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***  PROTEIN BINDING/HYDROLASE 07-DEC-11 3UZD  ***

elNémo ID: 20121814452198299

Job options:

ID        	=	 20121814452198299
JOBID     	=	 PROTEIN BINDING/HYDROLASE 07-DEC-11 3UZD
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    PROTEIN BINDING/HYDROLASE               07-DEC-11   3UZD              
TITLE     CRYSTAL STRUCTURE OF 14-3-3 GAMMA                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 14-3-3 PROTEIN GAMMA;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PROTEIN KINASE C INHIBITOR PROTEIN 1, KCIP-1, 14-3-3 PROTEIN
COMPND   5 GAMMA, N-TERMINALLY PROCESSED;                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: HISTONE DEACETYLASE 4;                                     
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: HD4;                                                        
COMPND  11 EC: 3.5.1.98;                                                        
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: YWHAG;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 OTHER_DETAILS: POLYPEPTIDE(L)                                        
KEYWDS    STRUCTURAL GENOMICS, SGC, STRUCTURAL GENOMICS CONSORTIUM, MAINLY      
KEYWDS   2 ALPHA, PHOSPHOSERINE, PHOSPHOTHREONINE, PROTEIN BINDING-HYDROLASE    
KEYWDS   3 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.XU,C.BIAN,F.MACKENZIE,C.BOUNTRA,J.WEIGELT,C.H.ARROWSMITH,           
AUTHOR   2 A.M.EDWARDS,J.MIN,STRUCTURAL GENOMICS CONSORTIUM (SGC)               
REVDAT   2   13-JUN-12 3UZD    1                                                
REVDAT   1   21-MAR-12 3UZD    0                                                
JRNL        AUTH   C.XU,J.JIN,C.BIAN,R.LAM,R.TIAN,R.WEIST,L.YOU,J.NIE,          
JRNL        AUTH 2 A.BOCHKAREV,W.TEMPEL,C.S.TAN,G.A.WASNEY,M.VEDADI,G.D.GISH,   
JRNL        AUTH 3 C.H.ARROWSMITH,T.PAWSON,X.J.YANG,J.MIN                       
JRNL        TITL   SEQUENCE-SPECIFIC RECOGNITION OF A PXLPXI/L MOTIF BY AN      
JRNL        TITL 2 ANKYRIN REPEAT TUMBLER LOCK.                                 
JRNL        REF    SCI.SIGNAL.                   V.   5  RA39 2012              
JRNL        REFN                   ESSN 1937-9145                               
JRNL        PMID   22649097                                                     
JRNL        DOI    10.1126/SCISIGNAL.2002979                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.86 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 1.86                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 66.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 24650                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1252                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.86                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1681                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.34                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3370                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 82                           
REMARK   3   BIN FREE R VALUE                    : 0.4010                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1862                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 13                                      
REMARK   3   SOLVENT ATOMS            : 138                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.36000                                             
REMARK   3    B22 (A**2) : -0.47000                                             
REMARK   3    B33 (A**2) : 0.82000                                              
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): 0.135         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.129         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.088         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.113         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1917 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2592 ; 1.526 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   236 ; 5.888 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    90 ;36.789 ;24.556       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   332 ;17.067 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;21.426 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   295 ; 0.158 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1442 ; 0.012 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1205 ; 1.331 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1909 ; 2.102 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   712 ; 3.797 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   683 ; 5.715 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
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     2        A    35                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.6633  28.8793  13.8176              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0533 T22:   0.0898                                     
REMARK   3      T33:   0.0980 T12:   0.0161                                     
REMARK   3      T13:   0.0273 T23:   0.0647                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0838 L22:   3.7423                                     
REMARK   3      L33:   8.7648 L12:   1.2532                                     
REMARK   3      L13:   1.4477 L23:   4.3038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0097 S12:   0.1277 S13:   0.1277                       
REMARK   3      S21:   0.0295 S22:  -0.0634 S23:   0.2658                       
REMARK   3      S31:  -0.0430 S32:  -0.4637 S33:   0.0537                       
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    36        A    55                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.0448  23.7154  17.6449              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0479 T22:   0.0461                                     
REMARK   3      T33:   0.0886 T12:  -0.0126                                     
REMARK   3      T13:  -0.0060 T23:   0.0091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4921 L22:   1.7653                                     
REMARK   3      L33:   7.5197 L12:  -0.6385                                     
REMARK   3      L13:  -4.1613 L23:   1.2354                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0279 S12:  -0.0031 S13:  -0.1747                       
REMARK   3      S21:   0.2427 S22:  -0.0040 S23:   0.1204                       
REMARK   3      S31:   0.2528 S32:  -0.0652 S33:   0.0319                       
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    56        A    70                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.0619  20.7127  -0.6156              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0942 T22:   0.3086                                     
REMARK   3      T33:   0.1086 T12:   0.0498                                     
REMARK   3      T13:  -0.0152 T23:  -0.0148                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2027 L22:   4.7495                                     
REMARK   3      L33:  14.3837 L12:  -0.0684                                     
REMARK   3      L13:  -2.8860 L23:   1.3922                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0312 S12:   0.1354 S13:  -0.1053                       
REMARK   3      S21:  -0.3414 S22:  -0.0303 S23:  -0.3154                       
REMARK   3      S31:   0.2161 S32:   1.0660 S33:  -0.0008                       
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    71        A    81                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.4145  26.8232 -12.1361              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4306 T22:   0.9784                                     
REMARK   3      T33:   0.3867 T12:  -0.0162                                     
REMARK   3      T13:   0.1562 T23:   0.0392                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0441 L22:  56.3737                                     
REMARK   3      L33:  19.4953 L12: -16.8626                                     
REMARK   3      L13:  -9.9158 L23:  33.1477                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4141 S12:  -0.1635 S13:   0.5302                       
REMARK   3      S21:  -1.2767 S22:   0.5818 S23:  -1.7794                       
REMARK   3      S31:  -0.7103 S32:   0.2998 S33:  -0.9958                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    82        A   109                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.6493  30.9656  10.3171              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0685 T22:   0.0734                                     
REMARK   3      T33:   0.1381 T12:  -0.0281                                     
REMARK   3      T13:   0.0088 T23:   0.0228                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1083 L22:   0.9793                                     
REMARK   3      L33:   9.4477 L12:  -1.0311                                     
REMARK   3      L13:  -2.9711 L23:   1.9920                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0557 S12:   0.1111 S13:   0.1651                       
REMARK   3      S21:  -0.0662 S22:   0.0519 S23:  -0.1362                       
REMARK   3      S31:  -0.2862 S32:   0.3977 S33:  -0.1076                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   110        A   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.5884  26.7765  33.4488              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3020 T22:   0.1741                                     
REMARK   3      T33:   0.2081 T12:  -0.0347                                     
REMARK   3      T13:   0.0728 T23:  -0.0455                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0814 L22:   2.6686                                     
REMARK   3      L33:   9.6788 L12:  -1.7564                                     
REMARK   3      L13:  -2.6197 L23:  -1.9714                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2713 S12:  -0.5047 S13:  -0.0535                       
REMARK   3      S21:   0.5628 S22:   0.4174 S23:   0.1968                       
REMARK   3      S31:  -0.4380 S32:   0.0243 S33:  -0.1461                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   121        A   147                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.0621  24.9143  17.3737              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0406 T22:   0.0417                                     
REMARK   3      T33:   0.0682 T12:  -0.0043                                     
REMARK   3      T13:  -0.0392 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3320 L22:   2.4556                                     
REMARK   3      L33:   4.6513 L12:   0.3766                                     
REMARK   3      L13:  -2.2105 L23:  -0.5566                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0332 S12:   0.1711 S13:   0.1375                       
REMARK   3      S21:   0.0242 S22:   0.0061 S23:  -0.2011                       
REMARK   3      S31:  -0.1750 S32:   0.1975 S33:  -0.0392                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   148        A   165                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.0441  20.8452  29.8915              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0911 T22:   0.1203                                     
REMARK   3      T33:   0.1162 T12:   0.0029                                     
REMARK   3      T13:  -0.0700 T23:  -0.0189                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3656 L22:   4.7598                                     
REMARK   3      L33:  16.8570 L12:   3.6379                                     
REMARK   3      L13:  -8.0135 L23:  -7.5670                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0925 S12:  -0.5235 S13:  -0.0806                       
REMARK   3      S21:   0.4196 S22:  -0.2399 S23:  -0.3254                       
REMARK   3      S31:  -0.1568 S32:   0.6322 S33:   0.1474                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   166        A   211                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.9333   9.7534  25.9527              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0808 T22:   0.0491                                     
REMARK   3      T33:   0.0705 T12:   0.0210                                     
REMARK   3      T13:  -0.0400 T23:  -0.0316                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7314 L22:   3.2981                                     
REMARK   3      L33:   2.2687 L12:   1.4590                                     
REMARK   3      L13:  -0.8863 L23:  -1.3052                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0286 S12:  -0.2156 S13:  -0.1505                       
REMARK   3      S21:   0.1115 S22:  -0.0587 S23:  -0.2380                       
REMARK   3      S31:   0.0975 S32:   0.2174 S33:   0.0301                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   212        A   234                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.9762   4.5267  22.0050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1152 T22:   0.0106                                     
REMARK   3      T33:   0.0566 T12:  -0.0088                                     
REMARK   3      T13:  -0.0401 T23:  -0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.6239 L22:   3.0764                                     
REMARK   3      L33:   6.9258 L12:   0.2541                                     
REMARK   3      L13:  -7.4868 L23:  -0.1425                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1408 S12:   0.1401 S13:  -0.2870                       
REMARK   3      S21:  -0.0765 S22:   0.0874 S23:  -0.1035                       
REMARK   3      S31:   0.1461 S32:   0.0469 S33:   0.0534                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   4                                                                      
REMARK   4 3UZD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB069399.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-AUG-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97924                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24650                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.860                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 66.480                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.89                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.84500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2B05                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3M MG (OAC)2, 20% PEG3350, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       30.25550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       39.61500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       61.11600            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       30.25550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       39.61500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       61.11600            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       30.25550            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       39.61500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       61.11600            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       30.25550            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       39.61500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       61.11600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12720 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 43740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 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        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 401  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A    72                                                      
REMARK 465     ASP A    73                                                      
REMARK 465     GLY A    74                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     SER A   235                                                      
REMARK 465     ASP A   236                                                      
REMARK 465     GLN A   237                                                      
REMARK 465     GLN A   238                                                      
REMARK 465     ASP A   239                                                      
REMARK 465     ASP A   240                                                      
REMARK 465     ASP A   241                                                      
REMARK 465     GLY A   242                                                      
REMARK 465     GLY A   243                                                      
REMARK 465     GLU A   244                                                      
REMARK 465     GLY A   245                                                      
REMARK 465     ASN A   246                                                      
REMARK 465     ASN A   247                                                      
REMARK 465     SER A   248                                                      
REMARK 465     LEU B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     TYR B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     LEU B    16                                                      
REMARK 465     PRO B    17                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A   2    CG1  CG2                                            
REMARK 470     ASP A   3    CG   OD1  OD2                                       
REMARK 470     GLU A   5    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  10    CE   NZ                                             
REMARK 470     GLN A  68    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  69    CG   CD   CE   NZ                                   
REMARK 470     THR A  70    OG1  CG2                                            
REMARK 470     SER A  71    CB   OG                                             
REMARK 470     GLU A  76    CG   CD   OE1  OE2                                  
REMARK 470     ILE A  79    CG1  CD1                                            
REMARK 470     GLU A  80    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  83    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A  87    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  91    CD   CE   NZ                                        
REMARK 470     GLU A 141    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 142    CG   CD   CE   NZ                                   
REMARK 470     LYS A 152    CE   NZ                                             
REMARK 470     LYS A 162    CD   CE   NZ                                        
REMARK 470     GLU A 163    OE1  OE2                                            
REMARK 470     GLU A 213    CD   OE1  OE2                                       
REMARK 470     LEU B  14    CD1                                                 
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A   42   N    CA   C    O    CB   CG   CD                    
REMARK 480     ARG A   42   NE   CZ   NH2                                       
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   O    HOH A   528     O    HOH A   528     2565     1.88            
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    ASN A  34       36.66     76.26                                   
REMARK 500    TYR A 107      -66.23   -133.58                                   
REMARK 500    ALA A 189       75.08   -118.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 513        DISTANCE =  7.20 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 480   O                                                      
REMARK 620 2 HOH A 459   O   136.5                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 101                 
DBREF  3UZD A    1   247  UNP    P61981   1433G_HUMAN      1    247             
DBREF  3UZD B    1    17  UNP    P56524   HDAC4_HUMAN    343    359             
SEQADV 3UZD SER A  248  UNP  P61981              EXPRESSION TAG                 
SEQRES   1 A  248  MET VAL ASP ARG GLU GLN LEU VAL GLN LYS ALA ARG LEU          
SEQRES   2 A  248  ALA GLU GLN ALA GLU ARG TYR ASP ASP MET ALA ALA ALA          
SEQRES   3 A  248  MET LYS ASN VAL THR GLU LEU ASN GLU PRO LEU SER ASN          
SEQRES   4 A  248  GLU GLU ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL          
SEQRES   5 A  248  VAL GLY ALA ARG ARG SER SER TRP ARG VAL ILE SER SER          
SEQRES   6 A  248  ILE GLU GLN LYS THR SER ALA ASP GLY ASN GLU LYS LYS          
SEQRES   7 A  248  ILE GLU MET VAL ARG ALA TYR ARG GLU LYS ILE GLU LYS          
SEQRES   8 A  248  GLU LEU GLU ALA VAL CYS GLN ASP VAL LEU SER LEU LEU          
SEQRES   9 A  248  ASP ASN TYR LEU ILE LYS ASN CYS SER GLU THR GLN TYR          
SEQRES  10 A  248  GLU SER LYS VAL PHE TYR LEU LYS MET LYS GLY ASP TYR          
SEQRES  11 A  248  TYR ARG TYR LEU ALA GLU VAL ALA THR GLY GLU LYS ARG          
SEQRES  12 A  248  ALA THR VAL VAL GLU SER SER GLU LYS ALA TYR SER GLU          
SEQRES  13 A  248  ALA HIS GLU ILE SER LYS GLU HIS MET GLN PRO THR HIS          
SEQRES  14 A  248  PRO ILE ARG LEU GLY LEU ALA LEU ASN TYR SER VAL PHE          
SEQRES  15 A  248  TYR TYR GLU ILE GLN ASN ALA PRO GLU GLN ALA CYS HIS          
SEQRES  16 A  248  LEU ALA LYS THR ALA PHE ASP ASP ALA ILE ALA GLU LEU          
SEQRES  17 A  248  ASP THR LEU ASN GLU ASP SER TYR LYS ASP SER THR LEU          
SEQRES  18 A  248  ILE MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP THR          
SEQRES  19 A  248  SER ASP GLN GLN ASP ASP ASP GLY GLY GLU GLY ASN ASN          
SEQRES  20 A  248  SER                                                          
SEQRES   1 B   17  LEU PRO LEU TYR THR SER PRO SEP LEU PRO ASN ILE THR          
SEQRES   2 B   17  LEU GLY LEU PRO                                              
MODRES 3UZD SEP B    8  SER  PHOSPHOSERINE                                      
HET    SEP  B   8      10                                                       
HET    NO3  A 301       4                                                       
HET    NO3  A 302       4                                                       
HET     MG  A 303       1                                                       
HET    NO3  B 101       4                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     NO3 NITRATE ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   2  SEP    C3 H8 N O6 P                                                 
FORMUL   3  NO3    3(N O3 1-)                                                   
FORMUL   5   MG    MG 2+                                                        
FORMUL   7  HOH   *138(H2 O)                                                    
HELIX    1   1 ASP A    3  ALA A   17  1                                  15    
HELIX    2   2 ARG A   19  GLU A   32  1                                  14    
HELIX    3   3 SER A   38  SER A   71  1                                  34    
HELIX    4   4 ASN A   75  GLU A   76  5                                   2    
HELIX    5   5 LYS A   78  LYS A   78  5                                   1    
HELIX    6   6 ILE A   79  TYR A  107  1                                  29    
HELIX    7   7 TYR A  107  CYS A  112  1                                   6    
HELIX    8   8 GLN A  116  ALA A  138  1                                  23    
HELIX    9   9 THR A  139  MET A  165  1                                  27    
HELIX   10  10 HIS A  169  ILE A  186  1                                  18    
HELIX   11  11 ALA A  189  GLU A  207  1                                  19    
HELIX   12  12 LEU A  208  LEU A  211  5                                   4    
HELIX   13  13 SER A  215  THR A  234  1                                  20    
LINK         C   PRO B   7                 N   SEP B   8     1555   1555  1.34  
LINK         C   SEP B   8                 N   LEU B   9     1555   1555  1.32  
LINK        MG    MG A 303                 O   HOH A 480     1555   1555  2.41  
LINK        MG    MG A 303                 O   HOH A 459     1555   1555  2.74  
SITE     1 AC1  7 SER A 113  GLU A 114  THR A 115  ALA A 189                    
SITE     2 AC1  7 PRO A 190  GLU A 191  GLN A 192                               
SITE     1 AC2  6 ASP A 214  SER A 215  TYR A 216  LYS A 217                    
SITE     2 AC2  6 ASP A 218  HOH A 429                                          
SITE     1 AC3  2 HOH A 459  HOH A 480                                          
SITE     1 AC4  2 GLU A 185  PRO B   7                                          
CRYST1   60.511   79.230  122.232  90.00  90.00  90.00 I 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016526  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012621  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008181        0.00000                         
ATOM      1  N   VAL A   2     -14.244  38.354  14.823  1.00 63.94           N  
ANISOU    1  N   VAL A   2     7763   8058   8472   2580   -821   -227       N  
ATOM      2  CA  VAL A   2     -14.506  37.004  15.262  1.00 61.99           C  
ANISOU    2  CA  VAL A   2     7067   8211   8273   2250   -550   -315       C  
ATOM      3  C   VAL A   2     -14.433  36.891  16.771  1.00 60.83           C  
ANISOU    3  C   VAL A   2     6746   8187   8179   2080   -293   -445       C  
ATOM      4  O   VAL A   2     -13.797  37.687  17.436  1.00 62.52           O  
ANISOU    4  O   VAL A   2     7214   8140   8402   2116   -271   -381       O  
ATOM      5  CB  VAL A   2     -13.501  36.034  14.656  1.00 58.88           C  
ANISOU    5  CB  VAL A   2     6822   7719   7829   1848   -408    -19       C  
ATOM      6  N   ASP A   3     -15.114  35.899  17.303  1.00 57.54           N  
ANISOU    6  N   ASP A   3     5923   8174   7766   1858    -94   -639       N  
ATOM      7  CA  ASP A   3     -14.917  35.485  18.689  1.00 52.08           C  
ANISOU    7  CA  ASP A   3     5141   7589   7057   1555    191   -703       C  
ATOM      8  C   ASP A   3     -13.864  34.374  18.692  1.00 45.19           C  
ANISOU    8  C   ASP A   3     4478   6566   6128   1131    356   -406       C  
ATOM      9  O   ASP A   3     -13.398  33.913  17.640  1.00 44.89           O  
ANISOU    9  O   ASP A   3     4572   6405   6078   1075    274   -207       O  
ATOM     10  CB  ASP A   3     -16.224  34.948  19.275  1.00 54.17           C  
ANISOU   10  CB  ASP A   3     4914   8377   7290   1454    339  -1093       C  
ATOM     11  N   ARG A   4     -13.489  33.934  19.877  1.00 40.97           N  
ANISOU   11  N   ARG A   4     3988   6041   5539    855    566   -398       N  
ATOM     12  CA  ARG A   4     -12.450  32.905  20.022  1.00 35.03           C  
ANISOU   12  CA  ARG A   4     3477   5117   4717    532    664   -157       C  
ATOM     13  C   ARG A   4     -12.985  31.567  19.499  1.00 35.67           C  
ANISOU   13  C   ARG A   4     3444   5386   4724    276    727   -175       C  
ATOM     14  O   ARG A   4     -12.296  30.832  18.790  1.00 34.25           O  
ANISOU   14  O   ARG A   4     3435   5052   4527    178    677     14       O  
ATOM     15  CB  ARG A   4     -12.108  32.809  21.499  1.00 36.46           C  
ANISOU   15  CB  ARG A   4     3760   5273   4819    341    829   -185       C  
ATOM     16  CG  ARG A   4     -10.909  31.968  21.819  1.00 29.10           C  
ANISOU   16  CG  ARG A   4     3131   4116   3809    125    854     33       C  
ATOM     17  CD  ARG A   4     -10.877  31.669  23.344  1.00 32.32           C  
ANISOU   17  CD  ARG A   4     3654   4551   4074   -102   1009    -29       C  
ATOM     18  NE  ARG A   4      -9.631  30.970  23.637  1.00 33.12           N  
ANISOU   18  NE  ARG A   4     4083   4404   4099   -201    948    162       N  
ATOM     19  CZ  ARG A   4      -8.458  31.549  23.900  1.00 30.57           C  
ANISOU   19  CZ  ARG A   4     3901   3891   3823    -63    859    246       C  
ATOM     20  NH1 ARG A   4      -8.328  32.882  24.033  1.00 30.59           N  
ANISOU   20  NH1 ARG A   4     3826   3867   3930    124    848    192       N  
ATOM     21  NH2 ARG A   4      -7.413  30.775  24.096  1.00 28.27           N  
ANISOU   21  NH2 ARG A   4     3848   3440   3452   -115    769    353       N  
ATOM     22  N   GLU A   5     -14.226  31.252  19.808  1.00 37.04           N  
ANISOU   22  N   GLU A   5     3317   5918   4840    152    840   -441       N  
ATOM     23  CA  GLU A   5     -14.830  30.000  19.398  1.00 36.81           C  
ANISOU   23  CA  GLU A   5     3190   6089   4708   -167    929   -500       C  
ATOM     24  C   GLU A   5     -14.851  29.843  17.891  1.00 36.38           C  
ANISOU   24  C   GLU A   5     3088   6010   4725     -4    745   -414       C  
ATOM     25  O   GLU A   5     -14.624  28.809  17.359  1.00 32.32           O  
ANISOU   25  O   GLU A   5     2696   5436   4150   -223    760   -301       O  
ATOM     26  CB  GLU A   5     -16.241  29.858  19.973  1.00 40.17           C  
ANISOU   26  CB  GLU A   5     3225   6997   5042   -360   1106   -885       C  
ATOM     27  N   GLN A   6     -15.112  30.945  17.215  1.00 36.30           N  
ANISOU   27  N   GLN A   6     2948   6017   4828    407    548   -471       N  
ATOM     28  CA  GLN A   6     -15.100  30.994  15.775  1.00 36.94           C  
ANISOU   28  CA  GLN A   6     3042   6046   4946    596    342   -378       C  
ATOM     29  C   GLN A   6     -13.688  30.814  15.179  1.00 31.26           C  
ANISOU   29  C   GLN A   6     2705   4943   4229    554    287    -39       C  
ATOM     30  O   GLN A   6     -13.539  30.137  14.235  1.00 30.89           O  
ANISOU   30  O   GLN A   6     2698   4886   4153    468    239     48       O  
ATOM     31  CB  GLN A   6     -15.748  32.276  15.254  1.00 38.64           C  
ANISOU   31  CB  GLN A   6     3124   6325   5231   1073     95   -528       C  
ATOM     32  CG  GLN A   6     -17.269  32.389  15.477  1.00 48.59           C  
ANISOU   32  CG  GLN A   6     3889   8079   6494   1202     80   -964       C  
ATOM     33  CD  GLN A   6     -17.848  33.669  14.918  1.00 58.60           C  
ANISOU   33  CD  GLN A   6     5088   9357   7822   1785   -253  -1130       C  
ATOM     34  OE1 GLN A   6     -17.473  34.750  15.305  1.00 60.47           O  
ANISOU   34  OE1 GLN A   6     5548   9326   8102   2067   -360  -1082       O  
ATOM     35  NE2 GLN A   6     -18.778  33.535  13.992  1.00 66.90           N  
ANISOU   35  NE2 GLN A   6     5860  10702   8857   1979   -446  -1341       N  
ATOM     36  N   LEU A   7     -12.671  31.420  15.761  1.00 30.89           N  
ANISOU   36  N   LEU A   7     2902   4627   4207    599    304    105       N  
ATOM     37  CA  LEU A   7     -11.300  31.177  15.270  1.00 29.18           C  
ANISOU   37  CA  LEU A   7     2968   4143   3976    516    282    340       C  
ATOM     38  C   LEU A   7     -10.954  29.704  15.409  1.00 28.35           C  
ANISOU   38  C   LEU A   7     2912   4049   3809    232    384    380       C  
ATOM     39  O   LEU A   7     -10.331  29.087  14.517  1.00 27.08           O  
ANISOU   39  O   LEU A   7     2850   3812   3626    178    332    478       O  
ATOM     40  CB  LEU A   7     -10.292  32.045  16.039  1.00 27.89           C  
ANISOU   40  CB  LEU A   7     3006   3755   3834    566    305    420       C  
ATOM     41  CG  LEU A   7     -10.388  33.558  15.719  1.00 32.70           C  
ANISOU   41  CG  LEU A   7     3724   4230   4471    834    169    423       C  
ATOM     42  CD1 LEU A   7      -9.766  34.393  16.858  1.00 36.96           C  
ANISOU   42  CD1 LEU A   7     4401   4612   5029    849    233    419       C  
ATOM     43  CD2 LEU A   7      -9.722  33.884  14.406  1.00 34.18           C  
ANISOU   43  CD2 LEU A   7     4131   4253   4602    845     52    579       C  
ATOM     44  N   VAL A   8     -11.328  29.125  16.536  1.00 28.92           N  
ANISOU   44  N   VAL A   8     2966   4196   3824     42    520    295       N  
ATOM     45  CA  VAL A   8     -10.983  27.726  16.770  1.00 28.52           C  
ANISOU   45  CA  VAL A   8     3098   4068   3669   -224    579    344       C  
ATOM     46  C   VAL A   8     -11.775  26.809  15.823  1.00 30.43           C  
ANISOU   46  C   VAL A   8     3232   4464   3865   -370    574    283       C  
ATOM     47  O   VAL A   8     -11.214  25.875  15.224  1.00 29.74           O  
ANISOU   47  O   VAL A   8     3319   4245   3737   -450    520    366       O  
ATOM     48  CB  VAL A   8     -11.220  27.343  18.244  1.00 28.40           C  
ANISOU   48  CB  VAL A   8     3199   4056   3537   -450    723    283       C  
ATOM     49  CG1 VAL A   8     -11.069  25.860  18.445  1.00 29.46           C  
ANISOU   49  CG1 VAL A   8     3623   4062   3507   -741    749    329       C  
ATOM     50  CG2 VAL A   8     -10.211  28.101  19.122  1.00 28.40           C  
ANISOU   50  CG2 VAL A   8     3348   3872   3571   -306    700    358       C  
ATOM     51  N   GLN A   9     -13.047  27.113  15.623  1.00 30.24           N  
ANISOU   51  N   GLN A   9     2900   4740   3849   -372    608    102       N  
ATOM     52  CA  GLN A   9     -13.817  26.411  14.615  1.00 33.38           C  
ANISOU   52  CA  GLN A   9     3141   5332   4211   -484    581     13       C  
ATOM     53  C   GLN A   9     -13.202  26.565  13.224  1.00 32.10           C  
ANISOU   53  C   GLN A   9     3037   5047   4111   -272    404    154       C  
ATOM     54  O   GLN A   9     -13.137  25.626  12.504  1.00 29.66           O  
ANISOU   54  O   GLN A   9     2795   4724   3750   -413    386    178       O  
ATOM     55  CB  GLN A   9     -15.274  26.820  14.617  1.00 36.64           C  
ANISOU   55  CB  GLN A   9     3136   6161   4624   -467    615   -275       C  
ATOM     56  CG  GLN A   9     -16.169  25.961  13.747  1.00 49.45           C  
ANISOU   56  CG  GLN A   9     4559   8053   6177   -664    618   -428       C  
ATOM     57  CD  GLN A   9     -15.966  24.470  13.965  1.00 57.58           C  
ANISOU   57  CD  GLN A   9     5872   8954   7051  -1132    762   -367       C  
ATOM     58  OE1 GLN A   9     -15.897  23.988  15.089  1.00 66.80           O  
ANISOU   58  OE1 GLN A   9     7246  10039   8096  -1435    930   -370       O  
ATOM     59  NE2 GLN A   9     -15.892  23.741  12.898  1.00 52.38           N  
ANISOU   59  NE2 GLN A   9     5276   8256   6370  -1193    682   -318       N  
ATOM     60  N   LYS A  10     -12.732  27.756  12.884  1.00 31.79           N  
ANISOU   60  N   LYS A  10     3019   4906   4154     31    284    239       N  
ATOM     61  CA  LYS A  10     -12.042  27.943  11.586  1.00 29.77           C  
ANISOU   61  CA  LYS A  10     2885   4527   3901    155    146    377       C  
ATOM     62  C   LYS A  10     -10.792  27.078  11.544  1.00 27.93           C  
ANISOU   62  C   LYS A  10     2879   4095   3637      9    192    491       C  
ATOM     63  O   LYS A  10     -10.500  26.519  10.520  1.00 27.43           O  
ANISOU   63  O   LYS A  10     2856   4030   3538    -30    139    520       O  
ATOM     64  CB  LYS A  10     -11.588  29.394  11.389  1.00 31.20           C  
ANISOU   64  CB  LYS A  10     3179   4562   4116    414     36    466       C  
ATOM     65  CG  LYS A  10     -10.917  29.649  10.018  1.00 34.49           C  
ANISOU   65  CG  LYS A  10     3770   4867   4468    457    -80    598       C  
ATOM     66  CD  LYS A  10     -10.485  31.102   9.880  1.00 44.00           C  
ANISOU   66  CD  LYS A  10     5198   5877   5645    628   -176    693       C  
ATOM     67  N   ALA A  11     -10.035  26.983  12.641  1.00 25.86           N  
ANISOU   67  N   ALA A  11     2760   3683   3382    -39    265    525       N  
ATOM     68  CA  ALA A  11      -8.841  26.132  12.608  1.00 24.36           C  
ANISOU   68  CA  ALA A  11     2765   3331   3160    -96    250    569       C  
ATOM     69  C   ALA A  11      -9.207  24.675  12.347  1.00 24.85           C  
ANISOU   69  C   ALA A  11     2908   3390   3145   -273    250    521       C  
ATOM     70  O   ALA A  11      -8.477  23.989  11.631  1.00 25.41           O  
ANISOU   70  O   ALA A  11     3076   3386   3193   -255    181    518       O  
ATOM     71  CB  ALA A  11      -7.994  26.272  13.893  1.00 21.09           C  
ANISOU   71  CB  ALA A  11     2498   2768   2748    -73    279    584       C  
ATOM     72  N   ARG A  12     -10.288  24.189  12.969  1.00 25.37           N  
ANISOU   72  N   ARG A  12     2954   3538   3147   -473    337    455       N  
ATOM     73  CA  ARG A  12     -10.700  22.797  12.810  1.00 27.61           C  
ANISOU   73  CA  ARG A  12     3394   3784   3314   -725    356    405       C  
ATOM     74  C   ARG A  12     -11.127  22.523  11.368  1.00 27.11           C  
ANISOU   74  C   ARG A  12     3170   3870   3262   -727    299    362       C  
ATOM     75  O   ARG A  12     -10.875  21.451  10.838  1.00 29.00           O  
ANISOU   75  O   ARG A  12     3586   3999   3434   -826    253    348       O  
ATOM     76  CB  ARG A  12     -11.853  22.433  13.755  1.00 28.03           C  
ANISOU   76  CB  ARG A  12     3444   3955   3249  -1044    511    307       C  
ATOM     77  CG  ARG A  12     -11.542  22.493  15.269  1.00 31.76           C  
ANISOU   77  CG  ARG A  12     4154   4271   3642  -1129    583    342       C  
ATOM     78  CD  ARG A  12     -12.784  22.004  16.052  1.00 37.75           C  
ANISOU   78  CD  ARG A  12     4918   5203   4222  -1562    781    205       C  
ATOM     79  NE  ARG A  12     -12.727  22.303  17.486  1.00 49.63           N  
ANISOU   79  NE  ARG A  12     6576   6651   5632  -1670    885    208       N  
ATOM     80  CZ  ARG A  12     -13.529  23.159  18.138  1.00 54.70           C  
ANISOU   80  CZ  ARG A  12     6902   7591   6289  -1721   1038     60       C  
ATOM     81  NH1 ARG A  12     -14.430  23.903  17.482  1.00 52.77           N  
ANISOU   81  NH1 ARG A  12     6154   7722   6174  -1594   1061   -115       N  
ATOM     82  NH2 ARG A  12     -13.432  23.273  19.467  1.00 52.39           N  
ANISOU   82  NH2 ARG A  12     6810   7228   5867  -1874   1144     61       N  
ATOM     83  N   LEU A  13     -11.789  23.487  10.744  1.00 26.10           N  
ANISOU   83  N   LEU A  13     2741   3976   3202   -596    275    329       N  
ATOM     84  CA  LEU A  13     -12.254  23.330   9.350  1.00 28.49           C  
ANISOU   84  CA  LEU A  13     2894   4440   3491   -575    191    286       C  
ATOM     85  C   LEU A  13     -11.059  23.382   8.407  1.00 28.11           C  
ANISOU   85  C   LEU A  13     2979   4244   3455   -428     97    388       C  
ATOM     86  O   LEU A  13     -10.960  22.577   7.480  1.00 28.78           O  
ANISOU   86  O   LEU A  13     3109   4339   3487   -501     56    356       O  
ATOM     87  CB  LEU A  13     -13.228  24.460   9.003  1.00 29.07           C  
ANISOU   87  CB  LEU A  13     2665   4771   3609   -393    124    212       C  
ATOM     88  CG  LEU A  13     -14.597  24.437   9.661  1.00 30.26           C  
ANISOU   88  CG  LEU A  13     2539   5220   3739   -523    209     -3       C  
ATOM     89  CD1 LEU A  13     -15.322  25.747   9.376  1.00 30.79           C  
ANISOU   89  CD1 LEU A  13     2333   5497   3869   -187     67   -102       C  
ATOM     90  CD2 LEU A  13     -15.421  23.231   9.162  1.00 36.74           C  
ANISOU   90  CD2 LEU A  13     3263   6240   4455   -842    263   -158       C  
ATOM     91  N   ALA A  14     -10.102  24.252   8.731  1.00 27.59           N  
ANISOU   91  N   ALA A  14     2985   4057   3442   -264     87    477       N  
ATOM     92  CA  ALA A  14      -8.935  24.468   7.863  1.00 25.60           C  
ANISOU   92  CA  ALA A  14     2813   3743   3173   -181     39    521       C  
ATOM     93  C   ALA A  14      -8.126  23.202   7.881  1.00 27.09           C  
ANISOU   93  C   ALA A  14     3141   3819   3333   -239     33    449       C  
ATOM     94  O   ALA A  14      -7.605  22.783   6.850  1.00 27.47           O  
ANISOU   94  O   ALA A  14     3197   3906   3336   -238     -5    395       O  
ATOM     95  CB  ALA A  14      -8.109  25.664   8.397  1.00 24.65           C  
ANISOU   95  CB  ALA A  14     2739   3538   3091    -69     61    589       C  
ATOM     96  N   GLU A  15      -8.011  22.582   9.040  1.00 26.23           N  
ANISOU   96  N   GLU A  15     3179   3560   3227   -276     51    429       N  
ATOM     97  CA  GLU A  15      -7.358  21.301   9.180  1.00 27.24           C  
ANISOU   97  CA  GLU A  15     3535   3513   3303   -279    -19    348       C  
ATOM     98  C   GLU A  15      -7.969  20.229   8.321  1.00 27.76           C  
ANISOU   98  C   GLU A  15     3660   3590   3296   -421    -47    286       C  
ATOM     99  O   GLU A  15      -7.276  19.555   7.651  1.00 27.56           O  
ANISOU   99  O   GLU A  15     3713   3513   3246   -344   -127    193       O  
ATOM    100  CB  GLU A  15      -7.360  20.839  10.626  1.00 26.03           C  
ANISOU  100  CB  GLU A  15     3632   3150   3107   -325    -23    367       C  
ATOM    101  CG  GLU A  15      -6.311  19.841  10.974  1.00 33.63           C  
ANISOU  101  CG  GLU A  15     4896   3868   4013   -186   -175    281       C  
ATOM    102  CD  GLU A  15      -6.779  18.406  10.905  1.00 47.42           C  
ANISOU  102  CD  GLU A  15     6990   5401   5626   -340   -246    242       C  
ATOM    103  OE1 GLU A  15      -7.976  18.141  10.871  1.00 56.39           O  
ANISOU  103  OE1 GLU A  15     8146   6586   6694   -639   -134    283       O  
ATOM    104  OE2 GLU A  15      -5.952  17.517  10.846  1.00 45.15           O  
ANISOU  104  OE2 GLU A  15     6965   4903   5287   -166   -424    137       O  
