CNRS Nantes University UFIP UFIP
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***  METAL TRANSPORT 03-MAR-11 3QYT  ***

elNémo ID: 2106161252132815

Job options:

ID        	=	 2106161252132815
JOBID     	=	 METAL TRANSPORT 03-MAR-11 3QYT
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    METAL TRANSPORT                         03-MAR-11   3QYT              
TITLE     DIFERRIC BOUND HUMAN SERUM TRANSFERRIN                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SEROTRANSFERRIN;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SERUM TRANSFERRIN, TRANSFERRIN, BETA-1 METAL-BINDING        
COMPND   5 GLOBULIN, SIDEROPHILIN                                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 OTHER_DETAILS: BLOOD                                                 
KEYWDS    DIFERRIC, HUMAN TRANSFERRIN, INTERMEDIATE, IRON TRANSPORTER, METAL    
KEYWDS   2 TRANSPORT                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.YANG,H.ZHANG,M.WANG,Q.HAO,H.SUN                                     
REVDAT   5   29-JUL-20 3QYT    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE                                     
REVDAT   4   08-NOV-17 3QYT    1       REMARK                                   
REVDAT   3   19-JUN-13 3QYT    1       JRNL                                     
REVDAT   2   26-DEC-12 3QYT    1       JRNL   AUTHOR REMARK                     
REVDAT   1   14-MAR-12 3QYT    0                                                
JRNL        AUTH   N.YANG,H.ZHANG,M.WANG,Q.HAO,H.SUN                            
JRNL        TITL   IRON AND BISMUTH BOUND HUMAN SERUM TRANSFERRIN REVEALS A     
JRNL        TITL 2 PARTIALLY-OPENED CONFORMATION IN THE N-LOBE                  
JRNL        REF    SCI REP                       V.   2   999 2012              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   23256035                                                     
JRNL        DOI    10.1038/SREP00999                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.07                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 16769                          
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) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 908                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 962                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 72.90                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3470                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 52                           
REMARK   3   BIN FREE R VALUE                    : 0.3630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5265                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 43                                      
REMARK   3   SOLVENT ATOMS            : 8                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.29000                                              
REMARK   3    B22 (A**2) : -0.30000                                             
REMARK   3    B33 (A**2) : 0.01000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.453         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.342         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 36.579        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.878                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5444 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3712 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7372 ; 1.154 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9053 ; 0.838 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   678 ; 6.617 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   245 ;35.744 ;24.571       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   917 ;17.862 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;17.683 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   786 ; 0.064 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6086 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1076 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3382 ; 2.133 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1375 ; 0.320 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5408 ; 3.466 ;10.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2062 ; 2.115 ; 5.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1964 ; 3.399 ;10.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  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     1        A    49                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.5390  16.3773 -13.2364              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7293 T22:   0.4797                                     
REMARK   3      T33:   0.4754 T12:  -0.2686                                     
REMARK   3      T13:   0.1661 T23:   0.1155                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2890 L22:   5.4522                                     
REMARK   3      L33:   8.2218 L12:  -2.1079                                     
REMARK   3      L13:  -0.6701 L23:   2.4920                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1490 S12:   0.3929 S13:   0.6114                       
REMARK   3      S21:  -0.5315 S22:   0.1856 S23:  -0.0165                       
REMARK   3      S31:  -1.4354 S32:   0.8636 S33:  -0.3345                       
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    50        A   112                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.0429   9.8057   6.0750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2506 T22:   0.1291                                     
REMARK   3      T33:   0.2517 T12:  -0.0338                                     
REMARK   3      T13:   0.0259 T23:   0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0639 L22:  -0.2593                                     
REMARK   3      L33:   7.6803 L12:   0.6886                                     
REMARK   3      L13:  -1.1659 L23:   0.5938                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1135 S12:   0.1529 S13:   0.0464                       
REMARK   3      S21:  -0.1335 S22:   0.1992 S23:  -0.1412                       
REMARK   3      S31:  -0.3275 S32:   0.2568 S33:  -0.0857                       
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   113        A   166                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.2692  20.0052  22.7056              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3642 T22:   0.2502                                     
REMARK   3      T33:   0.4152 T12:  -0.0419                                     
REMARK   3      T13:   0.0812 T23:  -0.0134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1094 L22:   6.7836                                     
REMARK   3      L33:   9.3014 L12:  -0.8434                                     
REMARK   3      L13:   3.1959 L23:  -1.4085                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1595 S12:   0.1354 S13:   0.9391                       
REMARK   3      S21:  -0.3780 S22:  -0.2584 S23:  -0.4053                       
REMARK   3      S31:  -0.9354 S32:   0.7553 S33:   0.0989                       
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   167        A   215                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.9026  11.8726  22.9021              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2781 T22:   0.7580                                     
REMARK   3      T33:   0.4895 T12:   0.0188                                     
REMARK   3      T13:   0.1496 T23:   0.1388                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0571 L22:   5.6666                                     
REMARK   3      L33:   4.0915 L12:   0.7826                                     
REMARK   3      L13:   1.3390 L23:  -1.7033                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3944 S12:   0.3515 S13:   1.5661                       
REMARK   3      S21:  -0.4377 S22:  -0.4060 S23:  -0.8628                       
REMARK   3      S31:  -0.6895 S32:   1.2769 S33:   0.0117                       
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   216        A   260                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.4367   2.4365  13.3343              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3461 T22:   0.2458                                     
REMARK   3      T33:   0.2372 T12:   0.0806                                     
REMARK   3      T13:   0.0256 T23:  -0.0355                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7330 L22:   0.8759                                     
REMARK   3      L33:   7.5400 L12:   0.8849                                     
REMARK   3      L13:  -2.5387 L23:  -1.2056                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1529 S12:   0.1680 S13:   0.0068                       
REMARK   3      S21:  -0.4601 S22:   0.0903 S23:  -0.1155                       
REMARK   3      S31:   0.9729 S32:  -0.2246 S33:   0.0626                       
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   261        A   340                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.0986   9.2396   0.0727              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2761 T22:   0.0802                                     
REMARK   3      T33:   0.1924 T12:  -0.0921                                     
REMARK   3      T13:  -0.0136 T23:   0.0956                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7092 L22:   3.2109                                     
REMARK   3      L33:   7.7146 L12:  -0.5757                                     
REMARK   3      L13:  -1.7626 L23:   1.1453                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1995 S12:  -0.1478 S13:   0.0743                       
REMARK   3      S21:  -0.1084 S22:   0.2207 S23:  -0.1262                       
REMARK   3      S31:  -0.5286 S32:   0.5162 S33:  -0.0211                       
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   341        A   443                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3820  -4.9419   1.4355              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1329 T22:   0.2554                                     
REMARK   3      T33:   0.1179 T12:   0.0174                                     
REMARK   3      T13:  -0.0231 T23:   0.1119                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7131 L22:   3.4279                                     
REMARK   3      L33:   3.0932 L12:   0.3951                                     
REMARK   3      L13:   0.8758 L23:   0.9326                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0320 S12:  -0.5476 S13:  -0.0207                       
REMARK   3      S21:   0.0937 S22:  -0.0677 S23:   0.1682                       
REMARK   3      S31:  -0.1114 S32:  -0.3152 S33:   0.0356                       
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   444        A   585                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.5238 -15.8460 -12.4809              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1293 T22:   0.0726                                     
REMARK   3      T33:   0.1624 T12:   0.0039                                     
REMARK   3      T13:  -0.0266 T23:   0.0686                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3301 L22:   2.8974                                     
REMARK   3      L33:   4.0743 L12:  -0.3661                                     
REMARK   3      L13:   0.5408 L23:   0.1929                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0959 S12:   0.0065 S13:  -0.4720                       
REMARK   3      S21:  -0.1008 S22:  -0.0375 S23:  -0.0388                       
REMARK   3      S31:   0.3534 S32:  -0.0966 S33:  -0.0584                       
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   586        A   625                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.5282  -0.3902  10.6509              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4006 T22:   0.5516                                     
REMARK   3      T33:   0.2952 T12:   0.0917                                     
REMARK   3      T13:   0.0209 T23:   0.0452                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.4565 L22:   4.8789                                     
REMARK   3      L33:   5.0305 L12:  -1.5226                                     
REMARK   3      L13:  -0.6922 L23:   0.1058                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2210 S12:  -1.3039 S13:  -0.0778                       
REMARK   3      S21:   0.3027 S22:  -0.1429 S23:   0.9220                       
REMARK   3      S31:  -0.0839 S32:  -1.0958 S33:  -0.0781                       
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   626        A   679                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.8104  -9.3673   3.6774              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2904 T22:   0.2726                                     
REMARK   3      T33:   0.2634 T12:  -0.0415                                     
REMARK   3      T13:  -0.0674 T23:   0.0834                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1507 L22:   2.2227                                     
REMARK   3      L33:   1.7511 L12:   0.9510                                     
REMARK   3      L13:   0.6700 L23:  -0.6144                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1674 S12:  -0.7295 S13:  -0.4754                       
REMARK   3      S21:   0.2549 S22:  -0.1179 S23:  -0.3541                       
REMARK   3      S31:   0.1837 S32:   0.1077 S33:  -0.0495                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES: RESIDUAL ONLY                                   
REMARK   4                                                                      
REMARK   4 3QYT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAR-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000064274.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
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          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17765                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.10600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52400                            
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: 2HAV, 1JNF                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01M HEPES, 15% PEG3000, PH 7.4,        
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 271K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       36.92250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.14950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.21750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.14950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.92250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.21750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN A   413     C2   NAG A   684              2.19            
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    VAL A  11      -67.65    -97.13                                   
REMARK 500    ALA A  57      162.66    172.77                                   
REMARK 500    SER A 125      -78.63    -62.71                                   
REMARK 500    TRP A 128      -67.02   -153.26                                   
REMARK 500    SER A 155       31.73    -93.78                                   
REMARK 500    CYS A 177       78.13    -57.98                                   
REMARK 500    CYS A 241       70.91   -165.10                                   
REMARK 500    GLN A 245       76.85   -119.38                                   
REMARK 500    HIS A 249      114.62   -160.98                                   
REMARK 500    MET A 256      -71.82   -100.11                                   
REMARK 500    GLU A 260      -72.14     34.76                                   
REMARK 500    ASP A 277       18.07     58.43                                   
REMARK 500    GLU A 281      -61.77   -107.91                                   
REMARK 500    LEU A 294      -42.19     72.87                                   
REMARK 500    ARG A 327      -64.29    -95.30                                   
REMARK 500    ASP A 337      -79.71    -51.16                                   
REMARK 500    GLU A 338      -48.56   -154.79                                   
REMARK 500    SER A 348      179.61     60.26                                   
REMARK 500    ASP A 392      150.17    -43.82                                   
REMARK 500    ALA A 453      155.71    176.91                                   
REMARK 500    TRP A 460      -65.50   -144.28                                   
REMARK 500    LYS A 470      -64.01   -102.21                                   
REMARK 500    LEU A 494        4.21    -69.76                                   
REMARK 500    LYS A 527      -47.26   -131.34                                   
REMARK 500    CYS A 577       53.14   -154.80                                   
REMARK 500    LEU A 630      -49.01     70.16                                   
REMARK 500    ASP A 643       14.43     56.56                                   
REMARK 500    ASN A 645       50.12   -106.94                                   
REMARK 500    ARG A 678      143.01    170.11                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 682  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A  95   OH                                                     
REMARK 620 2 TYR A 188   OH  116.5                                              
REMARK 620 3 CO3 A 683   O3  100.9  85.0                                        
REMARK 620 4 CO3 A 683   O2  151.4  79.3  54.7                                  
REMARK 620 5 SO4 A 686   O1  124.2  95.5 127.8  74.0                            
REMARK 620 6 SO4 A 686   O3   95.6 147.7  85.8  70.1  66.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 680  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 392   OD1                                                    
REMARK 620 2 TYR A 426   OH   97.3                                              
REMARK 620 3 TYR A 517   OH  153.1 109.5                                        
REMARK 620 4 HIS A 585   NE2  87.0  97.1  87.1                                  
REMARK 620 5 CO3 A 681   O3   89.5  91.3  92.5 171.2                            
REMARK 620 6 CO3 A 681   O2   80.1 151.1  77.8 111.4  60.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2HAV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4H0W   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THIS SEQUENCE IS NATURAL VARIANT.                                    
