820       C  
ATOM    443  O   ILE A1055      35.745  35.375  60.151  1.00112.14           O  
ANISOU  443  O   ILE A1055    12335  13110  17162   2401   1184   -884       O  
ATOM    444  CB  ILE A1055      34.183  33.153  62.085  1.00112.94           C  
ANISOU  444  CB  ILE A1055    12552  13018  17343   2423   1287   -780       C  
ATOM    445  CG1 ILE A1055      34.441  31.810  62.778  1.00112.36           C  
ANISOU  445  CG1 ILE A1055    12527  12821  17345   2503   1378   -681       C  
ATOM    446  CG2 ILE A1055      33.704  32.935  60.649  1.00113.26           C  
ANISOU  446  CG2 ILE A1055    12586  13029  17417   2378   1359   -928       C  
ATOM    447  CD1 ILE A1055      33.205  30.963  62.983  1.00112.51           C  
ANISOU  447  CD1 ILE A1055    12641  12716  17392   2437   1494   -740       C  
ATOM    448  N   PHE A1056      34.676  36.309  61.903  1.00113.22           N  
ANISOU  448  N   PHE A1056    12539  13313  17167   2340   1094   -822       N  
ATOM    449  CA  PHE A1056      34.506  37.626  61.286  1.00113.31           C  
ANISOU  449  CA  PHE A1056    12581  13388  17084   2297   1076   -892       C  
ATOM    450  C   PHE A1056      35.860  38.237  60.926  1.00113.61           C  
ANISOU  450  C   PHE A1056    12572  13476  17119   2291   1068   -885       C  
ATOM    451  O   PHE A1056      36.097  38.614  59.779  1.00112.45           O  
ANISOU  451  O   PHE A1056    12433  13323  16968   2293   1110   -956       O  
ATOM    452  CB  PHE A1056      33.742  38.568  62.231  1.00113.01           C  
ANISOU  452  CB  PHE A1056    12607  13399  16934   2252   1025   -871       C  
ATOM    453  CG  PHE A1056      32.244  38.356  62.252  1.00112.76           C  
ANISOU  453  CG  PHE A1056    12625  13356  16864   2246   1039   -924       C  
ATOM    454  CD1 PHE A1056      31.653  37.267  61.605  1.00112.96           C  
ANISOU  454  CD1 PHE A1056    12629  13334  16958   2258   1101   -993       C  
ATOM    455  CD2 PHE A1056      31.424  39.238  62.953  1.00111.54           C  
ANISOU  455  CD2 PHE A1056    12533  13251  16596   2219   1001   -916       C  
ATOM    456  CE1 PHE A1056      30.278  37.081  61.637  1.00112.24           C  
ANISOU  456  CE1 PHE A1056    12560  13270  16816   2232   1121  -1070       C  
ATOM    457  CE2 PHE A1056      30.051  39.053  62.991  1.00111.77           C  
ANISOU  457  CE2 PHE A1056    12588  13303  16575   2217   1011   -975       C  
ATOM    458  CZ  PHE A1056      29.477  37.973  62.331  1.00112.31           C  
ANISOU  458  CZ  PHE A1056    12617  13348  16706   2218   1070  -1060       C  
ATOM    459  N   THR A1057      36.751  38.326  61.909  1.00114.81           N  
ANISOU  459  N   THR A1057    12665  13695  17262   2284   1021   -810       N  
ATOM    460  CA  THR A1057      38.065  38.902  61.680  1.00115.17           C  
ANISOU  460  CA  THR A1057    12641  13826  17291   2254   1020   -826       C  
ATOM    461  C   THR A1057      38.673  38.239  60.451  1.00115.86           C  
ANISOU  461  C   THR A1057    12682  13869  17470   2307   1071   -865       C  
ATOM    462  O   THR A1057      39.085  38.926  59.518  1.00116.67           O  
ANISOU  462  O   THR A1057    12799  13979  17553   2268   1111   -938       O  
ATOM    463  CB  THR A1057      38.990  38.744  62.900  1.00116.79           C  
ANISOU  463  CB  THR A1057    12743  14156  17476   2265    961   -749       C  
ATOM    464  OG1 THR A1057      38.285  39.113  64.093  1.00115.00           O  
ANISOU  464  OG1 THR A1057    12561  13955  17179   2230    913   -703       O  
ATOM    465  CG2 THR A1057      40.235  39.629  62.747  1.00118.71           C  
ANISOU  465  CG2 THR A1057    12907  14533  17664   2186    966   -807       C  
ATOM    466  N   ILE A1058      38.693  36.902  60.460  1.00115.91           N  
ANISOU  466  N   ILE A1058    12653  13815  17572   2397   1088   -815       N  
ATOM    467  CA  ILE A1058      39.129  36.075  59.327  1.00113.49           C  
ANISOU  467  CA  ILE A1058    12315  13443  17364   2455   1150   -849       C  
ATOM    468  C   ILE A1058      38.420  36.492  58.039  1.00111.78           C  
ANISOU  468  C   ILE A1058    12162  13169  17139   2415   1198   -960       C  
ATOM    469  O   ILE A1058      39.066  36.673  57.008  1.00109.83           O  
ANISOU  469  O   ILE A1058    11889  12927  16916   2417   1231  -1014       O  
ATOM    470  CB  ILE A1058      38.877  34.568  59.613  1.00114.37           C  
ANISOU  470  CB  ILE A1058    12436  13452  17567   2547   1198   -784       C  
ATOM    471  CG1 ILE A1058      39.876  34.018  60.656  1.00115.30           C  
ANISOU  471  CG1 ILE A1058    12482  13643  17685   2650   1168   -659       C  
ATOM    472  CG2 ILE A1058      38.848  33.742  58.326  1.00114.92           C  
ANISOU  472  CG2 ILE A1058    12515  13416  17734   2575   1288   -850       C  
ATOM    473  CD1 ILE A1058      41.346  34.159  60.304  1.00116.31           C  
ANISOU  473  CD1 ILE A1058    12487  13894  17812   2696   1150   -656       C  
ATOM    474  N   GLU A1059      37.099  36.671  58.132  1.00111.53           N  
ANISOU  474  N   GLU A1059    12208  13108  17061   2388   1200   -994       N  
ATOM    475  CA  GLU A1059      36.241  37.058  57.002  1.00109.68           C  
ANISOU  475  CA  GLU A1059    12025  12865  16783   2380   1241  -1101       C  
ATOM    476  C   GLU A1059      36.534  38.476  56.509  1.00108.93           C  
ANISOU  476  C   GLU A1059    11981  12823  16586   2358   1243  -1136       C  
ATOM    477  O   GLU A1059      36.587  38.707  55.299  1.00109.21           O  
ANISOU  477  O   GLU A1059    12032  12854  16609   2384   1294  -1206       O  
ATOM    478  CB  GLU A1059      34.758  36.891  57.369  1.00108.65           C  
ANISOU  478  CB  GLU A1059    11943  12736  16603   2366   1240  -1134       C  
ATOM    479  CG  GLU A1059      33.774  37.123  56.234  1.00109.17           C  
ANISOU  479  CG  GLU A1059    12032  12846  16604   2383   1281  -1256       C  
ATOM    480  CD  GLU A1059      33.255  38.554  56.167  1.00109.98           C  
ANISOU  480  CD  GLU A1059    12213  13028  16548   2402   1259  -1270       C  
ATOM    481  OE1 GLU A1059      32.450  38.947  57.047  1.00108.64           O  
ANISOU  481  OE1 GLU A1059    12085  12893  16299   2388   1222  -1246       O  
ATOM    482  OE2 GLU A1059      33.637  39.279  55.218  1.00110.13           O  
ANISOU  482  OE2 GLU A1059    12264  13066  16513   2441   1293  -1304       O  
ATOM    483  N   ILE A1060      36.731  39.420  57.432  1.00108.22           N  
ANISOU  483  N   ILE A1060    11928  12776  16416   2309   1207  -1090       N  
ATOM    484  CA  ILE A1060      37.124  40.780  57.040  1.00108.54           C  
ANISOU  484  CA  ILE A1060    12045  12838  16358   2270   1249  -1124       C  
ATOM    485  C   ILE A1060      38.524  40.780  56.398  1.00109.57           C  
ANISOU  485  C   ILE A1060    12111  12975  16546   2246   1285  -1149       C  
ATOM    486  O   ILE A1060      38.742  41.438  55.378  1.00107.94           O  
ANISOU  486  O   ILE A1060    11968  12745  16298   2247   1358  -1209       O  
ATOM    487  CB  ILE A1060      36.987  41.817  58.195  1.00108.03           C  
ANISOU  487  CB  ILE A1060    12048  12809  16190   2200   1227  -1087       C  
ATOM    488  CG1 ILE A1060      36.833  43.243  57.650  1.00108.42           C  
ANISOU  488  CG1 ILE A1060    12249  12838  16109   2182   1316  -1134       C  
ATOM    489  CG2 ILE A1060      38.158  41.758  59.167  1.00108.85           C  
ANISOU  489  CG2 ILE A1060    12053  12981  16326   2126   1187  -1045       C  
ATOM    490  CD1 ILE A1060      35.426  43.609  57.204  1.00108.41           C  
ANISOU  490  CD1 ILE A1060    12362  12825  16006   2277   1340  -1152       C  
ATOM    491  N   ILE A1061      39.442  40.008  56.989  1.00111.06           N  
ANISOU  491  N   ILE A1061    12175  13204  16818   2240   1241  -1102       N  
ATOM    492  CA  ILE A1061      40.819  39.866  56.508  1.00112.24           C  
ANISOU  492  CA  ILE A1061    12229  13396  17020   2226   1264  -1125       C  
ATOM    493  C   ILE A1061      40.877  39.294  55.086  1.00114.07           C  
ANISOU  493  C   ILE A1061    12457  13558  17327   2288   1318  -1176       C  
ATOM    494  O   ILE A1061      41.729  39.695  54.282  1.00113.92           O  
ANISOU  494  O   ILE A1061    12424  13551  17311   2260   1369  -1231       O  
ATOM    495  CB  ILE A1061      41.679  39.035  57.497  1.00112.45           C  
ANISOU  495  CB  ILE A1061    12113  13515  17098   2256   1200  -1051       C  
ATOM    496  CG1 ILE A1061      42.086  39.905  58.699  1.00112.88           C  
ANISOU  496  CG1 ILE A1061    12139  13697  17055   2164   1162  -1039       C  
ATOM    497  CG2 ILE A1061      42.913  38.457  56.811  1.00113.48           C  
ANISOU  497  CG2 ILE A1061    12128  13688  17302   2296   1222  -1070       C  
ATOM    498  CD1 ILE A1061      42.896  39.192  59.770  1.00112.89           C  
ANISOU  498  CD1 ILE A1061    11988  13839  17066   2218   1092   -965       C  
ATOM    499  N   LEU A1062      39.956  38.374  54.785  1.00115.51           N  
ANISOU  499  N   LEU A1062    12652  13673  17565   2357   1316  -1171       N  
ATOM    500  CA  LEU A1062      39.845  37.763  53.453  1.00115.34           C  
ANISOU  500  CA  LEU A1062    12622  13595  17608   2408   1372  -1234       C  
ATOM    501  C   LEU A1062      39.462  38.784  52.380  1.00115.14           C  
ANISOU  501  C   LEU A1062    12691  13567  17489   2408   1427  -1314       C  
ATOM    502  O   LEU A1062      39.865  38.653  51.221  1.00116.01           O  
ANISOU  502  O   LEU A1062    12789  13658  17633   2435   1479  -1369       O  
ATOM    503  CB  LEU A1062      38.831  36.609  53.456  1.00114.91           C  
ANISOU  503  CB  LEU A1062    12564  13483  17613   2450   1379  -1240       C  
ATOM    504  CG  LEU A1062      39.008  35.444  54.440  1.00116.27           C  
ANISOU  504  CG  LEU A1062    12688  13616  17872   2479   1364  -1155       C  
ATOM    505  CD1 LEU A1062      37.959  34.358  54.226  1.00115.62           C  
ANISOU  505  CD1 LEU A1062    12631  13453  17845   2489   1420  -1197       C  
ATOM    506  CD2 LEU A1062      40.413  34.853  54.375  1.00118.17           C  
ANISOU  506  CD2 LEU A1062    12841  13863  18195   2529   1373  -1104       C  
ATOM    507  N   ARG A1063      38.691  39.798  52.775  1.00113.65           N  
ANISOU  507  N   ARG A1063    12607  13400  17176   2393   1426  -1312       N  
ATOM    508  CA  ARG A1063      38.207  40.820  51.842  1.00113.57           C  
ANISOU  508  CA  ARG A1063    12719  13389  17045   2434   1495  -1368       C  
ATOM    509  C   ARG A1063      39.289  41.823  51.426  1.00113.16           C  
ANISOU  509  C   ARG A1063    12730  13314  16953   2382   1573  -1388       C  
ATOM    510  O   ARG A1063      39.217  42.401  50.336  1.00112.96           O  
ANISOU  510  O   ARG A1063    12796  13264  16860   2435   1658  -1435       O  
ATOM    511  CB  ARG A1063      36.994  41.564  52.429  1.00114.52           C  
ANISOU  511  CB  ARG A1063    12945  13538  17029   2460   1484  -1352       C  
ATOM    512  CG  ARG A1063      35.730  40.722  52.572  1.00114.18           C  
ANISOU  512  CG  ARG A1063    12854  13538  16991   2510   1435  -1371       C  
ATOM    513  CD  ARG A1063      34.549  41.540  53.075  1.00113.95           C  
ANISOU  513  CD  ARG A1063    12924  13563  16808   2551   1426  -1362       C  
ATOM    514  NE  ARG A1063      33.285  40.884  52.739  1.00115.84           N  
ANISOU  514  NE  ARG A1063    13113  13888  17014   2613   1409  -1429       N  
ATOM    515  CZ  ARG A1063      32.080  41.255  53.176  1.00116.03           C  
ANISOU  515  CZ  ARG A1063    13177  13995  16913   2656   1388  -1439       C  
ATOM    516  NH1 ARG A1063      31.935  42.295  53.995  1.00114.07           N  
ANISOU  516  NH1 ARG A1063    13040  13735  16566   2655   1382  -1371       N  
ATOM    517  NH2 ARG A1063      31.008  40.570  52.791  1.00115.31           N  
ANISOU  517  NH2 ARG A1063    13008  14013  16791   2693   1381  -1531       N  
ATOM    518  N   ILE A1064      40.287  42.014  52.289  1.00112.43           N  
ANISOU  518  N   ILE A1064    12584  13243  16892   2278   1554  -1360       N  
ATOM    519  CA  ILE A1064      41.269  43.092  52.130  1.00112.86           C  
ANISOU  519  CA  ILE A1064    12702  13292  16888   2181   1645  -1402       C  
ATOM    520  C   ILE A1064      42.318  42.773  51.050  1.00115.34           C  
ANISOU  520  C   ILE A1064    12950  13596  17277   2177   1697  -1457       C  
ATOM    521  O   ILE A1064      42.824  43.680  50.374  1.00116.29           O  
ANISOU  521  O   ILE A1064    13172  13677  17336   2129   1814  -1515       O  
ATOM    522  CB  ILE A1064      41.937  43.466  53.481  1.00111.36           C  
ANISOU  522  CB  ILE A1064    12456  13176  16681   2051   1612  -1383       C  
ATOM    523  CG1 ILE A1064      40.876  43.601  54.573  1.00111.12           C  
ANISOU  523  CG1 ILE A1064    12475  13153  16593   2065   1547  -1321       C  
ATOM    524  CG2 ILE A1064      42.702  44.782  53.371  1.00111.07           C  
ANISOU  524  CG2 ILE A1064    12523  13127  16550   1917   1743  -1456       C  
ATOM    525  CD1 ILE A1064      41.411  43.493  55.987  1.00112.26           C  
ANISOU  525  CD1 ILE A1064    12509  13398  16746   1975   1472  -1286       C  
ATOM    526  N   TYR A1065      42.638  41.492  50.875  1.00115.90           N  
ANISOU  526  N   TYR A1065    12867  13691  17478   2227   1627  -1440       N  
ATOM    527  CA  TYR A1065      43.584  41.091  49.820  1.00117.26           C  
ANISOU  527  CA  TYR A1065    12971  13856  17727   2237   1671  -1489       C  
ATOM    528  C   TYR A1065      42.913  40.867  48.445  1.00115.67           C  
ANISOU  528  C   TYR A1065    12835  13586  17528   2340   1720  -1528       C  
ATOM    529  O   TYR A1065      43.520  40.287  47.542  1.00114.45           O  
ANISOU  529  O   TYR A1065    12613  13419  17454   2366   1744  -1563       O  
ATOM    530  CB  TYR A1065      44.441  39.885  50.254  1.00118.29           C  
ANISOU  530  CB  TYR A1065    12912  14050  17982   2253   1596  -1451       C  
ATOM    531  CG  TYR A1065      45.334  40.161  51.461  1.00119.71           C  
ANISOU  531  CG  TYR A1065    12995  14354  18134   2166   1554  -1432       C  
ATOM    532  CD1 TYR A1065      44.851  39.995  52.762  1.00119.12           C  
ANISOU  532  CD1 TYR A1065    12900  14326  18035   2170   1475  -1359       C  
ATOM    533  CD2 TYR A1065      46.665  40.578  51.302  1.00120.00           C  
ANISOU  533  CD2 TYR A1065    12948  14486  18159   2075   1598  -1498       C  
ATOM    534  CE1 TYR A1065      45.656  40.236  53.867  1.00119.07           C  
ANISOU  534  CE1 TYR A1065    12788  14468  17986   2100   1433  -1349       C  
ATOM    535  CE2 TYR A1065      47.477  40.823  52.408  1.00119.64           C  
ANISOU  535  CE2 TYR A1065    12784  14606  18066   1991   1560  -1504       C  
ATOM    536  CZ  TYR A1065      46.962  40.650  53.686  1.00119.29           C  
ANISOU  536  CZ  TYR A1065    12717  14617  17992   2011   1474  -1427       C  
ATOM    537  OH  TYR A1065      47.735  40.886  54.799  1.00119.57           O  
ANISOU  537  OH  TYR A1065    12621  14847  17964   1938   1432  -1438       O  
ATOM    538  N   VAL A1066      41.673  41.343  48.299  1.00114.15           N  
ANISOU  538  N   VAL A1066    12765  13373  17232   2404   1736  -1527       N  
ATOM    539  CA  VAL A1066      40.944  41.279  47.028  1.00113.68           C  
ANISOU  539  CA  VAL A1066    12762  13300  17129   2517   1784  -1576       C  
ATOM    540  C   VAL A1066      40.645  42.694  46.520  1.00114.91           C  
ANISOU  540  C   VAL A1066    13117  13428  17117   2559   1896  -1592       C  
ATOM    541  O   VAL A1066      41.215  43.142  45.515  1.00113.98           O  
ANISOU  541  O   VAL A1066    13066  13269  16973   2577   1996  -1633       O  
ATOM    542  CB  VAL A1066      39.620  40.475  47.146  1.00111.69           C  
ANISOU  542  CB  VAL A1066    12467  13094  16878   2594   1718  -1578       C  
ATOM    543  CG1 VAL A1066      38.931  40.354  45.787  1.00110.04           C  
ANISOU  543  CG1 VAL A1066    12278  12925  16609   2707   1767  -1654       C  
ATOM    544  CG2 VAL A1066      39.870  39.098  47.744  1.00110.74           C  
ANISOU  544  CG2 VAL A1066    12197  12965  16914   2554   1646  -1553       C  
ATOM    545  N   HIS A1067      39.749  43.387  47.225  1.00115.23           N  
ANISOU  545  N   HIS A1067    13265  13481  17037   2585   1893  -1556       N  
ATOM    546  CA  HIS A1067      39.346  44.748  46.865  1.00116.78           C  
ANISOU  546  CA  HIS A1067    13683  13638  17051   2654   2019  -1552       C  
ATOM    547  C   HIS A1067      40.410  45.756  47.221  1.00119.74           C  
ANISOU  547  C   HIS A1067    14169  13927  17402   2515   2130  -1557       C  
ATOM    548  O   HIS A1067      40.495  46.819  46.604  1.00119.25           O  
ANISOU  548  O   HIS A1067    14308  13787  17216   2553   2290  -1571       O  
ATOM    549  CB  HIS A1067      38.024  45.113  47.542  1.00114.63           C  
ANISOU  549  CB  HIS A1067    13485  13417  16654   2737   1982  -1511       C  
ATOM    550  CG  HIS A1067      36.808  44.478  46.897  1.00112.50           C  
ANISOU  550  CG  HIS A1067    13152  13262  16332   2897   1927  -1541       C  
ATOM    551  ND1 HIS A1067      36.145  43.438  47.454  1.00110.15           N  
ANISOU  551  ND1 HIS A1067    12698  13042  16111   2876   1805  -1551       N  
ATOM    552  CD2 HIS A1067      36.144  44.775  45.709  1.00111.78           C  
ANISOU  552  CD2 HIS A1067    13130  13239  16100   3081   1994  -1578       C  
ATOM    553  CE1 HIS A1067      35.120  43.085  46.660  1.00109.59           C  
ANISOU  553  CE1 HIS A1067    12588  13095  15958   3012   1797  -1611       C  
ATOM    554  NE2 HIS A1067      35.114  43.904  45.594  1.00110.49           N  
ANISOU  554  NE2 HIS A1067    12829  13220  15933   3149   1902  -1626       N  
ATOM    555  N   ARG A1068      41.237  45.402  48.209  1.00123.11           N  
ANISOU  555  N   ARG A1068    14463  14377  17937   2354   2061  -1553       N  
ATOM    556  CA  ARG A1068      42.288  46.272  48.782  1.00125.44           C  
ANISOU  556  CA  ARG A1068    14812  14641  18210   2175   2154  -1586       C  
ATOM    557  C   ARG A1068      41.870  47.733  49.020  1.00124.93           C  
ANISOU  557  C   ARG A1068    15009  14488  17972   2157   2309  -1583       C  
ATOM    558  O   ARG A1068      41.338  48.062  50.093  1.00123.56           O  
ANISOU  558  O   ARG A1068    14870  14331  17746   2122   2272  -1544       O  
ATOM    559  CB  ARG A1068      43.614  46.168  48.005  1.00127.72           C  
ANISOU  559  CB  ARG A1068    15036  14919  18573   2090   2225  -1660       C  
ATOM    560  CG  ARG A1068      44.813  46.574  48.855  1.00130.69           C  
ANISOU  560  CG  ARG A1068    15341  15349  18965   1873   2259  -1717       C  
ATOM    561  CD  ARG A1068      46.133  45.981  48.375  1.00132.31           C  
ANISOU  561  CD  ARG A1068    15369  15622  19280   1798   2252  -1784       C  
ATOM    562  NE  ARG A1068      47.133  46.063  49.441  1.00134.24           N  
ANISOU  562  NE  ARG A1068    15463  16003  19537   1618   2224  -1835       N  
ATOM    563  CZ  ARG A1068      48.438  45.850  49.291  1.00136.94           C  
ANISOU  563  CZ  ARG A1068    15648  16454  19931   1509   2242  -1919       C  
ATOM    564  NH1 ARG A1068      48.947  45.538  48.102  1.00139.67           N  
ANISOU  564  NH1 ARG A1068    15976  16760  20334   1551   2291  -1958       N  
ATOM    565  NH2 ARG A1068      49.243  45.956  50.342  1.00138.72           N  
ANISOU  565  NH2 ARG A1068    15719  16853  20136   1360   2209  -1973       N  
ATOM    566  N   ILE A1069      42.111  48.590  48.024  1.00124.03           N  
ANISOU  566  N   ILE A1069    15091  14270  17766   2188   2497  -1621       N  
ATOM    567  CA  ILE A1069      41.744  50.016  48.089  1.00123.82           C  
ANISOU  567  CA  ILE A1069    15364  14121  17559   2197   2697  -1614       C  
ATOM    568  C   ILE A1069      40.281  50.263  47.645  1.00122.40           C  
ANISOU  568  C   ILE A1069    15337  13934  17234   2462   2706  -1536       C  
ATOM    569  O   ILE A1069      39.764  51.379  47.729  1.00119.50           O  
ANISOU  569  O   ILE A1069    15233  13475  16698   2530   2864  -1504       O  
ATOM    570  CB  ILE A1069      42.763  50.885  47.301  1.00124.45           C  
ANISOU  570  CB  ILE A1069    15616  14076  17593   2096   2936  -1694       C  
ATOM    571  CG1 ILE A1069      42.990  52.227  47.996  1.00124.14           C  
ANISOU  571  CG1 ILE A1069    15814  13922  17431   1938   3146  -1729       C  
ATOM    572  CG2 ILE A1069      42.390  51.011  45.819  1.00124.48           C  
ANISOU  572  CG2 ILE A1069    15764  14011  17521   2315   3038  -1675       C  
ATOM    573  CD1 ILE A1069      44.376  52.795  47.759  1.00127.08           C  
ANISOU  573  CD1 ILE A1069    16234  14229  17822   1695   3338  -1857       C  
ATOM    574  N   SER A1070      39.636  49.194  47.175  1.00122.27           N  
ANISOU  574  N   SER A1070    15150  14029  17277   2611   2544  -1516       N  
ATOM    575  CA  SER A1070      38.219  49.193  46.805  1.00121.05           C  
ANISOU  575  CA  SER A1070    15057  13946  16989   2856   2511  -1468       C  
ATOM    576  C   SER A1070      37.373  48.776  48.012  1.00117.79           C  
ANISOU  576  C   SER A1070    14535  13626  16594   2838   2352  -1427       C  
ATOM    577  O   SER A1070      36.143  48.651  47.927  1.00115.95           O  
ANISOU  577  O   SER A1070    14304  13492  16259   3013   2296  -1401       O  
ATOM    578  CB  SER A1070      37.991  48.242  45.618  1.00122.72           C  
ANISOU  578  CB  SER A1070    15126  14253  17248   2995   2439  -1502       C  
ATOM    579  OG  SER A1070      36.637  48.241  45.199  1.00125.30           O  
ANISOU  579  OG  SER A1070    15484  14701  17424   3231   2412  -1483       O  
ATOM    580  N   PHE A1071      38.054  48.555  49.133  1.00115.72           N  
ANISOU  580  N   PHE A1071    14168  13350  16452   2628   2284  -1429       N  
ATOM    581  CA  PHE A1071      37.408  48.262  50.404  1.00113.25           C  
ANISOU  581  CA  PHE A1071    13772  13101  16157   2585   2153  -1386       C  
ATOM    582  C   PHE A1071      37.261  49.566  51.169  1.00112.27           C  
ANISOU  582  C   PHE A1071    13868  12895  15894   2534   2276  -1357       C  
ATOM    583  O   PHE A1071      36.143  49.989  51.462  1.00113.53           O  
ANISOU  583  O   PHE A1071    14135  13077  15923   2662   2278  -1309       O  
ATOM    584  CB  PHE A1071      38.237  47.247  51.202  1.00112.92           C  
ANISOU  584  CB  PHE A1071    13492  13107  16306   2414   2012  -1396       C  
ATOM    585  CG  PHE A1071      37.713  46.972  52.587  1.00111.56           C  
ANISOU  585  CG  PHE A1071    13245  12991  16154   2359   1892  -1347       C  
ATOM    586  CD1 PHE A1071      36.645  46.107  52.785  1.00111.23           C  
ANISOU  586  CD1 PHE A1071    13104  13024  16134   2457   1767  -1321       C  
ATOM    587  CD2 PHE A1071      38.314  47.555  53.698  1.00111.34           C  
ANISOU  587  CD2 PHE A1071    13238  12949  16118   2194   1911  -1342       C  
ATOM    588  CE1 PHE A1071      36.173  45.845  54.067  1.00111.74           C  
ANISOU  588  CE1 PHE A1071    13110  13130  16217   2404   1666  -1275       C  
ATOM    589  CE2 PHE A1071      37.851  47.297  54.980  1.00110.94           C  
ANISOU  589  CE2 PHE A1071    13118  12955  16080   2150   1799  -1294       C  
ATOM    590  CZ  PHE A1071      36.777  46.444  55.166  1.00110.89           C  
ANISOU  590  CZ  PHE A1071    13030  13002  16100   2260   1677  -1253       C  
ATOM    591  N   PHE A1072      38.390  50.215  51.452  1.00110.92           N  
ANISOU  591  N   PHE A1072    13764  12638  15743   2344   2394  -1399       N  
ATOM    592  CA  PHE A1072      38.419  51.461  52.227  1.00110.38           C  
ANISOU  592  CA  PHE A1072    13909  12477  15555   2243   2542  -1396       C  
ATOM    593  C   PHE A1072      37.787  52.646  51.490  1.00111.27           C  
ANISOU  593  C   PHE A1072    14352  12464  15463   2416   2763  -1366       C  
ATOM    594  O   PHE A1072      37.963  53.807  51.887  1.00112.88           O  
ANISOU  594  O   PHE A1072    14793  12540  15555   2329   2958  -1375       O  
ATOM    595  CB  PHE A1072      39.849  51.773  52.686  1.00109.78           C  
ANISOU  595  CB  PHE A1072    13788  12374  15548   1966   2623  -1483       C  
ATOM    596  CG  PHE A1072      40.397  50.763  53.659  1.00108.48           C  
ANISOU  596  CG  PHE A1072    13321  12358  15538   1827   2416  -1495       C  
ATOM    597  CD1 PHE A1072      41.086  49.640  53.204  1.00108.18           C  
ANISOU  597  CD1 PHE A1072    13049  12406  15649   1825   2297  -1517       C  
ATOM    598  CD2 PHE A1072      40.203  50.918  55.029  1.00106.51           C  
ANISOU  598  CD2 PHE A1072    13029  12166  15273   1721   2348  -1475       C  
ATOM    599  CE1 PHE A1072      41.574  48.702  54.101  1.00107.01           C  
ANISOU  599  CE1 PHE A1072    12643  12396  15621   1741   2124  -1510       C  
ATOM    600  CE2 PHE A1072      40.697  49.988  55.927  1.00105.15           C  
ANISOU  600  CE2 PHE A1072    12589  12142  15220   1629   2167  -1473       C  
ATOM    601  CZ  PHE A1072      41.377  48.878  55.464  1.00105.75           C  
ANISOU  601  CZ  PHE A1072    12447  12300  15434   1650   2060  -1485       C  
ATOM    602  N   LYS A1073      37.031  52.326  50.437  1.00110.02           N  
ANISOU  602  N   LYS A1073    14208  12351  15244   2667   2739  -1333       N  
ATOM    603  CA  LYS A1073      36.277  53.290  49.646  1.00110.84           C  
ANISOU  603  CA  LYS A1073    14601  12384  15128   2913   2925  -1285       C  
ATOM    604  C   LYS A1073      34.900  52.732  49.259  1.00110.80           C  
ANISOU  604  C   LYS A1073    14509  12554  15037   3191   2785  -1237       C  
ATOM    605  O   LYS A1073      34.318  53.127  48.246  1.00111.89           O  
ANISOU  605  O   LYS A1073    14791  12713  15007   3450   2887  -1211       O  
ATOM    606  CB  LYS A1073      37.074  53.703  48.400  1.00111.34           C  
ANISOU  606  CB  LYS A1073    14810  12331  15162   2941   3118  -1324       C  
ATOM    607  CG  LYS A1073      38.110  54.797  48.628  1.00111.22           C  
ANISOU  607  CG  LYS A1073    15027  12114  15118   2728   3374  -1374       C  
ATOM    608  CD  LYS A1073      39.338  54.603  47.750  1.00112.90           C  
ANISOU  608  CD  LYS A1073    15196  12269  15433   2604   3457  -1459       C  
ATOM    609  CE  LYS A1073      39.008  54.367  46.270  1.00113.00           C  
ANISOU  609  CE  LYS A1073    15255  12299  15382   2871   3488  -1432       C  
ATOM    610  NZ  LYS A1073      40.099  53.648  45.541  1.00110.88           N  
ANISOU  610  NZ  LYS A1073    14803  12048  15276   2749   3447  -1513       N  
ATOM    611  N   ASP A1074      34.387  51.805  50.064  1.00111.35           N  
ANISOU  611  N   ASP A1074    14338  12762  15209   3138   2561  -1236       N  
ATOM    612  CA  ASP A1074      32.983  51.385  49.956  1.00112.53           C  
ANISOU  612  CA  ASP A1074    14406  13092  15257   3358   2443  -1212       C  
ATOM    613  C   ASP A1074      32.231  51.557  51.290  1.00112.04           C  
ANISOU  613  C   ASP A1074    14342  13068  15159   3316   2364  -1169       C  
ATOM    614  O   ASP A1074      32.671  51.025  52.316  1.00110.22           O  
ANISOU  614  O   ASP A1074    13964  12825  15091   3096   2248  -1178       O  
ATOM    615  CB  ASP A1074      32.860  49.943  49.451  1.00112.42           C  
ANISOU  615  CB  ASP A1074    14096  13233  15386   3360   2261  -1274       C  
ATOM    616  CG  ASP A1074      31.447  49.608  48.979  1.00113.00           C  
ANISOU  616  CG  ASP A1074    14096  13523  15315   3601   2189  -1290       C  
ATOM    617  OD1 ASP A1074      30.827  48.676  49.552  1.00112.33           O  
ANISOU  617  OD1 ASP A1074    13804  13567  15308   3546   2026  -1322       O  
ATOM    618  OD2 ASP A1074      30.956  50.288  48.043  1.00112.36           O  
ANISOU  618  OD2 ASP A1074    14168  13495  15027   3848   2307  -1276       O  
ATOM    619  N   PRO A1075      31.101  52.305  51.270  1.00112.12           N  
ANISOU  619  N   PRO A1075    14519  13136  14945   3544   2431  -1117       N  
ATOM    620  CA  PRO A1075      30.296  52.609  52.450  1.00112.38           C  
ANISOU  620  CA  PRO A1075    14583  13205  14912   3537   2378  -1071       C  
ATOM    621  C   PRO A1075      29.720  51.378  53.158  1.00112.12           C  
ANISOU  621  C   PRO A1075    14253  13336  15009   3452   2139  -1104       C  
ATOM    622  O   PRO A1075      29.546  51.407  54.380  1.00111.31           O  
ANISOU  622  O   PRO A1075    14129  13216  14949   3325   2072  -1076       O  
ATOM    623  CB  PRO A1075      29.166  53.477  51.886  1.00113.33           C  
ANISOU  623  CB  PRO A1075    14909  13406  14745   3872   2497  -1019       C  
ATOM    624  CG  PRO A1075      29.725  54.068  50.641  1.00113.53           C  
ANISOU  624  CG  PRO A1075    15125  13332  14679   4004   2691  -1014       C  
ATOM    625  CD  PRO A1075      30.556  52.966  50.071  1.00113.89           C  
ANISOU  625  CD  PRO A1075    14927  13402  14943   3851   2577  -1094       C  
ATOM    626  N   TRP A1076      29.425  50.316  52.407  1.00112.52           N  
ANISOU  626  N   TRP A1076    14092  13540  15120   3515   2028  -1169       N  
ATOM    627  CA  TRP A1076      28.952  49.062  53.014  1.00113.27           C  
ANISOU  627  CA  TRP A1076    13924  13762  15352   3410   1837  -1216       C  
ATOM    628  C   TRP A1076      30.053  48.402  53.806  1.00112.24           C  
ANISOU  628  C   TRP A1076    13677  13506  15463   3141   1763  -1212       C  
ATOM    629  O   TRP A1076      29.807  47.773  54.837  1.00111.41           O  
ANISOU  629  O   TRP A1076    13449  13428  15452   3024   1646  -1204       O  
ATOM    630  CB  TRP A1076      28.421  48.091  51.958  1.00114.93           C  
ANISOU  630  CB  TRP A1076    13948  14157  15563   3519   1772  -1309       C  
ATOM    631  CG  TRP A1076      27.445  48.701  50.976  1.00118.18           C  
ANISOU  631  CG  TRP A1076    14445  14746  15713   3817   1846  -1326       C  
ATOM    632  CD1 TRP A1076      27.718  49.173  49.698  1.00119.67           C  
ANISOU  632  CD1 TRP A1076    14739  14940  15789   3993   1965  -1331       C  
ATOM    633  CD2 TRP A1076      26.004  48.915  51.160  1.00119.28           C  
ANISOU  633  CD2 TRP A1076    14564  15114  15643   4004   1811  -1343       C  
ATOM    634  NE1 TRP A1076      26.581  49.651  49.099  1.00121.41           N  
ANISOU  634  NE1 TRP A1076    15008  15380  15742   4289   2005  -1341       N  
ATOM    635  CE2 TRP A1076      25.518  49.527  49.923  1.00121.31           C  
ANISOU  635  CE2 TRP A1076    14915  15523  15656   4311   1914  -1353       C  
ATOM    636  CE3 TRP A1076      25.102  48.671  52.191  1.00120.13           C  
ANISOU  636  CE3 TRP A1076    14585  15326  15731   3958   1713  -1353       C  
ATOM    637  CZ2 TRP A1076      24.182  49.875  49.744  1.00123.32           C  
ANISOU  637  CZ2 TRP A1076    15161  16052  15645   4574   1910  -1374       C  
ATOM    638  CZ3 TRP A1076      23.759  49.027  52.002  1.00122.34           C  
ANISOU  638  CZ3 TRP A1076    14858  15869  15758   4199   1711  -1383       C  
ATOM    639  CH2 TRP A1076      23.313  49.616  50.803  1.00123.38           C  
ANISOU  639  CH2 TRP A1076    15065  16170  15643   4507   1804  -1394       C  
ATOM    640  N   SER A1077      31.281  48.559  53.326  1.00112.00           N  
ANISOU  640  N   SER A1077    13688  13349  15519   3054   1840  -1217       N  
ATOM    641  CA  SER A1077      32.445  47.900  53.904  1.00110.54           C  
ANISOU  641  CA  SER A1077    13371  13086  15545   2831   1776  -1222       C  
ATOM    642  C   SER A1077      33.007  48.643  55.123  1.00108.84           C  
ANISOU  642  C   SER A1077    13246  12776  15334   2669   1808  -1177       C  
ATOM    643  O   SER A1077      33.184  48.051  56.188  1.00107.28           O  
ANISOU  643  O   SER A1077    12916  12601  15246   2538   1695  -1159       O  
ATOM    644  CB  SER A1077      33.527  47.724  52.832  1.00111.31           C  
ANISOU  644  CB  SER A1077    13448  13122  15722   2807   1843  -1263       C  
ATOM    645  OG  SER A1077      33.071  46.914  51.761  1.00110.47           O  
ANISOU  645  OG  SER A1077    13232  13113  15629   2932   1803  -1315       O  
ATOM    646  N   LEU A1078      33.282  49.934  54.958  1.00108.79           N  
ANISOU  646  N   LEU A1078    13471  12666  15199   2679   1979  -1165       N  
ATOM    647  CA  LEU A1078      33.851  50.763  56.028  1.00108.54           C  
ANISOU  647  CA  LEU A1078    13544  12546  15152   2503   2048  -1150       C  
ATOM    648  C   LEU A1078      33.065  50.704  57.344  1.00107.57           C  
ANISOU  648  C   LEU A1078    13384  12479  15009   2471   1942  -1103       C  
ATOM    649  O   LEU A1078      33.652  50.873  58.413  1.00107.67           O  
ANISOU  649  O   LEU A1078    13365  12471  15073   2287   1924  -1102       O  
ATOM    650  CB  LEU A1078      34.002  52.219  55.568  1.00109.17           C  
ANISOU  650  CB  LEU A1078    13931  12485  15062   2545   2292  -1149       C  
ATOM    651  CG  LEU A1078      35.260  52.609  54.786  1.00109.01           C  
ANISOU  651  CG  LEU A1078    13986  12356  15076   2442   2450  -1210       C  
ATOM    652  CD1 LEU A1078      34.949  53.721  53.793  1.00109.64           C  
ANISOU  652  CD1 LEU A1078    14377  12315  14965   2620   2687  -1192       C  
ATOM    653  CD2 LEU A1078      36.379  53.022  55.735  1.00108.78           C  
ANISOU  653  CD2 LEU A1078    13945  12275  15110   2154   2506  -1264       C  
ATOM    654  N   PHE A1079      31.753  50.469  57.264  1.00106.01           N  
ANISOU  654  N   PHE A1079    13178  12372  14727   2647   1874  -1075       N  
ATOM    655  CA  PHE A1079      30.942  50.242  58.463  1.00104.38           C  
ANISOU  655  CA  PHE A1079    12910  12233  14515   2620   1758  -1038       C  
ATOM    656  C   PHE A1079      31.257  48.887  59.109  1.00103.59           C  
ANISOU  656  C   PHE A1079    12554  12195  14610   2493   1583  -1046       C  
ATOM    657  O   PHE A1079      31.424  48.810  60.327  1.00103.37           O  
ANISOU  657  O   PHE A1079    12478  12167  14631   2364   1518  -1014       O  
ATOM    658  CB  PHE A1079      29.435  50.372  58.174  1.00104.22           C  
ANISOU  658  CB  PHE A1079    12941  12323  14335   2843   1743  -1024       C  
ATOM    659  CG  PHE A1079      28.567  49.584  59.123  1.00103.99           C  
ANISOU  659  CG  PHE A1079    12756  12403  14351   2813   1584  -1017       C  
ATOM    660  CD1 PHE A1079      28.360  50.018  60.437  1.00103.59           C  
ANISOU  660  CD1 PHE A1079    12757  12323  14278   2719   1560   -968       C  
ATOM    661  CD2 PHE A1079      27.973  48.389  58.715  1.00104.35           C  
ANISOU  661  CD2 PHE A1079    12607  12578  14462   2863   1474  -1070       C  
ATOM    662  CE1 PHE A1079      27.581  49.279  61.320  1.00102.74           C  
ANISOU  662  CE1 PHE A1079    12515  12306  14214   2687   1423   -961       C  
ATOM    663  CE2 PHE A1079      27.191  47.643  59.597  1.00104.38           C  
ANISOU  663  CE2 PHE A1079    12483  12666  14510   2815   1354  -1076       C  
ATOM    664  CZ  PHE A1079      26.993  48.092  60.901  1.00103.58           C  
ANISOU  664  CZ  PHE A1079    12441  12529  14386   2733   1327  -1015       C  
ATOM    665  N   ASP A1080      31.328  47.829  58.296  1.00103.25           N  
ANISOU  665  N   ASP A1080    12360  12202  14667   2539   1523  -1085       N  
ATOM    666  CA  ASP A1080      31.615  46.472  58.783  1.00103.01           C  
ANISOU  666  CA  ASP A1080    12117  12207  14814   2448   1392  -1087       C  
ATOM    667  C   ASP A1080      32.950  46.431  59.540  1.00104.28           C  
ANISOU  667  C   ASP A1080    12220  12318  15082   2280   1377  -1063       C  
ATOM    668  O   ASP A1080      33.133  45.635  60.467  1.00104.61           O  
ANISOU  668  O   ASP A1080    12134  12391  15224   2208   1277  -1029       O  
ATOM    669  CB  ASP A1080      31.634  45.458  57.627  1.00102.23           C  
ANISOU  669  CB  ASP A1080    11901  12144  14799   2517   1375  -1144       C  
ATOM    670  CG  ASP A1080      30.359  45.479  56.788  1.00102.06           C  
ANISOU  670  CG  ASP A1080    11902  12225  14650   2683   1391  -1196       C  
ATOM    671  OD1 ASP A1080      29.324  45.972  57.263  1.00104.26           O  
ANISOU  671  OD1 ASP A1080    12247  12569  14798   2750   1383  -1181       O  
ATOM    672  OD2 ASP A1080      30.380  44.995  55.645  1.00101.19           O  
ANISOU  672  OD2 ASP A1080    11733  12154  14559   2754   1413  -1257       O  
ATOM    673  N   PHE A1081      33.871  47.301  59.138  1.00104.27           N  
ANISOU  673  N   PHE A1081    12315  12258  15046   2224   1488  -1086       N  
ATOM    674  CA  PHE A1081      35.155  47.449  59.809  1.00105.48           C  
ANISOU  674  CA  PHE A1081    12406  12409  15262   2054   1494  -1094       C  
ATOM    675  C   PHE A1081      34.957  48.005  61.221  1.00105.28           C  
ANISOU  675  C   PHE A1081    12417  12406  15178   1955   1470  -1060       C  
ATOM    676  O   PHE A1081      35.668  47.622  62.150  1.00105.09           O  
ANISOU  676  O   PHE A1081    12260  12450  15221   1843   1397  -1049       O  
ATOM    677  CB  PHE A1081      36.069  48.372  58.985  1.00107.74           C  
ANISOU  677  CB  PHE A1081    12809  12625  15500   1998   1653  -1155       C  
ATOM    678  CG  PHE A1081      37.537  48.259  59.324  1.00108.23           C  
ANISOU  678  CG  PHE A1081    12746  12733  15643   1827   1657  -1201       C  
ATOM    679  CD1 PHE A1081      38.315  47.235  58.785  1.00108.27           C  
ANISOU  679  CD1 PHE A1081    12574  12786  15779   1840   1593  -1218       C  
ATOM    680  CD2 PHE A1081      38.144  49.189  60.162  1.00108.68           C  
ANISOU  680  CD2 PHE A1081    12856  12803  15633   1654   1734  -1241       C  
ATOM    681  CE1 PHE A1081      39.667  47.135  59.089  1.00109.25           C  
ANISOU  681  CE1 PHE A1081    12564  12991  15955   1704   1594  -1266       C  
ATOM    682  CE2 PHE A1081      39.493  49.094  60.468  1.00109.81           C  
ANISOU  682  CE2 PHE A1081    12854  13040  15827   1494   1737  -1308       C  
ATOM    683  CZ  PHE A1081      40.257  48.069  59.928  1.00109.77           C  
ANISOU  683  CZ  PHE A1081    12661  13104  15942   1529   1662  -1317       C  
ATOM    684  N   PHE A1082      33.981  48.901  61.368  1.00105.29           N  
ANISOU  684  N   PHE A1082    12599  12366  15042   2013   1533  -1041       N  
ATOM    685  CA  PHE A1082      33.672  49.535  62.654  1.00105.33           C  
ANISOU  685  CA  PHE A1082    12665  12379  14975   1927   1527  -1011       C  
ATOM    686  C   PHE A1082      33.076  48.563  63.676  1.00105.50           C  
ANISOU  686  C   PHE A1082    12537  12483  15067   1936   1358   -954       C  
ATOM    687  O   PHE A1082      33.425  48.609  64.864  1.00104.67           O  
ANISOU  687  O   PHE A1082    12372  12423  14973   1819   1307   -934       O  
ATOM    688  CB  PHE A1082      32.712  50.714  62.454  1.00104.29           C  
ANISOU  688  CB  PHE A1082    12783  12175  14669   2023   1653   -997       C  
ATOM    689  CG  PHE A1082      33.387  52.058  62.393  1.00104.09           C  
ANISOU  689  CG  PHE A1082    12963  12044  14543   1916   1854  -1039       C  
ATOM    690  CD1 PHE A1082      33.377  52.798  61.225  1.00105.06           C  
ANISOU  690  CD1 PHE A1082    13285  12064  14569   2018   2030  -1059       C  
ATOM    691  CD2 PHE A1082      34.009  52.595  63.515  1.00104.29           C  
ANISOU  691  CD2 PHE A1082    12992  12075  14558   1710   1887  -1066       C  
ATOM    692  CE1 PHE A1082      33.988  54.043  61.169  1.00106.78           C  
ANISOU  692  CE1 PHE A1082    13726  12155  14690   1908   2255  -1104       C  
ATOM    693  CE2 PHE A1082      34.620  53.839  63.467  1.00105.02           C  
ANISOU  693  CE2 PHE A1082    13285  12064  14555   1579   2104  -1129       C  
ATOM    694  CZ  PHE A1082      34.607  54.566  62.294  1.00106.28           C  
ANISOU  694  CZ  PHE A1082    13667  12089  14625   1673   2299  -1148       C  
ATOM    695  N   VAL A1083      32.184  47.687  63.205  1.00105.18           N  
ANISOU  695  N   VAL A1083    12435  12466  15062   2069   1285   -940       N  
ATOM    696  CA  VAL A1083      31.476  46.745  64.079  1.00105.21           C  
ANISOU  696  CA  VAL A1083    12327  12525  15123   2081   1158   -897       C  
ATOM    697  C   VAL A1083      32.379  45.630  64.628  1.00106.60           C  
ANISOU  697  C   VAL A1083    12323  12733  15448   2012   1070   -869       C  
ATOM    698  O   VAL A1083      32.099  45.054  65.683  1.00106.11           O  
ANISOU  698  O   VAL A1083    12193  12703  15420   1990    987   -818       O  
ATOM    699  CB  VAL A1083      30.226  46.156  63.388  1.00104.29           C  
ANISOU  699  CB  VAL A1083    12199  12441  14986   2219   1134   -921       C  
ATOM    700  CG1 VAL A1083      30.598  45.038  62.426  1.00104.31           C  
ANISOU  700  CG1 VAL A1083    12078  12445  15111   2254   1119   -961       C  
ATOM    701  CG2 VAL A1083      29.238  45.661  64.421  1.00103.46           C  
ANISOU  701  CG2 VAL A1083    12050  12380  14879   2213   1048   -889       C  
ATOM    702  N   VAL A1084      33.452  45.324  63.904  1.00107.90           N  
ANISOU  702  N   VAL A1084    12417  12891  15688   1996   1097   -899       N  
ATOM    703  CA  VAL A1084      34.466  44.407  64.404  1.00108.50           C  
ANISOU  703  CA  VAL A1084    12332  13017  15877   1956   1032   -868       C  
ATOM    704  C   VAL A1084      35.405  45.199  65.307  1.00109.99           C  
ANISOU  704  C   VAL A1084    12501  13278  16011   1827   1040   -873       C  
ATOM    705  O   VAL A1084      35.681  44.776  66.433  1.00111.11           O  
ANISOU  705  O   VAL A1084    12543  13502  16170   1799    962   -822       O  
ATOM    706  CB  VAL A1084      35.274  43.734  63.263  1.00109.16           C  
ANISOU  706  CB  VAL A1084    12335  13084  16057   1997   1058   -904       C  
ATOM    707  CG1 VAL A1084      36.321  42.783  63.830  1.00110.08           C  
ANISOU  707  CG1 VAL A1084    12289  13269  16269   1991    997   -860       C  
ATOM    708  CG2 VAL A1084      34.356  42.978  62.312  1.00109.47           C  
ANISOU  708  CG2 VAL A1084    12386  13068  16140   2104   1065   -925       C  
ATOM    709  N   ALA A1085      35.864  46.355  64.813  1.00109.70           N  
ANISOU  709  N   ALA A1085    12566  13218  15897   1749   1151   -941       N  
ATOM    710  CA  ALA A1085      36.925  47.138  65.461  1.00110.74           C  
ANISOU  710  CA  ALA A1085    12669  13432  15975   1587   1195   -992       C  
ATOM    711  C   ALA A1085      36.582  47.585  66.867  1.00111.97           C  
ANISOU  711  C   ALA A1085    12838  13648  16057   1509   1155   -962       C  
ATOM    712  O   ALA A1085      37.456  47.642  67.726  1.00114.41           O  
ANISOU  712  O   ALA A1085    13024  14097  16351   1401   1125   -985       O  
ATOM    713  CB  ALA A1085      37.289  48.340  64.615  1.00112.38           C  
ANISOU  713  CB  ALA A1085    13035  13561  16105   1509   1364  -1081       C  
ATOM    714  N   ILE A1086      35.308  47.910  67.085  1.00112.09           N  
ANISOU  714  N   ILE A1086    12992  13581  16015   1568   1155   -919       N  
ATOM    715  CA  ILE A1086      34.796  48.299  68.398  1.00111.24           C  
ANISOU  715  CA  ILE A1086    12912  13514  15840   1509   1114   -882       C  
ATOM    716  C   ILE A1086      34.440  47.054  69.228  1.00110.87           C  
ANISOU  716  C   ILE A1086    12721  13533  15871   1587    962   -792       C  
ATOM    717  O   ILE A1086      34.579  47.062  70.451  1.00112.21           O  
ANISOU  717  O   ILE A1086    12826  13796  16011   1527    901   -761       O  
ATOM    718  CB  ILE A1086      33.609  49.290  68.257  1.00111.55           C  
ANISOU  718  CB  ILE A1086    13178  13441  15765   1547   1199   -877       C  
ATOM    719  CG1 ILE A1086      34.070  50.555  67.510  1.00112.04           C  
ANISOU  719  CG1 ILE A1086    13417  13417  15736   1475   1388   -957       C  
ATOM    720  CG2 ILE A1086      33.020  49.660  69.620  1.00111.61           C  
ANISOU  720  CG2 ILE A1086    13217  13485  15705   1490   1154   -837       C  
ATOM    721  CD1 ILE A1086      32.955  51.451  67.003  1.00112.20           C  
ANISOU  721  CD1 ILE A1086    13683  13314  15633   1584   1501   -941       C  
ATOM    722  N   SER A1087      34.011  45.982  68.557  1.00110.02           N  
ANISOU  722  N   SER A1087    12570  13375  15856   1717    917   -758       N  
ATOM    723  CA  SER A1087      33.809  44.674  69.200  1.00110.82           C  
ANISOU  723  CA  SER A1087    12555  13509  16044   1792    814   -679       C  
ATOM    724  C   SER A1087      35.134  43.993  69.581  1.00112.59           C  
ANISOU  724  C   SER A1087    12608  13847  16324   1790    770   -655       C  
ATOM    725  O   SER A1087      35.150  43.034  70.361  1.00112.53           O  
ANISOU  725  O   SER A1087    12516  13881  16358   1859    700   -573       O  
ATOM    726  CB  SER A1087      32.999  43.745  68.288  1.00110.47           C  
ANISOU  726  CB  SER A1087    12525  13371  16077   1906    818   -677       C  
ATOM    727  OG  SER A1087      32.908  42.429  68.817  1.00109.79           O  
ANISOU  727  OG  SER A1087    12353  13282  16079   1969    761   -610       O  
ATOM    728  N   LEU A1088      36.240  44.483  69.026  1.00113.27           N  
ANISOU  728  N   LEU A1088    12647  13992  16398   1723    821   -726       N  
ATOM    729  CA  LEU A1088      37.554  43.939  69.352  1.00114.89           C  
ANISOU  729  CA  LEU A1088    12670  14354  16629   1728    781   -719       C  
ATOM    730  C   LEU A1088      38.132  44.467  70.667  1.00115.52           C  
ANISOU  730  C   LEU A1088    12660  14624  16610   1630    741   -728       C  
ATOM    731  O   LEU A1088      38.913  43.769  71.321  1.00118.23           O  
ANISOU  731  O   LEU A1088    12836  15134  16952   1691    673   -683       O  
ATOM    732  CB  LEU A1088      38.536  44.132  68.191  1.00115.46           C  
ANISOU  732  CB  LEU A1088    12702  14437  16729   1696    851   -806       C  
ATOM    733  CG  LEU A1088      38.531  42.999  67.159  1.00115.18           C  
ANISOU  733  CG  LEU A1088    12639  14310  16815   1835    849   -773       C  
ATOM    734  CD1 LEU A1088      39.278  43.423  65.904  1.00114.70           C  
ANISOU  734  CD1 LEU A1088    12581  14228  16771   1789    933   -869       C  
ATOM    735  CD2 LEU A1088      39.117  41.717  67.751  1.00115.53           C  
ANISOU  735  CD2 LEU A1088    12529  14450  16915   1960    774   -683       C  
ATOM    736  N   VAL A1089      37.751  45.687  71.049  1.00113.62           N  
ANISOU  736  N   VAL A1089    12531  14367  16274   1489    793   -786       N  
ATOM    737  CA  VAL A1089      38.147  46.251  72.347  1.00113.92           C  
ANISOU  737  CA  VAL A1089    12493  14583  16207   1373    765   -809       C  
ATOM    738  C   VAL A1089      37.653  45.322  73.469  1.00112.83           C  
ANISOU  738  C   VAL A1089    12288  14499  16082   1497    644   -679       C  
ATOM    739  O   VAL A1089      36.447  45.079  73.579  1.00111.73           O  
ANISOU  739  O   VAL A1089    12272  14206  15974   1564    624   -607       O  
ATOM    740  CB  VAL A1089      37.611  47.690  72.551  1.00113.71           C  
ANISOU  740  CB  VAL A1089    12645  14480  16081   1209    865   -884       C  
ATOM    741  CG1 VAL A1089      38.382  48.403  73.657  1.00114.42           C  
ANISOU  741  CG1 VAL A1089    12633  14784  16057   1034    875   -965       C  
ATOM    742  CG2 VAL A1089      37.698  48.490  71.256  1.00113.12           C  
ANISOU  742  CG2 VAL A1089    12719  14258  16002   1148   1013   -975       C  
ATOM    743  N   PRO A1090      38.586  44.810  74.300  1.00112.64           N  
ANISOU  743  N   PRO A1090    12069  14709  16021   1536    571   -653       N  
ATOM    744  CA  PRO A1090      38.389  43.731  75.287  1.00113.03           C  
ANISOU  744  CA  PRO A1090    12041  14827  16078   1700    471   -515       C  
ATOM    745  C   PRO A1090      37.211  43.870  76.271  1.00112.10           C  
ANISOU  745  C   PRO A1090    12035  14629  15930   1695    435   -443       C  
ATOM    746  O   PRO A1090      36.601  44.943  76.395  1.00109.85           O  
ANISOU  746  O   PRO A1090    11870  14277  15592   1550    476   -505       O  
ATOM    747  CB  PRO A1090      39.710  43.725  76.070  1.00114.95           C  
ANISOU  747  CB  PRO A1090    12054  15405  16218   1694    423   -548       C  
ATOM    748  CG  PRO A1090      40.703  44.313  75.139  1.00115.68           C  
ANISOU  748  CG  PRO A1090    12077  15575  16301   1572    494   -693       C  
ATOM    749  CD  PRO A1090      39.955  45.354  74.363  1.00113.81           C  
ANISOU  749  CD  PRO A1090    12053  15099  16089   1413    598   -775       C  
ATOM    750  N   THR A1091      36.946  42.776  76.988  1.00112.59           N  
ANISOU  750  N   THR A1091    12064  14700  16016   1861    371   -310       N  
ATOM    751  CA  THR A1091      35.812  42.644  77.920  1.00112.22           C  
ANISOU  751  CA  THR A1091    12119  14565  15954   1883    337   -226       C  
ATOM    752  C   THR A1091      35.792  43.634  79.105  1.00111.54           C  
ANISOU  752  C   THR A1091    12007  14635  15738   1751    301   -261       C  
ATOM    753  O   THR A1091      34.932  43.550  79.977  1.00110.46           O  
ANISOU  753  O   THR A1091    11941  14451  15579   1768    267   -191       O  
ATOM    754  CB  THR A1091      35.654  41.166  78.390  1.00113.12           C  
ANISOU  754  CB  THR A1091    12220  14642  16121   2098    310    -76       C  
ATOM    755  OG1 THR A1091      34.488  41.029  79.214  1.00113.64           O  
ANISOU  755  OG1 THR A1091    12400  14600  16179   2104    295     -7       O  
ATOM    756  CG2 THR A1091      36.891  40.674  79.152  1.00115.01           C  
ANISOU  756  CG2 THR A1091    12270  15151  16277   2224    258    -17       C  
ATOM    757  N   SER A1092      36.730  44.578  79.109  1.00113.89           N  
ANISOU  757  N   SER A1092    12208  15115  15950   1602    323   -383       N  
ATOM    758  CA  SER A1092      36.813  45.641  80.124  1.00115.21           C  
ANISOU  758  CA  SER A1092    12350  15439  15988   1433    318   -454       C  
ATOM    759  C   SER A1092      37.280  46.956  79.473  1.00115.18           C  
ANISOU  759  C   SER A1092    12386  15441  15937   1206    429   -629       C  
ATOM    760  O   SER A1092      36.929  47.245  78.318  1.00113.17           O  
ANISOU  760  O   SER A1092    12273  14974  15751   1183    511   -666       O  
ATOM    761  CB  SER A1092      37.782  45.233  81.247  1.00117.51           C  
ANISOU  761  CB  SER A1092    12412  16064  16172   1497    234   -429       C  
ATOM    762  OG  SER A1092      37.353  44.050  81.904  1.00118.22           O  
ANISOU  762  OG  SER A1092    12498  16131  16290   1722    159   -256       O  
ATOM    763  N   SER A1093      38.078  47.730  80.216  1.00115.78           N  
ANISOU  763  N   SER A1093    12339  15766  15885   1040    444   -743       N  
ATOM    764  CA  SER A1093      38.772  48.925  79.706  1.00116.45           C  
ANISOU  764  CA  SER A1093    12439  15897  15909    799    578   -935       C  
ATOM    765  C   SER A1093      37.853  50.073  79.272  1.00114.95           C  
ANISOU  765  C   SER A1093    12528  15433  15716    659    714   -986       C  
ATOM    766  O   SER A1093      36.878  49.871  78.539  1.00111.58           O  
ANISOU  766  O   SER A1093    12280  14740  15376    773    728   -901       O  
ATOM    767  CB  SER A1093      39.757  48.567  78.575  1.00117.15           C  
ANISOU  767  CB  SER A1093    12430  16030  16054    829    615   -996       C  
ATOM    768  OG  SER A1093      41.028  48.181  79.087  1.00118.39           O  
ANISOU  768  OG  SER A1093    12302  16552  16129    838    552  -1052       O  
ATOM    769  N   GLY A1094      38.193  51.279  79.727  1.00115.87           N  
ANISOU  769  N   GLY A1094    12675  15632  15717    414    828  -1135       N  
ATOM    770  CA  GLY A1094      37.420  52.480  79.417  1.00115.20           C  
ANISOU  770  CA  GLY A1094    12875  15299  15599    282    991  -1188       C  
ATOM    771  C   GLY A1094      36.022  52.414  80.007  1.00113.40           C  
ANISOU  771  C   GLY A1094    12796  14911  15378    391    926  -1050       C  
ATOM    772  O   GLY A1094      35.853  52.352  81.234  1.00111.96           O  
ANISOU  772  O   GLY A1094    12533  14868  15137    366    843  -1019       O  
ATOM    773  N   PHE A1095      35.021  52.424  79.127  1.00 98.71           N  
ANISOU  773  N   PHE A1095     8352  12540  16612   1321    488     71       N  
ATOM    774  CA  PHE A1095      33.621  52.281  79.551  1.00 96.18           C  
ANISOU  774  CA  PHE A1095     8295  11960  16290   1182    545     32       C  
ATOM    775  C   PHE A1095      32.859  51.162  78.826  1.00 94.10           C  
ANISOU  775  C   PHE A1095     8203  11538  16012   1288    623    -40       C  
ATOM    776  O   PHE A1095      33.145  50.828  77.666  1.00 93.52           O  
ANISOU  776  O   PHE A1095     8034  11553  15947   1419    673    -70       O  
ATOM    777  CB  PHE A1095      32.851  53.623  79.518  1.00 95.08           C  
ANISOU  777  CB  PHE A1095     8110  11820  16195    924    611     36       C  
ATOM    778  CG  PHE A1095      33.652  54.801  78.993  1.00 98.24           C  
ANISOU  778  CG  PHE A1095     8246  12459  16623    849    608     77       C  
ATOM    779  CD1 PHE A1095      33.645  55.131  77.635  1.00 99.64           C  
ANISOU  779  CD1 PHE A1095     8276  12749  16833    864    700     49       C  
ATOM    780  CD2 PHE A1095      34.402  55.605  79.862  1.00 98.33           C  
ANISOU  780  CD2 PHE A1095     8174  12572  16614    743    514    144       C  
ATOM    781  CE1 PHE A1095      34.380  56.224  77.156  1.00 99.62           C  
ANISOU  781  CE1 PHE A1095     8055  12955  16842    772    710     88       C  
ATOM    782  CE2 PHE A1095      35.127  56.697  79.387  1.00 97.42           C  
ANISOU  782  CE2 PHE A1095     7834  12670  16513    639    515    181       C  
ATOM    783  CZ  PHE A1095      35.117  57.008  78.036  1.00 97.69           C  
ANISOU  783  CZ  PHE A1095     7729  12813  16578    650    620    153       C  
ATOM    784  N   GLU A1096      31.891  50.591  79.540  1.00 91.90           N  
ANISOU  784  N   GLU A1096     8193  11022  15704   1216    637    -67       N  
ATOM    785  CA  GLU A1096      31.118  49.435  79.087  1.00 91.69           C  
ANISOU  785  CA  GLU A1096     8382  10811  15644   1278    695   -134       C  
ATOM    786  C   GLU A1096      30.263  49.681  77.842  1.00 91.46           C  
ANISOU  786  C   GLU A1096     8290  10794  15668   1195    802   -193       C  
ATOM    787  O   GLU A1096      29.593  48.762  77.348  1.00 92.05           O  
ANISOU  787  O   GLU A1096     8533  10728  15713   1222    847   -253       O  
ATOM    788  CB  GLU A1096      30.236  48.915  80.229  1.00 91.55           C  
ANISOU  788  CB  GLU A1096     8658  10548  15580   1163    696   -145       C  
ATOM    789  CG  GLU A1096      29.415  49.967  80.988  1.00 89.25           C  
ANISOU  789  CG  GLU A1096     8361  10219  15332    912    736   -128       C  
ATOM    790  CD  GLU A1096      28.574  49.341  82.103  1.00 88.79           C  
ANISOU  790  CD  GLU A1096     8603   9918  15217    809    757   -141       C  
ATOM    791  OE1 GLU A1096      27.477  48.802  81.808  1.00 88.10           O  
ANISOU  791  OE1 GLU A1096     8648   9695  15132    717    847   -202       O  
ATOM    792  OE2 GLU A1096      29.015  49.370  83.273  1.00 87.27           O  
ANISOU  792  OE2 GLU A1096     8519   9670  14969    812    682    -92       O  
ATOM    793  N   ILE A1097      30.302  50.917  77.343  1.00 90.41           N  
ANISOU  793  N   ILE A1097     7930  10823  15599   1091    835   -175       N  
ATOM    794  CA  ILE A1097      29.437  51.381  76.255  1.00 88.61           C  
ANISOU  794  CA  ILE A1097     7638  10612  15418    996    922   -224       C  
ATOM    795  C   ILE A1097      29.880  50.789  74.910  1.00 88.93           C  
ANISOU  795  C   ILE A1097     7626  10723  15439   1168    950   -260       C  
ATOM    796  O   ILE A1097      29.035  50.492  74.055  1.00 89.49           O  
ANISOU  796  O   ILE A1097     7765  10722  15514   1136   1004   -322       O  
ATOM    797  CB  ILE A1097      29.405  52.929  76.187  1.00 87.29           C  
ANISOU  797  CB  ILE A1097     7285  10580  15302    845    943   -189       C  
ATOM    798  CG1 ILE A1097      29.344  53.516  77.599  1.00 86.91           C  
ANISOU  798  CG1 ILE A1097     7290  10482  15248    717    901   -139       C  
ATOM    799  CG2 ILE A1097      28.237  53.424  75.326  1.00 85.69           C  
ANISOU  799  CG2 ILE A1097     7068  10352  15140    734   1022   -242       C  
ATOM    800  CD1 ILE A1097      30.136  54.796  77.746  1.00 88.96           C  
ANISOU  800  CD1 ILE A1097     7374  10910  15518    646    869    -76       C  
ATOM    801  N   LEU A1098      31.190  50.615  74.729  1.00 88.59           N  
ANISOU  801  N   LEU A1098     7463  10826  15371   1350    913   -223       N  
ATOM    802  CA  LEU A1098      31.730  49.909  73.551  1.00 88.90           C  
ANISOU  802  CA  LEU A1098     7479  10924  15374   1555    948   -255       C  
ATOM    803  C   LEU A1098      31.255  48.453  73.546  1.00 89.02           C  
ANISOU  803  C   LEU A1098     7782  10722  15320   1665    944   -309       C  
ATOM    804  O   LEU A1098      30.970  47.883  72.488  1.00 88.98           O  
ANISOU  804  O   LEU A1098     7859  10667  15282   1738    995   -363       O  
ATOM    805  CB  LEU A1098      33.263  49.971  73.504  1.00 88.79           C  
ANISOU  805  CB  LEU A1098     7262  11127  15345   1742    914   -201       C  
ATOM    806  CG  LEU A1098      33.886  51.366  73.599  1.00 87.18           C  
ANISOU  806  CG  LEU A1098     6784  11146  15195   1614    908   -142       C  
ATOM    807  CD1 LEU A1098      34.930  51.404  74.708  1.00 87.92           C  
ANISOU  807  CD1 LEU A1098     6780  11348  15279   1673    802    -76       C  
ATOM    808  CD2 LEU A1098      34.458  51.808  72.256  1.00 86.80           C  
ANISOU  808  CD2 LEU A1098     6538  11289  15153   1671    993   -148       C  
ATOM    809  N   ARG A1099      31.133  47.880  74.741  1.00 88.75           N  
ANISOU  809  N   ARG A1099     7928  10543  15251   1659    885   -294       N  
ATOM    810  CA  ARG A1099      30.645  46.515  74.908  1.00 89.82           C  
ANISOU  810  CA  ARG A1099     8384  10443  15302   1729    879   -340       C  
ATOM    811  C   ARG A1099      29.112  46.419  74.717  1.00 88.31           C  
ANISOU  811  C   ARG A1099     8344  10081  15129   1496    937   -403       C  
ATOM    812  O   ARG A1099      28.574  45.321  74.541  1.00 89.88           O  
ANISOU  812  O   ARG A1099     8805  10090  15255   1512    950   -456       O  
ATOM    813  CB  ARG A1099      31.108  45.958  76.264  1.00 91.27           C  
ANISOU  813  CB  ARG A1099     8725  10529  15426   1807    793   -298       C  
ATOM    814  CG  ARG A1099      31.056  44.445  76.420  1.00 93.35           C  
ANISOU  814  CG  ARG A1099     9335  10567  15567   1965    773   -333       C  
ATOM    815  CD  ARG A1099      31.276  44.068  77.884  1.00 95.30           C  
ANISOU  815  CD  ARG A1099     9765  10690  15753   1984    689   -290       C  
ATOM    816  NE  ARG A1099      30.675  42.780  78.250  1.00 96.10           N  
ANISOU  816  NE  ARG A1099    10279  10498  15738   1995    693   -332       N  
ATOM    817  CZ  ARG A1099      30.557  42.330  79.500  1.00 96.16           C  
ANISOU  817  CZ  ARG A1099    10535  10329  15671   1964    641   -309       C  
ATOM    818  NH1 ARG A1099      30.982  43.067  80.520  1.00 94.48           N  
ANISOU  818  NH1 ARG A1099    10200  10206  15494   1923    573   -246       N  
ATOM    819  NH2 ARG A1099      30.008  41.138  79.727  1.00 96.95           N  
ANISOU  819  NH2 ARG A1099    11033  10153  15650   1962    657   -350       N  
ATOM    820  N   VAL A1100      28.416  47.558  74.733  1.00 85.34           N  
ANISOU  820  N   VAL A1100     7807   9778  14841   1282    971   -399       N  
ATOM    821  CA  VAL A1100      26.995  47.588  74.330  1.00 83.76           C  
ANISOU  821  CA  VAL A1100     7675   9478  14670   1083   1027   -462       C  
ATOM    822  C   VAL A1100      26.869  47.572  72.797  1.00 83.30           C  
ANISOU  822  C   VAL A1100     7549   9487  14613   1136   1060   -511       C  
ATOM    823  O   VAL A1100      26.052  46.821  72.236  1.00 82.95           O  
ANISOU  823  O   VAL A1100     7667   9316  14534   1084   1078   -577       O  
ATOM    824  CB  VAL A1100      26.202  48.797  74.915  1.00 82.28           C  
ANISOU  824  CB  VAL A1100     7356   9338  14568    860   1054   -444       C  
ATOM    825  CG1 VAL A1100      24.782  48.821  74.366  1.00 81.66           C  
ANISOU  825  CG1 VAL A1100     7302   9201  14525    687   1105   -512       C  
ATOM    826  CG2 VAL A1100      26.136  48.755  76.440  1.00 82.09           C  
ANISOU  826  CG2 VAL A1100     7447   9214  14529    782   1033   -404       C  
ATOM    827  N   LEU A1101      27.708  48.375  72.137  1.00 82.57           N  
ANISOU  827  N   LEU A1101     7234   9590  14550   1232   1068   -478       N  
ATOM    828  CA  LEU A1101      27.650  48.593  70.689  1.00 82.26           C  
ANISOU  828  CA  LEU A1101     7114   9632  14510   1274   1107   -516       C  
ATOM    829  C   LEU A1101      28.097  47.382  69.858  1.00 84.61           C  
ANISOU  829  C   LEU A1101     7575   9860  14714   1475   1115   -555       C  
ATOM    830  O   LEU A1101      28.348  47.501  68.652  1.00 85.57           O  
ANISOU  830  O   LEU A1101     7639  10059  14814   1560   1151   -578       O  
ATOM    831  CB  LEU A1101      28.476  49.825  70.325  1.00 81.43           C  
ANISOU  831  CB  LEU A1101     6743   9749  14448   1301   1126   -463       C  
ATOM    832  CG  LEU A1101      28.096  51.163  70.977  1.00 79.68           C  
ANISOU  832  CG  LEU A1101     6379   9598  14300   1112   1123   -423       C  
ATOM    833  CD1 LEU A1101      29.335  51.835  71.552  1.00 79.69           C  
ANISOU  833  CD1 LEU A1101     6212   9757  14310   1160   1100   -345       C  
ATOM    834  CD2 LEU A1101      27.371  52.080  69.997  1.00 78.01           C  
ANISOU  834  CD2 LEU A1101     6079   9444  14119   1008   1161   -452       C  
ATOM    835  N   ARG A1102      28.179  46.221  70.505  1.00 85.64           N  
ANISOU  835  N   ARG A1102     7939   9827  14774   1554   1085   -565       N  
ATOM    836  CA  ARG A1102      28.416  44.945  69.827  1.00 86.96           C  
ANISOU  836  CA  ARG A1102     8342   9869  14828   1734   1091   -610       C  
ATOM    837  C   ARG A1102      27.112  44.292  69.336  1.00 87.28           C  
ANISOU  837  C   ARG A1102     8611   9720  14830   1569   1097   -691       C  
ATOM    838  O   ARG A1102      27.115  43.139  68.890  1.00 89.20           O  
ANISOU  838  O   ARG A1102     9122   9808  14963   1673   1096   -735       O  
ATOM    839  CB  ARG A1102      29.155  43.979  70.758  1.00 88.83           C  
ANISOU  839  CB  ARG A1102     8761  10005  14986   1915   1049   -581       C  
ATOM    840  CG  ARG A1102      30.471  44.504  71.321  1.00 89.01           C  
ANISOU  840  CG  ARG A1102     8557  10224  15040   2083   1020   -503       C  
ATOM    841  CD  ARG A1102      31.120  43.473  72.223  1.00 90.12           C  
ANISOU  841  CD  ARG A1102     8904  10249  15088   2280    960   -480       C  
ATOM    842  NE  ARG A1102      32.302  43.986  72.905  1.00 90.01           N  
ANISOU  842  NE  ARG A1102     8661  10431  15107   2416    907   -404       N  
ATOM    843  CZ  ARG A1102      33.035  43.274  73.758  1.00 91.56           C  
ANISOU  843  CZ  ARG A1102     8977  10579  15231   2614    832   -371       C  
ATOM    844  NH1 ARG A1102      32.718  42.014  74.026  1.00 92.70           N  
ANISOU  844  NH1 ARG A1102     9498  10468  15257   2706    813   -406       N  
ATOM    845  NH2 ARG A1102      34.091  43.818  74.343  1.00 91.83           N  
ANISOU  845  NH2 ARG A1102     8768  10819  15303   2717    770   -303       N  
ATOM    846  N   VAL A1103      25.998  45.017  69.440  1.00 86.12           N  
ANISOU  846  N   VAL A1103     8365   9589  14768   1313   1101   -710       N  
ATOM    847  CA  VAL A1103      24.716  44.566  68.873  1.00 86.22           C  
ANISOU  847  CA  VAL A1103     8522   9476  14760   1131   1098   -787       C  
ATOM    848  C   VAL A1103      24.392  45.333  67.589  1.00 85.96           C  
ANISOU  848  C   VAL A1103     8324   9572  14765   1100   1108   -816       C  
ATOM    849  O   VAL A1103      23.227  45.426  67.179  1.00 85.16           O  
ANISOU  849  O   VAL A1103     8230   9439  14687    913   1091   -871       O  
ATOM    850  CB  VAL A1103      23.549  44.683  69.875  1.00 85.44           C  
ANISOU  850  CB  VAL A1103     8446   9299  14719    865   1096   -799       C  
ATOM    851  CG1 VAL A1103      23.550  43.521  70.848  1.00 86.82           C  
ANISOU  851  CG1 VAL A1103     8914   9266  14808    858   1088   -801       C  
ATOM    852  CG2 VAL A1103      23.638  45.985  70.633  1.00 84.44           C  
ANISOU  852  CG2 VAL A1103     8055   9325  14703    802   1108   -738       C  
ATOM    853  N   LEU A1104      25.439  45.891  66.975  1.00 86.49           N  
ANISOU  853  N   LEU A1104     8237   9792  14833   1283   1133   -779       N  
ATOM    854  CA  LEU A1104      25.350  46.485  65.642  1.00 86.87           C  
ANISOU  854  CA  LEU A1104     8183   9943  14881   1300   1150   -805       C  
ATOM    855  C   LEU A1104      25.718  45.440  64.581  1.00 89.62           C  
ANISOU  855  C   LEU A1104     8751  10196  15103   1468   1163   -852       C  
ATOM    856  O   LEU A1104      25.561  45.673  63.376  1.00 89.62           O  
ANISOU  856  O   LEU A1104     8746  10235  15072   1485   1173   -886       O  
ATOM    857  CB  LEU A1104      26.276  47.694  65.516  1.00 85.36           C  
ANISOU  857  CB  LEU A1104     7723   9965  14745   1381   1188   -739       C  
ATOM    858  CG  LEU A1104      26.109  48.905  66.432  1.00 84.28           C  
ANISOU  858  CG  LEU A1104     7375   9935  14712   1240   1182   -685       C  
ATOM    859  CD1 LEU A1104      27.114  49.984  66.035  1.00 83.76           C  
ANISOU  859  CD1 LEU A1104     7090  10068  14666   1319   1224   -628       C  
ATOM    860  CD2 LEU A1104      24.685  49.463  66.420  1.00 83.14           C  
ANISOU  860  CD2 LEU A1104     7201   9761  14627   1022   1157   -723       C  
ATOM    861  N   ARG A1105      26.210  44.287  65.030  1.00 91.65           N  
ANISOU  861  N   ARG A1105     9228  10319  15276   1603   1161   -853       N  
ATOM    862  CA  ARG A1105      26.561  43.220  64.101  1.00 95.01           C  
ANISOU  862  CA  ARG A1105     9909  10627  15562   1781   1178   -898       C  
ATOM    863  C   ARG A1105      25.291  42.447  63.680  1.00 96.15           C  
ANISOU  863  C   ARG A1105    10319  10572  15642   1590   1130   -982       C  
ATOM    864  O   ARG A1105      25.355  41.328  63.162  1.00 99.09           O  
ANISOU  864  O   ARG A1105    11000  10773  15876   1685   1127  -1028       O  
ATOM    865  CB  ARG A1105      27.719  42.331  64.642  1.00 96.17           C  
ANISOU  865  CB  ARG A1105    10193  10722  15626   2054   1198   -864       C  
ATOM    866  CG  ARG A1105      27.416  41.486  65.878  1.00 96.42           C  
ANISOU  866  CG  ARG A1105    10444  10568  15625   1996   1152   -861       C  
ATOM    867  CD  ARG A1105      28.487  40.424  66.124  1.00 97.83           C  
ANISOU  867  CD  ARG A1105    10836  10656  15677   2308   1161   -844       C  
ATOM    868  NE  ARG A1105      29.433  40.850  67.155  1.00 97.42           N  
ANISOU  868  NE  ARG A1105    10579  10746  15688   2436   1148   -765       N  
ATOM    869  CZ  ARG A1105      29.603  40.262  68.340  1.00 97.47           C  
ANISOU  869  CZ  ARG A1105    10740  10636  15659   2477   1101   -738       C  
ATOM    870  NH1 ARG A1105      28.913  39.179  68.674  1.00 97.79           N  
ANISOU  870  NH1 ARG A1105    11162  10401  15592   2401   1075   -783       N  
ATOM    871  NH2 ARG A1105      30.484  40.761  69.198  1.00 97.08           N  
ANISOU  871  NH2 ARG A1105    10476  10742  15670   2587   1075   -666       N  
ATOM    872  N   LEU A1106      24.139  43.069  63.905  1.00 95.00           N  
ANISOU  872  N   LEU A1106    10050  10455  15592   1318   1090  -1001       N  
ATOM    873  CA  LEU A1106      22.869  42.576  63.369  1.00 97.01           C  
ANISOU  873  CA  LEU A1106    10470  10585  15807   1103   1035  -1081       C  
ATOM    874  C   LEU A1106      22.348  43.522  62.284  1.00 96.17           C  
ANISOU  874  C   LEU A1106    10177  10615  15747   1030   1011  -1106       C  
ATOM    875  O   LEU A1106      21.448  43.180  61.513  1.00 95.47           O  
ANISOU  875  O   LEU A1106    10209  10456  15611    895    953  -1175       O  
ATOM    876  CB  LEU A1106      21.843  42.363  64.485  1.00 97.36           C  
ANISOU  876  CB  LEU A1106    10541  10545  15906    842   1007  -1094       C  
ATOM    877  CG  LEU A1106      22.282  41.415  65.617  1.00 99.50           C  
ANISOU  877  CG  LEU A1106    11037  10655  16115    897   1026  -1069       C  
ATOM    878  CD1 LEU A1106      21.122  41.167  66.574  1.00 99.78           C  
ANISOU  878  CD1 LEU A1106    11127  10595  16188    601   1012  -1092       C  
ATOM    879  CD2 LEU A1106      22.855  40.095  65.099  1.00100.88           C  
ANISOU  879  CD2 LEU A1106    11584  10635  16112   1079   1026  -1101       C  
ATOM    880  N   PHE A1107      22.939  44.714  62.244  1.00 95.87           N  
ANISOU  880  N   PHE A1107     9862  10771  15794   1116   1050  -1049       N  
ATOM    881  CA  PHE A1107      22.840  45.613  61.103  1.00 95.56           C  
ANISOU  881  CA  PHE A1107     9687  10858  15765   1131   1045  -1059       C  
ATOM    882  C   PHE A1107      23.759  45.113  60.015  1.00 96.89           C  
ANISOU  882  C   PHE A1107    10011  10998  15807   1357   1091  -1071       C  
ATOM    883  O   PHE A1107      23.979  45.800  59.016  1.00 97.09           O  
ANISOU  883  O   PHE A1107     9953  11121  15814   1419   1112  -1071       O  
ATOM    884  CB  PHE A1107      23.267  47.029  61.494  1.00 94.21           C  
ANISOU  884  CB  PHE A1107     9208  10883  15704   1144   1084   -989       C  
ATOM    885  CG  PHE A1107      22.178  48.067  61.348  1.00 92.85           C  
ANISOU  885  CG  PHE A1107     8867  10796  15615    964   1033  -1004       C  
ATOM    886  CD1 PHE A1107      21.768  48.814  62.449  1.00 90.75           C  
ANISOU  886  CD1 PHE A1107     8423  10597  15461    842   1033   -966       C  
ATOM    887  CD2 PHE A1107      21.583  48.317  60.103  1.00 91.93           C  
ANISOU  887  CD2 PHE A1107     8780  10694  15454    936    984  -1055       C  
ATOM    888  CE1 PHE A1107      20.786  49.781  62.314  1.00 90.53           C  
ANISOU  888  CE1 PHE A1107     8244  10652  15501    713    992   -979       C  
ATOM    889  CE2 PHE A1107      20.605  49.284  59.964  1.00 90.03           C  
ANISOU  889  CE2 PHE A1107     8384  10541  15284    804    929  -1068       C  
ATOM    890  CZ  PHE A1107      20.208  50.020  61.067  1.00 89.85           C  
ANISOU  890  CZ  PHE A1107     8176  10588  15373    702    936  -1030       C  
ATOM    891  N   ARG A1108      24.316  43.924  60.239  1.00 99.01           N  
ANISOU  891  N   ARG A1108    10516  11124  15978   1493   1115  -1079       N  
ATOM    892  CA  ARG A1108      25.136  43.235  59.241  1.00101.28           C  
ANISOU  892  CA  ARG A1108    11006  11353  16124   1729   1167  -1098       C  
ATOM    893  C   ARG A1108      24.252  42.236  58.507  1.00103.01           C  
ANISOU  893  C   ARG A1108    11556  11365  16219   1630   1100  -1186       C  
ATOM    894  O   ARG A1108      24.735  41.316  57.831  1.00104.13           O  
ANISOU  894  O   ARG A1108    11978  11377  16210   1803   1130  -1216       O  
ATOM    895  CB  ARG A1108      26.324  42.532  59.900  1.00101.53           C  
ANISOU  895  CB  ARG A1108    11114  11358  16107   1975   1230  -1055       C  
ATOM    896  CG  ARG A1108      27.608  42.627  59.095  1.00102.11           C  
ANISOU  896  CG  ARG A1108    11141  11543  16113   2268   1332  -1028       C  
ATOM    897  CD  ARG A1108      28.690  41.781  59.731  1.00104.27           C  
ANISOU  897  CD  ARG A1108    11509  11783  16326   2532   1378   -993       C  
ATOM    898  NE  ARG A1108      29.992  41.977  59.105  1.00105.12           N  
ANISOU  898  NE  ARG A1108    11495  12054  16393   2818   1489   -958       N  
ATOM    899  CZ  ARG A1108      30.960  41.068  59.113  1.00108.39           C  
ANISOU  899  CZ  ARG A1108    12054  12429  16700   3123   1546   -950       C  
ATOM    900  NH1 ARG A1108      30.766  39.892  59.701  1.00109.44           N  
ANISOU  900  NH1 ARG A1108    12499  12340  16745   3183   1495   -974       N  
ATOM    901  NH2 ARG A1108      32.119  41.325  58.518  1.00111.07           N  
ANISOU  901  NH2 ARG A1108    12238  12952  17013   3373   1659   -919       N  
ATOM    902  N   LEU A1109      22.944  42.430  58.681  1.00103.03           N  
ANISOU  902  N   LEU A1109    11522  11340  16283   1345   1008  -1225       N  
ATOM    903  CA  LEU A1109      21.914  41.660  58.001  1.00103.79           C  
ANISOU  903  CA  LEU A1109    11877  11275  16283   1177    919  -1311       C  
ATOM    904  C   LEU A1109      21.442  42.543  56.868  1.00103.05           C  
ANISOU  904  C   LEU A1109    11651  11298  16205   1123    873  -1337       C  
ATOM    905  O   LEU A1109      20.824  42.073  55.910  1.00104.63           O  
ANISOU  905  O   LEU A1109    12055  11398  16302   1045    798  -1406       O  
ATOM    906  CB  LEU A1109      20.779  41.321  58.983  1.00103.55           C  
ANISOU  906  CB  LEU A1109    11856  11171  16317    888    851  -1336       C  
ATOM    907  CG  LEU A1109      19.451  40.638  58.620  1.00104.91           C  
ANISOU  907  CG  LEU A1109    12215  11215  16432    609    743  -1423       C  
ATOM    908  CD1 LEU A1109      19.583  39.502  57.612  1.00107.09           C  
ANISOU  908  CD1 LEU A1109    12900  11285  16505    674    716  -1485       C  
ATOM    909  CD2 LEU A1109      18.791  40.144  59.905  1.00104.90           C  
ANISOU  909  CD2 LEU A1109    12244  11133  16481    388    736  -1425       C  
ATOM    910  N   VAL A1110      21.768  43.829  56.985  1.00100.54           N  
ANISOU  910  N   VAL A1110    11013  11185  16005   1168    912  -1279       N  
ATOM    911  CA  VAL A1110      21.467  44.804  55.945  1.00100.49           C  
ANISOU  911  CA  VAL A1110    10882  11294  16005   1153    880  -1291       C  
ATOM    912  C   VAL A1110      22.655  44.924  54.979  1.00100.78           C  
ANISOU  912  C   VAL A1110    10989  11363  15940   1409    979  -1269       C  
ATOM    913  O   VAL A1110      22.445  45.114  53.777  1.00102.10           O  
ANISOU  913  O   VAL A1110    11251  11521  16021   1427    950  -1307       O  
ATOM    914  CB  VAL A1110      21.081  46.187  56.535  1.00100.16           C  
ANISOU  914  CB  VAL A1110    10493  11440  16125   1049    868  -1245       C  
ATOM    915  CG1 VAL A1110      20.528  47.108  55.454  1.00100.19           C  
ANISOU  915  CG1 VAL A1110    10418  11531  16117   1012    805  -1269       C  
ATOM    916  CG2 VAL A1110      20.058  46.041  57.659  1.00 99.19           C  
ANISOU  916  CG2 VAL A1110    10284  11298  16105    825    807  -1257       C  
ATOM    917  N   THR A1111      23.890  44.807  55.484  1.00 99.16           N  
ANISOU  917  N   THR A1111    10737  11202  15738   1608   1097  -1210       N  
ATOM    918  CA  THR A1111      25.052  44.722  54.585  1.00 99.90           C  
ANISOU  918  CA  THR A1111    10909  11326  15722   1863   1210  -1194       C  
ATOM    919  C   THR A1111      25.067  43.428  53.791  1.00101.50           C  
ANISOU  919  C   THR A1111    11497  11324  15745   1966   1206  -1259       C  
ATOM    920  O   THR A1111      25.302  43.454  52.586  1.00102.87           O  
ANISOU  920  O   THR A1111    11802  11481  15803   2067   1242  -1286       O  
ATOM    921  CB  THR A1111      26.428  44.868  55.286  1.00 99.90           C  
ANISOU  921  CB  THR A1111    10741  11452  15765   2068   1336  -1116       C  
ATOM    922  OG1 THR A1111      26.339  44.434  56.648  1.00 99.45           O  
ANISOU  922  OG1 THR A1111    10650  11351  15784   2014   1301  -1093       O  
ATOM    923  CG2 THR A1111      26.907  46.306  55.250  1.00100.10           C  
ANISOU  923  CG2 THR A1111    10444  11703  15885   2057   1396  -1054       C  
ATOM    924  N   ALA A1112      24.803  42.309  54.468  1.00102.16           N  
ANISOU  924  N   ALA A1112    11788  11237  15790   1933   1164  -1285       N  
ATOM    925  CA  ALA A1112      25.002  40.970  53.897  1.00105.16           C  
ANISOU  925  CA  ALA A1112    12578  11397  15980   2064   1176  -1338       C  
ATOM    926  C   ALA A1112      23.870  40.485  52.973  1.00107.13           C  
ANISOU  926  C   ALA A1112    13106  11481  16119   1876   1056  -1427       C  
ATOM    927  O   ALA A1112      23.956  39.389  52.395  1.00108.55           O  
ANISOU  927  O   ALA A1112    13670  11455  16118   1962   1056  -1477       O  
ATOM    928  CB  ALA A1112      25.275  39.960  55.002  1.00105.34           C  
ANISOU  928  CB  ALA A1112    12753  11289  15984   2122   1185  -1326       C  
ATOM    929  N   VAL A1113      22.828  41.310  52.833  1.00106.84           N  
ANISOU  929  N   VAL A1113    12878  11536  16181   1628    949  -1445       N  
ATOM    930  CA  VAL A1113      21.655  40.998  51.998  1.00108.99           C  
ANISOU  930  CA  VAL A1113    13346  11696  16371   1418    806  -1528       C  
ATOM    931  C   VAL A1113      21.370  42.158  51.021  1.00109.16           C  
ANISOU  931  C   VAL A1113    13192  11866  16418   1394    767  -1531       C  
ATOM    932  O   VAL A1113      21.315  43.319  51.435  1.00108.01           O  
ANISOU  932  O   VAL A1113    12702  11912  16424   1355    777  -1481       O  
ATOM    933  CB  VAL A1113      20.406  40.678  52.867  1.00108.83           C  
ANISOU  933  CB  VAL A1113    13290  11626  16435   1101    680  -1562       C  
ATOM    934  CG1 VAL A1113      19.190  40.380  52.002  1.00110.16           C  
ANISOU  934  CG1 VAL A1113    13622  11711  16523    867    518  -1648       C  
ATOM    935  CG2 VAL A1113      20.681  39.496  53.790  1.00110.60           C  
ANISOU  935  CG2 VAL A1113    13745  11672  16605   1118    720  -1561       C  
ATOM    936  N   PRO A1114      21.191  41.850  49.722  1.00111.15           N  
ANISOU  936  N   PRO A1114    13710  12015  16507   1422    719  -1588       N  
ATOM    937  CA  PRO A1114      21.017  42.900  48.711  1.00111.87           C  
ANISOU  937  CA  PRO A1114    13692  12223  16589   1431    687  -1590       C  
ATOM    938  C   PRO A1114      19.613  43.521  48.707  1.00113.35           C  
ANISOU  938  C   PRO A1114    13705  12490  16872   1161    500  -1626       C  
ATOM    939  O   PRO A1114      19.443  44.683  48.302  1.00112.94           O  
ANISOU  939  O   PRO A1114    13450  12586  16875   1164    475  -1605       O  
ATOM    940  CB  PRO A1114      21.263  42.165  47.383  1.00113.09           C  
ANISOU  940  CB  PRO A1114    14251  12205  16513   1549    691  -1646       C  
ATOM    941  CG  PRO A1114      21.648  40.763  47.741  1.00114.78           C  
ANISOU  941  CG  PRO A1114    14777  12216  16617   1625    740  -1668       C  
ATOM    942  CD  PRO A1114      21.134  40.510  49.120  1.00113.69           C  
ANISOU  942  CD  PRO A1114    14484  12088  16625   1446    690  -1655       C  
ATOM    943  N   GLN A1115      18.623  42.741  49.145  1.00114.64           N  
ANISOU  943  N   GLN A1115    13956  12557  17045    932    373  -1680       N  
ATOM    944  CA  GLN A1115      17.227  43.177  49.190  1.00114.19           C  
ANISOU  944  CA  GLN A1115    13721  12588  17077    667    192  -1721       C  
ATOM    945  C   GLN A1115      17.024  44.218  50.280  1.00112.73           C  
ANISOU  945  C   GLN A1115    13118  12605  17108    615    222  -1661       C  
ATOM    946  O   GLN A1115      16.123  45.064  50.178  1.00112.60           O  
ANISOU  946  O   GLN A1115    12875  12728  17179    496    109  -1672       O  
ATOM    947  CB  GLN A1115      16.295  41.990  49.441  1.00115.75           C  
ANISOU  947  CB  GLN A1115    14119  12637  17223    415     71  -1793       C  
ATOM    948  CG  GLN A1115      16.445  40.836  48.462  1.00116.77           C  
ANISOU  948  CG  GLN A1115    14717  12530  17119    442     34  -1857       C  
ATOM    949  CD  GLN A1115      15.247  39.910  48.492  1.00118.24           C  
ANISOU  949  CD  GLN A1115    15074  12601  17250    121   -136  -1940       C  
ATOM    950  OE1 GLN A1115      14.153  40.283  48.061  1.00118.45           O  
ANISOU  950  OE1 GLN A1115    14972  12724  17308    -83   -312  -1987       O  
ATOM    951  NE2 GLN A1115      15.443  38.697  49.001  1.00118.46           N  
ANISOU  951  NE2 GLN A1115    15395  12426  17189     72    -89  -1957       N  
HETATM  952  N   MSE A1116      17.853  44.140  51.322  1.00110.84           N  
ANISOU  952  N   MSE A1116    12792  12378  16945    714    367  -1598       N  
HETATM  953  CA  MSE A1116      17.876  45.164  52.373  1.00110.02           C  
ANISOU  953  CA  MSE A1116    12325  12451  17027    697    420  -1531       C  
HETATM  954  C   MSE A1116      18.745  46.318  51.919  1.00108.60           C  
ANISOU  954  C   MSE A1116    12005  12400  16859    895    513  -1470       C  
HETATM  955  O   MSE A1116      18.414  47.477  52.168  1.00106.29           O  
ANISOU  955  O   MSE A1116    11449  12261  16676    858    493  -1437       O  
HETATM  956  CB  MSE A1116      18.336  44.591  53.716  1.00109.10           C  
ANISOU  956  CB  MSE A1116    12187  12287  16977    697    516  -1491       C  
HETATM  957  CG  MSE A1116      17.712  43.224  54.005  1.00110.95           C  
ANISOU  957  CG  MSE A1116    12677  12338  17142    526    452  -1553       C  
HETATM  958 SE   MSE A1116      15.834  43.371  54.602  1.00110.26          SE  
ANISOU  958 SE   MSE A1116    12376  12333  17184    137    293  -1608      SE  
HETATM  959  CE  MSE A1116      14.939  42.861  52.923  1.00113.83           C  
ANISOU  959  CE  MSE A1116    13079  12702  17470     14    103  -1714       C  
ATOM    960  N   ARG A1117      19.852  45.996  51.242  1.00109.59           N  
ANISOU  960  N   ARG A1117    12318  12460  16860   1105    621  -1456       N  
ATOM    961  CA  ARG A1117      20.730  46.985  50.597  1.00110.24           C  
ANISOU  961  CA  ARG A1117    12317  12652  16916   1281    723  -1406       C  
ATOM    962  C   ARG A1117      19.960  47.917  49.656  1.00110.30           C  
ANISOU  962  C   ARG A1117    12283  12725  16900   1216    611  -1433       C  
ATOM    963  O   ARG A1117      20.331  49.090  49.498  1.00109.99           O  
ANISOU  963  O   ARG A1117    12083  12812  16896   1282    667  -1382       O  
ATOM    964  CB  ARG A1117      21.832  46.292  49.778  1.00112.62           C  
ANISOU  964  CB  ARG A1117    12880  12857  17055   1499    843  -1410       C  
ATOM    965  CG  ARG A1117      23.070  45.819  50.534  1.00112.38           C  
ANISOU  965  CG  ARG A1117    12824  12834  17040   1675   1004  -1355       C  
ATOM    966  CD  ARG A1117      23.990  45.076  49.568  1.00113.96           C  
ANISOU  966  CD  ARG A1117    13305  12936  17060   1902   1113  -1373       C  
ATOM    967  NE  ARG A1117      25.235  44.614  50.181  1.00114.07           N  
ANISOU  967  NE  ARG A1117    13288  12978  17076   2113   1266  -1322       N  
ATOM    968  CZ  ARG A1117      26.065  43.725  49.632  1.00116.64           C  
ANISOU  968  CZ  ARG A1117    13860  13206  17251   2340   1371  -1336       C  
ATOM    969  NH1 ARG A1117      25.796  43.179  48.450  1.00119.03           N  
ANISOU  969  NH1 ARG A1117    14490  13357  17378   2376   1346  -1401       N  
ATOM    970  NH2 ARG A1117      27.170  43.371  50.276  1.00117.29           N  
ANISOU  970  NH2 ARG A1117    13869  13345  17351   2544   1499  -1287       N  
ATOM    971  N   LYS A1118      18.907  47.385  49.027  1.00109.74           N  
ANISOU  971  N   LYS A1118    12374  12564  16759   1085    447  -1512       N  
ATOM    972  CA  LYS A1118      18.090  48.147  48.076  1.00109.81           C  
ANISOU  972  CA  LYS A1118    12371  12623  16727   1032    307  -1546       C  
ATOM    973  C   LYS A1118      17.517  49.433  48.684  1.00108.13           C  
ANISOU  973  C   LYS A1118    11826  12588  16670    966    263  -1507       C  
ATOM    974  O   LYS A1118      17.497  50.487  48.033  1.00108.21           O  
ANISOU  974  O   LYS A1118    11791  12673  16650   1032    242  -1490       O  
ATOM    975  CB  LYS A1118      16.941  47.292  47.531  1.00110.60           C  
ANISOU  975  CB  LYS A1118    12653  12619  16750    862    112  -1639       C  
ATOM    976  CG  LYS A1118      16.420  47.775  46.188  1.00110.66           C  
ANISOU  976  CG  LYS A1118    12780  12626  16638    874    -25  -1682       C  
ATOM    977  CD  LYS A1118      14.901  47.776  46.119  1.00111.05           C  
ANISOU  977  CD  LYS A1118    12732  12730  16733    657   -263  -1748       C  
ATOM    978  CE  LYS A1118      14.433  48.325  44.771  1.00111.83           C  
ANISOU  978  CE  LYS A1118    12951  12835  16703    696   -414  -1787       C  
ATOM    979  NZ  LYS A1118      13.035  48.843  44.797  1.00110.84           N  
ANISOU  979  NZ  LYS A1118    12604  12848  16661    544   -637  -1827       N  
ATOM    980  N   ILE A1119      17.067  49.331  49.933  1.00105.42           N  
ANISOU  980  N   ILE A1119    11280  12297  16477    842    255  -1494       N  
ATOM    981  CA  ILE A1119      16.356  50.417  50.607  1.00103.26           C  
ANISOU  981  CA  ILE A1119    10707  12178  16348    768    206  -1467       C  
ATOM    982  C   ILE A1119      17.291  51.529  51.105  1.00101.80           C  
ANISOU  982  C   ILE A1119    10362  12091  16225    893    355  -1377       C  
ATOM    983  O   ILE A1119      16.952  52.721  51.008  1.00100.70           O  
ANISOU  983  O   ILE A1119    10084  12057  16122    911    320  -1353       O  
ATOM    984  CB  ILE A1119      15.510  49.879  51.783  1.00101.53           C  
ANISOU  984  CB  ILE A1119    10342  11978  16258    579    159  -1487       C  
ATOM    985  CG1 ILE A1119      14.896  48.528  51.420  1.00103.57           C  
ANISOU  985  CG1 ILE A1119    10810  12106  16435    437     54  -1569       C  
ATOM    986  CG2 ILE A1119      14.407  50.858  52.122  1.00100.51           C  
ANISOU  986  CG2 ILE A1119     9943  12004  16243    494     59  -1490       C  
ATOM    987  CD1 ILE A1119      14.892  47.522  52.544  1.00104.20           C  
ANISOU  987  CD1 ILE A1119    10913  12107  16570    317    111  -1570       C  
ATOM    988  N   VAL A1120      18.457  51.122  51.618  1.00100.35           N  
ANISOU  988  N   VAL A1120    10212  11872  16043    980    512  -1329       N  
ATOM    989  CA  VAL A1120      19.426  52.011  52.278  1.00 99.53           C  
ANISOU  989  CA  VAL A1120     9945  11865  16005   1066    655  -1242       C  
ATOM    990  C   VAL A1120      20.033  53.041  51.315  1.00100.00           C  
ANISOU  990  C   VAL A1120    10039  11978  15977   1181    711  -1210       C  
ATOM    991  O   VAL A1120      20.436  54.136  51.722  1.00 98.70           O  
ANISOU  991  O   VAL A1120     9727  11912  15865   1200    781  -1146       O  
ATOM    992  CB  VAL A1120      20.534  51.188  52.980  1.00 99.70           C  
ANISOU  992  CB  VAL A1120    10001  11843  16036   1140    790  -1206       C  
ATOM    993  CG1 VAL A1120      21.687  52.068  53.475  1.00 98.10           C  
ANISOU  993  CG1 VAL A1120     9641  11753  15878   1232    933  -1118       C  
ATOM    994  CG2 VAL A1120      19.934  50.380  54.124  1.00 99.81           C  
ANISOU  994  CG2 VAL A1120     9973  11807  16143   1012    745  -1224       C  
ATOM    995  N   SER A1121      20.091  52.685  50.038  1.00101.39           N  
ANISOU  995  N   SER A1121    10439  12077  16007   1248    683  -1254       N  
ATOM    996  CA  SER A1121      20.517  53.623  49.011  1.00102.60           C  
ANISOU  996  CA  SER A1121    10667  12262  16054   1340    726  -1233       C  
ATOM    997  C   SER A1121      19.425  54.673  48.777  1.00102.09           C  
ANISOU  997  C   SER A1121    10528  12252  16011   1277    581  -1246       C  
ATOM    998  O   SER A1121      19.649  55.868  48.989  1.00100.43           O  
ANISOU  998  O   SER A1121    10209  12123  15826   1296    630  -1191       O  
ATOM    999  CB  SER A1121      20.874  52.881  47.714  1.00104.35           C  
ANISOU  999  CB  SER A1121    11178  12370  16099   1435    742  -1280       C  
ATOM   1000  OG  SER A1121      21.925  51.948  47.939  1.00106.05           O  
ANISOU 1000  OG  SER A1121    11462  12542  16288   1530    887  -1265       O  
ATOM   1001  N   ALA A1122      18.241  54.206  48.377  1.00103.87           N  
ANISOU 1001  N   ALA A1122    10813  12433  16218   1201    397  -1321       N  
ATOM   1002  CA  ALA A1122      17.092  55.068  48.042  1.00103.62           C  
ANISOU 1002  CA  ALA A1122    10716  12462  16194   1166    229  -1346       C  
ATOM   1003  C   ALA A1122      16.684  56.067  49.144  1.00101.43           C  
ANISOU 1003  C   ALA A1122    10172  12304  16064   1127    232  -1299       C  
ATOM   1004  O   ALA A1122      16.355  57.221  48.845  1.00 98.97           O  
ANISOU 1004  O   ALA A1122     9832  12045  15726   1178    185  -1280       O  
ATOM   1005  CB  ALA A1122      15.899  54.212  47.638  1.00103.90           C  
ANISOU 1005  CB  ALA A1122    10810  12456  16212   1063     29  -1436       C  
ATOM   1006  N   LEU A1123      16.716  55.610  50.400  1.00 99.55           N  
ANISOU 1006  N   LEU A1123     9770  12092  15962   1045    291  -1280       N  
ATOM   1007  CA  LEU A1123      16.243  56.393  51.548  1.00 97.23           C  
ANISOU 1007  CA  LEU A1123     9238  11898  15808    996    295  -1242       C  
ATOM   1008  C   LEU A1123      17.209  57.477  51.970  1.00 96.06           C  
ANISOU 1008  C   LEU A1123     9041  11791  15666   1066    441  -1156       C  
ATOM   1009  O   LEU A1123      16.790  58.586  52.300  1.00 96.69           O  
ANISOU 1009  O   LEU A1123     9022  11936  15780   1079    418  -1127       O  
ATOM   1010  CB  LEU A1123      15.999  55.489  52.757  1.00 96.28           C  
ANISOU 1010  CB  LEU A1123     8994  11775  15814    876    319  -1251       C  
ATOM   1011  CG  LEU A1123      14.742  54.627  52.877  1.00 97.30           C  
ANISOU 1011  CG  LEU A1123     9075  11905  15992    736    177  -1328       C  
ATOM   1012  CD1 LEU A1123      14.836  53.853  54.182  1.00 95.93           C  
ANISOU 1012  CD1 LEU A1123     8815  11708  15925    628    257  -1315       C  
ATOM   1013  CD2 LEU A1123      13.448  55.439  52.812  1.00 96.80           C  
ANISOU 1013  CD2 LEU A1123     8843  11957  15977    711     35  -1357       C  
ATOM   1014  N   ILE A1124      18.495  57.139  51.989  1.00 94.67           N  
ANISOU 1014  N   ILE A1124     8936  11581  15453   1109    590  -1115       N  
ATOM   1015  CA  ILE A1124      19.541  58.043  52.452  1.00 93.48           C  
ANISOU 1015  CA  ILE A1124     8727  11482  15310   1143    736  -1032       C  
ATOM   1016  C   ILE A1124      20.009  59.040  51.363  1.00 94.37           C  
ANISOU 1016  C   ILE A1124     8977  11595  15284   1221    774  -1008       C  
ATOM   1017  O   ILE A1124      20.528  60.121  51.696  1.00 94.19           O  
ANISOU 1017  O   ILE A1124     8910  11620  15258   1218    856   -943       O  
ATOM   1018  CB  ILE A1124      20.681  57.228  53.120  1.00 93.94           C  
ANISOU 1018  CB  ILE A1124     8751  11535  15408   1149    872   -997       C  
ATOM   1019  CG1 ILE A1124      20.235  56.820  54.535  1.00 93.48           C  
ANISOU 1019  CG1 ILE A1124     8535  11490  15494   1057    851   -991       C  
ATOM   1020  CG2 ILE A1124      22.024  57.970  53.122  1.00 93.29           C  
ANISOU 1020  CG2 ILE A1124     8649  11512  15283   1196   1028   -921       C  
ATOM   1021  CD1 ILE A1124      21.061  55.719  55.183  1.00 95.05           C  
ANISOU 1021  CD1 ILE A1124     8733  11655  15725   1069    935   -978       C  
ATOM   1022  N   SER A1125      19.792  58.700  50.083  1.00 94.14           N  
ANISOU 1022  N   SER A1125     9135  11503  15130   1277    709  -1060       N  
ATOM   1023  CA  SER A1125      20.044  59.635  48.959  1.00 94.33           C  
ANISOU 1023  CA  SER A1125     9330  11508  15003   1347    725  -1046       C  
ATOM   1024  C   SER A1125      18.982  60.758  48.869  1.00 93.13           C  
ANISOU 1024  C   SER A1125     9166  11376  14841   1355    588  -1052       C  
ATOM   1025  O   SER A1125      18.935  61.532  47.898  1.00 91.73           O  
ANISOU 1025  O   SER A1125     9162  11165  14526   1419    559  -1050       O  
ATOM   1026  CB  SER A1125      20.188  58.889  47.612  1.00 97.15           C  
ANISOU 1026  CB  SER A1125     9923  11778  15212   1413    704  -1100       C  
ATOM   1027  OG  SER A1125      19.157  57.929  47.401  1.00 99.72           O  
ANISOU 1027  OG  SER A1125    10279  12055  15555   1382    536  -1180       O  
ATOM   1028  N   VAL A1126      18.142  60.823  49.903  1.00 91.63           N  
ANISOU 1028  N   VAL A1126     8781  11240  14792   1301    511  -1057       N  
ATOM   1029  CA  VAL A1126      17.113  61.837  50.043  1.00 91.28           C  
ANISOU 1029  CA  VAL A1126     8685  11236  14763   1330    392  -1060       C  
ATOM   1030  C   VAL A1126      17.595  62.922  50.997  1.00 90.54           C  
ANISOU 1030  C   VAL A1126     8511  11179  14712   1314    507   -980       C  
ATOM   1031  O   VAL A1126      17.193  64.078  50.866  1.00 91.70           O  
ANISOU 1031  O   VAL A1126     8713  11327  14801   1372    464   -960       O  
ATOM   1032  CB  VAL A1126      15.776  61.216  50.516  1.00 90.76           C  
ANISOU 1032  CB  VAL A1126     8449  11220  14814   1282    235  -1123       C  
ATOM   1033  CG1 VAL A1126      14.768  62.278  50.924  1.00 91.53           C  
ANISOU 1033  CG1 VAL A1126     8436  11388  14953   1330    141  -1118       C  
ATOM   1034  CG2 VAL A1126      15.184  60.354  49.411  1.00 92.28           C  
ANISOU 1034  CG2 VAL A1126     8758  11373  14932   1287     87  -1204       C  
ATOM   1035  N   ILE A1127      18.474  62.562  51.936  1.00 89.87           N  
ANISOU 1035  N   ILE A1127     8319  11114  14713   1241    645   -935       N  
ATOM   1036  CA  ILE A1127      18.950  63.527  52.954  1.00 89.43           C  
ANISOU 1036  CA  ILE A1127     8187  11092  14700   1200    746   -860       C  
ATOM   1037  C   ILE A1127      19.502  64.819  52.324  1.00 90.53           C  
ANISOU 1037  C   ILE A1127     8502  11203  14693   1235    806   -811       C  
ATOM   1038  O   ILE A1127      19.038  65.919  52.677  1.00 90.14           O  
ANISOU 1038  O   ILE A1127     8475  11149  14625   1255    776   -784       O  
ATOM   1039  CB  ILE A1127      19.971  62.928  53.975  1.00 87.52           C  
ANISOU 1039  CB  ILE A1127     7820  10880  14553   1118    879   -816       C  
ATOM   1040  CG1 ILE A1127      19.464  61.605  54.579  1.00 86.36           C  
ANISOU 1040  CG1 ILE A1127     7550  10736  14529   1080    828   -864       C  
ATOM   1041  CG2 ILE A1127      20.303  63.956  55.062  1.00 85.11           C  
ANISOU 1041  CG2 ILE A1127     7446  10604  14287   1061    952   -744       C  
ATOM   1042  CD1 ILE A1127      20.474  60.868  55.440  1.00 84.81           C  
ANISOU 1042  CD1 ILE A1127     7269  10553  14403   1031    940   -828       C  
ATOM   1043  N   PRO A1128      20.459  64.694  51.369  1.00 91.90           N  
ANISOU 1043  N   PRO A1128     8819  11349  14748   1245    895   -800       N  
ATOM   1044  CA  PRO A1128      21.079  65.900  50.787  1.00 93.11           C  
ANISOU 1044  CA  PRO A1128     9155  11472  14750   1246    976   -749       C  
ATOM   1045  C   PRO A1128      20.065  66.932  50.266  1.00 93.00           C  
ANISOU 1045  C   PRO A1128     9298  11401  14637   1332    847   -765       C  
ATOM   1046  O   PRO A1128      20.238  68.130  50.473  1.00 92.93           O  
ANISOU 1046  O   PRO A1128     9390  11365  14555   1316    890   -713       O  
ATOM   1047  CB  PRO A1128      21.921  65.345  49.621  1.00 94.03           C  
ANISOU 1047  CB  PRO A1128     9408  11567  14752   1269   1062   -763       C  
ATOM   1048  CG  PRO A1128      22.181  63.919  49.966  1.00 92.88           C  
ANISOU 1048  CG  PRO A1128     9114  11457  14718   1263   1083   -793       C  
ATOM   1049  CD  PRO A1128      20.954  63.463  50.712  1.00 92.41           C  
ANISOU 1049  CD  PRO A1128     8915  11403  14795   1263    929   -838       C  
ATOM   1050  N   GLY A1129      19.011  66.459  49.616  1.00 93.32           N  
ANISOU 1050  N   GLY A1129     9366  11424  14669   1422    683   -837       N  
ATOM   1051  CA  GLY A1129      18.061  67.340  48.967  1.00 95.21           C  
ANISOU 1051  CA  GLY A1129     9759  11618  14800   1536    541   -858       C  
ATOM   1052  C   GLY A1129      17.153  68.051  49.936  1.00 95.80           C  
ANISOU 1052  C   GLY A1129     9713  11729  14958   1574    466   -847       C  
ATOM   1053  O   GLY A1129      16.431  68.968  49.546  1.00 98.60           O  
ANISOU 1053  O   GLY A1129    10197  12050  15216   1691    362   -853       O  
HETATM 1054  N   MSE A1130      17.186  67.638  51.201  1.00 95.13           N  
ANISOU 1054  N   MSE A1130     9395  11709  15042   1491    520   -832       N  
HETATM 1055  CA  MSE A1130      16.288  68.216  52.214  1.00 95.59           C  
ANISOU 1055  CA  MSE A1130     9323  11807  15189   1529    464   -825       C  
HETATM 1056  C   MSE A1130      16.939  69.372  52.930  1.00 95.28           C  
ANISOU 1056  C   MSE A1130     9373  11727  15102   1489    588   -745       C  
HETATM 1057  O   MSE A1130      16.251  70.251  53.454  1.00 96.18           O  
ANISOU 1057  O   MSE A1130     9500  11834  15209   1566    546   -731       O  
HETATM 1058  CB  MSE A1130      15.789  67.135  53.182  1.00 93.56           C  
ANISOU 1058  CB  MSE A1130     8789  11633  15128   1460    443   -859       C  
HETATM 1059  CG  MSE A1130      14.461  66.598  52.648  1.00 93.47           C  
ANISOU 1059  CG  MSE A1130     8689  11675  15149   1536    256   -943       C  
HETATM 1060 SE   MSE A1130      13.812  65.020  53.635  1.00 93.05          SE  
ANISOU 1060 SE   MSE A1130     8324  11713  15317   1406    228   -999      SE  
HETATM 1061  CE  MSE A1130      13.930  65.713  55.486  1.00 90.68           C  
ANISOU 1061  CE  MSE A1130     7875  11441  15138   1356    368   -928       C  
ATOM   1062  N   LEU A1131      18.271  69.376  52.942  1.00 94.79           N  
ANISOU 1062  N   LEU A1131     9376  11642  14999   1371    740   -693       N  
ATOM   1063  CA  LEU A1131      19.068  70.446  53.550  1.00 94.43           C  
ANISOU 1063  CA  LEU A1131     9432  11557  14889   1287    863   -613       C  
ATOM   1064  C   LEU A1131      18.597  71.852  53.168  1.00 95.95           C  
ANISOU 1064  C   LEU A1131     9879  11660  14918   1386    816   -593       C  
ATOM   1065  O   LEU A1131      18.831  72.807  53.919  1.00 96.51           O  
ANISOU 1065  O   LEU A1131    10031  11688  14950   1339    880   -537       O  
ATOM   1066  CB  LEU A1131      20.550  70.283  53.188  1.00 92.86           C  
ANISOU 1066  CB  LEU A1131     9290  11363  14629   1157   1016   -570       C  
ATOM   1067  CG  LEU A1131      21.281  69.061  53.742  1.00 91.39           C  
ANISOU 1067  CG  LEU A1131     8875  11263  14586   1065   1091   -570       C  
ATOM   1068  CD1 LEU A1131      22.563  68.843  52.952  1.00 93.40           C  
ANISOU 1068  CD1 LEU A1131     9201  11537  14752   1000   1221   -547       C  
ATOM   1069  CD2 LEU A1131      21.591  69.219  55.225  1.00 89.61           C  
ANISOU 1069  CD2 LEU A1131     8498  11075  14474    962   1148   -521       C  
ATOM   1070  N   SER A1132      17.934  71.965  52.012  1.00 95.67           N  
ANISOU 1070  N   SER A1132     9989  11587  14776   1526    699   -639       N  
ATOM   1071  CA  SER A1132      17.402  73.243  51.519  1.00 96.87           C  
ANISOU 1071  CA  SER A1132    10413  11641  14751   1659    631   -627       C  
ATOM   1072  C   SER A1132      16.581  74.009  52.565  1.00 96.79           C  
ANISOU 1072  C   SER A1132    10360  11629  14785   1746    589   -611       C  
ATOM   1073  O   SER A1132      16.369  75.211  52.440  1.00 98.04           O  
ANISOU 1073  O   SER A1132    10773  11689  14789   1839    574   -582       O  
ATOM   1074  CB  SER A1132      16.556  73.026  50.260  1.00 97.57           C  
ANISOU 1074  CB  SER A1132    10600  11716  14757   1826    464   -693       C  
ATOM   1075  OG  SER A1132      17.341  72.533  49.192  1.00 96.83           O  
ANISOU 1075  OG  SER A1132    10629  11590  14572   1762    516   -702       O  
ATOM   1076  N   VAL A1133      16.119  73.307  53.592  1.00 95.62           N  
ANISOU 1076  N   VAL A1133     9914  11581  14836   1722    577   -632       N  
ATOM   1077  CA  VAL A1133      15.350  73.929  54.656  1.00 96.07           C  
ANISOU 1077  CA  VAL A1133     9909  11647  14946   1804    559   -620       C  
ATOM   1078  C   VAL A1133      15.723  73.397  56.039  1.00 94.63           C  
ANISOU 1078  C   VAL A1133     9498  11522  14934   1652    663   -594       C  
ATOM   1079  O   VAL A1133      15.255  73.920  57.056  1.00 92.71           O  
ANISOU 1079  O   VAL A1133     9221  11275  14730   1691    683   -574       O  
ATOM   1080  CB  VAL A1133      13.840  73.769  54.424  1.00 97.65           C  
ANISOU 1080  CB  VAL A1133     9978  11926  15198   2012    386   -689       C  
ATOM   1081  CG1 VAL A1133      13.305  74.936  53.606  1.00 99.85           C  
ANISOU 1081  CG1 VAL A1133    10543  12119  15278   2222    288   -689       C  
ATOM   1082  CG2 VAL A1133      13.544  72.426  53.762  1.00 97.58           C  
ANISOU 1082  CG2 VAL A1133     9772  12014  15292   1984    294   -760       C  
ATOM   1083  N   ILE A1134      16.563  72.361  56.071  1.00 93.77           N  
ANISOU 1083  N   ILE A1134     9254  11460  14916   1493    731   -594       N  
ATOM   1084  CA  ILE A1134      17.046  71.822  57.340  1.00 93.10           C  
ANISOU 1084  CA  ILE A1134     8980  11419  14975   1348    825   -566       C  
ATOM   1085  C   ILE A1134      18.058  72.795  57.925  1.00 93.70           C  
ANISOU 1085  C   ILE A1134     9222  11420  14959   1230    946   -483       C  
ATOM   1086  O   ILE A1134      18.079  73.034  59.145  1.00 93.87           O  
ANISOU 1086  O   ILE A1134     9188  11437  15042   1171    996   -450       O  
ATOM   1087  CB  ILE A1134      17.644  70.398  57.202  1.00 91.73           C  
ANISOU 1087  CB  ILE A1134     8628  11313  14914   1241    852   -591       C  
ATOM   1088  CG1 ILE A1134      16.532  69.354  56.982  1.00 92.35           C  
ANISOU 1088  CG1 ILE A1134     8520  11462  15106   1316    733   -673       C  
ATOM   1089  CG2 ILE A1134      18.454  70.024  58.439  1.00 90.48           C  
ANISOU 1089  CG2 ILE A1134     8342  11179  14859   1088    960   -545       C  
ATOM   1090  CD1 ILE A1134      15.463  69.302  58.070  1.00 90.78           C  
ANISOU 1090  CD1 ILE A1134     8144  11316  15032   1350    699   -692       C  
ATOM   1091  N   ALA A1135      18.878  73.364  57.040  1.00 93.54           N  
ANISOU 1091  N   ALA A1135     9420  11340  14781   1184    992   -452       N  
ATOM   1092  CA  ALA A1135      19.810  74.424  57.401  1.00 92.47           C  
ANISOU 1092  CA  ALA A1135     9485  11128  14520   1052   1098   -376       C  
ATOM   1093  C   ALA A1135      19.036  75.630  57.924  1.00 92.40           C  
ANISOU 1093  C   ALA A1135     9664  11022  14422   1157   1064   -357       C  
ATOM   1094  O   ALA A1135      19.539  76.376  58.762  1.00 92.69           O  
ANISOU 1094  O   ALA A1135     9813  10998  14408   1044   1139   -298       O  
ATOM   1095  CB  ALA A1135      20.670  74.804  56.203  1.00 93.34           C  
ANISOU 1095  CB  ALA A1135     9807  11194  14463    991   1152   -356       C  
ATOM   1096  N   LEU A1136      17.812  75.800  57.427  1.00 92.45           N  
ANISOU 1096  N   LEU A1136     9705  11017  14406   1378    946   -408       N  
ATOM   1097  CA  LEU A1136      16.862  76.775  57.966  1.00 94.28           C  
ANISOU 1097  CA  LEU A1136    10063  11181  14578   1540    902   -402       C  
ATOM   1098  C   LEU A1136      16.202  76.260  59.252  1.00 94.94           C  
ANISOU 1098  C   LEU A1136     9880  11346  14848   1560    905   -419       C  
ATOM   1099  O   LEU A1136      15.990  77.022  60.204  1.00 93.86           O  
ANISOU 1099  O   LEU A1136     9838  11147  14678   1583    948   -385       O  
ATOM   1100  CB  LEU A1136      15.791  77.103  56.918  1.00 95.65           C  
ANISOU 1100  CB  LEU A1136    10344  11338  14659   1793    764   -454       C  
ATOM   1101  CG  LEU A1136      14.637  78.070  57.222  1.00 96.38           C  
ANISOU 1101  CG  LEU A1136    10560  11382  14677   2038    692   -462       C  
ATOM   1102  CD1 LEU A1136      15.123  79.391  57.810  1.00 95.87           C  
ANISOU 1102  CD1 LEU A1136    10831  11154  14441   1998    786   -389       C  
ATOM   1103  CD2 LEU A1136      13.797  78.302  55.971  1.00 97.41           C  
ANISOU 1103  CD2 LEU A1136    10802  11508  14701   2275    541   -511       C  
HETATM 1104  N   MSE A1137      15.880  74.965  59.273  1.00 96.12           N  
ANISOU 1104  N   MSE A1137     9720  11623  15178   1544    865   -472       N  