ATOM    105  N   GLN A  16      -9.262  20.083   8.385  1.00 27.25           N  
ANISOU  105  N   GLN A  16     3538   3622   3193   -633     23    298       N  
ATOM    106  CA  GLN A  16      -9.886  19.069   7.612  1.00 29.90           C  
ANISOU  106  CA  GLN A  16     3930   3985   3446   -817      9    219       C  
ATOM    107  C   GLN A  16      -9.707  19.335   6.126  1.00 27.90           C  
ANISOU  107  C   GLN A  16     3482   3910   3211   -715    -45    189       C  
ATOM    108  O   GLN A  16      -9.632  18.439   5.376  1.00 29.72           O  
ANISOU  108  O   GLN A  16     3805   4106   3380   -776    -93    106       O  
ATOM    109  CB  GLN A  16     -11.343  18.949   7.989  1.00 31.52           C  
ANISOU  109  CB  GLN A  16     4035   4350   3589  -1110    118    178       C  
ATOM    110  CG  GLN A  16     -11.520  18.455   9.390  1.00 38.34           C  
ANISOU  110  CG  GLN A  16     5181   5026   4361  -1318    197    189       C  
ATOM    111  CD  GLN A  16     -12.939  18.438   9.830  1.00 43.66           C  
ANISOU  111  CD  GLN A  16     5693   5946   4950  -1666    356     89       C  
ATOM    112  OE1 GLN A  16     -13.411  19.379  10.417  1.00 44.59           O  
ANISOU  112  OE1 GLN A  16     5552   6265   5124  -1625    436     71       O  
ATOM    113  NE2 GLN A  16     -13.616  17.358   9.572  1.00 48.38           N  
ANISOU  113  NE2 GLN A  16     6440   6545   5398  -2025    408    -13       N  
ATOM    114  N   ALA A  17      -9.623  20.583   5.738  1.00 25.99           N  
ANISOU  114  N   ALA A  17     3024   3827   3023   -573    -43    258       N  
ATOM    115  CA  ALA A  17      -9.449  20.976   4.347  1.00 28.23           C  
ANISOU  115  CA  ALA A  17     3194   4264   3268   -512    -94    255       C  
ATOM    116  C   ALA A  17      -7.972  20.995   3.893  1.00 29.46           C  
ANISOU  116  C   ALA A  17     3418   4366   3409   -404   -104    211       C  
ATOM    117  O   ALA A  17      -7.666  21.313   2.717  1.00 29.57           O  
ANISOU  117  O   ALA A  17     3375   4514   3345   -410   -116    193       O  
ATOM    118  CB  ALA A  17     -10.087  22.328   4.113  1.00 29.73           C  
ANISOU  118  CB  ALA A  17     3223   4606   3466   -422   -121    347       C  
ATOM    119  N   GLU A  18      -7.082  20.613   4.783  1.00 27.81           N  
ANISOU  119  N   GLU A  18     3326   3994   3246   -320   -105    156       N  
ATOM    120  CA  GLU A  18      -5.658  20.656   4.533  1.00 28.68           C  
ANISOU  120  CA  GLU A  18     3420   4126   3349   -197   -116     30       C  
ATOM    121  C   GLU A  18      -5.218  22.026   4.090  1.00 26.78           C  
ANISOU  121  C   GLU A  18     3053   4044   3080   -220    -39     95       C  
ATOM    122  O   GLU A  18      -4.353  22.165   3.277  1.00 25.86           O  
ANISOU  122  O   GLU A  18     2870   4069   2886   -249     -4    -24       O  
ATOM    123  CB  GLU A  18      -5.235  19.593   3.555  1.00 29.41           C  
ANISOU  123  CB  GLU A  18     3541   4258   3377   -184   -172   -158       C  
ATOM    124  CG  GLU A  18      -5.275  18.237   4.124  1.00 36.54           C  
ANISOU  124  CG  GLU A  18     4684   4917   4283   -123   -282   -255       C  
ATOM    125  CD  GLU A  18      -5.065  17.170   3.092  1.00 44.57           C  
ANISOU  125  CD  GLU A  18     5760   5946   5230   -108   -354   -448       C  
ATOM    126  OE1 GLU A  18      -3.978  17.072   2.582  1.00 45.57           O  
ANISOU  126  OE1 GLU A  18     5782   6191   5343     43   -383   -661       O  
ATOM    127  OE2 GLU A  18      -5.988  16.449   2.771  1.00 45.92           O  
ANISOU  127  OE2 GLU A  18     6057   6040   5351   -264   -372   -420       O  
ATOM    128  N   ARG A  19      -5.803  23.036   4.682  1.00 24.95           N  
ANISOU  128  N   ARG A  19     2816   3777   2887   -225    -11    261       N  
ATOM    129  CA  ARG A  19      -5.368  24.408   4.425  1.00 26.51           C  
ANISOU  129  CA  ARG A  19     3006   4035   3032   -258     43    340       C  
ATOM    130  C   ARG A  19      -4.596  24.906   5.641  1.00 26.25           C  
ANISOU  130  C   ARG A  19     2978   3920   3076   -195     89    324       C  
ATOM    131  O   ARG A  19      -5.191  25.528   6.530  1.00 25.41           O  
ANISOU  131  O   ARG A  19     2904   3713   3037   -146     88    445       O  
ATOM    132  CB  ARG A  19      -6.586  25.284   4.137  1.00 27.36           C  
ANISOU  132  CB  ARG A  19     3146   4139   3110   -252    -10    512       C  
ATOM    133  CG  ARG A  19      -7.175  24.943   2.752  1.00 29.00           C  
ANISOU  133  CG  ARG A  19     3351   4468   3199   -315    -78    507       C  
ATOM    134  CD  ARG A  19      -8.497  25.605   2.489  1.00 27.92           C  
ANISOU  134  CD  ARG A  19     3213   4357   3036   -229   -201    613       C  
ATOM    135  NE  ARG A  19      -8.323  27.058   2.509  1.00 28.05           N  
ANISOU  135  NE  ARG A  19     3402   4273   2983   -169   -240    742       N  
ATOM    136  CZ  ARG A  19      -8.215  27.848   1.455  1.00 29.68           C  
ANISOU  136  CZ  ARG A  19     3828   4458   2992   -214   -316    832       C  
ATOM    137  NH1 ARG A  19      -8.228  27.371   0.196  1.00 29.03           N  
ANISOU  137  NH1 ARG A  19     3784   4492   2754   -323   -353    804       N  
ATOM    138  NH2 ARG A  19      -8.069  29.147   1.671  1.00 30.17           N  
ANISOU  138  NH2 ARG A  19     4130   4352   2982   -169   -361    952       N  
ATOM    139  N   TYR A  20      -3.308  24.538   5.735  1.00 24.81           N  
ANISOU  139  N   TYR A  20     2735   3808   2885   -171    113    130       N  
ATOM    140  CA  TYR A  20      -2.609  24.738   6.983  1.00 25.49           C  
ANISOU  140  CA  TYR A  20     2809   3828   3047    -72    114     72       C  
ATOM    141  C   TYR A  20      -2.162  26.162   7.246  1.00 26.97           C  
ANISOU  141  C   TYR A  20     2994   4050   3203   -177    212    131       C  
ATOM    142  O   TYR A  20      -1.967  26.543   8.402  1.00 25.28           O  
ANISOU  142  O   TYR A  20     2797   3748   3060   -107    212    150       O  
ATOM    143  CB  TYR A  20      -1.437  23.769   7.106  1.00 27.89           C  
ANISOU  143  CB  TYR A  20     3030   4211   3357     67     44   -216       C  
ATOM    144  CG  TYR A  20      -1.924  22.336   7.115  1.00 27.03           C  
ANISOU  144  CG  TYR A  20     3051   3951   3269    194    -92   -255       C  
ATOM    145  CD1 TYR A  20      -2.584  21.811   8.241  1.00 29.42           C  
ANISOU  145  CD1 TYR A  20     3562   3999   3617    264   -175   -137       C  
ATOM    146  CD2 TYR A  20      -1.780  21.540   5.996  1.00 31.51           C  
ANISOU  146  CD2 TYR A  20     3578   4618   3778    192   -124   -406       C  
ATOM    147  CE1 TYR A  20      -3.059  20.501   8.232  1.00 30.11           C  
ANISOU  147  CE1 TYR A  20     3864   3904   3673    300   -289   -164       C  
ATOM    148  CE2 TYR A  20      -2.261  20.225   5.966  1.00 32.58           C  
ANISOU  148  CE2 TYR A  20     3896   4572   3911    277   -253   -443       C  
ATOM    149  CZ  TYR A  20      -2.881  19.720   7.107  1.00 32.84           C  
ANISOU  149  CZ  TYR A  20     4185   4319   3972    317   -336   -316       C  
ATOM    150  OH  TYR A  20      -3.277  18.410   7.087  1.00 32.23           O  
ANISOU  150  OH  TYR A  20     4377   4024   3847    343   -461   -361       O  
ATOM    151  N   ASP A  21      -2.033  26.956   6.188  1.00 25.59           N  
ANISOU  151  N   ASP A  21     2856   3975   2892   -371    292    169       N  
ATOM    152  CA  ASP A  21      -1.716  28.359   6.380  1.00 28.37           C  
ANISOU  152  CA  ASP A  21     3320   4288   3169   -522    379    252       C  
ATOM    153  C   ASP A  21      -2.877  29.046   7.100  1.00 27.20           C  
ANISOU  153  C   ASP A  21     3318   3912   3106   -396    308    486       C  
ATOM    154  O   ASP A  21      -2.637  29.877   7.953  1.00 26.28           O  
ANISOU  154  O   ASP A  21     3263   3702   3018   -399    342    518       O  
ATOM    155  CB  ASP A  21      -1.445  29.057   5.039  1.00 31.35           C  
ANISOU  155  CB  ASP A  21     3838   4758   3316   -806    463    273       C  
ATOM    156  CG  ASP A  21      -0.195  28.533   4.338  1.00 36.30           C  
ANISOU  156  CG  ASP A  21     4271   5695   3827   -990    583    -31       C  
ATOM    157  OD1 ASP A  21       0.746  28.027   4.991  1.00 40.66           O  
ANISOU  157  OD1 ASP A  21     4578   6406   4466   -904    604   -293       O  
ATOM    158  OD2 ASP A  21      -0.123  28.714   3.117  1.00 46.45           O  
ANISOU  158  OD2 ASP A  21     5656   7087   4906  -1226    649    -34       O  
ATOM    159  N   ASP A  22      -4.110  28.761   6.665  1.00 25.97           N  
ANISOU  159  N   ASP A  22     3195   3704   2968   -298    211    607       N  
ATOM    160  CA  ASP A  22      -5.336  29.226   7.317  1.00 27.86           C  
ANISOU  160  CA  ASP A  22     3475   3817   3295   -137    131    736       C  
ATOM    161  C   ASP A  22      -5.411  28.731   8.762  1.00 25.68           C  
ANISOU  161  C   ASP A  22     3093   3499   3167    -38    156    686       C  
ATOM    162  O   ASP A  22      -5.724  29.488   9.662  1.00 27.16           O  
ANISOU  162  O   ASP A  22     3317   3595   3408     34    162    734       O  
ATOM    163  CB  ASP A  22      -6.580  28.654   6.606  1.00 26.71           C  
ANISOU  163  CB  ASP A  22     3268   3735   3146    -61     26    768       C  
ATOM    164  CG  ASP A  22      -6.947  29.417   5.361  1.00 28.81           C  
ANISOU  164  CG  ASP A  22     3705   3989   3251    -76    -72    863       C  
ATOM    165  OD1 ASP A  22      -6.246  30.386   5.026  1.00 30.36           O  
ANISOU  165  OD1 ASP A  22     4131   4092   3314   -189    -44    925       O  
ATOM    166  OD2 ASP A  22      -7.919  29.028   4.693  1.00 28.84           O  
ANISOU  166  OD2 ASP A  22     3648   4077   3233     -1   -182    865       O  
ATOM    167  N   MET A  23      -5.149  27.448   8.970  1.00 24.44           N  
ANISOU  167  N   MET A  23     2854   3384   3047    -35    155    585       N  
ATOM    168  CA  MET A  23      -5.192  26.882  10.326  1.00 25.60           C  
ANISOU  168  CA  MET A  23     3007   3447   3272     28    156    552       C  
ATOM    169  C   MET A  23      -4.189  27.629  11.268  1.00 23.84           C  
ANISOU  169  C   MET A  23     2809   3180   3071     55    196    516       C  
ATOM    170  O   MET A  23      -4.514  27.946  12.437  1.00 24.41           O  
ANISOU  170  O   MET A  23     2919   3168   3190     99    212    554       O  
ATOM    171  CB  MET A  23      -4.826  25.399  10.239  1.00 22.42           C  
ANISOU  171  CB  MET A  23     2635   3032   2854     40    100    440       C  
ATOM    172  CG  MET A  23      -5.234  24.571  11.459  1.00 24.48           C  
ANISOU  172  CG  MET A  23     3032   3148   3122     52     69    443       C  
ATOM    173  SD  MET A  23      -4.492  22.984  11.477  1.00 25.42           S  
ANISOU  173  SD  MET A  23     3333   3141   3184    132    -68    302       S  
ATOM    174  CE  MET A  23      -4.826  22.405  13.174  1.00 23.77           C  
ANISOU  174  CE  MET A  23     3431   2688   2913    107   -111    355       C  
ATOM    175  N   ALA A  24      -2.965  27.839  10.799  1.00 22.93           N  
ANISOU  175  N   ALA A  24     2649   3157   2906      4    222    402       N  
ATOM    176  CA  ALA A  24      -1.947  28.500  11.613  1.00 22.30           C  
ANISOU  176  CA  ALA A  24     2549   3093   2830     -7    262    313       C  
ATOM    177  C   ALA A  24      -2.334  29.962  11.892  1.00 24.10           C  
ANISOU  177  C   ALA A  24     2885   3221   3049    -79    327    450       C  
ATOM    178  O   ALA A  24      -2.236  30.435  13.033  1.00 23.40           O  
ANISOU  178  O   ALA A  24     2827   3057   3007    -33    341    453       O  
ATOM    179  CB  ALA A  24      -0.559  28.421  10.934  1.00 24.59           C  
ANISOU  179  CB  ALA A  24     2703   3598   3042   -100    301     84       C  
ATOM    180  N   ALA A  25      -2.817  30.664  10.863  1.00 23.36           N  
ANISOU  180  N   ALA A  25     2898   3099   2877   -168    340    561       N  
ATOM    181  CA  ALA A  25      -3.236  32.059  11.046  1.00 25.39           C  
ANISOU  181  CA  ALA A  25     3351   3195   3101   -184    343    684       C  
ATOM    182  C   ALA A  25      -4.407  32.176  12.057  1.00 26.09           C  
ANISOU  182  C   ALA A  25     3421   3181   3311     27    285    750       C  
ATOM    183  O   ALA A  25      -4.414  33.101  12.867  1.00 26.69           O  
ANISOU  183  O   ALA A  25     3591   3142   3408     63    301    764       O  
ATOM    184  CB  ALA A  25      -3.579  32.705   9.695  1.00 26.71           C  
ANISOU  184  CB  ALA A  25     3728   3305   3118   -280    303    794       C  
ATOM    185  N   ALA A  26      -5.321  31.190  12.093  1.00 24.05           N  
ANISOU  185  N   ALA A  26     3027   2993   3117    126    241    747       N  
ATOM    186  CA  ALA A  26      -6.433  31.244  13.058  1.00 24.39           C  
ANISOU  186  CA  ALA A  26     3003   3024   3241    253    231    743       C  
ATOM    187  C   ALA A  26      -5.896  31.009  14.474  1.00 24.66           C  
ANISOU  187  C   ALA A  26     3029   3027   3315    231    299    687       C  
ATOM    188  O   ALA A  26      -6.273  31.729  15.420  1.00 25.56           O  
ANISOU  188  O   ALA A  26     3159   3090   3462    295    326    675       O  
ATOM    189  CB  ALA A  26      -7.551  30.218  12.716  1.00 22.73           C  
ANISOU  189  CB  ALA A  26     2648   2944   3046    266    201    713       C  
ATOM    190  N   MET A  27      -4.986  30.060  14.606  1.00 23.72           N  
ANISOU  190  N   MET A  27     2904   2932   3176    171    302    633       N  
ATOM    191  CA  MET A  27      -4.437  29.736  15.929  1.00 23.61           C  
ANISOU  191  CA  MET A  27     2935   2872   3165    186    310    575       C  
ATOM    192  C   MET A  27      -3.484  30.805  16.476  1.00 24.89           C  
ANISOU  192  C   MET A  27     3123   3005   3328    178    342    533       C  
ATOM    193  O   MET A  27      -3.374  30.993  17.686  1.00 23.87           O  
ANISOU  193  O   MET A  27     3038   2829   3203    205    355    506       O  
ATOM    194  CB  MET A  27      -3.801  28.343  15.943  1.00 23.63           C  
ANISOU  194  CB  MET A  27     2978   2874   3127    202    229    500       C  
ATOM    195  CG  MET A  27      -4.841  27.217  15.799  1.00 24.64           C  
ANISOU  195  CG  MET A  27     3166   2974   3221    149    213    541       C  
ATOM    196  SD  MET A  27      -6.387  27.433  16.796  1.00 26.04           S  
ANISOU  196  SD  MET A  27     3350   3163   3381     43    323    587       S  
ATOM    197  CE  MET A  27      -5.744  27.516  18.482  1.00 21.78           C  
ANISOU  197  CE  MET A  27     2991   2503   2781     53    321    567       C  
ATOM    198  N   LYS A  28      -2.772  31.471  15.581  1.00 24.22           N  
ANISOU  198  N   LYS A  28     3034   2960   3210     94    365    512       N  
ATOM    199  CA  LYS A  28      -1.964  32.659  15.968  1.00 26.04           C  
ANISOU  199  CA  LYS A  28     3325   3161   3409      0    425    464       C  
ATOM    200  C   LYS A  28      -2.880  33.752  16.475  1.00 25.59           C  
ANISOU  200  C   LYS A  28     3401   2941   3379     60    440    563       C  
ATOM    201  O   LYS A  28      -2.607  34.365  17.506  1.00 26.48           O  
ANISOU  201  O   LYS A  28     3560   2998   3505     61    472    520       O  
ATOM    202  CB  LYS A  28      -1.162  33.164  14.770  1.00 25.53           C  
ANISOU  202  CB  LYS A  28     3288   3170   3241   -201    480    421       C  
ATOM    203  CG  LYS A  28      -0.390  34.479  14.984  1.00 25.38           C  
ANISOU  203  CG  LYS A  28     3402   3106   3137   -408    571    371       C  
ATOM    204  CD  LYS A  28       0.675  34.716  13.868  1.00 26.67           C  
ANISOU  204  CD  LYS A  28     3560   3435   3140   -722    672    249       C  
ATOM    205  CE  LYS A  28       1.463  35.998  14.132  1.00 28.55           C  
ANISOU  205  CE  LYS A  28     3965   3632   3252  -1023    790    176       C  
ATOM    206  NZ  LYS A  28       2.323  36.261  12.952  1.00 35.99           N  
ANISOU  206  NZ  LYS A  28     4947   4745   3984  -1418    925     60       N  
ATOM    207  N   ASN A  29      -3.969  33.998  15.746  1.00 24.46           N  
ANISOU  207  N   ASN A  29     3313   2739   3243    141    393    663       N  
ATOM    208  CA  ASN A  29      -4.979  34.964  16.183  1.00 26.16           C  
ANISOU  208  CA  ASN A  29     3621   2827   3492    292    356    695       C  
ATOM    209  C   ASN A  29      -5.527  34.596  17.573  1.00 24.98           C  
ANISOU  209  C   ASN A  29     3339   2737   3414    380    399    623       C  
ATOM    210  O   ASN A  29      -5.667  35.462  18.434  1.00 23.81           O  
ANISOU  210  O   ASN A  29     3258   2505   3284    442    418    580       O  
ATOM    211  CB  ASN A  29      -6.117  35.072  15.160  1.00 27.58           C  
ANISOU  211  CB  ASN A  29     3819   2998   3663    435    244    753       C  
ATOM    212  CG  ASN A  29      -5.812  36.041  14.013  1.00 37.61           C  
ANISOU  212  CG  ASN A  29     5390   4093   4805    381    166    846       C  
ATOM    213  OD1 ASN A  29      -6.427  35.958  12.951  1.00 44.17           O  
ANISOU  213  OD1 ASN A  29     6273   4927   5585    458     55    903       O  
ATOM    214  ND2 ASN A  29      -4.896  36.982  14.230  1.00 36.77           N  
ANISOU  214  ND2 ASN A  29     5527   3828   4618    221    220    857       N  
ATOM    215  N   VAL A  30      -5.819  33.315  17.807  1.00 22.79           N  
ANISOU  215  N   VAL A  30     2924   2589   3148    351    419    602       N  
ATOM    216  CA  VAL A  30      -6.289  32.864  19.121  1.00 24.05           C  
ANISOU  216  CA  VAL A  30     3033   2799   3305    341    481    539       C  
ATOM    217  C   VAL A  30      -5.238  33.176  20.185  1.00 24.32           C  
ANISOU  217  C   VAL A  30     3164   2763   3314    299    507    505       C  
ATOM    218  O   VAL A  30      -5.557  33.717  21.243  1.00 26.46           O  
ANISOU  218  O   VAL A  30     3454   3017   3582    323    559    451       O  
ATOM    219  CB  VAL A  30      -6.602  31.322  19.160  1.00 24.52           C  
ANISOU  219  CB  VAL A  30     3060   2942   3314    236    489    540       C  
ATOM    220  CG1 VAL A  30      -6.801  30.831  20.658  1.00 27.11           C  
ANISOU  220  CG1 VAL A  30     3470   3270   3559    138    560    491       C  
ATOM    221  CG2 VAL A  30      -7.851  31.040  18.335  1.00 26.79           C  
ANISOU  221  CG2 VAL A  30     3205   3356   3618    244    488    523       C  
ATOM    222  N   THR A  31      -3.994  32.831  19.904  1.00 21.82           N  
ANISOU  222  N   THR A  31     2876   2443   2970    246    465    494       N  
ATOM    223  CA  THR A  31      -2.897  33.142  20.827  1.00 22.88           C  
ANISOU  223  CA  THR A  31     3057   2564   3073    221    460    413       C  
ATOM    224  C   THR A  31      -2.810  34.650  21.124  1.00 22.68           C  
ANISOU  224  C   THR A  31     3099   2454   3065    198    520    394       C  
ATOM    225  O   THR A  31      -2.570  35.044  22.274  1.00 25.42           O  
ANISOU  225  O   THR A  31     3490   2777   3393    197    544    332       O  
ATOM    226  CB  THR A  31      -1.498  32.646  20.275  1.00 22.49           C  
ANISOU  226  CB  THR A  31     2942   2610   2991    187    393    315       C  
ATOM    227  OG1 THR A  31      -1.556  31.227  20.068  1.00 21.97           O  
ANISOU  227  OG1 THR A  31     2874   2572   2903    259    298    312       O  
ATOM    228  CG2 THR A  31      -0.411  32.927  21.299  1.00 22.44           C  
ANISOU  228  CG2 THR A  31     2931   2650   2945    186    361    174       C  
ATOM    229  N   GLU A  32      -2.976  35.482  20.086  1.00 23.90           N  
ANISOU  229  N   GLU A  32     3321   2534   3228    172    526    448       N  
ATOM    230  CA  GLU A  32      -2.909  36.923  20.230  1.00 24.94           C  
ANISOU  230  CA  GLU A  32     3630   2505   3341    144    550    442       C  
ATOM    231  C   GLU A  32      -4.061  37.560  20.990  1.00 27.99           C  
ANISOU  231  C   GLU A  32     4060   2797   3777    327    541    425       C  
ATOM    232  O   GLU A  32      -4.022  38.750  21.270  1.00 27.21           O  
ANISOU  232  O   GLU A  32     4148   2528   3662    346    537    397       O  
ATOM    233  CB  GLU A  32      -2.717  37.597  18.880  1.00 27.36           C  
ANISOU  233  CB  GLU A  32     4115   2702   3577     39    529    514       C  
ATOM    234  CG  GLU A  32      -1.341  37.234  18.317  1.00 24.61           C  
ANISOU  234  CG  GLU A  32     3699   2505   3147   -217    589    441       C  
ATOM    235  CD  GLU A  32      -1.150  37.573  16.864  1.00 30.00           C  
ANISOU  235  CD  GLU A  32     4543   3144   3713   -393    598    507       C  
ATOM    236  OE1 GLU A  32      -2.137  37.675  16.103  1.00 32.59           O  
ANISOU  236  OE1 GLU A  32     4997   3349   4038   -261    512    640       O  
ATOM    237  OE2 GLU A  32       0.025  37.729  16.489  1.00 31.37           O  
ANISOU  237  OE2 GLU A  32     4707   3438   3773   -685    692    395       O  
ATOM    238  N   LEU A  33      -5.086  36.768  21.343  1.00 29.31           N  
ANISOU  238  N   LEU A  33     4059   3091   3988    441    546    408       N  
ATOM    239  CA  LEU A  33      -6.126  37.261  22.266  1.00 29.36           C  
ANISOU  239  CA  LEU A  33     4018   3113   4025    586    574    303       C  
ATOM    240  C   LEU A  33      -5.533  37.410  23.651  1.00 28.73           C  
ANISOU  240  C   LEU A  33     3976   3033   3906    500    651    230       C  
ATOM    241  O   LEU A  33      -6.155  38.014  24.542  1.00 30.23           O  
ANISOU  241  O   LEU A  33     4156   3229   4103    589    695    113       O  
ATOM    242  CB  LEU A  33      -7.338  36.310  22.308  1.00 30.01           C  
ANISOU  242  CB  LEU A  33     3878   3407   4118    626    606    249       C  
ATOM    243  CG  LEU A  33      -8.101  36.246  20.979  1.00 30.15           C  
ANISOU  243  CG  LEU A  33     3821   3461   4174    751    506    279       C  
ATOM    244  CD1 LEU A  33      -9.256  35.245  21.139  1.00 31.32           C  
ANISOU  244  CD1 LEU A  33     3712   3877   4312    713    571    175       C  
ATOM    245  CD2 LEU A  33      -8.653  37.622  20.516  1.00 34.75           C  
ANISOU  245  CD2 LEU A  33     4517   3896   4791   1022    370    224       C  
ATOM    246  N   ASN A  34      -4.371  36.798  23.850  1.00 25.50           N  
ANISOU  246  N   ASN A  34     3591   2652   3447    352    653    262       N  
ATOM    247  CA  ASN A  34      -3.528  37.082  24.997  1.00 26.07           C  
ANISOU  247  CA  ASN A  34     3728   2713   3465    279    678    185       C  
ATOM    248  C   ASN A  34      -4.089  36.419  26.262  1.00 27.66           C  
ANISOU  248  C   ASN A  34     3907   3007   3595    272    728    136       C  
ATOM    249  O   ASN A  34      -4.019  36.990  27.363  1.00 27.40           O  
ANISOU  249  O   ASN A  34     3932   2959   3518    259    774     48       O  
ATOM    250  CB  ASN A  34      -3.426  38.596  25.212  1.00 27.10           C  
ANISOU  250  CB  ASN A  34     3998   2686   3613    297    701    124       C  
ATOM    251  CG  ASN A  34      -2.012  39.066  25.626  1.00 25.99           C  
ANISOU  251  CG  ASN A  34     3935   2527   3414    128    709     53       C  
ATOM    252  OD1 ASN A  34      -1.123  38.255  25.925  1.00 26.64           O  
ANISOU  252  OD1 ASN A  34     3920   2753   3448     58    676     11       O  
ATOM    253  ND2 ASN A  34      -1.805  40.382  25.591  1.00 25.23           N  
ANISOU  253  ND2 ASN A  34     4029   2253   3306     71    731     12       N  
ATOM    254  N   GLU A  35      -4.650  35.220  26.102  1.00 26.02           N  
ANISOU  254  N   GLU A  35     3655   2886   3345    237    727    188       N  
ATOM    255  CA  GLU A  35      -5.072  34.406  27.249  1.00 26.35           C  
ANISOU  255  CA  GLU A  35     3776   2993   3243    130    780    161       C  
ATOM    256  C   GLU A  35      -4.385  33.054  27.103  1.00 28.17           C  
ANISOU  256  C   GLU A  35     4142   3184   3377     81    658    245       C  
ATOM    257  O   GLU A  35      -3.901  32.748  26.005  1.00 24.69           O  
ANISOU  257  O   GLU A  35     3639   2728   3014    144    571    293       O  
ATOM    258  CB  GLU A  35      -6.589  34.205  27.248  1.00 31.01           C  
ANISOU  258  CB  GLU A  35     4240   3725   3818     76    908     99       C  
ATOM    259  CG  GLU A  35      -7.402  35.490  27.451  1.00 30.14           C  
ANISOU  259  CG  GLU A  35     3976   3679   3796    209    987    -56       C  
ATOM    260  CD  GLU A  35      -7.255  36.101  28.832  1.00 38.32           C  
ANISOU  260  CD  GLU A  35     5090   4719   4750    170   1065   -172       C  
ATOM    261  OE1 GLU A  35      -6.839  35.416  29.796  1.00 37.68           O  
ANISOU  261  OE1 GLU A  35     5176   4642   4500     -5   1091   -144       O  
ATOM    262  OE2 GLU A  35      -7.595  37.288  28.967  1.00 38.35           O  
ANISOU  262  OE2 GLU A  35     5025   4705   4839    332   1081   -304       O  
ATOM    263  N   PRO A  36      -4.354  32.240  28.183  1.00 30.07           N  
ANISOU  263  N   PRO A  36     4504   3395   3526   -539   1040   -184       N  
ATOM    264  CA  PRO A  36      -3.803  30.890  28.010  1.00 29.89           C  
ANISOU  264  CA  PRO A  36     4333   3539   3487   -511    787   -127       C  
ATOM    265  C   PRO A  36      -4.552  30.067  26.944  1.00 28.58           C  
ANISOU  265  C   PRO A  36     4060   3335   3464   -363    706     20       C  
ATOM    266  O   PRO A  36      -5.696  30.377  26.603  1.00 27.85           O  
ANISOU  266  O   PRO A  36     3955   3176   3449   -265    810     89       O  
ATOM    267  CB  PRO A  36      -3.987  30.249  29.393  1.00 32.90           C  
ANISOU  267  CB  PRO A  36     4738   4029   3735   -527    749   -111       C  
ATOM    268  CG  PRO A  36      -4.809  31.214  30.193  1.00 32.26           C  
ANISOU  268  CG  PRO A  36     4785   3841   3630   -572    962   -159       C  
ATOM    269  CD  PRO A  36      -4.603  32.553  29.604  1.00 32.10           C  
ANISOU  269  CD  PRO A  36     4862   3675   3661   -634   1145   -262       C  
ATOM    270  N   LEU A  37      -4.058  28.974  26.410  1.00 25.47           N  
ANISOU  270  N   LEU A  37     3575   3012   3091   -334    540     64       N  
ATOM    271  CA  LEU A  37      -4.726  28.071  25.482  1.00 23.01           C  
ANISOU  271  CA  LEU A  37     3168   2687   2888   -261    484    150       C  
ATOM    272  C   LEU A  37      -5.204  26.838  26.231  1.00 25.68           C  
ANISOU  272  C   LEU A  37     3532   3024   3200   -272    479    209       C  
ATOM    273  O   LEU A  37      -4.539  26.381  27.139  1.00 23.35           O  
ANISOU  273  O   LEU A  37     3320   2763   2790   -267    444    225       O  
ATOM    274  CB  LEU A  37      -3.719  27.647  24.406  1.00 24.37           C  
ANISOU  274  CB  LEU A  37     3275   2892   3091   -246    356    137       C  
ATOM    275  CG  LEU A  37      -3.159  28.703  23.443  1.00 31.67           C  
ANISOU  275  CG  LEU A  37     4193   3794   4048   -244    385     85       C  
ATOM    276  CD1 LEU A  37      -2.050  28.293  22.463  1.00 28.23           C  
ANISOU  276  CD1 LEU A  37     3692   3406   3629   -245    267     58       C  
ATOM    277  CD2 LEU A  37      -4.196  29.702  22.897  1.00 27.69           C  
ANISOU  277  CD2 LEU A  37     3708   3220   3595   -150    533    128       C  
ATOM    278  N   SER A  38      -6.348  26.300  25.822  1.00 25.77           N  
ANISOU  278  N   SER A  38     3473   3023   3296   -284    535    233       N  
ATOM    279  CA  SER A  38      -6.837  25.037  26.361  1.00 26.88           C  
ANISOU  279  CA  SER A  38     3674   3110   3429   -343    597    266       C  
ATOM    280  C   SER A  38      -6.133  23.899  25.633  1.00 27.29           C  
ANISOU  280  C   SER A  38     3755   3109   3507   -341    534    280       C  
ATOM    281  O   SER A  38      -5.633  24.085  24.524  1.00 25.79           O  
ANISOU  281  O   SER A  38     3470   2961   3367   -316    435    248       O  
ATOM    282  CB  SER A  38      -8.351  24.925  26.185  1.00 28.33           C  
ANISOU  282  CB  SER A  38     3737   3347   3681   -420    717    228       C  
ATOM    283  OG  SER A  38      -8.691  24.695  24.829  1.00 26.66           O  
ANISOU  283  OG  SER A  38     3348   3238   3543   -446    670    169       O  
ATOM    284  N   ASN A  39      -6.086  22.723  26.251  1.00 26.66           N  
ANISOU  284  N   ASN A  39     3838   2912   3382   -349    626    339       N  
ATOM    285  CA  ASN A  39      -5.369  21.588  25.646  1.00 28.34           C  
ANISOU  285  CA  ASN A  39     4142   3022   3603   -308    625    370       C  
ATOM    286  C   ASN A  39      -5.637  21.475  24.150  1.00 27.95           C  
ANISOU  286  C   ASN A  39     3936   3004   3678   -408    586    265       C  
ATOM    287  O   ASN A  39      -4.690  21.246  23.366  1.00 27.26           O  
ANISOU  287  O   ASN A  39     3843   2913   3600   -333    491    271       O  
ATOM    288  CB  ASN A  39      -5.646  20.252  26.363  1.00 31.19           C  
ANISOU  288  CB  ASN A  39     4758   3176   3918   -317    841    447       C  
ATOM    289  CG  ASN A  39      -4.899  20.137  27.699  1.00 37.59           C  
ANISOU  289  CG  ASN A  39     5755   3993   4536   -104    844    603       C  
ATOM    290  OD1 ASN A  39      -4.192  21.064  28.115  1.00 40.48           O  
ANISOU  290  OD1 ASN A  39     6020   4562   4801     -1    673    608       O  
ATOM    291  ND2 ASN A  39      -5.121  19.032  28.412  1.00 45.37           N  
ANISOU  291  ND2 ASN A  39     7017   4774   5447    -52   1072    714       N  
ATOM    292  N   GLU A  40      -6.903  21.610  23.765  1.00 27.54           N  
ANISOU  292  N   GLU A  40     3738   3031   3695   -564    659    163       N  
ATOM    293  CA  GLU A  40      -7.262  21.484  22.363  1.00 29.60           C  
ANISOU  293  CA  GLU A  40     3813   3410   4022   -657    619     45       C  
ATOM    294  C   GLU A  40      -6.615  22.613  21.555  1.00 28.88           C  
ANISOU  294  C   GLU A  40     3589   3453   3930   -506    434     70       C  
ATOM    295  O   GLU A  40      -6.079  22.359  20.463  1.00 25.73           O  
ANISOU  295  O   GLU A  40     3143   3076   3555   -498    359     32       O  
ATOM    296  CB  GLU A  40      -8.784  21.467  22.171  1.00 31.40           C  
ANISOU  296  CB  GLU A  40     3841   3821   4269   -836    724    -88       C  
ATOM    297  CG  GLU A  40      -9.179  21.412  20.688  1.00 34.21           C  
ANISOU  297  CG  GLU A  40     3945   4417   4635   -914    657   -230       C  
ATOM    298  CD  GLU A  40     -10.665  21.561  20.428  1.00 43.14           C  
ANISOU  298  CD  GLU A  40     4777   5886   5729  -1048    721   -378       C  
ATOM    299  OE1 GLU A  40     -11.378  22.149  21.263  1.00 43.81           O  
ANISOU  299  OE1 GLU A  40     4805   6049   5791   -999    774   -337       O  
ATOM    300  OE2 GLU A  40     -11.106  21.123  19.340  1.00 46.48           O  
ANISOU  300  OE2 GLU A  40     4991   6546   6122  -1193    712   -551       O  
ATOM    301  N   GLU A  41      -6.592  23.831  22.117  1.00 26.87           N  
ANISOU  301  N   GLU A  41     3319   3248   3642   -397    398    128       N  
ATOM    302  CA  GLU A  41      -6.012  24.993  21.401  1.00 25.33           C  
ANISOU  302  CA  GLU A  41     3062   3120   3442   -273    304    147       C  
ATOM    303  C   GLU A  41      -4.502  24.859  21.196  1.00 24.56           C  
ANISOU  303  C   GLU A  41     3054   2948   3332   -233    209    163       C  
ATOM    304  O   GLU A  41      -3.989  25.161  20.109  1.00 24.53           O  
ANISOU  304  O   GLU A  41     2989   2985   3349   -192    144    144       O  
ATOM    305  CB  GLU A  41      -6.370  26.330  22.098  1.00 23.78           C  
ANISOU  305  CB  GLU A  41     2890   2935   3210   -192    371    184       C  
ATOM    306  CG  GLU A  41      -7.853  26.682  21.975  1.00 23.99           C  
ANISOU  306  CG  GLU A  41     2768   3113   3234   -149    458    181       C  
ATOM    307  CD  GLU A  41      -8.286  27.743  22.974  1.00 26.99           C  
ANISOU  307  CD  GLU A  41     3229   3448   3577    -71    578    225       C  
ATOM    308  OE1 GLU A  41      -7.533  28.045  23.941  1.00 29.75           O  
ANISOU  308  OE1 GLU A  41     3754   3652   3897   -115    601    227       O  
ATOM    309  OE2 GLU A  41      -9.418  28.226  22.835  1.00 26.84           O  
ANISOU  309  OE2 GLU A  41     3084   3577   3538     35    661    245       O  
ATOM    310  N  AARG A  42      -3.916  24.291  22.245  1.00 24.88           N  
ANISOU  310  N  AARG A  42     3223   2914   3317   -231    216    200       N  
ATOM    311  N  BARG A  42      -3.823  24.389  22.240  0.00 24.77           N  
ANISOU  311  N  BARG A  42     3208   2906   3299   -225    209    200       N  
ATOM    312  CA AARG A  42      -2.490  23.989  22.256  1.00 25.68           C  
ANISOU  312  CA AARG A  42     3372   3024   3361   -158    128    219       C  
ATOM    313  CA BARG A  42      -2.417  24.022  22.212  0.00 25.38           C  
ANISOU  313  CA BARG A  42     3330   2991   3322   -155    121    217       C  
ATOM    314  C  AARG A  42      -2.123  23.025  21.132  1.00 23.82           C  
ANISOU  314  C  AARG A  42     3125   2745   3183   -144    100    210       C  
ATOM    315  C  BARG A  42      -2.122  23.045  21.063  0.00 23.74           C  
ANISOU  315  C  BARG A  42     3108   2737   3176   -146     97    207       C  
ATOM    316  O  AARG A  42      -1.128  23.222  20.434  1.00 23.71           O  
ANISOU  316  O  AARG A  42     3058   2785   3164    -93     14    190       O  
ATOM    317  O  BARG A  42      -1.124  23.198  20.364  0.00 23.19           O  
ANISOU  317  O  BARG A  42     2990   2717   3102    -94     13    189       O  
ATOM    318  CB AARG A  42      -2.077  23.402  23.607  1.00 27.40           C  
ANISOU  318  CB AARG A  42     3718   3236   3455    -88    151    290       C  
ATOM    319  CB BARG A  42      -2.063  23.340  23.549  0.00 27.37           C  
ANISOU  319  CB BARG A  42     3715   3228   3455    -86    151    291       C  
ATOM    320  CG AARG A  42      -0.578  23.417  23.858  1.00 30.89           C  
ANISOU  320  CG AARG A  42     4138   3829   3769     30     43    299       C  
ATOM    321  CG BARG A  42      -0.618  23.377  23.968  0.00 28.16           C  
ANISOU  321  CG BARG A  42     3804   3481   3416     34     49    305       C  
ATOM    322  CD AARG A  42      -0.237  22.800  25.204  1.00 38.17           C  
ANISOU  322  CD AARG A  42     5172   4821   4511    170     63    396       C  
ATOM    323  CD BARG A  42      -0.481  23.160  25.479  0.00 30.64           C  
ANISOU  323  CD BARG A  42     4212   3880   3551    124     74    374       C  
ATOM    324  NE AARG A  42      -0.907  21.518  25.404  1.00 40.72           N  
ANISOU  324  NE AARG A  42     5686   4927   4858    232    208    513       N  
ATOM    325  NE BARG A  42      -1.677  23.594  26.216  0.00 33.53           N  
ANISOU  325  NE BARG A  42     4640   4159   3943     14    180    368       N  
ATOM    326  CZ AARG A  42      -1.256  21.035  26.592  1.00 42.45           C  
ANISOU  326  CZ AARG A  42     6070   5101   4958    311    315    615       C  
ATOM    327  CZ BARG A  42      -2.094  23.090  27.372  0.00 34.67           C  
ANISOU  327  CZ BARG A  42     4922   4269   3981     69    270    453       C  
ATOM    328  NH1 ARG A  42      -0.998  21.727  27.693  1.00 47.18           N  
ANISOU  328  NH1 ARG A  42     6634   5901   5391    349    256    612       N  
ATOM    329  NH2AARG A  42      -1.863  19.859  26.679  1.00 35.76           N  
ANISOU  329  NH2AARG A  42     5442   4001   4145    332    513    706       N  
ATOM    330  NH2BARG A  42      -3.195  23.570  27.929  0.00 26.77           N  
ANISOU  330  NH2BARG A  42     3952   3200   3020    -45    372    429       N  
ATOM    331  N   ASN A  43      -2.964  22.017  20.926  1.00 24.10           N  
ANISOU  331  N   ASN A  43     3207   2682   3267   -223    202    196       N  
ATOM    332  CA  ASN A  43      -2.754  20.911  19.977  1.00 25.44           C  
ANISOU  332  CA  ASN A  43     3419   2763   3484   -255    243    158       C  
ATOM    333  C   ASN A  43      -3.015  21.434  18.576  1.00 26.26           C  
ANISOU  333  C   ASN A  43     3338   2998   3641   -316    164     63       C  
ATOM    334  O   ASN A  43      -2.239  21.164  17.667  1.00 25.69           O  
ANISOU  334  O   ASN A  43     3257   2922   3582   -277    112     42       O  
ATOM    335  CB  ASN A  43      -3.695  19.723  20.286  1.00 28.51           C  
ANISOU  335  CB  ASN A  43     3945   2989   3897   -399    449    122       C  
ATOM    336  CG  ASN A  43      -3.282  18.960  21.530  1.00 33.40           C  
ANISOU  336  CG  ASN A  43     4825   3430   4437   -275    575    258       C  
ATOM    337  OD1 ASN A  43      -2.169  19.121  22.026  1.00 36.22           O  
ANISOU  337  OD1 ASN A  43     5228   3834   4700    -54    480    373       O  
ATOM    338  ND2 ASN A  43      -4.152  18.089  22.014  1.00 38.68           N  
ANISOU  338  ND2 ASN A  43     5660   3918   5118   -412    810    238       N  
ATOM    339  N   LEU A  44      -4.041  22.281  18.429  1.00 24.38           N  
ANISOU  339  N   LEU A  44     2952   2904   3408   -363    155     25       N  
ATOM    340  CA  LEU A  44      -4.364  22.863  17.110  1.00 26.07           C  
ANISOU  340  CA  LEU A  44     2987   3300   3619   -348     88    -31       C  
ATOM    341  C   LEU A  44      -3.218  23.780  16.630  1.00 24.80           C  
ANISOU  341  C   LEU A  44     2843   3134   3448   -211     -2     27       C  
ATOM    342  O   LEU A  44      -2.805  23.733  15.468  1.00 24.58           O  
ANISOU  342  O   LEU A  44     2762   3160   3419   -188    -52     -5       O  
ATOM    343  CB  LEU A  44      -5.659  23.669  17.198  1.00 24.69           C  
ANISOU  343  CB  LEU A  44     2656   3318   3408   -329    116    -39       C  
ATOM    344  CG  LEU A  44      -6.920  22.808  17.281  1.00 24.92           C  
ANISOU  344  CG  LEU A  44     2572   3467   3430   -515    209   -162       C  
ATOM    345  CD1 LEU A  44      -8.134  23.656  17.678  1.00 28.13           C  
ANISOU  345  CD1 LEU A  44     2811   4092   3784   -450    245   -146       C  
ATOM    346  CD2 LEU A  44      -7.191  22.122  15.939  1.00 27.11           C  
ANISOU  346  CD2 LEU A  44     2695   3928   3677   -636    189   -314       C  
ATOM    347  N   LEU A  45      -2.717  24.599  17.539  1.00 24.74           N  
ANISOU  347  N   LEU A  45     2911   3068   3420   -154      3     86       N  
ATOM    348  CA  LEU A  45      -1.577  25.479  17.241  1.00 24.30           C  
ANISOU  348  CA  LEU A  45     2883   3003   3348    -99    -28     92       C  
ATOM    349  C   LEU A  45      -0.394  24.647  16.750  1.00 24.11           C  
ANISOU  349  C   LEU A  45     2867   2964   3331    -94    -98     68       C  
ATOM    350  O   LEU A  45       0.225  24.951  15.702  1.00 24.07           O  
ANISOU  350  O   LEU A  45     2823   2989   3333    -71   -124     43       O  
ATOM    351  CB  LEU A  45      -1.156  26.248  18.500  1.00 24.95           C  
ANISOU  351  CB  LEU A  45     3044   3051   3385   -118     13     96       C  
ATOM    352  CG  LEU A  45       0.042  27.192  18.242  1.00 24.64           C  
ANISOU  352  CG  LEU A  45     3024   3022   3316   -146     30     38       C  
ATOM    353  CD1 LEU A  45      -0.307  28.327  17.250  1.00 25.15           C  
ANISOU  353  CD1 LEU A  45     3123   3033   3399    -98    140     56       C  
ATOM    354  CD2 LEU A  45       0.571  27.754  19.517  1.00 24.23           C  
ANISOU  354  CD2 LEU A  45     3018   3001   3186   -228     69    -23       C  
ATOM    355  N   SER A  46      -0.066  23.600  17.507  1.00 22.71           N  
ANISOU  355  N   SER A  46     2756   2736   3135    -83   -103     91       N  
ATOM    356  CA  SER A  46       1.103  22.803  17.198  1.00 22.89           C  
ANISOU  356  CA  SER A  46     2801   2757   3139     -7   -143     96       C  
ATOM    357  C   SER A  46       0.925  22.062  15.866  1.00 23.27           C  
ANISOU  357  C   SER A  46     2838   2754   3248    -35   -128     52       C  
ATOM    358  O   SER A  46       1.861  22.009  15.050  1.00 23.42           O  
ANISOU  358  O   SER A  46     2822   2809   3268     14   -170     30       O  
ATOM    359  CB  SER A  46       1.352  21.783  18.321  1.00 23.10           C  
ANISOU  359  CB  SER A  46     2949   2729   3100     90   -103    176       C  
ATOM    360  OG  SER A  46       2.454  20.964  17.974  1.00 28.26           O  
ANISOU  360  OG  SER A  46     3631   3393   3716    235   -117    208       O  
ATOM    361  N   VAL A  47      -0.253  21.442  15.675  1.00 22.80           N  
ANISOU  361  N   VAL A  47     2800   2639   3225   -139    -53     13       N  
ATOM    362  CA  VAL A  47      -0.568  20.767  14.401  1.00 24.64           C  
ANISOU  362  CA  VAL A  47     3000   2876   3486   -226    -23    -85       C  
ATOM    363  C   VAL A  47      -0.440  21.715  13.175  1.00 24.93           C  
ANISOU  363  C   VAL A  47     2891   3077   3505   -198   -115   -116       C  
ATOM    364  O   VAL A  47       0.195  21.357  12.138  1.00 24.32           O  
ANISOU  364  O   VAL A  47     2807   3005   3427   -185   -133   -161       O  
ATOM    365  CB  VAL A  47      -1.943  20.042  14.440  1.00 24.95           C  