DBREF  3QYT A    1   679  UNP    P02787   TRFE_HUMAN      20    698             
SEQADV 3QYT VAL A  429  UNP  P02787    ILE   448 SEE REMARK 999                 
SEQRES   1 A  679  VAL PRO ASP LYS THR VAL ARG TRP CYS ALA VAL SER GLU          
SEQRES   2 A  679  HIS GLU ALA THR LYS CYS GLN SER PHE ARG ASP HIS MET          
SEQRES   3 A  679  LYS SER VAL ILE PRO SER ASP GLY PRO SER VAL ALA CYS          
SEQRES   4 A  679  VAL LYS LYS ALA SER TYR LEU ASP CYS ILE ARG ALA ILE          
SEQRES   5 A  679  ALA ALA ASN GLU ALA ASP ALA VAL THR LEU ASP ALA GLY          
SEQRES   6 A  679  LEU VAL TYR ASP ALA TYR LEU ALA PRO ASN ASN LEU LYS          
SEQRES   7 A  679  PRO VAL VAL ALA GLU PHE TYR GLY SER LYS GLU ASP PRO          
SEQRES   8 A  679  GLN THR PHE TYR TYR ALA VAL ALA VAL VAL LYS LYS ASP          
SEQRES   9 A  679  SER GLY PHE GLN MET ASN GLN LEU ARG GLY LYS LYS SER          
SEQRES  10 A  679  CYS HIS THR GLY LEU GLY ARG SER ALA GLY TRP ASN ILE          
SEQRES  11 A  679  PRO ILE GLY LEU LEU TYR CYS ASP LEU PRO GLU PRO ARG          
SEQRES  12 A  679  LYS PRO LEU GLU LYS ALA VAL ALA ASN PHE PHE SER GLY          
SEQRES  13 A  679  SER CYS ALA PRO CYS ALA ASP GLY THR ASP PHE PRO GLN          
SEQRES  14 A  679  LEU CYS GLN LEU CYS PRO GLY CYS GLY CYS SER THR LEU          
SEQRES  15 A  679  ASN GLN TYR PHE GLY TYR SER GLY ALA PHE LYS CYS LEU          
SEQRES  16 A  679  LYS ASP GLY ALA GLY ASP VAL ALA PHE VAL LYS HIS SER          
SEQRES  17 A  679  THR ILE PHE GLU ASN LEU ALA ASN LYS ALA ASP ARG ASP          
SEQRES  18 A  679  GLN TYR GLU LEU LEU CYS LEU ASP ASN THR ARG LYS PRO          
SEQRES  19 A  679  VAL ASP GLU TYR LYS ASP CYS HIS LEU ALA GLN VAL PRO          
SEQRES  20 A  679  SER HIS THR VAL VAL ALA ARG SER MET GLY GLY LYS GLU          
SEQRES  21 A  679  ASP LEU ILE TRP GLU LEU LEU ASN GLN ALA GLN GLU HIS          
SEQRES  22 A  679  PHE GLY LYS ASP LYS SER LYS GLU PHE GLN LEU PHE SER          
SEQRES  23 A  679  SER PRO HIS GLY LYS ASP LEU LEU PHE LYS ASP SER ALA          
SEQRES  24 A  679  HIS GLY PHE LEU LYS VAL PRO PRO ARG MET ASP ALA LYS          
SEQRES  25 A  679  MET TYR LEU GLY TYR GLU TYR VAL THR ALA ILE ARG ASN          
SEQRES  26 A  679  LEU ARG GLU GLY THR CYS PRO GLU ALA PRO THR ASP GLU          
SEQRES  27 A  679  CYS LYS PRO VAL LYS TRP CYS ALA LEU SER HIS HIS GLU          
SEQRES  28 A  679  ARG LEU LYS CYS ASP GLU TRP SER VAL ASN SER VAL GLY          
SEQRES  29 A  679  LYS ILE GLU CYS VAL SER ALA GLU THR THR GLU ASP CYS          
SEQRES  30 A  679  ILE ALA LYS ILE MET ASN GLY GLU ALA ASP ALA MET SER          
SEQRES  31 A  679  LEU ASP GLY GLY PHE VAL TYR ILE ALA GLY LYS CYS GLY          
SEQRES  32 A  679  LEU VAL PRO VAL LEU ALA GLU ASN TYR ASN LYS SER ASP          
SEQRES  33 A  679  ASN CYS GLU ASP THR PRO GLU ALA GLY TYR PHE ALA VAL          
SEQRES  34 A  679  ALA VAL VAL LYS LYS SER ALA SER ASP LEU THR TRP ASP          
SEQRES  35 A  679  ASN LEU LYS GLY LYS LYS SER CYS HIS THR ALA VAL GLY          
SEQRES  36 A  679  ARG THR ALA GLY TRP ASN ILE PRO MET GLY LEU LEU TYR          
SEQRES  37 A  679  ASN LYS ILE ASN HIS CYS ARG PHE ASP GLU PHE PHE SER          
SEQRES  38 A  679  GLU GLY CYS ALA PRO GLY SER LYS LYS ASP SER SER LEU          
SEQRES  39 A  679  CYS LYS LEU CYS MET GLY SER GLY LEU ASN LEU CYS GLU          
SEQRES  40 A  679  PRO ASN ASN LYS GLU GLY TYR TYR GLY TYR THR GLY ALA          
SEQRES  41 A  679  PHE ARG CYS LEU VAL GLU LYS GLY ASP VAL ALA PHE VAL          
SEQRES  42 A  679  LYS HIS GLN THR VAL PRO GLN ASN THR GLY GLY LYS ASN          
SEQRES  43 A  679  PRO ASP PRO TRP ALA LYS ASN LEU ASN GLU LYS ASP TYR          
SEQRES  44 A  679  GLU LEU LEU CYS LEU ASP GLY THR ARG LYS PRO VAL GLU          
SEQRES  45 A  679  GLU TYR ALA ASN CYS HIS LEU ALA ARG ALA PRO ASN HIS          
SEQRES  46 A  679  ALA VAL VAL THR ARG LYS ASP LYS GLU ALA CYS VAL HIS          
SEQRES  47 A  679  LYS ILE LEU ARG GLN GLN GLN HIS LEU PHE GLY SER ASN          
SEQRES  48 A  679  VAL THR ASP CYS SER GLY ASN PHE CYS LEU PHE ARG SER          
SEQRES  49 A  679  GLU THR LYS ASP LEU LEU PHE ARG ASP ASP THR VAL CYS          
SEQRES  50 A  679  LEU ALA LYS LEU HIS ASP ARG ASN THR TYR GLU LYS TYR          
SEQRES  51 A  679  LEU GLY GLU GLU TYR VAL LYS ALA VAL GLY ASN LEU ARG          
SEQRES  52 A  679  LYS CYS SER THR SER SER LEU LEU GLU ALA CYS THR PHE          
SEQRES  53 A  679  ARG ARG PRO                                                  
MODRES 3QYT ASN A  413  ASN  GLYCOSYLATION SITE                                 
MODRES 3QYT ASN A  611  ASN  GLYCOSYLATION SITE                                 
HET     FE  A 680       1                                                       
HET    CO3  A 681       4                                                       
HET     FE  A 682       1                                                       
HET    CO3  A 683       4                                                       
HET    NAG  A 684      14                                                       
HET    NAG  A 685      14                                                       
HET    SO4  A 686       5                                                       
HETNAM      FE FE (III) ION                                                     
HETNAM     CO3 CARBONATE ION                                                    
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2   FE    2(FE 3+)                                                     
FORMUL   3  CO3    2(C O3 2-)                                                   
FORMUL   6  NAG    2(C8 H15 N O6)                                               
FORMUL   8  SO4    O4 S 2-                                                      
FORMUL   9  HOH   *8(H2 O)                                                      
HELIX    1   1 SER A   12  ILE A   30  1                                  19    
HELIX    2   2 SER A   44  ALA A   54  1                                  11    
HELIX    3   3 ASP A   63  LEU A   72  1                                  10    
HELIX    4   4 GLN A  108  LEU A  112  5                                   5    
HELIX    5   5 TRP A  128  TYR A  136  1                                   9    
HELIX    6   6 CYS A  137  LEU A  139  5                                   3    
HELIX    7   7 PRO A  145  PHE A  154  1                                  10    
HELIX    8   8 PHE A  167  GLN A  172  5                                   6    
HELIX    9   9 PHE A  186  GLY A  198  1                                  13    
HELIX   10  10 ASN A  216  ASP A  221  1                                   6    
HELIX   11  11 GLU A  237  CYS A  241  5                                   5    
HELIX   12  12 GLU A  260  GLY A  275  1                                  16    
HELIX   13  13 ASP A  310  GLY A  316  1                                   7    
HELIX   14  14 GLY A  316  GLU A  328  1                                  13    
HELIX   15  15 SER A  348  SER A  362  1                                  15    
HELIX   16  16 THR A  373  GLY A  384  1                                  12    
HELIX   17  17 ASP A  392  CYS A  402  1                                  11    
HELIX   18  18 TRP A  460  ASN A  472  1                                  13    
HELIX   19  19 ARG A  475  PHE A  480  1                                   6    
HELIX   20  20 SER A  492  LYS A  496  5                                   5    
HELIX   21  21 TYR A  515  LYS A  527  1                                  13    
HELIX   22  22 GLN A  536  ASN A  541  1                                   6    
HELIX   23  23 ASP A  548  LYS A  552  5                                   5    
HELIX   24  24 ASN A  555  LYS A  557  5                                   3    
HELIX   25  25 GLU A  572  CYS A  577  5                                   6    
HELIX   26  26 ARG A  590  ASP A  592  5                                   3    
HELIX   27  27 LYS A  593  GLY A  609  1                                  17    
HELIX   28  28 THR A  646  GLY A  652  1                                   7    
HELIX   29  29 GLY A  652  LEU A  662  1                                  11    
HELIX   30  30 ARG A  663  SER A  666  5                                   4    
HELIX   31  31 SER A  668  ARG A  678  1                                  11    
SHEET    1   A 2 VAL A   6  ALA A  10  0                                        
SHEET    2   A 2 VAL A  37  LYS A  41  1  O  VAL A  40   N  ALA A  10           
SHEET    1   B 4 VAL A  60  LEU A  62  0                                        
SHEET    2   B 4 THR A 250  ARG A 254 -1  O  THR A 250   N  LEU A  62           
SHEET    3   B 4 LEU A  77  PHE A  84 -1  N  LYS A  78   O  ALA A 253           
SHEET    4   B 4 GLY A 301  LYS A 304 -1  O  LEU A 303   N  ALA A  82           
SHEET    1   C 6 SER A 157  CYS A 158  0                                        
SHEET    2   C 6 SER A 117  CYS A 118  1  N  SER A 117   O  CYS A 158           
SHEET    3   C 6 VAL A 202  LYS A 206  1  O  VAL A 202   N  CYS A 118           
SHEET    4   C 6 PHE A  94  LYS A 102 -1  N  VAL A  98   O  VAL A 205           
SHEET    5   C 6 TYR A 223  CYS A 227 -1  O  GLU A 224   N  VAL A 101           
SHEET    6   C 6 THR A 231  PRO A 234 -1  O  LYS A 233   N  LEU A 225           
SHEET    1   D 5 SER A 157  CYS A 158  0                                        
SHEET    2   D 5 SER A 117  CYS A 118  1  N  SER A 117   O  CYS A 158           
SHEET    3   D 5 VAL A 202  LYS A 206  1  O  VAL A 202   N  CYS A 118           
SHEET    4   D 5 PHE A  94  LYS A 102 -1  N  VAL A  98   O  VAL A 205           
SHEET    5   D 5 ALA A 244  PRO A 247 -1  O  ALA A 244   N  ALA A  97           
SHEET    1   E 2 VAL A 342  LEU A 347  0                                        
SHEET    2   E 2 ILE A 366  ALA A 371  1  O  GLU A 367   N  TRP A 344           
SHEET    1   F 4 MET A 389  LEU A 391  0                                        
SHEET    2   F 4 ALA A 586  THR A 589 -1  O  ALA A 586   N  LEU A 391           
SHEET    3   F 4 VAL A 405  ASN A 411 -1  N  VAL A 405   O  THR A 589           
SHEET    4   F 4 CYS A 637  LYS A 640 -1  O  ALA A 639   N  ALA A 409           
SHEET    1   G 6 GLU A 482  CYS A 484  0                                        
SHEET    2   G 6 LYS A 448  HIS A 451  1  N  HIS A 451   O  CYS A 484           
SHEET    3   G 6 VAL A 530  LYS A 534  1  O  PHE A 532   N  CYS A 450           
SHEET    4   G 6 TYR A 426  LYS A 433 -1  N  VAL A 429   O  VAL A 533           
SHEET    5   G 6 TYR A 559  LEU A 562 -1  O  LEU A 562   N  ALA A 430           
SHEET    6   G 6 ARG A 568  PRO A 570 -1  O  LYS A 569   N  LEU A 561           
SHEET    1   H 5 GLU A 482  CYS A 484  0                                        
SHEET    2   H 5 LYS A 448  HIS A 451  1  N  HIS A 451   O  CYS A 484           
SHEET    3   H 5 VAL A 530  LYS A 534  1  O  PHE A 532   N  CYS A 450           
SHEET    4   H 5 TYR A 426  LYS A 433 -1  N  VAL A 429   O  VAL A 533           
SHEET    5   H 5 ALA A 580  ALA A 582 -1  O  ALA A 582   N  TYR A 426           
SSBOND   1 CYS A    9    CYS A   48                          1555   1555  2.03  
SSBOND   2 CYS A   19    CYS A   39                          1555   1555  2.05  
SSBOND   3 CYS A  118    CYS A  194                          1555   1555  2.03  
SSBOND   4 CYS A  137    CYS A  331                          1555   1555  2.05  
SSBOND   5 CYS A  158    CYS A  174                          1555   1555  2.02  
SSBOND   6 CYS A  161    CYS A  179                          1555   1555  2.04  
SSBOND   7 CYS A  171    CYS A  177                          1555   1555  2.03  
SSBOND   8 CYS A  227    CYS A  241                          1555   1555  2.04  
SSBOND   9 CYS A  339    CYS A  596                          1555   1555  2.04  
SSBOND  10 CYS A  345    CYS A  377                          1555   1555  2.05  
SSBOND  11 CYS A  355    CYS A  368                          1555   1555  2.05  
SSBOND  12 CYS A  402    CYS A  674                          1555   1555  2.04  
SSBOND  13 CYS A  418    CYS A  637                          1555   1555  2.03  
SSBOND  14 CYS A  450    CYS A  523                          1555   1555  2.06  