HETATM 1105  CA  MSE A1137      15.225  74.349  60.432  1.00 95.96           C  
ANISOU 1105  CA  MSE A1137     9443  11684  15335   1545    874   -493       C  
HETATM 1106  C   MSE A1137      16.087  74.567  61.635  1.00 95.08           C  
ANISOU 1106  C   MSE A1137     9363  11524  15241   1371    994   -428       C  
HETATM 1107  O   MSE A1137      15.615  75.125  62.636  1.00 98.34           O  
ANISOU 1107  O   MSE A1137     9807  11901  15657   1417   1027   -409       O  
HETATM 1108  CB  MSE A1137      14.944  72.859  60.242  1.00 94.88           C  
ANISOU 1108  CB  MSE A1137     9011  11670  15369   1503    826   -554       C  
HETATM 1109  CG  MSE A1137      13.683  72.689  59.402  1.00 97.74           C  
ANISOU 1109  CG  MSE A1137     9293  12104  15740   1692    684   -627       C  
HETATM 1110 SE   MSE A1137      12.537  71.264  60.120  1.00 98.73          SE  
ANISOU 1110 SE   MSE A1137     9011  12394  16108   1670    638   -703      SE  
HETATM 1111  CE  MSE A1137      11.862  72.243  61.693  1.00 97.12           C  
ANISOU 1111  CE  MSE A1137     8796  12177  15927   1754    727   -666       C  
ATOM   1112  N   THR A1138      17.354  74.161  61.531  1.00 91.23           N  
ANISOU 1112  N   THR A1138     8874  11037  14754   1180   1057   -394       N  
ATOM   1113  CA  THR A1138      18.311  74.289  62.624  1.00 89.29           C  
ANISOU 1113  CA  THR A1138     8639  10762  14524    994   1154   -331       C  
ATOM   1114  C   THR A1138      18.422  75.756  63.032  1.00 89.79           C  
ANISOU 1114  C   THR A1138     8998  10697  14422    992   1194   -275       C  
ATOM   1115  O   THR A1138      18.498  76.073  64.235  1.00 87.29           O  
ANISOU 1115  O   THR A1138     8706  10338  14120    926   1243   -239       O  
ATOM   1116  CB  THR A1138      19.688  73.684  62.235  1.00 89.32           C  
ANISOU 1116  CB  THR A1138     8589  10813  14538    815   1206   -305       C  
ATOM   1117  OG1 THR A1138      19.528  72.292  61.916  1.00 88.02           O  
ANISOU 1117  OG1 THR A1138     8183  10747  14515    836   1170   -360       O  
ATOM   1118  CG2 THR A1138      20.738  73.835  63.355  1.00 87.11           C  
ANISOU 1118  CG2 THR A1138     8305  10524  14270    617   1287   -239       C  
ATOM   1119  N   LEU A1139      18.384  76.641  62.032  1.00 90.90           N  
ANISOU 1119  N   LEU A1139     9387  10759  14390   1071   1169   -269       N  
ATOM   1120  CA  LEU A1139      18.506  78.083  62.282  1.00 94.85           C  
ANISOU 1120  CA  LEU A1139    10233  11109  14697   1071   1204   -216       C  
ATOM   1121  C   LEU A1139      17.403  78.659  63.194  1.00 95.65           C  
ANISOU 1121  C   LEU A1139    10390  11156  14797   1244   1190   -223       C  
ATOM   1122  O   LEU A1139      17.701  79.354  64.169  1.00 95.74           O  
ANISOU 1122  O   LEU A1139    10563  11073  14741   1159   1253   -173       O  
ATOM   1123  CB  LEU A1139      18.588  78.870  60.973  1.00 97.26           C  
ANISOU 1123  CB  LEU A1139    10822  11328  14805   1141   1175   -214       C  
ATOM   1124  CG  LEU A1139      18.605  80.402  61.061  1.00 99.98           C  
ANISOU 1124  CG  LEU A1139    11586  11488  14913   1166   1201   -165       C  
ATOM   1125  CD1 LEU A1139      19.951  80.911  61.563  1.00100.66           C  
ANISOU 1125  CD1 LEU A1139    11829  11510  14907    865   1305    -90       C  
ATOM   1126  CD2 LEU A1139      18.273  81.018  59.707  1.00102.86           C  
ANISOU 1126  CD2 LEU A1139    12212  11772  15098   1321   1141   -183       C  
ATOM   1127  N   PHE A1140      16.145  78.364  62.872  1.00 96.05           N  
ANISOU 1127  N   PHE A1140    10305  11273  14916   1483   1109   -286       N  
ATOM   1128  CA  PHE A1140      14.997  78.859  63.643  1.00 95.75           C  
ANISOU 1128  CA  PHE A1140    10280  11215  14884   1684   1102   -301       C  
ATOM   1129  C   PHE A1140      15.062  78.428  65.111  1.00 95.28           C  
ANISOU 1129  C   PHE A1140    10063  11183  14956   1570   1183   -283       C  
ATOM   1130  O   PHE A1140      14.785  79.237  66.009  1.00 95.95           O  
ANISOU 1130  O   PHE A1140    10319  11173  14966   1625   1236   -253       O  
ATOM   1131  CB  PHE A1140      13.682  78.412  62.997  1.00 95.43           C  
ANISOU 1131  CB  PHE A1140    10037  11296  14926   1934    994   -378       C  
ATOM   1132  CG  PHE A1140      12.453  78.859  63.741  1.00 95.79           C  
ANISOU 1132  CG  PHE A1140    10045  11362  14991   2162    994   -399       C  
ATOM   1133  CD1 PHE A1140      12.242  80.208  64.033  1.00 96.61           C  
ANISOU 1133  CD1 PHE A1140    10485  11316  14906   2309   1024   -361       C  
ATOM   1134  CD2 PHE A1140      11.496  77.933  64.143  1.00 94.60           C  
ANISOU 1134  CD2 PHE A1140     9530  11379  15036   2231    972   -458       C  
ATOM   1135  CE1 PHE A1140      11.108  80.623  64.714  1.00 95.59           C  
ANISOU 1135  CE1 PHE A1140    10320  11214  14788   2548   1037   -381       C  
ATOM   1136  CE2 PHE A1140      10.365  78.347  64.825  1.00 94.51           C  
ANISOU 1136  CE2 PHE A1140     9459  11408  15042   2444    989   -478       C  
ATOM   1137  CZ  PHE A1140      10.170  79.693  65.107  1.00 94.87           C  
ANISOU 1137  CZ  PHE A1140     9830  11311  14903   2618   1024   -440       C  
ATOM   1138  N   PHE A1141      15.423  77.165  65.350  1.00 93.71           N  
ANISOU 1138  N   PHE A1141     9569  11099  14936   1420   1192   -302       N  
ATOM   1139  CA  PHE A1141      15.769  76.704  66.701  1.00 92.76           C  
ANISOU 1139  CA  PHE A1141     9338  10986  14921   1267   1268   -276       C  
ATOM   1140  C   PHE A1141      16.818  77.651  67.270  1.00 93.25           C  
ANISOU 1140  C   PHE A1141     9687  10908  14834   1102   1333   -197       C  
ATOM   1141  O   PHE A1141      16.525  78.455  68.162  1.00 91.76           O  
ANISOU 1141  O   PHE A1141     9681  10619  14567   1143   1380   -168       O  
ATOM   1142  CB  PHE A1141      16.351  75.285  66.674  1.00 89.55           C  
ANISOU 1142  CB  PHE A1141     8652  10693  14681   1106   1263   -295       C  
ATOM   1143  CG  PHE A1141      15.329  74.213  66.510  1.00 87.54           C  
ANISOU 1143  CG  PHE A1141     8108  10566  14588   1208   1215   -369       C  
ATOM   1144  CD1 PHE A1141      14.898  73.836  65.246  1.00 86.60           C  
ANISOU 1144  CD1 PHE A1141     7907  10517  14479   1310   1126   -423       C  
ATOM   1145  CD2 PHE A1141      14.799  73.572  67.628  1.00 86.96           C  
ANISOU 1145  CD2 PHE A1141     7858  10536  14647   1183   1259   -386       C  
ATOM   1146  CE1 PHE A1141      13.950  72.841  65.096  1.00 86.63           C  
ANISOU 1146  CE1 PHE A1141     7648  10642  14625   1374   1072   -493       C  
ATOM   1147  CE2 PHE A1141      13.849  72.572  67.490  1.00 87.03           C  
ANISOU 1147  CE2 PHE A1141     7603  10665  14798   1243   1220   -455       C  
ATOM   1148  CZ  PHE A1141      13.427  72.203  66.217  1.00 86.74           C  
ANISOU 1148  CZ  PHE A1141     7478  10707  14774   1331   1122   -509       C  
ATOM   1149  N   TYR A1142      18.024  77.570  66.696  1.00 93.94           N  
ANISOU 1149  N   TYR A1142     9822  10996  14874    917   1336   -165       N  
ATOM   1150  CA  TYR A1142      19.199  78.326  67.157  1.00 95.63           C  
ANISOU 1150  CA  TYR A1142    10264  11112  14959    698   1390    -90       C  
ATOM   1151  C   TYR A1142      18.859  79.768  67.570  1.00 96.25           C  
ANISOU 1151  C   TYR A1142    10713  11015  14841    766   1416    -54       C  
ATOM   1152  O   TYR A1142      19.250  80.214  68.652  1.00 94.42           O  
ANISOU 1152  O   TYR A1142    10617  10700  14560    639   1462     -7       O  
ATOM   1153  CB  TYR A1142      20.301  78.320  66.083  1.00 95.53           C  
ANISOU 1153  CB  TYR A1142    10292  11129  14876    551   1390    -70       C  
ATOM   1154  CG  TYR A1142      21.704  78.103  66.622  1.00 95.39           C  
ANISOU 1154  CG  TYR A1142    10221  11149  14872    269   1435    -15       C  
ATOM   1155  CD1 TYR A1142      22.493  77.034  66.163  1.00 94.04           C  
ANISOU 1155  CD1 TYR A1142     9791  11122  14816    171   1436    -25       C  
ATOM   1156  CD2 TYR A1142      22.249  78.960  67.593  1.00 95.19           C  
ANISOU 1156  CD2 TYR A1142    10407  11022  14738    105   1471     47       C  
ATOM   1157  CE1 TYR A1142      23.788  76.835  66.641  1.00 93.42           C  
ANISOU 1157  CE1 TYR A1142     9638  11107  14753    -65   1470     25       C  
ATOM   1158  CE2 TYR A1142      23.539  78.760  68.082  1.00 94.44           C  
ANISOU 1158  CE2 TYR A1142    10239  10986  14657   -158   1494     97       C  
ATOM   1159  CZ  TYR A1142      24.305  77.703  67.609  1.00 93.87           C  
ANISOU 1159  CZ  TYR A1142     9881  11079  14709   -236   1493     86       C  
ATOM   1160  OH  TYR A1142      25.577  77.518  68.117  1.00 92.71           O  
ANISOU 1160  OH  TYR A1142     9638  11012  14576   -475   1508    135       O  
ATOM   1161  N   ILE A1143      18.123  80.467  66.697  1.00 96.93           N  
ANISOU 1161  N   ILE A1143    10980  11041  14809    976   1379    -78       N  
ATOM   1162  CA  ILE A1143      17.654  81.829  66.945  1.00 97.21           C  
ANISOU 1162  CA  ILE A1143    11396  10899  14641   1103   1396    -52       C  
ATOM   1163  C   ILE A1143      16.748  81.850  68.161  1.00 97.25           C  
ANISOU 1163  C   ILE A1143    11350  10890  14711   1242   1430    -63       C  
ATOM   1164  O   ILE A1143      17.049  82.545  69.139  1.00 99.03           O  
ANISOU 1164  O   ILE A1143    11811  10984  14833   1151   1488    -15       O  
ATOM   1165  CB  ILE A1143      16.894  82.420  65.731  1.00 98.48           C  
ANISOU 1165  CB  ILE A1143    11723  11017  14676   1358   1332    -85       C  
ATOM   1166  CG1 ILE A1143      17.861  82.690  64.574  1.00100.18           C  
ANISOU 1166  CG1 ILE A1143    12107  11193  14762   1206   1323    -61       C  
ATOM   1167  CG2 ILE A1143      16.172  83.704  66.113  1.00 99.11           C  
ANISOU 1167  CG2 ILE A1143    12169  10923  14565   1565   1346    -68       C  
ATOM   1168  CD1 ILE A1143      17.191  82.832  63.220  1.00102.60           C  
ANISOU 1168  CD1 ILE A1143    12479  11505  14998   1437   1240   -105       C  
ATOM   1169  N   PHE A1144      15.656  81.084  68.106  1.00 94.52           N  
ANISOU 1169  N   PHE A1144    10703  10681  14531   1446   1399   -128       N  
ATOM   1170  CA  PHE A1144      14.627  81.165  69.150  1.00 93.39           C  
ANISOU 1170  CA  PHE A1144    10506  10538  14440   1616   1445   -146       C  
ATOM   1171  C   PHE A1144      15.012  80.455  70.458  1.00 90.61           C  
ANISOU 1171  C   PHE A1144     9993  10216  14219   1423   1514   -127       C  
ATOM   1172  O   PHE A1144      14.601  80.880  71.532  1.00 89.42           O  
ANISOU 1172  O   PHE A1144     9956   9988  14033   1479   1583   -112       O  
ATOM   1173  CB  PHE A1144      13.257  80.727  68.611  1.00 93.92           C  
ANISOU 1173  CB  PHE A1144    10318  10750  14616   1903   1389   -221       C  
ATOM   1174  CG  PHE A1144      12.458  81.854  68.009  1.00 95.67           C  
ANISOU 1174  CG  PHE A1144    10796  10892  14663   2200   1349   -231       C  
ATOM   1175  CD1 PHE A1144      12.939  82.563  66.914  1.00 95.99           C  
ANISOU 1175  CD1 PHE A1144    11118  10830  14525   2210   1289   -211       C  
ATOM   1176  CD2 PHE A1144      11.218  82.208  68.539  1.00 97.09           C  
ANISOU 1176  CD2 PHE A1144    10942  11101  14848   2483   1375   -261       C  
ATOM   1177  CE1 PHE A1144      12.208  83.606  66.367  1.00 97.56           C  
ANISOU 1177  CE1 PHE A1144    11587  10939  14544   2502   1244   -219       C  
ATOM   1178  CE2 PHE A1144      10.479  83.254  67.998  1.00 98.46           C  
ANISOU 1178  CE2 PHE A1144    11357  11202  14849   2793   1332   -269       C  
ATOM   1179  CZ  PHE A1144      10.977  83.954  66.913  1.00 99.15           C  
ANISOU 1179  CZ  PHE A1144    11751  11171  14752   2806   1260   -248       C  
ATOM   1180  N   ALA A1145      15.815  79.395  70.357  1.00 87.95           N  
ANISOU 1180  N   ALA A1145     9417   9980  14019   1208   1495   -128       N  
ATOM   1181  CA  ALA A1145      16.413  78.769  71.526  1.00 85.85           C  
ANISOU 1181  CA  ALA A1145     9048   9722  13848   1004   1543   -100       C  
ATOM   1182  C   ALA A1145      17.182  79.771  72.392  1.00 86.80           C  
ANISOU 1182  C   ALA A1145     9509   9673  13800    852   1589    -28       C  
ATOM   1183  O   ALA A1145      17.012  79.755  73.621  1.00 87.10           O  
ANISOU 1183  O   ALA A1145     9581   9658  13854    821   1645    -12       O  
ATOM   1184  CB  ALA A1145      17.301  77.610  71.123  1.00 84.41           C  
ANISOU 1184  CB  ALA A1145     8611   9661  13799    817   1505   -106       C  
ATOM   1185  N   ILE A1146      18.004  80.631  71.760  1.00 87.08           N  
ANISOU 1185  N   ILE A1146     9807   9615  13663    745   1568     15       N  
ATOM   1186  CA  ILE A1146      18.641  81.802  72.430  1.00 88.08           C  
ANISOU 1186  CA  ILE A1146    10328   9556  13583    602   1602     82       C  
ATOM   1187  C   ILE A1146      17.633  82.595  73.276  1.00 89.35           C  
ANISOU 1187  C   ILE A1146    10725   9579  13645    805   1659     81       C  
ATOM   1188  O   ILE A1146      17.805  82.733  74.490  1.00 87.82           O  
ANISOU 1188  O   ILE A1146    10638   9303  13425    707   1705    113       O  
ATOM   1189  CB  ILE A1146      19.354  82.781  71.433  1.00 89.16           C  
ANISOU 1189  CB  ILE A1146    10765   9598  13516    508   1580    117       C  
ATOM   1190  CG1 ILE A1146      20.700  82.216  70.951  1.00 88.11           C  
ANISOU 1190  CG1 ILE A1146    10469   9574  13435    223   1555    143       C  
ATOM   1191  CG2 ILE A1146      19.578  84.167  72.060  1.00 89.44           C  
ANISOU 1191  CG2 ILE A1146    11279   9403  13299    439   1616    174       C  
ATOM   1192  CD1 ILE A1146      21.210  82.838  69.666  1.00 87.98           C  
ANISOU 1192  CD1 ILE A1146    10634   9524  13269    169   1542    155       C  
HETATM 1193  N   MSE A1147      16.581  83.095  72.620  1.00 90.97           N  
ANISOU 1193  N   MSE A1147    11009   9765  13791   1101   1653     44       N  
HETATM 1194  CA  MSE A1147      15.542  83.894  73.272  1.00 93.52           C  
ANISOU 1194  CA  MSE A1147    11552   9972  14009   1354   1713     37       C  
HETATM 1195  C   MSE A1147      14.873  83.087  74.361  1.00 92.80           C  
ANISOU 1195  C   MSE A1147    11194   9973  14094   1410   1776      9       C  
HETATM 1196  O   MSE A1147      14.603  83.597  75.448  1.00 93.35           O  
ANISOU 1196  O   MSE A1147    11467   9921  14080   1449   1854     31       O  
HETATM 1197  CB  MSE A1147      14.527  84.335  72.216  1.00 96.54           C  
ANISOU 1197  CB  MSE A1147    11967  10377  14336   1684   1672     -7       C  
HETATM 1198  CG  MSE A1147      15.065  85.412  71.274  1.00100.50           C  
ANISOU 1198  CG  MSE A1147    12863  10724  14599   1664   1629     27       C  
HETATM 1199 SE   MSE A1147      14.747  84.960  69.370  1.00105.83          SE  
ANISOU 1199 SE   MSE A1147    13325  11553  15335   1818   1512    -30      SE  
HETATM 1200  CE  MSE A1147      12.952  85.770  69.204  1.00106.43           C  
ANISOU 1200  CE  MSE A1147    13524  11599  15315   2351   1496    -79       C  
ATOM   1201  N   ALA A1148      14.620  81.809  74.075  1.00 91.44           N  
ANISOU 1201  N   ALA A1148    10585  10005  14154   1402   1747    -40       N  
ATOM   1202  CA  ALA A1148      14.087  80.867  75.052  1.00 89.60           C  
ANISOU 1202  CA  ALA A1148    10076   9869  14099   1403   1809    -67       C  
ATOM   1203  C   ALA A1148      15.182  80.336  75.999  1.00 87.30           C  
ANISOU 1203  C   ALA A1148     9778   9541  13849   1094   1823    -22       C  
ATOM   1204  O   ALA A1148      15.196  79.153  76.353  1.00 85.94           O  
ANISOU 1204  O   ALA A1148     9306   9489  13859   1005   1826    -46       O  
ATOM   1205  CB  ALA A1148      13.363  79.724  74.347  1.00 88.89           C  
ANISOU 1205  CB  ALA A1148     9557   9997  14220   1503   1767   -139       C  
ATOM   1206  N   THR A1149      16.092  81.221  76.406  1.00 86.08           N  
ANISOU 1206  N   THR A1149     9972   9219  13515    930   1823     43       N  
ATOM   1207  CA  THR A1149      17.029  80.915  77.482  1.00 85.15           C  
ANISOU 1207  CA  THR A1149     9899   9051  13405    664   1830     90       C  
ATOM   1208  C   THR A1149      16.999  81.998  78.547  1.00 86.47           C  
ANISOU 1208  C   THR A1149    10475   9006  13375    656   1894    135       C  
ATOM   1209  O   THR A1149      17.004  81.700  79.741  1.00 87.50           O  
ANISOU 1209  O   THR A1149    10622   9092  13531    583   1942    150       O  
ATOM   1210  CB  THR A1149      18.460  80.677  76.958  1.00 84.61           C  
ANISOU 1210  CB  THR A1149     9787   9026  13334    385   1745    128       C  
ATOM   1211  OG1 THR A1149      18.476  79.474  76.162  1.00 84.50           O  
ANISOU 1211  OG1 THR A1149     9383   9206  13518    396   1700     83       O  
ATOM   1212  CG2 THR A1149      19.466  80.528  78.116  1.00 83.25           C  
ANISOU 1212  CG2 THR A1149     9694   8797  13140    116   1733    182       C  
ATOM   1213  N   GLN A1150      16.962  83.255  78.120  1.00 87.57           N  
ANISOU 1213  N   GLN A1150    10974   8998  13302    734   1894    158       N  
ATOM   1214  CA  GLN A1150      16.819  84.355  79.063  1.00 88.54           C  
ANISOU 1214  CA  GLN A1150    11535   8896  13211    763   1960    197       C  
ATOM   1215  C   GLN A1150      15.353  84.534  79.470  1.00 89.29           C  
ANISOU 1215  C   GLN A1150    11633   8979  13315   1114   2064    153       C  
ATOM   1216  O   GLN A1150      15.055  84.762  80.653  1.00 89.23           O  
ANISOU 1216  O   GLN A1150    11798   8861  13247   1140   2152    168       O  
ATOM   1217  CB  GLN A1150      17.444  85.659  78.533  1.00 90.22           C  
ANISOU 1217  CB  GLN A1150    12191   8927  13163    679   1923    243       C  
ATOM   1218  CG  GLN A1150      17.007  86.121  77.141  1.00 91.52           C  
ANISOU 1218  CG  GLN A1150    12390   9113  13269    882   1890    216       C  
ATOM   1219  CD  GLN A1150      17.588  87.484  76.744  1.00 93.30           C  
ANISOU 1219  CD  GLN A1150    13130   9118  13202    791   1871    266       C  
ATOM   1220  OE1 GLN A1150      16.867  88.368  76.271  1.00 94.42           O  
ANISOU 1220  OE1 GLN A1150    13550   9143  13184   1053   1891    254       O  
ATOM   1221  NE2 GLN A1150      18.898  87.653  76.930  1.00 92.94           N  
ANISOU 1221  NE2 GLN A1150    13215   9020  13077    416   1828    321       N  
ATOM   1222  N   LEU A1151      14.448  84.404  78.497  1.00 89.17           N  
ANISOU 1222  N   LEU A1151    11415   9089  13376   1381   2055     99       N  
ATOM   1223  CA  LEU A1151      13.010  84.557  78.752  1.00 91.02           C  
ANISOU 1223  CA  LEU A1151    11591   9360  13632   1736   2149     52       C  
ATOM   1224  C   LEU A1151      12.480  83.617  79.865  1.00 91.58           C  
ANISOU 1224  C   LEU A1151    11393   9528  13876   1728   2246     27       C  
ATOM   1225  O   LEU A1151      11.911  84.085  80.870  1.00 92.25           O  
ANISOU 1225  O   LEU A1151    11673   9507  13872   1855   2364     34       O  
ATOM   1226  CB  LEU A1151      12.177  84.440  77.453  1.00 90.20           C  
ANISOU 1226  CB  LEU A1151    11254   9416  13604   2000   2093     -6       C  
ATOM   1227  CG  LEU A1151      12.193  85.623  76.450  1.00 91.16           C  
ANISOU 1227  CG  LEU A1151    11720   9411  13507   2156   2032      9       C  
ATOM   1228  CD1 LEU A1151      11.246  85.425  75.268  1.00 90.08           C  
ANISOU 1228  CD1 LEU A1151    11329   9445  13454   2445   1969    -53       C  
ATOM   1229  CD2 LEU A1151      11.892  86.958  77.122  1.00 93.36           C  
ANISOU 1229  CD2 LEU A1151    12504   9446  13524   2324   2114     43       C  
ATOM   1230  N   PHE A1152      12.698  82.309  79.705  1.00 90.04           N  
ANISOU 1230  N   PHE A1152    10786   9517  13908   1574   2204      0       N  
ATOM   1231  CA  PHE A1152      12.101  81.329  80.609  1.00 89.71           C  
ANISOU 1231  CA  PHE A1152    10472   9579  14035   1572   2295    -32       C  
ATOM   1232  C   PHE A1152      13.128  80.550  81.420  1.00 89.47           C  
ANISOU 1232  C   PHE A1152    10410   9517  14067   1249   2275      4       C  
ATOM   1233  O   PHE A1152      12.789  79.923  82.437  1.00 90.42           O  
ANISOU 1233  O   PHE A1152    10437   9652  14267   1213   2364     -5       O  
ATOM   1234  CB  PHE A1152      11.220  80.361  79.831  1.00 88.99           C  
ANISOU 1234  CB  PHE A1152     9919   9734  14158   1703   2277   -105       C  
ATOM   1235  CG  PHE A1152      10.416  81.011  78.740  1.00 90.51           C  
ANISOU 1235  CG  PHE A1152    10097   9991  14303   1995   2239   -140       C  
ATOM   1236  CD1 PHE A1152      10.523  80.563  77.424  1.00 89.70           C  
ANISOU 1236  CD1 PHE A1152     9770  10024  14289   1993   2113   -172       C  
ATOM   1237  CD2 PHE A1152       9.553  82.069  79.021  1.00 92.17           C  
ANISOU 1237  CD2 PHE A1152    10533  10121  14368   2287   2324   -143       C  
ATOM   1238  CE1 PHE A1152       9.779  81.152  76.414  1.00 90.54           C  
ANISOU 1238  CE1 PHE A1152     9875  10186  14342   2268   2062   -205       C  
ATOM   1239  CE2 PHE A1152       8.816  82.666  78.015  1.00 93.26           C  
ANISOU 1239  CE2 PHE A1152    10664  10320  14452   2579   2273   -175       C  
ATOM   1240  CZ  PHE A1152       8.928  82.207  76.710  1.00 92.95           C  
ANISOU 1240  CZ  PHE A1152    10397  10415  14503   2565   2136   -206       C  
ATOM   1241  N   GLY A1153      14.383  80.607  80.984  1.00 88.48           N  
ANISOU 1241  N   GLY A1153    10369   9352  13897   1017   2160     46       N  
ATOM   1242  CA  GLY A1153      15.451  79.853  81.626  1.00 87.01           C  
ANISOU 1242  CA  GLY A1153    10126   9164  13772    724   2112     80       C  
ATOM   1243  C   GLY A1153      15.534  80.027  83.131  1.00 87.73           C  
ANISOU 1243  C   GLY A1153    10450   9105  13780    640   2189    115       C  
ATOM   1244  O   GLY A1153      15.614  79.040  83.857  1.00 87.95           O  
ANISOU 1244  O   GLY A1153    10310   9182  13927    535   2208    109       O  
ATOM   1245  N   GLU A1154      15.519  81.267  83.607  1.00 87.76           N  
ANISOU 1245  N   GLU A1154    10867   8912  13564    685   2232    153       N  
ATOM   1246  CA  GLU A1154      15.828  81.520  85.006  1.00 89.44           C  
ANISOU 1246  CA  GLU A1154    11367   8956  13663    560   2282    196       C  
ATOM   1247  C   GLU A1154      14.701  81.006  85.916  1.00 92.40           C  
ANISOU 1247  C   GLU A1154    11637   9352  14118    724   2435    158       C  
ATOM   1248  O   GLU A1154      14.953  80.391  86.974  1.00 91.87           O  
ANISOU 1248  O   GLU A1154    11577   9246  14084    581   2463    173       O  
ATOM   1249  CB  GLU A1154      16.105  83.016  85.241  1.00 89.91           C  
ANISOU 1249  CB  GLU A1154    11940   8780  13443    559   2288    245       C  
ATOM   1250  CG  GLU A1154      16.718  83.348  86.600  1.00 89.37           C  
ANISOU 1250  CG  GLU A1154    12217   8516  13223    361   2296    299       C  
ATOM   1251  CD  GLU A1154      18.175  82.921  86.729  1.00 87.41           C  
ANISOU 1251  CD  GLU A1154    11923   8294  12996      3   2143    345       C  
ATOM   1252  OE1 GLU A1154      18.444  81.883  87.366  1.00 85.62           O  
ANISOU 1252  OE1 GLU A1154    11484   8143  12903   -113   2122    343       O  
ATOM   1253  OE2 GLU A1154      19.056  83.626  86.196  1.00 87.22           O  
ANISOU 1253  OE2 GLU A1154    12076   8217  12847   -163   2044    384       O  
ATOM   1254  N   ARG A1155      13.461  81.266  85.490  1.00 94.43           N  
ANISOU 1254  N   ARG A1155    11799   9678  14402   1025   2534    108       N  
ATOM   1255  CA  ARG A1155      12.267  80.864  86.240  1.00 93.54           C  
ANISOU 1255  CA  ARG A1155    11559   9618  14365   1204   2702     67       C  
ATOM   1256  C   ARG A1155      12.092  79.342  86.128  1.00 90.02           C  
ANISOU 1256  C   ARG A1155    10653   9378  14172   1108   2692     23       C  
ATOM   1257  O   ARG A1155      11.789  78.690  87.120  1.00 88.42           O  
ANISOU 1257  O   ARG A1155    10400   9171  14025   1054   2793     15       O  
ATOM   1258  CB  ARG A1155      11.026  81.644  85.738  1.00 95.14           C  
ANISOU 1258  CB  ARG A1155    11772   9861  14516   1567   2796     27       C  
ATOM   1259  CG  ARG A1155       9.759  81.493  86.582  1.00 97.92           C  
ANISOU 1259  CG  ARG A1155    12040  10260  14905   1779   2997    -11       C  
ATOM   1260  CD  ARG A1155       9.813  82.189  87.953  1.00 99.83           C  
ANISOU 1260  CD  ARG A1155    12720  10262  14947   1776   3125     31       C  
ATOM   1261  NE  ARG A1155       8.714  81.748  88.833  1.00100.61           N  
ANISOU 1261  NE  ARG A1155    12676  10433  15117   1918   3331     -6       N  
ATOM   1262  CZ  ARG A1155       8.313  82.368  89.947  1.00102.95           C  
ANISOU 1262  CZ  ARG A1155    13300  10564  15252   2028   3499     11       C  
ATOM   1263  NH1 ARG A1155       8.914  83.479  90.367  1.00104.02           N  
ANISOU 1263  NH1 ARG A1155    13957  10433  15134   2010   3477     67       N  
ATOM   1264  NH2 ARG A1155       7.296  81.873  90.651  1.00103.89           N  
ANISOU 1264  NH2 ARG A1155    13235  10783  15454   2148   3697    -28       N  
ATOM   1265  N   PHE A1156      12.312  78.810  84.918  1.00 87.66           N  
ANISOU 1265  N   PHE A1156    10061   9241  14004   1082   2572     -4       N  
ATOM   1266  CA  PHE A1156      12.208  77.379  84.608  1.00 85.88           C  
ANISOU 1266  CA  PHE A1156     9424   9203  14004    989   2541    -48       C  
ATOM   1267  C   PHE A1156      13.523  76.897  83.987  1.00 85.09           C  
ANISOU 1267  C   PHE A1156     9259   9125  13944    761   2372    -20       C  
ATOM   1268  O   PHE A1156      13.731  77.073  82.769  1.00 85.58           O  
ANISOU 1268  O   PHE A1156     9226   9266  14024    802   2276    -31       O  
ATOM   1269  CB  PHE A1156      11.064  77.126  83.629  1.00 85.34           C  
ANISOU 1269  CB  PHE A1156     9030   9334  14061   1208   2563   -118       C  
ATOM   1270  CG  PHE A1156       9.694  77.386  84.200  1.00 87.70           C  
ANISOU 1270  CG  PHE A1156     9288   9675  14360   1438   2736   -155       C  
ATOM   1271  CD1 PHE A1156       9.158  78.683  84.221  1.00 89.24           C  
ANISOU 1271  CD1 PHE A1156     9732   9783  14392   1687   2801   -146       C  
ATOM   1272  CD2 PHE A1156       8.920  76.339  84.711  1.00 87.71           C  
ANISOU 1272  CD2 PHE A1156     9005   9806  14516   1413   2843   -202       C  
ATOM   1273  CE1 PHE A1156       7.892  78.923  84.737  1.00 90.41           C  
ANISOU 1273  CE1 PHE A1156     9820   9991  14540   1926   2971   -181       C  
ATOM   1274  CE2 PHE A1156       7.653  76.585  85.234  1.00 88.99           C  
ANISOU 1274  CE2 PHE A1156     9099  10031  14680   1621   3019   -237       C  
ATOM   1275  CZ  PHE A1156       7.141  77.875  85.239  1.00 90.32           C  
ANISOU 1275  CZ  PHE A1156     9490  10132  14694   1889   3083   -227       C  
ATOM   1276  N   PRO A1157      14.435  76.326  84.813  1.00 84.26           N  
ANISOU 1276  N   PRO A1157     9219   8952  13843    532   2335     19       N  
ATOM   1277  CA  PRO A1157      15.755  75.911  84.352  1.00 83.52           C  
ANISOU 1277  CA  PRO A1157     9070   8887  13776    325   2182     51       C  
ATOM   1278  C   PRO A1157      15.877  74.395  84.173  1.00 84.18           C  
ANISOU 1278  C   PRO A1157     8822   9110  14051    240   2143     16       C  
ATOM   1279  O   PRO A1157      16.972  73.877  83.883  1.00 84.33           O  
ANISOU 1279  O   PRO A1157     8769   9166  14105     85   2025     40       O  
ATOM   1280  CB  PRO A1157      16.681  76.392  85.477  1.00 83.75           C  
ANISOU 1280  CB  PRO A1157     9424   8742  13657    145   2156    119       C  
ATOM   1281  CG  PRO A1157      15.783  76.798  86.622  1.00 84.35           C  
ANISOU 1281  CG  PRO A1157     9709   8692  13649    251   2309    117       C  
ATOM   1282  CD  PRO A1157      14.400  76.337  86.280  1.00 84.98           C  
ANISOU 1282  CD  PRO A1157     9526   8903  13861    464   2429     47       C  
ATOM   1283  N   GLU A1158      14.759  73.691  84.342  1.00 84.03           N  
ANISOU 1283  N   GLU A1158     8609   9170  14148    342   2245    -40       N  
ATOM   1284  CA  GLU A1158      14.686  72.275  83.992  1.00 82.56           C  
ANISOU 1284  CA  GLU A1158     8120   9116  14135    281   2215    -83       C  
ATOM   1285  C   GLU A1158      14.468  72.125  82.466  1.00 80.70           C  
ANISOU 1285  C   GLU A1158     7645   9032  13984    374   2139   -127       C  
ATOM   1286  O   GLU A1158      14.890  71.140  81.867  1.00 78.58           O  
ANISOU 1286  O   GLU A1158     7184   8853  13820    297   2060   -147       O  
ATOM   1287  CB  GLU A1158      13.566  71.611  84.816  1.00 84.18           C  
ANISOU 1287  CB  GLU A1158     8233   9339  14414    318   2362   -125       C  
ATOM   1288  CG  GLU A1158      13.234  70.159  84.492  1.00 84.02           C  
ANISOU 1288  CG  GLU A1158     7921   9443  14560    257   2355   -179       C  
ATOM   1289  CD  GLU A1158      11.877  69.745  85.055  1.00 86.45           C  
ANISOU 1289  CD  GLU A1158     8110   9804  14933    314   2520   -230       C  
ATOM   1290  OE1 GLU A1158      11.559  70.169  86.206  1.00 86.32           O  
ANISOU 1290  OE1 GLU A1158     8285   9679  14833    324   2648   -208       O  
ATOM   1291  OE2 GLU A1158      11.135  69.003  84.346  1.00 85.40           O  
ANISOU 1291  OE2 GLU A1158     7696   9825  14928    340   2526   -293       O  
ATOM   1292  N   TRP A1159      13.832  73.119  81.849  1.00 80.38           N  
ANISOU 1292  N   TRP A1159     7646   9010  13884    549   2161   -141       N  
ATOM   1293  CA  TRP A1159      13.451  73.047  80.438  1.00 79.90           C  
ANISOU 1293  CA  TRP A1159     7382   9087  13889    662   2093   -187       C  
ATOM   1294  C   TRP A1159      14.117  74.092  79.550  1.00 80.32           C  
ANISOU 1294  C   TRP A1159     7602   9096  13819    697   2006   -153       C  
ATOM   1295  O   TRP A1159      14.149  73.938  78.313  1.00 79.60           O  
ANISOU 1295  O   TRP A1159     7372   9103  13771    745   1924   -181       O  
ATOM   1296  CB  TRP A1159      11.934  73.235  80.281  1.00 81.04           C  
ANISOU 1296  CB  TRP A1159     7385   9328  14078    875   2183   -246       C  
ATOM   1297  CG  TRP A1159      10.990  72.254  80.962  1.00 81.22           C  
ANISOU 1297  CG  TRP A1159     7198   9436  14229    858   2290   -294       C  
ATOM   1298  CD1 TRP A1159      11.170  70.887  81.187  1.00 79.71           C  
ANISOU 1298  CD1 TRP A1159     6838   9290  14160    688   2281   -316       C  
ATOM   1299  CD2 TRP A1159       9.636  72.547  81.469  1.00 82.10           C  
ANISOU 1299  CD2 TRP A1159     7235   9606  14352   1022   2434   -331       C  
ATOM   1300  NE1 TRP A1159      10.068  70.350  81.813  1.00 79.95           N  
ANISOU 1300  NE1 TRP A1159     6720   9390  14268    706   2410   -360       N  
ATOM   1301  CE2 TRP A1159       9.113  71.285  81.999  1.00 80.96           C  
ANISOU 1301  CE2 TRP A1159     6873   9545  14344    901   2510   -372       C  
ATOM   1302  CE3 TRP A1159       8.839  73.695  81.535  1.00 83.75           C  
ANISOU 1302  CE3 TRP A1159     7543   9810  14469   1257   2511   -334       C  
ATOM   1303  CZ2 TRP A1159       7.855  71.189  82.556  1.00 82.53           C  
ANISOU 1303  CZ2 TRP A1159     6931   9835  14591    990   2663   -414       C  
ATOM   1304  CZ3 TRP A1159       7.563  73.587  82.112  1.00 85.94           C  
ANISOU 1304  CZ3 TRP A1159     7667  10186  14799   1379   2664   -377       C  
ATOM   1305  CH2 TRP A1159       7.088  72.358  82.614  1.00 85.23           C  
ANISOU 1305  CH2 TRP A1159     7341  10193  14849   1236   2742   -416       C  
ATOM   1306  N   PHE A1160      14.601  75.190  80.138  1.00 92.87           N  
ANISOU 1306  N   PHE A1160     9717  10296  15272  -1493   -325  -1507       N  
ATOM   1307  CA  PHE A1160      15.092  76.323  79.322  1.00 92.46           C  
ANISOU 1307  CA  PHE A1160     9634  10167  15327  -1437   -244  -1527       C  
ATOM   1308  C   PHE A1160      16.359  77.013  79.821  1.00 95.41           C  
ANISOU 1308  C   PHE A1160    10040  10665  15548  -1850   -438  -1358       C  
ATOM   1309  O   PHE A1160      16.901  77.875  79.120  1.00 95.21           O  
ANISOU 1309  O   PHE A1160     9958  10605  15614  -1826   -417  -1318       O  
ATOM   1310  CB  PHE A1160      13.992  77.375  79.131  1.00 92.00           C  
ANISOU 1310  CB  PHE A1160     9788   9855  15313  -1352     98  -1804       C  
ATOM   1311  CG  PHE A1160      12.838  76.899  78.298  1.00 89.35           C  
ANISOU 1311  CG  PHE A1160     9304   9466  15178   -965    239  -1829       C  
ATOM   1312  CD1 PHE A1160      11.730  76.339  78.896  1.00 88.65           C  
ANISOU 1312  CD1 PHE A1160     9287   9365  15033   -950    344  -1897       C  
ATOM   1313  CD2 PHE A1160      12.868  77.010  76.914  1.00 87.67           C  
ANISOU 1313  CD2 PHE A1160     8881   9253  15174   -682    243  -1740       C  
ATOM   1314  CE1 PHE A1160      10.674  75.902  78.131  1.00 87.37           C  
ANISOU 1314  CE1 PHE A1160     8964   9209  15025   -690    412  -1831       C  
ATOM   1315  CE2 PHE A1160      11.815  76.564  76.142  1.00 85.94           C  
ANISOU 1315  CE2 PHE A1160     8549   9035  15070   -458    308  -1701       C  
ATOM   1316  CZ  PHE A1160      10.714  76.011  76.752  1.00 85.79           C  
ANISOU 1316  CZ  PHE A1160     8577   9021  14998   -476    374  -1725       C  
ATOM   1317  N   GLY A1161      16.810  76.645  81.027  1.00 97.51           N  
ANISOU 1317  N   GLY A1161    10392  11102  15557  -2287   -656  -1215       N  
ATOM   1318  CA  GLY A1161      17.986  77.242  81.669  1.00 99.36           C  
ANISOU 1318  CA  GLY A1161    10673  11522  15556  -2851   -923   -968       C  
ATOM   1319  C   GLY A1161      19.270  77.242  80.858  1.00 98.67           C  
ANISOU 1319  C   GLY A1161    10147  11655  15689  -2737  -1136   -532       C  
ATOM   1320  O   GLY A1161      20.062  78.164  80.974  1.00101.25           O  
ANISOU 1320  O   GLY A1161    10534  12067  15870  -3145  -1281   -391       O  
ATOM   1321  N   THR A1162      19.485  76.206  80.051  1.00 96.08           N  
ANISOU 1321  N   THR A1162     9414  11402  15691  -2206  -1123   -304       N  
ATOM   1322  CA  THR A1162      20.643  76.139  79.158  1.00 96.46           C  
ANISOU 1322  CA  THR A1162     9030  11624  15998  -1973  -1196    118       C  
ATOM   1323  C   THR A1162      20.173  76.133  77.707  1.00 93.04           C  
ANISOU 1323  C   THR A1162     8553  10977  15823  -1386   -893   -119       C  
ATOM   1324  O   THR A1162      19.181  75.500  77.381  1.00 89.98           O  
ANISOU 1324  O   THR A1162     8296  10399  15492  -1075   -709   -396       O  
ATOM   1325  CB  THR A1162      21.507  74.879  79.413  1.00 98.52           C  
ANISOU 1325  CB  THR A1162     8855  12133  16445  -1838  -1356    693       C  
ATOM   1326  OG1 THR A1162      21.655  74.658  80.822  1.00100.95           O  
ANISOU 1326  OG1 THR A1162     9222  12646  16489  -2397  -1656    904       O  
ATOM   1327  CG2 THR A1162      22.891  75.043  78.805  1.00101.29           C  
ANISOU 1327  CG2 THR A1162     8727  12735  17024  -1743  -1438   1266       C  
ATOM   1328  N   LEU A1163      20.888  76.858  76.849  1.00 93.95           N  
ANISOU 1328  N   LEU A1163     8492  11152  16053  -1310   -872     24       N  
ATOM   1329  CA  LEU A1163      20.618  76.908  75.406  1.00 91.74           C  
ANISOU 1329  CA  LEU A1163     8155  10729  15974   -833   -615   -128       C  
ATOM   1330  C   LEU A1163      20.271  75.520  74.853  1.00 91.26           C  
ANISOU 1330  C   LEU A1163     8050  10566  16058   -370   -427   -141       C  
ATOM   1331  O   LEU A1163      19.296  75.355  74.103  1.00 89.09           O  
ANISOU 1331  O   LEU A1163     7973  10093  15783   -146   -242   -464       O  
ATOM   1332  CB  LEU A1163      21.837  77.487  74.675  1.00 92.97           C  
ANISOU 1332  CB  LEU A1163     7992  11075  16258   -804   -657    232       C  
ATOM   1333  CG  LEU A1163      21.884  77.844  73.179  1.00 91.77           C  
ANISOU 1333  CG  LEU A1163     7755  10856  16257   -446   -435    163       C  
ATOM   1334  CD1 LEU A1163      22.050  76.622  72.292  1.00 92.23           C  
ANISOU 1334  CD1 LEU A1163     7687  10872  16486     66   -171    267       C  
ATOM   1335  CD2 LEU A1163      20.714  78.699  72.708  1.00 89.30           C  
ANISOU 1335  CD2 LEU A1163     7749  10301  15880   -461   -321   -289       C  
ATOM   1336  N   GLY A1164      21.076  74.529  75.234  1.00 93.85           N  
ANISOU 1336  N   GLY A1164     8133  11023  16504   -267   -474    259       N  
ATOM   1337  CA  GLY A1164      20.889  73.155  74.777  1.00 93.91           C  
ANISOU 1337  CA  GLY A1164     8168  10858  16655    160   -242    280       C  
ATOM   1338  C   GLY A1164      19.698  72.501  75.437  1.00 92.31           C  
ANISOU 1338  C   GLY A1164     8271  10497  16306     68   -283    -31       C  
ATOM   1339  O   GLY A1164      18.976  71.740  74.795  1.00 90.79           O  
ANISOU 1339  O   GLY A1164     8306  10076  16114    316    -88   -258       O  
ATOM   1340  N   GLU A1165      19.500  72.795  76.724  1.00 92.21           N  
ANISOU 1340  N   GLU A1165     8294  10614  16127   -345   -538    -26       N  
ATOM   1341  CA  GLU A1165      18.305  72.352  77.447  1.00 90.52           C  
ANISOU 1341  CA  GLU A1165     8360  10288  15745   -483   -573   -322       C  
ATOM   1342  C   GLU A1165      17.062  73.105  76.982  1.00 88.52           C  
ANISOU 1342  C   GLU A1165     8374   9877  15382   -491   -441   -776       C  
ATOM   1343  O   GLU A1165      15.959  72.757  77.391  1.00 88.65           O  
ANISOU 1343  O   GLU A1165     8583   9808  15293   -547   -418   -991       O  
ATOM   1344  CB  GLU A1165      18.460  72.542  78.952  1.00 91.55           C  
ANISOU 1344  CB  GLU A1165     8501  10610  15674   -971   -838   -193       C  
ATOM   1345  CG  GLU A1165      19.500  71.652  79.597  1.00 94.15           C  
ANISOU 1345  CG  GLU A1165     8512  11143  16117  -1023  -1027    363       C  
ATOM   1346  CD  GLU A1165      19.518  71.775  81.102  1.00 95.38           C  
ANISOU 1346  CD  GLU A1165     8732  11518  15990  -1612  -1330    490       C  
ATOM   1347  OE1 GLU A1165      19.099  70.818  81.779  1.00 95.73           O  
ANISOU 1347  OE1 GLU A1165     8813  11556  16002  -1641  -1395    547       O  
ATOM   1348  OE2 GLU A1165      19.936  72.827  81.608  1.00 96.76           O  
ANISOU 1348  OE2 GLU A1165     8971  11860  15934  -2096  -1500    525       O  
ATOM   1349  N   SER A1166      17.241  74.141  76.154  1.00 88.09           N  
ANISOU 1349  N   SER A1166     8286   9806  15378   -440   -355   -851       N  
ATOM   1350  CA  SER A1166      16.118  74.847  75.536  1.00 86.31           C  
ANISOU 1350  CA  SER A1166     8221   9439  15135   -386   -208  -1155       C  
ATOM   1351  C   SER A1166      15.848  74.148  74.223  1.00 85.39           C  
ANISOU 1351  C   SER A1166     8107   9239  15097    -74    -82  -1173       C  
ATOM   1352  O   SER A1166      14.698  73.805  73.903  1.00 84.16           O  
ANISOU 1352  O   SER A1166     8093   8997  14886    -45    -30  -1323       O  
ATOM   1353  CB  SER A1166      16.455  76.326  75.286  1.00 87.56           C  
ANISOU 1353  CB  SER A1166     8360   9595  15314   -513   -178  -1187       C  
ATOM   1354  OG  SER A1166      16.675  77.059  76.496  1.00 90.15           O  
ANISOU 1354  OG  SER A1166     8831   9939  15481   -905   -261  -1218       O  
ATOM   1355  N   PHE A1167      16.929  73.924  73.470  1.00 86.46           N  
ANISOU 1355  N   PHE A1167     8102   9412  15337    118    -21   -981       N  
ATOM   1356  CA  PHE A1167      16.895  73.099  72.249  1.00 86.25           C  
ANISOU 1356  CA  PHE A1167     8188   9263  15322    382    168  -1001       C  
ATOM   1357  C   PHE A1167      16.050  71.850  72.438  1.00 86.14           C  
ANISOU 1357  C   PHE A1167     8431   9094  15204    392    189  -1114       C  
ATOM   1358  O   PHE A1167      15.260  71.512  71.555  1.00 86.07           O  
ANISOU 1358  O   PHE A1167     8657   8977  15069    385    266  -1264       O  
ATOM   1359  CB  PHE A1167      18.299  72.679  71.817  1.00 88.06           C  
ANISOU 1359  CB  PHE A1167     8242   9516  15700    636    319   -713       C  
ATOM   1360  CG  PHE A1167      18.838  73.462  70.665  1.00 88.15           C  
ANISOU 1360  CG  PHE A1167     8152   9589  15752    740    446   -670       C  
ATOM   1361  CD1 PHE A1167      19.592  74.611  70.877  1.00 88.36           C  
ANISOU 1361  CD1 PHE A1167     7892   9817  15862    615    313   -492       C  
ATOM   1362  CD2 PHE A1167      18.605  73.041  69.361  1.00 88.69           C  
ANISOU 1362  CD2 PHE A1167     8457   9513  15727    898    693   -800       C  
ATOM   1363  CE1 PHE A1167      20.094  75.327  69.802  1.00 88.88           C  
ANISOU 1363  CE1 PHE A1167     7849   9954  15968    701    419   -426       C  
ATOM   1364  CE2 PHE A1167      19.101  73.750  68.283  1.00 89.08           C  
ANISOU 1364  CE2 PHE A1167     8420   9642  15783    967    815   -748       C  
ATOM   1365  CZ  PHE A1167      19.844  74.897  68.504  1.00 89.34           C  
ANISOU 1365  CZ  PHE A1167     8104   9891  15949    895    675   -552       C  
ATOM   1366  N   TYR A1168      16.212  71.177  73.584  1.00 86.17           N  
ANISOU 1366  N   TYR A1168     8401   9109  15232    341     88  -1006       N  
ATOM   1367  CA  TYR A1168      15.423  69.981  73.867  1.00 86.40           C  
ANISOU 1367  CA  TYR A1168     8676   8987  15166    319     82  -1089       C  
ATOM   1368  C   TYR A1168      13.917  70.301  73.905  1.00 84.69           C  
ANISOU 1368  C   TYR A1168     8598   8796  14786     95    -18  -1312       C  
ATOM   1369  O   TYR A1168      13.122  69.760  73.089  1.00 84.20           O  
ANISOU 1369  O   TYR A1168     8775   8624  14592     58     24  -1410       O  
ATOM   1370  CB  TYR A1168      15.852  69.268  75.166  1.00 87.13           C  
ANISOU 1370  CB  TYR A1168     8659   9121  15324    272    -41   -878       C  
ATOM   1371  CG  TYR A1168      15.243  67.884  75.263  1.00 88.27           C  
ANISOU 1371  CG  TYR A1168     9079   9050  15408    307     -1   -917       C  
ATOM   1372  CD1 TYR A1168      16.022  66.741  75.138  1.00 90.94           C  
ANISOU 1372  CD1 TYR A1168     9475   9173  15903    571    183   -695       C  
ATOM   1373  CD2 TYR A1168      13.863  67.720  75.426  1.00 87.72           C  
ANISOU 1373  CD2 TYR A1168     9219   8969  15142     82   -113  -1135       C  
ATOM   1374  CE1 TYR A1168      15.453  65.477  75.202  1.00 92.37           C  
ANISOU 1374  CE1 TYR A1168     9990   9087  16020    578    243   -746       C  
ATOM   1375  CE2 TYR A1168      13.282  66.461  75.490  1.00 88.52           C  
ANISOU 1375  CE2 TYR A1168     9605   8875  15155     44   -112  -1156       C  
ATOM   1376  CZ  TYR A1168      14.084  65.346  75.382  1.00 90.91           C  
ANISOU 1376  CZ  TYR A1168    10036   8918  15586    277     61   -990       C  
ATOM   1377  OH  TYR A1168      13.500  64.107  75.447  1.00 92.33           O  
ANISOU 1377  OH  TYR A1168    10570   8843  15668    211     80  -1023       O  
ATOM   1378  N   THR A1169      13.544  71.165  74.856  1.00 82.87           N  
ANISOU 1378  N   THR A1169     8234   8705  14548    -83   -126  -1350       N  
ATOM   1379  CA  THR A1169      12.148  71.517  75.111  1.00 81.37           C  
ANISOU 1379  CA  THR A1169     8092   8550  14275   -237   -146  -1467       C  
ATOM   1380  C   THR A1169      11.495  72.094  73.861  1.00 80.67           C  
ANISOU 1380  C   THR A1169     7990   8461  14200   -203    -78  -1486       C  
ATOM   1381  O   THR A1169      10.261  72.002  73.689  1.00 80.39           O  
ANISOU 1381  O   THR A1169     7969   8467  14109   -310   -104  -1458       O  
ATOM   1382  CB  THR A1169      12.015  72.545  76.245  1.00 81.29           C  
ANISOU 1382  CB  THR A1169     8008   8614  14264   -391   -131  -1522       C  
ATOM   1383  OG1 THR A1169      12.855  72.156  77.337  1.00 82.54           O  
ANISOU 1383  OG1 THR A1169     8163   8832  14365   -517   -248  -1443       O  
ATOM   1384  CG2 THR A1169      10.571  72.605  76.723  1.00 81.37           C  
ANISOU 1384  CG2 THR A1169     8058   8640  14222   -485    -69  -1576       C  
ATOM   1385  N   LEU A1170      12.324  72.689  72.996  1.00 79.69           N  
ANISOU 1385  N   LEU A1170     7796   8331  14151    -85     -9  -1464       N  
ATOM   1386  CA  LEU A1170      11.829  73.232  71.742  1.00 78.93           C  
ANISOU 1386  CA  LEU A1170     7674   8264  14051    -91     29  -1434       C  
ATOM   1387  C   LEU A1170      11.538  72.107  70.761  1.00 79.54           C  
ANISOU 1387  C   LEU A1170     8015   8275  13931   -157     16  -1437       C  
ATOM   1388  O   LEU A1170      10.519  72.132  70.079  1.00 79.73           O  
ANISOU 1388  O   LEU A1170     8078   8373  13844   -343    -58  -1361       O  
ATOM   1389  CB  LEU A1170      12.814  74.225  71.152  1.00 78.83           C  
ANISOU 1389  CB  LEU A1170     7520   8277  14156     19    102  -1402       C  
ATOM   1390  CG  LEU A1170      12.854  75.604  71.793  1.00 78.68           C  
ANISOU 1390  CG  LEU A1170     7336   8276  14285    -13    134  -1404       C  
ATOM   1391  CD1 LEU A1170      13.865  76.482  71.074  1.00 79.14           C  
ANISOU 1391  CD1 LEU A1170     7274   8364  14433     53    168  -1339       C  
ATOM   1392  CD2 LEU A1170      11.470  76.230  71.741  1.00 79.22           C  
ANISOU 1392  CD2 LEU A1170     7331   8340  14428    -63    193  -1357       C  
ATOM   1393  N   PHE A1171      12.427  71.111  70.718  1.00 80.03           N  
ANISOU 1393  N   PHE A1171     8278   8186  13943    -33    108  -1481       N  
ATOM   1394  CA  PHE A1171      12.266  69.979  69.824  1.00 81.30           C  
ANISOU 1394  CA  PHE A1171     8845   8170  13874   -109    190  -1539       C  
ATOM   1395  C   PHE A1171      10.958  69.296  70.143  1.00 81.67           C  
ANISOU 1395  C   PHE A1171     9059   8229  13743   -398     10  -1535       C  
ATOM   1396  O   PHE A1171      10.231  68.902  69.212  1.00 83.24           O  
ANISOU 1396  O   PHE A1171     9538   8413  13675   -681    -49  -1527       O  
ATOM   1397  CB  PHE A1171      13.426  68.981  69.954  1.00 82.67           C  
ANISOU 1397  CB  PHE A1171     9204   8100  14108    154    419  -1543       C  
ATOM   1398  CG  PHE A1171      13.236  67.724  69.139  1.00 85.09           C  
ANISOU 1398  CG  PHE A1171    10077   8100  14153     71    602  -1653       C  
ATOM   1399  CD1 PHE A1171      13.401  67.743  67.746  1.00 87.13           C  
ANISOU 1399  CD1 PHE A1171    10658   8256  14191      4    805  -1742       C  
ATOM   1400  CD2 PHE A1171      12.887  66.530  69.749  1.00 85.71           C  
ANISOU 1400  CD2 PHE A1171    10436   7966  14164      9    589  -1676       C  
ATOM   1401  CE1 PHE A1171      13.210  66.598  66.982  1.00 90.35           C  
ANISOU 1401  CE1 PHE A1171    11735   8322  14270   -159   1021  -1889       C  
ATOM   1402  CE2 PHE A1171      12.706  65.385  68.990  1.00 89.44           C  
ANISOU 1402  CE2 PHE A1171    11546   8080  14356   -120    792  -1804       C  
ATOM   1403  CZ  PHE A1171      12.858  65.416  67.607  1.00 91.62           C  
ANISOU 1403  CZ  PHE A1171    12220   8222  14368   -224   1023  -1930       C  
ATOM   1404  N   GLN A1172      10.666  69.187  71.455  1.00 80.32           N  
ANISOU 1404  N   GLN A1172     8720   8115  13684   -386    -96  -1507       N  
ATOM   1405  CA  GLN A1172       9.492  68.460  71.984  1.00 80.19           C  
ANISOU 1405  CA  GLN A1172     8810   8131  13527   -637   -264  -1462       C  
ATOM   1406  C   GLN A1172       8.248  69.195  71.601  1.00 80.11           C  
ANISOU 1406  C   GLN A1172     8599   8359  13482   -859   -392  -1306       C  
ATOM   1407  O   GLN A1172       7.323  68.616  71.036  1.00 82.20           O  
ANISOU 1407  O   GLN A1172     9039   8673  13519  -1178   -540  -1190       O  
ATOM   1408  CB  GLN A1172       9.536  68.339  73.505  1.00 79.20           C  
ANISOU 1408  CB  GLN A1172     8512   8052  13528   -572   -316  -1450       C  
ATOM   1409  CG  GLN A1172       8.513  67.365  74.072  1.00 79.74           C  
ANISOU 1409  CG  GLN A1172     8722   8129  13445   -809   -471  -1391       C  
ATOM   1410  CD  GLN A1172       8.363  67.417  75.598  1.00 78.87           C  
ANISOU 1410  CD  GLN A1172     8416   8132  13419   -808   -523  -1363       C  
ATOM   1411  OE1 GLN A1172       9.248  67.872  76.337  1.00 77.21           O  
ANISOU 1411  OE1 GLN A1172     8063   7938  13335   -668   -464  -1398       O  
ATOM   1412  NE2 GLN A1172       7.219  66.931  76.073  1.00 79.74           N  
ANISOU 1412  NE2 GLN A1172     8535   8346  13416  -1029   -650  -1267       N  
ATOM   1413  N   VAL A1173       8.239  70.488  71.894  1.00 78.77           N  
ANISOU 1413  N   VAL A1173     8063   8326  13541   -712   -325  -1253       N  
ATOM   1414  CA  VAL A1173       7.123  71.336  71.514  1.00 79.28           C  
ANISOU 1414  CA  VAL A1173     7846   8594  13682   -826   -366  -1010       C  
ATOM   1415  C   VAL A1173       6.904  71.139  70.019  1.00 81.02           C  
ANISOU 1415  C   VAL A1173     8216   8872  13694  -1069   -480   -887       C  
ATOM   1416  O   VAL A1173       5.800  70.795  69.598  1.00 83.44           O  
ANISOU 1416  O   VAL A1173     8511   9347  13845  -1402   -668   -626       O  
ATOM   1417  CB  VAL A1173       7.365  72.814  71.895  1.00 78.24           C  
ANISOU 1417  CB  VAL A1173     7400   8479  13848   -585   -179  -1002       C  
ATOM   1418  CG1 VAL A1173       6.419  73.727  71.142  1.00 79.52           C  
ANISOU 1418  CG1 VAL A1173     7258   8801  14155   -634   -165   -678       C  
ATOM   1419  CG2 VAL A1173       7.220  73.012  73.398  1.00 77.48           C  
ANISOU 1419  CG2 VAL A1173     7241   8345  13854   -495    -57  -1092       C  
HETATM 1420  N   MSE A1174       7.959  71.301  69.222  1.00 80.71           N  
ANISOU 1420  N   MSE A1174     8336   8718  13613   -960   -377  -1041       N  
HETATM 1421  CA  MSE A1174       7.871  71.046  67.775  1.00 82.76           C  
ANISOU 1421  CA  MSE A1174     8853   9007  13584  -1245   -445   -977       C  
HETATM 1422  C   MSE A1174       7.110  69.745  67.488  1.00 84.89           C  
ANISOU 1422  C   MSE A1174     9549   9238  13467  -1678   -616   -942       C  
HETATM 1423  O   MSE A1174       6.074  69.770  66.783  1.00 86.96           O  
ANISOU 1423  O   MSE A1174     9787   9731  13524  -2120   -851   -643       O  
HETATM 1424  CB  MSE A1174       9.263  71.118  67.136  1.00 82.84           C  
ANISOU 1424  CB  MSE A1174     9065   8839  13573  -1022   -223  -1200       C  
HETATM 1425  CG  MSE A1174       9.330  70.534  65.736  1.00 86.11           C  
ANISOU 1425  CG  MSE A1174     9951   9185  13583  -1335   -195  -1241       C  
HETATM 1426 SE   MSE A1174      11.105  70.932  64.997  1.00 87.29          SE  
ANISOU 1426 SE   MSE A1174    10190   9166  13811   -940    182  -1438      SE  
HETATM 1427  CE  MSE A1174      11.438  69.148  64.208  1.00 91.49           C  
ANISOU 1427  CE  MSE A1174    11657   9269  13837  -1136    477  -1707       C  
ATOM   1428  N   THR A1175       7.592  68.620  68.042  1.00 84.30           N  
ANISOU 1428  N   THR A1175     9853   8884  13295  -1596   -519  -1184       N  
ATOM   1429  CA  THR A1175       6.917  67.317  67.868  1.00 86.53           C  
ANISOU 1429  CA  THR A1175    10632   9047  13198  -2025   -659  -1183       C  
ATOM   1430  C   THR A1175       5.512  67.304  68.508  1.00 86.54           C  
ANISOU 1430  C   THR A1175    10319   9347  13214  -2313   -965   -860       C  
ATOM   1431  O   THR A1175       4.770  66.306  68.414  1.00 89.07           O  
ANISOU 1431  O   THR A1175    10985   9648  13211  -2761  -1163   -771       O  
ATOM   1432  CB  THR A1175       7.746  66.130  68.407  1.00 86.74           C  
ANISOU 1432  CB  THR A1175    11103   8657  13198  -1812   -441  -1462       C  
ATOM   1433  OG1 THR A1175       7.992  66.302  69.809  1.00 83.41           O  
ANISOU 1433  OG1 THR A1175    10280   8279  13132  -1457   -433  -1455       O  
ATOM   1434  CG2 THR A1175       9.063  65.996  67.655  1.00 87.82           C  
ANISOU 1434  CG2 THR A1175    11568   8483  13314  -1532    -67  -1691       C  
ATOM   1435  N   LEU A1176       5.165  68.427  69.144  1.00 83.82           N  
ANISOU 1435  N   LEU A1176     9348   9258  13243  -2059   -962   -666       N  
ATOM   1436  CA  LEU A1176       3.822  68.696  69.668  1.00 84.32           C  
ANISOU 1436  CA  LEU A1176     8984   9642  13414  -2231  -1144   -265       C  
ATOM   1437  C   LEU A1176       3.417  67.881  70.902  1.00 83.85           C  
ANISOU 1437  C   LEU A1176     8957   9545  13356  -2233  -1189   -296       C  
ATOM   1438  O   LEU A1176       2.326  68.098  71.456  1.00 84.66           O  
ANISOU 1438  O   LEU A1176     8673   9918  13577  -2322  -1277     52       O  
ATOM   1439  CB  LEU A1176       2.756  68.593  68.561  1.00 87.94           C  
ANISOU 1439  CB  LEU A1176     9430  10390  13591  -2813  -1450    176       C  
ATOM   1440  CG  LEU A1176       2.750  69.728  67.535  1.00 88.44           C  
ANISOU 1440  CG  LEU A1176     9190  10652  13763  -2827  -1452    425       C  
ATOM   1441  CD1 LEU A1176       1.657  69.556  66.477  1.00 92.13           C  
ANISOU 1441  CD1 LEU A1176     9618  11477  13909  -3517  -1830    971       C  
ATOM   1442  CD2 LEU A1176       2.640  71.073  68.252  1.00 86.56           C  
ANISOU 1442  CD2 LEU A1176     8297  10511  14080  -2310  -1221    584       C  
ATOM   1443  N   GLU A1177       4.281  66.961  71.339  1.00 82.56           N  
ANISOU 1443  N   GLU A1177     9213   9061  13095  -2117  -1104   -650       N  
ATOM   1444  CA  GLU A1177       3.948  66.128  72.485  1.00 82.14           C  
ANISOU 1444  CA  GLU A1177     9211   8971  13029  -2152  -1173   -659       C  
ATOM   1445  C   GLU A1177       4.147  66.851  73.812  1.00 79.53           C  
ANISOU 1445  C   GLU A1177     8475   8719  13026  -1773  -1004   -711       C  
ATOM   1446  O   GLU A1177       5.284  66.968  74.320  1.00 77.56           O  
ANISOU 1446  O   GLU A1177     8281   8283  12906  -1466   -841   -969       O  
ATOM   1447  CB  GLU A1177       4.698  64.807  72.467  1.00 83.19           C  
ANISOU 1447  CB  GLU A1177     9937   8714  12958  -2194  -1139   -927       C  
ATOM   1448  CG  GLU A1177       4.108  63.755  73.412  1.00 84.48           C  
ANISOU 1448  CG  GLU A1177    10222   8853  13024  -2392  -1298   -849       C  
ATOM   1449  CD  GLU A1177       4.566  63.904  74.867  1.00 82.38           C  
ANISOU 1449  CD  GLU A1177     9663   8604  13034  -2038  -1194   -925       C  
ATOM   1450  OE1 GLU A1177       3.722  63.660  75.751  1.00 82.45           O  
ANISOU 1450  OE1 GLU A1177     9490   8807  13030  -2190  -1329   -753       O  
ATOM   1451  OE2 GLU A1177       5.751  64.257  75.131  1.00 80.45           O  
ANISOU 1451  OE2 GLU A1177     9367   8212  12990  -1664   -993  -1112       O  
ATOM   1452  N   SER A1178       3.013  67.316  74.357  1.00 79.72           N  
ANISOU 1452  N   SER A1178     8105   9028  13158  -1839  -1031   -415       N  
ATOM   1453  CA  SER A1178       2.939  68.026  75.634  1.00 78.09           C  
ANISOU 1453  CA  SER A1178     7593   8890  13190  -1565   -809   -448       C  
ATOM   1454  C   SER A1178       3.530  69.426  75.547  1.00 76.42           C  
ANISOU 1454  C   SER A1178     7181   8625  13232  -1237   -535   -562       C  
ATOM   1455  O   SER A1178       4.415  69.813  76.329  1.00 74.47           O  
ANISOU 1455  O   SER A1178     6996   8238  13060  -1036   -371   -831       O  
ATOM   1456  CB  SER A1178       3.570  67.205  76.749  1.00 77.25           C  
ANISOU 1456  CB  SER A1178     7717   8633  13003  -1531   -824   -687       C  
ATOM   1457  OG  SER A1178       2.821  66.026  76.922  1.00 78.93           O  
ANISOU 1457  OG  SER A1178     8073   8903  13013  -1843  -1057   -527       O  
ATOM   1458  N   TRP A1179       3.035  70.178  74.570  1.00 76.92           N  
ANISOU 1458  N   TRP A1179     7009   8810  13405  -1246   -518   -309       N  
ATOM   1459  CA  TRP A1179       3.406  71.571  74.449  1.00 76.28           C  
ANISOU 1459  CA  TRP A1179     6719   8667  13596   -952   -245   -347       C  
ATOM   1460  C   TRP A1179       2.426  72.338  75.269  1.00 78.08           C  
ANISOU 1460  C   TRP A1179     6610   8987  14069   -797     46   -109       C  
ATOM   1461  O   TRP A1179       2.788  73.271  75.990  1.00 78.05           O  
ANISOU 1461  O   TRP A1179     6607   8815  14233   -548    387   -298       O  
ATOM   1462  CB  TRP A1179       3.452  72.022  72.991  1.00 76.85           C  
ANISOU 1462  CB  TRP A1179     6706   8804  13689  -1021   -346   -169       C  
ATOM   1463  CG  TRP A1179       2.142  71.922  72.279  1.00 79.78           C  
ANISOU 1463  CG  TRP A1179     6792   9474  14047  -1298   -529    370       C  
ATOM   1464  CD1 TRP A1179       1.612  70.820  71.623  1.00 81.52           C  
ANISOU 1464  CD1 TRP A1179     7196   9848  13929  -1763   -889    562       C  
ATOM   1465  CD2 TRP A1179       1.148  72.970  72.136  1.00 82.29           C  
ANISOU 1465  CD2 TRP A1179     6571   9987  14707  -1177   -364    883       C  
ATOM   1466  NE1 TRP A1179       0.386  71.111  71.103  1.00 84.83           N  
ANISOU 1466  NE1 TRP A1179     7195  10610  14425  -2001  -1029   1187       N  
ATOM   1467  CE2 TRP A1179       0.047  72.389  71.380  1.00 85.48           C  
ANISOU 1467  CE2 TRP A1179     6778  10742  14957  -1620   -709   1444       C  
ATOM   1468  CE3 TRP A1179       1.062  74.291  72.547  1.00 82.89           C  
ANISOU 1468  CE3 TRP A1179     6341   9957  15196   -772     51    968       C  
ATOM   1469  CZ2 TRP A1179      -1.083  73.117  71.054  1.00 89.13           C  
ANISOU 1469  CZ2 TRP A1179     6636  11502  15726  -1619   -661   2155       C  
ATOM   1470  CZ3 TRP A1179      -0.084  75.016  72.214  1.00 86.58           C  
ANISOU 1470  CZ3 TRP A1179     6257  10641  16000   -701    181   1628       C  
ATOM   1471  CH2 TRP A1179      -1.128  74.443  71.481  1.00 89.63           C  
ANISOU 1471  CH2 TRP A1179     6342  11427  16285  -1099   -179   2253       C  
ATOM   1472  N   SER A1180       1.173  71.908  75.214  1.00 80.47           N  
ANISOU 1472  N   SER A1180     6660   9543  14371   -972    -58    324       N  
ATOM   1473  CA  SER A1180       0.142  72.524  76.032  1.00 83.08           C  
ANISOU 1473  CA  SER A1180     6633   9969  14963   -782    296    631       C  
ATOM   1474  C   SER A1180       0.297  72.057  77.486  1.00 82.47           C  
ANISOU 1474  C   SER A1180     6791   9798  14747   -760    441    316       C  
ATOM   1475  O   SER A1180       1.129  72.598  78.217  1.00 81.29           O  
ANISOU 1475  O   SER A1180     6887   9402  14596   -596    694    -96       O  
ATOM   1476  CB  SER A1180      -1.258  72.233  75.465  1.00 86.57           C  
ANISOU 1476  CB  SER A1180     6628  10787  15478   -997    119   1334       C  
ATOM   1477  OG  SER A1180      -1.720  70.938  75.835  1.00 86.98           O  
ANISOU 1477  OG  SER A1180     6802  11013  15234  -1348   -201   1408       O  
HETATM 1478  N   MSE A1181      -0.470  71.027  77.862  1.00 83.62           N  
ANISOU 1478  N   MSE A1181     6882  10158  14730  -1004    231    535       N  
HETATM 1479  CA  MSE A1181      -0.543  70.516  79.240  1.00 83.74           C  
ANISOU 1479  CA  MSE A1181     7055  10160  14604  -1036    344    348       C  
HETATM 1480  C   MSE A1181       0.802  70.296  79.888  1.00 80.96           C  
ANISOU 1480  C   MSE A1181     7147   9558  14057  -1043    302   -213       C  
HETATM 1481  O   MSE A1181       0.860  70.146  81.110  1.00 81.62           O  
ANISOU 1481  O   MSE A1181     7370   9619  14023  -1076    451   -382       O  
HETATM 1482  CB  MSE A1181      -1.288  69.177  79.330  1.00 84.75           C  
ANISOU 1482  CB  MSE A1181     7154  10536  14510  -1395    -38    621       C  
HETATM 1483  CG  MSE A1181      -2.655  69.128  78.661  1.00 88.18           C  
ANISOU 1483  CG  MSE A1181     7119  11324  15063  -1551   -152   1308       C  
HETATM 1484 SE   MSE A1181      -4.068  69.913  79.782  1.00 92.91          SE  
ANISOU 1484 SE   MSE A1181     7147  12147  16010  -1236    466   1822      SE  
HETATM 1485  CE  MSE A1181      -4.199  68.437  81.075  1.00 92.48           C  
ANISOU 1485  CE  MSE A1181     7382  12199  15558  -1576    219   1643       C  
ATOM   1486  N   GLY A1182       1.874  70.271  79.088  1.00 65.66           N  
ANISOU 1486  N   GLY A1182     5086   7984  11879   1809   -364    171       N  
ATOM   1487  CA  GLY A1182       3.231  70.000  79.572  1.00 67.62           C  
ANISOU 1487  CA  GLY A1182     5423   8218  12050   2152   -594   -108       C  
ATOM   1488  C   GLY A1182       4.063  71.232  79.939  1.00 68.02           C  
ANISOU 1488  C   GLY A1182     5138   8451  12254   2215   -617   -284       C  
ATOM   1489  O   GLY A1182       4.434  71.419  81.116  1.00 69.34           O  
ANISOU 1489  O   GLY A1182     5449   8577  12320   2373   -714   -397       O  
ATOM   1490  N   ILE A1183       4.332  72.067  78.931  1.00 67.27           N  
ANISOU 1490  N   ILE A1183     4657   8545  12356   2039   -506   -313       N  
ATOM   1491  CA  ILE A1183       5.257  73.202  79.008  1.00 67.91           C  
ANISOU 1491  CA  ILE A1183     4456   8817  12531   1970   -477   -538       C  
ATOM   1492  C   ILE A1183       4.546  74.572  79.021  1.00 67.23           C  
ANISOU 1492  C   ILE A1183     4356   8625  12565   1731   -178   -369       C  
ATOM   1493  O   ILE A1183       4.846  75.395  79.885  1.00 68.08           O  
ANISOU 1493  O   ILE A1183     4537   8696  12633   1680   -116   -480       O  
ATOM   1494  CB  ILE A1183       6.268  73.159  77.821  1.00 68.65           C  
ANISOU 1494  CB  ILE A1183     4209   9183  12691   1928   -521   -753       C  
ATOM   1495  CG1 ILE A1183       6.810  71.743  77.643  1.00 70.28           C  
ANISOU 1495  CG1 ILE A1183     4501   9453  12750   2254   -760   -861       C  
ATOM   1496  CG2 ILE A1183       7.395  74.194  77.945  1.00 69.71           C  
ANISOU 1496  CG2 ILE A1183     4046   9596  12845   1769   -489  -1074       C  
ATOM   1497  CD1 ILE A1183       7.515  71.202  78.868  1.00 74.09           C  
ANISOU 1497  CD1 ILE A1183     5124  10012  13014   2635  -1018  -1052       C  
ATOM   1498  N   VAL A1184       3.647  74.847  78.068  1.00 65.97           N  
ANISOU 1498  N   VAL A1184     4137   8426  12502   1612     13   -110       N  
ATOM   1499  CA  VAL A1184       3.105  76.203  77.978  1.00 66.60           C  
ANISOU 1499  CA  VAL A1184     4255   8410  12638   1511    312     45       C  
ATOM   1500  C   VAL A1184       2.303  76.538  79.234  1.00 67.48           C  
ANISOU 1500  C   VAL A1184     4620   8338  12683   1614    425    197       C  
ATOM   1501  O   VAL A1184       2.626  77.490  79.960  1.00 68.92           O  
ANISOU 1501  O   VAL A1184     4975   8390  12822   1571    563     98       O  
ATOM   1502  CB  VAL A1184       2.207  76.464  76.747  1.00 66.04           C  
ANISOU 1502  CB  VAL A1184     4076   8391  12626   1475    476    328       C  
ATOM   1503  CG1 VAL A1184       1.720  77.911  76.765  1.00 67.08           C  
ANISOU 1503  CG1 VAL A1184     4365   8379  12741   1508    802    491       C  
ATOM   1504  CG2 VAL A1184       2.937  76.215  75.444  1.00 65.92           C  
ANISOU 1504  CG2 VAL A1184     3865   8517  12664   1345    408    194       C  
ATOM   1505  N   ARG A1185       1.262  75.738  79.475  1.00 67.20           N  
ANISOU 1505  N   ARG A1185     4631   8298  12604   1695    395    418       N  
ATOM   1506  CA  ARG A1185       0.358  75.887  80.617  1.00 67.59           C  
ANISOU 1506  CA  ARG A1185     4894   8213  12575   1783    526    578       C  
ATOM   1507  C   ARG A1185       1.054  76.270  81.930  1.00 68.76           C  
ANISOU 1507  C   ARG A1185     5309   8170  12644   1821    493    371       C  
ATOM   1508  O   ARG A1185       0.560  77.149  82.677  1.00 69.83           O  
ANISOU 1508  O   ARG A1185     5647   8144  12742   1866    731    471       O  
ATOM   1509  CB  ARG A1185      -0.438  74.606  80.803  1.00 67.20           C  
ANISOU 1509  CB  ARG A1185     4895   8214  12423   1749    428    694       C  
ATOM   1510  CG  ARG A1185      -1.390  74.343  79.670  1.00 66.92           C  
ANISOU 1510  CG  ARG A1185     4588   8437  12402   1638    504    922       C  
ATOM   1511  CD  ARG A1185      -2.648  75.137  79.893  1.00 68.51           C  
ANISOU 1511  CD  ARG A1185     4670   8774  12586   1731    781   1199       C  
ATOM   1512  NE  ARG A1185      -3.755  74.597  79.130  1.00 69.29           N  
ANISOU 1512  NE  ARG A1185     4475   9247  12604   1592    812   1403       N  
ATOM   1513  CZ  ARG A1185      -5.005  74.970  79.324  1.00 71.27           C  
ANISOU 1513  CZ  ARG A1185     4517   9786  12775   1672   1021   1639       C  
ATOM   1514  NH1 ARG A1185      -5.271  75.878  80.262  1.00 71.92           N  
ANISOU 1514  NH1 ARG A1185     4736   9727  12864   1934   1240   1712       N  
ATOM   1515  NH2 ARG A1185      -5.977  74.440  78.585  1.00 73.35           N  
ANISOU 1515  NH2 ARG A1185     4430  10522  12920   1486   1021   1789       N  
ATOM   1516  N   PRO A1186       2.176  75.607  82.236  1.00 69.02           N  
ANISOU 1516  N   PRO A1186     5360   8252  12614   1839    201     86       N  
ATOM   1517  CA  PRO A1186       2.779  76.068  83.487  1.00 70.85           C  
ANISOU 1517  CA  PRO A1186     5812   8382  12727   1854    159   -107       C  
ATOM   1518  C   PRO A1186       3.645  77.302  83.289  1.00 72.19           C  
ANISOU 1518  C   PRO A1186     5896   8617  12916   1652    280   -317       C  
ATOM   1519  O   PRO A1186       3.689  78.169  84.166  1.00 73.67           O  
ANISOU 1519  O   PRO A1186     6340   8647  13004   1558    436   -372       O  
ATOM   1520  CB  PRO A1186       3.587  74.848  83.977  1.00 71.63           C  
ANISOU 1520  CB  PRO A1186     5973   8571  12674   2034   -218   -318       C  
ATOM   1521  CG  PRO A1186       3.009  73.675  83.224  1.00 70.64           C  
ANISOU 1521  CG  PRO A1186     5845   8435  12559   2102   -280   -155       C  
ATOM   1522  CD  PRO A1186       2.583  74.235  81.885  1.00 68.69           C  
ANISOU 1522  CD  PRO A1186     5283   8304  12510   1927    -82     -8       C  
ATOM   1523  N   LEU A1187       4.293  77.386  82.127  1.00 72.57           N  
ANISOU 1523  N   LEU A1187     5644   8874  13057   1536    249   -438       N  
ATOM   1524  CA  LEU A1187       5.143  78.531  81.726  1.00 74.63           C  
ANISOU 1524  CA  LEU A1187     5841   9215  13302   1231    418   -669       C  
ATOM   1525  C   LEU A1187       4.309  79.816  81.628  1.00 75.19           C  
ANISOU 1525  C   LEU A1187     6246   8956  13366   1144    856   -436       C  
ATOM   1526  O   LEU A1187       4.845  80.912  81.499  1.00 77.00           O  
ANISOU 1526  O   LEU A1187     6649   9106  13503    853   1096   -598       O  
ATOM   1527  CB  LEU A1187       5.846  78.241  80.374  1.00 74.35           C  
ANISOU 1527  CB  LEU A1187     5434   9453  13363   1132    337   -809       C  
ATOM   1528  CG  LEU A1187       7.208  78.888  80.048  1.00 76.87           C  
ANISOU 1528  CG  LEU A1187     5541  10060  13606    776    364  -1220       C  
ATOM   1529  CD1 LEU A1187       8.359  78.332  80.868  1.00 79.21           C  
ANISOU 1529  CD1 LEU A1187     5577  10766  13753    818     19  -1595       C  
ATOM   1530  CD2 LEU A1187       7.543  78.728  78.584  1.00 75.90           C  
ANISOU 1530  CD2 LEU A1187     5140  10101  13596    681    404  -1258       C  
HETATM 1531  N   MSE A1188       2.991  79.672  81.709  1.00 74.45           N  
ANISOU 1531  N   MSE A1188     6275   8690  13323   1403    982    -64       N  
HETATM 1532  CA  MSE A1188       2.103  80.823  81.644  1.00 76.15           C  
ANISOU 1532  CA  MSE A1188     6808   8635  13492   1491   1396    198       C  
HETATM 1533  C   MSE A1188       1.882  81.398  83.016  1.00 77.14           C  
ANISOU 1533  C   MSE A1188     7348   8491  13470   1514   1567    192       C  
HETATM 1534  O   MSE A1188       1.925  82.617  83.197  1.00 78.79           O  
ANISOU 1534  O   MSE A1188     7978   8420  13540   1422   1917    183       O  
HETATM 1535  CB  MSE A1188       0.793  80.421  80.966  1.00 76.02           C  
ANISOU 1535  CB  MSE A1188     6606   8716  13564   1784   1450    587       C  
HETATM 1536  CG  MSE A1188       1.112  80.048  79.525  1.00 76.64           C  
ANISOU 1536  CG  MSE A1188     6360   9016  13744   1698   1323    570       C  
HETATM 1537 SE   MSE A1188      -0.574  79.982  78.532  1.00 80.73          SE  
ANISOU 1537 SE   MSE A1188     6664   9734  14275   2024   1461   1064      SE  
HETATM 1538  CE  MSE A1188      -0.531  81.835  77.851  1.00 81.92           C  
ANISOU 1538  CE  MSE A1188     7255   9585  14286   2155   1921   1177       C  
ATOM   1539  N   GLU A1189       1.656  80.515  83.986  1.00 76.20           N  
ANISOU 1539  N   GLU A1189     7202   8411  13339   1622   1346    190       N  
ATOM   1540  CA  GLU A1189       1.314  80.891  85.368  1.00 77.55           C  
ANISOU 1540  CA  GLU A1189     7779   8323  13362   1669   1492    210       C  
ATOM   1541  C   GLU A1189       2.284  81.942  85.946  1.00 80.15           C  
ANISOU 1541  C   GLU A1189     8464   8484  13506   1350   1626    -86       C  
ATOM   1542  O   GLU A1189       1.973  82.641  86.913  1.00 81.33           O  
ANISOU 1542  O   GLU A1189     9079   8330  13493   1343   1880    -52       O  
ATOM   1543  CB  GLU A1189       1.214  79.624  86.243  1.00 76.47           C  
ANISOU 1543  CB  GLU A1189     7589   8268  13198   1767   1170    175       C  
ATOM   1544  CG  GLU A1189      -0.109  78.868  86.046  1.00 75.54           C  
ANISOU 1544  CG  GLU A1189     7337   8210  13156   1982   1226    499       C  
ATOM   1545  CD  GLU A1189      -0.013  77.331  86.046  1.00 74.20           C  
ANISOU 1545  CD  GLU A1189     7024   8192  12977   1990    871    443       C  
ATOM   1546  OE1 GLU A1189       1.065  76.738  86.260  1.00 74.10           O  
ANISOU 1546  OE1 GLU A1189     7019   8237  12899   1961    545    179       O  
ATOM   1547  OE2 GLU A1189      -1.060  76.690  85.839  1.00 73.89           O  
ANISOU 1547  OE2 GLU A1189     6892   8233  12949   2034    939    664       O  
ATOM   1548  N   VAL A1190       3.452  82.057  85.311  1.00 81.14           N  
ANISOU 1548  N   VAL A1190     8373   8833  13624   1041   1485   -392       N  
ATOM   1549  CA  VAL A1190       4.424  83.108  85.618  1.00 84.50           C  
ANISOU 1549  CA  VAL A1190     9084   9193  13831    587   1653   -721       C  
ATOM   1550  C   VAL A1190       4.592  84.100  84.449  1.00 85.53           C  
ANISOU 1550  C   VAL A1190     9360   9198  13939    362   2007   -723       C  
ATOM   1551  O   VAL A1190       4.862  85.277  84.676  1.00 88.24           O  
ANISOU 1551  O   VAL A1190    10236   9249  14042     29   2379   -847       O  
ATOM   1552  CB  VAL A1190       5.813  82.532  85.983  1.00 85.98           C  
ANISOU 1552  CB  VAL A1190     8894   9850  13922    310   1225  -1171       C  
ATOM   1553  CG1 VAL A1190       6.514  83.474  86.962  1.00 90.86           C  
ANISOU 1553  CG1 VAL A1190     9891  10410  14221   -156   1366  -1488       C  
ATOM   1554  CG2 VAL A1190       5.705  81.130  86.579  1.00 84.02           C  
ANISOU 1554  CG2 VAL A1190     8379   9806  13738    691    773  -1125       C  
ATOM   1555  N   TYR A1191       4.431  83.613  83.214  1.00 83.48           N  
ANISOU 1555  N   TYR A1191     8713   9121  13883    520   1910   -591       N  
ATOM   1556  CA  TYR A1191       4.599  84.425  81.991  1.00 84.91           C  
ANISOU 1556  CA  TYR A1191     9036   9192  14033    338   2212   -582       C  
ATOM   1557  C   TYR A1191       3.329  84.473  81.124  1.00 83.35           C  
ANISOU 1557  C   TYR A1191     8882   8834  13952    819   2388   -111       C  
ATOM   1558  O   TYR A1191       3.245  83.766  80.107  1.00 80.47           O  
ANISOU 1558  O   TYR A1191     8076   8732  13765    932   2184    -25       O  
ATOM   1559  CB  TYR A1191       5.768  83.909  81.125  1.00 84.86           C  
ANISOU 1559  CB  TYR A1191     8506   9630  14106     15   1950   -919       C  
ATOM   1560  CG  TYR A1191       7.151  84.020  81.745  1.00 88.01           C  
ANISOU 1560  CG  TYR A1191     8756  10356  14326   -502   1806  -1438       C  
ATOM   1561  CD1 TYR A1191       7.622  83.045  82.625  1.00 87.65           C  
ANISOU 1561  CD1 TYR A1191     8315  10690  14296   -379   1353  -1616       C  
ATOM   1562  CD2 TYR A1191       7.996  85.090  81.426  1.00 92.00           C  
ANISOU 1562  CD2 TYR A1191     9524  10837  14593  -1126   2128  -1764       C  
ATOM   1563  CE1 TYR A1191       8.885  83.136  83.178  1.00 91.66           C  
ANISOU 1563  CE1 TYR A1191     8594  11638  14596   -797   1179  -2095       C  
ATOM   1564  CE2 TYR A1191       9.263  85.191  81.974  1.00 95.81           C  
ANISOU 1564  CE2 TYR A1191     9769  11767  14868  -1669   1989  -2276       C  
ATOM   1565  CZ  TYR A1191       9.704  84.213  82.848  1.00 95.79           C  
ANISOU 1565  CZ  TYR A1191     9268  12234  14893  -1471   1491  -2437       C  
ATOM   1566  OH  TYR A1191      10.968  84.317  83.391  1.00100.48           O  
ANISOU 1566  OH  TYR A1191     9541  13403  15232  -1963   1317  -2955       O  
ATOM   1567  N   PRO A1192       2.351  85.335  81.506  1.00 85.25           N  
ANISOU 1567  N   PRO A1192     9661   8679  14052   1121   2778    189       N  
ATOM   1568  CA  PRO A1192       1.032  85.366  80.843  1.00 85.03           C  
ANISOU 1568  CA  PRO A1192     9593   8634  14082   1685   2918    654       C  
ATOM   1569  C   PRO A1192       1.097  85.427  79.317  1.00 85.28           C  
ANISOU 1569  C   PRO A1192     9459   8785  14158   1705   2927    738       C  
ATOM   1570  O   PRO A1192       0.227  84.894  78.630  1.00 84.23           O  
ANISOU 1570  O   PRO A1192     8957   8907  14139   2073   2802   1038       O  
ATOM   1571  CB  PRO A1192       0.359  86.623  81.403  1.00 88.17           C  
ANISOU 1571  CB  PRO A1192    10743   8546  14211   1960   3434    861       C  
ATOM   1572  CG  PRO A1192       1.359  87.288  82.289  1.00 90.25           C  
ANISOU 1572  CG  PRO A1192    11523   8502  14264   1432   3595    489       C  
ATOM   1573  CD  PRO A1192       2.445  86.319  82.601  1.00 88.04           C  
ANISOU 1573  CD  PRO A1192    10687   8626  14140    968   3114     95       C  
ATOM   1574  N   TYR A1193       2.133  86.055  78.783  1.00 87.56           N  
ANISOU 1574  N   TYR A1193    10015   8926  14326   1256   3077    454       N  
ATOM   1575  CA  TYR A1193       2.209  86.223  77.339  1.00 88.09           C  
ANISOU 1575  CA  TYR A1193    10046   9034  14390   1255   3144    530       C  
ATOM   1576  C   TYR A1193       3.189  85.226  76.758  1.00 85.78           C  
ANISOU 1576  C   TYR A1193     9123   9164  14307    871   2753    219       C  
ATOM   1577  O   TYR A1193       3.826  85.501  75.756  1.00 87.28           O  
ANISOU 1577  O   TYR A1193     9359   9356  14447    584   2849     70       O  
ATOM   1578  CB  TYR A1193       2.566  87.674  76.986  1.00 92.65           C  
ANISOU 1578  CB  TYR A1193    11480   9098  14623   1042   3677    464       C  
ATOM   1579  CG  TYR A1193       1.615  88.688  77.635  1.00 96.23           C  
ANISOU 1579  CG  TYR A1193    12683   9071  14811   1511   4114    777       C  
ATOM   1580  CD1 TYR A1193       1.767  89.064  78.976  1.00 97.54           C  
ANISOU 1580  CD1 TYR A1193    13222   8990  14851   1347   4263    631       C  
ATOM   1581  CD2 TYR A1193       0.554  89.248  76.910  1.00 98.35           C  
ANISOU 1581  CD2 TYR A1193    13283   9165  14919   2176   4371   1224       C  
ATOM   1582  CE1 TYR A1193       0.899  89.964  79.570  1.00100.92           C  
ANISOU 1582  CE1 TYR A1193    14368   8960  15018   1815   4693    917       C  
ATOM   1583  CE2 TYR A1193      -0.316  90.151  77.499  1.00101.93           C  
ANISOU 1583  CE2 TYR A1193    14414   9217  15097   2721   4785   1519       C  
ATOM   1584  CZ  TYR A1193      -0.135  90.500  78.830  1.00103.34           C  
ANISOU 1584  CZ  TYR A1193    14985   9106  15172   2530   4962   1361       C  
ATOM   1585  OH  TYR A1193      -0.977  91.397  79.436  1.00107.64           O  
ANISOU 1585  OH  TYR A1193    16258   9219  15422   3090   5413   1646       O  
ATOM   1586  N   ALA A1194       3.296  84.055  77.388  1.00 83.14           N  
ANISOU 1586  N   ALA A1194     8252   9166  14171    902   2338    127       N  
ATOM   1587  CA  ALA A1194       4.190  82.997  76.911  1.00 81.07           C  
ANISOU 1587  CA  ALA A1194     7420   9307  14074    673   1962   -147       C  
ATOM   1588  C   ALA A1194       3.701  82.345  75.650  1.00 79.27           C  
ANISOU 1588  C   ALA A1194     6879   9260  13979    868   1830     75       C  
ATOM   1589  O   ALA A1194       4.464  81.670  74.992  1.00 79.40           O  
ANISOU 1589  O   ALA A1194     6545   9535  14090    678   1624   -139       O  
ATOM   1590  CB  ALA A1194       4.403  81.939  77.975  1.00 79.61           C  
ANISOU 1590  CB  ALA A1194     6910   9356  13982    744   1587   -279       C  
ATOM   1591  N   TRP A1195       2.438  82.523  75.300  1.00 79.23           N  
ANISOU 1591  N   TRP A1195     6975   9173  13954   1257   1945    494       N  
ATOM   1592  CA  TRP A1195       1.909  81.910  74.083  1.00 78.37           C  
ANISOU 1592  CA  TRP A1195     6559   9298  13920   1402   1804    707       C  
ATOM   1593  C   TRP A1195       2.397  82.637  72.855  1.00 80.16           C  
ANISOU 1593  C   TRP A1195     7007   9400  14048   1228   2017    653       C  
ATOM   1594  O   TRP A1195       2.472  82.057  71.751  1.00 78.87           O  
ANISOU 1594  O   TRP A1195     6578   9440  13949   1171   1868    675       O  
ATOM   1595  CB  TRP A1195       0.385  81.854  74.116  1.00 78.88           C  
ANISOU 1595  CB  TRP A1195     6560   9468  13942   1861   1832   1149       C  
ATOM   1596  CG  TRP A1195      -0.256  83.205  74.261  1.00 82.38           C  
ANISOU 1596  CG  TRP A1195     7506   9619  14175   2193   2233   1393       C  
ATOM   1597  CD1 TRP A1195      -0.602  83.863  75.446  1.00 84.12           C  
ANISOU 1597  CD1 TRP A1195     8081   9585  14295   2381   2462   1452       C  
ATOM   1598  CD2 TRP A1195      -0.645  84.110  73.183  1.00 85.20           C  
ANISOU 1598  CD2 TRP A1195     8179   9857  14337   2448   2489   1630       C  
ATOM   1599  NE1 TRP A1195      -1.171  85.079  75.175  1.00 88.08           N  
ANISOU 1599  NE1 TRP A1195     9105   9811  14551   2759   2855   1707       N  
ATOM   1600  CE2 TRP A1195      -1.225  85.289  73.824  1.00 89.01           C  
ANISOU 1600  CE2 TRP A1195     9240   9994  14587   2843   2883   1832       C  
ATOM   1601  CE3 TRP A1195      -0.588  84.055  71.794  1.00 85.77           C  
ANISOU 1601  CE3 TRP A1195     8173  10050  14366   2425   2442   1702       C  
ATOM   1602  CZ2 TRP A1195      -1.706  86.369  73.086  1.00 92.77           C  
ANISOU 1602  CZ2 TRP A1195    10236  10239  14772   3259   3220   2104       C  
ATOM   1603  CZ3 TRP A1195      -1.083  85.148  71.057  1.00 89.51           C  
ANISOU 1603  CZ3 TRP A1195     9140  10312  14558   2806   2756   1974       C  
ATOM   1604  CH2 TRP A1195      -1.626  86.276  71.694  1.00 92.93           C  
ANISOU 1604  CH2 TRP A1195    10166  10399  14744   3244   3137   2175       C  
ATOM   1605  N   VAL A1196       2.742  83.914  73.033  1.00 83.17           N  
ANISOU 1605  N   VAL A1196     7961   9409  14232   1103   2400    572       N  
ATOM   1606  CA  VAL A1196       3.322  84.702  71.933  1.00 85.54           C  
ANISOU 1606  CA  VAL A1196     8623   9508  14371    842   2678    469       C  
ATOM   1607  C   VAL A1196       4.696  84.137  71.517  1.00 85.05           C  
ANISOU 1607  C   VAL A1196     8195   9697  14423    292   2518     10       C  
ATOM   1608  O   VAL A1196       4.960  83.937  70.319  1.00 85.00           O  
ANISOU 1608  O   VAL A1196     8084   9784  14430    172   2507    -15       O  
ATOM   1609  CB  VAL A1196       3.335  86.226  72.208  1.00 89.23           C  
ANISOU 1609  CB  VAL A1196     9956   9437  14512    799   3199    488       C  
ATOM   1610  CG1 VAL A1196       3.484  86.984  70.904  1.00 91.22           C  
ANISOU 1610  CG1 VAL A1196    10694   9430  14536    715   3507    543       C  
ATOM   1611  CG2 VAL A1196       2.036  86.654  72.904  1.00 90.37           C  
ANISOU 1611  CG2 VAL A1196    10382   9401  14552   1433   3333    907       C  
ATOM   1612  N   PHE A1197       5.557  83.826  72.479  1.00 84.97           N  
ANISOU 1612  N   PHE A1197     7951   9857  14476      2   2377   -350       N  
ATOM   1613  CA  PHE A1197       6.776  83.131  72.074  1.00 85.17           C  
ANISOU 1613  CA  PHE A1197     7491  10268  14602   -369   2175   -760       C  
ATOM   1614  C   PHE A1197       6.543  81.791  71.367  1.00 82.16           C  
ANISOU 1614  C   PHE A1197     6592  10193  14432   -110   1810   -638       C  
ATOM   1615  O   PHE A1197       7.258  81.481  70.406  1.00 82.86           O  
ANISOU 1615  O   PHE A1197     6465  10467  14549   -331   1791   -837       O  
ATOM   1616  CB  PHE A1197       7.788  82.937  73.209  1.00 86.66           C  
ANISOU 1616  CB  PHE A1197     7419  10730  14776   -648   2025  -1181       C  
ATOM   1617  CG  PHE A1197       9.167  82.575  72.705  1.00 88.85           C  
ANISOU 1617  CG  PHE A1197     7240  11460  15057  -1056   1935  -1653       C  
ATOM   1618  CD1 PHE A1197      10.092  83.568  72.400  1.00 93.07           C  
ANISOU 1618  CD1 PHE A1197     7982  12008  15373  -1687   2289  -2021       C  
ATOM   1619  CD2 PHE A1197       9.528  81.241  72.477  1.00 87.44           C  
ANISOU 1619  CD2 PHE A1197     6463  11702  15057   -813   1541  -1737       C  
ATOM   1620  CE1 PHE A1197      11.353  83.240  71.923  1.00 95.36           C  
ANISOU 1620  CE1 PHE A1197     7763  12822  15646  -2074   2230  -2480       C  
ATOM   1621  CE2 PHE A1197      10.792  80.913  71.998  1.00 89.51           C  
ANISOU 1621  CE2 PHE A1197     6269  12440  15299  -1098   1481  -2169       C  
ATOM   1622  CZ  PHE A1197      11.704  81.915  71.729  1.00 93.48           C  
ANISOU 1622  CZ  PHE A1197     6858  13053  15608  -1732   1817  -2548       C  
ATOM   1623  N   PHE A1198       5.577  80.994  71.843  1.00 79.14           N  
ANISOU 1623  N   PHE A1198     6050   9857  14161    304   1558   -341       N  
ATOM   1624  CA  PHE A1198       5.421  79.606  71.332  1.00 76.10           C  
ANISOU 1624  CA  PHE A1198     5260   9739  13916    464   1222   -278       C  
ATOM   1625  C   PHE A1198       4.552  79.359  70.076  1.00 74.39           C  
ANISOU 1625  C   PHE A1198     5042   9527  13696    592   1225     47       C  
ATOM   1626  O   PHE A1198       5.069  78.927  69.065  1.00 73.30           O  
ANISOU 1626  O   PHE A1198     4760   9508  13582    438   1178    -73       O  
ATOM   1627  CB  PHE A1198       5.130  78.618  72.478  1.00 74.49           C  
ANISOU 1627  CB  PHE A1198     4886   9640  13777    701    928   -250       C  
ATOM   1628  CG  PHE A1198       6.312  78.410  73.368  1.00 75.55           C  
ANISOU 1628  CG  PHE A1198     4868   9941  13898    591    791   -650       C  
ATOM   1629  CD1 PHE A1198       6.397  79.049  74.591  1.00 76.40           C  
ANISOU 1629  CD1 PHE A1198     5155   9946  13928    555    860   -733       C  
ATOM   1630  CD2 PHE A1198       7.389  77.627  72.937  1.00 76.53           C  
ANISOU 1630  CD2 PHE A1198     4658  10373  14046    536    605   -960       C  
ATOM   1631  CE1 PHE A1198       7.525  78.893  75.380  1.00 78.23           C  
ANISOU 1631  CE1 PHE A1198     5196  10432  14096    436    704  -1122       C  
ATOM   1632  CE2 PHE A1198       8.525  77.469  73.725  1.00 78.16           C  
ANISOU 1632  CE2 PHE A1198     4637  10871  14190    495    456  -1345       C  
ATOM   1633  CZ  PHE A1198       8.587  78.103  74.951  1.00 78.96           C  
ANISOU 1633  CZ  PHE A1198     4881  10919  14201    429    487  -1428       C  
ATOM   1634  N   ILE A1199       3.253  79.648  70.132  1.00 74.09           N  
ANISOU 1634  N   ILE A1199     5139   9414  13598    876   1283    444       N  
ATOM   1635  CA  ILE A1199       2.342  79.338  69.015  1.00 73.62           C  
ANISOU 1635  CA  ILE A1199     4993   9496  13486   1008   1225    755       C  
ATOM   1636  C   ILE A1199       2.824  79.741  67.584  1.00 74.73           C  
ANISOU 1636  C   ILE A1199     5263   9582  13550    824   1363    704       C  
ATOM   1637  O   ILE A1199       2.380  79.143  66.598  1.00 74.22           O  
ANISOU 1637  O   ILE A1199     5048   9698  13452    833   1230    857       O  
ATOM   1638  CB  ILE A1199       0.902  79.807  69.316  1.00 74.53           C  
ANISOU 1638  CB  ILE A1199     5179   9652  13487   1389   1303   1171       C  
ATOM   1639  CG1 ILE A1199       0.386  79.157  70.615  1.00 73.57           C  
ANISOU 1639  CG1 ILE A1199     4886   9632  13436   1500   1154   1206       C  
ATOM   1640  CG2 ILE A1199      -0.034  79.525  68.143  1.00 75.43           C  
ANISOU 1640  CG2 ILE A1199     5125  10048  13485   1515   1214   1474       C  
ATOM   1641  CD1 ILE A1199      -0.423  77.879  70.459  1.00 72.10           C  
ANISOU 1641  CD1 ILE A1199     4358   9788  13248   1477    894   1345       C  
ATOM   1642  N   PRO A1200       3.716  80.750  67.461  1.00 76.39           N  
ANISOU 1642  N   PRO A1200     5791   9544  13690    599   1651    476       N  
ATOM   1643  CA  PRO A1200       4.337  80.938  66.145  1.00 77.46           C  
ANISOU 1643  CA  PRO A1200     6036   9641  13755    336   1779    353       C  
ATOM   1644  C   PRO A1200       5.460  79.933  65.892  1.00 76.32           C  
ANISOU 1644  C   PRO A1200     5504   9732  13760     41   1602    -27       C  
ATOM   1645  O   PRO A1200       5.462  79.269  64.859  1.00 75.26           O  
ANISOU 1645  O   PRO A1200     5241   9719  13635    -10   1499      5       O  
ATOM   1646  CB  PRO A1200       4.889  82.374  66.202  1.00 80.62           C  
ANISOU 1646  CB  PRO A1200     6984   9678  13969    123   2206    209       C  
ATOM   1647  CG  PRO A1200       4.134  83.031  67.308  1.00 81.59           C  
ANISOU 1647  CG  PRO A1200     7371   9610  14018    435   2310    423       C  
ATOM   1648  CD  PRO A1200       3.927  81.929  68.319  1.00 78.80           C  
ANISOU 1648  CD  PRO A1200     6503   9549  13888    569   1947    401       C  
ATOM   1649  N   PHE A1201       6.411  79.827  66.822  1.00 76.98           N  
ANISOU 1649  N   PHE A1201     5412   9912  13925   -119   1569   -385       N  
ATOM   1650  CA  PHE A1201       7.387  78.724  66.816  1.00 76.42           C  
ANISOU 1650  CA  PHE A1201     4912  10156  13970   -205   1344   -716       C  
ATOM   1651  C   PHE A1201       6.658  77.421  66.458  1.00 74.05           C  
ANISOU 1651  C   PHE A1201     4452   9953  13732     56   1052   -476       C  
ATOM   1652  O   PHE A1201       7.070  76.689  65.557  1.00 73.95           O  
ANISOU 1652  O   PHE A1201     4315  10056  13727    -16    990   -577       O  
ATOM   1653  CB  PHE A1201       8.054  78.590  68.191  1.00 76.97           C  
ANISOU 1653  CB  PHE A1201     4777  10389  14080   -187   1221   -993       C  
ATOM   1654  CG  PHE A1201       9.135  77.557  68.243  1.00 77.90           C  
ANISOU 1654  CG  PHE A1201     4465  10882  14250   -155   1002  -1344       C  
ATOM   1655  CD1 PHE A1201      10.487  77.942  68.193  1.00 81.48           C  
ANISOU 1655  CD1 PHE A1201     4666  11647  14647   -474   1125  -1810       C  
ATOM   1656  CD2 PHE A1201       8.826  76.210  68.355  1.00 76.29           C  
ANISOU 1656  CD2 PHE A1201     4134  10753  14099    195    700  -1227       C  
ATOM   1657  CE1 PHE A1201      11.514  77.001  68.241  1.00 82.65           C  
ANISOU 1657  CE1 PHE A1201     4355  12244  14805   -335    922  -2139       C  
ATOM   1658  CE2 PHE A1201       9.850  75.262  68.392  1.00 78.54           C  
ANISOU 1658  CE2 PHE A1201     4108  11360  14375    347    524  -1537       C  
ATOM   1659  CZ  PHE A1201      11.197  75.656  68.339  1.00 81.07           C  
ANISOU 1659  CZ  PHE A1201     4091  12059  14652    140    620  -1986       C  
ATOM   1660  N   ILE A1202       5.558  77.158  67.164  1.00 72.36           N  
ANISOU 1660  N   ILE A1202     4283   9689  13524    313    913   -172       N  
ATOM   1661  CA  ILE A1202       4.754  76.002  66.914  1.00 70.88           C  
ANISOU 1661  CA  ILE A1202     4012   9596  13325    444    686     46       C  
ATOM   1662  C   ILE A1202       4.262  76.084  65.478  1.00 71.79           C  
ANISOU 1662  C   ILE A1202     4199   9728  13348    337    752    243       C  
ATOM   1663  O   ILE A1202       4.548  75.150  64.696  1.00 72.27           O  
ANISOU 1663  O   ILE A1202     4199   9871  13389    229    650    162       O  
ATOM   1664  CB  ILE A1202       3.633  75.858  67.958  1.00 70.17           C  
ANISOU 1664  CB  ILE A1202     3946   9496  13218    654    588    309       C  
ATOM   1665  CG1 ILE A1202       4.236  75.340  69.267  1.00 69.30           C  
ANISOU 1665  CG1 ILE A1202     3790   9377  13165    755    449     80       C  
ATOM   1666  CG2 ILE A1202       2.518  74.906  67.475  1.00 70.26           C  
ANISOU 1666  CG2 ILE A1202     3906   9656  13134    654    435    582       C  
ATOM   1667  CD1 ILE A1202       3.628  75.936  70.518  1.00 69.23           C  
ANISOU 1667  CD1 ILE A1202     3882   9268  13154    900    501    210       C  
ATOM   1668  N   PHE A1203       3.589  77.191  65.118  1.00 72.32           N  
ANISOU 1668  N   PHE A1203     4451   9706  13320    397    934    491       N  
ATOM   1669  CA  PHE A1203       3.144  77.420  63.728  1.00 73.29           C  
ANISOU 1669  CA  PHE A1203     4690   9859  13300    343    996    690       C  
ATOM   1670  C   PHE A1203       4.283  77.265  62.714  1.00 73.49           C  
ANISOU 1670  C   PHE A1203     4759   9827  13336     48   1093    396       C  
ATOM   1671  O   PHE A1203       4.308  76.288  61.964  1.00 72.77           O  
ANISOU 1671  O   PHE A1203     4570   9856  13224    -61    953    379       O  
ATOM   1672  CB  PHE A1203       2.448  78.789  63.536  1.00 75.55           C  
ANISOU 1672  CB  PHE A1203     5278  10008  13420    560   1221    971       C  
ATOM   1673  CG  PHE A1203       0.942  78.714  63.407  1.00 76.48           C  
ANISOU 1673  CG  PHE A1203     5278  10394  13387    874   1086   1402       C  
ATOM   1674  CD1 PHE A1203       0.117  79.299  64.365  1.00 77.17           C  
ANISOU 1674  CD1 PHE A1203     5381  10506  13433   1226   1144   1622       C  
ATOM   1675  CD2 PHE A1203       0.340  78.065  62.313  1.00 77.21           C  
ANISOU 1675  CD2 PHE A1203     5217  10777  13342    804    909   1575       C  
ATOM   1676  CE1 PHE A1203      -1.273  79.227  64.243  1.00 78.70           C  
ANISOU 1676  CE1 PHE A1203     5357  11085  13458   1535   1026   1996       C  
ATOM   1677  CE2 PHE A1203      -1.053  77.991  62.195  1.00 78.54           C  
ANISOU 1677  CE2 PHE A1203     5169  11351  13322   1053    766   1940       C  
ATOM   1678  CZ  PHE A1203      -1.856  78.571  63.162  1.00 79.33           C  
ANISOU 1678  CZ  PHE A1203     5204  11547  13389   1435    824   2146       C  
ATOM   1679  N   VAL A1204       5.227  78.207  62.708  1.00 74.85           N  
ANISOU 1679  N   VAL A1204     5103   9825  13510   -125   1363    145       N  
ATOM   1680  CA  VAL A1204       6.231  78.277  61.644  1.00 76.80           C  
ANISOU 1680  CA  VAL A1204     5416  10043  13722   -446   1536   -126       C  
ATOM   1681  C   VAL A1204       6.701  76.869  61.294  1.00 76.57           C  
ANISOU 1681  C   VAL A1204     5084  10226  13783   -490   1321   -297       C  
ATOM   1682  O   VAL A1204       6.664  76.476  60.117  1.00 77.37           O  
ANISOU 1682  O   VAL A1204     5264  10332  13800   -610   1330   -251       O  
ATOM   1683  CB  VAL A1204       7.442  79.187  61.988  1.00 78.71           C  
ANISOU 1683  CB  VAL A1204     5746  10200  13959   -755   1838   -525       C  
ATOM   1684  CG1 VAL A1204       8.493  79.113  60.890  1.00 80.40           C  
ANISOU 1684  CG1 VAL A1204     5942  10476  14130  -1124   2025   -843       C  
ATOM   1685  CG2 VAL A1204       7.017  80.636  62.183  1.00 80.38           C  
ANISOU 1685  CG2 VAL A1204     6469  10079  13994   -757   2141   -362       C  
ATOM   1686  N   VAL A1205       7.104  76.108  62.321  1.00 76.37           N  
ANISOU 1686  N   VAL A1205     4788  10345  13885   -354   1137   -477       N  
ATOM   1687  CA  VAL A1205       7.520  74.697  62.155  1.00 76.47           C  
ANISOU 1687  CA  VAL A1205     4629  10500  13925   -273    945   -621       C  
ATOM   1688  C   VAL A1205       6.457  73.840  61.447  1.00 75.96           C  
ANISOU 1688  C   VAL A1205     4714  10400  13748   -258    791   -303       C  
ATOM   1689  O   VAL A1205       6.789  73.107  60.501  1.00 76.40           O  
ANISOU 1689  O   VAL A1205     4832  10464  13733   -365    798   -387       O  
ATOM   1690  CB  VAL A1205       7.920  74.024  63.492  1.00 75.69           C  
ANISOU 1690  CB  VAL A1205     4334  10519  13905    -13    751   -788       C  
ATOM   1691  CG1 VAL A1205       8.304  72.567  63.253  1.00 75.67           C  
ANISOU 1691  CG1 VAL A1205     4318  10583  13850    158    597   -902       C  
ATOM   1692  CG2 VAL A1205       9.070  74.778  64.142  1.00 77.64           C  
ANISOU 1692  CG2 VAL A1205     4359  10928  14211    -88    873  -1158       C  
ATOM   1693  N   THR A1206       5.198  73.939  61.900  1.00 75.35           N  
ANISOU 1693  N   THR A1206     4684  10323  13621   -157    672     39       N  
ATOM   1694  CA  THR A1206       4.105  73.168  61.294  1.00 76.21           C  
ANISOU 1694  CA  THR A1206     4870  10519  13567   -237    523    319       C  
ATOM   1695  C   THR A1206       4.040  73.487  59.801  1.00 78.33           C  
ANISOU 1695  C   THR A1206     5270  10791  13702   -439    625    401       C  
ATOM   1696  O   THR A1206       3.810  72.598  58.961  1.00 78.96           O  
ANISOU 1696  O   THR A1206     5445  10921  13634   -622    545    442       O  
ATOM   1697  CB  THR A1206       2.718  73.451  61.917  1.00 75.72           C  
ANISOU 1697  CB  THR A1206     4738  10597  13436   -122    421    665       C  
ATOM   1698  OG1 THR A1206       2.819  73.584  63.347  1.00 74.86           O  
ANISOU 1698  OG1 THR A1206     4554  10429  13459     78    396    596       O  
ATOM   1699  CG2 THR A1206       1.749  72.322  61.566  1.00 75.80           C  
ANISOU 1699  CG2 THR A1206     4756  10799  13245   -308    243    840       C  
ATOM   1700  N   PHE A1207       4.271  74.758  59.480  1.00 79.57           N  
ANISOU 1700  N   PHE A1207     5514  10853  13867   -430    829    414       N  
ATOM   1701  CA  PHE A1207       4.257  75.197  58.100  1.00 81.53           C  
ANISOU 1701  CA  PHE A1207     5973  11050  13952   -594    956    492       C  
ATOM   1702  C   PHE A1207       5.449  74.665  57.322  1.00 82.26           C  
ANISOU 1702  C   PHE A1207     6115  11063  14079   -835   1078    152       C  
ATOM   1703  O   PHE A1207       5.315  74.277  56.164  1.00 82.79           O  
ANISOU 1703  O   PHE A1207     6336  11132  13990  -1012   1078    212       O  
ATOM   1704  CB  PHE A1207       4.216  76.715  58.008  1.00 83.00           C  
ANISOU 1704  CB  PHE A1207     6396  11068  14071   -505   1197    588       C  
ATOM   1705  CG  PHE A1207       3.867  77.210  56.644  1.00 85.57           C  
ANISOU 1705  CG  PHE A1207     7025  11340  14146   -573   1291    779       C  
ATOM   1706  CD1 PHE A1207       2.538  77.259  56.229  1.00 86.81           C  
ANISOU 1706  CD1 PHE A1207     7185  11725  14076   -364   1106   1192       C  
ATOM   1707  CD2 PHE A1207       4.870  77.602  55.758  1.00 86.85           C  
ANISOU 1707  CD2 PHE A1207     7454  11283  14262   -851   1564    531       C  
ATOM   1708  CE1 PHE A1207       2.219  77.702  54.955  1.00 89.67           C  
ANISOU 1708  CE1 PHE A1207     7842  12074  14154   -375   1159   1377       C  
ATOM   1709  CE2 PHE A1207       4.560  78.051  54.491  1.00 88.93           C  
ANISOU 1709  CE2 PHE A1207     8078  11455  14257   -910   1658    709       C  
ATOM   1710  CZ  PHE A1207       3.233  78.095  54.085  1.00 90.48           C  
ANISOU 1710  CZ  PHE A1207     8306  11859  14214   -644   1437   1144       C  
ATOM   1711  N   VAL A1208       6.607  74.647  57.978  1.00 83.05           N  
ANISOU 1711  N   VAL A1208     6058  11144  14353   -827   1182   -212       N  
ATOM   1712  CA  VAL A1208       7.885  74.327  57.331  1.00 84.73           C  
ANISOU 1712  CA  VAL A1208     6227  11372  14594  -1004   1355   -589       C  
ATOM   1713  C   VAL A1208       8.086  72.828  57.186  1.00 85.40           C  
ANISOU 1713  C   VAL A1208     6266  11523  14658   -911   1196   -679       C  
ATOM   1714  O   VAL A1208       8.595  72.366  56.161  1.00 86.44           O  
ANISOU 1714  O   VAL A1208     6509  11628  14705  -1055   1311   -814       O  
ATOM   1715  CB  VAL A1208       9.072  74.952  58.099  1.00 85.07           C  
ANISOU 1715  CB  VAL A1208     6037  11513  14774  -1039   1530   -977       C  
ATOM   1716  CG1 VAL A1208      10.368  74.210  57.816  1.00 86.85           C  
ANISOU 1716  CG1 VAL A1208     6014  11947  15039  -1064   1608  -1396       C  
ATOM   1717  CG2 VAL A1208       9.208  76.421  57.744  1.00 86.58           C  
ANISOU 1717  CG2 VAL A1208     6470  11543  14882  -1310   1844   -997       C  
HETATM 1718  N   MSE A1209       7.688  72.077  58.217  1.00 85.81           N  
ANISOU 1718  N   MSE A1209     6239  11616  14749   -669    967   -606       N  
HETATM 1719  CA  MSE A1209       7.902  70.627  58.257  1.00 87.59           C  
ANISOU 1719  CA  MSE A1209     6569  11820  14893   -527    852   -697       C  
HETATM 1720  C   MSE A1209       6.917  69.999  57.288  1.00 88.04           C  
ANISOU 1720  C   MSE A1209     6945  11782  14725   -774    786   -429       C  
HETATM 1721  O   MSE A1209       7.215  68.979  56.658  1.00 89.18           O  
ANISOU 1721  O   MSE A1209     7336  11829  14720   -820    820   -526       O  
HETATM 1722  CB  MSE A1209       7.832  70.127  59.707  1.00 87.98           C  
ANISOU 1722  CB  MSE A1209     6533  11895  15001   -207    666   -717       C  
HETATM 1723  CG  MSE A1209       7.844  68.604  59.886  1.00 92.00           C  
ANISOU 1723  CG  MSE A1209     7339  12280  15337    -17    558   -749       C  
HETATM 1724 SE   MSE A1209       9.468  67.705  59.172  1.00 99.10          SE  
ANISOU 1724 SE   MSE A1209     8292  13208  16154    263    729  -1166      SE  
HETATM 1725  CE  MSE A1209      10.628  68.013  60.732  1.00 98.62           C  
ANISOU 1725  CE  MSE A1209     7741  13469  16260    794    632  -1493       C  
ATOM   1726  N   ILE A1210       5.749  70.623  57.134  1.00 87.03           N  
ANISOU 1726  N   ILE A1210     6820  11717  14529   -926    704   -100       N  
ATOM   1727  CA  ILE A1210       4.788  70.183  56.128  1.00 87.46           C  
ANISOU 1727  CA  ILE A1210     7090  11820  14322  -1217    624    145       C  
ATOM   1728  C   ILE A1210       5.304  70.600  54.762  1.00 89.21           C  
ANISOU 1728  C   ILE A1210     7456  11971  14470  -1412    806     71       C  
ATOM   1729  O   ILE A1210       5.384  69.771  53.861  1.00 91.81           O  
ANISOU 1729  O   ILE A1210     8043  12228  14611  -1626    833     28       O  
ATOM   1730  CB  ILE A1210       3.363  70.725  56.401  1.00 86.79           C  
ANISOU 1730  CB  ILE A1210     6865  11971  14141  -1244    458    515       C  
ATOM   1731  CG1 ILE A1210       2.612  69.772  57.341  1.00 85.61           C  
ANISOU 1731  CG1 ILE A1210     6706  11912  13910  -1267    282    598       C  
ATOM   1732  CG2 ILE A1210       2.592  70.928  55.102  1.00 88.56           C  
ANISOU 1732  CG2 ILE A1210     7191  12364  14094  -1500    416    749       C  
ATOM   1733  CD1 ILE A1210       1.373  70.368  57.974  1.00 85.51           C  
ANISOU 1733  CD1 ILE A1210     6427  12200  13863  -1196    154    895       C  
ATOM   1734  N   ASN A1211       5.681  71.871  54.618  1.00 89.78           N  
ANISOU 1734  N   ASN A1211     7443  12019  14652  -1368    969     40       N  
ATOM   1735  CA  ASN A1211       6.216  72.378  53.333  1.00 91.85           C  
ANISOU 1735  CA  ASN A1211     7911  12171  14816  -1585   1195    -48       C  
ATOM   1736  C   ASN A1211       7.397  71.600  52.751  1.00 92.64           C  
ANISOU 1736  C   ASN A1211     8090  12178  14931  -1688   1374   -403       C  
ATOM   1737  O   ASN A1211       7.510  71.455  51.529  1.00 94.28           O  
ANISOU 1737  O   ASN A1211     8559  12298  14965  -1929   1492   -412       O  
ATOM   1738  CB  ASN A1211       6.515  73.885  53.372  1.00 91.75           C  
ANISOU 1738  CB  ASN A1211     7921  12073  14866  -1562   1412    -67       C  
ATOM   1739  CG  ASN A1211       5.573  74.665  52.483  1.00 93.68           C  
ANISOU 1739  CG  ASN A1211     8447  12295  14853  -1604   1402    282       C  
ATOM   1740  OD1 ASN A1211       5.663  74.577  51.255  1.00 94.98           O  
ANISOU 1740  OD1 ASN A1211     8878  12387  14823  -1824   1487    293       O  
ATOM   1741  ND2 ASN A1211       4.639  75.408  53.087  1.00 93.27           N  
ANISOU 1741  ND2 ASN A1211     8353  12325  14761  -1345   1295    582       N  
ATOM   1742  N   LEU A1212       8.260  71.104  53.633  1.00 91.83           N  
ANISOU 1742  N   LEU A1212     7764  12122  15006  -1459   1393   -688       N  
ATOM   1743  CA  LEU A1212       9.333  70.203  53.248  1.00 93.54           C  
ANISOU 1743  CA  LEU A1212     8013  12323  15206  -1395   1537  -1013       C  
ATOM   1744  C   LEU A1212       8.787  68.990  52.458  1.00 94.83           C  
ANISOU 1744  C   LEU A1212     8595  12328  15107  -1524   1463   -873       C  
ATOM   1745  O   LEU A1212       9.358  68.593  51.430  1.00 96.14           O  
ANISOU 1745  O   LEU A1212     8980  12398  15150  -1655   1659  -1027       O  
ATOM   1746  CB  LEU A1212      10.088  69.755  54.502  1.00 92.72           C  
ANISOU 1746  CB  LEU A1212     7604  12363  15261   -992   1473  -1260       C  
ATOM   1747  CG  LEU A1212      11.422  69.051  54.289  1.00 95.16           C  
ANISOU 1747  CG  LEU A1212     7806  12790  15561   -759   1648  -1652       C  
ATOM   1748  CD1 LEU A1212      12.335  69.274  55.482  1.00 96.34           C  
ANISOU 1748  CD1 LEU A1212     7466  13259  15880   -407   1617  -1943       C  
ATOM   1749  CD2 LEU A1212      11.216  67.572  54.035  1.00 96.35           C  
ANISOU 1749  CD2 LEU A1212     8385  12730  15492   -571   1583  -1590       C  
ATOM   1750  N   VAL A1213       7.677  68.422  52.939  1.00 93.90           N  
ANISOU 1750  N   VAL A1213     8612  12193  14872  -1542   1211   -601       N  
ATOM   1751  CA  VAL A1213       7.089  67.226  52.340  1.00 95.52           C  
ANISOU 1751  CA  VAL A1213     9268  12260  14766  -1766   1150   -490       C  
ATOM   1752  C   VAL A1213       6.429  67.559  51.007  1.00 96.94           C  
ANISOU 1752  C   VAL A1213     9647  12466  14718  -2202   1159   -293       C  
ATOM   1753  O   VAL A1213       6.575  66.805  50.030  1.00 99.23           O  
ANISOU 1753  O   VAL A1213    10338  12599  14764  -2437   1267   -353       O  
ATOM   1754  CB  VAL A1213       6.076  66.541  53.278  1.00 94.95           C  
ANISOU 1754  CB  VAL A1213     9287  12211  14580  -1773    914   -293       C  
ATOM   1755  CG1 VAL A1213       5.599  65.214  52.684  1.00 97.48           C  
ANISOU 1755  CG1 VAL A1213    10183  12347  14506  -2098    919   -249       C  
ATOM   1756  CG2 VAL A1213       6.695  66.324  54.649  1.00 94.26           C  
ANISOU 1756  CG2 VAL A1213     9030  12089  14695  -1302    884   -463       C  
ATOM   1757  N   VAL A1214       5.718  68.688  50.964  1.00 95.68           N  
ANISOU 1757  N   VAL A1214     9258  12496  14598  -2267   1054    -55       N  
ATOM   1758  CA  VAL A1214       5.120  69.185  49.706  1.00 96.90           C  
ANISOU 1758  CA  VAL A1214     9586  12724  14506  -2576   1043    150       C  
ATOM   1759  C   VAL A1214       6.154  69.284  48.546  1.00 98.12           C  
ANISOU 1759  C   VAL A1214    10005  12655  14621  -2717   1342    -83       C  
ATOM   1760  O   VAL A1214       5.797  69.089  47.379  1.00 99.04           O  
ANISOU 1760  O   VAL A1214    10441  12746  14444  -3035   1347     21       O  
ATOM   1761  CB  VAL A1214       4.403  70.540  49.913  1.00 95.85           C  
ANISOU 1761  CB  VAL A1214     9212  12792  14414  -2435    942    420       C  
ATOM   1762  CG1 VAL A1214       3.736  71.002  48.622  1.00 97.44           C  
ANISOU 1762  CG1 VAL A1214     9633  13105  14286  -2655    893    661       C  
ATOM   1763  CG2 VAL A1214       3.393  70.443  51.050  1.00 93.91           C  
ANISOU 1763  CG2 VAL A1214     8673  12807  14203  -2282    683    635       C  
ATOM   1764  N   ALA A1215       7.419  69.574  48.877  1.00 97.21           N  
ANISOU 1764  N   ALA A1215     9731  12434  14769  -2509   1593   -413       N  
ATOM   1765  CA  ALA A1215       8.506  69.593  47.886  1.00 99.26           C  
ANISOU 1765  CA  ALA A1215    10171  12543  15000  -2644   1927   -698       C  
ATOM   1766  C   ALA A1215       9.064  68.192  47.581  1.00100.46           C  
ANISOU 1766  C   ALA A1215    10578  12556  15034  -2612   2029   -905       C  