ANISOU  365  CB  VAL A  47     3036   2908   3538   -415     94   -186       C  
ATOM    366  CG1 VAL A  47      -2.421  19.606  12.971  1.00 28.10           C  
ANISOU  366  CG1 VAL A  47     3318   3439   3919   -559    106   -354       C  
ATOM    367  CG2 VAL A  47      -1.871  18.760  15.373  1.00 23.05           C  
ANISOU  367  CG2 VAL A  47     3039   2405   3314   -448    274   -159       C  
ATOM    368  N   ALA A  48      -1.006  22.915  13.317  1.00 23.50           N  
ANISOU  368  N   ALA A  48     2628   3006   3296   -159   -142    -76       N  
ATOM    369  CA  ALA A  48      -1.005  23.912  12.271  1.00 24.76           C  
ANISOU  369  CA  ALA A  48     2706   3292   3408    -76   -173    -61       C  
ATOM    370  C   ALA A  48       0.450  24.226  11.904  1.00 24.86           C  
ANISOU  370  C   ALA A  48     2778   3230   3435    -27   -191    -45       C  
ATOM    371  O   ALA A  48       0.861  24.047  10.735  1.00 23.40           O  
ANISOU  371  O   ALA A  48     2565   3092   3233     -9   -210    -80       O  
ATOM    372  CB  ALA A  48      -1.721  25.159  12.716  1.00 25.18           C  
ANISOU  372  CB  ALA A  48     2742   3401   3423     12   -131     16       C  
ATOM    373  N   TYR A  49       1.244  24.624  12.886  1.00 22.63           N  
ANISOU  373  N   TYR A  49     2556   2876   3167    -24   -181    -19       N  
ATOM    374  CA  TYR A  49       2.575  25.091  12.539  1.00 22.72           C  
ANISOU  374  CA  TYR A  49     2572   2892   3170    -16   -179    -45       C  
ATOM    375  C   TYR A  49       3.507  23.968  12.125  1.00 24.05           C  
ANISOU  375  C   TYR A  49     2719   3068   3350     11   -228    -78       C  
ATOM    376  O   TYR A  49       4.398  24.179  11.287  1.00 24.16           O  
ANISOU  376  O   TYR A  49     2702   3120   3359     21   -225   -114       O  
ATOM    377  CB  TYR A  49       3.189  25.947  13.639  1.00 22.38           C  
ANISOU  377  CB  TYR A  49     2551   2852   3099    -66   -140    -65       C  
ATOM    378  CG  TYR A  49       2.786  27.413  13.508  1.00 26.30           C  
ANISOU  378  CG  TYR A  49     3124   3287   3580    -89     -6    -54       C  
ATOM    379  CD1 TYR A  49       3.440  28.263  12.611  1.00 23.81           C  
ANISOU  379  CD1 TYR A  49     2858   2936   3252   -110    102    -84       C  
ATOM    380  CD2 TYR A  49       1.754  27.941  14.267  1.00 24.43           C  
ANISOU  380  CD2 TYR A  49     2945   3002   3336    -72     56     -6       C  
ATOM    381  CE1 TYR A  49       3.089  29.617  12.507  1.00 22.52           C  
ANISOU  381  CE1 TYR A  49     2844   2648   3063   -101    302    -53       C  
ATOM    382  CE2 TYR A  49       1.428  29.329  14.197  1.00 25.43           C  
ANISOU  382  CE2 TYR A  49     3198   3026   3437    -49    239     22       C  
ATOM    383  CZ  TYR A  49       2.087  30.132  13.315  1.00 23.73           C  
ANISOU  383  CZ  TYR A  49     3072   2739   3205    -56    374      5       C  
ATOM    384  OH  TYR A  49       1.717  31.455  13.180  1.00 26.65           O  
ANISOU  384  OH  TYR A  49     3638   2949   3540      6    622     60       O  
ATOM    385  N   LYS A  50       3.296  22.771  12.673  1.00 22.94           N  
ANISOU  385  N   LYS A  50     2625   2870   3222     35   -236    -60       N  
ATOM    386  CA  LYS A  50       4.101  21.640  12.258  1.00 23.35           C  
ANISOU  386  CA  LYS A  50     2711   2885   3277    110   -228    -69       C  
ATOM    387  C   LYS A  50       3.894  21.363  10.777  1.00 23.35           C  
ANISOU  387  C   LYS A  50     2696   2875   3300     62   -212   -137       C  
ATOM    388  O   LYS A  50       4.858  21.057  10.080  1.00 24.32           O  
ANISOU  388  O   LYS A  50     2809   3011   3419    120   -210   -161       O  
ATOM    389  CB  LYS A  50       3.773  20.387  13.053  1.00 23.05           C  
ANISOU  389  CB  LYS A  50     2807   2712   3238    161   -157    -21       C  
ATOM    390  CG  LYS A  50       4.694  19.189  12.708  1.00 27.91           C  
ANISOU  390  CG  LYS A  50     3518   3246   3840    308    -89      2       C  
ATOM    391  CD  LYS A  50       5.869  18.975  13.684  1.00 39.50           C  
ANISOU  391  CD  LYS A  50     4976   4824   5210    549   -114    105       C  
ATOM    392  CE  LYS A  50       6.791  17.786  13.235  1.00 35.18           C  
ANISOU  392  CE  LYS A  50     4531   4204   4631    774    -17    156       C  
ATOM    393  NZ  LYS A  50       6.105  16.521  13.414  1.00 46.95           N  
ANISOU  393  NZ  LYS A  50     6306   5386   6147    803    189    205       N  
ATOM    394  N   ASN A  51       2.646  21.486  10.308  1.00 21.58           N  
ANISOU  394  N   ASN A  51     2447   2680   3073    -35   -201   -177       N  
ATOM    395  CA  ASN A  51       2.338  21.308   8.903  1.00 23.51           C  
ANISOU  395  CA  ASN A  51     2641   3005   3287    -83   -201   -259       C  
ATOM    396  C   ASN A  51       2.908  22.393   8.003  1.00 22.77           C  
ANISOU  396  C   ASN A  51     2491   3010   3151    -11   -234   -232       C  
ATOM    397  O   ASN A  51       3.489  22.089   6.965  1.00 23.83           O  
ANISOU  397  O   ASN A  51     2623   3165   3267     -1   -227   -280       O  
ATOM    398  CB  ASN A  51       0.816  21.166   8.687  1.00 23.62           C  
ANISOU  398  CB  ASN A  51     2576   3142   3255   -198   -191   -333       C  
ATOM    399  CG  ASN A  51       0.345  19.713   8.850  1.00 29.75           C  
ANISOU  399  CG  ASN A  51     3436   3808   4061   -361    -83   -454       C  
ATOM    400  OD1 ASN A  51       0.538  18.889   7.976  1.00 26.85           O  
ANISOU  400  OD1 ASN A  51     3106   3414   3681   -444    -22   -571       O  
ATOM    401  ND2 ASN A  51      -0.257  19.410   9.983  1.00 32.74           N  
ANISOU  401  ND2 ASN A  51     3873   4092   4474   -421    -19   -434       N  
ATOM    402  N   VAL A  52       2.839  23.643   8.461  1.00 23.57           N  
ANISOU  402  N   VAL A  52     2586   3132   3238     34   -227   -156       N  
ATOM    403  CA  VAL A  52       3.403  24.741   7.697  1.00 23.85           C  
ANISOU  403  CA  VAL A  52     2638   3193   3231     91   -180   -123       C  
ATOM    404  C   VAL A  52       4.925  24.595   7.598  1.00 23.18           C  
ANISOU  404  C   VAL A  52     2558   3065   3183     68   -164   -168       C  
ATOM    405  O   VAL A  52       5.496  24.621   6.493  1.00 25.41           O  
ANISOU  405  O   VAL A  52     2840   3375   3439     86   -136   -195       O  
ATOM    406  CB  VAL A  52       3.010  26.101   8.276  1.00 22.56           C  
ANISOU  406  CB  VAL A  52     2534   2994   3045    130    -97    -43       C  
ATOM    407  CG1 VAL A  52       3.797  27.262   7.593  1.00 23.30           C  
ANISOU  407  CG1 VAL A  52     2723   3027   3102    158     42    -19       C  
ATOM    408  CG2 VAL A  52       1.494  26.302   8.124  1.00 26.08           C  
ANISOU  408  CG2 VAL A  52     2935   3557   3418    223   -107     17       C  
ATOM    409  N   VAL A  53       5.596  24.464   8.736  1.00 19.73           N  
ANISOU  409  N   VAL A  53     2105   2612   2780     41   -179   -182       N  
ATOM    410  CA  VAL A  53       7.039  24.316   8.677  1.00 22.07           C  
ANISOU  410  CA  VAL A  53     2339   2973   3075     41   -174   -241       C  
ATOM    411  C   VAL A  53       7.465  23.017   7.939  1.00 22.84           C  
ANISOU  411  C   VAL A  53     2427   3065   3184    124   -202   -260       C  
ATOM    412  O   VAL A  53       8.461  22.991   7.185  1.00 23.22           O  
ANISOU  412  O   VAL A  53     2427   3173   3222    142   -174   -308       O  
ATOM    413  CB  VAL A  53       7.704  24.436  10.066  1.00 21.53           C  
ANISOU  413  CB  VAL A  53     2200   3001   2980     24   -200   -267       C  
ATOM    414  CG1 VAL A  53       7.667  23.119  10.829  1.00 24.19           C  
ANISOU  414  CG1 VAL A  53     2541   3342   3307    158   -270   -209       C  
ATOM    415  CG2 VAL A  53       9.167  24.905   9.896  1.00 24.60           C  
ANISOU  415  CG2 VAL A  53     2461   3561   3326    -37   -161   -376       C  
ATOM    416  N   GLY A  54       6.677  21.964   8.109  1.00 24.40           N  
ANISOU  416  N   GLY A  54     2693   3176   3403    153   -218   -238       N  
ATOM    417  CA  GLY A  54       6.993  20.655   7.510  1.00 23.85           C  
ANISOU  417  CA  GLY A  54     2683   3034   3346    215   -178   -269       C  
ATOM    418  C   GLY A  54       7.064  20.781   5.975  1.00 25.43           C  
ANISOU  418  C   GLY A  54     2869   3268   3525    169   -156   -338       C  
ATOM    419  O   GLY A  54       7.913  20.157   5.349  1.00 26.24           O  
ANISOU  419  O   GLY A  54     2985   3357   3628    233   -113   -375       O  
ATOM    420  N   ALA A  55       6.097  21.363   5.284  1.00 25.48           N  
ANISOU  420  N   ALA A  55     2860   3332   3488     92   -173   -356       N  
ATOM    421  CA  ALA A  55       6.123  21.167   3.818  1.00 27.38           C  
ANISOU  421  CA  ALA A  55     3099   3635   3669     74   -150   -428       C  
ATOM    422  C   ALA A  55       7.482  21.605   3.253  1.00 25.62           C  
ANISOU  422  C   ALA A  55     2856   3432   3448    134   -112   -423       C  
ATOM    423  O   ALA A  55       8.141  20.941   2.454  1.00 25.48           O  
ANISOU  423  O   ALA A  55     2855   3403   3423    158    -69   -485       O  
ATOM    424  CB  ALA A  55       4.994  21.939   3.156  1.00 27.68           C  
ANISOU  424  CB  ALA A  55     3087   3829   3600     58   -182   -417       C  
ATOM    425  N   ARG A  56       7.816  22.809   3.716  1.00 28.29           N  
ANISOU  425  N   ARG A  56     2910   4489   3349    280   -390   -224       N  
ATOM    426  CA  ARG A  56       9.057  23.491   3.434  1.00 28.42           C  
ANISOU  426  CA  ARG A  56     3106   4375   3319    310   -383   -116       C  
ATOM    427  C   ARG A  56      10.187  22.703   4.050  1.00 27.03           C  
ANISOU  427  C   ARG A  56     2966   4110   3195    175   -368   -117       C  
ATOM    428  O   ARG A  56      11.212  22.498   3.399  1.00 24.63           O  
ANISOU  428  O   ARG A  56     2656   3854   2850    177   -381   -103       O  
ATOM    429  CB  ARG A  56       9.032  24.910   4.003  1.00 28.14           C  
ANISOU  429  CB  ARG A  56     3275   4208   3209    392   -306    -15       C  
ATOM    430  CG  ARG A  56       8.035  25.834   3.322  1.00 36.92           C  
ANISOU  430  CG  ARG A  56     4448   5396   4184    693   -309     25       C  
ATOM    431  CD  ARG A  56       7.642  26.988   4.229  1.00 36.95           C  
ANISOU  431  CD  ARG A  56     4720   5221   4098    841   -179    107       C  
ATOM    432  NE  ARG A  56       6.650  27.860   3.607  1.00 34.31           N  
ANISOU  432  NE  ARG A  56     4485   4978   3573   1285   -173    163       N  
ATOM    433  CZ  ARG A  56       5.336  27.699   3.725  1.00 36.98           C  
ANISOU  433  CZ  ARG A  56     4505   5634   3914   1570   -212    111       C  
ATOM    434  NH1 ARG A  56       4.850  26.696   4.444  1.00 32.51           N  
ANISOU  434  NH1 ARG A  56     3553   5262   3537   1346   -221    -14       N  
ATOM    435  NH2 ARG A  56       4.506  28.540   3.124  1.00 40.08           N  
ANISOU  435  NH2 ARG A  56     4974   6181   4074   2091   -229    177       N  
ATOM    436  N   ARG A  57      10.032  22.231   5.288  1.00 25.02           N  
ANISOU  436  N   ARG A  57     2753   3758   2997    103   -333   -134       N  
ATOM    437  CA  ARG A  57      11.110  21.347   5.741  1.00 26.45           C  
ANISOU  437  CA  ARG A  57     2992   3899   3160    102   -349   -126       C  
ATOM    438  C   ARG A  57      11.382  20.214   4.724  1.00 27.86           C  
ANISOU  438  C   ARG A  57     3179   4107   3298    178   -353   -184       C  
ATOM    439  O   ARG A  57      12.436  19.579   4.745  1.00 27.42           O  
ANISOU  439  O   ARG A  57     3165   4076   3178    312   -358   -161       O  
ATOM    440  CB  ARG A  57      10.779  20.756   7.112  1.00 25.00           C  
ANISOU  440  CB  ARG A  57     2957   3557   2985     54   -302   -141       C  
ATOM    441  CG  ARG A  57      11.276  21.588   8.283  1.00 26.37           C  
ANISOU  441  CG  ARG A  57     3196   3697   3126     10   -319    -68       C  
ATOM    442  CD  ARG A  57      10.924  20.938   9.611  1.00 23.94           C  
ANISOU  442  CD  ARG A  57     3099   3204   2791    -18   -265    -80       C  
ATOM    443  NE  ARG A  57      11.905  19.930  10.004  1.00 25.24           N  
ANISOU  443  NE  ARG A  57     3392   3359   2838    140   -329    -55       N  
ATOM    444  CZ  ARG A  57      11.597  18.774  10.583  1.00 27.47           C  
ANISOU  444  CZ  ARG A  57     3984   3416   3038    196   -248    -82       C  
ATOM    445  NH1 ARG A  57      10.331  18.475  10.840  1.00 23.03           N  
ANISOU  445  NH1 ARG A  57     3567   2663   2522    -12    -83   -164       N  
ATOM    446  NH2 ARG A  57      12.555  17.916  10.905  1.00 25.39           N  
ANISOU  446  NH2 ARG A  57     3904   3140   2602    472   -309    -32       N  
ATOM    447  N   SER A  58      10.409  19.986   3.844  1.00 29.51           N  
ANISOU  447  N   SER A  58     3354   4352   3507    118   -351   -267       N  
ATOM    448  CA  SER A  58      10.414  18.985   2.797  1.00 28.61           C  
ANISOU  448  CA  SER A  58     3324   4233   3313    115   -338   -351       C  
ATOM    449  C   SER A  58      10.947  19.624   1.473  1.00 29.81           C  
ANISOU  449  C   SER A  58     3379   4528   3418    217   -389   -311       C  
ATOM    450  O   SER A  58      11.864  19.099   0.828  1.00 27.83           O  
ANISOU  450  O   SER A  58     3202   4276   3097    323   -351   -306       O  
ATOM    451  CB  SER A  58       8.991  18.430   2.614  1.00 29.49           C  
ANISOU  451  CB  SER A  58     3425   4384   3395   -116   -318   -501       C  
ATOM    452  OG  SER A  58       8.957  17.504   1.535  1.00 29.77           O  
ANISOU  452  OG  SER A  58     3607   4403   3302   -198   -302   -607       O  
ATOM    453  N   SER A  59      10.427  20.802   1.136  1.00 27.44           N  
ANISOU  453  N   SER A  59     2970   4335   3121    230   -443   -271       N  
ATOM    454  CA  SER A  59      10.845  21.481  -0.077  1.00 27.18           C  
ANISOU  454  CA  SER A  59     2960   4377   2991    313   -459   -228       C  
ATOM    455  C   SER A  59      12.362  21.808  -0.033  1.00 28.12           C  
ANISOU  455  C   SER A  59     3095   4498   3092    311   -374   -155       C  
ATOM    456  O   SER A  59      13.052  21.692  -1.054  1.00 28.58           O  
ANISOU  456  O   SER A  59     3179   4618   3062    346   -325   -160       O  
ATOM    457  CB  SER A  59      10.032  22.755  -0.261  1.00 27.69           C  
ANISOU  457  CB  SER A  59     3035   4493   2995    411   -504   -172       C  
ATOM    458  OG  SER A  59       8.646  22.463  -0.406  1.00 27.93           O  
ANISOU  458  OG  SER A  59     2913   4695   3003    449   -601   -261       O  
ATOM    459  N   TRP A  60      12.845  22.253   1.120  1.00 28.43           N  
ANISOU  459  N   TRP A  60     3094   4524   3182    242   -351   -105       N  
ATOM    460  CA  TRP A  60      14.245  22.601   1.301  1.00 28.67           C  
ANISOU  460  CA  TRP A  60     3033   4700   3159    162   -289    -74       C  
ATOM    461  C   TRP A  60      15.149  21.394   1.084  1.00 30.77           C  
ANISOU  461  C   TRP A  60     3171   5116   3404    330   -273   -107       C  
ATOM    462  O   TRP A  60      16.214  21.504   0.458  1.00 31.23           O  
ANISOU  462  O   TRP A  60     3091   5400   3376    333   -194   -113       O  
ATOM    463  CB  TRP A  60      14.447  23.243   2.673  1.00 30.13           C  
ANISOU  463  CB  TRP A  60     3212   4876   3361     17   -301    -41       C  
ATOM    464  CG  TRP A  60      15.862  23.712   2.934  1.00 31.90           C  
ANISOU  464  CG  TRP A  60     3270   5371   3478   -173   -258    -47       C  
ATOM    465  CD1 TRP A  60      16.350  24.971   2.768  1.00 33.62           C  
ANISOU  465  CD1 TRP A  60     3586   5626   3560   -494   -150    -48       C  
ATOM    466  CD2 TRP A  60      16.933  22.931   3.480  1.00 36.08           C  
ANISOU  466  CD2 TRP A  60     3514   6220   3976    -72   -315    -70       C  
ATOM    467  NE1 TRP A  60      17.669  25.027   3.168  1.00 32.12           N  
ANISOU  467  NE1 TRP A  60     3104   5832   3267   -703   -139   -101       N  
ATOM    468  CE2 TRP A  60      18.051  23.780   3.600  1.00 35.74           C  
ANISOU  468  CE2 TRP A  60     3272   6517   3790   -385   -264   -107       C  
ATOM    469  CE3 TRP A  60      17.050  21.597   3.896  1.00 33.30           C  
ANISOU  469  CE3 TRP A  60     3101   5905   3648    272   -391    -66       C  
ATOM    470  CZ2 TRP A  60      19.285  23.322   4.073  1.00 37.45           C  
ANISOU  470  CZ2 TRP A  60     3080   7246   3905   -324   -329   -150       C  
ATOM    471  CZ3 TRP A  60      18.265  21.151   4.368  1.00 38.08           C  
ANISOU  471  CZ3 TRP A  60     3415   6918   4135    436   -446    -74       C  
ATOM    472  CH2 TRP A  60      19.369  22.005   4.445  1.00 40.13           C  
ANISOU  472  CH2 TRP A  60     3331   7646   4270    160   -437   -119       C  
ATOM    473  N   ARG A  61      14.713  20.226   1.552  1.00 29.60           N  
ANISOU  473  N   ARG A  61     3118   4837   3293    483   -307   -136       N  
ATOM    474  CA  ARG A  61      15.521  19.015   1.410  1.00 29.37           C  
ANISOU  474  CA  ARG A  61     3116   4870   3176    758   -259   -150       C  
ATOM    475  C   ARG A  61      15.599  18.660  -0.042  1.00 30.69           C  
ANISOU  475  C   ARG A  61     3364   5029   3266    824   -177   -193       C  
ATOM    476  O   ARG A  61      16.662  18.338  -0.530  1.00 29.71           O  
ANISOU  476  O   ARG A  61     3141   5103   3045   1026    -91   -188       O  
ATOM    477  CB  ARG A  61      14.970  17.851   2.235  1.00 28.80           C  
ANISOU  477  CB  ARG A  61     3326   4534   3081    882   -258   -171       C  
ATOM    478  CG  ARG A  61      15.098  18.125   3.755  1.00 31.98           C  
ANISOU  478  CG  ARG A  61     3681   4956   3513    872   -332   -117       C  
ATOM    479  CD  ARG A  61      14.904  16.884   4.602  1.00 38.77           C  
ANISOU  479  CD  ARG A  61     4909   5555   4268   1072   -290   -119       C  
ATOM    480  NE  ARG A  61      13.565  16.347   4.417  1.00 46.46           N  
ANISOU  480  NE  ARG A  61     6191   6195   5268    830   -202   -211       N  
ATOM    481  CZ  ARG A  61      12.526  16.588   5.228  1.00 52.30           C  
ANISOU  481  CZ  ARG A  61     6991   6794   6088    562   -192   -245       C  
ATOM    482  NH1 ARG A  61      12.670  17.367   6.303  1.00 45.89           N  
ANISOU  482  NH1 ARG A  61     6041   6056   5340    535   -263   -176       N  
ATOM    483  NH2 ARG A  61      11.325  16.059   4.948  1.00 50.64           N  
ANISOU  483  NH2 ARG A  61     6964   6411   5866    282    -96   -369       N  
ATOM    484  N   VAL A  62      14.483  18.782  -0.757  1.00 28.93           N  
ANISOU  484  N   VAL A  62     3291   4644   3059    664   -207   -243       N  
ATOM    485  CA  VAL A  62      14.477  18.487  -2.177  1.00 30.17           C  
ANISOU  485  CA  VAL A  62     3573   4787   3104    695   -151   -292       C  
ATOM    486  C   VAL A  62      15.387  19.412  -2.990  1.00 30.85           C  
ANISOU  486  C   VAL A  62     3513   5076   3133    682    -74   -247       C  
ATOM    487  O   VAL A  62      16.133  18.942  -3.841  1.00 30.94           O  
ANISOU  487  O   VAL A  62     3561   5161   3032    821     49   -269       O  
ATOM    488  CB  VAL A  62      13.031  18.545  -2.751  1.00 30.15           C  
ANISOU  488  CB  VAL A  62     3687   4687   3080    510   -253   -369       C  
ATOM    489  CG1 VAL A  62      13.064  18.491  -4.269  1.00 32.73           C  
ANISOU  489  CG1 VAL A  62     4146   5039   3249    524   -230   -412       C  
ATOM    490  CG2 VAL A  62      12.209  17.401  -2.177  1.00 32.17           C  
ANISOU  490  CG2 VAL A  62     4130   4771   3324    407   -252   -470       C  
ATOM    491  N   ILE A  63      15.243  20.726  -2.811  1.00 29.14           N  
ANISOU  491  N   ILE A  63     3217   4908   2949    498   -106   -195       N  
ATOM    492  CA  ILE A  63      16.049  21.697  -3.568  1.00 29.63           C  
ANISOU  492  CA  ILE A  63     3259   5100   2899    374     24   -168       C  
ATOM    493  C   ILE A  63      17.531  21.619  -3.136  1.00 33.77           C  
ANISOU  493  C   ILE A  63     3473   5956   3401    359    146   -177       C  
ATOM    494  O   ILE A  63      18.446  21.681  -3.973  1.00 35.24           O  
ANISOU  494  O   ILE A  63     3570   6351   3469    340    315   -205       O  
ATOM    495  CB  ILE A  63      15.467  23.132  -3.421  1.00 29.38           C  
ANISOU  495  CB  ILE A  63     3392   4942   2828    187      3   -110       C  
ATOM    496  CG1 ILE A  63      14.002  23.181  -3.959  1.00 27.26           C  
ANISOU  496  CG1 ILE A  63     3330   4502   2527    324   -143   -106       C  
ATOM    497  CG2 ILE A  63      16.305  24.146  -4.193  1.00 30.23           C  
ANISOU  497  CG2 ILE A  63     3635   5100   2751    -23    201    -94       C  
ATOM    498  CD1 ILE A  63      13.829  22.691  -5.373  1.00 29.54           C  
ANISOU  498  CD1 ILE A  63     3760   4789   2673    423   -148   -150       C  
ATOM    499  N   SER A  64      17.783  21.365  -1.860  1.00 33.76           N  
ANISOU  499  N   SER A  64     3275   6069   3482    404     62   -166       N  
ATOM    500  CA  SER A  64      19.175  21.177  -1.415  1.00 38.55           C  
ANISOU  500  CA  SER A  64     3493   7134   4022    467    124   -188       C  
ATOM    501  C   SER A  64      19.818  19.980  -2.105  1.00 40.24           C  
ANISOU  501  C   SER A  64     3639   7500   4149    880    223   -212       C  
ATOM    502  O   SER A  64      20.968  20.025  -2.521  1.00 44.89           O  
ANISOU  502  O   SER A  64     3906   8528   4623    929    366   -249       O  
ATOM    503  CB  SER A  64      19.243  20.996   0.101  1.00 39.17           C  
ANISOU  503  CB  SER A  64     3426   7302   4154    526    -29   -164       C  
ATOM    504  OG  SER A  64      19.002  22.232   0.735  1.00 41.79           O  
ANISOU  504  OG  SER A  64     3791   7586   4504    115    -61   -156       O  
ATOM    505  N   SER A  65      19.039  18.919  -2.280  1.00 39.29           N  
ANISOU  505  N   SER A  65     3863   7016   4049   1149    184   -206       N  
ATOM    506  CA  SER A  65      19.532  17.731  -2.938  1.00 41.33           C  
ANISOU  506  CA  SER A  65     4245   7285   4173   1568    315   -227       C  
ATOM    507  C   SER A  65      19.832  17.962  -4.429  1.00 42.23           C  
ANISOU  507  C   SER A  65     4411   7447   4186   1497    496   -268       C  
ATOM    508  O   SER A  65      20.857  17.467  -4.963  1.00 42.27           O  
ANISOU  508  O   SER A  65     4272   7738   4050   1803    680   -288       O  
ATOM    509  CB  SER A  65      18.538  16.590  -2.765  1.00 40.66           C  
ANISOU  509  CB  SER A  65     4661   6716   4072   1729    272   -240       C  
ATOM    510  OG  SER A  65      19.036  15.471  -3.452  1.00 47.14           O  
ANISOU  510  OG  SER A  65     5742   7468   4701   2134    446   -262       O  
ATOM    511  N   ILE A  66      18.941  18.693  -5.099  1.00 39.58           N  
ANISOU  511  N   ILE A  66     4297   6855   3886   1155    451   -278       N  
ATOM    512  CA  ILE A  66      19.165  19.075  -6.508  1.00 41.19           C  
ANISOU  512  CA  ILE A  66     4627   7068   3956   1051    613   -307       C  
ATOM    513  C   ILE A  66      20.411  19.926  -6.591  1.00 44.28           C  
ANISOU  513  C   ILE A  66     4634   7906   4285    878    798   -316       C  
ATOM    514  O   ILE A  66      21.247  19.762  -7.498  1.00 43.75           O  
ANISOU  514  O   ILE A  66     4494   8056   4073    961   1032   -357       O  
ATOM    515  CB  ILE A  66      17.964  19.879  -7.092  1.00 38.80           C  
ANISOU  515  CB  ILE A  66     4634   6461   3646    773    490   -296       C  
ATOM    516  CG1 ILE A  66      16.759  18.940  -7.244  1.00 41.24           C  
ANISOU  516  CG1 ILE A  66     5247   6467   3954    866    331   -341       C  
ATOM    517  CG2 ILE A  66      18.354  20.540  -8.469  1.00 37.57           C  
ANISOU  517  CG2 ILE A  66     4650   6327   3298    643    675   -305       C  
ATOM    518  CD1 ILE A  66      15.412  19.639  -7.497  1.00 41.84           C  
ANISOU  518  CD1 ILE A  66     5475   6399   4023    680    129   -339       C  
ATOM    519  N   GLU A  67      20.531  20.851  -5.640  1.00 44.40           N  
ANISOU  519  N   GLU A  67     4418   8075   4378    584    719   -297       N  
ATOM    520  CA  GLU A  67      21.736  21.675  -5.537  1.00 50.36           C  
ANISOU  520  CA  GLU A  67     4775   9326   5034    275    899   -348       C  
ATOM    521  C   GLU A  67      23.044  20.869  -5.480  1.00 54.19           C  
ANISOU  521  C   GLU A  67     4739  10418   5434    604   1029   -404       C  
ATOM    522  O   GLU A  67      23.954  21.092  -6.288  1.00 58.37           O  
ANISOU  522  O   GLU A  67     5047  11318   5811    491   1295   -476       O  
ATOM    523  CB  GLU A  67      21.619  22.628  -4.359  1.00 49.62           C  
ANISOU  523  CB  GLU A  67     4576   9277   5000    -97    776   -337       C  
ATOM    524  CG  GLU A  67      22.827  23.517  -4.178  1.00 58.02           C  
ANISOU  524  CG  GLU A  67     5252  10884   5911   -573    963   -432       C  
ATOM    525  CD  GLU A  67      22.577  24.540  -3.105  1.00 60.92           C  
ANISOU  525  CD  GLU A  67     5702  11165   6281  -1018    866   -431       C  
ATOM    526  OE1 GLU A  67      21.768  24.248  -2.195  1.00 63.67           O  
ANISOU  526  OE1 GLU A  67     6171  11237   6786   -800    622   -357       O  
ATOM    527  OE2 GLU A  67      23.167  25.636  -3.171  1.00 63.18           O  
ANISOU  527  OE2 GLU A  67     5997  11626   6380  -1620   1066   -514       O  
ATOM    528  N   GLN A  68      23.111  19.909  -4.559  1.00 55.43           N  
ANISOU  528  N   GLN A  68     4736  10678   5648   1061    864   -370       N  
ATOM    529  CA  GLN A  68      24.276  19.030  -4.400  1.00 59.14           C  
ANISOU  529  CA  GLN A  68     4749  11736   5985   1582    951   -397       C  
ATOM    530  C   GLN A  68      24.565  18.148  -5.649  1.00 61.87           C  
ANISOU  530  C   GLN A  68     5299  12014   6196   2016   1199   -411       C  
ATOM    531  O   GLN A  68      25.714  18.054  -6.106  1.00 66.39           O  
ANISOU  531  O   GLN A  68     5418  13197   6609   2193   1427   -474       O  
ATOM    532  CB  GLN A  68      24.139  18.183  -3.120  1.00 59.10           C  
ANISOU  532  CB  GLN A  68     4730  11717   6008   2055    714   -328       C  
ATOM    533  N   LYS A  69      23.525  17.536  -6.214  1.00 58.59           N  
ANISOU  533  N   LYS A  69     5547  10902   5811   2142   1172   -372       N  
ATOM    534  CA  LYS A  69      23.641  16.806  -7.483  1.00 60.98           C  
ANISOU  534  CA  LYS A  69     6194  11021   5954   2435   1412   -398       C  
ATOM    535  C   LYS A  69      23.993  17.721  -8.663  1.00 61.03           C  
ANISOU  535  C   LYS A  69     6134  11171   5885   2011   1643   -459       C  
ATOM    536  O   LYS A  69      24.812  17.360  -9.481  1.00 64.40           O  
ANISOU  536  O   LYS A  69     6460  11870   6140   2258   1929   -505       O  
ATOM    537  CB  LYS A  69      22.367  15.991  -7.772  1.00 57.98           C  
ANISOU  537  CB  LYS A  69     6564   9888   5580   2518   1307   -380       C  
ATOM    538  N   THR A  70      23.398  18.917  -8.728  1.00 57.70           N  
ANISOU  538  N   THR A  70     5818  10556   5549   1406   1552   -455       N  
ATOM    539  CA  THR A  70      23.594  19.846  -9.876  1.00 57.33           C  
ANISOU  539  CA  THR A  70     5915  10499   5367    980   1788   -498       C  
ATOM    540  C   THR A  70      24.978  20.525  -9.893  1.00 61.25           C  
ANISOU  540  C   THR A  70     5817  11709   5747    694   2079   -589       C  
ATOM    541  O   THR A  70      25.589  20.696 -10.953  1.00 64.42           O  
ANISOU  541  O   THR A  70     6238  12274   5966    581   2409   -653       O  
ATOM    542  CB  THR A  70      22.474  20.937  -9.911  1.00 52.93           C  
ANISOU  542  CB  THR A  70     5785   9464   4862    518   1612   -447       C  
ATOM    543  N   SER A  71      25.475  20.897  -8.713  1.00 84.10           N  
ANISOU  543  N   SER A  71    11949  13496   6507   2645   -842   -433       N  
ATOM    544  CA  SER A  71      26.738  21.625  -8.594  1.00 87.73           C  
ANISOU  544  CA  SER A  71    11255  14233   7846   3217  -2081  -1618       C  
ATOM    545  C   SER A  71      27.937  20.681  -8.590  1.00 96.06           C  
ANISOU  545  C   SER A  71    12296  15131   9072   4275  -3343  -2721       C  
ATOM    546  O   SER A  71      28.395  20.239  -9.643  1.00 92.14           O  
ANISOU  546  O   SER A  71    10661  14908   9441   3654  -3014  -2922       O  
ATOM    547  N   ASN A  75      25.321  24.802 -16.692  1.00 84.76           N  
ANISOU  547  N   ASN A  75    11022  12973   8208   -286   3657    400       N  
ATOM    548  CA  ASN A  75      25.812  24.513 -15.367  1.00 79.94           C  
ANISOU  548  CA  ASN A  75     8871  12980   8524   -575   3080    -33       C  
ATOM    549  C   ASN A  75      25.610  25.719 -14.518  1.00 80.80           C  
ANISOU  549  C   ASN A  75     8787  13113   8801   -618   3074   -146       C  
ATOM    550  O   ASN A  75      25.054  25.657 -13.440  1.00 75.68           O  
ANISOU  550  O   ASN A  75     7730  13004   8022   -403   2182    -33       O  
ATOM    551  CB  ASN A  75      27.283  24.218 -15.414  1.00 86.24           C  
ANISOU  551  CB  ASN A  75     8780  13425  10562   -989   3727   -982       C  
ATOM    552  CG  ASN A  75      27.730  23.439 -14.243  1.00 85.44           C  
ANISOU  552  CG  ASN A  75     7582  13914  10969   -620   2412  -1587       C  
ATOM    553  OD1 ASN A  75      27.024  23.351 -13.260  1.00 78.63           O  
ANISOU  553  OD1 ASN A  75     6937  13492   9447   -179   1456  -1187       O  
ATOM    554  ND2 ASN A  75      28.899  22.864 -14.333  1.00 93.57           N  
ANISOU  554  ND2 ASN A  75     7694  14753  13104   -641   2395  -2698       N  
ATOM    555  N   GLU A  76      26.059  26.851 -15.006  1.00 86.59           N  
ANISOU  555  N   GLU A  76    10081  13039   9782   -921   4364   -389       N  
ATOM    556  CA  GLU A  76      25.927  28.021 -14.185  1.00 86.84           C  
ANISOU  556  CA  GLU A  76     9836  13077  10083  -1005   4410   -571       C  
ATOM    557  C   GLU A  76      24.986  29.061 -14.730  1.00 88.25           C  
ANISOU  557  C   GLU A  76    11631  12793   9109   -649   4773     78       C  
ATOM    558  O   GLU A  76      24.275  29.702 -13.979  1.00 84.22           O  
ANISOU  558  O   GLU A  76    10921  12702   8377   -446   4080    257       O  
ATOM    559  CB  GLU A  76      27.312  28.598 -13.892  1.00 96.88           C  
ANISOU  559  CB  GLU A  76     9982  13736  13092  -1639   5541  -1913       C  
ATOM    560  N   LYS A  78      21.840  28.148 -14.021  1.00 61.79           N  
ANISOU  560  N   LYS A  78     7866  11066   4545    590   1584    661       N  
ATOM    561  CA  LYS A  78      21.162  27.033 -13.391  1.00 58.59           C  
ANISOU  561  CA  LYS A  78     6482  11212   4569    472    983    483       C  
ATOM    562  C   LYS A  78      21.551  26.982 -11.929  1.00 54.58           C  
ANISOU  562  C   LYS A  78     5386  10915   4436     47   1157    559       C  
ATOM    563  O   LYS A  78      20.742  27.220 -11.056  1.00 54.62           O  
ANISOU  563  O   LYS A  78     5204  10991   4558     -1   1100    469       O  
ATOM    564  CB  LYS A  78      21.501  25.730 -14.078  1.00 58.60           C  
ANISOU  564  CB  LYS A  78     6445  11228   4593    456    970    473       C  
ATOM    565  CG  LYS A  78      20.345  24.763 -14.160  1.00 62.30           C  
ANISOU  565  CG  LYS A  78     6346  11880   5447    603    485    -42       C  
ATOM    566  CD  LYS A  78      20.594  23.684 -15.185  1.00 63.75           C  
ANISOU  566  CD  LYS A  78     6694  12009   5520    794    331   -119       C  
ATOM    567  CE  LYS A  78      19.358  22.981 -15.615  1.00 73.25           C  
ANISOU  567  CE  LYS A  78     7228  13245   7358   1157   -297  -1122       C  
ATOM    568  NZ  LYS A  78      18.977  23.382 -16.992  1.00 82.32           N  
ANISOU  568  NZ  LYS A  78     9262  14143   7873   2401  -1425  -1652       N  
ATOM    569  N   ILE A  79      22.812  26.710 -11.671  1.00 53.56           N  
ANISOU  569  N   ILE A  79     5097  10733   4519    -87   1314    495       N  
ATOM    570  CA  ILE A  79      23.291  26.729 -10.290  1.00 53.84           C  
ANISOU  570  CA  ILE A  79     4975  10810   4671     69    987    270       C  
ATOM    571  C   ILE A  79      22.818  28.001  -9.572  1.00 53.21           C  
ANISOU  571  C   ILE A  79     4903  10744   4571     59   1001    303       C  
ATOM    572  O   ILE A  79      22.296  27.922  -8.459  1.00 52.64           O  
ANISOU  572  O   ILE A  79     5214  10607   4179    257    852    388       O  
ATOM    573  CB  ILE A  79      24.836  26.565 -10.203  1.00 58.26           C  
ANISOU  573  CB  ILE A  79     4997  11257   5883    238    734   -497       C  
ATOM    574  CG2 ILE A  79      25.326  26.735  -8.764  1.00 62.15           C  
ANISOU  574  CG2 ILE A  79     5533  11696   6387    958   -189  -1134       C  
ATOM    575  N   GLU A  80      22.965  29.159 -10.218  1.00 52.81           N  
ANISOU  575  N   GLU A  80     4778  10559   4727   -143   1418    258       N  
ATOM    576  CA  GLU A  80      22.459  30.418  -9.644  1.00 53.80           C  
ANISOU  576  CA  GLU A  80     4964  10684   4794   -147   1452    318       C  
ATOM    577  C   GLU A  80      20.978  30.321  -9.241  1.00 51.71           C  
ANISOU  577  C   GLU A  80     4858  10603   4187    -40   1181    560       C  
ATOM    578  O   GLU A  80      20.584  30.739  -8.145  1.00 48.36           O  
ANISOU  578  O   GLU A  80     4430  10196   3748    -35   1137    556       O  
ATOM    579  CB  GLU A  80      22.670  31.573 -10.631  1.00 58.66           C  
ANISOU  579  CB  GLU A  80     6110  10804   5374   -277   2247    321       C  
ATOM    580  N   MET A  81      20.167  29.764 -10.135  1.00 53.81           N  
ANISOU  580  N   MET A  81     5182  10879   4383     84   1051    484       N  
ATOM    581  CA  MET A  81      18.743  29.595  -9.878  1.00 57.24           C  
ANISOU  581  CA  MET A  81     5228  11334   5187    115    916     23       C  
ATOM    582  C   MET A  81      18.512  28.679  -8.681  1.00 59.85           C  
ANISOU  582  C   MET A  81     5549  11418   5774   -301   1618    -11       C  
ATOM    583  O   MET A  81      17.943  29.094  -7.671  1.00 58.52           O  
ANISOU  583  O   MET A  81     5483  10997   5755   -483   2091   -128       O  
ATOM    584  CB  MET A  81      18.037  29.033 -11.114  1.00 62.10           C  
ANISOU  584  CB  MET A  81     5660  11930   6005    555    366   -598       C  
ATOM    585  CG  MET A  81      16.531  28.899 -10.962  1.00 71.23           C  
ANISOU  585  CG  MET A  81     5824  13004   8237    647    124  -1856       C  
ATOM    586  SD  MET A  81      15.651  30.416 -11.381  1.00 80.72           S  
ANISOU  586  SD  MET A  81     7127  14199   9343   1646  -1078  -2627       S  
ATOM    587  CE  MET A  81      17.019  31.551 -11.601  1.00 74.22           C  
ANISOU  587  CE  MET A  81     8003  13269   6928   1788   -786  -1111       C  
ATOM    588  N   VAL A  82      18.957  27.433  -8.801  1.00 33.32           N  
ANISOU  588  N   VAL A  82     3235   5919   3505    -20    734    391       N  
ATOM    589  CA  VAL A  82      18.814  26.464  -7.721  1.00 36.07           C  
ANISOU  589  CA  VAL A  82     3543   6232   3931     87    628    302       C  
ATOM    590  C   VAL A  82      19.158  27.101  -6.379  1.00 36.86           C  
ANISOU  590  C   VAL A  82     3600   6302   4105    -51    630    287       C  
ATOM    591  O   VAL A  82      18.352  27.087  -5.449  1.00 35.84           O  
ANISOU  591  O   VAL A  82     3559   5985   4074    -36    566    292       O  
ATOM    592  CB  VAL A  82      19.714  25.234  -7.942  1.00 36.68           C  
ANISOU  592  CB  VAL A  82     3508   6514   3915    267    611    210       C  
ATOM    593  CG1 VAL A  82      19.469  24.196  -6.858  1.00 41.57           C  
ANISOU  593  CG1 VAL A  82     4201   7024   4569    433    544    144       C  
ATOM    594  CG2 VAL A  82      19.473  24.642  -9.322  1.00 38.68           C  
ANISOU  594  CG2 VAL A  82     3808   6808   4081    372    627    205       C  
ATOM    595  N   ARG A  83      20.360  27.660  -6.288  1.00 39.74           N  
ANISOU  595  N   ARG A  83     3808   6891   4401   -211    713    244       N  
ATOM    596  CA  ARG A  83      20.808  28.335  -5.059  1.00 40.87           C  
ANISOU  596  CA  ARG A  83     3871   7082   4577   -398    735    184       C  
ATOM    597  C   ARG A  83      19.821  29.424  -4.604  1.00 39.65           C  
ANISOU  597  C   ARG A  83     3953   6584   4530   -555    776    272       C  
ATOM    598  O   ARG A  83      19.433  29.446  -3.418  1.00 36.54           O  
ANISOU  598  O   ARG A  83     3577   6085   4223   -549    707    247       O  
ATOM    599  CB  ARG A  83      22.241  28.906  -5.234  1.00 44.78           C  
ANISOU  599  CB  ARG A  83     4135   7946   4934   -644    864     75       C  
ATOM    600  CG  ARG A  83      22.688  29.821  -4.099  1.00 48.23           C  
ANISOU  600  CG  ARG A  83     4492   8459   5372   -946    931    -30       C  
ATOM    601  N   ALA A  84      19.411  30.310  -5.528  1.00 38.46           N  
ANISOU  601  N   ALA A  84     4008   6261   4343   -645    898    383       N  
ATOM    602  CA  ALA A  84      18.446  31.375  -5.187  1.00 39.06           C  
ANISOU  602  CA  ALA A  84     4369   6009   4464   -702    960    488       C  
ATOM    603  C   ALA A  84      17.154  30.787  -4.596  1.00 35.86           C  
ANISOU  603  C   ALA A  84     4003   5465   4159   -464    787    515       C  
ATOM    604  O   ALA A  84      16.674  31.253  -3.590  1.00 33.66           O  
ANISOU  604  O   ALA A  84     3811   5028   3952   -507    770    520       O  
ATOM    605  CB  ALA A  84      18.127  32.240  -6.383  1.00 39.27           C  
ANISOU  605  CB  ALA A  84     4662   5886   4374   -695   1120    629       C  
ATOM    606  N   TYR A  85      16.583  29.791  -5.269  1.00 35.55           N  
ANISOU  606  N   TYR A  85     3907   5498   4102   -249    682    512       N  
ATOM    607  CA  TYR A  85      15.356  29.145  -4.830  1.00 32.96           C  
ANISOU  607  CA  TYR A  85     3597   5094   3832    -95    555    488       C  
ATOM    608  C   TYR A  85      15.529  28.467  -3.448  1.00 33.38           C  
ANISOU  608  C   TYR A  85     3570   5120   3992   -115    475    396       C  
ATOM    609  O   TYR A  85      14.630  28.575  -2.605  1.00 30.60           O  
ANISOU  609  O   TYR A  85     3283   4636   3707    -99    423    396       O  
ATOM    610  CB  TYR A  85      14.877  28.127  -5.878  1.00 33.21           C  
ANISOU  610  CB  TYR A  85     3575   5252   3791     53    501    442       C  
ATOM    611  CG  TYR A  85      13.383  27.809  -5.803  1.00 30.85           C  
ANISOU  611  CG  TYR A  85     3303   4941   3477    149    422    400       C  
ATOM    612  CD1 TYR A  85      12.441  28.821  -5.778  1.00 32.81           C  
ANISOU  612  CD1 TYR A  85     3642   5154   3670    226    426    485       C  
ATOM    613  CD2 TYR A  85      12.930  26.495  -5.736  1.00 27.69           C  
ANISOU  613  CD2 TYR A  85     2853   4586   3082    157    371    255       C  
ATOM    614  CE1 TYR A  85      11.079  28.543  -5.698  1.00 30.12           C  
ANISOU  614  CE1 TYR A  85     3253   4920   3271    319    350    411       C  
ATOM    615  CE2 TYR A  85      11.551  26.193  -5.659  1.00 28.97           C  
ANISOU  615  CE2 TYR A  85     2998   4809   3199    164    326    160       C  
ATOM    616  CZ  TYR A  85      10.640  27.235  -5.639  1.00 28.78           C  
ANISOU  616  CZ  TYR A  85     2975   4846   3112    250    300    233       C  
ATOM    617  OH  TYR A  85       9.285  26.982  -5.524  1.00 29.34           O  
ANISOU  617  OH  TYR A  85     2963   5086   3099    266    249    112       O  
ATOM    618  N   ARG A  86      16.659  27.808  -3.216  1.00 33.10           N  
ANISOU  618  N   ARG A  86     3398   5238   3939   -112    473    323       N  
ATOM    619  CA  ARG A  86      16.921  27.216  -1.908  1.00 33.27           C  
ANISOU  619  CA  ARG A  86     3369   5265   4005    -60    413    254       C  
ATOM    620  C   ARG A  86      16.845  28.295  -0.830  1.00 32.93           C  
ANISOU  620  C   ARG A  86     3345   5134   4033   -220    425    268       C  
ATOM    621  O   ARG A  86      16.110  28.167   0.150  1.00 33.76           O  
ANISOU  621  O   ARG A  86     3520   5095   4214   -183    367    264       O  
ATOM    622  CB  ARG A  86      18.294  26.543  -1.887  1.00 33.71           C  
ANISOU  622  CB  ARG A  86     3256   5597   3956     38    421    179       C  
ATOM    623  CG  ARG A  86      18.673  25.949  -0.540  1.00 36.57           C  
ANISOU  623  CG  ARG A  86     3573   6025   4297    181    368    118       C  
ATOM    624  CD  ARG A  86      20.182  25.848  -0.386  1.00 45.55           C  
ANISOU  624  CD  ARG A  86     4454   7579   5274    254    380     31       C  
ATOM    625  NE  ARG A  86      20.732  26.975   0.363  1.00 50.64           N  
ANISOU  625  NE  ARG A  86     4923   8400   5918      0    402    -36       N  
ATOM    626  CZ  ARG A  86      21.930  27.505   0.142  1.00 56.51           C  