SSBOND  15 CYS A  474    CYS A  665                          1555   1555  2.03  
SSBOND  16 CYS A  484    CYS A  498                          1555   1555  2.03  
SSBOND  17 CYS A  495    CYS A  506                          1555   1555  2.06  
SSBOND  18 CYS A  563    CYS A  577                          1555   1555  2.04  
SSBOND  19 CYS A  615    CYS A  620                          1555   1555  2.03  
LINK         ND2 ASN A 413                 C1  NAG A 684     1555   1555  1.45  
LINK         ND2 ASN A 611                 C1  NAG A 685     1555   1555  1.45  
LINK         OH  TYR A  95                FE    FE A 682     1555   1555  2.04  
LINK         OH  TYR A 188                FE    FE A 682     1555   1555  1.87  
LINK         OD1 ASP A 392                FE    FE A 680     1555   1555  2.08  
LINK         OH  TYR A 426                FE    FE A 680     1555   1555  1.86  
LINK         OH  TYR A 517                FE    FE A 680     1555   1555  1.93  
LINK         NE2 HIS A 585                FE    FE A 680     1555   1555  2.08  
LINK        FE    FE A 680                 O3  CO3 A 681     1555   1555  2.06  
LINK        FE    FE A 680                 O2  CO3 A 681     1555   1555  2.39  
LINK        FE    FE A 682                 O3  CO3 A 683     1555   1555  2.28  
LINK        FE    FE A 682                 O2  CO3 A 683     1555   1555  2.57  
LINK        FE    FE A 682                 O1  SO4 A 686     1555   1555  1.93  
LINK        FE    FE A 682                 O3  SO4 A 686     1555   1555  2.38  
CISPEP   1 VAL A    1    PRO A    2          0        -3.69                     
CISPEP   2 ALA A   73    PRO A   74          0         2.85                     
CISPEP   3 GLU A  141    PRO A  142          0        -3.33                     
CISPEP   4 LYS A  144    PRO A  145          0        -1.67                     
CISPEP   5 GLY A  258    LYS A  259          0         2.25                     
CISPEP   6 GLU A  333    ALA A  334          0         3.75                     
CISPEP   7 SER A  501    GLY A  502          0       -23.79                     
CRYST1   73.845   90.435  112.299  90.00  90.00  90.00 P 21 21 21    4          
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      0.013542  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011058  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008905        0.00000                         
ATOM      1  N   VAL A   1      41.943  14.931 -28.645  1.00111.14           N  
ANISOU    1  N   VAL A   1    17453  13941  10835   2423  -2134   1507       N  
ATOM      2  CA  VAL A   1      41.171  13.800 -29.239  1.00112.44           C  
ANISOU    2  CA  VAL A   1    17137  14483  11101   2655  -2615   1096       C  
ATOM      3  C   VAL A   1      42.112  12.680 -29.727  1.00110.76           C  
ANISOU    3  C   VAL A   1    16847  14479  10756   2340  -2497    989       C  
ATOM      4  O   VAL A   1      42.347  12.538 -30.929  1.00113.70           O  
ANISOU    4  O   VAL A   1    17567  15003  10630   2593  -2661    998       O  
ATOM      5  CB  VAL A   1      40.247  14.285 -30.397  1.00118.04           C  
ANISOU    5  CB  VAL A   1    18152  15309  11388   3374  -3136   1045       C  
ATOM      6  CG1 VAL A   1      39.123  15.160 -29.845  1.00120.06           C  
ANISOU    6  CG1 VAL A   1    18309  15444  11864   3765  -3342   1029       C  
ATOM      7  CG2 VAL A   1      41.046  15.048 -31.452  1.00120.96           C  
ANISOU    7  CG2 VAL A   1    19406  15530  11024   3565  -2978   1430       C  
ATOM      8  N   PRO A   2      42.666  11.881 -28.792  1.00105.59           N  
ANISOU    8  N   PRO A   2    15774  13831  10514   1831  -2211    885       N  
ATOM      9  CA  PRO A   2      42.549  11.980 -27.336  1.00101.95           C  
ANISOU    9  CA  PRO A   2    14959  13194  10582   1508  -1961    892       C  
ATOM     10  C   PRO A   2      43.779  12.608 -26.659  1.00 98.53           C  
ANISOU   10  C   PRO A   2    14814  12543  10079   1110  -1429   1212       C  
ATOM     11  O   PRO A   2      44.907  12.400 -27.117  1.00 99.89           O  
ANISOU   11  O   PRO A   2    15207  12795   9950    905  -1194   1319       O  
ATOM     12  CB  PRO A   2      42.405  10.513 -26.912  1.00 99.23           C  
ANISOU   12  CB  PRO A   2    14033  13020  10648   1250  -2030    538       C  
ATOM     13  CG  PRO A   2      43.121   9.716 -27.998  1.00 99.72           C  
ANISOU   13  CG  PRO A   2    14266  13289  10335   1266  -2106    449       C  
ATOM     14  CD  PRO A   2      43.343  10.631 -29.185  1.00103.73           C  
ANISOU   14  CD  PRO A   2    15371  13815  10226   1618  -2187    688       C  
ATOM     15  N   ASP A   3      43.555  13.372 -25.587  1.00 93.75           N  
ANISOU   15  N   ASP A   3    14182  11692   9746   1009  -1248   1330       N  
ATOM     16  CA  ASP A   3      44.646  13.824 -24.716  1.00 86.85           C  
ANISOU   16  CA  ASP A   3    13445  10637   8917    572   -780   1532       C  
ATOM     17  C   ASP A   3      44.845  12.773 -23.632  1.00 79.10           C  
ANISOU   17  C   ASP A   3    11928   9756   8371    248   -659   1321       C  
ATOM     18  O   ASP A   3      43.905  12.075 -23.250  1.00 76.82           O  
ANISOU   18  O   ASP A   3    11216   9538   8432    343   -867   1084       O  
ATOM     19  CB  ASP A   3      44.369  15.215 -24.111  1.00 87.27           C  
ANISOU   19  CB  ASP A   3    13826  10336   8995    637   -646   1754       C  
ATOM     20  CG  ASP A   3      43.409  15.178 -22.919  1.00 84.39           C  
ANISOU   20  CG  ASP A   3    13044   9899   9123    695   -716   1596       C  
ATOM     21  OD1 ASP A   3      43.742  14.572 -21.875  1.00 79.65           O  
ANISOU   21  OD1 ASP A   3    12083   9334   8848    361   -518   1487       O  
ATOM     22  OD2 ASP A   3      42.327  15.788 -23.017  1.00 86.02           O  
ANISOU   22  OD2 ASP A   3    13302  10018   9362   1109   -957   1582       O  
ATOM     23  N   LYS A   4      46.074  12.651 -23.151  1.00 74.10           N  
ANISOU   23  N   LYS A   4    11319   9136   7699   -129   -315   1396       N  
ATOM     24  CA  LYS A   4      46.396  11.638 -22.159  1.00 70.09           C  
ANISOU   24  CA  LYS A   4    10399   8718   7515   -378   -198   1218       C  
ATOM     25  C   LYS A   4      47.199  12.172 -20.969  1.00 68.56           C  
ANISOU   25  C   LYS A   4    10228   8394   7430   -695    145   1323       C  
ATOM     26  O   LYS A   4      47.456  11.432 -20.013  1.00 63.36           O  
ANISOU   26  O   LYS A   4     9281   7784   7008   -852    245   1196       O  
ATOM     27  CB  LYS A   4      47.166  10.501 -22.831  1.00 70.36           C  
ANISOU   27  CB  LYS A   4    10339   9021   7372   -439   -214   1084       C  
ATOM     28  CG  LYS A   4      46.418   9.813 -23.975  1.00 73.02           C  
ANISOU   28  CG  LYS A   4    10637   9503   7604   -142   -581    912       C  
ATOM     29  CD  LYS A   4      45.345   8.857 -23.471  1.00 71.77           C  
ANISOU   29  CD  LYS A   4    10062   9329   7879    -96   -802    637       C  
ATOM     30  CE  LYS A   4      45.934   7.497 -23.116  1.00 68.66           C  
ANISOU   30  CE  LYS A   4     9461   9018   7609   -282   -714    451       C  
ATOM     31  NZ  LYS A   4      45.012   6.678 -22.290  1.00 66.04           N  
ANISOU   31  NZ  LYS A   4     8779   8570   7744   -360   -779    243       N  
ATOM     32  N   THR A   5      47.587  13.444 -21.007  1.00 70.47           N  
ANISOU   32  N   THR A   5    10841   8450   7483   -783    319   1541       N  
ATOM     33  CA  THR A   5      48.438  13.986 -19.956  1.00 68.81           C  
ANISOU   33  CA  THR A   5    10658   8136   7350  -1120    623   1595       C  
ATOM     34  C   THR A   5      47.598  14.384 -18.748  1.00 65.63           C  
ANISOU   34  C   THR A   5    10160   7497   7278  -1050    610   1565       C  
ATOM     35  O   THR A   5      46.570  15.044 -18.895  1.00 69.30           O  
ANISOU   35  O   THR A   5    10777   7765   7788   -779    466   1630       O  
ATOM     36  CB  THR A   5      49.276  15.183 -20.445  1.00 73.22           C  
ANISOU   36  CB  THR A   5    11671   8556   7593  -1338    865   1812       C  
ATOM     37  OG1 THR A   5      50.245  15.513 -19.439  1.00 73.21           O  
ANISOU   37  OG1 THR A   5    11594   8538   7683  -1726   1139   1777       O  
ATOM     38  CG2 THR A   5      48.399  16.399 -20.753  1.00 76.86           C  
ANISOU   38  CG2 THR A   5    12588   8651   7967  -1099    784   2006       C  
ATOM     39  N   VAL A   6      48.039  13.961 -17.564  1.00 60.79           N  
ANISOU   39  N   VAL A   6     9304   6928   6867  -1248    756   1454       N  
ATOM     40  CA  VAL A   6      47.370  14.286 -16.297  1.00 57.80           C  
ANISOU   40  CA  VAL A   6     8844   6349   6767  -1199    801   1417       C  
ATOM     41  C   VAL A   6      47.962  15.561 -15.681  1.00 56.37           C  
ANISOU   41  C   VAL A   6     8975   5934   6507  -1406   1006   1517       C  
ATOM     42  O   VAL A   6      49.152  15.600 -15.346  1.00 54.49           O  
ANISOU   42  O   VAL A   6     8732   5799   6172  -1720   1179   1479       O  
ATOM     43  CB  VAL A   6      47.496  13.121 -15.274  1.00 55.34           C  
ANISOU   43  CB  VAL A   6     8176   6179   6672  -1265    857   1248       C  
ATOM     44  CG1 VAL A   6      47.036  13.559 -13.885  1.00 53.82           C  
ANISOU   44  CG1 VAL A   6     7966   5791   6690  -1249    977   1228       C  
ATOM     45  CG2 VAL A   6      46.695  11.911 -15.735  1.00 55.16           C  
ANISOU   45  CG2 VAL A   6     7879   6282   6796  -1090    674   1128       C  
ATOM     46  N   ARG A   7      47.134  16.595 -15.535  1.00 55.62           N  
ANISOU   46  N   ARG A   7     9142   5535   6457  -1221    973   1612       N  
ATOM     47  CA  ARG A   7      47.593  17.871 -14.994  1.00 59.71           C  
ANISOU   47  CA  ARG A   7    10037   5749   6900  -1407   1154   1694       C  
ATOM     48  C   ARG A   7      47.639  17.842 -13.476  1.00 59.63           C  
ANISOU   48  C   ARG A   7     9864   5692   7099  -1491   1263   1554       C  
ATOM     49  O   ARG A   7      46.672  18.209 -12.807  1.00 61.02           O  
ANISOU   49  O   ARG A   7    10065   5682   7438  -1240   1232   1536       O  
ATOM     50  CB  ARG A   7      46.694  19.013 -15.450  1.00 64.36           C  
ANISOU   50  CB  ARG A   7    11058   5986   7412  -1106   1067   1850       C  
ATOM     51  CG  ARG A   7      46.728  19.276 -16.938  1.00 68.03           C  
ANISOU   51  CG  ARG A   7    11840   6431   7575   -996    978   2024       C  
ATOM     52  CD  ARG A   7      45.670  20.290 -17.301  1.00 73.25           C  
ANISOU   52  CD  ARG A   7    12919   6757   8154   -557    831   2157       C  
ATOM     53  NE  ARG A   7      44.327  19.727 -17.157  1.00 74.78           N  
ANISOU   53  NE  ARG A   7    12715   7115   8582   -100    557   2018       N  
ATOM     54  CZ  ARG A   7      43.212  20.440 -16.999  1.00 78.52           C  
ANISOU   54  CZ  ARG A   7    13331   7389   9115    352    411   2027       C  
ATOM     55  NH1 ARG A   7      43.253  21.766 -16.949  1.00 81.47           N  
ANISOU   55  NH1 ARG A   7    14320   7324   9310    449    500   2190       N  
ATOM     56  NH2 ARG A   7      42.041  19.822 -16.886  1.00 78.70           N  
ANISOU   56  NH2 ARG A   7    12873   7650   9381    709    182   1851       N  
ATOM     57  N   TRP A   8      48.781  17.428 -12.938  1.00 60.12           N  
ANISOU   57  N   TRP A   8     9765   5950   7129  -1811   1389   1441       N  
ATOM     58  CA  TRP A   8      48.928  17.240 -11.503  1.00 59.54           C  
ANISOU   58  CA  TRP A   8     9539   5892   7191  -1854   1466   1290       C  
ATOM     59  C   TRP A   8      49.338  18.539 -10.806  1.00 63.26           C  
ANISOU   59  C   TRP A   8    10349   6071   7614  -2053   1592   1268       C  
ATOM     60  O   TRP A   8      50.282  19.223 -11.240  1.00 61.71           O  
ANISOU   60  O   TRP A   8    10363   5823   7263  -2396   1692   1288       O  
ATOM     61  CB  TRP A   8      49.950  16.140 -11.224  1.00 57.71           C  