ATOM   1767  O   ALA A1215       9.541  67.933  46.464  1.00101.81           O  
ANISOU 1767  O   ALA A1215    11059  12583  15042  -2817   2260  -1033       O  
ATOM   1768  CB  ALA A1215       9.627  70.536  48.316  1.00 99.55           C  
ANISOU 1768  CB  ALA A1215     9879  12639  15306  -2512   2185  -1002       C  
ATOM   1769  N   ILE A1216       9.002  67.302  48.574  1.00 99.29           N  
ANISOU 1769  N   ILE A1216    10379  12415  14932  -2331   1886   -931       N  
ATOM   1770  CA  ILE A1216       9.370  65.889  48.386  1.00101.30           C  
ANISOU 1770  CA  ILE A1216    11042  12460  14987  -2227   1982  -1074       C  
ATOM   1771  C   ILE A1216       8.325  65.165  47.508  1.00101.77           C  
ANISOU 1771  C   ILE A1216    11668  12358  14642  -2704   1885   -831       C  
ATOM   1772  O   ILE A1216       8.671  64.279  46.723  1.00103.89           O  
ANISOU 1772  O   ILE A1216    12440  12380  14655  -2816   2079   -949       O  
ATOM   1773  CB  ILE A1216       9.563  65.158  49.749  1.00101.34           C  
ANISOU 1773  CB  ILE A1216    10957  12466  15083  -1755   1865  -1153       C  
ATOM   1774  CG1 ILE A1216      10.738  65.747  50.533  1.00101.19           C  
ANISOU 1774  CG1 ILE A1216    10367  12688  15394  -1294   1963  -1449       C  
ATOM   1775  CG2 ILE A1216       9.795  63.660  49.563  1.00104.76           C  
ANISOU 1775  CG2 ILE A1216    12009  12588  15206  -1610   1982  -1248       C  
ATOM   1776  CD1 ILE A1216      12.110  65.327  50.030  1.00105.10           C  
ANISOU 1776  CD1 ILE A1216    10845  13220  15870  -1008   2280  -1824       C  
ATOM   1777  N   ILE A1217       7.051  65.545  47.647  1.00 99.55           N  
ANISOU 1777  N   ILE A1217    11294  12262  14268  -2988   1596   -507       N  
ATOM   1778  CA  ILE A1217       5.987  65.053  46.758  1.00100.57           C  
ANISOU 1778  CA  ILE A1217    11825  12414  13973  -3532   1468   -283       C  
ATOM   1779  C   ILE A1217       6.300  65.382  45.294  1.00101.52           C  
ANISOU 1779  C   ILE A1217    12205  12443  13925  -3816   1647   -318       C  
ATOM   1780  O   ILE A1217       6.064  64.559  44.399  1.00103.70           O  
ANISOU 1780  O   ILE A1217    13011  12568  13823  -4208   1706   -312       O  
ATOM   1781  CB  ILE A1217       4.590  65.628  47.134  1.00 99.66           C  
ANISOU 1781  CB  ILE A1217    11378  12701  13789  -3721   1118     62       C  
ATOM   1782  CG1 ILE A1217       4.155  65.140  48.524  1.00 98.99           C  
ANISOU 1782  CG1 ILE A1217    11133  12685  13792  -3551    962     98       C  
ATOM   1783  CG2 ILE A1217       3.539  65.245  46.094  1.00101.90           C  
ANISOU 1783  CG2 ILE A1217    11958  13171  13588  -4316    967    266       C  
ATOM   1784  CD1 ILE A1217       3.146  66.038  49.223  1.00 97.42           C  
ANISOU 1784  CD1 ILE A1217    10404  12907  13704  -3481    693    369       C  
ATOM   1785  N   VAL A1218       6.841  66.584  45.077  1.00 99.53           N  
ANISOU 1785  N   VAL A1218    11648  12251  13916  -3656   1763   -367       N  
ATOM   1786  CA  VAL A1218       7.075  67.121  43.749  1.00100.46           C  
ANISOU 1786  CA  VAL A1218    12016  12283  13871  -3923   1936   -375       C  
ATOM   1787  C   VAL A1218       8.366  66.555  43.157  1.00101.93           C  
ANISOU 1787  C   VAL A1218    12482  12177  14071  -3881   2338   -738       C  
ATOM   1788  O   VAL A1218       8.366  66.043  42.027  1.00104.30           O  
ANISOU 1788  O   VAL A1218    13282  12292  14053  -4214   2468   -755       O  
ATOM   1789  CB  VAL A1218       7.078  68.677  43.758  1.00 99.61           C  
ANISOU 1789  CB  VAL A1218    11607  12301  13939  -3804   1948   -277       C  
ATOM   1790  CG1 VAL A1218       7.388  69.257  42.371  1.00101.57           C  
ANISOU 1790  CG1 VAL A1218    12226  12392  13975  -4079   2174   -300       C  
ATOM   1791  CG2 VAL A1218       5.745  69.209  44.274  1.00 98.49           C  
ANISOU 1791  CG2 VAL A1218    11217  12478  13725  -3751   1566    106       C  
ATOM   1792  N   ASP A1219       9.456  66.635  43.921  1.00100.66           N  
ANISOU 1792  N   ASP A1219    11979  12022  14244  -3465   2532  -1034       N  
ATOM   1793  CA  ASP A1219      10.779  66.258  43.409  1.00102.54           C  
ANISOU 1793  CA  ASP A1219    12325  12124  14513  -3333   2940  -1411       C  
ATOM   1794  C   ASP A1219      10.975  64.753  43.427  1.00104.48           C  
ANISOU 1794  C   ASP A1219    13006  12145  14547  -3166   3016  -1511       C  
ATOM   1795  O   ASP A1219      11.001  64.123  42.375  1.00107.47           O  
ANISOU 1795  O   ASP A1219    13950  12272  14611  -3432   3196  -1537       O  
ATOM   1796  CB  ASP A1219      11.895  66.945  44.200  1.00101.67           C  
ANISOU 1796  CB  ASP A1219    11601  12248  14780  -2964   3116  -1721       C  
ATOM   1797  CG  ASP A1219      11.944  68.450  43.972  1.00100.43           C  
ANISOU 1797  CG  ASP A1219    11210  12200  14749  -3210   3200  -1705       C  
ATOM   1798  OD1 ASP A1219      10.984  69.021  43.397  1.00 99.63           O  
ANISOU 1798  OD1 ASP A1219    11378  12006  14469  -3521   3049  -1387       O  
ATOM   1799  OD2 ASP A1219      12.955  69.062  44.382  1.00100.76           O  
ANISOU 1799  OD2 ASP A1219    10823  12442  15021  -3086   3431  -2021       O  
TER    1800      ASP A1219                                                      
HETATM 1801  N   MSE B1001     -29.536  16.522  43.205  1.00153.94           N  
ANISOU 1801  N   MSE B1001    20041  14816  23632  -1082   -393  -3327       N  
HETATM 1802  CA  MSE B1001     -29.410  17.748  44.054  1.00149.37           C  
ANISOU 1802  CA  MSE B1001    18970  14626  23157   -840   -656  -3054       C  
HETATM 1803  C   MSE B1001     -28.187  18.570  43.708  1.00145.01           C  
ANISOU 1803  C   MSE B1001    18083  14422  22593   -300   -933  -2892       C  
HETATM 1804  O   MSE B1001     -28.034  19.689  44.203  1.00140.59           O  
ANISOU 1804  O   MSE B1001    17111  14220  22085   -163  -1140  -2714       O  
HETATM 1805  CB  MSE B1001     -29.366  17.355  45.529  1.00151.85           C  
ANISOU 1805  CB  MSE B1001    19721  14538  23438   -701   -457  -2823       C  
HETATM 1806  CG  MSE B1001     -29.798  18.522  46.413  1.00149.71           C  
ANISOU 1806  CG  MSE B1001    18937  14654  23290   -746   -648  -2650       C  
HETATM 1807 SE   MSE B1001     -28.746  18.562  48.076  1.00152.04          SE  
ANISOU 1807 SE   MSE B1001    19563  14703  23502    -76   -639  -2222      SE  
HETATM 1808  CE  MSE B1001     -26.943  18.779  47.312  1.00148.78           C  
ANISOU 1808  CE  MSE B1001    18951  14590  22988    693   -890  -2183       C  
ATOM   1809  N   TYR B1002     -27.318  18.022  42.856  1.00146.01           N  
ANISOU 1809  N   TYR B1002    18398  14456  22623    -43   -899  -2996       N  
ATOM   1810  CA  TYR B1002     -26.104  18.710  42.383  1.00143.33           C  
ANISOU 1810  CA  TYR B1002    17728  14505  22227    368  -1088  -2961       C  
ATOM   1811  C   TYR B1002     -26.425  20.029  41.678  1.00139.16           C  
ANISOU 1811  C   TYR B1002    16683  14471  21719    108  -1322  -2997       C  
ATOM   1812  O   TYR B1002     -25.645  20.986  41.733  1.00135.81           O  
ANISOU 1812  O   TYR B1002    15966  14395  21238    303  -1446  -2913       O  
ATOM   1813  CB  TYR B1002     -25.319  17.799  41.432  1.00146.65           C  
ANISOU 1813  CB  TYR B1002    18433  14759  22527    594   -977  -3159       C  
ATOM   1814  CG  TYR B1002     -23.911  18.267  41.107  1.00146.77           C  
ANISOU 1814  CG  TYR B1002    18143  15183  22438   1046  -1087  -3206       C  
ATOM   1815  CD1 TYR B1002     -22.833  17.916  41.922  1.00149.21           C  
ANISOU 1815  CD1 TYR B1002    18536  15519  22636   1685  -1073  -3153       C  
ATOM   1816  CD2 TYR B1002     -23.653  19.043  39.973  1.00145.02           C  
ANISOU 1816  CD2 TYR B1002    17567  15361  22174    834  -1187  -3359       C  
ATOM   1817  CE1 TYR B1002     -21.543  18.334  41.627  1.00149.39           C  
ANISOU 1817  CE1 TYR B1002    18166  16062  22533   2051  -1150  -3316       C  
ATOM   1818  CE2 TYR B1002     -22.365  19.467  39.671  1.00144.98           C  
ANISOU 1818  CE2 TYR B1002    17275  15772  22038   1121  -1209  -3486       C  
ATOM   1819  CZ  TYR B1002     -21.317  19.108  40.500  1.00147.45           C  
ANISOU 1819  CZ  TYR B1002    17548  16209  22267   1704  -1187  -3497       C  
ATOM   1820  OH  TYR B1002     -20.040  19.518  40.201  1.00148.83           O  
ANISOU 1820  OH  TYR B1002    17328  16936  22284   1944  -1189  -3737       O  
ATOM   1821  N   LEU B1003     -27.580  20.063  41.019  1.00138.53           N  
ANISOU 1821  N   LEU B1003    16544  14429  21663   -326  -1364  -3162       N  
ATOM   1822  CA  LEU B1003     -28.029  21.232  40.278  1.00135.90           C  
ANISOU 1822  CA  LEU B1003    15868  14509  21259   -477  -1610  -3215       C  
ATOM   1823  C   LEU B1003     -28.821  22.201  41.162  1.00133.65           C  
ANISOU 1823  C   LEU B1003    15321  14431  21029   -538  -1760  -3065       C  
ATOM   1824  O   LEU B1003     -28.575  23.412  41.144  1.00130.50           O  
ANISOU 1824  O   LEU B1003    14752  14297  20536   -409  -1930  -2936       O  
ATOM   1825  CB  LEU B1003     -28.879  20.791  39.079  1.00136.97           C  
ANISOU 1825  CB  LEU B1003    16032  14687  21325   -803  -1639  -3529       C  
ATOM   1826  CG  LEU B1003     -28.183  20.130  37.884  1.00138.48           C  
ANISOU 1826  CG  LEU B1003    16437  14766  21412   -775  -1548  -3710       C  
ATOM   1827  CD1 LEU B1003     -29.111  19.126  37.212  1.00141.95           C  
ANISOU 1827  CD1 LEU B1003    17023  15073  21840  -1165  -1437  -4037       C  
ATOM   1828  CD2 LEU B1003     -27.691  21.168  36.882  1.00136.13           C  
ANISOU 1828  CD2 LEU B1003    16012  14789  20923   -681  -1736  -3722       C  
ATOM   1829  N   ARG B1004     -29.754  21.649  41.941  1.00135.13           N  
ANISOU 1829  N   ARG B1004    15537  14472  21335   -763  -1651  -3107       N  
ATOM   1830  CA  ARG B1004     -30.762  22.425  42.668  1.00133.99           C  
ANISOU 1830  CA  ARG B1004    15099  14574  21238   -884  -1779  -3072       C  
ATOM   1831  C   ARG B1004     -30.170  23.466  43.607  1.00132.40           C  
ANISOU 1831  C   ARG B1004    14785  14468  21054   -589  -1876  -2743       C  
ATOM   1832  O   ARG B1004     -30.482  24.649  43.482  1.00132.37           O  
ANISOU 1832  O   ARG B1004    14569  14767  20956   -510  -2097  -2695       O  
ATOM   1833  CB  ARG B1004     -31.695  21.492  43.442  1.00136.33           C  
ANISOU 1833  CB  ARG B1004    15498  14661  21638  -1256  -1535  -3218       C  
ATOM   1834  CG  ARG B1004     -32.970  22.144  43.948  1.00135.72           C  
ANISOU 1834  CG  ARG B1004    15018  14961  21586  -1475  -1652  -3354       C  
ATOM   1835  CD  ARG B1004     -33.773  21.144  44.759  1.00138.98           C  
ANISOU 1835  CD  ARG B1004    15592  15144  22071  -1957  -1303  -3545       C  
ATOM   1836  NE  ARG B1004     -34.938  21.743  45.402  1.00139.04           N  
ANISOU 1836  NE  ARG B1004    15158  15568  22105  -2176  -1375  -3716       N  
ATOM   1837  CZ  ARG B1004     -35.541  21.236  46.474  1.00141.30           C  
ANISOU 1837  CZ  ARG B1004    15551  15690  22447  -2565  -1065  -3798       C  
ATOM   1838  NH1 ARG B1004     -35.084  20.122  47.036  1.00142.47           N  
ANISOU 1838  NH1 ARG B1004    16353  15186  22595  -2742   -663  -3680       N  
ATOM   1839  NH2 ARG B1004     -36.598  21.848  46.992  1.00142.37           N  
ANISOU 1839  NH2 ARG B1004    15197  16305  22594  -2748  -1145  -4011       N  
ATOM   1840  N   ILE B1005     -29.322  23.021  44.536  1.00132.87           N  
ANISOU 1840  N   ILE B1005    15035  14268  21181   -394  -1711  -2539       N  
ATOM   1841  CA  ILE B1005     -28.663  23.914  45.501  1.00130.18           C  
ANISOU 1841  CA  ILE B1005    14568  14054  20840   -138  -1775  -2269       C  
ATOM   1842  C   ILE B1005     -27.934  25.084  44.829  1.00128.45           C  
ANISOU 1842  C   ILE B1005    14198  14142  20465    -17  -1923  -2240       C  
ATOM   1843  O   ILE B1005     -28.018  26.221  45.305  1.00125.66           O  
ANISOU 1843  O   ILE B1005    13710  13976  20058      9  -2023  -2103       O  
ATOM   1844  CB  ILE B1005     -27.688  23.160  46.445  1.00131.59           C  
ANISOU 1844  CB  ILE B1005    14981  13982  21034    169  -1612  -2120       C  
ATOM   1845  CG1 ILE B1005     -26.703  22.294  45.645  1.00134.64           C  
ANISOU 1845  CG1 ILE B1005    15580  14248  21330    395  -1527  -2254       C  
ATOM   1846  CG2 ILE B1005     -28.459  22.328  47.464  1.00132.96           C  
ANISOU 1846  CG2 ILE B1005    15436  13792  21290     30  -1430  -2066       C  
ATOM   1847  CD1 ILE B1005     -25.353  22.106  46.310  1.00137.55           C  
ANISOU 1847  CD1 ILE B1005    15982  14680  21601    902  -1502  -2168       C  
ATOM   1848  N   THR B1006     -27.240  24.793  43.725  1.00128.98           N  
ANISOU 1848  N   THR B1006    14355  14227  20425     15  -1893  -2390       N  
ATOM   1849  CA  THR B1006     -26.507  25.792  42.938  1.00128.18           C  
ANISOU 1849  CA  THR B1006    14223  14368  20111     21  -1944  -2427       C  
ATOM   1850  C   THR B1006     -27.445  26.874  42.402  1.00127.36           C  
ANISOU 1850  C   THR B1006    14153  14386  19853    -99  -2132  -2425       C  
ATOM   1851  O   THR B1006     -27.106  28.057  42.426  1.00127.86           O  
ANISOU 1851  O   THR B1006    14288  14572  19719    -93  -2156  -2334       O  
ATOM   1852  CB  THR B1006     -25.755  25.147  41.752  1.00131.33           C  
ANISOU 1852  CB  THR B1006    14735  14752  20413     26  -1853  -2643       C  
ATOM   1853  OG1 THR B1006     -25.200  23.885  42.151  1.00135.34           O  
ANISOU 1853  OG1 THR B1006    15305  15078  21041    235  -1714  -2685       O  
ATOM   1854  CG2 THR B1006     -24.633  26.049  41.267  1.00130.61           C  
ANISOU 1854  CG2 THR B1006    14618  14922  20086     -5  -1782  -2712       C  
ATOM   1855  N   ASN B1007     -28.622  26.466  41.928  1.00127.71           N  
ANISOU 1855  N   ASN B1007    14178  14413  19933   -191  -2256  -2564       N  
ATOM   1856  CA  ASN B1007     -29.648  27.417  41.489  1.00127.39           C  
ANISOU 1856  CA  ASN B1007    14138  14566  19699   -153  -2502  -2613       C  
ATOM   1857  C   ASN B1007     -30.528  27.945  42.636  1.00126.49           C  
ANISOU 1857  C   ASN B1007    13823  14556  19679    -94  -2600  -2503       C  
ATOM   1858  O   ASN B1007     -31.652  28.416  42.410  1.00127.28           O  
ANISOU 1858  O   ASN B1007    13820  14883  19658     -6  -2826  -2634       O  
ATOM   1859  CB  ASN B1007     -30.481  26.842  40.335  1.00129.32           C  
ANISOU 1859  CB  ASN B1007    14368  14909  19859   -235  -2632  -2913       C  
ATOM   1860  CG  ASN B1007     -29.868  27.137  38.971  1.00130.46           C  
ANISOU 1860  CG  ASN B1007    14809  15046  19715   -196  -2664  -2993       C  
ATOM   1861  OD1 ASN B1007     -29.828  28.290  38.527  1.00129.47           O  
ANISOU 1861  OD1 ASN B1007    14944  14983  19263    -40  -2792  -2921       O  
ATOM   1862  ND2 ASN B1007     -29.394  26.093  38.296  1.00131.61           N  
ANISOU 1862  ND2 ASN B1007    15000  15070  19936   -338  -2518  -3149       N  
ATOM   1863  N   ILE B1008     -29.997  27.844  43.858  1.00124.24           N  
ANISOU 1863  N   ILE B1008    13471  14154  19581    -98  -2441  -2299       N  
ATOM   1864  CA  ILE B1008     -30.498  28.565  45.030  1.00123.22           C  
ANISOU 1864  CA  ILE B1008    13210  14102  19508    -33  -2492  -2136       C  
ATOM   1865  C   ILE B1008     -29.360  29.454  45.548  1.00123.00           C  
ANISOU 1865  C   ILE B1008    13307  14049  19377     52  -2399  -1907       C  
ATOM   1866  O   ILE B1008     -29.584  30.598  45.950  1.00122.79           O  
ANISOU 1866  O   ILE B1008    13347  14097  19210    134  -2475  -1786       O  
ATOM   1867  CB  ILE B1008     -30.946  27.618  46.173  1.00123.24           C  
ANISOU 1867  CB  ILE B1008    13050  13984  19790   -173  -2347  -2122       C  
ATOM   1868  CG1 ILE B1008     -31.695  26.392  45.627  1.00126.71           C  
ANISOU 1868  CG1 ILE B1008    13456  14369  20319   -418  -2277  -2414       C  
ATOM   1869  CG2 ILE B1008     -31.794  28.373  47.194  1.00120.88           C  
ANISOU 1869  CG2 ILE B1008    12565  13836  19526   -144  -2430  -2042       C  
ATOM   1870  CD1 ILE B1008     -31.764  25.215  46.589  1.00127.62           C  
ANISOU 1870  CD1 ILE B1008    13683  14180  20626   -616  -2000  -2398       C  
ATOM   1871  N   VAL B1009     -28.141  28.910  45.524  1.00122.89           N  
ANISOU 1871  N   VAL B1009    13322  13970  19401     35  -2223  -1901       N  
ATOM   1872  CA  VAL B1009     -26.927  29.606  45.968  1.00121.00           C  
ANISOU 1872  CA  VAL B1009    13096  13839  19040     47  -2093  -1811       C  
ATOM   1873  C   VAL B1009     -26.696  30.936  45.235  1.00120.93           C  
ANISOU 1873  C   VAL B1009    13366  13899  18684    -57  -2090  -1830       C  
ATOM   1874  O   VAL B1009     -26.475  31.966  45.874  1.00122.59           O  
ANISOU 1874  O   VAL B1009    13659  14161  18759   -107  -2030  -1717       O  
ATOM   1875  CB  VAL B1009     -25.684  28.682  45.851  1.00122.70           C  
ANISOU 1875  CB  VAL B1009    13222  14100  19296    117  -1937  -1930       C  
ATOM   1876  CG1 VAL B1009     -24.379  29.459  46.016  1.00122.77           C  
ANISOU 1876  CG1 VAL B1009    13151  14395  19100     56  -1788  -1999       C  
ATOM   1877  CG2 VAL B1009     -25.764  27.556  46.876  1.00124.01           C  
ANISOU 1877  CG2 VAL B1009    13302  14120  19698    308  -1905  -1849       C  
ATOM   1878  N   GLU B1010     -26.761  30.912  43.906  1.00120.00           N  
ANISOU 1878  N   GLU B1010    13478  13739  18380   -105  -2126  -1977       N  
ATOM   1879  CA  GLU B1010     -26.512  32.103  43.086  1.00120.42           C  
ANISOU 1879  CA  GLU B1010    13989  13758  18009   -210  -2077  -2003       C  
ATOM   1880  C   GLU B1010     -27.674  33.115  43.027  1.00120.89           C  
ANISOU 1880  C   GLU B1010    14373  13721  17836    -11  -2296  -1890       C  
ATOM   1881  O   GLU B1010     -27.551  34.173  42.396  1.00121.38           O  
ANISOU 1881  O   GLU B1010    15004  13655  17459    -28  -2250  -1879       O  
ATOM   1882  CB  GLU B1010     -26.122  31.676  41.668  1.00122.09           C  
ANISOU 1882  CB  GLU B1010    14394  13941  18054   -306  -2027  -2207       C  
ATOM   1883  CG  GLU B1010     -24.626  31.690  41.394  1.00123.12           C  
ANISOU 1883  CG  GLU B1010    14523  14204  18053   -579  -1710  -2375       C  
ATOM   1884  CD  GLU B1010     -24.180  32.924  40.626  1.00125.76           C  
ANISOU 1884  CD  GLU B1010    15453  14455  17875   -855  -1512  -2443       C  
ATOM   1885  OE1 GLU B1010     -25.016  33.822  40.393  1.00127.33           O  
ANISOU 1885  OE1 GLU B1010    16153  14431  17796   -737  -1647  -2300       O  
ATOM   1886  OE2 GLU B1010     -22.991  32.997  40.246  1.00127.12           O  
ANISOU 1886  OE2 GLU B1010    15638  14790  17874  -1183  -1201  -2672       O  
ATOM   1887  N   SER B1011     -28.790  32.796  43.682  1.00119.96           N  
ANISOU 1887  N   SER B1011    13949  13669  17960    192  -2513  -1840       N  
ATOM   1888  CA  SER B1011     -29.999  33.615  43.584  1.00121.56           C  
ANISOU 1888  CA  SER B1011    14346  13904  17938    499  -2781  -1821       C  
ATOM   1889  C   SER B1011     -29.877  34.929  44.357  1.00121.33           C  
ANISOU 1889  C   SER B1011    14645  13771  17684    566  -2711  -1624       C  
ATOM   1890  O   SER B1011     -29.047  35.051  45.263  1.00118.41           O  
ANISOU 1890  O   SER B1011    14161  13379  17451    331  -2474  -1509       O  
ATOM   1891  CB  SER B1011     -31.231  32.825  44.041  1.00122.72           C  
ANISOU 1891  CB  SER B1011    13971  14262  18394    619  -2989  -1939       C  
ATOM   1892  OG  SER B1011     -31.250  32.664  45.450  1.00121.13           O  
ANISOU 1892  OG  SER B1011    13450  14074  18502    525  -2881  -1802       O  
ATOM   1893  N   SER B1012     -30.711  35.902  43.991  1.00123.71           N  
ANISOU 1893  N   SER B1012    15378  14027  17598    931  -2926  -1612       N  
ATOM   1894  CA  SER B1012     -30.672  37.236  44.593  1.00124.04           C  
ANISOU 1894  CA  SER B1012    15916  13887  17328   1044  -2850  -1433       C  
ATOM   1895  C   SER B1012     -31.202  37.274  46.033  1.00123.21           C  
ANISOU 1895  C   SER B1012    15341  13926  17546   1114  -2897  -1329       C  
ATOM   1896  O   SER B1012     -30.752  38.094  46.836  1.00121.24           O  
ANISOU 1896  O   SER B1012    15335  13534  17198    997  -2705  -1168       O  
ATOM   1897  CB  SER B1012     -31.418  38.246  43.717  1.00126.50           C  
ANISOU 1897  CB  SER B1012    16973  14055  17036   1550  -3086  -1455       C  
ATOM   1898  OG  SER B1012     -32.806  37.971  43.689  1.00127.28           O  
ANISOU 1898  OG  SER B1012    16670  14493  17200   2060  -3508  -1612       O  
ATOM   1899  N   PHE B1013     -32.152  36.392  46.356  1.00124.53           N  
ANISOU 1899  N   PHE B1013    14864  14382  18069   1240  -3111  -1457       N  
ATOM   1900  CA  PHE B1013     -32.708  36.320  47.721  1.00124.46           C  
ANISOU 1900  CA  PHE B1013    14401  14521  18368   1249  -3122  -1396       C  
ATOM   1901  C   PHE B1013     -31.766  35.591  48.677  1.00121.01           C  
ANISOU 1901  C   PHE B1013    13636  14018  18323    829  -2836  -1266       C  
ATOM   1902  O   PHE B1013     -31.760  35.861  49.876  1.00117.64           O  
ANISOU 1902  O   PHE B1013    13065  13597  18036    777  -2748  -1129       O  
ATOM   1903  CB  PHE B1013     -34.106  35.672  47.732  1.00125.91           C  
ANISOU 1903  CB  PHE B1013    14039  15078  18723   1450  -3390  -1663       C  
ATOM   1904  CG  PHE B1013     -34.736  35.585  49.107  1.00124.97           C  
ANISOU 1904  CG  PHE B1013    13471  15123  18887   1399  -3358  -1649       C  
ATOM   1905  CD1 PHE B1013     -34.781  36.698  49.952  1.00124.89           C  
ANISOU 1905  CD1 PHE B1013    13689  15032  18731   1587  -3342  -1463       C  
ATOM   1906  CD2 PHE B1013     -35.307  34.393  49.548  1.00125.43           C  
ANISOU 1906  CD2 PHE B1013    12951  15387  19318   1122  -3303  -1845       C  
ATOM   1907  CE1 PHE B1013     -35.367  36.616  51.213  1.00124.11           C  
ANISOU 1907  CE1 PHE B1013    13180  15093  18883   1526  -3300  -1464       C  
ATOM   1908  CE2 PHE B1013     -35.898  34.305  50.807  1.00124.80           C  
ANISOU 1908  CE2 PHE B1013    12519  15440  19458   1015  -3225  -1856       C  
ATOM   1909  CZ  PHE B1013     -35.929  35.419  51.640  1.00123.52           C  
ANISOU 1909  CZ  PHE B1013    12521  15236  19176   1234  -3241  -1662       C  
ATOM   1910  N   PHE B1014     -30.980  34.665  48.124  1.00121.83           N  
ANISOU 1910  N   PHE B1014    13649  14078  18562    595  -2712  -1330       N  
ATOM   1911  CA  PHE B1014     -29.989  33.894  48.879  1.00118.28           C  
ANISOU 1911  CA  PHE B1014    12946  13600  18396    341  -2483  -1252       C  
ATOM   1912  C   PHE B1014     -28.851  34.813  49.303  1.00115.91           C  
ANISOU 1912  C   PHE B1014    12881  13262  17898    194  -2271  -1134       C  
ATOM   1913  O   PHE B1014     -28.341  34.688  50.419  1.00115.42           O  
ANISOU 1913  O   PHE B1014    12592  13266  17997    107  -2149  -1040       O  
ATOM   1914  CB  PHE B1014     -29.453  32.740  48.015  1.00118.67           C  
ANISOU 1914  CB  PHE B1014    12911  13627  18552    231  -2426  -1398       C  
ATOM   1915  CG  PHE B1014     -28.896  31.580  48.800  1.00118.59           C  
ANISOU 1915  CG  PHE B1014    12627  13589  18845    153  -2283  -1369       C  
ATOM   1916  CD1 PHE B1014     -29.739  30.588  49.302  1.00118.94           C  
ANISOU 1916  CD1 PHE B1014    12475  13572  19146    136  -2303  -1404       C  
ATOM   1917  CD2 PHE B1014     -27.522  31.461  49.019  1.00118.79           C  
ANISOU 1917  CD2 PHE B1014    12632  13666  18835    111  -2111  -1354       C  
ATOM   1918  CE1 PHE B1014     -29.223  29.510  50.023  1.00118.76           C  
ANISOU 1918  CE1 PHE B1014    12402  13413  19307    128  -2151  -1354       C  
ATOM   1919  CE2 PHE B1014     -27.002  30.384  49.736  1.00118.05           C  
ANISOU 1919  CE2 PHE B1014    12369  13550  18936    201  -2026  -1336       C  
ATOM   1920  CZ  PHE B1014     -27.853  29.408  50.240  1.00117.31           C  
ANISOU 1920  CZ  PHE B1014    12241  13267  19064    235  -2044  -1301       C  
ATOM   1921  N   THR B1015     -28.484  35.737  48.409  1.00115.72           N  
ANISOU 1921  N   THR B1015    13351  13138  17477    143  -2209  -1173       N  
ATOM   1922  CA  THR B1015     -27.366  36.676  48.602  1.00115.03           C  
ANISOU 1922  CA  THR B1015    13578  13023  17104   -146  -1919  -1162       C  
ATOM   1923  C   THR B1015     -27.756  37.930  49.399  1.00114.19           C  
ANISOU 1923  C   THR B1015    13803  12797  16788    -98  -1884  -1009       C  
ATOM   1924  O   THR B1015     -26.889  38.648  49.889  1.00113.11           O  
ANISOU 1924  O   THR B1015    13840  12672  16463   -409  -1606  -1015       O  
ATOM   1925  CB  THR B1015     -26.789  37.149  47.250  1.00118.33           C  
ANISOU 1925  CB  THR B1015    14548  13310  17103   -328  -1770  -1303       C  
ATOM   1926  OG1 THR B1015     -27.157  36.242  46.201  1.00118.18           O  
ANISOU 1926  OG1 THR B1015    14427  13295  17182   -175  -1951  -1410       O  
ATOM   1927  CG2 THR B1015     -25.273  37.287  47.319  1.00119.56           C  
ANISOU 1927  CG2 THR B1015    14659  13639  17131   -799  -1394  -1475       C  
ATOM   1928  N   LYS B1016     -29.057  38.198  49.503  1.00114.57           N  
ANISOU 1928  N   LYS B1016    13924  12773  16833    288  -2154   -925       N  
ATOM   1929  CA  LYS B1016     -29.564  39.341  50.268  1.00114.19           C  
ANISOU 1929  CA  LYS B1016    14197  12606  16583    442  -2158   -789       C  
ATOM   1930  C   LYS B1016     -30.235  38.876  51.564  1.00111.67           C  
ANISOU 1930  C   LYS B1016    13273  12476  16680    556  -2277   -709       C  
ATOM   1931  O   LYS B1016     -30.812  39.682  52.300  1.00111.57           O  
ANISOU 1931  O   LYS B1016    13404  12418  16571    730  -2316   -613       O  
ATOM   1932  CB  LYS B1016     -30.532  40.179  49.422  1.00119.29           C  
ANISOU 1932  CB  LYS B1016    15473  13062  16790    904  -2380   -799       C  
ATOM   1933  CG  LYS B1016     -29.915  40.786  48.159  1.00123.30           C  
ANISOU 1933  CG  LYS B1016    16805  13276  16769    798  -2221   -853       C  
ATOM   1934  CD  LYS B1016     -30.975  41.337  47.209  1.00126.15           C  
ANISOU 1934  CD  LYS B1016    17760  13489  16681   1422  -2540   -884       C  
ATOM   1935  CE  LYS B1016     -30.340  41.913  45.953  1.00129.03           C  
ANISOU 1935  CE  LYS B1016    19079  13484  16461   1300  -2346   -920       C  
ATOM   1936  NZ  LYS B1016     -31.309  42.713  45.149  1.00133.77           N  
ANISOU 1936  NZ  LYS B1016    20512  13858  16457   2022  -2644   -914       N  
ATOM   1937  N   PHE B1017     -30.162  37.570  51.826  1.00109.64           N  
ANISOU 1937  N   PHE B1017    12420  12392  16844    457  -2309   -758       N  
ATOM   1938  CA  PHE B1017     -30.591  36.997  53.098  1.00107.79           C  
ANISOU 1938  CA  PHE B1017    11707  12278  16971    454  -2328   -686       C  
ATOM   1939  C   PHE B1017     -29.387  36.924  54.032  1.00108.20           C  
ANISOU 1939  C   PHE B1017    11634  12375  17103    196  -2093   -592       C  
ATOM   1940  O   PHE B1017     -29.518  37.066  55.258  1.00107.83           O  
ANISOU 1940  O   PHE B1017    11419  12374  17178    184  -2051   -477       O  
ATOM   1941  CB  PHE B1017     -31.199  35.610  52.894  1.00106.67           C  
ANISOU 1941  CB  PHE B1017    11154  12225  17150    469  -2436   -811       C  
ATOM   1942  CG  PHE B1017     -31.485  34.872  54.172  1.00106.18           C  
ANISOU 1942  CG  PHE B1017    10739  12200  17406    376  -2364   -747       C  
ATOM   1943  CD1 PHE B1017     -32.477  35.315  55.050  1.00106.12           C  
ANISOU 1943  CD1 PHE B1017    10596  12276  17449    455  -2419   -728       C  
ATOM   1944  CD2 PHE B1017     -30.763  33.724  54.499  1.00106.57           C  
ANISOU 1944  CD2 PHE B1017    10657  12182  17653    245  -2230   -720       C  
ATOM   1945  CE1 PHE B1017     -32.742  34.634  56.237  1.00105.29           C  
ANISOU 1945  CE1 PHE B1017    10247  12167  17594    313  -2305   -677       C  
ATOM   1946  CE2 PHE B1017     -31.028  33.036  55.681  1.00107.16           C  
ANISOU 1946  CE2 PHE B1017    10577  12203  17936    183  -2137   -644       C  
ATOM   1947  CZ  PHE B1017     -32.022  33.492  56.551  1.00105.80           C  
ANISOU 1947  CZ  PHE B1017    10287  12093  17819    170  -2157   -620       C  
ATOM   1948  N   ILE B1018     -28.213  36.702  53.439  1.00108.59           N  
ANISOU 1948  N   ILE B1018    11734  12473  17051      9  -1949   -686       N  
ATOM   1949  CA  ILE B1018     -26.955  36.646  54.189  1.00106.52           C  
ANISOU 1949  CA  ILE B1018    11276  12410  16785   -190  -1750   -711       C  
ATOM   1950  C   ILE B1018     -26.536  38.046  54.620  1.00105.74           C  
ANISOU 1950  C   ILE B1018    11486  12321  16370   -423  -1556   -697       C  
ATOM   1951  O   ILE B1018     -26.036  38.234  55.730  1.00104.28           O  
ANISOU 1951  O   ILE B1018    11091  12317  16212   -528  -1452   -672       O  
ATOM   1952  CB  ILE B1018     -25.837  35.913  53.405  1.00106.72           C  
ANISOU 1952  CB  ILE B1018    11164  12603  16781   -288  -1658   -914       C  
ATOM   1953  CG1 ILE B1018     -24.553  35.836  54.234  1.00106.76           C  
ANISOU 1953  CG1 ILE B1018    10852  12975  16738   -399  -1499  -1033       C  
ATOM   1954  CG2 ILE B1018     -25.608  36.535  52.029  1.00108.96           C  
ANISOU 1954  CG2 ILE B1018    11865  12787  16746   -470  -1566  -1054       C  
ATOM   1955  CD1 ILE B1018     -23.363  35.324  53.457  1.00108.82           C  
ANISOU 1955  CD1 ILE B1018    10937  13523  16886   -484  -1388  -1325       C  
ATOM   1956  N   ILE B1019     -26.780  39.016  53.743  1.00107.48           N  
ANISOU 1956  N   ILE B1019    12276  12315  16246   -487  -1500   -720       N  
ATOM   1957  CA  ILE B1019     -26.549  40.431  54.033  1.00111.47           C  
ANISOU 1957  CA  ILE B1019    13310  12682  16361   -718  -1270   -703       C  
ATOM   1958  C   ILE B1019     -27.551  40.934  55.078  1.00112.95           C  
ANISOU 1958  C   ILE B1019    13521  12759  16637   -465  -1400   -500       C  
ATOM   1959  O   ILE B1019     -27.220  41.773  55.924  1.00113.39           O  
ANISOU 1959  O   ILE B1019    13740  12811  16531   -676  -1202   -468       O  
ATOM   1960  CB  ILE B1019     -26.615  41.280  52.745  1.00113.48           C  
ANISOU 1960  CB  ILE B1019    14374  12607  16136   -780  -1166   -764       C  
ATOM   1961  CG1 ILE B1019     -25.409  40.961  51.847  1.00114.85           C  
ANISOU 1961  CG1 ILE B1019    14546  12933  16159  -1190   -921  -1021       C  
ATOM   1962  CG2 ILE B1019     -26.696  42.769  53.071  1.00115.73           C  
ANISOU 1962  CG2 ILE B1019    15427  12585  15960   -916   -938   -699       C  
ATOM   1963  CD1 ILE B1019     -25.508  41.486  50.425  1.00117.65           C  
ANISOU 1963  CD1 ILE B1019    15690  12943  16069  -1228   -840  -1085       C  
ATOM   1964  N   TYR B1020     -28.767  40.395  55.025  1.00114.80           N  
ANISOU 1964  N   TYR B1020    13549  12953  17115    -52  -1709   -415       N  
ATOM   1965  CA  TYR B1020     -29.812  40.738  55.988  1.00116.75           C  
ANISOU 1965  CA  TYR B1020    13706  13181  17473    206  -1843   -290       C  
ATOM   1966  C   TYR B1020     -29.496  40.240  57.400  1.00112.60           C  
ANISOU 1966  C   TYR B1020    12671  12850  17262     51  -1767   -210       C  
ATOM   1967  O   TYR B1020     -29.903  40.858  58.389  1.00111.48           O  
ANISOU 1967  O   TYR B1020    12563  12688  17109     93  -1740   -110       O  
ATOM   1968  CB  TYR B1020     -31.170  40.198  55.524  1.00120.09           C  
ANISOU 1968  CB  TYR B1020    13922  13653  18054    617  -2164   -345       C  
ATOM   1969  CG  TYR B1020     -32.305  40.482  56.482  1.00123.97           C  
ANISOU 1969  CG  TYR B1020    14215  14232  18656    872  -2294   -307       C  
ATOM   1970  CD1 TYR B1020     -32.928  41.737  56.512  1.00128.19           C  
ANISOU 1970  CD1 TYR B1020    15234  14637  18835   1200  -2358   -281       C  
ATOM   1971  CD2 TYR B1020     -32.755  39.496  57.364  1.00123.91           C  
ANISOU 1971  CD2 TYR B1020    13604  14415  19060    792  -2323   -319       C  
ATOM   1972  CE1 TYR B1020     -33.976  41.996  57.391  1.00130.75           C  
ANISOU 1972  CE1 TYR B1020    15320  15108  19251   1468  -2479   -298       C  
ATOM   1973  CE2 TYR B1020     -33.798  39.743  58.247  1.00126.62           C  
ANISOU 1973  CE2 TYR B1020    13734  14883  19493    958  -2399   -340       C  
ATOM   1974  CZ  TYR B1020     -34.407  40.989  58.257  1.00129.71           C  
ANISOU 1974  CZ  TYR B1020    14487  15231  19567   1307  -2491   -344       C  
ATOM   1975  OH  TYR B1020     -35.441  41.221  59.135  1.00131.55           O  
ANISOU 1975  OH  TYR B1020    14449  15651  19882   1499  -2567   -413       O  
ATOM   1976  N   LEU B1021     -28.777  39.124  57.490  1.00109.48           N  
ANISOU 1976  N   LEU B1021    11862  12631  17105    -71  -1741   -259       N  
ATOM   1977  CA  LEU B1021     -28.474  38.534  58.789  1.00107.13           C  
ANISOU 1977  CA  LEU B1021    11170  12495  17041   -110  -1702   -182       C  
ATOM   1978  C   LEU B1021     -27.358  39.279  59.517  1.00108.05           C  
ANISOU 1978  C   LEU B1021    11315  12794  16944   -374  -1486   -215       C  
ATOM   1979  O   LEU B1021     -27.502  39.607  60.702  1.00104.57           O  
ANISOU 1979  O   LEU B1021    10788  12404  16540   -389  -1449   -112       O  
ATOM   1980  CB  LEU B1021     -28.163  37.040  58.659  1.00104.72           C  
ANISOU 1980  CB  LEU B1021    10537  12265  16986    -24  -1768   -226       C  
ATOM   1981  CG  LEU B1021     -29.391  36.130  58.576  1.00104.27           C  
ANISOU 1981  CG  LEU B1021    10362  12062  17193    130  -1910   -204       C  
ATOM   1982  CD1 LEU B1021     -28.962  34.707  58.261  1.00106.39           C  
ANISOU 1982  CD1 LEU B1021    10504  12302  17616    181  -1911   -264       C  
ATOM   1983  CD2 LEU B1021     -30.241  36.172  59.844  1.00101.35           C  
ANISOU 1983  CD2 LEU B1021     9878  11664  16965    151  -1905    -89       C  
ATOM   1984  N   ILE B1022     -26.266  39.553  58.792  1.00110.18           N  
ANISOU 1984  N   ILE B1022    11691  13202  16969   -628  -1321   -408       N  
ATOM   1985  CA  ILE B1022     -25.115  40.318  59.304  1.00110.38           C  
ANISOU 1985  CA  ILE B1022    11713  13511  16717  -1006  -1054   -576       C  
ATOM   1986  C   ILE B1022     -25.559  41.597  60.014  1.00108.52           C  
ANISOU 1986  C   ILE B1022    11863  13087  16282  -1155   -919   -467       C  
ATOM   1987  O   ILE B1022     -25.153  41.846  61.146  1.00108.05           O  
ANISOU 1987  O   ILE B1022    11590  13259  16203  -1288   -827   -482       O  
ATOM   1988  CB  ILE B1022     -24.102  40.663  58.174  1.00113.89           C  
ANISOU 1988  CB  ILE B1022    12354  14082  16839  -1377   -818   -872       C  
ATOM   1989  CG1 ILE B1022     -23.245  39.440  57.799  1.00116.01           C  
ANISOU 1989  CG1 ILE B1022    12096  14729  17253  -1266   -895  -1075       C  
ATOM   1990  CG2 ILE B1022     -23.210  41.836  58.562  1.00115.71           C  
ANISOU 1990  CG2 ILE B1022    12787  14510  16666  -1928   -445  -1101       C  
ATOM   1991  CD1 ILE B1022     -22.241  39.000  58.853  1.00117.60           C  
ANISOU 1991  CD1 ILE B1022    11713  15501  17470  -1234   -882  -1255       C  
ATOM   1992  N   VAL B1023     -26.402  42.389  59.352  1.00107.96           N  
ANISOU 1992  N   VAL B1023    12389  12603  16029  -1070   -925   -370       N  
ATOM   1993  CA  VAL B1023     -26.865  43.656  59.912  1.00107.71           C  
ANISOU 1993  CA  VAL B1023    12870  12317  15739  -1128   -791   -272       C  
ATOM   1994  C   VAL B1023     -27.682  43.384  61.178  1.00107.00           C  
ANISOU 1994  C   VAL B1023    12403  12283  15967   -847   -975    -80       C  
ATOM   1995  O   VAL B1023     -27.370  43.918  62.252  1.00105.92           O  
ANISOU 1995  O   VAL B1023    12236  12252  15759  -1050   -820    -67       O  
ATOM   1996  CB  VAL B1023     -27.637  44.519  58.883  1.00107.42           C  
ANISOU 1996  CB  VAL B1023    13650  11808  15358   -920   -807   -215       C  
ATOM   1997  CG1 VAL B1023     -28.097  45.822  59.509  1.00107.50           C  
ANISOU 1997  CG1 VAL B1023    14284  11514  15049   -894   -663   -117       C  
ATOM   1998  CG2 VAL B1023     -26.773  44.819  57.666  1.00109.01           C  
ANISOU 1998  CG2 VAL B1023    14336  11902  15181  -1276   -559   -409       C  
ATOM   1999  N   LEU B1024     -28.694  42.525  61.062  1.00107.20           N  
ANISOU 1999  N   LEU B1024    12134  12272  16324   -447  -1268     23       N  
ATOM   2000  CA  LEU B1024     -29.462  42.095  62.239  1.00106.69           C  
ANISOU 2000  CA  LEU B1024    11689  12284  16564   -263  -1393    154       C  
ATOM   2001  C   LEU B1024     -28.569  41.528  63.349  1.00105.50           C  
ANISOU 2001  C   LEU B1024    11125  12412  16548   -453  -1304    165       C  
ATOM   2002  O   LEU B1024     -28.762  41.845  64.521  1.00102.77           O  
ANISOU 2002  O   LEU B1024    10708  12109  16232   -480  -1255    256       O  
ATOM   2003  CB  LEU B1024     -30.561  41.092  61.861  1.00105.12           C  
ANISOU 2003  CB  LEU B1024    11199  12071  16671     45  -1643    157       C  
ATOM   2004  CG  LEU B1024     -31.953  41.687  61.637  1.00106.69           C  
ANISOU 2004  CG  LEU B1024    11567  12167  16802    382  -1802    137       C  
ATOM   2005  CD1 LEU B1024     -32.010  42.500  60.353  1.00109.98           C  
ANISOU 2005  CD1 LEU B1024    12545  12396  16848    561  -1851     69       C  
ATOM   2006  CD2 LEU B1024     -33.014  40.596  61.624  1.00107.84           C  
ANISOU 2006  CD2 LEU B1024    11245  12457  17273    538  -1981     44       C  
ATOM   2007  N   ASN B1025     -27.594  40.700  62.970  1.00106.89           N  
ANISOU 2007  N   ASN B1025    11046  12801  16765   -525  -1299     51       N  
ATOM   2008  CA  ASN B1025     -26.659  40.123  63.934  1.00108.13           C  
ANISOU 2008  CA  ASN B1025    10828  13297  16961   -560  -1269     10       C  
ATOM   2009  C   ASN B1025     -25.854  41.217  64.633  1.00109.71           C  
ANISOU 2009  C   ASN B1025    11084  13736  16864   -895  -1048   -106       C  
ATOM   2010  O   ASN B1025     -25.888  41.318  65.863  1.00110.37           O  
ANISOU 2010  O   ASN B1025    11028  13936  16973   -876  -1042    -24       O  
ATOM   2011  CB  ASN B1025     -25.746  39.075  63.274  1.00107.86           C  
ANISOU 2011  CB  ASN B1025    10533  13490  16957   -467  -1327   -150       C  
ATOM   2012  CG  ASN B1025     -24.895  38.305  64.278  1.00108.04           C  
ANISOU 2012  CG  ASN B1025    10193  13878  16981   -283  -1380   -199       C  
ATOM   2013  OD1 ASN B1025     -23.953  37.610  63.894  1.00108.16           O  
ANISOU 2013  OD1 ASN B1025     9976  14193  16928   -149  -1421   -392       O  
ATOM   2014  ND2 ASN B1025     -25.231  38.408  65.565  1.00108.97           N  
ANISOU 2014  ND2 ASN B1025    10280  13986  17137   -212  -1394    -42       N  
ATOM   2015  N   GLY B1026     -25.163  42.044  63.846  1.00111.11           N  
ANISOU 2015  N   GLY B1026    11518  13971  16727  -1253   -832   -321       N  
ATOM   2016  CA  GLY B1026     -24.450  43.217  64.366  1.00112.69           C  
ANISOU 2016  CA  GLY B1026    11890  14354  16572  -1721   -528   -502       C  
ATOM   2017  C   GLY B1026     -25.309  44.064  65.295  1.00112.35           C  
ANISOU 2017  C   GLY B1026    12154  14026  16510  -1701   -486   -288       C  
ATOM   2018  O   GLY B1026     -24.825  44.553  66.312  1.00111.66           O  
ANISOU 2018  O   GLY B1026    11955  14189  16281  -1945   -337   -372       O  
ATOM   2019  N   ILE B1027     -26.584  44.232  64.931  1.00111.85           N  
ANISOU 2019  N   ILE B1027    12438  13496  16564  -1385   -627    -57       N  
ATOM   2020  CA  ILE B1027     -27.580  44.905  65.767  1.00109.53           C  
ANISOU 2020  CA  ILE B1027    12376  12953  16287  -1232   -642    132       C  
ATOM   2021  C   ILE B1027     -27.835  44.117  67.049  1.00107.42           C  
ANISOU 2021  C   ILE B1027    11576  12900  16337  -1060   -789    259       C  
ATOM   2022  O   ILE B1027     -27.602  44.634  68.134  1.00109.32           O  
ANISOU 2022  O   ILE B1027    11795  13262  16481  -1231   -663    267       O  
ATOM   2023  CB  ILE B1027     -28.930  45.096  65.023  1.00109.89           C  
ANISOU 2023  CB  ILE B1027    12772  12605  16376   -809   -827    261       C  
ATOM   2024  CG1 ILE B1027     -28.780  46.085  63.859  1.00111.81           C  
ANISOU 2024  CG1 ILE B1027    13780  12522  16180   -899   -668    175       C  
ATOM   2025  CG2 ILE B1027     -30.031  45.533  65.994  1.00109.49           C  
ANISOU 2025  CG2 ILE B1027    12757  12436  16410   -555   -897    402       C  
ATOM   2026  CD1 ILE B1027     -30.018  46.217  62.986  1.00112.61           C  
ANISOU 2026  CD1 ILE B1027    14217  12326  16242   -357   -915    248       C  
ATOM   2027  N   THR B1028     -28.299  42.872  66.914  1.00105.93           N  
ANISOU 2027  N   THR B1028    11039  12728  16483   -759  -1020    344       N  
ATOM   2028  CA  THR B1028     -28.764  42.065  68.048  1.00103.98           C  
ANISOU 2028  CA  THR B1028    10472  12541  16495   -588  -1124    484       C  
ATOM   2029  C   THR B1028     -27.635  41.583  68.958  1.00102.91           C  
ANISOU 2029  C   THR B1028    10043  12764  16294   -653  -1095    438       C  
ATOM   2030  O   THR B1028     -27.857  41.304  70.136  1.00 99.84           O  
ANISOU 2030  O   THR B1028     9546  12414  15976   -571  -1113    556       O  
ATOM   2031  CB  THR B1028     -29.605  40.850  67.585  1.00104.70           C  
ANISOU 2031  CB  THR B1028    10403  12489  16891   -333  -1301    540       C  
ATOM   2032  OG1 THR B1028     -30.459  40.413  68.654  1.00104.29           O  
ANISOU 2032  OG1 THR B1028    10234  12368  17022   -260  -1312    656       O  
ATOM   2033  CG2 THR B1028     -28.707  39.683  67.121  1.00104.78           C  
ANISOU 2033  CG2 THR B1028    10219  12636  16955   -262  -1369    476       C  
HETATM 2034  N   MSE B1029     -26.434  41.477  68.402  1.00104.97           N  
ANISOU 2034  N   MSE B1029    10172  13329  16384   -769  -1057    229       N  
HETATM 2035  CA  MSE B1029     -25.274  41.065  69.180  1.00108.19           C  
ANISOU 2035  CA  MSE B1029    10230  14228  16650   -739  -1072     85       C  
HETATM 2036  C   MSE B1029     -24.680  42.299  69.821  1.00108.39           C  
ANISOU 2036  C   MSE B1029    10280  14530  16372  -1143   -851    -85       C  
HETATM 2037  O   MSE B1029     -24.062  42.217  70.880  1.00110.79           O  
ANISOU 2037  O   MSE B1029    10313  15237  16547  -1116   -868   -171       O  
HETATM 2038  CB  MSE B1029     -24.309  40.263  68.299  1.00111.52           C  
ANISOU 2038  CB  MSE B1029    10404  14947  17020   -615  -1152   -136       C  
HETATM 2039  CG  MSE B1029     -23.010  39.913  69.018  1.00119.49           C  
ANISOU 2039  CG  MSE B1029    10986  16620  17795   -490  -1202   -394       C  
HETATM 2040 SE   MSE B1029     -22.802  37.977  69.307  1.00127.26          SE  
ANISOU 2040 SE   MSE B1029    11828  17634  18892    302  -1529   -279      SE  
HETATM 2041  CE  MSE B1029     -22.319  37.421  67.476  1.00124.00           C  
ANISOU 2041  CE  MSE B1029    11336  17250  18529    319  -1545   -509       C  
ATOM   2042  N   GLY B1030     -24.888  43.456  69.198  1.00108.12           N  
ANISOU 2042  N   GLY B1030    10645  14261  16175  -1507   -632   -146       N  
ATOM   2043  CA  GLY B1030     -24.438  44.730  69.756  1.00109.82           C  
ANISOU 2043  CA  GLY B1030    11056  14614  16057  -1982   -339   -314       C  
ATOM   2044  C   GLY B1030     -25.225  45.097  70.997  1.00109.62           C  
ANISOU 2044  C   GLY B1030    11130  14406  16114  -1885   -354    -81       C  
ATOM   2045  O   GLY B1030     -25.125  46.219  71.514  1.00113.63           O  
ANISOU 2045  O   GLY B1030    11916  14890  16366  -2246   -104   -160       O  
ATOM   2046  N   LEU B1031     -26.009  44.133  71.473  1.00105.26           N  
ANISOU 2046  N   LEU B1031    10394  13709  15892  -1439   -608    183       N  
ATOM   2047  CA  LEU B1031     -26.837  44.298  72.651  1.00101.67           C  
ANISOU 2047  CA  LEU B1031     9995  13090  15546  -1331   -624    395       C  
ATOM   2048  C   LEU B1031     -26.676  43.087  73.578  1.00100.30           C  
ANISOU 2048  C   LEU B1031     9475  13124  15508  -1020   -814    497       C  
ATOM   2049  O   LEU B1031     -27.401  42.939  74.557  1.00 99.14           O  
ANISOU 2049  O   LEU B1031     9375  12820  15472   -908   -833    685       O  
ATOM   2050  CB  LEU B1031     -28.287  44.505  72.220  1.00100.11           C  
ANISOU 2050  CB  LEU B1031    10098  12390  15550  -1140   -671    587       C  
ATOM   2051  CG  LEU B1031     -28.519  45.558  71.124  1.00100.20           C  
ANISOU 2051  CG  LEU B1031    10593  12117  15363  -1255   -547    511       C  
ATOM   2052  CD1 LEU B1031     -29.862  45.338  70.445  1.00100.21           C  
ANISOU 2052  CD1 LEU B1031    10714  11791  15570   -877   -723    625       C  
ATOM   2053  CD2 LEU B1031     -28.407  46.979  71.664  1.00102.38           C  
ANISOU 2053  CD2 LEU B1031    11305  12286  15308  -1554   -276    458       C  
ATOM   2054  N   GLU B1032     -25.705  42.234  73.262  1.00101.29           N  
ANISOU 2054  N   GLU B1032     9318  13596  15574   -856   -938    352       N  
ATOM   2055  CA  GLU B1032     -25.271  41.155  74.151  1.00105.32           C  
ANISOU 2055  CA  GLU B1032     9617  14346  16053   -474  -1117    401       C  
ATOM   2056  C   GLU B1032     -24.501  41.694  75.363  1.00107.91           C  
ANISOU 2056  C   GLU B1032     9754  15166  16080   -575  -1075    253       C  
ATOM   2057  O   GLU B1032     -24.537  41.117  76.460  1.00107.76           O  
ANISOU 2057  O   GLU B1032     9734  15203  16006   -270  -1191    386       O  
ATOM   2058  CB  GLU B1032     -24.355  40.192  73.397  1.00109.48           C  
ANISOU 2058  CB  GLU B1032     9913  15164  16519   -181  -1276    225       C  
ATOM   2059  CG  GLU B1032     -25.057  39.064  72.661  1.00109.70           C  
ANISOU 2059  CG  GLU B1032    10131  14726  16822    113  -1390    418       C  
ATOM   2060  CD  GLU B1032     -24.192  37.822  72.599  1.00112.84           C  
ANISOU 2060  CD  GLU B1032    10407  15372  17096    616  -1585    328       C  
ATOM   2061  OE1 GLU B1032     -22.970  37.965  72.389  1.00113.73           O  
ANISOU 2061  OE1 GLU B1032    10160  16097  16955    672  -1638     -1       O  
ATOM   2062  OE2 GLU B1032     -24.732  36.708  72.775  1.00114.54           O  
ANISOU 2062  OE2 GLU B1032    10914  15184  17422    952  -1663    546       O  
ATOM   2063  N   THR B1033     -23.793  42.799  75.133  1.00108.82           N  
ANISOU 2063  N   THR B1033     9758  15635  15954  -1036   -881    -51       N  
ATOM   2064  CA  THR B1033     -22.944  43.448  76.126  1.00110.46           C  
ANISOU 2064  CA  THR B1033     9720  16428  15822  -1267   -791   -317       C  
ATOM   2065  C   THR B1033     -23.719  44.043  77.284  1.00110.98           C  
ANISOU 2065  C   THR B1033    10034  16220  15913  -1379   -696    -86       C  
ATOM   2066  O   THR B1033     -23.324  43.890  78.446  1.00113.44           O  
ANISOU 2066  O   THR B1033    10157  16904  16042  -1234   -782   -130       O  
ATOM   2067  CB  THR B1033     -22.190  44.603  75.487  1.00110.41           C  
ANISOU 2067  CB  THR B1033     9679  16731  15538  -1921   -482   -726       C  
ATOM   2068  OG1 THR B1033     -23.101  45.327  74.653  1.00106.37           O  
ANISOU 2068  OG1 THR B1033     9718  15527  15172  -2189   -284   -533       O  
ATOM   2069  CG2 THR B1033     -21.051  44.074  74.659  1.00113.18           C  
ANISOU 2069  CG2 THR B1033     9598  17670  15736  -1879   -549  -1123       C  
ATOM   2070  N   SER B1034     -24.805  44.739  76.957  1.00109.32           N  
ANISOU 2070  N   SER B1034    10247  15401  15890  -1590   -532    129       N  
ATOM   2071  CA  SER B1034     -25.627  45.425  77.948  1.00109.81           C  
ANISOU 2071  CA  SER B1034    10565  15182  15976  -1708   -409    316       C  
ATOM   2072  C   SER B1034     -25.817  44.627  79.234  1.00110.09           C  
ANISOU 2072  C   SER B1034    10475  15303  16051  -1366   -576    500       C  
ATOM   2073  O   SER B1034     -26.126  43.431  79.199  1.00110.83           O  
ANISOU 2073  O   SER B1034    10555  15234  16322   -952   -772    683       O  
ATOM   2074  CB  SER B1034     -26.992  45.779  77.356  1.00107.50           C  
ANISOU 2074  CB  SER B1034    10673  14231  15942  -1667   -348    552       C  
ATOM   2075  OG  SER B1034     -27.933  46.049  78.385  1.00106.75           O  
ANISOU 2075  OG  SER B1034    10724  13897  15938  -1617   -301    746       O  
ATOM   2076  N   LYS B1035     -25.617  45.302  80.362  1.00110.52           N  
ANISOU 2076  N   LYS B1035    10521  15579  15892  -1569   -465    439       N  
ATOM   2077  CA  LYS B1035     -25.908  44.722  81.674  1.00111.59           C  
ANISOU 2077  CA  LYS B1035    10666  15721  16013  -1289   -577    633       C  
ATOM   2078  C   LYS B1035     -27.327  45.105  82.088  1.00109.70           C  
ANISOU 2078  C   LYS B1035    10767  14899  16015  -1378   -431    906       C  
ATOM   2079  O   LYS B1035     -27.596  45.446  83.245  1.00108.23           O  
ANISOU 2079  O   LYS B1035    10668  14720  15736  -1457   -348    977       O  
ATOM   2080  CB  LYS B1035     -24.862  45.138  82.727  1.00115.55           C  
ANISOU 2080  CB  LYS B1035    10910  16883  16112  -1406   -576    375       C  
ATOM   2081  CG  LYS B1035     -24.287  46.551  82.587  1.00115.28           C  
ANISOU 2081  CG  LYS B1035    10826  17147  15829  -2041   -287     30       C  
ATOM   2082  CD  LYS B1035     -23.724  47.033  83.914  1.00117.27           C  
ANISOU 2082  CD  LYS B1035    10909  17911  15736  -2211   -238   -159       C  
ATOM   2083  CE  LYS B1035     -24.831  47.221  84.944  1.00114.76           C  
ANISOU 2083  CE  LYS B1035    10945  17096  15561  -2158   -170    196       C  
ATOM   2084  NZ  LYS B1035     -24.299  47.728  86.231  1.00117.62           N  
ANISOU 2084  NZ  LYS B1035    11172  17944  15573  -2342   -115     12       N  
ATOM   2085  N   THR B1036     -28.220  45.056  81.099  1.00110.00           N  
ANISOU 2085  N   THR B1036    10957  14499  16338  -1348   -407   1008       N  
ATOM   2086  CA  THR B1036     -29.656  45.266  81.271  1.00109.32           C  
ANISOU 2086  CA  THR B1036    11085  13958  16494  -1341   -311   1179       C  
ATOM   2087  C   THR B1036     -30.404  44.407  80.240  1.00108.91           C  
ANISOU 2087  C   THR B1036    11022  13620  16738  -1129   -419   1248       C  
ATOM   2088  O   THR B1036     -31.426  43.795  80.560  1.00111.69           O  
ANISOU 2088  O   THR B1036    11411  13737  17289  -1044   -401   1354       O  
ATOM   2089  CB  THR B1036     -30.045  46.755  81.103  1.00108.10           C  
ANISOU 2089  CB  THR B1036    11172  13653  16248  -1594   -107   1095       C  
ATOM   2090  OG1 THR B1036     -29.052  47.583  81.722  1.00110.06           O  
ANISOU 2090  OG1 THR B1036    11438  14218  16161  -1909     32    938       O  
ATOM   2091  CG2 THR B1036     -31.393  47.039  81.746  1.00107.48           C  
ANISOU 2091  CG2 THR B1036    11226  13288  16323  -1529    -16   1208       C  
ATOM   2092  N   PHE B1037     -29.867  44.357  79.020  1.00106.70           N  
ANISOU 2092  N   PHE B1037    10686  13397  16457  -1101   -499   1141       N  
ATOM   2093  CA  PHE B1037     -30.469  43.653  77.876  1.00106.31           C  
ANISOU 2093  CA  PHE B1037    10620  13122  16652   -929   -603   1160       C  
ATOM   2094  C   PHE B1037     -30.592  42.142  78.093  1.00108.21           C  
ANISOU 2094  C   PHE B1037    10803  13282  17028   -724   -705   1266       C  
ATOM   2095  O   PHE B1037     -31.576  41.531  77.666  1.00106.38           O  
ANISOU 2095  O   PHE B1037    10595  12802  17023   -679   -702   1288       O  
ATOM   2096  CB  PHE B1037     -29.617  43.913  76.631  1.00104.62           C  
ANISOU 2096  CB  PHE B1037    10387  13030  16335   -975   -648   1011       C  
ATOM   2097  CG  PHE B1037     -30.314  43.662  75.325  1.00101.76           C  
ANISOU 2097  CG  PHE B1037    10080  12423  16162   -843   -728    996       C  
ATOM   2098  CD1 PHE B1037     -31.039  44.675  74.705  1.00101.64           C  
ANISOU 2098  CD1 PHE B1037    10308  12200  16110   -847   -671    951       C  
ATOM   2099  CD2 PHE B1037     -30.194  42.436  74.680  1.00101.74           C  
ANISOU 2099  CD2 PHE B1037     9937  12404  16316   -670   -869   1006       C  
ATOM   2100  CE1 PHE B1037     -31.666  44.458  73.484  1.00100.87           C  
ANISOU 2100  CE1 PHE B1037    10252  11944  16131   -659   -785    904       C  
ATOM   2101  CE2 PHE B1037     -30.813  42.209  73.458  1.00101.64           C  
ANISOU 2101  CE2 PHE B1037     9949  12213  16455   -572   -946    958       C  
ATOM   2102  CZ  PHE B1037     -31.555  43.221  72.860  1.00100.96           C  
ANISOU 2102  CZ  PHE B1037    10044  11984  16331   -558   -920    899       C  
HETATM 2103  N   MSE B1038     -29.586  41.554  78.746  1.00111.81           N  
ANISOU 2103  N   MSE B1038    11227  13966  17289   -587   -782   1292       N  
HETATM 2104  CA  MSE B1038     -29.502  40.102  78.969  1.00114.26           C  
ANISOU 2104  CA  MSE B1038    11670  14140  17602   -304   -871   1402       C  
HETATM 2105  C   MSE B1038     -30.130  39.777  80.301  1.00114.70           C  
ANISOU 2105  C   MSE B1038    11977  13996  17608   -327   -750   1559       C  
HETATM 2106  O   MSE B1038     -30.283  38.607  80.667  1.00115.52           O  
ANISOU 2106  O   MSE B1038    12389  13843  17659   -151   -737   1676       O  
HETATM 2107  CB  MSE B1038     -28.029  39.675  78.936  1.00118.47           C  
ANISOU 2107  CB  MSE B1038    12075  15079  17860     -2  -1058   1303       C  
HETATM 2108  CG  MSE B1038     -27.791  38.200  78.598  1.00122.33           C  
ANISOU 2108  CG  MSE B1038    12763  15392  18324    402  -1186   1370       C  
HETATM 2109 SE   MSE B1038     -27.861  37.865  76.651  1.00123.46          SE  
ANISOU 2109 SE   MSE B1038    12762  15411  18735    368  -1241   1244      SE  
HETATM 2110  CE  MSE B1038     -25.964  38.095  76.181  1.00122.82           C  
ANISOU 2110  CE  MSE B1038    12258  16079  18331    607  -1442    933       C  
ATOM   2111  N   GLN B1039     -30.501  40.820  81.036  1.00112.57           N  
ANISOU 2111  N   GLN B1039    11659  13798  17314   -562   -627   1554       N  
ATOM   2112  CA  GLN B1039     -31.173  40.654  82.316  1.00113.64           C  
ANISOU 2112  CA  GLN B1039    12021  13755  17401   -651   -473   1677       C  
ATOM   2113  C   GLN B1039     -32.693  40.623  82.139  1.00113.95           C  
ANISOU 2113  C   GLN B1039    12085  13486  17725   -898   -279   1645       C  
ATOM   2114  O   GLN B1039     -33.438  40.418  83.106  1.00114.05           O  
ANISOU 2114  O   GLN B1039    12276  13334  17725  -1060    -87   1692       O  
ATOM   2115  CB  GLN B1039     -30.745  41.752  83.293  1.00112.49           C  
ANISOU 2115  CB  GLN B1039    11799  13894  17049   -773   -431   1654       C  
ATOM   2116  CG  GLN B1039     -29.280  41.680  83.702  1.00110.96           C  
ANISOU 2116  CG  GLN B1039    11511  14145  16505   -545   -611   1595       C  
ATOM   2117  CD  GLN B1039     -29.026  42.280  85.067  1.00112.05           C  
ANISOU 2117  CD  GLN B1039    11686  14507  16381   -632   -551   1603       C  
ATOM   2118  OE1 GLN B1039     -29.860  42.177  85.971  1.00112.67           O  
ANISOU 2118  OE1 GLN B1039    12016  14306  16486   -727   -399   1748       O  
ATOM   2119  NE2 GLN B1039     -27.865  42.904  85.232  1.00113.48           N  
ANISOU 2119  NE2 GLN B1039    11598  15236  16281   -645   -644   1400       N  
ATOM   2120  N   SER B1040     -33.136  40.822  80.893  1.00113.51           N  
ANISOU 2120  N   SER B1040    11830  13409  17888   -921   -328   1517       N  
ATOM   2121  CA  SER B1040     -34.544  40.672  80.511  1.00112.70           C  
ANISOU 2121  CA  SER B1040    11632  13162  18028  -1084   -200   1378       C  
ATOM   2122  C   SER B1040     -34.696  39.857  79.231  1.00112.04           C  
ANISOU 2122  C   SER B1040    11482  12988  18101  -1021   -287   1285       C  
ATOM   2123  O   SER B1040     -35.182  38.722  79.272  1.00113.98           O  
ANISOU 2123  O   SER B1040    11881  13023  18402  -1147   -158   1256       O  
ATOM   2124  CB  SER B1040     -35.220  42.032  80.382  1.00111.00           C  
ANISOU 2124  CB  SER B1040    11219  13086  17868  -1114   -180   1244       C  
ATOM   2125  OG  SER B1040     -35.410  42.594  81.669  1.00113.40           O  
ANISOU 2125  OG  SER B1040    11604  13421  18063  -1239    -30   1296       O  
ATOM   2126  N   PHE B1041     -34.274  40.429  78.103  1.00109.30           N  
ANISOU 2126  N   PHE B1041    10976  12769  17785   -869   -467   1224       N  
ATOM   2127  CA  PHE B1041     -34.247  39.710  76.823  1.00109.26           C  
ANISOU 2127  CA  PHE B1041    10911  12703  17899   -784   -577   1141       C  
ATOM   2128  C   PHE B1041     -33.049  38.751  76.782  1.00110.99           C  
ANISOU 2128  C   PHE B1041    11316  12863  17994   -624   -662   1275       C  
ATOM   2129  O   PHE B1041     -32.291  38.731  75.800  1.00110.89           O  
ANISOU 2129  O   PHE B1041    11225  12945  17962   -475   -816   1240       O  
ATOM   2130  CB  PHE B1041     -34.145  40.695  75.655  1.00105.53           C  
ANISOU 2130  CB  PHE B1041    10303  12361  17433   -657   -727   1037       C  
ATOM   2131  CG  PHE B1041     -35.401  41.486  75.391  1.00105.14           C  
ANISOU 2131  CG  PHE B1041    10112  12377  17459   -626   -715    856       C  
ATOM   2132  CD1 PHE B1041     -35.639  42.682  76.055  1.00104.32           C  
ANISOU 2132  CD1 PHE B1041    10070  12331  17237   -599   -655    862       C  
ATOM   2133  CD2 PHE B1041     -36.318  41.060  74.434  1.00106.27           C  
ANISOU 2133  CD2 PHE B1041    10060  12570  17747   -568   -783    639       C  
ATOM   2134  CE1 PHE B1041     -36.778  43.425  75.791  1.00105.98           C  
ANISOU 2134  CE1 PHE B1041    10176  12636  17457   -428   -682    665       C  
ATOM   2135  CE2 PHE B1041     -37.458  41.798  74.161  1.00107.06           C  
ANISOU 2135  CE2 PHE B1041     9976  12849  17854   -410   -830    404       C  
ATOM   2136  CZ  PHE B1041     -37.688  42.984  74.841  1.00107.84           C  
ANISOU 2136  CZ  PHE B1041    10164  12993  17816   -293   -791    422       C  
ATOM   2137  N   GLY B1042     -32.892  37.955  77.842  1.00111.70           N  
ANISOU 2137  N   GLY B1042    11689  12796  17953   -612   -560   1408       N  
ATOM   2138  CA  GLY B1042     -31.680  37.171  78.069  1.00113.35           C  
ANISOU 2138  CA  GLY B1042    12129  13008  17930   -297   -680   1530       C  
ATOM   2139  C   GLY B1042     -31.503  35.949  77.192  1.00115.00           C  
ANISOU 2139  C   GLY B1042    12531  12994  18169   -136   -724   1513       C  
ATOM   2140  O   GLY B1042     -30.483  35.803  76.513  1.00115.73           O  
ANISOU 2140  O   GLY B1042    12520  13273  18178    150   -919   1481       O  
ATOM   2141  N   VAL B1043     -32.497  35.067  77.210  1.00115.93           N  
ANISOU 2141  N   VAL B1043    12937  12732  18381   -365   -505   1490       N  
ATOM   2142  CA  VAL B1043     -32.431  33.805  76.475  1.00116.83           C  
ANISOU 2142  CA  VAL B1043    13368  12537  18484   -278   -473   1467       C  
ATOM   2143  C   VAL B1043     -32.757  33.986  74.984  1.00115.07           C  
ANISOU 2143  C   VAL B1043    12753  12443  18527   -389   -566   1271       C  
ATOM   2144  O   VAL B1043     -32.583  33.047  74.202  1.00117.00           O  
ANISOU 2144  O   VAL B1043    13193  12488  18776   -305   -571   1230       O  
ATOM   2145  CB  VAL B1043     -33.353  32.734  77.107  1.00120.07           C  
ANISOU 2145  CB  VAL B1043    14360  12446  18815   -595   -112   1470       C  
ATOM   2146  CG1 VAL B1043     -32.958  31.338  76.652  1.00123.09           C  
ANISOU 2146  CG1 VAL B1043    15339  12402  19027   -395    -56   1514       C  
ATOM   2147  CG2 VAL B1043     -33.311  32.814  78.626  1.00121.92           C  
ANISOU 2147  CG2 VAL B1043    14967  12561  18795   -582     19   1642       C  
ATOM   2148  N   TYR B1044     -33.219  35.184  74.599  1.00112.14           N  
ANISOU 2148  N   TYR B1044    11904  12376  18328   -532   -639   1153       N  
ATOM   2149  CA  TYR B1044     -33.561  35.501  73.195  1.00110.75           C  
ANISOU 2149  CA  TYR B1044    11404  12341  18336   -565   -759    965       C  
ATOM   2150  C   TYR B1044     -32.391  35.355  72.211  1.00110.54           C  
ANISOU 2150  C   TYR B1044    11350  12401  18249   -280   -966    990       C  
ATOM   2151  O   TYR B1044     -32.506  34.640  71.210  1.00111.12           O  
ANISOU 2151  O   TYR B1044    11449  12363  18408   -278   -989    890       O  
ATOM   2152  CB  TYR B1044     -34.190  36.899  73.065  1.00109.09           C  
ANISOU 2152  CB  TYR B1044    10849  12398  18204   -628   -818    858       C  
ATOM   2153  CG  TYR B1044     -35.710  36.899  73.097  1.00112.48           C  
ANISOU 2153  CG  TYR B1044    11082  12878  18778   -878   -680    616       C  
ATOM   2154  CD1 TYR B1044     -36.408  37.511  74.144  1.00112.58           C  
ANISOU 2154  CD1 TYR B1044    11014  12984  18779  -1013   -546    582       C  
ATOM   2155  CD2 TYR B1044     -36.453  36.278  72.083  1.00113.32           C  
ANISOU 2155  CD2 TYR B1044    11031  13014  19010   -992   -677    359       C  
ATOM   2156  CE1 TYR B1044     -37.793  37.510  74.181  1.00114.56           C  
ANISOU 2156  CE1 TYR B1044    10988  13406  19134  -1235   -415    267       C  
ATOM   2157  CE2 TYR B1044     -37.839  36.264  72.117  1.00116.40           C  
ANISOU 2157  CE2 TYR B1044    11128  13604  19493  -1237   -550     24       C  
ATOM   2158  CZ  TYR B1044     -38.506  36.884  73.166  1.00118.46           C  
ANISOU 2158  CZ  TYR B1044    11265  14009  19735  -1349   -420    -39       C  
ATOM   2159  OH  TYR B1044     -39.891  36.878  73.202  1.00123.24           O  
ANISOU 2159  OH  TYR B1044    11483  14936  20407  -1586   -289   -465       O  
ATOM   2160  N   THR B1045     -31.276  36.023  72.511  1.00108.99           N  
ANISOU 2160  N   THR B1045    11079  12446  17886    -87  -1088   1073       N  
ATOM   2161  CA  THR B1045     -30.088  36.005  71.659  1.00109.22           C  
ANISOU 2161  CA  THR B1045    11005  12679  17816    128  -1249   1016       C  
ATOM   2162  C   THR B1045     -29.126  34.839  71.958  1.00113.72           C  
ANISOU 2162  C   THR B1045    11795  13212  18202    484  -1313   1075       C  
ATOM   2163  O   THR B1045     -28.248  34.537  71.142  1.00115.37           O  
ANISOU 2163  O   THR B1045    11908  13586  18343    697  -1437    973       O  
ATOM   2164  CB  THR B1045     -29.309  37.336  71.736  1.00108.60           C  
ANISOU 2164  CB  THR B1045    10707  12969  17587     77  -1297    959       C  
ATOM   2165  OG1 THR B1045     -30.202  38.406  72.073  1.00108.45           O  
ANISOU 2165  OG1 THR B1045    10666  12909  17631   -147  -1207    973       O  
ATOM   2166  CG2 THR B1045     -28.605  37.642  70.402  1.00106.86           C  
ANISOU 2166  CG2 THR B1045    10350  12925  17327     76  -1377    796       C  
ATOM   2167  N   THR B1046     -29.277  34.190  73.116  1.00115.73           N  
ANISOU 2167  N   THR B1046    12394  13251  18328    596  -1227   1221       N  
ATOM   2168  CA  THR B1046     -28.487  32.986  73.420  1.00119.31           C  
ANISOU 2168  CA  THR B1046    13238  13571  18524   1063  -1294   1291       C  
ATOM   2169  C   THR B1046     -28.806  31.869  72.415  1.00122.14           C  
ANISOU 2169  C   THR B1046    13877  13549  18983   1082  -1234   1247       C  
ATOM   2170  O   THR B1046     -27.904  31.158  71.960  1.00124.88           O  
ANISOU 2170  O   THR B1046    14346  13936  19165   1515  -1369   1206       O  
ATOM   2171  CB  THR B1046     -28.699  32.472  74.864  1.00121.71           C  
ANISOU 2171  CB  THR B1046    14053  13595  18595   1190  -1178   1479       C  
ATOM   2172  OG1 THR B1046     -28.758  33.574  75.776  1.00122.41           O  
ANISOU 2172  OG1 THR B1046    13876  13973  18661   1017  -1173   1511       O  
ATOM   2173  CG2 THR B1046     -27.556  31.573  75.281  1.00125.12           C  
ANISOU 2173  CG2 THR B1046    14857  14061  18622   1883  -1350   1531       C  
ATOM   2174  N   LEU B1047     -30.084  31.734  72.056  1.00120.89           N  
ANISOU 2174  N   LEU B1047    13778  13083  19071    617  -1030   1202       N  
ATOM   2175  CA  LEU B1047     -30.503  30.732  71.074  1.00122.62           C  
ANISOU 2175  CA  LEU B1047    14231  12972  19388    515   -932   1103       C  
ATOM   2176  C   LEU B1047     -30.764  31.325  69.673  1.00119.65           C  
ANISOU 2176  C   LEU B1047    13344  12850  19270    320  -1044    911       C  
ATOM   2177  O   LEU B1047     -30.969  30.580  68.699  1.00119.54           O  
ANISOU 2177  O   LEU B1047    13435  12654  19332    260  -1008    796       O  
ATOM   2178  CB  LEU B1047     -31.719  29.937  71.576  1.00125.91           C  
ANISOU 2178  CB  LEU B1047    15121  12899  19821     90   -579   1086       C  
ATOM   2179  CG  LEU B1047     -31.669  29.251  72.950  1.00129.72           C  
ANISOU 2179  CG  LEU B1047    16321  12976  19991    196   -379   1277       C  
ATOM   2180  CD1 LEU B1047     -33.012  28.615  73.281  1.00132.56           C  
ANISOU 2180  CD1 LEU B1047    17086  12899  20380   -445     63   1157       C  
ATOM   2181  CD2 LEU B1047     -30.562  28.212  73.031  1.00135.01           C  
ANISOU 2181  CD2 LEU B1047    17625  13371  20303    838   -477   1418       C  
ATOM   2182  N   PHE B1048     -30.747  32.656  69.574  1.00114.77           N  
ANISOU 2182  N   PHE B1048    12261  12613  18734    234  -1164    876       N  
ATOM   2183  CA  PHE B1048     -30.829  33.338  68.272  1.00113.38           C  
ANISOU 2183  CA  PHE B1048    11734  12654  18690    150  -1290    720       C  
ATOM   2184  C   PHE B1048     -29.495  33.160  67.525  1.00112.37           C  
ANISOU 2184  C   PHE B1048    11551  12705  18438    446  -1442    681       C  
ATOM   2185  O   PHE B1048     -29.477  32.740  66.356  1.00109.54           O  
ANISOU 2185  O   PHE B1048    11173  12295  18152    450  -1485    565       O  
ATOM   2186  CB  PHE B1048     -31.193  34.828  68.462  1.00110.75           C  
ANISOU 2186  CB  PHE B1048    11121  12575  18382     10  -1329    704       C  
ATOM   2187  CG  PHE B1048     -31.489  35.573  67.182  1.00108.95           C  
ANISOU 2187  CG  PHE B1048    10709  12476  18212    -37  -1436    557       C  
ATOM   2188  CD1 PHE B1048     -32.802  35.749  66.751  1.00109.51           C  
ANISOU 2188  CD1 PHE B1048    10663  12533  18411   -163  -1435    410       C  
ATOM   2189  CD2 PHE B1048     -30.455  36.136  66.423  1.00108.78           C  
ANISOU 2189  CD2 PHE B1048    10645  12629  18056     54  -1529    520       C  
ATOM   2190  CE1 PHE B1048     -33.083  36.445  65.575  1.00108.85           C  
ANISOU 2190  CE1 PHE B1048    10493  12567  18300    -87  -1574    276       C  
ATOM   2191  CE2 PHE B1048     -30.726  36.830  65.246  1.00108.04           C  
ANISOU 2191  CE2 PHE B1048    10536  12575  17940     25  -1603    404       C  
ATOM   2192  CZ  PHE B1048     -32.042  36.987  64.823  1.00108.54           C  
ANISOU 2192  CZ  PHE B1048    10552  12582  18107     10  -1651    305       C  
ATOM   2193  N   ASN B1049     -28.392  33.458  68.222  1.00112.49           N  
ANISOU 2193  N   ASN B1049    11505  12990  18245    685  -1515    729       N  
ATOM   2194  CA  ASN B1049     -27.026  33.258  67.708  1.00113.83           C  
ANISOU 2194  CA  ASN B1049    11535  13478  18237    990  -1647    602       C  
ATOM   2195  C   ASN B1049     -26.749  31.803  67.355  1.00116.64           C  
ANISOU 2195  C   ASN B1049    12201  13576  18540   1337  -1674    601       C  
ATOM   2196  O   ASN B1049     -26.030  31.521  66.390  1.00116.88           O  
ANISOU 2196  O   ASN B1049    12106  13774  18529   1502  -1759    443       O  
ATOM   2197  CB  ASN B1049     -25.968  33.743  68.717  1.00113.69           C  
ANISOU 2197  CB  ASN B1049    11338  13905  17953   1198  -1718    571       C  
ATOM   2198  CG  ASN B1049     -25.790  35.256  68.713  1.00110.03           C  
ANISOU 2198  CG  ASN B1049    10561  13789  17456    833  -1669    467       C  
ATOM   2199  OD1 ASN B1049     -25.910  35.907  67.673  1.00108.56           O  
ANISOU 2199  OD1 ASN B1049    10284  13622  17341    561  -1626    358       O  
ATOM   2200  ND2 ASN B1049     -25.493  35.819  69.880  1.00108.02           N  
ANISOU 2200  ND2 ASN B1049    10227  13775  17042    826  -1653    495       N  
ATOM   2201  N   GLN B1050     -27.322  30.894  68.151  1.00111.93           N  
ANISOU 2201  N   GLN B1050    12519  11207  18803   -764   -404  -1043       N  
ATOM   2202  CA  GLN B1050     -27.245  29.452  67.906  1.00110.92           C  
ANISOU 2202  CA  GLN B1050    12353  11073  18719   -908   -526  -1062       C  
ATOM   2203  C   GLN B1050     -27.886  29.064  66.570  1.00112.53           C  
ANISOU 2203  C   GLN B1050    12406  11345  19005  -1010   -696  -1041       C  
ATOM   2204  O   GLN B1050     -27.501  28.064  65.970  1.00112.57           O  
ANISOU 2204  O   GLN B1050    12428  11326  19017  -1145   -818  -1132       O  
ATOM   2205  CB  GLN B1050     -27.917  28.682  69.040  1.00110.45           C  
ANISOU 2205  CB  GLN B1050    12213  11011  18744   -926   -416   -958       C  
ATOM   2206  CG  GLN B1050     -27.355  27.286  69.268  1.00108.90           C  
ANISOU 2206  CG  GLN B1050    12047  10752  18579  -1045   -474   -988       C  
ATOM   2207  CD  GLN B1050     -26.429  27.211  70.473  1.00106.76           C  
ANISOU 2207  CD  GLN B1050    11919  10454  18192  -1011   -369   -993       C  
ATOM   2208  OE1 GLN B1050     -26.634  27.904  71.470  1.00106.78           O  
ANISOU 2208  OE1 GLN B1050    11954  10507  18112   -926   -219   -948       O  
ATOM   2209  NE2 GLN B1050     -25.414  26.354  70.392  1.00104.53           N  
ANISOU 2209  NE2 GLN B1050    11712  10099  17904  -1087   -438  -1043       N  
ATOM   2210  N   ILE B1051     -28.865  29.847  66.116  1.00115.03           N  
ANISOU 2210  N   ILE B1051    12568  11751  19389   -955   -694   -918       N  
ATOM   2211  CA  ILE B1051     -29.460  29.642  64.785  1.00116.23           C  
ANISOU 2211  CA  ILE B1051    12564  12022  19577  -1067   -875   -878       C  
ATOM   2212  C   ILE B1051     -28.663  30.407  63.722  1.00114.60           C  
ANISOU 2212  C   ILE B1051    12440  11860  19241  -1050   -975   -954       C  
ATOM   2213  O   ILE B1051     -28.534  29.951  62.590  1.00116.73           O  
ANISOU 2213  O   ILE B1051    12682  12218  19452  -1188  -1146  -1020       O  
ATOM   2214  CB  ILE B1051     -30.980  29.989  64.740  1.00118.97           C  
ANISOU 2214  CB  ILE B1051    12650  12476  20078  -1038   -848   -651       C  
ATOM   2215  CG1 ILE B1051     -31.785  29.043  65.654  1.00118.41           C  
ANISOU 2215  CG1 ILE B1051    12477  12373  20140  -1085   -772   -572       C  
ATOM   2216  CG2 ILE B1051     -31.525  29.915  63.313  1.00119.62           C  
ANISOU 2216  CG2 ILE B1051    12562  12730  20159  -1170  -1057   -590       C  
ATOM   2217  CD1 ILE B1051     -33.240  29.435  65.845  1.00119.75           C  
ANISOU 2217  CD1 ILE B1051    12392  12629  20478  -1026   -700   -328       C  
ATOM   2218  N   VAL B1052     -28.112  31.558  64.086  1.00113.63           N  
ANISOU 2218  N   VAL B1052    12424  11679  19070   -893   -862   -953       N  
ATOM   2219  CA  VAL B1052     -27.204  32.266  63.175  1.00113.99           C  
ANISOU 2219  CA  VAL B1052    12564  11747  18999   -871   -945  -1022       C  
ATOM   2220  C   VAL B1052     -26.077  31.330  62.709  1.00113.19           C  
ANISOU 2220  C   VAL B1052    12618  11613  18775   -996  -1061  -1217       C  
ATOM   2221  O   VAL B1052     -25.883  31.136  61.505  1.00111.56           O  
ANISOU 2221  O   VAL B1052    12387  11507  18494  -1096  -1210  -1266       O  
ATOM   2222  CB  VAL B1052     -26.630  33.567  63.798  1.00112.61           C  
ANISOU 2222  CB  VAL B1052    12509  11471  18808   -696   -786  -1024       C  
ATOM   2223  CG1 VAL B1052     -25.506  34.122  62.945  1.00111.40           C  
ANISOU 2223  CG1 VAL B1052    12473  11319  18535   -687   -874  -1107       C  
ATOM   2224  CG2 VAL B1052     -27.718  34.624  63.942  1.00115.68           C  
ANISOU 2224  CG2 VAL B1052    12725  11880  19349   -565   -661   -829       C  
ATOM   2225  N   ILE B1053     -25.370  30.735  63.678  1.00113.29           N  
ANISOU 2225  N   ILE B1053    12776  11496  18771   -995   -979  -1314       N  
ATOM   2226  CA  ILE B1053     -24.223  29.842  63.426  1.00109.51           C  
ANISOU 2226  CA  ILE B1053    12441  10945  18221  -1088  -1043  -1474       C  
ATOM   2227  C   ILE B1053     -24.603  28.615  62.591  1.00108.17           C  
ANISOU 2227  C   ILE B1053    12188  10814  18097  -1267  -1164  -1542       C  
ATOM   2228  O   ILE B1053     -23.936  28.319  61.597  1.00106.26           O  
ANISOU 2228  O   ILE B1053    12010  10590  17775  -1351  -1258  -1670       O  
ATOM   2229  CB  ILE B1053     -23.494  29.452  64.745  1.00109.04           C  
ANISOU 2229  CB  ILE B1053    12511  10760  18160  -1050   -925  -1501       C  
ATOM   2230  CG1 ILE B1053     -22.175  28.728  64.467  1.00106.97           C  
ANISOU 2230  CG1 ILE B1053    12385  10411  17846  -1112   -973  -1627       C  
ATOM   2231  CG2 ILE B1053     -24.398  28.656  65.684  1.00110.49           C  
ANISOU 2231  CG2 ILE B1053    12590  10926  18464  -1082   -851  -1411       C  
ATOM   2232  CD1 ILE B1053     -21.365  28.478  65.722  1.00106.95           C  
ANISOU 2232  CD1 ILE B1053    12488  10321  17826  -1075   -874  -1608       C  
ATOM   2233  N   THR B1054     -25.683  27.935  62.983  1.00108.21           N  
ANISOU 2233  N   THR B1054    12051  10831  18232  -1332  -1150  -1464       N  
ATOM   2234  CA  THR B1054     -26.218  26.795  62.228  1.00110.55           C  
ANISOU 2234  CA  THR B1054    12249  11162  18594  -1527  -1260  -1533       C  
ATOM   2235  C   THR B1054     -26.453  27.167  60.763  1.00112.83           C  
ANISOU 2235  C   THR B1054    12470  11628  18771  -1621  -1416  -1570       C  
ATOM   2236  O   THR B1054     -26.091  26.403  59.865  1.00113.63           O  
ANISOU 2236  O   THR B1054    12611  11742  18819  -1783  -1506  -1740       O  
ATOM   2237  CB  THR B1054     -27.523  26.241  62.851  1.00111.22           C  
ANISOU 2237  CB  THR B1054    12153  11260  18846  -1574  -1228  -1398       C  
ATOM   2238  OG1 THR B1054     -27.217  25.463  64.018  1.00111.17           O  
ANISOU 2238  OG1 THR B1054    12203  11096  18940  -1552  -1107  -1391       O  
ATOM   2239  CG2 THR B1054     -28.272  25.364  61.871  1.00112.84           C  
ANISOU 2239  CG2 THR B1054    12222  11548  19103  -1794  -1369  -1455       C  
ATOM   2240  N   ILE B1055     -27.034  28.347  60.531  1.00115.03           N  
ANISOU 2240  N   ILE B1055    12643  12047  19017  -1522  -1434  -1406       N  
ATOM   2241  CA  ILE B1055     -27.310  28.827  59.172  1.00117.05           C  
ANISOU 2241  CA  ILE B1055    12800  12517  19158  -1603  -1588  -1377       C  
ATOM   2242  C   ILE B1055     -26.027  29.156  58.386  1.00115.95           C  
ANISOU 2242  C   ILE B1055    12829  12384  18843  -1594  -1631  -1522       C  
ATOM   2243  O   ILE B1055     -25.946  28.862  57.194  1.00118.06           O  
ANISOU 2243  O   ILE B1055    13075  12800  18981  -1749  -1764  -1614       O  
ATOM   2244  CB  ILE B1055     -28.351  29.983  59.146  1.00118.91           C  
ANISOU 2244  CB  ILE B1055    12832  12894  19454  -1490  -1583  -1106       C  
ATOM   2245  CG1 ILE B1055     -29.244  29.873  57.915  1.00121.67           C  
ANISOU 2245  CG1 ILE B1055    12969  13509  19750  -1665  -1773  -1013       C  
ATOM   2246  CG2 ILE B1055     -27.696  31.361  59.186  1.00118.25           C  
ANISOU 2246  CG2 ILE B1055    12825  12782  19323  -1291  -1506  -1034       C  
ATOM   2247  CD1 ILE B1055     -30.608  30.504  58.105  1.00124.28           C  
ANISOU 2247  CD1 ILE B1055    13033  13961  20228  -1599  -1762   -710       C  
ATOM   2248  N   PHE B1056     -25.033  29.746  59.055  1.00111.55           N  
ANISOU 2248  N   PHE B1056    12435  11679  18271  -1428  -1516  -1544       N  
ATOM   2249  CA  PHE B1056     -23.761  30.065  58.410  1.00110.51           C  
ANISOU 2249  CA  PHE B1056    12458  11536  17994  -1406  -1542  -1663       C  
ATOM   2250  C   PHE B1056     -23.051  28.800  57.962  1.00113.08           C  
ANISOU 2250  C   PHE B1056    12896  11793  18276  -1562  -1573  -1891       C  
ATOM   2251  O   PHE B1056     -22.705  28.654  56.785  1.00113.93           O  
ANISOU 2251  O   PHE B1056    13024  12017  18247  -1671  -1667  -2000       O  
ATOM   2252  CB  PHE B1056     -22.837  30.865  59.342  1.00108.41           C  
ANISOU 2252  CB  PHE B1056    12340  11113  17737  -1220  -1412  -1643       C  
ATOM   2253  CG  PHE B1056     -22.887  32.352  59.122  1.00107.11           C  
ANISOU 2253  CG  PHE B1056    12131  11016  17550  -1078  -1396  -1497       C  
ATOM   2254  CD1 PHE B1056     -23.364  33.198  60.117  1.00105.56           C  
ANISOU 2254  CD1 PHE B1056    11900  10745  17465   -933  -1264  -1370       C  
ATOM   2255  CD2 PHE B1056     -22.467  32.907  57.911  1.00106.59           C  
ANISOU 2255  CD2 PHE B1056    12052  11083  17363  -1094  -1495  -1484       C  
ATOM   2256  CE1 PHE B1056     -23.420  34.571  59.910  1.00106.65           C  
ANISOU 2256  CE1 PHE B1056    11989  10905  17628   -800  -1221  -1238       C  
ATOM   2257  CE2 PHE B1056     -22.530  34.276  57.698  1.00106.34           C  
ANISOU 2257  CE2 PHE B1056    11958  11097  17351   -959  -1471  -1320       C  
ATOM   2258  CZ  PHE B1056     -23.002  35.111  58.699  1.00106.19           C  
ANISOU 2258  CZ  PHE B1056    11903  10967  17478   -810  -1328  -1200       C  
ATOM   2259  N   THR B1057     -22.840  27.892  58.917  1.00113.37           N  
ANISOU 2259  N   THR B1057    12998  11641  18438  -1570  -1479  -1953       N  
ATOM   2260  CA  THR B1057     -22.160  26.620  58.676  1.00112.18           C  
ANISOU 2260  CA  THR B1057    12942  11361  18319  -1697  -1461  -2152       C  
ATOM   2261  C   THR B1057     -22.851  25.815  57.565  1.00113.44           C  
ANISOU 2261  C   THR B1057    13013  11639  18450  -1924  -1569  -2281       C  
ATOM   2262  O   THR B1057     -22.178  25.178  56.753  1.00112.12           O  
ANISOU 2262  O   THR B1057    12936  11443  18220  -2041  -1579  -2485       O  
ATOM   2263  CB  THR B1057     -22.046  25.799  59.984  1.00112.37           C  
ANISOU 2263  CB  THR B1057    12994  11178  18524  -1664  -1339  -2125       C  
ATOM   2264  OG1 THR B1057     -21.452  26.609  61.003  1.00107.99           O  
ANISOU 2264  OG1 THR B1057    12517  10562  17950  -1483  -1253  -2011       O  
ATOM   2265  CG2 THR B1057     -21.185  24.553  59.792  1.00115.30           C  
ANISOU 2265  CG2 THR B1057    13458  11372  18977  -1762  -1286  -2300       C  
ATOM   2266  N   ILE B1058     -24.186  25.856  57.525  1.00114.56           N  
ANISOU 2266  N   ILE B1058    12974  11919  18636  -1997  -1644  -2166       N  
ATOM   2267  CA  ILE B1058     -24.928  25.246  56.412  1.00118.80           C  
ANISOU 2267  CA  ILE B1058    13405  12625  19108  -2241  -1777  -2271       C  
ATOM   2268  C   ILE B1058     -24.607  25.986  55.102  1.00119.98           C  
ANISOU 2268  C   ILE B1058    13564  13014  19008  -2285  -1894  -2304       C  
ATOM   2269  O   ILE B1058     -24.335  25.343  54.082  1.00121.21           O  
ANISOU 2269  O   ILE B1058    13770  13245  19041  -2480  -1952  -2522       O  
ATOM   2270  CB  ILE B1058     -26.462  25.170  56.668  1.00120.55           C  
ANISOU 2270  CB  ILE B1058    13401  12965  19437  -2314  -1845  -2098       C  
ATOM   2271  CG1 ILE B1058     -26.806  24.136  57.759  1.00120.43           C  
ANISOU 2271  CG1 ILE B1058    13367  12726  19663  -2335  -1740  -2103       C  
ATOM   2272  CG2 ILE B1058     -27.225  24.856  55.383  1.00122.07           C  
ANISOU 2272  CG2 ILE B1058    13462  13415  19502  -2575  -2023  -2167       C  
ATOM   2273  CD1 ILE B1058     -26.834  22.686  57.306  1.00122.05           C  
ANISOU 2273  CD1 ILE B1058    13591  12832  19952  -2583  -1754  -2340       C  
ATOM   2274  N   GLU B1059     -24.605  27.325  55.152  1.00117.87           N  
ANISOU 2274  N   GLU B1059    13252  12858  18675  -2106  -1910  -2094       N  
ATOM   2275  CA  GLU B1059     -24.288  28.170  53.987  1.00116.94           C  
ANISOU 2275  CA  GLU B1059    13119  12974  18338  -2116  -2012  -2060       C  
ATOM   2276  C   GLU B1059     -22.872  27.927  53.471  1.00115.55           C  
ANISOU 2276  C   GLU B1059    13152  12716  18037  -2122  -1964  -2281       C  
ATOM   2277  O   GLU B1059     -22.640  27.987  52.260  1.00115.81           O  
ANISOU 2277  O   GLU B1059    13188  12954  17860  -2246  -2056  -2368       O  
ATOM   2278  CB  GLU B1059     -24.468  29.664  54.307  1.00115.95           C  
ANISOU 2278  CB  GLU B1059    12908  12910  18237  -1892  -1995  -1777       C  
ATOM   2279  CG  GLU B1059     -24.208  30.605  53.130  1.00115.80           C  
ANISOU 2279  CG  GLU B1059    12836  13139  18023  -1889  -2098  -1682       C  
ATOM   2280  CD  GLU B1059     -23.281  31.775  53.471  1.00114.80           C  
ANISOU 2280  CD  GLU B1059    12807  12900  17912  -1650  -2002  -1583       C  
ATOM   2281  OE1 GLU B1059     -23.082  32.075  54.674  1.00112.51           O  
ANISOU 2281  OE1 GLU B1059    12588  12377  17783  -1481  -1865  -1545       O  
ATOM   2282  OE2 GLU B1059     -22.741  32.403  52.525  1.00113.76           O  
ANISOU 2282  OE2 GLU B1059    12678  12924  17622  -1644  -2064  -1545       O  
ATOM   2283  N   ILE B1060     -21.933  27.664  54.384  1.00114.13           N  
ANISOU 2283  N   ILE B1060    13132  12255  17977  -1992  -1819  -2352       N  
ATOM   2284  CA  ILE B1060     -20.540  27.419  53.991  1.00113.62           C  
ANISOU 2284  CA  ILE B1060    13252  12086  17832  -1977  -1753  -2532       C  
ATOM   2285  C   ILE B1060     -20.385  26.055  53.319  1.00114.09           C  
ANISOU 2285  C   ILE B1060    13373  12101  17877  -2200  -1738  -2815       C  
ATOM   2286  O   ILE B1060     -19.575  25.908  52.408  1.00114.02           O  
ANISOU 2286  O   ILE B1060    13464  12137  17722  -2263  -1727  -2981       O  
ATOM   2287  CB  ILE B1060     -19.533  27.590  55.162  1.00112.08           C  
ANISOU 2287  CB  ILE B1060    13189  11629  17769  -1779  -1612  -2489       C  
ATOM   2288  CG1 ILE B1060     -18.169  28.065  54.644  1.00110.62           C  
ANISOU 2288  CG1 ILE B1060    13139  11427  17463  -1699  -1580  -2545       C  
ATOM   2289  CG2 ILE B1060     -19.380  26.310  55.977  1.00112.20           C  
ANISOU 2289  CG2 ILE B1060    13256  11398  17977  -1828  -1505  -2597       C  
ATOM   2290  CD1 ILE B1060     -17.952  29.559  54.783  1.00110.73           C  
ANISOU 2290  CD1 ILE B1060    13136  11520  17416  -1523  -1604  -2345       C  
ATOM   2291  N   ILE B1061     -21.172  25.076  53.763  1.00114.63           N  
ANISOU 2291  N   ILE B1061    13377  12074  18105  -2321  -1724  -2872       N  
ATOM   2292  CA  ILE B1061     -21.197  23.746  53.137  1.00117.16           C  
ANISOU 2292  CA  ILE B1061    13737  12330  18447  -2561  -1699  -3155       C  
ATOM   2293  C   ILE B1061     -21.947  23.802  51.796  1.00119.78           C  
ANISOU 2293  C   ILE B1061    13976  12994  18540  -2799  -1863  -3246       C  
ATOM   2294  O   ILE B1061     -21.629  23.058  50.855  1.00119.59           O  
ANISOU 2294  O   ILE B1061    14032  13002  18406  -3003  -1848  -3527       O  
ATOM   2295  CB  ILE B1061     -21.786  22.669  54.092  1.00116.61           C  
ANISOU 2295  CB  ILE B1061    13617  12030  18660  -2618  -1623  -3170       C  
ATOM   2296  CG1 ILE B1061     -20.815  22.408  55.262  1.00113.44           C  
ANISOU 2296  CG1 ILE B1061    13321  11315  18465  -2423  -1451  -3113       C  
ATOM   2297  CG2 ILE B1061     -22.078  21.368  53.345  1.00118.28           C  
ANISOU 2297  CG2 ILE B1061    13837  12196  18909  -2904  -1612  -3464       C  
ATOM   2298  CD1 ILE B1061     -21.414  21.672  56.446  1.00111.73           C  
ANISOU 2298  CD1 ILE B1061    13024  10909  18519  -2412  -1381  -3012       C  
ATOM   2299  N   LEU B1062     -22.917  24.713  51.715  1.00120.36           N  
ANISOU 2299  N   LEU B1062    13875  13324  18531  -2775  -2008  -2998       N  
ATOM   2300  CA  LEU B1062     -23.713  24.913  50.504  1.00123.89           C  
ANISOU 2300  CA  LEU B1062    14187  14146  18738  -2995  -2193  -2998       C  
ATOM   2301  C   LEU B1062     -22.883  25.437  49.333  1.00125.32           C  
ANISOU 2301  C   LEU B1062    14452  14537  18627  -3023  -2232  -3082       C  
ATOM   2302  O   LEU B1062     -23.082  25.002  48.196  1.00131.98           O  
ANISOU 2302  O   LEU B1062    15284  15618  19246  -3285  -2323  -3268       O  
ATOM   2303  CB  LEU B1062     -24.908  25.842  50.771  1.00123.16           C  
ANISOU 2303  CB  LEU B1062    13859  14264  18673  -2924  -2320  -2646       C  
ATOM   2304  CG  LEU B1062     -26.157  25.260  51.447  1.00122.91           C  
ANISOU 2304  CG  LEU B1062    13667  14187  18846  -3012  -2351  -2559       C  
ATOM   2305  CD1 LEU B1062     -26.992  26.366  52.073  1.00121.23           C  
ANISOU 2305  CD1 LEU B1062    13263  14064  18734  -2817  -2384  -2178       C  
ATOM   2306  CD2 LEU B1062     -26.990  24.441  50.474  1.00126.38           C  
ANISOU 2306  CD2 LEU B1062    13999  14860  19161  -3368  -2502  -2713       C  
ATOM   2307  N   ARG B1063     -21.967  26.366  49.603  1.00120.99           N  
ANISOU 2307  N   ARG B1063    13984  13915  18070  -2770  -2163  -2949       N  
ATOM   2308  CA  ARG B1063     -21.141  26.952  48.546  1.00120.78           C  
ANISOU 2308  CA  ARG B1063    14024  14084  17782  -2768  -2191  -2986       C  
ATOM   2309  C   ARG B1063     -20.036  25.991  48.116  1.00120.75           C  
ANISOU 2309  C   ARG B1063    14232  13915  17732  -2860  -2053  -3339       C  
ATOM   2310  O   ARG B1063     -19.617  26.004  46.957  1.00121.72           O  
ANISOU 2310  O   ARG B1063    14403  14254  17591  -2990  -2083  -3481       O  
ATOM   2311  CB  ARG B1063     -20.537  28.295  48.980  1.00119.95           C  
ANISOU 2311  CB  ARG B1063    13923  13941  17711  -2473  -2160  -2717       C  
ATOM   2312  CG  ARG B1063     -21.556  29.370  49.358  1.00120.40           C  
ANISOU 2312  CG  ARG B1063    13769  14137  17839  -2357  -2256  -2362       C  
ATOM   2313  CD  ARG B1063     -20.948  30.770  49.336  1.00119.85           C  
ANISOU 2313  CD  ARG B1063    13690  14101  17744  -2125  -2239  -2128       C  
ATOM   2314  NE  ARG B1063     -20.039  31.026  50.457  1.00117.88           N  
ANISOU 2314  NE  ARG B1063    13595  13513  17683  -1898  -2081  -2132       N  
ATOM   2315  CZ  ARG B1063     -19.323  32.141  50.622  1.00117.62           C  
ANISOU 2315  CZ  ARG B1063    13595  13428  17666  -1698  -2035  -1979       C  
ATOM   2316  NH1 ARG B1063     -19.383  33.134  49.740  1.00118.17           N  
ANISOU 2316  NH1 ARG B1063    13552  13744  17604  -1671  -2121  -1789       N  
ATOM   2317  NH2 ARG B1063     -18.536  32.264  51.682  1.00116.71           N  
ANISOU 2317  NH2 ARG B1063    13618  13020  17706  -1535  -1904  -2004       N  
ATOM   2318  N   ILE B1064     -19.569  25.160  49.052  1.00119.72           N  
ANISOU 2318  N   ILE B1064    14216  13408  17864  -2791  -1890  -3464       N  
ATOM   2319  CA  ILE B1064     -18.495  24.196  48.772  1.00118.69           C  
ANISOU 2319  CA  ILE B1064    14272  13058  17768  -2848  -1717  -3772       C  
ATOM   2320  C   ILE B1064     -18.911  23.335  47.595  1.00122.15           C  
ANISOU 2320  C   ILE B1064    14720  13673  18019  -3178  -1754  -4083       C  
ATOM   2321  O   ILE B1064     -18.197  23.283  46.598  1.00123.90           O  
ANISOU 2321  O   ILE B1064    15044  14009  18024  -3260  -1709  -4272       O  
ATOM   2322  CB  ILE B1064     -18.118  23.317  50.003  1.00116.56           C  
ANISOU 2322  CB  ILE B1064    14073  12362  17851  -2747  -1543  -3815       C  
ATOM   2323  CG1 ILE B1064     -17.628  24.164  51.189  1.00111.51           C  
ANISOU 2323  CG1 ILE B1064    13438  11576  17356  -2448  -1506  -3529       C  
ATOM   2324  CG2 ILE B1064     -17.045  22.295  49.646  1.00117.82           C  
ANISOU 2324  CG2 ILE B1064    14397  12284  18085  -2807  -1345  -4113       C  
ATOM   2325  CD1 ILE B1064     -16.351  24.945  50.955  1.00109.07           C  
ANISOU 2325  CD1 ILE B1064    13233  11265  16943  -2276  -1453  -3473       C  
ATOM   2326  N   TYR B1065     -20.086  22.703  47.710  1.00126.26           N  
ANISOU 2326  N   TYR B1065    15129  14234  18611  -3375  -1837  -4130       N  
ATOM   2327  CA  TYR B1065     -20.685  21.864  46.645  1.00130.02           C  
ANISOU 2327  CA  TYR B1065    15593  14903  18906  -3740  -1899  -4433       C  
ATOM   2328  C   TYR B1065     -21.223  22.656  45.437  1.00131.27           C  
ANISOU 2328  C   TYR B1065    15637  15582  18659  -3903  -2118  -4352       C  
ATOM   2329  O   TYR B1065     -22.135  22.202  44.755  1.00134.11           O  
ANISOU 2329  O   TYR B1065    15905  16191  18861  -4213  -2250  -4479       O  
ATOM   2330  CB  TYR B1065     -21.817  20.995  47.212  1.00131.60           C  
ANISOU 2330  CB  TYR B1065    15685  14988  19331  -3903  -1936  -4469       C  
ATOM   2331  CG  TYR B1065     -21.394  19.863  48.129  1.00131.86           C  
ANISOU 2331  CG  TYR B1065    15819  14538  19746  -3852  -1714  -4625       C  
ATOM   2332  CD1 TYR B1065     -21.685  19.905  49.494  1.00129.25           C  
ANISOU 2332  CD1 TYR B1065    15413  13972  19724  -3647  -1679  -4369       C  
ATOM   2333  CD2 TYR B1065     -20.732  18.734  47.629  1.00134.54           C  
ANISOU 2333  CD2 TYR B1065    16316  14657  20144  -4016  -1526  -5020       C  
ATOM   2334  CE1 TYR B1065     -21.315  18.870  50.340  1.00129.24           C  
ANISOU 2334  CE1 TYR B1065    15476  13555  20075  -3603  -1484  -4463       C  
ATOM   2335  CE2 TYR B1065     -20.359  17.689  48.468  1.00135.14           C  
ANISOU 2335  CE2 TYR B1065    16456  14278  20613  -3962  -1311  -5121       C  
ATOM   2336  CZ  TYR B1065     -20.652  17.764  49.824  1.00132.83           C  
ANISOU 2336  CZ  TYR B1065    16070  13784  20617  -3755  -1302  -4824       C  
ATOM   2337  OH  TYR B1065     -20.285  16.733  50.667  1.00133.40           O  
ANISOU 2337  OH  TYR B1065    16179  13428  21079  -3701  -1095  -4878       O  
ATOM   2338  N   VAL B1066     -20.661  23.837  45.189  1.00131.02           N  
ANISOU 2338  N   VAL B1066    15596  15719  18467  -3703  -2160  -4123       N  
ATOM   2339  CA  VAL B1066     -20.993  24.661  44.023  1.00133.35           C  
ANISOU 2339  CA  VAL B1066    15774  16511  18380  -3825  -2350  -3999       C  
ATOM   2340  C   VAL B1066     -19.711  24.951  43.235  1.00135.00           C  
ANISOU 2340  C   VAL B1066    16142  16780  18370  -3767  -2246  -4126       C  
ATOM   2341  O   VAL B1066     -19.690  24.875  42.007  1.00136.22           O  
ANISOU 2341  O   VAL B1066    16305  17280  18173  -4000  -2311  -4283       O  
ATOM   2342  CB  VAL B1066     -21.703  25.972  44.442  1.00131.15           C  
ANISOU 2342  CB  VAL B1066    15275  16414  18141  -3628  -2511  -3519       C  
ATOM   2343  CG1 VAL B1066     -21.701  26.994  43.315  1.00132.67           C  
ANISOU 2343  CG1 VAL B1066    15354  17068  17985  -3667  -2664  -3322       C  
ATOM   2344  CG2 VAL B1066     -23.125  25.688  44.900  1.00132.38           C  
ANISOU 2344  CG2 VAL B1066    15237  16628  18434  -3750  -2639  -3393       C  
ATOM   2345  N   HIS B1067     -18.648  25.289  43.963  1.00134.72           N  
ANISOU 2345  N   HIS B1067    16224  16425  18538  -3464  -2086  -4046       N  
ATOM   2346  CA  HIS B1067     -17.296  25.407  43.409  1.00136.37           C  
ANISOU 2346  CA  HIS B1067    16599  16593  18622  -3380  -1941  -4178       C  
ATOM   2347  C   HIS B1067     -16.295  25.306  44.522  1.00134.24           C  
ANISOU 2347  C   HIS B1067    16455  15863  18687  -3099  -1746  -4146       C  
ATOM   2348  O   HIS B1067     -15.939  26.310  45.148  1.00131.02           O  
ANISOU 2348  O   HIS B1067    16010  15394  18377  -2835  -1765  -3847       O  
ATOM   2349  CB  HIS B1067     -17.108  26.675  42.555  1.00137.68           C  
ANISOU 2349  CB  HIS B1067    16674  17154  18484  -3319  -2072  -3926       C  
ATOM   2350  CG  HIS B1067     -17.571  27.965  43.212  1.00135.91           C  
ANISOU 2350  CG  HIS B1067    16275  16985  18380  -3081  -2201  -3471       C  
ATOM   2351  ND1 HIS B1067     -18.505  28.003  44.187  1.00135.05           N  
ANISOU 2351  ND1 HIS B1067    16051  16748  18515  -3021  -2261  -3305       N  
ATOM   2352  CD2 HIS B1067     -17.221  29.288  42.956  1.00134.99           C  
ANISOU 2352  CD2 HIS B1067    16075  17045  18171  -2895  -2264  -3151       C  
ATOM   2353  CE1 HIS B1067     -18.719  29.279  44.552  1.00134.83           C  
ANISOU 2353  CE1 HIS B1067    15885  16791  18552  -2805  -2339  -2922       C  
ATOM   2354  NE2 HIS B1067     -17.935  30.066  43.799  1.00134.20           N  
ANISOU 2354  NE2 HIS B1067    15822  16889  18280  -2729  -2343  -2825       N  
ATOM   2355  N   ARG B1068     -15.850  24.074  44.782  1.00135.66           N  
ANISOU 2355  N   ARG B1068    16773  15715  19055  -3167  -1553  -4451       N  
ATOM   2356  CA  ARG B1068     -15.003  23.781  45.946  1.00134.36           C  
ANISOU 2356  CA  ARG B1068    16699  15106  19245  -2930  -1371  -4404       C  
ATOM   2357  C   ARG B1068     -13.539  24.227  45.791  1.00133.15           C  
ANISOU 2357  C   ARG B1068    16663  14858  19072  -2732  -1234  -4369       C  
ATOM   2358  O   ARG B1068     -12.985  24.888  46.691  1.00127.89           O  
ANISOU 2358  O   ARG B1068    15990  14030  18571  -2476  -1217  -4116       O  
ATOM   2359  CB  ARG B1068     -15.112  22.303  46.355  1.00135.07           C  
ANISOU 2359  CB  ARG B1068    16857  14863  19602  -3060  -1208  -4681       C  
ATOM   2360  CG  ARG B1068     -14.849  21.303  45.249  1.00139.30           C  
ANISOU 2360  CG  ARG B1068    17508  15413  20007  -3319  -1075  -5104       C  
ATOM   2361  CD  ARG B1068     -14.867  19.885  45.793  1.00142.39           C  
ANISOU 2361  CD  ARG B1068    17958  15396  20749  -3408   -878  -5345       C  
ATOM   2362  NE  ARG B1068     -14.222  18.944  44.873  1.00145.09           N  
ANISOU 2362  NE  ARG B1068    18449  15632  21046  -3584   -656  -5760       N  
ATOM   2363  CZ  ARG B1068     -14.249  17.620  45.007  1.00148.51           C  
ANISOU 2363  CZ  ARG B1068    18943  15730  21754  -3726   -454  -6054       C  
ATOM   2364  NH1 ARG B1068     -14.899  17.050  46.022  1.00148.05           N  
ANISOU 2364  NH1 ARG B1068    18799  15423  22031  -3717   -461  -5959       N  
ATOM   2365  NH2 ARG B1068     -13.627  16.856  44.117  1.00153.09           N  
ANISOU 2365  NH2 ARG B1068    19666  16214  22286  -3881   -227  -6445       N  
ATOM   2366  N   ILE B1069     -12.929  23.883  44.651  1.00133.34           N  
ANISOU 2366  N   ILE B1069    16786  14993  18882  -2861  -1136  -4625       N  
ATOM   2367  CA  ILE B1069     -11.593  24.386  44.301  1.00130.66           C  
ANISOU 2367  CA  ILE B1069    16537  14632  18477  -2693  -1019  -4579       C  
ATOM   2368  C   ILE B1069     -11.591  25.924  44.317  1.00127.33           C  
ANISOU 2368  C   ILE B1069    16011  14459  17911  -2518  -1199  -4206       C  
ATOM   2369  O   ILE B1069     -10.702  26.547  44.908  1.00123.05           O  
ANISOU 2369  O   ILE B1069    15492  13755  17506  -2277  -1146  -4004       O  
ATOM   2370  CB  ILE B1069     -11.109  23.855  42.927  1.00132.86           C  
ANISOU 2370  CB  ILE B1069    16925  15070  18486  -2889   -894  -4916       C  
ATOM   2371  CG1 ILE B1069     -11.100  22.318  42.919  1.00134.99           C  
ANISOU 2371  CG1 ILE B1069    17303  15045  18943  -3066   -679  -5312       C  
ATOM   2372  CG2 ILE B1069      -9.712  24.382  42.613  1.00132.41           C  
ANISOU 2372  CG2 ILE B1069    16946  14980  18384  -2697   -761  -4839       C  
ATOM   2373  CD1 ILE B1069     -10.948  21.690  41.544  1.00137.30           C  
ANISOU 2373  CD1 ILE B1069    17702  15522  18943  -3335   -562  -5715       C  
ATOM   2374  N   SER B1070     -12.611  26.514  43.693  1.00126.69           N  
ANISOU 2374  N   SER B1070    15801  14762  17575  -2649  -1409  -4104       N  
ATOM   2375  CA  SER B1070     -12.767  27.968  43.623  1.00123.92           C  
ANISOU 2375  CA  SER B1070    15319  14655  17109  -2503  -1575  -3737       C  
ATOM   2376  C   SER B1070     -13.067  28.649  44.965  1.00119.55           C  
ANISOU 2376  C   SER B1070    14688  13895  16840  -2279  -1629  -3440       C  
ATOM   2377  O   SER B1070     -12.858  29.856  45.087  1.00118.96           O  
ANISOU 2377  O   SER B1070    14543  13901  16755  -2105  -1696  -3154       O  
ATOM   2378  CB  SER B1070     -13.837  28.345  42.592  1.00126.20           C  
ANISOU 2378  CB  SER B1070    15459  15420  17072  -2715  -1780  -3678       C  
ATOM   2379  OG  SER B1070     -13.419  28.040  41.274  1.00126.86           O  
ANISOU 2379  OG  SER B1070    15609  15772  16822  -2902  -1742  -3899       O  
ATOM   2380  N   PHE B1071     -13.559  27.894  45.953  1.00117.44           N  
ANISOU 2380  N   PHE B1071    14432  13368  16823  -2291  -1589  -3511       N  
ATOM   2381  CA  PHE B1071     -13.837  28.442  47.291  1.00115.08           C  
ANISOU 2381  CA  PHE B1071    14075  12872  16779  -2095  -1614  -3263       C  
ATOM   2382  C   PHE B1071     -12.524  28.682  48.038  1.00113.79           C  
ANISOU 2382  C   PHE B1071    14023  12424  16788  -1875  -1477  -3197       C  
ATOM   2383  O   PHE B1071     -12.225  29.810  48.447  1.00110.46           O  
ANISOU 2383  O   PHE B1071    13567  12005  16397  -1696  -1517  -2954       O  
ATOM   2384  CB  PHE B1071     -14.760  27.503  48.095  1.00114.82           C  
ANISOU 2384  CB  PHE B1071    14009  12672  16944  -2188  -1607  -3350       C  
ATOM   2385  CG  PHE B1071     -14.914  27.878  49.556  1.00111.89           C  
ANISOU 2385  CG  PHE B1071    13608  12074  16832  -1996  -1589  -3140       C  
ATOM   2386  CD1 PHE B1071     -16.050  28.544  49.998  1.00111.20           C  
ANISOU 2386  CD1 PHE B1071    13372  12102  16777  -1965  -1709  -2926       C  
ATOM   2387  CD2 PHE B1071     -13.933  27.542  50.501  1.00108.77           C  
ANISOU 2387  CD2 PHE B1071    13322  11359  16647  -1855  -1442  -3150       C  
ATOM   2388  CE1 PHE B1071     -16.197  28.888  51.344  1.00108.46           C  
ANISOU 2388  CE1 PHE B1071    13008  11555  16645  -1800  -1669  -2760       C  
ATOM   2389  CE2 PHE B1071     -14.081  27.882  51.842  1.00105.21           C  
ANISOU 2389  CE2 PHE B1071    12845  10740  16389  -1706  -1429  -2968       C  
ATOM   2390  CZ  PHE B1071     -15.217  28.552  52.265  1.00103.81           C  
ANISOU 2390  CZ  PHE B1071    12542  10679  16223  -1681  -1534  -2791       C  
ATOM   2391  N   PHE B1072     -11.748  27.606  48.196  1.00114.96           N  
ANISOU 2391  N   PHE B1072    14294  12322  17061  -1899  -1309  -3410       N  
ATOM   2392  CA  PHE B1072     -10.446  27.632  48.866  1.00111.60           C  
ANISOU 2392  CA  PHE B1072    13962  11630  16812  -1718  -1172  -3350       C  
ATOM   2393  C   PHE B1072      -9.371  28.297  47.987  1.00111.19           C  
ANISOU 2393  C   PHE B1072    13958  11700  16590  -1648  -1139  -3318       C  
ATOM   2394  O   PHE B1072      -8.188  27.924  48.029  1.00110.06           O  
ANISOU 2394  O   PHE B1072    13905  11371  16541  -1573   -986  -3374       O  
ATOM   2395  CB  PHE B1072     -10.030  26.210  49.272  1.00112.11           C  
ANISOU 2395  CB  PHE B1072    14107  11389  17099  -1770   -990  -3555       C  
ATOM   2396  CG  PHE B1072     -10.968  25.553  50.250  1.00112.02           C  
ANISOU 2396  CG  PHE B1072    14042  11232  17291  -1818  -1007  -3549       C  
ATOM   2397  CD1 PHE B1072     -11.949  24.675  49.812  1.00114.99           C  
ANISOU 2397  CD1 PHE B1072    14388  11656  17646  -2030  -1023  -3757       C  
ATOM   2398  CD2 PHE B1072     -10.860  25.799  51.613  1.00110.64           C  
ANISOU 2398  CD2 PHE B1072    13841  10880  17319  -1666  -1006  -3338       C  
ATOM   2399  CE1 PHE B1072     -12.809  24.065  50.711  1.00114.90           C  
ANISOU 2399  CE1 PHE B1072    14313  11506  17836  -2073  -1034  -3733       C  
ATOM   2400  CE2 PHE B1072     -11.718  25.195  52.522  1.00110.89           C  
ANISOU 2400  CE2 PHE B1072    13813  10793  17528  -1707  -1012  -3316       C  
ATOM   2401  CZ  PHE B1072     -12.694  24.326  52.070  1.00112.75           C  
ANISOU 2401  CZ  PHE B1072    14010  11063  17765  -1902  -1025  -3504       C  
ATOM   2402  N   LYS B1073      -9.808  29.271  47.186  1.00110.50           N  
ANISOU 2402  N   LYS B1073    13791  11930  16265  -1671  -1279  -3201       N  
ATOM   2403  CA  LYS B1073      -8.932  30.103  46.365  1.00110.97           C  
ANISOU 2403  CA  LYS B1073    13861  12148  16154  -1596  -1276  -3106       C  
ATOM   2404  C   LYS B1073      -9.341  31.579  46.438  1.00110.59           C  
ANISOU 2404  C   LYS B1073    13689  12278  16053  -1484  -1432  -2793       C  
ATOM   2405  O   LYS B1073      -8.578  32.458  46.019  1.00112.60           O  
ANISOU 2405  O   LYS B1073    13934  12614  16234  -1379  -1433  -2644       O  
ATOM   2406  CB  LYS B1073      -8.912  29.632  44.908  1.00114.01           C  
ANISOU 2406  CB  LYS B1073    14275  12793  16252  -1782  -1250  -3324       C  
ATOM   2407  CG  LYS B1073      -7.972  28.463  44.641  1.00117.14           C  
ANISOU 2407  CG  LYS B1073    14817  12985  16707  -1831  -1027  -3613       C  
ATOM   2408  CD  LYS B1073      -7.846  28.157  43.149  1.00120.41           C  
ANISOU 2408  CD  LYS B1073    15272  13681  16796  -2012   -980  -3837       C  
ATOM   2409  CE  LYS B1073      -6.932  29.157  42.446  1.00119.78           C  
ANISOU 2409  CE  LYS B1073    15181  13789  16542  -1894   -978  -3662       C  
ATOM   2410  NZ  LYS B1073      -6.971  29.020  40.968  1.00121.45           N  
ANISOU 2410  NZ  LYS B1073    15409  14362  16376  -2084   -965  -3839       N  
ATOM   2411  N   ASP B1074     -10.531  31.850  46.974  1.00107.94           N  
ANISOU 2411  N   ASP B1074    13248  11986  15780  -1502  -1545  -2684       N  
ATOM   2412  CA  ASP B1074     -11.002  33.230  47.132  1.00107.00           C  
ANISOU 2412  CA  ASP B1074    12997  11987  15670  -1386  -1660  -2382       C  
ATOM   2413  C   ASP B1074     -10.653  33.848  48.519  1.00104.46           C  
ANISOU 2413  C   ASP B1074    12705  11378  15608  -1195  -1614  -2234       C  
ATOM   2414  O   ASP B1074     -10.945  33.252  49.564  1.00102.56           O  
ANISOU 2414  O   ASP B1074    12504  10930  15535  -1191  -1571  -2303       O  
ATOM   2415  CB  ASP B1074     -12.504  33.315  46.837  1.00107.58           C  
ANISOU 2415  CB  ASP B1074    12914  12299  15664  -1507  -1799  -2311       C  
ATOM   2416  CG  ASP B1074     -12.905  34.647  46.211  1.00109.52           C  
ANISOU 2416  CG  ASP B1074    12990  12812  15810  -1448  -1915  -2010       C  
ATOM   2417  OD1 ASP B1074     -13.936  35.215  46.633  1.00109.34           O  
ANISOU 2417  OD1 ASP B1074    12823  12829  15891  -1410  -1990  -1817       O  
ATOM   2418  OD2 ASP B1074     -12.187  35.131  45.303  1.00109.56           O  
ANISOU 2418  OD2 ASP B1074    12993  12983  15652  -1432  -1918  -1948       O  
ATOM   2419  N   PRO B1075     -10.036  35.051  48.530  1.00103.45           N  
ANISOU 2419  N   PRO B1075    12553  11248  15506  -1049  -1621  -2030       N  
ATOM   2420  CA  PRO B1075      -9.588  35.662  49.786  1.00102.84           C  
ANISOU 2420  CA  PRO B1075    12520  10912  15643   -899  -1571  -1924       C  
ATOM   2421  C   PRO B1075     -10.748  36.069  50.694  1.00103.61           C  
ANISOU 2421  C   PRO B1075    12536  10957  15875   -867  -1607  -1825       C  
ATOM   2422  O   PRO B1075     -10.540  36.412  51.867  1.00102.29           O  
ANISOU 2422  O   PRO B1075    12417  10578  15869   -776  -1554  -1785       O  
ATOM   2423  CB  PRO B1075      -8.817  36.908  49.322  1.00102.31           C  
ANISOU 2423  CB  PRO B1075    12421  10901  15553   -787  -1582  -1733       C  
ATOM   2424  CG  PRO B1075      -8.543  36.694  47.868  1.00103.77           C  
ANISOU 2424  CG  PRO B1075    12580  11343  15506   -869  -1607  -1768       C  
ATOM   2425  CD  PRO B1075      -9.721  35.915  47.378  1.00105.58           C  
ANISOU 2425  CD  PRO B1075    12748  11762  15607  -1031  -1673  -1884       C  
ATOM   2426  N   TRP B1076     -11.957  36.016  50.148  1.00104.91           N  
ANISOU 2426  N   TRP B1076    12572  11327  15963   -952  -1691  -1786       N  
ATOM   2427  CA  TRP B1076     -13.165  36.380  50.880  1.00104.24           C  
ANISOU 2427  CA  TRP B1076    12382  11217  16009   -922  -1714  -1674       C  
ATOM   2428  C   TRP B1076     -13.839  35.152  51.426  1.00103.39           C  
ANISOU 2428  C   TRP B1076    12301  11041  15942  -1032  -1703  -1842       C  
ATOM   2429  O   TRP B1076     -14.618  35.234  52.373  1.00102.29           O  