ANISOU  626  CZ  ARG A  86     5399   9543   6528   -164    465   -144       C  
ATOM    627  NH1 ARG A  86      22.349  28.530   0.873  1.00 61.05           N  
ANISOU  627  NH1 ARG A  86     5843  10262   7090   -469    516   -246       N  
ATOM    628  NH2 ARG A  86      22.711  27.012  -0.809  1.00 57.84           N  
ANISOU  628  NH2 ARG A  86     5429   9989   6558    -53    493   -176       N  
ATOM    629  N   GLU A  87      17.613  29.360  -1.032  1.00 34.80           N  
ANISOU  629  N   GLU A  87     3542   5451   4228   -428    526    268       N  
ATOM    630  CA  GLU A  87      17.624  30.548  -0.129  1.00 33.31           C  
ANISOU  630  CA  GLU A  87     3426   5153   4080   -649    593    259       C  
ATOM    631  C   GLU A  87      16.217  31.166   0.080  1.00 33.00           C  
ANISOU  631  C   GLU A  87     3635   4792   4111   -596    585    366       C  
ATOM    632  O   GLU A  87      15.861  31.547   1.201  1.00 31.10           O  
ANISOU  632  O   GLU A  87     3445   4436   3934   -642    561    348       O  
ATOM    633  CB  GLU A  87      18.659  31.611  -0.599  1.00 36.47           C  
ANISOU  633  CB  GLU A  87     3814   5658   4385   -960    777    216       C  
ATOM    634  N   LYS A  88      15.386  31.203  -0.964  1.00 32.74           N  
ANISOU  634  N   LYS A  88     3729   4670   4040   -459    593    465       N  
ATOM    635  CA  LYS A  88      13.996  31.679  -0.793  1.00 31.76           C  
ANISOU  635  CA  LYS A  88     3782   4361   3923   -325    566    547       C  
ATOM    636  C   LYS A  88      13.193  30.776   0.152  1.00 30.98           C  
ANISOU  636  C   LYS A  88     3592   4268   3913   -224    422    480       C  
ATOM    637  O   LYS A  88      12.514  31.258   1.072  1.00 29.62           O  
ANISOU  637  O   LYS A  88     3500   3971   3783   -216    402    494       O  
ATOM    638  CB  LYS A  88      13.283  31.799  -2.147  1.00 34.42           C  
ANISOU  638  CB  LYS A  88     4210   4731   4138   -143    589    638       C  
ATOM    639  CG  LYS A  88      11.772  31.981  -2.080  1.00 31.84           C  
ANISOU  639  CG  LYS A  88     3958   4386   3755     80    522    680       C  
ATOM    640  CD  LYS A  88      11.178  31.836  -3.503  1.00 37.42           C  
ANISOU  640  CD  LYS A  88     4654   5271   4290    293    517    723       C  
ATOM    641  CE  LYS A  88       9.629  31.926  -3.570  1.00 36.59           C  
ANISOU  641  CE  LYS A  88     4529   5319   4054    553    436    719       C  
ATOM    642  NZ  LYS A  88       9.117  33.333  -3.426  1.00 35.85           N  
ANISOU  642  NZ  LYS A  88     4719   5077   3826    760    533    874       N  
ATOM    643  N   ILE A  89      13.237  29.479  -0.101  1.00 28.68           N  
ANISOU  643  N   ILE A  89     3174   4096   3626   -152    352    407       N  
ATOM    644  CA  ILE A  89      12.594  28.511   0.774  1.00 29.60           C  
ANISOU  644  CA  ILE A  89     3268   4179   3799   -103    275    329       C  
ATOM    645  C   ILE A  89      13.157  28.615   2.207  1.00 28.92           C  
ANISOU  645  C   ILE A  89     3165   4036   3786   -157    258    303       C  
ATOM    646  O   ILE A  89      12.427  28.569   3.168  1.00 27.05           O  
ANISOU  646  O   ILE A  89     2975   3702   3601   -148    220    287       O  
ATOM    647  CB  ILE A  89      12.793  27.068   0.232  1.00 29.67           C  
ANISOU  647  CB  ILE A  89     3242   4266   3767    -38    269    247       C  
ATOM    648  CG1 ILE A  89      12.030  26.913  -1.110  1.00 29.96           C  
ANISOU  648  CG1 ILE A  89     3268   4401   3713     -5    276    231       C  
ATOM    649  CG2 ILE A  89      12.316  26.000   1.287  1.00 26.38           C  
ANISOU  649  CG2 ILE A  89     2900   3740   3382    -16    257    163       C  
ATOM    650  CD1 ILE A  89      12.463  25.713  -1.952  1.00 29.99           C  
ANISOU  650  CD1 ILE A  89     3264   4480   3651     30    307    151       C  
ATOM    651  N   GLU A  90      14.462  28.714   2.339  1.00 30.36           N  
ANISOU  651  N   GLU A  90     3252   4339   3944   -210    286    278       N  
ATOM    652  CA  GLU A  90      15.114  28.877   3.618  1.00 29.92           C  
ANISOU  652  CA  GLU A  90     3125   4338   3906   -253    267    224       C  
ATOM    653  C   GLU A  90      14.558  30.064   4.375  1.00 30.77           C  
ANISOU  653  C   GLU A  90     3329   4286   4077   -387    287    251       C  
ATOM    654  O   GLU A  90      14.258  29.956   5.521  1.00 28.04           O  
ANISOU  654  O   GLU A  90     2991   3887   3774   -360    238    223       O  
ATOM    655  CB  GLU A  90      16.599  29.050   3.415  1.00 32.05           C  
ANISOU  655  CB  GLU A  90     3213   4881   4083   -332    311    157       C  
ATOM    656  CG  GLU A  90      17.412  28.301   4.307  1.00 35.60           C  
ANISOU  656  CG  GLU A  90     3514   5557   4456   -189    259     72       C  
ATOM    657  CD  GLU A  90      18.863  28.316   3.923  1.00 38.41           C  
ANISOU  657  CD  GLU A  90     3621   6310   4663   -220    294    -24       C  
ATOM    658  OE1 GLU A  90      19.534  29.205   4.402  1.00 41.14           O  
ANISOU  658  OE1 GLU A  90     3818   6848   4965   -452    338   -122       O  
ATOM    659  OE2 GLU A  90      19.318  27.454   3.178  1.00 37.75           O  
ANISOU  659  OE2 GLU A  90     3487   6369   4488    -32    291    -23       O  
ATOM    660  N   LYS A  91      14.439  31.194   3.712  1.00 29.72           N  
ANISOU  660  N   LYS A  91     3312   4058   3924   -508    380    311       N  
ATOM    661  CA  LYS A  91      13.934  32.395   4.382  1.00 31.08           C  
ANISOU  661  CA  LYS A  91     3658   4031   4121   -606    440    343       C  
ATOM    662  C   LYS A  91      12.477  32.229   4.817  1.00 30.55           C  
ANISOU  662  C   LYS A  91     3680   3831   4097   -426    356    395       C  
ATOM    663  O   LYS A  91      12.091  32.671   5.897  1.00 28.56           O  
ANISOU  663  O   LYS A  91     3490   3474   3887   -448    342    382       O  
ATOM    664  CB  LYS A  91      14.108  33.663   3.531  1.00 32.51           C  
ANISOU  664  CB  LYS A  91     4060   4072   4222   -737    616    414       C  
ATOM    665  CG  LYS A  91      15.518  34.251   3.577  1.00 39.64           C  
ANISOU  665  CG  LYS A  91     4912   5079   5071  -1064    760    307       C  
ATOM    666  N   GLU A  92      11.670  31.548   4.005  1.00 29.66           N  
ANISOU  666  N   GLU A  92     3545   3772   3954   -266    304    425       N  
ATOM    667  CA  GLU A  92      10.325  31.232   4.425  1.00 27.35           C  
ANISOU  667  CA  GLU A  92     3260   3465   3668   -142    231    416       C  
ATOM    668  C   GLU A  92      10.329  30.356   5.671  1.00 27.67           C  
ANISOU  668  C   GLU A  92     3228   3494   3790   -174    169    334       C  
ATOM    669  O   GLU A  92       9.595  30.611   6.615  1.00 25.31           O  
ANISOU  669  O   GLU A  92     2969   3127   3522   -157    141    326       O  
ATOM    670  CB  GLU A  92       9.549  30.510   3.310  1.00 29.12           C  
ANISOU  670  CB  GLU A  92     3414   3842   3809    -32    201    395       C  
ATOM    671  CG  GLU A  92       8.933  31.426   2.322  1.00 30.09           C  
ANISOU  671  CG  GLU A  92     3622   4014   3796    118    239    485       C  
ATOM    672  CD  GLU A  92       8.079  30.706   1.278  1.00 29.54           C  
ANISOU  672  CD  GLU A  92     3421   4199   3604    229    194    421       C  
ATOM    673  OE1 GLU A  92       7.596  29.589   1.539  1.00 32.02           O  
ANISOU  673  OE1 GLU A  92     3607   4618   3942    147    147    283       O  
ATOM    674  OE2 GLU A  92       7.939  31.254   0.177  1.00 34.84           O  
ANISOU  674  OE2 GLU A  92     4139   4966   4132    380    229    496       O  
ATOM    675  N   LEU A  93      11.129  29.297   5.642  1.00 28.66           N  
ANISOU  675  N   LEU A  93     3278   3690   3923   -179    160    280       N  
ATOM    676  CA  LEU A  93      11.220  28.373   6.761  1.00 28.58           C  
ANISOU  676  CA  LEU A  93     3272   3649   3938   -141    134    223       C  
ATOM    677  C   LEU A  93      11.693  29.080   8.054  1.00 28.19           C  
ANISOU  677  C   LEU A  93     3206   3579   3927   -181    114    219       C  
ATOM    678  O   LEU A  93      11.094  28.904   9.128  1.00 25.88           O  
ANISOU  678  O   LEU A  93     2963   3207   3665   -154     89    203       O  
ATOM    679  CB  LEU A  93      12.119  27.175   6.392  1.00 29.22           C  
ANISOU  679  CB  LEU A  93     3337   3808   3957    -50    157    187       C  
ATOM    680  CG  LEU A  93      12.250  26.025   7.391  1.00 29.30           C  
ANISOU  680  CG  LEU A  93     3452   3754   3928     79    177    150       C  
ATOM    681  CD1 LEU A  93      12.871  24.879   6.579  1.00 34.08           C  
ANISOU  681  CD1 LEU A  93     4122   4396   4431    210    236    128       C  
ATOM    682  CD2 LEU A  93      13.188  26.437   8.577  1.00 27.89           C  
ANISOU  682  CD2 LEU A  93     3184   3687   3727    150    134    148       C  
ATOM    683  N   GLU A  94      12.681  29.962   7.925  1.00 28.87           N  
ANISOU  683  N   GLU A  94     3227   3746   3995   -286    143    214       N  
ATOM    684  CA  GLU A  94      13.150  30.724   9.081  1.00 29.02           C  
ANISOU  684  CA  GLU A  94     3215   3786   4024   -388    145    165       C  
ATOM    685  C   GLU A  94      12.046  31.640   9.645  1.00 28.20           C  
ANISOU  685  C   GLU A  94     3264   3472   3977   -424    153    207       C  
ATOM    686  O   GLU A  94      11.862  31.719  10.851  1.00 25.34           O  
ANISOU  686  O   GLU A  94     2904   3082   3640   -419    118    172       O  
ATOM    687  CB  GLU A  94      14.422  31.485   8.724  1.00 30.38           C  
ANISOU  687  CB  GLU A  94     3287   4124   4134   -582    219     99       C  
ATOM    688  CG  GLU A  94      15.591  30.481   8.473  1.00 34.09           C  
ANISOU  688  CG  GLU A  94     3541   4907   4503   -477    187     31       C  
ATOM    689  CD  GLU A  94      16.871  31.109   7.904  1.00 41.52           C  
ANISOU  689  CD  GLU A  94     4317   6111   5346   -695    273    -66       C  
ATOM    690  OE1 GLU A  94      16.824  32.241   7.367  1.00 46.13           O  
ANISOU  690  OE1 GLU A  94     5025   6555   5948   -952    394    -55       O  
ATOM    691  OE2 GLU A  94      17.928  30.446   7.982  1.00 43.92           O  
ANISOU  691  OE2 GLU A  94     4387   6778   5524   -595    239   -159       O  
ATOM    692  N   ALA A  95      11.280  32.279   8.758  1.00 27.39           N  
ANISOU  692  N   ALA A  95     3294   3251   3864   -406    200    287       N  
ATOM    693  CA  ALA A  95      10.212  33.177   9.180  1.00 25.81           C  
ANISOU  693  CA  ALA A  95     3255   2888   3662   -354    218    338       C  
ATOM    694  C   ALA A  95       9.069  32.416   9.871  1.00 26.14           C  
ANISOU  694  C   ALA A  95     3246   2955   3733   -226    127    321       C  
ATOM    695  O   ALA A  95       8.518  32.889  10.864  1.00 25.96           O  
ANISOU  695  O   ALA A  95     3283   2853   3726   -206    114    315       O  
ATOM    696  CB  ALA A  95       9.687  33.990   8.002  1.00 27.14           C  
ANISOU  696  CB  ALA A  95     3592   2979   3740   -264    299    439       C  
ATOM    697  N   VAL A  96       8.746  31.217   9.382  1.00 25.49           N  
ANISOU  697  N   VAL A  96     3067   2976   3641   -173     89    291       N  
ATOM    698  CA  VAL A  96       7.780  30.380  10.087  1.00 24.20           C  
ANISOU  698  CA  VAL A  96     2878   2832   3486   -142     55    235       C  
ATOM    699  C   VAL A  96       8.284  30.078  11.527  1.00 24.93           C  
ANISOU  699  C   VAL A  96     2987   2856   3631   -166     38    205       C  
ATOM    700  O   VAL A  96       7.508  30.126  12.490  1.00 25.47           O  
ANISOU  700  O   VAL A  96     3085   2882   3711   -153     25    186       O  
ATOM    701  CB  VAL A  96       7.502  29.056   9.296  1.00 24.03           C  
ANISOU  701  CB  VAL A  96     2812   2897   3422   -158     75    171       C  
ATOM    702  CG1 VAL A  96       6.696  28.045  10.152  1.00 22.23           C  
ANISOU  702  CG1 VAL A  96     2623   2639   3185   -213    107     82       C  
ATOM    703  CG2 VAL A  96       6.743  29.399   7.967  1.00 24.07           C  
ANISOU  703  CG2 VAL A  96     2756   3054   3335   -112     74    174       C  
ATOM    704  N   CYS A  97       9.542  29.681  11.647  1.00 24.21           N  
ANISOU  704  N   CYS A  97     2858   2807   3536   -166     40    191       N  
ATOM    705  CA  CYS A  97      10.089  29.335  12.953  1.00 24.72           C  
ANISOU  705  CA  CYS A  97     2916   2886   3589   -116     20    158       C  
ATOM    706  C   CYS A  97      10.068  30.534  13.869  1.00 26.23           C  
ANISOU  706  C   CYS A  97     3103   3050   3813   -191     -1    145       C  
ATOM    707  O   CYS A  97       9.705  30.415  15.051  1.00 24.86           O  
ANISOU  707  O   CYS A  97     2961   2841   3645   -147    -24    128       O  
ATOM    708  CB  CYS A  97      11.522  28.788  12.847  1.00 23.85           C  
ANISOU  708  CB  CYS A  97     2716   2945   3402    -37     18    130       C  
ATOM    709  SG  CYS A  97      11.562  27.117  12.079  1.00 25.76           S  
ANISOU  709  SG  CYS A  97     3066   3154   3567    121     76    142       S  
ATOM    710  N   GLN A  98      10.426  31.640  13.388  1.00 25.07           N  
ANISOU  710  N   GLN A  98     2958   2894   3672   -308     30    149       N  
ATOM    711  CA  GLN A  98      10.456  32.851  14.200  1.00 26.91           C  
ANISOU  711  CA  GLN A  98     3256   3055   3915   -418     56    116       C  
ATOM    712  C   GLN A  98       9.017  33.257  14.582  1.00 26.56           C  
ANISOU  712  C   GLN A  98     3344   2851   3895   -327     48    172       C  
ATOM    713  O   GLN A  98       8.767  33.762  15.682  1.00 25.32           O  
ANISOU  713  O   GLN A  98     3236   2636   3747   -340     40    142       O  
ATOM    714  CB  GLN A  98      11.213  33.944  13.450  1.00 26.73           C  
ANISOU  714  CB  GLN A  98     3292   3005   3858   -609    161     97       C  
ATOM    715  CG  GLN A  98      12.682  33.712  13.216  1.00 35.95           C  
ANISOU  715  CG  GLN A  98     4274   4419   4968   -746    180     -4       C  
ATOM    716  CD  GLN A  98      13.565  33.537  14.453  1.00 32.54           C  
ANISOU  716  CD  GLN A  98     3649   4241   4473   -793    133   -148       C  
ATOM    717  OE1 GLN A  98      13.390  34.231  15.459  1.00 39.15           O  
ANISOU  717  OE1 GLN A  98     4541   5023   5313   -889    147   -212       O  
ATOM    718  NE2 GLN A  98      14.336  32.468  14.462  1.00 35.19           N  
ANISOU  718  NE2 GLN A  98     3778   4861   4731   -641     64   -186       N  
ATOM    719  N   ASP A  99       8.078  33.000  13.678  1.00 24.02           N  
ANISOU  719  N   ASP A  99     3049   2521   3558   -224     46    233       N  
ATOM    720  CA  ASP A  99       6.670  33.268  13.944  1.00 26.35           C  
ANISOU  720  CA  ASP A  99     3395   2793   3822   -103     31    257       C  
ATOM    721  C   ASP A  99       6.187  32.475  15.156  1.00 24.87           C  
ANISOU  721  C   ASP A  99     3148   2637   3665    -96    -14    203       C  
ATOM    722  O   ASP A  99       5.473  33.001  16.010  1.00 24.62           O  
ANISOU  722  O   ASP A  99     3162   2571   3623    -46    -24    198       O  
ATOM    723  CB  ASP A  99       5.818  32.929  12.719  1.00 24.97           C  
ANISOU  723  CB  ASP A  99     3171   2744   3574      0     28    282       C  
ATOM    724  CG  ASP A  99       4.397  33.444  12.837  1.00 33.62           C  
ANISOU  724  CG  ASP A  99     4276   3930   4567    171     15    290       C  
ATOM    725  OD1 ASP A  99       4.142  34.292  13.718  1.00 37.82           O  
ANISOU  725  OD1 ASP A  99     4921   4358   5091    234     26    311       O  
ATOM    726  OD2 ASP A  99       3.536  33.001  12.049  1.00 40.06           O  
ANISOU  726  OD2 ASP A  99     4970   4968   5283    251     -2    256       O  
ATOM    727  N   VAL A 100       6.583  31.207  15.226  1.00 23.84           N  
ANISOU  727  N   VAL A 100     2959   2552   3549   -126    -18    168       N  
ATOM    728  CA  VAL A 100       6.202  30.332  16.355  1.00 26.41           C  
ANISOU  728  CA  VAL A 100     3307   2858   3871   -114    -12    129       C  
ATOM    729  C   VAL A 100       6.993  30.712  17.620  1.00 25.29           C  
ANISOU  729  C   VAL A 100     3177   2690   3741    -90    -43    121       C  
ATOM    730  O   VAL A 100       6.486  30.714  18.763  1.00 23.76           O  
ANISOU  730  O   VAL A 100     3020   2464   3542    -61    -50    105       O  
ATOM    731  CB  VAL A 100       6.520  28.841  15.998  1.00 25.52           C  
ANISOU  731  CB  VAL A 100     3238   2738   3721   -115     47    106       C  
ATOM    732  CG1 VAL A 100       6.363  27.990  17.242  1.00 33.21           C  
ANISOU  732  CG1 VAL A 100     4335   3629   4656    -75    100     89       C  
ATOM    733  CG2 VAL A 100       5.616  28.401  14.948  1.00 32.95           C  
ANISOU  733  CG2 VAL A 100     4155   3737   4629   -193     91     64       C  
ATOM    734  N   LEU A 101       8.270  30.987  17.436  1.00 24.80           N  
ANISOU  734  N   LEU A 101     3057   2694   3671   -112    -58    108       N  
ATOM    735  CA  LEU A 101       9.124  31.225  18.572  1.00 26.03           C  
ANISOU  735  CA  LEU A 101     3160   2940   3789    -99    -89     53       C  
ATOM    736  C   LEU A 101       8.732  32.528  19.310  1.00 25.12           C  
ANISOU  736  C   LEU A 101     3091   2749   3704   -191    -92     21       C  
ATOM    737  O   LEU A 101       8.779  32.620  20.540  1.00 24.33           O  
ANISOU  737  O   LEU A 101     2982   2686   3578   -161   -120    -24       O  
ATOM    738  CB  LEU A 101      10.568  31.257  18.100  1.00 25.63           C  
ANISOU  738  CB  LEU A 101     2975   3083   3679   -136    -94     -1       C  
ATOM    739  CG  LEU A 101      11.180  29.904  17.748  1.00 25.92           C  
ANISOU  739  CG  LEU A 101     2982   3236   3632     46    -93     20       C  
ATOM    740  CD1 LEU A 101      12.533  30.232  17.113  1.00 24.78           C  
ANISOU  740  CD1 LEU A 101     2652   3346   3417    -21    -99    -52       C  
ATOM    741  CD2 LEU A 101      11.413  29.096  19.055  1.00 25.86           C  
ANISOU  741  CD2 LEU A 101     3006   3313   3508    274   -110     12       C  
ATOM    742  N   SER A 102       8.298  33.516  18.554  1.00 25.78           N  
ANISOU  742  N   SER A 102     3265   2713   3818   -268    -48     52       N  
ATOM    743  CA  SER A 102       7.808  34.725  19.188  1.00 27.63           C  
ANISOU  743  CA  SER A 102     3632   2816   4050   -306    -15     37       C  
ATOM    744  C   SER A 102       6.423  34.544  19.883  1.00 26.27           C  
ANISOU  744  C   SER A 102     3501   2599   3880   -157    -49     75       C  
ATOM    745  O   SER A 102       6.231  35.032  21.020  1.00 24.85           O  
ANISOU  745  O   SER A 102     3369   2382   3692   -154    -57     35       O  
ATOM    746  CB  SER A 102       7.916  35.925  18.241  1.00 30.16           C  
ANISOU  746  CB  SER A 102     4128   2986   4345   -394     91     65       C  
ATOM    747  OG  SER A 102       6.659  36.101  17.668  1.00 39.07           O  
ANISOU  747  OG  SER A 102     5361   4040   5446   -203     97    165       O  
ATOM    748  N   LEU A 103       5.584  33.655  19.354  1.00 23.63           N  
ANISOU  748  N   LEU A 103     3112   2325   3543    -70    -66    116       N  
ATOM    749  CA  LEU A 103       4.336  33.287  20.091  1.00 23.89           C  
ANISOU  749  CA  LEU A 103     3130   2397   3551      9    -78    106       C  
ATOM    750  C   LEU A 103       4.707  32.614  21.415  1.00 25.24           C  
ANISOU  750  C   LEU A 103     3293   2568   3731     -3    -93     70       C  
ATOM    751  O   LEU A 103       4.127  32.903  22.485  1.00 24.03           O  
ANISOU  751  O   LEU A 103     3167   2402   3561     36   -101     51       O  
ATOM    752  CB  LEU A 103       3.440  32.374  19.263  1.00 22.48           C  
ANISOU  752  CB  LEU A 103     2871   2337   3332     14    -59     96       C  
ATOM    753  CG  LEU A 103       2.807  32.947  17.984  1.00 23.28           C  
ANISOU  753  CG  LEU A 103     2941   2539   3365     98    -55    123       C  
ATOM    754  CD1 LEU A 103       1.959  31.871  17.279  1.00 24.52           C  
ANISOU  754  CD1 LEU A 103     2961   2902   3456     40    -32     49       C  
ATOM    755  CD2 LEU A 103       1.950  34.180  18.350  1.00 24.46           C  
ANISOU  755  CD2 LEU A 103     3159   2704   3431    275    -61    149       C  
ATOM    756  N   LEU A 104       5.662  31.695  21.336  1.00 23.47           N  
ANISOU  756  N   LEU A 104     3043   2375   3500    -10    -89     66       N  
ATOM    757  CA  LEU A 104       6.118  31.010  22.528  1.00 23.52           C  
ANISOU  757  CA  LEU A 104     3073   2406   3456     68    -91     51       C  
ATOM    758  C   LEU A 104       6.743  32.002  23.531  1.00 24.27           C  
ANISOU  758  C   LEU A 104     3124   2561   3538     61   -146     -6       C  
ATOM    759  O   LEU A 104       6.421  31.964  24.722  1.00 25.38           O  
ANISOU  759  O   LEU A 104     3296   2704   3642    125   -155    -21       O  
ATOM    760  CB  LEU A 104       7.114  29.926  22.139  1.00 21.94           C  
ANISOU  760  CB  LEU A 104     2880   2260   3195    151    -68     67       C  
ATOM    761  CG  LEU A 104       6.480  28.751  21.399  1.00 21.60           C  
ANISOU  761  CG  LEU A 104     2953   2118   3137    135     29     95       C  
ATOM    762  CD1 LEU A 104       7.620  27.842  20.885  1.00 22.66           C  
ANISOU  762  CD1 LEU A 104     3128   2290   3191    263     58    118       C  
ATOM    763  CD2 LEU A 104       5.527  27.919  22.318  1.00 25.28           C  
ANISOU  763  CD2 LEU A 104     3591   2472   3545    140    134     93       C  
ATOM    764  N   ASP A 105       7.674  32.833  23.076  1.00 24.80           N  
ANISOU  764  N   ASP A 105     3123   2689   3610    -45   -160    -58       N  
ATOM    765  CA  ASP A 105       8.425  33.675  24.014  1.00 27.45           C  
ANISOU  765  CA  ASP A 105     3402   3132   3897   -125   -182   -170       C  
ATOM    766  C   ASP A 105       7.578  34.821  24.551  1.00 27.05           C  
ANISOU  766  C   ASP A 105     3483   2913   3882   -189   -155   -187       C  
ATOM    767  O   ASP A 105       7.808  35.286  25.676  1.00 30.07           O  
ANISOU  767  O   ASP A 105     3852   3356   4216   -220   -171   -279       O  
ATOM    768  CB  ASP A 105       9.676  34.237  23.384  1.00 28.34           C  
ANISOU  768  CB  ASP A 105     3408   3386   3975   -304   -159   -270       C  
ATOM    769  CG  ASP A 105      10.829  33.200  23.346  1.00 37.39           C  
ANISOU  769  CG  ASP A 105     4358   4841   5007   -181   -207   -307       C  
ATOM    770  OD1 ASP A 105      10.824  32.205  24.137  1.00 36.57           O  
ANISOU  770  OD1 ASP A 105     4240   4838   4817     68   -249   -271       O  
ATOM    771  OD2 ASP A 105      11.749  33.406  22.520  1.00 41.64           O  
ANISOU  771  OD2 ASP A 105     4782   5528   5513   -311   -183   -372       O  
ATOM    772  N   ASN A 106       6.659  35.341  23.738  1.00 26.31           N  
ANISOU  772  N   ASN A 106     3521   2638   3837   -183   -110   -110       N  
ATOM    773  CA  ASN A 106       6.033  36.608  24.095  1.00 26.47           C  
ANISOU  773  CA  ASN A 106     3721   2492   3843   -195    -56   -124       C  
ATOM    774  C   ASN A 106       4.641  36.376  24.682  1.00 26.13           C  
ANISOU  774  C   ASN A 106     3701   2437   3791     -9    -88    -67       C  
ATOM    775  O   ASN A 106       4.013  37.305  25.182  1.00 25.83           O  
ANISOU  775  O   ASN A 106     3805   2295   3714     54    -55    -75       O  
ATOM    776  CB  ASN A 106       6.011  37.585  22.916  1.00 28.19           C  
ANISOU  776  CB  ASN A 106     4129   2534   4047   -244     46    -82       C  
ATOM    777  CG  ASN A 106       7.410  37.968  22.484  1.00 31.59           C  
ANISOU  777  CG  ASN A 106     4554   2984   4466   -506    117   -178       C  
ATOM    778  OD1 ASN A 106       8.316  37.981  23.302  1.00 33.92           O  
ANISOU  778  OD1 ASN A 106     4729   3427   4733   -668    103   -320       O  
ATOM    779  ND2 ASN A 106       7.600  38.237  21.208  1.00 34.90           N  
ANISOU  779  ND2 ASN A 106     5069   3312   4878   -548    195   -120       N  
ATOM    780  N   TYR A 107       4.154  35.145  24.584  1.00 25.18           N  
ANISOU  780  N   TYR A 107     3460   2424   3682     62   -125    -23       N  
ATOM    781  CA  TYR A 107       2.803  34.836  25.085  1.00 23.59           C  
ANISOU  781  CA  TYR A 107     3245   2274   3447    171   -126     -6       C  
ATOM    782  C   TYR A 107       2.807  33.572  25.906  1.00 25.94           C  
ANISOU  782  C   TYR A 107     3489   2635   3733    161   -124    -18       C  
ATOM    783  O   TYR A 107       2.433  33.590  27.072  1.00 28.28           O  
ANISOU  783  O   TYR A 107     3807   2942   3996    205   -126    -40       O  
ATOM    784  CB  TYR A 107       1.776  34.657  23.958  1.00 24.85           C  
ANISOU  784  CB  TYR A 107     3353   2522   3567    234   -106     29       C  
ATOM    785  CG  TYR A 107       1.632  35.853  23.012  1.00 23.09           C  
ANISOU  785  CG  TYR A 107     3239   2237   3297    340    -83     75       C  
ATOM    786  CD1 TYR A 107       0.554  36.700  23.103  1.00 19.44           C  
ANISOU  786  CD1 TYR A 107     2844   1821   2721    549    -68     92       C  
ATOM    787  CD2 TYR A 107       2.557  36.081  22.012  1.00 25.14           C  
ANISOU  787  CD2 TYR A 107     3557   2403   3591    266    -58    106       C  
ATOM    788  CE1 TYR A 107       0.394  37.825  22.221  1.00 23.08           C  
ANISOU  788  CE1 TYR A 107     3497   2192   3079    737    -11    161       C  
ATOM    789  CE2 TYR A 107       2.416  37.175  21.140  1.00 30.89           C  
ANISOU  789  CE2 TYR A 107     4466   3029   4243    382      6    165       C  
ATOM    790  CZ  TYR A 107       1.325  38.000  21.220  1.00 25.64           C  
ANISOU  790  CZ  TYR A 107     3920   2379   3445    639     34    203       C  
ATOM    791  OH  TYR A 107       1.224  39.054  20.339  1.00 27.09           O  
ANISOU  791  OH  TYR A 107     4360   2429   3505    824    128    285       O  
ATOM    792  N   LEU A 108       3.081  32.454  25.249  1.00 24.28           N  
ANISOU  792  N   LEU A 108     3254   2445   3528    121    -93      4       N  
ATOM    793  CA  LEU A 108       2.683  31.163  25.778  1.00 24.46           C  
ANISOU  793  CA  LEU A 108     3330   2466   3498    114    -17      4       C  
ATOM    794  C   LEU A 108       3.549  30.745  26.956  1.00 25.30           C  
ANISOU  794  C   LEU A 108     3510   2553   3551    219    -22     16       C  
ATOM    795  O   LEU A 108       3.032  30.407  28.045  1.00 27.23           O  
ANISOU  795  O   LEU A 108     3832   2779   3734    261     25     16       O  
ATOM    796  CB  LEU A 108       2.723  30.136  24.650  1.00 22.61           C  
ANISOU  796  CB  LEU A 108     3116   2217   3258     37     54     12       C  
ATOM    797  CG  LEU A 108       1.722  30.443  23.519  1.00 26.37           C  
ANISOU  797  CG  LEU A 108     3480   2803   3736    -47     60    -25       C  
ATOM    798  CD1 LEU A 108       1.963  29.559  22.283  1.00 23.96           C  
ANISOU  798  CD1 LEU A 108     3180   2498   3426   -138    118    -36       C  
ATOM    799  CD2 LEU A 108       0.256  30.310  24.034  1.00 30.15           C  
ANISOU  799  CD2 LEU A 108     3905   3415   4136   -114    122   -102       C  
ATOM    800  N   ILE A 109       4.870  30.747  26.747  1.00 26.28           N  
ANISOU  800  N   ILE A 109     3593   2730   3661    280    -73     18       N  
ATOM    801  CA  ILE A 109       5.790  30.551  27.856  1.00 27.27           C  
ANISOU  801  CA  ILE A 109     3719   2961   3680    436   -106      3       C  
ATOM    802  C   ILE A 109       5.674  31.755  28.814  1.00 27.88           C  
ANISOU  802  C   ILE A 109     3726   3098   3771    398   -176    -71       C  
ATOM    803  O   ILE A 109       5.681  31.559  30.043  1.00 30.41           O  
ANISOU  803  O   ILE A 109     4080   3477   3999    519   -181    -81       O  
ATOM    804  CB  ILE A 109       7.253  30.324  27.372  1.00 28.92           C  
ANISOU  804  CB  ILE A 109     3827   3340   3821    520   -151    -19       C  
ATOM    805  CG1 ILE A 109       7.332  29.037  26.511  1.00 28.46           C  
ANISOU  805  CG1 ILE A 109     3902   3189   3724    604    -59     61       C  
ATOM    806  CG2 ILE A 109       8.225  30.170  28.556  1.00 29.03           C  
ANISOU  806  CG2 ILE A 109     3775   3599   3657    736   -201    -67       C  
ATOM    807  CD1 ILE A 109       8.524  28.971  25.555  1.00 28.02           C  
ANISOU  807  CD1 ILE A 109     3717   3291   3638    639   -102     41       C  
ATOM    808  N   LYS A 110       5.679  32.951  28.288  1.00 35.50           N  
ANISOU  808  N   LYS A 110     5926   3153   4411  -1300    602  -1062       N  
ATOM    809  CA  LYS A 110       5.738  34.101  29.151  1.00 38.25           C  
ANISOU  809  CA  LYS A 110     6671   3282   4580  -1384    679  -1207       C  
ATOM    810  C   LYS A 110       4.656  34.060  30.203  1.00 36.68           C  
ANISOU  810  C   LYS A 110     6620   3062   4255  -1085    768  -1167       C  
ATOM    811  O   LYS A 110       4.913  34.302  31.332  1.00 39.04           O  
ANISOU  811  O   LYS A 110     7106   3347   4380  -1146    735  -1298       O  
ATOM    812  CB  LYS A 110       5.644  35.380  28.351  1.00 39.58           C  
ANISOU  812  CB  LYS A 110     7179   3118   4741  -1422    859  -1220       C  
ATOM    813  CG  LYS A 110       5.566  36.638  29.159  1.00 43.80           C  
ANISOU  813  CG  LYS A 110     8266   3313   5063  -1485   1003  -1372       C  
ATOM    814  CD  LYS A 110       5.469  37.836  28.255  1.00 45.77           C  
ANISOU  814  CD  LYS A 110     8901   3184   5308  -1485   1239  -1346       C  
ATOM    815  CE  LYS A 110       5.953  39.080  28.939  1.00 57.24           C  
ANISOU  815  CE  LYS A 110    10956   4236   6555  -1776   1353  -1572       C  
ATOM    816  NZ  LYS A 110       4.875  40.029  29.189  1.00 55.45           N  
ANISOU  816  NZ  LYS A 110    11304   3626   6139  -1377   1668  -1515       N  
ATOM    817  N   ASN A 111       3.450  33.708  29.808  1.00 37.40           N  
ANISOU  817  N   ASN A 111     6588   3205   4416   -765    875   -974       N  
ATOM    818  CA  ASN A 111       2.283  33.879  30.676  1.00 38.68           C  
ANISOU  818  CA  ASN A 111     6896   3360   4442   -430   1022   -878       C  
ATOM    819  C   ASN A 111       1.735  32.615  31.255  1.00 36.60           C  
ANISOU  819  C   ASN A 111     6301   3373   4232   -307    964   -752       C  
ATOM    820  O   ASN A 111       0.754  32.652  31.973  1.00 38.20           O  
ANISOU  820  O   ASN A 111     6557   3626   4331    -27   1094   -633       O  
ATOM    821  CB  ASN A 111       1.177  34.669  29.978  1.00 39.56           C  
ANISOU  821  CB  ASN A 111     7150   3367   4512   -108   1246   -712       C  
ATOM    822  CG  ASN A 111       1.591  36.075  29.685  1.00 41.09           C  
ANISOU  822  CG  ASN A 111     7838   3184   4588   -157   1396   -823       C  
ATOM    823  OD1 ASN A 111       2.113  36.779  30.559  1.00 41.90           O  
ANISOU  823  OD1 ASN A 111     8358   3041   4523   -293   1427  -1013       O  
ATOM    824  ND2 ASN A 111       1.444  36.480  28.440  1.00 38.73           N  
ANISOU  824  ND2 ASN A 111     7527   2825   4365    -88   1488   -722       N  
ATOM    825  N   CYS A 112       2.432  31.515  31.036  1.00 34.70           N  
ANISOU  825  N   CYS A 112     5763   3296   4126   -503    799   -768       N  
ATOM    826  CA  CYS A 112       1.988  30.216  31.512  1.00 35.16           C  
ANISOU  826  CA  CYS A 112     5559   3554   4245   -421    778   -642       C  
ATOM    827  C   CYS A 112       1.938  30.215  33.058  1.00 36.73           C  
ANISOU  827  C   CYS A 112     5908   3790   4257   -283    816   -666       C  
ATOM    828  O   CYS A 112       2.923  30.579  33.699  1.00 37.70           O  
ANISOU  828  O   CYS A 112     6190   3894   4238   -404    723   -839       O  
ATOM    829  CB  CYS A 112       2.978  29.162  31.006  1.00 34.80           C  
ANISOU  829  CB  CYS A 112     5297   3605   4320   -624    632   -673       C  
ATOM    830  SG  CYS A 112       2.374  27.541  31.219  1.00 38.98           S  
ANISOU  830  SG  CYS A 112     5598   4264   4948   -560    667   -507       S  
ATOM    831  N   SER A 113       0.820  29.813  33.665  1.00 36.61           N  
ANISOU  831  N   SER A 113     5824   3868   4218    -43    948   -489       N  
ATOM    832  CA  SER A 113       0.724  29.918  35.117  1.00 40.14           C  
ANISOU  832  CA  SER A 113     6451   4345   4455    147   1011   -498       C  
ATOM    833  C   SER A 113       1.570  28.840  35.814  1.00 38.02           C  
ANISOU  833  C   SER A 113     6057   4221   4166     74    904   -524       C  
ATOM    834  O   SER A 113       1.915  27.838  35.194  1.00 35.30           O  
ANISOU  834  O   SER A 113     5481   3942   3990    -61    844   -469       O  
ATOM    835  CB  SER A 113      -0.751  29.991  35.581  1.00 42.27           C  
ANISOU  835  CB  SER A 113     6700   4692   4669    480   1227   -263       C  
ATOM    836  OG  SER A 113      -1.355  28.715  35.557  1.00 48.82           O  
ANISOU  836  OG  SER A 113     7187   5706   5656    466   1267    -58       O  
ATOM    837  N   GLU A 114       1.954  29.057  37.069  1.00 39.00           N  
ANISOU  837  N   GLU A 114     6369   4402   4049    188    890   -611       N  
ATOM    838  CA  GLU A 114       3.031  28.265  37.696  1.00 39.21           C  
ANISOU  838  CA  GLU A 114     6296   4624   3979    139    763   -663       C  
ATOM    839  C   GLU A 114       2.708  26.775  37.722  1.00 38.61           C  
ANISOU  839  C   GLU A 114     5980   4647   4045    252    859   -429       C  
ATOM    840  O   GLU A 114       3.560  25.895  37.624  1.00 37.98           O  
ANISOU  840  O   GLU A 114     5769   4684   3979    208    793   -409       O  
ATOM    841  CB  GLU A 114       3.255  28.751  39.130  1.00 45.36           C  
ANISOU  841  CB  GLU A 114     7320   5494   4422    298    747   -775       C  
ATOM    842  CG  GLU A 114       4.114  27.824  39.993  1.00 51.10           C  
ANISOU  842  CG  GLU A 114     7911   6519   4986    386    661   -753       C  
ATOM    843  CD  GLU A 114       5.565  27.770  39.515  1.00 60.42           C  
ANISOU  843  CD  GLU A 114     8929   7894   6135    104    433   -902       C  
ATOM    844  OE1 GLU A 114       6.004  28.712  38.795  1.00 58.69           O  
ANISOU  844  OE1 GLU A 114     8780   7562   5957   -208    320  -1089       O  
ATOM    845  OE2 GLU A 114       6.268  26.786  39.871  1.00 63.12           O  
ANISOU  845  OE2 GLU A 114     9072   8520   6392    221    394   -804       O  
ATOM    846  N   THR A 115       1.426  26.459  37.910  1.00 37.20           N  
ANISOU  846  N   THR A 115     5761   4426   3948    417   1051   -225       N  
ATOM    847  CA  THR A 115       0.995  25.072  38.176  1.00 36.34           C  
ANISOU  847  CA  THR A 115     5500   4366   3941    499   1195      5       C  
ATOM    848  C   THR A 115       0.639  24.237  36.936  1.00 34.15           C  
ANISOU  848  C   THR A 115     5037   3994   3944    263   1219     96       C  
ATOM    849  O   THR A 115       0.268  23.068  37.035  1.00 32.33           O  
ANISOU  849  O   THR A 115     4741   3733   3808    248   1357    266       O  
ATOM    850  CB  THR A 115      -0.198  25.035  39.154  1.00 38.25           C  
ANISOU  850  CB  THR A 115     5767   4661   4106    765   1413    212       C  
ATOM    851  OG1 THR A 115      -1.322  25.700  38.565  1.00 42.54           O  
ANISOU  851  OG1 THR A 115     6236   5181   4745    751   1487    289       O  
ATOM    852  CG2 THR A 115       0.164  25.722  40.462  1.00 33.81           C  
ANISOU  852  CG2 THR A 115     5445   4185   3218   1035   1401    117       C  
ATOM    853  N   GLN A 116       0.763  24.870  35.781  1.00 32.23           N  
ANISOU  853  N   GLN A 116     4753   3686   3808     69   1096    -29       N  
ATOM    854  CA  GLN A 116       0.496  24.327  34.491  1.00 32.10           C  
ANISOU  854  CA  GLN A 116     4592   3598   4004   -163   1071     -3       C  
ATOM    855  C   GLN A 116       1.774  23.718  33.948  1.00 31.89           C  
ANISOU  855  C   GLN A 116     4596   3523   4000   -269    963   -100       C  
ATOM    856  O   GLN A 116       2.311  24.163  32.985  1.00 30.62           O  
ANISOU  856  O   GLN A 116     4415   3331   3889   -401    839   -219       O  
ATOM    857  CB  GLN A 116      -0.080  25.400  33.590  1.00 33.08           C  
ANISOU  857  CB  GLN A 116     4667   3723   4181   -225   1022    -53       C  
ATOM    858  CG  GLN A 116      -1.471  25.847  33.946  1.00 39.59           C  
ANISOU  858  CG  GLN A 116     5409   4662   4971    -67   1167    115       C  
ATOM    859  CD  GLN A 116      -2.534  24.847  33.552  1.00 50.60           C  
ANISOU  859  CD  GLN A 116     6542   6170   6512   -221   1253    303       C  
ATOM    860  OE1 GLN A 116      -2.350  23.660  33.644  1.00 54.91           O  
ANISOU  860  OE1 GLN A 116     7072   6649   7144   -376   1284    342       O  
ATOM    861  NE2 GLN A 116      -3.647  25.341  33.083  1.00 50.19           N  
ANISOU  861  NE2 GLN A 116     6296   6307   6467   -189   1301    426       N  
ATOM    862  N   TYR A 117       2.258  22.693  34.605  1.00 31.16           N  
ANISOU  862  N   TYR A 117     4558   3441   3841   -158   1043    -16       N  
ATOM    863  CA  TYR A 117       3.575  22.101  34.227  1.00 29.97           C  
ANISOU  863  CA  TYR A 117     4439   3309   3640   -145    975    -60       C  
ATOM    864  C   TYR A 117       3.525  21.469  32.877  1.00 27.72           C  
ANISOU  864  C   TYR A 117     4154   2857   3522   -338    975    -66       C  
ATOM    865  O   TYR A 117       4.529  21.459  32.158  1.00 28.71           O  
ANISOU  865  O   TYR A 117     4275   3009   3624   -355    880   -136       O  
ATOM    866  CB  TYR A 117       4.014  21.037  35.250  1.00 30.26           C  
ANISOU  866  CB  TYR A 117     4569   3401   3528    111   1122     88       C  
ATOM    867  CG  TYR A 117       4.231  21.679  36.592  1.00 35.14           C  
ANISOU  867  CG  TYR A 117     5192   4243   3919    323   1087     68       C  
ATOM    868  CD1 TYR A 117       5.299  22.566  36.791  1.00 38.71           C  
ANISOU  868  CD1 TYR A 117     5589   4930   4189    320    880   -101       C  
ATOM    869  CD2 TYR A 117       3.346  21.464  37.627  1.00 36.27           C  
ANISOU  869  CD2 TYR A 117     5394   4373   4013    490   1256    204       C  
ATOM    870  CE1 TYR A 117       5.489  23.182  38.029  1.00 40.45           C  
ANISOU  870  CE1 TYR A 117     5853   5359   4156    468    825   -164       C  
ATOM    871  CE2 TYR A 117       3.516  22.089  38.866  1.00 42.13           C  
ANISOU  871  CE2 TYR A 117     6183   5318   4506    711   1222    169       C  
ATOM    872  CZ  TYR A 117       4.592  22.952  39.042  1.00 40.18           C  
ANISOU  872  CZ  TYR A 117     5918   5290   4058    685    993    -37       C  
ATOM    873  OH  TYR A 117       4.779  23.575  40.252  1.00 44.86           O  
ANISOU  873  OH  TYR A 117     6597   6085   4363    856    936   -115       O  
ATOM    874  N   GLU A 118       2.455  20.927  32.506  1.00 27.85           N  
ANISOU  874  N   GLU A 118     4171   2733   3678   -488   1074      6       N  
ATOM    875  CA  GLU A 118       2.308  20.196  31.249  1.00 30.59           C  
ANISOU  875  CA  GLU A 118     4569   2906   4147   -710   1076    -22       C  
ATOM    876  C   GLU A 118       2.383  21.187  30.067  1.00 28.19           C  
ANISOU  876  C   GLU A 118     4142   2663   3905   -842    890   -164       C  
ATOM    877  O   GLU A 118       3.067  20.911  29.098  1.00 28.48           O  
ANISOU  877  O   GLU A 118     4241   2628   3951   -889    832   -231       O  
ATOM    878  CB  GLU A 118       1.016  19.387  31.182  1.00 32.25           C  
ANISOU  878  CB  GLU A 118     4786   2994   4472   -938   1213     75       C  
ATOM    879  CG  GLU A 118       0.901  18.219  32.140  1.00 40.17           C  
ANISOU  879  CG  GLU A 118     5978   3848   5438   -858   1456    237       C  
ATOM    880  CD  GLU A 118      -0.448  17.540  32.031  1.00 49.36           C  
ANISOU  880  CD  GLU A 118     7110   4916   6729  -1193   1587    330       C  
ATOM    881  OE1 GLU A 118      -1.353  18.081  31.362  1.00 49.32           O  
ANISOU  881  OE1 GLU A 118     6860   5067   6814  -1441   1467    285       O  
ATOM    882  OE2 GLU A 118      -0.610  16.477  32.659  1.00 57.16           O  
ANISOU  882  OE2 GLU A 118     8304   5706   7708  -1202   1825    468       O  
ATOM    883  N   SER A 119       1.640  22.282  30.230  1.00 28.55           N  
ANISOU  883  N   SER A 119     4049   2833   3967   -846    842   -177       N  
ATOM    884  CA  SER A 119       1.783  23.362  29.240  1.00 27.21           C  
ANISOU  884  CA  SER A 119     3808   2709   3821   -898    709   -285       C  
ATOM    885  C   SER A 119       3.210  23.869  29.125  1.00 27.36           C  
ANISOU  885  C   SER A 119     3889   2740   3767   -833    615   -387       C  
ATOM    886  O   SER A 119       3.738  24.053  28.017  1.00 25.25           O  
ANISOU  886  O   SER A 119     3610   2448   3537   -907    538   -451       O  