ANISOU   61  CB  TRP A   8     8982   6033   6913  -2017   1489   1145       C  
ATOM     62  CG  TRP A   8      49.823  15.544  -9.862  1.00 55.55           C  
ANISOU   62  CG  TRP A   8     8536   5815   6757  -1906   1518   1011       C  
ATOM     63  CD1 TRP A   8      50.185  16.115  -8.687  1.00 56.87           C  
ANISOU   63  CD1 TRP A   8     8806   5891   6910  -1989   1598    903       C  
ATOM     64  CD2 TRP A   8      49.302  14.253  -9.540  1.00 53.93           C  
ANISOU   64  CD2 TRP A   8     8080   5743   6668  -1691   1481    971       C  
ATOM     65  NE1 TRP A   8      49.918  15.264  -7.644  1.00 57.50           N  
ANISOU   65  NE1 TRP A   8     8734   6057   7056  -1797   1616    818       N  
ATOM     66  CE2 TRP A   8      49.377  14.111  -8.142  1.00 53.85           C  
ANISOU   66  CE2 TRP A   8     8067   5710   6682  -1631   1568    872       C  
ATOM     67  CE3 TRP A   8      48.780  13.201 -10.299  1.00 54.85           C  
ANISOU   67  CE3 TRP A   8     8009   5971   6859  -1555   1390    998       C  
ATOM     68  CZ2 TRP A   8      48.952  12.962  -7.484  1.00 53.96           C  
ANISOU   68  CZ2 TRP A   8     7941   5782   6778  -1447   1609    839       C  
ATOM     69  CZ3 TRP A   8      48.359  12.058  -9.647  1.00 54.82           C  
ANISOU   69  CZ3 TRP A   8     7840   6011   6978  -1417   1422    937       C  
ATOM     70  CH2 TRP A   8      48.444  11.948  -8.250  1.00 54.60           C  
ANISOU   70  CH2 TRP A   8     7855   5932   6960  -1365   1552    879       C  
ATOM     71  N   CYS A   9      48.626  18.849  -9.718  1.00 63.56           N  
ANISOU   71  N   CYS A   9    10441   5922   7786  -1856   1608   1209       N  
ATOM     72  CA  CYS A   9      48.821  20.082  -8.953  1.00 66.90           C  
ANISOU   72  CA  CYS A   9    11225   6017   8177  -1976   1702   1156       C  
ATOM     73  C   CYS A   9      49.938  19.882  -7.930  1.00 66.26           C  
ANISOU   73  C   CYS A   9    11002   6125   8050  -2262   1766    935       C  
ATOM     74  O   CYS A   9      49.940  18.889  -7.208  1.00 64.48           O  
ANISOU   74  O   CYS A   9    10469   6160   7871  -2128   1741    831       O  
ATOM     75  CB  CYS A   9      47.512  20.466  -8.240  1.00 68.24           C  
ANISOU   75  CB  CYS A   9    11503   5942   8486  -1568   1689   1165       C  
ATOM     76  SG  CYS A   9      47.336  22.233  -7.794  1.00 72.87           S  
ANISOU   76  SG  CYS A   9    12713   5971   9005  -1557   1761   1167       S  
ATOM     77  N   ALA A  10      50.880  20.823  -7.868  1.00 69.59           N  
ANISOU   77  N   ALA A  10    11663   6409   8369  -2653   1846    850       N  
ATOM     78  CA  ALA A  10      52.000  20.752  -6.921  1.00 71.71           C  
ANISOU   78  CA  ALA A  10    11769   6894   8584  -2937   1862    578       C  
ATOM     79  C   ALA A  10      51.955  21.935  -5.960  1.00 76.93           C  
ANISOU   79  C   ALA A  10    12803   7180   9246  -3024   1904    439       C  
ATOM     80  O   ALA A  10      51.552  23.029  -6.351  1.00 80.47           O  
ANISOU   80  O   ALA A  10    13701   7179   9695  -3074   1970    557       O  
ATOM     81  CB  ALA A  10      53.319  20.733  -7.668  1.00 72.83           C  
ANISOU   81  CB  ALA A  10    11752   7300   8619  -3405   1922    506       C  
ATOM     82  N   VAL A  11      52.385  21.714  -4.715  1.00 79.36           N  
ANISOU   82  N   VAL A  11    12970   7660   9522  -3013   1854    180       N  
ATOM     83  CA  VAL A  11      52.334  22.748  -3.664  1.00 84.30           C  
ANISOU   83  CA  VAL A  11    13945   7957  10126  -3052   1866     -7       C  
ATOM     84  C   VAL A  11      53.665  23.504  -3.474  1.00 87.34           C  
ANISOU   84  C   VAL A  11    14381   8359  10444  -3628   1874   -294       C  
ATOM     85  O   VAL A  11      53.753  24.699  -3.764  1.00 90.60           O  
ANISOU   85  O   VAL A  11    15220   8333  10872  -3934   1969   -291       O  
ATOM     86  CB  VAL A  11      51.891  22.145  -2.308  1.00 83.41           C  
ANISOU   86  CB  VAL A  11    13722   7988   9981  -2645   1809   -138       C  
ATOM     87  CG1 VAL A  11      51.789  23.241  -1.249  1.00 89.05           C  
ANISOU   87  CG1 VAL A  11    14838   8356  10642  -2641   1814   -346       C  
ATOM     88  CG2 VAL A  11      50.567  21.430  -2.459  1.00 79.04           C  
ANISOU   88  CG2 VAL A  11    13084   7416   9531  -2162   1853    112       C  
ATOM     89  N   SER A  12      54.686  22.806  -2.981  1.00 86.57           N  
ANISOU   89  N   SER A  12    13857   8762  10271  -3765   1773   -558       N  
ATOM     90  CA  SER A  12      55.992  23.409  -2.729  1.00 91.11           C  
ANISOU   90  CA  SER A  12    14341   9473  10803  -4318   1753   -911       C  
ATOM     91  C   SER A  12      56.728  23.744  -4.022  1.00 92.31           C  
ANISOU   91  C   SER A  12    14425   9656  10994  -4860   1913   -827       C  
ATOM     92  O   SER A  12      56.333  23.318  -5.109  1.00 89.82           O  
ANISOU   92  O   SER A  12    14085   9350  10692  -4747   1999   -507       O  
ATOM     93  CB  SER A  12      56.862  22.463  -1.885  1.00 92.29           C  
ANISOU   93  CB  SER A  12    13993  10240  10834  -4214   1560  -1234       C  
ATOM     94  OG  SER A  12      56.295  22.221  -0.609  1.00 93.31           O  
ANISOU   94  OG  SER A  12    14251  10331  10871  -3744   1441  -1328       O  
ATOM     95  N   GLU A  13      57.795  24.527  -3.892  1.00 95.84           N  
ANISOU   95  N   GLU A  13    14850  10117  11448  -5466   1965  -1136       N  
ATOM     96  CA  GLU A  13      58.792  24.637  -4.945  1.00 97.08           C  
ANISOU   96  CA  GLU A  13    14774  10495  11619  -6043   2145  -1152       C  
ATOM     97  C   GLU A  13      59.316  23.233  -5.153  1.00 91.89           C  
ANISOU   97  C   GLU A  13    13456  10566  10893  -5807   2028  -1203       C  
ATOM     98  O   GLU A  13      59.389  22.732  -6.271  1.00 89.61           O  
ANISOU   98  O   GLU A  13    13017  10450  10580  -5822   2149   -969       O  
ATOM     99  CB  GLU A  13      59.962  25.516  -4.512  1.00105.42           C  
ANISOU   99  CB  GLU A  13    15746  11593  12718  -6749   2194  -1594       C  
ATOM    100  CG  GLU A  13      59.620  26.949  -4.141  1.00110.96           C  
ANISOU  100  CG  GLU A  13    17132  11548  13481  -7046   2293  -1644       C  
ATOM    101  CD  GLU A  13      60.803  27.674  -3.522  1.00118.08           C  
ANISOU  101  CD  GLU A  13    17865  12557  14441  -7744   2284  -2181       C  
ATOM    102  OE1 GLU A  13      61.918  27.107  -3.519  1.00119.75           O  
ANISOU  102  OE1 GLU A  13    17384  13462  14654  -8026   2224  -2501       O  
ATOM    103  OE2 GLU A  13      60.619  28.811  -3.037  1.00123.04           O  
ANISOU  103  OE2 GLU A  13    19045  12588  15117  -8001   2326  -2315       O  
ATOM    104  N   HIS A  14      59.655  22.607  -4.031  1.00 90.44           N  
ANISOU  104  N   HIS A  14    12936  10785  10644  -5535   1780  -1516       N  
ATOM    105  CA  HIS A  14      60.195  21.258  -3.988  1.00 87.56           C  
ANISOU  105  CA  HIS A  14    11999  11095  10176  -5222   1623  -1620       C  
ATOM    106  C   HIS A  14      59.303  20.249  -4.702  1.00 83.04           C  
ANISOU  106  C   HIS A  14    11459  10502   9591  -4727   1649  -1207       C  
ATOM    107  O   HIS A  14      59.805  19.389  -5.425  1.00 83.42           O  
ANISOU  107  O   HIS A  14    11133  10978   9584  -4684   1658  -1177       O  
ATOM    108  CB  HIS A  14      60.359  20.809  -2.540  1.00 86.89           C  
ANISOU  108  CB  HIS A  14    11770  11275   9971  -4840   1339  -1939       C  
ATOM    109  CG  HIS A  14      61.094  21.785  -1.674  1.00 92.12           C  
ANISOU  109  CG  HIS A  14    12432  11937  10631  -5247   1244  -2396       C  
ATOM    110  ND1 HIS A  14      60.472  22.855  -1.068  1.00 93.57           N  
ANISOU  110  ND1 HIS A  14    13153  11532  10866  -5336   1275  -2412       N  
ATOM    111  CD2 HIS A  14      62.391  21.836  -1.288  1.00 96.88           C  
ANISOU  111  CD2 HIS A  14    12546  13078  11185  -5570   1096  -2896       C  
ATOM    112  CE1 HIS A  14      61.356  23.531  -0.357  1.00 99.01           C  
ANISOU  112  CE1 HIS A  14    13722  12357  11542  -5731   1151  -2900       C  
ATOM    113  NE2 HIS A  14      62.528  22.932  -0.472  1.00100.80           N  
ANISOU  113  NE2 HIS A  14    13297  13286  11715  -5891   1034  -3212       N  
ATOM    114  N   GLU A  15      57.988  20.354  -4.491  1.00 79.93           N  
ANISOU  114  N   GLU A  15    11488   9631   9250  -4355   1659   -924       N  
ATOM    115  CA  GLU A  15      57.008  19.420  -5.085  1.00 73.95           C  
ANISOU  115  CA  GLU A  15    10753   8830   8517  -3900   1667   -574       C  
ATOM    116  C   GLU A  15      56.933  19.572  -6.601  1.00 72.02           C  
ANISOU  116  C   GLU A  15    10567   8494   8304  -4117   1826   -308       C  
ATOM    117  O   GLU A  15      56.843  18.586  -7.325  1.00 67.55           O  
ANISOU  117  O   GLU A  15     9783   8177   7705  -3907   1805   -169       O  
ATOM    118  CB  GLU A  15      55.601  19.617  -4.495  1.00 72.50           C  
ANISOU  118  CB  GLU A  15    10952   8187   8407  -3498   1664   -381       C  
ATOM    119  CG  GLU A  15      55.306  18.789  -3.237  1.00 72.57           C  
ANISOU  119  CG  GLU A  15    10875   8355   8345  -3043   1541   -489       C  
ATOM    120  CD  GLU A  15      53.808  18.610  -2.960  1.00 71.80           C  
ANISOU  120  CD  GLU A  15    11026   7912   8341  -2616   1605   -235       C  
ATOM    121  OE1 GLU A  15      52.988  19.361  -3.532  1.00 73.32           O  
ANISOU  121  OE1 GLU A  15    11486   7719   8654  -2641   1697    -39       O  
ATOM    122  OE2 GLU A  15      53.450  17.711  -2.166  1.00 70.31           O  
ANISOU  122  OE2 GLU A  15    10769   7849   8097  -2242   1577   -239       O  
ATOM    123  N   ALA A  16      56.953  20.817  -7.064  1.00 76.06           N  
ANISOU  123  N   ALA A  16    11435   8614   8852  -4517   1988   -237       N  
ATOM    124  CA  ALA A  16      57.009  21.119  -8.488  1.00 76.60           C  
ANISOU  124  CA  ALA A  16    11648   8571   8886  -4761   2172     11       C  
ATOM    125  C   ALA A  16      58.290  20.570  -9.118  1.00 78.09           C  
ANISOU  125  C   ALA A  16    11358   9329   8985  -5083   2251   -144       C  
ATOM    126  O   ALA A  16      58.298  20.198 -10.292  1.00 77.20           O  
ANISOU  126  O   ALA A  16    11211   9327   8794  -5075   2352     62       O  
ATOM    127  CB  ALA A  16      56.907  22.627  -8.710  1.00 80.70           C  
ANISOU  127  CB  ALA A  16    12727   8510   9425  -5153   2357     93       C  
ATOM    128  N   THR A  17      59.370  20.524  -8.338  1.00 80.58           N  
ANISOU  128  N   THR A  17    11288  10035   9294  -5334   2194   -534       N  
ATOM    129  CA  THR A  17      60.623  19.944  -8.809  1.00 82.74           C  
ANISOU  129  CA  THR A  17    11005  10948   9487  -5577   2248   -750       C  
ATOM    130  C   THR A  17      60.426  18.468  -9.125  1.00 78.28           C  
ANISOU  130  C   THR A  17    10137  10770   8834  -5027   2098   -656       C  
ATOM    131  O   THR A  17      60.776  18.022 -10.217  1.00 78.67           O  
ANISOU  131  O   THR A  17    10018  11076   8798  -5080   2219   -554       O  
ATOM    132  CB  THR A  17      61.766  20.097  -7.777  1.00 86.64           C  
ANISOU  132  CB  THR A  17    11071  11860   9988  -5851   2137  -1253       C  
ATOM    133  OG1 THR A  17      62.019  21.487  -7.535  1.00 90.99           O  
ANISOU  133  OG1 THR A  17    11906  12029  10635  -6448   2291  -1384       O  
ATOM    134  CG2 THR A  17      63.047  19.421  -8.271  1.00 87.49           C  
ANISOU  134  CG2 THR A  17    10516  12717  10009  -6023   2176  -1510       C  
ATOM    135  N   LYS A  18      59.854  17.718  -8.184  1.00 74.70           N  
ANISOU  135  N   LYS A  18     9666  10328   8387  -4503   1859   -688       N  
ATOM    136  CA  LYS A  18      59.669  16.277  -8.388  1.00 72.57           C  