ANISOU 2429  O   TRP B1076    12119  10802  15945   -994  -1682  -1788       O  
ATOM   2430  CB  TRP B1076     -14.107  37.132  49.958  1.00106.41           C  
ANISOU 2430  CB  TRP B1076    12458  11769  16204   -943  -1818  -1468       C  
ATOM   2431  CG  TRP B1076     -13.402  38.171  49.122  1.00108.68           C  
ANISOU 2431  CG  TRP B1076    12699  12173  16419   -866  -1837  -1298       C  
ATOM   2432  CD1 TRP B1076     -12.799  37.998  47.876  1.00110.41           C  
ANISOU 2432  CD1 TRP B1076    12924  12615  16413   -944  -1883  -1328       C  
ATOM   2433  CD2 TRP B1076     -13.194  39.584  49.454  1.00107.84           C  
ANISOU 2433  CD2 TRP B1076    12532  11965  16478   -695  -1795  -1065       C  
ATOM   2434  NE1 TRP B1076     -12.249  39.178  47.428  1.00110.31           N  
ANISOU 2434  NE1 TRP B1076    12845  12654  16412   -829  -1884  -1107       N  
ATOM   2435  CE2 TRP B1076     -12.458  40.168  48.324  1.00108.54           C  
ANISOU 2435  CE2 TRP B1076    12577  12231  16433   -679  -1833   -942       C  
ATOM   2436  CE3 TRP B1076     -13.535  40.394  50.532  1.00105.36           C  
ANISOU 2436  CE3 TRP B1076    12196  11432  16403   -567  -1717   -962       C  
ATOM   2437  CZ2 TRP B1076     -12.092  41.500  48.297  1.00108.92           C  
ANISOU 2437  CZ2 TRP B1076    12551  12218  16614   -536  -1800   -708       C  
ATOM   2438  CZ3 TRP B1076     -13.164  41.734  50.493  1.00107.22           C  
ANISOU 2438  CZ3 TRP B1076    12371  11597  16769   -432  -1673   -758       C  
ATOM   2439  CH2 TRP B1076     -12.459  42.274  49.399  1.00110.13           C  
ANISOU 2439  CH2 TRP B1076    12687  12123  17033   -415  -1717   -625       C  
ATOM   2440  N   SER B1077     -13.534  34.001  50.834  1.00103.26           N  
ANISOU 2440  N   SER B1077    12355  11066  15813  -1169  -1700  -2050       N  
ATOM   2441  CA  SER B1077     -14.117  32.742  51.270  1.00104.81           C  
ANISOU 2441  CA  SER B1077    12574  11178  16071  -1288  -1679  -2221       C  
ATOM   2442  C   SER B1077     -13.398  32.209  52.511  1.00102.99           C  
ANISOU 2442  C   SER B1077    12471  10643  16019  -1213  -1561  -2293       C  
ATOM   2443  O   SER B1077     -13.956  32.237  53.618  1.00100.86           O  
ANISOU 2443  O   SER B1077    12177  10254  15892  -1165  -1537  -2229       O  
ATOM   2444  CB  SER B1077     -14.122  31.704  50.132  1.00108.32           C  
ANISOU 2444  CB  SER B1077    13041  11769  16345  -1484  -1701  -2438       C  
ATOM   2445  OG  SER B1077     -14.959  32.104  49.049  1.00110.28           O  
ANISOU 2445  OG  SER B1077    13148  12350  16402  -1593  -1834  -2359       O  
ATOM   2446  N   LEU B1078     -12.161  31.737  52.334  1.00102.23           N  
ANISOU 2446  N   LEU B1078    12495  10435  15912  -1204  -1482  -2404       N  
ATOM   2447  CA  LEU B1078     -11.372  31.189  53.453  1.00100.79           C  
ANISOU 2447  CA  LEU B1078    12410   9989  15898  -1141  -1377  -2434       C  
ATOM   2448  C   LEU B1078     -11.403  32.096  54.690  1.00101.65           C  
ANISOU 2448  C   LEU B1078    12512  10000  16109  -1012  -1374  -2263       C  
ATOM   2449  O   LEU B1078     -11.164  31.638  55.812  1.00102.43           O  
ANISOU 2449  O   LEU B1078    12654   9930  16333   -988  -1312  -2259       O  
ATOM   2450  CB  LEU B1078      -9.928  30.909  53.021  1.00 97.95           C  
ANISOU 2450  CB  LEU B1078    12150   9547  15519  -1112  -1294  -2501       C  
ATOM   2451  CG  LEU B1078      -9.654  29.556  52.358  1.00 98.24           C  
ANISOU 2451  CG  LEU B1078    12238   9531  15558  -1233  -1206  -2724       C  
ATOM   2452  CD1 LEU B1078      -8.438  29.619  51.444  1.00 98.76           C  
ANISOU 2452  CD1 LEU B1078    12372   9620  15532  -1208  -1138  -2778       C  
ATOM   2453  CD2 LEU B1078      -9.483  28.466  53.403  1.00 96.79           C  
ANISOU 2453  CD2 LEU B1078    12085   9093  15598  -1238  -1103  -2768       C  
ATOM   2454  N   PHE B1079     -11.688  33.383  54.464  1.00102.10           N  
ANISOU 2454  N   PHE B1079    12511  10171  16114   -938  -1432  -2122       N  
ATOM   2455  CA  PHE B1079     -11.994  34.341  55.524  1.00100.27           C  
ANISOU 2455  CA  PHE B1079    12260   9862  15976   -836  -1415  -1989       C  
ATOM   2456  C   PHE B1079     -13.237  33.825  56.256  1.00100.63           C  
ANISOU 2456  C   PHE B1079    12241   9890  16103   -880  -1407  -1999       C  
ATOM   2457  O   PHE B1079     -13.157  33.328  57.385  1.00 98.25           O  
ANISOU 2457  O   PHE B1079    11991   9449  15892   -876  -1345  -2023       O  
ATOM   2458  CB  PHE B1079     -12.252  35.722  54.904  1.00 99.62           C  
ANISOU 2458  CB  PHE B1079    12094   9903  15854   -761  -1462  -1838       C  
ATOM   2459  CG  PHE B1079     -12.121  36.885  55.866  1.00 97.83           C  
ANISOU 2459  CG  PHE B1079    11886   9551  15735   -646  -1407  -1729       C  
ATOM   2460  CD1 PHE B1079     -11.191  37.889  55.629  1.00 96.61           C  
ANISOU 2460  CD1 PHE B1079    11764   9364  15579   -569  -1399  -1652       C  
ATOM   2461  CD2 PHE B1079     -12.958  37.004  56.972  1.00 97.53           C  
ANISOU 2461  CD2 PHE B1079    11827   9430  15800   -623  -1353  -1712       C  
ATOM   2462  CE1 PHE B1079     -11.081  38.972  56.486  1.00 95.47           C  
ANISOU 2462  CE1 PHE B1079    11642   9091  15541   -487  -1337  -1582       C  
ATOM   2463  CE2 PHE B1079     -12.852  38.086  57.832  1.00 96.10           C  
ANISOU 2463  CE2 PHE B1079    11675   9132  15707   -535  -1279  -1650       C  
ATOM   2464  CZ  PHE B1079     -11.912  39.070  57.589  1.00 94.97           C  
ANISOU 2464  CZ  PHE B1079    11573   8942  15568   -474  -1271  -1596       C  
ATOM   2465  N   ASP B1080     -14.378  33.911  55.584  1.00103.13           N  
ANISOU 2465  N   ASP B1080    12432  10370  16382   -931  -1474  -1961       N  
ATOM   2466  CA  ASP B1080     -15.653  33.461  56.144  1.00107.68           C  
ANISOU 2466  CA  ASP B1080    12919  10954  17041   -978  -1475  -1946       C  
ATOM   2467  C   ASP B1080     -15.570  32.051  56.763  1.00109.83           C  
ANISOU 2467  C   ASP B1080    13252  11096  17383  -1064  -1426  -2083       C  
ATOM   2468  O   ASP B1080     -16.088  31.828  57.862  1.00109.70           O  
ANISOU 2468  O   ASP B1080    13219  10987  17474  -1043  -1373  -2046       O  
ATOM   2469  CB  ASP B1080     -16.759  33.529  55.077  1.00108.27           C  
ANISOU 2469  CB  ASP B1080    12835  11260  17042  -1063  -1579  -1890       C  
ATOM   2470  CG  ASP B1080     -16.868  34.907  54.413  1.00106.02           C  
ANISOU 2470  CG  ASP B1080    12454  11114  16713   -974  -1624  -1704       C  
ATOM   2471  OD1 ASP B1080     -16.182  35.857  54.847  1.00103.43           O  
ANISOU 2471  OD1 ASP B1080    12186  10674  16439   -842  -1561  -1631       O  
ATOM   2472  OD2 ASP B1080     -17.643  35.034  53.444  1.00106.00           O  
ANISOU 2472  OD2 ASP B1080    12305  11341  16629  -1048  -1724  -1619       O  
ATOM   2473  N   PHE B1081     -14.909  31.124  56.060  1.00110.57           N  
ANISOU 2473  N   PHE B1081    13408  11177  17427  -1155  -1428  -2231       N  
ATOM   2474  CA  PHE B1081     -14.654  29.760  56.551  1.00111.46           C  
ANISOU 2474  CA  PHE B1081    13573  11129  17647  -1229  -1357  -2353       C  
ATOM   2475  C   PHE B1081     -14.141  29.750  57.990  1.00111.28           C  
ANISOU 2475  C   PHE B1081    13608  10932  17743  -1136  -1273  -2271       C  
ATOM   2476  O   PHE B1081     -14.888  29.433  58.923  1.00110.88           O  
ANISOU 2476  O   PHE B1081    13507  10834  17787  -1143  -1246  -2221       O  
ATOM   2477  CB  PHE B1081     -13.655  29.048  55.627  1.00113.12           C  
ANISOU 2477  CB  PHE B1081    13867  11307  17808  -1294  -1323  -2511       C  
ATOM   2478  CG  PHE B1081     -13.305  27.640  56.050  1.00114.93           C  
ANISOU 2478  CG  PHE B1081    14139  11336  18194  -1360  -1220  -2626       C  
ATOM   2479  CD1 PHE B1081     -14.239  26.606  55.954  1.00115.58           C  
ANISOU 2479  CD1 PHE B1081    14161  11398  18356  -1499  -1216  -2735       C  
ATOM   2480  CD2 PHE B1081     -12.026  27.339  56.514  1.00115.75           C  
ANISOU 2480  CD2 PHE B1081    14327  11267  18388  -1287  -1122  -2609       C  
ATOM   2481  CE1 PHE B1081     -13.910  25.309  56.330  1.00116.02           C  
ANISOU 2481  CE1 PHE B1081    14243  11239  18599  -1555  -1101  -2828       C  
ATOM   2482  CE2 PHE B1081     -11.689  26.040  56.887  1.00116.60           C  
ANISOU 2482  CE2 PHE B1081    14448  11175  18681  -1335  -1009  -2678       C  
ATOM   2483  CZ  PHE B1081     -12.635  25.023  56.795  1.00116.61           C  
ANISOU 2483  CZ  PHE B1081    14393  11133  18781  -1466   -991  -2791       C  
ATOM   2484  N   PHE B1082     -12.872  30.119  58.160  1.00112.42           N  
ANISOU 2484  N   PHE B1082    13845  11003  17867  -1060  -1238  -2245       N  
ATOM   2485  CA  PHE B1082     -12.227  30.115  59.473  1.00112.35           C  
ANISOU 2485  CA  PHE B1082    13888  10866  17935   -999  -1175  -2159       C  
ATOM   2486  C   PHE B1082     -12.865  31.094  60.449  1.00111.61           C  
ANISOU 2486  C   PHE B1082    13772  10806  17827   -934  -1175  -2053       C  
ATOM   2487  O   PHE B1082     -12.986  30.781  61.636  1.00110.53           O  
ANISOU 2487  O   PHE B1082    13638  10609  17749   -933  -1124  -2000       O  
ATOM   2488  CB  PHE B1082     -10.722  30.378  59.358  1.00111.65           C  
ANISOU 2488  CB  PHE B1082    13885  10718  17819   -946  -1154  -2137       C  
ATOM   2489  CG  PHE B1082      -9.914  29.162  58.956  1.00114.14           C  
ANISOU 2489  CG  PHE B1082    14226  10923  18220   -993  -1089  -2213       C  
ATOM   2490  CD1 PHE B1082      -9.409  29.040  57.653  1.00112.86           C  
ANISOU 2490  CD1 PHE B1082    14092  10794  17994  -1014  -1085  -2320       C  
ATOM   2491  CD2 PHE B1082      -9.639  28.144  59.880  1.00111.02           C  
ANISOU 2491  CD2 PHE B1082    13818  10387  17976  -1012  -1014  -2166       C  
ATOM   2492  CE1 PHE B1082      -8.651  27.936  57.286  1.00109.83           C  
ANISOU 2492  CE1 PHE B1082    13735  10283  17712  -1050   -986  -2406       C  
ATOM   2493  CE2 PHE B1082      -8.881  27.040  59.514  1.00108.62           C  
ANISOU 2493  CE2 PHE B1082    13523   9948  17800  -1041   -924  -2219       C  
ATOM   2494  CZ  PHE B1082      -8.386  26.939  58.219  1.00109.69           C  
ANISOU 2494  CZ  PHE B1082    13698  10093  17885  -1057   -900  -2352       C  
ATOM   2495  N   VAL B1083     -13.281  32.261  59.943  1.00111.03           N  
ANISOU 2495  N   VAL B1083    13669  10832  17685   -882  -1217  -2016       N  
ATOM   2496  CA  VAL B1083     -13.893  33.323  60.779  1.00109.99           C  
ANISOU 2496  CA  VAL B1083    13518  10708  17565   -810  -1182  -1931       C  
ATOM   2497  C   VAL B1083     -15.295  32.932  61.308  1.00110.92           C  
ANISOU 2497  C   VAL B1083    13538  10852  17753   -836  -1154  -1904       C  
ATOM   2498  O   VAL B1083     -15.762  33.472  62.312  1.00108.59           O  
ANISOU 2498  O   VAL B1083    13240  10533  17488   -788  -1083  -1852       O  
ATOM   2499  CB  VAL B1083     -13.854  34.712  60.075  1.00105.48           C  
ANISOU 2499  CB  VAL B1083    12928  10199  16952   -733  -1209  -1873       C  
ATOM   2500  CG1 VAL B1083     -14.751  35.718  60.762  1.00103.86           C  
ANISOU 2500  CG1 VAL B1083    12673   9984  16807   -661  -1143  -1798       C  
ATOM   2501  CG2 VAL B1083     -12.425  35.241  60.025  1.00102.23           C  
ANISOU 2501  CG2 VAL B1083    12621   9729  16494   -696  -1209  -1875       C  
ATOM   2502  N   VAL B1084     -15.938  31.975  60.639  1.00112.76           N  
ANISOU 2502  N   VAL B1084    13694  11136  18014   -923  -1202  -1950       N  
ATOM   2503  CA  VAL B1084     -17.089  31.271  61.212  1.00115.96           C  
ANISOU 2503  CA  VAL B1084    14007  11543  18509   -973  -1177  -1927       C  
ATOM   2504  C   VAL B1084     -16.627  30.084  62.066  1.00116.61           C  
ANISOU 2504  C   VAL B1084    14137  11506  18665  -1023  -1121  -1957       C  
ATOM   2505  O   VAL B1084     -17.274  29.755  63.069  1.00116.87           O  
ANISOU 2505  O   VAL B1084    14124  11514  18766  -1026  -1063  -1895       O  
ATOM   2506  CB  VAL B1084     -18.095  30.796  60.134  1.00118.58           C  
ANISOU 2506  CB  VAL B1084    14215  11994  18848  -1071  -1263  -1955       C  
ATOM   2507  CG1 VAL B1084     -19.022  29.718  60.685  1.00119.01           C  
ANISOU 2507  CG1 VAL B1084    14186  12015  19017  -1154  -1240  -1956       C  
ATOM   2508  CG2 VAL B1084     -18.912  31.971  59.605  1.00118.74           C  
ANISOU 2508  CG2 VAL B1084    14126  12152  18837  -1012  -1305  -1841       C  
ATOM   2509  N   ALA B1085     -15.514  29.453  61.667  1.00115.09           N  
ANISOU 2509  N   ALA B1085    14018  11240  18469  -1057  -1126  -2028       N  
ATOM   2510  CA  ALA B1085     -14.948  28.297  62.394  1.00113.31           C  
ANISOU 2510  CA  ALA B1085    13815  10886  18351  -1095  -1063  -2019       C  
ATOM   2511  C   ALA B1085     -14.561  28.621  63.841  1.00111.17           C  
ANISOU 2511  C   ALA B1085    13581  10590  18067  -1039  -1005  -1898       C  
ATOM   2512  O   ALA B1085     -14.885  27.861  64.758  1.00109.79           O  
ANISOU 2512  O   ALA B1085    13359  10377  17980  -1069   -952  -1827       O  
ATOM   2513  CB  ALA B1085     -13.766  27.702  61.641  1.00113.12           C  
ANISOU 2513  CB  ALA B1085    13855  10779  18347  -1121  -1055  -2101       C  
ATOM   2514  N   ILE B1086     -13.888  29.759  64.031  1.00108.61           N  
ANISOU 2514  N   ILE B1086    13336  10301  17629   -971  -1014  -1875       N  
ATOM   2515  CA  ILE B1086     -13.541  30.282  65.361  1.00106.00           C  
ANISOU 2515  CA  ILE B1086    13055   9985  17237   -944   -967  -1790       C  
ATOM   2516  C   ILE B1086     -14.769  30.380  66.275  1.00105.56           C  
ANISOU 2516  C   ILE B1086    12940   9979  17191   -942   -906  -1746       C  
ATOM   2517  O   ILE B1086     -14.638  30.350  67.503  1.00105.12           O  
ANISOU 2517  O   ILE B1086    12903   9947  17091   -955   -850  -1676       O  
ATOM   2518  CB  ILE B1086     -12.845  31.664  65.260  1.00104.91           C  
ANISOU 2518  CB  ILE B1086    13007   9874  16982   -888   -985  -1808       C  
ATOM   2519  CG1 ILE B1086     -11.611  31.579  64.353  1.00104.44           C  
ANISOU 2519  CG1 ILE B1086    12994   9774  16914   -884  -1038  -1832       C  
ATOM   2520  CG2 ILE B1086     -12.448  32.191  66.639  1.00103.58           C  
ANISOU 2520  CG2 ILE B1086    12901   9732  16723   -897   -936  -1756       C  
ATOM   2521  CD1 ILE B1086     -11.354  32.835  63.534  1.00104.94           C  
ANISOU 2521  CD1 ILE B1086    13097   9868  16908   -826  -1077  -1867       C  
ATOM   2522  N   SER B1087     -15.954  30.487  65.670  1.00105.11           N  
ANISOU 2522  N   SER B1087    12799   9955  17183   -933   -917  -1775       N  
ATOM   2523  CA  SER B1087     -17.213  30.543  66.419  1.00105.33           C  
ANISOU 2523  CA  SER B1087    12747  10026  17249   -923   -848  -1720       C  
ATOM   2524  C   SER B1087     -17.709  29.184  66.903  1.00105.92           C  
ANISOU 2524  C   SER B1087    12735  10073  17436   -993   -825  -1664       C  
ATOM   2525  O   SER B1087     -18.472  29.114  67.870  1.00105.57           O  
ANISOU 2525  O   SER B1087    12639  10066  17408   -987   -748  -1589       O  
ATOM   2526  CB  SER B1087     -18.316  31.207  65.595  1.00104.43           C  
ANISOU 2526  CB  SER B1087    12544   9967  17168   -886   -870  -1728       C  
ATOM   2527  OG  SER B1087     -19.564  31.087  66.259  1.00103.59           O  
ANISOU 2527  OG  SER B1087    12335   9894  17130   -878   -798  -1657       O  
ATOM   2528  N   LEU B1088     -17.277  28.118  66.229  1.00106.16           N  
ANISOU 2528  N   LEU B1088    12748  10032  17556  -1059   -874  -1702       N  
ATOM   2529  CA  LEU B1088     -17.863  26.788  66.415  1.00106.87           C  
ANISOU 2529  CA  LEU B1088    12736  10064  17806  -1136   -852  -1665       C  
ATOM   2530  C   LEU B1088     -17.447  26.110  67.719  1.00107.50           C  
ANISOU 2530  C   LEU B1088    12805  10110  17931  -1146   -777  -1529       C  
ATOM   2531  O   LEU B1088     -18.153  25.226  68.200  1.00110.68           O  
ANISOU 2531  O   LEU B1088    13103  10485  18464  -1190   -734  -1450       O  
ATOM   2532  CB  LEU B1088     -17.559  25.882  65.217  1.00108.29           C  
ANISOU 2532  CB  LEU B1088    12904  10154  18085  -1215   -902  -1781       C  
ATOM   2533  CG  LEU B1088     -17.722  26.427  63.792  1.00108.38           C  
ANISOU 2533  CG  LEU B1088    12932  10232  18017  -1233   -990  -1914       C  
ATOM   2534  CD1 LEU B1088     -17.158  25.441  62.783  1.00110.65           C  
ANISOU 2534  CD1 LEU B1088    13241  10425  18377  -1325  -1003  -2051       C  
ATOM   2535  CD2 LEU B1088     -19.161  26.767  63.454  1.00108.74           C  
ANISOU 2535  CD2 LEU B1088    12863  10391  18063  -1259  -1035  -1900       C  
ATOM   2536  N   VAL B1089     -16.306  26.514  68.278  1.00107.31           N  
ANISOU 2536  N   VAL B1089    12873  10101  17800  -1114   -768  -1483       N  
ATOM   2537  CA  VAL B1089     -15.870  26.050  69.612  1.00108.41           C  
ANISOU 2537  CA  VAL B1089    12992  10269  17929  -1132   -710  -1317       C  
ATOM   2538  C   VAL B1089     -16.829  26.602  70.682  1.00109.08           C  
ANISOU 2538  C   VAL B1089    13053  10481  17911  -1116   -643  -1258       C  
ATOM   2539  O   VAL B1089     -17.048  27.816  70.743  1.00107.41           O  
ANISOU 2539  O   VAL B1089    12915  10341  17554  -1070   -630  -1337       O  
ATOM   2540  CB  VAL B1089     -14.406  26.462  69.933  1.00106.25           C  
ANISOU 2540  CB  VAL B1089    12813  10019  17537  -1124   -736  -1273       C  
ATOM   2541  CG1 VAL B1089     -14.050  26.157  71.381  1.00104.57           C  
ANISOU 2541  CG1 VAL B1089    12568   9906  17260  -1161   -693  -1080       C  
ATOM   2542  CG2 VAL B1089     -13.427  25.775  68.988  1.00105.16           C  
ANISOU 2542  CG2 VAL B1089    12679   9744  17531  -1131   -767  -1300       C  
ATOM   2543  N   PRO B1090     -17.414  25.708  71.509  1.00110.67           N  
ANISOU 2543  N   PRO B1090    13144  10699  18205  -1153   -583  -1117       N  
ATOM   2544  CA  PRO B1090     -18.454  26.024  72.494  1.00112.50           C  
ANISOU 2544  CA  PRO B1090    13330  11049  18367  -1141   -496  -1051       C  
ATOM   2545  C   PRO B1090     -18.089  27.146  73.456  1.00113.13           C  
ANISOU 2545  C   PRO B1090    13521  11273  18192  -1124   -443  -1062       C  
ATOM   2546  O   PRO B1090     -16.972  27.653  73.418  1.00113.67           O  
ANISOU 2546  O   PRO B1090    13696  11354  18138  -1133   -491  -1104       O  
ATOM   2547  CB  PRO B1090     -18.616  24.705  73.257  1.00114.73           C  
ANISOU 2547  CB  PRO B1090    13480  11321  18790  -1195   -451   -853       C  
ATOM   2548  CG  PRO B1090     -18.320  23.670  72.229  1.00115.60           C  
ANISOU 2548  CG  PRO B1090    13536  11247  19139  -1229   -506   -884       C  
ATOM   2549  CD  PRO B1090     -17.185  24.252  71.426  1.00113.62           C  
ANISOU 2549  CD  PRO B1090    13415  10954  18803  -1206   -578  -1012       C  
ATOM   2550  N   THR B1091     -19.041  27.517  74.312  1.00115.52           N  
ANISOU 2550  N   THR B1091    13795  11678  18418  -1109   -335  -1033       N  
ATOM   2551  CA  THR B1091     -18.876  28.631  75.247  1.00116.57           C  
ANISOU 2551  CA  THR B1091    14043  11944  18306  -1108   -248  -1090       C  
ATOM   2552  C   THR B1091     -17.572  28.560  76.067  1.00119.46           C  
ANISOU 2552  C   THR B1091    14483  12421  18486  -1192   -285  -1016       C  
ATOM   2553  O   THR B1091     -16.674  29.404  75.894  1.00120.46           O  
ANISOU 2553  O   THR B1091    14738  12552  18481  -1204   -330  -1125       O  
ATOM   2554  CB  THR B1091     -20.129  28.836  76.149  1.00116.23           C  
ANISOU 2554  CB  THR B1091    13942  11999  18222  -1087    -91  -1053       C  
ATOM   2555  OG1 THR B1091     -19.842  29.801  77.172  1.00117.58           O  
ANISOU 2555  OG1 THR B1091    14239  12305  18132  -1115     13  -1127       O  
ATOM   2556  CG2 THR B1091     -20.579  27.539  76.796  1.00115.24           C  
ANISOU 2556  CG2 THR B1091    13665  11926  18195  -1132    -67   -842       C  
ATOM   2557  N   SER B1092     -17.462  27.546  76.924  1.00120.71           N  
ANISOU 2557  N   SER B1092    14544  12673  18648  -1256   -273   -810       N  
ATOM   2558  CA  SER B1092     -16.316  27.412  77.828  1.00122.07           C  
ANISOU 2558  CA  SER B1092    14746  13002  18635  -1351   -311   -680       C  
ATOM   2559  C   SER B1092     -15.530  26.125  77.590  1.00121.37           C  
ANISOU 2559  C   SER B1092    14538  12839  18739  -1377   -398   -467       C  
ATOM   2560  O   SER B1092     -15.892  25.049  78.093  1.00121.37           O  
ANISOU 2560  O   SER B1092    14387  12861  18865  -1398   -362   -254       O  
ATOM   2561  CB  SER B1092     -16.761  27.514  79.297  1.00125.12           C  
ANISOU 2561  CB  SER B1092    15118  13630  18794  -1422   -200   -585       C  
ATOM   2562  OG  SER B1092     -17.780  26.565  79.594  1.00126.59           O  
ANISOU 2562  OG  SER B1092    15144  13815  19139  -1398   -129   -426       O  
ATOM   2563  N   SER B1093     -14.464  26.251  76.803  1.00119.69           N  
ANISOU 2563  N   SER B1093    14383  12523  18572  -1368   -496   -518       N  
ATOM   2564  CA  SER B1093     -13.462  25.193  76.635  1.00120.37           C  
ANISOU 2564  CA  SER B1093    14370  12537  18828  -1390   -558   -316       C  
ATOM   2565  C   SER B1093     -12.112  25.806  76.229  1.00119.13           C  
ANISOU 2565  C   SER B1093    14314  12374  18576  -1405   -651   -368       C  
ATOM   2566  O   SER B1093     -12.022  26.570  75.254  1.00116.55           O  
ANISOU 2566  O   SER B1093    14099  11938  18248  -1351   -684   -588       O  
ATOM   2567  CB  SER B1093     -13.911  24.127  75.617  1.00118.32           C  
ANISOU 2567  CB  SER B1093    14008  12029  18918  -1334   -545   -320       C  
ATOM   2568  OG  SER B1093     -14.924  23.279  76.144  1.00116.31           O  
ANISOU 2568  OG  SER B1093    13616  11781  18796  -1344   -469   -187       O  
ATOM   2569  N   GLY B1094     -11.074  25.466  76.990  1.00118.03           N  
ANISOU 2569  N   GLY B1094    14117  12369  18362  -1481   -695   -136       N  
ATOM   2570  CA  GLY B1094      -9.728  25.969  76.746  1.00114.71           C  
ANISOU 2570  CA  GLY B1094    13762  11969  17855  -1511   -789   -130       C  
ATOM   2571  C   GLY B1094      -9.574  27.392  77.241  1.00113.34           C  
ANISOU 2571  C   GLY B1094    13750  11970  17342  -1582   -815   -304       C  
ATOM   2572  O   GLY B1094      -9.057  27.624  78.349  1.00110.58           O  
ANISOU 2572  O   GLY B1094    13400  11868  16750  -1708   -847   -177       O  
ATOM   2573  N   PHE B1095     -10.029  28.342  76.418  1.00110.10           N  
ANISOU 2573  N   PHE B1095    13473  11437  16922  -1512   -798   -590       N  
ATOM   2574  CA  PHE B1095      -9.890  29.771  76.725  1.00109.21           C  
ANISOU 2574  CA  PHE B1095    13522  11423  16548  -1565   -798   -790       C  
ATOM   2575  C   PHE B1095     -10.947  30.690  76.101  1.00106.00           C  
ANISOU 2575  C   PHE B1095    13213  10895  16167  -1472   -717  -1061       C  
ATOM   2576  O   PHE B1095     -11.342  30.501  74.952  1.00104.83           O  
ANISOU 2576  O   PHE B1095    13040  10562  16228  -1363   -723  -1130       O  
ATOM   2577  CB  PHE B1095      -8.472  30.276  76.390  1.00108.68           C  
ANISOU 2577  CB  PHE B1095    13512  11357  16424  -1611   -910   -782       C  
ATOM   2578  CG  PHE B1095      -7.823  29.597  75.206  1.00107.25           C  
ANISOU 2578  CG  PHE B1095    13263  10978  16508  -1518   -967   -708       C  
ATOM   2579  CD1 PHE B1095      -8.392  29.663  73.931  1.00106.92           C  
ANISOU 2579  CD1 PHE B1095    13249  10727  16650  -1392   -939   -878       C  
ATOM   2580  CD2 PHE B1095      -6.608  28.929  75.358  1.00108.74           C  
ANISOU 2580  CD2 PHE B1095    13356  11206  16754  -1564  -1041   -464       C  
ATOM   2581  CE1 PHE B1095      -7.771  29.053  72.840  1.00106.31           C  
ANISOU 2581  CE1 PHE B1095    13124  10484  16786  -1323   -974   -839       C  
ATOM   2582  CE2 PHE B1095      -5.984  28.314  74.273  1.00107.58           C  
ANISOU 2582  CE2 PHE B1095    13152  10863  16861  -1474  -1059   -411       C  
ATOM   2583  CZ  PHE B1095      -6.567  28.375  73.014  1.00106.51           C  
ANISOU 2583  CZ  PHE B1095    13065  10521  16883  -1358  -1020   -617       C  
ATOM   2584  N   GLU B1096     -11.374  31.699  76.864  1.00105.81           N  
ANISOU 2584  N   GLU B1096    13295  10982  15927  -1526   -634  -1207       N  
ATOM   2585  CA  GLU B1096     -12.314  32.725  76.376  1.00105.71           C  
ANISOU 2585  CA  GLU B1096    13365  10850  15949  -1436   -532  -1442       C  
ATOM   2586  C   GLU B1096     -11.849  33.471  75.126  1.00103.82           C  
ANISOU 2586  C   GLU B1096    13189  10437  15822  -1358   -594  -1569       C  
ATOM   2587  O   GLU B1096     -12.668  34.119  74.472  1.00102.96           O  
ANISOU 2587  O   GLU B1096    13099  10208  15814  -1257   -526  -1702       O  
ATOM   2588  CB  GLU B1096     -12.669  33.743  77.472  1.00107.97           C  
ANISOU 2588  CB  GLU B1096    13766  11267  15991  -1519   -403  -1592       C  
ATOM   2589  CG  GLU B1096     -13.653  33.217  78.518  1.00110.78           C  
ANISOU 2589  CG  GLU B1096    14060  11769  16263  -1547   -281  -1519       C  
ATOM   2590  CD  GLU B1096     -14.222  34.301  79.422  1.00111.12           C  
ANISOU 2590  CD  GLU B1096    14226  11898  16098  -1602   -101  -1722       C  
ATOM   2591  OE1 GLU B1096     -13.859  35.487  79.256  1.00111.16           O  
ANISOU 2591  OE1 GLU B1096    14368  11829  16039  -1623    -65  -1931       O  
ATOM   2592  OE2 GLU B1096     -15.043  33.962  80.302  1.00111.30           O  
ANISOU 2592  OE2 GLU B1096    14205  12052  16032  -1625     22  -1674       O  
ATOM   2593  N   ILE B1097     -10.549  33.382  74.810  1.00102.78           N  
ANISOU 2593  N   ILE B1097    13072  10302  15676  -1402   -718  -1502       N  
ATOM   2594  CA  ILE B1097      -9.972  33.947  73.572  1.00100.56           C  
ANISOU 2594  CA  ILE B1097    12832   9869  15506  -1330   -786  -1583       C  
ATOM   2595  C   ILE B1097     -10.801  33.536  72.347  1.00100.33           C  
ANISOU 2595  C   ILE B1097    12730   9691  15699  -1194   -778  -1608       C  
ATOM   2596  O   ILE B1097     -11.129  34.379  71.500  1.00101.04           O  
ANISOU 2596  O   ILE B1097    12855   9683  15851  -1115   -761  -1728       O  
ATOM   2597  CB  ILE B1097      -8.503  33.492  73.309  1.00 98.55           C  
ANISOU 2597  CB  ILE B1097    12554   9627  15264  -1378   -916  -1443       C  
ATOM   2598  CG1 ILE B1097      -7.670  33.425  74.597  1.00100.45           C  
ANISOU 2598  CG1 ILE B1097    12804  10069  15294  -1539   -958  -1324       C  
ATOM   2599  CG2 ILE B1097      -7.831  34.401  72.278  1.00 96.19           C  
ANISOU 2599  CG2 ILE B1097    12324   9211  15012  -1328   -968  -1545       C  
ATOM   2600  CD1 ILE B1097      -6.341  32.703  74.422  1.00 98.95           C  
ANISOU 2600  CD1 ILE B1097    12532   9902  15162  -1576  -1076  -1108       C  
ATOM   2601  N   LEU B1098     -11.130  32.246  72.255  1.00 98.62           N  
ANISOU 2601  N   LEU B1098    12401   9464  15605  -1181   -790  -1484       N  
ATOM   2602  CA  LEU B1098     -11.930  31.739  71.143  1.00 97.31           C  
ANISOU 2602  CA  LEU B1098    12162   9182  15631  -1093   -790  -1517       C  
ATOM   2603  C   LEU B1098     -13.326  32.372  71.145  1.00 97.64           C  
ANISOU 2603  C   LEU B1098    12194   9221  15685  -1037   -700  -1614       C  
ATOM   2604  O   LEU B1098     -13.785  32.853  70.107  1.00 97.63           O  
ANISOU 2604  O   LEU B1098    12181   9146  15767   -963   -712  -1694       O  
ATOM   2605  CB  LEU B1098     -12.007  30.202  71.166  1.00 96.05           C  
ANISOU 2605  CB  LEU B1098    11883   8994  15616  -1113   -801  -1377       C  
ATOM   2606  CG  LEU B1098     -10.792  29.417  70.662  1.00 94.05           C  
ANISOU 2606  CG  LEU B1098    11602   8669  15463  -1126   -867  -1284       C  
ATOM   2607  CD1 LEU B1098     -10.698  28.072  71.354  1.00 95.64           C  
ANISOU 2607  CD1 LEU B1098    11687   8876  15774  -1172   -840  -1090       C  
ATOM   2608  CD2 LEU B1098     -10.824  29.233  69.150  1.00 92.93           C  
ANISOU 2608  CD2 LEU B1098    11456   8394  15461  -1066   -897  -1393       C  
ATOM   2609  N   ARG B1099     -13.973  32.391  72.315  1.00 97.41           N  
ANISOU 2609  N   ARG B1099    12159   9286  15569  -1072   -604  -1590       N  
ATOM   2610  CA  ARG B1099     -15.306  32.985  72.490  1.00 97.85           C  
ANISOU 2610  CA  ARG B1099    12193   9339  15646  -1014   -485  -1661       C  
ATOM   2611  C   ARG B1099     -15.325  34.455  72.096  1.00 98.37           C  
ANISOU 2611  C   ARG B1099    12347   9342  15688   -957   -436  -1804       C  
ATOM   2612  O   ARG B1099     -16.316  34.963  71.551  1.00 98.14           O  
ANISOU 2612  O   ARG B1099    12265   9252  15772   -868   -374  -1840       O  
ATOM   2613  CB  ARG B1099     -15.749  32.862  73.948  1.00 98.89           C  
ANISOU 2613  CB  ARG B1099    12328   9601  15644  -1075   -370  -1620       C  
ATOM   2614  CG  ARG B1099     -17.178  33.307  74.203  1.00 98.88           C  
ANISOU 2614  CG  ARG B1099    12283   9595  15692  -1008   -219  -1667       C  
ATOM   2615  CD  ARG B1099     -17.473  33.402  75.685  1.00100.37           C  
ANISOU 2615  CD  ARG B1099    12508   9929  15700  -1076    -80  -1661       C  
ATOM   2616  NE  ARG B1099     -17.323  32.122  76.371  1.00101.22           N  
ANISOU 2616  NE  ARG B1099    12530  10154  15774  -1152   -124  -1479       N  
ATOM   2617  CZ  ARG B1099     -17.449  31.963  77.687  1.00105.65           C  
ANISOU 2617  CZ  ARG B1099    13099  10892  16152  -1234    -31  -1421       C  
ATOM   2618  NH1 ARG B1099     -17.731  33.009  78.470  1.00107.72           N  
ANISOU 2618  NH1 ARG B1099    13471  11227  16231  -1260    123  -1571       N  
ATOM   2619  NH2 ARG B1099     -17.293  30.759  78.227  1.00105.95           N  
ANISOU 2619  NH2 ARG B1099    13031  11033  16192  -1296    -79  -1212       N  
ATOM   2620  N   VAL B1100     -14.219  35.131  72.389  1.00 98.61           N  
ANISOU 2620  N   VAL B1100    12494   9386  15586  -1014   -463  -1863       N  
ATOM   2621  CA  VAL B1100     -14.084  36.550  72.105  1.00 98.67           C  
ANISOU 2621  CA  VAL B1100    12591   9312  15587   -975   -407  -1998       C  
ATOM   2622  C   VAL B1100     -14.077  36.817  70.598  1.00 98.93           C  
ANISOU 2622  C   VAL B1100    12572   9235  15781   -875   -487  -1990       C  
ATOM   2623  O   VAL B1100     -14.903  37.588  70.105  1.00100.40           O  
ANISOU 2623  O   VAL B1100    12720   9350  16078   -783   -410  -2025       O  
ATOM   2624  CB  VAL B1100     -12.860  37.149  72.822  1.00 96.42           C  
ANISOU 2624  CB  VAL B1100    12439   9078  15120  -1091   -427  -2064       C  
ATOM   2625  CG1 VAL B1100     -12.425  38.444  72.169  1.00 96.45           C  
ANISOU 2625  CG1 VAL B1100    12517   8957  15175  -1051   -416  -2176       C  
ATOM   2626  CG2 VAL B1100     -13.207  37.403  74.272  1.00 98.82           C  
ANISOU 2626  CG2 VAL B1100    12809   9494  15242  -1186   -291  -2135       C  
ATOM   2627  N   LEU B1101     -13.180  36.150  69.871  1.00 96.91           N  
ANISOU 2627  N   LEU B1101    12301   8976  15543   -893   -630  -1926       N  
ATOM   2628  CA  LEU B1101     -13.017  36.404  68.442  1.00 94.88           C  
ANISOU 2628  CA  LEU B1101    12007   8650  15393   -819   -709  -1924       C  
ATOM   2629  C   LEU B1101     -14.215  35.865  67.652  1.00 95.96           C  
ANISOU 2629  C   LEU B1101    12015   8789  15656   -758   -716  -1884       C  
ATOM   2630  O   LEU B1101     -14.135  35.681  66.427  1.00 95.79           O  
ANISOU 2630  O   LEU B1101    11942   8757  15697   -728   -803  -1867       O  
ATOM   2631  CB  LEU B1101     -11.700  35.803  67.921  1.00 93.27           C  
ANISOU 2631  CB  LEU B1101    11826   8446  15167   -858   -834  -1877       C  
ATOM   2632  CG  LEU B1101     -10.355  35.971  68.652  1.00 92.17           C  
ANISOU 2632  CG  LEU B1101    11777   8336  14909   -944   -871  -1860       C  
ATOM   2633  CD1 LEU B1101      -9.234  35.402  67.786  1.00 92.98           C  
ANISOU 2633  CD1 LEU B1101    11862   8411  15053   -942   -977  -1792       C  
ATOM   2634  CD2 LEU B1101     -10.040  37.407  69.023  1.00 92.54           C  
ANISOU 2634  CD2 LEU B1101    11922   8354  14884   -961   -821  -1955       C  
ATOM   2635  N   ARG B1102     -15.323  35.617  68.356  1.00 96.25           N  
ANISOU 2635  N   ARG B1102    11996   8856  15719   -754   -623  -1867       N  
ATOM   2636  CA  ARG B1102     -16.528  35.075  67.726  1.00 96.90           C  
ANISOU 2636  CA  ARG B1102    11939   8956  15923   -719   -634  -1815       C  
ATOM   2637  C   ARG B1102     -17.194  36.113  66.850  1.00 96.99           C  
ANISOU 2637  C   ARG B1102    11886   8943  16024   -627   -613  -1806       C  
ATOM   2638  O   ARG B1102     -17.346  35.906  65.641  1.00 97.61           O  
ANISOU 2638  O   ARG B1102    11884   9049  16155   -617   -715  -1770       O  
ATOM   2639  CB  ARG B1102     -17.534  34.555  68.760  1.00 97.57           C  
ANISOU 2639  CB  ARG B1102    11966   9082  16024   -736   -532  -1774       C  
ATOM   2640  CG  ARG B1102     -17.372  33.086  69.122  1.00 96.96           C  
ANISOU 2640  CG  ARG B1102    11851   9038  15953   -817   -584  -1712       C  
ATOM   2641  CD  ARG B1102     -18.697  32.505  69.570  1.00 97.00           C  
ANISOU 2641  CD  ARG B1102    11734   9079  16044   -815   -514  -1643       C  
ATOM   2642  NE  ARG B1102     -18.529  31.355  70.452  1.00 96.51           N  
ANISOU 2642  NE  ARG B1102    11650   9050  15968   -889   -504  -1565       N  
ATOM   2643  CZ  ARG B1102     -19.504  30.510  70.781  1.00 97.17           C  
ANISOU 2643  CZ  ARG B1102    11614   9156  16151   -909   -466  -1480       C  
ATOM   2644  NH1 ARG B1102     -20.736  30.659  70.294  1.00 96.23           N  
ANISOU 2644  NH1 ARG B1102    11382   9037  16145   -868   -444  -1465       N  
ATOM   2645  NH2 ARG B1102     -19.241  29.502  71.600  1.00 98.58           N  
ANISOU 2645  NH2 ARG B1102    11766   9362  16329   -973   -453  -1383       N  
ATOM   2646  N   VAL B1103     -17.568  37.232  67.466  1.00 96.60           N  
ANISOU 2646  N   VAL B1103    11866   8846  15992   -569   -470  -1834       N  
ATOM   2647  CA  VAL B1103     -18.315  38.292  66.794  1.00 98.96           C  
ANISOU 2647  CA  VAL B1103    12075   9102  16425   -465   -409  -1785       C  
ATOM   2648  C   VAL B1103     -17.527  38.927  65.619  1.00100.47           C  
ANISOU 2648  C   VAL B1103    12275   9270  16629   -434   -512  -1769       C  
ATOM   2649  O   VAL B1103     -18.050  39.796  64.898  1.00100.46           O  
ANISOU 2649  O   VAL B1103    12174   9246  16749   -346   -483  -1687       O  
ATOM   2650  CB  VAL B1103     -18.875  39.320  67.821  1.00100.39           C  
ANISOU 2650  CB  VAL B1103    12289   9200  16653   -407   -187  -1834       C  
ATOM   2651  CG1 VAL B1103     -17.761  40.116  68.484  1.00 99.02           C  
ANISOU 2651  CG1 VAL B1103    12296   8951  16376   -448   -126  -1971       C  
ATOM   2652  CG2 VAL B1103     -19.916  40.239  67.191  1.00102.01           C  
ANISOU 2652  CG2 VAL B1103    12346   9351  17060   -282    -93  -1731       C  
ATOM   2653  N   LEU B1104     -16.283  38.467  65.426  1.00 99.79           N  
ANISOU 2653  N   LEU B1104    12289   9196  16432   -502   -626  -1819       N  
ATOM   2654  CA  LEU B1104     -15.517  38.712  64.192  1.00 99.59           C  
ANISOU 2654  CA  LEU B1104    12258   9184  16400   -487   -745  -1790       C  
ATOM   2655  C   LEU B1104     -16.252  38.193  62.941  1.00101.37           C  
ANISOU 2655  C   LEU B1104    12333   9514  16667   -481   -848  -1704       C  
ATOM   2656  O   LEU B1104     -15.978  38.627  61.812  1.00101.45           O  
ANISOU 2656  O   LEU B1104    12297   9568  16680   -453   -923  -1649       O  
ATOM   2657  CB  LEU B1104     -14.131  38.058  64.275  1.00 97.39           C  
ANISOU 2657  CB  LEU B1104    12093   8905  16005   -565   -834  -1844       C  
ATOM   2658  CG  LEU B1104     -12.922  38.896  64.709  1.00 96.34           C  
ANISOU 2658  CG  LEU B1104    12086   8700  15817   -577   -815  -1892       C  
ATOM   2659  CD1 LEU B1104     -11.712  38.019  65.006  1.00 93.16           C  
ANISOU 2659  CD1 LEU B1104    11762   8319  15314   -663   -895  -1906       C  
ATOM   2660  CD2 LEU B1104     -12.578  39.894  63.619  1.00 97.02           C  
ANISOU 2660  CD2 LEU B1104    12144   8756  15963   -508   -847  -1846       C  
ATOM   2661  N   ARG B1105     -17.192  37.276  63.153  1.00101.39           N  
ANISOU 2661  N   ARG B1105    12255   9573  16694   -521   -851  -1688       N  
ATOM   2662  CA  ARG B1105     -17.946  36.681  62.065  1.00103.73           C  
ANISOU 2662  CA  ARG B1105    12411   9989  17014   -556   -956  -1627       C  
ATOM   2663  C   ARG B1105     -18.817  37.694  61.316  1.00105.62           C  
ANISOU 2663  C   ARG B1105    12496  10290  17345   -476   -949  -1486       C  
ATOM   2664  O   ARG B1105     -19.405  37.373  60.273  1.00108.61           O  
ANISOU 2664  O   ARG B1105    12740  10810  17717   -519  -1058  -1410       O  
ATOM   2665  CB  ARG B1105     -18.764  35.491  62.572  1.00106.74           C  
ANISOU 2665  CB  ARG B1105    12734  10398  17423   -629   -953  -1639       C  
ATOM   2666  CG  ARG B1105     -19.729  35.798  63.705  1.00109.15           C  
ANISOU 2666  CG  ARG B1105    12994  10664  17813   -576   -811  -1590       C  
ATOM   2667  CD  ARG B1105     -20.376  34.515  64.213  1.00110.01           C  
ANISOU 2667  CD  ARG B1105    13050  10800  17950   -657   -816  -1591       C  
ATOM   2668  NE  ARG B1105     -21.426  34.802  65.189  1.00112.34           N  
ANISOU 2668  NE  ARG B1105    13276  11082  18327   -603   -674  -1525       N  
ATOM   2669  CZ  ARG B1105     -22.066  33.878  65.896  1.00112.92           C  
ANISOU 2669  CZ  ARG B1105    13298  11170  18438   -653   -638  -1500       C  
ATOM   2670  NH1 ARG B1105     -21.775  32.591  65.736  1.00109.65           N  
ANISOU 2670  NH1 ARG B1105    12887  10764  18011   -760   -733  -1536       N  
ATOM   2671  NH2 ARG B1105     -23.005  34.245  66.763  1.00115.67           N  
ANISOU 2671  NH2 ARG B1105    13582  11512  18855   -592   -489  -1434       N  
ATOM   2672  N   LEU B1106     -18.876  38.914  61.843  1.00104.28           N  
ANISOU 2672  N   LEU B1106    12340  10015  17265   -371   -816  -1446       N  
ATOM   2673  CA  LEU B1106     -19.598  40.010  61.208  1.00106.17           C  
ANISOU 2673  CA  LEU B1106    12422  10276  17642   -272   -776  -1278       C  
ATOM   2674  C   LEU B1106     -18.763  40.725  60.142  1.00104.64           C  
ANISOU 2674  C   LEU B1106    12228  10111  17420   -243   -857  -1220       C  
ATOM   2675  O   LEU B1106     -19.281  41.572  59.390  1.00104.52           O  
ANISOU 2675  O   LEU B1106    12053  10145  17515   -167   -853  -1037       O  
ATOM   2676  CB  LEU B1106     -20.060  41.024  62.260  1.00109.38           C  
ANISOU 2676  CB  LEU B1106    12840  10520  18200   -166   -556  -1270       C  
ATOM   2677  CG  LEU B1106     -21.097  40.571  63.282  1.00110.72           C  
ANISOU 2677  CG  LEU B1106    12970  10672  18426   -165   -436  -1282       C  
ATOM   2678  CD1 LEU B1106     -21.216  41.624  64.365  1.00111.23           C  
ANISOU 2678  CD1 LEU B1106    13106  10558  18599    -76   -191  -1340       C  
ATOM   2679  CD2 LEU B1106     -22.437  40.326  62.608  1.00111.56           C  
ANISOU 2679  CD2 LEU B1106    12834  10909  18645   -147   -483  -1088       C  
ATOM   2680  N   PHE B1107     -17.473  40.397  60.076  1.00101.15           N  
ANISOU 2680  N   PHE B1107    11946   9643  16845   -298   -923  -1346       N  
ATOM   2681  CA  PHE B1107     -16.609  40.965  59.035  1.00100.92           C  
ANISOU 2681  CA  PHE B1107    11916   9655  16773   -278  -1003  -1289       C  
ATOM   2682  C   PHE B1107     -16.945  40.439  57.630  1.00100.00           C  
ANISOU 2682  C   PHE B1107    11666   9765  16566   -337  -1161  -1196       C  
ATOM   2683  O   PHE B1107     -16.096  40.439  56.742  1.00 96.69           O  
ANISOU 2683  O   PHE B1107    11276   9423  16040   -362  -1249  -1197       O  
ATOM   2684  CB  PHE B1107     -15.121  40.772  59.365  1.00 98.51           C  
ANISOU 2684  CB  PHE B1107    11804   9262  16362   -319  -1021  -1430       C  
ATOM   2685  CG  PHE B1107     -14.458  41.982  59.999  1.00 96.71           C  
ANISOU 2685  CG  PHE B1107    11664   8861  16218   -254   -910  -1447       C  
ATOM   2686  CD1 PHE B1107     -13.966  41.920  61.304  1.00 95.05           C  
ANISOU 2686  CD1 PHE B1107    11609   8528  15979   -293   -826  -1589       C  
ATOM   2687  CD2 PHE B1107     -14.292  43.171  59.282  1.00 96.34           C  
ANISOU 2687  CD2 PHE B1107    11542   8785  16276   -170   -890  -1317       C  
ATOM   2688  CE1 PHE B1107     -13.330  43.013  61.882  1.00 94.86           C  
ANISOU 2688  CE1 PHE B1107    11675   8352  16014   -269   -729  -1636       C  
ATOM   2689  CE2 PHE B1107     -13.664  44.270  59.859  1.00 96.67           C  
ANISOU 2689  CE2 PHE B1107    11669   8643  16417   -128   -779  -1352       C  
ATOM   2690  CZ  PHE B1107     -13.182  44.192  61.160  1.00 95.61           C  
ANISOU 2690  CZ  PHE B1107    11703   8386  16239   -187   -699  -1529       C  
ATOM   2691  N   ARG B1108     -18.196  40.005  57.460  1.00103.04           N  
ANISOU 2691  N   ARG B1108    11899  10266  16983   -369  -1190  -1118       N  
ATOM   2692  CA  ARG B1108     -18.759  39.539  56.186  1.00105.40           C  
ANISOU 2692  CA  ARG B1108    12044  10816  17187   -456  -1342  -1024       C  
ATOM   2693  C   ARG B1108     -19.694  40.589  55.572  1.00108.48           C  
ANISOU 2693  C   ARG B1108    12199  11317  17703   -373  -1340   -745       C  
ATOM   2694  O   ARG B1108     -20.303  40.364  54.519  1.00109.21           O  
ANISOU 2694  O   ARG B1108    12122  11658  17715   -451  -1473   -615       O  
ATOM   2695  CB  ARG B1108     -19.534  38.240  56.406  1.00106.34           C  
ANISOU 2695  CB  ARG B1108    12136  11006  17263   -579  -1393  -1117       C  
ATOM   2696  CG  ARG B1108     -18.669  37.012  56.601  1.00105.80           C  
ANISOU 2696  CG  ARG B1108    12246  10881  17072   -686  -1425  -1351       C  
ATOM   2697  CD  ARG B1108     -19.490  35.903  57.226  1.00107.00           C  
ANISOU 2697  CD  ARG B1108    12373  11018  17266   -773  -1418  -1424       C  
ATOM   2698  NE  ARG B1108     -19.536  34.692  56.401  1.00107.49           N  
ANISOU 2698  NE  ARG B1108    12425  11204  17213   -941  -1532  -1543       N  
ATOM   2699  CZ  ARG B1108     -20.130  34.618  55.210  1.00109.22           C  
ANISOU 2699  CZ  ARG B1108    12505  11655  17339  -1042  -1658  -1482       C  
ATOM   2700  NH1 ARG B1108     -20.693  35.700  54.682  1.00108.04           N  
ANISOU 2700  NH1 ARG B1108    12195  11646  17210   -973  -1693  -1262       N  
ATOM   2701  NH2 ARG B1108     -20.135  33.468  54.533  1.00110.51           N  
ANISOU 2701  NH2 ARG B1108    12684  11913  17391  -1220  -1741  -1640       N  
ATOM   2702  N   LEU B1109     -19.823  41.729  56.251  1.00108.98           N  
ANISOU 2702  N   LEU B1109    12243  11196  17970   -226  -1180   -650       N  
ATOM   2703  CA  LEU B1109     -20.479  42.895  55.671  1.00108.73           C  
ANISOU 2703  CA  LEU B1109    11987  11215  18111   -116  -1143   -357       C  
ATOM   2704  C   LEU B1109     -19.518  43.544  54.677  1.00109.11           C  
ANISOU 2704  C   LEU B1109    12034  11332  18091    -95  -1215   -270       C  
ATOM   2705  O   LEU B1109     -19.899  44.445  53.930  1.00111.91           O  
ANISOU 2705  O   LEU B1109    12185  11779  18558    -21  -1220      8       O  
ATOM   2706  CB  LEU B1109     -20.885  43.888  56.756  1.00108.39           C  
ANISOU 2706  CB  LEU B1109    11936  10907  18338     35   -908   -314       C  
ATOM   2707  CG  LEU B1109     -21.542  45.201  56.324  1.00109.30           C  
ANISOU 2707  CG  LEU B1109    11815  10997  18718    180   -808      0       C  
ATOM   2708  CD1 LEU B1109     -22.979  44.977  55.882  1.00110.87           C  
ANISOU 2708  CD1 LEU B1109    11733  11396  18997    172   -861    253       C  
ATOM   2709  CD2 LEU B1109     -21.473  46.218  57.456  1.00110.09           C  
ANISOU 2709  CD2 LEU B1109    12000  10761  19070    317   -537    -63       C  
ATOM   2710  N   VAL B1110     -18.268  43.086  54.677  1.00106.51           N  
ANISOU 2710  N   VAL B1110    11917  10959  17592   -155  -1262   -481       N  
ATOM   2711  CA  VAL B1110     -17.337  43.450  53.613  1.00106.66           C  
ANISOU 2711  CA  VAL B1110    11936  11091  17500   -161  -1351   -411       C  
ATOM   2712  C   VAL B1110     -17.369  42.382  52.524  1.00106.07           C  
ANISOU 2712  C   VAL B1110    11826  11316  17159   -318  -1535   -453       C  
ATOM   2713  O   VAL B1110     -17.397  42.718  51.340  1.00108.69           O  
ANISOU 2713  O   VAL B1110    12015  11884  17399   -340  -1635   -270       O  
ATOM   2714  CB  VAL B1110     -15.893  43.687  54.123  1.00105.69           C  
ANISOU 2714  CB  VAL B1110    12038  10758  17360   -133  -1289   -582       C  
ATOM   2715  CG1 VAL B1110     -14.948  43.954  52.959  1.00105.47           C  
ANISOU 2715  CG1 VAL B1110    11998  10869  17207   -144  -1383   -500       C  
ATOM   2716  CG2 VAL B1110     -15.855  44.854  55.096  1.00103.47           C  
ANISOU 2716  CG2 VAL B1110    11787  10196  17331     -6  -1106   -553       C  
ATOM   2717  N   THR B1111     -17.391  41.107  52.925  1.00104.68           N  
ANISOU 2717  N   THR B1111    11774  11136  16865   -435  -1568   -690       N  
ATOM   2718  CA  THR B1111     -17.445  39.984  51.968  1.00106.37           C  
ANISOU 2718  CA  THR B1111    11979  11598  16839   -607  -1715   -790       C  
ATOM   2719  C   THR B1111     -18.696  40.011  51.083  1.00109.26           C  
ANISOU 2719  C   THR B1111    12093  12263  17158   -685  -1832   -584       C  
ATOM   2720  O   THR B1111     -18.602  40.204  49.870  1.00111.13           O  
ANISOU 2720  O   THR B1111    12224  12767  17233   -749  -1944   -464       O  
ATOM   2721  CB  THR B1111     -17.405  38.601  52.651  1.00104.33           C  
ANISOU 2721  CB  THR B1111    11871  11240  16530   -716  -1704  -1063       C  
ATOM   2722  OG1 THR B1111     -16.303  38.521  53.559  1.00102.99           O  
ANISOU 2722  OG1 THR B1111    11908  10815  16407   -654  -1603  -1219       O  
ATOM   2723  CG2 THR B1111     -17.256  37.526  51.604  1.00104.94           C  
ANISOU 2723  CG2 THR B1111    11965  11531  16378   -896  -1821  -1204       C  
ATOM   2724  N   ALA B1112     -19.857  39.813  51.705  1.00109.29           N  
ANISOU 2724  N   ALA B1112    11991  12239  17294   -688  -1808   -529       N  
ATOM   2725  CA  ALA B1112     -21.108  39.658  50.983  1.00112.18           C  
ANISOU 2725  CA  ALA B1112    12110  12893  17620   -789  -1931   -340       C  
ATOM   2726  C   ALA B1112     -21.552  40.948  50.279  1.00114.87           C  
ANISOU 2726  C   ALA B1112    12199  13392  18055   -688  -1953     41       C  
ATOM   2727  O   ALA B1112     -22.072  40.892  49.155  1.00117.37           O  
ANISOU 2727  O   ALA B1112    12321  14058  18218   -807  -2111    217       O  
ATOM   2728  CB  ALA B1112     -22.195  39.129  51.913  1.00111.73           C  
ANISOU 2728  CB  ALA B1112    11999  12742  17711   -805  -1882   -363       C  
ATOM   2729  N   VAL B1113     -21.336  42.094  50.932  1.00113.25           N  
ANISOU 2729  N   VAL B1113    11991  12937  18102   -481  -1790    170       N  
ATOM   2730  CA  VAL B1113     -21.722  43.407  50.381  1.00114.45           C  
ANISOU 2730  CA  VAL B1113    11893  13168  18423   -353  -1766    556       C  
ATOM   2731  C   VAL B1113     -20.682  43.919  49.369  1.00113.66           C  
ANISOU 2731  C   VAL B1113    11809  13198  18177   -350  -1835    632       C  
ATOM   2732  O   VAL B1113     -19.521  44.170  49.727  1.00111.03           O  
ANISOU 2732  O   VAL B1113    11686  12643  17856   -280  -1749    466       O  
ATOM   2733  CB  VAL B1113     -21.986  44.440  51.503  1.00114.28           C  
ANISOU 2733  CB  VAL B1113    11857  12796  18770   -139  -1530    649       C  
ATOM   2734  CG1 VAL B1113     -22.178  45.840  50.934  1.00116.90           C  
ANISOU 2734  CG1 VAL B1113    11947  13146  19323     11  -1471   1038       C  
ATOM   2735  CG2 VAL B1113     -23.197  44.024  52.328  1.00113.50           C  
ANISOU 2735  CG2 VAL B1113    11676  12635  18813   -137  -1463    652       C  
ATOM   2736  N   PRO B1114     -21.102  44.071  48.098  1.00115.20           N  
ANISOU 2736  N   PRO B1114    11770  13776  18227   -436  -1994    900       N  
ATOM   2737  CA  PRO B1114     -20.180  44.279  46.969  1.00116.51           C  
ANISOU 2737  CA  PRO B1114    11944  14160  18163   -485  -2092    954       C  
ATOM   2738  C   PRO B1114     -19.440  45.621  46.926  1.00116.68           C  
ANISOU 2738  C   PRO B1114    11932  14007  18392   -290  -1975   1165       C  
ATOM   2739  O   PRO B1114     -18.375  45.700  46.309  1.00117.89           O  
ANISOU 2739  O   PRO B1114    12184  14232  18377   -310  -2012   1114       O  
ATOM   2740  CB  PRO B1114     -21.085  44.127  45.733  1.00118.73           C  
ANISOU 2740  CB  PRO B1114    11938  14931  18244   -642  -2293   1230       C  
ATOM   2741  CG  PRO B1114     -22.314  43.430  46.231  1.00119.61           C  
ANISOU 2741  CG  PRO B1114    11963  15073  18410   -730  -2328   1195       C  
ATOM   2742  CD  PRO B1114     -22.492  43.920  47.637  1.00117.79           C  
ANISOU 2742  CD  PRO B1114    11805  14395  18555   -523  -2108   1160       C  
ATOM   2743  N   GLN B1115     -19.985  46.653  47.568  1.00116.33           N  
ANISOU 2743  N   GLN B1115    11751  13727  18724   -106  -1821   1394       N  
ATOM   2744  CA  GLN B1115     -19.413  48.004  47.491  1.00116.65           C  
ANISOU 2744  CA  GLN B1115    11720  13586  19015     74  -1695   1627       C  
ATOM   2745  C   GLN B1115     -18.083  48.155  48.242  1.00115.37           C  
ANISOU 2745  C   GLN B1115    11868  13070  18897    139  -1570   1321       C  
ATOM   2746  O   GLN B1115     -17.128  48.743  47.715  1.00114.93           O  
ANISOU 2746  O   GLN B1115    11832  13011  18826    182  -1570   1403       O  
ATOM   2747  CB  GLN B1115     -20.430  49.037  47.969  1.00117.63           C  
ANISOU 2747  CB  GLN B1115    11601  13531  19561    247  -1534   1946       C  
ATOM   2748  CG  GLN B1115     -21.537  49.298  46.962  1.00121.49           C  
ANISOU 2748  CG  GLN B1115    11699  14400  20060    219  -1659   2407       C  
ATOM   2749  CD  GLN B1115     -22.832  49.758  47.607  1.00123.46           C  
ANISOU 2749  CD  GLN B1115    11727  14504  20676    340  -1517   2636       C  
ATOM   2750  OE1 GLN B1115     -22.931  49.859  48.835  1.00122.14           O  
ANISOU 2750  OE1 GLN B1115    11717  13949  20742    441  -1313   2420       O  
ATOM   2751  NE2 GLN B1115     -23.840  50.033  46.778  1.00125.33           N  
ANISOU 2751  NE2 GLN B1115    11588  15070  20961    323  -1622   3088       N  
HETATM 2752  N   MSE B1116     -18.036  47.615  49.463  1.00114.38           N  
ANISOU 2752  N   MSE B1116    11970  12670  18821    134  -1472    990       N  
HETATM 2753  CA  MSE B1116     -16.825  47.584  50.288  1.00112.00           C  
ANISOU 2753  CA  MSE B1116    11965  12066  18525    158  -1376    682       C  
HETATM 2754  C   MSE B1116     -15.790  46.653  49.709  1.00112.42           C  
ANISOU 2754  C   MSE B1116    12191  12285  18239     25  -1514    470       C  
HETATM 2755  O   MSE B1116     -14.592  46.882  49.905  1.00112.63           O  
ANISOU 2755  O   MSE B1116    12386  12149  18259     54  -1469    348       O  
HETATM 2756  CB  MSE B1116     -17.097  47.111  51.716  1.00111.21           C  
ANISOU 2756  CB  MSE B1116    12045  11698  18513    159  -1256    400       C  
HETATM 2757  CG  MSE B1116     -18.557  47.209  52.156  1.00115.62           C  
ANISOU 2757  CG  MSE B1116    12425  12244  19260    206  -1182    537       C  
HETATM 2758 SE   MSE B1116     -18.920  48.939  53.034  1.00117.04          SE  
ANISOU 2758 SE   MSE B1116    12508  12018  19946    436   -874    718      SE  
HETATM 2759  CE  MSE B1116     -19.833  49.834  51.537  1.00120.30           C  
ANISOU 2759  CE  MSE B1116    12470  12719  20518    518   -948   1302       C  
ATOM   2760  N   ARG B1117     -16.241  45.606  48.999  1.00112.68           N  
ANISOU 2760  N   ARG B1117    12181  12633  18000   -126  -1670    423       N  
ATOM   2761  CA  ARG B1117     -15.361  44.570  48.408  1.00111.45           C  
ANISOU 2761  CA  ARG B1117    12189  12636  17519   -268  -1777    189       C  
ATOM   2762  C   ARG B1117     -14.239  45.127  47.519  1.00110.46           C  
ANISOU 2762  C   ARG B1117    12069  12603  17299   -238  -1802    293       C  
ATOM   2763  O   ARG B1117     -13.062  44.819  47.749  1.00108.01           O  
ANISOU 2763  O   ARG B1117    11967  12153  16920   -243  -1765     84       O  
ATOM   2764  CB  ARG B1117     -16.180  43.521  47.629  1.00115.52           C  
ANISOU 2764  CB  ARG B1117    12614  13501  17776   -451  -1932    153       C  
ATOM   2765  CG  ARG B1117     -16.298  42.133  48.274  1.00114.26           C  
ANISOU 2765  CG  ARG B1117    12637  13260  17515   -575  -1938   -197       C  
ATOM   2766  CD  ARG B1117     -16.917  41.124  47.300  1.00116.06           C  
ANISOU 2766  CD  ARG B1117    12787  13845  17464   -788  -2093   -257       C  
ATOM   2767  NE  ARG B1117     -16.856  39.732  47.774  1.00115.41           N  
ANISOU 2767  NE  ARG B1117    12889  13671  17290   -919  -2087   -607       N  
ATOM   2768  CZ  ARG B1117     -17.363  38.676  47.123  1.00116.88           C  
ANISOU 2768  CZ  ARG B1117    13052  14096  17260  -1129  -2195   -747       C  
ATOM   2769  NH1 ARG B1117     -17.982  38.822  45.953  1.00118.02           N  
ANISOU 2769  NH1 ARG B1117    13001  14630  17210  -1253  -2337   -574       N  
ATOM   2770  NH2 ARG B1117     -17.250  37.456  47.643  1.00114.03           N  
ANISOU 2770  NH2 ARG B1117    12859  13590  16879  -1228  -2159  -1057       N  
ATOM   2771  N   LYS B1118     -14.612  45.938  46.519  1.00110.51           N  
ANISOU 2771  N   LYS B1118    11828  12851  17309   -206  -1861    643       N  
ATOM   2772  CA  LYS B1118     -13.656  46.594  45.601  1.00109.64           C  
ANISOU 2772  CA  LYS B1118    11674  12859  17125   -167  -1881    814       C  
ATOM   2773  C   LYS B1118     -12.718  47.586  46.301  1.00108.31           C  
ANISOU 2773  C   LYS B1118    11600  12318  17236     -8  -1734    833       C  
ATOM   2774  O   LYS B1118     -11.534  47.687  45.947  1.00106.21           O  
ANISOU 2774  O   LYS B1118    11434  12038  16882     -1  -1731    790       O  
ATOM   2775  CB  LYS B1118     -14.395  47.329  44.479  1.00111.19           C  
ANISOU 2775  CB  LYS B1118    11544  13398  17305   -159  -1970   1245       C  
ATOM   2776  CG  LYS B1118     -14.965  46.431  43.403  1.00112.20           C  
ANISOU 2776  CG  LYS B1118    11575  14001  17054   -362  -2150   1248       C  
ATOM   2777  CD  LYS B1118     -14.285  46.645  42.062  1.00112.66           C  
ANISOU 2777  CD  LYS B1118    11553  14411  16843   -420  -2237   1413       C  
ATOM   2778  CE  LYS B1118     -15.136  46.033  40.959  1.00115.05           C  
ANISOU 2778  CE  LYS B1118    11682  15239  16794   -630  -2421   1508       C  
ATOM   2779  NZ  LYS B1118     -14.798  46.535  39.599  1.00116.78           N  
ANISOU 2779  NZ  LYS B1118    11721  15874  16776   -677  -2512   1808       N  
ATOM   2780  N   ILE B1119     -13.249  48.330  47.273  1.00108.01           N  
ANISOU 2780  N   ILE B1119    11522  11981  17535    111  -1605    897       N  
ATOM   2781  CA  ILE B1119     -12.444  49.341  47.969  1.00108.48           C  
ANISOU 2781  CA  ILE B1119    11665  11677  17875    238  -1457    901       C  
ATOM   2782  C   ILE B1119     -11.449  48.680  48.928  1.00106.18           C  
ANISOU 2782  C   ILE B1119    11683  11151  17511    188  -1416    517       C  
ATOM   2783  O   ILE B1119     -10.287  49.090  49.006  1.00105.04           O  
ANISOU 2783  O   ILE B1119    11643  10863  17405    217  -1379    478       O  
ATOM   2784  CB  ILE B1119     -13.304  50.449  48.640  1.00109.22           C  
ANISOU 2784  CB  ILE B1119    11612  11516  18370    378  -1298   1090       C  
ATOM   2785  CG1 ILE B1119     -14.114  51.225  47.580  1.00112.68           C  
ANISOU 2785  CG1 ILE B1119    11702  12191  18918    445  -1335   1552       C  
ATOM   2786  CG2 ILE B1119     -12.439  51.413  49.452  1.00108.05           C  
ANISOU 2786  CG2 ILE B1119    11587  10967  18499    472  -1132   1016       C  
ATOM   2787  CD1 ILE B1119     -13.301  52.125  46.653  1.00112.59           C  
ANISOU 2787  CD1 ILE B1119    11569  12252  18959    507  -1347   1833       C  
ATOM   2788  N   VAL B1120     -11.904  47.639  49.622  1.00104.77           N  
ANISOU 2788  N   VAL B1120    11629  10952  17227    107  -1431    262       N  
ATOM   2789  CA  VAL B1120     -11.018  46.772  50.405  1.00102.71           C  
ANISOU 2789  CA  VAL B1120    11631  10542  16851     38  -1420    -70       C  
ATOM   2790  C   VAL B1120      -9.949  46.161  49.486  1.00101.84           C  
ANISOU 2790  C   VAL B1120    11592  10616  16486    -33  -1513   -126       C  
ATOM   2791  O   VAL B1120      -8.772  46.051  49.866  1.00 99.43           O  
ANISOU 2791  O   VAL B1120    11449  10161  16170    -36  -1482   -262       O  
ATOM   2792  CB  VAL B1120     -11.829  45.707  51.201  1.00101.98           C  
ANISOU 2792  CB  VAL B1120    11617  10431  16698    -38  -1423   -284       C  
ATOM   2793  CG1 VAL B1120     -10.987  44.485  51.569  1.00 99.42           C  
ANISOU 2793  CG1 VAL B1120    11509  10077  16187   -138  -1456   -571       C  
ATOM   2794  CG2 VAL B1120     -12.430  46.347  52.449  1.00101.07           C  
ANISOU 2794  CG2 VAL B1120    11516  10043  16844     40  -1279   -305       C  
ATOM   2795  N   SER B1121     -10.362  45.797  48.271  1.00102.92           N  
ANISOU 2795  N   SER B1121    11597  11090  16419    -96  -1620    -11       N  
ATOM   2796  CA  SER B1121      -9.423  45.345  47.245  1.00103.81           C  
ANISOU 2796  CA  SER B1121    11751  11408  16283   -159  -1683    -41       C  
ATOM   2797  C   SER B1121      -8.391  46.441  46.944  1.00104.93           C  
ANISOU 2797  C   SER B1121    11863  11464  16541    -56  -1639    146       C  
ATOM   2798  O   SER B1121      -7.192  46.160  46.863  1.00104.42           O  
ANISOU 2798  O   SER B1121    11932  11348  16396    -68  -1622     35       O  
ATOM   2799  CB  SER B1121     -10.158  44.904  45.969  1.00104.46           C  
ANISOU 2799  CB  SER B1121    11679  11904  16108   -264  -1803     63       C  
ATOM   2800  OG  SER B1121     -10.863  43.689  46.167  1.00102.59           O  
ANISOU 2800  OG  SER B1121    11505  11743  15730   -394  -1848   -166       O  
ATOM   2801  N   ALA B1122      -8.867  47.682  46.806  1.00106.59           N  
ANISOU 2801  N   ALA B1122    11886  11642  16971     48  -1608    441       N  
ATOM   2802  CA  ALA B1122      -8.008  48.854  46.598  1.00107.44           C  
ANISOU 2802  CA  ALA B1122    11939  11626  17257    152  -1550    647       C  
ATOM   2803  C   ALA B1122      -7.247  49.305  47.864  1.00107.39           C  
ANISOU 2803  C   ALA B1122    12104  11209  17491    202  -1437    488       C  
ATOM   2804  O   ALA B1122      -6.324  50.127  47.784  1.00107.80           O  
ANISOU 2804  O   ALA B1122    12152  11129  17678    259  -1393    596       O  
ATOM   2805  CB  ALA B1122      -8.828  50.005  46.038  1.00108.52           C  
ANISOU 2805  CB  ALA B1122    11797  11847  17588    245  -1537   1033       C  
ATOM   2806  N   LEU B1123      -7.639  48.772  49.022  1.00107.02           N  
ANISOU 2806  N   LEU B1123    12199  10978  17488    166  -1395    239       N  
ATOM   2807  CA  LEU B1123      -6.996  49.102  50.298  1.00106.36           C  
ANISOU 2807  CA  LEU B1123    12283  10549  17579    177  -1299     63       C  
ATOM   2808  C   LEU B1123      -5.710  48.295  50.565  1.00104.25           C  
ANISOU 2808  C   LEU B1123    12213  10250  17149    101  -1336   -146       C  
ATOM   2809  O   LEU B1123      -4.692  48.841  51.024  1.00104.03           O  
ANISOU 2809  O   LEU B1123    12265  10030  17233    109  -1295   -166       O  
ATOM   2810  CB  LEU B1123      -7.981  48.961  51.479  1.00108.72           C  
ANISOU 2810  CB  LEU B1123    12636  10679  17992    171  -1223    -90       C  
ATOM   2811  CG  LEU B1123      -9.247  49.848  51.579  1.00113.11           C  
ANISOU 2811  CG  LEU B1123    13013  11168  18794    262  -1132     94       C  
ATOM   2812  CD1 LEU B1123      -9.928  49.719  52.941  1.00112.21           C  
ANISOU 2812  CD1 LEU B1123    13002  10839  18793    252  -1022   -110       C  
ATOM   2813  CD2 LEU B1123      -9.008  51.321  51.244  1.00114.82           C  
ANISOU 2813  CD2 LEU B1123    13090  11240  19295    370  -1041    348       C  
ATOM   2814  N   ILE B1124      -5.756  46.998  50.275  1.00100.56           N  
ANISOU 2814  N   ILE B1124    11810   9963  16436     23  -1405   -292       N  
ATOM   2815  CA  ILE B1124      -4.603  46.131  50.490  1.00 96.35           C  
ANISOU 2815  CA  ILE B1124    11437   9397  15774    -38  -1420   -466       C  
ATOM   2816  C   ILE B1124      -3.626  46.197  49.304  1.00 96.16           C  
ANISOU 2816  C   ILE B1124    11369   9536  15633    -23  -1452   -341       C  
ATOM   2817  O   ILE B1124      -2.435  45.874  49.451  1.00 93.87           O  
ANISOU 2817  O   ILE B1124    11179   9173  15314    -41  -1439   -409       O  
ATOM   2818  CB  ILE B1124      -5.045  44.683  50.787  1.00 95.49           C  
ANISOU 2818  CB  ILE B1124    11420   9357  15503   -126  -1446   -688       C  
ATOM   2819  CG1 ILE B1124      -6.277  44.688  51.711  1.00 95.02           C  
ANISOU 2819  CG1 ILE B1124    11353   9205  15544   -131  -1418   -754       C  
ATOM   2820  CG2 ILE B1124      -3.896  43.897  51.416  1.00 94.64           C  
ANISOU 2820  CG2 ILE B1124    11473   9127  15358   -173  -1427   -851       C  
ATOM   2821  CD1 ILE B1124      -7.216  43.502  51.558  1.00 93.94           C  
ANISOU 2821  CD1 ILE B1124    11210   9219  15266   -206  -1460   -875       C  
ATOM   2822  N   SER B1125      -4.119  46.656  48.147  1.00 96.89           N  
ANISOU 2822  N   SER B1125    11293   9856  15663      9  -1488   -133       N  
ATOM   2823  CA  SER B1125      -3.310  46.719  46.911  1.00 97.76           C  
ANISOU 2823  CA  SER B1125    11343  10177  15626     18  -1513      3       C  
ATOM   2824  C   SER B1125      -2.173  47.739  46.998  1.00 97.46           C  
ANISOU 2824  C   SER B1125    11293   9970  15766     91  -1470    156       C  
ATOM   2825  O   SER B1125      -1.403  47.923  46.044  1.00 96.70           O  
ANISOU 2825  O   SER B1125    11139  10023  15580    113  -1476    298       O  
ATOM   2826  CB  SER B1125      -4.181  47.022  45.695  1.00 98.19           C  
ANISOU 2826  CB  SER B1125    11200  10554  15556     20  -1572    221       C  
ATOM   2827  OG  SER B1125      -4.677  48.340  45.766  1.00 99.21           O  
ANISOU 2827  OG  SER B1125    11165  10598  15931    114  -1552    488       O  
ATOM   2828  N   VAL B1126      -2.079  48.385  48.157  1.00 96.39           N  
ANISOU 2828  N   VAL B1126    11215   9531  15877    115  -1422    116       N  
ATOM   2829  CA  VAL B1126      -1.052  49.376  48.425  1.00 97.11           C  
ANISOU 2829  CA  VAL B1126    11306   9421  16169    157  -1382    227       C  
ATOM   2830  C   VAL B1126       0.253  48.710  48.924  1.00 96.25           C  
ANISOU 2830  C   VAL B1126    11354   9217  15999    100  -1384     71       C  
ATOM   2831  O   VAL B1126       1.323  48.912  48.317  1.00 96.28           O  
ANISOU 2831  O   VAL B1126    11329   9266  15988    122  -1385    194       O  
ATOM   2832  CB  VAL B1126      -1.573  50.443  49.417  1.00 97.98           C  
ANISOU 2832  CB  VAL B1126    11404   9249  16576    186  -1314    240       C  
ATOM   2833  CG1 VAL B1126      -0.530  51.521  49.665  1.00 99.07           C  
ANISOU 2833  CG1 VAL B1126    11537   9168  16937    205  -1270    343       C  
ATOM   2834  CG2 VAL B1126      -2.855  51.068  48.889  1.00100.27           C  
ANISOU 2834  CG2 VAL B1126    11508   9629  16961    259  -1294    435       C  
ATOM   2835  N   ILE B1127       0.157  47.892  49.983  1.00 92.04           N  
ANISOU 2835  N   ILE B1127    10967   8571  15432     31  -1383   -168       N  
ATOM   2836  CA  ILE B1127       1.349  47.397  50.694  1.00 90.49           C  
ANISOU 2836  CA  ILE B1127    10896   8253  15234    -26  -1384   -276       C  
ATOM   2837  C   ILE B1127       2.420  46.677  49.839  1.00 91.73           C  
ANISOU 2837  C   ILE B1127    11054   8550  15249    -19  -1387   -234       C  
ATOM   2838  O   ILE B1127       3.607  46.785  50.160  1.00 92.20           O  
ANISOU 2838  O   ILE B1127    11146   8507  15378    -35  -1383   -194       O  
ATOM   2839  CB  ILE B1127       1.011  46.637  52.018  1.00 88.60           C  
ANISOU 2839  CB  ILE B1127    10791   7893  14982   -105  -1383   -504       C  
ATOM   2840  CG1 ILE B1127       2.273  46.389  52.853  1.00 86.02           C  
ANISOU 2840  CG1 ILE B1127    10556   7439  14689   -172  -1395   -550       C  
ATOM   2841  CG2 ILE B1127       0.275  45.325  51.752  1.00 91.32           C  
ANISOU 2841  CG2 ILE B1127    11162   8387  15147   -127  -1392   -639       C  
ATOM   2842  CD1 ILE B1127       2.006  46.104  54.320  1.00 85.18           C  
ANISOU 2842  CD1 ILE B1127    10557   7200  14606   -262  -1397   -717       C  
ATOM   2843  N   PRO B1128       2.025  45.959  48.752  1.00 93.52           N  
ANISOU 2843  N   PRO B1128    11240   9014  15277     -5  -1384   -243       N  
ATOM   2844  CA  PRO B1128       3.085  45.421  47.882  1.00 93.17           C  
ANISOU 2844  CA  PRO B1128    11194   9092  15114      9  -1350   -201       C  
ATOM   2845  C   PRO B1128       4.063  46.496  47.435  1.00 94.42           C  
ANISOU 2845  C   PRO B1128    11263   9226  15384     67  -1344     37       C  
ATOM   2846  O   PRO B1128       5.197  46.171  47.077  1.00 96.70           O  
ANISOU 2846  O   PRO B1128    11561   9537  15643     81  -1304     83       O  
ATOM   2847  CB  PRO B1128       2.316  44.897  46.666  1.00 94.62           C  
ANISOU 2847  CB  PRO B1128    11322   9563  15067      2  -1349   -222       C  
ATOM   2848  CG  PRO B1128       0.983  44.510  47.206  1.00 95.32           C  
ANISOU 2848  CG  PRO B1128    11438   9644  15135    -46  -1385   -368       C  
ATOM   2849  CD  PRO B1128       0.690  45.451  48.355  1.00 94.84           C  
ANISOU 2849  CD  PRO B1128    11378   9347  15309    -25  -1404   -324       C  
ATOM   2850  N   GLY B1129       3.622  47.757  47.453  1.00 94.06           N  
ANISOU 2850  N   GLY B1129    11123   9125  15492    105  -1368    197       N  
ATOM   2851  CA  GLY B1129       4.496  48.909  47.168  1.00 93.85           C  
ANISOU 2851  CA  GLY B1129    11002   9025  15632    154  -1359    434       C  
ATOM   2852  C   GLY B1129       4.900  49.695  48.412  1.00 91.46           C  
ANISOU 2852  C   GLY B1129    10751   8418  15584    114  -1365    411       C  
ATOM   2853  O   GLY B1129       5.159  50.903  48.339  1.00 89.71           O  
ANISOU 2853  O   GLY B1129    10438   8082  15563    144  -1355    589       O  
HETATM 2854  N   MSE B1130       4.950  48.996  49.547  1.00 90.22           N  
ANISOU 2854  N   MSE B1130    10732   8135  15412     35  -1379    193       N  
HETATM 2855  CA  MSE B1130       5.287  49.592  50.842  1.00 91.46           C  
ANISOU 2855  CA  MSE B1130    10960   8040  15750    -44  -1391    121       C  
HETATM 2856  C   MSE B1130       6.260  48.743  51.636  1.00 91.39           C  
ANISOU 2856  C   MSE B1130    11052   7982  15689   -130  -1421     19       C  
HETATM 2857  O   MSE B1130       6.712  49.159  52.724  1.00 90.98           O  
ANISOU 2857  O   MSE B1130    11058   7762  15746   -228  -1448    -35       O  
HETATM 2858  CB  MSE B1130       4.025  49.832  51.667  1.00 92.12           C  
ANISOU 2858  CB  MSE B1130    11093   8018  15891    -70  -1373    -29       C  
HETATM 2859  CG  MSE B1130       3.608  51.297  51.582  1.00 95.68           C  
ANISOU 2859  CG  MSE B1130    11450   8327  16576    -27  -1326     99       C  
HETATM 2860 SE   MSE B1130       2.118  51.737  52.806  1.00100.97          SE  
ANISOU 2860 SE   MSE B1130    12187   8802  17376    -59  -1253   -103      SE  
HETATM 2861  CE  MSE B1130       2.923  51.349  54.568  1.00 94.69           C  
ANISOU 2861  CE  MSE B1130    11598   7833  16545   -244  -1281   -374       C  
ATOM   2862  N   LEU B1131       6.614  47.569  51.096  1.00 89.29           N  
ANISOU 2862  N   LEU B1131    10799   7865  15263   -104  -1407     -1       N  
ATOM   2863  CA  LEU B1131       7.508  46.632  51.796  1.00 86.45           C  
ANISOU 2863  CA  LEU B1131    10505   7464  14875   -169  -1418    -61       C  
ATOM   2864  C   LEU B1131       8.921  47.168  51.952  1.00 85.64           C  
ANISOU 2864  C   LEU B1131    10357   7286  14898   -201  -1444    106       C  
ATOM   2865  O   LEU B1131       9.506  47.060  53.037  1.00 83.82           O  
ANISOU 2865  O   LEU B1131    10170   6955  14722   -305  -1494     78       O  
ATOM   2866  CB  LEU B1131       7.546  45.260  51.121  1.00 85.16           C  
ANISOU 2866  CB  LEU B1131    10356   7443  14556   -124  -1360   -121       C  
ATOM   2867  CG  LEU B1131       6.251  44.471  50.982  1.00 84.62           C  
ANISOU 2867  CG  LEU B1131    10336   7461  14353   -119  -1340   -302       C  
ATOM   2868  CD1 LEU B1131       6.540  43.281  50.084  1.00 85.04           C  
ANISOU 2868  CD1 LEU B1131    10392   7644  14276    -83  -1259   -349       C  
ATOM   2869  CD2 LEU B1131       5.677  44.038  52.329  1.00 82.33           C  
ANISOU 2869  CD2 LEU B1131    10136   7059  14088   -201  -1372   -462       C  
ATOM   2870  N   SER B1132       9.460  47.739  50.872  1.00 86.30           N  
ANISOU 2870  N   SER B1132    10339   7435  15018   -122  -1417    296       N  
ATOM   2871  CA  SER B1132      10.830  48.273  50.876  1.00 87.92           C  
ANISOU 2871  CA  SER B1132    10474   7578  15353   -144  -1437    486       C  
ATOM   2872  C   SER B1132      11.038  49.078  52.150  1.00 87.49           C  
ANISOU 2872  C   SER B1132    10461   7335  15447   -281  -1515    446       C  
ATOM   2873  O   SER B1132      11.920  48.767  52.951  1.00 87.36           O  
ANISOU 2873  O   SER B1132    10462   7271  15460   -382  -1567    462       O  
ATOM   2874  CB  SER B1132      11.100  49.147  49.641  1.00 89.49           C  
ANISOU 2874  CB  SER B1132    10547   7850  15604    -47  -1401    705       C  
ATOM   2875  OG  SER B1132      10.995  48.398  48.442  1.00 89.68           O  
ANISOU 2875  OG  SER B1132    10538   8084  15453     55  -1325    733       O  
ATOM   2876  N   VAL B1133      10.176  50.081  52.330  1.00 87.26           N  
ANISOU 2876  N   VAL B1133    10442   7208  15506   -292  -1514    391       N  
ATOM   2877  CA  VAL B1133      10.102  50.902  53.538  1.00 87.20           C  
ANISOU 2877  CA  VAL B1133    10497   7009  15625   -433  -1555    284       C  
ATOM   2878  C   VAL B1133       9.909  50.013  54.779  1.00 86.88           C  
ANISOU 2878  C   VAL B1133    10579   6969  15463   -550  -1597     82       C  
ATOM   2879  O   VAL B1133      10.711  50.072  55.721  1.00 86.17           O  
ANISOU 2879  O   VAL B1133    10519   6823  15397   -699  -1666     71       O  
ATOM   2880  CB  VAL B1133       8.916  51.896  53.434  1.00 87.32           C  
ANISOU 2880  CB  VAL B1133    10505   6920  15752   -389  -1496    228       C  
ATOM   2881  CG1 VAL B1133       8.962  52.935  54.550  1.00 87.60           C  
ANISOU 2881  CG1 VAL B1133    10600   6725  15959   -535  -1498    115       C  
ATOM   2882  CG2 VAL B1133       8.890  52.571  52.065  1.00 87.61           C  
ANISOU 2882  CG2 VAL B1133    10394   7016  15878   -246  -1449    463       C  
ATOM   2883  N   ILE B1134       8.853  49.187  54.750  1.00 85.87           N  
ANISOU 2883  N   ILE B1134    10505   6921  15199   -492  -1562    -56       N  
ATOM   2884  CA  ILE B1134       8.420  48.362  55.890  1.00 85.17           C  
ANISOU 2884  CA  ILE B1134    10524   6837  15000   -586  -1586   -242       C  
ATOM   2885  C   ILE B1134       9.469  47.363  56.418  1.00 84.99           C  
ANISOU 2885  C   ILE B1134    10502   6877  14912   -661  -1642   -185       C  
ATOM   2886  O   ILE B1134       9.688  47.288  57.641  1.00 84.00           O  
ANISOU 2886  O   ILE B1134    10434   6722  14761   -812  -1702   -256       O  
ATOM   2887  CB  ILE B1134       7.079  47.659  55.568  1.00 85.18           C  
ANISOU 2887  CB  ILE B1134    10557   6917  14891   -495  -1532   -368       C  
ATOM   2888  CG1 ILE B1134       5.908  48.603  55.899  1.00 86.60           C  
ANISOU 2888  CG1 ILE B1134    10765   6992  15147   -496  -1490   -478       C  
ATOM   2889  CG2 ILE B1134       6.945  46.322  56.297  1.00 84.49           C  
ANISOU 2889  CG2 ILE B1134    10536   6892  14675   -546  -1547   -479       C  
ATOM   2890  CD1 ILE B1134       4.632  48.345  55.113  1.00 85.30           C  
ANISOU 2890  CD1 ILE B1134    10565   6918  14929   -375  -1438   -503       C  
ATOM   2891  N   ALA B1135      10.103  46.609  55.505  1.00 84.16           N  
ANISOU 2891  N   ALA B1135    10325   6867  14783   -560  -1610    -49       N  
ATOM   2892  CA  ALA B1135      11.140  45.619  55.871  1.00 82.90           C  
ANISOU 2892  CA  ALA B1135    10134   6754  14611   -600  -1632     52       C  
ATOM   2893  C   ALA B1135      12.315  46.257  56.627  1.00 84.02           C  
ANISOU 2893  C   ALA B1135    10233   6848  14844   -744  -1729    186       C  
ATOM   2894  O   ALA B1135      12.668  45.789  57.713  1.00 83.61           O  
ANISOU 2894  O   ALA B1135    10196   6815  14757   -875  -1797    185       O  
ATOM   2895  CB  ALA B1135      11.638  44.862  54.640  1.00 81.59           C  
ANISOU 2895  CB  ALA B1135     9894   6670  14436   -455  -1541    169       C  
ATOM   2896  N   LEU B1136      12.905  47.321  56.057  1.00 83.95           N  
ANISOU 2896  N   LEU B1136    10159   6790  14950   -733  -1741    313       N  
ATOM   2897  CA  LEU B1136      14.044  48.015  56.676  1.00 84.77           C  
ANISOU 2897  CA  LEU B1136    10208   6845  15153   -886  -1839    445       C  
ATOM   2898  C   LEU B1136      13.649  48.746  57.966  1.00 84.96           C  
ANISOU 2898  C   LEU B1136    10331   6789  15162  -1089  -1917    266       C  
ATOM   2899  O   LEU B1136      14.477  48.948  58.861  1.00 85.08           O  
ANISOU 2899  O   LEU B1136    10329   6812  15184  -1278  -2022    319       O  
ATOM   2900  CB  LEU B1136      14.681  49.011  55.697  1.00 86.10           C  
ANISOU 2900  CB  LEU B1136    10279   6967  15470   -821  -1820    623       C  
ATOM   2901  CG  LEU B1136      15.984  49.715  56.136  1.00 88.20           C  
ANISOU 2901  CG  LEU B1136    10461   7186  15865   -973  -1919    797       C  
ATOM   2902  CD1 LEU B1136      17.201  48.786  56.116  1.00 88.69           C  
ANISOU 2902  CD1 LEU B1136    10413   7353  15933   -970  -1945   1025       C  
ATOM   2903  CD2 LEU B1136      16.254  50.939  55.280  1.00 89.27           C  
ANISOU 2903  CD2 LEU B1136    10518   7231  16168   -920  -1891    921       C  
HETATM 2904  N   MSE B1137      12.380  49.137  58.044  1.00 84.13           N  
ANISOU 2904  N   MSE B1137    10321   6616  15027  -1057  -1858     57       N  
HETATM 2905  CA  MSE B1137      11.843  49.880  59.183  1.00 83.89           C  
ANISOU 2905  CA  MSE B1137    10398   6489  14986  -1230  -1883   -153       C  
HETATM 2906  C   MSE B1137      11.813  49.020  60.448  1.00 82.70           C  
ANISOU 2906  C   MSE B1137    10316   6441  14666  -1381  -1950   -250       C  
HETATM 2907  O   MSE B1137      12.086  49.525  61.549  1.00 82.84           O  
ANISOU 2907  O   MSE B1137    10389   6442  14644  -1602  -2021   -344       O  
HETATM 2908  CB  MSE B1137      10.474  50.362  58.713  1.00 84.06           C  
ANISOU 2908  CB  MSE B1137    10468   6423  15046  -1101  -1770   -298       C  
HETATM 2909  CG  MSE B1137       9.705  51.036  59.817  1.00 86.79           C  
ANISOU 2909  CG  MSE B1137    10934   6653  15388  -1242  -1742   -545       C  
HETATM 2910 SE   MSE B1137      10.728  52.660  60.141  1.00 94.39          SE  
ANISOU 2910 SE   MSE B1137    11878   7428  16559  -1433  -1777   -520      SE  
HETATM 2911  CE  MSE B1137       9.712  53.743  58.830  1.00 92.13           C  
ANISOU 2911  CE  MSE B1137    11522   6962  16522  -1193  -1614   -471       C  
ATOM   2912  N   THR B1138      11.493  47.727  60.294  1.00 87.60           N  
ANISOU 2912  N   THR B1138     9311   9346  14628   2659   1281    -65       N  
ATOM   2913  CA  THR B1138      11.529  46.759  61.402  1.00 86.14           C  
ANISOU 2913  CA  THR B1138     9091   9152  14485   2654   1185    -89       C  
ATOM   2914  C   THR B1138      12.965  46.293  61.713  1.00 86.86           C  
ANISOU 2914  C   THR B1138     9098   9244  14661   2733   1254   -103       C  
ATOM   2915  O   THR B1138      13.318  46.056  62.871  1.00 86.21           O  
ANISOU 2915  O   THR B1138     8918   9173  14665   2715   1196   -109       O  
ATOM   2916  CB  THR B1138      10.593  45.539  61.167  1.00 85.59           C  
ANISOU 2916  CB  THR B1138     9182   9030  14307   2650   1076   -111       C  
ATOM   2917  OG1 THR B1138      10.610  44.686  62.313  1.00 84.61           O  
ANISOU 2917  OG1 THR B1138     9024   8898  14224   2630    977   -128       O  
ATOM   2918  CG2 THR B1138      11.011  44.716  59.961  1.00 86.86           C  
ANISOU 2918  CG2 THR B1138     9493   9133  14378   2748   1136   -133       C  
ATOM   2919  N   LEU B1139      13.796  46.176  60.679  1.00 87.57           N  
ANISOU 2919  N   LEU B1139     9224   9324  14724   2822   1378   -106       N  
ATOM   2920  CA  LEU B1139      15.185  45.784  60.867  1.00 87.94           C  
ANISOU 2920  CA  LEU B1139     9177   9383  14854   2909   1457   -116       C  
ATOM   2921  C   LEU B1139      16.014  46.959  61.407  1.00 87.31           C  
ANISOU 2921  C   LEU B1139     8902   9365  14907   2870   1524    -77       C  
ATOM   2922  O   LEU B1139      17.195  46.800  61.737  1.00 87.92           O  
ANISOU 2922  O   LEU B1139     8861   9465  15080   2924   1580    -74       O  
ATOM   2923  CB  LEU B1139      15.767  45.233  59.566  1.00 90.03           C  
ANISOU 2923  CB  LEU B1139     9546   9624  15036   3027   1576   -133       C  
ATOM   2924  CG  LEU B1139      16.836  44.149  59.734  1.00 91.81           C  
ANISOU 2924  CG  LEU B1139     9750   9835  15300   3147   1605   -167       C  
ATOM   2925  CD1 LEU B1139      16.281  42.950  60.502  1.00 91.62           C  
ANISOU 2925  CD1 LEU B1139     9812   9749  15250   3143   1443   -206       C  
ATOM   2926  CD2 LEU B1139      17.363  43.714  58.368  1.00 93.94           C  
ANISOU 2926  CD2 LEU B1139    10131  10088  15475   3274   1738   -184       C  
ATOM   2927  N   PHE B1140      15.382  48.133  61.464  1.00 85.37           N  
ANISOU 2927  N   PHE B1140     8630   9144  14664   2778   1512    -44       N  
ATOM   2928  CA  PHE B1140      15.856  49.291  62.224  1.00 84.33           C  
ANISOU 2928  CA  PHE B1140     8336   9055  14650   2712   1522     -7       C  
ATOM   2929  C   PHE B1140      15.287  49.199  63.653  1.00 82.91           C  
ANISOU 2929  C   PHE B1140     8110   8872  14521   2645   1377    -20       C  
ATOM   2930  O   PHE B1140      15.925  49.613  64.631  1.00 81.83           O  
ANISOU 2930  O   PHE B1140     7840   8755  14497   2616   1355     -5       O  
ATOM   2931  CB  PHE B1140      15.361  50.561  61.532  1.00 84.12           C  
ANISOU 2931  CB  PHE B1140     8336   9043  14582   2655   1567     28       C  
ATOM   2932  CG  PHE B1140      15.782  51.844  62.194  1.00 83.49           C  
ANISOU 2932  CG  PHE B1140     8118   8995  14608   2583   1570     69       C  
ATOM   2933  CD1 PHE B1140      17.123  52.241  62.190  1.00 84.50           C  
ANISOU 2933  CD1 PHE B1140     8116   9155  14836   2597   1665    104       C  
ATOM   2934  CD2 PHE B1140      14.833  52.677  62.781  1.00 81.66           C  
ANISOU 2934  CD2 PHE B1140     7891   8762  14372   2503   1478     76       C  
ATOM   2935  CE1 PHE B1140      17.508  53.436  62.781  1.00 84.17           C  
ANISOU 2935  CE1 PHE B1140     7959   9133  14888   2521   1654    147       C  
ATOM   2936  CE2 PHE B1140      15.209  53.872  63.374  1.00 81.50           C  
ANISOU 2936  CE2 PHE B1140     7768   8760  14440   2441   1471    111       C  
ATOM   2937  CZ  PHE B1140      16.547  54.255  63.375  1.00 82.80           C  
ANISOU 2937  CZ  PHE B1140     7812   8946  14702   2444   1553    149       C  
ATOM   2938  N   PHE B1141      14.083  48.637  63.749  1.00 81.88           N  
ANISOU 2938  N   PHE B1141     8093   8718  14302   2618   1279    -44       N  
ATOM   2939  CA  PHE B1141      13.405  48.427  65.015  1.00 80.81           C  
ANISOU 2939  CA  PHE B1141     7932   8583  14188   2555   1148    -55       C  
ATOM   2940  C   PHE B1141      13.929  47.234  65.813  1.00 81.32           C  
ANISOU 2940  C   PHE B1141     7983   8622  14292   2589   1087    -82       C  
ATOM   2941  O   PHE B1141      13.671  47.147  67.022  1.00 80.48           O  
ANISOU 2941  O   PHE B1141     7830   8521  14228   2535    990    -86       O  
ATOM   2942  CB  PHE B1141      11.901  48.274  64.782  1.00 80.32           C  
ANISOU 2942  CB  PHE B1141     7986   8515  14016   2507   1069    -62       C  
ATOM   2943  CG  PHE B1141      11.085  49.430  65.298  1.00 79.52           C  
ANISOU 2943  CG  PHE B1141     7836   8451  13927   2430   1028    -42       C  
ATOM   2944  CD1 PHE B1141      11.181  50.680  64.719  1.00 79.32           C  
ANISOU 2944  CD1 PHE B1141     7784   8442  13912   2421   1098    -17       C  
ATOM   2945  CD2 PHE B1141      10.219  49.258  66.375  1.00 79.14           C  
ANISOU 2945  CD2 PHE B1141     7772   8422  13874   2370    919    -49       C  
ATOM   2946  CE1 PHE B1141      10.443  51.735  65.203  1.00 78.69           C  
ANISOU 2946  CE1 PHE B1141     7669   8389  13839   2364   1054     -4       C  
ATOM   2947  CE2 PHE B1141       9.481  50.314  66.873  1.00 78.26           C  
ANISOU 2947  CE2 PHE B1141     7616   8350  13770   2317    886    -36       C  
ATOM   2948  CZ  PHE B1141       9.593  51.552  66.279  1.00 78.40           C  
ANISOU 2948  CZ  PHE B1141     7614   8375  13799   2319    951    -16       C  
ATOM   2949  N   TYR B1142      14.655  46.317  65.154  1.00 82.14           N  
ANISOU 2949  N   TYR B1142     8133   8696  14378   2682   1140   -103       N  
ATOM   2950  CA  TYR B1142      15.161  45.108  65.840  1.00 82.15           C  
ANISOU 2950  CA  TYR B1142     8139   8662  14410   2728   1073   -133       C  
ATOM   2951  C   TYR B1142      16.563  45.296  66.434  1.00 82.92           C  
ANISOU 2951  C   TYR B1142     8081   8779  14647   2769   1116   -125       C  
ATOM   2952  O   TYR B1142      16.938  44.604  67.399  1.00 82.80           O  
ANISOU 2952  O   TYR B1142     8033   8740  14688   2778   1032   -142       O  
ATOM   2953  CB  TYR B1142      15.073  43.852  64.950  1.00 82.49           C  
ANISOU 2953  CB  TYR B1142     8341   8652  14352   2813   1074   -166       C  
ATOM   2954  CG  TYR B1142      15.561  42.598  65.654  1.00 83.00           C  
ANISOU 2954  CG  TYR B1142     8426   8669  14442   2863    991   -199       C  
ATOM   2955  CD1 TYR B1142      14.884  42.086  66.772  1.00 82.08           C  
ANISOU 2955  CD1 TYR B1142     8335   8531  14321   2785    844   -205       C  
ATOM   2956  CD2 TYR B1142      16.726  41.934  65.224  1.00 84.17           C  
ANISOU 2956  CD2 TYR B1142     8566   8796  14619   2993   1060   -224       C  
ATOM   2957  CE1 TYR B1142      15.344  40.945  67.429  1.00 82.44           C  
ANISOU 2957  CE1 TYR B1142     8410   8525  14387   2827    759   -233       C  
ATOM   2958  CE2 TYR B1142      17.192  40.790  65.873  1.00 84.09           C  
ANISOU 2958  CE2 TYR B1142     8581   8736  14635   3048    975   -257       C  
ATOM   2959  CZ  TYR B1142      16.505  40.297  66.971  1.00 83.36           C  
ANISOU 2959  CZ  TYR B1142     8526   8612  14535   2962    819   -261       C  
ATOM   2960  OH  TYR B1142      16.985  39.172  67.616  1.00 83.59           O  
ANISOU 2960  OH  TYR B1142     8591   8584  14587   3013    726   -292       O  
ATOM   2961  N   ILE B1143      17.315  46.235  65.846  1.00 83.50           N  
ANISOU 2961  N   ILE B1143     8060   8893  14774   2789   1240    -94       N  
ATOM   2962  CA  ILE B1143      18.599  46.726  66.378  1.00 84.19           C  
ANISOU 2962  CA  ILE B1143     7972   9011  15005   2802   1284    -70       C  
ATOM   2963  C   ILE B1143      18.432  47.819  67.447  1.00 83.02           C  
ANISOU 2963  C   ILE B1143     7723   8883  14937   2693   1218    -39       C  
ATOM   2964  O   ILE B1143      19.161  47.830  68.445  1.00 83.08           O  
ANISOU 2964  O   ILE B1143     7621   8890  15054   2682   1167    -32       O  
ATOM   2965  CB  ILE B1143      19.455  47.304  65.243  1.00 85.94           C  
ANISOU 2965  CB  ILE B1143     8135   9273  15244   2856   1449    -40       C  
ATOM   2966  CG1 ILE B1143      20.131  46.162  64.476  1.00 88.69           C  
ANISOU 2966  CG1 ILE B1143     8532   9608  15558   2993   1522    -72       C  
ATOM   2967  CG2 ILE B1143      20.496  48.277  65.785  1.00 86.21           C  
ANISOU 2967  CG2 ILE B1143     7978   9352  15424   2817   1486      8       C  
ATOM   2968  CD1 ILE B1143      20.007  46.274  62.969  1.00 90.20           C  
ANISOU 2968  CD1 ILE B1143     8822   9810  15641   3047   1655    -68       C  
ATOM   2969  N   PHE B1144      17.482  48.734  67.223  1.00 81.57           N  
ANISOU 2969  N   PHE B1144     7586   8714  14695   2620   1215    -22       N  
ATOM   2970  CA  PHE B1144      17.279  49.881  68.102  1.00 80.43           C  
ANISOU 2970  CA  PHE B1144     7365   8585  14609   2528   1162      5       C  
ATOM   2971  C   PHE B1144      16.429  49.550  69.318  1.00 79.65           C  
ANISOU 2971  C   PHE B1144     7302   8469  14493   2473   1024    -18       C  
ATOM   2972  O   PHE B1144      16.125  50.440  70.130  1.00 78.55           O  
ANISOU 2972  O   PHE B1144     7120   8338  14385   2404    970     -4       O  
ATOM   2973  CB  PHE B1144      16.674  51.063  67.338  1.00 79.64           C  
ANISOU 2973  CB  PHE B1144     7299   8504  14456   2484   1218     33       C  
ATOM   2974  CG  PHE B1144      17.668  52.146  67.006  1.00 79.78           C  
ANISOU 2974  CG  PHE B1144     7209   8546  14557   2468   1307     82       C  
ATOM   2975  CD1 PHE B1144      18.361  52.131  65.808  1.00 80.36           C  
ANISOU 2975  CD1 PHE B1144     7276   8639  14620   2521   1440    102       C  
ATOM   2976  CD2 PHE B1144      17.893  53.188  67.889  1.00 79.46           C  
ANISOU 2976  CD2 PHE B1144     7082   8508  14600   2395   1254    111       C  
ATOM   2977  CE1 PHE B1144      19.268  53.123  65.500  1.00 80.86           C  
ANISOU 2977  CE1 PHE B1144     7235   8731  14758   2493   1523    156       C  
ATOM   2978  CE2 PHE B1144      18.800  54.181  67.589  1.00 80.01           C  
ANISOU 2978  CE2 PHE B1144     7058   8596  14747   2367   1324    164       C  
ATOM   2979  CZ  PHE B1144      19.495  54.143  66.394  1.00 80.73           C  
ANISOU 2979  CZ  PHE B1144     7130   8713  14831   2411   1460    190       C  
ATOM   2980  N   ALA B1145      16.058  48.272  69.432  1.00 79.96           N  
ANISOU 2980  N   ALA B1145     7425   8481  14475   2505    967    -53       N  
ATOM   2981  CA  ALA B1145      15.298  47.781  70.581  1.00 79.96           C  
ANISOU 2981  CA  ALA B1145     7463   8467  14451   2451    838    -72       C  
ATOM   2982  C   ALA B1145      16.204  47.039  71.531  1.00 80.84           C  
ANISOU 2982  C   ALA B1145     7520   8548  14647   2474    775    -85       C  
ATOM   2983  O   ALA B1145      16.061  47.155  72.748  1.00 81.11           O  
ANISOU 2983  O   ALA B1145     7526   8577  14716   2418    683    -84       O  
ATOM   2984  CB  ALA B1145      14.154  46.883  70.143  1.00 79.77           C  
ANISOU 2984  CB  ALA B1145     7580   8430  14300   2447    795    -94       C  
ATOM   2985  N   ILE B1146      17.130  46.272  70.965  1.00 81.95           N  
ANISOU 2985  N   ILE B1146     7653   8669  14817   2564    825    -97       N  
ATOM   2986  CA  ILE B1146      18.070  45.483  71.755  1.00 82.42           C  
ANISOU 2986  CA  ILE B1146     7661   8695  14960   2605    764   -112       C  
ATOM   2987  C   ILE B1146      18.912  46.421  72.615  1.00 82.29           C  
ANISOU 2987  C   ILE B1146     7496   8695  15077   2566    752    -81       C  
ATOM   2988  O   ILE B1146      18.917  46.291  73.846  1.00 81.80           O  
ANISOU 2988  O   ILE B1146     7418   8608  15055   2519    641    -85       O  
ATOM   2989  CB  ILE B1146      18.959  44.585  70.857  1.00 83.54           C  
ANISOU 2989  CB  ILE B1146     7812   8820  15110   2729    837   -132       C  
ATOM   2990  CG1 ILE B1146      18.113  43.477  70.212  1.00 83.20           C  
ANISOU 2990  CG1 ILE B1146     7945   8738  14929   2764    810   -167       C  
ATOM   2991  CG2 ILE B1146      20.135  44.010  71.647  1.00 84.29           C  
ANISOU 2991  CG2 ILE B1146     7817   8890  15321   2782    786   -140       C  
ATOM   2992  CD1 ILE B1146      17.941  42.235  71.073  1.00 83.46           C  
ANISOU 2992  CD1 ILE B1146     8059   8711  14942   2765    671   -197       C  
HETATM 2993  N   MSE B1147      19.581  47.377  71.966  1.00 82.33           N  
ANISOU 2993  N   MSE B1147     7403   8737  15142   2577    859    -47       N  
HETATM 2994  CA  MSE B1147      20.485  48.313  72.652  1.00 82.54           C  
ANISOU 2994  CA  MSE B1147     7285   8775  15301   2536    848     -8       C  
HETATM 2995  C   MSE B1147      19.752  49.056  73.735  1.00 81.30           C  
ANISOU 2995  C   MSE B1147     7148   8608  15136   2435    748     -2       C  
HETATM 2996  O   MSE B1147      20.379  49.621  74.637  1.00 81.02           O  
ANISOU 2996  O   MSE B1147     7024   8561  15199   2393    691     21       O  
HETATM 2997  CB  MSE B1147      21.114  49.326  71.696  1.00 83.30           C  
ANISOU 2997  CB  MSE B1147     7292   8916  15442   2541    979     37       C  
HETATM 2998  CG  MSE B1147      21.724  48.652  70.480  1.00 84.14           C  
ANISOU 2998  CG  MSE B1147     7394   9044  15533   2647   1103     29       C  
HETATM 2999 SE   MSE B1147      22.152  50.006  69.129  1.00 85.43          SE  
ANISOU 2999 SE   MSE B1147     7487   9269  15703   2630   1279     91      SE  
HETATM 3000  CE  MSE B1147      23.565  50.954  70.143  1.00 85.29           C  
ANISOU 3000  CE  MSE B1147     7246   9270  15889   2566   1242    156       C  
ATOM   3001  N   ALA B1148      18.421  49.060  73.658  1.00 80.29           N  
ANISOU 3001  N   ALA B1148     7134   8484  14887   2398    725    -21       N  
ATOM   3002  CA  ALA B1148      17.608  49.628  74.740  1.00 79.69           C  
ANISOU 3002  CA  ALA B1148     7089   8406  14786   2317    631    -22       C  
ATOM   3003  C   ALA B1148      17.471  48.614  75.886  1.00 79.73           C  
ANISOU 3003  C   ALA B1148     7135   8375  14784   2304    512    -49       C  
ATOM   3004  O   ALA B1148      17.429  48.977  77.076  1.00 79.96           O  
ANISOU 3004  O   ALA B1148     7149   8388  14843   2249    424    -46       O  
ATOM   3005  CB  ALA B1148      16.244  50.067  74.232  1.00 78.34           C  
ANISOU 3005  CB  ALA B1148     7006   8264  14495   2286    655    -28       C  
ATOM   3006  N   THR B1149      17.443  47.341  75.524  1.00 79.32           N  
ANISOU 3006  N   THR B1149     7145   8303  14689   2356    504    -75       N  
ATOM   3007  CA  THR B1149      17.115  46.315  76.482  1.00 78.92           C  
ANISOU 3007  CA  THR B1149     7163   8216  14606   2335    389    -99       C  
ATOM   3008  C   THR B1149      18.263  46.042  77.458  1.00 79.41           C  
ANISOU 3008  C   THR B1149     7152   8235  14784   2348    314    -98       C  
ATOM   3009  O   THR B1149      18.027  45.566  78.576  1.00 79.24           O  
ANISOU 3009  O   THR B1149     7177   8181  14749   2305    201   -109       O  
ATOM   3010  CB  THR B1149      16.637  45.019  75.777  1.00 78.98           C  
ANISOU 3010  CB  THR B1149     7284   8205  14518   2379    387   -126       C  
ATOM   3011  OG1 THR B1149      15.627  45.338  74.800  1.00 77.84           O  
ANISOU 3011  OG1 THR B1149     7202   8099  14275   2366    453   -122       O  
ATOM   3012  CG2 THR B1149      16.074  44.015  76.800  1.00 78.29           C  
ANISOU 3012  CG2 THR B1149     7288   8082  14377   2332    257   -143       C  
ATOM   3013  N   GLN B1150      19.494  46.354  77.056  1.00 79.99           N  
ANISOU 3013  N   GLN B1150     7111   8310  14971   2403    372    -80       N  
ATOM   3014  CA  GLN B1150      20.676  45.930  77.859  1.00 80.64           C  
ANISOU 3014  CA  GLN B1150     7116   8350  15173   2431    297    -79       C  
ATOM   3015  C   GLN B1150      21.523  47.106  78.392  1.00 80.47           C  
ANISOU 3015  C   GLN B1150     6962   8336  15279   2390    289    -39       C  
ATOM   3016  O   GLN B1150      22.488  46.902  79.175  1.00 80.78           O  
ANISOU 3016  O   GLN B1150     6928   8338  15427   2398    210    -30       O  
ATOM   3017  CB  GLN B1150      21.548  44.890  77.113  1.00 81.34           C  
ANISOU 3017  CB  GLN B1150     7180   8425  15299   2548    341    -98       C  
ATOM   3018  CG  GLN B1150      22.205  45.430  75.850  1.00 82.16           C  
ANISOU 3018  CG  GLN B1150     7189   8581  15447   2610    494    -75       C  
ATOM   3019  CD  GLN B1150      23.204  44.468  75.259  1.00 83.97           C  
ANISOU 3019  CD  GLN B1150     7376   8802  15727   2738    538    -93       C  
ATOM   3020  OE1 GLN B1150      23.752  43.613  75.967  1.00 84.70           O  
ANISOU 3020  OE1 GLN B1150     7463   8847  15872   2778    441   -114       O  
ATOM   3021  NE2 GLN B1150      23.468  44.606  73.952  1.00 84.62           N  
ANISOU 3021  NE2 GLN B1150     7432   8930  15791   2808    686    -86       N  
ATOM   3022  N   LEU B1151      21.150  48.317  77.960  1.00 79.09           N  
ANISOU 3022  N   LEU B1151     6765   8201  15087   2344    360    -12       N  
ATOM   3023  CA  LEU B1151      21.766  49.545  78.438  1.00 79.01           C  
ANISOU 3023  CA  LEU B1151     6656   8190  15174   2288    342     30       C  
ATOM   3024  C   LEU B1151      20.838  50.141  79.496  1.00 78.32           C  
ANISOU 3024  C   LEU B1151     6651   8082  15024   2204    250     23       C  
ATOM   3025  O   LEU B1151      21.142  50.112  80.697  1.00 78.24           O  
ANISOU 3025  O   LEU B1151     6640   8027  15060   2168    134     23       O  
ATOM   3026  CB  LEU B1151      21.952  50.515  77.265  1.00 79.11           C  
ANISOU 3026  CB  LEU B1151     6606   8251  15199   2291    475     66       C  
ATOM   3027  CG  LEU B1151      23.016  51.619  77.221  1.00 79.56           C  
ANISOU 3027  CG  LEU B1151     6526   8318  15384   2257    499    125       C  
ATOM   3028  CD1 LEU B1151      23.158  52.129  75.789  1.00 79.17           C  
ANISOU 3028  CD1 LEU B1151     6437   8323  15320   2281    653    153       C  
ATOM   3029  CD2 LEU B1151      22.683  52.760  78.175  1.00 79.24           C  
ANISOU 3029  CD2 LEU B1151     6510   8247  15349   2162    408    143       C  
ATOM   3030  N   PHE B1152      19.695  50.658  79.034  1.00 77.50           N  
ANISOU 3030  N   PHE B1152     6623   8014  14810   2180    302     15       N  
ATOM   3031  CA  PHE B1152      18.669  51.226  79.887  1.00 76.46           C  
ANISOU 3031  CA  PHE B1152     6572   7879  14599   2118    237      4       C  
ATOM   3032  C   PHE B1152      18.087  50.212  80.880  1.00 76.82           C  
ANISOU 3032  C   PHE B1152     6706   7903  14581   2102    140    -28       C  
ATOM   3033  O   PHE B1152      18.465  50.211  82.075  1.00 77.22           O  
ANISOU 3033  O   PHE B1152     6758   7909  14674   2068     36    -28       O  
ATOM   3034  CB  PHE B1152      17.565  51.802  79.017  1.00 75.40           C  
ANISOU 3034  CB  PHE B1152     6492   7794  14361   2115    321      1       C  
ATOM   3035  CG  PHE B1152      18.018  52.932  78.139  1.00 75.53           C  
ANISOU 3035  CG  PHE B1152     6445   7827  14426   2116    405     36       C  
ATOM   3036  CD1 PHE B1152      17.581  53.024  76.823  1.00 75.26           C  
ANISOU 3036  CD1 PHE B1152     6431   7831  14333   2146    512     38       C  
ATOM   3037  CD2 PHE B1152      18.886  53.913  78.627  1.00 75.70           C  
ANISOU 3037  CD2 PHE B1152     6393   7819  14549   2078    369     71       C  
ATOM   3038  CE1 PHE B1152      18.001  54.071  76.012  1.00 75.07           C  
ANISOU 3038  CE1 PHE B1152     6358   7820  14346   2139    588     75       C  
ATOM   3039  CE2 PHE B1152      19.317  54.948  77.817  1.00 75.71           C  
ANISOU 3039  CE2 PHE B1152     6340   7833  14592   2066    441    111       C  
ATOM   3040  CZ  PHE B1152      18.871  55.028  76.510  1.00 75.41           C  
ANISOU 3040  CZ  PHE B1152     6325   7836  14490   2096    554    113       C  
ATOM   3041  N   GLY B1153      17.197  49.346  80.372  1.00 76.49           N  
ANISOU 3041  N   GLY B1153     6741   7887  14434   2119    168    -52       N  
ATOM   3042  CA  GLY B1153      16.384  48.412  81.179  1.00 76.14           C  
ANISOU 3042  CA  GLY B1153     6795   7835  14302   2088     86    -76       C  
ATOM   3043  C   GLY B1153      16.912  47.768  82.464  1.00 76.16           C  
ANISOU 3043  C   GLY B1153     6815   7778  14343   2065    -36    -84       C  
ATOM   3044  O   GLY B1153      16.124  47.371  83.321  1.00 75.67           O  
ANISOU 3044  O   GLY B1153     6837   7715  14197   2015   -104    -95       O  
ATOM   3045  N   GLU B1154      18.231  47.651  82.603  1.00 76.52           N  
ANISOU 3045  N   GLU B1154     6783   7778  14515   2098    -66    -74       N  
ATOM   3046  CA  GLU B1154      18.830  47.055  83.807  1.00 76.84           C  
ANISOU 3046  CA  GLU B1154     6840   7753  14603   2081   -194    -80       C  
ATOM   3047  C   GLU B1154      18.511  47.876  85.063  1.00 76.76           C  
ANISOU 3047  C   GLU B1154     6865   7726  14574   2008   -272    -73       C  
ATOM   3048  O   GLU B1154      18.544  47.356  86.189  1.00 76.00           O  
ANISOU 3048  O   GLU B1154     6832   7583  14464   1973   -383    -81       O  
ATOM   3049  CB  GLU B1154      20.342  46.895  83.618  1.00 77.18           C  
ANISOU 3049  CB  GLU B1154     6769   7757  14798   2138   -206    -66       C  
ATOM   3050  CG  GLU B1154      20.955  45.677  84.291  1.00 77.42           C  
ANISOU 3050  CG  GLU B1154     6827   7721  14866   2164   -318    -83       C  
ATOM   3051  CD  GLU B1154      20.261  44.348  83.982  1.00 77.09           C  
ANISOU 3051  CD  GLU B1154     6900   7674  14718   2188   -327   -115       C  
ATOM   3052  OE1 GLU B1154      20.285  43.450  84.869  1.00 76.91           O  
ANISOU 3052  OE1 GLU B1154     6956   7593  14675   2170   -447   -129       O  
ATOM   3053  OE2 GLU B1154      19.706  44.185  82.865  1.00 76.83           O  
ANISOU 3053  OE2 GLU B1154     6887   7687  14618   2221   -226   -122       O  
ATOM   3054  N   ARG B1155      18.184  49.152  84.833  1.00 77.24           N  
ANISOU 3054  N   ARG B1155     6899   7823  14627   1988   -213    -58       N  
ATOM   3055  CA  ARG B1155      17.758  50.091  85.880  1.00 77.98           C  
ANISOU 3055  CA  ARG B1155     7039   7906  14684   1933   -270    -56       C  
ATOM   3056  C   ARG B1155      16.489  50.829  85.462  1.00 77.16           C  
ANISOU 3056  C   ARG B1155     6977   7871  14468   1923   -190    -63       C  
ATOM   3057  O   ARG B1155      16.121  51.853  86.052  1.00 76.59           O  
ANISOU 3057  O   ARG B1155     6934   7800  14366   1897   -209    -62       O  
ATOM   3058  CB  ARG B1155      18.878  51.094  86.244  1.00 79.21           C  
ANISOU 3058  CB  ARG B1155     7118   8011  14965   1921   -316    -27       C  
ATOM   3059  CG  ARG B1155      19.531  50.836  87.598  1.00 80.11           C  
ANISOU 3059  CG  ARG B1155     7262   8046  15130   1888   -459    -26       C  
ATOM   3060  CD  ARG B1155      19.915  52.152  88.257  1.00 81.25           C  
ANISOU 3060  CD  ARG B1155     7401   8148  15321   1848   -517     -4       C  
ATOM   3061  NE  ARG B1155      21.169  52.679  87.713  1.00 82.80           N  
ANISOU 3061  NE  ARG B1155     7466   8323  15671   1857   -509     36       N  
ATOM   3062  CZ  ARG B1155      21.632  53.917  87.877  1.00 82.97           C  
ANISOU 3062  CZ  ARG B1155     7457   8315  15753   1822   -539     69       C  
ATOM   3063  NH1 ARG B1155      20.941  54.824  88.569  1.00 82.65           N  
ANISOU 3063  NH1 ARG B1155     7518   8254  15629   1788   -579     58       N  
ATOM   3064  NH2 ARG B1155      22.799  54.246  87.332  1.00 83.38           N  
ANISOU 3064  NH2 ARG B1155     7375   8356  15948   1823   -528    113       N  
ATOM   3065  N   PHE B1156      15.847  50.294  84.422  1.00 77.00           N  
ANISOU 3065  N   PHE B1156     6963   7904  14388   1950   -106    -71       N  
ATOM   3066  CA  PHE B1156      14.511  50.721  83.974  1.00 76.55           C  
ANISOU 3066  CA  PHE B1156     6949   7919  14217   1943    -38    -79       C  
ATOM   3067  C   PHE B1156      13.729  49.472  83.557  1.00 76.51           C  
ANISOU 3067  C   PHE B1156     6997   7948  14124   1942    -23    -91       C  
ATOM   3068  O   PHE B1156      13.795  49.050  82.402  1.00 76.72           O  
ANISOU 3068  O   PHE B1156     7006   7989  14156   1979     41    -90       O  
ATOM   3069  CB  PHE B1156      14.612  51.716  82.814  1.00 76.20           C  
ANISOU 3069  CB  PHE B1156     6848   7901  14204   1974     58    -64       C  
ATOM   3070  CG  PHE B1156      14.846  53.134  83.247  1.00 76.23           C  
ANISOU 3070  CG  PHE B1156     6834   7885  14244   1959     42    -52       C  
ATOM   3071  CD1 PHE B1156      16.136  53.603  83.485  1.00 76.62           C  
ANISOU 3071  CD1 PHE B1156     6820   7876  14418   1953      3    -28       C  
ATOM   3072  CD2 PHE B1156      13.772  54.008  83.415  1.00 75.89           C  
ANISOU 3072  CD2 PHE B1156     6840   7881  14111   1953     59    -63       C  
ATOM   3073  CE1 PHE B1156      16.347  54.911  83.885  1.00 76.91           C  
ANISOU 3073  CE1 PHE B1156     6856   7883  14484   1931    -27    -13       C  
ATOM   3074  CE2 PHE B1156      13.979  55.322  83.802  1.00 75.84           C  
ANISOU 3074  CE2 PHE B1156     6838   7847  14132   1946     34    -54       C  
ATOM   3075  CZ  PHE B1156      15.268  55.774  84.035  1.00 76.44           C  
ANISOU 3075  CZ  PHE B1156     6863   7854  14326   1930    -13    -29       C  
ATOM   3076  N   PRO B1157      13.006  48.863  84.502  1.00 76.48           N  
ANISOU 3076  N   PRO B1157     7067   7955  14036   1895    -87   -100       N  
ATOM   3077  CA  PRO B1157      12.393  47.571  84.283  1.00 76.60           C  
ANISOU 3077  CA  PRO B1157     7141   7986  13976   1877   -101   -104       C  
ATOM   3078  C   PRO B1157      11.244  47.627  83.272  1.00 76.41           C  
ANISOU 3078  C   PRO B1157     7127   8038  13865   1879    -22   -101       C  
ATOM   3079  O   PRO B1157      11.391  47.143  82.137  1.00 76.12           O  
ANISOU 3079  O   PRO B1157     7087   7997  13839   1915     23   -101       O  
ATOM   3080  CB  PRO B1157      11.866  47.197  85.678  1.00 77.32           C  
ANISOU 3080  CB  PRO B1157     7304   8079  13996   1811   -186   -106       C  
ATOM   3081  CG  PRO B1157      12.589  48.094  86.643  1.00 77.44           C  
ANISOU 3081  CG  PRO B1157     7300   8049  14076   1810   -232   -107       C  
ATOM   3082  CD  PRO B1157      12.738  49.360  85.861  1.00 77.57           C  
ANISOU 3082  CD  PRO B1157     7245   8087  14140   1853   -151   -104       C  
ATOM   3083  N   GLU B1158      10.119  48.222  83.674  1.00 76.13           N  
ANISOU 3083  N   GLU B1158     7107   8071  13746   1846     -6    -98       N  
ATOM   3084  CA  GLU B1158       8.891  48.178  82.860  1.00 75.91           C  
ANISOU 3084  CA  GLU B1158     7090   8122  13631   1838     51    -92       C  
ATOM   3085  C   GLU B1158       9.088  48.637  81.404  1.00 76.64           C  
ANISOU 3085  C   GLU B1158     7144   8215  13759   1895    132    -90       C  
ATOM   3086  O   GLU B1158       8.454  48.078  80.483  1.00 76.51           O  
ANISOU 3086  O   GLU B1158     7154   8228  13690   1894    159    -85       O  
ATOM   3087  CB  GLU B1158       7.733  48.920  83.547  1.00 74.70           C  
ANISOU 3087  CB  GLU B1158     6937   8049  13394   1810     63    -90       C  
ATOM   3088  CG  GLU B1158       7.085  48.089  84.650  1.00 74.56           C  
ANISOU 3088  CG  GLU B1158     6972   8062  13294   1739      2    -81       C  
ATOM   3089  CD  GLU B1158       6.010  48.811  85.474  1.00 74.52           C  
ANISOU 3089  CD  GLU B1158     6964   8145  13205   1720     21    -80       C  
ATOM   3090  OE1 GLU B1158       5.183  49.592  84.922  1.00 73.91           O  
ANISOU 3090  OE1 GLU B1158     6847   8140  13094   1750     85    -81       O  
ATOM   3091  OE2 GLU B1158       5.968  48.558  86.704  1.00 74.48           O  