ATOM    887  CB  SER A 119       0.862  24.545  29.618  1.00 29.22           C  
ANISOU  887  CB  SER A 119     3986   3073   4044   -809    732   -253       C  
ATOM    888  OG  SER A 119      -0.502  24.133  29.529  1.00 33.47           O  
ANISOU  888  OG  SER A 119     4368   3710   4640   -885    807   -125       O  
ATOM    889  N   LYS A 120       3.855  24.073  30.269  1.00 26.40           N  
ANISOU  889  N   LYS A 120     3813   2699   3519   -704    619   -393       N  
ATOM    890  CA  LYS A 120       5.220  24.581  30.270  1.00 28.30           C  
ANISOU  890  CA  LYS A 120     4046   3047   3659   -702    512   -483       C  
ATOM    891  C   LYS A 120       6.126  23.684  29.460  1.00 26.11           C  
ANISOU  891  C   LYS A 120     3745   2784   3392   -690    502   -446       C  
ATOM    892  O   LYS A 120       6.922  24.155  28.676  1.00 26.07           O  
ANISOU  892  O   LYS A 120     3681   2836   3389   -760    420   -498       O  
ATOM    893  CB  LYS A 120       5.775  24.773  31.680  1.00 29.96           C  
ANISOU  893  CB  LYS A 120     4280   3423   3679   -584    495   -500       C  
ATOM    894  CG  LYS A 120       5.411  26.139  32.304  1.00 40.48           C  
ANISOU  894  CG  LYS A 120     5710   4740   4930   -624    462   -614       C  
ATOM    895  CD  LYS A 120       6.054  26.405  33.698  1.00 46.16           C  
ANISOU  895  CD  LYS A 120     6485   5652   5404   -547    407   -682       C  
ATOM    896  CE  LYS A 120       5.166  25.899  34.851  1.00 44.09           C  
ANISOU  896  CE  LYS A 120     6295   5391   5067   -306    539   -568       C  
ATOM    897  NZ  LYS A 120       5.745  26.296  36.170  1.00 49.82           N  
ANISOU  897  NZ  LYS A 120     7103   6318   5510   -216    470   -659       N  
ATOM    898  N   VAL A 121       6.036  22.382  29.704  1.00 22.75           N  
ANISOU  898  N   VAL A 121     3598   2377   2669    162    -18   -122       N  
ATOM    899  CA  VAL A 121       6.921  21.434  29.096  1.00 21.94           C  
ANISOU  899  CA  VAL A 121     3447   2298   2591    148   -112    -90       C  
ATOM    900  C   VAL A 121       6.541  21.358  27.599  1.00 23.01           C  
ANISOU  900  C   VAL A 121     3440   2462   2842    135   -116    -91       C  
ATOM    901  O   VAL A 121       7.407  21.286  26.744  1.00 20.97           O  
ANISOU  901  O   VAL A 121     3129   2223   2617    128   -195    -93       O  
ATOM    902  CB  VAL A 121       6.759  20.080  29.779  1.00 24.54           C  
ANISOU  902  CB  VAL A 121     3844   2605   2877    152    -62    -34       C  
ATOM    903  CG1 VAL A 121       7.526  18.991  29.063  1.00 21.26           C  
ANISOU  903  CG1 VAL A 121     3393   2170   2513    162   -105      5       C  
ATOM    904  CG2 VAL A 121       7.248  20.199  31.321  1.00 23.58           C  
ANISOU  904  CG2 VAL A 121     3868   2502   2590    175    -81    -11       C  
ATOM    905  N   PHE A 122       5.243  21.330  27.313  1.00 22.74           N  
ANISOU  905  N   PHE A 122     3331   2460   2851    127    -29    -87       N  
ATOM    906  CA  PHE A 122       4.784  21.268  25.901  1.00 22.83           C  
ANISOU  906  CA  PHE A 122     3187   2559   2930    100    -48    -85       C  
ATOM    907  C   PHE A 122       5.375  22.487  25.130  1.00 22.22           C  
ANISOU  907  C   PHE A 122     3074   2495   2874    152   -114    -71       C  
ATOM    908  O   PHE A 122       5.863  22.330  23.998  1.00 22.07           O  
ANISOU  908  O   PHE A 122     2984   2526   2874    127   -177    -71       O  
ATOM    909  CB  PHE A 122       3.252  21.292  25.880  1.00 23.17           C  
ANISOU  909  CB  PHE A 122     3117   2690   2995     91     45    -68       C  
ATOM    910  CG  PHE A 122       2.628  21.185  24.508  1.00 24.69           C  
ANISOU  910  CG  PHE A 122     3122   3042   3218     46     11    -61       C  
ATOM    911  CD1 PHE A 122       2.122  19.963  24.052  1.00 26.39           C  
ANISOU  911  CD1 PHE A 122     3269   3328   3431    -98     31   -112       C  
ATOM    912  CD2 PHE A 122       2.541  22.301  23.672  1.00 25.37           C  
ANISOU  912  CD2 PHE A 122     3109   3212   3317    135    -32     -3       C  
ATOM    913  CE1 PHE A 122       1.522  19.849  22.794  1.00 29.13           C  
ANISOU  913  CE1 PHE A 122     3434   3869   3764   -177    -15   -126       C  
ATOM    914  CE2 PHE A 122       1.937  22.193  22.412  1.00 24.09           C  
ANISOU  914  CE2 PHE A 122     2761   3249   3142     97    -80     21       C  
ATOM    915  CZ  PHE A 122       1.359  20.986  22.010  1.00 26.85           C  
ANISOU  915  CZ  PHE A 122     3020   3716   3467    -68    -80    -47       C  
ATOM    916  N   TYR A 123       5.363  23.682  25.732  1.00 21.96           N  
ANISOU  916  N   TYR A 123     3110   2399   2834    214    -75    -65       N  
ATOM    917  CA  TYR A 123       5.842  24.867  24.991  1.00 21.44           C  
ANISOU  917  CA  TYR A 123     3036   2309   2803    253    -97    -42       C  
ATOM    918  C   TYR A 123       7.362  24.926  24.902  1.00 20.51           C  
ANISOU  918  C   TYR A 123     2975   2152   2667    190   -190    -81       C  
ATOM    919  O   TYR A 123       7.925  25.363  23.854  1.00 22.63           O  
ANISOU  919  O   TYR A 123     3191   2439   2969    185   -228    -55       O  
ATOM    920  CB  TYR A 123       5.311  26.184  25.607  1.00 23.67           C  
ANISOU  920  CB  TYR A 123     3403   2492   3099    336     21    -31       C  
ATOM    921  CG  TYR A 123       3.803  26.339  25.609  1.00 22.91           C  
ANISOU  921  CG  TYR A 123     3210   2457   3038    441    132     36       C  
ATOM    922  CD1 TYR A 123       3.050  26.113  24.441  1.00 23.78           C  
ANISOU  922  CD1 TYR A 123     3120   2733   3181    483    105    124       C  
ATOM    923  CD2 TYR A 123       3.133  26.779  26.740  1.00 24.17           C  
ANISOU  923  CD2 TYR A 123     3462   2536   3184    499    270     16       C  
ATOM    924  CE1 TYR A 123       1.671  26.367  24.404  1.00 21.44           C  
ANISOU  924  CE1 TYR A 123     2685   2546   2916    592    199    209       C  
ATOM    925  CE2 TYR A 123       1.753  27.013  26.712  1.00 25.21           C  
ANISOU  925  CE2 TYR A 123     3474   2742   3362    621    392     96       C  
ATOM    926  CZ  TYR A 123       1.026  26.747  25.554  1.00 22.78           C  
ANISOU  926  CZ  TYR A 123     2930   2629   3095    665    346    198       C  
ATOM    927  OH  TYR A 123      -0.332  26.959  25.532  1.00 28.44           O  
ANISOU  927  OH  TYR A 123     3478   3475   3851    788    453    292       O  
ATOM    928  N   LEU A 124       8.049  24.531  25.983  1.00 22.32           N  
ANISOU  928  N   LEU A 124     3297   2352   2831    145   -225   -128       N  
ATOM    929  CA  LEU A 124       9.514  24.451  25.936  1.00 21.32           C  
ANISOU  929  CA  LEU A 124     3171   2247   2680     89   -327   -150       C  
ATOM    930  C   LEU A 124       9.981  23.403  24.935  1.00 22.12           C  
ANISOU  930  C   LEU A 124     3168   2413   2821     96   -378   -117       C  
ATOM    931  O   LEU A 124      10.995  23.613  24.272  1.00 21.02           O  
ANISOU  931  O   LEU A 124     2976   2306   2705     72   -431   -116       O  
ATOM    932  CB  LEU A 124      10.118  24.211  27.322  1.00 19.46           C  
ANISOU  932  CB  LEU A 124     3027   2027   2338     53   -372   -183       C  
ATOM    933  CG  LEU A 124      10.009  25.430  28.275  1.00 22.25           C  
ANISOU  933  CG  LEU A 124     3513   2316   2624     -2   -322   -261       C  
ATOM    934  CD1 LEU A 124      10.264  25.046  29.724  1.00 26.06           C  
ANISOU  934  CD1 LEU A 124     4094   2854   2955    -36   -357   -291       C  
ATOM    935  CD2 LEU A 124      10.905  26.603  27.824  1.00 28.94           C  
ANISOU  935  CD2 LEU A 124     4368   3128   3499    -95   -344   -315       C  
ATOM    936  N   LYS A 125       9.267  22.270  24.818  1.00 22.29           N  
ANISOU  936  N   LYS A 125     3171   2447   2852    115   -341   -103       N  
ATOM    937  CA  LYS A 125       9.607  21.301  23.810  1.00 21.94           C  
ANISOU  937  CA  LYS A 125     3062   2432   2842    107   -350   -101       C  
ATOM    938  C   LYS A 125       9.418  21.931  22.422  1.00 23.48           C  
ANISOU  938  C   LYS A 125     3166   2687   3067     90   -356   -100       C  
ATOM    939  O   LYS A 125      10.316  21.795  21.570  1.00 22.02           O  
ANISOU  939  O   LYS A 125     2939   2532   2896     82   -384   -103       O  
ATOM    940  CB  LYS A 125       8.745  20.018  23.925  1.00 22.64           C  
ANISOU  940  CB  LYS A 125     3174   2493   2934     86   -275   -111       C  
ATOM    941  CG  LYS A 125       8.927  19.014  22.794  1.00 19.87           C  
ANISOU  941  CG  LYS A 125     2789   2148   2614     47   -246   -146       C  
ATOM    942  CD  LYS A 125       7.898  17.886  22.893  1.00 21.29           C  
ANISOU  942  CD  LYS A 125     3007   2285   2799    -28   -146   -184       C  
ATOM    943  CE  LYS A 125       7.619  17.198  21.538  1.00 22.24           C  
ANISOU  943  CE  LYS A 125     3081   2445   2923   -134   -106   -269       C  
ATOM    944  NZ  LYS A 125       7.029  18.299  20.604  1.00 25.55           N  
ANISOU  944  NZ  LYS A 125     3358   3044   3308   -162   -181   -268       N  
ATOM    945  N   MET A 126       8.281  22.624  22.184  1.00 23.12           N  
ANISOU  945  N   MET A 126     3084   2677   3025    103   -321    -77       N  
ATOM    946  CA  MET A 126       8.054  23.297  20.879  1.00 22.50           C  
ANISOU  946  CA  MET A 126     2916   2684   2950    115   -330    -36       C  
ATOM    947  C   MET A 126       9.198  24.263  20.598  1.00 23.10           C  
ANISOU  947  C   MET A 126     3022   2710   3044    123   -353    -13       C  
ATOM    948  O   MET A 126       9.725  24.293  19.491  1.00 22.08           O  
ANISOU  948  O   MET A 126     2841   2640   2907    107   -372      4       O  
ATOM    949  CB  MET A 126       6.749  24.100  20.840  1.00 22.30           C  
ANISOU  949  CB  MET A 126     2835   2709   2927    181   -284     30       C  
ATOM    950  CG  MET A 126       5.536  23.291  20.681  1.00 32.84           C  
ANISOU  950  CG  MET A 126     4069   4169   4239    146   -267     21       C  
ATOM    951  SD  MET A 126       4.109  24.396  20.423  1.00 31.28           S  
ANISOU  951  SD  MET A 126     3741   4097   4048    271   -219    146       S  
ATOM    952  CE  MET A 126       4.343  25.139  18.870  1.00 25.38           C  
ANISOU  952  CE  MET A 126     2905   3478   3260    326   -272    250       C  
ATOM    953  N   LYS A 127       9.617  25.015  21.620  1.00 23.28           N  
ANISOU  953  N   LYS A 127     3135   2630   3079    123   -342    -28       N  
ATOM    954  CA  LYS A 127      10.742  25.960  21.472  1.00 23.70           C  
ANISOU  954  CA  LYS A 127     3221   2632   3151     79   -352    -30       C  
ATOM    955  C   LYS A 127      12.020  25.201  21.050  1.00 22.27           C  
ANISOU  955  C   LYS A 127     2974   2519   2968     31   -418    -53       C  
ATOM    956  O   LYS A 127      12.664  25.599  20.081  1.00 22.97           O  
ANISOU  956  O   LYS A 127     3016   2636   3075      7   -412    -26       O  
ATOM    957  CB  LYS A 127      10.963  26.727  22.755  1.00 25.56           C  
ANISOU  957  CB  LYS A 127     3574   2763   3373     38   -330    -83       C  
ATOM    958  CG  LYS A 127      12.025  27.835  22.641  1.00 28.11           C  
ANISOU  958  CG  LYS A 127     3941   3022   3717    -58   -317   -109       C  
ATOM    959  CD  LYS A 127      11.994  28.755  23.847  1.00 23.84           C  
ANISOU  959  CD  LYS A 127     3551   2359   3147   -127   -261   -191       C  
ATOM    960  CE  LYS A 127      13.012  29.880  23.693  1.00 26.65           C  
ANISOU  960  CE  LYS A 127     3963   2634   3527   -272   -226   -240       C  
ATOM    961  NZ  LYS A 127      13.031  30.682  24.962  1.00 26.94           N  
ANISOU  961  NZ  LYS A 127     4170   2557   3509   -384   -168   -365       N  
ATOM    962  N   GLY A 128      12.314  24.080  21.708  1.00 21.52           N  
ANISOU  962  N   GLY A 128     2874   2450   2852     40   -457    -82       N  
ATOM    963  CA  GLY A 128      13.429  23.204  21.262  1.00 21.79           C  
ANISOU  963  CA  GLY A 128     2835   2546   2897     46   -488    -81       C  
ATOM    964  C   GLY A 128      13.270  22.763  19.800  1.00 23.55           C  
ANISOU  964  C   GLY A 128     3004   2812   3132     56   -446    -76       C  
ATOM    965  O   GLY A 128      14.246  22.788  19.024  1.00 20.86           O  
ANISOU  965  O   GLY A 128     2601   2519   2807     46   -440    -68       O  
ATOM    966  N   ASP A 129      12.064  22.285  19.462  1.00 21.38           N  
ANISOU  966  N   ASP A 129     2746   2544   2836     60   -412    -89       N  
ATOM    967  CA  ASP A 129      11.765  21.790  18.104  1.00 21.56           C  
ANISOU  967  CA  ASP A 129     2724   2641   2826     35   -380   -110       C  
ATOM    968  C   ASP A 129      12.046  22.890  17.073  1.00 21.83           C  
ANISOU  968  C   ASP A 129     2713   2741   2841     28   -383    -55       C  
ATOM    969  O   ASP A 129      12.669  22.637  16.052  1.00 24.94           O  
ANISOU  969  O   ASP A 129     3074   3194   3209     10   -359    -66       O  
ATOM    970  CB  ASP A 129      10.301  21.356  17.986  1.00 21.19           C  
ANISOU  970  CB  ASP A 129     2671   2640   2739      1   -363   -135       C  
ATOM    971  CG  ASP A 129       9.992  20.080  18.798  1.00 23.86           C  
ANISOU  971  CG  ASP A 129     3074   2898   3095    -19   -320   -193       C  
ATOM    972  OD1 ASP A 129      10.937  19.283  19.060  1.00 22.03           O  
ANISOU  972  OD1 ASP A 129     2891   2584   2894     12   -290   -210       O  
ATOM    973  OD2 ASP A 129       8.778  19.866  19.099  1.00 21.56           O  
ANISOU  973  OD2 ASP A 129     2774   2632   2787    -61   -301   -208       O  
ATOM    974  N   TYR A 130      11.523  24.093  17.287  1.00 22.00           N  
ANISOU  974  N   TYR A 130     2747   2742   2870     52   -387     12       N  
ATOM    975  CA  TYR A 130      11.606  25.103  16.208  1.00 22.57           C  
ANISOU  975  CA  TYR A 130     2795   2863   2917     64   -363     97       C  
ATOM    976  C   TYR A 130      13.013  25.721  16.100  1.00 23.18           C  
ANISOU  976  C   TYR A 130     2884   2884   3040     22   -342    108       C  
ATOM    977  O   TYR A 130      13.460  26.037  14.997  1.00 21.90           O  
ANISOU  977  O   TYR A 130     2693   2781   2847      9   -308    156       O  
ATOM    978  CB  TYR A 130      10.478  26.160  16.296  1.00 23.58           C  
ANISOU  978  CB  TYR A 130     2937   2979   3044    139   -337    198       C  
ATOM    979  CG  TYR A 130       9.156  25.615  15.821  1.00 20.17           C  
ANISOU  979  CG  TYR A 130     2419   2707   2538    168   -363    218       C  
ATOM    980  CD1 TYR A 130       8.757  25.737  14.480  1.00 21.37           C  
ANISOU  980  CD1 TYR A 130     2489   3043   2589    184   -379    296       C  
ATOM    981  CD2 TYR A 130       8.324  24.910  16.690  1.00 24.05           C  
ANISOU  981  CD2 TYR A 130     2897   3197   3042    157   -374    157       C  
ATOM    982  CE1 TYR A 130       7.560  25.152  14.021  1.00 23.11           C  
ANISOU  982  CE1 TYR A 130     2596   3472   2714    169   -425    296       C  
ATOM    983  CE2 TYR A 130       7.128  24.285  16.221  1.00 24.24           C  
ANISOU  983  CE2 TYR A 130     2813   3404   2995    134   -399    153       C  
ATOM    984  CZ  TYR A 130       6.782  24.398  14.884  1.00 22.46           C  
ANISOU  984  CZ  TYR A 130     2488   3386   2661    128   -434    213       C  
ATOM    985  OH  TYR A 130       5.613  23.817  14.406  1.00 23.93           O  
ANISOU  985  OH  TYR A 130     2537   3804   2751     71   -477    199       O  
ATOM    986  N   TYR A 131      13.750  25.821  17.203  1.00 22.14           N  
ANISOU  986  N   TYR A 131     2778   2671   2964    -16   -363     59       N  
ATOM    987  CA  TYR A 131      15.182  26.104  17.078  1.00 22.32           C  
ANISOU  987  CA  TYR A 131     2755   2703   3021    -86   -358     49       C  
ATOM    988  C   TYR A 131      15.958  24.972  16.343  1.00 23.89           C  
ANISOU  988  C   TYR A 131     2863   3005   3208    -67   -352     25       C  
ATOM    989  O   TYR A 131      16.949  25.233  15.641  1.00 24.49           O  
ANISOU  989  O   TYR A 131     2876   3131   3299   -106   -312     45       O  
ATOM    990  CB  TYR A 131      15.790  26.407  18.454  1.00 22.75           C  
ANISOU  990  CB  TYR A 131     2829   2710   3106   -151   -405     -4       C  
ATOM    991  CG  TYR A 131      15.647  27.856  18.888  1.00 24.97           C  
ANISOU  991  CG  TYR A 131     3212   2865   3409   -228   -357     -3       C  
ATOM    992  CD1 TYR A 131      16.261  28.893  18.143  1.00 24.62           C  
ANISOU  992  CD1 TYR A 131     3178   2776   3401   -311   -279     36       C  
ATOM    993  CD2 TYR A 131      14.902  28.209  20.035  1.00 20.99           C  
ANISOU  993  CD2 TYR A 131     2818   2265   2892   -223   -356    -45       C  
ATOM    994  CE1 TYR A 131      16.137  30.236  18.537  1.00 26.07           C  
ANISOU  994  CE1 TYR A 131     3496   2791   3619   -391   -191     30       C  
ATOM    995  CE2 TYR A 131      14.738  29.567  20.413  1.00 26.73           C  
ANISOU  995  CE2 TYR A 131     3678   2833   3645   -291   -267    -61       C  
ATOM    996  CZ  TYR A 131      15.355  30.563  19.662  1.00 30.32           C  
ANISOU  996  CZ  TYR A 131     4158   3216   4147   -375   -180    -25       C  
ATOM    997  OH  TYR A 131      15.226  31.895  19.999  1.00 27.97           O  
ANISOU  997  OH  TYR A 131     4026   2715   3888   -449    -53    -44       O  
ATOM    998  N   ARG A 132      15.581  23.715  16.589  1.00 23.20           N  
ANISOU  998  N   ARG A 132     2780   2930   3104    -11   -367    -21       N  
ATOM    999  CA  ARG A 132      16.171  22.578  15.880  1.00 23.73           C  
ANISOU  999  CA  ARG A 132     2803   3047   3165     24   -316    -55       C  
ATOM   1000  C   ARG A 132      15.854  22.662  14.360  1.00 23.69           C  
ANISOU 1000  C   ARG A 132     2801   3115   3085     -2   -255    -55       C  
ATOM   1001  O   ARG A 132      16.706  22.400  13.536  1.00 24.13           O  
ANISOU 1001  O   ARG A 132     2813   3223   3131     -1   -188    -64       O  
ATOM   1002  CB  ARG A 132      15.711  21.231  16.505  1.00 23.78           C  
ANISOU 1002  CB  ARG A 132     2861   2998   3176     81   -308   -106       C  
ATOM   1003  CG  ARG A 132      16.099  19.959  15.686  1.00 20.63           C  
ANISOU 1003  CG  ARG A 132     2473   2596   2772    120   -203   -161       C  
ATOM   1004  CD  ARG A 132      15.874  18.678  16.435  1.00 24.55           C  
ANISOU 1004  CD  ARG A 132     3043   2985   3299    184   -158   -190       C  
ATOM   1005  NE  ARG A 132      14.486  18.534  16.849  1.00 22.07           N  
ANISOU 1005  NE  ARG A 132     2810   2628   2950    122   -182   -226       N  
ATOM   1006  CZ  ARG A 132      13.565  17.931  16.126  1.00 24.14           C  
ANISOU 1006  CZ  ARG A 132     3128   2888   3156     38   -123   -315       C  
ATOM   1007  NH1 ARG A 132      13.877  17.433  14.913  1.00 23.45           N  
ANISOU 1007  NH1 ARG A 132     3055   2829   3025      1    -34   -391       N  
ATOM   1008  NH2 ARG A 132      12.318  17.882  16.584  1.00 19.79           N  
ANISOU 1008  NH2 ARG A 132     2608   2331   2580    -28   -151   -335       N  
ATOM   1009  N   TYR A 133      14.654  23.101  13.982  1.00 22.88           N  
ANISOU 1009  N   TYR A 133     2735   3044   2914    -19   -277    -30       N  
ATOM   1010  CA  TYR A 133      14.364  23.246  12.555  1.00 21.74           C  
ANISOU 1010  CA  TYR A 133     2581   3022   2659    -44   -240     -8       C  
ATOM   1011  C   TYR A 133      15.231  24.358  11.970  1.00 24.16           C  
ANISOU 1011  C   TYR A 133     2864   3341   2976    -54   -198     86       C  
ATOM   1012  O   TYR A 133      15.666  24.272  10.816  1.00 23.62           O  
ANISOU 1012  O   TYR A 133     2781   3366   2829    -74   -135     94       O  
ATOM   1013  CB  TYR A 133      12.873  23.544  12.297  1.00 19.37           C  
ANISOU 1013  CB  TYR A 133     2282   2808   2270    -43   -289     33       C  
ATOM   1014  CG  TYR A 133      11.955  22.502  12.927  1.00 24.13           C  
ANISOU 1014  CG  TYR A 133     2897   3401   2871    -68   -318    -63       C  
ATOM   1015  CD1 TYR A 133      12.365  21.162  13.057  1.00 22.22           C  
ANISOU 1015  CD1 TYR A 133     2695   3099   2647   -104   -267   -189       C  
ATOM   1016  CD2 TYR A 133      10.682  22.844  13.369  1.00 23.77           C  
ANISOU 1016  CD2 TYR A 133     2824   3395   2811    -51   -367    -19       C  
ATOM   1017  CE1 TYR A 133      11.527  20.216  13.627  1.00 22.45           C  
ANISOU 1017  CE1 TYR A 133     2758   3089   2681   -148   -263   -272       C  
ATOM   1018  CE2 TYR A 133       9.819  21.883  13.952  1.00 26.34           C  
ANISOU 1018  CE2 TYR A 133     3153   3718   3139   -101   -375   -107       C  
ATOM   1019  CZ  TYR A 133      10.248  20.576  14.050  1.00 25.80           C  
ANISOU 1019  CZ  TYR A 133     3144   3573   3085   -164   -322   -236       C  
ATOM   1020  OH  TYR A 133       9.430  19.639  14.639  1.00 24.22           O  
ANISOU 1020  OH  TYR A 133     2971   3336   2896   -229   -301   -317       O  
ATOM   1021  N   LEU A 134      15.463  25.424  12.756  1.00 23.84           N  
ANISOU 1021  N   LEU A 134     2838   3199   3023    -59   -213    149       N  
ATOM   1022  CA  LEU A 134      16.345  26.505  12.279  1.00 24.20           C  
ANISOU 1022  CA  LEU A 134     2877   3222   3096   -106   -145    228       C  
ATOM   1023  C   LEU A 134      17.767  25.954  12.161  1.00 25.90           C  
ANISOU 1023  C   LEU A 134     3002   3480   3357   -147   -106    172       C  
ATOM   1024  O   LEU A 134      18.482  26.249  11.179  1.00 28.10           O  
ANISOU 1024  O   LEU A 134     3247   3821   3609   -181    -19    215       O  
ATOM   1025  CB  LEU A 134      16.326  27.678  13.252  1.00 24.37           C  
ANISOU 1025  CB  LEU A 134     2958   3097   3206   -141   -146    265       C  
ATOM   1026  CG  LEU A 134      15.076  28.561  13.290  1.00 24.60           C  
ANISOU 1026  CG  LEU A 134     3080   3053   3216    -69   -130    363       C  
ATOM   1027  CD1 LEU A 134      15.289  29.608  14.416  1.00 25.50           C  
ANISOU 1027  CD1 LEU A 134     3283   2975   3430   -128    -94    347       C  
ATOM   1028  CD2 LEU A 134      14.963  29.300  11.924  1.00 23.49           C  
ANISOU 1028  CD2 LEU A 134     2960   2963   3001    -33    -46    514       C  
ATOM   1029  N   ALA A 135      18.172  25.114  13.114  1.00 23.17           N  
ANISOU 1029  N   ALA A 135     2608   3121   3073   -126   -156     94       N  
ATOM   1030  CA  ALA A 135      19.525  24.522  13.043  1.00 25.29           C  
ANISOU 1030  CA  ALA A 135     2757   3459   3394   -121   -113     68       C  
ATOM   1031  C   ALA A 135      19.775  23.619  11.835  1.00 26.96           C  
ANISOU 1031  C   ALA A 135     2955   3745   3545    -69     -9     38       C  
ATOM   1032  O   ALA A 135      20.910  23.540  11.326  1.00 26.62           O  
ANISOU 1032  O   ALA A 135     2811   3772   3531    -70     79     50       O  
ATOM   1033  CB  ALA A 135      19.860  23.756  14.351  1.00 22.67           C  
ANISOU 1033  CB  ALA A 135     2372   3115   3125    -66   -190     29       C  
ATOM   1034  N   GLU A 136      18.717  22.942  11.369  1.00 25.11           N  
ANISOU 1034  N   GLU A 136     2817   3505   3218    -40     -5    -13       N  
ATOM   1035  CA  GLU A 136      18.777  22.097  10.192  1.00 25.05           C  
ANISOU 1035  CA  GLU A 136     2840   3562   3115    -27    103    -78       C  
ATOM   1036  C   GLU A 136      19.279  22.850   8.948  1.00 27.88           C  
ANISOU 1036  C   GLU A 136     3177   4023   3393    -76    189    -16       C  
ATOM   1037  O   GLU A 136      19.959  22.267   8.093  1.00 29.80           O  
ANISOU 1037  O   GLU A 136     3407   4325   3593    -61    317    -64       O  
ATOM   1038  CB  GLU A 136      17.377  21.505   9.918  1.00 25.78           C  
ANISOU 1038  CB  GLU A 136     3037   3665   3092    -55     67   -152       C  
ATOM   1039  CG  GLU A 136      17.042  20.279  10.830  1.00 27.60           C  
ANISOU 1039  CG  GLU A 136     3317   3782   3389    -14     63   -246       C  
ATOM   1040  CD  GLU A 136      15.648  19.675  10.547  1.00 31.48           C  
ANISOU 1040  CD  GLU A 136     3895   4297   3768    -92     40   -339       C  
ATOM   1041  OE1 GLU A 136      14.820  20.301   9.820  1.00 30.95           O  
ANISOU 1041  OE1 GLU A 136     3820   4369   3570   -160    -16   -309       O  
ATOM   1042  OE2 GLU A 136      15.374  18.562  11.065  1.00 33.23           O  
ANISOU 1042  OE2 GLU A 136     4186   4410   4030    -88     84   -431       O  
ATOM   1043  N   VAL A 137      18.978  24.145   8.877  1.00 26.67           N  
ANISOU 1043  N   VAL A 137     3035   3874   3225   -124    145     97       N  
ATOM   1044  CA  VAL A 137      19.357  24.955   7.741  1.00 28.68           C  
ANISOU 1044  CA  VAL A 137     3293   4208   3396   -166    237    190       C  
ATOM   1045  C   VAL A 137      20.467  25.971   8.001  1.00 30.67           C  
ANISOU 1045  C   VAL A 137     3471   4413   3769   -229    293    272       C  
ATOM   1046  O   VAL A 137      21.007  26.531   7.052  1.00 33.80           O  
ANISOU 1046  O   VAL A 137     3862   4866   4113   -273    407    348       O  
ATOM   1047  CB  VAL A 137      18.096  25.615   7.015  1.00 29.67           C  
ANISOU 1047  CB  VAL A 137     3510   4404   3361   -162    194    289       C  
ATOM   1048  CG1 VAL A 137      17.043  24.578   6.769  1.00 28.79           C  
ANISOU 1048  CG1 VAL A 137     3434   4385   3120   -150    131    185       C  
ATOM   1049  CG2 VAL A 137      17.487  26.775   7.819  1.00 25.98           C  
ANISOU 1049  CG2 VAL A 137     3076   3818   2976   -146    125    404       C  
ATOM   1050  N   ALA A 138      20.731  26.282   9.266  1.00 29.95           N  
ANISOU 1050  N   ALA A 138     3333   4227   3819   -258    216    258       N  
ATOM   1051  CA  ALA A 138      21.698  27.309   9.607  1.00 31.77           C  
ANISOU 1051  CA  ALA A 138     3497   4421   4155   -373    259    308       C  
ATOM   1052  C   ALA A 138      23.117  26.803   9.350  1.00 34.00           C  
ANISOU 1052  C   ALA A 138     3603   4822   4493   -394    344    278       C  
ATOM   1053  O   ALA A 138      23.368  25.589   9.388  1.00 33.04           O  
ANISOU 1053  O   ALA A 138     3413   4767   4374   -286    345    209       O  
ATOM   1054  CB  ALA A 138      21.539  27.733  11.059  1.00 29.33           C  
ANISOU 1054  CB  ALA A 138     3194   4008   3943   -423    146    271       C  
ATOM   1055  N   THR A 139      24.043  27.738   9.101  1.00 35.45           N  
ANISOU 1055  N   THR A 139     3713   5026   4732   -530    436    335       N  
ATOM   1056  CA  THR A 139      25.479  27.426   9.132  1.00 38.41           C  
ANISOU 1056  CA  THR A 139     3860   5541   5193   -572    502    315       C  
ATOM   1057  C   THR A 139      26.253  28.427  10.000  1.00 39.95           C  
ANISOU 1057  C   THR A 139     3943   5735   5499   -776    468    314       C  
ATOM   1058  O   THR A 139      25.700  29.451  10.438  1.00 40.72           O  
ANISOU 1058  O   THR A 139     4186   5679   5608   -894    436    324       O  
ATOM   1059  CB  THR A 139      26.089  27.411   7.719  1.00 40.42           C  
ANISOU 1059  CB  THR A 139     4081   5889   5386   -574    696    367       C  
ATOM   1060  OG1 THR A 139      25.873  28.698   7.136  1.00 41.41           O  
ANISOU 1060  OG1 THR A 139     4332   5929   5474   -707    780    467       O  
ATOM   1061  CG2 THR A 139      25.411  26.308   6.852  1.00 39.77           C  
ANISOU 1061  CG2 THR A 139     4110   5835   5165   -405    738    326       C  
ATOM   1062  N   GLY A 140      27.528  28.144  10.251  1.00 42.29           N  
ANISOU 1062  N   GLY A 140     3981   6212   5877   -825    486    298       N  
ATOM   1063  CA  GLY A 140      28.429  29.166  10.814  1.00 43.13           C  
ANISOU 1063  CA  GLY A 140     3947   6371   6067  -1085    485    286       C  
ATOM   1064  C   GLY A 140      28.025  29.547  12.228  1.00 42.79           C  
ANISOU 1064  C   GLY A 140     3957   6259   6041  -1182    307    210       C  
ATOM   1065  O   GLY A 140      27.502  28.699  12.967  1.00 41.28           O  
ANISOU 1065  O   GLY A 140     3782   6079   5822  -1017    165    177       O  
ATOM   1066  N   GLU A 141      28.236  30.817  12.600  1.00 42.61           N  
ANISOU 1066  N   GLU A 141     3987   6146   6056  -1458    335    176       N  
ATOM   1067  CA  GLU A 141      27.885  31.296  13.939  1.00 42.21           C  
ANISOU 1067  CA  GLU A 141     4016   6021   6002  -1589    195     76       C  
ATOM   1068  C   GLU A 141      26.371  31.243  14.193  1.00 40.28           C  
ANISOU 1068  C   GLU A 141     4064   5540   5702  -1421    146     79       C  
ATOM   1069  O   GLU A 141      25.932  30.997  15.339  1.00 38.70           O  
ANISOU 1069  O   GLU A 141     3900   5333   5471  -1396     -1      5       O  
ATOM   1070  CB  GLU A 141      28.404  32.713  14.176  1.00 45.44           C  
ANISOU 1070  CB  GLU A 141     4468   6338   6461  -1950    286     15       C  
ATOM   1071  N   LYS A 142      25.582  31.422  13.129  1.00 38.53           N  
ANISOU 1071  N   LYS A 142     4027   5163   5451  -1298    266    174       N  
ATOM   1072  CA  LYS A 142      24.110  31.338  13.236  1.00 36.60           C  
ANISOU 1072  CA  LYS A 142     4013   4744   5150  -1122    225    199       C  
ATOM   1073  C   LYS A 142      23.675  29.961  13.678  1.00 33.50           C  
ANISOU 1073  C   LYS A 142     3553   4462   4712   -915     80    162       C  
ATOM   1074  O   LYS A 142      22.802  29.821  14.558  1.00 32.30           O  
ANISOU 1074  O   LYS A 142     3508   4227   4538   -852    -19    119       O  
ATOM   1075  CB  LYS A 142      23.431  31.691  11.912  1.00 37.08           C  
ANISOU 1075  CB  LYS A 142     4226   4704   5159  -1017    363    332       C  
ATOM   1076  N   ARG A 143      24.299  28.932  13.111  1.00 32.29           N  
ANISOU 1076  N   ARG A 143     3233   4483   4552   -808     90    178       N  
ATOM   1077  CA  ARG A 143      24.020  27.558  13.554  1.00 30.71           C  
ANISOU 1077  CA  ARG A 143     2981   4359   4327   -616    -11    145       C  
ATOM   1078  C   ARG A 143      24.339  27.352  15.053  1.00 31.01           C  
ANISOU 1078  C   ARG A 143     2928   4467   4390   -651   -163     87       C  
ATOM   1079  O   ARG A 143      23.511  26.810  15.813  1.00 29.95           O  
ANISOU 1079  O   ARG A 143     2888   4271   4220   -546   -257     60       O  
ATOM   1080  CB  ARG A 143      24.756  26.529  12.703  1.00 30.61           C  
ANISOU 1080  CB  ARG A 143     2823   4491   4317   -492     72    167       C  
ATOM   1081  CG  ARG A 143      24.214  25.100  12.886  1.00 28.96           C  
ANISOU 1081  CG  ARG A 143     2649   4275   4078   -280     33    138       C  
ATOM   1082  CD  ARG A 143      25.050  24.078  12.129  1.00 34.27           C  
ANISOU 1082  CD  ARG A 143     3194   5059   4769   -148    155    148       C  
ATOM   1083  NE  ARG A 143      24.466  22.750  12.214  1.00 33.46           N  
ANISOU 1083  NE  ARG A 143     3181   4890   4641     34    164    108       N  
ATOM   1084  CZ  ARG A 143      24.699  21.874  13.196  1.00 37.11           C  
ANISOU 1084  CZ  ARG A 143     3576   5368   5155    165    103    118       C  
ATOM   1085  NH1 ARG A 143      25.505  22.186  14.205  1.00 31.44           N  
ANISOU 1085  NH1 ARG A 143     2674   4779   4493    137     -3    168       N  
ATOM   1086  NH2 ARG A 143      24.114  20.679  13.166  1.00 32.71           N  
ANISOU 1086  NH2 ARG A 143     3142   4704   4581    314    155     80       N  
ATOM   1087  N   ALA A 144      25.523  27.776  15.461  1.00 33.63           N  
ANISOU 1087  N   ALA A 144     3067   4948   4764   -810   -185     70       N  
ATOM   1088  CA  ALA A 144      25.968  27.650  16.859  1.00 34.68           C  
ANISOU 1088  CA  ALA A 144     3077   5217   4881   -872   -345     21       C  
ATOM   1089  C   ALA A 144      24.906  28.264  17.790  1.00 34.51           C  
ANISOU 1089  C   ALA A 144     3291   5012   4808   -945   -415    -50       C  
ATOM   1090  O   ALA A 144      24.530  27.666  18.802  1.00 33.05           O  
ANISOU 1090  O   ALA A 144     3126   4861   4570   -855   -537    -70       O  
ATOM   1091  CB  ALA A 144      27.344  28.322  17.046  1.00 37.92           C  
ANISOU 1091  CB  ALA A 144     3243   5837   5328  -1113   -353     -2       C  
ATOM   1092  N   THR A 145      24.454  29.477  17.466  1.00 33.99           N  
ANISOU 1092  N   THR A 145     3409   4747   4760  -1099   -316    -77       N  
ATOM   1093  CA  THR A 145      23.430  30.149  18.281  1.00 34.49           C  
ANISOU 1093  CA  THR A 145     3710   4608   4788  -1150   -334   -142       C  
ATOM   1094  C   THR A 145      22.103  29.365  18.382  1.00 32.00           C  
ANISOU 1094  C   THR A 145     3533   4194   4433   -904   -369   -106       C  
ATOM   1095  O   THR A 145      21.586  29.156  19.489  1.00 29.41           O  
ANISOU 1095  O   THR A 145     3274   3847   4053   -880   -459   -160       O  
ATOM   1096  CB  THR A 145      23.153  31.591  17.775  1.00 35.42           C  
ANISOU 1096  CB  THR A 145     4021   4486   4951  -1311   -169   -145       C  
ATOM   1097  OG1 THR A 145      24.395  32.285  17.687  1.00 39.97           O  
ANISOU 1097  OG1 THR A 145     4469   5148   5568  -1579   -119   -192       O  
ATOM   1098  CG2 THR A 145      22.274  32.357  18.762  1.00 37.55           C  
ANISOU 1098  CG2 THR A 145     4528   4544   5195  -1376   -158   -230       C  
ATOM   1099  N   VAL A 146      21.544  28.930  17.250  1.00 27.35           N  
ANISOU 1099  N   VAL A 146     2981   3560   3852   -743   -294    -23       N  
ATOM   1100  CA  VAL A 146      20.250  28.235  17.310  1.00 27.51           C  
ANISOU 1100  CA  VAL A 146     3116   3507   3831   -558   -322     -4       C  
ATOM   1101  C   VAL A 146      20.361  26.841  17.947  1.00 27.27           C  
ANISOU 1101  C   VAL A 146     2991   3594   3775   -432   -424    -22       C  
ATOM   1102  O   VAL A 146      19.439  26.372  18.656  1.00 25.35           O  
ANISOU 1102  O   VAL A 146     2842   3293   3497   -347   -473    -40       O  
ATOM   1103  CB  VAL A 146      19.534  28.184  15.927  1.00 27.34           C  
ANISOU 1103  CB  VAL A 146     3157   3442   3790   -452   -229     78       C  
ATOM   1104  CG1 VAL A 146      19.128  29.624  15.502  1.00 27.99           C  
ANISOU 1104  CG1 VAL A 146     3380   3368   3890   -524   -120    138       C  
ATOM   1105  CG2 VAL A 146      20.404  27.553  14.882  1.00 24.95           C  
ANISOU 1105  CG2 VAL A 146     2719   3273   3486   -425   -179    106       C  
ATOM   1106  N   VAL A 147      21.506  26.188  17.737  1.00 26.61           N  
ANISOU 1106  N   VAL A 147     2724   3672   3715   -409   -436     -4       N  
ATOM   1107  CA  VAL A 147      21.759  24.917  18.402  1.00 27.28           C  
ANISOU 1107  CA  VAL A 147     2723   3856   3788   -266   -508     11       C  
ATOM   1108  C   VAL A 147      21.784  25.092  19.930  1.00 28.11           C  
ANISOU 1108  C   VAL A 147     2832   4009   3841   -323   -638    -21       C  
ATOM   1109  O   VAL A 147      21.164  24.320  20.664  1.00 27.99           O  
ANISOU 1109  O   VAL A 147     2890   3962   3785   -206   -685    -10       O  
ATOM   1110  CB  VAL A 147      23.069  24.286  17.896  1.00 29.91           C  
ANISOU 1110  CB  VAL A 147     2836   4362   4166   -202   -473     61       C  
ATOM   1111  CG1 VAL A 147      23.506  23.123  18.829  1.00 29.63           C  
ANISOU 1111  CG1 VAL A 147     2694   4442   4122    -37   -549    113       C  
ATOM   1112  CG2 VAL A 147      22.879  23.816  16.408  1.00 25.90           C  
ANISOU 1112  CG2 VAL A 147     2368   3797   3677   -113   -325     76       C  
ATOM   1113  N   GLU A 148      22.474  26.122  20.406  1.00 28.98           N  
ANISOU 1113  N   GLU A 148     2276   4311   4425   -450   -570     97       N  
ATOM   1114  CA  GLU A 148      22.517  26.403  21.839  1.00 32.28           C  
ANISOU 1114  CA  GLU A 148     2689   5009   4566   -820   -755    107       C  
ATOM   1115  C   GLU A 148      21.114  26.645  22.399  1.00 30.06           C  
ANISOU 1115  C   GLU A 148     2857   4310   4254   -816   -685   -204       C  
ATOM   1116  O   GLU A 148      20.750  26.112  23.447  1.00 29.98           O  
ANISOU 1116  O   GLU A 148     2851   4391   4148   -811   -762   -161       O  
ATOM   1117  CB  GLU A 148      23.413  27.611  22.122  1.00 33.37           C  
ANISOU 1117  CB  GLU A 148     2818   5479   4384  -1486   -881     85       C  
ATOM   1118  CG  GLU A 148      23.792  27.773  23.585  1.00 43.19           C  
ANISOU 1118  CG  GLU A 148     3999   7214   5199  -2061  -1100    190       C  
ATOM   1119  CD  GLU A 148      24.652  28.997  23.832  1.00 53.78           C  
ANISOU 1119  CD  GLU A 148     5469   8897   6068  -2969  -1197    126       C  
ATOM   1120  OE1 GLU A 148      25.133  29.595  22.847  1.00 58.78           O  
ANISOU 1120  OE1 GLU A 148     6106   9462   6765  -3058  -1114     82       O  
ATOM   1121  OE2 GLU A 148      24.846  29.360  25.011  1.00 63.53           O  
ANISOU 1121  OE2 GLU A 148     6857  10472   6810  -3680  -1342    107       O  
ATOM   1122  N   SER A 149      20.338  27.454  21.686  1.00 27.74           N  
ANISOU 1122  N   SER A 149     2899   3609   4033   -764   -503   -436       N  
ATOM   1123  CA  SER A 149      18.965  27.796  22.073  1.00 28.37           C  
ANISOU 1123  CA  SER A 149     3332   3362   4085   -639   -336   -582       C  
ATOM   1124  C   SER A 149      18.050  26.572  22.052  1.00 26.63           C  
ANISOU 1124  C   SER A 149     2968   3149   4002   -297   -373   -493       C  
ATOM   1125  O   SER A 149      17.245  26.419  22.992  1.00 25.75           O  
ANISOU 1125  O   SER A 149     2985   2997   3802   -269   -355   -512       O  
ATOM   1126  CB  SER A 149      18.395  28.875  21.159  1.00 28.55           C  
ANISOU 1126  CB  SER A 149     3624   3067   4156   -521    -57   -656       C  
ATOM   1127  OG  SER A 149      19.123  30.075  21.284  1.00 31.53           O  
ANISOU 1127  OG  SER A 149     4330   3315   4336   -910     81   -788       O  
ATOM   1128  N   SER A 150      18.193  25.698  21.041  1.00 23.88           N  
ANISOU 1128  N   SER A 150     2439   2828   3807   -114   -380   -407       N  
ATOM   1129  CA  SER A 150      17.423  24.437  21.012  1.00 25.72           C  
ANISOU 1129  CA  SER A 150     2683   3037   4053     29   -361   -355       C  
ATOM   1130  C   SER A 150      17.738  23.603  22.269  1.00 26.13           C  
ANISOU 1130  C   SER A 150     2682   3196   4049     61   -438   -265       C  
ATOM   1131  O   SER A 150      16.833  23.165  23.004  1.00 24.75           O  
ANISOU 1131  O   SER A 150     2604   2999   3801     71   -452   -288       O  
ATOM   1132  CB  SER A 150      17.734  23.598  19.763  1.00 24.38           C  
ANISOU 1132  CB  SER A 150     2540   2776   3948     96   -238   -311       C  
ATOM   1133  OG  SER A 150      16.873  22.451  19.723  1.00 23.17           O  
ANISOU 1133  OG  SER A 150     2581   2543   3680     47   -151   -316       O  
ATOM   1134  N   GLU A 151      19.081  23.504  22.609  1.00 26.64           N  
ANISOU 1134  N   GLU A 151     2518   3490   4113     63   -500    -85       N  
ATOM   1135  CA  GLU A 151      19.383  22.580  23.701  1.00 28.14           C  
ANISOU 1135  CA  GLU A 151     2581   3877   4235    174   -536    134       C  
ATOM   1136  C   GLU A 151      18.919  23.199  25.035  1.00 27.88           C  
ANISOU 1136  C   GLU A 151     2622   3963   4007   -108   -716     14       C  
ATOM   1137  O   GLU A 151      18.427  22.491  25.912  1.00 26.55           O  
ANISOU 1137  O   GLU A 151     2500   3804   3783    -26   -731     61       O  
ATOM   1138  CB  GLU A 151      20.875  22.304  23.732  1.00 32.47           C  
ANISOU 1138  CB  GLU A 151     2731   4829   4778    295   -532    538       C  
ATOM   1139  CG  GLU A 151      21.329  21.313  24.763  1.00 45.33           C  
ANISOU 1139  CG  GLU A 151     4120   6777   6326    529   -505    947       C  
ATOM   1140  CD  GLU A 151      22.811  21.038  24.720  1.00 60.14           C  
ANISOU 1140  CD  GLU A 151     5451   9225   8173    754   -442   1554       C  
ATOM   1141  OE1 GLU A 151      23.544  21.664  23.883  1.00 56.79           O  
ANISOU 1141  OE1 GLU A 151     4833   8956   7790    664   -452   1617       O  
ATOM   1142  OE2 GLU A 151      23.267  20.301  25.631  1.00 68.22           O  
ANISOU 1142  OE2 GLU A 151     6161  10669   9092    990   -410   2041       O  
ATOM   1143  N   LYS A 152      19.052  24.473  25.151  1.00 27.87           N  
ANISOU 1143  N   LYS A 152     2734   3980   3875   -448   -776   -148       N  
ATOM   1144  CA  LYS A 152      18.628  25.138  26.381  1.00 30.11           C  
ANISOU 1144  CA  LYS A 152     3286   4254   3899   -775   -815   -295       C  
ATOM   1145  C   LYS A 152      17.118  24.902  26.608  1.00 27.88           C  
ANISOU 1145  C   LYS A 152     3260   3637   3697   -514   -664   -419       C  
ATOM   1146  O   LYS A 152      16.700  24.601  27.727  1.00 27.15           O  
ANISOU 1146  O   LYS A 152     3262   3583   3472   -566   -700   -420       O  
ATOM   1147  CB  LYS A 152      18.929  26.630  26.267  1.00 32.34           C  