ANISOU  136  CA  LYS A  18     9172  10362   8039  -3994   1724   -618       C  
ATOM    137  C   LYS A  18      58.613  15.972  -9.445  1.00 69.17           C  
ANISOU  137  C   LYS A  18     9011   9628   7644  -3790   1788   -236       C  
ATOM    138  O   LYS A  18      58.717  14.969 -10.146  1.00 67.08           O  
ANISOU  138  O   LYS A  18     8555   9632   7298  -3569   1755   -183       O  
ATOM    139  CB  LYS A  18      59.303  15.543  -7.093  1.00 70.14           C  
ANISOU  139  CB  LYS A  18     8856  10086   7708  -3506   1502   -723       C  
ATOM    140  CG  LYS A  18      59.701  14.057  -7.136  1.00 68.47           C  
ANISOU  140  CG  LYS A  18     8334  10322   7360  -3076   1362   -799       C  
ATOM    141  CD  LYS A  18      58.639  13.109  -6.580  1.00 65.38           C  
ANISOU  141  CD  LYS A  18     8174   9685   6981  -2543   1268   -618       C  
ATOM    142  CE  LYS A  18      58.643  13.053  -5.054  1.00 66.08           C  
ANISOU  142  CE  LYS A  18     8353   9765   6990  -2289   1137   -790       C  
ATOM    143  NZ  LYS A  18      58.001  11.817  -4.506  1.00 61.78           N  
ANISOU  143  NZ  LYS A  18     7962   9134   6378  -1755   1075   -668       N  
ATOM    144  N   CYS A  19      57.607  16.835  -9.549  1.00 69.15           N  
ANISOU  144  N   CYS A  19     9449   9080   7744  -3833   1856     -4       N  
ATOM    145  CA  CYS A  19      56.516  16.655 -10.503  1.00 68.72           C  
ANISOU  145  CA  CYS A  19     9646   8743   7720  -3605   1869    322       C  
ATOM    146  C   CYS A  19      57.040  16.623 -11.950  1.00 70.04           C  
ANISOU  146  C   CYS A  19     9769   9092   7751  -3816   2006    430       C  
ATOM    147  O   CYS A  19      56.634  15.763 -12.736  1.00 67.93           O  
ANISOU  147  O   CYS A  19     9447   8931   7433  -3535   1937    556       O  
ATOM    148  CB  CYS A  19      55.449  17.746 -10.294  1.00 72.07           C  
ANISOU  148  CB  CYS A  19    10544   8586   8255  -3590   1904    503       C  
ATOM    149  SG  CYS A  19      54.032  17.756 -11.441  1.00 73.08           S  
ANISOU  149  SG  CYS A  19    10986   8371   8411  -3272   1870    859       S  
ATOM    150  N   GLN A  20      57.946  17.535 -12.298  1.00 73.08           N  
ANISOU  150  N   GLN A  20    10185   9515   8066  -4324   2217    365       N  
ATOM    151  CA  GLN A  20      58.563  17.510 -13.636  1.00 76.33           C  
ANISOU  151  CA  GLN A  20    10551  10143   8308  -4556   2414    459       C  
ATOM    152  C   GLN A  20      59.622  16.406 -13.770  1.00 75.65           C  
ANISOU  152  C   GLN A  20     9894  10732   8119  -4500   2386    214       C  
ATOM    153  O   GLN A  20      59.742  15.790 -14.832  1.00 77.39           O  
ANISOU  153  O   GLN A  20    10041  11174   8190  -4379   2438    310       O  
ATOM    154  CB  GLN A  20      59.139  18.880 -14.037  1.00 82.52           C  
ANISOU  154  CB  GLN A  20    11615  10694   9046  -5167   2726    503       C  
ATOM    155  CG  GLN A  20      58.314  19.620 -15.117  1.00 85.23           C  
ANISOU  155  CG  GLN A  20    12582  10522   9279  -5150   2859    893       C  
ATOM    156  CD  GLN A  20      58.557  19.113 -16.556  1.00 86.30           C  
ANISOU  156  CD  GLN A  20    12701  10915   9173  -5102   2990   1061       C  
ATOM    157  OE1 GLN A  20      59.398  18.240 -16.799  1.00 84.56           O  
ANISOU  157  OE1 GLN A  20    11990  11263   8875  -5118   3017    880       O  
ATOM    158  NE2 GLN A  20      57.811  19.673 -17.511  1.00 85.85           N  
ANISOU  158  NE2 GLN A  20    13210  10443   8965  -4991   3059   1398       N  
ATOM    159  N   SER A  21      60.383  16.148 -12.710  1.00 73.61           N  
ANISOU  159  N   SER A  21     9249  10811   7910  -4535   2286   -118       N  
ATOM    160  CA  SER A  21      61.312  15.015 -12.716  1.00 75.19           C  
ANISOU  160  CA  SER A  21     8915  11658   7996  -4338   2200   -372       C  
ATOM    161  C   SER A  21      60.547  13.711 -12.928  1.00 71.42           C  
ANISOU  161  C   SER A  21     8481  11175   7482  -3733   1995   -239       C  
ATOM    162  O   SER A  21      61.034  12.785 -13.579  1.00 72.08           O  
ANISOU  162  O   SER A  21     8314  11652   7423  -3535   1982   -305       O  
ATOM    163  CB  SER A  21      62.096  14.940 -11.408  1.00 78.13           C  
ANISOU  163  CB  SER A  21     8921  12360   8404  -4348   2048   -757       C  
ATOM    164  OG  SER A  21      62.928  13.790 -11.386  1.00 79.36           O  
ANISOU  164  OG  SER A  21     8596  13137   8422  -4036   1922  -1003       O  
ATOM    165  N   PHE A  22      59.350  13.661 -12.353  1.00 67.79           N  
ANISOU  165  N   PHE A  22     8339  10260   7157  -3458   1851    -73       N  
ATOM    166  CA  PHE A  22      58.424  12.551 -12.520  1.00 65.36           C  
ANISOU  166  CA  PHE A  22     8129   9832   6874  -2974   1688     65       C  
ATOM    167  C   PHE A  22      57.943  12.466 -13.970  1.00 64.65           C  
ANISOU  167  C   PHE A  22     8212   9641   6711  -2958   1753    293       C  
ATOM    168  O   PHE A  22      57.883  11.382 -14.547  1.00 61.32           O  
ANISOU  168  O   PHE A  22     7694   9398   6206  -2667   1662    284       O  
ATOM    169  CB  PHE A  22      57.258  12.741 -11.530  1.00 65.08           C  
ANISOU  169  CB  PHE A  22     8364   9341   7023  -2787   1590    172       C  
ATOM    170  CG  PHE A  22      56.134  11.742 -11.660  1.00 63.02           C  
ANISOU  170  CG  PHE A  22     8214   8882   6847  -2387   1469    315       C  
ATOM    171  CD1 PHE A  22      56.385  10.386 -11.840  1.00 63.12           C  
ANISOU  171  CD1 PHE A  22     8060   9147   6777  -2090   1371    230       C  
ATOM    172  CD2 PHE A  22      54.812  12.166 -11.543  1.00 62.09           C  
ANISOU  172  CD2 PHE A  22     8365   8320   6905  -2308   1457    506       C  
ATOM    173  CE1 PHE A  22      55.333   9.475 -11.938  1.00 61.96           C  
ANISOU  173  CE1 PHE A  22     8034   8771   6739  -1798   1282    336       C  
ATOM    174  CE2 PHE A  22      53.759  11.264 -11.637  1.00 61.10           C  
ANISOU  174  CE2 PHE A  22     8278   8038   6898  -2007   1364    594       C  
ATOM    175  CZ  PHE A  22      54.018   9.915 -11.832  1.00 59.86           C  
ANISOU  175  CZ  PHE A  22     7972   8094   6676  -1787   1285    508       C  
ATOM    176  N   ARG A  23      57.618  13.612 -14.562  1.00 67.83           N  
ANISOU  176  N   ARG A  23     8915   9742   7114  -3246   1900    485       N  
ATOM    177  CA  ARG A  23      57.224  13.653 -15.964  1.00 71.37           C  
ANISOU  177  CA  ARG A  23     9583  10108   7427  -3211   1956    701       C  
ATOM    178  C   ARG A  23      58.347  13.131 -16.861  1.00 73.10           C  
ANISOU  178  C   ARG A  23     9535  10828   7411  -3302   2089    592       C  
ATOM    179  O   ARG A  23      58.140  12.196 -17.637  1.00 71.30           O  
ANISOU  179  O   ARG A  23     9275  10748   7069  -3001   1990    613       O  
ATOM    180  CB  ARG A  23      56.846  15.076 -16.379  1.00 77.08           C  
ANISOU  180  CB  ARG A  23    10745  10411   8131  -3496   2119    927       C  
ATOM    181  CG  ARG A  23      56.630  15.241 -17.876  1.00 82.43           C  
ANISOU  181  CG  ARG A  23    11706  11036   8578  -3469   2207   1152       C  
ATOM    182  CD  ARG A  23      56.446  16.690 -18.245  1.00 88.91           C  
ANISOU  182  CD  ARG A  23    13032  11425   9323  -3759   2409   1379       C  
ATOM    183  NE  ARG A  23      56.201  16.844 -19.676  1.00 94.72           N  
ANISOU  183  NE  ARG A  23    14117  12095   9777  -3664   2483   1618       N  
ATOM    184  CZ  ARG A  23      57.151  16.965 -20.607  1.00101.23           C  
ANISOU  184  CZ  ARG A  23    14963  13168  10329  -3945   2773   1658       C  
ATOM    185  NH1 ARG A  23      58.443  16.955 -20.279  1.00102.55           N  
ANISOU  185  NH1 ARG A  23    14750  13710  10505  -4371   3021   1446       N  
ATOM    186  NH2 ARG A  23      56.804  17.100 -21.883  1.00105.27           N  
ANISOU  186  NH2 ARG A  23    15871  13585  10542  -3783   2820   1895       N  
ATOM    187  N   ASP A  24      59.526  13.742 -16.750  1.00 75.61           N  
ANISOU  187  N   ASP A  24     9649  11418   7662  -3726   2320    447       N  
ATOM    188  CA  ASP A  24      60.689  13.343 -17.546  1.00 80.57           C  
ANISOU  188  CA  ASP A  24     9952  12591   8071  -3853   2504    308       C  
ATOM    189  C   ASP A  24      60.893  11.828 -17.507  1.00 79.35           C  
ANISOU  189  C   ASP A  24     9473  12827   7851  -3362   2286    123       C  
ATOM    190  O   ASP A  24      61.062  11.192 -18.547  1.00 82.88           O  
ANISOU  190  O   ASP A  24     9894  13502   8095  -3185   2324    146       O  
ATOM    191  CB  ASP A  24      61.971  14.053 -17.062  1.00 85.32           C  
ANISOU  191  CB  ASP A  24    10209  13519   8689  -4372   2738     60       C  
ATOM    192  CG  ASP A  24      62.009  15.547 -17.422  1.00 88.21           C  
ANISOU  192  CG  ASP A  24    10941  13518   9059  -4959   3059    240       C  
ATOM    193  OD1 ASP A  24      62.996  16.220 -17.051  1.00 89.59           O  
ANISOU  193  OD1 ASP A  24    10860  13899   9281  -5476   3275     25       O  
ATOM    194  OD2 ASP A  24      61.064  16.051 -18.066  1.00 87.56           O  
ANISOU  194  OD2 ASP A  24    11411  12934   8925  -4900   3091    577       O  
ATOM    195  N   HIS A  25      60.857  11.253 -16.309  1.00 76.80           N  
ANISOU  195  N   HIS A  25     8966  12544   7668  -3115   2062    -55       N  
ATOM    196  CA  HIS A  25      61.109   9.822 -16.136  1.00 76.02           C  
ANISOU  196  CA  HIS A  25     8632  12759   7492  -2630   1863   -237       C  
ATOM    197  C   HIS A  25      60.017   8.933 -16.734  1.00 75.01           C  
ANISOU  197  C   HIS A  25     8797  12336   7367  -2239   1694    -65       C  
ATOM    198  O   HIS A  25      60.319   7.866 -17.272  1.00 76.84           O  
ANISOU  198  O   HIS A  25     8922  12828   7445  -1923   1622   -171       O  
ATOM    199  CB  HIS A  25      61.321   9.481 -14.661  1.00 74.35           C  
ANISOU  199  CB  HIS A  25     8250  12613   7385  -2441   1680   -443       C  
ATOM    200  CG  HIS A  25      62.710   9.756 -14.179  1.00 76.92           C  
ANISOU  200  CG  HIS A  25     8105  13490   7629  -2635   1746   -771       C  
ATOM    201  ND1 HIS A  25      63.037  10.876 -13.448  1.00 76.87           N  
ANISOU  201  ND1 HIS A  25     8022  13447   7738  -3061   1824   -869       N  
ATOM    202  CD2 HIS A  25      63.860   9.060 -14.337  1.00 79.31           C  
ANISOU  202  CD2 HIS A  25     7961  14423   7750  -2455   1733  -1061       C  
ATOM    203  CE1 HIS A  25      64.328  10.854 -13.168  1.00 81.22           C  
ANISOU  203  CE1 HIS A  25     8060  14603   8198  -3169   1845  -1225       C  
ATOM    204  NE2 HIS A  25      64.850   9.763 -13.698  1.00 80.98           N  
ANISOU  204  NE2 HIS A  25     7778  15007   7984  -2785   1792  -1345       N  
ATOM    205  N   MET A  26      58.759   9.360 -16.644  1.00 72.03           N  
ANISOU  205  N   MET A  26     8769  11435   7164  -2250   1623    165       N  
ATOM    206  CA  MET A  26      57.670   8.641 -17.312  1.00 69.43           C  
ANISOU  206  CA  MET A  26     8672  10846   6863  -1954   1462    293       C  
ATOM    207  C   MET A  26      57.894   8.593 -18.825  1.00 71.34           C  
ANISOU  207  C   MET A  26     8986  11267   6852  -1961   1542    355       C  
ATOM    208  O   MET A  26      57.683   7.556 -19.455  1.00 70.87           O  
ANISOU  208  O   MET A  26     8946  11281   6699  -1655   1405    294       O  
ATOM    209  CB  MET A  26      56.318   9.288 -17.012  1.00 67.90           C  
ANISOU  209  CB  MET A  26     8768  10133   6897  -1989   1389    498       C  
ATOM    210  CG  MET A  26      55.768   8.994 -15.615  1.00 67.02           C  
ANISOU  210  CG  MET A  26     8642   9798   7025  -1858   1289    452       C  
ATOM    211  SD  MET A  26      55.133   7.317 -15.371  1.00 63.17           S  
ANISOU  211  SD  MET A  26     8149   9225   6629  -1448   1100    365       S  