ANISOU 3091  OE2 GLU B1158     7000   8137  13161   1677    -29    -80       O  
ATOM   3092  N   TRP B1159       9.986  49.618  81.204  1.00 77.36           N  
ANISOU 3092  N   TRP B1159     7182   8272  13938   1937    165    -92       N  
ATOM   3093  CA  TRP B1159      10.122  50.314  79.905  1.00 77.59           C  
ANISOU 3093  CA  TRP B1159     7177   8309  13994   1983    249    -87       C  
ATOM   3094  C   TRP B1159      11.092  49.663  78.964  1.00 77.85           C  
ANISOU 3094  C   TRP B1159     7197   8296  14088   2024    281    -84       C  
ATOM   3095  O   TRP B1159      10.870  49.700  77.752  1.00 78.73           O  
ANISOU 3095  O   TRP B1159     7315   8422  14175   2053    347    -80       O  
ATOM   3096  CB  TRP B1159      10.478  51.807  80.057  1.00 77.58           C  
ANISOU 3096  CB  TRP B1159     7132   8300  14044   2000    272    -83       C  
ATOM   3097  CG  TRP B1159       9.500  52.648  80.848  1.00 77.23           C  
ANISOU 3097  CG  TRP B1159     7106   8302  13934   1983    254    -91       C  
ATOM   3098  CD1 TRP B1159       8.155  52.405  81.067  1.00 77.09           C  
ANISOU 3098  CD1 TRP B1159     7121   8359  13813   1963    252    -96       C  
ATOM   3099  CD2 TRP B1159       9.767  53.930  81.516  1.00 77.47           C  
ANISOU 3099  CD2 TRP B1159     7128   8312  13995   1991    235    -94       C  
ATOM   3100  NE1 TRP B1159       7.587  53.411  81.821  1.00 77.19           N  
ANISOU 3100  NE1 TRP B1159     7138   8403  13789   1970    243   -106       N  
ATOM   3101  CE2 TRP B1159       8.501  54.355  82.118  1.00 77.19           C  
ANISOU 3101  CE2 TRP B1159     7125   8341  13861   1988    229   -108       C  
ATOM   3102  CE3 TRP B1159      10.895  54.739  81.676  1.00 77.90           C  
ANISOU 3102  CE3 TRP B1159     7152   8301  14145   1997    219    -83       C  
ATOM   3103  CZ2 TRP B1159       8.391  55.531  82.856  1.00 77.06           C  
ANISOU 3103  CZ2 TRP B1159     7126   8318  13836   2005    207   -119       C  
ATOM   3104  CZ3 TRP B1159      10.770  55.929  82.419  1.00 77.64           C  
ANISOU 3104  CZ3 TRP B1159     7142   8253  14104   2000    186    -90       C  
ATOM   3105  CH2 TRP B1159       9.545  56.309  82.997  1.00 77.23           C  
ANISOU 3105  CH2 TRP B1159     7136   8258  13949   2009    180   -111       C  
ATOM   3106  N   PHE B1160      12.182  49.092  79.476  1.00 77.50           N  
ANISOU 3106  N   PHE B1160     7133   8195  14119   2033    236    -87       N  
ATOM   3107  CA  PHE B1160      13.134  48.425  78.579  1.00 78.10           C  
ANISOU 3107  CA  PHE B1160     7191   8233  14252   2088    273    -88       C  
ATOM   3108  C   PHE B1160      13.791  47.151  79.149  1.00 79.26           C  
ANISOU 3108  C   PHE B1160     7362   8326  14428   2097    197   -100       C  
ATOM   3109  O   PHE B1160      14.916  46.813  78.744  1.00 80.21           O  
ANISOU 3109  O   PHE B1160     7437   8408  14631   2154    217   -101       O  
ATOM   3110  CB  PHE B1160      14.256  49.364  78.156  1.00 77.98           C  
ANISOU 3110  CB  PHE B1160     7084   8200  14343   2123    332    -71       C  
ATOM   3111  CG  PHE B1160      13.812  50.692  77.615  1.00 77.59           C  
ANISOU 3111  CG  PHE B1160     7015   8187  14278   2116    396    -57       C  
ATOM   3112  CD1 PHE B1160      13.757  51.809  78.439  1.00 77.44           C  
ANISOU 3112  CD1 PHE B1160     6973   8167  14282   2082    362    -49       C  
ATOM   3113  CD2 PHE B1160      13.538  50.845  76.262  1.00 77.94           C  
ANISOU 3113  CD2 PHE B1160     7074   8255  14285   2148    486    -51       C  
ATOM   3114  CE1 PHE B1160      13.393  53.043  77.930  1.00 77.90           C  
ANISOU 3114  CE1 PHE B1160     7025   8248  14325   2080    412    -36       C  
ATOM   3115  CE2 PHE B1160      13.175  52.076  75.734  1.00 77.72           C  
ANISOU 3115  CE2 PHE B1160     7036   8252  14243   2142    538    -36       C  
ATOM   3116  CZ  PHE B1160      13.099  53.179  76.571  1.00 78.04           C  
ANISOU 3116  CZ  PHE B1160     7054   8290  14307   2109    499    -29       C  
ATOM   3117  N   GLY B1161      13.125  46.450  80.074  1.00 78.90           N  
ANISOU 3117  N   GLY B1161     7383   8278  14316   2043    111   -107       N  
ATOM   3118  CA  GLY B1161      13.673  45.207  80.622  1.00 79.24           C  
ANISOU 3118  CA  GLY B1161     7470   8262  14377   2047     25   -118       C  
ATOM   3119  C   GLY B1161      13.842  44.129  79.555  1.00 80.67           C  
ANISOU 3119  C   GLY B1161     7699   8416  14535   2104     47   -130       C  
ATOM   3120  O   GLY B1161      14.957  43.614  79.333  1.00 80.85           O  
ANISOU 3120  O   GLY B1161     7696   8387  14634   2172     43   -141       O  
ATOM   3121  N   THR B1162      12.726  43.815  78.876  1.00 80.53           N  
ANISOU 3121  N   THR B1162     7753   8434  14410   2080     70   -128       N  
ATOM   3122  CA  THR B1162      12.620  42.720  77.888  1.00 79.96           C  
ANISOU 3122  CA  THR B1162     7764   8332  14284   2121     73   -139       C  
ATOM   3123  C   THR B1162      12.765  43.266  76.460  1.00 80.00           C  
ANISOU 3123  C   THR B1162     7743   8359  14296   2188    192   -139       C  
ATOM   3124  O   THR B1162      12.732  44.476  76.242  1.00 79.94           O  
ANISOU 3124  O   THR B1162     7659   8395  14319   2186    264   -126       O  
ATOM   3125  CB  THR B1162      11.248  42.031  78.044  1.00 79.65           C  
ANISOU 3125  CB  THR B1162     7827   8316  14119   2039     10   -128       C  
ATOM   3126  OG1 THR B1162      11.049  41.670  79.418  1.00 79.26           O  
ANISOU 3126  OG1 THR B1162     7801   8258  14055   1965    -88   -121       O  
ATOM   3127  CG2 THR B1162      11.120  40.787  77.157  1.00 80.27           C  
ANISOU 3127  CG2 THR B1162     8020   8345  14134   2070    -17   -138       C  
ATOM   3128  N   LEU B1163      12.932  42.383  75.484  1.00 80.47           N  
ANISOU 3128  N   LEU B1163     7875   8381  14318   2249    208   -153       N  
ATOM   3129  CA  LEU B1163      13.019  42.820  74.095  1.00 80.55           C  
ANISOU 3129  CA  LEU B1163     7881   8408  14316   2311    321   -153       C  
ATOM   3130  C   LEU B1163      11.642  43.173  73.523  1.00 80.42           C  
ANISOU 3130  C   LEU B1163     7920   8439  14197   2253    335   -137       C  
ATOM   3131  O   LEU B1163      11.535  44.024  72.640  1.00 80.60           O  
ANISOU 3131  O   LEU B1163     7916   8493  14217   2276    426   -129       O  
ATOM   3132  CB  LEU B1163      13.733  41.776  73.227  1.00 81.05           C  
ANISOU 3132  CB  LEU B1163     8012   8412  14370   2410    339   -178       C  
ATOM   3133  CG  LEU B1163      14.342  42.251  71.886  1.00 82.00           C  
ANISOU 3133  CG  LEU B1163     8103   8545  14509   2501    476   -180       C  
ATOM   3134  CD1 LEU B1163      13.472  41.894  70.689  1.00 82.43           C  
ANISOU 3134  CD1 LEU B1163     8286   8592  14442   2511    501   -183       C  
ATOM   3135  CD2 LEU B1163      14.713  43.738  71.846  1.00 81.31           C  
ANISOU 3135  CD2 LEU B1163     7880   8513  14499   2487    567   -154       C  
ATOM   3136  N   GLY B1164      10.595  42.511  74.019  1.00 80.35           N  
ANISOU 3136  N   GLY B1164     7988   8436  14105   2176    243   -130       N  
ATOM   3137  CA  GLY B1164       9.228  42.790  73.576  1.00 80.01           C  
ANISOU 3137  CA  GLY B1164     7984   8445  13970   2115    243   -110       C  
ATOM   3138  C   GLY B1164       8.812  44.137  74.122  1.00 78.50           C  
ANISOU 3138  C   GLY B1164     7692   8326  13809   2075    279    -95       C  
ATOM   3139  O   GLY B1164       8.206  44.967  73.428  1.00 77.71           O  
ANISOU 3139  O   GLY B1164     7575   8269  13682   2076    335    -85       O  
ATOM   3140  N   GLU B1165       9.178  44.346  75.379  1.00 78.06           N  
ANISOU 3140  N   GLU B1165     7578   8274  13807   2047    239    -97       N  
ATOM   3141  CA  GLU B1165       8.912  45.585  76.085  1.00 77.55           C  
ANISOU 3141  CA  GLU B1165     7429   8264  13770   2018    260    -88       C  
ATOM   3142  C   GLU B1165       9.614  46.813  75.471  1.00 77.77           C  
ANISOU 3142  C   GLU B1165     7384   8295  13872   2075    354    -88       C  
ATOM   3143  O   GLU B1165       9.062  47.916  75.544  1.00 77.97           O  
ANISOU 3143  O   GLU B1165     7370   8367  13888   2059    383    -80       O  
ATOM   3144  CB  GLU B1165       9.211  45.413  77.580  1.00 76.81           C  
ANISOU 3144  CB  GLU B1165     7314   8160  13709   1976    187    -90       C  
ATOM   3145  CG  GLU B1165       8.224  44.468  78.249  1.00 76.30           C  
ANISOU 3145  CG  GLU B1165     7319   8116  13554   1896    102    -79       C  
ATOM   3146  CD  GLU B1165       8.464  44.255  79.736  1.00 76.40           C  
ANISOU 3146  CD  GLU B1165     7328   8116  13582   1848     27    -79       C  
ATOM   3147  OE1 GLU B1165       7.757  43.417  80.326  1.00 76.51           O  
ANISOU 3147  OE1 GLU B1165     7403   8144  13523   1776    -44    -66       O  
ATOM   3148  OE2 GLU B1165       9.342  44.906  80.334  1.00 76.73           O  
ANISOU 3148  OE2 GLU B1165     7315   8134  13707   1876     32    -90       O  
ATOM   3149  N   SER B1166      10.783  46.636  74.840  1.00 77.93           N  
ANISOU 3149  N   SER B1166     7387   8266  13956   2142    401    -96       N  
ATOM   3150  CA  SER B1166      11.407  47.747  74.090  1.00 78.63           C  
ANISOU 3150  CA  SER B1166     7412   8361  14103   2186    497    -87       C  
ATOM   3151  C   SER B1166      10.647  48.110  72.793  1.00 79.40           C  
ANISOU 3151  C   SER B1166     7557   8484  14127   2199    562    -79       C  
ATOM   3152  O   SER B1166      10.322  49.291  72.542  1.00 78.86           O  
ANISOU 3152  O   SER B1166     7455   8446  14060   2190    604    -67       O  
ATOM   3153  CB  SER B1166      12.866  47.463  73.768  1.00 79.11           C  
ANISOU 3153  CB  SER B1166     7427   8378  14255   2252    540    -90       C  
ATOM   3154  OG  SER B1166      13.658  47.641  74.919  1.00 79.97           O  
ANISOU 3154  OG  SER B1166     7462   8467  14454   2237    490    -88       O  
ATOM   3155  N   PHE B1167      10.370  47.097  71.969  1.00 79.70           N  
ANISOU 3155  N   PHE B1167     7683   8500  14098   2222    561    -88       N  
ATOM   3156  CA  PHE B1167       9.482  47.283  70.835  1.00 79.55           C  
ANISOU 3156  CA  PHE B1167     7731   8499  13995   2223    595    -80       C  
ATOM   3157  C   PHE B1167       8.211  47.974  71.331  1.00 78.91           C  
ANISOU 3157  C   PHE B1167     7634   8478  13869   2158    554    -68       C  
ATOM   3158  O   PHE B1167       7.762  48.970  70.747  1.00 79.42           O  
ANISOU 3158  O   PHE B1167     7688   8571  13919   2162    599    -58       O  
ATOM   3159  CB  PHE B1167       9.152  45.947  70.166  1.00 80.15           C  
ANISOU 3159  CB  PHE B1167     7925   8536  13990   2238    560    -90       C  
ATOM   3160  CG  PHE B1167      10.193  45.479  69.178  1.00 80.88           C  
ANISOU 3160  CG  PHE B1167     8057   8578  14097   2327    631   -105       C  
ATOM   3161  CD1 PHE B1167      11.253  44.660  69.584  1.00 81.01           C  
ANISOU 3161  CD1 PHE B1167     8061   8550  14168   2377    618   -123       C  
ATOM   3162  CD2 PHE B1167      10.106  45.842  67.834  1.00 80.93           C  
ANISOU 3162  CD2 PHE B1167     8115   8579  14056   2368    712   -100       C  
ATOM   3163  CE1 PHE B1167      12.202  44.230  68.670  1.00 81.31           C  
ANISOU 3163  CE1 PHE B1167     8128   8551  14216   2473    693   -138       C  
ATOM   3164  CE2 PHE B1167      11.058  45.406  66.919  1.00 81.05           C  
ANISOU 3164  CE2 PHE B1167     8169   8554  14074   2458    790   -113       C  
ATOM   3165  CZ  PHE B1167      12.102  44.604  67.341  1.00 81.31           C  
ANISOU 3165  CZ  PHE B1167     8178   8553  14162   2514    784   -133       C  
ATOM   3166  N   TYR B1168       7.649  47.484  72.431  1.00 78.13           N  
ANISOU 3166  N   TYR B1168     7533   8402  13752   2102    472    -68       N  
ATOM   3167  CA  TYR B1168       6.470  48.144  72.989  1.00 77.88           C  
ANISOU 3167  CA  TYR B1168     7472   8441  13680   2049    442    -57       C  
ATOM   3168  C   TYR B1168       6.713  49.655  73.133  1.00 78.37           C  
ANISOU 3168  C   TYR B1168     7460   8523  13794   2072    495    -56       C  
ATOM   3169  O   TYR B1168       5.866  50.477  72.726  1.00 78.51           O  
ANISOU 3169  O   TYR B1168     7473   8583  13774   2072    513    -49       O  
ATOM   3170  CB  TYR B1168       6.024  47.519  74.316  1.00 76.24           C  
ANISOU 3170  CB  TYR B1168     7257   8259  13451   1986    360    -54       C  
ATOM   3171  CG  TYR B1168       4.719  48.080  74.806  1.00 75.50           C  
ANISOU 3171  CG  TYR B1168     7132   8251  13303   1939    340    -41       C  
ATOM   3172  CD1 TYR B1168       3.711  48.448  73.905  1.00 75.27           C  
ANISOU 3172  CD1 TYR B1168     7115   8265  13219   1939    358    -28       C  
ATOM   3173  CD2 TYR B1168       4.475  48.255  76.183  1.00 75.53           C  
ANISOU 3173  CD2 TYR B1168     7095   8296  13309   1899    303    -41       C  
ATOM   3174  CE1 TYR B1168       2.494  48.970  74.358  1.00 75.22           C  
ANISOU 3174  CE1 TYR B1168     7066   8348  13167   1906    341    -15       C  
ATOM   3175  CE2 TYR B1168       3.257  48.774  76.646  1.00 74.92           C  
ANISOU 3175  CE2 TYR B1168     6982   8309  13176   1868    295    -29       C  
ATOM   3176  CZ  TYR B1168       2.277  49.125  75.726  1.00 74.86           C  
ANISOU 3176  CZ  TYR B1168     6972   8349  13121   1875    316    -17       C  
ATOM   3177  OH  TYR B1168       1.091  49.645  76.132  1.00 74.71           O  
ANISOU 3177  OH  TYR B1168     6906   8426  13055   1856    312     -6       O  
ATOM   3178  N   THR B1169       7.885  49.997  73.676  1.00 78.07           N  
ANISOU 3178  N   THR B1169     7371   8450  13844   2093    511    -62       N  
ATOM   3179  CA  THR B1169       8.232  51.373  74.018  1.00 77.82           C  
ANISOU 3179  CA  THR B1169     7277   8424  13868   2103    539    -59       C  
ATOM   3180  C   THR B1169       8.649  52.208  72.779  1.00 78.68           C  
ANISOU 3180  C   THR B1169     7384   8514  13996   2143    621    -48       C  
ATOM   3181  O   THR B1169       8.403  53.431  72.709  1.00 78.36           O  
ANISOU 3181  O   THR B1169     7325   8488  13960   2145    639    -41       O  
ATOM   3182  CB  THR B1169       9.351  51.365  75.068  1.00 77.42           C  
ANISOU 3182  CB  THR B1169     7175   8335  13905   2099    510    -63       C  
ATOM   3183  OG1 THR B1169       8.959  50.519  76.146  1.00 77.25           O  
ANISOU 3183  OG1 THR B1169     7173   8325  13854   2059    433    -72       O  
ATOM   3184  CG2 THR B1169       9.616  52.757  75.608  1.00 77.75           C  
ANISOU 3184  CG2 THR B1169     7169   8377  13996   2097    514    -57       C  
ATOM   3185  N   LEU B1170       9.277  51.550  71.803  1.00 78.73           N  
ANISOU 3185  N   LEU B1170     7418   8487  14007   2176    669    -45       N  
ATOM   3186  CA  LEU B1170       9.772  52.269  70.622  1.00 78.87           C  
ANISOU 3186  CA  LEU B1170     7438   8488  14040   2211    757    -30       C  
ATOM   3187  C   LEU B1170       8.676  52.577  69.601  1.00 78.54           C  
ANISOU 3187  C   LEU B1170     7467   8467  13908   2213    773    -26       C  
ATOM   3188  O   LEU B1170       8.801  53.507  68.804  1.00 78.09           O  
ANISOU 3188  O   LEU B1170     7416   8402  13851   2227    830    -12       O  
ATOM   3189  CB  LEU B1170      10.966  51.558  69.988  1.00 78.80           C  
ANISOU 3189  CB  LEU B1170     7426   8443  14074   2257    817    -29       C  
ATOM   3190  CG  LEU B1170      12.211  51.669  70.868  1.00 78.68           C  
ANISOU 3190  CG  LEU B1170     7315   8408  14170   2258    811    -23       C  
ATOM   3191  CD1 LEU B1170      13.005  50.386  70.747  1.00 79.29           C  
ANISOU 3191  CD1 LEU B1170     7398   8456  14271   2304    817    -37       C  
ATOM   3192  CD2 LEU B1170      13.062  52.889  70.526  1.00 78.40           C  
ANISOU 3192  CD2 LEU B1170     7211   8369  14207   2259    878      6       C  
ATOM   3193  N   PHE B1171       7.601  51.795  69.652  1.00 78.34           N  
ANISOU 3193  N   PHE B1171     7495   8466  13807   2192    716    -35       N  
ATOM   3194  CA  PHE B1171       6.415  52.066  68.846  1.00 78.55           C  
ANISOU 3194  CA  PHE B1171     7578   8516  13751   2186    708    -28       C  
ATOM   3195  C   PHE B1171       5.653  53.238  69.466  1.00 78.24           C  
ANISOU 3195  C   PHE B1171     7491   8524  13712   2169    681    -27       C  
ATOM   3196  O   PHE B1171       5.045  54.057  68.761  1.00 77.81           O  
ANISOU 3196  O   PHE B1171     7461   8480  13624   2182    695    -20       O  
ATOM   3197  CB  PHE B1171       5.528  50.827  68.807  1.00 78.39           C  
ANISOU 3197  CB  PHE B1171     7618   8509  13657   2157    643    -31       C  
ATOM   3198  CG  PHE B1171       4.311  50.981  67.959  1.00 78.17           C  
ANISOU 3198  CG  PHE B1171     7647   8505  13549   2146    622    -20       C  
ATOM   3199  CD1 PHE B1171       4.368  50.741  66.586  1.00 79.20           C  
ANISOU 3199  CD1 PHE B1171     7870   8592  13631   2174    656    -15       C  
ATOM   3200  CD2 PHE B1171       3.105  51.342  68.524  1.00 77.59           C  
ANISOU 3200  CD2 PHE B1171     7536   8499  13446   2110    565    -13       C  
ATOM   3201  CE1 PHE B1171       3.231  50.874  65.790  1.00 79.34           C  
ANISOU 3201  CE1 PHE B1171     7947   8625  13575   2161    622     -2       C  
ATOM   3202  CE2 PHE B1171       1.966  51.472  67.738  1.00 78.19           C  
ANISOU 3202  CE2 PHE B1171     7653   8600  13455   2100    536      1       C  
ATOM   3203  CZ  PHE B1171       2.029  51.236  66.372  1.00 78.79           C  
ANISOU 3203  CZ  PHE B1171     7827   8624  13487   2122    558      7       C  
ATOM   3204  N   GLN B1172       5.714  53.298  70.798  1.00 77.62           N  
ANISOU 3204  N   GLN B1172     7353   8469  13670   2147    639    -35       N  
ATOM   3205  CA  GLN B1172       5.088  54.339  71.585  1.00 76.77           C  
ANISOU 3205  CA  GLN B1172     7204   8403  13562   2143    612    -40       C  
ATOM   3206  C   GLN B1172       5.821  55.653  71.319  1.00 76.92           C  
ANISOU 3206  C   GLN B1172     7207   8384  13634   2170    655    -35       C  
ATOM   3207  O   GLN B1172       5.181  56.706  71.173  1.00 77.38           O  
ANISOU 3207  O   GLN B1172     7272   8460  13668   2186    649    -36       O  
ATOM   3208  CB  GLN B1172       5.123  53.944  73.065  1.00 76.40           C  
ANISOU 3208  CB  GLN B1172     7115   8380  13534   2113    561    -51       C  
ATOM   3209  CG  GLN B1172       4.552  54.957  74.045  1.00 76.54           C  
ANISOU 3209  CG  GLN B1172     7098   8439  13546   2118    534    -61       C  
ATOM   3210  CD  GLN B1172       4.544  54.429  75.472  1.00 76.85           C  
ANISOU 3210  CD  GLN B1172     7112   8501  13586   2086    486    -70       C  
ATOM   3211  OE1 GLN B1172       4.214  53.264  75.705  1.00 77.29           O  
ANISOU 3211  OE1 GLN B1172     7179   8579  13608   2048    456    -65       O  
ATOM   3212  NE2 GLN B1172       4.905  55.279  76.433  1.00 76.43           N  
ANISOU 3212  NE2 GLN B1172     7037   8436  13567   2097    470    -81       N  
ATOM   3213  N   VAL B1173       7.153  55.595  71.231  1.00 76.53           N  
ANISOU 3213  N   VAL B1173     7138   8284  13657   2173    693    -26       N  
ATOM   3214  CA  VAL B1173       7.935  56.788  70.878  1.00 76.62           C  
ANISOU 3214  CA  VAL B1173     7134   8258  13721   2184    735     -9       C  
ATOM   3215  C   VAL B1173       7.738  57.076  69.389  1.00 77.45           C  
ANISOU 3215  C   VAL B1173     7297   8350  13781   2203    792      6       C  
ATOM   3216  O   VAL B1173       7.926  58.214  68.942  1.00 78.29           O  
ANISOU 3216  O   VAL B1173     7415   8434  13899   2206    816     22       O  
ATOM   3217  CB  VAL B1173       9.447  56.640  71.204  1.00 76.60           C  
ANISOU 3217  CB  VAL B1173     7075   8214  13817   2176    760      4       C  
ATOM   3218  CG1 VAL B1173      10.243  57.857  70.749  1.00 76.44           C  
ANISOU 3218  CG1 VAL B1173     7036   8158  13848   2171    802     33       C  
ATOM   3219  CG2 VAL B1173       9.674  56.379  72.690  1.00 75.94           C  
ANISOU 3219  CG2 VAL B1173     6946   8132  13776   2155    692     -9       C  
HETATM 3220  N   MSE B1174       7.353  56.049  68.625  1.00 77.36           N  
ANISOU 3220  N   MSE B1174     7334   8345  13713   2212    807      2       N  
HETATM 3221  CA  MSE B1174       7.121  56.218  67.190  1.00 77.61           C  
ANISOU 3221  CA  MSE B1174     7440   8360  13690   2231    856     14       C  
HETATM 3222  C   MSE B1174       5.810  56.947  67.008  1.00 77.35           C  
ANISOU 3222  C   MSE B1174     7441   8354  13594   2232    810     11       C  
HETATM 3223  O   MSE B1174       5.744  57.920  66.234  1.00 78.28           O  
ANISOU 3223  O   MSE B1174     7598   8450  13696   2243    835     24       O  
HETATM 3224  CB  MSE B1174       7.204  54.921  66.379  1.00 78.05           C  
ANISOU 3224  CB  MSE B1174     7555   8400  13699   2246    883     11       C  
HETATM 3225  CG  MSE B1174       7.017  55.193  64.886  1.00 78.97           C  
ANISOU 3225  CG  MSE B1174     7763   8490  13752   2267    935     25       C  
HETATM 3226 SE   MSE B1174       7.548  53.617  63.831  1.00 81.00          SE  
ANISOU 3226 SE   MSE B1174     8110   8708  13957   2304    988     18      SE  
HETATM 3227  CE  MSE B1174       5.823  52.649  63.788  1.00 79.94           C  
ANISOU 3227  CE  MSE B1174     8060   8594  13720   2277    870      5       C  
ATOM   3228  N   THR B1175       4.760  56.518  67.715  1.00 76.00           N  
ANISOU 3228  N   THR B1175     7253   8233  13389   2220    741     -5       N  
ATOM   3229  CA  THR B1175       3.507  57.286  67.677  1.00 75.64           C  
ANISOU 3229  CA  THR B1175     7218   8227  13296   2231    696     -9       C  
ATOM   3230  C   THR B1175       3.742  58.661  68.309  1.00 75.57           C  
ANISOU 3230  C   THR B1175     7175   8210  13329   2247    690    -14       C  
ATOM   3231  O   THR B1175       2.939  59.571  68.129  1.00 76.14           O  
ANISOU 3231  O   THR B1175     7265   8296  13368   2273    662    -18       O  
ATOM   3232  CB  THR B1175       2.334  56.628  68.444  1.00 74.95           C  
ANISOU 3232  CB  THR B1175     7096   8213  13169   2213    629    -19       C  
ATOM   3233  OG1 THR B1175       2.684  56.496  69.826  1.00 74.76           O  
ANISOU 3233  OG1 THR B1175     7007   8211  13187   2198    611    -31       O  
ATOM   3234  CG2 THR B1175       1.946  55.280  67.859  1.00 74.53           C  
ANISOU 3234  CG2 THR B1175     7089   8165  13066   2186    612    -10       C  
ATOM   3235  N   LEU B1176       4.844  58.795  69.045  1.00 74.91           N  
ANISOU 3235  N   LEU B1176     7048   8098  13316   2235    707    -13       N  
ATOM   3236  CA  LEU B1176       5.133  59.980  69.834  1.00 74.67           C  
ANISOU 3236  CA  LEU B1176     6993   8051  13326   2242    684    -17       C  
ATOM   3237  C   LEU B1176       4.010  60.232  70.860  1.00 74.78           C  
ANISOU 3237  C   LEU B1176     6984   8125  13303   2262    621    -43       C  
ATOM   3238  O   LEU B1176       3.630  61.398  71.127  1.00 74.69           O  
ANISOU 3238  O   LEU B1176     6987   8110  13283   2295    592    -54       O  
ATOM   3239  CB  LEU B1176       5.347  61.209  68.940  1.00 74.54           C  
ANISOU 3239  CB  LEU B1176     7027   7986  13309   2255    705      1       C  
ATOM   3240  CG  LEU B1176       6.449  61.311  67.901  1.00 74.20           C  
ANISOU 3240  CG  LEU B1176     7009   7888  13296   2235    777     34       C  
ATOM   3241  CD1 LEU B1176       5.858  61.856  66.624  1.00 74.92           C  
ANISOU 3241  CD1 LEU B1176     7181   7961  13322   2252    792     46       C  
ATOM   3242  CD2 LEU B1176       7.498  62.283  68.370  1.00 74.48           C  
ANISOU 3242  CD2 LEU B1176     7018   7877  13405   2212    777     54       C  
ATOM   3243  N   GLU B1177       3.470  59.140  71.419  1.00 74.68           N  
ANISOU 3243  N   GLU B1177     6940   8169  13265   2245    600    -53       N  
ATOM   3244  CA  GLU B1177       2.481  59.247  72.516  1.00 74.71           C  
ANISOU 3244  CA  GLU B1177     6909   8243  13234   2259    554    -74       C  
ATOM   3245  C   GLU B1177       3.244  59.414  73.795  1.00 74.44           C  
ANISOU 3245  C   GLU B1177     6847   8188  13247   2248    537    -85       C  
ATOM   3246  O   GLU B1177       4.073  58.554  74.140  1.00 74.63           O  
ANISOU 3246  O   GLU B1177     6856   8188  13312   2210    542    -78       O  
ATOM   3247  CB  GLU B1177       1.582  58.011  72.629  1.00 74.56           C  
ANISOU 3247  CB  GLU B1177     6868   8296  13164   2229    535    -70       C  
ATOM   3248  CG  GLU B1177       0.292  58.271  73.397  1.00 75.11           C  
ANISOU 3248  CG  GLU B1177     6897   8460  13182   2250    502    -83       C  
ATOM   3249  CD  GLU B1177       0.303  57.762  74.837  1.00 75.88           C  
ANISOU 3249  CD  GLU B1177     6954   8600  13278   2223    483    -92       C  
ATOM   3250  OE1 GLU B1177      -0.253  58.457  75.738  1.00 76.42           O  
ANISOU 3250  OE1 GLU B1177     6997   8718  13323   2260    470   -111       O  
ATOM   3251  OE2 GLU B1177       0.842  56.657  75.078  1.00 75.37           O  
ANISOU 3251  OE2 GLU B1177     6890   8518  13230   2170    478    -81       O  
ATOM   3252  N   SER B1178       2.990  60.525  74.484  1.00 74.11           N  
ANISOU 3252  N   SER B1178     6812   8149  13200   2286    509   -103       N  
ATOM   3253  CA  SER B1178       3.675  60.810  75.735  1.00 73.57           C  
ANISOU 3253  CA  SER B1178     6735   8050  13169   2278    481   -114       C  
ATOM   3254  C   SER B1178       5.210  60.661  75.576  1.00 73.64           C  
ANISOU 3254  C   SER B1178     6741   7975  13266   2237    494    -92       C  
ATOM   3255  O   SER B1178       5.941  60.459  76.577  1.00 73.69           O  
ANISOU 3255  O   SER B1178     6731   7954  13316   2212    466    -95       O  
ATOM   3256  CB  SER B1178       3.123  59.887  76.814  1.00 73.27           C  
ANISOU 3256  CB  SER B1178     6664   8082  13095   2259    461   -127       C  
ATOM   3257  OG  SER B1178       4.121  59.605  77.768  1.00 74.28           O  
ANISOU 3257  OG  SER B1178     6788   8163  13273   2226    437   -127       O  
ATOM   3258  N   TRP B1179       5.678  60.795  74.321  1.00 73.09           N  
ANISOU 3258  N   TRP B1179     6685   7868  13219   2231    538    -69       N  
ATOM   3259  CA  TRP B1179       7.022  60.362  73.902  1.00 72.97           C  
ANISOU 3259  CA  TRP B1179     6649   7798  13280   2196    574    -43       C  
ATOM   3260  C   TRP B1179       8.199  60.829  74.714  1.00 73.05           C  
ANISOU 3260  C   TRP B1179     6634   7750  13372   2171    546    -32       C  
ATOM   3261  O   TRP B1179       9.165  60.080  74.832  1.00 72.92           O  
ANISOU 3261  O   TRP B1179     6576   7712  13418   2144    559    -18       O  
ATOM   3262  CB  TRP B1179       7.273  60.648  72.409  1.00 73.29           C  
ANISOU 3262  CB  TRP B1179     6717   7812  13319   2200    633    -18       C  
ATOM   3263  CG  TRP B1179       7.909  61.987  72.050  1.00 73.24           C  
ANISOU 3263  CG  TRP B1179     6734   7746  13349   2195    638      6       C  
ATOM   3264  CD1 TRP B1179       7.274  63.104  71.525  1.00 73.10           C  
ANISOU 3264  CD1 TRP B1179     6774   7714  13286   2220    625      5       C  
ATOM   3265  CD2 TRP B1179       9.327  62.365  72.143  1.00 73.37           C  
ANISOU 3265  CD2 TRP B1179     6717   7705  13457   2156    652     39       C  
ATOM   3266  NE1 TRP B1179       8.164  64.125  71.316  1.00 73.64           N  
ANISOU 3266  NE1 TRP B1179     6859   7717  13404   2194    625     36       N  
ATOM   3267  CE2 TRP B1179       9.413  63.746  71.672  1.00 73.87           C  
ANISOU 3267  CE2 TRP B1179     6828   7721  13517   2151    642     60       C  
ATOM   3268  CE3 TRP B1179      10.478  61.735  72.591  1.00 73.54           C  
ANISOU 3268  CE3 TRP B1179     6673   7710  13560   2125    662     55       C  
ATOM   3269  CZ2 TRP B1179      10.616  64.445  71.643  1.00 74.53           C  
ANISOU 3269  CZ2 TRP B1179     6892   7747  13678   2104    645    102       C  
ATOM   3270  CZ3 TRP B1179      11.689  62.446  72.557  1.00 74.43           C  
ANISOU 3270  CZ3 TRP B1179     6752   7770  13757   2086    667     96       C  
ATOM   3271  CH2 TRP B1179      11.754  63.766  72.079  1.00 74.86           C  
ANISOU 3271  CH2 TRP B1179     6852   7783  13807   2070    660    122       C  
ATOM   3272  N   SER B1180       8.125  62.058  75.246  1.00 73.12           N  
ANISOU 3272  N   SER B1180     6672   7728  13380   2183    500    -37       N  
ATOM   3273  CA  SER B1180       9.237  62.707  75.953  1.00 73.40           C  
ANISOU 3273  CA  SER B1180     6699   7695  13494   2153    458    -20       C  
ATOM   3274  C   SER B1180       9.000  62.938  77.461  1.00 73.16           C  
ANISOU 3274  C   SER B1180     6689   7659  13448   2162    380    -49       C  
ATOM   3275  O   SER B1180       9.952  62.876  78.238  1.00 73.35           O  
ANISOU 3275  O   SER B1180     6693   7637  13540   2126    338    -38       O  
ATOM   3276  CB  SER B1180       9.615  64.027  75.251  1.00 74.17           C  
ANISOU 3276  CB  SER B1180     6835   7735  13611   2146    459      8       C  
ATOM   3277  OG  SER B1180      10.260  64.948  76.137  1.00 75.22           O  
ANISOU 3277  OG  SER B1180     6990   7801  13791   2124    386     16       O  
HETATM 3278  N   MSE B1181       7.759  63.221  77.866  1.00 72.63           N  
ANISOU 3278  N   MSE B1181     6662   7641  13294   2211    362    -85       N  
HETATM 3279  CA  MSE B1181       7.417  63.374  79.293  1.00 72.53           C  
ANISOU 3279  CA  MSE B1181     6675   7635  13246   2229    301   -116       C  
HETATM 3280  C   MSE B1181       7.380  62.008  79.960  1.00 72.01           C  
ANISOU 3280  C   MSE B1181     6569   7617  13176   2201    304   -123       C  
HETATM 3281  O   MSE B1181       7.985  61.825  81.031  1.00 71.65           O  
ANISOU 3281  O   MSE B1181     6528   7534  13160   2175    253   -126       O  
HETATM 3282  CB  MSE B1181       6.080  64.087  79.559  1.00 72.81           C  
ANISOU 3282  CB  MSE B1181     6758   7722  13184   2303    290   -153       C  
HETATM 3283  CG  MSE B1181       5.776  65.320  78.726  1.00 73.18           C  
ANISOU 3283  CG  MSE B1181     6856   7737  13213   2346    288   -152       C  
HETATM 3284 SE   MSE B1181       6.897  66.816  79.347  1.00 75.25          SE  
ANISOU 3284 SE   MSE B1181     7202   7861  13528   2333    198   -141      SE  
HETATM 3285  CE  MSE B1181       5.738  67.438  80.817  1.00 75.21           C  
ANISOU 3285  CE  MSE B1181     7273   7889  13414   2431    141   -207       C  
ATOM   3286  N   GLY B1182       6.695  61.041  79.328  1.00 71.28           N  
ANISOU 3286  N   GLY B1182     6444   7596  13045   2200    354   -123       N  
ATOM   3287  CA  GLY B1182       6.680  59.645  79.812  1.00 71.21           C  
ANISOU 3287  CA  GLY B1182     6404   7624  13029   2163    352   -123       C  
ATOM   3288  C   GLY B1182       7.906  58.730  79.578  1.00 71.26           C  
ANISOU 3288  C   GLY B1182     6375   7580  13120   2118    357   -100       C  
ATOM   3289  O   GLY B1182       7.929  57.601  80.078  1.00 71.46           O  
ANISOU 3289  O   GLY B1182     6390   7623  13138   2090    340   -103       O  
ATOM   3290  N   ILE B1183       8.923  59.185  78.836  1.00 70.72           N  
ANISOU 3290  N   ILE B1183     6289   7452  13130   2111    378    -76       N  
ATOM   3291  CA  ILE B1183      10.061  58.338  78.514  1.00 70.53           C  
ANISOU 3291  CA  ILE B1183     6219   7392  13186   2084    395    -54       C  
ATOM   3292  C   ILE B1183      11.437  59.026  78.634  1.00 71.12           C  
ANISOU 3292  C   ILE B1183     6261   7393  13369   2063    375    -26       C  
ATOM   3293  O   ILE B1183      12.163  58.813  79.609  1.00 71.17           O  
ANISOU 3293  O   ILE B1183     6250   7361  13431   2038    315    -24       O  
ATOM   3294  CB  ILE B1183       9.879  57.669  77.121  1.00 70.70           C  
ANISOU 3294  CB  ILE B1183     6232   7441  13188   2098    470    -44       C  
ATOM   3295  CG1 ILE B1183       8.881  56.487  77.191  1.00 70.56           C  
ANISOU 3295  CG1 ILE B1183     6235   7483  13092   2096    465    -62       C  
ATOM   3296  CG2 ILE B1183      11.220  57.268  76.480  1.00 70.61           C  
ANISOU 3296  CG2 ILE B1183     6173   7387  13268   2090    509    -18       C  
ATOM   3297  CD1 ILE B1183       9.030  55.553  78.385  1.00 70.92           C  
ANISOU 3297  CD1 ILE B1183     6277   7527  13140   2067    406    -74       C  
ATOM   3298  N   VAL B1184      11.811  59.841  77.656  1.00 71.44           N  
ANISOU 3298  N   VAL B1184     6293   7413  13439   2065    420      0       N  
ATOM   3299  CA  VAL B1184      13.176  60.367  77.622  1.00 72.41           C  
ANISOU 3299  CA  VAL B1184     6367   7475  13670   2031    410     39       C  
ATOM   3300  C   VAL B1184      13.592  61.240  78.821  1.00 72.89           C  
ANISOU 3300  C   VAL B1184     6448   7478  13770   2003    313     43       C  
ATOM   3301  O   VAL B1184      14.648  61.019  79.374  1.00 73.80           O  
ANISOU 3301  O   VAL B1184     6513   7551  13975   1970    270     64       O  
ATOM   3302  CB  VAL B1184      13.516  61.061  76.285  1.00 73.11           C  
ANISOU 3302  CB  VAL B1184     6445   7556  13778   2027    483     75       C  
ATOM   3303  CG1 VAL B1184      14.981  61.527  76.284  1.00 73.81           C  
ANISOU 3303  CG1 VAL B1184     6465   7594  13986   1980    476    126       C  
ATOM   3304  CG2 VAL B1184      13.219  60.121  75.105  1.00 72.76           C  
ANISOU 3304  CG2 VAL B1184     6393   7560  13694   2057    576     72       C  
ATOM   3305  N   ARG B1185      12.792  62.223  79.226  1.00 72.97           N  
ANISOU 3305  N   ARG B1185     6534   7478  13712   2022    272     22       N  
ATOM   3306  CA  ARG B1185      13.138  63.000  80.422  1.00 73.17           C  
ANISOU 3306  CA  ARG B1185     6602   7440  13760   2002    171     20       C  
ATOM   3307  C   ARG B1185      13.403  62.066  81.624  1.00 73.42           C  
ANISOU 3307  C   ARG B1185     6621   7467  13809   1988    113      3       C  
ATOM   3308  O   ARG B1185      14.524  62.055  82.140  1.00 74.29           O  
ANISOU 3308  O   ARG B1185     6696   7518  14013   1945     54     30       O  
ATOM   3309  CB  ARG B1185      12.074  64.052  80.766  1.00 73.14           C  
ANISOU 3309  CB  ARG B1185     6697   7434  13659   2046    137    -12       C  
ATOM   3310  CG  ARG B1185      11.695  65.033  79.659  1.00 73.49           C  
ANISOU 3310  CG  ARG B1185     6774   7474  13674   2066    176      0       C  
ATOM   3311  CD  ARG B1185      12.477  66.343  79.711  1.00 73.94           C  
ANISOU 3311  CD  ARG B1185     6873   7438  13784   2029    111     35       C  
ATOM   3312  NE  ARG B1185      11.725  67.408  79.070  1.00 73.83           N  
ANISOU 3312  NE  ARG B1185     6937   7413  13702   2068    115     26       N  
ATOM   3313  CZ  ARG B1185      12.246  68.493  78.510  1.00 74.78           C  
ANISOU 3313  CZ  ARG B1185     7094   7465  13853   2034     91     66       C  
ATOM   3314  NH1 ARG B1185      13.555  68.689  78.483  1.00 75.63           N  
ANISOU 3314  NH1 ARG B1185     7155   7516  14066   1951     65    124       N  
ATOM   3315  NH2 ARG B1185      11.443  69.397  77.969  1.00 75.42           N  
ANISOU 3315  NH2 ARG B1185     7258   7536  13861   2079     87     51       N  
ATOM   3316  N   PRO B1186      12.403  61.254  82.064  1.00 72.83           N  
ANISOU 3316  N   PRO B1186     6572   7454  13646   2017    124    -37       N  
ATOM   3317  CA  PRO B1186      12.691  60.452  83.267  1.00 72.77           C  
ANISOU 3317  CA  PRO B1186     6569   7430  13649   1996     59    -50       C  
ATOM   3318  C   PRO B1186      13.904  59.555  83.063  1.00 73.28           C  
ANISOU 3318  C   PRO B1186     6551   7467  13824   1961     57    -21       C  
ATOM   3319  O   PRO B1186      14.585  59.178  84.029  1.00 73.74           O  
ANISOU 3319  O   PRO B1186     6607   7479  13933   1934    -21    -18       O  
ATOM   3320  CB  PRO B1186      11.436  59.595  83.455  1.00 72.27           C  
ANISOU 3320  CB  PRO B1186     6531   7451  13477   2021     93    -85       C  
ATOM   3321  CG  PRO B1186      10.640  59.735  82.197  1.00 72.13           C  
ANISOU 3321  CG  PRO B1186     6500   7495  13412   2054    179    -85       C  
ATOM   3322  CD  PRO B1186      11.023  61.049  81.579  1.00 72.35           C  
ANISOU 3322  CD  PRO B1186     6537   7475  13477   2062    185    -66       C  
ATOM   3323  N   LEU B1187      14.176  59.227  81.806  1.00 73.31           N  
ANISOU 3323  N   LEU B1187     6493   7498  13864   1970    141      0       N  
ATOM   3324  CA  LEU B1187      15.334  58.414  81.465  1.00 73.75           C  
ANISOU 3324  CA  LEU B1187     6464   7536  14023   1955    155     26       C  
ATOM   3325  C   LEU B1187      16.559  59.291  81.611  1.00 74.74           C  
ANISOU 3325  C   LEU B1187     6539   7595  14262   1917    111     70       C  
ATOM   3326  O   LEU B1187      17.568  58.857  82.157  1.00 75.73           O  
ANISOU 3326  O   LEU B1187     6609   7683  14482   1894     55     88       O  
ATOM   3327  CB  LEU B1187      15.232  57.907  80.018  1.00 73.43           C  
ANISOU 3327  CB  LEU B1187     6384   7544  13972   1984    267     35       C  
ATOM   3328  CG  LEU B1187      15.347  56.416  79.714  1.00 73.18           C  
ANISOU 3328  CG  LEU B1187     6326   7538  13941   2007    298     22       C  
ATOM   3329  CD1 LEU B1187      14.136  55.662  80.225  1.00 73.00           C  
ANISOU 3329  CD1 LEU B1187     6375   7553  13807   2013    273    -16       C  
ATOM   3330  CD2 LEU B1187      15.466  56.203  78.221  1.00 73.22           C  
ANISOU 3330  CD2 LEU B1187     6300   7573  13945   2038    407     37       C  
HETATM 3331  N   MSE B1188      16.461  60.531  81.134  1.00 75.01           N  
ANISOU 3331  N   MSE B1188     6595   7615  14290   1907    126     90       N  
HETATM 3332  CA  MSE B1188      17.575  61.460  81.149  1.00 76.11           C  
ANISOU 3332  CA  MSE B1188     6691   7694  14534   1857     84    142       C  
HETATM 3333  C   MSE B1188      17.892  61.845  82.566  1.00 76.22           C  
ANISOU 3333  C   MSE B1188     6751   7637  14572   1824    -50    138       C  
HETATM 3334  O   MSE B1188      19.048  62.154  82.878  1.00 77.15           O  
ANISOU 3334  O   MSE B1188     6812   7698  14802   1773   -114    183       O  
HETATM 3335  CB  MSE B1188      17.263  62.699  80.333  1.00 77.30           C  
ANISOU 3335  CB  MSE B1188     6881   7837  14652   1850    120    163       C  
HETATM 3336  CG  MSE B1188      17.690  62.543  78.881  1.00 79.31           C  
ANISOU 3336  CG  MSE B1188     7059   8133  14943   1850    238    200       C  
HETATM 3337 SE   MSE B1188      17.109  64.141  77.878  1.00 82.94          SE  
ANISOU 3337 SE   MSE B1188     7601   8577  15338   1839    271    222      SE  
HETATM 3338  CE  MSE B1188      18.225  65.513  78.768  1.00 83.30           C  
ANISOU 3338  CE  MSE B1188     7653   8514  15484   1749    134    280       C  
ATOM   3339  N   GLU B1189      16.895  61.802  83.450  1.00 75.09           N  
ANISOU 3339  N   GLU B1189     6709   7496  14324   1852    -95     87       N  
ATOM   3340  CA  GLU B1189      17.148  62.094  84.853  1.00 75.21           C  
ANISOU 3340  CA  GLU B1189     6789   7442  14347   1827   -223     79       C  
ATOM   3341  C   GLU B1189      18.153  61.100  85.477  1.00 75.49           C  
ANISOU 3341  C   GLU B1189     6755   7448  14478   1797   -282     94       C  
ATOM   3342  O   GLU B1189      18.811  61.413  86.464  1.00 76.29           O  
ANISOU 3342  O   GLU B1189     6882   7473  14632   1758   -399    108       O  
ATOM   3343  CB  GLU B1189      15.839  62.193  85.642  1.00 74.76           C  
ANISOU 3343  CB  GLU B1189     6852   7408  14147   1871   -241     21       C  
ATOM   3344  CG  GLU B1189      14.873  63.308  85.187  1.00 74.63           C  
ANISOU 3344  CG  GLU B1189     6909   7409  14039   1912   -206      3       C  
ATOM   3345  CD  GLU B1189      14.916  64.586  86.038  1.00 75.48           C  
ANISOU 3345  CD  GLU B1189     7126   7430  14121   1909   -311     -2       C  
ATOM   3346  OE1 GLU B1189      15.892  65.354  85.929  1.00 76.47           O  
ANISOU 3346  OE1 GLU B1189     7242   7477  14336   1858   -372     43       O  
ATOM   3347  OE2 GLU B1189      13.960  64.852  86.805  1.00 75.08           O  
ANISOU 3347  OE2 GLU B1189     7177   7391  13957   1959   -334    -50       O  
ATOM   3348  N   VAL B1190      18.288  59.916  84.878  1.00 75.31           N  
ANISOU 3348  N   VAL B1190     6654   7481  14481   1818   -209     91       N  
ATOM   3349  CA  VAL B1190      19.316  58.919  85.265  1.00 75.60           C  
ANISOU 3349  CA  VAL B1190     6613   7493  14620   1803   -256    106       C  
ATOM   3350  C   VAL B1190      20.517  58.975  84.295  1.00 76.38           C  
ANISOU 3350  C   VAL B1190     6571   7597  14855   1789   -205    162       C  
ATOM   3351  O   VAL B1190      21.582  59.467  84.674  1.00 77.40           O  
ANISOU 3351  O   VAL B1190     6643   7669  15097   1741   -282    207       O  
ATOM   3352  CB  VAL B1190      18.755  57.464  85.391  1.00 74.60           C  
ANISOU 3352  CB  VAL B1190     6502   7412  14430   1839   -228     65       C  
ATOM   3353  CG1 VAL B1190      19.837  56.499  85.814  1.00 74.85           C  
ANISOU 3353  CG1 VAL B1190     6465   7407  14568   1831   -291     79       C  
ATOM   3354  CG2 VAL B1190      17.636  57.389  86.410  1.00 74.22           C  
ANISOU 3354  CG2 VAL B1190     6580   7369  14253   1842   -276     21       C  
ATOM   3355  N   TYR B1191      20.365  58.459  83.073  1.00 75.93           N  
ANISOU 3355  N   TYR B1191     6457   7607  14785   1829    -78    162       N  
ATOM   3356  CA  TYR B1191      21.464  58.499  82.110  1.00 77.07           C  
ANISOU 3356  CA  TYR B1191     6469   7770  15046   1824    -10    214       C  
ATOM   3357  C   TYR B1191      21.235  59.730  81.239  1.00 77.34           C  
ANISOU 3357  C   TYR B1191     6515   7816  15056   1800     54    245       C  
ATOM   3358  O   TYR B1191      20.392  59.699  80.327  1.00 77.48           O  
ANISOU 3358  O   TYR B1191     6572   7884  14982   1837    153    224       O  
ATOM   3359  CB  TYR B1191      21.547  57.226  81.227  1.00 77.19           C  
ANISOU 3359  CB  TYR B1191     6424   7845  15060   1887     93    198       C  
ATOM   3360  CG  TYR B1191      21.328  55.899  81.951  1.00 77.18           C  
ANISOU 3360  CG  TYR B1191     6459   7836  15031   1921     39    152       C  
ATOM   3361  CD1 TYR B1191      20.145  55.155  81.755  1.00 76.38           C  
ANISOU 3361  CD1 TYR B1191     6450   7772  14800   1958     80    103       C  
ATOM   3362  CD2 TYR B1191      22.286  55.393  82.840  1.00 77.46           C  
ANISOU 3362  CD2 TYR B1191     6441   7823  15168   1910    -62    163       C  
ATOM   3363  CE1 TYR B1191      19.939  53.945  82.410  1.00 75.71           C  
ANISOU 3363  CE1 TYR B1191     6407   7676  14683   1977     24     68       C  
ATOM   3364  CE2 TYR B1191      22.084  54.191  83.503  1.00 77.09           C  
ANISOU 3364  CE2 TYR B1191     6442   7761  15090   1937   -121    123       C  
ATOM   3365  CZ  TYR B1191      20.912  53.472  83.281  1.00 76.49           C  
ANISOU 3365  CZ  TYR B1191     6462   7721  14880   1967    -76     76       C  
ATOM   3366  OH  TYR B1191      20.700  52.286  83.948  1.00 76.53           O  
ANISOU 3366  OH  TYR B1191     6524   7708  14848   1981   -141     43       O  
ATOM   3367  N   PRO B1192      21.996  60.817  81.488  1.00 77.76           N  
ANISOU 3367  N   PRO B1192     6537   7816  15190   1734    -11    298       N  
ATOM   3368  CA  PRO B1192      21.645  62.090  80.875  1.00 77.39           C  
ANISOU 3368  CA  PRO B1192     6540   7761  15103   1705     18    323       C  
ATOM   3369  C   PRO B1192      22.075  62.185  79.418  1.00 77.72           C  
ANISOU 3369  C   PRO B1192     6492   7858  15178   1705    154    368       C  
ATOM   3370  O   PRO B1192      22.281  63.296  78.925  1.00 78.17           O  
ANISOU 3370  O   PRO B1192     6556   7897  15250   1653    162    416       O  
ATOM   3371  CB  PRO B1192      22.401  63.114  81.736  1.00 78.25           C  
ANISOU 3371  CB  PRO B1192     6656   7784  15292   1625   -117    369       C  
ATOM   3372  CG  PRO B1192      23.253  62.323  82.704  1.00 78.62           C  
ANISOU 3372  CG  PRO B1192     6634   7801  15436   1613   -209    374       C  
ATOM   3373  CD  PRO B1192      23.279  60.911  82.207  1.00 78.53           C  
ANISOU 3373  CD  PRO B1192     6547   7860  15430   1680   -113    346       C  
ATOM   3374  N   TYR B1193      22.202  61.038  78.738  1.00 77.51           N  
ANISOU 3374  N   TYR B1193     6398   7896  15158   1762    255    353       N  
ATOM   3375  CA  TYR B1193      22.591  61.020  77.315  1.00 77.85           C  
ANISOU 3375  CA  TYR B1193     6365   7997  15219   1774    398    391       C  
ATOM   3376  C   TYR B1193      21.506  60.490  76.408  1.00 76.76           C  
ANISOU 3376  C   TYR B1193     6304   7909  14953   1842    503    342       C  
ATOM   3377  O   TYR B1193      21.633  60.590  75.184  1.00 76.83           O  
ANISOU 3377  O   TYR B1193     6286   7960  14947   1854    621    368       O  
ATOM   3378  CB  TYR B1193      23.896  60.229  77.069  1.00 78.79           C  
ANISOU 3378  CB  TYR B1193     6322   8149  15467   1788    444    428       C  
ATOM   3379  CG  TYR B1193      25.185  61.005  77.314  1.00 80.13           C  
ANISOU 3379  CG  TYR B1193     6370   8294  15781   1705    393    511       C  
ATOM   3380  CD1 TYR B1193      26.079  60.590  78.294  1.00 80.88           C  
ANISOU 3380  CD1 TYR B1193     6377   8359  15995   1689    290    526       C  
ATOM   3381  CD2 TYR B1193      25.504  62.149  76.570  1.00 80.88           C  
ANISOU 3381  CD2 TYR B1193     6442   8394  15895   1636    439    579       C  
ATOM   3382  CE1 TYR B1193      27.261  61.280  78.533  1.00 82.42           C  
ANISOU 3382  CE1 TYR B1193     6453   8533  16329   1606    233    608       C  
ATOM   3383  CE2 TYR B1193      26.677  62.858  76.807  1.00 82.47           C  
ANISOU 3383  CE2 TYR B1193     6530   8574  16231   1546    385    664       C  
ATOM   3384  CZ  TYR B1193      27.559  62.414  77.797  1.00 83.29           C  
ANISOU 3384  CZ  TYR B1193     6536   8653  16459   1531    280    679       C  
ATOM   3385  OH  TYR B1193      28.748  63.068  78.073  1.00 84.50           O  
ANISOU 3385  OH  TYR B1193     6564   8785  16755   1435    212    769       O  
ATOM   3386  N   ALA B1194      20.454  59.922  77.011  1.00105.86           N  
ANISOU 3386  N   ALA B1194    11895  14660  13665   1475   -421  -1773       N  
ATOM   3387  CA  ALA B1194      19.371  59.224  76.279  1.00103.68           C  
ANISOU 3387  CA  ALA B1194    11865  13963  13568   1178   -183  -1227       C  
ATOM   3388  C   ALA B1194      18.714  60.087  75.192  1.00101.05           C  
ANISOU 3388  C   ALA B1194    11482  13259  13655    570   -182  -1212       C  
ATOM   3389  O   ALA B1194      17.921  59.596  74.385  1.00 98.92           O  
ANISOU 3389  O   ALA B1194    11365  12643  13577    276    -33   -855       O  
ATOM   3390  CB  ALA B1194      18.326  58.681  77.248  1.00104.85           C  
ANISOU 3390  CB  ALA B1194    12210  14135  13494   1560     20   -826       C  
ATOM   3391  N   TRP B1195      19.051  61.378  75.200  1.00101.75           N  
ANISOU 3391  N   TRP B1195    11344  13428  13887    419   -341  -1621       N  
ATOM   3392  CA  TRP B1195      18.687  62.314  74.131  1.00 99.77           C  
ANISOU 3392  CA  TRP B1195    11029  12855  14022   -117   -336  -1669       C  
ATOM   3393  C   TRP B1195      19.526  62.104  72.900  1.00 98.31           C  
ANISOU 3393  C   TRP B1195    10820  12494  14038   -442   -345  -1761       C  
ATOM   3394  O   TRP B1195      19.125  62.507  71.821  1.00 96.40           O  
ANISOU 3394  O   TRP B1195    10616  11937  14073   -851   -284  -1658       O  
ATOM   3395  CB  TRP B1195      18.811  63.765  74.606  1.00101.16           C  
ANISOU 3395  CB  TRP B1195    10965  13159  14312   -142   -452  -2082       C  
ATOM   3396  CG  TRP B1195      20.226  64.185  74.940  1.00103.55           C  
ANISOU 3396  CG  TRP B1195    10997  13749  14598      9   -616  -2644       C  
ATOM   3397  CD1 TRP B1195      20.835  64.177  76.187  1.00106.43           C  
ANISOU 3397  CD1 TRP B1195    11214  14558  14667    510   -763  -2974       C  
ATOM   3398  CD2 TRP B1195      21.261  64.677  74.015  1.00103.40           C  
ANISOU 3398  CD2 TRP B1195    10798  13604  14886   -316   -645  -2988       C  
ATOM   3399  NE1 TRP B1195      22.133  64.624  76.103  1.00108.06           N  
ANISOU 3399  NE1 TRP B1195    11137  14925  14996    502   -901  -3527       N  
ATOM   3400  CE2 TRP B1195      22.449  64.947  74.834  1.00106.21           C  
ANISOU 3400  CE2 TRP B1195    10869  14343  15141      3   -818  -3555       C  
ATOM   3401  CE3 TRP B1195      21.318  64.915  72.641  1.00101.40           C  
ANISOU 3401  CE3 TRP B1195    10589  12974  14965   -791   -534  -2894       C  
ATOM   3402  CZ2 TRP B1195      23.631  65.433  74.287  1.00106.93           C  
ANISOU 3402  CZ2 TRP B1195    10710  14404  15514   -194   -859  -4015       C  
ATOM   3403  CZ3 TRP B1195      22.514  65.410  72.103  1.00102.91           C  
ANISOU 3403  CZ3 TRP B1195    10561  13132  15408   -964   -553  -3313       C  
ATOM   3404  CH2 TRP B1195      23.644  65.660  72.913  1.00105.30           C  
ANISOU 3404  CH2 TRP B1195    10571  13776  15661   -691   -703  -3867       C  
ATOM   3405  N   VAL B1196      20.705  61.500  73.045  1.00 99.54           N  
ANISOU 3405  N   VAL B1196    10916  12862  14045   -238   -421  -1963       N  
ATOM   3406  CA  VAL B1196      21.465  61.087  71.862  1.00 98.55           C  
ANISOU 3406  CA  VAL B1196    10805  12556  14085   -524   -405  -1984       C  
ATOM   3407  C   VAL B1196      21.020  59.691  71.411  1.00 97.38           C  
ANISOU 3407  C   VAL B1196    10909  12246  13843   -518   -278  -1523       C  
ATOM   3408  O   VAL B1196      21.195  59.308  70.251  1.00 95.53           O  
ANISOU 3408  O   VAL B1196    10745  11774  13779   -820   -233  -1414       O  
ATOM   3409  CB  VAL B1196      22.999  61.117  72.047  1.00100.27           C  
ANISOU 3409  CB  VAL B1196    10814  13032  14252   -373   -539  -2448       C  
ATOM   3410  CG1 VAL B1196      23.658  61.591  70.754  1.00 98.95           C  
ANISOU 3410  CG1 VAL B1196    10559  12602  14434   -813   -510  -2618       C  
ATOM   3411  CG2 VAL B1196      23.407  62.014  73.195  1.00102.77           C  
ANISOU 3411  CG2 VAL B1196    10874  13690  14483    -81   -685  -2914       C  
ATOM   3412  N   PHE B1197      20.448  58.933  72.339  1.00 98.59           N  
ANISOU 3412  N   PHE B1197    11195  12525  13740   -157   -200  -1263       N  
ATOM   3413  CA  PHE B1197      19.837  57.661  71.999  1.00 98.05           C  
ANISOU 3413  CA  PHE B1197    11349  12255  13653   -156    -22   -819       C  
ATOM   3414  C   PHE B1197      18.576  57.928  71.186  1.00 95.96           C  
ANISOU 3414  C   PHE B1197    11163  11626  13673   -542     73   -565       C  
ATOM   3415  O   PHE B1197      18.477  57.499  70.039  1.00 95.08           O  
ANISOU 3415  O   PHE B1197    11114  11260  13753   -848    113   -440       O  
ATOM   3416  CB  PHE B1197      19.507  56.883  73.271  1.00100.37           C  
ANISOU 3416  CB  PHE B1197    11761  12747  13628    362     99   -600       C  
ATOM   3417  CG  PHE B1197      19.072  55.458  73.045  1.00100.56           C  
ANISOU 3417  CG  PHE B1197    11992  12568  13648    426    334   -177       C  
ATOM   3418  CD1 PHE B1197      19.920  54.401  73.377  1.00102.48           C  
ANISOU 3418  CD1 PHE B1197    12310  12979  13650    767    390   -131       C  
ATOM   3419  CD2 PHE B1197      17.801  55.164  72.556  1.00 99.22           C  
ANISOU 3419  CD2 PHE B1197    11927  12043  13729    175    513    157       C  
ATOM   3420  CE1 PHE B1197      19.512  53.080  73.212  1.00103.02           C  
ANISOU 3420  CE1 PHE B1197    12561  12833  13749    838    651    260       C  
ATOM   3421  CE2 PHE B1197      17.391  53.848  72.378  1.00 99.74           C  
ANISOU 3421  CE2 PHE B1197    12145  11897  13855    231    759    504       C  
ATOM   3422  CZ  PHE B1197      18.245  52.807  72.706  1.00101.67           C  
ANISOU 3422  CZ  PHE B1197    12470  12281  13880    556    844    567       C  
ATOM   3423  N   PHE B1198      17.638  58.672  71.769  1.00 95.67           N  
ANISOU 3423  N   PHE B1198    11109  11586  13656   -511     91   -520       N  
ATOM   3424  CA  PHE B1198      16.303  58.824  71.196  1.00 93.65           C  
ANISOU 3424  CA  PHE B1198    10931  11019  13632   -792    191   -262       C  
ATOM   3425  C   PHE B1198      16.069  59.964  70.186  1.00 91.78           C  
ANISOU 3425  C   PHE B1198    10617  10598  13656  -1205    104   -403       C  
ATOM   3426  O   PHE B1198      15.183  59.860  69.339  1.00 90.22           O  
ANISOU 3426  O   PHE B1198    10494  10136  13651  -1459    163   -209       O  
ATOM   3427  CB  PHE B1198      15.281  58.898  72.319  1.00 94.56           C  
ANISOU 3427  CB  PHE B1198    11096  11190  13641   -533    297    -78       C  
ATOM   3428  CG  PHE B1198      14.957  57.568  72.935  1.00 95.33           C  
ANISOU 3428  CG  PHE B1198    11345  11275  13602   -215    511    245       C  
ATOM   3429  CD1 PHE B1198      15.483  57.217  74.167  1.00 97.24           C  
ANISOU 3429  CD1 PHE B1198    11617  11826  13504    292    547    230       C  
ATOM   3430  CD2 PHE B1198      14.096  56.679  72.295  1.00 94.02           C  
ANISOU 3430  CD2 PHE B1198    11282  10781  13659   -395    700    551       C  
ATOM   3431  CE1 PHE B1198      15.170  56.000  74.748  1.00 98.32           C  
ANISOU 3431  CE1 PHE B1198    11917  11924  13516    624    807    567       C  
ATOM   3432  CE2 PHE B1198      13.782  55.462  72.874  1.00 95.19           C  
ANISOU 3432  CE2 PHE B1198    11560  10868  13741   -105    961    852       C  
ATOM   3433  CZ  PHE B1198      14.324  55.122  74.101  1.00 97.30           C  
ANISOU 3433  CZ  PHE B1198    11889  11422  13659    409   1036    886       C  
ATOM   3434  N   ILE B1199      16.830  61.049  70.275  1.00 92.36           N  
ANISOU 3434  N   ILE B1199    10537  10807  13750  -1248    -17   -748       N  
ATOM   3435  CA  ILE B1199      16.705  62.125  69.279  1.00 91.33           C  
ANISOU 3435  CA  ILE B1199    10351  10475  13875  -1610    -40   -862       C  
ATOM   3436  C   ILE B1199      17.050  61.643  67.851  1.00 89.95           C  
ANISOU 3436  C   ILE B1199    10254  10082  13839  -1876    -15   -784       C  
ATOM   3437  O   ILE B1199      16.202  61.755  66.971  1.00 88.70           O  
ANISOU 3437  O   ILE B1199    10183   9692  13826  -2094     29   -605       O  
ATOM   3438  CB  ILE B1199      17.456  63.425  69.680  1.00 92.49           C  
ANISOU 3438  CB  ILE B1199    10291  10766  14085  -1609   -119  -1269       C  
ATOM   3439  CG1 ILE B1199      16.880  64.019  70.986  1.00 93.92           C  
ANISOU 3439  CG1 ILE B1199    10398  11140  14148  -1368   -153  -1336       C  
ATOM   3440  CG2 ILE B1199      17.448  64.446  68.550  1.00 92.02           C  
ANISOU 3440  CG2 ILE B1199    10199  10453  14310  -1964    -72  -1353       C  
ATOM   3441  CD1 ILE B1199      15.425  64.455  70.947  1.00 92.83           C  
ANISOU 3441  CD1 ILE B1199    10352  10821  14098  -1487    -83  -1078       C  
ATOM   3442  N   PRO B1200      18.272  61.092  67.619  1.00 90.37           N  
ANISOU 3442  N   PRO B1200    10275  10227  13836  -1832    -50   -929       N  
ATOM   3443  CA  PRO B1200      18.565  60.558  66.276  1.00 89.08           C  
ANISOU 3443  CA  PRO B1200    10199   9863  13785  -2060    -22   -835       C  
ATOM   3444  C   PRO B1200      17.649  59.393  65.872  1.00 88.53           C  
ANISOU 3444  C   PRO B1200    10284   9643  13709  -2077     40   -494       C  
ATOM   3445  O   PRO B1200      17.354  59.227  64.686  1.00 87.35           O  
ANISOU 3445  O   PRO B1200    10207   9291  13691  -2293     54   -395       O  
ATOM   3446  CB  PRO B1200      20.020  60.093  66.386  1.00 89.59           C  
ANISOU 3446  CB  PRO B1200    10188  10096  13758  -1949    -73  -1056       C  
ATOM   3447  CG  PRO B1200      20.586  60.909  67.487  1.00 91.29           C  
ANISOU 3447  CG  PRO B1200    10219  10560  13907  -1759   -143  -1383       C  
ATOM   3448  CD  PRO B1200      19.473  61.064  68.479  1.00 91.82           C  
ANISOU 3448  CD  PRO B1200    10320  10702  13864  -1581   -131  -1229       C  
ATOM   3449  N   PHE B1201      17.204  58.593  66.836  1.00 89.84           N  
ANISOU 3449  N   PHE B1201    10494   9902  13739  -1833     94   -332       N  
ATOM   3450  CA  PHE B1201      16.193  57.593  66.530  1.00 90.21           C  
ANISOU 3450  CA  PHE B1201    10650   9761  13864  -1865    200    -36       C  
ATOM   3451  C   PHE B1201      15.027  58.319  65.862  1.00 89.52           C  
ANISOU 3451  C   PHE B1201    10570   9475  13968  -2098    193     30       C  
ATOM   3452  O   PHE B1201      14.770  58.117  64.670  1.00 89.27           O  
ANISOU 3452  O   PHE B1201    10577   9268  14075  -2304    175     71       O  
ATOM   3453  CB  PHE B1201      15.739  56.829  67.780  1.00 91.73           C  
ANISOU 3453  CB  PHE B1201    10888  10044  13921  -1547    329    149       C  
ATOM   3454  CG  PHE B1201      14.626  55.852  67.525  1.00 91.98           C  
ANISOU 3454  CG  PHE B1201    10997   9834  14117  -1593    491    428       C  
ATOM   3455  CD1 PHE B1201      14.892  54.581  67.009  1.00 92.42           C  
ANISOU 3455  CD1 PHE B1201    11106   9776  14233  -1603    582    539       C  
ATOM   3456  CD2 PHE B1201      13.305  56.193  67.806  1.00 92.37           C  
ANISOU 3456  CD2 PHE B1201    11044   9758  14296  -1628    566    555       C  
ATOM   3457  CE1 PHE B1201      13.864  53.670  66.773  1.00 92.96           C  
ANISOU 3457  CE1 PHE B1201    11203   9596  14523  -1655    756    747       C  
ATOM   3458  CE2 PHE B1201      12.270  55.284  67.585  1.00 93.01           C  
ANISOU 3458  CE2 PHE B1201    11154   9597  14590  -1676    736    764       C  
ATOM   3459  CZ  PHE B1201      12.552  54.022  67.062  1.00 93.47           C  
ANISOU 3459  CZ  PHE B1201    11243   9528  14741  -1693    837    847       C  
ATOM   3460  N   ILE B1202      14.371  59.206  66.612  1.00 89.88           N  
ANISOU 3460  N   ILE B1202    10576   9573  14002  -2040    193     16       N  
ATOM   3461  CA  ILE B1202      13.219  59.981  66.115  1.00 89.01           C  
ANISOU 3461  CA  ILE B1202    10470   9301  14050  -2223    185     73       C  
ATOM   3462  C   ILE B1202      13.461  60.668  64.776  1.00 88.04           C  
ANISOU 3462  C   ILE B1202    10357   9058  14037  -2465    118    -29       C  
ATOM   3463  O   ILE B1202      12.543  60.765  63.975  1.00 87.65           O  
ANISOU 3463  O   ILE B1202    10347   8850  14105  -2595    113     61       O  
ATOM   3464  CB  ILE B1202      12.712  61.000  67.162  1.00 89.51           C  
ANISOU 3464  CB  ILE B1202    10477   9469  14066  -2120    183     27       C  
ATOM   3465  CG1 ILE B1202      11.649  60.341  68.060  1.00 89.85           C  
ANISOU 3465  CG1 ILE B1202    10558   9487  14094  -1947    299    251       C  
ATOM   3466  CG2 ILE B1202      12.179  62.263  66.481  1.00 88.78           C  
ANISOU 3466  CG2 ILE B1202    10365   9262  14108  -2331    138    -41       C  
ATOM   3467  CD1 ILE B1202      11.167  61.212  69.199  1.00 90.25           C  
ANISOU 3467  CD1 ILE B1202    10563   9663  14064  -1797    305    225       C  
ATOM   3468  N   PHE B1203      14.689  61.131  64.544  1.00 88.56           N  
ANISOU 3468  N   PHE B1203    10381   9201  14068  -2497     84   -225       N  
ATOM   3469  CA  PHE B1203      15.080  61.763  63.276  1.00 88.43           C  
ANISOU 3469  CA  PHE B1203    10392   9056  14152  -2688     79   -304       C  
ATOM   3470  C   PHE B1203      14.986  60.771  62.106  1.00 88.16           C  
ANISOU 3470  C   PHE B1203    10453   8897  14147  -2770     65   -182       C  
ATOM   3471  O   PHE B1203      14.369  61.075  61.084  1.00 87.60           O  
ANISOU 3471  O   PHE B1203    10445   8690  14148  -2872     57   -123       O  
ATOM   3472  CB  PHE B1203      16.506  62.324  63.359  1.00 88.79           C  
ANISOU 3472  CB  PHE B1203    10349   9189  14199  -2694     87   -558       C  
ATOM   3473  CG  PHE B1203      16.596  63.777  63.763  1.00 89.24           C  
ANISOU 3473  CG  PHE B1203    10302   9258  14349  -2728    125   -743       C  
ATOM   3474  CD1 PHE B1203      16.072  64.231  64.970  1.00 89.63           C  
ANISOU 3474  CD1 PHE B1203    10269   9435  14350  -2604     99   -786       C  
ATOM   3475  CD2 PHE B1203      17.282  64.687  62.953  1.00 89.87           C  
ANISOU 3475  CD2 PHE B1203    10355   9209  14582  -2870    216   -889       C  
ATOM   3476  CE1 PHE B1203      16.191  65.567  65.346  1.00 90.12           C  
ANISOU 3476  CE1 PHE B1203    10211   9504  14525  -2639    137   -991       C  
ATOM   3477  CE2 PHE B1203      17.407  66.022  63.325  1.00 90.58           C  
ANISOU 3477  CE2 PHE B1203    10326   9275  14814  -2909    294  -1082       C  
ATOM   3478  CZ  PHE B1203      16.859  66.461  64.525  1.00 90.60           C  
ANISOU 3478  CZ  PHE B1203    10232   9416  14777  -2801    241  -1147       C  
ATOM   3479  N   VAL B1204      15.582  59.589  62.266  1.00 89.05           N  
ANISOU 3479  N   VAL B1204    10572   9068  14194  -2695     62   -157       N  
ATOM   3480  CA  VAL B1204      15.628  58.584  61.177  1.00 89.68           C  
ANISOU 3480  CA  VAL B1204    10721   9041  14314  -2768     47    -79       C  
ATOM   3481  C   VAL B1204      14.283  57.853  60.952  1.00 90.49           C  
ANISOU 3481  C   VAL B1204    10842   9022  14519  -2780     54     77       C  
ATOM   3482  O   VAL B1204      13.958  57.484  59.809  1.00 90.09           O  
ANISOU 3482  O   VAL B1204    10825   8863  14542  -2866     10     90       O  
ATOM   3483  CB  VAL B1204      16.814  57.589  61.336  1.00 89.42           C  
ANISOU 3483  CB  VAL B1204    10685   9097  14195  -2694     53   -121       C  
ATOM   3484  CG1 VAL B1204      16.802  56.540  60.242  1.00 88.56           C  
ANISOU 3484  CG1 VAL B1204    10635   8873  14141  -2770     39    -47       C  
ATOM   3485  CG2 VAL B1204      18.142  58.333  61.295  1.00 89.69           C  
ANISOU 3485  CG2 VAL B1204    10671   9222  14186  -2715     40   -331       C  
ATOM   3486  N   VAL B1205      13.510  57.665  62.028  1.00 91.82           N  
ANISOU 3486  N   VAL B1205    10974   9209  14703  -2677    115    171       N  
ATOM   3487  CA  VAL B1205      12.187  57.035  61.943  1.00 93.70           C  
ANISOU 3487  CA  VAL B1205    11193   9308  15103  -2692    160    288       C  
ATOM   3488  C   VAL B1205      11.215  57.862  61.087  1.00 94.50           C  
ANISOU 3488  C   VAL B1205    11290   9321  15297  -2807     76    250       C  
ATOM   3489  O   VAL B1205      10.892  57.483  59.956  1.00 94.53           O  
ANISOU 3489  O   VAL B1205    11296   9236  15385  -2880     12    213       O  
ATOM   3490  CB  VAL B1205      11.571  56.812  63.335  1.00 94.58           C  
ANISOU 3490  CB  VAL B1205    11275   9443  15217  -2537    287    410       C  
ATOM   3491  CG1 VAL B1205      10.196  56.179  63.202  1.00 95.74           C  
ANISOU 3491  CG1 VAL B1205    11375   9403  15600  -2575    370    505       C  
ATOM   3492  CG2 VAL B1205      12.469  55.927  64.178  1.00 95.08           C  
ANISOU 3492  CG2 VAL B1205    11364   9610  15153  -2350    387    468       C  
ATOM   3493  N   THR B1206      10.760  58.986  61.643  1.00 95.76           N  
ANISOU 3493  N   THR B1206    11440   9520  15425  -2794     74    247       N  
ATOM   3494  CA  THR B1206       9.909  59.958  60.942  1.00 96.60           C  
ANISOU 3494  CA  THR B1206    11558   9567  15579  -2866      7    218       C  
ATOM   3495  C   THR B1206      10.397  60.154  59.503  1.00 97.85           C  
ANISOU 3495  C   THR B1206    11786   9695  15699  -2927    -67    146       C  
ATOM   3496  O   THR B1206       9.636  59.993  58.538  1.00 97.80           O  
ANISOU 3496  O   THR B1206    11785   9625  15750  -2937   -140    127       O  
ATOM   3497  CB  THR B1206       9.860  61.304  61.719  1.00 95.62           C  
ANISOU 3497  CB  THR B1206    11428   9512  15391  -2846     29    198       C  
ATOM   3498  OG1 THR B1206       9.105  61.118  62.931  1.00 96.17           O  
ANISOU 3498  OG1 THR B1206    11443   9601  15496  -2762     91    281       O  
ATOM   3499  CG2 THR B1206       9.241  62.436  60.885  1.00 94.23           C  
ANISOU 3499  CG2 THR B1206    11293   9276  15233  -2902    -14    173       C  
ATOM   3500  N   PHE B1207      11.684  60.472  59.376  1.00 99.03           N  
ANISOU 3500  N   PHE B1207    11979   9898  15751  -2941    -42     89       N  
ATOM   3501  CA  PHE B1207      12.340  60.634  58.080  1.00 99.61           C  
ANISOU 3501  CA  PHE B1207    12135   9934  15778  -2974    -64     42       C  
ATOM   3502  C   PHE B1207      11.804  59.594  57.089  1.00100.38           C  
ANISOU 3502  C   PHE B1207    12241   9981  15918  -2965   -151     49       C  
ATOM   3503  O   PHE B1207      11.419  59.941  55.972  1.00100.76           O  
ANISOU 3503  O   PHE B1207    12351   9999  15934  -2932   -208     28       O  
ATOM   3504  CB  PHE B1207      13.870  60.548  58.268  1.00 99.25           C  
ANISOU 3504  CB  PHE B1207    12091   9943  15674  -2992     -9    -32       C  
ATOM   3505  CG  PHE B1207      14.667  60.778  57.023  1.00 99.33           C  
ANISOU 3505  CG  PHE B1207    12192   9898  15651  -3021     15    -70       C  
ATOM   3506  CD1 PHE B1207      14.667  62.020  56.390  1.00100.16           C  
ANISOU 3506  CD1 PHE B1207    12371   9929  15757  -3022     98    -75       C  
ATOM   3507  CD2 PHE B1207      15.449  59.754  56.496  1.00 99.45           C  
ANISOU 3507  CD2 PHE B1207    12228   9921  15636  -3029    -12    -88       C  
ATOM   3508  CE1 PHE B1207      15.413  62.226  55.235  1.00100.95           C  
ANISOU 3508  CE1 PHE B1207    12575   9958  15825  -3012    170    -81       C  
ATOM   3509  CE2 PHE B1207      16.197  59.949  55.344  1.00 99.93           C  
ANISOU 3509  CE2 PHE B1207    12382   9927  15660  -3038     27   -111       C  
ATOM   3510  CZ  PHE B1207      16.175  61.187  54.709  1.00100.94           C  
ANISOU 3510  CZ  PHE B1207    12593   9975  15784  -3020    128   -101       C  
ATOM   3511  N   VAL B1208      11.716  58.337  57.531  1.00101.04           N  
ANISOU 3511  N   VAL B1208    12254  10057  16081  -2965   -149     69       N  
ATOM   3512  CA  VAL B1208      11.311  57.217  56.656  1.00101.72           C  
ANISOU 3512  CA  VAL B1208    12304  10083  16262  -2968   -218     28       C  
ATOM   3513  C   VAL B1208       9.788  56.982  56.617  1.00102.61           C  
ANISOU 3513  C   VAL B1208    12314  10126  16547  -2956   -261     -3       C  
ATOM   3514  O   VAL B1208       9.303  56.171  55.819  1.00104.29           O  
ANISOU 3514  O   VAL B1208    12456  10291  16878  -2951   -335   -102       O  
ATOM   3515  CB  VAL B1208      12.075  55.916  57.009  1.00101.39           C  
ANISOU 3515  CB  VAL B1208    12232  10034  16259  -2976   -157     49       C  
ATOM   3516  CG1 VAL B1208      11.695  54.789  56.066  1.00101.67           C  
ANISOU 3516  CG1 VAL B1208    12208   9993  16429  -2990   -218    -28       C  
ATOM   3517  CG2 VAL B1208      13.581  56.157  56.945  1.00100.49           C  
ANISOU 3517  CG2 VAL B1208    12199   9998  15983  -2982   -137     36       C  
HETATM 3518  N   MSE B1209       9.038  57.690  57.460  1.00101.83           N  
ANISOU 3518  N   MSE B1209    12186  10024  16481  -2948   -219     51       N  
HETATM 3519  CA  MSE B1209       7.571  57.671  57.378  1.00102.07           C  
ANISOU 3519  CA  MSE B1209    12112   9990  16681  -2937   -262     -1       C  
HETATM 3520  C   MSE B1209       7.122  58.766  56.445  1.00101.85           C  
ANISOU 3520  C   MSE B1209    12147  10013  16536  -2885   -384    -65       C  
HETATM 3521  O   MSE B1209       6.003  58.734  55.928  1.00101.89           O  
ANISOU 3521  O   MSE B1209    12069  10002  16642  -2840   -481   -171       O  
HETATM 3522  CB  MSE B1209       6.945  57.885  58.752  1.00102.27           C  
ANISOU 3522  CB  MSE B1209    12083   9981  16793  -2935   -142    102       C  
HETATM 3523  CG  MSE B1209       6.730  56.561  59.461  1.00104.11           C  
ANISOU 3523  CG  MSE B1209    12217  10105  17234  -2934      5    152       C  
HETATM 3524 SE   MSE B1209       5.118  55.707  58.729  1.00109.18          SE  
ANISOU 3524 SE   MSE B1209    12644  10576  18262  -2973    -31    -30      SE  
HETATM 3525  CE  MSE B1209       5.892  54.032  58.034  1.00108.99           C  
ANISOU 3525  CE  MSE B1209    12561  10468  18381  -3005      9   -113       C  
ATOM   3526  N   ILE B1210       8.001  59.748  56.236  1.00101.38           N  
ANISOU 3526  N   ILE B1210    12229  10013  16278  -2869   -360    -11       N  
ATOM   3527  CA  ILE B1210       7.743  60.876  55.338  1.00102.01           C  
ANISOU 3527  CA  ILE B1210    12412  10125  16221  -2780   -411    -25       C  
ATOM   3528  C   ILE B1210       7.874  60.428  53.884  1.00102.52           C  
ANISOU 3528  C   ILE B1210    12527  10222  16205  -2678   -521   -118       C  
ATOM   3529  O   ILE B1210       7.120  60.874  53.015  1.00103.50           O  
ANISOU 3529  O   ILE B1210    12682  10390  16253  -2535   -618   -180       O  
ATOM   3530  CB  ILE B1210       8.729  62.044  55.597  1.00101.77           C  
ANISOU 3530  CB  ILE B1210    12503  10100  16065  -2799   -282     56       C  
ATOM   3531  CG1 ILE B1210       8.677  62.515  57.057  1.00100.73           C  
ANISOU 3531  CG1 ILE B1210    12307   9971  15995  -2871   -195    106       C  
ATOM   3532  CG2 ILE B1210       8.454  63.213  54.662  1.00102.94           C  
ANISOU 3532  CG2 ILE B1210    12780  10244  16088  -2680   -267     79       C  
ATOM   3533  CD1 ILE B1210       9.902  63.313  57.479  1.00 99.62           C  
ANISOU 3533  CD1 ILE B1210    12213   9842  15797  -2913    -71    106       C  
ATOM   3534  N   ASN B1211       8.829  59.532  53.641  1.00102.32           N  
ANISOU 3534  N   ASN B1211    12508  10192  16178  -2723   -511   -134       N  
ATOM   3535  CA  ASN B1211       9.166  59.052  52.286  1.00103.22           C  
ANISOU 3535  CA  ASN B1211    12678  10346  16195  -2620   -606   -220       C  
ATOM   3536  C   ASN B1211       8.426  57.768  51.863  1.00103.16           C  
ANISOU 3536  C   ASN B1211    12504  10341  16352  -2602   -749   -395       C  
ATOM   3537  O   ASN B1211       8.683  57.217  50.789  1.00103.50           O  
ANISOU 3537  O   ASN B1211    12562  10432  16331  -2510   -849   -503       O  
ATOM   3538  CB  ASN B1211      10.687  58.881  52.165  1.00102.32           C  
ANISOU 3538  CB  ASN B1211    12666  10220  15990  -2676   -508   -155       C  
ATOM   3539  CG  ASN B1211      11.436  59.768  53.143  1.00101.66           C  
ANISOU 3539  CG  ASN B1211    12632  10108  15887  -2768   -346    -49       C  
ATOM   3540  OD1 ASN B1211      11.123  60.952  53.284  1.00102.10           O  
ANISOU 3540  OD1 ASN B1211    12744  10151  15900  -2733   -282      1       O  
ATOM   3541  ND2 ASN B1211      12.402  59.193  53.851  1.00100.84           N  
ANISOU 3541  ND2 ASN B1211    12489  10002  15823  -2870   -281    -37       N  
ATOM   3542  N   LEU B1212       7.512  57.306  52.713  1.00102.57           N  
ANISOU 3542  N   LEU B1212    12259  10202  16511  -2683   -738   -436       N  
ATOM   3543  CA  LEU B1212       6.597  56.224  52.365  1.00103.77           C  
ANISOU 3543  CA  LEU B1212    12205  10318  16906  -2673   -839   -646       C  
ATOM   3544  C   LEU B1212       5.326  56.785  51.735  1.00104.56           C  
ANISOU 3544  C   LEU B1212    12233  10490  17006  -2527   -998   -814       C  
ATOM   3545  O   LEU B1212       4.866  56.280  50.719  1.00106.07           O  
ANISOU 3545  O   LEU B1212    12321  10748  17234  -2403  -1167  -1053       O  
ATOM   3546  CB  LEU B1212       6.257  55.383  53.597  1.00104.68           C  
ANISOU 3546  CB  LEU B1212    12165  10287  17320  -2820   -687   -603       C  
ATOM   3547  CG  LEU B1212       5.134  54.351  53.449  1.00107.16           C  
ANISOU 3547  CG  LEU B1212    12219  10498  17998  -2838   -718   -832       C  
ATOM   3548  CD1 LEU B1212       5.510  53.069  54.160  1.00108.20           C  
ANISOU 3548  CD1 LEU B1212    12257  10469  18383  -2953   -523   -776       C  
ATOM   3549  CD2 LEU B1212       3.807  54.888  53.970  1.00108.71           C  
ANISOU 3549  CD2 LEU B1212    12298  10653  18353  -2831   -715   -881       C  
ATOM   3550  N   VAL B1213       4.760  57.821  52.354  1.00103.67           N  
ANISOU 3550  N   VAL B1213    12162  10378  16851  -2522   -953   -711       N  
ATOM   3551  CA  VAL B1213       3.592  58.531  51.817  1.00104.65           C  
ANISOU 3551  CA  VAL B1213    12245  10587  16929  -2358  -1096   -844       C  
ATOM   3552  C   VAL B1213       3.859  59.003  50.373  1.00105.88           C  
ANISOU 3552  C   VAL B1213    12551  10902  16776  -2103  -1238   -914       C  
ATOM   3553  O   VAL B1213       3.123  58.638  49.446  1.00107.42           O  
ANISOU 3553  O   VAL B1213    12628  11204  16981  -1920  -1436  -1176       O  
ATOM   3554  CB  VAL B1213       3.177  59.717  52.735  1.00103.35           C  
ANISOU 3554  CB  VAL B1213    12153  10398  16718  -2395   -995   -670       C  
ATOM   3555  CG1 VAL B1213       2.049  60.535  52.121  1.00104.50           C  
ANISOU 3555  CG1 VAL B1213    12287  10646  16772  -2197  -1139   -789       C  
ATOM   3556  CG2 VAL B1213       2.764  59.213  54.111  1.00102.43           C  
ANISOU 3556  CG2 VAL B1213    11887  10143  16890  -2584   -860   -614       C  
ATOM   3557  N   VAL B1214       4.929  59.781  50.194  1.00104.72           N  
ANISOU 3557  N   VAL B1214    12650  10768  16370  -2070  -1120   -696       N  
ATOM   3558  CA  VAL B1214       5.351  60.285  48.878  1.00106.17           C  
ANISOU 3558  CA  VAL B1214    13026  11070  16242  -1804  -1172   -691       C  
ATOM   3559  C   VAL B1214       5.496  59.159  47.825  1.00107.71           C  
ANISOU 3559  C   VAL B1214    13141  11355  16428  -1684  -1343   -912       C  
ATOM   3560  O   VAL B1214       5.283  59.387  46.622  1.00109.11           O  
ANISOU 3560  O   VAL B1214    13401  11687  16368  -1372  -1475  -1019       O  
ATOM   3561  CB  VAL B1214       6.654  61.127  49.002  1.00104.88           C  
ANISOU 3561  CB  VAL B1214    13108  10837  15906  -1850   -942   -423       C  
ATOM   3562  CG1 VAL B1214       7.157  61.598  47.646  1.00106.34           C  
ANISOU 3562  CG1 VAL B1214    13511  11103  15788  -1560   -926   -379       C  
ATOM   3563  CG2 VAL B1214       6.432  62.330  49.907  1.00104.25           C  
ANISOU 3563  CG2 VAL B1214    13088  10685  15838  -1927   -788   -258       C  
ATOM   3564  N   ALA B1215       5.831  57.950  48.288  1.00107.08           N  
ANISOU 3564  N   ALA B1215    12902  11186  16599  -1903  -1334   -986       N  
ATOM   3565  CA  ALA B1215       5.979  56.770  47.416  1.00108.53           C  
ANISOU 3565  CA  ALA B1215    12970  11427  16840  -1835  -1481  -1218       C  
ATOM   3566  C   ALA B1215       4.652  56.254  46.867  1.00110.84           C  
ANISOU 3566  C   ALA B1215    13007  11816  17293  -1684  -1716  -1587       C  
ATOM   3567  O   ALA B1215       4.605  55.701  45.771  1.00112.40           O  
ANISOU 3567  O   ALA B1215    13142  12146  17418  -1484  -1898  -1831       O  
ATOM   3568  CB  ALA B1215       6.718  55.649  48.139  1.00107.20           C  
ANISOU 3568  CB  ALA B1215    12706  11111  16915  -2110  -1363  -1173       C  
ATOM   3569  N   ILE B1216       3.584  56.435  47.637  1.00111.48           N  
ANISOU 3569  N   ILE B1216    12923  11834  17602  -1772  -1711  -1652       N  
ATOM   3570  CA  ILE B1216       2.239  56.027  47.217  1.00114.41           C  
ANISOU 3570  CA  ILE B1216    13008  12282  18181  -1642  -1922  -2043       C  
ATOM   3571  C   ILE B1216       1.505  57.182  46.499  1.00116.59           C  
ANISOU 3571  C   ILE B1216    13388  12769  18143  -1302  -2082  -2106       C  
ATOM   3572  O   ILE B1216       0.336  57.045  46.103  1.00118.48           O  
ANISOU 3572  O   ILE B1216    13398  13119  18501  -1136  -2287  -2455       O  
ATOM   3573  CB  ILE B1216       1.396  55.497  48.415  1.00114.14           C  
ANISOU 3573  CB  ILE B1216    12707  12042  18620  -1910  -1806  -2111       C  
ATOM   3574  CG1 ILE B1216       2.249  54.663  49.403  1.00111.75           C  
ANISOU 3574  CG1 ILE B1216    12404  11516  18541  -2214  -1555  -1899       C  
ATOM   3575  CG2 ILE B1216       0.148  54.762  47.930  1.00116.68           C  
ANISOU 3575  CG2 ILE B1216    12659  12396  19276  -1821  -1999  -2596       C  
ATOM   3576  CD1 ILE B1216       2.952  53.452  48.818  1.00112.28           C  
ANISOU 3576  CD1 ILE B1216    12393  11558  18710  -2247  -1580  -2037       C  
ATOM   3577  N   ILE B1217       2.196  58.315  46.332  1.00115.88           N  
ANISOU 3577  N   ILE B1217    13633  12727  17670  -1183  -1971  -1783       N  
ATOM   3578  CA  ILE B1217       1.666  59.450  45.557  1.00117.67           C  
ANISOU 3578  CA  ILE B1217    14021  13147  17541   -805  -2069  -1781       C  
ATOM   3579  C   ILE B1217       2.288  59.519  44.157  1.00119.65           C  
ANISOU 3579  C   ILE B1217    14470  13587  17403   -435  -2157  -1804       C  
ATOM   3580  O   ILE B1217       1.578  59.741  43.170  1.00122.83           O  
ANISOU 3580  O   ILE B1217    14860  14227  17582    -26  -2371  -2033       O  
ATOM   3581  CB  ILE B1217       1.807  60.788  46.310  1.00115.38           C  
ANISOU 3581  CB  ILE B1217    13957  12761  17121   -878  -1845  -1418       C  
ATOM   3582  CG1 ILE B1217       0.732  60.883  47.395  1.00114.99           C  
ANISOU 3582  CG1 ILE B1217    13697  12619  17376  -1077  -1845  -1484       C  
ATOM   3583  CG2 ILE B1217       1.650  61.962  45.358  1.00116.92           C  
ANISOU 3583  CG2 ILE B1217    14407  13125  16891   -454  -1859  -1326       C  
ATOM   3584  CD1 ILE B1217       1.206  61.524  48.683  1.00112.93           C  
ANISOU 3584  CD1 ILE B1217    13546  12167  17194  -1370  -1583  -1148       C  
ATOM   3585  N   VAL B1218       3.605  59.329  44.083  1.00118.07           N  
ANISOU 3585  N   VAL B1218    14452  13294  17116   -552  -1990  -1578       N  
ATOM   3586  CA  VAL B1218       4.302  59.183  42.804  1.00119.34           C  
ANISOU 3586  CA  VAL B1218    14785  13604  16955   -236  -2047  -1598       C  
ATOM   3587  C   VAL B1218       3.669  58.012  42.037  1.00121.98           C  
ANISOU 3587  C   VAL B1218    14834  14114  17397    -74  -2367  -2065       C  
ATOM   3588  O   VAL B1218       3.119  58.192  40.944  1.00124.99           O  
ANISOU 3588  O   VAL B1218    15231  14757  17504    380  -2581  -2287       O  
ATOM   3589  CB  VAL B1218       5.828  58.960  43.005  1.00116.77           C  
ANISOU 3589  CB  VAL B1218    14633  13113  16622   -468  -1813  -1322       C  
ATOM   3590  CG1 VAL B1218       6.505  58.504  41.719  1.00117.82           C  
ANISOU 3590  CG1 VAL B1218    14885  13386  16495   -182  -1893  -1394       C  
ATOM   3591  CG2 VAL B1218       6.494  60.226  43.533  1.00115.34           C  
ANISOU 3591  CG2 VAL B1218    14724  12784  16315   -548  -1501   -926       C  
ATOM   3592  N   ASP B1219       3.719  56.827  42.642  1.00120.96           N  
ANISOU 3592  N   ASP B1219    14434  13844  17682   -425  -2388  -2228       N  
ATOM   3593  CA  ASP B1219       3.211  55.606  42.029  1.00123.09           C  
ANISOU 3593  CA  ASP B1219    14385  14220  18162   -346  -2646  -2697       C  
ATOM   3594  C   ASP B1219       1.686  55.614  41.986  1.00125.70           C  
ANISOU 3594  C   ASP B1219    14417  14670  18675   -201  -2872  -3094       C  
ATOM   3595  O   ASP B1219       1.063  54.684  41.474  1.00128.24           O  
ANISOU 3595  O   ASP B1219    14412  15091  19224   -109  -3105  -3572       O  
ATOM   3596  CB  ASP B1219       3.701  54.385  42.811  1.00121.34           C  
ANISOU 3596  CB  ASP B1219    13968  13756  18378   -782  -2525  -2715       C  
ATOM   3597  CG  ASP B1219       5.217  54.305  42.894  1.00119.29           C  
ANISOU 3597  CG  ASP B1219    13973  13391  17960   -931  -2320  -2362       C  
ATOM   3598  OD1 ASP B1219       5.895  55.360  42.912  1.00118.13           O  
ANISOU 3598  OD1 ASP B1219    14149  13242  17494   -865  -2159  -2007       O  
ATOM   3599  OD2 ASP B1219       5.734  53.171  42.958  1.00119.32           O  
ANISOU 3599  OD2 ASP B1219    13845  13298  18193  -1120  -2301  -2456       O  
TER    3600      ASP B1219                                                      
HETATM 3601  N   MSE C1001      49.241  90.170 132.928  1.00140.39           N  
ANISOU 3601  N   MSE C1001    13383  16375  23584  -3236  -4438    110       N  
HETATM 3602  CA  MSE C1001      48.255  90.686 131.935  1.00139.60           C  
ANISOU 3602  CA  MSE C1001    13334  16275  23431  -3174  -4285    -46       C  
HETATM 3603  C   MSE C1001      47.021  89.810 131.920  1.00137.90           C  
ANISOU 3603  C   MSE C1001    13366  16058  22972  -3121  -4142   -308       C  
HETATM 3604  O   MSE C1001      46.146  89.970 131.059  1.00136.17           O  
ANISOU 3604  O   MSE C1001    13207  15851  22681  -3052  -3993   -435       O  
HETATM 3605  CB  MSE C1001      48.923  90.733 130.557  1.00141.34           C  
ANISOU 3605  CB  MSE C1001    13346  16568  23788  -2989  -4120    183       C  
HETATM 3606  CG  MSE C1001      48.350  91.853 129.689  1.00142.84           C  
ANISOU 3606  CG  MSE C1001    13494  16746  24032  -2998  -4069    114       C  
HETATM 3607 SE   MSE C1001      48.930  91.705 127.809  1.00145.02          SE  
ANISOU 3607 SE   MSE C1001    13564  17119  24418  -2728  -3801    357      SE  
HETATM 3608  CE  MSE C1001      47.974  90.043 127.345  1.00143.76           C  
ANISOU 3608  CE  MSE C1001    13680  16970  23974  -2534  -3548    161       C  
ATOM   3609  N   TYR C1002      46.938  88.888 132.884  1.00137.18           N  
ANISOU 3609  N   TYR C1002    13417  15953  22753  -3166  -4197   -381       N  
ATOM   3610  CA  TYR C1002      45.825  87.924 132.985  1.00134.21           C  
ANISOU 3610  CA  TYR C1002    13279  15580  22137  -3136  -4084   -605       C  
ATOM   3611  C   TYR C1002      44.521  88.581 133.461  1.00132.06           C  
ANISOU 3611  C   TYR C1002    13161  15277  21738  -3272  -4129   -877       C  
ATOM   3612  O   TYR C1002      43.469  88.432 132.835  1.00127.97           O  
ANISOU 3612  O   TYR C1002    12747  14783  21094  -3222  -3987  -1028       O  
ATOM   3613  CB  TYR C1002      46.221  86.771 133.917  1.00134.40           C  
ANISOU 3613  CB  TYR C1002    13398  15597  22072  -3150  -4145   -578       C  
ATOM   3614  CG  TYR C1002      45.291  85.574 133.905  1.00132.48           C  
ANISOU 3614  CG  TYR C1002    13386  15360  21590  -3100  -4024   -749       C  
ATOM   3615  CD1 TYR C1002      45.364  84.620 132.891  1.00131.55           C  
ANISOU 3615  CD1 TYR C1002    13306  15266  21411  -2907  -3836   -679       C  
ATOM   3616  CD2 TYR C1002      44.355  85.383 134.925  1.00131.75           C  
ANISOU 3616  CD2 TYR C1002    13486  15248  21326  -3247  -4104   -969       C  
ATOM   3617  CE1 TYR C1002      44.518  83.521 132.882  1.00131.36           C  
ANISOU 3617  CE1 TYR C1002    13514  15235  21163  -2881  -3748   -826       C  
ATOM   3618  CE2 TYR C1002      43.507  84.284 134.928  1.00130.64           C  
ANISOU 3618  CE2 TYR C1002    13550  15118  20968  -3222  -4008  -1105       C  
ATOM   3619  CZ  TYR C1002      43.590  83.355 133.904  1.00130.85           C  
ANISOU 3619  CZ  TYR C1002    13619  15157  20939  -3048  -3840  -1033       C  
ATOM   3620  OH  TYR C1002      42.752  82.255 133.895  1.00129.68           O  
ANISOU 3620  OH  TYR C1002    13695  15007  20569  -3040  -3766  -1159       O  
ATOM   3621  N   LEU C1003      44.613  89.313 134.572  1.00133.41           N  
ANISOU 3621  N   LEU C1003    13351  15397  21941  -3440  -4331   -926       N  
ATOM   3622  CA  LEU C1003      43.487  90.061 135.143  1.00131.64           C  
ANISOU 3622  CA  LEU C1003    13271  15141  21604  -3558  -4388  -1164       C  
ATOM   3623  C   LEU C1003      43.085  91.259 134.268  1.00130.43           C  
ANISOU 3623  C   LEU C1003    13040  14982  21536  -3534  -4339  -1194       C  
ATOM   3624  O   LEU C1003      41.908  91.614 134.203  1.00128.86           O  
ANISOU 3624  O   LEU C1003    12955  14791  21214  -3549  -4278  -1393       O  
ATOM   3625  CB  LEU C1003      43.839  90.531 136.565  1.00132.19           C  
ANISOU 3625  CB  LEU C1003    13401  15140  21684  -3728  -4626  -1186       C  
ATOM   3626  CG  LEU C1003      44.392  89.492 137.555  1.00131.95           C  
ANISOU 3626  CG  LEU C1003    13434  15105  21597  -3774  -4716  -1135       C  
ATOM   3627  CD1 LEU C1003      45.237  90.172 138.622  1.00133.51           C  
ANISOU 3627  CD1 LEU C1003    13604  15224  21900  -3928  -4973  -1046       C  
ATOM   3628  CD2 LEU C1003      43.293  88.630 138.178  1.00129.55           C  
ANISOU 3628  CD2 LEU C1003    13351  14826  21044  -3798  -4655  -1353       C  
ATOM   3629  N   ARG C1004      44.076  91.865 133.607  1.00130.80           N  
ANISOU 3629  N   ARG C1004    12884  15020  21793  -3498  -4366   -983       N  
ATOM   3630  CA  ARG C1004      43.881  92.991 132.689  1.00129.41           C  
ANISOU 3630  CA  ARG C1004    12611  14837  21724  -3471  -4325   -971       C  
ATOM   3631  C   ARG C1004      43.045  92.635 131.455  1.00128.14           C  
ANISOU 3631  C   ARG C1004    12468  14737  21481  -3326  -4087  -1048       C  
ATOM   3632  O   ARG C1004      42.258  93.462 130.973  1.00126.49           O  
ANISOU 3632  O   ARG C1004    12280  14523  21260  -3327  -4043  -1162       O  
ATOM   3633  CB  ARG C1004      45.234  93.535 132.228  1.00130.52           C  
ANISOU 3633  CB  ARG C1004    12512  14971  22107  -3460  -4401   -687       C  
ATOM   3634  CG  ARG C1004      45.132  94.858 131.487  1.00131.53           C  
ANISOU 3634  CG  ARG C1004    12544  15072  22359  -3474  -4413   -665       C  
ATOM   3635  CD  ARG C1004      46.289  95.109 130.529  1.00132.72           C  
ANISOU 3635  CD  ARG C1004    12436  15264  22726  -3397  -4384   -369       C  
ATOM   3636  NE  ARG C1004      45.822  95.906 129.390  1.00132.41           N  
ANISOU 3636  NE  ARG C1004    12338  15234  22736  -3332  -4272   -394       N  
ATOM   3637  CZ  ARG C1004      46.573  96.307 128.370  1.00132.58           C  
ANISOU 3637  CZ  ARG C1004    12147  15296  22931  -3256  -4216   -170       C  
ATOM   3638  NH1 ARG C1004      47.867  96.004 128.320  1.00134.52           N  
ANISOU 3638  NH1 ARG C1004    12196  15588  23325  -3229  -4257    116       N  
ATOM   3639  NH2 ARG C1004      46.019  97.022 127.397  1.00131.17           N  
ANISOU 3639  NH2 ARG C1004    11945  15119  22776  -3205  -4118   -224       N  
ATOM   3640  N   ILE C1005      43.231  91.411 130.950  1.00127.67           N  
ANISOU 3640  N   ILE C1005    12416  14730  21362  -3201  -3943   -980       N  
ATOM   3641  CA  ILE C1005      42.576  90.942 129.716  1.00125.13           C  
ANISOU 3641  CA  ILE C1005    12128  14457  20960  -3058  -3726  -1021       C  
ATOM   3642  C   ILE C1005      41.206  90.302 129.971  1.00122.22           C  
ANISOU 3642  C   ILE C1005    11976  14108  20353  -3087  -3654  -1259       C  
ATOM   3643  O   ILE C1005      40.303  90.430 129.148  1.00120.44           O  
ANISOU 3643  O   ILE C1005    11795  13910  20057  -3039  -3529  -1355       O  
ATOM   3644  CB  ILE C1005      43.507  90.012 128.882  1.00126.02           C  
ANISOU 3644  CB  ILE C1005    12153  14604  21126  -2884  -3598   -809       C  
ATOM   3645  CG1 ILE C1005      43.138  90.051 127.394  1.00124.98           C  
ANISOU 3645  CG1 ILE C1005    11997  14502  20989  -2736  -3402   -791       C  
ATOM   3646  CG2 ILE C1005      43.524  88.584 129.430  1.00127.02           C  
ANISOU 3646  CG2 ILE C1005    12428  14735  21098  -2853  -3574   -833       C  
ATOM   3647  CD1 ILE C1005      44.277  89.673 126.466  1.00125.74           C  
ANISOU 3647  CD1 ILE C1005    11944  14628  21203  -2555  -3292   -533       C  
ATOM   3648  N   THR C1006      41.066  89.632 131.116  1.00122.09           N  
ANISOU 3648  N   THR C1006    12087  14083  20218  -3173  -3741  -1338       N  
ATOM   3649  CA  THR C1006      39.830  88.945 131.512  1.00121.00           C  
ANISOU 3649  CA  THR C1006    12148  13976  19851  -3220  -3693  -1539       C  
ATOM   3650  C   THR C1006      38.643  89.909 131.576  1.00120.95           C  
ANISOU 3650  C   THR C1006    12186  13988  19783  -3289  -3692  -1720       C  
ATOM   3651  O   THR C1006      37.519  89.552 131.202  1.00119.94           O  
ANISOU 3651  O   THR C1006    12157  13912  19503  -3278  -3584  -1843       O  
ATOM   3652  CB  THR C1006      39.995  88.240 132.880  1.00121.39           C  
ANISOU 3652  CB  THR C1006    12308  14010  19804  -3320  -3816  -1579       C  
ATOM   3653  OG1 THR C1006      41.097  87.324 132.826  1.00122.09           O  
ANISOU 3653  OG1 THR C1006    12355  14085  19947  -3243  -3814  -1404       O  
ATOM   3654  CG2 THR C1006      38.732  87.485 133.272  1.00120.47           C  
ANISOU 3654  CG2 THR C1006    12385  13938  19448  -3373  -3764  -1764       C  
ATOM   3655  N   ASN C1007      38.907  91.132 132.035  1.00121.63           N  
ANISOU 3655  N   ASN C1007    12201  14028  19985  -3358  -3817  -1724       N  
ATOM   3656  CA  ASN C1007      37.879  92.168 132.150  1.00121.03           C  
ANISOU 3656  CA  ASN C1007    12169  13956  19859  -3404  -3825  -1885       C  
ATOM   3657  C   ASN C1007      37.377  92.750 130.819  1.00120.23           C  
ANISOU 3657  C   ASN C1007    11991  13883  19808  -3315  -3690  -1887       C  
ATOM   3658  O   ASN C1007      36.382  93.476 130.798  1.00119.65           O  
ANISOU 3658  O   ASN C1007    11960  13830  19671  -3332  -3667  -2023       O  
ATOM   3659  CB  ASN C1007      38.350  93.272 133.097  1.00121.25           C  
ANISOU 3659  CB  ASN C1007    12188  13902  19978  -3504  -4017  -1890       C  
ATOM   3660  CG  ASN C1007      38.721  92.736 134.463  1.00122.24           C  
ANISOU 3660  CG  ASN C1007    12414  13999  20035  -3602  -4157  -1907       C  
ATOM   3661  OD1 ASN C1007      38.415  91.587 134.790  1.00120.17           O  
ANISOU 3661  OD1 ASN C1007    12242  13785  19632  -3602  -4103  -1949       O  
ATOM   3662  ND2 ASN C1007      39.392  93.563 135.270  1.00124.88           N  
ANISOU 3662  ND2 ASN C1007    12743  14244  20462  -3694  -4348  -1869       N  
ATOM   3663  N   ILE C1008      38.056  92.429 129.719  1.00120.26           N  
ANISOU 3663  N   ILE C1008    11884  13893  19918  -3211  -3597  -1731       N  
ATOM   3664  CA  ILE C1008      37.583  92.823 128.392  1.00120.94           C  
ANISOU 3664  CA  ILE C1008    11911  14007  20035  -3120  -3457  -1726       C  
ATOM   3665  C   ILE C1008      36.614  91.765 127.827  1.00122.70           C  
ANISOU 3665  C   ILE C1008    12254  14293  20071  -3072  -3307  -1807       C  
ATOM   3666  O   ILE C1008      35.922  92.009 126.824  1.00122.07           O  
ANISOU 3666  O   ILE C1008    12166  14246  19969  -3017  -3193  -1841       O  
ATOM   3667  CB  ILE C1008      38.736  93.089 127.387  1.00120.58           C  
ANISOU 3667  CB  ILE C1008    11689  13938  20188  -3022  -3420  -1512       C  
ATOM   3668  CG1 ILE C1008      39.987  93.637 128.079  1.00120.95           C  
ANISOU 3668  CG1 ILE C1008    11618  13929  20408  -3083  -3588  -1368       C  
ATOM   3669  CG2 ILE C1008      38.287  94.065 126.302  1.00120.38           C  
ANISOU 3669  CG2 ILE C1008    11587  13919  20234  -2971  -3341  -1523       C  
ATOM   3670  CD1 ILE C1008      41.232  93.570 127.213  1.00120.47           C  
ANISOU 3670  CD1 ILE C1008    11374  13874  20525  -2979  -3543  -1117       C  
ATOM   3671  N   VAL C1009      36.556  90.602 128.488  1.00124.07           N  
ANISOU 3671  N   VAL C1009    12549  14482  20109  -3104  -3319  -1834       N  
ATOM   3672  CA  VAL C1009      35.702  89.481 128.059  1.00122.83           C  
ANISOU 3672  CA  VAL C1009    12533  14373  19762  -3082  -3207  -1896       C  
ATOM   3673  C   VAL C1009      34.447  89.360 128.933  1.00122.61           C  
ANISOU 3673  C   VAL C1009    12629  14405  19551  -3198  -3239  -2073       C  
ATOM   3674  O   VAL C1009      33.367  89.796 128.535  1.00121.93           O  
ANISOU 3674  O   VAL C1009    12555  14376  19398  -3211  -3178  -2167       O  
ATOM   3675  CB  VAL C1009      36.470  88.131 128.063  1.00122.93           C  
ANISOU 3675  CB  VAL C1009    12618  14360  19729  -3024  -3186  -1789       C  
ATOM   3676  CG1 VAL C1009      35.653  87.056 127.351  1.00122.40           C  
ANISOU 3676  CG1 VAL C1009    12711  14319  19476  -2991  -3071  -1831       C  
ATOM   3677  CG2 VAL C1009      37.852  88.275 127.425  1.00122.57           C  
ANISOU 3677  CG2 VAL C1009    12429  14270  19873  -2901  -3164  -1588       C  
ATOM   3678  N   GLU C1010      34.614  88.779 130.125  1.00123.71           N  
ANISOU 3678  N   GLU C1010    12852  14541  19612  -3278  -3333  -2106       N  
ATOM   3679  CA  GLU C1010      33.531  88.508 131.087  1.00123.70           C  
ANISOU 3679  CA  GLU C1010    12971  14604  19424  -3387  -3366  -2253       C  
ATOM   3680  C   GLU C1010      32.550  89.666 131.324  1.00124.89           C  
ANISOU 3680  C   GLU C1010    13093  14806  19553  -3423  -3368  -2377       C  
ATOM   3681  O   GLU C1010      31.450  89.451 131.841  1.00124.78           O  
ANISOU 3681  O   GLU C1010    13163  14877  19371  -3487  -3351  -2486       O  
ATOM   3682  CB  GLU C1010      34.141  88.092 132.432  1.00124.21           C  
ANISOU 3682  CB  GLU C1010    13095  14636  19465  -3463  -3496  -2253       C  
ATOM   3683  CG  GLU C1010      34.998  89.179 133.088  1.00123.81           C  
ANISOU 3683  CG  GLU C1010    12952  14514  19576  -3484  -3625  -2224       C  
ATOM   3684  CD  GLU C1010      35.575  88.779 134.434  1.00123.68           C  
ANISOU 3684  CD  GLU C1010    13003  14460  19529  -3569  -3765  -2223       C  
ATOM   3685  OE1 GLU C1010      35.634  87.565 134.743  1.00123.56           O  
ANISOU 3685  OE1 GLU C1010    13080  14460  19405  -3589  -3758  -2207       O  
ATOM   3686  OE2 GLU C1010      35.980  89.694 135.182  1.00123.67           O  
ANISOU 3686  OE2 GLU C1010    12977  14404  19609  -3621  -3892  -2236       O  
ATOM   3687  N   SER C1011      32.971  90.883 130.973  1.00126.15           N  
ANISOU 3687  N   SER C1011    13137  14915  19878  -3378  -3391  -2350       N  
ATOM   3688  CA  SER C1011      32.169  92.094 131.152  1.00126.03           C  
ANISOU 3688  CA  SER C1011    13101  14926  19857  -3387  -3397  -2458       C  
ATOM   3689  C   SER C1011      30.952  92.088 130.236  1.00124.48           C  
ANISOU 3689  C   SER C1011    12902  14826  19570  -3352  -3260  -2510       C  
ATOM   3690  O   SER C1011      31.015  91.564 129.123  1.00124.54           O  
ANISOU 3690  O   SER C1011    12884  14840  19597  -3301  -3169  -2436       O  
ATOM   3691  CB  SER C1011      33.021  93.345 130.899  1.00127.41           C  
ANISOU 3691  CB  SER C1011    13164  15006  20239  -3351  -3467  -2395       C  
ATOM   3692  OG  SER C1011      33.533  93.369 129.574  1.00127.63           O  
ANISOU 3692  OG  SER C1011    13081  15015  20397  -3267  -3386  -2275       O  
ATOM   3693  N   SER C1012      29.857  92.679 130.709  1.00123.99           N  
ANISOU 3693  N   SER C1012    12870  14836  19403  -3374  -3248  -2629       N  
ATOM   3694  CA  SER C1012      28.581  92.652 129.999  1.00124.59           C  
ANISOU 3694  CA  SER C1012    12937  15027  19375  -3357  -3129  -2673       C  
ATOM   3695  C   SER C1012      28.659  93.261 128.598  1.00126.51           C  
ANISOU 3695  C   SER C1012    13077  15244  19748  -3274  -3053  -2614       C  
ATOM   3696  O   SER C1012      27.948  92.805 127.686  1.00125.04           O  
ANISOU 3696  O   SER C1012    12889  15126  19494  -3263  -2954  -2597       O  
ATOM   3697  CB  SER C1012      27.475  93.327 130.821  1.00123.31           C  
ANISOU 3697  CB  SER C1012    12807  14954  19093  -3371  -3127  -2794       C  
ATOM   3698  OG  SER C1012      27.427  94.728 130.573  1.00122.14           O  
ANISOU 3698  OG  SER C1012    12595  14763  19050  -3298  -3132  -2828       O  
ATOM   3699  N   PHE C1013      29.518  94.274 128.429  1.00128.33           N  
ANISOU 3699  N   PHE C1013    13228  15373  20159  -3226  -3107  -2577       N  
ATOM   3700  CA  PHE C1013      29.702  94.914 127.120  1.00131.81           C  
ANISOU 3700  CA  PHE C1013    13564  15782  20736  -3147  -3041  -2510       C  
ATOM   3701  C   PHE C1013      30.130  93.937 126.025  1.00133.15           C  
ANISOU 3701  C   PHE C1013    13722  15944  20926  -3108  -2959  -2398       C  
ATOM   3702  O   PHE C1013      29.514  93.907 124.952  1.00134.43           O  
ANISOU 3702  O   PHE C1013    13865  16148  21063  -3068  -2858  -2386       O  
ATOM   3703  CB  PHE C1013      30.682  96.095 127.159  1.00133.53           C  
ANISOU 3703  CB  PHE C1013    13699  15886  21149  -3119  -3132  -2464       C  
ATOM   3704  CG  PHE C1013      31.101  96.572 125.785  1.00134.20           C  
ANISOU 3704  CG  PHE C1013    13668  15934  21386  -3042  -3068  -2362       C  
ATOM   3705  CD1 PHE C1013      30.152  97.037 124.865  1.00134.02           C  
ANISOU 3705  CD1 PHE C1013    13614  15968  21339  -2994  -2966  -2402       C  
ATOM   3706  CD2 PHE C1013      32.438  96.540 125.404  1.00135.66           C  
ANISOU 3706  CD2 PHE C1013    13770  16039  21737  -3015  -3105  -2215       C  
ATOM   3707  CE1 PHE C1013      30.532  97.461 123.598  1.00133.69           C  
ANISOU 3707  CE1 PHE C1013    13474  15893  21430  -2924  -2906  -2308       C  
ATOM   3708  CE2 PHE C1013      32.824  96.969 124.139  1.00135.87           C  
ANISOU 3708  CE2 PHE C1013    13686  16041  21895  -2939  -3036  -2112       C  
ATOM   3709  CZ  PHE C1013      31.870  97.429 123.236  1.00134.41           C  
ANISOU 3709  CZ  PHE C1013    13487  15904  21681  -2894  -2937  -2164       C  
ATOM   3710  N   PHE C1014      31.183  93.158 126.286  1.00132.52           N  
ANISOU 3710  N   PHE C1014    13663  15806  20884  -3112  -3002  -2312       N  
ATOM   3711  CA  PHE C1014      31.649  92.169 125.316  1.00131.29           C  
ANISOU 3711  CA  PHE C1014    13527  15632  20727  -3051  -2920  -2202       C  
ATOM   3712  C   PHE C1014      30.465  91.383 124.783  1.00131.49           C  
ANISOU 3712  C   PHE C1014    13655  15737  20570  -3074  -2830  -2254       C  
ATOM   3713  O   PHE C1014      30.254  91.344 123.571  1.00132.32           O  
ANISOU 3713  O   PHE C1014    13749  15842  20684  -3013  -2739  -2208       O  
ATOM   3714  CB  PHE C1014      32.689  91.231 125.924  1.00131.70           C  
ANISOU 3714  CB  PHE C1014    13624  15633  20784  -3056  -2978  -2124       C  
ATOM   3715  CG  PHE C1014      33.324  90.295 124.929  1.00131.58           C  
ANISOU 3715  CG  PHE C1014    13635  15583  20775  -2959  -2890  -1997       C  
ATOM   3716  CD1 PHE C1014      34.276  90.756 124.022  1.00132.46           C  
ANISOU 3716  CD1 PHE C1014    13625  15645  21059  -2848  -2846  -1861       C  
ATOM   3717  CD2 PHE C1014      32.984  88.949 124.907  1.00131.49           C  
ANISOU 3717  CD2 PHE C1014    13784  15585  20590  -2972  -2853  -2006       C  
ATOM   3718  CE1 PHE C1014      34.869  89.894 123.110  1.00131.99           C  
ANISOU 3718  CE1 PHE C1014    13605  15556  20992  -2732  -2750  -1740       C  
ATOM   3719  CE2 PHE C1014      33.574  88.083 123.997  1.00131.35           C  
ANISOU 3719  CE2 PHE C1014    13827  15520  20559  -2863  -2771  -1893       C  
ATOM   3720  CZ  PHE C1014      34.518  88.555 123.097  1.00131.59           C  
ANISOU 3720  CZ  PHE C1014    13737  15506  20756  -2732  -2712  -1761       C  
ATOM   3721  N   THR C1015      29.686  90.799 125.702  1.00131.64           N  
ANISOU 3721  N   THR C1015    13772  15824  20421  -3170  -2865  -2342       N  
ATOM   3722  CA  THR C1015      28.443  90.073 125.378  1.00130.01           C  
ANISOU 3722  CA  THR C1015    13660  15710  20026  -3228  -2807  -2385       C  
ATOM   3723  C   THR C1015      27.505  90.912 124.502  1.00128.24           C  
ANISOU 3723  C   THR C1015    13361  15549  19816  -3203  -2734  -2413       C  
ATOM   3724  O   THR C1015      26.997  90.428 123.491  1.00126.89           O  
ANISOU 3724  O   THR C1015    13236  15400  19578  -3197  -2666  -2376       O  
ATOM   3725  CB  THR C1015      27.676  89.636 126.654  1.00130.37           C  
ANISOU 3725  CB  THR C1015    13782  15844  19908  -3343  -2864  -2473       C  
ATOM   3726  OG1 THR C1015      28.595  89.162 127.646  1.00131.12           O  
ANISOU 3726  OG1 THR C1015    13925  15877  20018  -3366  -2950  -2461       O  
ATOM   3727  CG2 THR C1015      26.670  88.535 126.339  1.00130.16           C  
ANISOU 3727  CG2 THR C1015    13871  15900  19685  -3423  -2827  -2470       C  
ATOM   3728  N   LYS C1016      27.300  92.172 124.895  1.00127.41           N  
ANISOU 3728  N   LYS C1016    13156  15462  19793  -3184  -2757  -2475       N  
ATOM   3729  CA  LYS C1016      26.409  93.086 124.176  1.00125.93           C  
ANISOU 3729  CA  LYS C1016    12889  15335  19623  -3150  -2693  -2505       C  
ATOM   3730  C   LYS C1016      27.017  93.579 122.860  1.00125.47           C  
ANISOU 3730  C   LYS C1016    12755  15197  19719  -3057  -2639  -2423       C  
ATOM   3731  O   LYS C1016      26.333  94.219 122.057  1.00124.40           O  
ANISOU 3731  O   LYS C1016    12563  15103  19601  -3025  -2580  -2432       O  
ATOM   3732  CB  LYS C1016      25.988  94.266 125.069  1.00125.67           C  
ANISOU 3732  CB  LYS C1016    12802  15336  19610  -3144  -2734  -2601       C  
ATOM   3733  CG  LYS C1016      25.152  93.862 126.281  1.00124.97           C  
ANISOU 3733  CG  LYS C1016    12782  15354  19345  -3221  -2761  -2681       C  
ATOM   3734  CD  LYS C1016      24.099  94.899 126.627  1.00123.95           C  
ANISOU 3734  CD  LYS C1016    12606  15321  19170  -3188  -2733  -2764       C  
ATOM   3735  CE  LYS C1016      23.048  94.306 127.551  1.00124.48           C  
ANISOU 3735  CE  LYS C1016    12726  15537  19033  -3258  -2722  -2812       C  
ATOM   3736  NZ  LYS C1016      21.751  95.052 127.507  1.00124.10           N  
ANISOU 3736  NZ  LYS C1016    12613  15629  18909  -3215  -2650  -2852       N  
ATOM   3737  N   PHE C1017      28.297  93.274 122.644  1.00125.39           N  
ANISOU 3737  N   PHE C1017    12741  15084  19818  -3008  -2657  -2334       N  
ATOM   3738  CA  PHE C1017      28.954  93.581 121.378  1.00126.29           C  
ANISOU 3738  CA  PHE C1017    12788  15130  20065  -2911  -2594  -2233       C  
ATOM   3739  C   PHE C1017      28.747  92.470 120.345  1.00126.95           C  
ANISOU 3739  C   PHE C1017    12977  15215  20043  -2887  -2508  -2172       C  
ATOM   3740  O   PHE C1017      28.570  92.749 119.153  1.00127.99           O  
ANISOU 3740  O   PHE C1017    13084  15338  20210  -2827  -2432  -2129       O  
ATOM   3741  CB  PHE C1017      30.451  93.864 121.573  1.00127.25           C  
ANISOU 3741  CB  PHE C1017    12833  15154  20363  -2857  -2646  -2138       C  
ATOM   3742  CG  PHE C1017      31.172  94.188 120.293  1.00128.56           C  
ANISOU 3742  CG  PHE C1017    12915  15264  20667  -2749  -2574  -2015       C  
ATOM   3743  CD1 PHE C1017      30.876  95.354 119.586  1.00129.97           C  
ANISOU 3743  CD1 PHE C1017    12992  15443  20946  -2715  -2546  -2021       C  
ATOM   3744  CD2 PHE C1017      32.128  93.319 119.779  1.00129.66           C  
ANISOU 3744  CD2 PHE C1017    13082  15355  20827  -2671  -2527  -1888       C  
ATOM   3745  CE1 PHE C1017      31.525  95.650 118.394  1.00131.34           C  
ANISOU 3745  CE1 PHE C1017    13088  15574  21243  -2617  -2476  -1901       C  
ATOM   3746  CE2 PHE C1017      32.782  93.609 118.588  1.00131.66           C  
ANISOU 3746  CE2 PHE C1017    13258  15569  21197  -2557  -2446  -1764       C  
ATOM   3747  CZ  PHE C1017      32.482  94.777 117.894  1.00132.07           C  
ANISOU 3747  CZ  PHE C1017    13203  15626  21353  -2536  -2422  -1770       C  
ATOM   3748  N   ILE C1018      28.777  91.218 120.802  1.00125.63           N  
ANISOU 3748  N   ILE C1018    12946  15048  19739  -2935  -2528  -2168       N  
ATOM   3749  CA  ILE C1018      28.624  90.067 119.917  1.00124.24           C  
ANISOU 3749  CA  ILE C1018    12919  14850  19438  -2916  -2467  -2112       C  
ATOM   3750  C   ILE C1018      27.205  90.031 119.371  1.00122.84           C  
ANISOU 3750  C   ILE C1018    12789  14758  19128  -2990  -2435  -2162       C  
ATOM   3751  O   ILE C1018      26.996  89.983 118.153  1.00121.25           O  
ANISOU 3751  O   ILE C1018    12623  14533  18915  -2942  -2367  -2113       O  
ATOM   3752  CB  ILE C1018      28.898  88.733 120.645  1.00125.52           C  
ANISOU 3752  CB  ILE C1018    13236  14988  19466  -2965  -2513  -2104       C  
ATOM   3753  CG1 ILE C1018      30.153  88.822 121.518  1.00123.93           C  
ANISOU 3753  CG1 ILE C1018    12970  14730  19387  -2924  -2571  -2067       C  