ANISOU 1147  CB  LYS A 152     3897   4412   3977  -1209   -717   -495       C  
ATOM   1148  CG  LYS A 152      18.663  27.458  27.514  1.00 41.91           C  
ANISOU 1148  CG  LYS A 152     5614   5509   4801  -1683   -618   -681       C  
ATOM   1149  CD  LYS A 152      19.256  28.894  27.365  1.00 45.65           C  
ANISOU 1149  CD  LYS A 152     6564   5829   4954  -2280   -435   -881       C  
ATOM   1150  N   ALA A 153      16.314  25.000  25.538  1.00 25.02           N  
ANISOU 1150  N   ALA A 153     2941   3055   3511   -264   -512   -457       N  
ATOM   1151  CA  ALA A 153      14.880  24.821  25.644  1.00 24.87           C  
ANISOU 1151  CA  ALA A 153     3015   2928   3506    -63   -384   -435       C  
ATOM   1152  C   ALA A 153      14.552  23.363  25.991  1.00 24.54           C  
ANISOU 1152  C   ALA A 153     2846   2996   3483     15   -495   -356       C  
ATOM   1153  O   ALA A 153      13.793  23.106  26.937  1.00 22.69           O  
ANISOU 1153  O   ALA A 153     2691   2771   3159     36   -482   -342       O  
ATOM   1154  CB  ALA A 153      14.171  25.263  24.338  1.00 22.67           C  
ANISOU 1154  CB  ALA A 153     2679   2614   3321    105   -234   -357       C  
ATOM   1155  N   TYR A 154      15.182  22.409  25.300  1.00 22.81           N  
ANISOU 1155  N   TYR A 154     2517   2799   3351     62   -523   -296       N  
ATOM   1156  CA  TYR A 154      14.935  21.008  25.619  1.00 23.92           C  
ANISOU 1156  CA  TYR A 154     2720   2909   3460    130   -479   -222       C  
ATOM   1157  C   TYR A 154      15.365  20.648  27.056  1.00 25.06           C  
ANISOU 1157  C   TYR A 154     2814   3175   3534    176   -566   -124       C  
ATOM   1158  O   TYR A 154      14.646  19.905  27.752  1.00 26.44           O  
ANISOU 1158  O   TYR A 154     3100   3311   3636    199   -538   -111       O  
ATOM   1159  CB  TYR A 154      15.685  20.093  24.662  1.00 24.25           C  
ANISOU 1159  CB  TYR A 154     2833   2815   3566    233   -306   -138       C  
ATOM   1160  CG  TYR A 154      15.064  19.944  23.296  1.00 24.16           C  
ANISOU 1160  CG  TYR A 154     2996   2681   3504     58   -187   -238       C  
ATOM   1161  CD1 TYR A 154      13.680  19.666  23.139  1.00 23.38           C  
ANISOU 1161  CD1 TYR A 154     3004   2669   3211   -218   -202   -287       C  
ATOM   1162  CD2 TYR A 154      15.854  20.106  22.158  1.00 23.07           C  
ANISOU 1162  CD2 TYR A 154     2872   2445   3449     99    -76   -231       C  
ATOM   1163  CE1 TYR A 154      13.116  19.497  21.850  1.00 24.24           C  
ANISOU 1163  CE1 TYR A 154     3230   2838   3144   -548   -135   -314       C  
ATOM   1164  CE2 TYR A 154      15.322  19.908  20.873  1.00 24.82           C  
ANISOU 1164  CE2 TYR A 154     3301   2588   3543   -160     37   -317       C  
ATOM   1165  CZ  TYR A 154      13.959  19.615  20.729  1.00 19.94           C  
ANISOU 1165  CZ  TYR A 154     2780   2129   2669   -530    -13   -355       C  
ATOM   1166  OH  TYR A 154      13.510  19.405  19.424  1.00 23.83           O  
ANISOU 1166  OH  TYR A 154     3453   2681   2921   -941     66   -391       O  
ATOM   1167  N   SER A 155      16.524  21.164  27.487  1.00 25.88           N  
ANISOU 1167  N   SER A 155     2725   3507   3603    117   -686    -18       N  
ATOM   1168  CA  SER A 155      17.045  20.892  28.825  1.00 28.85           C  
ANISOU 1168  CA  SER A 155     2961   4181   3819     59   -817    164       C  
ATOM   1169  C   SER A 155      16.059  21.408  29.903  1.00 28.16           C  
ANISOU 1169  C   SER A 155     3116   4015   3569   -148   -872    -38       C  
ATOM   1170  O   SER A 155      15.779  20.718  30.871  1.00 29.41           O  
ANISOU 1170  O   SER A 155     3287   4245   3642    -97   -902     49       O  
ATOM   1171  CB  SER A 155      18.427  21.523  28.997  1.00 30.27           C  
ANISOU 1171  CB  SER A 155     2825   4814   3861   -170   -984    368       C  
ATOM   1172  OG  SER A 155      18.971  21.129  30.238  1.00 36.94           O  
ANISOU 1172  OG  SER A 155     3430   6127   4478   -272  -1137    666       O  
ATOM   1173  N   GLU A 156      15.521  22.610  29.722  1.00 25.80           N  
ANISOU 1173  N   GLU A 156     3056   3524   3222   -317   -799   -265       N  
ATOM   1174  CA  GLU A 156      14.593  23.126  30.707  1.00 28.91           C  
ANISOU 1174  CA  GLU A 156     3765   3766   3453   -412   -696   -392       C  
ATOM   1175  C   GLU A 156      13.288  22.334  30.746  1.00 27.74           C  
ANISOU 1175  C   GLU A 156     3615   3514   3411   -131   -604   -348       C  
ATOM   1176  O   GLU A 156      12.754  22.061  31.844  1.00 28.32           O  
ANISOU 1176  O   GLU A 156     3807   3591   3362   -145   -593   -343       O  
ATOM   1177  CB  GLU A 156      14.295  24.615  30.512  1.00 30.66           C  
ANISOU 1177  CB  GLU A 156     4370   3707   3572   -543   -441   -559       C  
ATOM   1178  CG  GLU A 156      13.446  25.084  31.694  1.00 38.61           C  
ANISOU 1178  CG  GLU A 156     5814   4495   4360   -594   -202   -635       C  
ATOM   1179  CD  GLU A 156      13.236  26.574  31.756  1.00 46.38           C  
ANISOU 1179  CD  GLU A 156     7415   5061   5147   -716    246   -772       C  
ATOM   1180  OE1 GLU A 156      13.622  27.264  30.777  1.00 46.06           O  
ANISOU 1180  OE1 GLU A 156     7415   4907   5178   -719    356   -801       O  
ATOM   1181  OE2 GLU A 156      12.672  27.020  32.793  1.00 48.81           O  
ANISOU 1181  OE2 GLU A 156     8235   5100   5210   -787    559   -837       O  
ATOM   1182  N   ALA A 157      12.760  21.990  29.566  1.00 23.92           N  
ANISOU 1182  N   ALA A 157     3007   2996   3087     30   -543   -301       N  
ATOM   1183  CA  ALA A 157      11.608  21.110  29.469  1.00 25.19           C  
ANISOU 1183  CA  ALA A 157     3125   3206   3240    101   -500   -218       C  
ATOM   1184  C   ALA A 157      11.850  19.759  30.189  1.00 28.81           C  
ANISOU 1184  C   ALA A 157     3622   3670   3656     91   -566   -184       C  
ATOM   1185  O   ALA A 157      10.967  19.244  30.975  1.00 28.21           O  
ANISOU 1185  O   ALA A 157     3613   3623   3482     80   -543   -151       O  
ATOM   1186  CB  ALA A 157      11.230  20.877  27.943  1.00 22.43           C  
ANISOU 1186  CB  ALA A 157     2658   2929   2937     53   -462   -163       C  
ATOM   1187  N   HIS A 158      13.069  19.248  30.021  1.00 25.86           N  
ANISOU 1187  N   HIS A 158     3197   3287   3342    152   -595   -122       N  
ATOM   1188  CA  HIS A 158      13.446  17.956  30.597  1.00 28.81           C  
ANISOU 1188  CA  HIS A 158     3629   3635   3684    288   -521     33       C  
ATOM   1189  C   HIS A 158      13.435  18.008  32.124  1.00 29.19           C  
ANISOU 1189  C   HIS A 158     3633   3852   3604    271   -649     96       C  
ATOM   1190  O   HIS A 158      12.927  17.090  32.771  1.00 29.81           O  
ANISOU 1190  O   HIS A 158     3840   3867   3621    338   -571    154       O  
ATOM   1191  CB  HIS A 158      14.841  17.569  30.087  1.00 30.98           C  
ANISOU 1191  CB  HIS A 158     3775   3948   4047    503   -425    256       C  
ATOM   1192  CG  HIS A 158      15.290  16.209  30.525  1.00 39.97           C  
ANISOU 1192  CG  HIS A 158     5016   5009   5162    815   -169    552       C  
ATOM   1193  ND1 HIS A 158      16.289  16.026  31.460  1.00 52.29           N  
ANISOU 1193  ND1 HIS A 158     6253   6945   6670   1040   -226    945       N  
ATOM   1194  CD2 HIS A 158      14.885  14.969  30.154  1.00 41.85           C  
ANISOU 1194  CD2 HIS A 158     5692   4846   5363    925    216    568       C  
ATOM   1195  CE1 HIS A 158      16.484  14.731  31.646  1.00 52.97           C  
ANISOU 1195  CE1 HIS A 158     6529   6844   6752   1430    156   1251       C  
ATOM   1196  NE2 HIS A 158      15.656  14.070  30.852  1.00 53.54           N  
ANISOU 1196  NE2 HIS A 158     7155   6359   6830   1350    470    983       N  
ATOM   1197  N   GLU A 159      13.938  19.106  32.681  1.00 28.95           N  
ANISOU 1197  N   GLU A 159     3508   4018   3474     92   -814     59       N  
ATOM   1198  CA  GLU A 159      14.030  19.278  34.135  1.00 33.08           C  
ANISOU 1198  CA  GLU A 159     4058   4742   3767    -81   -938    100       C  
ATOM   1199  C   GLU A 159      12.642  19.416  34.744  1.00 29.93           C  
ANISOU 1199  C   GLU A 159     3932   4124   3316    -94   -834    -72       C  
ATOM   1200  O   GLU A 159      12.348  18.869  35.795  1.00 30.01           O  
ANISOU 1200  O   GLU A 159     4000   4194   3209    -92   -858    -11       O  
ATOM   1201  CB  GLU A 159      14.858  20.513  34.476  1.00 34.17           C  
ANISOU 1201  CB  GLU A 159     4198   5110   3675   -490  -1079     44       C  
ATOM   1202  CG  GLU A 159      16.321  20.316  34.211  1.00 42.87           C  
ANISOU 1202  CG  GLU A 159     4882   6677   4729   -541  -1240    362       C  
ATOM   1203  CD  GLU A 159      16.876  19.106  34.934  1.00 53.01           C  
ANISOU 1203  CD  GLU A 159     5832   8354   5956   -293  -1294    812       C  
ATOM   1204  OE1 GLU A 159      16.758  19.052  36.182  1.00 51.95           O  
ANISOU 1204  OE1 GLU A 159     5726   8462   5551   -519  -1421    875       O  
ATOM   1205  OE2 GLU A 159      17.403  18.208  34.247  1.00 54.23           O  
ANISOU 1205  OE2 GLU A 159     5754   8533   6317    163  -1134   1131       O  
ATOM   1206  N   ILE A 160      11.775  20.144  34.071  1.00 27.93           N  
ANISOU 1206  N   ILE A 160     3800   3672   3142    -59   -684   -206       N  
ATOM   1207  CA  ILE A 160      10.440  20.337  34.609  1.00 26.96           C  
ANISOU 1207  CA  ILE A 160     3841   3444   2960     20   -515   -222       C  
ATOM   1208  C   ILE A 160       9.666  19.003  34.517  1.00 27.50           C  
ANISOU 1208  C   ILE A 160     3794   3577   3076    107   -528   -118       C  
ATOM   1209  O   ILE A 160       8.917  18.617  35.445  1.00 25.96           O  
ANISOU 1209  O   ILE A 160     3679   3402   2782    123   -485    -78       O  
ATOM   1210  CB  ILE A 160       9.728  21.441  33.844  1.00 26.01           C  
ANISOU 1210  CB  ILE A 160     3781   3209   2892    147   -273   -208       C  
ATOM   1211  CG1 ILE A 160      10.445  22.787  34.070  1.00 29.39           C  
ANISOU 1211  CG1 ILE A 160     4546   3432   3187    -15   -131   -356       C  
ATOM   1212  CG2 ILE A 160       8.249  21.581  34.293  1.00 25.67           C  
ANISOU 1212  CG2 ILE A 160     3775   3186   2793    364    -15    -34       C  
ATOM   1213  CD1 ILE A 160       9.975  23.878  33.064  1.00 30.47           C  
ANISOU 1213  CD1 ILE A 160     4765   3401   3412    207    192   -285       C  
ATOM   1214  N   SER A 161       9.773  18.342  33.363  1.00 24.97           N  
ANISOU 1214  N   SER A 161     3373   3263   2853     92   -535    -89       N  
ATOM   1215  CA  SER A 161       9.053  17.086  33.205  1.00 27.10           C  
ANISOU 1215  CA  SER A 161     3714   3537   3047    -12   -472    -38       C  
ATOM   1216  C   SER A 161       9.514  15.985  34.178  1.00 26.87           C  
ANISOU 1216  C   SER A 161     3850   3395   2966     63   -445      7       C  
ATOM   1217  O   SER A 161       8.669  15.214  34.666  1.00 28.83           O  
ANISOU 1217  O   SER A 161     4232   3633   3090    -39   -373     30       O  
ATOM   1218  CB  SER A 161       9.044  16.613  31.741  1.00 28.20           C  
ANISOU 1218  CB  SER A 161     3890   3647   3176   -195   -402    -53       C  
ATOM   1219  OG  SER A 161      10.293  16.087  31.383  1.00 33.64           O  
ANISOU 1219  OG  SER A 161     4717   4107   3959    -69   -321    -66       O  
ATOM   1220  N   LYS A 162      10.824  15.931  34.493  1.00 27.15           N  
ANISOU 1220  N   LYS A 162     3825   3429   3060    239   -489     96       N  
ATOM   1221  CA  LYS A 162      11.342  14.955  35.424  1.00 29.65           C  
ANISOU 1221  CA  LYS A 162     4202   3749   3315    416   -424    292       C  
ATOM   1222  C   LYS A 162      10.754  15.185  36.801  1.00 30.30           C  
ANISOU 1222  C   LYS A 162     4289   3962   3259    336   -548    266       C  
ATOM   1223  O   LYS A 162      10.541  14.255  37.569  1.00 31.17           O  
ANISOU 1223  O   LYS A 162     4523   4030   3289    423   -459    378       O  
ATOM   1224  CB  LYS A 162      12.882  15.093  35.509  1.00 34.13           C  
ANISOU 1224  CB  LYS A 162     4497   4555   3915    616   -489    562       C  
ATOM   1225  CG  LYS A 162      13.637  13.831  35.405  1.00 39.47           C  
ANISOU 1225  CG  LYS A 162     5234   5139   4622   1006   -177    925       C  
ATOM   1226  N   GLU A 163      10.534  16.447  37.143  1.00 29.73           N  
ANISOU 1226  N   GLU A 163     4170   3995   3133    179   -681    127       N  
ATOM   1227  CA  GLU A 163      10.080  16.788  38.490  1.00 31.96           C  
ANISOU 1227  CA  GLU A 163     4573   4341   3231     78   -720     91       C  
ATOM   1228  C   GLU A 163       8.580  16.638  38.668  1.00 31.28           C  
ANISOU 1228  C   GLU A 163     4610   4137   3139    106   -570     36       C  
ATOM   1229  O   GLU A 163       8.095  16.271  39.752  1.00 31.26           O  
ANISOU 1229  O   GLU A 163     4719   4147   3012    103   -546     67       O  
ATOM   1230  CB  GLU A 163      10.521  18.202  38.869  1.00 32.32           C  
ANISOU 1230  CB  GLU A 163     4725   4441   3113   -167   -775    -36       C  
ATOM   1231  CG  GLU A 163      10.312  18.537  40.376  1.00 36.77           C  
ANISOU 1231  CG  GLU A 163     5556   5046   3369   -390   -769    -84       C  
ATOM   1232  CD  GLU A 163      11.510  18.153  41.234  1.00 40.38           C  
ANISOU 1232  CD  GLU A 163     5837   5936   3571   -631  -1035    114       C  
ATOM   1233  N   HIS A 164       7.840  16.941  37.613  1.00 28.79           N  
ANISOU 1233  N   HIS A 164     4215   3804   2920    117   -472     23       N  
ATOM   1234  CA  HIS A 164       6.396  17.121  37.713  1.00 30.47           C  
ANISOU 1234  CA  HIS A 164     4385   4117   3075    145   -322    122       C  
ATOM   1235  C   HIS A 164       5.533  16.151  36.938  1.00 29.72           C  
ANISOU 1235  C   HIS A 164     4156   4207   2928    -41   -312    233       C  
ATOM   1236  O   HIS A 164       4.326  16.125  37.120  1.00 31.93           O  
ANISOU 1236  O   HIS A 164     4293   4747   3093    -86   -227    420       O  
ATOM   1237  CB  HIS A 164       6.039  18.568  37.367  1.00 30.32           C  
ANISOU 1237  CB  HIS A 164     4346   4088   3084    305   -131    178       C  
ATOM   1238  CG  HIS A 164       6.495  19.536  38.414  1.00 30.41           C  
ANISOU 1238  CG  HIS A 164     4722   3853   2979    329      5     48       C  
ATOM   1239  ND1 HIS A 164       7.627  20.304  38.267  1.00 36.33           N  
ANISOU 1239  ND1 HIS A 164     5651   4460   3692    172    -44   -126       N  
ATOM   1240  CD2 HIS A 164       6.045  19.767  39.669  1.00 30.49           C  
ANISOU 1240  CD2 HIS A 164     5025   3744   2817    358    188     44       C  
ATOM   1241  CE1 HIS A 164       7.828  21.012  39.368  1.00 34.07           C  
ANISOU 1241  CE1 HIS A 164     5805   3986   3155      8    112   -249       C  
ATOM   1242  NE2 HIS A 164       6.889  20.690  40.239  1.00 38.01           N  
ANISOU 1242  NE2 HIS A 164     6404   4459   3578    144    268   -159       N  
ATOM   1243  N   MET A 165       6.117  15.387  36.023  1.00 29.16           N  
ANISOU 1243  N   MET A 165     4157   4043   2879   -209   -352    159       N  
ATOM   1244  CA  MET A 165       5.285  14.445  35.274  1.00 30.47           C  
ANISOU 1244  CA  MET A 165     4369   4361   2847   -609   -293    215       C  
ATOM   1245  C   MET A 165       5.708  13.000  35.498  1.00 31.91           C  
ANISOU 1245  C   MET A 165     5001   4203   2922   -758   -148    116       C  
ATOM   1246  O   MET A 165       6.888  12.726  35.721  1.00 29.57           O  
ANISOU 1246  O   MET A 165     4875   3593   2768   -461    -79     80       O  
ATOM   1247  CB  MET A 165       5.312  14.768  33.781  1.00 30.88           C  
ANISOU 1247  CB  MET A 165     4292   4563   2879   -820   -314    231       C  
ATOM   1248  CG  MET A 165       4.990  16.225  33.433  1.00 33.65           C  
ANISOU 1248  CG  MET A 165     4239   5201   3347   -567   -353    402       C  
ATOM   1249  SD  MET A 165       5.304  16.581  31.663  1.00 42.00           S  
ANISOU 1249  SD  MET A 165     5159   6397   4403   -771   -394    415       S  
ATOM   1250  CE  MET A 165       3.730  16.199  30.992  1.00 44.35           C  
ANISOU 1250  CE  MET A 165     5109   7453   4289  -1328   -432    778       C  
ATOM   1251  N   GLN A 166       4.798  12.067  35.341  1.00 29.96           N  
ANISOU 1251  N   GLN A 166     4315   4013   3053   -140    444   -603       N  
ATOM   1252  CA  GLN A 166       5.162  10.655  35.329  1.00 32.12           C  
ANISOU 1252  CA  GLN A 166     4577   4364   3262   -148    278   -400       C  
ATOM   1253  C   GLN A 166       6.030  10.295  34.104  1.00 28.43           C  
ANISOU 1253  C   GLN A 166     4063   3798   2942    -91    100   -335       C  
ATOM   1254  O   GLN A 166       5.899  10.907  33.078  1.00 29.17           O  
ANISOU 1254  O   GLN A 166     4111   3766   3207    -35    112   -388       O  
ATOM   1255  CB  GLN A 166       3.907   9.787  35.353  1.00 32.80           C  
ANISOU 1255  CB  GLN A 166     4602   4436   3423   -122    354   -249       C  
ATOM   1256  CG  GLN A 166       2.881  10.155  36.360  1.00 45.89           C  
ANISOU 1256  CG  GLN A 166     6275   6172   4987   -157    575   -303       C  
ATOM   1257  CD  GLN A 166       3.141   9.545  37.670  1.00 55.35           C  
ANISOU 1257  CD  GLN A 166     7556   7579   5894   -261    574   -237       C  
ATOM   1258  OE1 GLN A 166       4.272   9.306  38.014  1.00 64.07           O  
ANISOU 1258  OE1 GLN A 166     8721   8786   6836   -320    417   -213       O  
ATOM   1259  NE2 GLN A 166       2.096   9.268  38.420  1.00 58.32           N  
ANISOU 1259  NE2 GLN A 166     7920   8038   6202   -290    746   -181       N  
ATOM   1260  N   PRO A 167       6.897   9.300  34.238  1.00 28.38           N  
ANISOU 1260  N   PRO A 167     4062   3852   2871   -104    -50   -207       N  
ATOM   1261  CA  PRO A 167       7.754   8.850  33.154  1.00 27.85           C  
ANISOU 1261  CA  PRO A 167     3950   3691   2941    -45   -180   -156       C  
ATOM   1262  C   PRO A 167       6.955   8.317  31.974  1.00 26.30           C  
ANISOU 1262  C   PRO A 167     3706   3352   2936     14   -165   -107       C  
ATOM   1263  O   PRO A 167       7.474   8.272  30.888  1.00 25.36           O  
ANISOU 1263  O   PRO A 167     3562   3150   2922     53   -223   -127       O  
ATOM   1264  CB  PRO A 167       8.601   7.707  33.781  1.00 27.66           C  
ANISOU 1264  CB  PRO A 167     3920   3750   2839    -61   -305     13       C  
ATOM   1265  CG  PRO A 167       8.008   7.429  35.095  1.00 29.96           C  
ANISOU 1265  CG  PRO A 167     4252   4185   2944   -136   -254     88       C  
ATOM   1266  CD  PRO A 167       7.200   8.622  35.505  1.00 29.85           C  
ANISOU 1266  CD  PRO A 167     4288   4210   2842   -180    -94    -97       C  
ATOM   1267  N   THR A 168       5.711   7.909  32.204  1.00 26.58           N  
ANISOU 1267  N   THR A 168     3725   3376   2998      2    -85    -44       N  
ATOM   1268  CA  THR A 168       4.862   7.474  31.107  1.00 25.12           C  
ANISOU 1268  CA  THR A 168     3485   3079   2979     20    -88     -3       C  
ATOM   1269  C   THR A 168       4.091   8.609  30.443  1.00 25.34           C  
ANISOU 1269  C   THR A 168     3457   3068   3104     40    -15    -75       C  
ATOM   1270  O   THR A 168       3.403   8.378  29.439  1.00 26.11           O  
ANISOU 1270  O   THR A 168     3494   3104   3321     35    -44    -28       O  
ATOM   1271  CB  THR A 168       3.843   6.358  31.513  1.00 27.75           C  
ANISOU 1271  CB  THR A 168     3795   3405   3345    -18    -59    136       C  
ATOM   1272  OG1 THR A 168       2.987   6.805  32.578  1.00 28.91           O  
ANISOU 1272  OG1 THR A 168     3930   3646   3410    -42     76    148       O  
ATOM   1273  CG2 THR A 168       4.530   5.046  31.883  1.00 26.40           C  
ANISOU 1273  CG2 THR A 168     3657   3214   3159    -27   -142    258       C  
ATOM   1274  N   HIS A 169       4.097   9.811  31.028  1.00 25.36           N  
ANISOU 1274  N   HIS A 169     3468   3101   3066     50     86   -177       N  
ATOM   1275  CA  HIS A 169       3.279  10.875  30.452  1.00 25.71           C  
ANISOU 1275  CA  HIS A 169     3433   3074   3261     87    175   -207       C  
ATOM   1276  C   HIS A 169       3.670  11.083  28.969  1.00 23.94           C  
ANISOU 1276  C   HIS A 169     3170   2785   3142    105     62   -186       C  
ATOM   1277  O   HIS A 169       4.840  11.261  28.668  1.00 25.15           O  
ANISOU 1277  O   HIS A 169     3373   2938   3244    106     -9   -245       O  
ATOM   1278  CB  HIS A 169       3.424  12.174  31.248  1.00 24.94           C  
ANISOU 1278  CB  HIS A 169     3368   2971   3137     96    317   -355       C  
ATOM   1279  CG  HIS A 169       2.349  13.180  30.952  1.00 30.49           C  
ANISOU 1279  CG  HIS A 169     3966   3575   4044    154    464   -357       C  
ATOM   1280  ND1 HIS A 169       2.244  13.819  29.737  1.00 28.41           N  
ANISOU 1280  ND1 HIS A 169     3611   3215   3968    198    416   -298       N  
ATOM   1281  CD2 HIS A 169       1.330  13.656  31.714  1.00 32.94           C  
ANISOU 1281  CD2 HIS A 169     4231   3866   4420    180    671   -389       C  
ATOM   1282  CE1 HIS A 169       1.178  14.608  29.745  1.00 30.86           C  
ANISOU 1282  CE1 HIS A 169     3806   3441   4477    258    567   -263       C  
ATOM   1283  NE2 HIS A 169       0.642  14.571  30.953  1.00 33.33           N  
ANISOU 1283  NE2 HIS A 169     4147   3786   4731    255    742   -339       N  
ATOM   1284  N   PRO A 170       2.685  11.109  28.056  1.00 23.08           N  
ANISOU 1284  N   PRO A 170     2959   2641   3168    107     47    -88       N  
ATOM   1285  CA  PRO A 170       3.003  11.229  26.627  1.00 22.76           C  
ANISOU 1285  CA  PRO A 170     2891   2584   3174     94    -67    -52       C  
ATOM   1286  C   PRO A 170       3.854  12.483  26.279  1.00 22.23           C  
ANISOU 1286  C   PRO A 170     2829   2478   3138    130    -52   -116       C  
ATOM   1287  O   PRO A 170       4.692  12.458  25.346  1.00 20.24           O  
ANISOU 1287  O   PRO A 170     2602   2238   2849    113   -140   -121       O  
ATOM   1288  CB  PRO A 170       1.617  11.306  25.948  1.00 22.61           C  
ANISOU 1288  CB  PRO A 170     2733   2566   3291     74    -79     90       C  
ATOM   1289  CG  PRO A 170       0.656  10.730  26.916  1.00 29.99           C  
ANISOU 1289  CG  PRO A 170     3632   3515   4247     66      5    132       C  
ATOM   1290  CD  PRO A 170       1.238  10.977  28.304  1.00 25.61           C  
ANISOU 1290  CD  PRO A 170     3174   2965   3593    105    128     12       C  
ATOM   1291  N   ILE A 171       3.642  13.562  27.011  1.00 21.31           N  
ANISOU 1291  N   ILE A 171     2691   2307   3099    173     78   -171       N  
ATOM   1292  CA  ILE A 171       4.376  14.785  26.712  1.00 23.58           C  
ANISOU 1292  CA  ILE A 171     2979   2524   3458    193    103   -228       C  
ATOM   1293  C   ILE A 171       5.821  14.611  27.144  1.00 23.10           C  
ANISOU 1293  C   ILE A 171     3029   2504   3244    158     50   -352       C  
ATOM   1294  O   ILE A 171       6.750  14.966  26.413  1.00 21.33           O  
ANISOU 1294  O   ILE A 171     2807   2271   3026    147    -15   -354       O  
ATOM   1295  CB  ILE A 171       3.786  16.053  27.345  1.00 25.59           C  
ANISOU 1295  CB  ILE A 171     3183   2661   3878    243    280   -281       C  
ATOM   1296  CG1 ILE A 171       2.398  16.367  26.747  1.00 26.44           C  
ANISOU 1296  CG1 ILE A 171     3125   2715   4205    297    327   -104       C  
ATOM   1297  CG2 ILE A 171       4.766  17.249  27.101  1.00 23.90           C  
ANISOU 1297  CG2 ILE A 171     2993   2350   3740    240    298   -361       C  
ATOM   1298  CD1 ILE A 171       1.749  17.592  27.351  1.00 34.74           C  
ANISOU 1298  CD1 ILE A 171     4105   3611   5485    373    542   -149       C  
ATOM   1299  N   ARG A 172       6.026  13.977  28.297  1.00 23.68           N  
ANISOU 1299  N   ARG A 172     3178   2644   3174    133     67   -422       N  
ATOM   1300  CA  ARG A 172       7.403  13.649  28.715  1.00 22.98           C  
ANISOU 1300  CA  ARG A 172     3164   2624   2945     94    -18   -488       C  
ATOM   1301  C   ARG A 172       8.114  12.693  27.752  1.00 23.47           C  
ANISOU 1301  C   ARG A 172     3216   2713   2988    103   -142   -411       C  
ATOM   1302  O   ARG A 172       9.321  12.872  27.416  1.00 21.74           O  
ANISOU 1302  O   ARG A 172     2999   2508   2755     95   -200   -439       O  
ATOM   1303  CB  ARG A 172       7.355  13.064  30.137  1.00 23.86           C  
ANISOU 1303  CB  ARG A 172     3341   2831   2892     53      8   -524       C  
ATOM   1304  CG  ARG A 172       8.730  12.618  30.668  1.00 27.82           C  
ANISOU 1304  CG  ARG A 172     3888   3433   3251      6   -107   -536       C  
ATOM   1305  CD  ARG A 172       8.727  12.533  32.203  1.00 26.60           C  
ANISOU 1305  CD  ARG A 172     3803   3403   2901    -70    -77   -585       C  
ATOM   1306  NE  ARG A 172       9.979  11.846  32.589  1.00 28.82           N  
ANISOU 1306  NE  ARG A 172     4085   3798   3067   -110   -229   -514       N  
ATOM   1307  CZ  ARG A 172      10.272  11.401  33.791  1.00 31.08           C  
ANISOU 1307  CZ  ARG A 172     4411   4242   3157   -186   -278   -473       C  
ATOM   1308  NH1 ARG A 172       9.416  11.573  34.802  1.00 26.83           N  
ANISOU 1308  NH1 ARG A 172     3941   3780   2472   -247   -165   -528       N  
ATOM   1309  NH2 ARG A 172      11.434  10.763  33.971  1.00 30.23           N  
ANISOU 1309  NH2 ARG A 172     4260   4223   3001   -203   -435   -356       N  
ATOM   1310  N   LEU A 173       7.378  11.674  27.284  1.00 21.48           N  
ANISOU 1310  N   LEU A 173     2950   2461   2749    112   -169   -326       N  
ATOM   1311  CA  LEU A 173       7.927  10.712  26.335  1.00 21.74           C  
ANISOU 1311  CA  LEU A 173     2992   2494   2774    113   -249   -292       C  
ATOM   1312  C   LEU A 173       8.245  11.356  24.987  1.00 22.13           C  
ANISOU 1312  C   LEU A 173     3008   2531   2869    108   -268   -290       C  
ATOM   1313  O   LEU A 173       9.299  11.066  24.413  1.00 22.00           O  
ANISOU 1313  O   LEU A 173     3005   2527   2828    113   -298   -315       O  
ATOM   1314  CB  LEU A 173       6.932   9.568  26.126  1.00 20.42           C  
ANISOU 1314  CB  LEU A 173     2827   2312   2621     91   -264   -227       C  
ATOM   1315  CG  LEU A 173       6.875   8.601  27.316  1.00 20.22           C  
ANISOU 1315  CG  LEU A 173     2837   2298   2548     91   -258   -190       C  
ATOM   1316  CD1 LEU A 173       5.712   7.643  27.177  1.00 22.04           C  
ANISOU 1316  CD1 LEU A 173     3055   2496   2824     52   -258   -117       C  
ATOM   1317  CD2 LEU A 173       8.167   7.792  27.474  1.00 21.38           C  
ANISOU 1317  CD2 LEU A 173     3014   2438   2672    118   -310   -186       C  
ATOM   1318  N   GLY A 174       7.383  12.269  24.528  1.00 21.27           N  
ANISOU 1318  N   GLY A 174     2842   2402   2837    102   -241   -241       N  
ATOM   1319  CA  GLY A 174       7.599  12.890  23.220  1.00 21.43           C  
ANISOU 1319  CA  GLY A 174     2822   2435   2887     83   -270   -190       C  
ATOM   1320  C   GLY A 174       8.774  13.840  23.307  1.00 21.94           C  
ANISOU 1320  C   GLY A 174     2883   2477   2975     97   -247   -240       C  
ATOM   1321  O   GLY A 174       9.463  14.068  22.300  1.00 21.68           O  
ANISOU 1321  O   GLY A 174     2836   2475   2927     77   -270   -212       O  
ATOM   1322  N   LEU A 175       8.902  14.528  24.442  1.00 21.46           N  
ANISOU 1322  N   LEU A 175     2833   2367   2955    111   -192   -310       N  
ATOM   1323  CA  LEU A 175      10.105  15.336  24.703  1.00 22.66           C  
ANISOU 1323  CA  LEU A 175     2988   2499   3123     93   -185   -380       C  
ATOM   1324  C   LEU A 175      11.383  14.505  24.595  1.00 24.49           C  
ANISOU 1324  C   LEU A 175     3237   2806   3262     86   -250   -403       C  
ATOM   1325  O   LEU A 175      12.334  14.881  23.863  1.00 23.00           O  
ANISOU 1325  O   LEU A 175     3012   2630   3099     73   -261   -387       O  
ATOM   1326  CB  LEU A 175      10.033  16.069  26.049  1.00 22.68           C  
ANISOU 1326  CB  LEU A 175     3024   2452   3143     73   -118   -495       C  
ATOM   1327  CG  LEU A 175      11.339  16.669  26.591  1.00 23.46           C  
ANISOU 1327  CG  LEU A 175     3141   2559   3216     11   -141   -595       C  
ATOM   1328  CD1 LEU A 175      11.765  17.823  25.575  1.00 22.59           C  
ANISOU 1328  CD1 LEU A 175     2965   2356   3261     -2   -121   -550       C  
ATOM   1329  CD2 LEU A 175      11.087  17.314  27.988  1.00 23.94           C  
ANISOU 1329  CD2 LEU A 175     3265   2588   3244    -45    -65   -748       C  
ATOM   1330  N   ALA A 176      11.439  13.387  25.328  1.00 25.30           N  
ANISOU 1330  N   ALA A 176     3378   2952   3281    100   -281   -419       N  
ATOM   1331  CA  ALA A 176      12.634  12.544  25.232  1.00 24.79           C  
ANISOU 1331  CA  ALA A 176     3300   2935   3184    117   -328   -410       C  
ATOM   1332  C   ALA A 176      12.893  12.147  23.771  1.00 24.02           C  
ANISOU 1332  C   ALA A 176     3185   2834   3106    136   -310   -383       C  
ATOM   1333  O   ALA A 176      14.059  12.165  23.320  1.00 23.88           O  
ANISOU 1333  O   ALA A 176     3123   2841   3111    146   -304   -385       O  
ATOM   1334  CB  ALA A 176      12.505  11.278  26.152  1.00 26.24           C  
ANISOU 1334  CB  ALA A 176     3515   3143   3311    140   -362   -382       C  
ATOM   1335  N   LEU A 177      11.842  11.770  23.030  1.00 21.43           N  
ANISOU 1335  N   LEU A 177     2888   2494   2760    125   -298   -360       N  
ATOM   1336  CA  LEU A 177      12.008  11.411  21.624  1.00 22.17           C  
ANISOU 1336  CA  LEU A 177     2989   2615   2819    105   -279   -358       C  
ATOM   1337  C   LEU A 177      12.698  12.511  20.826  1.00 23.11           C  
ANISOU 1337  C   LEU A 177     3057   2773   2951     82   -256   -326       C  
ATOM   1338  O   LEU A 177      13.662  12.240  20.118  1.00 24.94           O  
ANISOU 1338  O   LEU A 177     3276   3041   3158     86   -214   -349       O  
ATOM   1339  CB  LEU A 177      10.644  11.029  20.977  1.00 21.96           C  
ANISOU 1339  CB  LEU A 177     2994   2601   2748     52   -301   -327       C  
ATOM   1340  CG  LEU A 177      10.663  10.440  19.555  1.00 23.91           C  
ANISOU 1340  CG  LEU A 177     3282   2905   2899    -12   -290   -356       C  
ATOM   1341  CD1 LEU A 177      11.419   9.079  19.459  1.00 29.31           C  
ANISOU 1341  CD1 LEU A 177     4026   3538   3573     16   -231   -470       C  
ATOM   1342  CD2 LEU A 177       9.215  10.297  18.960  1.00 24.55           C  
ANISOU 1342  CD2 LEU A 177     3370   3033   2925   -105   -355   -296       C  
ATOM   1343  N   ASN A 178      12.181  13.736  20.889  1.00 22.40           N  
ANISOU 1343  N   ASN A 178     2929   2662   2918     60   -265   -265       N  
ATOM   1344  CA  ASN A 178      12.754  14.836  20.081  1.00 22.69           C  
ANISOU 1344  CA  ASN A 178     2909   2719   2995     28   -243   -197       C  
ATOM   1345  C   ASN A 178      14.092  15.338  20.620  1.00 23.47           C  
ANISOU 1345  C   ASN A 178     2965   2797   3157     33   -226   -241       C  
ATOM   1346  O   ASN A 178      15.002  15.699  19.859  1.00 24.02           O  
ANISOU 1346  O   ASN A 178     2985   2909   3233     10   -195   -203       O  
ATOM   1347  CB  ASN A 178      11.734  15.987  19.981  1.00 22.46           C  
ANISOU 1347  CB  ASN A 178     2835   2633   3066     12   -249    -90       C  
ATOM   1348  CG  ASN A 178      10.578  15.635  19.058  1.00 21.66           C  
ANISOU 1348  CG  ASN A 178     2730   2601   2900    -23   -291     15       C  
ATOM   1349  OD1 ASN A 178      10.495  14.503  18.582  1.00 24.55           O  
ANISOU 1349  OD1 ASN A 178     3152   3047   3129    -51   -313    -33       O  
ATOM   1350  ND2 ASN A 178       9.716  16.611  18.735  1.00 19.69           N  
ANISOU 1350  ND2 ASN A 178     2401   2319   2761    -31   -304    168       N  
ATOM   1351  N   TYR A 179      14.254  15.348  21.921  1.00 20.86           N  
ANISOU 1351  N   TYR A 179     2644   2423   2857     46   -250   -313       N  
ATOM   1352  CA  TYR A 179      15.521  15.719  22.516  1.00 22.49           C  
ANISOU 1352  CA  TYR A 179     2801   2639   3105     22   -268   -350       C  
ATOM   1353  C   TYR A 179      16.594  14.736  22.079  1.00 24.58           C  
ANISOU 1353  C   TYR A 179     3022   2977   3341     60   -260   -339       C  
ATOM   1354  O   TYR A 179      17.667  15.102  21.748  1.00 25.16           O  
ANISOU 1354  O   TYR A 179     3015   3080   3465     41   -244   -314       O  
ATOM   1355  CB  TYR A 179      15.396  15.773  24.015  1.00 22.51           C  
ANISOU 1355  CB  TYR A 179     2838   2625   3091      1   -310   -430       C  
ATOM   1356  CG  TYR A 179      16.433  16.544  24.800  1.00 24.90           C  
ANISOU 1356  CG  TYR A 179     3097   2936   3427    -78   -351   -484       C  
ATOM   1357  CD1 TYR A 179      17.464  17.193  24.216  1.00 23.58           C  
ANISOU 1357  CD1 TYR A 179     2844   2771   3344   -121   -349   -449       C  
ATOM   1358  CD2 TYR A 179      16.352  16.606  26.158  1.00 26.62           C  
ANISOU 1358  CD2 TYR A 179     3362   3177   3577   -132   -395   -571       C  
ATOM   1359  CE1 TYR A 179      18.370  17.878  24.966  1.00 29.87           C  
ANISOU 1359  CE1 TYR A 179     3594   3579   4174   -222   -404   -502       C  
ATOM   1360  CE2 TYR A 179      17.246  17.275  26.885  1.00 29.25           C  
ANISOU 1360  CE2 TYR A 179     3664   3538   3910   -240   -451   -634       C  
ATOM   1361  CZ  TYR A 179      18.248  17.905  26.291  1.00 28.07           C  
ANISOU 1361  CZ  TYR A 179     3422   3378   3864   -288   -463   -601       C  
ATOM   1362  OH  TYR A 179      19.110  18.572  27.059  1.00 29.25           O  
ANISOU 1362  OH  TYR A 179     3538   3560   4016   -423   -535   -670       O  
ATOM   1363  N   SER A 180      16.272  13.469  22.047  1.00 23.10           N  
ANISOU 1363  N   SER A 180     2879   2799   3097    116   -254   -355       N  
ATOM   1364  CA  SER A 180      17.291  12.540  21.605  1.00 23.36           C  
ANISOU 1364  CA  SER A 180     2863   2862   3152    170   -209   -354       C  
ATOM   1365  C   SER A 180      17.560  12.669  20.106  1.00 24.11           C  
ANISOU 1365  C   SER A 180     2949   2996   3215    155   -110   -348       C  
ATOM   1366  O   SER A 180      18.692  12.481  19.698  1.00 23.38           O  
ANISOU 1366  O   SER A 180     2775   2936   3171    184    -42   -341       O  
ATOM   1367  CB  SER A 180      16.989  11.094  21.997  1.00 25.62           C  
ANISOU 1367  CB  SER A 180     3195   3110   3431    236   -209   -374       C  
ATOM   1368  OG  SER A 180      15.854  10.630  21.311  1.00 30.79           O  
ANISOU 1368  OG  SER A 180     3948   3737   4013    219   -178   -412       O  
ATOM   1369  N   VAL A 181      16.527  12.935  19.298  1.00 23.44           N  
ANISOU 1369  N   VAL A 181     2936   2928   3043    107   -101   -337       N  
ATOM   1370  CA  VAL A 181      16.740  13.214  17.856  1.00 25.33           C  
ANISOU 1370  CA  VAL A 181     3173   3251   3202     57    -22   -307       C  
ATOM   1371  C   VAL A 181      17.650  14.421  17.729  1.00 25.57           C  
ANISOU 1371  C   VAL A 181     3099   3305   3313     26     -6   -225       C  
ATOM   1372  O   VAL A 181      18.560  14.437  16.863  1.00 25.82           O  
ANISOU 1372  O   VAL A 181     3078   3410   3322     15     93   -206       O  
ATOM   1373  CB  VAL A 181      15.414  13.421  17.108  1.00 25.76           C  
ANISOU 1373  CB  VAL A 181     3298   3348   3141    -15    -60   -260       C  
ATOM   1374  CG1 VAL A 181      15.625  14.089  15.746  1.00 29.69           C  
ANISOU 1374  CG1 VAL A 181     3775   3967   3540    -96    -12   -168       C  
ATOM   1375  CG2 VAL A 181      14.735  12.039  16.870  1.00 26.43           C  
ANISOU 1375  CG2 VAL A 181     3485   3431   3126    -19    -51   -364       C  
ATOM   1376  N   PHE A 182      17.445  15.421  18.588  1.00 23.26           N  
ANISOU 1376  N   PHE A 182     2775   2942   3120      4    -82   -186       N  
ATOM   1377  CA  PHE A 182      18.330  16.607  18.590  1.00 24.63           C  
ANISOU 1377  CA  PHE A 182     2848   3103   3406    -47    -74   -120       C  
ATOM   1378  C   PHE A 182      19.790  16.169  18.773  1.00 25.46           C  
ANISOU 1378  C   PHE A 182     2854   3256   3566    -22    -38   -143       C  
ATOM   1379  O   PHE A 182      20.677  16.559  17.984  1.00 26.01           O  
ANISOU 1379  O   PHE A 182     2835   3384   3666    -51     39    -77       O  
ATOM   1380  CB  PHE A 182      17.915  17.618  19.689  1.00 24.45           C  
ANISOU 1380  CB  PHE A 182     2829   2965   3497    -84   -145   -137       C  
ATOM   1381  CG  PHE A 182      18.913  18.714  19.911  1.00 25.26           C  
ANISOU 1381  CG  PHE A 182     2836   3026   3735   -158   -147   -110       C  
ATOM   1382  CD1 PHE A 182      18.978  19.825  19.067  1.00 21.19           C  
ANISOU 1382  CD1 PHE A 182     2269   2474   3307   -218   -102     11       C  
ATOM   1383  CD2 PHE A 182      19.787  18.653  20.973  1.00 26.77           C  
ANISOU 1383  CD2 PHE A 182     2979   3221   3970   -187   -207   -186       C  
ATOM   1384  CE1 PHE A 182      19.908  20.855  19.281  1.00 24.58           C  
ANISOU 1384  CE1 PHE A 182     2607   2842   3890   -306   -102     37       C  
ATOM   1385  CE2 PHE A 182      20.732  19.675  21.204  1.00 25.41           C  
ANISOU 1385  CE2 PHE A 182     2712   3014   3927   -289   -225   -171       C  
ATOM   1386  CZ  PHE A 182      20.801  20.788  20.347  1.00 27.83           C  
ANISOU 1386  CZ  PHE A 182     2973   3255   4345   -350   -164    -69       C  
ATOM   1387  N   TYR A 183      20.048  15.299  19.751  1.00 23.83           N  
ANISOU 1387  N   TYR A 183     2642   3035   3378     36    -86   -209       N  
ATOM   1388  CA  TYR A 183      21.452  14.861  19.957  1.00 26.10           C  
ANISOU 1388  CA  TYR A 183     2791   3368   3756     72    -64   -187       C  
ATOM   1389  C   TYR A 183      21.984  14.090  18.768  1.00 25.11           C  
ANISOU 1389  C   TYR A 183     2635   3294   3611    135     95   -188       C  
ATOM   1390  O   TYR A 183      23.123  14.276  18.388  1.00 28.61           O  
ANISOU 1390  O   TYR A 183     2940   3789   4141    137    171   -135       O  
ATOM   1391  CB  TYR A 183      21.631  13.988  21.207  1.00 26.01           C  
ANISOU 1391  CB  TYR A 183     2761   3346   3777    127   -157   -206       C  
ATOM   1392  CG  TYR A 183      21.548  14.762  22.514  1.00 32.44           C  
ANISOU 1392  CG  TYR A 183     3574   4155   4595     36   -304   -217       C  
ATOM   1393  CD1 TYR A 183      20.676  14.361  23.527  1.00 38.25           C  
ANISOU 1393  CD1 TYR A 183     4414   4871   5250     41   -383   -263       C  
ATOM   1394  CD2 TYR A 183      22.372  15.865  22.751  1.00 38.48           C  
ANISOU 1394  CD2 TYR A 183     4240   4943   5439    -71   -353   -193       C  
ATOM   1395  CE1 TYR A 183      20.636  15.042  24.738  1.00 41.19           C  
ANISOU 1395  CE1 TYR A 183     4802   5260   5588    -60   -494   -304       C  
ATOM   1396  CE2 TYR A 183      22.332  16.558  23.958  1.00 42.12           C  
ANISOU 1396  CE2 TYR A 183     4720   5402   5883   -184   -477   -247       C  
ATOM   1397  CZ  TYR A 183      21.462  16.133  24.938  1.00 42.13           C  
ANISOU 1397  CZ  TYR A 183     4838   5398   5771   -177   -539   -311       C  
ATOM   1398  OH  TYR A 183      21.430  16.798  26.135  1.00 50.40           O  
ANISOU 1398  OH  TYR A 183     5923   6464   6762   -307   -639   -392       O  
ATOM   1399  N   TYR A 184      21.172  13.187  18.235  1.00 24.92           N  
ANISOU 1399  N   TYR A 184     2736   3254   3477    178    155   -261       N  
ATOM   1400  CA  TYR A 184      21.593  12.335  17.129  1.00 27.01           C  
ANISOU 1400  CA  TYR A 184     3008   3555   3700    224    334   -318       C  
ATOM   1401  C   TYR A 184      21.895  13.119  15.840  1.00 29.13           C  
ANISOU 1401  C   TYR A 184     3259   3935   3875    144    446   -272       C  
ATOM   1402  O   TYR A 184      23.007  12.969  15.251  1.00 28.06           O  
ANISOU 1402  O   TYR A 184     3015   3854   3791    174    602   -264       O  
ATOM   1403  CB  TYR A 184      20.579  11.206  16.868  1.00 26.95           C  
ANISOU 1403  CB  TYR A 184     3159   3495   3584    249    363   -435       C  
ATOM   1404  CG  TYR A 184      21.153  10.139  15.930  1.00 31.42           C  
ANISOU 1404  CG  TYR A 184     3740   4058   4141    303    575   -548       C  
ATOM   1405  CD1 TYR A 184      21.896   9.057  16.429  1.00 34.67           C  
ANISOU 1405  CD1 TYR A 184     4073   4359   4741    436    656   -582       C  
ATOM   1406  CD2 TYR A 184      20.977  10.240  14.556  1.00 38.29           C  
ANISOU 1406  CD2 TYR A 184     4694   5033   4820    218    705   -613       C  
ATOM   1407  CE1 TYR A 184      22.475   8.117  15.561  1.00 41.42           C  
ANISOU 1407  CE1 TYR A 184     4933   5173   5631    499    896   -707       C  
ATOM   1408  CE2 TYR A 184      21.510   9.274  13.679  1.00 43.19           C  