ATOM    212  CE  MET A  26      56.475   6.555 -14.473  1.00 64.76           C  
ANISOU  212  CE  MET A  26     8126   9804   6675  -1283   1107    127       C  
ATOM    213  N   LYS A  27      58.348   9.707 -19.394  1.00 72.75           N  
ANISOU  213  N   LYS A  27     9242  11500   6901  -2317   1782    468       N  
ATOM    214  CA  LYS A  27      58.601   9.794 -20.833  1.00 77.33           C  
ANISOU  214  CA  LYS A  27     9955  12243   7182  -2343   1919    561       C  
ATOM    215  C   LYS A  27      59.700   8.826 -21.295  1.00 76.89           C  
ANISOU  215  C   LYS A  27     9573  12745   6897  -2184   1985    329       C  
ATOM    216  O   LYS A  27      59.741   8.440 -22.461  1.00 75.82           O  
ANISOU  216  O   LYS A  27     9549  12756   6502  -2029   2014    357       O  
ATOM    217  CB  LYS A  27      58.978  11.226 -21.222  1.00 83.50           C  
ANISOU  217  CB  LYS A  27    10930  12938   7858  -2808   2239    740       C  
ATOM    218  CG  LYS A  27      57.894  12.269 -20.941  1.00 84.85           C  
ANISOU  218  CG  LYS A  27    11513  12534   8192  -2903   2183    984       C  
ATOM    219  CD  LYS A  27      56.870  12.366 -22.067  1.00 86.79           C  
ANISOU  219  CD  LYS A  27    12187  12513   8277  -2650   2058   1213       C  
ATOM    220  CE  LYS A  27      55.900  13.524 -21.829  1.00 87.14           C  
ANISOU  220  CE  LYS A  27    12646  12023   8441  -2708   2023   1445       C  
ATOM    221  NZ  LYS A  27      54.952  13.725 -22.964  1.00 88.12           N  
ANISOU  221  NZ  LYS A  27    13195  11927   8357  -2416   1879   1653       N  
ATOM    222  N   SER A  28      60.578   8.441 -20.373  1.00 76.24           N  
ANISOU  222  N   SER A  28     9097  12986   6884  -2176   1991     83       N  
ATOM    223  CA  SER A  28      61.677   7.523 -20.662  1.00 77.19           C  
ANISOU  223  CA  SER A  28     8857  13679   6792  -1957   2034   -181       C  
ATOM    224  C   SER A  28      61.236   6.071 -20.889  1.00 74.64           C  
ANISOU  224  C   SER A  28     8626  13320   6416  -1406   1755   -279       C  
ATOM    225  O   SER A  28      61.863   5.356 -21.675  1.00 78.31           O  
ANISOU  225  O   SER A  28     8974  14159   6621  -1171   1798   -423       O  
ATOM    226  CB  SER A  28      62.694   7.555 -19.517  1.00 78.65           C  
ANISOU  226  CB  SER A  28     8592  14229   7063  -2041   2059   -447       C  
ATOM    227  OG  SER A  28      62.915   8.878 -19.062  1.00 80.80           O  
ANISOU  227  OG  SER A  28     8824  14413   7465  -2574   2255   -387       O  
ATOM    228  N   VAL A  29      60.186   5.631 -20.194  1.00 68.85           N  
ANISOU  228  N   VAL A  29     8105  12133   5922  -1214   1499   -217       N  
ATOM    229  CA  VAL A  29      59.760   4.225 -20.251  1.00 66.42           C  
ANISOU  229  CA  VAL A  29     7914  11715   5608   -753   1255   -331       C  
ATOM    230  C   VAL A  29      58.278   3.995 -20.571  1.00 63.77           C  
ANISOU  230  C   VAL A  29     7933  10854   5444   -684   1059   -177       C  
ATOM    231  O   VAL A  29      57.839   2.840 -20.609  1.00 62.43           O  
ANISOU  231  O   VAL A  29     7887  10526   5308   -375    869   -283       O  
ATOM    232  CB  VAL A  29      60.087   3.480 -18.923  1.00 66.77           C  
ANISOU  232  CB  VAL A  29     7829  11781   5761   -499   1132   -501       C  
ATOM    233  CG1 VAL A  29      61.575   3.557 -18.614  1.00 69.17           C  
ANISOU  233  CG1 VAL A  29     7712  12690   5880   -474   1253   -733       C  
ATOM    234  CG2 VAL A  29      59.260   4.033 -17.760  1.00 63.06           C  
ANISOU  234  CG2 VAL A  29     7482  10882   5596   -674   1083   -357       C  
ATOM    235  N   ILE A  30      57.508   5.065 -20.793  1.00 61.68           N  
ANISOU  235  N   ILE A  30     7832  10318   5288   -959   1098     47       N  
ATOM    236  CA  ILE A  30      56.091   4.927 -21.167  1.00 58.53           C  
ANISOU  236  CA  ILE A  30     7692   9501   5046   -877    891    152       C  
ATOM    237  C   ILE A  30      55.859   5.377 -22.597  1.00 59.58           C  
ANISOU  237  C   ILE A  30     8020   9688   4931   -888    892    257       C  
ATOM    238  O   ILE A  30      56.297   6.462 -22.980  1.00 60.35           O  
ANISOU  238  O   ILE A  30     8173   9889   4868  -1128   1107    410       O  
ATOM    239  CB  ILE A  30      55.159   5.745 -20.257  1.00 55.59           C  
ANISOU  239  CB  ILE A  30     7387   8742   4991  -1062    873    312       C  
ATOM    240  CG1 ILE A  30      55.034   5.064 -18.903  1.00 54.42           C  
ANISOU  240  CG1 ILE A  30     7146   8451   5082   -967    824    216       C  
ATOM    241  CG2 ILE A  30      53.772   5.911 -20.892  1.00 52.25           C  
ANISOU  241  CG2 ILE A  30     7168   8003   4683  -1002    682    415       C  
ATOM    242  CD1 ILE A  30      54.044   5.737 -17.998  1.00 55.83           C  
ANISOU  242  CD1 ILE A  30     7390   8261   5561  -1101    820    351       C  
ATOM    243  N   PRO A  31      55.137   4.562 -23.381  1.00 61.13           N  
ANISOU  243  N   PRO A  31     8360   9783   5083   -636    654    171       N  
ATOM    244  CA  PRO A  31      54.883   4.873 -24.781  1.00 64.53           C  
ANISOU  244  CA  PRO A  31     9016  10283   5217   -558    603    242       C  
ATOM    245  C   PRO A  31      53.978   6.095 -24.983  1.00 63.66           C  
ANISOU  245  C   PRO A  31     9121   9902   5166   -690    569    486       C  
ATOM    246  O   PRO A  31      53.329   6.561 -24.048  1.00 62.32           O  
ANISOU  246  O   PRO A  31     8906   9452   5322   -810    535    566       O  
ATOM    247  CB  PRO A  31      54.182   3.611 -25.281  1.00 64.61           C  
ANISOU  247  CB  PRO A  31     9098  10194   5257   -258    286     25       C  
ATOM    248  CG  PRO A  31      53.460   3.111 -24.100  1.00 61.44           C  
ANISOU  248  CG  PRO A  31     8584   9470   5291   -293    165    -40       C  
ATOM    249  CD  PRO A  31      54.403   3.353 -22.962  1.00 60.64           C  
ANISOU  249  CD  PRO A  31     8298   9484   5261   -433    413      1       C  
ATOM    250  N   SER A  32      53.942   6.590 -26.211  1.00 65.36           N  
ANISOU  250  N   SER A  32     9603  10201   5029   -618    581    599       N  
ATOM    251  CA  SER A  32      53.176   7.786 -26.551  1.00 65.88           C  
ANISOU  251  CA  SER A  32     9965  10017   5050   -658    549    845       C  
ATOM    252  C   SER A  32      51.654   7.583 -26.530  1.00 67.27           C  
ANISOU  252  C   SER A  32    10170   9912   5480   -433    146    782       C  
ATOM    253  O   SER A  32      50.910   8.561 -26.447  1.00 66.89           O  
ANISOU  253  O   SER A  32    10292   9624   5500   -430     89    958       O  
ATOM    254  CB  SER A  32      53.607   8.283 -27.927  1.00 67.05           C  
ANISOU  254  CB  SER A  32    10462  10340   4676   -587    684    989       C  
ATOM    255  OG  SER A  32      53.733   7.193 -28.822  1.00 64.86           O  
ANISOU  255  OG  SER A  32    10180  10311   4152   -299    520    777       O  
ATOM    256  N   ASP A  33      51.194   6.331 -26.613  1.00 68.16           N  
ANISOU  256  N   ASP A  33    10114  10051   5731   -247   -126    512       N  
ATOM    257  CA  ASP A  33      49.761   6.021 -26.477  1.00 69.19           C  
ANISOU  257  CA  ASP A  33    10156   9955   6180   -109   -487    383       C  
ATOM    258  C   ASP A  33      49.348   5.768 -25.015  1.00 66.03           C  
ANISOU  258  C   ASP A  33     9471   9331   6285   -290   -436    334       C  
ATOM    259  O   ASP A  33      48.306   5.161 -24.753  1.00 65.75           O  
ANISOU  259  O   ASP A  33     9269   9144   6571   -240   -667    159       O  
ATOM    260  CB  ASP A  33      49.363   4.828 -27.362  1.00 73.27           C  
ANISOU  260  CB  ASP A  33    10664  10571   6605    130   -809     85       C  
ATOM    261  CG  ASP A  33      50.031   3.526 -26.941  1.00 74.46           C  
ANISOU  261  CG  ASP A  33    10659  10781   6851     92   -737   -135       C  
ATOM    262  OD1 ASP A  33      51.261   3.529 -26.734  1.00 74.93           O  
ANISOU  262  OD1 ASP A  33    10716  11029   6726     20   -441    -64       O  
ATOM    263  OD2 ASP A  33      49.328   2.498 -26.835  1.00 75.22           O  
ANISOU  263  OD2 ASP A  33    10644  10735   7199    141   -975   -395       O  
ATOM    264  N   GLY A  34      50.163   6.241 -24.074  1.00 63.31           N  
ANISOU  264  N   GLY A  34     9072   8981   6000   -510   -124    474       N  
ATOM    265  CA  GLY A  34      49.877   6.123 -22.648  1.00 60.22           C  
ANISOU  265  CA  GLY A  34     8480   8392   6011   -655    -38    460       C  
ATOM    266  C   GLY A  34      49.818   7.491 -21.991  1.00 61.59           C  
ANISOU  266  C   GLY A  34     8725   8419   6258   -812    133    689       C  
ATOM    267  O   GLY A  34      49.922   8.516 -22.665  1.00 63.23           O  
ANISOU  267  O   GLY A  34     9169   8631   6225   -814    179    865       O  
ATOM    268  N   PRO A  35      49.654   7.518 -20.660  1.00 61.82           N  
ANISOU  268  N   PRO A  35     8608   8287   6593   -933    243    690       N  
ATOM    269  CA  PRO A  35      49.543   8.761 -19.909  1.00 62.07           C  
ANISOU  269  CA  PRO A  35     8719   8145   6718  -1068    393    864       C  
ATOM    270  C   PRO A  35      50.888   9.429 -19.614  1.00 61.87           C  
ANISOU  270  C   PRO A  35     8764   8250   6495  -1302    666    953       C  
ATOM    271  O   PRO A  35      51.837   8.761 -19.208  1.00 60.84           O  
ANISOU  271  O   PRO A  35     8474   8325   6317  -1366    768    836       O  
ATOM    272  CB  PRO A  35      48.897   8.305 -18.605  1.00 60.21           C  
ANISOU  272  CB  PRO A  35     8291   7730   6855  -1082    411    784       C  
ATOM    273  CG  PRO A  35      49.413   6.933 -18.413  1.00 58.47           C  
ANISOU  273  CG  PRO A  35     7944   7630   6642  -1057    412    615       C  
ATOM    274  CD  PRO A  35      49.537   6.340 -19.782  1.00 60.08           C  
ANISOU  274  CD  PRO A  35     8198   8007   6623   -927    241    523       C  
ATOM    275  N   SER A  36      50.953  10.740 -19.829  1.00 62.89           N  
ANISOU  275  N   SER A  36     9135   8254   6507  -1422    778   1139       N  
ATOM    276  CA  SER A  36      52.088  11.551 -19.410  1.00 63.90           C  
ANISOU  276  CA  SER A  36     9318   8440   6520  -1734   1056   1201       C  
ATOM    277  C   SER A  36      51.649  12.375 -18.201  1.00 63.10           C  
ANISOU  277  C   SER A  36     9267   8044   6664  -1829   1114   1250       C  
ATOM    278  O   SER A  36      50.528  12.217 -17.724  1.00 62.44           O  
ANISOU  278  O   SER A  36     9142   7763   6819  -1634    965   1238       O  
ATOM    279  CB  SER A  36      52.541  12.453 -20.556  1.00 68.12           C  
ANISOU  279  CB  SER A  36    10174   8988   6720  -1856   1198   1379       C  
ATOM    280  OG  SER A  36      51.445  13.156 -21.113  1.00 70.52           O  
ANISOU  280  OG  SER A  36    10808   8996   6992  -1653   1052   1548       O  
ATOM    281  N   VAL A  37      52.530  13.231 -17.695  1.00 64.90           N  
ANISOU  281  N   VAL A  37     9563   8260   6837  -2139   1337   1275       N  
ATOM    282  CA  VAL A  37      52.209  14.081 -16.554  1.00 66.59           C  
ANISOU  282  CA  VAL A  37     9873   8186   7242  -2234   1396   1296       C  
ATOM    283  C   VAL A  37      52.584  15.519 -16.843  1.00 72.07           C  
ANISOU  283  C   VAL A  37    10937   8652   7795  -2514   1587   1447       C  
ATOM    284  O   VAL A  37      53.661  15.777 -17.366  1.00 75.82           O  
ANISOU  284  O   VAL A  37    11434   9306   8069  -2817   1783   1449       O  
ATOM    285  CB  VAL A  37      52.998  13.676 -15.301  1.00 65.71           C  
ANISOU  285  CB  VAL A  37     9482   8253   7231  -2367   1467   1100       C  
ATOM    286  CG1 VAL A  37      52.273  14.164 -14.058  1.00 64.81           C  
ANISOU  286  CG1 VAL A  37     9444   7841   7340  -2303   1451   1094       C  