ATOM   3754  CG2 ILE C1018      28.993  87.584 119.639  1.00126.28           C  
ANISOU 3754  CG2 ILE C1018    13515  15021  19446  -2913  -2453  -2030       C  
ATOM   3755  CD1 ILE C1018      30.031  88.042 122.808  1.00123.47           C  
ANISOU 3755  CD1 ILE C1018    13006  14696  19210  -3027  -2657  -2121       C  
ATOM   3756  N   ILE C1019      26.243  90.063 120.293  1.00122.02           N  
ANISOU 3756  N   ILE C1019    12682  14758  18923  -3105  -2485  -2248       N  
ATOM   3757  CA  ILE C1019      24.817  90.029 119.965  1.00122.63           C  
ANISOU 3757  CA  ILE C1019    12779  14948  18869  -3192  -2468  -2280       C  
ATOM   3758  C   ILE C1019      24.428  91.217 119.073  1.00122.78           C  
ANISOU 3758  C   ILE C1019    12665  14990  18996  -3129  -2409  -2280       C  
ATOM   3759  O   ILE C1019      23.489  91.133 118.273  1.00120.21           O  
ANISOU 3759  O   ILE C1019    12362  14722  18590  -3167  -2375  -2263       O  
ATOM   3760  CB  ILE C1019      23.957  89.972 121.247  1.00121.44           C  
ANISOU 3760  CB  ILE C1019    12615  14922  18606  -3306  -2524  -2358       C  
ATOM   3761  CG1 ILE C1019      24.497  88.883 122.184  1.00120.53           C  
ANISOU 3761  CG1 ILE C1019    12623  14769  18405  -3362  -2588  -2357       C  
ATOM   3762  CG2 ILE C1019      22.495  89.709 120.902  1.00123.19           C  
ANISOU 3762  CG2 ILE C1019    12857  15277  18674  -3408  -2509  -2355       C  
ATOM   3763  CD1 ILE C1019      23.823  88.806 123.542  1.00120.82           C  
ANISOU 3763  CD1 ILE C1019    12651  14919  18336  -3464  -2644  -2428       C  
ATOM   3764  N   TYR C1020      25.182  92.308 119.220  1.00124.27           N  
ANISOU 3764  N   TYR C1020    12723  15127  19367  -3040  -2409  -2291       N  
ATOM   3765  CA  TYR C1020      25.077  93.495 118.371  1.00124.23           C  
ANISOU 3765  CA  TYR C1020    12595  15114  19493  -2964  -2361  -2283       C  
ATOM   3766  C   TYR C1020      25.460  93.187 116.922  1.00124.35           C  
ANISOU 3766  C   TYR C1020    12655  15055  19538  -2892  -2290  -2190       C  
ATOM   3767  O   TYR C1020      24.923  93.788 115.991  1.00125.22           O  
ANISOU 3767  O   TYR C1020    12714  15187  19677  -2865  -2241  -2178       O  
ATOM   3768  CB  TYR C1020      25.967  94.613 118.935  1.00122.44           C  
ANISOU 3768  CB  TYR C1020    12248  14826  19449  -2900  -2403  -2301       C  
ATOM   3769  CG  TYR C1020      26.178  95.810 118.029  1.00121.97           C  
ANISOU 3769  CG  TYR C1020    12070  14724  19548  -2814  -2365  -2271       C  
ATOM   3770  CD1 TYR C1020      25.161  96.746 117.829  1.00122.91           C  
ANISOU 3770  CD1 TYR C1020    12120  14916  19665  -2812  -2344  -2329       C  
ATOM   3771  CD2 TYR C1020      27.406  96.024 117.395  1.00121.15           C  
ANISOU 3771  CD2 TYR C1020    11917  14515  19600  -2729  -2349  -2174       C  
ATOM   3772  CE1 TYR C1020      25.352  97.851 117.009  1.00122.55           C  
ANISOU 3772  CE1 TYR C1020    11975  14826  19764  -2736  -2317  -2303       C  
ATOM   3773  CE2 TYR C1020      27.606  97.126 116.575  1.00121.13           C  
ANISOU 3773  CE2 TYR C1020    11805  14477  19743  -2660  -2321  -2138       C  
ATOM   3774  CZ  TYR C1020      26.576  98.034 116.388  1.00121.94           C  
ANISOU 3774  CZ  TYR C1020    11855  14640  19838  -2667  -2309  -2208       C  
ATOM   3775  OH  TYR C1020      26.761  99.130 115.581  1.00122.42           O  
ANISOU 3775  OH  TYR C1020    11816  14659  20039  -2602  -2286  -2174       O  
ATOM   3776  N   LEU C1021      26.386  92.249 116.743  1.00124.19           N  
ANISOU 3776  N   LEU C1021    12738  14946  19501  -2852  -2282  -2121       N  
ATOM   3777  CA  LEU C1021      26.931  91.954 115.427  1.00124.70           C  
ANISOU 3777  CA  LEU C1021    12860  14927  19593  -2752  -2205  -2024       C  
ATOM   3778  C   LEU C1021      26.130  90.851 114.748  1.00124.97           C  
ANISOU 3778  C   LEU C1021    13089  14969  19427  -2810  -2185  -2009       C  
ATOM   3779  O   LEU C1021      25.800  90.960 113.568  1.00126.35           O  
ANISOU 3779  O   LEU C1021    13300  15125  19585  -2775  -2129  -1969       O  
ATOM   3780  CB  LEU C1021      28.411  91.568 115.534  1.00125.95           C  
ANISOU 3780  CB  LEU C1021    13027  14987  19842  -2649  -2195  -1938       C  
ATOM   3781  CG  LEU C1021      29.416  92.064 114.484  1.00126.89           C  
ANISOU 3781  CG  LEU C1021    13067  15031  20115  -2499  -2116  -1825       C  
ATOM   3782  CD1 LEU C1021      29.549  93.584 114.503  1.00127.04           C  
ANISOU 3782  CD1 LEU C1021    12875  15069  20326  -2484  -2133  -1836       C  
ATOM   3783  CD2 LEU C1021      30.778  91.421 114.712  1.00126.92           C  
ANISOU 3783  CD2 LEU C1021    13092  14963  20168  -2402  -2105  -1723       C  
ATOM   3784  N   ILE C1022      25.801  89.805 115.503  1.00123.61           N  
ANISOU 3784  N   ILE C1022    13051  14820  19097  -2909  -2243  -2037       N  
ATOM   3785  CA  ILE C1022      25.072  88.647 114.971  1.00121.88           C  
ANISOU 3785  CA  ILE C1022    13047  14594  18669  -2989  -2254  -2014       C  
ATOM   3786  C   ILE C1022      23.768  89.029 114.254  1.00120.58           C  
ANISOU 3786  C   ILE C1022    12861  14514  18440  -3072  -2248  -2023       C  
ATOM   3787  O   ILE C1022      23.607  88.743 113.071  1.00122.11           O  
ANISOU 3787  O   ILE C1022    13169  14650  18576  -3045  -2211  -1968       O  
ATOM   3788  CB  ILE C1022      24.803  87.586 116.071  1.00121.66           C  
ANISOU 3788  CB  ILE C1022    13143  14596  18486  -3111  -2336  -2047       C  
ATOM   3789  CG1 ILE C1022      26.115  86.975 116.576  1.00121.87           C  
ANISOU 3789  CG1 ILE C1022    13236  14520  18550  -3021  -2341  -2016       C  
ATOM   3790  CG2 ILE C1022      23.870  86.493 115.564  1.00122.64           C  
ANISOU 3790  CG2 ILE C1022    13486  14725  18387  -3231  -2374  -2019       C  
ATOM   3791  CD1 ILE C1022      26.937  86.259 115.521  1.00122.38           C  
ANISOU 3791  CD1 ILE C1022    13468  14446  18583  -2886  -2276  -1924       C  
ATOM   3792  N   VAL C1023      22.851  89.672 114.973  1.00118.52           N  
ANISOU 3792  N   VAL C1023    12459  14391  18182  -3164  -2283  -2086       N  
ATOM   3793  CA  VAL C1023      21.574  90.119 114.418  1.00116.62           C  
ANISOU 3793  CA  VAL C1023    12161  14259  17892  -3239  -2278  -2085       C  
ATOM   3794  C   VAL C1023      21.779  91.035 113.199  1.00117.15           C  
ANISOU 3794  C   VAL C1023    12148  14275  18089  -3127  -2205  -2053       C  
ATOM   3795  O   VAL C1023      21.004  90.975 112.232  1.00114.71           O  
ANISOU 3795  O   VAL C1023    11887  13988  17709  -3170  -2195  -2012       O  
ATOM   3796  CB  VAL C1023      20.720  90.821 115.497  1.00115.57           C  
ANISOU 3796  CB  VAL C1023    11860  14286  17764  -3308  -2306  -2153       C  
ATOM   3797  CG1 VAL C1023      19.328  91.140 114.972  1.00117.00           C  
ANISOU 3797  CG1 VAL C1023    11979  14602  17873  -3390  -2303  -2129       C  
ATOM   3798  CG2 VAL C1023      20.619  89.947 116.736  1.00114.94           C  
ANISOU 3798  CG2 VAL C1023    11854  14254  17562  -3410  -2373  -2181       C  
ATOM   3799  N   LEU C1024      22.830  91.864 113.252  1.00117.69           N  
ANISOU 3799  N   LEU C1024    12098  14275  18345  -2993  -2164  -2061       N  
ATOM   3800  CA  LEU C1024      23.216  92.730 112.129  1.00118.52           C  
ANISOU 3800  CA  LEU C1024    12125  14321  18588  -2877  -2094  -2020       C  
ATOM   3801  C   LEU C1024      23.751  91.901 110.960  1.00120.65           C  
ANISOU 3801  C   LEU C1024    12576  14471  18796  -2811  -2045  -1934       C  
ATOM   3802  O   LEU C1024      23.506  92.218 109.789  1.00123.64           O  
ANISOU 3802  O   LEU C1024    12968  14824  19184  -2771  -1996  -1891       O  
ATOM   3803  CB  LEU C1024      24.251  93.774 112.565  1.00116.94           C  
ANISOU 3803  CB  LEU C1024    11756  14077  18598  -2771  -2082  -2033       C  
ATOM   3804  CG  LEU C1024      24.740  94.805 111.538  1.00116.01           C  
ANISOU 3804  CG  LEU C1024    11529  13903  18646  -2656  -2019  -1984       C  
ATOM   3805  CD1 LEU C1024      23.574  95.616 110.975  1.00114.84           C  
ANISOU 3805  CD1 LEU C1024    11303  13837  18493  -2690  -2006  -2013       C  
ATOM   3806  CD2 LEU C1024      25.814  95.706 112.148  1.00114.33           C  
ANISOU 3806  CD2 LEU C1024    11168  13646  18629  -2583  -2038  -1982       C  
ATOM   3807  N   ASN C1025      24.473  90.836 111.297  1.00119.61           N  
ANISOU 3807  N   ASN C1025    12594  14263  18589  -2792  -2057  -1908       N  
ATOM   3808  CA  ASN C1025      24.966  89.873 110.323  1.00119.27           C  
ANISOU 3808  CA  ASN C1025    12772  14099  18446  -2717  -2011  -1830       C  
ATOM   3809  C   ASN C1025      23.829  89.066 109.662  1.00121.04           C  
ANISOU 3809  C   ASN C1025    13203  14329  18456  -2838  -2051  -1819       C  
ATOM   3810  O   ASN C1025      23.940  88.642 108.502  1.00122.19           O  
ANISOU 3810  O   ASN C1025    13523  14379  18525  -2777  -2008  -1757       O  
ATOM   3811  CB  ASN C1025      25.968  88.944 111.008  1.00117.73           C  
ANISOU 3811  CB  ASN C1025    12685  13830  18217  -2663  -2022  -1808       C  
ATOM   3812  CG  ASN C1025      26.679  88.027 110.041  1.00117.79           C  
ANISOU 3812  CG  ASN C1025    12920  13701  18134  -2534  -1956  -1720       C  
ATOM   3813  OD1 ASN C1025      27.034  86.901 110.397  1.00116.88           O  
ANISOU 3813  OD1 ASN C1025    12996  13522  17893  -2528  -1980  -1705       O  
ATOM   3814  ND2 ASN C1025      26.899  88.500 108.812  1.00118.11           N  
ANISOU 3814  ND2 ASN C1025    12955  13692  18230  -2419  -1869  -1660       N  
ATOM   3815  N   GLY C1026      22.740  88.863 110.401  1.00120.43           N  
ANISOU 3815  N   GLY C1026    13112  14368  18278  -3013  -2136  -1868       N  
ATOM   3816  CA  GLY C1026      21.583  88.136 109.893  1.00120.58           C  
ANISOU 3816  CA  GLY C1026    13301  14414  18098  -3164  -2199  -1840       C  
ATOM   3817  C   GLY C1026      20.911  88.854 108.736  1.00120.72           C  
ANISOU 3817  C   GLY C1026    13266  14457  18145  -3164  -2168  -1808       C  
ATOM   3818  O   GLY C1026      20.815  88.312 107.636  1.00120.20           O  
ANISOU 3818  O   GLY C1026    13405  14295  17971  -3158  -2164  -1749       O  
ATOM   3819  N   ILE C1027      20.471  90.087 108.986  1.00121.05           N  
ANISOU 3819  N   ILE C1027    13046  14619  18330  -3162  -2148  -1847       N  
ATOM   3820  CA  ILE C1027      19.706  90.881 108.012  1.00119.81           C  
ANISOU 3820  CA  ILE C1027    12803  14510  18209  -3172  -2125  -1820       C  
ATOM   3821  C   ILE C1027      20.491  91.143 106.710  1.00119.96           C  
ANISOU 3821  C   ILE C1027    12891  14389  18298  -3020  -2041  -1770       C  
ATOM   3822  O   ILE C1027      19.892  91.269 105.633  1.00118.63           O  
ANISOU 3822  O   ILE C1027    12780  14211  18082  -3046  -2038  -1724       O  
ATOM   3823  CB  ILE C1027      19.197  92.210 108.632  1.00118.30           C  
ANISOU 3823  CB  ILE C1027    12321  14464  18163  -3167  -2112  -1876       C  
ATOM   3824  CG1 ILE C1027      18.746  91.997 110.078  1.00119.07           C  
ANISOU 3824  CG1 ILE C1027    12348  14685  18209  -3265  -2170  -1930       C  
ATOM   3825  CG2 ILE C1027      18.028  92.765 107.836  1.00118.34           C  
ANISOU 3825  CG2 ILE C1027    12254  14562  18147  -3232  -2118  -1840       C  
ATOM   3826  CD1 ILE C1027      18.902  93.214 110.973  1.00119.27           C  
ANISOU 3826  CD1 ILE C1027    12139  14783  18395  -3189  -2142  -2006       C  
ATOM   3827  N   THR C1028      21.822  91.206 106.814  1.00119.68           N  
ANISOU 3827  N   THR C1028    12848  14253  18372  -2863  -1975  -1767       N  
ATOM   3828  CA  THR C1028      22.684  91.413 105.641  1.00119.86           C  
ANISOU 3828  CA  THR C1028    12927  14152  18461  -2699  -1881  -1703       C  
ATOM   3829  C   THR C1028      23.019  90.118 104.879  1.00120.75           C  
ANISOU 3829  C   THR C1028    13365  14125  18389  -2661  -1869  -1641       C  
ATOM   3830  O   THR C1028      23.378  90.168 103.696  1.00119.76           O  
ANISOU 3830  O   THR C1028    13341  13906  18257  -2548  -1796  -1580       O  
ATOM   3831  CB  THR C1028      23.971  92.202 105.990  1.00120.67           C  
ANISOU 3831  CB  THR C1028    12843  14225  18782  -2540  -1811  -1698       C  
ATOM   3832  OG1 THR C1028      24.637  92.590 104.782  1.00122.05           O  
ANISOU 3832  OG1 THR C1028    13028  14314  19032  -2391  -1715  -1621       O  
ATOM   3833  CG2 THR C1028      24.927  91.380 106.855  1.00120.73           C  
ANISOU 3833  CG2 THR C1028    12924  14180  18769  -2495  -1819  -1693       C  
HETATM 3834  N   MSE C1029      22.906  88.977 105.567  1.00121.53           N  
ANISOU 3834  N   MSE C1029    13639  14206  18330  -2748  -1939  -1655       N  
HETATM 3835  CA  MSE C1029      23.057  87.650 104.954  1.00121.69           C  
ANISOU 3835  CA  MSE C1029    14014  14086  18136  -2734  -1954  -1605       C  
HETATM 3836  C   MSE C1029      21.706  87.177 104.477  1.00122.48           C  
ANISOU 3836  C   MSE C1029    14277  14211  18048  -2931  -2058  -1593       C  
HETATM 3837  O   MSE C1029      21.610  86.315 103.591  1.00124.57           O  
ANISOU 3837  O   MSE C1029    14853  14347  18130  -2932  -2079  -1543       O  
HETATM 3838  CB  MSE C1029      23.621  86.648 105.961  1.00122.19           C  
ANISOU 3838  CB  MSE C1029    14197  14110  18121  -2737  -1991  -1622       C  
HETATM 3839  CG  MSE C1029      25.136  86.481 105.845  1.00123.46           C  
ANISOU 3839  CG  MSE C1029    14388  14160  18361  -2502  -1882  -1575       C  
HETATM 3840 SE   MSE C1029      25.683  84.583 105.991  1.00125.53          SE  
ANISOU 3840 SE   MSE C1029    15080  14254  18362  -2455  -1914  -1540      SE  
HETATM 3841  CE  MSE C1029      25.604  84.097 104.085  1.00125.50           C  
ANISOU 3841  CE  MSE C1029    15435  14075  18175  -2337  -1849  -1459       C  
ATOM   3842  N   GLY C1030      20.652  87.743 105.070  1.00120.80           N  
ANISOU 3842  N   GLY C1030    13860  14165  17873  -3095  -2127  -1630       N  
ATOM   3843  CA  GLY C1030      19.275  87.502 104.644  1.00119.28           C  
ANISOU 3843  CA  GLY C1030    13746  14039  17536  -3296  -2230  -1596       C  
ATOM   3844  C   GLY C1030      18.892  88.329 103.430  1.00117.74           C  
ANISOU 3844  C   GLY C1030    13492  13843  17400  -3259  -2187  -1559       C  
ATOM   3845  O   GLY C1030      17.747  88.278 102.975  1.00117.34           O  
ANISOU 3845  O   GLY C1030    13477  13857  17252  -3420  -2270  -1517       O  
ATOM   3846  N   LEU C1031      19.851  89.102 102.922  1.00115.72           N  
ANISOU 3846  N   LEU C1031    13137  13523  17310  -3055  -2063  -1563       N  
ATOM   3847  CA  LEU C1031      19.677  89.854 101.691  1.00116.10           C  
ANISOU 3847  CA  LEU C1031    13152  13545  17415  -2993  -2009  -1524       C  
ATOM   3848  C   LEU C1031      20.576  89.334 100.564  1.00117.38           C  
ANISOU 3848  C   LEU C1031    13579  13515  17506  -2828  -1930  -1468       C  
ATOM   3849  O   LEU C1031      20.294  89.582  99.384  1.00117.81           O  
ANISOU 3849  O   LEU C1031    13718  13516  17526  -2807  -1910  -1421       O  
ATOM   3850  CB  LEU C1031      19.913  91.346 101.927  1.00116.05           C  
ANISOU 3850  CB  LEU C1031    12796  13636  17663  -2899  -1933  -1562       C  
ATOM   3851  CG  LEU C1031      18.766  92.199 102.480  1.00116.09           C  
ANISOU 3851  CG  LEU C1031    12547  13826  17735  -3030  -1989  -1597       C  
ATOM   3852  CD1 LEU C1031      19.306  93.491 103.080  1.00115.58           C  
ANISOU 3852  CD1 LEU C1031    12184  13823  17909  -2914  -1921  -1654       C  
ATOM   3853  CD2 LEU C1031      17.729  92.496 101.404  1.00116.13           C  
ANISOU 3853  CD2 LEU C1031    12575  13864  17683  -3115  -2022  -1542       C  
ATOM   3854  N   GLU C1032      21.641  88.609 100.927  1.00117.56           N  
ANISOU 3854  N   GLU C1032    13734  13436  17496  -2704  -1883  -1466       N  
ATOM   3855  CA  GLU C1032      22.517  87.933  99.946  1.00117.98           C  
ANISOU 3855  CA  GLU C1032    14076  13306  17445  -2525  -1800  -1404       C  
ATOM   3856  C   GLU C1032      21.719  87.012  99.013  1.00117.79           C  
ANISOU 3856  C   GLU C1032    14422  13173  17159  -2634  -1888  -1364       C  
ATOM   3857  O   GLU C1032      22.244  86.479  98.027  1.00118.26           O  
ANISOU 3857  O   GLU C1032    14768  13070  17097  -2493  -1827  -1312       O  
ATOM   3858  CB  GLU C1032      23.643  87.157 100.644  1.00118.38           C  
ANISOU 3858  CB  GLU C1032    14221  13282  17476  -2394  -1755  -1403       C  
ATOM   3859  CG  GLU C1032      24.789  88.038 101.138  1.00119.64           C  
ANISOU 3859  CG  GLU C1032    14076  13493  17888  -2221  -1641  -1399       C  
ATOM   3860  CD  GLU C1032      26.005  87.251 101.627  1.00120.32           C  
ANISOU 3860  CD  GLU C1032    14266  13498  17954  -2062  -1583  -1367       C  
ATOM   3861  OE1 GLU C1032      26.156  86.064 101.244  1.00120.70           O  
ANISOU 3861  OE1 GLU C1032    14662  13411  17786  -2013  -1587  -1336       O  
ATOM   3862  OE2 GLU C1032      26.817  87.829 102.394  1.00118.44           O  
ANISOU 3862  OE2 GLU C1032    13767  13324  17910  -1985  -1538  -1367       O  
ATOM   3863  N   THR C1033      20.444  86.850  99.348  1.00116.33           N  
ANISOU 3863  N   THR C1033    14230  13084  16887  -2885  -2034  -1379       N  
ATOM   3864  CA  THR C1033      19.481  86.105  98.563  1.00117.38           C  
ANISOU 3864  CA  THR C1033    14669  13145  16786  -3050  -2157  -1330       C  
ATOM   3865  C   THR C1033      19.195  86.796  97.230  1.00118.03           C  
ANISOU 3865  C   THR C1033    14761  13193  16893  -3007  -2116  -1284       C  
ATOM   3866  O   THR C1033      18.901  86.132  96.218  1.00119.06           O  
ANISOU 3866  O   THR C1033    15235  13181  16821  -3041  -2170  -1231       O  
ATOM   3867  CB  THR C1033      18.160  85.978  99.353  1.00116.40           C  
ANISOU 3867  CB  THR C1033    14434  13183  16608  -3339  -2319  -1336       C  
ATOM   3868  OG1 THR C1033      18.400  85.236 100.554  1.00115.34           O  
ANISOU 3868  OG1 THR C1033    14329  13070  16426  -3389  -2365  -1373       O  
ATOM   3869  CG2 THR C1033      17.082  85.278  98.525  1.00117.47           C  
ANISOU 3869  CG2 THR C1033    14861  13260  16511  -3545  -2472  -1261       C  
ATOM   3870  N   SER C1034      19.296  88.124  97.242  1.00116.31           N  
ANISOU 3870  N   SER C1034    14183  13095  16915  -2933  -2026  -1306       N  
ATOM   3871  CA  SER C1034      18.818  88.960  96.148  1.00115.98           C  
ANISOU 3871  CA  SER C1034    14074  13066  16925  -2931  -2005  -1268       C  
ATOM   3872  C   SER C1034      19.772  89.029  94.959  1.00115.52           C  
ANISOU 3872  C   SER C1034    14188  12845  16860  -2699  -1872  -1225       C  
ATOM   3873  O   SER C1034      20.909  88.573  95.033  1.00115.18           O  
ANISOU 3873  O   SER C1034    14260  12697  16805  -2509  -1772  -1220       O  
ATOM   3874  CB  SER C1034      18.527  90.367  96.672  1.00115.82           C  
ANISOU 3874  CB  SER C1034    13613  13235  17158  -2940  -1968  -1308       C  
ATOM   3875  OG  SER C1034      17.814  91.123  95.713  1.00117.73           O  
ANISOU 3875  OG  SER C1034    13786  13511  17434  -2984  -1978  -1270       O  
ATOM   3876  N   LYS C1035      19.280  89.576  93.852  1.00116.21           N  
ANISOU 3876  N   LYS C1035    14294  12916  16944  -2714  -1870  -1183       N  
ATOM   3877  CA  LYS C1035      20.139  89.989  92.747  1.00117.38           C  
ANISOU 3877  CA  LYS C1035    14507  12952  17139  -2486  -1724  -1140       C  
ATOM   3878  C   LYS C1035      20.059  91.510  92.612  1.00118.28           C  
ANISOU 3878  C   LYS C1035    14233  13197  17511  -2449  -1657  -1149       C  
ATOM   3879  O   LYS C1035      20.787  92.120  91.820  1.00119.59           O  
ANISOU 3879  O   LYS C1035    14356  13310  17772  -2265  -1529  -1111       O  
ATOM   3880  CB  LYS C1035      19.752  89.311  91.435  1.00116.92           C  
ANISOU 3880  CB  LYS C1035    14855  12731  16840  -2508  -1770  -1079       C  
ATOM   3881  CG  LYS C1035      20.922  89.203  90.475  1.00116.94           C  
ANISOU 3881  CG  LYS C1035    15050  12573  16808  -2225  -1603  -1031       C  
ATOM   3882  CD  LYS C1035      20.479  89.246  89.025  1.00117.64           C  
ANISOU 3882  CD  LYS C1035    15386  12550  16762  -2226  -1616   -973       C  
ATOM   3883  CE  LYS C1035      21.666  89.022  88.102  1.00117.92           C  
ANISOU 3883  CE  LYS C1035    15647  12425  16733  -1925  -1438   -917       C  
ATOM   3884  NZ  LYS C1035      21.274  89.116  86.671  1.00118.36           N  
ANISOU 3884  NZ  LYS C1035    15949  12367  16655  -1912  -1442   -862       N  
ATOM   3885  N   THR C1036      19.166  92.107  93.400  1.00117.97           N  
ANISOU 3885  N   THR C1036    13919  13329  17575  -2620  -1745  -1192       N  
ATOM   3886  CA  THR C1036      19.069  93.556  93.539  1.00117.41           C  
ANISOU 3886  CA  THR C1036    13469  13389  17751  -2589  -1696  -1215       C  
ATOM   3887  C   THR C1036      20.041  94.062  94.619  1.00117.58           C  
ANISOU 3887  C   THR C1036    13234  13467  17972  -2468  -1615  -1266       C  
ATOM   3888  O   THR C1036      20.789  95.020  94.383  1.00116.73           O  
ANISOU 3888  O   THR C1036    12938  13362  18054  -2319  -1512  -1255       O  
ATOM   3889  CB  THR C1036      17.610  93.988  93.814  1.00116.17           C  
ANISOU 3889  CB  THR C1036    13152  13389  17596  -2808  -1821  -1226       C  
ATOM   3890  OG1 THR C1036      16.879  93.950  92.585  1.00116.38           O  
ANISOU 3890  OG1 THR C1036    13343  13368  17511  -2882  -1872  -1160       O  
ATOM   3891  CG2 THR C1036      17.527  95.394  94.381  1.00115.47           C  
ANISOU 3891  CG2 THR C1036    12670  13448  17757  -2771  -1779  -1273       C  
ATOM   3892  N   PHE C1037      20.044  93.412  95.782  1.00117.94           N  
ANISOU 3892  N   PHE C1037    13284  13555  17972  -2540  -1672  -1313       N  
ATOM   3893  CA  PHE C1037      20.948  93.803  96.866  1.00119.34           C  
ANISOU 3893  CA  PHE C1037    13244  13779  18322  -2444  -1616  -1358       C  
ATOM   3894  C   PHE C1037      22.381  93.363  96.590  1.00120.85           C  
ANISOU 3894  C   PHE C1037    13556  13839  18521  -2235  -1500  -1311       C  
ATOM   3895  O   PHE C1037      23.321  93.928  97.158  1.00121.67           O  
ANISOU 3895  O   PHE C1037    13455  13969  18806  -2121  -1433  -1314       O  
ATOM   3896  CB  PHE C1037      20.474  93.261  98.217  1.00119.74           C  
ANISOU 3896  CB  PHE C1037    13259  13920  18317  -2589  -1714  -1421       C  
ATOM   3897  CG  PHE C1037      21.125  93.921  99.408  1.00119.50           C  
ANISOU 3897  CG  PHE C1037    12961  13964  18477  -2529  -1684  -1478       C  
ATOM   3898  CD1 PHE C1037      20.709  95.179  99.844  1.00119.94           C  
ANISOU 3898  CD1 PHE C1037    12724  14143  18707  -2555  -1692  -1522       C  
ATOM   3899  CD2 PHE C1037      22.143  93.276 100.111  1.00119.55           C  
ANISOU 3899  CD2 PHE C1037    13026  13913  18482  -2447  -1655  -1483       C  
ATOM   3900  CE1 PHE C1037      21.309  95.783 100.953  1.00120.11           C  
ANISOU 3900  CE1 PHE C1037    12534  14214  18889  -2507  -1681  -1575       C  
ATOM   3901  CE2 PHE C1037      22.740  93.871 101.220  1.00118.66           C  
ANISOU 3901  CE2 PHE C1037    12682  13863  18540  -2408  -1645  -1529       C  
ATOM   3902  CZ  PHE C1037      22.324  95.127 101.641  1.00118.65           C  
ANISOU 3902  CZ  PHE C1037    12408  13971  18703  -2442  -1662  -1577       C  
HETATM 3903  N   MSE C1038      22.550  92.377  95.709  1.00121.57           N  
ANISOU 3903  N   MSE C1038    13983  13792  18415  -2181  -1479  -1257       N  
HETATM 3904  CA  MSE C1038      23.894  91.898  95.351  1.00123.16           C  
ANISOU 3904  CA  MSE C1038    14323  13873  18602  -1952  -1351  -1194       C  
HETATM 3905  C   MSE C1038      24.509  92.649  94.170  1.00122.17           C  
ANISOU 3905  C   MSE C1038    14150  13698  18571  -1773  -1220  -1116       C  
HETATM 3906  O   MSE C1038      25.661  92.398  93.802  1.00122.17           O  
ANISOU 3906  O   MSE C1038    14222  13619  18579  -1560  -1093  -1042       O  
HETATM 3907  CB  MSE C1038      23.897  90.375  95.161  1.00125.68           C  
ANISOU 3907  CB  MSE C1038    15053  14055  18645  -1952  -1386  -1178       C  
HETATM 3908  CG  MSE C1038      23.574  89.625  96.455  1.00127.02           C  
ANISOU 3908  CG  MSE C1038    15244  14272  18745  -2099  -1498  -1242       C  
HETATM 3909 SE   MSE C1038      25.125  89.481  97.668  1.00132.37          SE  
ANISOU 3909 SE   MSE C1038    15758  14964  19574  -1918  -1405  -1241      SE  
HETATM 3910  CE  MSE C1038      24.624  90.882  98.957  1.00129.17           C  
ANISOU 3910  CE  MSE C1038    14863  14774  19443  -2074  -1475  -1329       C  
ATOM   3911  N   GLN C1039      23.761  93.583  93.581  1.00120.48           N  
ANISOU 3911  N   GLN C1039    13806  13540  18432  -1851  -1246  -1122       N  
ATOM   3912  CA  GLN C1039      24.292  94.432  92.495  1.00119.87           C  
ANISOU 3912  CA  GLN C1039    13650  13431  18465  -1698  -1128  -1048       C  
ATOM   3913  C   GLN C1039      24.487  95.919  92.883  1.00118.46           C  
ANISOU 3913  C   GLN C1039    13069  13371  18572  -1692  -1108  -1061       C  
ATOM   3914  O   GLN C1039      25.116  96.687  92.147  1.00117.03           O  
ANISOU 3914  O   GLN C1039    12779  13173  18514  -1558  -1009   -990       O  
ATOM   3915  CB  GLN C1039      23.453  94.286  91.209  1.00119.19           C  
ANISOU 3915  CB  GLN C1039    13797  13273  18218  -1752  -1157  -1021       C  
ATOM   3916  CG  GLN C1039      22.100  94.990  91.223  1.00117.87           C  
ANISOU 3916  CG  GLN C1039    13484  13212  18091  -1963  -1278  -1071       C  
ATOM   3917  CD  GLN C1039      21.327  94.808  89.925  1.00118.28           C  
ANISOU 3917  CD  GLN C1039    13775  13187  17981  -2020  -1315  -1027       C  
ATOM   3918  OE1 GLN C1039      21.532  93.835  89.197  1.00119.37           O  
ANISOU 3918  OE1 GLN C1039    14269  13180  17907  -1960  -1297   -984       O  
ATOM   3919  NE2 GLN C1039      20.427  95.745  89.631  1.00117.07           N  
ANISOU 3919  NE2 GLN C1039    13439  13124  17918  -2134  -1372  -1037       N  
ATOM   3920  N   SER C1040      23.951  96.316  94.035  1.00117.95           N  
ANISOU 3920  N   SER C1040    12797  13418  18599  -1834  -1205  -1147       N  
ATOM   3921  CA  SER C1040      24.163  97.667  94.558  1.00117.89           C  
ANISOU 3921  CA  SER C1040    12444  13505  18844  -1828  -1202  -1169       C  
ATOM   3922  C   SER C1040      25.026  97.634  95.823  1.00118.07           C  
ANISOU 3922  C   SER C1040    12321  13560  18980  -1793  -1204  -1190       C  
ATOM   3923  O   SER C1040      25.909  98.492  96.013  1.00118.03           O  
ANISOU 3923  O   SER C1040    12101  13571  19175  -1701  -1157  -1149       O  
ATOM   3924  CB  SER C1040      22.827  98.376  94.833  1.00117.96           C  
ANISOU 3924  CB  SER C1040    12317  13621  18884  -2000  -1308  -1247       C  
ATOM   3925  OG  SER C1040      22.184  98.772  93.627  1.00119.36           O  
ANISOU 3925  OG  SER C1040    12548  13779  19024  -2016  -1300  -1210       O  
ATOM   3926  N   PHE C1041      24.772  96.637  96.675  1.00116.62           N  
ANISOU 3926  N   PHE C1041    12261  13384  18664  -1875  -1268  -1244       N  
ATOM   3927  CA  PHE C1041      25.503  96.470  97.936  1.00115.75           C  
ANISOU 3927  CA  PHE C1041    12042  13303  18634  -1860  -1285  -1269       C  
ATOM   3928  C   PHE C1041      26.327  95.180  97.919  1.00117.03           C  
ANISOU 3928  C   PHE C1041    12434  13372  18659  -1755  -1231  -1215       C  
ATOM   3929  O   PHE C1041      26.680  94.643  98.974  1.00116.44           O  
ANISOU 3929  O   PHE C1041    12355  13313  18574  -1776  -1267  -1245       O  
ATOM   3930  CB  PHE C1041      24.539  96.483  99.136  1.00114.19           C  
ANISOU 3930  CB  PHE C1041    11767  13208  18415  -2040  -1407  -1383       C  
ATOM   3931  CG  PHE C1041      23.838  97.802  99.354  1.00112.19           C  
ANISOU 3931  CG  PHE C1041    11273  13051  18306  -2111  -1452  -1437       C  
ATOM   3932  CD1 PHE C1041      22.856  98.250  98.471  1.00111.44           C  
ANISOU 3932  CD1 PHE C1041    11186  12981  18175  -2166  -1464  -1435       C  
ATOM   3933  CD2 PHE C1041      24.141  98.583 100.454  1.00111.86           C  
ANISOU 3933  CD2 PHE C1041    11012  13068  18424  -2121  -1489  -1488       C  
ATOM   3934  CE1 PHE C1041      22.213  99.459  98.667  1.00110.14           C  
ANISOU 3934  CE1 PHE C1041    10809  12903  18137  -2212  -1500  -1481       C  
ATOM   3935  CE2 PHE C1041      23.495  99.795 100.661  1.00112.02           C  
ANISOU 3935  CE2 PHE C1041    10841  13162  18559  -2167  -1529  -1542       C  
ATOM   3936  CZ  PHE C1041      22.529 100.232  99.765  1.00110.58           C  
ANISOU 3936  CZ  PHE C1041    10662  13009  18344  -2206  -1529  -1538       C  
ATOM   3937  N   GLY C1042      26.629  94.698  96.711  1.00119.14           N  
ANISOU 3937  N   GLY C1042    12913  13541  18815  -1632  -1141  -1133       N  
ATOM   3938  CA  GLY C1042      27.449  93.501  96.500  1.00120.51           C  
ANISOU 3938  CA  GLY C1042    13337  13610  18841  -1489  -1068  -1067       C  
ATOM   3939  C   GLY C1042      28.825  93.571  97.141  1.00121.43           C  
ANISOU 3939  C   GLY C1042    13294  13739  19104  -1341   -994   -997       C  
ATOM   3940  O   GLY C1042      29.288  92.592  97.719  1.00122.99           O  
ANISOU 3940  O   GLY C1042    13624  13900  19207  -1298   -994   -991       O  
ATOM   3941  N   VAL C1043      29.476  94.729  97.042  1.00121.43           N  
ANISOU 3941  N   VAL C1043    13010  13793  19335  -1270   -942   -935       N  
ATOM   3942  CA  VAL C1043      30.796  94.945  97.647  1.00122.39           C  
ANISOU 3942  CA  VAL C1043    12937  13942  19623  -1150   -889   -843       C  
ATOM   3943  C   VAL C1043      30.664  95.340  99.127  1.00121.93           C  
ANISOU 3943  C   VAL C1043    12675  13965  19689  -1301  -1015   -934       C  
ATOM   3944  O   VAL C1043      31.480  94.926  99.961  1.00122.71           O  
ANISOU 3944  O   VAL C1043    12727  14071  19827  -1256  -1019   -899       O  
ATOM   3945  CB  VAL C1043      31.627  96.004  96.867  1.00123.24           C  
ANISOU 3945  CB  VAL C1043    12833  14070  19923  -1015   -788   -709       C  
ATOM   3946  CG1 VAL C1043      32.983  96.237  97.527  1.00123.62           C  
ANISOU 3946  CG1 VAL C1043    12660  14160  20150   -914   -753   -591       C  
ATOM   3947  CG2 VAL C1043      31.821  95.582  95.413  1.00123.66           C  
ANISOU 3947  CG2 VAL C1043    13099  14043  19842   -844   -649   -612       C  
ATOM   3948  N   TYR C1044      29.636  96.134  99.440  1.00120.20           N  
ANISOU 3948  N   TYR C1044    12342  13805  19522  -1469  -1115  -1046       N  
ATOM   3949  CA  TYR C1044      29.324  96.537 100.819  1.00119.15           C  
ANISOU 3949  CA  TYR C1044    12050  13746  19476  -1613  -1236  -1148       C  
ATOM   3950  C   TYR C1044      29.154  95.328 101.731  1.00119.53           C  
ANISOU 3950  C   TYR C1044    12261  13787  19367  -1676  -1291  -1210       C  
ATOM   3951  O   TYR C1044      29.346  95.428 102.944  1.00118.50           O  
ANISOU 3951  O   TYR C1044    12017  13701  19307  -1743  -1366  -1259       O  
ATOM   3952  CB  TYR C1044      28.017  97.324 100.867  1.00118.22           C  
ANISOU 3952  CB  TYR C1044    11861  13691  19367  -1764  -1318  -1260       C  
ATOM   3953  CG  TYR C1044      28.094  98.809 100.572  1.00117.85           C  
ANISOU 3953  CG  TYR C1044    11580  13673  19523  -1753  -1318  -1242       C  
ATOM   3954  CD1 TYR C1044      28.024  99.285  99.258  1.00118.20           C  
ANISOU 3954  CD1 TYR C1044    11634  13687  19589  -1683  -1244  -1175       C  
ATOM   3955  CD2 TYR C1044      28.170  99.743 101.610  1.00116.73           C  
ANISOU 3955  CD2 TYR C1044    11232  13582  19539  -1820  -1403  -1297       C  
ATOM   3956  CE1 TYR C1044      28.059 100.645  98.989  1.00117.72           C  
ANISOU 3956  CE1 TYR C1044    11370  13648  19709  -1681  -1254  -1159       C  
ATOM   3957  CE2 TYR C1044      28.206 101.102 101.350  1.00116.10           C  
ANISOU 3957  CE2 TYR C1044    10967  13513  19632  -1815  -1418  -1283       C  
ATOM   3958  CZ  TYR C1044      28.149 101.544 100.040  1.00116.80           C  
ANISOU 3958  CZ  TYR C1044    11058  13574  19745  -1747  -1344  -1213       C  
ATOM   3959  OH  TYR C1044      28.182 102.886  99.770  1.00116.61           O  
ANISOU 3959  OH  TYR C1044    10861  13556  19890  -1746  -1365  -1197       O  
ATOM   3960  N   THR C1045      28.764  94.202 101.135  1.00121.31           N  
ANISOU 3960  N   THR C1045    12769  13949  19372  -1661  -1264  -1208       N  
ATOM   3961  CA  THR C1045      28.503  92.968 101.869  1.00122.40           C  
ANISOU 3961  CA  THR C1045    13106  14068  19334  -1732  -1325  -1262       C  
ATOM   3962  C   THR C1045      29.719  92.047 101.822  1.00124.73           C  
ANISOU 3962  C   THR C1045    13530  14282  19579  -1556  -1240  -1163       C  
ATOM   3963  O   THR C1045      30.178  91.572 102.866  1.00125.97           O  
ANISOU 3963  O   THR C1045    13667  14453  19745  -1569  -1281  -1177       O  
ATOM   3964  CB  THR C1045      27.262  92.231 101.315  1.00122.12           C  
ANISOU 3964  CB  THR C1045    13330  14003  19066  -1849  -1375  -1316       C  
ATOM   3965  OG1 THR C1045      26.214  93.175 101.053  1.00120.12           O  
ANISOU 3965  OG1 THR C1045    12945  13826  18868  -1970  -1424  -1370       O  
ATOM   3966  CG2 THR C1045      26.762  91.185 102.312  1.00122.91           C  
ANISOU 3966  CG2 THR C1045    13578  14114  19008  -1984  -1477  -1388       C  
ATOM   3967  N   THR C1046      30.230  91.803 100.611  1.00126.14           N  
ANISOU 3967  N   THR C1046    13843  14381  19702  -1382  -1119  -1059       N  
ATOM   3968  CA  THR C1046      31.416  90.963 100.393  1.00128.79           C  
ANISOU 3968  CA  THR C1046    14309  14643  19983  -1168  -1010   -942       C  
ATOM   3969  C   THR C1046      32.546  91.301 101.373  1.00131.31           C  
ANISOU 3969  C   THR C1046    14370  15023  20499  -1108  -1004   -878       C  
ATOM   3970  O   THR C1046      33.154  90.399 101.962  1.00133.17           O  
ANISOU 3970  O   THR C1046    14702  15229  20668  -1041   -997   -848       O  
ATOM   3971  CB  THR C1046      31.921  91.067  98.935  1.00129.12           C  
ANISOU 3971  CB  THR C1046    14442  14620  19999   -963   -858   -819       C  
ATOM   3972  OG1 THR C1046      30.991  90.413  98.056  1.00129.29           O  
ANISOU 3972  OG1 THR C1046    14789  14551  19783  -1003   -870   -867       O  
ATOM   3973  CG2 THR C1046      33.307  90.435  98.773  1.00129.66           C  
ANISOU 3973  CG2 THR C1046    14565  14644  20057   -706   -721   -668       C  
ATOM   3974  N   LEU C1047      32.808  92.597 101.549  1.00130.59           N  
ANISOU 3974  N   LEU C1047    13963  15011  20644  -1141  -1018   -853       N  
ATOM   3975  CA  LEU C1047      33.822  93.055 102.490  1.00131.22           C  
ANISOU 3975  CA  LEU C1047    13786  15148  20924  -1119  -1042   -786       C  
ATOM   3976  C   LEU C1047      33.319  92.967 103.933  1.00131.06           C  
ANISOU 3976  C   LEU C1047    13720  15171  20907  -1309  -1193   -922       C  
ATOM   3977  O   LEU C1047      34.105  92.703 104.854  1.00131.37           O  
ANISOU 3977  O   LEU C1047    13679  15226  21010  -1291  -1224   -881       O  
ATOM   3978  CB  LEU C1047      34.271  94.488 102.168  1.00132.01           C  
ANISOU 3978  CB  LEU C1047    13588  15302  21266  -1103  -1026   -706       C  
ATOM   3979  CG  LEU C1047      35.029  94.787 100.867  1.00132.79           C  
ANISOU 3979  CG  LEU C1047    13652  15385  21420   -905   -873   -535       C  
ATOM   3980  CD1 LEU C1047      35.122  96.289 100.648  1.00132.73           C  
ANISOU 3980  CD1 LEU C1047    13363  15430  21638   -958   -902   -496       C  
ATOM   3981  CD2 LEU C1047      36.416  94.157 100.839  1.00134.14           C  
ANISOU 3981  CD2 LEU C1047    13805  15552  21612   -695   -763   -350       C  
ATOM   3982  N   PHE C1048      32.015  93.183 104.128  1.00129.18           N  
ANISOU 3982  N   PHE C1048    13528  14958  20596  -1487  -1283  -1071       N  
ATOM   3983  CA  PHE C1048      31.429  93.135 105.472  1.00128.40           C  
ANISOU 3983  CA  PHE C1048    13389  14912  20486  -1663  -1417  -1200       C  
ATOM   3984  C   PHE C1048      31.646  91.773 106.125  1.00128.92           C  
ANISOU 3984  C   PHE C1048    13651  14940  20393  -1658  -1438  -1211       C  
ATOM   3985  O   PHE C1048      31.896  91.692 107.336  1.00129.82           O  
ANISOU 3985  O   PHE C1048    13684  15088  20554  -1728  -1518  -1249       O  
ATOM   3986  CB  PHE C1048      29.939  93.485 105.463  1.00126.78           C  
ANISOU 3986  CB  PHE C1048    13213  14754  20203  -1833  -1491  -1335       C  
ATOM   3987  CG  PHE C1048      29.308  93.439 106.823  1.00126.17           C  
ANISOU 3987  CG  PHE C1048    13095  14743  20101  -1997  -1612  -1456       C  
ATOM   3988  CD1 PHE C1048      29.364  94.539 107.663  1.00127.66           C  
ANISOU 3988  CD1 PHE C1048    13054  14992  20460  -2058  -1679  -1503       C  
ATOM   3989  CD2 PHE C1048      28.681  92.288 107.276  1.00126.38           C  
ANISOU 3989  CD2 PHE C1048    13326  14768  19926  -2089  -1662  -1518       C  
ATOM   3990  CE1 PHE C1048      28.795  94.499 108.928  1.00128.01           C  
ANISOU 3990  CE1 PHE C1048    13074  15096  20468  -2192  -1781  -1613       C  
ATOM   3991  CE2 PHE C1048      28.109  92.239 108.536  1.00126.79           C  
ANISOU 3991  CE2 PHE C1048    13335  14891  19950  -2234  -1765  -1620       C  
ATOM   3992  CZ  PHE C1048      28.166  93.346 109.365  1.00127.16           C  
ANISOU 3992  CZ  PHE C1048    13153  15002  20162  -2278  -1818  -1669       C  
ATOM   3993  N   ASN C1049      31.539  90.715 105.319  1.00126.84           N  
ANISOU 3993  N   ASN C1049    13662  14597  19934  -1577  -1372  -1179       N  
ATOM   3994  CA  ASN C1049      31.907  89.365 105.741  1.00125.85           C  
ANISOU 3994  CA  ASN C1049    13758  14409  19648  -1530  -1374  -1164       C  
ATOM   3995  C   ASN C1049      33.290  89.345 106.399  1.00124.78           C  
ANISOU 3995  C   ASN C1049    13472  14284  19654  -1405  -1342  -1060       C  
ATOM   3996  O   ASN C1049      33.421  88.949 107.557  1.00122.20           O  
ANISOU 3996  O   ASN C1049    13129  13979  19324  -1482  -1425  -1104       O  
ATOM   3997  CB  ASN C1049      31.872  88.401 104.548  1.00126.64           C  
ANISOU 3997  CB  ASN C1049    14180  14398  19540  -1400  -1283  -1109       C  
ATOM   3998  CG  ASN C1049      30.474  88.216 103.983  1.00125.37           C  
ANISOU 3998  CG  ASN C1049    14208  14218  19209  -1552  -1344  -1203       C  
ATOM   3999  OD1 ASN C1049      29.541  87.864 104.709  1.00124.21           O  
ANISOU 3999  OD1 ASN C1049    14121  14106  18965  -1747  -1465  -1307       O  
ATOM   4000  ND2 ASN C1049      30.326  88.437 102.676  1.00124.43           N  
ANISOU 4000  ND2 ASN C1049    14180  14048  19049  -1465  -1263  -1153       N  
ATOM   4001  N   GLN C1050      34.295  89.814 105.654  1.00125.60           N  
ANISOU 4001  N   GLN C1050    13453  14382  19887  -1218  -1224   -911       N  
ATOM   4002  CA  GLN C1050      35.698  89.864 106.099  1.00126.21           C  
ANISOU 4002  CA  GLN C1050    13357  14482  20115  -1082  -1182   -766       C  
ATOM   4003  C   GLN C1050      35.906  90.655 107.398  1.00124.30           C  
ANISOU 4003  C   GLN C1050    12847  14319  20064  -1229  -1311   -803       C  
ATOM   4004  O   GLN C1050      36.581  90.175 108.314  1.00122.78           O  
ANISOU 4004  O   GLN C1050    12624  14132  19894  -1218  -1352   -766       O  
ATOM   4005  CB  GLN C1050      36.603  90.404 104.974  1.00126.97           C  
ANISOU 4005  CB  GLN C1050    13335  14582  20326   -875  -1034   -585       C  
ATOM   4006  CG  GLN C1050      38.032  90.770 105.390  1.00127.63           C  
ANISOU 4006  CG  GLN C1050    13155  14723  20616   -760  -1002   -403       C  
ATOM   4007  CD  GLN C1050      38.935  89.569 105.637  1.00127.95           C  
ANISOU 4007  CD  GLN C1050    13324  14731  20561   -584   -933   -294       C  
ATOM   4008  OE1 GLN C1050      38.838  88.547 104.958  1.00129.14           O  
ANISOU 4008  OE1 GLN C1050    13765  14801  20501   -441   -834   -285       O  
ATOM   4009  NE2 GLN C1050      39.831  89.698 106.604  1.00127.39           N  
ANISOU 4009  NE2 GLN C1050    13046  14716  20640   -592   -989   -205       N  
ATOM   4010  N   ILE C1051      35.320  91.851 107.470  1.00123.27           N  
ANISOU 4010  N   ILE C1051    12542  14238  20059  -1363  -1378   -876       N  
ATOM   4011  CA  ILE C1051      35.424  92.708 108.665  1.00122.69           C  
ANISOU 4011  CA  ILE C1051    12245  14221  20151  -1506  -1511   -925       C  
ATOM   4012  C   ILE C1051      34.889  91.996 109.914  1.00121.93           C  
ANISOU 4012  C   ILE C1051    12260  14131  19936  -1646  -1623  -1059       C  
ATOM   4013  O   ILE C1051      35.560  91.963 110.947  1.00121.41           O  
ANISOU 4013  O   ILE C1051    12098  14081  19952  -1675  -1695  -1032       O  
ATOM   4014  CB  ILE C1051      34.751  94.092 108.451  1.00121.36           C  
ANISOU 4014  CB  ILE C1051    11918  14089  20104  -1611  -1560   -995       C  
ATOM   4015  CG1 ILE C1051      35.555  94.916 107.431  1.00121.85           C  
ANISOU 4015  CG1 ILE C1051    11816  14152  20330  -1482  -1470   -833       C  
ATOM   4016  CG2 ILE C1051      34.643  94.864 109.763  1.00119.82           C  
ANISOU 4016  CG2 ILE C1051    11569  13933  20025  -1767  -1710  -1080       C  
ATOM   4017  CD1 ILE C1051      34.794  96.056 106.784  1.00120.86           C  
ANISOU 4017  CD1 ILE C1051    11610  14041  20272  -1544  -1478   -891       C  
ATOM   4018  N   VAL C1052      33.702  91.403 109.796  1.00121.66           N  
ANISOU 4018  N   VAL C1052    12432  14087  19706  -1735  -1639  -1189       N  
ATOM   4019  CA  VAL C1052      33.110  90.602 110.876  1.00121.11           C  
ANISOU 4019  CA  VAL C1052    12493  14028  19496  -1868  -1736  -1306       C  
ATOM   4020  C   VAL C1052      33.963  89.363 111.217  1.00121.37           C  
ANISOU 4020  C   VAL C1052    12666  14009  19442  -1770  -1712  -1230       C  
ATOM   4021  O   VAL C1052      34.275  89.136 112.392  1.00119.10           O  
ANISOU 4021  O   VAL C1052    12334  13739  19178  -1836  -1798  -1255       O  
ATOM   4022  CB  VAL C1052      31.630  90.253 110.565  1.00120.80           C  
ANISOU 4022  CB  VAL C1052    12631  14002  19267  -1993  -1761  -1431       C  
ATOM   4023  CG1 VAL C1052      31.118  89.113 111.434  1.00120.89           C  
ANISOU 4023  CG1 VAL C1052    12829  14011  19091  -2103  -1838  -1511       C  
ATOM   4024  CG2 VAL C1052      30.755  91.483 110.759  1.00120.26           C  
ANISOU 4024  CG2 VAL C1052    12391  14010  19291  -2117  -1818  -1526       C  
ATOM   4025  N   ILE C1053      34.349  88.589 110.195  1.00122.48           N  
ANISOU 4025  N   ILE C1053    12981  14079  19478  -1603  -1596  -1136       N  
ATOM   4026  CA  ILE C1053      35.248  87.434 110.369  1.00124.47           C  
ANISOU 4026  CA  ILE C1053    13376  14271  19644  -1463  -1551  -1043       C  
ATOM   4027  C   ILE C1053      36.507  87.830 111.143  1.00127.37           C  
ANISOU 4027  C   ILE C1053    13500  14680  20214  -1402  -1569   -929       C  
ATOM   4028  O   ILE C1053      36.909  87.122 112.074  1.00129.04           O  
ANISOU 4028  O   ILE C1053    13758  14884  20388  -1416  -1625   -926       O  
ATOM   4029  CB  ILE C1053      35.683  86.802 109.025  1.00124.95           C  
ANISOU 4029  CB  ILE C1053    13629  14251  19597  -1238  -1397   -927       C  
ATOM   4030  CG1 ILE C1053      34.483  86.250 108.255  1.00125.45           C  
ANISOU 4030  CG1 ILE C1053    13982  14251  19433  -1304  -1398  -1027       C  
ATOM   4031  CG2 ILE C1053      36.679  85.673 109.262  1.00125.84           C  
ANISOU 4031  CG2 ILE C1053    13877  14305  19629  -1066  -1344   -821       C  
ATOM   4032  CD1 ILE C1053      34.751  86.044 106.776  1.00126.27           C  
ANISOU 4032  CD1 ILE C1053    14242  14278  19457  -1102  -1251   -928       C  
ATOM   4033  N   THR C1054      37.120  88.953 110.746  1.00127.87           N  
ANISOU 4033  N   THR C1054    13309  14788  20490  -1344  -1531   -826       N  
ATOM   4034  CA  THR C1054      38.296  89.508 111.426  1.00127.57           C  
ANISOU 4034  CA  THR C1054    13009  14796  20666  -1315  -1570   -696       C  
ATOM   4035  C   THR C1054      37.992  89.690 112.908  1.00126.42           C  
ANISOU 4035  C   THR C1054    12799  14679  20553  -1517  -1739   -817       C  
ATOM   4036  O   THR C1054      38.740  89.203 113.750  1.00127.60           O  
ANISOU 4036  O   THR C1054    12922  14832  20729  -1503  -1786   -756       O  
ATOM   4037  CB  THR C1054      38.752  90.856 110.807  1.00128.65           C  
ANISOU 4037  CB  THR C1054    12881  14976  21023  -1282  -1539   -589       C  
ATOM   4038  OG1 THR C1054      39.083  90.668 109.428  1.00131.68           O  
ANISOU 4038  OG1 THR C1054    13324  15338  21371  -1081  -1372   -465       O  
ATOM   4039  CG2 THR C1054      39.978  91.409 111.516  1.00129.72           C  
ANISOU 4039  CG2 THR C1054    12751  15159  21377  -1275  -1602   -433       C  
ATOM   4040  N   ILE C1055      36.882  90.366 113.212  1.00124.52           N  
ANISOU 4040  N   ILE C1055    12547  14464  20302  -1694  -1824   -983       N  
ATOM   4041  CA  ILE C1055      36.449  90.605 114.597  1.00123.13           C  
ANISOU 4041  CA  ILE C1055    12330  14318  20136  -1881  -1976  -1113       C  
ATOM   4042  C   ILE C1055      36.275  89.290 115.369  1.00123.31           C  
ANISOU 4042  C   ILE C1055    12555  14319  19978  -1917  -2014  -1173       C  
ATOM   4043  O   ILE C1055      36.752  89.160 116.500  1.00122.84           O  
ANISOU 4043  O   ILE C1055    12442  14270  19963  -1977  -2109  -1171       O  
ATOM   4044  CB  ILE C1055      35.167  91.484 114.652  1.00120.99           C  
ANISOU 4044  CB  ILE C1055    12038  14083  19850  -2031  -2032  -1277       C  
ATOM   4045  CG1 ILE C1055      35.453  92.865 114.040  1.00120.65           C  
ANISOU 4045  CG1 ILE C1055    11786  14052  20004  -2002  -2017  -1213       C  
ATOM   4046  CG2 ILE C1055      34.654  91.632 116.083  1.00119.03           C  
ANISOU 4046  CG2 ILE C1055    11782  13868  19576  -2201  -2172  -1413       C  
ATOM   4047  CD1 ILE C1055      34.227  93.658 113.628  1.00119.53           C  
ANISOU 4047  CD1 ILE C1055    11644  13938  19835  -2085  -2021  -1340       C  
ATOM   4048  N   PHE C1056      35.626  88.311 114.741  1.00124.03           N  
ANISOU 4048  N   PHE C1056    12888  14372  19863  -1884  -1948  -1217       N  
ATOM   4049  CA  PHE C1056      35.440  86.990 115.351  1.00125.19           C  
ANISOU 4049  CA  PHE C1056    13259  14486  19821  -1917  -1984  -1265       C  
ATOM   4050  C   PHE C1056      36.704  86.131 115.369  1.00125.78           C  
ANISOU 4050  C   PHE C1056    13381  14511  19899  -1742  -1929  -1115       C  
ATOM   4051  O   PHE C1056      36.731  85.081 116.021  1.00127.07           O  
ANISOU 4051  O   PHE C1056    13710  14642  19929  -1762  -1972  -1141       O  
ATOM   4052  CB  PHE C1056      34.299  86.227 114.677  1.00125.98           C  
ANISOU 4052  CB  PHE C1056    13624  14553  19691  -1959  -1955  -1353       C  
ATOM   4053  CG  PHE C1056      32.940  86.603 115.185  1.00127.18           C  
ANISOU 4053  CG  PHE C1056    13774  14770  19777  -2172  -2048  -1512       C  
ATOM   4054  CD1 PHE C1056      32.065  87.334 114.387  1.00127.64           C  
ANISOU 4054  CD1 PHE C1056    13794  14862  19842  -2215  -2018  -1558       C  
ATOM   4055  CD2 PHE C1056      32.529  86.228 116.463  1.00128.11           C  
ANISOU 4055  CD2 PHE C1056    13924  14927  19824  -2323  -2160  -1606       C  
ATOM   4056  CE1 PHE C1056      30.802  87.682 114.852  1.00128.38           C  
ANISOU 4056  CE1 PHE C1056    13872  15034  19874  -2395  -2094  -1687       C  
ATOM   4057  CE2 PHE C1056      31.267  86.573 116.934  1.00128.21           C  
ANISOU 4057  CE2 PHE C1056    13924  15019  19770  -2503  -2231  -1735       C  
ATOM   4058  CZ  PHE C1056      30.403  87.303 116.129  1.00128.21           C  
ANISOU 4058  CZ  PHE C1056    13876  15059  19779  -2534  -2195  -1771       C  
ATOM   4059  N   THR C1057      37.736  86.563 114.646  1.00124.52           N  
ANISOU 4059  N   THR C1057    13075  14350  19885  -1565  -1831   -948       N  
ATOM   4060  CA  THR C1057      39.041  85.915 114.716  1.00125.17           C  
ANISOU 4060  CA  THR C1057    13142  14412  20006  -1382  -1772   -774       C  
ATOM   4061  C   THR C1057      39.708  86.349 116.022  1.00125.46           C  
ANISOU 4061  C   THR C1057    12964  14498  20205  -1481  -1901   -742       C  
ATOM   4062  O   THR C1057      40.222  85.516 116.777  1.00126.85           O  
ANISOU 4062  O   THR C1057    13205  14658  20333  -1459  -1940   -706       O  
ATOM   4063  CB  THR C1057      39.938  86.271 113.506  1.00125.80           C  
ANISOU 4063  CB  THR C1057    13112  14495  20192  -1154  -1618   -580       C  
ATOM   4064  OG1 THR C1057      39.283  85.905 112.284  1.00124.74           O  
ANISOU 4064  OG1 THR C1057    13197  14304  19895  -1068  -1506   -618       O  
ATOM   4065  CG2 THR C1057      41.283  85.552 113.590  1.00127.38           C  
ANISOU 4065  CG2 THR C1057    13287  14690  20421   -944  -1544   -380       C  
ATOM   4066  N   ILE C1058      39.662  87.657 116.283  1.00123.73           N  
ANISOU 4066  N   ILE C1058    12508  14331  20170  -1596  -1975   -758       N  
ATOM   4067  CA  ILE C1058      40.264  88.282 117.464  1.00121.50           C  
ANISOU 4067  CA  ILE C1058    12023  14086  20055  -1708  -2117   -727       C  
ATOM   4068  C   ILE C1058      39.487  87.950 118.746  1.00120.62           C  
ANISOU 4068  C   ILE C1058    12026  13971  19831  -1902  -2256   -912       C  
ATOM   4069  O   ILE C1058      40.065  87.924 119.837  1.00120.66           O  
ANISOU 4069  O   ILE C1058    11956  13985  19904  -1968  -2367   -882       O  
ATOM   4070  CB  ILE C1058      40.384  89.822 117.284  1.00120.19           C  
ANISOU 4070  CB  ILE C1058    11610  13957  20101  -1775  -2164   -694       C  
ATOM   4071  CG1 ILE C1058      40.882  90.192 115.873  1.00119.97           C  
ANISOU 4071  CG1 ILE C1058    11488  13938  20157  -1599  -2015   -535       C  
ATOM   4072  CG2 ILE C1058      41.249  90.454 118.374  1.00120.86           C  
ANISOU 4072  CG2 ILE C1058    11492  14063  20368  -1869  -2314   -611       C  
ATOM   4073  CD1 ILE C1058      42.219  89.602 115.458  1.00121.70           C  
ANISOU 4073  CD1 ILE C1058    11637  14170  20434  -1386  -1911   -290       C  
ATOM   4074  N   GLU C1059      38.185  87.687 118.610  1.00118.94           N  
ANISOU 4074  N   GLU C1059    11993  13753  19446  -1993  -2250  -1088       N  
ATOM   4075  CA  GLU C1059      37.341  87.348 119.760  1.00118.15           C  
ANISOU 4075  CA  GLU C1059    12003  13666  19221  -2172  -2367  -1257       C  
ATOM   4076  C   GLU C1059      37.708  86.009 120.404  1.00119.10           C  
ANISOU 4076  C   GLU C1059    12289  13753  19212  -2150  -2390  -1236       C  
ATOM   4077  O   GLU C1059      37.816  85.911 121.630  1.00118.77           O  
ANISOU 4077  O   GLU C1059    12228  13724  19174  -2261  -2508  -1282       O  
ATOM   4078  CB  GLU C1059      35.859  87.374 119.381  1.00116.49           C  
ANISOU 4078  CB  GLU C1059    11926  13477  18859  -2271  -2349  -1418       C  
ATOM   4079  CG  GLU C1059      35.240  88.758 119.439  1.00115.60           C  
ANISOU 4079  CG  GLU C1059    11655  13414  18855  -2369  -2392  -1501       C  
ATOM   4080  CD  GLU C1059      33.743  88.749 119.200  1.00114.66           C  
ANISOU 4080  CD  GLU C1059    11649  13335  18582  -2472  -2382  -1648       C  
ATOM   4081  OE1 GLU C1059      33.026  87.967 119.858  1.00114.70           O  
ANISOU 4081  OE1 GLU C1059    11800  13361  18418  -2576  -2431  -1741       O  
ATOM   4082  OE2 GLU C1059      33.280  89.544 118.360  1.00114.85           O  
ANISOU 4082  OE2 GLU C1059    11604  13376  18657  -2454  -2330  -1660       O  
ATOM   4083  N   ILE C1060      37.901  84.987 119.573  1.00120.09           N  
ANISOU 4083  N   ILE C1060    12590  13826  19213  -2000  -2280  -1167       N  
ATOM   4084  CA  ILE C1060      38.264  83.652 120.057  1.00121.45           C  
ANISOU 4084  CA  ILE C1060    12949  13950  19246  -1954  -2292  -1139       C  
ATOM   4085  C   ILE C1060      39.706  83.617 120.599  1.00123.58           C  
ANISOU 4085  C   ILE C1060    13060  14223  19670  -1851  -2312   -972       C  
ATOM   4086  O   ILE C1060      39.992  82.921 121.576  1.00123.82           O  
ANISOU 4086  O   ILE C1060    13156  14241  19649  -1894  -2392   -977       O  
ATOM   4087  CB  ILE C1060      37.997  82.559 118.978  1.00121.70           C  
ANISOU 4087  CB  ILE C1060    13260  13905  19076  -1817  -2175  -1120       C  
ATOM   4088  CG1 ILE C1060      37.862  81.167 119.610  1.00121.32           C  
ANISOU 4088  CG1 ILE C1060    13474  13798  18823  -1844  -2226  -1161       C  
ATOM   4089  CG2 ILE C1060      39.038  82.581 117.858  1.00123.01           C  
ANISOU 4089  CG2 ILE C1060    13374  14042  19324  -1558  -2024   -933       C  
ATOM   4090  CD1 ILE C1060      36.425  80.708 119.786  1.00120.41           C  
ANISOU 4090  CD1 ILE C1060    13571  13678  18501  -2037  -2296  -1332       C  
ATOM   4091  N   ILE C1061      40.594  84.394 119.973  1.00124.95           N  
ANISOU 4091  N   ILE C1061    13016  14423  20037  -1724  -2246   -812       N  
ATOM   4092  CA  ILE C1061      41.994  84.523 120.403  1.00126.85           C  
ANISOU 4092  CA  ILE C1061    13056  14689  20454  -1634  -2269   -617       C  
ATOM   4093  C   ILE C1061      42.120  84.977 121.868  1.00127.50           C  
ANISOU 4093  C   ILE C1061    13015  14799  20629  -1831  -2455   -669       C  
ATOM   4094  O   ILE C1061      42.947  84.448 122.625  1.00129.00           O  
ANISOU 4094  O   ILE C1061    13178  14988  20849  -1806  -2513   -573       O  
ATOM   4095  CB  ILE C1061      42.788  85.470 119.466  1.00127.05           C  
ANISOU 4095  CB  ILE C1061    12838  14756  20681  -1502  -2180   -434       C  
ATOM   4096  CG1 ILE C1061      43.068  84.774 118.126  1.00128.53           C  
ANISOU 4096  CG1 ILE C1061    13151  14911  20772  -1247  -1982   -321       C  
ATOM   4097  CG2 ILE C1061      44.099  85.911 120.112  1.00128.09           C  
ANISOU 4097  CG2 ILE C1061    12704  14936  21028  -1488  -2257   -235       C  
ATOM   4098  CD1 ILE C1061      43.651  85.673 117.047  1.00128.62           C  
ANISOU 4098  CD1 ILE C1061    12953  14967  20950  -1114  -1872   -156       C  
ATOM   4099  N   LEU C1062      41.292  85.948 122.254  1.00126.15           N  
ANISOU 4099  N   LEU C1062    12785  14650  20495  -2016  -2548   -820       N  
ATOM   4100  CA  LEU C1062      41.273  86.478 123.619  1.00125.16           C  
ANISOU 4100  CA  LEU C1062    12579  14540  20436  -2206  -2726   -893       C  
ATOM   4101  C   LEU C1062      40.665  85.478 124.612  1.00124.49           C  
ANISOU 4101  C   LEU C1062    12706  14438  20159  -2310  -2797  -1035       C  
ATOM   4102  O   LEU C1062      41.167  85.327 125.736  1.00123.70           O  
ANISOU 4102  O   LEU C1062    12573  14334  20091  -2387  -2919  -1015       O  
ATOM   4103  CB  LEU C1062      40.492  87.800 123.667  1.00124.51           C  
ANISOU 4103  CB  LEU C1062    12407  14479  20424  -2344  -2786  -1018       C  
ATOM   4104  CG  LEU C1062      40.935  88.959 122.764  1.00125.17           C  
ANISOU 4104  CG  LEU C1062    12284  14576  20698  -2281  -2742   -904       C  
ATOM   4105  CD1 LEU C1062      39.806  89.971 122.604  1.00123.22           C  
ANISOU 4105  CD1 LEU C1062    12039  14340  20441  -2391  -2764  -1071       C  
ATOM   4106  CD2 LEU C1062      42.206  89.624 123.293  1.00126.96           C  
ANISOU 4106  CD2 LEU C1062    12287  14809  21144  -2299  -2854   -724       C  
ATOM   4107  N   ARG C1063      39.597  84.799 124.182  1.00122.68           N  
ANISOU 4107  N   ARG C1063    12691  14196  19727  -2321  -2728  -1165       N  
ATOM   4108  CA  ARG C1063      38.865  83.851 125.026  1.00121.78           C  
ANISOU 4108  CA  ARG C1063    12787  14072  19412  -2436  -2792  -1300       C  
ATOM   4109  C   ARG C1063      39.682  82.610 125.386  1.00122.28           C  
ANISOU 4109  C   ARG C1063    12963  14091  19408  -2344  -2794  -1200       C  
ATOM   4110  O   ARG C1063      39.578  82.105 126.509  1.00122.49           O  
ANISOU 4110  O   ARG C1063    13068  14115  19359  -2457  -2901  -1264       O  
ATOM   4111  CB  ARG C1063      37.562  83.420 124.357  1.00121.77           C  
ANISOU 4111  CB  ARG C1063    12981  14072  19215  -2474  -2724  -1428       C  
ATOM   4112  CG  ARG C1063      36.403  84.394 124.490  1.00121.77           C  
ANISOU 4112  CG  ARG C1063    12923  14133  19212  -2624  -2760  -1578       C  
ATOM   4113  CD  ARG C1063      35.226  83.887 123.665  1.00121.51           C  
ANISOU 4113  CD  ARG C1063    13069  14105  18993  -2645  -2687  -1660       C  
ATOM   4114  NE  ARG C1063      34.076  84.786 123.686  1.00121.37           N  
ANISOU 4114  NE  ARG C1063    12988  14160  18969  -2768  -2705  -1784       N  
ATOM   4115  CZ  ARG C1063      32.958  84.586 122.990  1.00122.87           C  
ANISOU 4115  CZ  ARG C1063    13288  14375  19022  -2812  -2656  -1849       C  
ATOM   4116  NH1 ARG C1063      32.829  83.514 122.211  1.00125.24           N  
ANISOU 4116  NH1 ARG C1063    13792  14620  19174  -2755  -2598  -1809       N  
ATOM   4117  NH2 ARG C1063      31.961  85.457 123.067  1.00122.38           N  
ANISOU 4117  NH2 ARG C1063    13143  14392  18965  -2911  -2671  -1947       N  
ATOM   4118  N   ILE C1064      40.486  82.128 124.435  1.00122.11           N  
ANISOU 4118  N   ILE C1064    12954  14034  19408  -2131  -2672  -1042       N  
ATOM   4119  CA  ILE C1064      41.347  80.944 124.635  1.00122.86           C  
ANISOU 4119  CA  ILE C1064    13159  14083  19440  -1996  -2651   -924       C  
ATOM   4120  C   ILE C1064      42.246  81.066 125.873  1.00123.45           C  
ANISOU 4120  C   ILE C1064    13082  14180  19641  -2057  -2782   -847       C  
ATOM   4121  O   ILE C1064      42.565  80.058 126.519  1.00123.40           O  
ANISOU 4121  O   ILE C1064    13205  14142  19541  -2040  -2823   -826       O  
ATOM   4122  CB  ILE C1064      42.199  80.637 123.372  1.00123.56           C  
ANISOU 4122  CB  ILE C1064    13241  14144  19562  -1721  -2482   -736       C  
ATOM   4123  CG1 ILE C1064      41.333  79.985 122.289  1.00123.55           C  
ANISOU 4123  CG1 ILE C1064    13509  14081  19352  -1650  -2368   -817       C  
ATOM   4124  CG2 ILE C1064      43.376  79.721 123.692  1.00124.01           C  
ANISOU 4124  CG2 ILE C1064    13319  14176  19622  -1555  -2464   -566       C  
ATOM   4125  CD1 ILE C1064      41.866  80.172 120.883  1.00124.27           C  
ANISOU 4125  CD1 ILE C1064    13562  14160  19495  -1412  -2196   -672       C  
ATOM   4126  N   TYR C1065      42.627  82.302 126.205  1.00123.42           N  
ANISOU 4126  N   TYR C1065    12822  14226  19846  -2136  -2858   -805       N  
ATOM   4127  CA  TYR C1065      43.534  82.574 127.320  1.00123.33           C  
ANISOU 4127  CA  TYR C1065    12652  14232  19976  -2207  -3000   -712       C  
ATOM   4128  C   TYR C1065      42.836  82.856 128.649  1.00121.82           C  
ANISOU 4128  C   TYR C1065    12510  14044  19732  -2449  -3169   -892       C  
ATOM   4129  O   TYR C1065      43.475  82.833 129.703  1.00122.26           O  
ANISOU 4129  O   TYR C1065    12502  14097  19852  -2523  -3301   -840       O  
ATOM   4130  CB  TYR C1065      44.502  83.697 126.952  1.00124.40           C  
ANISOU 4130  CB  TYR C1065    12492  14408  20367  -2156  -3007   -527       C  
ATOM   4131  CG  TYR C1065      45.557  83.245 125.973  1.00125.81           C  
ANISOU 4131  CG  TYR C1065    12589  14599  20612  -1899  -2859   -287       C  
ATOM   4132  CD1 TYR C1065      45.327  83.297 124.596  1.00125.35           C  
ANISOU 4132  CD1 TYR C1065    12562  14542  20525  -1740  -2684   -259       C  
ATOM   4133  CD2 TYR C1065      46.778  82.739 126.424  1.00126.93           C  
ANISOU 4133  CD2 TYR C1065    12632  14759  20837  -1804  -2889    -81       C  
ATOM   4134  CE1 TYR C1065      46.292  82.867 123.697  1.00127.25           C  
ANISOU 4134  CE1 TYR C1065    12742  14798  20810  -1482  -2533    -35       C  
ATOM   4135  CE2 TYR C1065      47.747  82.309 125.534  1.00128.75           C  
ANISOU 4135  CE2 TYR C1065    12784  15015  21119  -1543  -2738    153       C  
ATOM   4136  CZ  TYR C1065      47.502  82.375 124.174  1.00128.77           C  
ANISOU 4136  CZ  TYR C1065    12827  15017  21084  -1377  -2555    174       C  
ATOM   4137  OH  TYR C1065      48.469  81.948 123.292  1.00130.86           O  
ANISOU 4137  OH  TYR C1065    13024  15311  21387  -1097  -2392    413       O  
ATOM   4138  N   VAL C1066      41.529  83.109 128.595  1.00119.66           N  
ANISOU 4138  N   VAL C1066    12351  13780  19336  -2565  -3162  -1093       N  
ATOM   4139  CA  VAL C1066      40.732  83.290 129.805  1.00119.05           C  
ANISOU 4139  CA  VAL C1066    12347  13716  19173  -2772  -3295  -1270       C  
ATOM   4140  C   VAL C1066      40.443  81.933 130.459  1.00120.38           C  
ANISOU 4140  C   VAL C1066    12737  13863  19141  -2808  -3321  -1331       C  
ATOM   4141  O   VAL C1066      40.563  81.785 131.677  1.00121.52           O  
ANISOU 4141  O   VAL C1066    12904  14005  19263  -2926  -3451  -1370       O  
ATOM   4142  CB  VAL C1066      39.407  84.042 129.518  1.00116.93           C  
ANISOU 4142  CB  VAL C1066    12106  13482  18839  -2869  -3268  -1446       C  
ATOM   4143  CG1 VAL C1066      38.620  84.289 130.801  1.00115.50           C  
ANISOU 4143  CG1 VAL C1066    11990  13327  18568  -3060  -3393  -1613       C  
ATOM   4144  CG2 VAL C1066      39.681  85.360 128.809  1.00116.98           C  
ANISOU 4144  CG2 VAL C1066    11910  13500  19036  -2827  -3241  -1386       C  
ATOM   4145  N   HIS C1067      40.091  80.943 129.641  1.00120.82           N  
ANISOU 4145  N   HIS C1067    12969  13892  19045  -2707  -3205  -1332       N  
ATOM   4146  CA  HIS C1067      39.580  79.670 130.145  1.00121.15           C  
ANISOU 4146  CA  HIS C1067    13258  13906  18867  -2763  -3232  -1410       C  
ATOM   4147  C   HIS C1067      40.569  78.527 130.017  1.00123.79           C  
ANISOU 4147  C   HIS C1067    13687  14177  19169  -2602  -3198  -1265       C  
ATOM   4148  O   HIS C1067      40.817  77.792 130.981  1.00124.22           O  
ANISOU 4148  O   HIS C1067    13832  14211  19154  -2657  -3289  -1268       O  
ATOM   4149  CB  HIS C1067      38.281  79.309 129.425  1.00119.46           C  
ANISOU 4149  CB  HIS C1067    13225  13698  18466  -2804  -3158  -1532       C  
ATOM   4150  CG  HIS C1067      37.375  80.493 129.122  1.00118.32           C  
ANISOU 4150  CG  HIS C1067    12965  13619  18371  -2894  -3142  -1636       C  
ATOM   4151  ND1 HIS C1067      37.563  81.303 128.050  1.00117.47           N  
ANISOU 4151  ND1 HIS C1067    12725  13516  18393  -2787  -3048  -1577       N  
ATOM   4152  CD2 HIS C1067      36.228  80.958 129.768  1.00117.16           C  
ANISOU 4152  CD2 HIS C1067    12827  13541  18147  -3074  -3203  -1793       C  
ATOM   4153  CE1 HIS C1067      36.599  82.246 128.025  1.00115.93           C  
ANISOU 4153  CE1 HIS C1067    12460  13381  18206  -2896  -3057  -1694       C  
ATOM   4154  NE2 HIS C1067      35.779  82.033 129.071  1.00115.92           N  
ANISOU 4154  NE2 HIS C1067    12544  13422  18077  -3064  -3147  -1824       N  
ATOM   4155  N   ARG C1068      41.137  78.383 128.819  1.00125.82           N  
ANISOU 4155  N   ARG C1068    13929  14405  19472  -2390  -3061  -1134       N  
ATOM   4156  CA  ARG C1068      41.982  77.238 128.425  1.00128.27           C  
ANISOU 4156  CA  ARG C1068    14369  14650  19719  -2183  -2986   -991       C  
ATOM   4157  C   ARG C1068      41.316  75.854 128.557  1.00129.23           C  
ANISOU 4157  C   ARG C1068    14830  14699  19571  -2210  -2995  -1083       C  
ATOM   4158  O   ARG C1068      40.695  75.380 127.603  1.00130.59           O  
ANISOU 4158  O   ARG C1068    15201  14823  19595  -2150  -2905  -1124       O  
ATOM   4159  CB  ARG C1068      43.370  77.276 129.091  1.00129.98           C  
ANISOU 4159  CB  ARG C1068    14401  14881  20105  -2105  -3042   -813       C  
ATOM   4160  CG  ARG C1068      44.410  76.440 128.352  1.00132.21           C  
ANISOU 4160  CG  ARG C1068    14732  15120  20381  -1821  -2916   -614       C  
ATOM   4161  CD  ARG C1068      44.719  77.021 126.973  1.00132.98           C  
ANISOU 4161  CD  ARG C1068    14713  15236  20577  -1633  -2754   -501       C  
ATOM   4162  NE  ARG C1068      44.920  75.988 125.955  1.00133.46           N  
ANISOU 4162  NE  ARG C1068    14999  15223  20485  -1381  -2596   -425       N  
ATOM   4163  CZ  ARG C1068      45.457  76.201 124.754  1.00133.61           C  
ANISOU 4163  CZ  ARG C1068    14949  15249  20566  -1148  -2433   -280       C  
ATOM   4164  NH1 ARG C1068      45.868  77.414 124.403  1.00133.34           N  
ANISOU 4164  NH1 ARG C1068    14608  15298  20756  -1143  -2408   -185       N  
ATOM   4165  NH2 ARG C1068      45.596  75.195 123.902  1.00134.18           N  
ANISOU 4165  NH2 ARG C1068    15275  15239  20470   -914  -2295   -224       N  
ATOM   4166  N   ILE C1069      41.445  75.212 129.720  1.00129.81           N  
ANISOU 4166  N   ILE C1069    14982  14759  19580  -2309  -3113  -1111       N  
ATOM   4167  CA  ILE C1069      40.933  73.846 129.914  1.00129.61           C  
ANISOU 4167  CA  ILE C1069    15284  14659  19304  -2337  -3138  -1176       C  
ATOM   4168  C   ILE C1069      39.419  73.804 130.147  1.00128.28           C  
ANISOU 4168  C   ILE C1069    15260  14516  18966  -2572  -3199  -1370       C  
ATOM   4169  O   ILE C1069      38.779  72.771 129.932  1.00129.23           O  
ANISOU 4169  O   ILE C1069    15666  14572  18863  -2602  -3203  -1423       O  
ATOM   4170  CB  ILE C1069      41.687  73.090 131.042  1.00131.91           C  
ANISOU 4170  CB  ILE C1069    15615  14923  19582  -2341  -3240  -1117       C  
ATOM   4171  CG1 ILE C1069      41.436  71.574 130.944  1.00133.02           C  
ANISOU 4171  CG1 ILE C1069    16115  14957  19470  -2292  -3236  -1135       C  
ATOM   4172  CG2 ILE C1069      41.333  73.654 132.421  1.00131.42           C  
ANISOU 4172  CG2 ILE C1069    15432  14932  19571  -2591  -3398  -1223       C  
ATOM   4173  CD1 ILE C1069      42.418  70.720 131.725  1.00134.40           C  
ANISOU 4173  CD1 ILE C1069    16344  15085  19637  -2206  -3294  -1030       C  
ATOM   4174  N   SER C1070      38.851  74.929 130.576  1.00126.19           N  
ANISOU 4174  N   SER C1070    14801  14345  18799  -2735  -3249  -1464       N  
ATOM   4175  CA  SER C1070      37.401  75.043 130.756  1.00123.60           C  
ANISOU 4175  CA  SER C1070    14562  14071  18329  -2942  -3290  -1627       C  
ATOM   4176  C   SER C1070      36.641  75.262 129.433  1.00121.87           C  
ANISOU 4176  C   SER C1070    14401  13849  18054  -2902  -3183  -1653       C  
ATOM   4177  O   SER C1070      35.418  75.130 129.388  1.00120.29           O  
ANISOU 4177  O   SER C1070    14310  13687  17707  -3055  -3207  -1760       O  
ATOM   4178  CB  SER C1070      37.083  76.160 131.756  1.00121.26           C  
ANISOU 4178  CB  SER C1070    14054  13874  18144  -3109  -3378  -1715       C  
ATOM   4179  OG  SER C1070      37.541  75.814 133.046  1.00119.70           O  
ANISOU 4179  OG  SER C1070    13863  13675  17945  -3186  -3496  -1715       O  
ATOM   4180  N   PHE C1071      37.377  75.597 128.372  1.00121.75           N  
ANISOU 4180  N   PHE C1071    14304  13797  18158  -2697  -3067  -1543       N  
ATOM   4181  CA  PHE C1071      36.802  75.926 127.067  1.00121.65           C  
ANISOU 4181  CA  PHE C1071    14324  13779  18120  -2639  -2961  -1554       C  
ATOM   4182  C   PHE C1071      36.658  74.665 126.220  1.00122.35           C  
ANISOU 4182  C   PHE C1071    14738  13753  17997  -2536  -2906  -1520       C  
ATOM   4183  O   PHE C1071      35.585  74.388 125.667  1.00120.99           O  
ANISOU 4183  O   PHE C1071    14737  13569  17665  -2631  -2904  -1594       O  
ATOM   4184  CB  PHE C1071      37.693  76.943 126.344  1.00122.03           C  
ANISOU 4184  CB  PHE C1071    14124  13844  18399  -2467  -2863  -1443       C  
ATOM   4185  CG  PHE C1071      37.015  77.663 125.211  1.00121.88           C  
ANISOU 4185  CG  PHE C1071    14063  13848  18398  -2452  -2775  -1476       C  
ATOM   4186  CD1 PHE C1071      36.491  78.943 125.399  1.00121.82           C  
ANISOU 4186  CD1 PHE C1071    13835  13932  18517  -2572  -2802  -1551       C  
ATOM   4187  CD2 PHE C1071      36.923  77.082 123.949  1.00122.34           C  
ANISOU 4187  CD2 PHE C1071    14313  13828  18342  -2309  -2665  -1428       C  
ATOM   4188  CE1 PHE C1071      35.876  79.624 124.354  1.00121.67           C  
ANISOU 4188  CE1 PHE C1071    13773  13937  18521  -2555  -2722  -1577       C  
ATOM   4189  CE2 PHE C1071      36.311  77.755 122.899  1.00122.44           C  
ANISOU 4189  CE2 PHE C1071    14287  13861  18374  -2300  -2589  -1454       C  
ATOM   4190  CZ  PHE C1071      35.785  79.027 123.101  1.00122.08           C  
ANISOU 4190  CZ  PHE C1071    14005  13917  18465  -2425  -2617  -1527       C  
ATOM   4191  N   PHE C1072      37.750  73.907 126.125  1.00122.95           N  
ANISOU 4191  N   PHE C1072    14906  13743  18069  -2340  -2865  -1399       N  
ATOM   4192  CA  PHE C1072      37.768  72.658 125.373  1.00122.98           C  
ANISOU 4192  CA  PHE C1072    15253  13614  17861  -2208  -2815  -1357       C  
ATOM   4193  C   PHE C1072      36.963  71.565 126.086  1.00123.33           C  
ANISOU 4193  C   PHE C1072    15579  13612  17669  -2396  -2942  -1452       C  
ATOM   4194  O   PHE C1072      36.757  70.472 125.543  1.00124.66           O  
ANISOU 4194  O   PHE C1072    16084  13657  17623  -2339  -2935  -1440       O  
ATOM   4195  CB  PHE C1072      39.210  72.217 125.105  1.00123.68           C  
ANISOU 4195  CB  PHE C1072    15342  13633  18018  -1918  -2724  -1188       C  
ATOM   4196  CG  PHE C1072      39.931  73.072 124.094  1.00123.36           C  
ANISOU 4196  CG  PHE C1072    15092  13621  18158  -1706  -2576  -1069       C  
ATOM   4197  CD1 PHE C1072      41.041  73.820 124.466  1.00123.53           C  
ANISOU 4197  CD1 PHE C1072    14789  13719  18427  -1612  -2556   -945       C  
ATOM   4198  CD2 PHE C1072      39.503  73.127 122.766  1.00122.69           C  
ANISOU 4198  CD2 PHE C1072    15136  13486  17993  -1609  -2466  -1069       C  
ATOM   4199  CE1 PHE C1072      41.712  74.608 123.536  1.00123.52           C  
ANISOU 4199  CE1 PHE C1072    14585  13754  18594  -1426  -2424   -817       C  
ATOM   4200  CE2 PHE C1072      40.167  73.912 121.835  1.00122.54           C  
ANISOU 4200  CE2 PHE C1072    14923  13498  18136  -1413  -2326   -953       C  
ATOM   4201  CZ  PHE C1072      41.275  74.652 122.221  1.00123.06           C  
ANISOU 4201  CZ  PHE C1072    14654  13650  18452  -1322  -2304   -823       C  
ATOM   4202  N   LYS C1073      36.512  71.880 127.302  1.00121.70           N  
ANISOU 4202  N   LYS C1073    15242  13502  17495  -2619  -3061  -1540       N  
ATOM   4203  CA  LYS C1073      35.529  71.069 128.026  1.00119.74           C  
ANISOU 4203  CA  LYS C1073    15207  13253  17037  -2847  -3188  -1638       C  
ATOM   4204  C   LYS C1073      34.168  71.787 128.132  1.00117.45           C  
ANISOU 4204  C   LYS C1073    14818  13086  16723  -3085  -3231  -1755       C  
ATOM   4205  O   LYS C1073      33.413  71.582 129.088  1.00116.19           O  
ANISOU 4205  O   LYS C1073    14683  12995  16471  -3301  -3339  -1833       O  
ATOM   4206  CB  LYS C1073      36.075  70.659 129.403  1.00118.82           C  
ANISOU 4206  CB  LYS C1073    15063  13148  16937  -2907  -3292  -1634       C  
ATOM   4207  CG  LYS C1073      37.123  69.555 129.324  1.00119.67           C  
ANISOU 4207  CG  LYS C1073    15371  13119  16978  -2705  -3273  -1525       C  
ATOM   4208  CD  LYS C1073      37.961  69.438 130.590  1.00119.74           C  
ANISOU 4208  CD  LYS C1073    15263  13152  17080  -2714  -3353  -1489       C  
ATOM   4209  CE  LYS C1073      37.334  68.522 131.626  1.00118.80           C  
ANISOU 4209  CE  LYS C1073    15347  13019  16771  -2922  -3496  -1569       C  
ATOM   4210  NZ  LYS C1073      38.201  68.433 132.831  1.00118.43           N  
ANISOU 4210  NZ  LYS C1073    15187  12991  16821  -2923  -3575  -1528       N  
ATOM   4211  N   ASP C1074      33.877  72.635 127.145  1.00116.29           N  
ANISOU 4211  N   ASP C1074    14554  12972  16660  -3032  -3139  -1755       N  
ATOM   4212  CA  ASP C1074      32.566  73.262 127.021  1.00116.30           C  
ANISOU 4212  CA  ASP C1074    14481  13082  16625  -3223  -3161  -1847       C  
ATOM   4213  C   ASP C1074      31.977  73.103 125.602  1.00117.64           C  
ANISOU 4213  C   ASP C1074    14812  13195  16692  -3181  -3094  -1828       C  
ATOM   4214  O   ASP C1074      32.617  73.477 124.610  1.00118.09           O  
ANISOU 4214  O   ASP C1074    14825  13195  16847  -2980  -2981  -1763       O  
ATOM   4215  CB  ASP C1074      32.608  74.732 127.417  1.00114.98           C  
ANISOU 4215  CB  ASP C1074    13963  13043  16681  -3247  -3138  -1887       C  
ATOM   4216  CG  ASP C1074      31.226  75.359 127.461  1.00114.73           C  
ANISOU 4216  CG  ASP C1074    13851  13138  16602  -3438  -3162  -1980       C  
ATOM   4217  OD1 ASP C1074      30.938  76.230 126.604  1.00114.52           O  
ANISOU 4217  OD1 ASP C1074    13699  13148  16666  -3392  -3085  -1983       O  
ATOM   4218  OD2 ASP C1074      30.420  74.964 128.338  1.00114.00           O  
ANISOU 4218  OD2 ASP C1074    13819  13117  16379  -3631  -3256  -2041       O  
ATOM   4219  N   PRO C1075      30.750  72.547 125.510  1.00117.08           N  
ANISOU 4219  N   PRO C1075    14926  13141  16419  -3378  -3171  -1875       N  
ATOM   4220  CA  PRO C1075      30.112  72.273 124.232  1.00116.86           C  
ANISOU 4220  CA  PRO C1075    15091  13048  16263  -3374  -3140  -1854       C  
ATOM   4221  C   PRO C1075      29.802  73.547 123.448  1.00116.00           C  
ANISOU 4221  C   PRO C1075    14742  13023  16308  -3335  -3046  -1866       C  
ATOM   4222  O   PRO C1075      30.220  73.679 122.291  1.00115.74           O  
ANISOU 4222  O   PRO C1075    14765  12904  16307  -3159  -2947  -1813       O  
ATOM   4223  CB  PRO C1075      28.811  71.566 124.640  1.00118.51           C  
ANISOU 4223  CB  PRO C1075    15473  13304  16253  -3650  -3274  -1894       C  
ATOM   4224  CG  PRO C1075      29.043  71.090 126.048  1.00118.06           C  
ANISOU 4224  CG  PRO C1075    15407  13280  16170  -3744  -3366  -1920       C  
ATOM   4225  CD  PRO C1075      29.884  72.164 126.639  1.00116.86           C  
ANISOU 4225  CD  PRO C1075    14927  13205  16271  -3628  -3299  -1938       C  
ATOM   4226  N   TRP C1076      29.086  74.481 124.077  1.00114.37           N  
ANISOU 4226  N   TRP C1076    14280  12983  16193  -3486  -3072  -1934       N  
ATOM   4227  CA  TRP C1076      28.721  75.740 123.420  1.00112.94           C  
ANISOU 4227  CA  TRP C1076    13867  12889  16156  -3459  -2993  -1952       C  
ATOM   4228  C   TRP C1076      29.936  76.468 122.891  1.00113.07           C  
ANISOU 4228  C   TRP C1076    13726  12851  16383  -3218  -2878  -1901       C  
ATOM   4229  O   TRP C1076      29.869  77.125 121.842  1.00112.52           O  
ANISOU 4229  O   TRP C1076    13588  12778  16389  -3130  -2792  -1878       O  
ATOM   4230  CB  TRP C1076      27.918  76.635 124.358  1.00110.87           C  
ANISOU 4230  CB  TRP C1076    13356  12807  15961  -3624  -3035  -2031       C  
ATOM   4231  CG  TRP C1076      26.778  75.937 125.051  1.00109.68           C  
ANISOU 4231  CG  TRP C1076    13320  12739  15613  -3862  -3146  -2063       C  
ATOM   4232  CD1 TRP C1076      26.712  75.548 126.381  1.00109.76           C  
ANISOU 4232  CD1 TRP C1076    13327  12807  15568  -3980  -3232  -2098       C  
ATOM   4233  CD2 TRP C1076      25.502  75.524 124.470  1.00110.19           C  
ANISOU 4233  CD2 TRP C1076    13517  12849  15502  -4029  -3192  -2047       C  
ATOM   4234  NE1 TRP C1076      25.515  74.948 126.664  1.00109.42           N  
ANISOU 4234  NE1 TRP C1076    13392  12849  15335  -4198  -3318  -2101       N  
ATOM   4235  CE2 TRP C1076      24.741  74.897 125.552  1.00110.59           C  
ANISOU 4235  CE2 TRP C1076    13621  12995  15403  -4243  -3305  -2065       C  
ATOM   4236  CE3 TRP C1076      24.930  75.597 123.196  1.00110.30           C  
ANISOU 4236  CE3 TRP C1076    13609  12835  15464  -4029  -3161  -2009       C  
ATOM   4237  CZ2 TRP C1076      23.464  74.369 125.347  1.00110.60           C  
ANISOU 4237  CZ2 TRP C1076    13736  13071  15218  -4455  -3385  -2032       C  
ATOM   4238  CZ3 TRP C1076      23.644  75.066 123.007  1.00109.73           C  
ANISOU 4238  CZ3 TRP C1076    13661  12829  15204  -4247  -3249  -1983       C  
ATOM   4239  CH2 TRP C1076      22.932  74.472 124.061  1.00110.08           C  
ANISOU 4239  CH2 TRP C1076    13739  12974  15112  -4457  -3360  -1988       C  
ATOM   4240  N   SER C1077      31.052  76.341 123.618  1.00113.50           N  
ANISOU 4240  N   SER C1077    13721  12870  16534  -3116  -2882  -1869       N  
ATOM   4241  CA  SER C1077      32.358  76.863 123.197  1.00113.77           C  
ANISOU 4241  CA  SER C1077    13612  12853  16761  -2884  -2784  -1784       C  
ATOM   4242  C   SER C1077      32.945  76.089 122.006  1.00114.27           C  
ANISOU 4242  C   SER C1077    13903  12773  16740  -2679  -2692  -1687       C  
ATOM   4243  O   SER C1077      33.389  76.686 121.023  1.00113.70           O  
ANISOU 4243  O   SER C1077    13741  12681  16778  -2518  -2581  -1625       O  
ATOM   4244  CB  SER C1077      33.336  76.835 124.372  1.00114.08           C  
ANISOU 4244  CB  SER C1077    13536  12901  16910  -2855  -2834  -1760       C  
ATOM   4245  OG  SER C1077      32.817  77.547 125.479  1.00114.06           O  
ANISOU 4245  OG  SER C1077    13353  13016  16968  -3031  -2917  -1852       O  
ATOM   4246  N   LEU C1078      32.945  74.760 122.107  1.00114.84           N  
ANISOU 4246  N   LEU C1078    14284  12741  16608  -2681  -2740  -1672       N  
ATOM   4247  CA  LEU C1078      33.373  73.896 121.016  1.00116.34           C  
ANISOU 4247  CA  LEU C1078    14761  12778  16666  -2490  -2664  -1592       C  
ATOM   4248  C   LEU C1078      32.449  74.020 119.790  1.00116.97           C  
ANISOU 4248  C   LEU C1078    14974  12830  16640  -2527  -2630  -1612       C  
ATOM   4249  O   LEU C1078      32.839  73.655 118.676  1.00117.64           O  
ANISOU 4249  O   LEU C1078    15247  12795  16655  -2337  -2538  -1543       O  
ATOM   4250  CB  LEU C1078      33.435  72.440 121.484  1.00117.57           C  
ANISOU 4250  CB  LEU C1078    15250  12820  16602  -2513  -2747  -1586       C  
ATOM   4251  CG  LEU C1078      34.697  71.908 122.165  1.00118.10           C  
ANISOU 4251  CG  LEU C1078    15318  12834  16721  -2350  -2736  -1511       C  
ATOM   4252  CD1 LEU C1078      34.330  70.811 123.154  1.00118.48           C  
ANISOU 4252  CD1 LEU C1078    15590  12843  16585  -2511  -2878  -1560       C  
ATOM   4253  CD2 LEU C1078      35.706  71.396 121.144  1.00119.14           C  
ANISOU 4253  CD2 LEU C1078    15620  12829  16819  -2032  -2602  -1389       C  
ATOM   4254  N   PHE C1079      31.227  74.519 119.995  1.00115.79           N  
ANISOU 4254  N   PHE C1079    14733  12792  16472  -2764  -2704  -1698       N  
ATOM   4255  CA  PHE C1079      30.365  74.865 118.869  1.00115.60           C  
ANISOU 4255  CA  PHE C1079    14764  12769  16391  -2808  -2673  -1709       C  
ATOM   4256  C   PHE C1079      30.876  76.124 118.202  1.00115.20           C  
ANISOU 4256  C   PHE C1079    14434  12767  16567  -2653  -2545  -1677       C  
ATOM   4257  O   PHE C1079      30.819  76.246 116.980  1.00115.17           O  
ANISOU 4257  O   PHE C1079    14523  12701  16536  -2547  -2465  -1637       O  
ATOM   4258  CB  PHE C1079      28.913  75.082 119.298  1.00115.52           C  
ANISOU 4258  CB  PHE C1079    14702  12886  16305  -3099  -2784  -1789       C  
ATOM   4259  CG  PHE C1079      27.998  75.443 118.154  1.00115.06           C  
ANISOU 4259  CG  PHE C1079    14687  12837  16192  -3156  -2764  -1787       C  
ATOM   4260  CD1 PHE C1079      27.431  74.447 117.358  1.00116.23           C  
ANISOU 4260  CD1 PHE C1079    15196  12865  16101  -3214  -2819  -1757       C  
ATOM   4261  CD2 PHE C1079      27.722  76.772 117.859  1.00113.53           C  
ANISOU 4261  CD2 PHE C1079    14193  12763  16181  -3152  -2698  -1810       C  
ATOM   4262  CE1 PHE C1079      26.601  74.776 116.298  1.00116.31           C  
ANISOU 4262  CE1 PHE C1079    15252  12881  16060  -3274  -2812  -1746       C  
ATOM   4263  CE2 PHE C1079      26.894  77.108 116.803  1.00113.83           C  
ANISOU 4263  CE2 PHE C1079    14267  12811  16172  -3201  -2682  -1802       C  
ATOM   4264  CZ  PHE C1079      26.334  76.109 116.019  1.00115.48           C  
ANISOU 4264  CZ  PHE C1079    14824  12906  16146  -3265  -2739  -1768       C  
ATOM   4265  N   ASP C1080      31.361  77.054 119.025  1.00115.72           N  
ANISOU 4265  N   ASP C1080    14175  12941  16851  -2649  -2537  -1692       N  
ATOM   4266  CA  ASP C1080      31.863  78.343 118.566  1.00116.21           C  
ANISOU 4266  CA  ASP C1080    13947  13061  17149  -2530  -2439  -1660       C  
ATOM   4267  C   ASP C1080      33.219  78.244 117.870  1.00117.20           C  
ANISOU 4267  C   ASP C1080    14077  13094  17361  -2249  -2315  -1532       C  
ATOM   4268  O   ASP C1080      33.445  78.908 116.859  1.00117.12           O  
ANISOU 4268  O   ASP C1080    13978  13078  17443  -2122  -2211  -1480       O  
ATOM   4269  CB  ASP C1080      31.955  79.323 119.734  1.00116.93           C  
ANISOU 4269  CB  ASP C1080    13725  13278  17425  -2628  -2493  -1712       C  
ATOM   4270  CG  ASP C1080      30.597  79.831 120.193  1.00117.48           C  
ANISOU 4270  CG  ASP C1080    13716  13469  17453  -2859  -2571  -1825       C  
ATOM   4271  OD1 ASP C1080      29.563  79.308 119.715  1.00116.57           O  
ANISOU 4271  OD1 ASP C1080    13783  13351  17159  -2971  -2600  -1853       O  
ATOM   4272  OD2 ASP C1080      30.578  80.766 121.041  1.00118.03           O  
ANISOU 4272  OD2 ASP C1080    13542  13637  17665  -2925  -2605  -1875       O  
ATOM   4273  N   PHE C1081      34.119  77.424 118.411  1.00118.54           N  
ANISOU 4273  N   PHE C1081    14341  13200  17500  -2146  -2322  -1473       N  
ATOM   4274  CA  PHE C1081      35.470  77.309 117.860  1.00120.15           C  
ANISOU 4274  CA  PHE C1081    14523  13338  17791  -1862  -2198  -1329       C  
ATOM   4275  C   PHE C1081      35.459  76.600 116.510  1.00121.97           C  
ANISOU 4275  C   PHE C1081    15057  13439  17848  -1690  -2097  -1272       C  
ATOM   4276  O   PHE C1081      36.293  76.888 115.642  1.00123.37           O  
ANISOU 4276  O   PHE C1081    15175  13589  18111  -1453  -1958  -1156       O  
ATOM   4277  CB  PHE C1081      36.408  76.585 118.829  1.00120.94           C  
ANISOU 4277  CB  PHE C1081    14645  13410  17896  -1794  -2236  -1271       C  
ATOM   4278  CG  PHE C1081      37.870  76.756 118.501  1.00122.79           C  
ANISOU 4278  CG  PHE C1081    14737  13633  18286  -1519  -2116  -1101       C  
ATOM   4279  CD1 PHE C1081      38.653  77.664 119.210  1.00122.88           C  
ANISOU 4279  CD1 PHE C1081    14397  13743  18547  -1522  -2136  -1039       C  
ATOM   4280  CD2 PHE C1081      38.472  76.007 117.488  1.00124.15           C  
ANISOU 4280  CD2 PHE C1081    15129  13694  18347  -1255  -1986   -988       C  
ATOM   4281  CE1 PHE C1081      40.002  77.827 118.916  1.00123.06           C  
ANISOU 4281  CE1 PHE C1081    14264  13774  18721  -1282  -2034   -854       C  
ATOM   4282  CE2 PHE C1081      39.816  76.169 117.187  1.00125.07           C  
ANISOU 4282  CE2 PHE C1081    15092  13822  18607   -990  -1863   -809       C  
ATOM   4283  CZ  PHE C1081      40.583  77.079 117.906  1.00124.72           C  
ANISOU 4283  CZ  PHE C1081    14669  13895  18825  -1011  -1889   -734       C  
ATOM   4284  N   PHE C1082      34.515  75.672 116.345  1.00122.22           N  
ANISOU 4284  N   PHE C1082    15420  13389  17629  -1813  -2172  -1346       N  
ATOM   4285  CA  PHE C1082      34.382  74.894 115.115  1.00122.12           C  
ANISOU 4285  CA  PHE C1082    15764  13228  17408  -1678  -2107  -1307       C  
ATOM   4286  C   PHE C1082      33.545  75.608 114.045  1.00122.11           C  
ANISOU 4286  C   PHE C1082    15742  13248  17407  -1738  -2072  -1339       C  
ATOM   4287  O   PHE C1082      33.631  75.262 112.866  1.00123.20           O  
ANISOU 4287  O   PHE C1082    16115  13271  17424  -1581  -1986  -1286       O  
ATOM   4288  CB  PHE C1082      33.801  73.511 115.413  1.00121.55           C  
ANISOU 4288  CB  PHE C1082    16093  13038  17054  -1791  -2225  -1357       C  
ATOM   4289  CG  PHE C1082      34.821  72.493 115.860  1.00121.76           C  
ANISOU 4289  CG  PHE C1082    16294  12964  17007  -1610  -2207  -1285       C  
ATOM   4290  CD1 PHE C1082      34.973  72.183 117.206  1.00121.07           C  
ANISOU 4290  CD1 PHE C1082    16124  12927  16949  -1730  -2312  -1318       C  
ATOM   4291  CD2 PHE C1082      35.601  71.811 114.929  1.00122.98           C  
ANISOU 4291  CD2 PHE C1082    16713  12968  17046  -1311  -2083  -1183       C  
ATOM   4292  CE1 PHE C1082      35.894  71.227 117.618  1.00121.98           C  
ANISOU 4292  CE1 PHE C1082    16404  12949  16993  -1562  -2300  -1248       C  
ATOM   4293  CE2 PHE C1082      36.524  70.854 115.335  1.00123.86           C  
ANISOU 4293  CE2 PHE C1082    16993  12987  17080  -1126  -2061  -1110       C  
ATOM   4294  CZ  PHE C1082      36.672  70.562 116.682  1.00123.02           C  
ANISOU 4294  CZ  PHE C1082    16790  12935  17015  -1256  -2173  -1142       C  
ATOM   4295  N   VAL C1083      32.740  76.593 114.446  1.00121.50           N  
ANISOU 4295  N   VAL C1083    15399  13312  17454  -1953  -2136  -1422       N  
ATOM   4296  CA  VAL C1083      31.995  77.407 113.471  1.00121.68           C  
ANISOU 4296  CA  VAL C1083    15354  13372  17508  -2002  -2099  -1444       C  
ATOM   4297  C   VAL C1083      32.853  78.533 112.888  1.00121.90           C  
ANISOU 4297  C   VAL C1083    15094  13449  17774  -1808  -1958  -1365       C  
ATOM   4298  O   VAL C1083      32.712  78.887 111.710  1.00121.70           O  
ANISOU 4298  O   VAL C1083    15111  13389  17740  -1718  -1873  -1331       O  
ATOM   4299  CB  VAL C1083      30.661  77.968 114.033  1.00120.64           C  
ANISOU 4299  CB  VAL C1083    15081  13372  17385  -2301  -2221  -1556       C  
ATOM   4300  CG1 VAL C1083      30.888  79.039 115.089  1.00118.04           C  
ANISOU 4300  CG1 VAL C1083    14364  13193  17294  -2366  -2240  -1595       C  
ATOM   4301  CG2 VAL C1083      29.809  78.526 112.901  1.00121.07           C  
ANISOU 4301  CG2 VAL C1083    15150  13438  17415  -2349  -2194  -1567       C  
ATOM   4302  N   VAL C1084      33.735  79.080 113.724  1.00121.32           N  
ANISOU 4302  N   VAL C1084    14734  13454  17908  -1755  -1945  -1329       N  
ATOM   4303  CA  VAL C1084      34.626  80.168 113.341  1.00120.96           C  
ANISOU 4303  CA  VAL C1084    14387  13466  18105  -1596  -1835  -1236       C  
ATOM   4304  C   VAL C1084      35.664  79.708 112.316  1.00122.54           C  
ANISOU 4304  C   VAL C1084    14718  13569  18273  -1291  -1679  -1088       C  
ATOM   4305  O   VAL C1084      35.885  80.390 111.317  1.00123.25           O  
ANISOU 4305  O   VAL C1084    14713  13667  18449  -1168  -1569  -1021       O  
ATOM   4306  CB  VAL C1084      35.305  80.787 114.584  1.00120.93           C  
ANISOU 4306  CB  VAL C1084    14070  13561  18315  -1642  -1891  -1224       C  
ATOM   4307  CG1 VAL C1084      36.524  81.618 114.202  1.00122.61           C  
ANISOU 4307  CG1 VAL C1084    14017  13810  18761  -1446  -1782  -1077       C  
ATOM   4308  CG2 VAL C1084      34.308  81.635 115.362  1.00119.73           C  
ANISOU 4308  CG2 VAL C1084    13738  13519  18233  -1900  -2008  -1359       C  
ATOM   4309  N   ALA C1085      36.284  78.552 112.567  1.00123.38           N  
ANISOU 4309  N   ALA C1085    15047  13584  18247  -1162  -1665  -1033       N  
ATOM   4310  CA  ALA C1085      37.313  77.990 111.681  1.00124.24           C  
ANISOU 4310  CA  ALA C1085    15308  13599  18299   -839  -1506   -882       C  
ATOM   4311  C   ALA C1085      36.792  77.731 110.263  1.00124.33           C  
ANISOU 4311  C   ALA C1085    15605  13503  18131   -748  -1424   -883       C  
ATOM   4312  O   ALA C1085      37.457  78.065 109.280  1.00124.20           O  
ANISOU 4312  O   ALA C1085    15546  13473  18170   -514  -1268   -765       O  
ATOM   4313  CB  ALA C1085      37.894  76.716 112.281  1.00125.19           C  
ANISOU 4313  CB  ALA C1085    15660  13632  18276   -736  -1525   -843       C  
ATOM   4314  N   ILE C1086      35.598  77.141 110.175  1.00124.31           N  
ANISOU 4314  N   ILE C1086    15891  13428  17912   -943  -1537  -1008       N  
ATOM   4315  CA  ILE C1086      34.922  76.882 108.899  1.00124.33           C  
ANISOU 4315  CA  ILE C1086    16192  13321  17726   -915  -1502  -1024       C  
ATOM   4316  C   ILE C1086      34.498  78.210 108.263  1.00123.88           C  
ANISOU 4316  C   ILE C1086    15861  13367  17841   -980  -1461  -1037       C  
ATOM   4317  O   ILE C1086      34.350  78.305 107.041  1.00124.99           O  
ANISOU 4317  O   ILE C1086    16148  13439  17905   -871  -1375  -1001       O  
ATOM   4318  CB  ILE C1086      33.718  75.920 109.075  1.00124.13           C  
ANISOU 4318  CB  ILE C1086    16528  13202  17432  -1150  -1666  -1139       C  
ATOM   4319  CG1 ILE C1086      34.200  74.541 109.563  1.00125.05           C  
ANISOU 4319  CG1 ILE C1086    16968  13188  17356  -1056  -1699  -1115       C  
ATOM   4320  CG2 ILE C1086      32.917  75.787 107.780  1.00124.63           C  
ANISOU 4320  CG2 ILE C1086    16876  13163  17316  -1167  -1659  -1154       C  
ATOM   4321  CD1 ILE C1086      33.113  73.635 110.117  1.00124.30           C  
ANISOU 4321  CD1 ILE C1086    17157  13032  17038  -1331  -1894  -1220       C  
ATOM   4322  N   SER C1087      34.328  79.235 109.100  1.00122.47           N  
ANISOU 4322  N   SER C1087    15299  13345  17890  -1149  -1525  -1086       N  
ATOM   4323  CA  SER C1087      34.106  80.603 108.631  1.00121.42           C  
ANISOU 4323  CA  SER C1087    14863  13316  17956  -1188  -1483  -1087       C  
ATOM   4324  C   SER C1087      35.392  81.210 108.049  1.00122.69           C  
ANISOU 4324  C   SER C1087    14820  13500  18298   -916  -1317   -931       C  
ATOM   4325  O   SER C1087      35.339  82.140 107.246  1.00122.30           O  
ANISOU 4325  O   SER C1087    14616  13490  18361   -877  -1245   -898       O  
ATOM   4326  CB  SER C1087      33.566  81.474 109.770  1.00119.07           C  
ANISOU 4326  CB  SER C1087    14252  13163  17826  -1436  -1607  -1187       C  
ATOM   4327  OG  SER C1087      33.319  82.798 109.335  1.00117.71           O  
ANISOU 4327  OG  SER C1087    13809  13080  17836  -1473  -1575  -1192       O  
ATOM   4328  N   LEU C1088      36.542  80.675 108.456  1.00124.73           N  
ANISOU 4328  N   LEU C1088    15069  13738  18583   -730  -1257   -823       N  
ATOM   4329  CA  LEU C1088      37.836  81.134 107.956  1.00126.71           C  
ANISOU 4329  CA  LEU C1088    15120  14025  18998   -461  -1096   -641       C  
ATOM   4330  C   LEU C1088      38.347  80.331 106.754  1.00128.66           C  
ANISOU 4330  C   LEU C1088    15674  14149  19063   -160   -931   -528       C  
ATOM   4331  O   LEU C1088      39.283  80.761 106.068  1.00129.41           O  
ANISOU 4331  O   LEU C1088    15622  14278  19270     79   -774   -366       O  
ATOM   4332  CB  LEU C1088      38.877  81.128 109.080  1.00127.81           C  
ANISOU 4332  CB  LEU C1088    15026  14238  19298   -417  -1120   -555       C  
ATOM   4333  CG  LEU C1088      38.919  82.379 109.953  1.00127.34           C  
ANISOU 4333  CG  LEU C1088    14553  14318  19510   -605  -1217   -580       C  
ATOM   4334  CD1 LEU C1088      39.485  82.042 111.326  1.00128.19           C  
ANISOU 4334  CD1 LEU C1088    14557  14465  19685   -664  -1315   -567       C  
ATOM   4335  CD2 LEU C1088      39.722  83.488 109.280  1.00127.88           C  
ANISOU 4335  CD2 LEU C1088    14316  14466  19807   -468  -1106   -425       C  
ATOM   4336  N   VAL C1089      37.745  79.165 106.515  1.00129.06           N  
ANISOU 4336  N   VAL C1089    16158  14054  18825   -168   -970   -604       N  
ATOM   4337  CA  VAL C1089      38.032  78.375 105.314  1.00131.36           C  
ANISOU 4337  CA  VAL C1089    16818  14199  18896    101   -830   -525       C  
ATOM   4338  C   VAL C1089      37.692  79.221 104.079  1.00131.10           C  
ANISOU 4338  C   VAL C1089    16735  14176  18902    136   -743   -506       C  
ATOM   4339  O   VAL C1089      36.561  79.700 103.954  1.00129.68           O  
ANISOU 4339  O   VAL C1089    16546  14014  18715   -114   -852   -632       O  
ATOM   4340  CB  VAL C1089      37.261  77.030 105.303  1.00131.83           C  
ANISOU 4340  CB  VAL C1089    17383  14083  18624     27   -932   -630       C  
ATOM   4341  CG1 VAL C1089      37.413  76.314 103.965  1.00133.28           C  
ANISOU 4341  CG1 VAL C1089    17989  14093  18559    288   -803   -565       C  
ATOM   4342  CG2 VAL C1089      37.741  76.132 106.436  1.00132.64           C  
ANISOU 4342  CG2 VAL C1089    17556  14163  18679     38   -997   -628       C  
ATOM   4343  N   PRO C1090      38.678  79.424 103.177  1.00132.05           N  
ANISOU 4343  N   PRO C1090    16809  14297  19067    451   -543   -336       N  
ATOM   4344  CA  PRO C1090      38.527  80.343 102.047  1.00132.47           C  
ANISOU 4344  CA  PRO C1090    16757  14382  19196    502   -446   -294       C  
ATOM   4345  C   PRO C1090      37.299  80.083 101.172  1.00132.97           C  
ANISOU 4345  C   PRO C1090    17171  14320  19033    377   -507   -418       C  
ATOM   4346  O   PRO C1090      36.715  78.997 101.218  1.00133.31           O  
ANISOU 4346  O   PRO C1090    17618  14220  18813    318   -594   -505       O  
ATOM   4347  CB  PRO C1090      39.809  80.115 101.241  1.00133.61           C  
ANISOU 4347  CB  PRO C1090    16932  14507  19326    906   -213    -82       C  
ATOM   4348  CG  PRO C1090      40.800  79.669 102.251  1.00133.85           C  
ANISOU 4348  CG  PRO C1090    16826  14592  19439   1013   -201     13       C  
ATOM   4349  CD  PRO C1090      40.017  78.806 103.194  1.00133.15           C  
ANISOU 4349  CD  PRO C1090    16976  14421  19194    785   -391   -160       C  
ATOM   4350  N   THR C1091      36.918  81.090 100.388  1.00133.20           N  
ANISOU 4350  N   THR C1091    17043  14401  19165    328   -472   -419       N  
ATOM   4351  CA  THR C1091      35.868  80.946  99.374  1.00133.44           C  
ANISOU 4351  CA  THR C1091    17385  14319  18996    242   -509   -501       C  
ATOM   4352  C   THR C1091      36.378  80.133  98.163  1.00135.94           C  
ANISOU 4352  C   THR C1091    18111  14472  19070    567   -345   -399       C  
ATOM   4353  O   THR C1091      35.611  79.830  97.242  1.00136.58           O  
ANISOU 4353  O   THR C1091    18531  14424  18939    531   -371   -453       O  
ATOM   4354  CB  THR C1091      35.286  82.328  98.946  1.00131.34           C  
ANISOU 4354  CB  THR C1091    16810  14167  18927     84   -528   -533       C  
ATOM   4355  OG1 THR C1091      34.183  82.143  98.049  1.00130.76           O  
ANISOU 4355  OG1 THR C1091    17040  13989  18656    -31   -589   -615       O  
ATOM   4356  CG2 THR C1091      36.342  83.203  98.272  1.00131.98           C  
ANISOU 4356  CG2 THR C1091    16614  14330  19203    330   -336   -366       C  
ATOM   4357  N   SER C1092      37.666  79.774  98.192  1.00137.68           N  
ANISOU 4357  N   SER C1092    18302  14697  19312    885   -180   -246       N  
ATOM   4358  CA  SER C1092      38.323  79.045  97.096  1.00140.78           C  
ANISOU 4358  CA  SER C1092    19055  14951  19485   1252     10   -125       C  
ATOM   4359  C   SER C1092      38.769  77.636  97.508  1.00141.76           C  
ANISOU 4359  C   SER C1092    19548  14938  19377   1422     19   -108       C  
ATOM   4360  O   SER C1092      39.056  77.390  98.681  1.00141.31           O  
ANISOU 4360  O   SER C1092    19332  14945  19414   1342    -60   -124       O  
ATOM   4361  CB  SER C1092      39.534  79.837  96.571  1.00142.09           C  
ANISOU 4361  CB  SER C1092    18884  15246  19856   1546    238     83       C  
ATOM   4362  OG  SER C1092      39.193  81.175  96.235  1.00140.32           O  
ANISOU 4362  OG  SER C1092    18306  15148  19859   1391    225     76       O  
ATOM   4363  N   SER C1093      38.829  76.730  96.528  1.00143.61           N  
ANISOU 4363  N   SER C1093    20288  14975  19303   1662    112    -77       N  
ATOM   4364  CA  SER C1093      39.280  75.332  96.703  1.00145.66           C  
ANISOU 4364  CA  SER C1093    20981  15067  19295   1881    142    -51       C  
ATOM   4365  C   SER C1093      38.291  74.438  97.461  1.00145.35           C  
ANISOU 4365  C   SER C1093    21256  14902  19069   1580   -108   -227       C  
ATOM   4366  O   SER C1093      37.703  74.851  98.463  1.00143.15           O  
ANISOU 4366  O   SER C1093    20692  14740  18958   1242   -284   -331       O  
ATOM   4367  CB  SER C1093      40.673  75.250  97.352  1.00145.78           C  
ANISOU 4367  CB  SER C1093    20717  15203  19471   2156    293    118       C  
ATOM   4368  OG  SER C1093      41.684  75.745  96.492  1.00145.95           O  
ANISOU 4368  OG  SER C1093    20573  15302  19578   2510    549    318       O  
ATOM   4369  N   GLY C1094      38.125  73.209  96.970  1.00147.41           N  
ANISOU 4369  N   GLY C1094    22117  14919  18971   1712   -123   -250       N  
ATOM   4370  CA  GLY C1094      37.254  72.218  97.605  1.00147.18           C  
ANISOU 4370  CA  GLY C1094    22450  14747  18726   1451   -360   -393       C  
ATOM   4371  C   GLY C1094      35.849  72.212  97.033  1.00146.22           C  
ANISOU 4371  C   GLY C1094    22603  14515  18438   1136   -548   -523       C  
ATOM   4372  O   GLY C1094      35.596  71.583  95.999  1.00147.57           O  
ANISOU 4372  O   GLY C1094    23287  14470  18312   1256   -534   -521       O  
ATOM   4373  N   PHE C1095      34.936  72.900  97.727  1.00143.03           N  
ANISOU 4373  N   PHE C1095    21865  14261  18219    736   -727   -629       N  
ATOM   4374  CA  PHE C1095      33.555  73.104  97.261  1.00141.86           C  
ANISOU 4374  CA  PHE C1095    21859  14067  17973    404   -909   -733       C  
ATOM   4375  C   PHE C1095      32.911  74.408  97.764  1.00138.63           C  
ANISOU 4375  C   PHE C1095    20893  13902  17880     97   -987   -792       C  
ATOM   4376  O   PHE C1095      33.581  75.271  98.342  1.00137.02           O  
ANISOU 4376  O   PHE C1095    20193  13892  17977    157   -888   -750       O  
ATOM   4377  CB  PHE C1095      32.637  71.889  97.539  1.00143.10           C  
ANISOU 4377  CB  PHE C1095    22515  14035  17822    168  -1148   -826       C  
ATOM   4378  CG  PHE C1095      33.156  70.928  98.583  1.00144.68           C  
ANISOU 4378  CG  PHE C1095    22833  14188  17951    224  -1189   -829       C  
ATOM   4379  CD1 PHE C1095      33.247  71.299  99.923  1.00142.43           C  
ANISOU 4379  CD1 PHE C1095    22104  14101  17913     54  -1249   -864       C  
ATOM   4380  CD2 PHE C1095      33.517  69.627  98.224  1.00146.83           C  
ANISOU 4380  CD2 PHE C1095    23692  14204  17894    443  -1178   -801       C  
ATOM   4381  CE1 PHE C1095      33.715  70.400 100.872  1.00143.29           C  
ANISOU 4381  CE1 PHE C1095    22330  14161  17951    101  -1293   -865       C  
ATOM   4382  CE2 PHE C1095      33.981  68.726  99.172  1.00146.56           C  
ANISOU 4382  CE2 PHE C1095    23781  14119  17788    496  -1221   -803       C  
ATOM   4383  CZ  PHE C1095      34.080  69.113 100.496  1.00144.99           C  
ANISOU 4383  CZ  PHE C1095    23116  14126  17846    320  -1279   -834       C  
ATOM   4384  N   GLU C1096      31.608  74.536  97.516  1.00137.09           N  
ANISOU 4384  N   GLU C1096    20798  13687  17602   -227  -1170   -880       N  
ATOM   4385  CA  GLU C1096      30.842  75.728  97.855  1.00134.35           C  
ANISOU 4385  CA  GLU C1096    19988  13550  17510   -512  -1249   -938       C  
ATOM   4386  C   GLU C1096      29.915  75.453  99.045  1.00133.02           C  
ANISOU 4386  C   GLU C1096    19741  13457  17344   -879  -1477  -1038       C  
ATOM   4387  O   GLU C1096      29.299  76.373  99.597  1.00130.31           O  
ANISOU 4387  O   GLU C1096    18996  13304  17213  -1115  -1549  -1090       O  
ATOM   4388  CB  GLU C1096      30.033  76.165  96.633  1.00134.93           C  
ANISOU 4388  CB  GLU C1096    20197  13569  17500   -596  -1274   -943       C  
ATOM   4389  CG  GLU C1096      29.535  77.603  96.649  1.00132.73           C  
ANISOU 4389  CG  GLU C1096    19420  13504  17508   -766  -1275   -967       C  
ATOM   4390  CD  GLU C1096      28.650  77.919  95.455  1.00132.45           C  
ANISOU 4390  CD  GLU C1096    19558  13404  17365   -869  -1323   -971       C  
ATOM   4391  OE1 GLU C1096      27.849  77.043  95.055  1.00131.62           O  
ANISOU 4391  OE1 GLU C1096    19897  13135  16977  -1014  -1476   -998       O  
ATOM   4392  OE2 GLU C1096      28.751  79.048  94.921  1.00132.36           O  
ANISOU 4392  OE2 GLU C1096    19242  13501  17550   -814  -1218   -942       O  
ATOM   4393  N   ILE C1097      29.824  74.176  99.424  1.00134.50           N  
ANISOU 4393  N   ILE C1097    20329  13491  17284   -913  -1587  -1058       N  
ATOM   4394  CA  ILE C1097      29.059  73.737 100.602  1.00132.83           C  
ANISOU 4394  CA  ILE C1097    20084  13339  17046  -1235  -1798  -1136       C  
ATOM   4395  C   ILE C1097      29.575  74.460 101.845  1.00130.34           C  
ANISOU 4395  C   ILE C1097    19240  13245  17039  -1252  -1750  -1154       C  
ATOM   4396  O   ILE C1097      28.788  74.931 102.667  1.00127.10           O  
ANISOU 4396  O   ILE C1097    18549  12993  16750  -1542  -1877  -1221       O  
ATOM   4397  CB  ILE C1097      29.155  72.204 100.830  1.00133.63           C  
ANISOU 4397  CB  ILE C1097    20710  13225  16839  -1209  -1897  -1138       C  
ATOM   4398  CG1 ILE C1097      29.276  71.454  99.496  1.00136.08           C  
ANISOU 4398  CG1 ILE C1097    21587  13270  16847  -1009  -1857  -1090       C  
ATOM   4399  CG2 ILE C1097      27.965  71.709 101.643  1.00132.24           C  
ANISOU 4399  CG2 ILE C1097    20606  13077  16561  -1613  -2158  -1208       C  
ATOM   4400  CD1 ILE C1097      29.852  70.053  99.607  1.00139.49           C  
ANISOU 4400  CD1 ILE C1097    22525  13473  17003   -827  -1869  -1068       C  
ATOM   4401  N   LEU C1098      30.903  74.545 101.949  1.00131.53           N  
ANISOU 4401  N   LEU C1098    19266  13403  17305   -934  -1565  -1083       N  
ATOM   4402  CA  LEU C1098      31.595  75.206 103.061  1.00131.90           C  
ANISOU 4402  CA  LEU C1098    18838  13638  17641   -911  -1511  -1077       C  
ATOM   4403  C   LEU C1098      31.294  76.706 103.079  1.00130.69           C  
ANISOU 4403  C   LEU C1098    18193  13686  17776  -1027  -1484  -1097       C  
ATOM   4404  O   LEU C1098      31.200  77.321 104.150  1.00128.33           O  
ANISOU 4404  O   LEU C1098    17525  13553  17682  -1182  -1541  -1144       O  
ATOM   4405  CB  LEU C1098      33.112  74.972 102.972  1.00132.75           C  
ANISOU 4405  CB  LEU C1098    18935  13705  17799   -526  -1314   -962       C  
ATOM   4406  CG  LEU C1098      33.647  73.547 102.768  1.00134.64           C  
ANISOU 4406  CG  LEU C1098    19675  13730  17754   -309  -1287   -917       C  
ATOM   4407  CD1 LEU C1098      35.072  73.583 102.231  1.00135.60           C  
ANISOU 4407  CD1 LEU C1098    19760  13829  17931    121  -1042   -772       C  
ATOM   4408  CD2 LEU C1098      33.564  72.706 104.038  1.00134.05           C  
ANISOU 4408  CD2 LEU C1098    19677  13644  17614   -455  -1432   -972       C  
ATOM   4409  N   ARG C1099      31.136  77.271 101.879  1.00131.20           N  
ANISOU 4409  N   ARG C1099    18283  13725  17843   -946  -1400  -1062       N  
ATOM   4410  CA  ARG C1099      30.800  78.682 101.689  1.00129.33           C  
ANISOU 4410  CA  ARG C1099    17636  13652  17852  -1041  -1372  -1076       C  
ATOM   4411  C   ARG C1099      29.382  79.012 102.182  1.00127.79           C  
ANISOU 4411  C   ARG C1099    17334  13556  17663  -1413  -1562  -1184       C  
ATOM   4412  O   ARG C1099      29.152  80.092 102.736  1.00126.82           O  
ANISOU 4412  O   ARG C1099    16800  13608  17776  -1533  -1577  -1221       O  
ATOM   4413  CB  ARG C1099      30.964  79.064 100.215  1.00129.76           C  
ANISOU 4413  CB  ARG C1099    17801  13633  17869   -856  -1239  -1007       C  
ATOM   4414  CG  ARG C1099      30.981  80.555  99.941  1.00128.92           C  
ANISOU 4414  CG  ARG C1099    17257  13685  18040   -869  -1165   -990       C  
ATOM   4415  CD  ARG C1099      30.529  80.855  98.521  1.00129.90           C  
ANISOU 4415  CD  ARG C1099    17550  13734  18073   -826  -1117   -965       C  