ANISOU 1408  CE2 TYR A 184     5350   5649   5413    254    938   -763       C  
ATOM   1409  CZ  TYR A 184      22.279   8.239  14.184  1.00 45.20           C  
ANISOU 1409  CZ  TYR A 184     5522   5757   5895    403   1049   -821       C  
ATOM   1410  OH  TYR A 184      22.798   7.287  13.319  1.00 51.57           O  
ANISOU 1410  OH  TYR A 184     6363   6521   6712    450   1320   -993       O  
ATOM   1411  N   GLU A 185      20.957  13.993  15.453  1.00 27.48           N  
ANISOU 1411  N   GLU A 185     3129   3761   3552     46    372   -213       N  
ATOM   1412  CA  GLU A 185      20.935  14.608  14.103  1.00 29.42           C  
ANISOU 1412  CA  GLU A 185     3389   4136   3653    -48    461   -138       C  
ATOM   1413  C   GLU A 185      21.597  15.973  14.080  1.00 30.33           C  
ANISOU 1413  C   GLU A 185     3373   4268   3882   -109    443     22       C  
ATOM   1414  O   GLU A 185      22.365  16.286  13.173  1.00 31.84           O  
ANISOU 1414  O   GLU A 185     3494   4567   4036   -152    573     91       O  
ATOM   1415  CB  GLU A 185      19.500  14.717  13.557  1.00 30.57           C  
ANISOU 1415  CB  GLU A 185     3671   4327   3617   -128    382   -113       C  
ATOM   1416  CG  GLU A 185      18.844  13.343  13.354  1.00 33.86           C  
ANISOU 1416  CG  GLU A 185     4225   4741   3901   -110    412   -281       C  
ATOM   1417  CD  GLU A 185      19.466  12.550  12.190  1.00 45.49           C  
ANISOU 1417  CD  GLU A 185     5745   6323   5218   -134    617   -401       C  
ATOM   1418  OE1 GLU A 185      20.275  13.132  11.421  1.00 49.26           O  
ANISOU 1418  OE1 GLU A 185     6152   6917   5647   -177    733   -326       O  
ATOM   1419  OE2 GLU A 185      19.136  11.351  12.020  1.00 49.10           O  
ANISOU 1419  OE2 GLU A 185     6313   6742   5599   -122    680   -578       O  
ATOM   1420  N   ILE A 186      21.393  16.752  15.128  1.00 27.42           N  
ANISOU 1420  N   ILE A 186     2968   3786   3664   -120    302     65       N  
ATOM   1421  CA  ILE A 186      21.987  18.095  15.161  1.00 27.40           C  
ANISOU 1421  CA  ILE A 186     2849   3757   3803   -198    283    199       C  
ATOM   1422  C   ILE A 186      23.404  18.066  15.772  1.00 28.15           C  
ANISOU 1422  C   ILE A 186     2786   3848   4063   -182    303    186       C  
ATOM   1423  O   ILE A 186      24.322  18.706  15.241  1.00 28.00           O  
ANISOU 1423  O   ILE A 186     2639   3880   4119   -241    379    292       O  
ATOM   1424  CB  ILE A 186      21.063  19.095  15.901  1.00 26.35           C  
ANISOU 1424  CB  ILE A 186     2757   3483   3770   -241    150    236       C  
ATOM   1425  CG1 ILE A 186      19.659  19.127  15.234  1.00 23.99           C  
ANISOU 1425  CG1 ILE A 186     2569   3205   3342   -251    125    299       C  
ATOM   1426  CG2 ILE A 186      21.696  20.507  15.984  1.00 26.11           C  
ANISOU 1426  CG2 ILE A 186     2614   3376   3930   -336    142    353       C  
ATOM   1427  CD1 ILE A 186      19.693  19.407  13.712  1.00 28.66           C  
ANISOU 1427  CD1 ILE A 186     3147   3949   3793   -323    208    460       C  
ATOM   1428  N   GLN A 187      23.580  17.482  16.865  1.00 26.77           N  
ANISOU 1428  N   GLN A 187     2596   3620   3955   -125    221     95       N  
ATOM   1429  CA  GLN A 187      24.888  17.416  17.496  1.00 29.94           C  
ANISOU 1429  CA  GLN A 187     2822   4040   4513   -120    204    116       C  
ATOM   1430  C   GLN A 187      25.655  16.163  17.154  1.00 30.34           C  
ANISOU 1430  C   GLN A 187     2792   4158   4578     -1    333     91       C  
ATOM   1431  O   GLN A 187      26.778  16.001  17.542  1.00 30.84           O  
ANISOU 1431  O   GLN A 187     2673   4252   4793     22    336    144       O  
ATOM   1432  CB  GLN A 187      24.788  17.627  18.990  1.00 29.93           C  
ANISOU 1432  CB  GLN A 187     2821   3968   4583   -156     19     65       C  
ATOM   1433  CG  GLN A 187      24.368  18.996  19.252  1.00 36.18           C  
ANISOU 1433  CG  GLN A 187     3652   4671   5424   -282    -53     76       C  
ATOM   1434  CD  GLN A 187      24.164  19.317  20.660  1.00 41.95           C  
ANISOU 1434  CD  GLN A 187     4420   5336   6185   -347   -205    -15       C  
ATOM   1435  OE1 GLN A 187      23.895  18.436  21.459  1.00 48.05           O  
ANISOU 1435  OE1 GLN A 187     5241   6134   6881   -286   -273    -82       O  
ATOM   1436  NE2 GLN A 187      24.251  20.562  20.993  1.00 36.74           N  
ANISOU 1436  NE2 GLN A 187     3747   4586   5628   -481   -250    -26       N  
ATOM   1437  N   ASN A 188      25.080  15.262  16.367  1.00 30.10           N  
ANISOU 1437  N   ASN A 188     2884   4145   4405     71    456     12       N  
ATOM   1438  CA  ASN A 188      25.835  14.069  15.966  1.00 33.15           C  
ANISOU 1438  CA  ASN A 188     3200   4556   4841    192    631    -39       C  
ATOM   1439  C   ASN A 188      26.569  13.433  17.154  1.00 33.64           C  
ANISOU 1439  C   ASN A 188     3112   4565   5105    284    543     -8       C  
ATOM   1440  O   ASN A 188      27.755  13.111  17.089  1.00 34.87           O  
ANISOU 1440  O   ASN A 188     3065   4750   5432    350    643     58       O  
ATOM   1441  CB  ASN A 188      26.827  14.410  14.853  1.00 35.91           C  
ANISOU 1441  CB  ASN A 188     3422   5014   5208    168    837     25       C  
ATOM   1442  CG  ASN A 188      27.735  13.246  14.506  1.00 42.29           C  
ANISOU 1442  CG  ASN A 188     4122   5824   6124    307   1057    -33       C  
ATOM   1443  OD1 ASN A 188      27.293  12.100  14.430  1.00 41.32           O  
ANISOU 1443  OD1 ASN A 188     4112   5628   5960    402   1135   -169       O  
ATOM   1444  ND2 ASN A 188      29.013  13.536  14.292  1.00 47.29           N  
ANISOU 1444  ND2 ASN A 188     4521   6521   6924    320   1172     73       N  
ATOM   1445  N   ALA A 189      25.814  13.271  18.230  1.00 28.66           N  
ANISOU 1445  N   ALA A 189     2573   3867   4448    281    357    -35       N  
ATOM   1446  CA  ALA A 189      26.216  12.720  19.506  1.00 30.06           C  
ANISOU 1446  CA  ALA A 189     2649   4019   4755    335    217     19       C  
ATOM   1447  C   ALA A 189      25.363  11.472  19.718  1.00 29.80           C  
ANISOU 1447  C   ALA A 189     2759   3894   4671    438    234    -63       C  
ATOM   1448  O   ALA A 189      24.404  11.507  20.512  1.00 28.12           O  
ANISOU 1448  O   ALA A 189     2675   3649   4361    398     87    -92       O  
ATOM   1449  CB  ALA A 189      25.941  13.762  20.627  1.00 28.13           C  
ANISOU 1449  CB  ALA A 189     2421   3791   4474    197    -14     46       C  
ATOM   1450  N   PRO A 190      25.701  10.380  18.990  1.00 31.79           N  
ANISOU 1450  N   PRO A 190     2988   4091   4999    564    436   -111       N  
ATOM   1451  CA  PRO A 190      24.815   9.196  18.984  1.00 32.26           C  
ANISOU 1451  CA  PRO A 190     3208   4033   5018    640    482   -215       C  
ATOM   1452  C   PRO A 190      24.742   8.462  20.346  1.00 31.47           C  
ANISOU 1452  C   PRO A 190     3060   3864   5034    707    324   -119       C  
ATOM   1453  O   PRO A 190      23.670   7.997  20.723  1.00 32.86           O  
ANISOU 1453  O   PRO A 190     3395   3973   5117    696    257   -172       O  
ATOM   1454  CB  PRO A 190      25.418   8.309  17.884  1.00 33.18           C  
ANISOU 1454  CB  PRO A 190     3291   4092   5225    745    766   -306       C  
ATOM   1455  CG  PRO A 190      26.867   8.819  17.688  1.00 37.72           C  
ANISOU 1455  CG  PRO A 190     3611   4753   5968    776    850   -186       C  
ATOM   1456  CD  PRO A 190      26.725  10.301  17.935  1.00 34.43           C  
ANISOU 1456  CD  PRO A 190     3191   4463   5426    615    668   -110       C  
ATOM   1457  N   GLU A 191      25.797   8.528  21.170  1.00 32.89           N  
ANISOU 1457  N   GLU A 191     3017   4094   5387    740    226     51       N  
ATOM   1458  CA  GLU A 191      25.740   7.970  22.552  1.00 31.50           C  
ANISOU 1458  CA  GLU A 191     2786   3907   5276    768     35    190       C  
ATOM   1459  C   GLU A 191      24.809   8.748  23.484  1.00 31.00           C  
ANISOU 1459  C   GLU A 191     2864   3921   4992    619   -182    170       C  
ATOM   1460  O   GLU A 191      24.015   8.171  24.260  1.00 27.97           O  
ANISOU 1460  O   GLU A 191     2583   3500   4545    626   -272    188       O  
ATOM   1461  CB  GLU A 191      27.153   7.857  23.164  1.00 34.08           C  
ANISOU 1461  CB  GLU A 191     2810   4306   5834    820    -38    409       C  
ATOM   1462  CG  GLU A 191      28.060   6.812  22.466  1.00 39.02           C  
ANISOU 1462  CG  GLU A 191     3259   4812   6755   1016    200    461       C  
ATOM   1463  CD  GLU A 191      29.481   6.764  23.038  1.00 49.81           C  
ANISOU 1463  CD  GLU A 191     4275   6262   8387   1073    122    720       C  
ATOM   1464  OE1 GLU A 191      29.842   7.655  23.842  1.00 46.62           O  
ANISOU 1464  OE1 GLU A 191     3773   6036   7905    925   -120    837       O  
ATOM   1465  OE2 GLU A 191      30.228   5.815  22.714  1.00 54.52           O  
ANISOU 1465  OE2 GLU A 191     4688   6743   9285   1258    302    810       O  
ATOM   1466  N   GLN A 192      24.901  10.072  23.408  1.00 29.49           N  
ANISOU 1466  N   GLN A 192     2679   3827   4700    484   -245    132       N  
ATOM   1467  CA  GLN A 192      24.054  10.944  24.211  1.00 30.50           C  
ANISOU 1467  CA  GLN A 192     2942   4003   4645    343   -401     77       C  
ATOM   1468  C   GLN A 192      22.597  10.811  23.785  1.00 28.49           C  
ANISOU 1468  C   GLN A 192     2915   3661   4249    347   -334    -55       C  
ATOM   1469  O   GLN A 192      21.684  11.015  24.584  1.00 27.74           O  
ANISOU 1469  O   GLN A 192     2938   3571   4032    286   -430    -89       O  
ATOM   1470  CB  GLN A 192      24.509  12.399  24.083  1.00 30.57           C  
ANISOU 1470  CB  GLN A 192     2902   4082   4633    201   -445     52       C  
ATOM   1471  CG  GLN A 192      25.568  12.810  25.093  1.00 39.62           C  
ANISOU 1471  CG  GLN A 192     3869   5349   5837    103   -619    162       C  
ATOM   1472  CD  GLN A 192      25.725  14.314  25.193  1.00 42.88           C  
ANISOU 1472  CD  GLN A 192     4290   5794   6209    -80   -682     93       C  
ATOM   1473  OE1 GLN A 192      26.709  14.880  24.718  1.00 47.74           O  
ANISOU 1473  OE1 GLN A 192     4746   6446   6947   -128   -658    150       O  
ATOM   1474  NE2 GLN A 192      24.752  14.970  25.815  1.00 39.93           N  
ANISOU 1474  NE2 GLN A 192     4096   5391   5684   -184   -745    -32       N  
ATOM   1475  N   ALA A 193      22.388  10.463  22.519  1.00 27.86           N  
ANISOU 1475  N   ALA A 193     2889   3518   4179    407   -164   -128       N  
ATOM   1476  CA  ALA A 193      21.045  10.281  21.984  1.00 28.69           C  
ANISOU 1476  CA  ALA A 193     3185   3563   4153    393   -114   -234       C  
ATOM   1477  C   ALA A 193      20.444   8.967  22.468  1.00 29.16           C  
ANISOU 1477  C   ALA A 193     3313   3534   4233    468   -120   -235       C  
ATOM   1478  O   ALA A 193      19.327   8.936  22.984  1.00 28.51           O  
ANISOU 1478  O   ALA A 193     3348   3434   4052    426   -190   -258       O  
ATOM   1479  CB  ALA A 193      21.067  10.330  20.465  1.00 27.41           C  
ANISOU 1479  CB  ALA A 193     3061   3400   3953    395     53   -308       C  
ATOM   1480  N   CYS A 194      21.194   7.882  22.301  1.00 29.08           N  
ANISOU 1480  N   CYS A 194     3215   3454   4381    582    -29   -199       N  
ATOM   1481  CA  CYS A 194      20.743   6.567  22.740  1.00 30.47           C  
ANISOU 1481  CA  CYS A 194     3437   3507   4633    659    -19   -177       C  
ATOM   1482  C   CYS A 194      20.537   6.532  24.267  1.00 31.12           C  
ANISOU 1482  C   CYS A 194     3489   3641   4693    634   -209    -34       C  
ATOM   1483  O   CYS A 194      19.539   5.977  24.771  1.00 29.86           O  
ANISOU 1483  O   CYS A 194     3439   3429   4479    621   -250    -30       O  
ATOM   1484  CB  CYS A 194      21.719   5.485  22.320  1.00 31.83           C  
ANISOU 1484  CB  CYS A 194     3491   3562   5040    801    135   -149       C  
ATOM   1485  SG  CYS A 194      21.836   5.180  20.524  1.00 36.71           S  
ANISOU 1485  SG  CYS A 194     4191   4107   5652    823    414   -367       S  
ATOM   1486  N   HIS A 195      21.402   7.212  25.007  1.00 29.76           N  
ANISOU 1486  N   HIS A 195     3180   3596   4531    597   -331     78       N  
ATOM   1487  CA  HIS A 195      21.250   7.168  26.455  1.00 31.15           C  
ANISOU 1487  CA  HIS A 195     3339   3862   4636    543   -512    207       C  
ATOM   1488  C   HIS A 195      19.910   7.820  26.895  1.00 29.57           C  
ANISOU 1488  C   HIS A 195     3324   3699   4212    429   -564     99       C  
ATOM   1489  O   HIS A 195      19.176   7.305  27.764  1.00 28.80           O  
ANISOU 1489  O   HIS A 195     3295   3607   4039    413   -625    155       O  
ATOM   1490  CB  HIS A 195      22.394   7.905  27.155  1.00 33.46           C  
ANISOU 1490  CB  HIS A 195     3461   4317   4935    473   -655    320       C  
ATOM   1491  CG  HIS A 195      22.250   7.884  28.639  1.00 35.25           C  
ANISOU 1491  CG  HIS A 195     3685   4679   5030    382   -848    442       C  
ATOM   1492  ND1 HIS A 195      21.885   8.996  29.366  1.00 40.16           N  
ANISOU 1492  ND1 HIS A 195     4395   5431   5431    211   -955    351       N  
ATOM   1493  CD2 HIS A 195      22.288   6.849  29.514  1.00 39.42           C  
ANISOU 1493  CD2 HIS A 195     4156   5226   5597    429   -935    641       C  
ATOM   1494  CE1 HIS A 195      21.817   8.668  30.648  1.00 37.50           C  
ANISOU 1494  CE1 HIS A 195     4053   5226   4970    142  -1106    479       C  
ATOM   1495  NE2 HIS A 195      22.015   7.364  30.757  1.00 40.20           N  
ANISOU 1495  NE2 HIS A 195     4305   5508   5461    272  -1105    675       N  
ATOM   1496  N   LEU A 196      19.631   8.978  26.322  1.00 27.72           N  
ANISOU 1496  N   LEU A 196     3152   3489   3893    353   -529    -34       N  
ATOM   1497  CA  LEU A 196      18.407   9.668  26.621  1.00 28.19           C  
ANISOU 1497  CA  LEU A 196     3355   3556   3800    268   -544   -131       C  
ATOM   1498  C   LEU A 196      17.191   8.868  26.206  1.00 27.04           C  
ANISOU 1498  C   LEU A 196     3326   3310   3639    312   -469   -169       C  
ATOM   1499  O   LEU A 196      16.221   8.755  26.980  1.00 27.62           O  
ANISOU 1499  O   LEU A 196     3479   3393   3622    276   -503   -164       O  
ATOM   1500  CB  LEU A 196      18.432  11.068  25.982  1.00 28.90           C  
ANISOU 1500  CB  LEU A 196     3458   3656   3867    195   -509   -230       C  
ATOM   1501  CG  LEU A 196      17.165  11.919  26.074  1.00 32.97           C  
ANISOU 1501  CG  LEU A 196     4094   4141   4291    130   -486   -324       C  
ATOM   1502  CD1 LEU A 196      16.700  11.971  27.540  1.00 42.03           C  
ANISOU 1502  CD1 LEU A 196     5295   5347   5325     68   -560   -332       C  
ATOM   1503  CD2 LEU A 196      17.586  13.275  25.581  1.00 33.47           C  
ANISOU 1503  CD2 LEU A 196     4123   4200   4395     64   -466   -371       C  
ATOM   1504  N   ALA A 197      17.188   8.359  24.981  1.00 24.80           N  
ANISOU 1504  N   ALA A 197     3056   2940   3428    369   -362   -218       N  
ATOM   1505  CA  ALA A 197      16.046   7.562  24.540  1.00 26.68           C  
ANISOU 1505  CA  ALA A 197     3403   3086   3648    377   -307   -266       C  
ATOM   1506  C   ALA A 197      15.863   6.303  25.426  1.00 26.49           C  
ANISOU 1506  C   ALA A 197     3379   2997   3689    426   -338   -168       C  
ATOM   1507  O   ALA A 197      14.730   5.954  25.806  1.00 26.80           O  
ANISOU 1507  O   ALA A 197     3499   3008   3675    390   -354   -162       O  
ATOM   1508  CB  ALA A 197      16.223   7.164  23.108  1.00 27.72           C  
ANISOU 1508  CB  ALA A 197     3558   3155   3819    402   -186   -356       C  
ATOM   1509  N   LYS A 198      16.962   5.590  25.670  1.00 27.28           N  
ANISOU 1509  N   LYS A 198     3371   3062   3932    511   -335    -70       N  
ATOM   1510  CA  LYS A 198      16.947   4.364  26.460  1.00 28.07           C  
ANISOU 1510  CA  LYS A 198     3442   3082   4142    570   -363     73       C  
ATOM   1511  C   LYS A 198      16.481   4.638  27.892  1.00 28.23           C  
ANISOU 1511  C   LYS A 198     3473   3232   4020    498   -500    193       C  
ATOM   1512  O   LYS A 198      15.674   3.884  28.447  1.00 27.31           O  
ANISOU 1512  O   LYS A 198     3412   3068   3898    490   -511    267       O  
ATOM   1513  CB  LYS A 198      18.323   3.696  26.461  1.00 30.58           C  
ANISOU 1513  CB  LYS A 198     3597   3343   4678    689   -336    196       C  
ATOM   1514  CG  LYS A 198      18.350   2.402  27.247  1.00 33.39           C  
ANISOU 1514  CG  LYS A 198     3899   3589   5198    764   -363    391       C  
ATOM   1515  CD  LYS A 198      19.763   1.785  27.277  1.00 36.48           C  
ANISOU 1515  CD  LYS A 198     4084   3916   5859    902   -335    556       C  
ATOM   1516  CE  LYS A 198      19.717   0.384  27.836  1.00 47.63           C  
ANISOU 1516  CE  LYS A 198     5442   5153   7501    998   -324    758       C  
ATOM   1517  NZ  LYS A 198      19.145   0.411  29.194  1.00 46.35           N  
ANISOU 1517  NZ  LYS A 198     5299   5140   7172    908   -509    952       N  
ATOM   1518  N   THR A 199      16.908   5.776  28.448  1.00 28.30           N  
ANISOU 1518  N   THR A 199     3447   3409   3897    425   -589    188       N  
ATOM   1519  CA  THR A 199      16.567   6.108  29.840  1.00 29.29           C  
ANISOU 1519  CA  THR A 199     3597   3687   3844    331   -704    267       C  
ATOM   1520  C   THR A 199      15.058   6.378  29.913  1.00 27.49           C  
ANISOU 1520  C   THR A 199     3513   3440   3493    272   -644    160       C  
ATOM   1521  O   THR A 199      14.411   5.991  30.860  1.00 28.24           O  
ANISOU 1521  O   THR A 199     3649   3587   3494    232   -672    244       O  
ATOM   1522  CB  THR A 199      17.354   7.369  30.316  1.00 29.25           C  
ANISOU 1522  CB  THR A 199     3542   3850   3722    233   -796    226       C  
ATOM   1523  OG1 THR A 199      18.753   7.067  30.326  1.00 31.81           O  
ANISOU 1523  OG1 THR A 199     3696   4213   4176    280   -868    365       O  
ATOM   1524  CG2 THR A 199      16.942   7.776  31.762  1.00 33.63           C  
ANISOU 1524  CG2 THR A 199     4157   4581   4040    100   -892    253       C  
ATOM   1525  N   ALA A 200      14.548   7.166  28.975  1.00 25.07           N  
ANISOU 1525  N   ALA A 200     3263   3083   3180    257   -566     -3       N  
ATOM   1526  CA  ALA A 200      13.127   7.546  28.927  1.00 25.13           C  
ANISOU 1526  CA  ALA A 200     3367   3070   3112    210   -506    -86       C  
ATOM   1527  C   ALA A 200      12.263   6.269  28.767  1.00 25.56           C  
ANISOU 1527  C   ALA A 200     3457   3020   3236    241   -470    -21       C  
ATOM   1528  O   ALA A 200      11.248   6.072  29.465  1.00 24.53           O  
ANISOU 1528  O   ALA A 200     3368   2912   3039    200   -458     20       O  
ATOM   1529  CB  ALA A 200      12.865   8.503  27.734  1.00 24.88           C  
ANISOU 1529  CB  ALA A 200     3350   2992   3109    202   -445   -214       C  
ATOM   1530  N   PHE A 201      12.694   5.400  27.881  1.00 23.91           N  
ANISOU 1530  N   PHE A 201     3229   2689   3167    303   -438    -19       N  
ATOM   1531  CA  PHE A 201      11.982   4.133  27.684  1.00 27.17           C  
ANISOU 1531  CA  PHE A 201     3680   2966   3676    314   -400     21       C  
ATOM   1532  C   PHE A 201      12.020   3.272  28.970  1.00 27.12           C  
ANISOU 1532  C   PHE A 201     3644   2970   3691    327   -451    215       C  
ATOM   1533  O   PHE A 201      10.987   2.791  29.475  1.00 27.25           O  
ANISOU 1533  O   PHE A 201     3701   2970   3684    281   -443    279       O  
ATOM   1534  CB  PHE A 201      12.611   3.361  26.514  1.00 25.97           C  
ANISOU 1534  CB  PHE A 201     3523   2664   3681    374   -328    -49       C  
ATOM   1535  CG  PHE A 201      11.940   2.025  26.265  1.00 30.60           C  
ANISOU 1535  CG  PHE A 201     4161   3072   4393    367   -277    -42       C  
ATOM   1536  CD1 PHE A 201      10.822   1.948  25.447  1.00 28.11           C  
ANISOU 1536  CD1 PHE A 201     3929   2716   4036    275   -247   -161       C  
ATOM   1537  CD2 PHE A 201      12.319   0.902  26.995  1.00 25.32           C  
ANISOU 1537  CD2 PHE A 201     3448   2290   3883    431   -279    117       C  
ATOM   1538  CE1 PHE A 201      10.121   0.712  25.271  1.00 29.05           C  
ANISOU 1538  CE1 PHE A 201     4100   2664   4274    231   -210   -165       C  
ATOM   1539  CE2 PHE A 201      11.636  -0.334  26.846  1.00 34.59           C  
ANISOU 1539  CE2 PHE A 201     4672   3267   5204    409   -227    131       C  
ATOM   1540  CZ  PHE A 201      10.539  -0.424  25.955  1.00 32.70           C  
ANISOU 1540  CZ  PHE A 201     4531   2974   4920    300   -189    -33       C  
ATOM   1541  N   ASP A 202      13.223   3.073  29.509  1.00 27.61           N  
ANISOU 1541  N   ASP A 202     3616   3073   3799    382   -511    338       N  
ATOM   1542  CA  ASP A 202      13.364   2.279  30.738  1.00 29.03           C  
ANISOU 1542  CA  ASP A 202     3749   3294   3989    387   -583    575       C  
ATOM   1543  C   ASP A 202      12.527   2.806  31.911  1.00 27.69           C  
ANISOU 1543  C   ASP A 202     3633   3309   3578    279   -627    621       C  
ATOM   1544  O   ASP A 202      12.026   2.018  32.741  1.00 29.47           O  
ANISOU 1544  O   ASP A 202     3863   3545   3789    254   -643    798       O  
ATOM   1545  CB  ASP A 202      14.827   2.197  31.152  1.00 31.64           C  
ANISOU 1545  CB  ASP A 202     3943   3692   4389    447   -672    727       C  
ATOM   1546  CG  ASP A 202      15.629   1.251  30.273  1.00 35.03           C  
ANISOU 1546  CG  ASP A 202     4289   3901   5120    582   -595    756       C  
ATOM   1547  OD1 ASP A 202      15.015   0.527  29.459  1.00 34.50           O  
ANISOU 1547  OD1 ASP A 202     4295   3625   5189    612   -477    655       O  
ATOM   1548  OD2 ASP A 202      16.863   1.231  30.395  1.00 32.59           O  
ANISOU 1548  OD2 ASP A 202     3837   3629   4918    651   -643    872       O  
ATOM   1549  N   ASP A 203      12.536   4.123  32.078  1.00 26.20           N  
ANISOU 1549  N   ASP A 203     3476   3270   3208    213   -639    481       N  
ATOM   1550  CA  ASP A 203      11.827   4.742  33.210  1.00 29.27           C  
ANISOU 1550  CA  ASP A 203     3926   3836   3358    106   -641    476       C  
ATOM   1551  C   ASP A 203      10.320   4.558  33.032  1.00 27.66           C  
ANISOU 1551  C   ASP A 203     3789   3556   3163     86   -531    427       C  
ATOM   1552  O   ASP A 203       9.632   4.300  34.006  1.00 28.84           O  
ANISOU 1552  O   ASP A 203     3967   3798   3192     27   -510    523       O  
ATOM   1553  CB  ASP A 203      12.147   6.237  33.336  1.00 27.49           C  
ANISOU 1553  CB  ASP A 203     3729   3735   2983     37   -645    294       C  
ATOM   1554  CG  ASP A 203      13.560   6.498  33.899  1.00 31.78           C  
ANISOU 1554  CG  ASP A 203     4197   4423   3456     -1   -783    366       C  
ATOM   1555  OD1 ASP A 203      14.259   5.547  34.268  1.00 31.16           O  
ANISOU 1555  OD1 ASP A 203     4030   4370   3438     34   -880    586       O  
ATOM   1556  OD2 ASP A 203      13.998   7.659  33.867  1.00 33.28           O  
ANISOU 1556  OD2 ASP A 203     4398   4680   3567    -65   -796    213       O  
ATOM   1557  N   ALA A 204       9.805   4.676  31.800  1.00 25.19           N  
ANISOU 1557  N   ALA A 204     3493   3097   2984    123   -464    296       N  
ATOM   1558  CA  ALA A 204       8.365   4.394  31.568  1.00 24.33           C  
ANISOU 1558  CA  ALA A 204     3413   2919   2912     92   -384    284       C  
ATOM   1559  C   ALA A 204       8.019   2.936  31.822  1.00 27.54           C  
ANISOU 1559  C   ALA A 204     3810   3227   3427     93   -391    456       C  
ATOM   1560  O   ALA A 204       7.049   2.608  32.525  1.00 28.33           O  
ANISOU 1560  O   ALA A 204     3918   3366   3481     39   -349    550       O  
ATOM   1561  CB  ALA A 204       7.946   4.802  30.164  1.00 25.33           C  
ANISOU 1561  CB  ALA A 204     3544   2942   3139    105   -348    139       C  
ATOM   1562  N   ILE A 205       8.818   2.033  31.264  1.00 28.02           N  
ANISOU 1562  N   ILE A 205     3847   3143   3656    155   -424    502       N  
ATOM   1563  CA  ILE A 205       8.597   0.604  31.472  1.00 31.17           C  
ANISOU 1563  CA  ILE A 205     4232   3393   4216    163   -420    669       C  
ATOM   1564  C   ILE A 205       8.543   0.271  32.962  1.00 33.16           C  
ANISOU 1564  C   ILE A 205     4458   3783   4357    129   -460    909       C  
ATOM   1565  O   ILE A 205       7.670  -0.468  33.417  1.00 33.56           O  
ANISOU 1565  O   ILE A 205     4514   3792   4445     79   -427   1043       O  
ATOM   1566  CB  ILE A 205       9.697  -0.241  30.804  1.00 31.03           C  
ANISOU 1566  CB  ILE A 205     4179   3188   4423    259   -424    686       C  
ATOM   1567  CG1 ILE A 205       9.302  -1.719  30.796  1.00 37.42           C  
ANISOU 1567  CG1 ILE A 205     4988   3767   5461    260   -386    814       C  
ATOM   1568  CG2 ILE A 205      11.026  -0.043  31.515  1.00 34.82           C  
ANISOU 1568  CG2 ILE A 205     4576   3783   4870    325   -506    824       C  
ATOM   1569  CD1 ILE A 205       8.999  -2.263  29.416  1.00 36.42           C  
ANISOU 1569  CD1 ILE A 205     4922   3409   5508    246   -304    611       C  
ATOM   1570  N   ALA A 206       9.488   0.829  33.711  1.00 33.29           N  
ANISOU 1570  N   ALA A 206     4444   3981   4224    137   -537    971       N  
ATOM   1571  CA  ALA A 206       9.587   0.634  35.165  1.00 35.58           C  
ANISOU 1571  CA  ALA A 206     4714   4469   4336     77   -600   1203       C  
ATOM   1572  C   ALA A 206       8.331   1.050  35.907  1.00 35.18           C  
ANISOU 1572  C   ALA A 206     4727   4564   4076    -28   -516   1180       C  
ATOM   1573  O   ALA A 206       8.106   0.596  37.019  1.00 34.29           O  
ANISOU 1573  O   ALA A 206     4609   4587   3832    -93   -532   1394       O  
ATOM   1574  CB  ALA A 206      10.786   1.370  35.737  1.00 36.45           C  
ANISOU 1574  CB  ALA A 206     4785   4786   4277     62   -713   1221       C  
ATOM   1575  N   GLU A 207       7.544   1.920  35.309  1.00 31.98           N  
ANISOU 1575  N   GLU A 207     4368   4140   3644    -43   -421    943       N  
ATOM   1576  CA  GLU A 207       6.358   2.443  35.939  1.00 34.02           C  
ANISOU 1576  CA  GLU A 207     4664   4521   3742   -122   -306    899       C  
ATOM   1577  C   GLU A 207       5.105   2.362  35.099  1.00 30.23           C  
ANISOU 1577  C   GLU A 207     4171   3892   3425   -118   -207    815       C  
ATOM   1578  O   GLU A 207       4.427   3.318  34.952  1.00 30.67           O  
ANISOU 1578  O   GLU A 207     4232   3992   3429   -131   -116    664       O  
ATOM   1579  CB  GLU A 207       6.609   3.859  36.405  1.00 32.30           C  
ANISOU 1579  CB  GLU A 207     4495   4485   3294   -163   -273    711       C  
ATOM   1580  CG  GLU A 207       7.746   3.916  37.361  1.00 40.82           C  
ANISOU 1580  CG  GLU A 207     5582   5757   4170   -215   -390    808       C  
ATOM   1581  CD  GLU A 207       7.740   5.125  38.211  1.00 43.98           C  
ANISOU 1581  CD  GLU A 207     6057   6373   4281   -317   -333    640       C  
ATOM   1582  OE1 GLU A 207       6.794   5.323  38.961  1.00 49.15           O  
ANISOU 1582  OE1 GLU A 207     6761   7136   4777   -387   -196    617       O  
ATOM   1583  OE2 GLU A 207       8.678   5.882  38.121  1.00 45.11           O  
ANISOU 1583  OE2 GLU A 207     6209   6567   4364   -335   -410    517       O  
ATOM   1584  N   LEU A 208       4.716   1.216  34.459  1.00 30.57           N  
ANISOU 1584  N   LEU A 208     4184   3739   3693   -110   -223    909       N  
ATOM   1585  CA  LEU A 208       3.487   1.077  33.692  1.00 30.16           C  
ANISOU 1585  CA  LEU A 208     4105   3574   3781   -146   -159    850       C  
ATOM   1586  C   LEU A 208       2.310   1.363  34.572  1.00 31.02           C  
ANISOU 1586  C   LEU A 208     4184   3818   3783   -211    -42    917       C  
ATOM   1587  O   LEU A 208       1.245   1.756  34.090  1.00 30.21           O  
ANISOU 1587  O   LEU A 208     4031   3694   3752   -236     28    847       O  
ATOM   1588  CB  LEU A 208       3.362  -0.332  33.101  1.00 32.44           C  
ANISOU 1588  CB  LEU A 208     4381   3636   4306   -165   -199    947       C  
ATOM   1589  CG  LEU A 208       4.312  -0.908  32.045  1.00 32.74           C  
ANISOU 1589  CG  LEU A 208     4446   3474   4518   -107   -264    863       C  
ATOM   1590  CD1 LEU A 208       4.196  -2.363  31.613  1.00 33.31           C  
ANISOU 1590  CD1 LEU A 208     4523   3289   4843   -136   -266    940       C  
ATOM   1591  CD2 LEU A 208       4.760   0.071  30.951  1.00 31.41           C  
ANISOU 1591  CD2 LEU A 208     4301   3320   4313    -67   -281    626       C  
ATOM   1592  N   ASP A 209       2.588   1.217  35.857  1.00 33.98           N  
ANISOU 1592  N   ASP A 209     4582   4353   3974   -240    -24   1059       N  
ATOM   1593  CA  ASP A 209       1.434   1.501  36.706  1.00 35.00           C  
ANISOU 1593  CA  ASP A 209     4687   4625   3988   -306    128   1108       C  
ATOM   1594  C   ASP A 209       1.062   2.977  36.675  1.00 35.71           C  
ANISOU 1594  C   ASP A 209     4784   4811   3976   -284    248    878       C  
ATOM   1595  O   ASP A 209      -0.048   3.346  37.052  1.00 37.25           O  
ANISOU 1595  O   ASP A 209     4929   5069   4155   -312    410    871       O  
ATOM   1596  CB  ASP A 209       1.692   1.057  38.152  1.00 40.95           C  
ANISOU 1596  CB  ASP A 209     5472   5574   4513   -371    143   1316       C  
ATOM   1597  CG  ASP A 209       2.889   1.788  38.794  1.00 43.51           C  
ANISOU 1597  CG  ASP A 209     5872   6085   4576   -372     75   1241       C  
ATOM   1598  OD1 ASP A 209       3.570   2.575  38.125  1.00 43.81           O  
ANISOU 1598  OD1 ASP A 209     5933   6075   4639   -315     20   1038       O  
ATOM   1599  OD2 ASP A 209       3.228   1.472  39.947  1.00 59.21           O  
ANISOU 1599  OD2 ASP A 209     7889   8272   6337   -446     52   1418       O  
ATOM   1600  N   THR A 210       1.939   3.790  36.099  1.00 31.91           N  
ANISOU 1600  N   THR A 210     4341   4302   3481   -227    179    699       N  
ATOM   1601  CA  THR A 210       1.648   5.203  35.903  1.00 32.25           C  
ANISOU 1601  CA  THR A 210     4384   4373   3497   -196    287    485       C  
ATOM   1602  C   THR A 210       0.960   5.534  34.568  1.00 30.81           C  
ANISOU 1602  C   THR A 210     4115   4032   3558   -148    287    417       C  
ATOM   1603  O   THR A 210       0.919   6.701  34.179  1.00 30.33           O  
ANISOU 1603  O   THR A 210     4040   3954   3530   -103    344    265       O  
ATOM   1604  CB  THR A 210       2.924   6.060  36.027  1.00 31.00           C  
ANISOU 1604  CB  THR A 210     4305   4276   3198   -181    221    332       C  
ATOM   1605  OG1 THR A 210       3.820   5.745  34.954  1.00 30.78           O  
ANISOU 1605  OG1 THR A 210     4267   4118   3308   -128     60    327       O  
ATOM   1606  CG2 THR A 210       3.617   5.795  37.354  1.00 32.79           C  
ANISOU 1606  CG2 THR A 210     4605   4703   3151   -260    189    413       C  
ATOM   1607  N   LEU A 211       0.417   4.537  33.865  1.00 29.31           N  
ANISOU 1607  N   LEU A 211     3866   3732   3540   -172    220    534       N  
ATOM   1608  CA  LEU A 211      -0.291   4.842  32.617  1.00 29.56           C  
ANISOU 1608  CA  LEU A 211     3809   3661   3762   -162    196    490       C  
ATOM   1609  C   LEU A 211      -1.656   5.375  33.025  1.00 32.21           C  
ANISOU 1609  C   LEU A 211     4027   4052   4157   -169    361    531       C  
ATOM   1610  O   LEU A 211      -2.221   4.912  34.027  1.00 33.60           O  
ANISOU 1610  O   LEU A 211     4187   4305   4275   -210    469    638       O  
ATOM   1611  CB  LEU A 211      -0.499   3.584  31.752  1.00 30.60           C  
ANISOU 1611  CB  LEU A 211     3921   3665   4041   -225     72    576       C  
ATOM   1612  CG  LEU A 211       0.781   3.105  31.081  1.00 26.18           C  
ANISOU 1612  CG  LEU A 211     3455   3012   3482   -201    -58    508       C  
ATOM   1613  CD1 LEU A 211       0.604   1.685  30.554  1.00 31.31           C  
ANISOU 1613  CD1 LEU A 211     4113   3511   4272   -274   -130    580       C  
ATOM   1614  CD2 LEU A 211       1.249   4.124  29.984  1.00 24.09           C  
ANISOU 1614  CD2 LEU A 211     3195   2738   3222   -155   -105    352       C  
ATOM   1615  N   ASN A 212      -2.211   6.289  32.372  1.00 32.28           N  
ANISOU 1615  N   ASN A 212     4105   4886   3272    -41    214   -174       N  
ATOM   1616  CA  ASN A 212      -3.513   6.944  32.593  1.00 33.83           C  
ANISOU 1616  CA  ASN A 212     4240   4988   3626    -41    391   -324       C  
ATOM   1617  C   ASN A 212      -4.511   6.286  31.629  1.00 32.02           C  
ANISOU 1617  C   ASN A 212     4034   4442   3690      5    341    -25       C  
ATOM   1618  O   ASN A 212      -4.193   6.087  30.448  1.00 29.45           O  
ANISOU 1618  O   ASN A 212     3782   3872   3537      4    201     57       O  
ATOM   1619  CB  ASN A 212      -3.360   8.439  32.243  1.00 34.92           C  
ANISOU 1619  CB  ASN A 212     4376   4847   4043    -71    533   -736       C  
ATOM   1620  CG  ASN A 212      -4.598   9.271  32.565  1.00 40.59           C  
ANISOU 1620  CG  ASN A 212     4982   5428   5011    -19    814   -902       C  
ATOM   1621  OD1 ASN A 212      -5.697   8.731  32.702  1.00 45.46           O  
ANISOU 1621  OD1 ASN A 212     5533   6120   5620     49    826   -663       O  
ATOM   1622  ND2 ASN A 212      -4.416  10.554  32.784  1.00 39.66           N  
ANISOU 1622  ND2 ASN A 212     4805   5104   5160    -68   1107  -1348       N  
ATOM   1623  N   GLU A 213      -5.723   6.031  32.107  1.00 30.83           N  
ANISOU 1623  N   GLU A 213     3769   4380   3565     11    470     67       N  
ATOM   1624  CA  GLU A 213      -6.769   5.450  31.273  1.00 30.80           C  
ANISOU 1624  CA  GLU A 213     3684   4210   3809    -16    442    240       C  
ATOM   1625  C   GLU A 213      -7.176   6.322  30.078  1.00 30.16           C  
ANISOU 1625  C   GLU A 213     3525   3981   3953     63    370    190       C  
ATOM   1626  O   GLU A 213      -7.855   5.842  29.171  1.00 29.76           O  
ANISOU 1626  O   GLU A 213     3333   3976   3997     11    278    289       O  
ATOM   1627  CB  GLU A 213      -8.001   5.120  32.120  1.00 32.71           C  
ANISOU 1627  CB  GLU A 213     3765   4623   4042    -35    632    329       C  
ATOM   1628  CG  GLU A 213      -8.664   6.334  32.750  1.00 42.75           C  
ANISOU 1628  CG  GLU A 213     4925   6002   5315     63    811    111       C  
ATOM   1629  N   ASP A 214      -6.775   7.593  30.070  1.00 28.91           N  
ANISOU 1629  N   ASP A 214     3397   3696   3891    181    457     49       N  
ATOM   1630  CA  ASP A 214      -7.172   8.484  28.979  1.00 31.77           C  
ANISOU 1630  CA  ASP A 214     3630   3922   4517    354    477    194       C  
ATOM   1631  C   ASP A 214      -6.044   8.658  27.978  1.00 30.54           C  
ANISOU 1631  C   ASP A 214     3595   3643   4367    362    338    251       C  
ATOM   1632  O   ASP A 214      -6.269   9.174  26.873  1.00 30.28           O  
ANISOU 1632  O   ASP A 214     3421   3623   4460    522    318    510       O  
ATOM   1633  CB  ASP A 214      -7.628   9.853  29.519  1.00 33.62           C  
ANISOU 1633  CB  ASP A 214     3762   3945   5067    528    828     84       C  
ATOM   1634  CG  ASP A 214      -8.992   9.780  30.196  1.00 45.43           C  
ANISOU 1634  CG  ASP A 214     5055   5600   6605    581    985    104       C  
ATOM   1635  OD1 ASP A 214      -9.774   8.860  29.876  1.00 45.03           O  
ANISOU 1635  OD1 ASP A 214     4869   5821   6419    526    808    302       O  
ATOM   1636  OD2 ASP A 214      -9.290  10.650  31.046  1.00 56.06           O  
ANISOU 1636  OD2 ASP A 214     6345   6802   8153    647   1330   -142       O  
ATOM   1637  N   SER A 215      -4.849   8.170  28.322  1.00 27.49           N  
ANISOU 1637  N   SER A 215     3412   3229   3804    218    243     84       N  
ATOM   1638  CA  SER A 215      -3.688   8.451  27.487  1.00 28.43           C  
ANISOU 1638  CA  SER A 215     3637   3216   3951    221    158     95       C  
ATOM   1639  C   SER A 215      -2.749   7.262  27.233  1.00 26.45           C  
ANISOU 1639  C   SER A 215     3514   3050   3485     86    -48     85       C  
ATOM   1640  O   SER A 215      -1.654   7.439  26.734  1.00 24.94           O  
ANISOU 1640  O   SER A 215     3410   2777   3287     73   -103     52       O  
ATOM   1641  CB  SER A 215      -2.879   9.626  28.056  1.00 29.95           C  
ANISOU 1641  CB  SER A 215     3883   3178   4317    214    383   -170       C  
ATOM   1642  OG  SER A 215      -2.472   9.324  29.382  1.00 31.29           O  
ANISOU 1642  OG  SER A 215     4086   3566   4236     63    402   -481       O  
ATOM   1643  N   TYR A 216      -3.160   6.058  27.604  1.00 27.16           N  
ANISOU 1643  N   TYR A 216     3594   3247   3478     -4    -91    130       N  
ATOM   1644  CA  TYR A 216      -2.185   4.951  27.623  1.00 25.85           C  
ANISOU 1644  CA  TYR A 216     3531   3048   3244    -76   -149    161       C  
ATOM   1645  C   TYR A 216      -1.787   4.570  26.191  1.00 23.93           C  
ANISOU 1645  C   TYR A 216     3296   2739   3059   -139   -251    125       C  
ATOM   1646  O   TYR A 216      -0.700   4.027  25.966  1.00 22.89           O  
ANISOU 1646  O   TYR A 216     3253   2515   2929   -157   -271    111       O  
ATOM   1647  CB  TYR A 216      -2.751   3.763  28.416  1.00 26.45           C  
ANISOU 1647  CB  TYR A 216     3562   3141   3347   -124    -30    304       C  
ATOM   1648  CG  TYR A 216      -3.827   3.029  27.668  1.00 24.30           C  
ANISOU 1648  CG  TYR A 216     3169   2797   3266   -272     14    259       C  
ATOM   1649  CD1 TYR A 216      -5.159   3.401  27.767  1.00 25.84           C  
ANISOU 1649  CD1 TYR A 216     3200   3138   3480   -294     44    238       C  
ATOM   1650  CD2 TYR A 216      -3.505   1.943  26.871  1.00 24.20           C  
ANISOU 1650  CD2 TYR A 216     3152   2605   3439   -421     67    166       C  
ATOM   1651  CE1 TYR A 216      -6.141   2.739  27.026  1.00 30.83           C  
ANISOU 1651  CE1 TYR A 216     3626   3847   4240   -489     67    114       C  
ATOM   1652  CE2 TYR A 216      -4.481   1.259  26.128  1.00 30.34           C  
ANISOU 1652  CE2 TYR A 216     3741   3404   4384   -664    142    -58       C  
ATOM   1653  CZ  TYR A 216      -5.792   1.671  26.217  1.00 32.83           C  
ANISOU 1653  CZ  TYR A 216     3857   3974   4644   -708    114    -82       C  
ATOM   1654  OH  TYR A 216      -6.727   1.009  25.475  1.00 40.18           O  
ANISOU 1654  OH  TYR A 216     4515   5064   5686   -998    170   -372       O  
ATOM   1655  N   LYS A 217      -2.703   4.751  25.240  1.00 23.85           N  
ANISOU 1655  N   LYS A 217     3131   2877   3055   -173   -300    110       N  
ATOM   1656  CA  LYS A 217      -2.412   4.430  23.832  1.00 24.65           C  
ANISOU 1656  CA  LYS A 217     3154   3134   3077   -264   -396     17       C  
ATOM   1657  C   LYS A 217      -1.306   5.363  23.334  1.00 25.66           C  
ANISOU 1657  C   LYS A 217     3381   3220   3149   -129   -441    114       C  
ATOM   1658  O   LYS A 217      -0.357   4.924  22.659  1.00 25.34           O  
ANISOU 1658  O   LYS A 217     3400   3171   3057   -195   -474     16       O  
ATOM   1659  CB  LYS A 217      -3.669   4.588  22.976  1.00 25.11           C  
ANISOU 1659  CB  LYS A 217     2904   3626   3010   -305   -465     24       C  
ATOM   1660  CG  LYS A 217      -4.746   3.532  23.312  1.00 30.60           C  
ANISOU 1660  CG  LYS A 217     3443   4381   3804   -538   -387   -180       C  
ATOM   1661  CD  LYS A 217      -5.874   3.479  22.291  1.00 37.52           C  
ANISOU 1661  CD  LYS A 217     3901   5882   4472   -671   -489   -299       C  
ATOM   1662  CE  LYS A 217      -6.526   4.823  22.194  1.00 39.64           C  
ANISOU 1662  CE  LYS A 217     3985   6458   4619   -343   -567    120       C  
ATOM   1663  NZ  LYS A 217      -7.808   4.737  21.395  1.00 45.05           N  
ANISOU 1663  NZ  LYS A 217     4146   7920   5050   -427   -677    100       N  
ATOM   1664  N   ASP A 218      -1.439   6.659  23.640  1.00 25.75           N  
ANISOU 1664  N   ASP A 218     3383   3158   3243     48   -372    284       N  
ATOM   1665  CA  ASP A 218      -0.388   7.634  23.296  1.00 26.86           C  
ANISOU 1665  CA  ASP A 218     3598   3139   3467    144   -306    365       C  
ATOM   1666  C   ASP A 218       0.948   7.309  23.954  1.00 26.99           C  
ANISOU 1666  C   ASP A 218     3794   2979   3483     45   -313    158       C  
ATOM   1667  O   ASP A 218       2.008   7.380  23.293  1.00 27.12           O  
ANISOU 1667  O   ASP A 218     3853   2970   3481     30   -333    154       O  
ATOM   1668  CB  ASP A 218      -0.806   9.055  23.702  1.00 27.64           C  
ANISOU 1668  CB  ASP A 218     3636   3019   3848    316    -76    507       C  