ATOM    287  CG2 VAL A  37      53.211  12.173 -15.259  1.00 64.69           C  
ANISOU  287  CG2 VAL A  37     9045   8425   7111  -2164   1357    947       C  
ATOM    288  N   ALA A  38      51.701  16.450 -16.490  1.00 73.51           N  
ANISOU  288  N   ALA A  38    11418   8431   8081  -2417   1555   1563       N  
ATOM    289  CA  ALA A  38      52.006  17.878 -16.572  1.00 75.66           C  
ANISOU  289  CA  ALA A  38    12133   8372   8241  -2685   1749   1700       C  
ATOM    290  C   ALA A  38      51.880  18.496 -15.184  1.00 73.10           C  
ANISOU  290  C   ALA A  38    11842   7807   8124  -2775   1788   1601       C  
ATOM    291  O   ALA A  38      51.163  17.978 -14.328  1.00 68.02           O  
ANISOU  291  O   ALA A  38    10982   7171   7690  -2512   1646   1504       O  
ATOM    292  CB  ALA A  38      51.078  18.572 -17.564  1.00 78.39           C  
ANISOU  292  CB  ALA A  38    12952   8397   8437  -2410   1665   1945       C  
ATOM    293  N   CYS A  39      52.579  19.606 -14.967  1.00 76.89           N  
ANISOU  293  N   CYS A  39    12615   8064   8537  -3167   2001   1614       N  
ATOM    294  CA  CYS A  39      52.616  20.243 -13.654  1.00 76.25           C  
ANISOU  294  CA  CYS A  39    12593   7763   8617  -3294   2039   1473       C  
ATOM    295  C   CYS A  39      52.000  21.633 -13.648  1.00 75.12           C  
ANISOU  295  C   CYS A  39    13062   7032   8449  -3268   2101   1632       C  
ATOM    296  O   CYS A  39      52.213  22.436 -14.561  1.00 77.37           O  
ANISOU  296  O   CYS A  39    13798   7055   8542  -3446   2250   1822       O  
ATOM    297  CB  CYS A  39      54.049  20.303 -13.136  1.00 79.84           C  
ANISOU  297  CB  CYS A  39    12804   8479   9052  -3803   2203   1242       C  
ATOM    298  SG  CYS A  39      54.826  18.675 -13.087  1.00 81.61           S  
ANISOU  298  SG  CYS A  39    12345   9399   9266  -3734   2109   1033       S  
ATOM    299  N   VAL A  40      51.215  21.879 -12.603  1.00 71.43           N  
ANISOU  299  N   VAL A  40    12637   6349   8153  -3008   1999   1557       N  
ATOM    300  CA  VAL A  40      50.623  23.173 -12.328  1.00 72.82           C  
ANISOU  300  CA  VAL A  40    13380   5962   8324  -2919   2039   1646       C  
ATOM    301  C   VAL A  40      51.050  23.553 -10.920  1.00 71.98           C  
ANISOU  301  C   VAL A  40    13234   5775   8341  -3138   2096   1396       C  
ATOM    302  O   VAL A  40      51.083  22.702 -10.037  1.00 71.41           O  
ANISOU  302  O   VAL A  40    12710   6033   8390  -3034   2010   1209       O  
ATOM    303  CB  VAL A  40      49.085  23.112 -12.412  1.00 70.60           C  
ANISOU  303  CB  VAL A  40    13172   5531   8120  -2277   1834   1762       C  
ATOM    304  CG1 VAL A  40      48.472  24.458 -12.057  1.00 73.32           C  
ANISOU  304  CG1 VAL A  40    14117   5298   8443  -2101   1865   1829       C  
ATOM    305  CG2 VAL A  40      48.645  22.674 -13.806  1.00 68.90           C  
ANISOU  305  CG2 VAL A  40    12963   5450   7766  -2023   1714   1958       C  
ATOM    306  N   LYS A  41      51.381  24.827 -10.720  1.00 76.33           N  
ANISOU  306  N   LYS A  41    14303   5861   8836  -3433   2243   1386       N  
ATOM    307  CA  LYS A  41      51.873  25.331  -9.433  1.00 75.90           C  
ANISOU  307  CA  LYS A  41    14278   5693   8868  -3691   2286   1107       C  
ATOM    308  C   LYS A  41      50.861  26.310  -8.833  1.00 76.21           C  
ANISOU  308  C   LYS A  41    14838   5178   8942  -3338   2248   1140       C  
ATOM    309  O   LYS A  41      50.442  27.262  -9.501  1.00 76.63           O  
ANISOU  309  O   LYS A  41    15495   4730   8892  -3259   2312   1349       O  
ATOM    310  CB  LYS A  41      53.235  26.020  -9.632  1.00 80.02           C  
ANISOU  310  CB  LYS A  41    14948   6141   9317  -4427   2505    987       C  
ATOM    311  CG  LYS A  41      53.944  26.489  -8.354  1.00 81.75           C  
ANISOU  311  CG  LYS A  41    15119   6325   9618  -4782   2516    617       C  
ATOM    312  CD  LYS A  41      55.271  27.204  -8.660  1.00 86.14           C  
ANISOU  312  CD  LYS A  41    15777   6817  10135  -5586   2753    467       C  
ATOM    313  CE  LYS A  41      55.821  27.942  -7.436  1.00 88.50           C  
ANISOU  313  CE  LYS A  41    16169   6943  10515  -5941   2739     78       C  
ATOM    314  NZ  LYS A  41      57.191  28.494  -7.654  1.00 92.42           N  
ANISOU  314  NZ  LYS A  41    16598   7496  11023  -6795   2961   -156       N  
ATOM    315  N   LYS A  42      50.457  26.059  -7.586  1.00 75.51           N  
ANISOU  315  N   LYS A  42    14548   5179   8965  -3079   2151    941       N  
ATOM    316  CA  LYS A  42      49.643  27.012  -6.825  1.00 80.92           C  
ANISOU  316  CA  LYS A  42    15698   5377   9670  -2767   2139    898       C  
ATOM    317  C   LYS A  42      50.067  27.084  -5.353  1.00 80.22           C  
ANISOU  317  C   LYS A  42    15504   5354   9622  -2888   2127    559       C  
ATOM    318  O   LYS A  42      50.755  26.198  -4.848  1.00 74.58           O  
ANISOU  318  O   LYS A  42    14284   5125   8927  -3057   2084    378       O  
ATOM    319  CB  LYS A  42      48.139  26.722  -6.974  1.00 81.19           C  
ANISOU  319  CB  LYS A  42    15684   5398   9767  -2053   2022   1069       C  
ATOM    320  CG  LYS A  42      47.526  27.270  -8.286  1.00 85.42           C  
ANISOU  320  CG  LYS A  42    16635   5623  10198  -1814   1995   1369       C  
ATOM    321  CD  LYS A  42      46.078  27.747  -8.118  1.00 87.39           C  
ANISOU  321  CD  LYS A  42    17118   5609  10477  -1110   1888   1437       C  
ATOM    322  CE  LYS A  42      45.453  28.185  -9.442  1.00 90.47           C  
ANISOU  322  CE  LYS A  42    17888   5764  10721   -774   1797   1716       C  
ATOM    323  NZ  LYS A  42      44.045  28.647  -9.273  1.00 92.29           N  
ANISOU  323  NZ  LYS A  42    18283   5805  10977    -26   1660   1738       N  
ATOM    324  N   ALA A  43      49.640  28.156  -4.687  1.00 85.60           N  
ANISOU  324  N   ALA A  43    16709   5532  10282  -2750   2150    470       N  
ATOM    325  CA  ALA A  43      50.195  28.580  -3.396  1.00 89.11           C  
ANISOU  325  CA  ALA A  43    17245   5904  10710  -2957   2144    116       C  
ATOM    326  C   ALA A  43      49.963  27.624  -2.223  1.00 87.27           C  
ANISOU  326  C   ALA A  43    16537   6126  10495  -2629   2054    -65       C  
ATOM    327  O   ALA A  43      50.779  27.575  -1.301  1.00 88.28           O  
ANISOU  327  O   ALA A  43    16546   6428  10568  -2881   2005   -378       O  
ATOM    328  CB  ALA A  43      49.661  29.972  -3.038  1.00 95.28           C  
ANISOU  328  CB  ALA A  43    18781   5978  11443  -2807   2189     77       C  
ATOM    329  N   SER A  44      48.854  26.884  -2.247  1.00 85.44           N  
ANISOU  329  N   SER A  44    16054   6082  10327  -2074   2037    116       N  
ATOM    330  CA  SER A  44      48.513  25.955  -1.163  1.00 82.92           C  
ANISOU  330  CA  SER A  44    15358   6139  10011  -1747   2020     -2       C  
ATOM    331  C   SER A  44      47.533  24.880  -1.637  1.00 79.94           C  
ANISOU  331  C   SER A  44    14567   6054   9752  -1352   2036    236       C  
ATOM    332  O   SER A  44      47.007  24.968  -2.749  1.00 81.04           O  
ANISOU  332  O   SER A  44    14731   6095   9965  -1256   2018    462       O  
ATOM    333  CB  SER A  44      47.919  26.721   0.021  1.00 85.32           C  
ANISOU  333  CB  SER A  44    16034   6133  10249  -1422   2059   -176       C  
ATOM    334  OG  SER A  44      46.784  27.469  -0.377  1.00 87.94           O  
ANISOU  334  OG  SER A  44    16711   6066  10635  -1026   2106     -9       O  
ATOM    335  N   TYR A  45      47.292  23.873  -0.792  1.00 76.62           N  
ANISOU  335  N   TYR A  45    13799   5979   9335  -1128   2073    173       N  
ATOM    336  CA  TYR A  45      46.331  22.801  -1.106  1.00 73.50           C  
ANISOU  336  CA  TYR A  45    13005   5843   9080   -809   2124    356       C  
ATOM    337  C   TYR A  45      44.940  23.364  -1.378  1.00 73.34           C  
ANISOU  337  C   TYR A  45    13106   5580   9180   -380   2173    477       C  
ATOM    338  O   TYR A  45      44.206  22.830  -2.204  1.00 68.54           O  
ANISOU  338  O   TYR A  45    12217   5109   8717   -215   2147    636       O  
ATOM    339  CB  TYR A  45      46.217  21.779   0.031  1.00 73.90           C  
ANISOU  339  CB  TYR A  45    12802   6191   9086   -629   2225    270       C  
ATOM    340  CG  TYR A  45      47.502  21.076   0.409  1.00 74.17           C  
ANISOU  340  CG  TYR A  45    12688   6528   8967   -909   2146    133       C  
ATOM    341  CD1 TYR A  45      48.027  21.201   1.693  1.00 78.41           C  
ANISOU  341  CD1 TYR A  45    13382   7108   9300   -869   2145    -97       C  
ATOM    342  CD2 TYR A  45      48.185  20.277  -0.507  1.00 71.94           C  
ANISOU  342  CD2 TYR A  45    12107   6513   8713  -1158   2053    209       C  
ATOM    343  CE1 TYR A  45      49.201  20.556   2.056  1.00 80.18           C  
ANISOU  343  CE1 TYR A  45    13451   7657   9358  -1049   2027   -256       C  
ATOM    344  CE2 TYR A  45      49.362  19.627  -0.156  1.00 73.33           C  
ANISOU  344  CE2 TYR A  45    12120   7008   8735  -1341   1963     56       C  
ATOM    345  CZ  TYR A  45      49.867  19.774   1.128  1.00 78.93           C  
ANISOU  345  CZ  TYR A  45    12969   7775   9245  -1276   1937   -180       C  
ATOM    346  OH  TYR A  45      51.034  19.145   1.501  1.00 82.63           O  
ANISOU  346  OH  TYR A  45    13262   8601   9533  -1385   1803   -366       O  
ATOM    347  N   LEU A  46      44.589  24.439  -0.671  1.00 77.13           N  
ANISOU  347  N   LEU A  46    13997   5718   9590   -175   2222    366       N  
ATOM    348  CA  LEU A  46      43.315  25.129  -0.875  1.00 80.56           C  
ANISOU  348  CA  LEU A  46    14592   5911  10106    301   2251    441       C  
ATOM    349  C   LEU A  46      43.163  25.583  -2.333  1.00 79.88           C  
ANISOU  349  C   LEU A  46    14649   5644  10059    289   2108    634       C  
ATOM    350  O   LEU A  46      42.111  25.371  -2.945  1.00 79.33           O  
ANISOU  350  O   LEU A  46    14356   5674  10111    662   2064    748       O  
ATOM    351  CB  LEU A  46      43.182  26.333   0.076  1.00 87.17           C  
ANISOU  351  CB  LEU A  46    15962   6347  10813    498   2308    264       C  
ATOM    352  CG  LEU A  46      42.971  26.066   1.579  1.00 90.15           C  
ANISOU  352  CG  LEU A  46    16285   6863  11106    707   2469     73       C  
ATOM    353  CD1 LEU A  46      44.216  25.463   2.244  1.00 88.38           C  
ANISOU  353  CD1 LEU A  46    15975   6864  10741    296   2442    -72       C  
ATOM    354  CD2 LEU A  46      42.550  27.355   2.308  1.00 94.31           C  
ANISOU  354  CD2 LEU A  46    17366   6955  11511   1032   2513    -90       C  
ATOM    355  N   ASP A  47      44.216  26.196  -2.884  1.00 78.75           N  
ANISOU  355  N   ASP A  47    14871   5253   9796   -141   2042    655       N  
ATOM    356  CA  ASP A  47      44.207  26.660  -4.279  1.00 79.58           C  
ANISOU  356  CA  ASP A  47    15220   5149   9867   -185   1944    865       C  
ATOM    357  C   ASP A  47      44.081  25.492  -5.260  1.00 79.66           C  
ANISOU  357  C   ASP A  47    14702   5596   9970   -211   1861   1016       C  
ATOM    358  O   ASP A  47      43.380  25.596  -6.273  1.00 81.88           O  
ANISOU  358  O   ASP A  47    15011   5839  10261     74   1749   1177       O  
ATOM    359  CB  ASP A  47      45.474  27.463  -4.611  1.00 77.98           C  
ANISOU  359  CB  ASP A  47    15495   4617   9519   -750   1971    850       C  
ATOM    360  CG  ASP A  47      45.516  28.821  -3.932  1.00 80.09           C  
ANISOU  360  CG  ASP A  47    16431   4311   9689   -730   2027    717       C  
ATOM    361  OD1 ASP A  47      44.735  29.035  -2.983  1.00 80.99           O  
ANISOU  361  OD1 ASP A  47    16589   4358   9826   -297   2048    590       O  
ATOM    362  OD2 ASP A  47      46.339  29.675  -4.342  1.00 78.80           O  