ATOM   4416  NE  ARG C1099      31.513  80.453  97.518  1.00131.77           N  
ANISOU 4416  NE  ARG C1099    18023  13841  18203   -482   -933   -851       N  
ATOM   4417  CZ  ARG C1099      31.372  80.644  96.208  1.00132.96           C  
ANISOU 4417  CZ  ARG C1099    18352  13908  18259   -375   -855   -808       C  
ATOM   4418  NH1 ARG C1099      30.282  81.233  95.730  1.00132.31           N  
ANISOU 4418  NH1 ARG C1099    18233  13855  18182   -597   -953   -867       N  
ATOM   4419  NH2 ARG C1099      32.321  80.245  95.370  1.00134.49           N  
ANISOU 4419  NH2 ARG C1099    18762  13990  18347    -38   -674   -698       N  
ATOM   4420  N   VAL C1100      28.444  78.084 101.982  1.00127.47           N  
ANISOU 4420  N   VAL C1100    17670  13404  17359  -1589  -1709  -1223       N  
ATOM   4421  CA  VAL C1100      27.065  78.253 102.468  1.00125.63           C  
ANISOU 4421  CA  VAL C1100    17354  13272  17105  -1945  -1896  -1299       C  
ATOM   4422  C   VAL C1100      26.940  77.912 103.961  1.00125.26           C  
ANISOU 4422  C   VAL C1100    17175  13321  17096  -2108  -2005  -1355       C  
ATOM   4423  O   VAL C1100      26.109  78.498 104.666  1.00124.14           O  
ANISOU 4423  O   VAL C1100    16763  13345  17060  -2345  -2100  -1411       O  
ATOM   4424  CB  VAL C1100      26.044  77.438 101.642  1.00125.81           C  
ANISOU 4424  CB  VAL C1100    17816  13150  16835  -2103  -2034  -1296       C  
ATOM   4425  CG1 VAL C1100      24.637  77.631 102.184  1.00124.27           C  
ANISOU 4425  CG1 VAL C1100    17493  13091  16632  -2471  -2223  -1345       C  
ATOM   4426  CG2 VAL C1100      26.095  77.851 100.178  1.00126.61           C  
ANISOU 4426  CG2 VAL C1100    18041  13164  16901  -1958  -1934  -1245       C  
ATOM   4427  N   LEU C1101      27.772  76.981 104.435  1.00124.82           N  
ANISOU 4427  N   LEU C1101    17311  13164  16951  -1969  -1983  -1335       N  
ATOM   4428  CA  LEU C1101      27.821  76.609 105.850  1.00123.34           C  
ANISOU 4428  CA  LEU C1101    17013  13053  16798  -2091  -2072  -1381       C  
ATOM   4429  C   LEU C1101      28.197  77.802 106.738  1.00123.45           C  
ANISOU 4429  C   LEU C1101    16510  13270  17126  -2094  -2014  -1407       C  
ATOM   4430  O   LEU C1101      28.227  77.691 107.971  1.00123.03           O  
ANISOU 4430  O   LEU C1101    16311  13303  17133  -2201  -2084  -1450       O  
ATOM   4431  CB  LEU C1101      28.818  75.467 106.063  1.00123.86           C  
ANISOU 4431  CB  LEU C1101    17372  12962  16725  -1886  -2031  -1339       C  
ATOM   4432  CG  LEU C1101      28.378  74.034 105.756  1.00125.07           C  
ANISOU 4432  CG  LEU C1101    18069  12912  16538  -1950  -2153  -1337       C  
ATOM   4433  CD1 LEU C1101      29.576  73.139 105.470  1.00126.08           C  
ANISOU 4433  CD1 LEU C1101    18503  12858  16542  -1625  -2040  -1272       C  
ATOM   4434  CD2 LEU C1101      27.543  73.464 106.894  1.00124.83           C  
ANISOU 4434  CD2 LEU C1101    18065  12941  16425  -2260  -2353  -1398       C  
ATOM   4435  N   ARG C1102      28.478  78.943 106.107  1.00122.92           N  
ANISOU 4435  N   ARG C1102    16183  13271  17251  -1980  -1895  -1380       N  
ATOM   4436  CA  ARG C1102      28.813  80.170 106.829  1.00121.77           C  
ANISOU 4436  CA  ARG C1102    15570  13299  17399  -1985  -1851  -1400       C  
ATOM   4437  C   ARG C1102      27.567  80.918 107.340  1.00120.69           C  
ANISOU 4437  C   ARG C1102    15206  13320  17330  -2265  -1966  -1484       C  
ATOM   4438  O   ARG C1102      27.659  82.041 107.842  1.00120.38           O  
ANISOU 4438  O   ARG C1102    14803  13418  17518  -2284  -1941  -1511       O  
ATOM   4439  CB  ARG C1102      29.719  81.065 105.975  1.00121.57           C  
ANISOU 4439  CB  ARG C1102    15363  13275  17551  -1742  -1681  -1320       C  
ATOM   4440  CG  ARG C1102      31.138  80.530 105.851  1.00122.05           C  
ANISOU 4440  CG  ARG C1102    15513  13245  17615  -1449  -1551  -1219       C  
ATOM   4441  CD  ARG C1102      31.908  81.214 104.738  1.00122.13           C  
ANISOU 4441  CD  ARG C1102    15428  13240  17738  -1204  -1379  -1116       C  
ATOM   4442  NE  ARG C1102      32.886  80.305 104.143  1.00123.68           N  
ANISOU 4442  NE  ARG C1102    15900  13295  17797   -917  -1255  -1010       N  
ATOM   4443  CZ  ARG C1102      33.479  80.498 102.968  1.00124.88           C  
ANISOU 4443  CZ  ARG C1102    16116  13389  17943   -672  -1096   -907       C  
ATOM   4444  NH1 ARG C1102      33.206  81.578 102.247  1.00125.36           N  
ANISOU 4444  NH1 ARG C1102    15978  13516  18135   -692  -1048   -897       N  
ATOM   4445  NH2 ARG C1102      34.346  79.606 102.509  1.00125.77           N  
ANISOU 4445  NH2 ARG C1102    16498  13377  17911   -396   -980   -810       N  
ATOM   4446  N   VAL C1103      26.410  80.274 107.217  1.00120.40           N  
ANISOU 4446  N   VAL C1103    15396  13263  17089  -2476  -2095  -1515       N  
ATOM   4447  CA  VAL C1103      25.172  80.749 107.835  1.00119.23           C  
ANISOU 4447  CA  VAL C1103    15060  13274  16966  -2746  -2213  -1577       C  
ATOM   4448  C   VAL C1103      24.997  80.097 109.204  1.00118.52           C  
ANISOU 4448  C   VAL C1103    14974  13239  16818  -2893  -2321  -1622       C  
ATOM   4449  O   VAL C1103      23.974  80.300 109.871  1.00117.84           O  
ANISOU 4449  O   VAL C1103    14761  13293  16722  -3118  -2423  -1664       O  
ATOM   4450  CB  VAL C1103      23.933  80.405 106.983  1.00119.55           C  
ANISOU 4450  CB  VAL C1103    15320  13286  16816  -2925  -2311  -1561       C  
ATOM   4451  CG1 VAL C1103      24.028  81.029 105.603  1.00120.30           C  
ANISOU 4451  CG1 VAL C1103    15432  13324  16954  -2793  -2212  -1518       C  
ATOM   4452  CG2 VAL C1103      23.781  78.901 106.874  1.00121.00           C  
ANISOU 4452  CG2 VAL C1103    15948  13311  16717  -2990  -2414  -1535       C  
ATOM   4453  N   LEU C1104      25.985  79.290 109.594  1.00118.49           N  
ANISOU 4453  N   LEU C1104    15125  13129  16767  -2758  -2296  -1603       N  
ATOM   4454  CA  LEU C1104      26.005  78.635 110.907  1.00118.10           C  
ANISOU 4454  CA  LEU C1104    15088  13115  16668  -2869  -2389  -1640       C  
ATOM   4455  C   LEU C1104      26.661  79.504 111.987  1.00116.66           C  
ANISOU 4455  C   LEU C1104    14536  13058  16729  -2817  -2343  -1676       C  
ATOM   4456  O   LEU C1104      26.638  79.153 113.166  1.00116.11           O  
ANISOU 4456  O   LEU C1104    14427  13043  16647  -2919  -2419  -1715       O  
ATOM   4457  CB  LEU C1104      26.686  77.259 110.844  1.00117.06           C  
ANISOU 4457  CB  LEU C1104    15332  12799  16345  -2761  -2402  -1600       C  
ATOM   4458  CG  LEU C1104      26.010  76.066 110.164  1.00115.98           C  
ANISOU 4458  CG  LEU C1104    15646  12512  15909  -2861  -2506  -1575       C  
ATOM   4459  CD1 LEU C1104      27.041  74.976 109.954  1.00116.75           C  
ANISOU 4459  CD1 LEU C1104    16082  12410  15868  -2645  -2461  -1529       C  
ATOM   4460  CD2 LEU C1104      24.836  75.520 110.960  1.00115.10           C  
ANISOU 4460  CD2 LEU C1104    15598  12478  15658  -3179  -2691  -1608       C  
ATOM   4461  N   ARG C1105      27.255  80.624 111.582  1.00111.32           N  
ANISOU 4461  N   ARG C1105    11510  13013  17773  -2176  -3069  -1225       N  
ATOM   4462  CA  ARG C1105      27.712  81.618 112.552  1.00115.19           C  
ANISOU 4462  CA  ARG C1105    12242  13454  18069  -2432  -3172  -1218       C  
ATOM   4463  C   ARG C1105      26.524  82.421 113.097  1.00115.82           C  
ANISOU 4463  C   ARG C1105    12692  13241  18073  -2358  -3120  -1331       C  
ATOM   4464  O   ARG C1105      26.663  83.160 114.076  1.00119.33           O  
ANISOU 4464  O   ARG C1105    13396  13595  18350  -2525  -3184  -1343       O  
ATOM   4465  CB  ARG C1105      28.826  82.535 112.000  1.00116.73           C  
ANISOU 4465  CB  ARG C1105    12465  13743  18144  -2734  -3274  -1148       C  
ATOM   4466  CG  ARG C1105      28.573  83.138 110.627  1.00116.73           C  
ANISOU 4466  CG  ARG C1105    12515  13648  18187  -2709  -3225  -1185       C  
ATOM   4467  CD  ARG C1105      29.326  84.445 110.437  1.00118.55           C  
ANISOU 4467  CD  ARG C1105    12954  13855  18236  -3036  -3327  -1157       C  
ATOM   4468  NE  ARG C1105      29.831  84.599 109.068  1.00119.51           N  
ANISOU 4468  NE  ARG C1105    12920  14074  18414  -3080  -3325  -1114       N  
ATOM   4469  CZ  ARG C1105      29.226  85.271 108.088  1.00118.77           C  
ANISOU 4469  CZ  ARG C1105    12979  13802  18346  -3018  -3261  -1186       C  
ATOM   4470  NH1 ARG C1105      28.060  85.865 108.284  1.00117.88           N  
ANISOU 4470  NH1 ARG C1105    13177  13409  18203  -2890  -3185  -1298       N  
ATOM   4471  NH2 ARG C1105      29.791  85.342 106.891  1.00119.52           N  
ANISOU 4471  NH2 ARG C1105    12908  14012  18492  -3070  -3268  -1136       N  
ATOM   4472  N   LEU C1106      25.362  82.267 112.464  1.00112.96           N  
ANISOU 4472  N   LEU C1106    12356  12742  17820  -2106  -3001  -1402       N  
ATOM   4473  CA  LEU C1106      24.118  82.791 113.014  1.00113.34           C  
ANISOU 4473  CA  LEU C1106    12698  12552  17812  -1962  -2927  -1488       C  
ATOM   4474  C   LEU C1106      23.691  81.927 114.205  1.00112.87           C  
ANISOU 4474  C   LEU C1106    12583  12520  17783  -1833  -2910  -1494       C  
ATOM   4475  O   LEU C1106      23.090  82.418 115.165  1.00112.56           O  
ANISOU 4475  O   LEU C1106    12808  12325  17636  -1804  -2895  -1537       O  
ATOM   4476  CB  LEU C1106      23.011  82.833 111.943  1.00112.17           C  
ANISOU 4476  CB  LEU C1106    12554  12299  17768  -1731  -2805  -1538       C  
ATOM   4477  CG  LEU C1106      23.270  83.579 110.621  1.00112.15           C  
ANISOU 4477  CG  LEU C1106    12582  12266  17764  -1809  -2801  -1537       C  
ATOM   4478  CD1 LEU C1106      22.059  83.484 109.711  1.00109.55           C  
ANISOU 4478  CD1 LEU C1106    12236  11850  17537  -1557  -2676  -1579       C  
ATOM   4479  CD2 LEU C1106      23.654  85.040 110.832  1.00114.71           C  
ANISOU 4479  CD2 LEU C1106    13261  12438  17886  -2031  -2857  -1554       C  
ATOM   4480  N   PHE C1107      24.029  80.640 114.138  1.00112.51           N  
ANISOU 4480  N   PHE C1107    12207  12667  17874  -1754  -2910  -1446       N  
ATOM   4481  CA  PHE C1107      23.696  79.686 115.199  1.00112.70           C  
ANISOU 4481  CA  PHE C1107    12146  12737  17938  -1632  -2895  -1444       C  
ATOM   4482  C   PHE C1107      24.479  79.934 116.485  1.00115.34           C  
ANISOU 4482  C   PHE C1107    12571  13118  18134  -1831  -3000  -1410       C  
ATOM   4483  O   PHE C1107      24.280  79.233 117.477  1.00115.94           O  
ANISOU 4483  O   PHE C1107    12599  13229  18225  -1752  -2997  -1407       O  
ATOM   4484  CB  PHE C1107      23.863  78.234 114.719  1.00109.78           C  
ANISOU 4484  CB  PHE C1107    11429  12546  17736  -1490  -2857  -1399       C  
ATOM   4485  CG  PHE C1107      22.675  77.699 113.955  1.00107.52           C  
ANISOU 4485  CG  PHE C1107    11091  12187  17576  -1249  -2741  -1447       C  
ATOM   4486  CD1 PHE C1107      22.708  77.597 112.566  1.00105.84           C  
ANISOU 4486  CD1 PHE C1107    10758  12006  17451  -1212  -2700  -1439       C  
ATOM   4487  CD2 PHE C1107      21.520  77.297 114.626  1.00106.24           C  
ANISOU 4487  CD2 PHE C1107    10994  11938  17434  -1071  -2676  -1491       C  
ATOM   4488  CE1 PHE C1107      21.620  77.094 111.862  1.00103.36           C  
ANISOU 4488  CE1 PHE C1107    10396  11639  17237  -1017  -2602  -1473       C  
ATOM   4489  CE2 PHE C1107      20.430  76.802 113.927  1.00104.10           C  
ANISOU 4489  CE2 PHE C1107    10663  11630  17260   -879  -2579  -1517       C  
ATOM   4490  CZ  PHE C1107      20.482  76.700 112.543  1.00103.18           C  
ANISOU 4490  CZ  PHE C1107    10433  11547  17225   -859  -2544  -1508       C  
ATOM   4491  N   ARG C1108      25.355  80.943 116.458  1.00118.95           N  
ANISOU 4491  N   ARG C1108    13170  13578  18447  -2101  -3094  -1380       N  
ATOM   4492  CA  ARG C1108      26.033  81.458 117.663  1.00122.33           C  
ANISOU 4492  CA  ARG C1108    13765  14017  18697  -2342  -3202  -1351       C  
ATOM   4493  C   ARG C1108      25.033  82.160 118.598  1.00122.65           C  
ANISOU 4493  C   ARG C1108    14184  13796  18621  -2278  -3161  -1438       C  
ATOM   4494  O   ARG C1108      25.306  82.330 119.785  1.00125.01           O  
ANISOU 4494  O   ARG C1108    14623  14081  18794  -2405  -3226  -1429       O  
ATOM   4495  CB  ARG C1108      27.178  82.421 117.287  1.00124.33           C  
ANISOU 4495  CB  ARG C1108    14097  14338  18806  -2676  -3316  -1292       C  
ATOM   4496  CG  ARG C1108      28.324  82.513 118.297  1.00125.72           C  
ANISOU 4496  CG  ARG C1108    14259  14681  18830  -2970  -3457  -1202       C  
ATOM   4497  CD  ARG C1108      29.430  83.417 117.762  1.00128.96           C  
ANISOU 4497  CD  ARG C1108    14715  15187  19098  -3310  -3569  -1128       C  
ATOM   4498  NE  ARG C1108      30.782  83.017 118.177  1.00131.14           N  
ANISOU 4498  NE  ARG C1108    14734  15787  19308  -3546  -3696   -981       N  
ATOM   4499  CZ  ARG C1108      31.549  83.673 119.058  1.00134.47           C  
ANISOU 4499  CZ  ARG C1108    15316  16266  19509  -3887  -3830   -921       C  
ATOM   4500  NH1 ARG C1108      31.120  84.782 119.654  1.00135.72           N  
ANISOU 4500  NH1 ARG C1108    15933  16153  19483  -4040  -3854  -1005       N  
ATOM   4501  NH2 ARG C1108      32.763  83.216 119.350  1.00135.36           N  
ANISOU 4501  NH2 ARG C1108    15140  16721  19572  -4079  -3938   -765       N  
ATOM   4502  N   LEU C1109      23.879  82.552 118.059  1.00120.85           N  
ANISOU 4502  N   LEU C1109    14116  13374  18429  -2072  -3048  -1513       N  
ATOM   4503  CA  LEU C1109      22.803  83.156 118.853  1.00121.03           C  
ANISOU 4503  CA  LEU C1109    14482  13157  18346  -1943  -2978  -1582       C  
ATOM   4504  C   LEU C1109      22.144  82.162 119.832  1.00119.71           C  
ANISOU 4504  C   LEU C1109    14206  13025  18254  -1743  -2934  -1591       C  
ATOM   4505  O   LEU C1109      21.202  82.514 120.553  1.00119.86           O  
ANISOU 4505  O   LEU C1109    14472  12873  18197  -1602  -2867  -1637       O  
ATOM   4506  CB  LEU C1109      21.744  83.775 117.931  1.00119.92           C  
ANISOU 4506  CB  LEU C1109    14497  12843  18224  -1749  -2858  -1633       C  
ATOM   4507  CG  LEU C1109      20.843  84.847 118.542  1.00120.37           C  
ANISOU 4507  CG  LEU C1109    14999  12630  18105  -1661  -2786  -1687       C  
ATOM   4508  CD1 LEU C1109      21.466  86.220 118.358  1.00123.03           C  
ANISOU 4508  CD1 LEU C1109    15688  12817  18240  -1914  -2842  -1697       C  
ATOM   4509  CD2 LEU C1109      19.459  84.806 117.921  1.00119.98           C  
ANISOU 4509  CD2 LEU C1109    14952  12497  18139  -1332  -2635  -1712       C  
ATOM   4510  N   VAL C1110      22.639  80.927 119.852  1.00117.64           N  
ANISOU 4510  N   VAL C1110    13582  12983  18132  -1720  -2965  -1541       N  
ATOM   4511  CA  VAL C1110      22.183  79.933 120.823  1.00117.32           C  
ANISOU 4511  CA  VAL C1110    13429  12993  18154  -1567  -2939  -1543       C  
ATOM   4512  C   VAL C1110      23.267  79.721 121.896  1.00116.97           C  
ANISOU 4512  C   VAL C1110    13343  13076  18023  -1782  -3058  -1489       C  
ATOM   4513  O   VAL C1110      22.961  79.544 123.081  1.00116.41           O  
ANISOU 4513  O   VAL C1110    13373  12960  17897  -1746  -3062  -1504       O  
ATOM   4514  CB  VAL C1110      21.742  78.608 120.134  1.00116.92           C  
ANISOU 4514  CB  VAL C1110    13040  13071  18313  -1345  -2865  -1529       C  
ATOM   4515  CG1 VAL C1110      21.446  77.511 121.152  1.00116.61           C  
ANISOU 4515  CG1 VAL C1110    12874  13103  18329  -1222  -2852  -1521       C  
ATOM   4516  CG2 VAL C1110      20.515  78.842 119.256  1.00115.51           C  
ANISOU 4516  CG2 VAL C1110    12926  12769  18195  -1137  -2749  -1576       C  
ATOM   4517  N   THR C1111      24.529  79.767 121.476  1.00116.34           N  
ANISOU 4517  N   THR C1111    13113  13169  17923  -2007  -3154  -1416       N  
ATOM   4518  CA  THR C1111      25.655  79.638 122.400  1.00116.86           C  
ANISOU 4518  CA  THR C1111    13116  13398  17888  -2240  -3276  -1339       C  
ATOM   4519  C   THR C1111      25.899  80.932 123.147  1.00119.43           C  
ANISOU 4519  C   THR C1111    13825  13574  17978  -2496  -3356  -1359       C  
ATOM   4520  O   THR C1111      26.298  80.911 124.311  1.00122.19           O  
ANISOU 4520  O   THR C1111    14245  13963  18217  -2632  -3430  -1332       O  
ATOM   4521  CB  THR C1111      26.955  79.248 121.676  1.00116.53           C  
ANISOU 4521  CB  THR C1111    12760  13631  17885  -2392  -3350  -1227       C  
ATOM   4522  OG1 THR C1111      27.226  80.187 120.627  1.00116.13           O  
ANISOU 4522  OG1 THR C1111    12809  13529  17787  -2528  -3367  -1231       O  
ATOM   4523  CG2 THR C1111      26.824  77.870 121.078  1.00115.69           C  
ANISOU 4523  CG2 THR C1111    12299  13671  17985  -2143  -3270  -1198       C  
ATOM   4524  N   ALA C1112      25.661  82.056 122.473  1.00120.07           N  
ANISOU 4524  N   ALA C1112    14171  13477  17973  -2567  -3338  -1405       N  
ATOM   4525  CA  ALA C1112      25.892  83.376 123.049  1.00122.82           C  
ANISOU 4525  CA  ALA C1112    14943  13649  18073  -2824  -3405  -1428       C  
ATOM   4526  C   ALA C1112      24.739  83.850 123.946  1.00124.01           C  
ANISOU 4526  C   ALA C1112    15471  13518  18128  -2662  -3321  -1518       C  
ATOM   4527  O   ALA C1112      24.965  84.250 125.099  1.00124.74           O  
ANISOU 4527  O   ALA C1112    15810  13540  18047  -2823  -3384  -1519       O  
ATOM   4528  CB  ALA C1112      26.182  84.391 121.951  1.00123.69           C  
ANISOU 4528  CB  ALA C1112    15202  13682  18112  -2974  -3419  -1433       C  
ATOM   4529  N   VAL C1113      23.513  83.801 123.418  1.00122.93           N  
ANISOU 4529  N   VAL C1113    15376  13236  18096  -2345  -3178  -1583       N  
ATOM   4530  CA  VAL C1113      22.333  84.251 124.163  1.00123.75           C  
ANISOU 4530  CA  VAL C1113    15819  13091  18110  -2144  -3077  -1651       C  
ATOM   4531  C   VAL C1113      22.011  83.238 125.269  1.00123.66           C  
ANISOU 4531  C   VAL C1113    15653  13162  18168  -2006  -3068  -1645       C  
ATOM   4532  O   VAL C1113      21.710  82.076 124.977  1.00120.18           O  
ANISOU 4532  O   VAL C1113    14852  12879  17932  -1812  -3025  -1628       O  
ATOM   4533  CB  VAL C1113      21.115  84.518 123.242  1.00122.37           C  
ANISOU 4533  CB  VAL C1113    15710  12774  18011  -1843  -2925  -1697       C  
ATOM   4534  CG1 VAL C1113      19.916  85.004 124.045  1.00123.11           C  
ANISOU 4534  CG1 VAL C1113    16149  12637  17991  -1617  -2811  -1743       C  
ATOM   4535  CG2 VAL C1113      21.468  85.541 122.174  1.00122.39           C  
ANISOU 4535  CG2 VAL C1113    15877  12689  17937  -1984  -2934  -1703       C  
ATOM   4536  N   PRO C1114      22.092  83.683 126.542  1.00126.41           N  
ANISOU 4536  N   PRO C1114    16296  13399  18336  -2119  -3110  -1658       N  
ATOM   4537  CA  PRO C1114      22.010  82.840 127.745  1.00127.42           C  
ANISOU 4537  CA  PRO C1114    16314  13608  18492  -2059  -3130  -1646       C  
ATOM   4538  C   PRO C1114      20.697  82.076 127.938  1.00127.50           C  
ANISOU 4538  C   PRO C1114    16215  13586  18643  -1681  -2996  -1679       C  
ATOM   4539  O   PRO C1114      20.712  81.003 128.552  1.00126.75           O  
ANISOU 4539  O   PRO C1114    15868  13636  18654  -1606  -3011  -1656       O  
ATOM   4540  CB  PRO C1114      22.199  83.841 128.891  1.00128.28           C  
ANISOU 4540  CB  PRO C1114    16882  13525  18333  -2257  -3182  -1668       C  
ATOM   4541  CG  PRO C1114      22.911  84.992 128.272  1.00129.47           C  
ANISOU 4541  CG  PRO C1114    17280  13593  18322  -2541  -3249  -1662       C  
ATOM   4542  CD  PRO C1114      22.320  85.093 126.900  1.00128.34           C  
ANISOU 4542  CD  PRO C1114    17037  13414  18311  -2338  -3146  -1684       C  
ATOM   4543  N   GLN C1115      19.583  82.616 127.436  1.00127.34           N  
ANISOU 4543  N   GLN C1115    16379  13390  18612  -1449  -2866  -1719       N  
ATOM   4544  CA  GLN C1115      18.274  81.989 127.652  1.00125.83           C  
ANISOU 4544  CA  GLN C1115    16104  13182  18523  -1102  -2739  -1732       C  
ATOM   4545  C   GLN C1115      17.863  81.083 126.495  1.00125.01           C  
ANISOU 4545  C   GLN C1115    15614  13236  18647   -927  -2682  -1713       C  
ATOM   4546  O   GLN C1115      16.916  80.288 126.607  1.00124.64           O  
ANISOU 4546  O   GLN C1115    15404  13243  18710   -681  -2600  -1707       O  
ATOM   4547  CB  GLN C1115      17.212  83.034 127.993  1.00126.78           C  
ANISOU 4547  CB  GLN C1115    16652  13045  18475   -921  -2621  -1764       C  
ATOM   4548  CG  GLN C1115      17.344  83.523 129.432  1.00128.50           C  
ANISOU 4548  CG  GLN C1115    17215  13118  18490  -1013  -2654  -1782       C  
ATOM   4549  CD  GLN C1115      16.448  84.697 129.748  1.00130.10           C  
ANISOU 4549  CD  GLN C1115    17907  13041  18483   -851  -2533  -1807       C  
ATOM   4550  OE1 GLN C1115      15.238  84.540 129.924  1.00130.10           O  
ANISOU 4550  OE1 GLN C1115    17926  13001  18506   -525  -2399  -1798       O  
ATOM   4551  NE2 GLN C1115      17.042  85.885 129.839  1.00131.45           N  
ANISOU 4551  NE2 GLN C1115    18491  13021  18434  -1079  -2577  -1830       N  
HETATM 4552  N   MSE C1116      18.610  81.194 125.396  1.00124.41           N  
ANISOU 4552  N   MSE C1116    15400  13240  18630  -1073  -2731  -1699       N  
HETATM 4553  CA  MSE C1116      18.507  80.277 124.260  1.00119.46           C  
ANISOU 4553  CA  MSE C1116    14400  12778  18211   -969  -2701  -1676       C  
HETATM 4554  C   MSE C1116      19.273  79.017 124.588  1.00117.01           C  
ANISOU 4554  C   MSE C1116    13753  12684  18021  -1039  -2776  -1638       C  
HETATM 4555  O   MSE C1116      19.295  78.084 123.796  1.00114.65           O  
ANISOU 4555  O   MSE C1116    13147  12528  17886   -960  -2755  -1615       O  
HETATM 4556  CB  MSE C1116      19.121  80.989 123.051  1.00118.91           C  
ANISOU 4556  CB  MSE C1116    14352  12698  18130  -1116  -2730  -1673       C  
HETATM 4557  CG  MSE C1116      18.510  80.559 121.720  1.00117.24           C  
ANISOU 4557  CG  MSE C1116    13920  12547  18079   -940  -2646  -1668       C  
HETATM 4558 SE   MSE C1116      16.892  81.607 121.293  1.00116.16          SE  
ANISOU 4558 SE   MSE C1116    14089  12189  17856   -667  -2485  -1698      SE  
HETATM 4559  CE  MSE C1116      17.715  83.272 120.626  1.00117.38           C  
ANISOU 4559  CE  MSE C1116    14591  12173  17834   -912  -2532  -1719       C  
ATOM   4560  N   ARG C1117      19.915  78.993 125.758  1.00117.96           N  
ANISOU 4560  N   ARG C1117    13945  12827  18048  -1187  -2860  -1625       N  
ATOM   4561  CA  ARG C1117      20.694  77.837 126.228  1.00117.26           C  
ANISOU 4561  CA  ARG C1117    13557  12948  18046  -1250  -2930  -1576       C  
ATOM   4562  C   ARG C1117      19.804  76.799 126.922  1.00115.47           C  
ANISOU 4562  C   ARG C1117    13215  12746  17911  -1018  -2863  -1587       C  
ATOM   4563  O   ARG C1117      19.825  75.612 126.572  1.00113.41           O  
ANISOU 4563  O   ARG C1117    12654  12634  17803   -918  -2842  -1559       O  
ATOM   4564  CB  ARG C1117      21.807  78.277 127.193  1.00119.02           C  
ANISOU 4564  CB  ARG C1117    13897  13210  18115  -1530  -3057  -1544       C  
ATOM   4565  CG  ARG C1117      22.920  79.112 126.572  1.00121.29           C  
ANISOU 4565  CG  ARG C1117    14238  13539  18307  -1815  -3152  -1507       C  
ATOM   4566  CD  ARG C1117      23.938  79.550 127.619  1.00122.85           C  
ANISOU 4566  CD  ARG C1117    14564  13787  18325  -2114  -3284  -1464       C  
ATOM   4567  NE  ARG C1117      25.147  80.107 127.010  1.00123.92           N  
ANISOU 4567  NE  ARG C1117    14660  14042  18381  -2411  -3390  -1399       N  
ATOM   4568  CZ  ARG C1117      26.222  80.515 127.685  1.00126.21           C  
ANISOU 4568  CZ  ARG C1117    15017  14432  18505  -2732  -3525  -1334       C  
ATOM   4569  NH1 ARG C1117      26.264  80.440 129.014  1.00126.55           N  
ANISOU 4569  NH1 ARG C1117    15181  14458  18443  -2800  -3571  -1331       N  
ATOM   4570  NH2 ARG C1117      27.265  81.004 127.023  1.00126.80           N  
ANISOU 4570  NH2 ARG C1117    15032  14637  18509  -2997  -3618  -1263       N  
ATOM   4571  N   LYS C1118      19.026  77.263 127.900  1.00114.37           N  
ANISOU 4571  N   LYS C1118    13335  12455  17666   -933  -2824  -1623       N  
ATOM   4572  CA  LYS C1118      18.176  76.400 128.714  1.00112.17           C  
ANISOU 4572  CA  LYS C1118    12982  12194  17444   -732  -2768  -1629       C  
ATOM   4573  C   LYS C1118      17.021  75.779 127.914  1.00111.89           C  
ANISOU 4573  C   LYS C1118    12789  12180  17544   -481  -2655  -1632       C  
ATOM   4574  O   LYS C1118      16.677  74.614 128.115  1.00111.36           O  
ANISOU 4574  O   LYS C1118    12504  12221  17588   -365  -2630  -1616       O  
ATOM   4575  CB  LYS C1118      17.639  77.178 129.914  1.00110.42           C  
ANISOU 4575  CB  LYS C1118    13103  11797  17053   -703  -2749  -1660       C  
ATOM   4576  CG  LYS C1118      17.115  76.303 131.038  1.00109.18           C  
ANISOU 4576  CG  LYS C1118    12872  11683  16929   -568  -2728  -1656       C  
ATOM   4577  CD  LYS C1118      16.539  77.156 132.155  1.00110.65           C  
ANISOU 4577  CD  LYS C1118    13424  11681  16936   -520  -2696  -1685       C  
ATOM   4578  CE  LYS C1118      16.208  76.336 133.392  1.00109.46           C  
ANISOU 4578  CE  LYS C1118    13209  11579  16801   -427  -2695  -1679       C  
ATOM   4579  NZ  LYS C1118      15.975  77.224 134.563  1.00110.05           N  
ANISOU 4579  NZ  LYS C1118    13664  11472  16677   -442  -2689  -1703       N  
ATOM   4580  N   ILE C1119      16.433  76.565 127.012  1.00112.35           N  
ANISOU 4580  N   ILE C1119    12968  12141  17580   -410  -2589  -1647       N  
ATOM   4581  CA  ILE C1119      15.259  76.159 126.222  1.00110.23           C  
ANISOU 4581  CA  ILE C1119    12579  11895  17407   -187  -2482  -1638       C  
ATOM   4582  C   ILE C1119      15.628  75.136 125.143  1.00109.15           C  
ANISOU 4582  C   ILE C1119    12116  11918  17440   -206  -2494  -1616       C  
ATOM   4583  O   ILE C1119      14.796  74.334 124.727  1.00107.16           O  
ANISOU 4583  O   ILE C1119    11700  11733  17282    -56  -2428  -1600       O  
ATOM   4584  CB  ILE C1119      14.563  77.400 125.606  1.00110.46           C  
ANISOU 4584  CB  ILE C1119    12853  11777  17341   -102  -2404  -1649       C  
ATOM   4585  CG1 ILE C1119      14.071  78.350 126.722  1.00110.97           C  
ANISOU 4585  CG1 ILE C1119    13276  11667  17220    -37  -2367  -1664       C  
ATOM   4586  CG2 ILE C1119      13.474  77.015 124.598  1.00108.12           C  
ANISOU 4586  CG2 ILE C1119    12396  11544  17142     95  -2306  -1622       C  
ATOM   4587  CD1 ILE C1119      13.299  77.688 127.854  1.00109.98           C  
ANISOU 4587  CD1 ILE C1119    13125  11572  17092    123  -2328  -1650       C  
ATOM   4588  N   VAL C1120      16.881  75.174 124.701  1.00110.21           N  
ANISOU 4588  N   VAL C1120    12167  12114  17594   -398  -2576  -1607       N  
ATOM   4589  CA  VAL C1120      17.441  74.096 123.890  1.00109.67           C  
ANISOU 4589  CA  VAL C1120    11800  12202  17668   -419  -2591  -1577       C  
ATOM   4590  C   VAL C1120      17.790  72.946 124.846  1.00110.51           C  
ANISOU 4590  C   VAL C1120    11757  12417  17816   -409  -2624  -1554       C  
ATOM   4591  O   VAL C1120      17.630  71.778 124.492  1.00108.48           O  
ANISOU 4591  O   VAL C1120    11292  12256  17669   -320  -2590  -1535       O  
ATOM   4592  CB  VAL C1120      18.667  74.562 123.047  1.00108.72           C  
ANISOU 4592  CB  VAL C1120    11633  12132  17545   -609  -2658  -1558       C  
ATOM   4593  CG1 VAL C1120      19.234  73.425 122.217  1.00106.76           C  
ANISOU 4593  CG1 VAL C1120    11091  12042  17431   -598  -2658  -1517       C  
ATOM   4594  CG2 VAL C1120      18.274  75.696 122.115  1.00108.81           C  
ANISOU 4594  CG2 VAL C1120    11807  12024  17512   -612  -2621  -1584       C  
ATOM   4595  N   SER C1121      18.229  73.292 126.064  1.00112.85           N  
ANISOU 4595  N   SER C1121    12181  12688  18010   -501  -2685  -1556       N  
ATOM   4596  CA  SER C1121      18.601  72.301 127.090  1.00113.09           C  
ANISOU 4596  CA  SER C1121    12088  12819  18063   -498  -2721  -1531       C  
ATOM   4597  C   SER C1121      17.441  71.363 127.428  1.00112.94           C  
ANISOU 4597  C   SER C1121    12001  12798  18113   -292  -2642  -1542       C  
ATOM   4598  O   SER C1121      17.604  70.141 127.396  1.00113.94           O  
ANISOU 4598  O   SER C1121    11926  13035  18331   -240  -2632  -1515       O  
ATOM   4599  CB  SER C1121      19.142  72.966 128.369  1.00112.52           C  
ANISOU 4599  CB  SER C1121    12199  12704  17849   -640  -2800  -1532       C  
ATOM   4600  OG  SER C1121      20.341  73.688 128.122  1.00113.27           O  
ANISOU 4600  OG  SER C1121    12330  12840  17868   -871  -2891  -1504       O  
ATOM   4601  N   ALA C1122      16.275  71.930 127.737  1.00112.60           N  
ANISOU 4601  N   ALA C1122    12134  12636  18013   -174  -2581  -1572       N  
ATOM   4602  CA  ALA C1122      15.085  71.130 128.058  1.00111.75           C  
ANISOU 4602  CA  ALA C1122    11964  12545  17952     12  -2508  -1568       C  
ATOM   4603  C   ALA C1122      14.579  70.345 126.837  1.00112.20           C  
ANISOU 4603  C   ALA C1122    11832  12676  18124     92  -2450  -1551       C  
ATOM   4604  O   ALA C1122      13.632  69.551 126.942  1.00113.57           O  
ANISOU 4604  O   ALA C1122    11926  12889  18337    215  -2396  -1536       O  
ATOM   4605  CB  ALA C1122      13.982  72.005 128.642  1.00111.31           C  
ANISOU 4605  CB  ALA C1122    12137  12367  17789    132  -2449  -1583       C  
ATOM   4606  N   LEU C1123      15.206  70.579 125.683  1.00110.14           N  
ANISOU 4606  N   LEU C1123    11508  12433  17906      9  -2464  -1548       N  
ATOM   4607  CA  LEU C1123      14.968  69.763 124.492  1.00107.37           C  
ANISOU 4607  CA  LEU C1123    10982  12154  17661     53  -2420  -1531       C  
ATOM   4608  C   LEU C1123      16.143  68.792 124.313  1.00105.62           C  
ANISOU 4608  C   LEU C1123    10589  12036  17508    -22  -2462  -1506       C  
ATOM   4609  O   LEU C1123      15.948  67.652 123.907  1.00104.82           O  
ANISOU 4609  O   LEU C1123    10355  11995  17478     37  -2424  -1489       O  
ATOM   4610  CB  LEU C1123      14.758  70.633 123.238  1.00107.21           C  
ANISOU 4610  CB  LEU C1123    11006  12086  17642     41  -2391  -1538       C  
ATOM   4611  CG  LEU C1123      13.778  71.827 123.249  1.00106.31           C  
ANISOU 4611  CG  LEU C1123    11087  11867  17439    122  -2341  -1549       C  
ATOM   4612  CD1 LEU C1123      14.067  72.810 122.116  1.00105.43           C  
ANISOU 4612  CD1 LEU C1123    11040  11703  17316     61  -2338  -1559       C  
ATOM   4613  CD2 LEU C1123      12.329  71.381 123.195  1.00105.26           C  
ANISOU 4613  CD2 LEU C1123    10910  11769  17315    287  -2260  -1521       C  
ATOM   4614  N   ILE C1124      17.353  69.248 124.633  1.00105.85           N  
ANISOU 4614  N   ILE C1124    10631  12090  17497   -153  -2536  -1495       N  
ATOM   4615  CA  ILE C1124      18.535  68.374 124.674  1.00106.44           C  
ANISOU 4615  CA  ILE C1124    10539  12291  17611   -207  -2573  -1448       C  
ATOM   4616  C   ILE C1124      18.298  67.248 125.679  1.00106.77           C  
ANISOU 4616  C   ILE C1124    10523  12377  17669   -120  -2559  -1436       C  
ATOM   4617  O   ILE C1124      18.095  66.103 125.280  1.00106.14           O  
ANISOU 4617  O   ILE C1124    10332  12340  17657    -32  -2508  -1420       O  
ATOM   4618  CB  ILE C1124      19.845  69.135 125.047  1.00106.31           C  
ANISOU 4618  CB  ILE C1124    10545  12329  17520   -382  -2667  -1417       C  
ATOM   4619  CG1 ILE C1124      20.207  70.167 123.973  1.00105.62           C  
ANISOU 4619  CG1 ILE C1124    10505  12211  17415   -486  -2685  -1421       C  
ATOM   4620  CG2 ILE C1124      21.006  68.161 125.226  1.00104.79           C  
ANISOU 4620  CG2 ILE C1124    10159  12303  17354   -406  -2697  -1343       C  
ATOM   4621  CD1 ILE C1124      21.007  71.334 124.495  1.00105.69           C  
ANISOU 4621  CD1 ILE C1124    10648  12206  17303   -679  -2777  -1413       C  
ATOM   4622  N   SER C1125      18.285  67.602 126.969  1.00107.84           N  
ANISOU 4622  N   SER C1125    10758  12486  17731   -147  -2602  -1447       N  
ATOM   4623  CA  SER C1125      18.255  66.647 128.092  1.00107.85           C  
ANISOU 4623  CA  SER C1125    10710  12535  17734    -88  -2605  -1432       C  
ATOM   4624  C   SER C1125      16.986  65.783 128.195  1.00107.87           C  
ANISOU 4624  C   SER C1125    10703  12502  17780     61  -2530  -1452       C  
ATOM   4625  O   SER C1125      16.607  65.342 129.292  1.00108.80           O  
ANISOU 4625  O   SER C1125    10846  12617  17874    114  -2531  -1456       O  
ATOM   4626  CB  SER C1125      18.510  67.378 129.419  1.00108.20           C  
ANISOU 4626  CB  SER C1125    10888  12548  17676   -169  -2672  -1441       C  
ATOM   4627  OG  SER C1125      17.445  68.260 129.735  1.00105.97           O  
ANISOU 4627  OG  SER C1125    10801  12129  17334   -124  -2646  -1491       O  
ATOM   4628  N   VAL C1126      16.340  65.553 127.052  1.00106.09           N  
ANISOU 4628  N   VAL C1126    10441  12259  17609    115  -2470  -1458       N  
ATOM   4629  CA  VAL C1126      15.279  64.560 126.937  1.00105.06           C  
ANISOU 4629  CA  VAL C1126    10274  12131  17515    219  -2406  -1458       C  
ATOM   4630  C   VAL C1126      15.813  63.404 126.098  1.00104.92           C  
ANISOU 4630  C   VAL C1126    10135  12170  17560    228  -2375  -1429       C  
ATOM   4631  O   VAL C1126      15.540  62.243 126.392  1.00103.93           O  
ANISOU 4631  O   VAL C1126     9975  12066  17448    286  -2343  -1415       O  
ATOM   4632  CB  VAL C1126      14.003  65.149 126.295  1.00104.87           C  
ANISOU 4632  CB  VAL C1126    10312  12054  17480    267  -2358  -1473       C  
ATOM   4633  CG1 VAL C1126      12.944  64.068 126.087  1.00103.07           C  
ANISOU 4633  CG1 VAL C1126    10028  11859  17274    338  -2301  -1455       C  
ATOM   4634  CG2 VAL C1126      13.458  66.285 127.156  1.00105.85           C  
ANISOU 4634  CG2 VAL C1126    10585  12111  17522    294  -2368  -1491       C  
ATOM   4635  N   ILE C1127      16.586  63.740 125.062  1.00105.43           N  
ANISOU 4635  N   ILE C1127    10154  12254  17652    173  -2382  -1417       N  
ATOM   4636  CA  ILE C1127      17.178  62.751 124.153  1.00104.22           C  
ANISOU 4636  CA  ILE C1127     9906  12147  17545    195  -2342  -1383       C  
ATOM   4637  C   ILE C1127      18.043  61.753 124.922  1.00104.95           C  
ANISOU 4637  C   ILE C1127     9935  12312  17629    235  -2345  -1339       C  
ATOM   4638  O   ILE C1127      17.942  60.552 124.661  1.00105.96           O  
ANISOU 4638  O   ILE C1127    10044  12442  17772    307  -2286  -1319       O  
ATOM   4639  CB  ILE C1127      18.012  63.393 123.012  1.00103.61           C  
ANISOU 4639  CB  ILE C1127     9784  12093  17489    130  -2354  -1367       C  
ATOM   4640  CG1 ILE C1127      17.259  64.538 122.343  1.00101.57           C  
ANISOU 4640  CG1 ILE C1127     9600  11763  17228     91  -2355  -1408       C  
ATOM   4641  CG2 ILE C1127      18.403  62.347 121.976  1.00104.42           C  
ANISOU 4641  CG2 ILE C1127     9817  12225  17631    179  -2293  -1332       C  
ATOM   4642  CD1 ILE C1127      18.109  65.319 121.368  1.00101.69           C  
ANISOU 4642  CD1 ILE C1127     9585  11797  17255     11  -2379  -1396       C  
ATOM   4643  N   PRO C1128      18.894  62.240 125.863  1.00104.53           N  
ANISOU 4643  N   PRO C1128     9859  12318  17538    184  -2412  -1316       N  
ATOM   4644  CA  PRO C1128      19.637  61.312 126.719  1.00104.95           C  
ANISOU 4644  CA  PRO C1128     9845  12457  17575    233  -2414  -1264       C  
ATOM   4645  C   PRO C1128      18.734  60.401 127.550  1.00104.12           C  
ANISOU 4645  C   PRO C1128     9791  12304  17465    318  -2379  -1288       C  
ATOM   4646  O   PRO C1128      19.147  59.286 127.889  1.00105.76           O  
ANISOU 4646  O   PRO C1128     9957  12558  17668    395  -2344  -1246       O  
ATOM   4647  CB  PRO C1128      20.443  62.249 127.626  1.00106.51           C  
ANISOU 4647  CB  PRO C1128    10033  12719  17715    127  -2506  -1243       C  
ATOM   4648  CG  PRO C1128      20.691  63.440 126.769  1.00106.18           C  
ANISOU 4648  CG  PRO C1128    10013  12660  17668     19  -2541  -1256       C  
ATOM   4649  CD  PRO C1128      19.389  63.620 126.032  1.00104.56           C  
ANISOU 4649  CD  PRO C1128     9898  12329  17502     66  -2487  -1323       C  
ATOM   4650  N   GLY C1129      17.529  60.880 127.869  1.00101.42           N  
ANISOU 4650  N   GLY C1129     9543  11879  17115    312  -2383  -1345       N  
ATOM   4651  CA  GLY C1129      16.501  60.066 128.510  1.00 99.61           C  
ANISOU 4651  CA  GLY C1129     9358  11611  16877    381  -2347  -1362       C  
ATOM   4652  C   GLY C1129      15.581  59.363 127.520  1.00 98.61           C  
ANISOU 4652  C   GLY C1129     9252  11442  16773    411  -2280  -1371       C  
ATOM   4653  O   GLY C1129      14.757  58.536 127.918  1.00 98.41           O  
ANISOU 4653  O   GLY C1129     9262  11399  16731    449  -2249  -1373       O  
HETATM 4654  N   MSE C1130      15.718  59.687 126.233  1.00 98.69           N  
ANISOU 4654  N   MSE C1130     9246  11442  16812    379  -2261  -1370       N  
HETATM 4655  CA  MSE C1130      14.905  59.064 125.169  1.00 99.50           C  
ANISOU 4655  CA  MSE C1130     9375  11508  16924    381  -2201  -1373       C  
HETATM 4656  C   MSE C1130      15.688  58.051 124.370  1.00100.40           C  
ANISOU 4656  C   MSE C1130     9475  11624  17048    409  -2150  -1341       C  
HETATM 4657  O   MSE C1130      15.139  57.429 123.454  1.00100.48           O  
ANISOU 4657  O   MSE C1130     9531  11593  17052    398  -2099  -1341       O  
HETATM 4658  CB  MSE C1130      14.354  60.094 124.182  1.00 99.05           C  
ANISOU 4658  CB  MSE C1130     9324  11429  16881    333  -2204  -1392       C  
HETATM 4659  CG  MSE C1130      12.826  60.204 124.197  1.00 99.18           C  
ANISOU 4659  CG  MSE C1130     9379  11437  16869    333  -2186  -1398       C  
HETATM 4660 SE   MSE C1130      12.217  61.801 123.186  1.00101.10          SE  
ANISOU 4660 SE   MSE C1130     9631  11667  17115    304  -2190  -1410      SE  
HETATM 4661  CE  MSE C1130      13.106  61.343 121.485  1.00100.10           C  
ANISOU 4661  CE  MSE C1130     9462  11529  17043    252  -2161  -1404       C  
ATOM   4662  N   LEU C1131      16.969  57.869 124.709  1.00101.20           N  
ANISOU 4662  N   LEU C1131     9520  11780  17152    447  -2159  -1304       N  
ATOM   4663  CA  LEU C1131      17.849  56.942 123.977  1.00100.65           C  
ANISOU 4663  CA  LEU C1131     9440  11725  17079    510  -2096  -1256       C  
ATOM   4664  C   LEU C1131      17.476  55.482 124.193  1.00100.82           C  
ANISOU 4664  C   LEU C1131     9555  11695  17059    580  -2027  -1244       C  
ATOM   4665  O   LEU C1131      18.092  54.598 123.606  1.00101.12           O  
ANISOU 4665  O   LEU C1131     9628  11719  17072    653  -1956  -1202       O  
ATOM   4666  CB  LEU C1131      19.319  57.160 124.342  1.00100.79           C  
ANISOU 4666  CB  LEU C1131     9351  11853  17093    543  -2122  -1194       C  
ATOM   4667  CG  LEU C1131      20.052  58.384 123.790  1.00100.90           C  
ANISOU 4667  CG  LEU C1131     9278  11930  17129    465  -2176  -1180       C  
ATOM   4668  CD1 LEU C1131      21.479  58.422 124.327  1.00102.06           C  
ANISOU 4668  CD1 LEU C1131     9307  12223  17249    484  -2206  -1095       C  
ATOM   4669  CD2 LEU C1131      20.040  58.414 122.268  1.00 99.22           C  
ANISOU 4669  CD2 LEU C1131     9076  11680  16944    459  -2128  -1181       C  
ATOM   4670  N   SER C1132      16.472  55.246 125.041  1.00100.87           N  
ANISOU 4670  N   SER C1132     9613  11669  17044    561  -2044  -1275       N  
ATOM   4671  CA  SER C1132      15.932  53.906 125.287  1.00100.54           C  
ANISOU 4671  CA  SER C1132     9684  11569  16950    595  -1987  -1269       C  
ATOM   4672  C   SER C1132      14.936  53.539 124.192  1.00 99.37           C  
ANISOU 4672  C   SER C1132     9632  11349  16776    521  -1949  -1288       C  
ATOM   4673  O   SER C1132      14.614  52.363 123.998  1.00 99.19           O  
ANISOU 4673  O   SER C1132     9738  11260  16691    525  -1890  -1277       O  
ATOM   4674  CB  SER C1132      15.242  53.835 126.655  1.00100.73           C  
ANISOU 4674  CB  SER C1132     9713  11605  16954    591  -2027  -1288       C  
ATOM   4675  OG  SER C1132      15.998  54.484 127.664  1.00101.27           O  
ANISOU 4675  OG  SER C1132     9690  11744  17044    622  -2082  -1279       O  
ATOM   4676  N   VAL C1133      14.445  54.563 123.495  1.00 98.61           N  
ANISOU 4676  N   VAL C1133     9485  11267  16716    446  -1982  -1311       N  
ATOM   4677  CA  VAL C1133      13.482  54.394 122.402  1.00 98.42           C  
ANISOU 4677  CA  VAL C1133     9526  11202  16666    358  -1957  -1319       C  
ATOM   4678  C   VAL C1133      14.201  54.463 121.056  1.00 99.27           C  
ANISOU 4678  C   VAL C1133     9642  11281  16794    360  -1918  -1310       C  
ATOM   4679  O   VAL C1133      13.936  53.641 120.168  1.00 99.33           O  
ANISOU 4679  O   VAL C1133     9764  11224  16753    325  -1863  -1301       O  
ATOM   4680  CB  VAL C1133      12.369  55.466 122.423  1.00 96.95           C  
ANISOU 4680  CB  VAL C1133     9278  11064  16495    287  -2008  -1336       C  
ATOM   4681  CG1 VAL C1133      11.163  54.977 121.643  1.00 97.49           C  
ANISOU 4681  CG1 VAL C1133     9411  11125  16505    187  -1986  -1321       C  
ATOM   4682  CG2 VAL C1133      11.955  55.817 123.848  1.00 96.55           C  
ANISOU 4682  CG2 VAL C1133     9189  11055  16438    319  -2053  -1342       C  
ATOM   4683  N   ILE C1134      15.123  55.426 120.928  1.00 99.38           N  
ANISOU 4683  N   ILE C1134     9548  11342  16869    393  -1948  -1308       N  
ATOM   4684  CA  ILE C1134      15.874  55.671 119.676  1.00 99.42           C  
ANISOU 4684  CA  ILE C1134     9535  11341  16901    399  -1918  -1294       C  
ATOM   4685  C   ILE C1134      17.017  54.658 119.395  1.00 99.93           C  
ANISOU 4685  C   ILE C1134     9646  11389  16935    507  -1843  -1244       C  
ATOM   4686  O   ILE C1134      17.845  54.877 118.501  1.00100.00           O  
ANISOU 4686  O   ILE C1134     9618  11414  16962    539  -1816  -1217       O  
ATOM   4687  CB  ILE C1134      16.408  57.132 119.571  1.00 99.13           C  
ANISOU 4687  CB  ILE C1134     9372  11368  16926    374  -1981  -1303       C  
ATOM   4688  CG1 ILE C1134      15.665  58.079 120.532  1.00 98.81           C  
ANISOU 4688  CG1 ILE C1134     9297  11351  16894    331  -2051  -1336       C  
ATOM   4689  CG2 ILE C1134      16.305  57.631 118.128  1.00 98.95           C  
ANISOU 4689  CG2 ILE C1134     9346  11322  16928    320  -1965  -1311       C  
ATOM   4690  CD1 ILE C1134      16.232  59.495 120.604  1.00 97.59           C  
ANISOU 4690  CD1 ILE C1134     9068  11237  16774    299  -2112  -1346       C  
ATOM   4691  N   ALA C1135      17.060  53.557 120.143  1.00 99.61           N  
ANISOU 4691  N   ALA C1135     9689  11319  16838    575  -1803  -1225       N  
ATOM   4692  CA  ALA C1135      17.971  52.468 119.810  1.00100.46           C  
ANISOU 4692  CA  ALA C1135     9886  11393  16891    700  -1707  -1170       C  
ATOM   4693  C   ALA C1135      17.191  51.339 119.152  1.00101.38           C  
ANISOU 4693  C   ALA C1135    10223  11374  16923    664  -1634  -1183       C  
ATOM   4694  O   ALA C1135      17.718  50.652 118.278  1.00102.37           O  
ANISOU 4694  O   ALA C1135    10466  11433  16996    733  -1545  -1151       O  
ATOM   4695  CB  ALA C1135      18.718  51.964 121.043  1.00100.61           C  
ANISOU 4695  CB  ALA C1135     9869  11471  16886    821  -1698  -1124       C  
ATOM   4696  N   LEU C1136      15.937  51.151 119.576  1.00100.81           N  
ANISOU 4696  N   LEU C1136    10215  11265  16822    550  -1670  -1224       N  
ATOM   4697  CA  LEU C1136      15.088  50.078 119.037  1.00100.63           C  
ANISOU 4697  CA  LEU C1136    10413  11125  16697    468  -1616  -1231       C  
ATOM   4698  C   LEU C1136      14.558  50.463 117.662  1.00100.39           C  
ANISOU 4698  C   LEU C1136    10412  11066  16667    347  -1618  -1248       C  
ATOM   4699  O   LEU C1136      14.316  49.604 116.821  1.00 99.51           O  
ANISOU 4699  O   LEU C1136    10499  10847  16463    298  -1554  -1241       O  
ATOM   4700  CB  LEU C1136      13.937  49.748 120.000  1.00 99.69           C  
ANISOU 4700  CB  LEU C1136    10331  11011  16536    373  -1662  -1251       C  
ATOM   4701  CG  LEU C1136      12.783  48.815 119.593  1.00 99.33           C  
ANISOU 4701  CG  LEU C1136    10488  10880  16372    221  -1641  -1254       C  
ATOM   4702  CD1 LEU C1136      13.221  47.365 119.396  1.00 99.96           C  
ANISOU 4702  CD1 LEU C1136    10836  10814  16328    277  -1537  -1232       C  
ATOM   4703  CD2 LEU C1136      11.666  48.906 120.623  1.00 98.27           C  
ANISOU 4703  CD2 LEU C1136    10299  10817  16224    127  -1711  -1261       C  
HETATM 4704  N   MSE C1137      14.412  51.769 117.447  1.00101.20           N  
ANISOU 4704  N   MSE C1137    10330  11258  16864    302  -1688  -1267       N  
HETATM 4705  CA  MSE C1137      13.926  52.329 116.183  1.00101.76           C  
ANISOU 4705  CA  MSE C1137    10391  11324  16948    195  -1698  -1280       C  
HETATM 4706  C   MSE C1137      14.918  52.138 115.054  1.00101.08           C  
ANISOU 4706  C   MSE C1137    10361  11183  16861    265  -1628  -1261       C  
HETATM 4707  O   MSE C1137      14.532  51.759 113.945  1.00100.34           O  
ANISOU 4707  O   MSE C1137    10396  11017  16713    183  -1590  -1262       O  
HETATM 4708  CB  MSE C1137      13.608  53.814 116.378  1.00101.97           C  
ANISOU 4708  CB  MSE C1137    10218  11456  17069    159  -1782  -1301       C  
HETATM 4709  CG  MSE C1137      12.308  54.023 117.145  1.00104.12           C  
ANISOU 4709  CG  MSE C1137    10458  11783  17319     74  -1838  -1308       C  
HETATM 4710 SE   MSE C1137      10.771  53.696 115.958  1.00110.60          SE  
ANISOU 4710 SE   MSE C1137    11369  12604  18050   -124  -1834  -1289      SE  
HETATM 4711  CE  MSE C1137      10.426  51.808 116.437  1.00108.86           C  
ANISOU 4711  CE  MSE C1137    11390  12286  17684   -181  -1784  -1270       C  
ATOM   4712  N   THR C1138      16.196  52.399 115.322  1.00100.43           N  
ANISOU 4712  N   THR C1138    10182  11146  16829    410  -1612  -1234       N  
ATOM   4713  CA  THR C1138      17.236  52.235 114.305  1.00101.09           C  
ANISOU 4713  CA  THR C1138    10296  11204  16907    504  -1539  -1198       C  
ATOM   4714  C   THR C1138      17.303  50.780 113.836  1.00102.43           C  
ANISOU 4714  C   THR C1138    10730  11236  16953    556  -1426  -1173       C  
ATOM   4715  O   THR C1138      17.282  50.505 112.627  1.00102.63           O  
ANISOU 4715  O   THR C1138    10882  11179  16934    528  -1369  -1170       O  
ATOM   4716  CB  THR C1138      18.617  52.720 114.797  1.00100.60           C  
ANISOU 4716  CB  THR C1138    10065  11257  16902    648  -1544  -1148       C  
ATOM   4717  OG1 THR C1138      18.518  54.087 115.220  1.00 99.73           O  
ANISOU 4717  OG1 THR C1138     9756  11251  16884    573  -1651  -1176       O  
ATOM   4718  CG2 THR C1138      19.655  52.619 113.687  1.00100.15           C  
ANISOU 4718  CG2 THR C1138    10017  11201  16835    747  -1468  -1095       C  
ATOM   4719  N   LEU C1139      17.348  49.855 114.793  1.00102.26           N  
ANISOU 4719  N   LEU C1139    10812  11178  16866    628  -1390  -1156       N  
ATOM   4720  CA  LEU C1139      17.392  48.424 114.474  1.00102.99           C  
ANISOU 4720  CA  LEU C1139    11199  11116  16816    684  -1275  -1132       C  
ATOM   4721  C   LEU C1139      16.061  47.904 113.897  1.00102.59           C  
ANISOU 4721  C   LEU C1139    11359  10949  16673    474  -1283  -1174       C  
ATOM   4722  O   LEU C1139      16.067  46.987 113.061  1.00104.66           O  
ANISOU 4722  O   LEU C1139    11888  11064  16813    468  -1191  -1162       O  
ATOM   4723  CB  LEU C1139      17.846  47.602 115.684  1.00103.37           C  
ANISOU 4723  CB  LEU C1139    11304  11160  16813    828  -1232  -1097       C  
ATOM   4724  CG  LEU C1139      19.110  48.156 116.356  1.00104.31           C  
ANISOU 4724  CG  LEU C1139    11187  11434  17013   1008  -1241  -1039       C  
ATOM   4725  CD1 LEU C1139      19.136  47.842 117.847  1.00104.70           C  
ANISOU 4725  CD1 LEU C1139    11191  11534  17057   1066  -1267  -1029       C  
ATOM   4726  CD2 LEU C1139      20.382  47.684 115.661  1.00105.46           C  
ANISOU 4726  CD2 LEU C1139    11391  11574  17104   1218  -1117   -953       C  
ATOM   4727  N   PHE C1140      14.937  48.492 114.322  1.00 99.06           N  
ANISOU 4727  N   PHE C1140    10797  10573  16269    302  -1389  -1214       N  
ATOM   4728  CA  PHE C1140      13.628  48.163 113.740  1.00 97.07           C  
ANISOU 4728  CA  PHE C1140    10687  10266  15928     76  -1414  -1234       C  
ATOM   4729  C   PHE C1140      13.664  48.401 112.229  1.00 96.29           C  
ANISOU 4729  C   PHE C1140    10647  10120  15817     10  -1385  -1235       C  
ATOM   4730  O   PHE C1140      13.404  47.479 111.435  1.00 96.59           O  
ANISOU 4730  O   PHE C1140    10957  10021  15720    -73  -1321  -1228       O  
ATOM   4731  CB  PHE C1140      12.496  48.980 114.389  1.00 95.42           C  
ANISOU 4731  CB  PHE C1140    10285  10192  15778    -64  -1530  -1253       C  
ATOM   4732  CG  PHE C1140      11.124  48.440 114.112  1.00 95.14           C  
ANISOU 4732  CG  PHE C1140    10387  10140  15624   -293  -1558  -1246       C  
ATOM   4733  CD1 PHE C1140      10.664  47.305 114.763  1.00 96.35           C  
ANISOU 4733  CD1 PHE C1140    10735  10223  15651   -355  -1538  -1235       C  
ATOM   4734  CD2 PHE C1140      10.289  49.064 113.195  1.00 95.22           C  
ANISOU 4734  CD2 PHE C1140    10328  10216  15636   -457  -1606  -1241       C  
ATOM   4735  CE1 PHE C1140       9.402  46.790 114.494  1.00 97.38           C  
ANISOU 4735  CE1 PHE C1140    10992  10357  15652   -597  -1572  -1215       C  
ATOM   4736  CE2 PHE C1140       9.016  48.568 112.933  1.00 95.62           C  
ANISOU 4736  CE2 PHE C1140    10484  10286  15559   -688  -1638  -1214       C  
ATOM   4737  CZ  PHE C1140       8.574  47.424 113.582  1.00 96.57           C  
ANISOU 4737  CZ  PHE C1140    10801  10344  15548   -769  -1625  -1200       C  
ATOM   4738  N   PHE C1141      14.020  49.630 111.844  1.00 93.76           N  
ANISOU 4738  N   PHE C1141    10091   9905  15629     44  -1432  -1244       N  
ATOM   4739  CA  PHE C1141      14.176  49.993 110.438  1.00 92.30           C  
ANISOU 4739  CA  PHE C1141     9925   9690  15453      2  -1408  -1245       C  
ATOM   4740  C   PHE C1141      15.335  49.246 109.796  1.00 93.37           C  
ANISOU 4740  C   PHE C1141    10236   9711  15531    164  -1287  -1214       C  
ATOM   4741  O   PHE C1141      15.301  48.953 108.592  1.00 92.99           O  
ANISOU 4741  O   PHE C1141    10347   9570  15417    111  -1234  -1211       O  
ATOM   4742  CB  PHE C1141      14.385  51.492 110.277  1.00 89.76           C  
ANISOU 4742  CB  PHE C1141     9318   9504  15281     17  -1481  -1258       C  
ATOM   4743  CG  PHE C1141      13.116  52.275 110.194  1.00 88.19           C  
ANISOU 4743  CG  PHE C1141     9005   9393  15109   -158  -1571  -1277       C  
ATOM   4744  CD1 PHE C1141      12.409  52.598 111.342  1.00 87.95           C  
ANISOU 4744  CD1 PHE C1141     8864   9453  15101   -190  -1640  -1283       C  
ATOM   4745  CD2 PHE C1141      12.638  52.716 108.964  1.00 87.82           C  
ANISOU 4745  CD2 PHE C1141     8956   9352  15059   -275  -1581  -1280       C  
ATOM   4746  CE1 PHE C1141      11.239  53.348 111.267  1.00 87.77           C  
ANISOU 4746  CE1 PHE C1141     8728   9531  15090   -321  -1710  -1280       C  
ATOM   4747  CE2 PHE C1141      11.473  53.461 108.874  1.00 87.14           C  
ANISOU 4747  CE2 PHE C1141     8751   9371  14988   -415  -1655  -1278       C  
ATOM   4748  CZ  PHE C1141      10.767  53.775 110.029  1.00 87.39           C  
ANISOU 4748  CZ  PHE C1141     8671   9500  15035   -430  -1716  -1273       C  
ATOM   4749  N   TYR C1142      16.363  48.924 110.587  1.00 94.00           N  
ANISOU 4749  N   TYR C1142    10290   9804  15622    370  -1237  -1181       N  
ATOM   4750  CA  TYR C1142      17.491  48.189 110.009  1.00 94.88           C  
ANISOU 4750  CA  TYR C1142    10562   9825  15661    561  -1105  -1129       C  
ATOM   4751  C   TYR C1142      17.026  46.832 109.541  1.00 96.01           C  
ANISOU 4751  C   TYR C1142    11091   9767  15621    507  -1011  -1129       C  
ATOM   4752  O   TYR C1142      17.445  46.361 108.485  1.00 97.63           O  
ANISOU 4752  O   TYR C1142    11495   9857  15743    562   -912  -1106       O  
ATOM   4753  CB  TYR C1142      18.703  48.064 110.931  1.00 94.31           C  
ANISOU 4753  CB  TYR C1142    10381   9835  15619    804  -1062  -1069       C  
ATOM   4754  CG  TYR C1142      19.942  47.722 110.141  1.00 94.81           C  
ANISOU 4754  CG  TYR C1142    10513   9874  15637   1015   -937   -995       C  
ATOM   4755  CD1 TYR C1142      20.350  48.532 109.075  1.00 94.62           C  
ANISOU 4755  CD1 TYR C1142    10365   9905  15682   1008   -946   -987       C  
ATOM   4756  CD2 TYR C1142      20.698  46.575 110.430  1.00 96.04           C  
ANISOU 4756  CD2 TYR C1142    10866   9953  15670   1235   -801   -925       C  
ATOM   4757  CE1 TYR C1142      21.487  48.220 108.327  1.00 95.85           C  
ANISOU 4757  CE1 TYR C1142    10577  10054  15789   1212   -826   -907       C  
ATOM   4758  CE2 TYR C1142      21.840  46.254 109.693  1.00 96.74           C  
ANISOU 4758  CE2 TYR C1142    11018  10036  15703   1459   -672   -838       C  
ATOM   4759  CZ  TYR C1142      22.230  47.078 108.642  1.00 96.51           C  
ANISOU 4759  CZ  TYR C1142    10849  10073  15746   1445   -686   -827       C  
ATOM   4760  OH  TYR C1142      23.349  46.791 107.900  1.00 96.81           O  
ANISOU 4760  OH  TYR C1142    10935  10123  15726   1671   -557   -731       O  
ATOM   4761  N   ILE C1143      16.132  46.228 110.316  1.00 95.47           N  
ANISOU 4761  N   ILE C1143    11141   9653  15480    386  -1044  -1152       N  
ATOM   4762  CA  ILE C1143      15.512  44.970 109.927  1.00 96.38           C  
ANISOU 4762  CA  ILE C1143    11645   9575  15401    272   -975  -1156       C  
ATOM   4763  C   ILE C1143      14.599  45.144 108.692  1.00 96.13           C  
ANISOU 4763  C   ILE C1143    11711   9496  15317     22  -1011  -1183       C  
ATOM   4764  O   ILE C1143      14.702  44.384 107.722  1.00 96.77           O  
ANISOU 4764  O   ILE C1143    12104   9408  15257     -1   -918  -1173       O  
ATOM   4765  CB  ILE C1143      14.830  44.301 111.142  1.00 96.19           C  
ANISOU 4765  CB  ILE C1143    11706   9534  15309    200  -1007  -1166       C  
ATOM   4766  CG1 ILE C1143      15.921  43.880 112.141  1.00 96.67           C  
ANISOU 4766  CG1 ILE C1143    11748   9601  15381    480   -932  -1126       C  
ATOM   4767  CG2 ILE C1143      13.985  43.106 110.706  1.00 97.30           C  
ANISOU 4767  CG2 ILE C1143    12251   9485  15234      6   -963  -1173       C  
ATOM   4768  CD1 ILE C1143      15.447  43.464 113.517  1.00 96.65           C  
ANISOU 4768  CD1 ILE C1143    11742   9623  15359    454   -975  -1134       C  
ATOM   4769  N   PHE C1144      13.744  46.164 108.715  1.00 94.96           N  
ANISOU 4769  N   PHE C1144    11304   9501  15275   -153  -1140  -1210       N  
ATOM   4770  CA  PHE C1144      12.842  46.443 107.590  1.00 95.22           C  
ANISOU 4770  CA  PHE C1144    11380   9534  15268   -392  -1186  -1222       C  
ATOM   4771  C   PHE C1144      13.549  46.877 106.280  1.00 95.42           C  
ANISOU 4771  C   PHE C1144    11402   9522  15331   -320  -1133  -1220       C  
ATOM   4772  O   PHE C1144      13.166  46.421 105.194  1.00 96.17           O  
ANISOU 4772  O   PHE C1144    11729   9506  15307   -464  -1099  -1219       O  
ATOM   4773  CB  PHE C1144      11.769  47.456 108.000  1.00 94.24           C  
ANISOU 4773  CB  PHE C1144    10964   9604  15241   -557  -1325  -1233       C  
ATOM   4774  CG  PHE C1144      10.625  46.854 108.767  1.00 95.00           C  
ANISOU 4774  CG  PHE C1144    11144   9723  15230   -742  -1379  -1223       C  
ATOM   4775  CD1 PHE C1144      10.660  46.771 110.156  1.00 94.72           C  
ANISOU 4775  CD1 PHE C1144    11012   9743  15236   -650  -1404  -1225       C  
ATOM   4776  CD2 PHE C1144       9.499  46.374 108.099  1.00 96.26           C  
ANISOU 4776  CD2 PHE C1144    11473   9862  15238  -1024  -1409  -1203       C  
ATOM   4777  CE1 PHE C1144       9.601  46.208 110.862  1.00 94.98           C  
ANISOU 4777  CE1 PHE C1144    11116   9805  15165   -823  -1454  -1209       C  
ATOM   4778  CE2 PHE C1144       8.435  45.814 108.799  1.00 96.46           C  
ANISOU 4778  CE2 PHE C1144    11565   9933  15152  -1214  -1465  -1179       C  
ATOM   4779  CZ  PHE C1144       8.484  45.738 110.181  1.00 96.02           C  
ANISOU 4779  CZ  PHE C1144    11409   9930  15144  -1107  -1486  -1182       C  
ATOM   4780  N   ALA C1145      14.566  47.745 106.385  1.00 94.04           N  
ANISOU 4780  N   ALA C1145    10974   9445  15313   -115  -1130  -1213       N  
ATOM   4781  CA  ALA C1145      15.377  48.183 105.232  1.00 93.33           C  
ANISOU 4781  CA  ALA C1145    10856   9339  15268    -19  -1077  -1201       C  
ATOM   4782  C   ALA C1145      16.137  47.036 104.573  1.00 95.01           C  
ANISOU 4782  C   ALA C1145    11409   9359  15331    116   -923  -1168       C  
ATOM   4783  O   ALA C1145      16.328  47.023 103.360  1.00 95.58           O  
ANISOU 4783  O   ALA C1145    11598   9355  15362     99   -871  -1163       O  
ATOM   4784  CB  ALA C1145      16.358  49.262 105.650  1.00 92.42           C  
ANISOU 4784  CB  ALA C1145    10408   9379  15326    164  -1108  -1188       C  
ATOM   4785  N   ILE C1146      16.586  46.089 105.390  1.00 95.94           N  
ANISOU 4785  N   ILE C1146    11693   9399  15363    265   -845  -1141       N  
ATOM   4786  CA  ILE C1146      17.244  44.896 104.903  1.00 97.72           C  
ANISOU 4786  CA  ILE C1146    12289   9426  15417    417   -682  -1100       C  
ATOM   4787  C   ILE C1146      16.220  43.993 104.202  1.00 99.16           C  
ANISOU 4787  C   ILE C1146    12863   9411  15402    169   -661  -1129       C  
ATOM   4788  O   ILE C1146      16.528  43.361 103.192  1.00100.35           O  
ANISOU 4788  O   ILE C1146    13324   9389  15416    204   -548  -1112       O  
ATOM   4789  CB  ILE C1146      17.985  44.188 106.060  1.00 98.37           C  
ANISOU 4789  CB  ILE C1146    12422   9494  15458    657   -605  -1055       C  
ATOM   4790  CG1 ILE C1146      19.312  44.908 106.320  1.00 97.43           C  
ANISOU 4790  CG1 ILE C1146    11991   9548  15480    932   -582   -994       C  
ATOM   4791  CG2 ILE C1146      18.180  42.689 105.786  1.00100.55           C  
ANISOU 4791  CG2 ILE C1146    13188   9519  15498    749   -441  -1023       C  
ATOM   4792  CD1 ILE C1146      20.048  44.419 107.544  1.00 98.42           C  
ANISOU 4792  CD1 ILE C1146    12080   9723  15591   1161   -528   -937       C  
HETATM 4793  N   MSE C1147      14.997  43.958 104.724  1.00 99.36           N  
ANISOU 4793  N   MSE C1147    12876   9473  15402    -92   -771  -1164       N  
HETATM 4794  CA  MSE C1147      13.930  43.177 104.100  1.00101.37           C  
ANISOU 4794  CA  MSE C1147    13473   9582  15461   -383   -777  -1180       C  
HETATM 4795  C   MSE C1147      13.574  43.805 102.786  1.00100.83           C  
ANISOU 4795  C   MSE C1147    13357   9539  15414   -544   -815  -1192       C  
HETATM 4796  O   MSE C1147      13.309  43.098 101.803  1.00102.18           O  
ANISOU 4796  O   MSE C1147    13882   9536  15407   -681   -756  -1190       O  
HETATM 4797  CB  MSE C1147      12.678  43.088 104.977  1.00102.47           C  
ANISOU 4797  CB  MSE C1147    13554   9807  15571   -634   -898  -1195       C  
HETATM 4798  CG  MSE C1147      12.769  42.039 106.084  1.00105.17           C  
ANISOU 4798  CG  MSE C1147    14111  10047  15802   -558   -844  -1185       C  
HETATM 4799 SE   MSE C1147      13.099  40.270 105.283  1.00111.97          SE  
ANISOU 4799 SE   MSE C1147    15676  10534  16333   -548   -654  -1167      SE  
HETATM 4800  CE  MSE C1147      15.057  40.440 105.120  1.00112.39           C  
ANISOU 4800  CE  MSE C1147    15653  10558  16492    -32   -484  -1124       C  
ATOM   4801  N   ALA C1148      13.589  45.137 102.752  1.00 98.11           N  
ANISOU 4801  N   ALA C1148    12595   9402  15278   -529   -911  -1204       N  
ATOM   4802  CA  ALA C1148      13.207  45.882 101.561  1.00 96.74           C  
ANISOU 4802  CA  ALA C1148    12327   9283  15148   -679   -960  -1214       C  
ATOM   4803  C   ALA C1148      13.969  45.453 100.308  1.00 97.39           C  
ANISOU 4803  C   ALA C1148    12671   9193  15140   -583   -835  -1202       C  
ATOM   4804  O   ALA C1148      13.477  44.629  99.520  1.00 98.37           O  
ANISOU 4804  O   ALA C1148    13156   9149  15069   -761   -792  -1202       O  
ATOM   4805  CB  ALA C1148      13.370  47.368 101.793  1.00 94.42           C  
ANISOU 4805  CB  ALA C1148    11572   9214  15089   -607  -1055  -1225       C  
ATOM   4806  N   THR C1149      15.170  46.000 100.143  1.00 96.17           N  
ANISOU 4806  N   THR C1149    12343   9083  15113   -309   -777  -1186       N  
ATOM   4807  CA  THR C1149      15.913  45.893  98.885  1.00 96.34           C  
ANISOU 4807  CA  THR C1149    12521   8994  15088   -202   -671  -1167       C  
ATOM   4808  C   THR C1149      15.765  44.546  98.191  1.00 97.91           C  
ANISOU 4808  C   THR C1149    13247   8925  15030   -267   -550  -1158       C  
ATOM   4809  O   THR C1149      15.519  44.504  96.983  1.00 98.27           O  
ANISOU 4809  O   THR C1149    13461   8880  14996   -399   -530  -1165       O  
ATOM   4810  CB  THR C1149      17.412  46.217  99.075  1.00 96.45           C  
ANISOU 4810  CB  THR C1149    12364   9071  15212    156   -585  -1121       C  
ATOM   4811  OG1 THR C1149      17.556  47.531  99.653  1.00 94.69           O  
ANISOU 4811  OG1 THR C1149    11677   9088  15213    183   -704  -1131       O  
ATOM   4812  CG2 THR C1149      18.164  46.130  97.739  1.00 96.41           C  
ANISOU 4812  CG2 THR C1149    12510   8968  15155    275   -471  -1091       C  
ATOM   4813  N   GLN C1150      15.907  43.451  98.939  1.00 98.45           N  
ANISOU 4813  N   GLN C1150    13594   8857  14956   -181   -469  -1141       N  
ATOM   4814  CA  GLN C1150      15.904  42.133  98.302  1.00100.07           C  
ANISOU 4814  CA  GLN C1150    14354   8775  14892   -208   -331  -1128       C  
ATOM   4815  C   GLN C1150      14.505  41.738  97.830  1.00100.29           C  
ANISOU 4815  C   GLN C1150    14623   8722  14759   -629   -417  -1163       C  
ATOM   4816  O   GLN C1150      14.355  41.154  96.763  1.00101.21           O  
ANISOU 4816  O   GLN C1150    15114   8648  14693   -747   -348  -1162       O  
ATOM   4817  CB  GLN C1150      16.604  41.072  99.162  1.00101.43           C  
ANISOU 4817  CB  GLN C1150    14784   8810  14944     50   -195  -1090       C  
ATOM   4818  CG  GLN C1150      18.111  41.326  99.276  1.00101.76           C  
ANISOU 4818  CG  GLN C1150    14656   8919  15089    477    -76  -1026       C  
ATOM   4819  CD  GLN C1150      18.962  40.090  99.575  1.00104.08           C  
ANISOU 4819  CD  GLN C1150    15338   9017  15191    779    124   -962       C  
ATOM   4820  OE1 GLN C1150      18.720  38.994  99.063  1.00106.30           O  
ANISOU 4820  OE1 GLN C1150    16142   9026  15222    722    236   -962       O  
ATOM   4821  NE2 GLN C1150      19.992  40.278 100.389  1.00103.92           N  
ANISOU 4821  NE2 GLN C1150    15070   9139  15276   1107    175   -897       N  
ATOM   4822  N   LEU C1151      13.483  42.113  98.598  1.00 78.51           N  
ANISOU 4822  N   LEU C1151     9707   6646  13479   -860   -923   -221       N  
ATOM   4823  CA  LEU C1151      12.085  41.866  98.210  1.00 78.98           C  
ANISOU 4823  CA  LEU C1151     9745   6665  13599  -1085   -998   -138       C  
ATOM   4824  C   LEU C1151      11.667  42.618  96.940  1.00 78.44           C  
ANISOU 4824  C   LEU C1151     9584   6622  13597  -1127  -1049   -166       C  
ATOM   4825  O   LEU C1151      11.066  42.020  96.061  1.00 79.98           O  
ANISOU 4825  O   LEU C1151     9904   6704  13781  -1251  -1164   -138       O  
ATOM   4826  CB  LEU C1151      11.112  42.212  99.348  1.00 79.24           C  
ANISOU 4826  CB  LEU C1151     9580   6822  13704  -1196   -931    -47       C  
ATOM   4827  CG  LEU C1151      11.003  41.426 100.666  1.00 79.99           C  
ANISOU 4827  CG  LEU C1151     9740   6902  13750  -1221   -885     28       C  
ATOM   4828  CD1 LEU C1151      10.020  42.138 101.579  1.00 80.07           C  
ANISOU 4828  CD1 LEU C1151     9501   7083  13839  -1288   -800    116       C  
ATOM   4829  CD2 LEU C1151      10.602  39.961 100.531  1.00 81.46           C  
ANISOU 4829  CD2 LEU C1151    10172   6904  13875  -1372   -984    107       C  
ATOM   4830  N   PHE C1152      11.972  43.914  96.831  1.00 76.84           N  
ANISOU 4830  N   PHE C1152     9182   6555  13459  -1030   -975   -220       N  
ATOM   4831  CA  PHE C1152      11.498  44.696  95.675  1.00 76.33           C  
ANISOU 4831  CA  PHE C1152     9023   6522  13458  -1067  -1014   -238       C  
ATOM   4832  C   PHE C1152      12.554  45.481  94.863  1.00 75.45           C  
ANISOU 4832  C   PHE C1152     8896   6435  13337   -897   -980   -327       C  
ATOM   4833  O   PHE C1152      12.226  46.450  94.176  1.00 75.33           O  
ANISOU 4833  O   PHE C1152     8753   6483  13386   -903   -975   -343       O  
ATOM   4834  CB  PHE C1152      10.395  45.669  96.110  1.00 76.08           C  
ANISOU 4834  CB  PHE C1152     8737   6642  13530  -1159   -969   -185       C  
ATOM   4835  CG  PHE C1152       9.532  45.174  97.254  1.00 76.74           C  
ANISOU 4835  CG  PHE C1152     8763   6769  13626  -1279   -947    -81       C  
ATOM   4836  CD1 PHE C1152       9.427  45.922  98.429  1.00 75.75           C  
ANISOU 4836  CD1 PHE C1152     8468   6785  13527  -1215   -835    -63       C  
ATOM   4837  CD2 PHE C1152       8.787  44.006  97.137  1.00 77.59           C  
ANISOU 4837  CD2 PHE C1152     8988   6777  13715  -1458  -1042      7       C  
ATOM   4838  CE1 PHE C1152       8.622  45.501  99.469  1.00 76.32           C  
ANISOU 4838  CE1 PHE C1152     8480   6915  13602  -1305   -799     47       C  
ATOM   4839  CE2 PHE C1152       7.992  43.580  98.179  1.00 78.44           C  
ANISOU 4839  CE2 PHE C1152     9025   6939  13839  -1576  -1011    124       C  
ATOM   4840  CZ  PHE C1152       7.913  44.322  99.346  1.00 77.92           C  
ANISOU 4840  CZ  PHE C1152     8779   7031  13795  -1489   -880    148       C  
ATOM   4841  N   GLY C1153      13.814  45.090  94.925  1.00 75.09           N  
ANISOU 4841  N   GLY C1153     8972   6350  13209   -742   -953   -373       N  
ATOM   4842  CA  GLY C1153      14.844  45.918  94.324  1.00 74.03           C  
ANISOU 4842  CA  GLY C1153     8774   6276  13077   -589   -902   -429       C  
ATOM   4843  C   GLY C1153      15.113  45.608  92.876  1.00 74.27           C  
ANISOU 4843  C   GLY C1153     8953   6219  13047   -527   -960   -448       C  
ATOM   4844  O   GLY C1153      16.089  46.102  92.296  1.00 73.91           O  
ANISOU 4844  O   GLY C1153     8882   6219  12982   -382   -913   -477       O  
ATOM   4845  N   GLU C1154      14.258  44.788  92.289  1.00 75.15           N  
ANISOU 4845  N   GLU C1154     9223   6206  13125   -637  -1066   -424       N  
ATOM   4846  CA  GLU C1154      14.507  44.295  90.941  1.00 76.22           C  
ANISOU 4846  CA  GLU C1154     9564   6227  13170   -560  -1141   -446       C  
ATOM   4847  C   GLU C1154      13.595  45.001  89.903  1.00 75.98           C  
ANISOU 4847  C   GLU C1154     9451   6209  13209   -651  -1196   -446       C  
ATOM   4848  O   GLU C1154      13.933  45.119  88.711  1.00 75.47           O  
ANISOU 4848  O   GLU C1154     9481   6104  13091   -546  -1221   -473       O  
ATOM   4849  CB  GLU C1154      14.310  42.781  90.918  1.00 77.80           C  
ANISOU 4849  CB  GLU C1154    10065   6243  13253   -602  -1251   -429       C  
ATOM   4850  CG  GLU C1154      15.368  42.034  90.136  1.00 79.54           C  
ANISOU 4850  CG  GLU C1154    10555   6357  13308   -387  -1271   -463       C  
ATOM   4851  CD  GLU C1154      16.553  41.631  90.996  1.00 80.65           C  
ANISOU 4851  CD  GLU C1154    10737   6538  13369   -215  -1180   -468       C  
ATOM   4852  OE1 GLU C1154      17.681  41.545  90.447  1.00 81.54           O  
ANISOU 4852  OE1 GLU C1154    10935   6671  13375     18  -1132   -488       O  
ATOM   4853  OE2 GLU C1154      16.360  41.392  92.218  1.00 80.80           O  
ANISOU 4853  OE2 GLU C1154    10699   6580  13423   -300  -1154   -445       O  
ATOM   4854  N   ARG C1155      12.442  45.461  90.386  1.00 75.40           N  
ANISOU 4854  N   ARG C1155     9201   6203  13244   -829  -1210   -408       N  
ATOM   4855  CA  ARG C1155      11.461  46.151  89.576  1.00 75.04           C  
ANISOU 4855  CA  ARG C1155     9048   6194  13267   -921  -1260   -397       C  
ATOM   4856  C   ARG C1155      11.297  47.614  90.039  1.00 73.68           C  
ANISOU 4856  C   ARG C1155     8592   6195  13206   -906  -1149   -398       C  
ATOM   4857  O   ARG C1155      10.565  48.403  89.400  1.00 73.29           O  
ANISOU 4857  O   ARG C1155     8430   6202  13214   -946  -1167   -392       O  
ATOM   4858  CB  ARG C1155      10.119  45.421  89.664  1.00 76.45           C  
ANISOU 4858  CB  ARG C1155     9261   6317  13469  -1144  -1387   -332       C  
ATOM   4859  CG  ARG C1155       9.306  45.487  88.371  1.00 77.69           C  
ANISOU 4859  CG  ARG C1155     9464   6427  13629  -1219  -1515   -331       C  
ATOM   4860  CD  ARG C1155       9.695  44.360  87.434  1.00 78.81           C  
ANISOU 4860  CD  ARG C1155     9941   6363  13638  -1177  -1645   -365       C  
ATOM   4861  NE  ARG C1155       9.671  44.764  86.034  1.00 79.03           N  
ANISOU 4861  NE  ARG C1155    10037   6359  13631  -1095  -1703   -409       N  
ATOM   4862  CZ  ARG C1155      10.068  43.975  85.033  1.00 80.83           C  
ANISOU 4862  CZ  ARG C1155    10570   6417  13726  -1004  -1810   -449       C  
ATOM   4863  NH1 ARG C1155      10.522  42.740  85.286  1.00 82.05           N  
ANISOU 4863  NH1 ARG C1155    10997   6411  13766   -984  -1871   -453       N  
ATOM   4864  NH2 ARG C1155      10.003  44.407  83.775  1.00 80.88           N  
ANISOU 4864  NH2 ARG C1155    10630   6404  13696   -918  -1857   -485       N  
ATOM   4865  N   PHE C1156      11.970  47.969  91.146  1.00 71.82           N  
ANISOU 4865  N   PHE C1156     8260   6037  12991   -840  -1044   -407       N  
ATOM   4866  CA  PHE C1156      11.826  49.290  91.746  1.00 70.42           C  
ANISOU 4866  CA  PHE C1156     7857   5999  12902   -825   -952   -411       C  
ATOM   4867  C   PHE C1156      13.169  49.939  92.223  1.00 69.55           C  
ANISOU 4867  C   PHE C1156     7696   5939  12790   -682   -857   -457       C  
ATOM   4868  O   PHE C1156      13.300  50.334  93.397  1.00 69.28           O  
ANISOU 4868  O   PHE C1156     7564   5976  12785   -676   -800   -458       O  
ATOM   4869  CB  PHE C1156      10.806  49.205  92.885  1.00 70.78           C  
ANISOU 4869  CB  PHE C1156     7791   6112  12990   -944   -942   -352       C  
ATOM   4870  CG  PHE C1156       9.469  48.624  92.480  1.00 72.29           C  
ANISOU 4870  CG  PHE C1156     7988   6282  13197  -1110  -1040   -283       C  
ATOM   4871  CD1 PHE C1156       9.208  47.257  92.614  1.00 73.92           C  
ANISOU 4871  CD1 PHE C1156     8351   6382  13355  -1220  -1125   -238       C  
ATOM   4872  CD2 PHE C1156       8.450  49.439  91.995  1.00 72.34           C  
ANISOU 4872  CD2 PHE C1156     7844   6379  13263  -1163  -1055   -254       C  
ATOM   4873  CE1 PHE C1156       7.969  46.718  92.244  1.00 75.02           C  
ANISOU 4873  CE1 PHE C1156     8486   6501  13516  -1406  -1236   -161       C  
ATOM   4874  CE2 PHE C1156       7.213  48.907  91.638  1.00 73.57           C  
ANISOU 4874  CE2 PHE C1156     7977   6537  13438  -1329  -1157   -177       C  
ATOM   4875  CZ  PHE C1156       6.969  47.548  91.761  1.00 74.76           C  
ANISOU 4875  CZ  PHE C1156     8273   6580  13551  -1463  -1254   -128       C  
ATOM   4876  N   PRO C1157      14.172  50.069  91.318  1.00 69.17           N  
ANISOU 4876  N   PRO C1157     7712   5865  12705   -566   -843   -486       N  
ATOM   4877  CA  PRO C1157      15.507  50.476  91.751  1.00 68.80           C  
ANISOU 4877  CA  PRO C1157     7616   5873  12652   -449   -770   -507       C  
ATOM   4878  C   PRO C1157      15.525  51.802  92.543  1.00 68.67           C  
ANISOU 4878  C   PRO C1157     7414   5954  12724   -467   -713   -521       C  
ATOM   4879  O   PRO C1157      15.833  51.791  93.749  1.00 68.44           O  
ANISOU 4879  O   PRO C1157     7343   5963  12697   -462   -688   -529       O  
ATOM   4880  CB  PRO C1157      16.279  50.599  90.432  1.00 69.00           C  
ANISOU 4880  CB  PRO C1157     7702   5878  12636   -338   -761   -510       C  
ATOM   4881  CG  PRO C1157      15.562  49.721  89.476  1.00 69.65           C  
ANISOU 4881  CG  PRO C1157     7955   5853  12656   -365   -846   -504       C  
ATOM   4882  CD  PRO C1157      14.123  49.897  89.853  1.00 69.91           C  
ANISOU 4882  CD  PRO C1157     7914   5890  12758   -529   -894   -491       C  
ATOM   4883  N   GLU C1158      15.200  52.925  91.884  1.00 68.53           N  
ANISOU 4883  N   GLU C1158     7309   5965  12765   -477   -699   -526       N  
ATOM   4884  CA  GLU C1158      15.028  54.220  92.573  1.00 67.92           C  
ANISOU 4884  CA  GLU C1158     7097   5952  12758   -495   -662   -541       C  
ATOM   4885  C   GLU C1158      14.390  54.009  93.954  1.00 67.89           C  
ANISOU 4885  C   GLU C1158     7061   5981  12754   -541   -659   -537       C  
ATOM   4886  O   GLU C1158      14.990  54.344  94.969  1.00 68.13           O  
ANISOU 4886  O   GLU C1158     7056   6044  12788   -509   -635   -559       O  
ATOM   4887  CB  GLU C1158      14.186  55.179  91.720  1.00 67.98           C  
ANISOU 4887  CB  GLU C1158     7053   5967  12809   -519   -664   -537       C  
ATOM   4888  CG  GLU C1158      13.807  56.506  92.376  1.00 68.16           C  
ANISOU 4888  CG  GLU C1158     6977   6039  12882   -523   -635   -552       C  
ATOM   4889  CD  GLU C1158      13.111  57.472  91.398  1.00 68.82           C  
ANISOU 4889  CD  GLU C1158     7029   6124  12994   -518   -633   -547       C  
ATOM   4890  OE1 GLU C1158      13.064  57.152  90.186  1.00 68.22           O  
ANISOU 4890  OE1 GLU C1158     7002   6016  12904   -510   -654   -535       O  
ATOM   4891  OE2 GLU C1158      12.609  58.553  91.836  1.00 68.95           O  
ANISOU 4891  OE2 GLU C1158     6991   6172  13034   -505   -613   -557       O  
ATOM   4892  N   TRP C1159      13.202  53.415  94.002  1.00 67.81           N  
ANISOU 4892  N   TRP C1159     7064   5966  12735   -615   -687   -502       N  
ATOM   4893  CA  TRP C1159      12.519  53.230  95.277  1.00 68.06           C  
ANISOU 4893  CA  TRP C1159     7050   6046  12762   -651   -669   -475       C  
ATOM   4894  C   TRP C1159      13.268  52.422  96.329  1.00 68.40           C  
ANISOU 4894  C   TRP C1159     7156   6074  12758   -621   -657   -482       C  
ATOM   4895  O   TRP C1159      13.720  52.992  97.353  1.00 67.98           O  
ANISOU 4895  O   TRP C1159     7060   6065  12706   -565   -622   -509       O  
ATOM   4896  CB  TRP C1159      11.114  52.685  95.045  1.00 68.31           C  
ANISOU 4896  CB  TRP C1159     7064   6092  12799   -755   -705   -409       C  
ATOM   4897  CG  TRP C1159      10.154  53.728  94.523  1.00 67.92           C  
ANISOU 4897  CG  TRP C1159     6904   6110  12793   -763   -699   -393       C  
ATOM   4898  CD1 TRP C1159      10.238  55.112  94.666  1.00 67.17           C  
ANISOU 4898  CD1 TRP C1159     6735   6065  12722   -683   -651   -427       C  
ATOM   4899  CD2 TRP C1159       8.908  53.496  93.788  1.00 68.36           C  
ANISOU 4899  CD2 TRP C1159     6916   6194  12864   -854   -751   -334       C  
ATOM   4900  NE1 TRP C1159       9.175  55.728  94.065  1.00 67.25           N  
ANISOU 4900  NE1 TRP C1159     6668   6131  12753   -696   -658   -396       N  
ATOM   4901  CE2 TRP C1159       8.332  54.812  93.529  1.00 68.00           C  
ANISOU 4901  CE2 TRP C1159     6761   6229  12847   -798   -718   -337       C  
ATOM   4902  CE3 TRP C1159       8.237  52.365  93.339  1.00 69.10           C  
ANISOU 4902  CE3 TRP C1159     7059   6250  12948   -977   -833   -278       C  
ATOM   4903  CZ2 TRP C1159       7.137  54.970  92.847  1.00 68.62           C  
ANISOU 4903  CZ2 TRP C1159     6759   6370  12941   -850   -756   -284       C  
ATOM   4904  CZ3 TRP C1159       7.029  52.537  92.648  1.00 69.99           C  
ANISOU 4904  CZ3 TRP C1159     7086   6421  13087  -1054   -886   -223       C  
ATOM   4905  CH2 TRP C1159       6.494  53.810  92.407  1.00 69.52           C  
ANISOU 4905  CH2 TRP C1159     6899   6462  13054   -985   -844   -225       C  
ATOM   4906  N   PHE C1160      13.407  51.106  96.077  1.00 68.70           N  
ANISOU 4906  N   PHE C1160     7316   6041  12744   -649   -694   -460       N  
ATOM   4907  CA  PHE C1160      13.957  50.136  97.046  1.00 68.64           C  
ANISOU 4907  CA  PHE C1160     7395   6009  12676   -621   -686   -455       C  
ATOM   4908  C   PHE C1160      15.305  49.483  96.645  1.00 68.86           C  
ANISOU 4908  C   PHE C1160     7541   5983  12641   -523   -698   -487       C  
ATOM   4909  O   PHE C1160      16.011  48.910  97.505  1.00 68.90           O  
ANISOU 4909  O   PHE C1160     7600   5988  12590   -461   -683   -494       O  
ATOM   4910  CB  PHE C1160      12.926  49.047  97.294  1.00 69.31           C  
ANISOU 4910  CB  PHE C1160     7546   6052  12735   -732   -720   -385       C  
ATOM   4911  CG  PHE C1160      11.699  49.527  98.013  1.00 69.47           C  
ANISOU 4911  CG  PHE C1160     7432   6162  12799   -803   -688   -327       C  
ATOM   4912  CD1 PHE C1160      10.636  50.078  97.308  1.00 69.45           C  
ANISOU 4912  CD1 PHE C1160     7331   6204  12851   -877   -707   -292       C  
ATOM   4913  CD2 PHE C1160      11.597  49.409  99.394  1.00 69.52           C  
ANISOU 4913  CD2 PHE C1160     7412   6221  12781   -777   -634   -299       C  
ATOM   4914  CE1 PHE C1160       9.499  50.516  97.973  1.00 69.91           C  
ANISOU 4914  CE1 PHE C1160     7253   6374  12937   -917   -668   -222       C  
ATOM   4915  CE2 PHE C1160      10.472  49.860 100.068  1.00 69.97           C  
ANISOU 4915  CE2 PHE C1160     7342   6381  12861   -812   -589   -231       C  
ATOM   4916  CZ  PHE C1160       9.420  50.416  99.358  1.00 70.27           C  
ANISOU 4916  CZ  PHE C1160     7270   6478  12952   -878   -603   -188       C  
ATOM   4917  N   GLY C1161      15.660  49.591  95.355  1.00 68.34           N  
ANISOU 4917  N   GLY C1161     7512   5884  12572   -491   -719   -499       N  
ATOM   4918  CA  GLY C1161      16.797  48.872  94.761  1.00 67.80           C  
ANISOU 4918  CA  GLY C1161     7568   5771  12422   -378   -726   -509       C  
ATOM   4919  C   GLY C1161      18.172  48.963  95.394  1.00 67.43           C  
ANISOU 4919  C   GLY C1161     7485   5791  12344   -256   -683   -527       C  
ATOM   4920  O   GLY C1161      19.141  48.479  94.784  1.00 67.69           O  
ANISOU 4920  O   GLY C1161     7595   5818  12306   -138   -677   -521       O  
ATOM   4921  N   THR C1162      18.278  49.565  96.589  1.00 66.78           N  
ANISOU 4921  N   THR C1162     7291   5780  12305   -271   -658   -543       N  
ATOM   4922  CA  THR C1162      19.578  49.683  97.320  1.00 67.31           C  
ANISOU 4922  CA  THR C1162     7309   5922  12346   -169   -638   -560       C  
ATOM   4923  C   THR C1162      19.419  50.013  98.816  1.00 67.78           C  
ANISOU 4923  C   THR C1162     7310   6023  12421   -191   -633   -581       C  
ATOM   4924  O   THR C1162      18.792  51.014  99.185  1.00 67.80           O  
ANISOU 4924  O   THR C1162     7219   6050  12492   -255   -630   -597       O  
ATOM   4925  CB  THR C1162      20.529  50.723  96.660  1.00 66.85           C  
ANISOU 4925  CB  THR C1162     7122   5938  12340   -129   -622   -560       C  
ATOM   4926  OG1 THR C1162      21.299  50.095  95.630  1.00 66.89           O  
ANISOU 4926  OG1 THR C1162     7196   5942  12277    -24   -609   -529       O  
ATOM   4927  CG2 THR C1162      21.472  51.313  97.648  1.00 67.05           C  
ANISOU 4927  CG2 THR C1162     7036   6052  12385    -99   -625   -577       C  
ATOM   4928  N   LEU C1163      20.002  49.182  99.676  1.00 68.65           N  
ANISOU 4928  N   LEU C1163     7490   6141  12454   -117   -633   -582       N  
ATOM   4929  CA  LEU C1163      19.860  49.347 101.134  1.00 69.47           C  
ANISOU 4929  CA  LEU C1163     7569   6279  12549   -114   -629   -601       C  
ATOM   4930  C   LEU C1163      19.647  50.809 101.567  1.00 69.37           C  
ANISOU 4930  C   LEU C1163     7421   6317  12619   -158   -636   -634       C  
ATOM   4931  O   LEU C1163      18.822  51.096 102.435  1.00 69.42           O  
ANISOU 4931  O   LEU C1163     7422   6326  12630   -186   -624   -638       O  
ATOM   4932  CB  LEU C1163      21.042  48.697 101.911  1.00 69.87           C  
ANISOU 4932  CB  LEU C1163     7662   6371  12514      9   -635   -612       C  
ATOM   4933  CG  LEU C1163      20.907  48.514 103.439  1.00 70.01           C  
ANISOU 4933  CG  LEU C1163     7708   6406  12487     39   -633   -627       C  
ATOM   4934  CD1 LEU C1163      21.262  49.760 104.233  1.00 70.45           C  
ANISOU 4934  CD1 LEU C1163     7641   6535  12593     42   -662   -674       C  
ATOM   4935  CD2 LEU C1163      19.511  48.075 103.850  1.00 70.27           C  
ANISOU 4935  CD2 LEU C1163     7812   6374  12512    -41   -604   -591       C  
ATOM   4936  N   GLY C1164      20.399  51.721 100.966  1.00 69.62           N  
ANISOU 4936  N   GLY C1164     7356   6389  12708   -157   -654   -651       N  
ATOM   4937  CA  GLY C1164      20.242  53.134 101.263  1.00 70.83           C  
ANISOU 4937  CA  GLY C1164     7417   6563  12932   -204   -675   -683       C  
ATOM   4938  C   GLY C1164      18.816  53.591 100.990  1.00 70.44           C  
ANISOU 4938  C   GLY C1164     7369   6475  12920   -271   -651   -675       C  
ATOM   4939  O   GLY C1164      18.103  54.085 101.897  1.00 70.57           O  
ANISOU 4939  O   GLY C1164     7385   6498  12931   -270   -646   -690       O  
ATOM   4940  N   GLU C1165      18.392  53.390  99.744  1.00 69.67           N  
ANISOU 4940  N   GLU C1165     7278   6346  12848   -311   -635   -645       N  
ATOM   4941  CA  GLU C1165      17.128  53.923  99.281  1.00 69.52           C  
ANISOU 4941  CA  GLU C1165     7235   6309  12869   -373   -621   -631       C  
ATOM   4942  C   GLU C1165      15.940  53.434 100.108  1.00 70.44           C  
ANISOU 4942  C   GLU C1165     7378   6433  12954   -395   -598   -601       C  
ATOM   4943  O   GLU C1165      15.014  54.226 100.383  1.00 70.56           O  
ANISOU 4943  O   GLU C1165     7343   6477  12990   -406   -580   -594       O  
ATOM   4944  CB  GLU C1165      16.959  53.657  97.799  1.00 68.80           C  
ANISOU 4944  CB  GLU C1165     7162   6183  12797   -404   -622   -604       C  
ATOM   4945  CG  GLU C1165      17.724  54.656  96.946  1.00 68.10           C  
ANISOU 4945  CG  GLU C1165     7010   6104  12760   -393   -625   -617       C  
ATOM   4946  CD  GLU C1165      18.051  54.120  95.574  1.00 67.79           C  
ANISOU 4946  CD  GLU C1165     7013   6039  12706   -372   -621   -588       C  
ATOM   4947  OE1 GLU C1165      17.703  54.796  94.592  1.00 67.71           O  
ANISOU 4947  OE1 GLU C1165     6976   6015  12737   -394   -615   -580       O  
ATOM   4948  OE2 GLU C1165      18.644  53.029  95.479  1.00 67.38           O  
ANISOU 4948  OE2 GLU C1165     7035   5976  12588   -317   -622   -574       O  
ATOM   4949  N   SER C1166      16.002  52.169 100.548  1.00 71.10           N  
ANISOU 4949  N   SER C1166     7540   6496  12977   -389   -594   -574       N  
ATOM   4950  CA  SER C1166      14.963  51.580 101.414  1.00 72.06           C  
ANISOU 4950  CA  SER C1166     7684   6631  13065   -418   -566   -523       C  
ATOM   4951  C   SER C1166      14.727  52.455 102.640  1.00 73.26           C  
ANISOU 4951  C   SER C1166     7786   6845  13206   -357   -538   -541       C  
ATOM   4952  O   SER C1166      13.577  52.697 103.017  1.00 73.81           O  
ANISOU 4952  O   SER C1166     7811   6960  13274   -372   -501   -492       O  
ATOM   4953  CB  SER C1166      15.331  50.170 101.870  1.00 72.11           C  
ANISOU 4953  CB  SER C1166     7806   6594  12999   -405   -569   -497       C  
ATOM   4954  OG  SER C1166      15.903  49.389 100.823  1.00 72.12           O  
ANISOU 4954  OG  SER C1166     7895   6526  12980   -410   -603   -499       O  
ATOM   4955  N   PHE C1167      15.814  52.937 103.253  1.00 73.95           N  
ANISOU 4955  N   PHE C1167     7882   6939  13276   -280   -562   -605       N  
ATOM   4956  CA  PHE C1167      15.707  53.744 104.456  1.00 75.25           C  
ANISOU 4956  CA  PHE C1167     8041   7141  13409   -206   -557   -636       C  
ATOM   4957  C   PHE C1167      14.816  54.951 104.152  1.00 75.53           C  
ANISOU 4957  C   PHE C1167     8020   7196  13483   -212   -543   -636       C  
ATOM   4958  O   PHE C1167      13.638  54.983 104.537  1.00 75.91           O  
ANISOU 4958  O   PHE C1167     8045   7291  13505   -196   -491   -581       O  
ATOM   4959  CB  PHE C1167      17.087  54.234 104.911  1.00 76.50           C  
ANISOU 4959  CB  PHE C1167     8213   7295  13560   -151   -619   -711       C  
ATOM   4960  CG  PHE C1167      17.736  53.396 105.991  1.00 76.80           C  
ANISOU 4960  CG  PHE C1167     8316   7346  13519    -78   -627   -721       C  
ATOM   4961  CD1 PHE C1167      18.707  52.448 105.667  1.00 76.18           C  
ANISOU 4961  CD1 PHE C1167     8261   7262  13422    -69   -644   -717       C  
ATOM   4962  CD2 PHE C1167      17.425  53.605 107.335  1.00 77.87           C  
ANISOU 4962  CD2 PHE C1167     8499   7504  13586      6   -617   -734       C  
ATOM   4963  CE1 PHE C1167      19.328  51.704 106.651  1.00 76.30           C  
ANISOU 4963  CE1 PHE C1167     8341   7293  13356     13   -652   -726       C  
ATOM   4964  CE2 PHE C1167      18.041  52.852 108.326  1.00 77.82           C  
ANISOU 4964  CE2 PHE C1167     8559   7509  13500     84   -626   -744       C  
ATOM   4965  CZ  PHE C1167      18.993  51.902 107.978  1.00 77.30           C  
ANISOU 4965  CZ  PHE C1167     8511   7437  13421     83   -645   -741       C  
ATOM   4966  N   TYR C1168      15.383  55.929 103.443  1.00 75.51           N  
ANISOU 4966  N   TYR C1168     7993   7164  13535   -229   -587   -686       N  
ATOM   4967  CA  TYR C1168      14.666  57.168 103.045  1.00 75.63           C  
ANISOU 4967  CA  TYR C1168     7977   7180  13579   -223   -582   -694       C  
ATOM   4968  C   TYR C1168      13.203  56.933 102.632  1.00 74.67           C  
ANISOU 4968  C   TYR C1168     7805   7108  13459   -245   -522   -618       C  
ATOM   4969  O   TYR C1168      12.344  57.760 102.929  1.00 74.13           O  
ANISOU 4969  O   TYR C1168     7722   7079  13366   -184   -494   -606       O  
ATOM   4970  CB  TYR C1168      15.435  57.877 101.914  1.00 75.47           C  
ANISOU 4970  CB  TYR C1168     7933   7111  13631   -277   -627   -727       C  
ATOM   4971  CG  TYR C1168      14.665  58.940 101.141  1.00 74.76           C  
ANISOU 4971  CG  TYR C1168     7821   7010  13575   -284   -616   -723       C  
ATOM   4972  CD1 TYR C1168      14.403  60.202 101.696  1.00 75.47           C  
ANISOU 4972  CD1 TYR C1168     7958   7079  13638   -219   -634   -761       C  
ATOM   4973  CD2 TYR C1168      14.264  58.713  99.841  1.00 74.10           C  
ANISOU 4973  CD2 TYR C1168     7693   6925  13537   -342   -597   -685       C  
ATOM   4974  CE1 TYR C1168      13.736  61.187 100.974  1.00 74.69           C  
ANISOU 4974  CE1 TYR C1168     7857   6965  13558   -207   -623   -757       C  
ATOM   4975  CE2 TYR C1168      13.598  59.694  99.113  1.00 73.90           C  
ANISOU 4975  CE2 TYR C1168     7651   6891  13535   -336   -588   -682       C  
ATOM   4976  CZ  TYR C1168      13.338  60.922  99.684  1.00 74.04           C  
ANISOU 4976  CZ  TYR C1168     7712   6894  13526   -267   -597   -716       C  
ATOM   4977  OH  TYR C1168      12.655  61.867  98.961  1.00 73.46           O  
ANISOU 4977  OH  TYR C1168     7638   6811  13463   -243   -585   -709       O  
ATOM   4978  N   THR C1169      12.947  55.798 101.962  1.00 73.48           N  
ANISOU 4978  N   THR C1169     7635   6956  13327   -328   -512   -564       N  
ATOM   4979  CA  THR C1169      11.601  55.406 101.524  1.00 72.58           C  
ANISOU 4979  CA  THR C1169     7461   6892  13223   -385   -478   -479       C  
ATOM   4980  C   THR C1169      10.726  54.894 102.682  1.00 72.92           C  
ANISOU 4980  C   THR C1169     7484   7013  13209   -356   -421   -402       C  
ATOM   4981  O   THR C1169       9.507  55.107 102.685  1.00 72.86           O  
ANISOU 4981  O   THR C1169     7393   7093  13198   -358   -380   -325       O  
ATOM   4982  CB  THR C1169      11.672  54.344 100.419  1.00 71.90           C  
ANISOU 4982  CB  THR C1169     7394   6755  13169   -493   -512   -450       C  
ATOM   4983  OG1 THR C1169      12.522  54.809  99.363  1.00 71.35           O  
ANISOU 4983  OG1 THR C1169     7343   6629  13140   -495   -549   -508       O  
ATOM   4984  CG2 THR C1169      10.304  54.062  99.867  1.00 72.54           C  
ANISOU 4984  CG2 THR C1169     7406   6886  13270   -575   -506   -364       C  
ATOM   4985  N   LEU C1170      11.341  54.212 103.653  1.00 72.38           N  
ANISOU 4985  N   LEU C1170     7484   6927  13091   -323   -415   -412       N  
ATOM   4986  CA  LEU C1170      10.597  53.723 104.817  1.00 73.07           C  
ANISOU 4986  CA  LEU C1170     7562   7088  13116   -283   -351   -331       C  
ATOM   4987  C   LEU C1170      10.278  54.874 105.811  1.00 73.49           C  
ANISOU 4987  C   LEU C1170     7608   7207  13107   -127   -309   -350       C  
ATOM   4988  O   LEU C1170       9.327  54.802 106.608  1.00 73.67           O  
ANISOU 4988  O   LEU C1170     7589   7329  13073    -65   -234   -261       O  
ATOM   4989  CB  LEU C1170      11.334  52.552 105.473  1.00 73.29           C  
ANISOU 4989  CB  LEU C1170     7683   7065  13099   -290   -358   -331       C  
ATOM   4990  CG  LEU C1170      11.211  51.166 104.807  1.00 73.45           C  
ANISOU 4990  CG  LEU C1170     7741   7028  13140   -427   -381   -269       C  
ATOM   4991  CD1 LEU C1170      12.093  50.115 105.491  1.00 73.59           C  
ANISOU 4991  CD1 LEU C1170     7883   6984  13095   -397   -389   -284       C  
ATOM   4992  CD2 LEU C1170       9.765  50.682 104.756  1.00 74.46           C  
ANISOU 4992  CD2 LEU C1170     7787   7224  13282   -530   -343   -131       C  
ATOM   4993  N   PHE C1171      11.077  55.941 105.718  1.00 72.85           N  
ANISOU 4993  N   PHE C1171     7577   7070  13032    -63   -360   -459       N  
ATOM   4994  CA  PHE C1171      10.780  57.241 106.314  1.00 73.06           C  
ANISOU 4994  CA  PHE C1171     7634   7123  13004     78   -349   -496       C  
ATOM   4995  C   PHE C1171       9.507  57.768 105.659  1.00 73.26           C  
ANISOU 4995  C   PHE C1171     7562   7229  13044     83   -300   -424       C  
ATOM   4996  O   PHE C1171       8.628  58.333 106.328  1.00 74.22           O  
ANISOU 4996  O   PHE C1171     7672   7441  13089    217   -238   -376       O  
ATOM   4997  CB  PHE C1171      11.937  58.203 106.001  1.00 72.67           C  
ANISOU 4997  CB  PHE C1171     7658   6968  12984     82   -442   -618       C  
ATOM   4998  CG  PHE C1171      12.100  59.334 106.980  1.00 72.99           C  
ANISOU 4998  CG  PHE C1171     7807   6984  12943    228   -472   -685       C  
ATOM   4999  CD1 PHE C1171      13.338  59.595 107.524  1.00 73.40           C  
ANISOU 4999  CD1 PHE C1171     7952   6955  12982    239   -563   -778       C  
ATOM   5000  CD2 PHE C1171      11.037  60.147 107.329  1.00 73.79           C  
ANISOU 5000  CD2 PHE C1171     7925   7141  12971    361   -419   -654       C  
ATOM   5001  CE1 PHE C1171      13.511  60.638 108.423  1.00 74.98           C  
ANISOU 5001  CE1 PHE C1171     8282   7108  13099    364   -618   -848       C  
ATOM   5002  CE2 PHE C1171      11.199  61.195 108.228  1.00 74.95           C  
ANISOU 5002  CE2 PHE C1171     8215   7242  13021    515   -458   -723       C  
ATOM   5003  CZ  PHE C1171      12.437  61.443 108.780  1.00 75.28           C  
ANISOU 5003  CZ  PHE C1171     8371   7179  13051    509   -566   -825       C  
ATOM   5004  N   GLN C1172       9.415  57.583 104.340  1.00 72.09           N  
ANISOU 5004  N   GLN C1172     7350   7058  12984    -46   -328   -412       N  
ATOM   5005  CA  GLN C1172       8.244  58.017 103.581  1.00 72.44           C  
ANISOU 5005  CA  GLN C1172     7293   7184  13049    -53   -296   -344       C  
ATOM   5006  C   GLN C1172       6.958  57.370 104.136  1.00 73.96           C  
ANISOU 5006  C   GLN C1172     7374   7525  13201    -45   -215   -199       C  
ATOM   5007  O   GLN C1172       5.904  57.991 104.177  1.00 74.64           O  
ANISOU 5007  O   GLN C1172     7379   7731  13252     41   -161   -130       O  
ATOM   5008  CB  GLN C1172       8.450  57.694 102.104  1.00 70.92           C  
ANISOU 5008  CB  GLN C1172     7065   6931  12949   -199   -351   -356       C  
ATOM   5009  CG  GLN C1172       7.645  58.528 101.125  1.00 70.45           C  
ANISOU 5009  CG  GLN C1172     6937   6915  12915   -187   -349   -336       C  
ATOM   5010  CD  GLN C1172       8.101  58.324  99.691  1.00 69.12           C  
ANISOU 5010  CD  GLN C1172     6774   6663  12825   -304   -411   -370       C  
ATOM   5011  OE1 GLN C1172       9.275  58.475  99.381  1.00 68.24           O  
ANISOU 5011  OE1 GLN C1172     6742   6446  12741   -321   -453   -452       O  
ATOM   5012  NE2 GLN C1172       7.182  57.965  98.818  1.00 69.02           N  
ANISOU 5012  NE2 GLN C1172     6674   6707  12844   -380   -421   -300       N  
ATOM   5013  N   VAL C1173       7.085  56.129 104.588  1.00 74.89           N  
ANISOU 5013  N   VAL C1173     7493   7641  13320   -130   -206   -145       N  
ATOM   5014  CA  VAL C1173       5.982  55.341 105.140  1.00 76.66           C  
ANISOU 5014  CA  VAL C1173     7612   7997  13518   -162   -133     12       C  
ATOM   5015  C   VAL C1173       5.679  55.706 106.611  1.00 77.83           C  
ANISOU 5015  C   VAL C1173     7779   8240  13552     29    -42     53       C  
ATOM   5016  O   VAL C1173       4.540  55.585 107.067  1.00 78.88           O  
ANISOU 5016  O   VAL C1173     7793   8535  13644     71     46    199       O  
ATOM   5017  CB  VAL C1173       6.296  53.824 105.016  1.00 76.86           C  
ANISOU 5017  CB  VAL C1173     7669   7952  13582   -336   -169     54       C  
ATOM   5018  CG1 VAL C1173       5.057  52.969 105.290  1.00 78.23           C  
ANISOU 5018  CG1 VAL C1173     7716   8252  13756   -435   -116    240       C  
ATOM   5019  CG2 VAL C1173       6.904  53.506 103.647  1.00 75.23           C  
ANISOU 5019  CG2 VAL C1173     7508   7619  13458   -474   -268    -19       C  
HETATM 5020  N   MSE C1174       6.699  56.144 107.348  1.00 77.86           N  
ANISOU 5020  N   MSE C1174     7932   8153  13501    149    -65    -68       N  
HETATM 5021  CA  MSE C1174       6.510  56.605 108.746  1.00 79.49           C  
ANISOU 5021  CA  MSE C1174     8199   8427  13578    361      7    -53       C  
HETATM 5022  C   MSE C1174       5.679  57.880 108.750  1.00 80.88           C  
ANISOU 5022  C   MSE C1174     8344   8696  13690    532     52    -35       C  
HETATM 5023  O   MSE C1174       4.666  57.975 109.458  1.00 82.93           O  
ANISOU 5023  O   MSE C1174     8533   9115  13860    669    158     89       O  
HETATM 5024  CB  MSE C1174       7.848  56.822 109.466  1.00 78.16           C  
ANISOU 5024  CB  MSE C1174     8209   8125  13364    439    -60   -198       C  
HETATM 5025  CG  MSE C1174       7.597  57.235 110.896  1.00 79.41           C  
ANISOU 5025  CG  MSE C1174     8450   8346  13375    667      4   -182       C  
HETATM 5026 SE   MSE C1174       9.236  57.338 111.994  1.00 79.53          SE  
ANISOU 5026 SE   MSE C1174     8691   8208  13318    761    -98   -352      SE  
HETATM 5027  CE  MSE C1174       9.779  59.215 111.631  1.00 79.57           C  
ANISOU 5027  CE  MSE C1174     8829   8096  13310    854   -218   -517       C  
ATOM   5028  N   THR C1175       6.081  58.851 107.935  1.00 79.87           N  
ANISOU 5028  N   THR C1175     8268   8476  13601    533    -22   -146       N  
ATOM   5029  CA  THR C1175       5.410  60.138 107.876  1.00 80.90           C  
ANISOU 5029  CA  THR C1175     8414   8665  13661    708      7   -149       C  
ATOM   5030  C   THR C1175       4.069  60.044 107.150  1.00 81.59           C  
ANISOU 5030  C   THR C1175     8301   8922  13777    675     75     -4       C  
ATOM   5031  O   THR C1175       3.396  61.057 106.938  1.00 82.27           O  
ANISOU 5031  O   THR C1175     8375   9077  13805    822    106     10       O  
ATOM   5032  CB  THR C1175       6.293  61.143 107.131  1.00 80.56           C  
ANISOU 5032  CB  THR C1175     8494   8454  13661    687   -101   -303       C  
ATOM   5033  OG1 THR C1175       6.520  60.673 105.788  1.00 80.16           O  
ANISOU 5033  OG1 THR C1175     8350   8357  13749    473   -151   -308       O  
ATOM   5034  CG2 THR C1175       7.641  61.299 107.845  1.00 79.99           C  
ANISOU 5034  CG2 THR C1175     8601   8227  13566    705   -187   -437       C  
ATOM   5035  N   LEU C1176       3.703  58.820 106.759  1.00 81.66           N  
ANISOU 5035  N   LEU C1176     8162   8992  13872    479     87    103       N  
ATOM   5036  CA  LEU C1176       2.510  58.528 105.928  1.00 81.97           C  
ANISOU 5036  CA  LEU C1176     7993   9185  13967    380    116    246       C  
ATOM   5037  C   LEU C1176       2.382  59.445 104.693  1.00 81.14           C  
ANISOU 5037  C   LEU C1176     7876   9047  13908    377     60    181       C  
ATOM   5038  O   LEU C1176       1.289  59.897 104.357  1.00 82.33           O  
ANISOU 5038  O   LEU C1176     7891   9357  14032    447    107    279       O  
ATOM   5039  CB  LEU C1176       1.231  58.557 106.785  1.00 84.09           C  
ANISOU 5039  CB  LEU C1176     8118   9696  14137    529    247    429       C  
ATOM   5040  CG  LEU C1176       1.319  58.128 108.267  1.00 85.17           C  
ANISOU 5040  CG  LEU C1176     8310   9879  14171    650    334    486       C  
ATOM   5041  CD1 LEU C1176      -0.010  58.353 108.985  1.00 87.06           C  
ANISOU 5041  CD1 LEU C1176     8393  10385  14299    836    479    682       C  
ATOM   5042  CD2 LEU C1176       1.793  56.687 108.448  1.00 84.53           C  
ANISOU 5042  CD2 LEU C1176     8229   9725  14164    432    306    519       C  
ATOM   5043  N   GLU C1177       3.516  59.723 104.044  1.00 79.41           N  
ANISOU 5043  N   GLU C1177     7793   8630  13748    305    -36     24       N  
ATOM   5044  CA  GLU C1177       3.585  60.561 102.840  1.00 78.66           C  
ANISOU 5044  CA  GLU C1177     7714   8473  13700    292    -92    -46       C  
ATOM   5045  C   GLU C1177       3.494  59.700 101.575  1.00 78.22           C  
ANISOU 5045  C   GLU C1177     7561   8396  13761     66   -155    -16       C  
ATOM   5046  O   GLU C1177       4.502  59.132 101.127  1.00 77.24           O  
ANISOU 5046  O   GLU C1177     7517   8125  13705    -68   -225    -95       O  
ATOM   5047  CB  GLU C1177       4.901  61.358 102.830  1.00 77.30           C  
ANISOU 5047  CB  GLU C1177     7740   8103  13527    332   -160   -215       C  
ATOM   5048  CG  GLU C1177       4.994  62.463 101.767  1.00 76.52           C  
ANISOU 5048  CG  GLU C1177     7691   7931  13452    358   -204   -285       C  
ATOM   5049  CD  GLU C1177       5.520  61.974 100.423  1.00 74.98           C  
ANISOU 5049  CD  GLU C1177     7465   7648  13378    164   -273   -317       C  
ATOM   5050  OE1 GLU C1177       5.000  62.409  99.378  1.00 75.12           O  
ANISOU 5050  OE1 GLU C1177     7431   7690  13421    156   -284   -301       O  
ATOM   5051  OE2 GLU C1177       6.447  61.152 100.397  1.00 73.53           O  
ANISOU 5051  OE2 GLU C1177     7314   7374  13250     38   -316   -356       O  
ATOM   5052  N   SER C1178       2.290  59.595 101.012  1.00 78.91           N  
ANISOU 5052  N   SER C1178     7481   8638  13863     33   -137    104       N  
ATOM   5053  CA  SER C1178       2.072  58.892  99.742  1.00 78.63           C  
ANISOU 5053  CA  SER C1178     7368   8582  13925   -168   -217    131       C  
ATOM   5054  C   SER C1178       2.325  57.371  99.796  1.00 79.27           C  
ANISOU 5054  C   SER C1178     7443   8611  14064   -376   -262    177       C  
ATOM   5055  O   SER C1178       2.246  56.696  98.751  1.00 79.39           O  
ANISOU 5055  O   SER C1178     7439   8576  14148   -546   -348    187       O  
ATOM   5056  CB  SER C1178       2.934  59.503  98.636  1.00 76.76           C  
ANISOU 5056  CB  SER C1178     7251   8181  13733   -183   -288     -7       C  
ATOM   5057  OG  SER C1178       2.890  60.908  98.665  1.00 76.89           O  
ANISOU 5057  OG  SER C1178     7324   8200  13691      3   -255    -63       O  
ATOM   5058  N   TRP C1179       2.626  56.837 100.988  1.00 79.34           N  
ANISOU 5058  N   TRP C1179     7491   8620  14033   -354   -212    201       N  
ATOM   5059  CA  TRP C1179       3.078  55.437 101.145  1.00 79.35           C  
ANISOU 5059  CA  TRP C1179     7542   8534  14072   -526   -254    223       C  
ATOM   5060  C   TRP C1179       2.338  54.443 100.300  1.00 80.73           C  
ANISOU 5060  C   TRP C1179     7625   8736  14314   -741   -327    327       C  
ATOM   5061  O   TRP C1179       2.956  53.522  99.763  1.00 80.60           O  
ANISOU 5061  O   TRP C1179     7717   8571  14338   -884   -412    284       O  
ATOM   5062  CB  TRP C1179       3.023  54.975 102.605  1.00 79.85           C  
ANISOU 5062  CB  TRP C1179     7609   8658  14071   -465   -170    293       C  
ATOM   5063  CG  TRP C1179       1.621  54.757 103.129  1.00 80.96           C  
ANISOU 5063  CG  TRP C1179     7556   9018  14185   -468    -93    490       C  
ATOM   5064  CD1 TRP C1179       0.726  55.716 103.581  1.00 81.83           C  
ANISOU 5064  CD1 TRP C1179     7546   9320  14227   -283      2    567       C  
ATOM   5065  CD2 TRP C1179       0.918  53.489 103.273  1.00 82.02           C  
ANISOU 5065  CD2 TRP C1179     7588   9221  14356   -663   -100    656       C  
ATOM   5066  NE1 TRP C1179      -0.453  55.145 103.979  1.00 83.15           N  
ANISOU 5066  NE1 TRP C1179     7518   9688  14387   -343     63    775       N  
ATOM   5067  CE2 TRP C1179      -0.401  53.808 103.818  1.00 83.72           C  
ANISOU 5067  CE2 TRP C1179     7588   9693  14529   -587      1    841       C  
ATOM   5068  CE3 TRP C1179       1.233  52.162 103.002  1.00 82.28           C  
ANISOU 5068  CE3 TRP C1179     7693   9126  14442   -884   -181    677       C  
ATOM   5069  CZ2 TRP C1179      -1.349  52.823 104.074  1.00 85.47           C  
ANISOU 5069  CZ2 TRP C1179     7648  10048  14780   -757     17   1050       C  
ATOM   5070  CZ3 TRP C1179       0.274  51.176 103.273  1.00 83.62           C  
ANISOU 5070  CZ3 TRP C1179     7736   9401  14636  -1056   -176    874       C  
ATOM   5071  CH2 TRP C1179      -0.983  51.502 103.795  1.00 85.28           C  
ANISOU 5071  CH2 TRP C1179     7714   9869  14821  -1007    -79   1062       C  
ATOM   5072  N   SER C1180       1.015  54.617 100.171  1.00 82.39           N  
ANISOU 5072  N   SER C1180     7642   9136  14528   -760   -303    469       N  
ATOM   5073  CA  SER C1180       0.165  53.656  99.435  1.00 83.26           C  
ANISOU 5073  CA  SER C1180     7641   9290  14703   -992   -392    592       C  
ATOM   5074  C   SER C1180       0.167  53.892  97.923  1.00 82.34           C  
ANISOU 5074  C   SER C1180     7547   9100  14638  -1062   -506    520       C  
ATOM   5075  O   SER C1180       0.733  53.079  97.189  1.00 81.29           O  
ANISOU 5075  O   SER C1180     7548   8796  14543  -1207   -614    460       O  
ATOM   5076  CB  SER C1180      -1.264  53.624  99.997  1.00 85.52           C  
ANISOU 5076  CB  SER C1180     7680   9839  14975  -1004   -323    805       C  
ATOM   5077  OG  SER C1180      -2.160  52.956  99.120  1.00 86.57           O  
ANISOU 5077  OG  SER C1180     7682  10032  15178  -1228   -432    922       O  
HETATM 5078  N   MSE C1181      -0.442  55.000  97.471  1.00 82.22           N  