ATOM   1669  CG  ASP A 218      -1.916   9.612  22.814  1.00 37.32           C  
ANISOU 1669  CG  ASP A 218     4600   4470   5108    539    -27    915       C  
ATOM   1670  OD1 ASP A 218      -2.170   9.041  21.729  1.00 35.11           O  
ANISOU 1670  OD1 ASP A 218     4159   4654   4525    529   -213   1056       O  
ATOM   1671  OD2 ASP A 218      -2.537  10.612  23.212  1.00 40.06           O  
ANISOU 1671  OD2 ASP A 218     4849   4593   5777    725    227   1080       O  
ATOM   1672  N   SER A 219       0.916   6.957  25.246  1.00 25.36           N  
ANISOU 1672  N   SER A 219     3633   2753   3250     -2   -292     30       N  
ATOM   1673  CA  SER A 219       2.140   6.557  25.945  1.00 24.59           C  
ANISOU 1673  CA  SER A 219     3592   2701   3052    -50   -323    -76       C  
ATOM   1674  C   SER A 219       2.799   5.376  25.289  1.00 23.34           C  
ANISOU 1674  C   SER A 219     3470   2529   2868    -62   -396     -4       C  
ATOM   1675  O   SER A 219       3.998   5.428  25.017  1.00 22.46           O  
ANISOU 1675  O   SER A 219     3373   2418   2742    -60   -420    -39       O  
ATOM   1676  CB  SER A 219       1.883   6.168  27.410  1.00 24.92           C  
ANISOU 1676  CB  SER A 219     3585   2941   2941    -53   -292    -97       C  
ATOM   1677  OG  SER A 219       1.334   7.256  28.127  1.00 28.53           O  
ANISOU 1677  OG  SER A 219     3984   3434   3422    -81   -166   -294       O  
ATOM   1678  N   THR A 220       2.034   4.315  25.001  1.00 23.50           N  
ANISOU 1678  N   THR A 220     3475   2508   2946   -101   -375     42       N  
ATOM   1679  CA  THR A 220       2.680   3.107  24.497  1.00 25.25           C  
ANISOU 1679  CA  THR A 220     3710   2603   3279   -135   -314     24       C  
ATOM   1680  C   THR A 220       3.215   3.337  23.038  1.00 24.78           C  
ANISOU 1680  C   THR A 220     3647   2595   3174   -199   -364   -130       C  
ATOM   1681  O   THR A 220       4.232   2.737  22.595  1.00 25.73           O  
ANISOU 1681  O   THR A 220     3785   2623   3369   -199   -302   -193       O  
ATOM   1682  CB  THR A 220       1.732   1.913  24.550  1.00 27.21           C  
ANISOU 1682  CB  THR A 220     3905   2704   3730   -236   -159     -1       C  
ATOM   1683  OG1 THR A 220       0.517   2.225  23.870  1.00 30.07           O  
ANISOU 1683  OG1 THR A 220     4168   3234   4023   -373   -219   -166       O  
ATOM   1684  CG2 THR A 220       1.368   1.526  26.007  1.00 27.23           C  
ANISOU 1684  CG2 THR A 220     3889   2679   3777   -131    -47    276       C  
ATOM   1685  N   LEU A 221       2.471   4.123  22.278  1.00 23.48           N  
ANISOU 1685  N   LEU A 221     3409   2634   2879   -224   -438   -139       N  
ATOM   1686  CA  LEU A 221       2.861   4.472  20.908  1.00 24.37           C  
ANISOU 1686  CA  LEU A 221     3450   2974   2836   -245   -477   -171       C  
ATOM   1687  C   LEU A 221       4.235   5.149  20.958  1.00 24.09           C  
ANISOU 1687  C   LEU A 221     3509   2804   2842   -156   -458    -84       C  
ATOM   1688  O   LEU A 221       5.167   4.776  20.210  1.00 24.68           O  
ANISOU 1688  O   LEU A 221     3583   2919   2875   -192   -430   -177       O  
ATOM   1689  CB  LEU A 221       1.835   5.421  20.273  0.65 24.44           C  
ANISOU 1689  CB  LEU A 221     3286   3321   2678   -169   -533     30       C  
ATOM   1690  CG  LEU A 221       1.966   5.768  18.790  0.65 29.84           C  
ANISOU 1690  CG  LEU A 221     3783   4483   3071   -147   -568    136       C  
ATOM   1691  CD1 LEU A 221       0.572   6.038  18.190  0.65 34.89           C  
ANISOU 1691  CD1 LEU A 221     4105   5697   3454   -102   -646    309       C  
ATOM   1692  CD2 LEU A 221       2.858   6.974  18.577  0.65 28.30           C  
ANISOU 1692  CD2 LEU A 221     3647   4138   2967     39   -475    469       C  
ATOM   1693  N   ILE A 222       4.408   6.126  21.848  1.00 22.58           N  
ANISOU 1693  N   ILE A 222     3363   2465   2753    -81   -431     15       N  
ATOM   1694  CA  ILE A 222       5.687   6.864  21.837  1.00 21.56           C  
ANISOU 1694  CA  ILE A 222     3252   2239   2699    -74   -371      5       C  
ATOM   1695  C   ILE A 222       6.833   6.006  22.413  1.00 23.52           C  
ANISOU 1695  C   ILE A 222     3514   2490   2931    -97   -409   -112       C  
ATOM   1696  O   ILE A 222       7.986   6.103  21.937  1.00 23.17           O  
ANISOU 1696  O   ILE A 222     3442   2461   2902   -109   -383   -143       O  
ATOM   1697  CB  ILE A 222       5.588   8.222  22.600  1.00 23.22           C  
ANISOU 1697  CB  ILE A 222     3441   2276   3105    -72   -232    -14       C  
ATOM   1698  CG1 ILE A 222       4.500   9.108  21.984  1.00 26.69           C  
ANISOU 1698  CG1 ILE A 222     3816   2653   3674     52   -106    250       C  
ATOM   1699  CG2 ILE A 222       6.946   8.989  22.555  1.00 20.81           C  
ANISOU 1699  CG2 ILE A 222     3099   1858   2951   -157   -106   -134       C  
ATOM   1700  CD1 ILE A 222       4.132  10.367  22.799  1.00 24.82           C  
ANISOU 1700  CD1 ILE A 222     3541   2100   3789     68    159    189       C  
ATOM   1701  N   MET A 223       6.515   5.149  23.398  1.00 22.78           N  
ANISOU 1701  N   MET A 223     3419   2419   2819    -64   -438    -95       N  
ATOM   1702  CA  MET A 223       7.472   4.138  23.880  1.00 22.41           C  
ANISOU 1702  CA  MET A 223     3313   2414   2789     20   -421    -16       C  
ATOM   1703  C   MET A 223       8.009   3.365  22.676  1.00 24.86           C  
ANISOU 1703  C   MET A 223     3642   2585   3221     17   -336    -73       C  
ATOM   1704  O   MET A 223       9.232   3.137  22.585  1.00 26.12           O  
ANISOU 1704  O   MET A 223     3728   2777   3420     88   -302    -42       O  
ATOM   1705  CB  MET A 223       6.788   3.174  24.873  1.00 21.45           C  
ANISOU 1705  CB  MET A 223     3163   2286   2699    109   -366    172       C  
ATOM   1706  CG  MET A 223       6.666   3.856  26.247  1.00 23.56           C  
ANISOU 1706  CG  MET A 223     3333   2886   2731    126   -439    203       C  
ATOM   1707  SD  MET A 223       5.631   3.015  27.424  1.00 26.88           S  
ANISOU 1707  SD  MET A 223     3703   3404   3108    230   -352    489       S  
ATOM   1708  CE  MET A 223       6.709   1.675  27.930  1.00 25.35           C  
ANISOU 1708  CE  MET A 223     3326   3327   2979    507   -228    975       C  
ATOM   1709  N   GLN A 224       7.107   2.893  21.802  1.00 23.57           N  
ANISOU 1709  N   GLN A 224     3518   2340   3098    -82   -279   -206       N  
ATOM   1710  CA  GLN A 224       7.547   2.139  20.621  1.00 25.31           C  
ANISOU 1710  CA  GLN A 224     3709   2514   3394   -157   -147   -420       C  
ATOM   1711  C   GLN A 224       8.418   3.016  19.705  1.00 24.76           C  
ANISOU 1711  C   GLN A 224     3619   2646   3143   -166   -202   -441       C  
ATOM   1712  O   GLN A 224       9.403   2.546  19.119  1.00 26.84           O  
ANISOU 1712  O   GLN A 224     3841   2884   3471   -157    -88   -550       O  
ATOM   1713  CB  GLN A 224       6.364   1.541  19.826  1.00 27.77           C  
ANISOU 1713  CB  GLN A 224     3968   2893   3689   -357    -74   -710       C  
ATOM   1714  CG  GLN A 224       6.783   0.639  18.622  1.00 32.43           C  
ANISOU 1714  CG  GLN A 224     4468   3503   4349   -521    138  -1128       C  
ATOM   1715  CD  GLN A 224       7.662  -0.506  19.057  1.00 35.94           C  
ANISOU 1715  CD  GLN A 224     4926   3456   5275   -418    442  -1136       C  
ATOM   1716  OE1 GLN A 224       8.804  -0.657  18.604  1.00 36.67           O  
ANISOU 1716  OE1 GLN A 224     4993   3505   5435   -343    549  -1184       O  
ATOM   1717  NE2 GLN A 224       7.148  -1.312  19.969  1.00 37.78           N  
ANISOU 1717  NE2 GLN A 224     5165   3308   5882   -370    626  -1003       N  
ATOM   1718  N   LEU A 225       8.086   4.298  19.590  1.00 22.30           N  
ANISOU 1718  N   LEU A 225     3313   2488   2673   -165   -308   -301       N  
ATOM   1719  CA  LEU A 225       8.885   5.188  18.753  1.00 24.01           C  
ANISOU 1719  CA  LEU A 225     3487   2834   2800   -157   -273   -217       C  
ATOM   1720  C   LEU A 225      10.280   5.327  19.281  1.00 23.18           C  
ANISOU 1720  C   LEU A 225     3362   2609   2835   -127   -239   -224       C  
ATOM   1721  O   LEU A 225      11.227   5.404  18.499  1.00 24.12           O  
ANISOU 1721  O   LEU A 225     3426   2804   2933   -138   -157   -245       O  
ATOM   1722  CB  LEU A 225       8.252   6.587  18.680  1.00 23.13           C  
ANISOU 1722  CB  LEU A 225     3356   2757   2678   -111   -264     40       C  
ATOM   1723  CG  LEU A 225       6.911   6.545  17.922  1.00 24.19           C  
ANISOU 1723  CG  LEU A 225     3395   3214   2583    -91   -312    149       C  
ATOM   1724  CD1 LEU A 225       6.363   8.000  17.823  1.00 20.25           C  
ANISOU 1724  CD1 LEU A 225     2821   2693   2179     63   -211    568       C  
ATOM   1725  CD2 LEU A 225       7.078   5.935  16.493  1.00 25.85           C  
ANISOU 1725  CD2 LEU A 225     3466   3902   2454   -166   -303     29       C  
ATOM   1726  N   LEU A 226      10.409   5.484  20.595  1.00 23.18           N  
ANISOU 1726  N   LEU A 226     3350   2538   2921   -102   -298   -211       N  
ATOM   1727  CA  LEU A 226      11.747   5.468  21.247  1.00 24.12           C  
ANISOU 1727  CA  LEU A 226     3331   2751   3081    -82   -304   -242       C  
ATOM   1728  C   LEU A 226      12.520   4.176  20.932  1.00 26.71           C  
ANISOU 1728  C   LEU A 226     3596   3072   3483     48   -236   -204       C  
ATOM   1729  O   LEU A 226      13.699   4.228  20.509  1.00 27.31           O  
ANISOU 1729  O   LEU A 226     3554   3228   3594     61   -177   -230       O  
ATOM   1730  CB  LEU A 226      11.620   5.661  22.764  1.00 23.71           C  
ANISOU 1730  CB  LEU A 226     3183   2867   2959    -81   -396   -258       C  
ATOM   1731  CG  LEU A 226      11.215   7.083  23.221  1.00 23.83           C  
ANISOU 1731  CG  LEU A 226     3189   2855   3011   -255   -355   -446       C  
ATOM   1732  CD1 LEU A 226      10.601   7.015  24.656  1.00 29.67           C  
ANISOU 1732  CD1 LEU A 226     3857   3829   3589   -261   -432   -517       C  
ATOM   1733  CD2 LEU A 226      12.397   8.115  23.146  1.00 24.94           C  
ANISOU 1733  CD2 LEU A 226     3160   3045   3273   -441   -240   -675       C  
ATOM   1734  N   ARG A 227      11.868   3.047  21.089  1.00 25.68           N  
ANISOU 1734  N   ARG A 227     3517   2786   3454    135   -173   -154       N  
ATOM   1735  CA  ARG A 227      12.456   1.781  20.756  1.00 27.97           C  
ANISOU 1735  CA  ARG A 227     3740   2900   3986    265     33   -137       C  
ATOM   1736  C   ARG A 227      12.900   1.677  19.295  1.00 28.51           C  
ANISOU 1736  C   ARG A 227     3824   2945   4064    160    173   -409       C  
ATOM   1737  O   ARG A 227      13.950   1.191  19.014  1.00 29.43           O  
ANISOU 1737  O   ARG A 227     3827   3019   4339    263    326   -415       O  
ATOM   1738  CB  ARG A 227      11.498   0.665  21.123  1.00 28.29           C  
ANISOU 1738  CB  ARG A 227     3831   2648   4270    316    194    -86       C  
ATOM   1739  CG  ARG A 227      11.863  -0.665  20.573  1.00 39.82           C  
ANISOU 1739  CG  ARG A 227     5235   3736   6158    389    563   -185       C  
ATOM   1740  CD  ARG A 227      13.166  -1.199  21.102  1.00 45.32           C  
ANISOU 1740  CD  ARG A 227     5726   4402   7091    712    711    179       C  
ATOM   1741  NE  ARG A 227      13.276  -1.114  22.537  1.00 55.73           N  
ANISOU 1741  NE  ARG A 227     6896   5987   8293    956    572    701       N  
ATOM   1742  CZ  ARG A 227      14.421  -0.952  23.167  1.00 59.97           C  
ANISOU 1742  CZ  ARG A 227     7161   6928   8698   1194    479   1041       C  
ATOM   1743  NH1 ARG A 227      15.548  -0.880  22.484  1.00 56.76           N  
ANISOU 1743  NH1 ARG A 227     6637   6578   8352   1229    534    930       N  
ATOM   1744  NH2 ARG A 227      14.445  -0.850  24.468  1.00 61.82           N  
ANISOU 1744  NH2 ARG A 227     7187   7621   8683   1381    331   1471       N  
ATOM   1745  N   ASP A 228      12.081   2.153  18.386  1.00 27.03           N  
ANISOU 1745  N   ASP A 228     3726   2884   3661    -25    127   -599       N  
ATOM   1746  CA  ASP A 228      12.392   2.106  16.968  1.00 30.32           C  
ANISOU 1746  CA  ASP A 228     4097   3493   3929   -140    249   -850       C  
ATOM   1747  C   ASP A 228      13.668   2.897  16.746  1.00 28.45           C  
ANISOU 1747  C   ASP A 228     3787   3386   3639    -85    240   -704       C  
ATOM   1748  O   ASP A 228      14.526   2.448  15.975  1.00 29.29           O  
ANISOU 1748  O   ASP A 228     3805   3545   3780    -82    421   -865       O  
ATOM   1749  CB  ASP A 228      11.291   2.751  16.091  1.00 30.95           C  
ANISOU 1749  CB  ASP A 228     4180   3948   3631   -293    146   -908       C  
ATOM   1750  CG  ASP A 228      10.009   1.975  16.078  1.00 34.58           C  
ANISOU 1750  CG  ASP A 228     4632   4417   4091   -427    165  -1165       C  
ATOM   1751  OD1 ASP A 228      10.048   0.760  16.371  1.00 32.13           O  
ANISOU 1751  OD1 ASP A 228     4320   3756   4132   -460    377  -1419       O  
ATOM   1752  OD2 ASP A 228       8.970   2.569  15.665  1.00 34.97           O  
ANISOU 1752  OD2 ASP A 228     4623   4847   3816   -500     24  -1105       O  
ATOM   1753  N   ASN A 229      13.757   4.109  17.321  1.00 26.17           N  
ANISOU 1753  N   ASN A 229     3507   3143   3295    -86     93   -472       N  
ATOM   1754  CA  ASN A 229      14.984   4.898  17.110  1.00 27.27           C  
ANISOU 1754  CA  ASN A 229     3530   3368   3462   -105    150   -398       C  
ATOM   1755  C   ASN A 229      16.243   4.204  17.685  1.00 27.93           C  
ANISOU 1755  C   ASN A 229     3444   3439   3730     13    192   -422       C  
ATOM   1756  O   ASN A 229      17.313   4.175  17.033  1.00 28.08           O  
ANISOU 1756  O   ASN A 229     3334   3551   3784     20    326   -465       O  
ATOM   1757  CB  ASN A 229      14.855   6.362  17.591  1.00 26.29           C  
ANISOU 1757  CB  ASN A 229     3402   3200   3387   -198    112   -260       C  
ATOM   1758  CG  ASN A 229      13.902   7.185  16.710  1.00 30.26           C  
ANISOU 1758  CG  ASN A 229     3980   3746   3773   -217    183    -55       C  
ATOM   1759  OD1 ASN A 229      13.462   6.711  15.680  1.00 31.09           O  
ANISOU 1759  OD1 ASN A 229     4088   4101   3625   -189    202    -39       O  
ATOM   1760  ND2 ASN A 229      13.614   8.434  17.104  1.00 29.44           N  
ANISOU 1760  ND2 ASN A 229     3872   3448   3865   -261    271     99       N  
ATOM   1761  N   LEU A 230      16.122   3.676  18.908  1.00 27.65           N  
ANISOU 1761  N   LEU A 230     3355   3364   3786    138     93   -322       N  
ATOM   1762  CA  LEU A 230      17.241   2.974  19.548  1.00 30.81           C  
ANISOU 1762  CA  LEU A 230     3499   3882   4325    344    134   -179       C  
ATOM   1763  C   LEU A 230      17.776   1.842  18.673  1.00 33.10           C  
ANISOU 1763  C   LEU A 230     3749   3969   4857    491    415   -235       C  
ATOM   1764  O   LEU A 230      18.999   1.656  18.526  1.00 35.03           O  
ANISOU 1764  O   LEU A 230     3761   4338   5212    613    522   -176       O  
ATOM   1765  CB  LEU A 230      16.788   2.405  20.900  1.00 31.45           C  
ANISOU 1765  CB  LEU A 230     3504   4029   4415    525     37     75       C  
ATOM   1766  CG  LEU A 230      16.819   3.465  21.987  1.00 31.68           C  
ANISOU 1766  CG  LEU A 230     3394   4467   4176    391   -201     52       C  
ATOM   1767  CD1 LEU A 230      15.911   3.069  23.193  1.00 35.15           C  
ANISOU 1767  CD1 LEU A 230     3834   5021   4500    508   -300    262       C  
ATOM   1768  CD2 LEU A 230      18.246   3.616  22.408  1.00 32.74           C  
ANISOU 1768  CD2 LEU A 230     3124   5084   4233    446   -246    101       C  
ATOM   1769  N   THR A 231      16.848   1.064  18.127  1.00 33.62           N  
ANISOU 1769  N   THR A 231     3998   3735   5040    458    576   -408       N  
ATOM   1770  CA  THR A 231      17.155  -0.053  17.233  1.00 36.47           C  
ANISOU 1770  CA  THR A 231     4324   3835   5698    507    947   -656       C  
ATOM   1771  C   THR A 231      17.883   0.452  15.969  1.00 38.56           C  
ANISOU 1771  C   THR A 231     4544   4353   5753    360   1026   -915       C  
ATOM   1772  O   THR A 231      18.924  -0.069  15.577  1.00 40.55           O  
ANISOU 1772  O   THR A 231     4628   4554   6226    484   1279   -978       O  
ATOM   1773  CB  THR A 231      15.853  -0.777  16.830  1.00 36.78           C  
ANISOU 1773  CB  THR A 231     4528   3608   5838    342   1104   -985       C  
ATOM   1774  OG1 THR A 231      15.318  -1.439  17.978  1.00 36.88           O  
ANISOU 1774  OG1 THR A 231     4546   3304   6163    517   1152   -690       O  
ATOM   1775  CG2 THR A 231      16.097  -1.804  15.704  1.00 40.66           C  
ANISOU 1775  CG2 THR A 231     4953   3887   6608    248   1558  -1500       C  
ATOM   1776  N   LEU A 232      17.350   1.498  15.360  1.00 36.68           N  
ANISOU 1776  N   LEU A 232     4421   4410   5106    136    845   -981       N  
ATOM   1777  CA  LEU A 232      17.987   2.087  14.185  1.00 40.45           C  
ANISOU 1777  CA  LEU A 232     4827   5209   5332     23    939  -1084       C  
ATOM   1778  C   LEU A 232      19.422   2.517  14.531  1.00 40.25           C  
ANISOU 1778  C   LEU A 232     4608   5231   5456    130    955   -880       C  
ATOM   1779  O   LEU A 232      20.396   2.076  13.907  1.00 42.27           O  
ANISOU 1779  O   LEU A 232     4707   5541   5813    189   1193  -1009       O  
ATOM   1780  CB  LEU A 232      17.144   3.268  13.696  1.00 38.31           C  
ANISOU 1780  CB  LEU A 232     4656   5241   4661   -135    769   -939       C  
ATOM   1781  CG  LEU A 232      17.600   4.023  12.450  1.00 45.19           C  
ANISOU 1781  CG  LEU A 232     5429   6530   5211   -217    894   -862       C  
ATOM   1782  CD1 LEU A 232      17.437   3.181  11.169  1.00 49.33           C  
ANISOU 1782  CD1 LEU A 232     5864   7452   5426   -319   1101  -1282       C  
ATOM   1783  CD2 LEU A 232      16.758   5.272  12.391  1.00 43.24           C  
ANISOU 1783  CD2 LEU A 232     5243   6428   4760   -249    763   -476       C  
ATOM   1784  N   TRP A 233      19.559   3.265  15.613  1.00 36.28           N  
ANISOU 1784  N   TRP A 233     4059   4738   4989    143    728   -632       N  
ATOM   1785  CA  TRP A 233      20.828   3.882  15.949  1.00 37.82           C  
ANISOU 1785  CA  TRP A 233     3996   5113   5259    137    718   -531       C  
ATOM   1786  C   TRP A 233      21.895   2.905  16.440  1.00 40.32           C  
ANISOU 1786  C   TRP A 233     4023   5480   5818    401    809   -449       C  
ATOM   1787  O   TRP A 233      23.079   3.207  16.349  1.00 42.43           O  
ANISOU 1787  O   TRP A 233     4011   5977   6134    401    869   -427       O  
ATOM   1788  CB  TRP A 233      20.599   4.974  16.999  1.00 35.94           C  
ANISOU 1788  CB  TRP A 233     3727   4950   4980    -11    495   -454       C  
ATOM   1789  CG  TRP A 233      19.740   6.084  16.506  1.00 36.39           C  
ANISOU 1789  CG  TRP A 233     3993   4890   4944   -211    514   -432       C  
ATOM   1790  CD1 TRP A 233      19.489   6.415  15.208  1.00 39.69           C  
ANISOU 1790  CD1 TRP A 233     4517   5330   5234   -260    683   -358       C  
ATOM   1791  CD2 TRP A 233      19.032   7.031  17.312  1.00 33.92           C  
ANISOU 1791  CD2 TRP A 233     3746   4469   4671   -349    411   -426       C  
ATOM   1792  NE1 TRP A 233      18.657   7.511  15.154  1.00 41.25           N  
ANISOU 1792  NE1 TRP A 233     4829   5416   5428   -358    700   -182       N  
ATOM   1793  CE2 TRP A 233      18.347   7.898  16.433  1.00 36.29           C  
ANISOU 1793  CE2 TRP A 233     4202   4628   4960   -424    559   -265       C  
ATOM   1794  CE3 TRP A 233      18.863   7.192  18.694  1.00 31.69           C  
ANISOU 1794  CE3 TRP A 233     3372   4259   4408   -397    237   -531       C  
ATOM   1795  CZ2 TRP A 233      17.563   8.977  16.893  1.00 35.74           C  
ANISOU 1795  CZ2 TRP A 233     4206   4330   5045   -530    603   -198       C  
ATOM   1796  CZ3 TRP A 233      18.039   8.245  19.157  1.00 32.54           C  
ANISOU 1796  CZ3 TRP A 233     3578   4188   4600   -569    257   -600       C  
ATOM   1797  CH2 TRP A 233      17.398   9.113  18.249  1.00 35.79           C  
ANISOU 1797  CH2 TRP A 233     4159   4304   5136   -619    463   -428       C  
ATOM   1798  N   THR A 234      21.484   1.751  16.963  1.00 41.34           N  
ANISOU 1798  N   THR A 234     4172   5389   6147    646    867   -347       N  
ATOM   1799  CA  THR A 234      22.426   0.796  17.555  1.00 47.76           C  
ANISOU 1799  CA  THR A 234     4649   6233   7265   1011   1012    -74       C  
ATOM   1800  C   THR A 234      22.686  -0.399  16.643  1.00 51.81           C  
ANISOU 1800  C   THR A 234     5164   6346   8175   1184   1469   -235       C  
ATOM   1801  O   THR A 234      22.216  -0.407  15.502  1.00 51.68           O  
ANISOU 1801  O   THR A 234     5377   6186   8073    947   1629   -662       O  
ATOM   1802  CB  THR A 234      21.974   0.311  18.946  1.00 49.05           C  
ANISOU 1802  CB  THR A 234     4711   6445   7479   1260    870    324       C  
ATOM   1803  OG1 THR A 234      20.627  -0.180  18.875  1.00 48.48           O  
ANISOU 1803  OG1 THR A 234     4986   5929   7504   1204    942    227       O  
ATOM   1804  CG2 THR A 234      22.030   1.463  19.968  1.00 49.70           C  
ANISOU 1804  CG2 THR A 234     4641   7093   7152   1081    467    383       C  
TER    1805      THR A 234                                                      
ATOM   1806  N   SER B   6      10.509  12.885  11.285  1.00 45.22           N  
ATOM   1807  CA  SER B   6      11.669  12.097  10.793  1.00 44.74           C  
ATOM   1808  C   SER B   6      11.853  10.836  11.695  1.00 42.46           C  
ATOM   1809  O   SER B   6      10.919  10.014  11.859  1.00 42.81           O  
ATOM   1810  CB  SER B   6      12.935  13.001  10.652  1.00 47.14           C  
ATOM   1811  OG  SER B   6      13.022  14.079  11.612  1.00 44.15           O  
ATOM   1812  N   PRO B   7      12.959  10.829  12.414  1.00 38.67           N  
ATOM   1813  CA  PRO B   7      13.013  10.088  13.661  1.00 36.69           C  
ATOM   1814  C   PRO B   7      12.350  10.926  14.763  1.00 32.85           C  
ATOM   1815  O   PRO B   7      12.607  10.627  15.930  1.00 30.64           O  
ATOM   1816  CB  PRO B   7      14.514   9.961  13.922  1.00 38.55           C  
ATOM   1817  CG  PRO B   7      15.124   9.971  12.570  1.00 41.31           C  
ATOM   1818  CD  PRO B   7      14.270  10.889  11.743  1.00 35.49           C  
HETATM 1819  N   SEP B   8      11.535  11.943  14.442  1.00 28.51           N  
HETATM 1820  CA  SEP B   8      10.981  12.762  15.575  1.00 26.49           C  
HETATM 1821  CB  SEP B   8      11.138  14.271  15.338  1.00 26.39           C  
HETATM 1822  OG  SEP B   8      10.384  14.675  14.136  1.00 27.55           O  
HETATM 1823  C   SEP B   8       9.498  12.479  15.795  1.00 25.59           C  
HETATM 1824  O   SEP B   8       8.923  11.671  15.025  1.00 24.41           O  
HETATM 1825  P   SEP B   8      10.486  16.197  13.641  1.00 22.77           P  
HETATM 1826  O1P SEP B   8      10.170  17.132  14.744  1.00 21.86           O  
HETATM 1827  O2P SEP B   8      11.898  16.346  13.108  1.00 19.55           O  
HETATM 1828  O3P SEP B   8       9.474  16.359  12.467  1.00 20.38           O  
ATOM   1829  N   LEU B   9       8.877  13.117  16.772  1.00 24.05           N  
ATOM   1830  CA  LEU B   9       7.479  12.815  17.110  1.00 25.94           C  
ATOM   1831  C   LEU B   9       6.546  13.180  15.965  1.00 25.92           C  
ATOM   1832  O   LEU B   9       6.599  14.293  15.460  1.00 26.19           O  
ATOM   1833  CB  LEU B   9       7.066  13.595  18.358  1.00 22.90           C  
ATOM   1834  CG  LEU B   9       5.726  13.260  19.012  1.00 25.87           C  
ATOM   1835  CD1 LEU B   9       5.693  11.897  19.687  1.00 23.93           C  
ATOM   1836  CD2 LEU B   9       5.442  14.333  20.047  1.00 26.15           C  
ATOM   1837  N   PRO B  10       5.743  12.173  15.638  1.00 27.76           N  
ATOM   1838  CA  PRO B  10       4.555  12.284  14.812  1.00 27.60           C  
ATOM   1839  C   PRO B  10       3.673  13.380  15.359  1.00 29.52           C  
ATOM   1840  O   PRO B  10       3.455  13.553  16.558  1.00 24.78           O  
ATOM   1841  CB  PRO B  10       3.880  10.925  14.992  1.00 29.74           C  
ATOM   1842  CG  PRO B  10       4.289  10.490  16.356  1.00 31.74           C  
ATOM   1843  CD  PRO B  10       5.685  11.014  16.547  1.00 26.21           C  
ATOM   1844  N   ASN B  11       3.172  14.123  14.400  1.00 30.55           N  
ATOM   1845  CA  ASN B  11       2.361  15.318  14.558  1.00 35.05           C  
ATOM   1846  C   ASN B  11       1.057  14.923  15.272  1.00 36.21           C  
ATOM   1847  O   ASN B  11       0.562  13.810  15.106  1.00 35.85           O  
ATOM   1848  CB  ASN B  11       2.109  15.910  13.163  1.00 37.82           C  
ATOM   1849  CG  ASN B  11       1.526  17.302  13.202  1.00 38.72           C  
ATOM   1850  OD1 ASN B  11       1.799  18.072  14.125  1.00 48.35           O  
ATOM   1851  ND2 ASN B  11       0.779  17.657  12.185  1.00 30.32           N  
ATOM   1852  N   ILE B  12       0.479  15.742  16.138  1.00 39.60           N  
ATOM   1853  CA  ILE B  12      -0.659  15.225  16.934  1.00 44.30           C  
ATOM   1854  C   ILE B  12      -1.901  14.779  16.126  1.00 45.52           C  
ATOM   1855  O   ILE B  12      -2.287  15.476  15.187  1.00 43.05           O  
ATOM   1856  CB  ILE B  12      -1.104  16.245  18.001  1.00 45.63           C  
ATOM   1857  CG1 ILE B  12      -0.083  16.305  19.139  1.00 47.95           C  
ATOM   1858  CG2 ILE B  12      -2.484  15.891  18.534  1.00 47.06           C  
ATOM   1859  CD1 ILE B  12       0.299  17.713  19.542  1.00 52.65           C  
ATOM   1860  N   THR B  13      -2.544  13.651  16.478  1.00 47.20           N  
ATOM   1861  CA  THR B  13      -3.825  13.350  15.837  1.00 49.71           C  
ATOM   1862  C   THR B  13      -4.980  14.079  16.566  1.00 50.20           C  
ATOM   1863  O   THR B  13      -5.113  14.004  17.798  1.00 49.01           O  
ATOM   1864  CB  THR B  13      -4.056  11.809  15.722  1.00 52.08           C  
ATOM   1865  OG1 THR B  13      -3.593  11.178  16.921  1.00 53.17           O  
ATOM   1866  CG2 THR B  13      -3.252  11.211  14.512  1.00 49.15           C  
ATOM   1867  N   LEU B  14      -5.755  14.854  15.806  1.00 50.62           N  
ATOM   1868  CA  LEU B  14      -6.821  15.693  16.379  1.00 51.49           C  
ATOM   1869  C   LEU B  14      -8.156  14.944  16.546  1.00 52.99           C  
ATOM   1870  O   LEU B  14      -8.327  13.842  16.022  1.00 52.04           O  
ATOM   1871  CB  LEU B  14      -7.013  16.972  15.547  1.00 51.12           C  
ATOM   1872  CG  LEU B  14      -5.836  17.958  15.552  1.00 47.69           C  
ATOM   1873  CD2 LEU B  14      -5.670  18.657  16.927  1.00 44.09           C  
TER    1874      LEU B  14                                                      
HETATM 1875  N   NO3 A 301      28.704  10.668  21.605  1.00 39.10           N  
HETATM 1876  O1  NO3 A 301      29.980  10.941  22.111  1.00 43.24           O  
HETATM 1877  O2  NO3 A 301      27.616  11.300  22.186  1.00 36.52           O  
HETATM 1878  O3  NO3 A 301      28.547   9.721  20.589  1.00 38.99           O  
HETATM 1879  N   NO3 A 302      25.070  32.377  36.660  1.00 31.29           N  
HETATM 1880  O1  NO3 A 302      26.251  31.710  36.959  1.00 33.98           O  
HETATM 1881  O2  NO3 A 302      25.024  33.346  35.696  1.00 28.35           O  
HETATM 1882  O3  NO3 A 302      23.867  32.105  37.291  1.00 36.67           O  
HETATM 1883 MG    MG A 303       8.333   9.701  39.243  1.00 57.83          MG  
HETATM 1884  N   NO3 B 101      16.287  10.485   9.972  1.00 63.01           N  
HETATM 1885  O1  NO3 B 101      15.280   9.583   9.584  1.00 61.69           O  
HETATM 1886  O2  NO3 B 101      16.610  11.589   9.147  1.00 62.92           O  
HETATM 1887  O3  NO3 B 101      16.948  10.279  11.205  1.00 62.47           O  
HETATM 1888  O   HOH A 401      -0.013  39.606  14.132  0.50 30.00           O  
HETATM 1889  O   HOH A 402      22.622  23.101   7.797  1.00 38.64           O  
HETATM 1890  O   HOH A 403      -1.729  33.899  24.745  1.00 18.26           O  
HETATM 1891  O   HOH A 404      -4.021  27.454   3.684  1.00 22.62           O  
HETATM 1892  O   HOH A 405      -1.228  28.385  27.583  1.00 15.38           O  
HETATM 1893  O   HOH A 406       7.237  32.191   5.968  1.00 20.38           O  
HETATM 1894  O   HOH A 407      -7.644  22.421  28.479  1.00 18.89           O  
HETATM 1895  O   HOH A 408      17.936   2.940  32.144  1.00 21.66           O  
HETATM 1896  O   HOH A 409      10.676   6.703  15.861  1.00 21.15           O  
HETATM 1897  O   HOH A 410       7.597  13.049  38.546  1.00 26.75           O  
HETATM 1898  O   HOH A 411       5.412  20.130  22.243  1.00 19.39           O  
HETATM 1899  O   HOH A 412       1.035   8.809  31.941  1.00 17.81           O  
HETATM 1900  O   HOH A 413      -5.590  33.399  23.935  1.00 19.39           O  
HETATM 1901  O   HOH A 414       8.789  17.395   6.535  1.00 33.90           O  
HETATM 1902  O   HOH A 415       4.525  31.676   9.748  1.00 25.05           O  
HETATM 1903  O   HOH A 416     -15.990  19.857  11.320  1.00 27.66           O  
HETATM 1904  O   HOH A 417      22.895  30.334   8.679  1.00 23.03           O  
HETATM 1905  O   HOH A 418       4.378  17.815  23.119  1.00 31.97           O  
HETATM 1906  O   HOH A 419      -7.456  24.891  -0.686  1.00 13.08           O  
HETATM 1907  O   HOH A 420      10.180   8.549  30.536  1.00 24.34           O  
HETATM 1908  O   HOH A 421      -2.152  12.107  29.859  1.00 23.90           O  
HETATM 1909  O   HOH A 422      11.436  33.770   0.914  1.00 18.10           O  
HETATM 1910  O   HOH A 423       5.881  33.331   8.025  1.00 25.31           O  
HETATM 1911  O   HOH A 424     -15.743  32.836  21.756  1.00 21.82           O  
HETATM 1912  O   HOH A 425       9.130  33.665  -0.220  1.00 19.39           O  
HETATM 1913  O   HOH A 426      15.896  -0.941  27.152  1.00 31.02           O  
HETATM 1914  O   HOH A 427      13.224  34.824   6.857  1.00 19.19           O  
HETATM 1915  O   HOH A 428      11.956  29.974  30.005  1.00 32.11           O  
HETATM 1916  O   HOH A 429      -7.901   5.826  26.411  1.00 17.67           O  
HETATM 1917  O   HOH A 430      14.411  22.786   8.850  1.00 18.89           O  
HETATM 1918  O   HOH A 431       0.065  32.278  10.831  1.00 30.34           O  
HETATM 1919  O   HOH A 432       4.656  22.217  16.238  1.00 20.02           O  
HETATM 1920  O   HOH A 433      19.868  19.587   7.607  1.00 21.13           O  
HETATM 1921  O   HOH A 434       4.759   0.206  23.001  1.00 18.36           O  
HETATM 1922  O   HOH A 435      -9.218  21.369  25.648  1.00 15.24           O  
HETATM 1923  O   HOH A 436       9.005  -3.534  34.468  1.00 26.79           O  
HETATM 1924  O   HOH A 437      -0.618   7.419  30.013  1.00 16.53           O  
HETATM 1925  O   HOH A 438      26.148  25.546  19.626  1.00 17.54           O  
HETATM 1926  O   HOH A 439      -0.665   2.640  21.244  1.00 33.56           O  
HETATM 1927  O   HOH A 440      -3.085  35.461  12.052  1.00 20.98           O  
HETATM 1928  O   HOH A 441       5.904  -1.507  35.232  1.00 25.30           O  
HETATM 1929  O   HOH A 442      16.352  28.533  24.489  1.00 20.20           O  
HETATM 1930  O   HOH A 443     -10.010  19.805  17.492  1.00 28.44           O  
HETATM 1931  O   HOH A 444      24.745  34.163  15.884  1.00 30.58           O  
HETATM 1932  O   HOH A 445       8.421  35.694  11.145  1.00 23.65           O  
HETATM 1933  O   HOH A 446      21.907  30.794  22.115  1.00 26.26           O  
HETATM 1934  O   HOH A 447       5.441  38.805  19.640  1.00 18.86           O  
HETATM 1935  O   HOH A 448      13.149  -0.341  33.053  1.00 23.26           O  
HETATM 1936  O   HOH A 449     -10.059  19.379  12.531  1.00 21.98           O  
HETATM 1937  O   HOH A 450       5.760  15.548  23.678  1.00 20.29           O  
HETATM 1938  O   HOH A 451     -10.477  34.997  24.443  1.00 15.33           O  
HETATM 1939  O   HOH A 452      -1.930  34.675  28.812  1.00 27.31           O  
HETATM 1940  O   HOH A 453      18.144  25.259  29.880  1.00 26.32           O  
HETATM 1941  O   HOH A 454       6.203  17.582  17.784  1.00 20.15           O  
HETATM 1942  O   HOH A 455       8.249  -0.851  14.936  1.00 29.99           O  
HETATM 1943  O   HOH A 456     -16.509  17.214  10.392  1.00 26.92           O  
HETATM 1944  O   HOH A 457       6.337   2.409  15.752  1.00 28.35           O  
HETATM 1945  O   HOH A 458      -0.935  22.437  31.825  1.00 12.90           O  
HETATM 1946  O   HOH A 459       9.933  10.923  37.387  1.00 26.85           O  
HETATM 1947  O   HOH A 460      -0.010  20.328  34.442  1.00 25.02           O  
HETATM 1948  O   HOH A 461       0.424  10.794  33.723  1.00 19.84           O  
HETATM 1949  O   HOH A 462      -7.318  31.832   9.151  1.00 25.74           O  
HETATM 1950  O   HOH A 463      -1.132  35.225  10.373  1.00 23.84           O  
HETATM 1951  O   HOH A 464       6.629  20.829  18.176  1.00 32.81           O  
HETATM 1952  O   HOH A 465       8.414  18.846  -0.799  1.00 20.28           O  
HETATM 1953  O   HOH A 466       2.179  38.169  17.676  1.00 18.50           O  
HETATM 1954  O   HOH A 467       9.287  37.853  26.603  1.00 40.06           O  
HETATM 1955  O   HOH A 468       8.956  33.949  27.889  1.00 29.85           O  
HETATM 1956  O   HOH A 469      13.873   0.802  13.841  1.00 20.34           O  
HETATM 1957  O   HOH A 470      -1.718  26.843  29.854  1.00 18.12           O  
HETATM 1958  O   HOH A 471      -0.374  31.319   8.314  1.00 23.14           O  
HETATM 1959  O   HOH A 472      14.895  19.450   6.869  1.00 28.19           O  
HETATM 1960  O   HOH A 473      11.341  34.991  17.039  1.00 26.59           O  
HETATM 1961  O   HOH A 474      10.529  -3.282  19.124  1.00 21.69           O  
HETATM 1962  O   HOH A 475      18.345  29.018  10.382  1.00 19.80           O  
HETATM 1963  O   HOH A 476     -10.718  24.704  23.780  1.00 24.54           O  
HETATM 1964  O   HOH A 477      18.783  32.229  19.605  1.00 30.34           O  
HETATM 1965  O   HOH A 478      16.437   7.597  35.466  1.00 24.98           O  
HETATM 1966  O   HOH A 479       7.403  19.342  10.532  1.00 24.05           O  
HETATM 1967  O   HOH A 480       6.249   8.494  39.228  1.00 31.80           O  
HETATM 1968  O   HOH A 481      -9.141  28.640  26.365  1.00 28.03           O  
HETATM 1969  O   HOH A 482       4.219  20.189  19.788  1.00 19.67           O  
HETATM 1970  O   HOH A 483      -8.538  17.477   2.823  1.00 23.36           O  
HETATM 1971  O   HOH A 484      11.694  10.805  30.443  1.00 28.64           O  
HETATM 1972  O   HOH A 485      16.370  17.309  13.323  1.00 21.63           O  
HETATM 1973  O   HOH A 486      -0.887   8.739  35.604  1.00 26.04           O  
HETATM 1974  O   HOH A 487      27.924  25.470   9.586  1.00 39.54           O  
HETATM 1975  O   HOH A 488     -10.002  32.014   7.389  1.00 40.84           O  
HETATM 1976  O   HOH A 489       5.199   4.035  40.017  1.00 23.23           O  
HETATM 1977  O   HOH A 490      15.861  34.673   7.427  1.00 29.88           O  
HETATM 1978  O   HOH A 491      -0.589  35.737  26.821  1.00 20.02           O  
HETATM 1979  O   HOH A 492      28.489  26.482  13.744  1.00 21.38           O  
HETATM 1980  O   HOH A 493      -2.060  37.572  13.676  1.00 20.27           O  
HETATM 1981  O   HOH A 494       1.812  30.253   7.186  1.00 32.92           O  
HETATM 1982  O   HOH A 495      21.677  26.478   4.485  1.00 21.87           O  
HETATM 1983  O   HOH A 496       1.176  19.111   5.550  1.00 28.65           O  
HETATM 1984  O   HOH A 497      24.534   5.573  24.797  1.00 27.14           O  
HETATM 1985  O   HOH A 498       7.185   8.014  13.424  1.00 25.06           O  
HETATM 1986  O   HOH A 499       4.557  -0.448  37.311  1.00 25.13           O  
HETATM 1987  O   HOH A 500      -4.661  24.844  -0.368  1.00 22.71           O  
HETATM 1988  O   HOH A 501      -4.763  22.343   0.542  1.00 22.36           O  
HETATM 1989  O   HOH A 502      -2.194  24.989  -1.367  1.00 26.15           O  
HETATM 1990  O   HOH A 503       7.674  36.536   6.221  1.00 31.85           O  
HETATM 1991  O   HOH A 504     -14.977  42.150  13.666  1.00 53.27           O  
HETATM 1992  O   HOH A 505       9.524   4.712  14.139  1.00 17.87           O  
HETATM 1993  O   HOH A 506       4.574   3.762  17.657  1.00 23.08           O  
HETATM 1994  O   HOH A 507      17.239  33.159  16.200  1.00 36.57           O  
HETATM 1995  O   HOH A 508     -18.112  28.283  16.415  1.00 23.71           O  
HETATM 1996  O   HOH A 509       3.902  17.763   9.346  1.00 34.79           O  
HETATM 1997  O   HOH A 510       8.305  24.844  36.421  1.00 20.64           O  
HETATM 1998  O   HOH A 511      -7.189  17.963  20.374  1.00 29.79           O  
HETATM 1999  O   HOH A 512       8.127   5.761  12.635  1.00 27.96           O  
HETATM 2000  O   HOH A 513     -13.953  32.668   6.175  1.00 42.52           O  
HETATM 2001  O   HOH A 514      10.953  22.113  37.628  1.00 23.36           O  
HETATM 2002  O   HOH A 515       0.336  30.304  28.285  1.00 26.89           O  
HETATM 2003  O   HOH A 516       8.135  34.517   4.485  1.00 25.08           O  
HETATM 2004  O   HOH A 517       6.558  20.690   0.545  1.00 18.55           O  
HETATM 2005  O   HOH A 518      10.558  34.900   3.380  1.00 22.65           O  
HETATM 2006  O   HOH A 519       2.724  34.329  34.985  1.00 33.06           O  
HETATM 2007  O   HOH A 520      14.400  28.212  26.837  1.00 33.64           O  
HETATM 2008  O   HOH A 521       1.345  23.396   4.666  1.00 26.36           O  
HETATM 2009  O   HOH A 522       2.110  12.760  34.952  1.00 23.72           O  
HETATM 2010  O   HOH A 523      14.905  21.950   6.333  1.00 19.20           O  
HETATM 2011  O   HOH A 524      -8.072  33.612  11.225  1.00 33.26           O  
HETATM 2012  O   HOH A 525      22.471   3.758  25.408  1.00 26.19           O  
HETATM 2013  O   HOH A 526      -2.172  39.362  29.067  1.00 26.79           O  
HETATM 2014  O   HOH A 527      15.851  34.761  -0.834  1.00 22.92           O  
HETATM 2015  O   HOH A 528       0.717  40.224  12.365  1.00 30.00           O  
HETATM 2016  O   HOH B 201      12.222   9.648   9.064  1.00 53.09           O  
HETATM 2017  O   HOH B 202       1.978  18.571  16.556  1.00 24.02           O  
HETATM 2018  O   HOH B 203       3.321  13.522  11.317  1.00 34.93           O  
HETATM 2019  O   HOH B 204       3.831  16.493  17.475  1.00 21.38           O  
HETATM 2020  O   HOH B 205       8.174  16.308  16.329  1.00  8.17           O  
HETATM 2021  O   HOH B 206       8.969   8.975  15.286  1.00 19.99           O  
HETATM 2022  O   HOH B 207      16.350  14.376  12.268  1.00 36.38           O  
HETATM 2023  O   HOH B 208      -2.243  15.430  12.888  1.00 40.29           O  
HETATM 2024  O   HOH B 209       7.717  12.198  12.610  1.00 51.16           O  
HETATM 2025  O   HOH B 210      -6.113  10.566  20.134  1.00 61.07           O  
CONECT 1814 1819                                                                
CONECT 1819 1814 1820                                                           
CONECT 1820 1819 1821 1823                                                      
CONECT 1821 1820 1822                                                           
CONECT 1822 1821 1825                                                           
CONECT 1823 1820 1824 1829                                                      
CONECT 1824 1823                                                                
CONECT 1825 1822 1826 1827 1828                                                 
CONECT 1826 1825                                                                
CONECT 1827 1825                                                                
CONECT 1828 1825                                                                
CONECT 1829 1823                                                                
CONECT 1875 1876 1877 1878                                                      
CONECT 1876 1875                                                                
CONECT 1877 1875                                                                
CONECT 1878 1875                                                                
CONECT 1879 1880 1881 1882                                                      
CONECT 1880 1879                                                                
CONECT 1881 1879                                                                
CONECT 1882 1879                                                                
CONECT 1883 1946 1967                                                           
CONECT 1884 1885 1886 1887                                                      
CONECT 1885 1884                                                                
CONECT 1886 1884                                                                
CONECT 1887 1884                                                                
CONECT 1946 1883                                                                
CONECT 1967 1883                                                                
MASTER      619    0    5   13    0    0    6    6 2013    2   27   22          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.