ANISOU 5078  N   MSE C1181     7422   9208  14609   -939   -480    524       N  
HETATM 5079  CA  MSE C1181      -0.510  55.337  96.026  1.00 81.53           C  
ANISOU 5079  CA  MSE C1181     7352   9067  14559   -979   -580    460       C  
HETATM 5080  C   MSE C1181       0.862  55.576  95.424  1.00 79.78           C  
ANISOU 5080  C   MSE C1181     7352   8618  14343   -934   -615    277       C  
HETATM 5081  O   MSE C1181       1.129  55.121  94.318  1.00 79.15           O  
ANISOU 5081  O   MSE C1181     7354   8421  14298  -1042   -722    228       O  
HETATM 5082  CB  MSE C1181      -1.411  56.526  95.708  1.00 81.68           C  
ANISOU 5082  CB  MSE C1181     7221   9266  14548   -829   -536    502       C  
HETATM 5083  CG  MSE C1181      -2.768  56.464  96.412  1.00 83.76           C  
ANISOU 5083  CG  MSE C1181     7234   9803  14787   -820   -470    703       C  
HETATM 5084 SE   MSE C1181      -4.052  55.271  95.494  1.00 85.45          SE  
ANISOU 5084 SE   MSE C1181     7237  10140  15089  -1140   -629    888      SE  
HETATM 5085  CE  MSE C1181      -5.675  56.191  96.128  1.00 87.35           C  
ANISOU 5085  CE  MSE C1181     7130  10794  15265   -956   -496   1106       C  
ATOM   5086  N   GLY C1182       1.743  56.275  96.144  1.00 78.77           N  
ANISOU 5086  N   GLY C1182     7323   8431  14176   -774   -532    181       N  
ATOM   5087  CA  GLY C1182       3.124  56.459  95.699  1.00 77.56           C  
ANISOU 5087  CA  GLY C1182     7355   8082  14032   -742   -559     30       C  
ATOM   5088  C   GLY C1182       3.997  55.195  95.683  1.00 77.81           C  
ANISOU 5088  C   GLY C1182     7517   7966  14083   -869   -617     -3       C  
ATOM   5089  O   GLY C1182       4.822  55.011  94.761  1.00 77.15           O  
ANISOU 5089  O   GLY C1182     7555   7743  14015   -895   -678    -88       O  
ATOM   5090  N   ILE C1183       3.832  54.323  96.690  1.00 77.72           N  
ANISOU 5090  N   ILE C1183     7489   7983  14056   -931   -592     71       N  
ATOM   5091  CA  ILE C1183       4.690  53.132  96.838  1.00 76.59           C  
ANISOU 5091  CA  ILE C1183     7493   7696  13910  -1022   -637     40       C  
ATOM   5092  C   ILE C1183       3.924  51.793  96.785  1.00 77.97           C  
ANISOU 5092  C   ILE C1183     7651   7873  14100  -1220   -708    160       C  
ATOM   5093  O   ILE C1183       4.133  50.988  95.849  1.00 78.07           O  
ANISOU 5093  O   ILE C1183     7779   7759  14126  -1336   -817    138       O  
ATOM   5094  CB  ILE C1183       5.548  53.212  98.131  1.00 75.96           C  
ANISOU 5094  CB  ILE C1183     7479   7596  13788   -911   -556     -5       C  
ATOM   5095  CG1 ILE C1183       6.593  54.337  98.036  1.00 74.23           C  
ANISOU 5095  CG1 ILE C1183     7325   7319  13560   -763   -530   -136       C  
ATOM   5096  CG2 ILE C1183       6.178  51.860  98.473  1.00 76.09           C  
ANISOU 5096  CG2 ILE C1183     7625   7499  13785   -999   -591     -1       C  
ATOM   5097  CD1 ILE C1183       7.501  54.237  96.835  1.00 72.74           C  
ANISOU 5097  CD1 ILE C1183     7241   7000  13398   -790   -597   -222       C  
ATOM   5098  N   VAL C1184       3.031  51.569  97.759  1.00 78.47           N  
ANISOU 5098  N   VAL C1184     7581   8076  14157  -1255   -650    292       N  
ATOM   5099  CA  VAL C1184       2.413  50.246  97.964  1.00 79.48           C  
ANISOU 5099  CA  VAL C1184     7702   8197  14299  -1459   -709    422       C  
ATOM   5100  C   VAL C1184       1.432  49.780  96.876  1.00 80.42           C  
ANISOU 5100  C   VAL C1184     7752   8335  14470  -1656   -840    507       C  
ATOM   5101  O   VAL C1184       1.452  48.609  96.531  1.00 81.64           O  
ANISOU 5101  O   VAL C1184     8027   8361  14633  -1836   -951    537       O  
ATOM   5102  CB  VAL C1184       1.736  50.095  99.352  1.00 80.92           C  
ANISOU 5102  CB  VAL C1184     7750   8537  14458  -1447   -600    566       C  
ATOM   5103  CG1 VAL C1184       1.322  48.637  99.586  1.00 82.28           C  
ANISOU 5103  CG1 VAL C1184     7958   8660  14646  -1675   -665    696       C  
ATOM   5104  CG2 VAL C1184       2.659  50.559 100.474  1.00 79.88           C  
ANISOU 5104  CG2 VAL C1184     7700   8386  14264  -1246   -485    480       C  
ATOM   5105  N   ARG C1185       0.568  50.655  96.357  1.00 70.49           N  
ANISOU 5105  N   ARG C1185     6830   7146  12807  -1152    225    833       N  
ATOM   5106  CA  ARG C1185      -0.309  50.268  95.250  1.00 71.02           C  
ANISOU 5106  CA  ARG C1185     6976   7203  12807  -1193    120    852       C  
ATOM   5107  C   ARG C1185       0.556  49.865  94.054  1.00 72.17           C  
ANISOU 5107  C   ARG C1185     7279   7306  12835  -1203    162    799       C  
ATOM   5108  O   ARG C1185       0.478  48.705  93.593  1.00 72.69           O  
ANISOU 5108  O   ARG C1185     7415   7344  12861  -1238    116    752       O  
ATOM   5109  CB  ARG C1185      -1.284  51.384  94.843  1.00 71.41           C  
ANISOU 5109  CB  ARG C1185     7007   7271  12853  -1185     50    927       C  
ATOM   5110  CG  ARG C1185      -2.280  51.870  95.906  1.00 70.81           C  
ANISOU 5110  CG  ARG C1185     6781   7219  12905  -1172     26    990       C  
ATOM   5111  CD  ARG C1185      -3.624  51.124  95.917  1.00 70.48           C  
ANISOU 5111  CD  ARG C1185     6675   7160  12943  -1210   -101   1029       C  
ATOM   5112  NE  ARG C1185      -4.432  51.666  97.015  1.00 70.11           N  
ANISOU 5112  NE  ARG C1185     6488   7118  13033  -1185    -66   1096       N  
ATOM   5113  CZ  ARG C1185      -5.686  51.328  97.330  1.00 70.14           C  
ANISOU 5113  CZ  ARG C1185     6386   7090  13176  -1202   -130   1156       C  
ATOM   5114  NH1 ARG C1185      -6.349  50.423  96.625  1.00 71.02           N  
ANISOU 5114  NH1 ARG C1185     6497   7161  13326  -1252   -265   1150       N  
ATOM   5115  NH2 ARG C1185      -6.277  51.913  98.369  1.00 69.30           N  
ANISOU 5115  NH2 ARG C1185     6169   6976  13185  -1165    -50   1218       N  
ATOM   5116  N   PRO C1186       1.422  50.795  93.560  1.00 72.71           N  
ANISOU 5116  N   PRO C1186     7409   7356  12862  -1168    272    802       N  
ATOM   5117  CA  PRO C1186       2.229  50.431  92.380  1.00 73.45           C  
ANISOU 5117  CA  PRO C1186     7674   7392  12841  -1166    350    762       C  
ATOM   5118  C   PRO C1186       3.146  49.250  92.666  1.00 73.10           C  
ANISOU 5118  C   PRO C1186     7631   7303  12840  -1181    425    688       C  
ATOM   5119  O   PRO C1186       3.569  48.570  91.712  1.00 74.36           O  
ANISOU 5119  O   PRO C1186     7941   7408  12904  -1191    472    644       O  
ATOM   5120  CB  PRO C1186       3.079  51.675  92.123  1.00 73.48           C  
ANISOU 5120  CB  PRO C1186     7691   7364  12863  -1117    497    792       C  
ATOM   5121  CG  PRO C1186       2.368  52.780  92.819  1.00 73.06           C  
ANISOU 5121  CG  PRO C1186     7508   7362  12889  -1102    444    852       C  
ATOM   5122  CD  PRO C1186       1.749  52.158  94.028  1.00 72.11           C  
ANISOU 5122  CD  PRO C1186     7253   7289  12856  -1127    350    838       C  
ATOM   5123  N   LEU C1187       3.457  49.020  93.947  1.00 71.05           N  
ANISOU 5123  N   LEU C1187     7220   7062  12715  -1175    440    677       N  
ATOM   5124  CA  LEU C1187       4.267  47.861  94.311  1.00 70.88           C  
ANISOU 5124  CA  LEU C1187     7182   6998  12752  -1183    496    622       C  
ATOM   5125  C   LEU C1187       3.473  46.573  94.099  1.00 71.50           C  
ANISOU 5125  C   LEU C1187     7300   7073  12793  -1230    400    601       C  
ATOM   5126  O   LEU C1187       3.966  45.625  93.470  1.00 72.06           O  
ANISOU 5126  O   LEU C1187     7465   7083  12832  -1250    449    546       O  
ATOM   5127  CB  LEU C1187       4.783  47.948  95.756  1.00 69.52           C  
ANISOU 5127  CB  LEU C1187     6854   6846  12713  -1152    511    622       C  
ATOM   5128  CG  LEU C1187       5.938  47.008  96.158  1.00 68.88           C  
ANISOU 5128  CG  LEU C1187     6740   6708  12722  -1141    583    576       C  
ATOM   5129  CD1 LEU C1187       7.297  47.525  95.719  1.00 68.65           C  
ANISOU 5129  CD1 LEU C1187     6719   6600  12766  -1117    718    546       C  
ATOM   5130  CD2 LEU C1187       5.937  46.750  97.657  1.00 68.10           C  
ANISOU 5130  CD2 LEU C1187     6518   6653  12706  -1109    526    589       C  
HETATM 5131  N   MSE C1188       2.235  46.572  94.600  1.00 71.68           N  
ANISOU 5131  N   MSE C1188     7247   7147  12841  -1246    276    643       N  
HETATM 5132  CA  MSE C1188       1.366  45.385  94.647  1.00 72.23           C  
ANISOU 5132  CA  MSE C1188     7301   7202  12943  -1290    180    631       C  
HETATM 5133  C   MSE C1188       1.157  44.819  93.247  1.00 73.27           C  
ANISOU 5133  C   MSE C1188     7594   7285  12961  -1332    121    572       C  
HETATM 5134  O   MSE C1188       0.986  43.604  93.085  1.00 73.45           O  
ANISOU 5134  O   MSE C1188     7636   7259  13012  -1370     88    520       O  
HETATM 5135  CB  MSE C1188       0.051  45.687  95.403  1.00 72.00           C  
ANISOU 5135  CB  MSE C1188     7145   7215  12996  -1293     81    702       C  
HETATM 5136  CG  MSE C1188       0.230  45.607  96.921  1.00 71.82           C  
ANISOU 5136  CG  MSE C1188     6994   7216  13076  -1251    148    742       C  
HETATM 5137 SE   MSE C1188      -1.404  45.860  98.050  1.00 74.06          SE  
ANISOU 5137 SE   MSE C1188     7127   7525  13487  -1236     93    844      SE  
HETATM 5138  CE  MSE C1188      -2.780  44.879  97.007  1.00 74.03           C  
ANISOU 5138  CE  MSE C1188     7119   7454  13556  -1319    -62    835       C  
ATOM   5139  N   GLU C1189       1.215  45.689  92.233  1.00 73.79           N  
ANISOU 5139  N   GLU C1189     7789   7356  12891  -1317    115    576       N  
ATOM   5140  CA  GLU C1189       0.935  45.293  90.838  1.00 75.39           C  
ANISOU 5140  CA  GLU C1189     8189   7519  12936  -1341     38    520       C  
ATOM   5141  C   GLU C1189       1.585  43.980  90.503  1.00 75.51           C  
ANISOU 5141  C   GLU C1189     8292   7459  12940  -1367    105    427       C  
ATOM   5142  O   GLU C1189       0.905  43.054  90.067  1.00 76.56           O  
ANISOU 5142  O   GLU C1189     8475   7558  13057  -1413    -20    366       O  
ATOM   5143  CB  GLU C1189       1.390  46.353  89.830  1.00 76.45           C  
ANISOU 5143  CB  GLU C1189     8490   7652  12905  -1295    104    543       C  
ATOM   5144  CG  GLU C1189       0.558  47.626  89.803  1.00 77.00           C  
ANISOU 5144  CG  GLU C1189     8516   7783  12958  -1271      8    634       C  
ATOM   5145  CD  GLU C1189       1.252  48.730  89.035  1.00 78.37           C  
ANISOU 5145  CD  GLU C1189     8824   7944  13010  -1211    136    677       C  
ATOM   5146  OE1 GLU C1189       2.508  48.718  89.009  1.00 78.56           O  
ANISOU 5146  OE1 GLU C1189     8887   7916  13046  -1185    340    652       O  
ATOM   5147  OE2 GLU C1189       0.561  49.613  88.453  1.00 79.73           O  
ANISOU 5147  OE2 GLU C1189     9057   8145  13093  -1186     43    743       O  
ATOM   5148  N   VAL C1190       2.898  43.907  90.714  1.00 74.80           N  
ANISOU 5148  N   VAL C1190     8207   7331  12882  -1337    300    413       N  
ATOM   5149  CA  VAL C1190       3.650  42.661  90.532  1.00 75.23           C  
ANISOU 5149  CA  VAL C1190     8317   7301  12966  -1356    399    335       C  
ATOM   5150  C   VAL C1190       3.582  41.793  91.791  1.00 74.50           C  
ANISOU 5150  C   VAL C1190     8030   7211  13064  -1374    389    347       C  
ATOM   5151  O   VAL C1190       3.450  40.576  91.703  1.00 75.13           O  
ANISOU 5151  O   VAL C1190     8123   7234  13191  -1412    372    290       O  
ATOM   5152  CB  VAL C1190       5.142  42.898  90.207  1.00 74.88           C  
ANISOU 5152  CB  VAL C1190     8345   7189  12917  -1312    628    323       C  
ATOM   5153  CG1 VAL C1190       5.793  41.581  89.804  1.00 75.58           C  
ANISOU 5153  CG1 VAL C1190     8519   7173  13023  -1333    731    238       C  
ATOM   5154  CG2 VAL C1190       5.320  43.948  89.122  1.00 75.40           C  
ANISOU 5154  CG2 VAL C1190     8590   7246  12811  -1273    689    343       C  
ATOM   5155  N   TYR C1191       3.672  42.434  92.953  1.00 73.36           N  
ANISOU 5155  N   TYR C1191     7720   7129  13026  -1341    402    422       N  
ATOM   5156  CA  TYR C1191       3.828  41.734  94.219  1.00 73.08           C  
ANISOU 5156  CA  TYR C1191     7527   7096  13145  -1331    422    450       C  
ATOM   5157  C   TYR C1191       2.578  41.945  95.079  1.00 73.08           C  
ANISOU 5157  C   TYR C1191     7403   7161  13203  -1334    302    517       C  
ATOM   5158  O   TYR C1191       2.524  42.893  95.875  1.00 72.66           O  
ANISOU 5158  O   TYR C1191     7267   7171  13170  -1293    303    577       O  
ATOM   5159  CB  TYR C1191       5.118  42.192  94.931  1.00 72.15           C  
ANISOU 5159  CB  TYR C1191     7335   6976  13101  -1276    544    470       C  
ATOM   5160  CG  TYR C1191       6.369  41.941  94.098  1.00 72.96           C  
ANISOU 5160  CG  TYR C1191     7536   6986  13198  -1270    692    414       C  
ATOM   5161  CD1 TYR C1191       6.973  42.972  93.380  1.00 72.83           C  
ANISOU 5161  CD1 TYR C1191     7599   6951  13122  -1246    780    411       C  
ATOM   5162  CD2 TYR C1191       6.937  40.657  94.012  1.00 73.70           C  
ANISOU 5162  CD2 TYR C1191     7643   6995  13366  -1285    768    372       C  
ATOM   5163  CE1 TYR C1191       8.111  42.747  92.610  1.00 73.71           C  
ANISOU 5163  CE1 TYR C1191     7800   6955  13249  -1234    952    371       C  
ATOM   5164  CE2 TYR C1191       8.078  40.421  93.246  1.00 74.53           C  
ANISOU 5164  CE2 TYR C1191     7836   6996  13486  -1276    931    325       C  
ATOM   5165  CZ  TYR C1191       8.663  41.468  92.535  1.00 74.39           C  
ANISOU 5165  CZ  TYR C1191     7900   6956  13410  -1249   1030    325       C  
ATOM   5166  OH  TYR C1191       9.791  41.237  91.753  1.00 74.60           O  
ANISOU 5166  OH  TYR C1191     8017   6857  13469  -1233   1228    288       O  
ATOM   5167  N   PRO C1192       1.571  41.058  94.913  1.00 73.69           N  
ANISOU 5167  N   PRO C1192     7466   7207  13326  -1381    208    504       N  
ATOM   5168  CA  PRO C1192       0.223  41.285  95.438  1.00 73.64           C  
ANISOU 5168  CA  PRO C1192     7352   7234  13394  -1391     98    568       C  
ATOM   5169  C   PRO C1192       0.119  41.368  96.942  1.00 73.01           C  
ANISOU 5169  C   PRO C1192     7128   7190  13422  -1340    156    656       C  
ATOM   5170  O   PRO C1192      -0.364  42.373  97.461  1.00 72.99           O  
ANISOU 5170  O   PRO C1192     7071   7245  13418  -1309    137    718       O  
ATOM   5171  CB  PRO C1192      -0.583  40.086  94.909  1.00 75.03           C  
ANISOU 5171  CB  PRO C1192     7533   7331  13644  -1456      6    516       C  
ATOM   5172  CG  PRO C1192       0.420  39.085  94.439  1.00 75.23           C  
ANISOU 5172  CG  PRO C1192     7651   7287  13645  -1470     95    432       C  
ATOM   5173  CD  PRO C1192       1.641  39.855  94.060  1.00 74.62           C  
ANISOU 5173  CD  PRO C1192     7678   7238  13437  -1431    201    415       C  
ATOM   5174  N   TYR C1193       0.561  40.335  97.647  1.00 73.20           N  
ANISOU 5174  N   TYR C1193     7105   7176  13533  -1322    232    665       N  
ATOM   5175  CA  TYR C1193       0.371  40.264  99.109  1.00 73.04           C  
ANISOU 5175  CA  TYR C1193     6977   7181  13593  -1260    286    758       C  
ATOM   5176  C   TYR C1193       1.266  41.239  99.919  1.00 72.68           C  
ANISOU 5176  C   TYR C1193     6931   7207  13477  -1185    336    782       C  
ATOM   5177  O   TYR C1193       1.181  41.278 101.159  1.00 72.61           O  
ANISOU 5177  O   TYR C1193     6869   7226  13493  -1118    373    851       O  
ATOM   5178  CB  TYR C1193       0.616  38.832  99.599  1.00 73.15           C  
ANISOU 5178  CB  TYR C1193     6953   7125  13716  -1252    353    772       C  
ATOM   5179  CG  TYR C1193      -0.297  37.790  99.005  1.00 73.91           C  
ANISOU 5179  CG  TYR C1193     7023   7132  13928  -1322    308    745       C  
ATOM   5180  CD1 TYR C1193      -0.072  37.268  97.723  1.00 74.45           C  
ANISOU 5180  CD1 TYR C1193     7181   7142  13965  -1393    261    634       C  
ATOM   5181  CD2 TYR C1193      -1.371  37.307  99.732  1.00 74.49           C  
ANISOU 5181  CD2 TYR C1193     6985   7164  14154  -1313    319    828       C  
ATOM   5182  CE1 TYR C1193      -0.913  36.315  97.183  1.00 75.32           C  
ANISOU 5182  CE1 TYR C1193     7266   7159  14191  -1460    195    588       C  
ATOM   5183  CE2 TYR C1193      -2.215  36.347  99.205  1.00 75.34           C  
ANISOU 5183  CE2 TYR C1193     7042   7169  14414  -1382    269    796       C  
ATOM   5184  CZ  TYR C1193      -1.978  35.859  97.939  1.00 76.07           C  
ANISOU 5184  CZ  TYR C1193     7222   7211  14472  -1457    192    668       C  
ATOM   5185  OH  TYR C1193      -2.827  34.903  97.439  1.00 78.25           O  
ANISOU 5185  OH  TYR C1193     7447   7375  14911  -1527    120    619       O  
ATOM   5186  N   ALA C1194       2.112  42.020  99.240  1.00 72.32           N  
ANISOU 5186  N   ALA C1194     6950   7179  13347  -1190    340    724       N  
ATOM   5187  CA  ALA C1194       3.077  42.877  99.939  1.00 72.30           C  
ANISOU 5187  CA  ALA C1194     6931   7220  13318  -1127    376    725       C  
ATOM   5188  C   ALA C1194       2.469  43.810 101.014  1.00 72.61           C  
ANISOU 5188  C   ALA C1194     6919   7327  13343  -1073    354    785       C  
ATOM   5189  O   ALA C1194       3.182  44.631 101.595  1.00 72.22           O  
ANISOU 5189  O   ALA C1194     6860   7310  13270  -1022    361    770       O  
ATOM   5190  CB  ALA C1194       3.951  43.650  98.953  1.00 71.46           C  
ANISOU 5190  CB  ALA C1194     6888   7100  13162  -1144    403    663       C  
ATOM   5191  N   TRP C1195       1.169  43.668 101.298  1.00 73.79           N  
ANISOU 5191  N   TRP C1195     7032   7481  13525  -1081    334    847       N  
ATOM   5192  CA  TRP C1195       0.538  44.449 102.391  1.00 74.57           C  
ANISOU 5192  CA  TRP C1195     7092   7625  13616  -1020    347    910       C  
ATOM   5193  C   TRP C1195       1.070  44.060 103.735  1.00 75.20           C  
ANISOU 5193  C   TRP C1195     7173   7719  13679   -933    393    942       C  
ATOM   5194  O   TRP C1195       1.370  44.936 104.566  1.00 75.24           O  
ANISOU 5194  O   TRP C1195     7194   7771  13624   -867    393    938       O  
ATOM   5195  CB  TRP C1195      -1.000  44.415 102.374  1.00 74.65           C  
ANISOU 5195  CB  TRP C1195     7048   7615  13703  -1045    337    981       C  
ATOM   5196  CG  TRP C1195      -1.618  43.054 102.536  1.00 75.35           C  
ANISOU 5196  CG  TRP C1195     7092   7636  13900  -1062    362   1026       C  
ATOM   5197  CD1 TRP C1195      -1.734  42.064 101.576  1.00 76.28           C  
ANISOU 5197  CD1 TRP C1195     7209   7692  14081  -1136    318    984       C  
ATOM   5198  CD2 TRP C1195      -2.272  42.504 103.728  1.00 76.27           C  
ANISOU 5198  CD2 TRP C1195     7162   7723  14094   -999    453   1124       C  
ATOM   5199  NE1 TRP C1195      -2.384  40.967 102.081  1.00 77.00           N  
ANISOU 5199  NE1 TRP C1195     7236   7714  14306  -1131    366   1044       N  
ATOM   5200  CE2 TRP C1195      -2.732  41.171 103.369  1.00 76.52           C  
ANISOU 5200  CE2 TRP C1195     7144   7667  14262  -1047    460   1139       C  
ATOM   5201  CE3 TRP C1195      -2.517  42.973 105.025  1.00 76.82           C  
ANISOU 5201  CE3 TRP C1195     7240   7819  14130   -903    540   1199       C  
ATOM   5202  CZ2 TRP C1195      -3.382  40.353 104.271  1.00 76.61           C  
ANISOU 5202  CZ2 TRP C1195     7099   7614  14393  -1000    564   1239       C  
ATOM   5203  CZ3 TRP C1195      -3.181  42.128 105.923  1.00 76.30           C  
ANISOU 5203  CZ3 TRP C1195     7143   7693  14153   -849    650   1303       C  
ATOM   5204  CH2 TRP C1195      -3.595  40.852 105.548  1.00 76.35           C  
ANISOU 5204  CH2 TRP C1195     7085   7610  14312   -897    668   1328       C  
ATOM   5205  N   VAL C1196       1.209  42.746 103.941  1.00 75.69           N  
ANISOU 5205  N   VAL C1196     7230   7737  13793   -927    425    969       N  
ATOM   5206  CA  VAL C1196       1.820  42.174 105.159  1.00 75.48           C  
ANISOU 5206  CA  VAL C1196     7220   7716  13743   -834    461   1010       C  
ATOM   5207  C   VAL C1196       3.129  42.878 105.540  1.00 75.02           C  
ANISOU 5207  C   VAL C1196     7191   7699  13615   -784    411    946       C  
ATOM   5208  O   VAL C1196       3.377  43.120 106.713  1.00 75.55           O  
ANISOU 5208  O   VAL C1196     7291   7801  13615   -689    399    971       O  
ATOM   5209  CB  VAL C1196       2.054  40.648 104.995  1.00 75.79           C  
ANISOU 5209  CB  VAL C1196     7241   7686  13868   -850    500   1033       C  
ATOM   5210  CG1 VAL C1196       2.982  40.083 106.067  1.00 75.27           C  
ANISOU 5210  CG1 VAL C1196     7200   7625  13774   -752    516   1070       C  
ATOM   5211  CG2 VAL C1196       0.710  39.915 104.967  1.00 76.68           C  
ANISOU 5211  CG2 VAL C1196     7308   7742  14084   -879    554   1108       C  
ATOM   5212  N   PHE C1197       3.964  43.223 104.568  1.00 74.23           N  
ANISOU 5212  N   PHE C1197     7083   7584  13538   -840    381    861       N  
ATOM   5213  CA  PHE C1197       5.210  43.887 104.934  1.00 74.89           C  
ANISOU 5213  CA  PHE C1197     7163   7681  13611   -795    333    799       C  
ATOM   5214  C   PHE C1197       5.010  45.283 105.557  1.00 75.20           C  
ANISOU 5214  C   PHE C1197     7212   7776  13584   -752    293    777       C  
ATOM   5215  O   PHE C1197       5.510  45.550 106.655  1.00 75.97           O  
ANISOU 5215  O   PHE C1197     7328   7899  13636   -667    240    765       O  
ATOM   5216  CB  PHE C1197       6.201  43.948 103.763  1.00 74.99           C  
ANISOU 5216  CB  PHE C1197     7157   7639  13696   -857    347    724       C  
ATOM   5217  CG  PHE C1197       7.512  44.586 104.128  1.00 75.27           C  
ANISOU 5217  CG  PHE C1197     7155   7661  13784   -813    302    661       C  
ATOM   5218  CD1 PHE C1197       8.355  43.985 105.064  1.00 75.30           C  
ANISOU 5218  CD1 PHE C1197     7133   7651  13826   -742    249    668       C  
ATOM   5219  CD2 PHE C1197       7.899  45.804 103.553  1.00 75.28           C  
ANISOU 5219  CD2 PHE C1197     7136   7652  13815   -839    305    600       C  
ATOM   5220  CE1 PHE C1197       9.554  44.582 105.417  1.00 76.15           C  
ANISOU 5220  CE1 PHE C1197     7187   7732  14015   -703    177    602       C  
ATOM   5221  CE2 PHE C1197       9.111  46.404 103.902  1.00 75.72           C  
ANISOU 5221  CE2 PHE C1197     7131   7671  13967   -802    260    535       C  
ATOM   5222  CZ  PHE C1197       9.935  45.793 104.839  1.00 76.15           C  
ANISOU 5222  CZ  PHE C1197     7150   7710  14073   -737    183    531       C  
ATOM   5223  N   PHE C1198       4.270  46.153 104.863  1.00 74.43           N  
ANISOU 5223  N   PHE C1198     7110   7693  13478   -805    310    770       N  
ATOM   5224  CA  PHE C1198       4.078  47.548 105.276  1.00 73.38           C  
ANISOU 5224  CA  PHE C1198     6978   7597  13308   -776    289    743       C  
ATOM   5225  C   PHE C1198       3.066  47.835 106.413  1.00 74.25           C  
ANISOU 5225  C   PHE C1198     7122   7745  13344   -709    311    802       C  
ATOM   5226  O   PHE C1198       3.406  48.580 107.345  1.00 74.10           O  
ANISOU 5226  O   PHE C1198     7134   7753  13270   -639    277    761       O  
ATOM   5227  CB  PHE C1198       3.771  48.406 104.052  1.00 71.67           C  
ANISOU 5227  CB  PHE C1198     6742   7369  13121   -850    308    723       C  
ATOM   5228  CG  PHE C1198       4.920  48.520 103.100  1.00 70.76           C  
ANISOU 5228  CG  PHE C1198     6615   7207  13065   -889    317    658       C  
ATOM   5229  CD1 PHE C1198       5.136  47.550 102.126  1.00 70.42           C  
ANISOU 5229  CD1 PHE C1198     6594   7120  13043   -941    350    660       C  
ATOM   5230  CD2 PHE C1198       5.795  49.607 103.172  1.00 70.47           C  
ANISOU 5230  CD2 PHE C1198     6543   7152  13079   -869    307    591       C  
ATOM   5231  CE1 PHE C1198       6.192  47.657 101.236  1.00 69.98           C  
ANISOU 5231  CE1 PHE C1198     6542   7005  13045   -968    395    608       C  
ATOM   5232  CE2 PHE C1198       6.865  49.710 102.293  1.00 70.27           C  
ANISOU 5232  CE2 PHE C1198     6497   7060  13143   -898    348    544       C  
ATOM   5233  CZ  PHE C1198       7.058  48.731 101.321  1.00 70.02           C  
ANISOU 5233  CZ  PHE C1198     6502   6985  13116   -944    403    558       C  
ATOM   5234  N   ILE C1199       1.850  47.269 106.337  1.00 74.85           N  
ANISOU 5234  N   ILE C1199     7193   7812  13435   -728    370    890       N  
ATOM   5235  CA  ILE C1199       0.769  47.574 107.318  1.00 76.13           C  
ANISOU 5235  CA  ILE C1199     7381   7986  13558   -665    435    962       C  
ATOM   5236  C   ILE C1199       1.218  47.505 108.799  1.00 78.20           C  
ANISOU 5236  C   ILE C1199     7732   8274  13706   -543    437    965       C  
ATOM   5237  O   ILE C1199       1.123  48.513 109.512  1.00 79.54           O  
ANISOU 5237  O   ILE C1199     7951   8468  13803   -486    438    933       O  
ATOM   5238  CB  ILE C1199      -0.506  46.698 107.167  1.00 76.23           C  
ANISOU 5238  CB  ILE C1199     7355   7955  13652   -692    511   1070       C  
ATOM   5239  CG1 ILE C1199      -1.121  46.755 105.750  1.00 75.99           C  
ANISOU 5239  CG1 ILE C1199     7253   7897  13723   -804    475   1066       C  
ATOM   5240  CG2 ILE C1199      -1.511  47.065 108.244  1.00 76.95           C  
ANISOU 5240  CG2 ILE C1199     7474   8039  13723   -614    612   1150       C  
ATOM   5241  CD1 ILE C1199      -2.278  47.709 105.537  1.00 75.13           C  
ANISOU 5241  CD1 ILE C1199     7095   7780  13671   -825    494   1108       C  
ATOM   5242  N   PRO C1200       1.715  46.335 109.277  1.00 78.85           N  
ANISOU 5242  N   PRO C1200     7848   8346  13764   -496    433   1000       N  
ATOM   5243  CA  PRO C1200       2.045  46.309 110.699  1.00 79.94           C  
ANISOU 5243  CA  PRO C1200     8098   8511  13765   -364    423   1013       C  
ATOM   5244  C   PRO C1200       3.362  47.027 110.968  1.00 81.06           C  
ANISOU 5244  C   PRO C1200     8261   8682  13855   -333    278    888       C  
ATOM   5245  O   PRO C1200       3.659  47.348 112.116  1.00 82.98           O  
ANISOU 5245  O   PRO C1200     8611   8954  13966   -224    228    863       O  
ATOM   5246  CB  PRO C1200       2.170  44.818 111.016  1.00 80.22           C  
ANISOU 5246  CB  PRO C1200     8152   8519  13811   -324    461   1103       C  
ATOM   5247  CG  PRO C1200       2.041  44.090 109.706  1.00 79.53           C  
ANISOU 5247  CG  PRO C1200     7952   8386  13881   -448    478   1108       C  
ATOM   5248  CD  PRO C1200       2.192  45.115 108.614  1.00 78.69           C  
ANISOU 5248  CD  PRO C1200     7783   8291  13824   -546    421   1012       C  
ATOM   5249  N   PHE C1201       4.144  47.278 109.916  1.00 80.83           N  
ANISOU 5249  N   PHE C1201     8138   8637  13938   -424    213    807       N  
ATOM   5250  CA  PHE C1201       5.316  48.155 110.019  1.00 80.71           C  
ANISOU 5250  CA  PHE C1201     8102   8623  13940   -411     90    682       C  
ATOM   5251  C   PHE C1201       4.896  49.572 110.329  1.00 80.28           C  
ANISOU 5251  C   PHE C1201     8072   8588  13842   -397     89    623       C  
ATOM   5252  O   PHE C1201       5.523  50.225 111.154  1.00 81.23           O  
ANISOU 5252  O   PHE C1201     8239   8718  13906   -328    -12    534       O  
ATOM   5253  CB  PHE C1201       6.119  48.170 108.726  1.00 80.51           C  
ANISOU 5253  CB  PHE C1201     7967   8552  14070   -511     74    627       C  
ATOM   5254  CG  PHE C1201       7.018  49.360 108.590  1.00 80.88           C  
ANISOU 5254  CG  PHE C1201     7960   8577  14192   -521     -4    508       C  
ATOM   5255  CD1 PHE C1201       8.254  49.389 109.234  1.00 82.04           C  
ANISOU 5255  CD1 PHE C1201     8089   8701  14382   -464   -137    428       C  
ATOM   5256  CD2 PHE C1201       6.635  50.451 107.817  1.00 80.37           C  
ANISOU 5256  CD2 PHE C1201     7854   8502  14180   -585     51    479       C  
ATOM   5257  CE1 PHE C1201       9.092  50.483 109.105  1.00 82.66           C  
ANISOU 5257  CE1 PHE C1201     8093   8737  14577   -477   -210    312       C  
ATOM   5258  CE2 PHE C1201       7.471  51.551 107.687  1.00 80.97           C  
ANISOU 5258  CE2 PHE C1201     7869   8540  14358   -593     -1    374       C  
ATOM   5259  CZ  PHE C1201       8.700  51.568 108.333  1.00 81.81           C  
ANISOU 5259  CZ  PHE C1201     7942   8613  14530   -542   -129    285       C  
ATOM   5260  N   ILE C1202       3.859  50.051 109.638  1.00 79.03           N  
ANISOU 5260  N   ILE C1202     7879   8428  13723   -463    190    666       N  
ATOM   5261  CA  ILE C1202       3.282  51.370 109.940  1.00 78.72           C  
ANISOU 5261  CA  ILE C1202     7857   8397  13656   -448    219    630       C  
ATOM   5262  C   ILE C1202       2.814  51.325 111.392  1.00 79.78           C  
ANISOU 5262  C   ILE C1202     8127   8555  13631   -327    245    657       C  
ATOM   5263  O   ILE C1202       3.075  52.261 112.168  1.00 79.60           O  
ANISOU 5263  O   ILE C1202     8171   8540  13534   -265    195    567       O  
ATOM   5264  CB  ILE C1202       2.101  51.742 108.998  1.00 77.57           C  
ANISOU 5264  CB  ILE C1202     7648   8238  13588   -529    324    702       C  
ATOM   5265  CG1 ILE C1202       2.506  51.575 107.528  1.00 77.30           C  
ANISOU 5265  CG1 ILE C1202     7525   8181  13666   -633    304    693       C  
ATOM   5266  CG2 ILE C1202       1.652  53.176 109.225  1.00 77.28           C  
ANISOU 5266  CG2 ILE C1202     7611   8198  13555   -516    355    662       C  
ATOM   5267  CD1 ILE C1202       1.367  51.692 106.528  1.00 77.01           C  
ANISOU 5267  CD1 ILE C1202     7440   8132  13689   -707    367    771       C  
ATOM   5268  N   PHE C1203       2.155  50.205 111.735  1.00 79.86           N  
ANISOU 5268  N   PHE C1203     8185   8566  13594   -291    330    778       N  
ATOM   5269  CA  PHE C1203       1.538  49.983 113.042  1.00 80.57           C  
ANISOU 5269  CA  PHE C1203     8421   8663  13530   -167    411    844       C  
ATOM   5270  C   PHE C1203       2.509  50.248 114.174  1.00 80.87           C  
ANISOU 5270  C   PHE C1203     8592   8730  13403    -52    280    749       C  
ATOM   5271  O   PHE C1203       2.318  51.208 114.930  1.00 81.72           O  
ANISOU 5271  O   PHE C1203     8802   8845  13403     15    283    685       O  
ATOM   5272  CB  PHE C1203       0.990  48.551 113.170  1.00 81.36           C  
ANISOU 5272  CB  PHE C1203     8534   8741  13638   -143    513    989       C  
ATOM   5273  CG  PHE C1203      -0.511  48.459 113.145  1.00 81.61           C  
ANISOU 5273  CG  PHE C1203     8544   8729  13736   -152    701   1113       C  
ATOM   5274  CD1 PHE C1203      -1.193  48.269 111.942  1.00 80.28           C  
ANISOU 5274  CD1 PHE C1203     8222   8525  13756   -276    737   1156       C  
ATOM   5275  CD2 PHE C1203      -1.248  48.539 114.336  1.00 82.44           C  
ANISOU 5275  CD2 PHE C1203     8786   8815  13722    -29    844   1188       C  
ATOM   5276  CE1 PHE C1203      -2.581  48.166 111.928  1.00 80.71           C  
ANISOU 5276  CE1 PHE C1203     8229   8521  13915   -285    891   1269       C  
ATOM   5277  CE2 PHE C1203      -2.636  48.445 114.321  1.00 82.56           C  
ANISOU 5277  CE2 PHE C1203     8757   8764  13847    -35   1037   1312       C  
ATOM   5278  CZ  PHE C1203      -3.306  48.259 113.118  1.00 81.55           C  
ANISOU 5278  CZ  PHE C1203     8445   8596  13944   -167   1051   1352       C  
ATOM   5279  N   VAL C1204       3.551  49.422 114.266  1.00 79.86           N  
ANISOU 5279  N   VAL C1204     8464   8612  13267    -29    156    732       N  
ATOM   5280  CA  VAL C1204       4.431  49.432 115.443  1.00 81.27           C  
ANISOU 5280  CA  VAL C1204     8784   8816  13281     99      4    663       C  
ATOM   5281  C   VAL C1204       5.261  50.718 115.555  1.00 81.64           C  
ANISOU 5281  C   VAL C1204     8814   8862  13345     92   -163    480       C  
ATOM   5282  O   VAL C1204       5.662  51.108 116.655  1.00 82.55           O  
ANISOU 5282  O   VAL C1204     9077   8994  13295    206   -283    398       O  
ATOM   5283  CB  VAL C1204       5.306  48.157 115.557  1.00 81.14           C  
ANISOU 5283  CB  VAL C1204     8760   8798  13272    134    -91    710       C  
ATOM   5284  CG1 VAL C1204       6.014  48.121 116.897  1.00 82.47           C  
ANISOU 5284  CG1 VAL C1204     9104   8994  13238    291   -253    665       C  
ATOM   5285  CG2 VAL C1204       4.459  46.897 115.412  1.00 80.72           C  
ANISOU 5285  CG2 VAL C1204     8708   8727  13234    135     88    887       C  
ATOM   5286  N   VAL C1205       5.478  51.387 114.423  1.00 80.81           N  
ANISOU 5286  N   VAL C1205     8537   8728  13437    -36   -165    416       N  
ATOM   5287  CA  VAL C1205       6.138  52.688 114.425  1.00 81.98           C  
ANISOU 5287  CA  VAL C1205     8642   8854  13653    -54   -283    251       C  
ATOM   5288  C   VAL C1205       5.207  53.809 114.931  1.00 83.64           C  
ANISOU 5288  C   VAL C1205     8943   9068  13769    -21   -190    218       C  
ATOM   5289  O   VAL C1205       5.583  54.562 115.839  1.00 86.34           O  
ANISOU 5289  O   VAL C1205     9389   9407  14011     57   -302     91       O  
ATOM   5290  CB  VAL C1205       6.776  53.039 113.070  1.00 80.32           C  
ANISOU 5290  CB  VAL C1205     8228   8597  13694   -186   -296    204       C  
ATOM   5291  CG1 VAL C1205       7.442  54.406 113.131  1.00 80.51           C  
ANISOU 5291  CG1 VAL C1205     8195   8577  13819   -199   -400     39       C  
ATOM   5292  CG2 VAL C1205       7.802  51.983 112.693  1.00 80.71           C  
ANISOU 5292  CG2 VAL C1205     8199   8624  13841   -205   -382    220       C  
ATOM   5293  N   THR C1206       4.001  53.921 114.377  1.00 82.99           N  
ANISOU 5293  N   THR C1206     8825   8982  13726    -76      6    325       N  
ATOM   5294  CA  THR C1206       3.013  54.850 114.936  1.00 83.98           C  
ANISOU 5294  CA  THR C1206     9040   9098  13770    -33    126    321       C  
ATOM   5295  C   THR C1206       2.652  54.469 116.386  1.00 86.22           C  
ANISOU 5295  C   THR C1206     9558   9403  13798    122    160    351       C  
ATOM   5296  O   THR C1206       2.496  55.341 117.255  1.00 87.64           O  
ANISOU 5296  O   THR C1206     9876   9573  13851    202    162    261       O  
ATOM   5297  CB  THR C1206       1.730  54.896 114.095  1.00 83.14           C  
ANISOU 5297  CB  THR C1206     8838   8973  13778   -113    323    454       C  
ATOM   5298  OG1 THR C1206       2.075  54.840 112.705  1.00 81.96           O  
ANISOU 5298  OG1 THR C1206     8509   8813  13818   -240    290    461       O  
ATOM   5299  CG2 THR C1206       0.918  56.184 114.398  1.00 83.25           C  
ANISOU 5299  CG2 THR C1206     8883   8956  13795    -96    434    421       C  
ATOM   5300  N   PHE C1207       2.523  53.168 116.640  1.00 85.97           N  
ANISOU 5300  N   PHE C1207     9584   9391  13688    171    198    477       N  
ATOM   5301  CA  PHE C1207       2.297  52.677 117.991  1.00 87.87           C  
ANISOU 5301  CA  PHE C1207    10065   9648  13674    333    235    526       C  
ATOM   5302  C   PHE C1207       3.413  53.176 118.914  1.00 89.96           C  
ANISOU 5302  C   PHE C1207    10470   9934  13776    430     -3    354       C  
ATOM   5303  O   PHE C1207       3.134  53.725 119.976  1.00 91.94           O  
ANISOU 5303  O   PHE C1207    10934  10184  13814    550     18    300       O  
ATOM   5304  CB  PHE C1207       2.231  51.155 117.979  1.00 87.36           C  
ANISOU 5304  CB  PHE C1207    10005   9593  13597    360    287    684       C  
ATOM   5305  CG  PHE C1207       1.508  50.556 119.143  1.00 88.75           C  
ANISOU 5305  CG  PHE C1207    10404   9761  13555    516    444    810       C  
ATOM   5306  CD1 PHE C1207       0.276  49.942 118.956  1.00 88.34           C  
ANISOU 5306  CD1 PHE C1207    10317   9663  13584    505    703    990       C  
ATOM   5307  CD2 PHE C1207       2.071  50.566 120.417  1.00 90.54           C  
ANISOU 5307  CD2 PHE C1207    10880  10017  13506    681    333    756       C  
ATOM   5308  CE1 PHE C1207      -0.397  49.366 120.028  1.00 90.19           C  
ANISOU 5308  CE1 PHE C1207    10756   9871  13642    658    888   1124       C  
ATOM   5309  CE2 PHE C1207       1.404  49.990 121.487  1.00 92.58           C  
ANISOU 5309  CE2 PHE C1207    11373  10262  13543    842    506    889       C  
ATOM   5310  CZ  PHE C1207       0.168  49.387 121.294  1.00 91.96           C  
ANISOU 5310  CZ  PHE C1207    11251  10127  13562    831    802   1081       C  
ATOM   5311  N   VAL C1208       4.671  53.013 118.501  1.00 90.02           N  
ANISOU 5311  N   VAL C1208    10360   9950  13894    381   -230    260       N  
ATOM   5312  CA  VAL C1208       5.801  53.506 119.307  1.00 92.13           C  
ANISOU 5312  CA  VAL C1208    10724  10222  14061    462   -499     81       C  
ATOM   5313  C   VAL C1208       5.911  55.033 119.242  1.00 92.10           C  
ANISOU 5313  C   VAL C1208    10679  10180  14134    418   -553   -100       C  
ATOM   5314  O   VAL C1208       6.325  55.658 120.217  1.00 93.57           O  
ANISOU 5314  O   VAL C1208    11025  10363  14165    516   -709   -249       O  
ATOM   5315  CB  VAL C1208       7.142  52.784 118.977  1.00 92.44           C  
ANISOU 5315  CB  VAL C1208    10636  10258  14229    435   -727     48       C  
ATOM   5316  CG1 VAL C1208       8.351  53.545 119.522  1.00 94.49           C  
ANISOU 5316  CG1 VAL C1208    10907  10494  14500    477  -1030   -166       C  
ATOM   5317  CG2 VAL C1208       7.129  51.361 119.520  1.00 92.37           C  
ANISOU 5317  CG2 VAL C1208    10745  10283  14068    536   -714    201       C  
HETATM 5318  N   MSE C1209       5.524  55.627 118.110  1.00 90.44           N  
ANISOU 5318  N   MSE C1209    10267   9938  14157    278   -426    -87       N  
HETATM 5319  CA  MSE C1209       5.404  57.095 118.010  1.00 91.69           C  
ANISOU 5319  CA  MSE C1209    10384  10051  14404    237   -416   -227       C  
HETATM 5320  C   MSE C1209       4.498  57.585 119.124  1.00 93.24           C  
ANISOU 5320  C   MSE C1209    10822  10251  14355    355   -301   -239       C  
HETATM 5321  O   MSE C1209       4.776  58.614 119.752  1.00 94.19           O  
ANISOU 5321  O   MSE C1209    11031  10339  14418    401   -397   -414       O  
HETATM 5322  CB  MSE C1209       4.872  57.590 116.653  1.00 89.89           C  
ANISOU 5322  CB  MSE C1209     9936   9791  14428     89   -252   -163       C  
HETATM 5323  CG  MSE C1209       5.951  57.816 115.596  1.00 89.78           C  
ANISOU 5323  CG  MSE C1209     9695   9736  14680    -23   -371   -236       C  
HETATM 5324 SE   MSE C1209       7.014  59.450 115.925  1.00 94.11          SE  
ANISOU 5324 SE   MSE C1209    10182  10198  15379    -27   -567   -509      SE  
HETATM 5325  CE  MSE C1209       8.155  58.832 117.417  1.00 93.41           C  
ANISOU 5325  CE  MSE C1209    10276  10133  15084    121   -893   -647       C  
ATOM   5326  N   ILE C1210       3.419  56.837 119.375  1.00 93.24           N  
ANISOU 5326  N   ILE C1210    10929  10274  14224    407    -83    -56       N  
ATOM   5327  CA  ILE C1210       2.517  57.095 120.500  1.00 95.49           C  
ANISOU 5327  CA  ILE C1210    11472  10550  14262    541     74    -33       C  
ATOM   5328  C   ILE C1210       3.262  57.008 121.829  1.00 98.36           C  
ANISOU 5328  C   ILE C1210    12106  10938  14329    703   -126   -155       C  
ATOM   5329  O   ILE C1210       3.194  57.945 122.635  1.00100.61           O  
ANISOU 5329  O   ILE C1210    12568  11196  14465    783   -150   -298       O  
ATOM   5330  CB  ILE C1210       1.314  56.121 120.514  1.00 95.17           C  
ANISOU 5330  CB  ILE C1210    11474  10509  14175    573    350    207       C  
ATOM   5331  CG1 ILE C1210       0.359  56.435 119.360  1.00 93.14           C  
ANISOU 5331  CG1 ILE C1210    10987  10214  14189    433    545    310       C  
ATOM   5332  CG2 ILE C1210       0.583  56.182 121.852  1.00 97.16           C  
ANISOU 5332  CG2 ILE C1210    12036  10743  14138    748    513    242       C  
ATOM   5333  CD1 ILE C1210      -0.443  55.246 118.879  1.00 92.09           C  
ANISOU 5333  CD1 ILE C1210    10772  10078  14141    402    715    528       C  
ATOM   5334  N   ASN C1211       3.968  55.891 122.041  1.00 98.42           N  
ANISOU 5334  N   ASN C1211    12150  10989  14255    754   -276   -101       N  
ATOM   5335  CA  ASN C1211       4.801  55.687 123.237  1.00100.87           C  
ANISOU 5335  CA  ASN C1211    12707  11328  14289    913   -520   -207       C  
ATOM   5336  C   ASN C1211       5.919  56.712 123.433  1.00101.62           C  
ANISOU 5336  C   ASN C1211    12774  11399  14439    898   -837   -476       C  
ATOM   5337  O   ASN C1211       6.067  57.240 124.525  1.00103.97           O  
ANISOU 5337  O   ASN C1211    13328  11692  14484   1029   -956   -616       O  
ATOM   5338  CB  ASN C1211       5.406  54.283 123.240  1.00101.32           C  
ANISOU 5338  CB  ASN C1211    12751  11428  14318    950   -630    -84       C  
ATOM   5339  CG  ASN C1211       4.814  53.394 124.312  1.00103.75           C  
ANISOU 5339  CG  ASN C1211    13360  11762  14297   1133   -495     73       C  
ATOM   5340  OD1 ASN C1211       4.959  53.663 125.512  1.00106.88           O  
ANISOU 5340  OD1 ASN C1211    14062  12170  14377   1300   -593    -10       O  
ATOM   5341  ND2 ASN C1211       4.151  52.316 123.891  1.00102.60           N  
ANISOU 5341  ND2 ASN C1211    13142  11618  14223   1110   -269    300       N  
ATOM   5342  N   LEU C1212       6.690  56.993 122.378  1.00100.12           N  
ANISOU 5342  N   LEU C1212    12278  11180  14584    745   -964   -548       N  
ATOM   5343  CA  LEU C1212       7.819  57.931 122.456  1.00100.84           C  
ANISOU 5343  CA  LEU C1212    12284  11221  14809    716  -1260   -798       C  
ATOM   5344  C   LEU C1212       7.386  59.304 122.972  1.00101.49           C  
ANISOU 5344  C   LEU C1212    12488  11256  14819    743  -1221   -967       C  
ATOM   5345  O   LEU C1212       8.106  59.891 123.777  1.00103.93           O  
ANISOU 5345  O   LEU C1212    12919  11537  15033    819  -1485  -1181       O  
ATOM   5346  CB  LEU C1212       8.569  58.048 121.107  1.00 99.05           C  
ANISOU 5346  CB  LEU C1212    11694  10948  14995    541  -1315   -815       C  
ATOM   5347  CG  LEU C1212       9.896  58.845 121.015  1.00100.16           C  
ANISOU 5347  CG  LEU C1212    11673  11008  15375    495  -1616  -1049       C  
ATOM   5348  CD1 LEU C1212      10.840  58.278 119.949  1.00 98.60           C  
ANISOU 5348  CD1 LEU C1212    11181  10774  15508    383  -1688  -1001       C  
ATOM   5349  CD2 LEU C1212       9.686  60.346 120.796  1.00 99.79           C  
ANISOU 5349  CD2 LEU C1212    11549  10885  15482    428  -1560  -1206       C  
ATOM   5350  N   VAL C1213       6.225  59.790 122.510  1.00 99.16           N  
ANISOU 5350  N   VAL C1213    12152  10943  14579    683   -906   -874       N  
ATOM   5351  CA  VAL C1213       5.643  61.079 122.938  1.00 99.67           C  
ANISOU 5351  CA  VAL C1213    12323  10952  14596    705   -805  -1005       C  
ATOM   5352  C   VAL C1213       5.034  60.949 124.338  1.00101.97           C  
ANISOU 5352  C   VAL C1213    13009  11266  14469    896   -737  -1009       C  
ATOM   5353  O   VAL C1213       5.475  61.603 125.292  1.00104.02           O  
ANISOU 5353  O   VAL C1213    13477  11499  14545    995   -924  -1221       O  
ATOM   5354  CB  VAL C1213       4.548  61.586 121.951  1.00 97.47           C  
ANISOU 5354  CB  VAL C1213    11860  10640  14534    584   -480   -876       C  
ATOM   5355  CG1 VAL C1213       3.855  62.837 122.479  1.00 98.39           C  
ANISOU 5355  CG1 VAL C1213    12101  10690  14591    622   -342   -990       C  
ATOM   5356  CG2 VAL C1213       5.114  61.847 120.557  1.00 95.15           C  
ANISOU 5356  CG2 VAL C1213    11213  10315  14625    410   -527   -877       C  
TER    5357      VAL C1213                                                      
HETATM 5358  N   MSE D1001     -27.354 110.470 132.807  1.00131.23           N  
ANISOU 5358  N   MSE D1001    14105  16190  19567   2239   1391  -3147       N  
HETATM 5359  CA  MSE D1001     -26.947 109.571 131.681  1.00129.20           C  
ANISOU 5359  CA  MSE D1001    13951  15857  19284   2176   1370  -2969       C  
HETATM 5360  C   MSE D1001     -25.640 108.876 131.984  1.00129.72           C  
ANISOU 5360  C   MSE D1001    14015  16091  19182   2239   1333  -3046       C  
HETATM 5361  O   MSE D1001     -25.268 107.929 131.286  1.00128.94           O  
ANISOU 5361  O   MSE D1001    14003  15976  19014   2218   1317  -2902       O  
HETATM 5362  CB  MSE D1001     -26.826 110.364 130.378  1.00129.00           C  
ANISOU 5362  CB  MSE D1001    13931  15609  19476   2035   1373  -2940       C  
HETATM 5363  CG  MSE D1001     -26.916 109.458 129.148  1.00128.77           C  
ANISOU 5363  CG  MSE D1001    14026  15474  19426   1983   1354  -2714       C  
HETATM 5364 SE   MSE D1001     -26.242 110.323 127.502  1.00130.72          SE  
ANISOU 5364 SE   MSE D1001    14297  15489  19883   1854   1368  -2688      SE  
HETATM 5365  CE  MSE D1001     -24.498 110.999 128.138  1.00127.64           C  
ANISOU 5365  CE  MSE D1001    13770  15202  19524   1854   1382  -2976       C  
ATOM   5366  N   TYR D1002     -24.941 109.333 133.026  1.00131.33           N  
ANISOU 5366  N   TYR D1002    14116  16462  19321   2326   1314  -3283       N  
ATOM   5367  CA  TYR D1002     -23.658 108.756 133.443  1.00131.36           C  
ANISOU 5367  CA  TYR D1002    14099  16649  19163   2408   1268  -3396       C  
ATOM   5368  C   TYR D1002     -23.758 107.236 133.645  1.00131.71           C  
ANISOU 5368  C   TYR D1002    14257  16815  18971   2509   1275  -3200       C  
ATOM   5369  O   TYR D1002     -22.891 106.487 133.194  1.00131.47           O  
ANISOU 5369  O   TYR D1002    14272  16818  18862   2501   1248  -3152       O  
ATOM   5370  CB  TYR D1002     -23.155 109.435 134.726  1.00134.19           C  
ANISOU 5370  CB  TYR D1002    14324  17197  19464   2529   1235  -3693       C  
ATOM   5371  CG  TYR D1002     -21.647 109.634 134.813  1.00135.95           C  
ANISOU 5371  CG  TYR D1002    14452  17513  19689   2541   1174  -3923       C  
ATOM   5372  CD1 TYR D1002     -21.107 110.891 135.115  1.00136.94           C  
ANISOU 5372  CD1 TYR D1002    14414  17620  19995   2513   1150  -4221       C  
ATOM   5373  CD2 TYR D1002     -20.759 108.567 134.601  1.00136.49           C  
ANISOU 5373  CD2 TYR D1002    14582  17679  19599   2581   1141  -3856       C  
ATOM   5374  CE1 TYR D1002     -19.734 111.082 135.203  1.00137.61           C  
ANISOU 5374  CE1 TYR D1002    14392  17779  20117   2524   1094  -4453       C  
ATOM   5375  CE2 TYR D1002     -19.384 108.747 134.684  1.00137.09           C  
ANISOU 5375  CE2 TYR D1002    14561  17835  19690   2593   1083  -4075       C  
ATOM   5376  CZ  TYR D1002     -18.876 110.004 134.987  1.00138.72           C  
ANISOU 5376  CZ  TYR D1002    14597  18019  20090   2565   1059  -4378       C  
ATOM   5377  OH  TYR D1002     -17.511 110.177 135.072  1.00139.74           O  
ANISOU 5377  OH  TYR D1002    14611  18217  20264   2577   1002  -4614       O  
ATOM   5378  N   LEU D1003     -24.815 106.786 134.322  1.00133.27           N  
ANISOU 5378  N   LEU D1003    14497  17067  19071   2605   1325  -3086       N  
ATOM   5379  CA  LEU D1003     -25.069 105.352 134.497  1.00132.70           C  
ANISOU 5379  CA  LEU D1003    14528  17075  18817   2699   1364  -2876       C  
ATOM   5380  C   LEU D1003     -26.521 104.938 134.207  1.00131.55           C  
ANISOU 5380  C   LEU D1003    14448  16785  18749   2667   1433  -2648       C  
ATOM   5381  O   LEU D1003     -27.002 103.916 134.712  1.00131.98           O  
ANISOU 5381  O   LEU D1003    14559  16910  18678   2778   1500  -2498       O  
ATOM   5382  CB  LEU D1003     -24.627 104.874 135.886  1.00134.94           C  
ANISOU 5382  CB  LEU D1003    14795  17634  18843   2920   1375  -2969       C  
ATOM   5383  CG  LEU D1003     -23.135 104.607 136.119  1.00136.87           C  
ANISOU 5383  CG  LEU D1003    15008  18052  18943   2990   1304  -3123       C  
ATOM   5384  CD1 LEU D1003     -22.385 105.884 136.468  1.00138.24           C  
ANISOU 5384  CD1 LEU D1003    15043  18279  19202   2979   1230  -3443       C  
ATOM   5385  CD2 LEU D1003     -22.957 103.577 137.225  1.00138.10           C  
ANISOU 5385  CD2 LEU D1003    15210  18454  18807   3226   1341  -3076       C  
ATOM   5386  N   ARG D1004     -27.209 105.739 133.394  1.00129.24           N  
ANISOU 5386  N   ARG D1004    14141  16286  18677   2524   1425  -2626       N  
ATOM   5387  CA  ARG D1004     -28.482 105.336 132.799  1.00127.44           C  
ANISOU 5387  CA  ARG D1004    13970  15889  18562   2467   1464  -2419       C  
ATOM   5388  C   ARG D1004     -28.152 104.377 131.666  1.00126.45           C  
ANISOU 5388  C   ARG D1004    13928  15677  18442   2394   1432  -2264       C  
ATOM   5389  O   ARG D1004     -28.894 103.432 131.390  1.00127.26           O  
ANISOU 5389  O   ARG D1004    14084  15713  18557   2402   1465  -2085       O  
ATOM   5390  CB  ARG D1004     -29.234 106.553 132.258  1.00125.71           C  
ANISOU 5390  CB  ARG D1004    13708  15489  18566   2352   1453  -2461       C  
ATOM   5391  CG  ARG D1004     -30.698 106.297 131.933  1.00123.73           C  
ANISOU 5391  CG  ARG D1004    13488  15090  18435   2323   1491  -2292       C  
ATOM   5392  CD  ARG D1004     -31.431 107.606 131.689  1.00122.05           C  
ANISOU 5392  CD  ARG D1004    13220  14737  18415   2244   1487  -2361       C  
ATOM   5393  NE  ARG D1004     -32.885 107.451 131.701  1.00119.17           N  
ANISOU 5393  NE  ARG D1004    12860  14263  18155   2245   1530  -2238       N  
ATOM   5394  CZ  ARG D1004     -33.740 108.409 131.350  1.00119.26           C  
ANISOU 5394  CZ  ARG D1004    12837  14129  18347   2177   1526  -2254       C  
ATOM   5395  NH1 ARG D1004     -33.290 109.594 130.953  1.00119.81           N  
ANISOU 5395  NH1 ARG D1004    12870  14141  18514   2104   1494  -2377       N  
ATOM   5396  NH2 ARG D1004     -35.047 108.186 131.387  1.00118.91           N  
ANISOU 5396  NH2 ARG D1004    12789  13990  18402   2184   1562  -2147       N  
ATOM   5397  N   ILE D1005     -27.023 104.651 131.016  1.00125.44           N  
ANISOU 5397  N   ILE D1005    13799  15542  18320   2327   1372  -2346       N  
ATOM   5398  CA  ILE D1005     -26.417 103.779 130.018  1.00122.48           C  
ANISOU 5398  CA  ILE D1005    13500  15120  17915   2275   1336  -2233       C  
ATOM   5399  C   ILE D1005     -26.118 102.418 130.658  1.00123.48           C  
ANISOU 5399  C   ILE D1005    13669  15401  17845   2393   1368  -2146       C  
ATOM   5400  O   ILE D1005     -26.680 101.404 130.243  1.00122.11           O  
ANISOU 5400  O   ILE D1005    13557  15162  17678   2391   1390  -1969       O  
ATOM   5401  CB  ILE D1005     -25.144 104.445 129.415  1.00121.36           C  
ANISOU 5401  CB  ILE D1005    13335  14962  17814   2202   1287  -2363       C  
ATOM   5402  CG1 ILE D1005     -24.358 103.477 128.519  1.00119.93           C  
ANISOU 5402  CG1 ILE D1005    13234  14765  17568   2170   1255  -2257       C  
ATOM   5403  CG2 ILE D1005     -24.255 105.032 130.513  1.00122.01           C  
ANISOU 5403  CG2 ILE D1005    13322  15220  17816   2278   1282  -2591       C  
ATOM   5404  CD1 ILE D1005     -23.225 104.129 127.746  1.00117.48           C  
ANISOU 5404  CD1 ILE D1005    12909  14396  17333   2089   1227  -2353       C  
ATOM   5405  N   THR D1006     -25.273 102.435 131.695  1.00125.66           N  
ANISOU 5405  N   THR D1006    13905  15882  17958   2506   1372  -2280       N  
ATOM   5406  CA  THR D1006     -24.806 101.255 132.450  1.00126.35           C  
ANISOU 5406  CA  THR D1006    14029  16152  17828   2652   1409  -2221       C  
ATOM   5407  C   THR D1006     -25.890 100.201 132.733  1.00128.48           C  
ANISOU 5407  C   THR D1006    14351  16393  18075   2724   1504  -2010       C  
ATOM   5408  O   THR D1006     -25.648  98.988 132.585  1.00124.88           O  
ANISOU 5408  O   THR D1006    13953  15963  17533   2766   1535  -1872       O  
ATOM   5409  CB  THR D1006     -24.175 101.697 133.795  1.00126.77           C  
ANISOU 5409  CB  THR D1006    14014  16439  17716   2807   1407  -2419       C  
ATOM   5410  OG1 THR D1006     -23.113 102.625 133.547  1.00126.37           O  
ANISOU 5410  OG1 THR D1006    13891  16405  17718   2740   1324  -2636       O  
ATOM   5411  CG2 THR D1006     -23.630 100.509 134.580  1.00128.05           C  
ANISOU 5411  CG2 THR D1006    14219  16803  17630   2985   1447  -2357       C  
ATOM   5412  N   ASN D1007     -27.072 100.677 133.139  1.00130.96           N  
ANISOU 5412  N   ASN D1007    14635  16641  18484   2736   1558  -1989       N  
ATOM   5413  CA  ASN D1007     -28.209  99.811 133.487  1.00132.06           C  
ANISOU 5413  CA  ASN D1007    14801  16729  18646   2805   1670  -1802       C  
ATOM   5414  C   ASN D1007     -28.704  98.913 132.350  1.00129.91           C  
ANISOU 5414  C   ASN D1007    14576  16270  18514   2700   1667  -1624       C  
ATOM   5415  O   ASN D1007     -29.307  97.860 132.594  1.00129.34           O  
ANISOU 5415  O   ASN D1007    14524  16170  18449   2767   1766  -1466       O  
ATOM   5416  CB  ASN D1007     -29.344 100.646 134.071  1.00134.02           C  
ANISOU 5416  CB  ASN D1007    14998  16928  18995   2823   1722  -1835       C  
ATOM   5417  CG  ASN D1007     -29.071 101.055 135.502  1.00140.08           C  
ANISOU 5417  CG  ASN D1007    15730  17914  19579   3000   1769  -1960       C  
ATOM   5418  OD1 ASN D1007     -28.735 100.211 136.337  1.00142.25           O  
ANISOU 5418  OD1 ASN D1007    16038  18353  19657   3172   1844  -1904       O  
ATOM   5419  ND2 ASN D1007     -29.209 102.351 135.799  1.00141.46           N  
ANISOU 5419  ND2 ASN D1007    15839  18097  19813   2973   1727  -2135       N  
ATOM   5420  N   ILE D1008     -28.435  99.339 131.119  1.00126.69           N  
ANISOU 5420  N   ILE D1008    14180  15734  18222   2549   1560  -1657       N  
ATOM   5421  CA  ILE D1008     -28.635  98.511 129.941  1.00125.63           C  
ANISOU 5421  CA  ILE D1008    14094  15452  18188   2461   1525  -1527       C  
ATOM   5422  C   ILE D1008     -27.415  97.603 129.750  1.00125.19           C  
ANISOU 5422  C   ILE D1008    14089  15499  17979   2490   1505  -1500       C  
ATOM   5423  O   ILE D1008     -27.562  96.410 129.489  1.00123.09           O  
ANISOU 5423  O   ILE D1008    13858  15197  17715   2509   1542  -1364       O  
ATOM   5424  CB  ILE D1008     -28.829  99.377 128.675  1.00125.43           C  
ANISOU 5424  CB  ILE D1008    14074  15259  18326   2316   1421  -1569       C  
ATOM   5425  CG1 ILE D1008     -29.778 100.552 128.959  1.00125.80           C  
ANISOU 5425  CG1 ILE D1008    14063  15234  18501   2291   1431  -1636       C  
ATOM   5426  CG2 ILE D1008     -29.315  98.527 127.504  1.00124.59           C  
ANISOU 5426  CG2 ILE D1008    14010  14998  18333   2252   1378  -1441       C  
ATOM   5427  CD1 ILE D1008     -29.617 101.720 128.005  1.00125.37           C  
ANISOU 5427  CD1 ILE D1008    14008  15069  18558   2181   1347  -1719       C  
ATOM   5428  N   VAL D1009     -26.223  98.180 129.927  1.00125.08           N  
ANISOU 5428  N   VAL D1009    14069  15610  17848   2496   1453  -1640       N  
ATOM   5429  CA  VAL D1009     -24.930  97.574 129.551  1.00123.28           C  
ANISOU 5429  CA  VAL D1009    13882  15462  17498   2495   1409  -1648       C  
ATOM   5430  C   VAL D1009     -24.638  96.196 130.166  1.00123.29           C  
ANISOU 5430  C   VAL D1009    13918  15584  17342   2620   1484  -1535       C  
ATOM   5431  O   VAL D1009     -24.527  95.212 129.438  1.00123.31           O  
ANISOU 5431  O   VAL D1009    13970  15517  17365   2584   1480  -1415       O  
ATOM   5432  CB  VAL D1009     -23.752  98.553 129.816  1.00123.30           C  
ANISOU 5432  CB  VAL D1009    13842  15578  17429   2492   1351  -1849       C  
ATOM   5433  CG1 VAL D1009     -22.404  97.897 129.549  1.00123.29           C  
ANISOU 5433  CG1 VAL D1009    13874  15671  17301   2505   1315  -1864       C  
ATOM   5434  CG2 VAL D1009     -23.901  99.809 128.968  1.00122.66           C  
ANISOU 5434  CG2 VAL D1009    13734  15343  17528   2356   1294  -1934       C  
ATOM   5435  N   GLU D1010     -24.511  96.118 131.489  1.00123.51           N  
ANISOU 5435  N   GLU D1010    13922  15792  17212   2779   1556  -1571       N  
ATOM   5436  CA  GLU D1010     -24.158  94.849 132.131  1.00121.94           C  
ANISOU 5436  CA  GLU D1010    13763  15722  16847   2926   1643  -1458       C  
ATOM   5437  C   GLU D1010     -25.353  93.899 132.293  1.00121.50           C  
ANISOU 5437  C   GLU D1010    13722  15560  16882   2972   1774  -1256       C  
ATOM   5438  O   GLU D1010     -25.178  92.754 132.720  1.00122.78           O  
ANISOU 5438  O   GLU D1010    13917  15788  16943   3088   1873  -1128       O  
ATOM   5439  CB  GLU D1010     -23.467  95.082 133.482  1.00122.84           C  
ANISOU 5439  CB  GLU D1010    13853  16091  16728   3114   1669  -1576       C  
ATOM   5440  CG  GLU D1010     -22.399  94.042 133.792  1.00125.27           C  
ANISOU 5440  CG  GLU D1010    14205  16562  16831   3234   1687  -1534       C  
ATOM   5441  CD  GLU D1010     -22.217  93.772 135.277  1.00127.90           C  
ANISOU 5441  CD  GLU D1010    14538  17135  16923   3490   1775  -1548       C  
ATOM   5442  OE1 GLU D1010     -23.232  93.699 136.009  1.00130.90           O  
ANISOU 5442  OE1 GLU D1010    14917  17510  17308   3595   1896  -1458       O  
ATOM   5443  OE2 GLU D1010     -21.055  93.610 135.710  1.00127.35           O  
ANISOU 5443  OE2 GLU D1010    14470  17262  16656   3601   1727  -1648       O  
ATOM   5444  N   SER D1011     -26.554  94.369 131.942  1.00119.87           N  
ANISOU 5444  N   SER D1011    13484  15180  16880   2884   1783  -1228       N  
ATOM   5445  CA  SER D1011     -27.788  93.581 132.105  1.00118.80           C  
ANISOU 5445  CA  SER D1011    13338  14918  16882   2919   1913  -1059       C  
ATOM   5446  C   SER D1011     -27.768  92.260 131.326  1.00116.94           C  
ANISOU 5446  C   SER D1011    13132  14573  16727   2878   1936   -914       C  
ATOM   5447  O   SER D1011     -27.203  92.178 130.231  1.00114.00           O  
ANISOU 5447  O   SER D1011    12787  14140  16388   2760   1816   -944       O  
ATOM   5448  CB  SER D1011     -29.038  94.412 131.750  1.00118.57           C  
ANISOU 5448  CB  SER D1011    13259  14715  17077   2818   1892  -1083       C  
ATOM   5449  OG  SER D1011     -29.226  94.565 130.347  1.00115.33           O  
ANISOU 5449  OG  SER D1011    12853  14128  16839   2649   1769  -1095       O  
ATOM   5450  N   SER D1012     -28.378  91.230 131.909  1.00116.89           N  
ANISOU 5450  N   SER D1012    13118  14537  16758   2986   2102   -757       N  
ATOM   5451  CA  SER D1012     -28.489  89.931 131.250  1.00117.29           C  
ANISOU 5451  CA  SER D1012    13177  14464  16925   2954   2147   -621       C  
ATOM   5452  C   SER D1012     -29.301  90.061 129.964  1.00117.05           C  
ANISOU 5452  C   SER D1012    13110  14200  17163   2779   2041   -639       C  
ATOM   5453  O   SER D1012     -29.084  89.319 129.001  1.00116.46           O  
ANISOU 5453  O   SER D1012    13048  14032  17169   2704   1982   -605       O  
ATOM   5454  CB  SER D1012     -29.093  88.873 132.183  1.00118.08           C  
ANISOU 5454  CB  SER D1012    13259  14551  17054   3110   2377   -445       C  
ATOM   5455  OG  SER D1012     -30.226  89.370 132.867  1.00119.44           O  
ANISOU 5455  OG  SER D1012    13382  14667  17334   3159   2481   -425       O  
ATOM   5456  N   PHE D1013     -30.223  91.022 129.959  1.00116.31           N  
ANISOU 5456  N   PHE D1013    12970  14022  17199   2727   2012   -702       N  
ATOM   5457  CA  PHE D1013     -30.965  91.401 128.760  1.00115.82           C  
ANISOU 5457  CA  PHE D1013    12877  13766  17363   2579   1885   -750       C  
ATOM   5458  C   PHE D1013     -30.020  91.777 127.603  1.00115.05           C  
ANISOU 5458  C   PHE D1013    12837  13683  17194   2472   1701   -840       C  
ATOM   5459  O   PHE D1013     -30.218  91.352 126.459  1.00112.99           O  
ANISOU 5459  O   PHE D1013    12579  13290  17063   2390   1611   -830       O  
ATOM   5460  CB  PHE D1013     -31.909  92.574 129.083  1.00113.94           C  
ANISOU 5460  CB  PHE D1013    12590  13479  17222   2558   1880   -818       C  
ATOM   5461  CG  PHE D1013     -32.836  92.937 127.961  1.00111.85           C  
ANISOU 5461  CG  PHE D1013    12286  13016  17197   2435   1765   -859       C  
ATOM   5462  CD1 PHE D1013     -34.093  92.359 127.870  1.00113.23           C  
ANISOU 5462  CD1 PHE D1013    12383  13017  17624   2431   1833   -793       C  
ATOM   5463  CD2 PHE D1013     -32.452  93.854 126.996  1.00111.13           C  
ANISOU 5463  CD2 PHE D1013    12231  12908  17084   2338   1595   -964       C  
ATOM   5464  CE1 PHE D1013     -34.953  92.688 126.830  1.00113.27           C  
ANISOU 5464  CE1 PHE D1013    12344  12851  17844   2336   1710   -849       C  
ATOM   5465  CE2 PHE D1013     -33.302  94.187 125.950  1.00111.10           C  
ANISOU 5465  CE2 PHE D1013    12199  12737  17277   2254   1485   -998       C  
ATOM   5466  CZ  PHE D1013     -34.557  93.604 125.868  1.00111.65           C  
ANISOU 5466  CZ  PHE D1013    12188  12649  17584   2255   1531   -949       C  
ATOM   5467  N   PHE D1014     -28.987  92.556 127.931  1.00115.53           N  
ANISOU 5467  N   PHE D1014    12939  13904  17054   2487   1654   -933       N  
ATOM   5468  CA  PHE D1014     -28.113  93.206 126.958  1.00115.01           C  
ANISOU 5468  CA  PHE D1014    12920  13846  16935   2391   1504  -1029       C  
ATOM   5469  C   PHE D1014     -27.386  92.206 126.082  1.00116.41           C  
ANISOU 5469  C   PHE D1014    13148  14004  17080   2360   1453   -975       C  
ATOM   5470  O   PHE D1014     -27.723  92.035 124.902  1.00116.20           O  
ANISOU 5470  O   PHE D1014    13133  13836  17179   2280   1362   -965       O  
ATOM   5471  CB  PHE D1014     -27.094  94.063 127.700  1.00115.20           C  
ANISOU 5471  CB  PHE D1014    12953  14051  16768   2434   1496  -1143       C  
ATOM   5472  CG  PHE D1014     -26.380  95.059 126.836  1.00115.80           C  
ANISOU 5472  CG  PHE D1014    13051  14106  16840   2334   1373  -1256       C  
ATOM   5473  CD1 PHE D1014     -26.980  96.270 126.507  1.00117.76           C  
ANISOU 5473  CD1 PHE D1014    13273  14260  17210   2266   1325  -1331       C  
ATOM   5474  CD2 PHE D1014     -25.094  94.807 126.382  1.00116.64           C  
ANISOU 5474  CD2 PHE D1014    13205  14283  16829   2316   1321  -1284       C  
ATOM   5475  CE1 PHE D1014     -26.319  97.202 125.724  1.00117.80           C  
ANISOU 5475  CE1 PHE D1014    13298  14232  17227   2187   1240  -1420       C  
ATOM   5476  CE2 PHE D1014     -24.420  95.736 125.603  1.00116.93           C  
ANISOU 5476  CE2 PHE D1014    13260  14286  16882   2232   1235  -1378       C  
ATOM   5477  CZ  PHE D1014     -25.034  96.935 125.273  1.00117.18           C  
ANISOU 5477  CZ  PHE D1014    13266  14216  17043   2171   1202  -1442       C  
ATOM   5478  N   THR D1015     -26.403  91.537 126.688  1.00117.20           N  
ANISOU 5478  N   THR D1015    13277  14253  17002   2439   1512   -945       N  
ATOM   5479  CA  THR D1015     -25.509  90.607 126.005  1.00113.94           C  
ANISOU 5479  CA  THR D1015    12915  13853  16523   2421   1474   -900       C  
ATOM   5480  C   THR D1015     -26.267  89.442 125.387  1.00114.10           C  
ANISOU 5480  C   THR D1015    12920  13719  16712   2401   1498   -791       C  
ATOM   5481  O   THR D1015     -25.817  88.883 124.393  1.00115.95           O  
ANISOU 5481  O   THR D1015    13193  13903  16961   2348   1421   -779       O  
ATOM   5482  CB  THR D1015     -24.427  90.064 126.958  1.00114.37           C  
ANISOU 5482  CB  THR D1015    12993  14106  16357   2535   1550   -882       C  
ATOM   5483  OG1 THR D1015     -24.081  91.067 127.922  1.00113.55           O  
ANISOU 5483  OG1 THR D1015    12869  14150  16124   2597   1561   -990       O  
ATOM   5484  CG2 THR D1015     -23.170  89.649 126.178  1.00114.26           C  
ANISOU 5484  CG2 THR D1015    13038  14134  16242   2492   1469   -897       C  
ATOM   5485  N   LYS D1016     -27.411  89.080 125.970  1.00113.93           N  
ANISOU 5485  N   LYS D1016    12836  13619  16834   2447   1609   -722       N  
ATOM   5486  CA  LYS D1016     -28.261  88.024 125.410  1.00112.51           C  
ANISOU 5486  CA  LYS D1016    12610  13266  16873   2425   1639   -642       C  
ATOM   5487  C   LYS D1016     -28.814  88.403 124.044  1.00111.09           C  
ANISOU 5487  C   LYS D1016    12422  12930  16857   2314   1475   -716       C  
ATOM   5488  O   LYS D1016     -28.718  87.617 123.099  1.00111.97           O  
ANISOU 5488  O   LYS D1016    12541  12959  17042   2277   1408   -704       O  
ATOM   5489  CB  LYS D1016     -29.393  87.648 126.368  1.00112.97           C  
ANISOU 5489  CB  LYS D1016    12589  13257  17077   2501   1812   -557       C  
ATOM   5490  CG  LYS D1016     -28.965  86.724 127.501  1.00113.72           C  
ANISOU 5490  CG  LYS D1016    12692  13462  17052   2640   2004   -434       C  
ATOM   5491  CD  LYS D1016     -28.884  85.281 127.041  1.00113.35           C  
ANISOU 5491  CD  LYS D1016    12630  13321  17117   2643   2062   -337       C  
ATOM   5492  CE  LYS D1016     -28.826  84.339 128.228  1.00115.23           C  
ANISOU 5492  CE  LYS D1016    12860  13620  17302   2799   2299   -184       C  
ATOM   5493  NZ  LYS D1016     -28.895  82.921 127.767  1.00118.25           N  
ANISOU 5493  NZ  LYS D1016    13207  13872  17851   2795   2377    -86       N  
ATOM   5494  N   PHE D1017     -29.364  89.612 123.936  1.00109.82           N  
ANISOU 5494  N   PHE D1017    12248  12737  16741   2273   1408   -795       N  
ATOM   5495  CA  PHE D1017     -29.868  90.125 122.657  1.00109.55           C  
ANISOU 5495  CA  PHE D1017    12218  12574  16833   2193   1249   -866       C  
ATOM   5496  C   PHE D1017     -28.728  90.272 121.644  1.00109.07           C  
ANISOU 5496  C   PHE D1017    12251  12562  16629   2153   1124   -905       C  
ATOM   5497  O   PHE D1017     -28.936  90.199 120.428  1.00108.95           O  
ANISOU 5497  O   PHE D1017    12257  12450  16689   2117    999   -935       O  
ATOM   5498  CB  PHE D1017     -30.574  91.472 122.853  1.00109.61           C  
ANISOU 5498  CB  PHE D1017    12200  12554  16894   2171   1222   -934       C  
ATOM   5499  CG  PHE D1017     -31.145  92.047 121.585  1.00109.18           C  
ANISOU 5499  CG  PHE D1017    12153  12375  16957   2115   1066   -999       C  
ATOM   5500  CD1 PHE D1017     -32.442  91.740 121.192  1.00109.07           C  
ANISOU 5500  CD1 PHE D1017    12060  12206  17178   2110   1034  -1009       C  
ATOM   5501  CD2 PHE D1017     -30.382  92.894 120.778  1.00108.11           C  
ANISOU 5501  CD2 PHE D1017    12101  12274  16703   2082    958  -1053       C  
ATOM   5502  CE1 PHE D1017     -32.968  92.265 120.019  1.00108.91           C  
ANISOU 5502  CE1 PHE D1017    12048  12086  17245   2085    879  -1077       C  
ATOM   5503  CE2 PHE D1017     -30.904  93.416 119.603  1.00107.07           C  
ANISOU 5503  CE2 PHE D1017    11988  12035  16658   2060    825  -1098       C  
ATOM   5504  CZ  PHE D1017     -32.200  93.104 119.224  1.00106.90           C  
ANISOU 5504  CZ  PHE D1017    11894  11879  16845   2068    776  -1114       C  
ATOM   5505  N   ILE D1018     -27.527  90.486 122.169  1.00108.02           N  
ANISOU 5505  N   ILE D1018    12171  12584  16289   2172   1161   -908       N  
ATOM   5506  CA  ILE D1018     -26.312  90.574 121.375  1.00106.30           C  
ANISOU 5506  CA  ILE D1018    12037  12421  15933   2141   1076   -936       C  
ATOM   5507  C   ILE D1018     -25.916  89.191 120.836  1.00105.68           C  
ANISOU 5507  C   ILE D1018    11982  12323  15850   2150   1068   -871       C  
ATOM   5508  O   ILE D1018     -25.768  89.007 119.623  1.00104.63           O  
ANISOU 5508  O   ILE D1018    11893  12119  15742   2117    957   -887       O  
ATOM   5509  CB  ILE D1018     -25.179  91.218 122.212  1.00106.81           C  
ANISOU 5509  CB  ILE D1018    12125  12653  15806   2163   1124   -981       C  
ATOM   5510  CG1 ILE D1018     -25.558  92.654 122.650  1.00107.40           C  
ANISOU 5510  CG1 ILE D1018    12168  12734  15906   2148   1123  -1065       C  
ATOM   5511  CG2 ILE D1018     -23.832  91.126 121.498  1.00107.17           C  
ANISOU 5511  CG2 ILE D1018    12244  12754  15720   2137   1063  -1000       C  
ATOM   5512  CD1 ILE D1018     -26.235  93.534 121.606  1.00105.91           C  
ANISOU 5512  CD1 ILE D1018    11990  12405  15847   2086   1026  -1103       C  
ATOM   5513  N   ILE D1019     -25.772  88.221 121.742  1.00105.98           N  
ANISOU 5513  N   ILE D1019    11990  12422  15857   2209   1191   -796       N  
ATOM   5514  CA  ILE D1019     -25.492  86.828 121.375  1.00105.49           C  
ANISOU 5514  CA  ILE D1019    11933  12330  15818   2224   1211   -726       C  
ATOM   5515  C   ILE D1019     -26.659  86.235 120.566  1.00106.33           C  
ANISOU 5515  C   ILE D1019    11980  12250  16171   2196   1160   -727       C  
ATOM   5516  O   ILE D1019     -26.507  85.187 119.921  1.00106.01           O  
ANISOU 5516  O   ILE D1019    11939  12153  16188   2192   1134   -703       O  
ATOM   5517  CB  ILE D1019     -25.129  85.958 122.611  1.00104.78           C  
ANISOU 5517  CB  ILE D1019    11823  12344  15645   2314   1380   -632       C  
ATOM   5518  CG1 ILE D1019     -23.980  86.598 123.389  1.00104.90           C  
ANISOU 5518  CG1 ILE D1019    11886  12556  15413   2357   1402   -666       C  
ATOM   5519  CG2 ILE D1019     -24.711  84.546 122.202  1.00103.25           C  
ANISOU 5519  CG2 ILE D1019    11639  12120  15473   2327   1407   -558       C  
ATOM   5520  CD1 ILE D1019     -23.876  86.148 124.831  1.00107.54           C  
ANISOU 5520  CD1 ILE D1019    12197  13016  15647   2482   1567   -593       C  
ATOM   5521  N   TYR D1020     -27.809  86.914 120.585  1.00106.29           N  
ANISOU 5521  N   TYR D1020    11916  12150  16318   2180   1139   -769       N  
ATOM   5522  CA  TYR D1020     -28.918  86.559 119.696  1.00107.50           C  
ANISOU 5522  CA  TYR D1020    12005  12131  16711   2156   1053   -810       C  
ATOM   5523  C   TYR D1020     -28.630  86.981 118.249  1.00106.57           C  
ANISOU 5523  C   TYR D1020    11960  11984  16550   2122    861   -889       C  
ATOM   5524  O   TYR D1020     -29.133  86.374 117.301  1.00106.81           O  
ANISOU 5524  O   TYR D1020    11960  11905  16719   2122    762   -931       O  
ATOM   5525  CB  TYR D1020     -30.260  87.132 120.190  1.00108.91           C  
ANISOU 5525  CB  TYR D1020    12092  12216  17075   2157   1093   -833       C  
ATOM   5526  CG  TYR D1020     -31.406  86.987 119.190  1.00111.08           C  
ANISOU 5526  CG  TYR D1020    12294  12318  17595   2136    970   -911       C  
ATOM   5527  CD1 TYR D1020     -31.820  85.721 118.742  1.00112.35           C  
ANISOU 5527  CD1 TYR D1020    12376  12361  17949   2142    967   -915       C  
ATOM   5528  CD2 TYR D1020     -32.074  88.112 118.693  1.00111.02           C  
ANISOU 5528  CD2 TYR D1020    12286  12263  17633   2118    855   -992       C  
ATOM   5529  CE1 TYR D1020     -32.853  85.585 117.823  1.00112.91           C  
ANISOU 5529  CE1 TYR D1020    12366  12283  18252   2135    836  -1018       C  
ATOM   5530  CE2 TYR D1020     -33.113  87.983 117.780  1.00112.22           C  
ANISOU 5530  CE2 TYR D1020    12369  12273  17997   2118    727  -1078       C  
ATOM   5531  CZ  TYR D1020     -33.496  86.720 117.348  1.00113.44           C  
ANISOU 5531  CZ  TYR D1020    12440  12321  18341   2128    711  -1100       C  
ATOM   5532  OH  TYR D1020     -34.526  86.585 116.443  1.00114.40           O  
ANISOU 5532  OH  TYR D1020    12477  12307  18683   2140    568  -1215       O  
ATOM   5533  N   LEU D1021     -27.812  88.013 118.081  1.00104.95           N  
ANISOU 5533  N   LEU D1021    11847  11873  16157   2107    815   -912       N  
ATOM   5534  CA  LEU D1021     -27.498  88.499 116.744  1.00104.48           C  
ANISOU 5534  CA  LEU D1021    11869  11787  16041   2096    661   -965       C  
ATOM   5535  C   LEU D1021     -26.309  87.724 116.170  1.00103.67           C  
ANISOU 5535  C   LEU D1021    11844  11744  15801   2100    636   -936       C  
ATOM   5536  O   LEU D1021     -26.303  87.356 114.996  1.00102.37           O  
ANISOU 5536  O   LEU D1021    11719  11524  15654   2114    519   -965       O  
ATOM   5537  CB  LEU D1021     -27.275  90.024 116.749  1.00103.35           C  
ANISOU 5537  CB  LEU D1021    11778  11684  15807   2080    642   -999       C  
ATOM   5538  CG  LEU D1021     -28.453  90.889 117.255  1.00103.22           C  
ANISOU 5538  CG  LEU D1021    11688  11606  15923   2076    659  -1033       C  
ATOM   5539  CD1 LEU D1021     -27.998  92.282 117.667  1.00102.89           C  
ANISOU 5539  CD1 LEU D1021    11682  11630  15780   2056    693  -1058       C  
ATOM   5540  CD2 LEU D1021     -29.598  90.988 116.249  1.00104.15           C  
ANISOU 5540  CD2 LEU D1021    11779  11591  16203   2094    531  -1085       C  
ATOM   5541  N   ILE D1022     -25.335  87.440 117.031  1.00103.87           N  
ANISOU 5541  N   ILE D1022    11888  11887  15692   2099    745   -883       N  
ATOM   5542  CA  ILE D1022     -24.094  86.724 116.667  1.00102.86           C  
ANISOU 5542  CA  ILE D1022    11830  11830  15421   2101    742   -850       C  
ATOM   5543  C   ILE D1022     -24.345  85.354 116.026  1.00102.00           C  
ANISOU 5543  C   ILE D1022    11697  11644  15415   2115    705   -833       C  
ATOM   5544  O   ILE D1022     -23.501  84.847 115.289  1.00101.99           O  
ANISOU 5544  O   ILE D1022    11763  11666  15320   2117    654   -826       O  
ATOM   5545  CB  ILE D1022     -23.155  86.597 117.903  1.00103.29           C  
ANISOU 5545  CB  ILE D1022    11884  12031  15329   2117    873   -805       C  
ATOM   5546  CG1 ILE D1022     -22.795  87.989 118.467  1.00103.58           C  
ANISOU 5546  CG1 ILE D1022    11935  12149  15271   2105    892   -856       C  
ATOM   5547  CG2 ILE D1022     -21.916  85.751 117.612  1.00102.53           C  
ANISOU 5547  CG2 ILE D1022    11849  12008  15101   2123    877   -767       C  
ATOM   5548  CD1 ILE D1022     -22.543  89.078 117.432  1.00102.44           C  
ANISOU 5548  CD1 ILE D1022    11857  11960  15105   2069    792   -912       C  
ATOM   5549  N   VAL D1023     -25.515  84.779 116.304  1.00101.93           N  
ANISOU 5549  N   VAL D1023    11583  11531  15614   2125    735   -834       N  
ATOM   5550  CA  VAL D1023     -25.941  83.500 115.733  1.00101.07           C  
ANISOU 5550  CA  VAL D1023    11417  11319  15667   2137    705   -843       C  
ATOM   5551  C   VAL D1023     -26.913  83.729 114.560  1.00102.31           C  
ANISOU 5551  C   VAL D1023    11546  11353  15972   2145    536   -950       C  
ATOM   5552  O   VAL D1023     -26.804  83.062 113.528  1.00101.76           O  
ANISOU 5552  O   VAL D1023    11493  11240  15932   2163    426   -999       O  
ATOM   5553  CB  VAL D1023     -26.553  82.586 116.821  1.00100.79           C  
ANISOU 5553  CB  VAL D1023    11264  11233  15797   2154    872   -776       C  
ATOM   5554  CG1 VAL D1023     -27.008  81.253 116.252  1.00100.59           C  
ANISOU 5554  CG1 VAL D1023    11157  11079  15984   2160    856   -797       C  
ATOM   5555  CG2 VAL D1023     -25.552  82.361 117.950  1.00100.64           C  
ANISOU 5555  CG2 VAL D1023    11285  11358  15596   2179   1030   -672       C  
ATOM   5556  N   LEU D1024     -27.835  84.687 114.707  1.00103.63           N  
ANISOU 5556  N   LEU D1024    11676  11474  16223   2142    508   -993       N  
ATOM   5557  CA  LEU D1024     -28.786  85.036 113.631  1.00104.97           C  
ANISOU 5557  CA  LEU D1024    11822  11542  16518   2169    339  -1101       C  
ATOM   5558  C   LEU D1024     -28.101  85.722 112.444  1.00104.99           C  
ANISOU 5558  C   LEU D1024    11964  11598  16328   2202    197  -1132       C  
ATOM   5559  O   LEU D1024     -28.613  85.699 111.318  1.00105.15           O  
ANISOU 5559  O   LEU D1024    11992  11558  16404   2257     39  -1219       O  
ATOM   5560  CB  LEU D1024     -29.922  85.920 114.156  1.00105.23           C  
ANISOU 5560  CB  LEU D1024    11781  11517  16685   2162    357  -1130       C  
ATOM   5561  CG  LEU D1024     -31.165  86.032 113.264  1.00105.82           C  
ANISOU 5561  CG  LEU D1024    11783  11467  16956   2200    200  -1251       C  
ATOM   5562  CD1 LEU D1024     -32.002  84.764 113.346  1.00107.05           C  
ANISOU 5562  CD1 LEU D1024    11783  11494  17396   2201    219  -1301       C  
ATOM   5563  CD2 LEU D1024     -31.999  87.247 113.637  1.00106.16           C  
ANISOU 5563  CD2 LEU D1024    11800  11484  17051   2195    202  -1271       C  
ATOM   5564  N   ASN D1025     -26.957  86.346 112.719  1.00105.31           N  
ANISOU 5564  N   ASN D1025    12111  11752  16152   2181    261  -1064       N  
ATOM   5565  CA  ASN D1025     -26.059  86.868 111.684  1.00105.70           C  
ANISOU 5565  CA  ASN D1025    12299  11851  16013   2212    177  -1064       C  
ATOM   5566  C   ASN D1025     -25.044  85.802 111.240  1.00105.49           C  
ANISOU 5566  C   ASN D1025    12325  11867  15888   2218    172  -1035       C  
ATOM   5567  O   ASN D1025     -24.566  85.817 110.095  1.00105.40           O  
ANISOU 5567  O   ASN D1025    12412  11863  15774   2269     72  -1052       O  
ATOM   5568  CB  ASN D1025     -25.332  88.119 112.188  1.00105.09           C  
ANISOU 5568  CB  ASN D1025    12288  11850  15790   2181    260  -1020       C  
ATOM   5569  CG  ASN D1025     -24.776  88.972 111.066  1.00105.40           C  
ANISOU 5569  CG  ASN D1025    12454  11895  15697   2226    186  -1022       C  
ATOM   5570  OD1 ASN D1025     -23.714  89.580 111.216  1.00105.52           O  
ANISOU 5570  OD1 ASN D1025    12538  11974  15579   2202    258   -981       O  
ATOM   5571  ND2 ASN D1025     -25.494  89.038 109.939  1.00105.21           N  
ANISOU 5571  ND2 ASN D1025    12456  11802  15716   2304     47  -1072       N  
ATOM   5572  N   GLY D1026     -24.733  84.881 112.157  1.00103.57           N  
ANISOU 5572  N   GLY D1026    12022  11654  15676   2180    288   -985       N  
ATOM   5573  CA  GLY D1026     -23.866  83.740 111.882  1.00101.57           C  
ANISOU 5573  CA  GLY D1026    11799  11434  15361   2182    299   -954       C  
ATOM   5574  C   GLY D1026     -24.414  82.854 110.781  1.00102.14           C  
ANISOU 5574  C   GLY D1026    11842  11415  15551   2228    165  -1031       C  
ATOM   5575  O   GLY D1026     -23.698  82.508 109.847  1.00101.59           O  
ANISOU 5575  O   GLY D1026    11859  11372  15370   2261     88  -1041       O  
ATOM   5576  N   ILE D1027     -25.690  82.490 110.885  1.00103.53           N  
ANISOU 5576  N   ILE D1027    11890  11481  15965   2236    136  -1098       N  
ATOM   5577  CA  ILE D1027     -26.348  81.659 109.868  1.00103.99           C  
ANISOU 5577  CA  ILE D1027    11889  11443  16178   2286     -7  -1211       C  
ATOM   5578  C   ILE D1027     -26.493  82.393 108.526  1.00104.99           C  
ANISOU 5578  C   ILE D1027    12111  11576  16205   2370   -199  -1296       C  
ATOM   5579  O   ILE D1027     -26.119  81.843 107.486  1.00105.61           O  
ANISOU 5579  O   ILE D1027    12243  11662  16221   2430   -313  -1348       O  
ATOM   5580  CB  ILE D1027     -27.702  81.082 110.361  1.00105.07           C  
ANISOU 5580  CB  ILE D1027    11841  11445  16636   2273     20  -1275       C  
ATOM   5581  CG1 ILE D1027     -28.291  80.110 109.329  1.00105.63           C  
ANISOU 5581  CG1 ILE D1027    11828  11415  16893   2324   -130  -1420       C  
ATOM   5582  CG2 ILE D1027     -28.682  82.200 110.734  1.00106.48           C  
ANISOU 5582  CG2 ILE D1027    11979  11590  16890   2270     12  -1301       C  
ATOM   5583  CD1 ILE D1027     -29.621  79.484 109.733  1.00107.74           C  
ANISOU 5583  CD1 ILE D1027    11889  11524  17524   2311   -102  -1505       C  
ATOM   5584  N   THR D1028     -27.001  83.632 108.553  1.00105.35           N  
ANISOU 5584  N   THR D1028    12183  11623  16224   2385   -227  -1303       N  
ATOM   5585  CA  THR D1028     -27.168  84.441 107.331  1.00106.31           C  
ANISOU 5585  CA  THR D1028    12403  11753  16237   2488   -388  -1363       C  
ATOM   5586  C   THR D1028     -25.820  84.778 106.681  1.00106.71           C  
ANISOU 5586  C   THR D1028    12631  11897  16016   2522   -381  -1286       C  
ATOM   5587  O   THR D1028     -25.763  85.132 105.498  1.00106.77           O  
ANISOU 5587  O   THR D1028    12739  11917  15911   2634   -507  -1322       O  
ATOM   5588  CB  THR D1028     -28.026  85.717 107.567  1.00105.97           C  
ANISOU 5588  CB  THR D1028    12344  11681  16237   2499   -398  -1376       C  
ATOM   5589  OG1 THR D1028     -28.524  86.213 106.317  1.00106.03           O  
ANISOU 5589  OG1 THR D1028    12412  11673  16200   2628   -576  -1460       O  
ATOM   5590  CG2 THR D1028     -27.230  86.818 108.249  1.00104.70           C  
ANISOU 5590  CG2 THR D1028    12272  11593  15916   2441   -259  -1258       C  
HETATM 5591  N   MSE D1029     -24.752  84.661 107.475  1.00106.94           N  
ANISOU 5591  N   MSE D1029    12693  11994  15947   2436   -229  -1180       N  
HETATM 5592  CA  MSE D1029     -23.367  84.784 107.010  1.00107.02           C  
ANISOU 5592  CA  MSE D1029    12845  12083  15734   2449   -195  -1107       C  
HETATM 5593  C   MSE D1029     -23.008  83.658 106.057  1.00108.17           C  
ANISOU 5593  C   MSE D1029    13025  12229  15846   2509   -291  -1148       C  
HETATM 5594  O   MSE D1029     -22.332  83.880 105.048  1.00108.56           O  
ANISOU 5594  O   MSE D1029    13206  12314  15728   2588   -347  -1132       O  
HETATM 5595  CB  MSE D1029     -22.458  84.762 108.235  1.00104.85           C  
ANISOU 5595  CB  MSE D1029    12557  11877  15406   2344    -20  -1014       C  
HETATM 5596  CG  MSE D1029     -21.084  85.350 107.961  1.00104.45           C  
ANISOU 5596  CG  MSE D1029    12638  11901  15149   2342     39   -943       C  
HETATM 5597 SE   MSE D1029     -21.164  87.294 108.186  1.00106.21          SE  
ANISOU 5597 SE   MSE D1029    12906  12120  15329   2337     97   -920      SE  
HETATM 5598  CE  MSE D1029     -21.428  87.337 110.132  1.00103.66           C  
ANISOU 5598  CE  MSE D1029    12437  11838  15110   2223    240   -912       C  
ATOM   5599  N   GLY D1030     -23.452  82.443 106.370  1.00108.60           N  
ANISOU 5599  N   GLY D1030    12958  12237  16068   2478   -299  -1199       N  
ATOM   5600  CA  GLY D1030     -23.279  81.310 105.470  1.00111.05           C  
ANISOU 5600  CA  GLY D1030    13272  12532  16390   2536   -402  -1266       C  
ATOM   5601  C   GLY D1030     -24.112  81.495 104.216  1.00114.34           C  
ANISOU 5601  C   GLY D1030    13705  12909  16831   2670   -606  -1398       C  
ATOM   5602  O   GLY D1030     -23.640  81.256 103.104  1.00114.83           O  
ANISOU 5602  O   GLY D1030    13867  13005  16756   2771   -711  -1431       O  
ATOM   5603  N   LEU D1031     -25.355  81.933 104.410  1.00117.39           N  
ANISOU 5603  N   LEU D1031    13991  13229  17383   2683   -662  -1476       N  
ATOM   5604  CA  LEU D1031     -26.295  82.228 103.320  1.00119.01           C  
ANISOU 5604  CA  LEU D1031    14195  13401  17622   2825   -865  -1616       C  
ATOM   5605  C   LEU D1031     -25.735  83.164 102.244  1.00119.32           C  
ANISOU 5605  C   LEU D1031    14430  13517  17391   2959   -937  -1575       C  
ATOM   5606  O   LEU D1031     -26.046  83.001 101.062  1.00123.42           O  
ANISOU 5606  O   LEU D1031    14992  14047  17856   3116  -1114  -1683       O  
ATOM   5607  CB  LEU D1031     -27.594  82.816 103.884  1.00118.38           C  
ANISOU 5607  CB  LEU D1031    13990  13248  17742   2803   -878  -1674       C  
ATOM   5608  CG  LEU D1031     -28.587  81.826 104.490  1.00119.40           C  
ANISOU 5608  CG  LEU D1031    13903  13265  18200   2739   -874  -1778       C  
ATOM   5609  CD1 LEU D1031     -29.563  82.524 105.430  1.00117.99           C  
ANISOU 5609  CD1 LEU D1031    13620  13024  18188   2675   -800  -1767       C  
ATOM   5610  CD2 LEU D1031     -29.319  81.060 103.393  1.00121.45           C  
ANISOU 5610  CD2 LEU D1031    14081  13470  18593   2859  -1092  -1984       C  
ATOM   5611  N   GLU D1032     -24.918  84.133 102.659  1.00116.83           N  
ANISOU 5611  N   GLU D1032    14225  13251  16913   2907   -792  -1424       N  
ATOM   5612  CA  GLU D1032     -24.280  85.089 101.743  1.00116.75           C  
ANISOU 5612  CA  GLU D1032    14401  13295  16663   3026   -805  -1352       C  
ATOM   5613  C   GLU D1032     -23.490  84.416 100.619  1.00115.96           C  
ANISOU 5613  C   GLU D1032    14418  13244  16398   3139   -881  -1362       C  
ATOM   5614  O   GLU D1032     -23.230  85.028  99.586  1.00117.26           O  
ANISOU 5614  O   GLU D1032    14731  13444  16380   3294   -933  -1333       O  
ATOM   5615  CB  GLU D1032     -23.382  86.074 102.513  1.00116.41           C  
ANISOU 5615  CB  GLU D1032    14426  13280  16523   2923   -607  -1198       C  
ATOM   5616  CG  GLU D1032     -24.143  87.230 103.166  1.00117.04           C  
ANISOU 5616  CG  GLU D1032    14457  13323  16690   2885   -559  -1185       C  
ATOM   5617  CD  GLU D1032     -23.265  88.112 104.039  1.00114.68           C  
ANISOU 5617  CD  GLU D1032    14194  13049  16330   2774   -367  -1065       C  
ATOM   5618  OE1 GLU D1032     -22.431  87.573 104.797  1.00113.47           O  
ANISOU 5618  OE1 GLU D1032    14012  12934  16168   2662   -259  -1020       O  
ATOM   5619  OE2 GLU D1032     -23.415  89.350 103.975  1.00113.71           O  
ANISOU 5619  OE2 GLU D1032    14119  12907  16177   2805   -325  -1025       O  
ATOM   5620  N   THR D1033     -23.134  83.151 100.826  1.00114.62           N  
ANISOU 5620  N   THR D1033    14180  13075  16295   3071   -879  -1397       N  
ATOM   5621  CA  THR D1033     -22.370  82.373  99.859  1.00113.82           C  
ANISOU 5621  CA  THR D1033    14172  13018  16056   3162   -945  -1414       C  
ATOM   5622  C   THR D1033     -23.217  81.916  98.659  1.00115.81           C  
ANISOU 5622  C   THR D1033    14412  13263  16327   3349  -1180  -1590       C  
ATOM   5623  O   THR D1033     -22.877  82.211  97.503  1.00115.58           O  
ANISOU 5623  O   THR D1033    14535  13289  16090   3527  -1264  -1587       O  
ATOM   5624  CB  THR D1033     -21.679  81.181 100.552  1.00113.49           C  
ANISOU 5624  CB  THR D1033    14056  12976  16089   3023   -850  -1388       C  
ATOM   5625  OG1 THR D1033     -20.572  81.660 101.337  1.00112.40           O  
ANISOU 5625  OG1 THR D1033    13981  12879  15845   2907   -655  -1227       O  
ATOM   5626  CG2 THR D1033     -21.187  80.157  99.541  1.00114.45           C  
ANISOU 5626  CG2 THR D1033    14231  13125  16131   3119   -954  -1453       C  
ATOM   5627  N   SER D1034     -24.319  81.217  98.932  1.00116.52           N  
ANISOU 5627  N   SER D1034    14317  13285  16669   3321  -1282  -1747       N  
ATOM   5628  CA  SER D1034     -25.161  80.661  97.865  1.00117.91           C  
ANISOU 5628  CA  SER D1034    14442  13451  16905   3494  -1522  -1956       C  
ATOM   5629  C   SER D1034     -25.617  81.731  96.894  1.00118.43           C  
ANISOU 5629  C   SER D1034    14630  13565  16802   3703  -1651  -1984       C  
ATOM   5630  O   SER D1034     -26.030  82.806  97.314  1.00117.97           O  
ANISOU 5630  O   SER D1034    14584  13491  16748   3681  -1591  -1915       O  
ATOM   5631  CB  SER D1034     -26.378  79.940  98.437  1.00118.24           C  
ANISOU 5631  CB  SER D1034    14241  13388  17296   3418  -1587  -2123       C  
ATOM   5632  OG  SER D1034     -27.009  79.172  97.422  1.00119.49           O  
ANISOU 5632  OG  SER D1034    14328  13535  17537   3572  -1819  -2352       O  
ATOM   5633  N   LYS D1035     -25.538  81.424  95.600  1.00121.02           N  
ANISOU 5633  N   LYS D1035    15050  13956  16976   3917  -1824  -2086       N  
ATOM   5634  CA  LYS D1035     -25.835  82.397  94.543  1.00123.92           C  
ANISOU 5634  CA  LYS D1035    15567  14388  17128   4164  -1941  -2094       C  
ATOM   5635  C   LYS D1035     -27.333  82.602  94.323  1.00128.68           C  
ANISOU 5635  C   LYS D1035    16038  14958  17895   4273  -2140  -2292       C  
ATOM   5636  O   LYS D1035     -27.795  83.749  94.259  1.00130.53           O  
ANISOU 5636  O   LYS D1035    16334  15201  18061   4351  -2135  -2236       O  
ATOM   5637  CB  LYS D1035     -25.129  82.035  93.231  1.00122.91           C  
ANISOU 5637  CB  LYS D1035    15607  14355  16738   4384  -2042  -2114       C  
ATOM   5638  CG  LYS D1035     -25.565  80.715  92.609  1.00124.44           C  
ANISOU 5638  CG  LYS D1035    15683  14555  17043   4473  -2261  -2365       C  
ATOM   5639  CD  LYS D1035     -24.456  80.089  91.777  1.00125.08           C  
ANISOU 5639  CD  LYS D1035    15911  14713  16899   4576  -2267  -2331       C  
ATOM   5640  CE  LYS D1035     -24.338  80.736  90.406  1.00127.30           C  
ANISOU 5640  CE  LYS D1035    16406  15105  16855   4902  -2383  -2324       C  
ATOM   5641  NZ  LYS D1035     -23.163  80.194  89.668  1.00128.50           N  
ANISOU 5641  NZ  LYS D1035    16717  15329  16779   4993  -2351  -2259       N  
ATOM   5642  N   THR D1036     -28.083  81.497  94.223  1.00130.68           N  
ANISOU 5642  N   THR D1036    16103  15167  18384   4275  -2306  -2528       N  
ATOM   5643  CA  THR D1036     -29.539  81.538  93.992  1.00132.22           C  
ANISOU 5643  CA  THR D1036    16138  15321  18780   4379  -2515  -2759       C  
ATOM   5644  C   THR D1036     -30.242  82.317  95.109  1.00131.56           C  
ANISOU 5644  C   THR D1036    15950  15151  18884   4215  -2392  -2685       C  
ATOM   5645  O   THR D1036     -31.343  82.842  94.920  1.00133.19           O  
ANISOU 5645  O   THR D1036    16085  15338  19182   4316  -2525  -2806       O  
ATOM   5646  CB  THR D1036     -30.162  80.123  93.909  1.00133.18           C  
ANISOU 5646  CB  THR D1036    16029  15373  19201   4356  -2671  -3028       C  
ATOM   5647  OG1 THR D1036     -29.146  79.143  93.641  1.00132.03           O  
ANISOU 5647  OG1 THR D1036    15933  15257  18975   4329  -2635  -3008       O  
ATOM   5648  CG2 THR D1036     -31.229  80.073  92.824  1.00134.18           C  
ANISOU 5648  CG2 THR D1036    16090  15535  19356   4621  -2981  -3313       C  
ATOM   5649  N   PHE D1037     -29.587  82.365  96.268  1.00128.34           N  
ANISOU 5649  N   PHE D1037    15535  14698  18529   3972  -2143  -2493       N  
ATOM   5650  CA  PHE D1037     -30.015  83.154  97.409  1.00127.39           C  
ANISOU 5650  CA  PHE D1037    15348  14514  18541   3811  -1989  -2386       C  
ATOM   5651  C   PHE D1037     -29.623  84.624  97.218  1.00128.33           C  
ANISOU 5651  C   PHE D1037    15665  14695  18399   3885  -1905  -2206       C  
ATOM   5652  O   PHE D1037     -30.316  85.519  97.701  1.00129.45           O  
ANISOU 5652  O   PHE D1037    15767  14799  18618   3855  -1870  -2180       O  
ATOM   5653  CB  PHE D1037     -29.386  82.586  98.687  1.00126.46           C  
ANISOU 5653  CB  PHE D1037    15154  14342  18552   3554  -1761  -2259       C  
ATOM   5654  CG  PHE D1037     -29.784  83.308  99.943  1.00127.31           C  
ANISOU 5654  CG  PHE D1037    15188  14392  18793   3391  -1595  -2154       C  
ATOM   5655  CD1 PHE D1037     -30.955  82.963 100.619  1.00128.96           C  
ANISOU 5655  CD1 PHE D1037    15181  14492  19327   3313  -1614  -2273       C  
ATOM   5656  CD2 PHE D1037     -28.986  84.324 100.464  1.00125.90           C  
ANISOU 5656  CD2 PHE D1037    15148  14261  18430   3319  -1414  -1946       C  
ATOM   5657  CE1 PHE D1037     -31.328  83.623 101.783  1.00127.21           C  
ANISOU 5657  CE1 PHE D1037    14896  14221  19216   3175  -1457  -2174       C  
ATOM   5658  CE2 PHE D1037     -29.358  84.991 101.626  1.00126.29           C  
ANISOU 5658  CE2 PHE D1037    15125  14264  18596   3181  -1271  -1866       C  
ATOM   5659  CZ  PHE D1037     -30.528  84.637 102.288  1.00126.06           C  
ANISOU 5659  CZ  PHE D1037    14894  14137  18865   3112  -1292  -1975       C  
HETATM 5660  N   MSE D1038     -28.526  84.874  96.502  1.00127.76           N  
ANISOU 5660  N   MSE D1038    15801  14710  18034   3987  -1863  -2083       N  
HETATM 5661  CA  MSE D1038     -28.000  86.241  96.352  1.00127.92           C  
ANISOU 5661  CA  MSE D1038    16008  14770  17828   4046  -1737  -1890       C  
HETATM 5662  C   MSE D1038     -28.640  87.042  95.227  1.00129.36           C  
ANISOU 5662  C   MSE D1038    16295  14999  17857   4324  -1895  -1943       C  
HETATM 5663  O   MSE D1038     -28.368  88.242  95.091  1.00128.60           O  
ANISOU 5663  O   MSE D1038    16340  14918  17606   4389  -1785  -1786       O  
HETATM 5664  CB  MSE D1038     -26.478  86.208  96.175  1.00127.85           C  
ANISOU 5664  CB  MSE D1038    16167  14812  17598   4020  -1580  -1714       C  
HETATM 5665  CG  MSE D1038     -25.744  85.864  97.469  1.00126.59           C  
ANISOU 5665  CG  MSE D1038    15933  14615  17550   3746  -1374  -1608       C  
HETATM 5666 SE   MSE D1038     -25.267  87.480  98.487  1.00127.11          SE  
ANISOU 5666 SE   MSE D1038    16060  14654  17580   3605  -1111  -1390      SE  
HETATM 5667  CE  MSE D1038     -26.719  87.415  99.821  1.00127.27           C  
ANISOU 5667  CE  MSE D1038    15829  14590  17940   3435  -1130  -1502       C  
ATOM   5668  N   GLN D1039     -29.487  86.400  94.418  1.00129.39           N  
ANISOU 5668  N   GLN D1039    16227  15027  17910   4500  -2148  -2168       N  
ATOM   5669  CA  GLN D1039     -30.153  87.080  93.296  1.00130.22           C  
ANISOU 5669  CA  GLN D1039    16428  15196  17855   4803  -2327  -2242       C  
ATOM   5670  C   GLN D1039     -31.569  87.580  93.605  1.00131.42           C  
ANISOU 5670  C   GLN D1039    16431  15294  18209   4819  -2438  -2372       C  
ATOM   5671  O   GLN D1039     -32.005  88.606  93.073  1.00130.40           O  
ANISOU 5671  O   GLN D1039    16400  15200  17944   5009  -2485  -2338       O  
ATOM   5672  CB  GLN D1039     -30.177  86.189  92.064  1.00131.40           C  
ANISOU 5672  CB  GLN D1039    16611  15430  17883   5044  -2561  -2425       C  
ATOM   5673  CG  GLN D1039     -28.921  86.285  91.220  1.00130.66           C  
ANISOU 5673  CG  GLN D1039    16763  15427  17454   5190  -2482  -2267       C  
ATOM   5674  CD  GLN D1039     -28.898  85.258  90.111  1.00130.21           C  
ANISOU 5674  CD  GLN D1039    16724  15456  17294   5407  -2710  -2462       C  
ATOM   5675  OE1 GLN D1039     -28.826  85.604  88.931  1.00129.99           O  
ANISOU 5675  OE1 GLN D1039    16869  15533  16990   5721  -2818  -2468       O  
ATOM   5676  NE2 GLN D1039     -28.971  83.985  90.485  1.00129.72           N  
ANISOU 5676  NE2 GLN D1039    16481  15349  17458   5253  -2778  -2624       N  
ATOM   5677  N   SER D1040     -32.281  86.841  94.451  1.00131.63           N  
ANISOU 5677  N   SER D1040    16218  15229  18565   4629  -2471  -2515       N  
ATOM   5678  CA  SER D1040     -33.592  87.260  94.935  1.00131.47           C  
ANISOU 5678  CA  SER D1040    16032  15136  18784   4598  -2542  -2628       C  
ATOM   5679  C   SER D1040     -33.410  87.880  96.320  1.00129.11           C  
ANISOU 5679  C   SER D1040    15693  14757  18606   4328  -2282  -2440       C  
ATOM   5680  O   SER D1040     -33.506  89.098  96.482  1.00128.21           O  
ANISOU 5680  O   SER D1040    15667  14644  18402   4350  -2192  -2310       O  
ATOM   5681  CB  SER D1040     -34.548  86.064  94.996  1.00133.68           C  
ANISOU 5681  CB  SER D1040    16058  15348  19385   4570  -2728  -2912       C  
ATOM   5682  OG  SER D1040     -34.263  85.121  93.966  1.00135.81           O  
ANISOU 5682  OG  SER D1040    16353  15687  19561   4737  -2909  -3067       O  
ATOM   5683  N   PHE D1041     -33.100  87.032  97.302  1.00127.05           N  
ANISOU 5683  N   PHE D1041    15306  14430  18537   4088  -2157  -2424       N  
ATOM   5684  CA  PHE D1041     -32.914  87.439  98.696  1.00124.05           C  
ANISOU 5684  CA  PHE D1041    14871  13984  18277   3838  -1918  -2268       C  
ATOM   5685  C   PHE D1041     -31.609  88.221  98.900  1.00122.04           C  
ANISOU 5685  C   PHE D1041    14815  13787  17768   3783  -1708  -2021       C  
ATOM   5686  O   PHE D1041     -31.179  88.455 100.037  1.00118.81           O  
ANISOU 5686  O   PHE D1041    14378  13346  17420   3581  -1505  -1892       O  
ATOM   5687  CB  PHE D1041     -32.959  86.205  99.618  1.00123.18           C  
ANISOU 5687  CB  PHE D1041    14574  13796  18434   3636  -1848  -2326       C  
ATOM   5688  CG  PHE D1041     -34.312  85.531  99.684  1.00125.13           C  
ANISOU 5688  CG  PHE D1041    14585  13946  19013   3645  -1999  -2558       C  
ATOM   5689  CD1 PHE D1041     -34.779  84.748  98.620  1.00126.55           C  
ANISOU 5689  CD1 PHE D1041    14701  14135  19245   3815  -2243  -2788       C  
ATOM   5690  CD2 PHE D1041     -35.115  85.662 100.819  1.00124.70           C  
ANISOU 5690  CD2 PHE D1041    14361  13785  19232   3488  -1893  -2558       C  
ATOM   5691  CE1 PHE D1041     -36.020  84.125  98.686  1.00127.79           C  
ANISOU 5691  CE1 PHE D1041    14619  14190  19747   3819  -2380  -3023       C  
ATOM   5692  CE2 PHE D1041     -36.357  85.041 100.889  1.00125.62           C  
ANISOU 5692  CE2 PHE D1041    14248  13793  19687   3493  -2014  -2772       C  
ATOM   5693  CZ  PHE D1041     -36.810  84.271  99.822  1.00127.34           C  
ANISOU 5693  CZ  PHE D1041    14391  14012  19980   3653  -2258  -3011       C  
ATOM   5694  N   GLY D1042     -30.997  88.635  97.792  1.00123.11           N  
ANISOU 5694  N   GLY D1042    15147  14004  17626   3977  -1756  -1963       N  
ATOM   5695  CA  GLY D1042     -29.692  89.301  97.810  1.00122.76           C  
ANISOU 5695  CA  GLY D1042    15288  14002  17353   3948  -1559  -1742       C  
ATOM   5696  C   GLY D1042     -29.673  90.697  98.399  1.00120.96           C  
ANISOU 5696  C   GLY D1042    15109  13742  17106   3887  -1392  -1593       C  
ATOM   5697  O   GLY D1042     -28.656  91.139  98.936  1.00118.90           O  
ANISOU 5697  O   GLY D1042    14922  13483  16774   3765  -1188  -1432       O  
ATOM   5698  N   VAL D1043     -30.799  91.393  98.293  1.00122.01           N  
ANISOU 5698  N   VAL D1043    15194  13846  17318   3975  -1483  -1660       N  
ATOM   5699  CA  VAL D1043     -30.916  92.746  98.827  1.00121.44           C  
ANISOU 5699  CA  VAL D1043    15155  13736  17251   3926  -1337  -1536       C  
ATOM   5700  C   VAL D1043     -31.435  92.746 100.272  1.00120.63           C  
ANISOU 5700  C   VAL D1043    14870  13562  17401   3685  -1242  -1557       C  
ATOM   5701  O   VAL D1043     -31.363  93.767 100.960  1.00121.14           O  
ANISOU 5701  O   VAL D1043    14944  13594  17490   3596  -1090  -1454       O  
ATOM   5702  CB  VAL D1043     -31.773  93.641  97.901  1.00122.13           C  
ANISOU 5702  CB  VAL D1043    15314  13834  17256   4172  -1464  -1568       C  
ATOM   5703  CG1 VAL D1043     -33.263  93.400  98.124  1.00123.22           C  
ANISOU 5703  CG1 VAL D1043    15267  13930  17622   4180  -1641  -1759       C  
ATOM   5704  CG2 VAL D1043     -31.406  95.107  98.083  1.00121.17           C  
ANISOU 5704  CG2 VAL D1043    15306  13685  17050   4174  -1271  -1383       C  
ATOM   5705  N   TYR D1044     -31.947  91.597 100.720  1.00120.36           N  
ANISOU 5705  N   TYR D1044    14669  13499  17561   3592  -1323  -1691       N  
ATOM   5706  CA  TYR D1044     -32.391  91.414 102.104  1.00120.52           C  
ANISOU 5706  CA  TYR D1044    14520  13454  17820   3377  -1216  -1703       C  
ATOM   5707  C   TYR D1044     -31.217  91.526 103.081  1.00120.06           C  
ANISOU 5707  C   TYR D1044    14500  13416  17700   3196   -987  -1548       C  
ATOM   5708  O   TYR D1044     -31.224  92.371 103.987  1.00118.99           O  
ANISOU 5708  O   TYR D1044    14343  13259  17609   3089   -844  -1470       O  
ATOM   5709  CB  TYR D1044     -33.059  90.044 102.286  1.00120.85           C  
ANISOU 5709  CB  TYR D1044    14382  13450  18087   3332  -1326  -1865       C  
ATOM   5710  CG  TYR D1044     -34.513  89.963 101.869  1.00123.61           C  
ANISOU 5710  CG  TYR D1044    14599  13742  18623   3440  -1523  -2053       C  
ATOM   5711  CD1 TYR D1044     -34.869  89.697 100.541  1.00125.39           C  
ANISOU 5711  CD1 TYR D1044    14864  14007  18770   3662  -1753  -2193       C  
ATOM   5712  CD2 TYR D1044     -35.535  90.122 102.804  1.00122.98           C  
ANISOU 5712  CD2 TYR D1044    14350  13574  18804   3332  -1482  -2102       C  
ATOM   5713  CE1 TYR D1044     -36.196  89.607 100.154  1.00126.02           C  
ANISOU 5713  CE1 TYR D1044    14808  14041  19032   3771  -1950  -2391       C  
ATOM   5714  CE2 TYR D1044     -36.866  90.034 102.425  1.00124.98           C  
ANISOU 5714  CE2 TYR D1044    14468  13768  19253   3429  -1663  -2286       C  
ATOM   5715  CZ  TYR D1044     -37.191  89.778 101.101  1.00126.57           C  
ANISOU 5715  CZ  TYR D1044    14702  14012  19380   3647  -1903  -2438       C  
ATOM   5716  OH  TYR D1044     -38.517  89.697 100.726  1.00128.54           O  
ANISOU 5716  OH  TYR D1044    14802  14206  19831   3753  -2097  -2645       O  
ATOM   5717  N   THR D1045     -30.214  90.671 102.869  1.00120.16           N  
ANISOU 5717  N   THR D1045    14568  13476  17612   3175   -962  -1516       N  
ATOM   5718  CA  THR D1045     -29.093  90.489 103.793  1.00119.01           C  
ANISOU 5718  CA  THR D1045    14437  13358  17425   3010   -770  -1401       C  
ATOM   5719  C   THR D1045     -28.136  91.689 103.798  1.00120.44           C  
ANISOU 5719  C   THR D1045    14759  13570  17433   3006   -625  -1258       C  
ATOM   5720  O   THR D1045     -27.710  92.132 104.872  1.00120.85           O  
ANISOU 5720  O   THR D1045    14776  13624  17519   2865   -464  -1190       O  
ATOM   5721  CB  THR D1045     -28.332  89.156 103.522  1.00118.06           C  
ANISOU 5721  CB  THR D1045    14325  13274  17258   2995   -794  -1418       C  
ATOM   5722  OG1 THR D1045     -29.247  88.047 103.552  1.00115.39           O  
ANISOU 5722  OG1 THR D1045    13834  12886  17123   2993   -914  -1561       O  
ATOM   5723  CG2 THR D1045     -27.238  88.911 104.565  1.00117.32           C  
ANISOU 5723  CG2 THR D1045    14229  13215  17132   2831   -603  -1310       C  
ATOM   5724  N   THR D1046     -27.819  92.218 102.613  1.00121.61           N  
ANISOU 5724  N   THR D1046    15059  13739  17408   3172   -675  -1218       N  
ATOM   5725  CA  THR D1046     -26.900  93.363 102.486  1.00122.34           C  
ANISOU 5725  CA  THR D1046    15284  13836  17362   3186   -520  -1078       C  
ATOM   5726  C   THR D1046     -27.375  94.579 103.296  1.00122.96           C  
ANISOU 5726  C   THR D1046    15309  13866  17546   3111   -416  -1047       C  
ATOM   5727  O   THR D1046     -26.583  95.201 104.010  1.00122.25           O  
ANISOU 5727  O   THR D1046    15225  13772  17451   2998   -243   -967       O  
ATOM   5728  CB  THR D1046     -26.663  93.757 101.009  1.00124.28           C  
ANISOU 5728  CB  THR D1046    15705  14100  17416   3415   -583  -1032       C  
ATOM   5729  OG1 THR D1046     -26.380  92.585 100.235  1.00126.10           O  
ANISOU 5729  OG1 THR D1046    15974  14380  17557   3500   -707  -1088       O  
ATOM   5730  CG2 THR D1046     -25.488  94.725 100.884  1.00124.16           C  
ANISOU 5730  CG2 THR D1046    15820  14074  17280   3415   -385   -874       C  
ATOM   5731  N   LEU D1047     -28.664  94.904 103.179  1.00125.02           N  
ANISOU 5731  N   LEU D1047    15507  14088  17908   3179   -527  -1123       N  
ATOM   5732  CA  LEU D1047     -29.301  95.923 104.014  1.00124.75           C  
ANISOU 5732  CA  LEU D1047    15395  14003  18000   3101   -447  -1114       C  
ATOM   5733  C   LEU D1047     -29.260  95.514 105.489  1.00123.51           C  
ANISOU 5733  C   LEU D1047    15096  13847  17985   2893   -350  -1137       C  
ATOM   5734  O   LEU D1047     -28.943  96.331 106.351  1.00122.28           O  
ANISOU 5734  O   LEU D1047    14917  13682  17862   2789   -202  -1087       O  
ATOM   5735  CB  LEU D1047     -30.752  96.161 103.570  1.00126.62           C  
ANISOU 5735  CB  LEU D1047    15579  14201  18328   3221   -608  -1209       C  
ATOM   5736  CG  LEU D1047     -31.075  97.342 102.644  1.00128.98           C  
ANISOU 5736  CG  LEU D1047    15996  14479  18533   3405   -631  -1157       C  
ATOM   5737  CD1 LEU D1047     -32.258  97.022 101.738  1.00130.90           C  
ANISOU 5737  CD1 LEU D1047    16218  14726  18793   3592   -862  -1281       C  
ATOM   5738  CD2 LEU D1047     -31.335  98.624 103.434  1.00127.62           C  
ANISOU 5738  CD2 LEU D1047    15786  14249  18455   3321   -489  -1100       C  
ATOM   5739  N   PHE D1048     -29.567  94.246 105.767  1.00122.97           N  
ANISOU 5739  N   PHE D1048    14930  13790  18001   2845   -425  -1215       N  
ATOM   5740  CA  PHE D1048     -29.590  93.727 107.139  1.00123.10           C  
ANISOU 5740  CA  PHE D1048    14816  13810  18146