ANISOU  362  OD2 ASP A  47    16767   3753   9422  -1167   2074    726       O  
ATOM    363  N   CYS A  48      44.768  24.390  -4.960  1.00 76.52           N  
ANISOU  363  N   CYS A  48    13858   5602   9613   -518   1893    944       N  
ATOM    364  CA  CYS A  48      44.738  23.211  -5.821  1.00 75.00           C  
ANISOU  364  CA  CYS A  48    13193   5805   9500   -569   1819   1051       C  
ATOM    365  C   CYS A  48      43.327  22.660  -6.011  1.00 76.25           C  
ANISOU  365  C   CYS A  48    12999   6138   9835    -92   1771   1098       C  
ATOM    366  O   CYS A  48      42.936  22.332  -7.137  1.00 77.70           O  
ANISOU  366  O   CYS A  48    13030   6440  10053     13   1633   1213       O  
ATOM    367  CB  CYS A  48      45.654  22.108  -5.280  1.00 72.78           C  
ANISOU  367  CB  CYS A  48    12540   5898   9217   -888   1868    940       C  
ATOM    368  SG  CYS A  48      47.391  22.267  -5.762  1.00 71.71           S  
ANISOU  368  SG  CYS A  48    12517   5818   8911  -1500   1856    895       S  
ATOM    369  N   ILE A  49      42.564  22.556  -4.926  1.00 76.13           N  
ANISOU  369  N   ILE A  49    12838   6163   9926    188   1890    986       N  
ATOM    370  CA  ILE A  49      41.187  22.083  -5.041  1.00 79.17           C  
ANISOU  370  CA  ILE A  49    12825   6744  10513    602   1885    985       C  
ATOM    371  C   ILE A  49      40.395  22.990  -5.981  1.00 82.99           C  
ANISOU  371  C   ILE A  49    13527   7028  10977    988   1707   1066       C  
ATOM    372  O   ILE A  49      39.681  22.498  -6.857  1.00 83.71           O  
ANISOU  372  O   ILE A  49    13282   7343  11181   1183   1557   1102       O  
ATOM    373  CB  ILE A  49      40.462  21.994  -3.684  1.00 82.02           C  
ANISOU  373  CB  ILE A  49    13040   7157  10965    854   2108    852       C  
ATOM    374  CG1 ILE A  49      41.098  20.923  -2.788  1.00 80.77           C  
ANISOU  374  CG1 ILE A  49    12668   7225  10797    561   2281    795       C  
ATOM    375  CG2 ILE A  49      38.992  21.650  -3.896  1.00 84.23           C  
ANISOU  375  CG2 ILE A  49    12868   7655  11479   1261   2122    821       C  
ATOM    376  CD1 ILE A  49      42.039  21.465  -1.745  1.00 81.48           C  
ANISOU  376  CD1 ILE A  49    13152   7135  10672    402   2359    692       C  
ATOM    377  N   ARG A  50      40.538  24.304  -5.801  1.00 66.17           N  
ANISOU  377  N   ARG A  50    13203   5443   6496  -1109    846   1154       N  
ATOM    378  CA  ARG A  50      39.889  25.283  -6.675  1.00 72.21           C  
ANISOU  378  CA  ARG A  50    14488   5959   6989   -857    887   1355       C  
ATOM    379  C   ARG A  50      40.337  25.082  -8.115  1.00 72.06           C  
ANISOU  379  C   ARG A  50    14375   6097   6907  -1139    881   1369       C  
ATOM    380  O   ARG A  50      39.520  25.105  -9.037  1.00 73.12           O  
ANISOU  380  O   ARG A  50    14501   6328   6954   -833    844   1533       O  
ATOM    381  CB  ARG A  50      40.215  26.721  -6.246  1.00 79.37           C  
ANISOU  381  CB  ARG A  50    16216   6329   7610   -953   1023   1388       C  
ATOM    382  CG  ARG A  50      39.553  27.178  -4.949  1.00 81.81           C  
ANISOU  382  CG  ARG A  50    16764   6409   7911   -573   1048   1420       C  
ATOM    383  CD  ARG A  50      40.145  28.511  -4.490  1.00 86.90           C  
ANISOU  383  CD  ARG A  50    18238   6511   8268   -824   1213   1398       C  
ATOM    384  NE  ARG A  50      39.832  29.593  -5.427  1.00 92.59           N  
ANISOU  384  NE  ARG A  50    19681   6856   8643   -667   1299   1581       N  
ATOM    385  CZ  ARG A  50      40.577  30.685  -5.629  1.00 96.01           C  
ANISOU  385  CZ  ARG A  50    20887   6835   8759  -1068   1458   1563       C  
ATOM    386  NH1 ARG A  50      41.721  30.876  -4.971  1.00 97.44           N  
ANISOU  386  NH1 ARG A  50    21193   6926   8902  -1701   1553   1355       N  
ATOM    387  NH2 ARG A  50      40.176  31.594  -6.512  1.00 97.67           N  
ANISOU  387  NH2 ARG A  50    21762   6698   8649   -849   1528   1754       N  
ATOM    388  N   ALA A  51      41.641  24.887  -8.298  1.00 70.80           N  
ANISOU  388  N   ALA A  51    14122   6009   6770  -1723    917   1191       N  
ATOM    389  CA  ALA A  51      42.203  24.630  -9.621  1.00 68.14           C  
ANISOU  389  CA  ALA A  51    13649   5861   6381  -2051    910   1167       C  
ATOM    390  C   ALA A  51      41.458  23.497 -10.309  1.00 62.62           C  
ANISOU  390  C   ALA A  51    12354   5563   5877  -1781    806   1220       C  
ATOM    391  O   ALA A  51      40.883  23.684 -11.372  1.00 62.96           O  
ANISOU  391  O   ALA A  51    12478   5645   5798  -1625    792   1368       O  
ATOM    392  CB  ALA A  51      43.683  24.294  -9.513  1.00 66.43           C  
ANISOU  392  CB  ALA A  51    13225   5818   6196  -2666    943    929       C  
ATOM    393  N   ILE A  52      41.445  22.328  -9.680  1.00 60.38           N  
ANISOU  393  N   ILE A  52    11500   5573   5869  -1731    743   1100       N  
ATOM    394  CA  ILE A  52      40.908  21.131 -10.322  1.00 59.83           C  
ANISOU  394  CA  ILE A  52    10875   5891   5966  -1597    670   1104       C  
ATOM    395  C   ILE A  52      39.421  21.288 -10.614  1.00 60.08           C  
ANISOU  395  C   ILE A  52    10939   5978   5911  -1090    631   1311       C  
ATOM    396  O   ILE A  52      38.922  20.749 -11.603  1.00 54.52           O  
ANISOU  396  O   ILE A  52     9962   5555   5198  -1030    599   1371       O  
ATOM    397  CB  ILE A  52      41.161  19.859  -9.470  1.00 57.64           C  
ANISOU  397  CB  ILE A  52    10076   5859   5966  -1627    628    937       C  
ATOM    398  CG1 ILE A  52      42.661  19.542  -9.431  1.00 56.28           C  
ANISOU  398  CG1 ILE A  52     9765   5776   5843  -2095    660    731       C  
ATOM    399  CG2 ILE A  52      40.388  18.655 -10.026  1.00 53.52           C  
ANISOU  399  CG2 ILE A  52     9078   5684   5573  -1459    575    953       C  
ATOM    400  CD1 ILE A  52      43.080  18.700  -8.242  1.00 53.08           C  
ANISOU  400  CD1 ILE A  52     9038   5491   5637  -2089    640    582       C  
ATOM    401  N   ALA A  53      38.725  22.035  -9.757  1.00 61.90           N  
ANISOU  401  N   ALA A  53    11493   5977   6050   -726    639   1415       N  
ATOM    402  CA  ALA A  53      37.289  22.246  -9.915  1.00 62.09           C  
ANISOU  402  CA  ALA A  53    11535   6116   5943   -182    601   1609       C  
ATOM    403  C   ALA A  53      36.995  23.024 -11.192  1.00 62.56           C  
ANISOU  403  C   ALA A  53    11921   6117   5731    -78    626   1791       C  
ATOM    404  O   ALA A  53      36.222  22.568 -12.035  1.00 61.69           O  
ANISOU  404  O   ALA A  53    11509   6365   5566    107    582   1886       O  
ATOM    405  CB  ALA A  53      36.718  22.963  -8.706  1.00 63.63           C  
ANISOU  405  CB  ALA A  53    12047   6059   6069    192    613   1668       C  
ATOM    406  N   ALA A  54      37.652  24.171 -11.349  1.00 65.02           N  
ANISOU  406  N   ALA A  54    12859   5995   5852   -240    706   1830       N  
ATOM    407  CA  ALA A  54      37.467  25.027 -12.528  1.00 68.18           C  
ANISOU  407  CA  ALA A  54    13687   6259   5959   -158    743   2012       C  
ATOM    408  C   ALA A  54      38.099  24.467 -13.822  1.00 67.66           C  
ANISOU  408  C   ALA A  54    13333   6443   5932   -591    729   1955       C  
ATOM    409  O   ALA A  54      38.113  25.146 -14.849  1.00 71.66           O  
ANISOU  409  O   ALA A  54    14191   6836   6201   -616    762   2087       O  
ATOM    410  CB  ALA A  54      38.001  26.436 -12.236  1.00 69.62           C  
ANISOU  410  CB  ALA A  54    14718   5845   5888   -246    855   2060       C  
ATOM    411  N   ASN A  55      38.612  23.238 -13.765  1.00 65.13           N  
ANISOU  411  N   ASN A  55    12403   6451   5894   -912    687   1760       N  
ATOM    412  CA  ASN A  55      39.202  22.546 -14.918  1.00 65.10           C  
ANISOU  412  CA  ASN A  55    12055   6726   5952  -1305    675   1677       C  
ATOM    413  C   ASN A  55      40.490  23.212 -15.409  1.00 65.24           C  
ANISOU  413  C   ASN A  55    12445   6498   5843  -1830    741   1593       C  
ATOM    414  O   ASN A  55      40.713  23.352 -16.610  1.00 63.90           O  
ANISOU  414  O   ASN A  55    12324   6410   5547  -2034    750   1639       O  
ATOM    415  CB  ASN A  55      38.180  22.386 -16.055  1.00 67.61           C  
ANISOU  415  CB  ASN A  55    12201   7347   6140  -1027    640   1856       C  
ATOM    416  CG  ASN A  55      38.444  21.155 -16.919  1.00 67.77           C  
ANISOU  416  CG  ASN A  55    11629   7796   6323  -1337    614   1732       C  
ATOM    417  OD1 ASN A  55      39.412  21.106 -17.677  1.00 67.20           O  
ANISOU  417  OD1 ASN A  55    11560   7720   6251  -1776    639   1637       O  
ATOM    418  ND2 ASN A  55      37.571  20.156 -16.809  1.00 69.01           N  
ANISOU  418  ND2 ASN A  55    11294   8334   6591  -1125    573   1724       N  
ATOM    419  N   GLU A  56      41.335  23.610 -14.461  1.00 65.07           N  
ANISOU  419  N   GLU A  56    12670   6218   5834  -2077    790   1462       N  
ATOM    420  CA  GLU A  56      42.670  24.116 -14.763  1.00 71.08           C  
ANISOU  420  CA  GLU A  56    13706   6844   6459  -2667    858   1328       C  
ATOM    421  C   GLU A  56      43.724  23.274 -14.042  1.00 70.56           C  
ANISOU  421  C   GLU A  56    13194   7008   6605  -3022    851   1063       C  
ATOM    422  O   GLU A  56      44.801  23.753 -13.682  1.00 73.52           O  
ANISOU  422  O   GLU A  56    13793   7283   6860  -3457    915    921       O  
ATOM    423  CB  GLU A  56      42.760  25.601 -14.405  1.00 77.44           C  
ANISOU  423  CB  GLU A  56    15348   7122   6956  -2691    956   1425       C  
ATOM    424  CG  GLU A  56      42.301  26.514 -15.560  1.00 83.23           C  
ANISOU  424  CG  GLU A  56    16609   7635   7381  -2579    990   1645       C  
ATOM    425  CD  GLU A  56      41.341  27.626 -15.140  1.00 88.28           C  
ANISOU  425  CD  GLU A  56    17933   7825   7786  -2049   1042   1875       C  
ATOM    426  OE1 GLU A  56      40.985  27.730 -13.945  1.00 87.13           O  
ANISOU  426  OE1 GLU A  56    17855   7531   7719  -1771   1051   1862       O  
ATOM    427  OE2 GLU A  56      40.937  28.403 -16.032  1.00 93.52           O  
ANISOU  427  OE2 GLU A  56    19080   8287   8167  -1887   1075   2075       O  
ATOM    428  N   ALA A  57      43.388  22.001 -13.860  1.00 68.81           N  
ANISOU  428  N   ALA A  57    12352   7128   6666  -2830    779    999       N  
ATOM    429  CA  ALA A  57      44.253  21.013 -13.220  1.00 65.02           C  
ANISOU  429  CA  ALA A  57    11404   6907   6395  -3044    764    770       C  
ATOM    430  C   ALA A  57      43.423  19.749 -13.053  1.00 60.16           C  
ANISOU  430  C   ALA A  57    10273   6547   6039  -2692    697    778       C  
ATOM    431  O   ALA A  57      42.190  19.809 -13.127  1.00 57.45           O  
ANISOU  431  O   ALA A  57     9969   6168   5691  -2299    666    949       O  
ATOM    432  CB  ALA A  57      44.751  21.507 -11.881  1.00 65.40           C  
ANISOU  432  CB  ALA A  57    11671   6757   6422  -3120    803    686       C  
ATOM    433  N   ASP A  58      44.091  18.620 -12.824  1.00 57.72           N  
ANISOU  433  N   ASP A  58     9505   6511   5914  -2829    683    594       N  
ATOM    434  CA  ASP A  58      43.426  17.312 -12.848  1.00 55.43           C  
ANISOU  434  CA  ASP A  58     8768   6460   5832  -2590    643    577       C  
ATOM    435  C   ASP A  58      43.426  16.544 -11.535  1.00 49.68           C  
ANISOU  435  C   ASP A  58     7820   5760   5295  -2418    624    483       C  
ATOM    436  O   ASP A  58      42.396  15.977 -11.177  1.00 51.00           O  
ANISOU  436  O   ASP A  58     7848   5966   5562  -2117    594    550       O  
ATOM    437  CB  ASP A  58      44.029  16.442 -13.946  1.00 59.90           C  
ANISOU  437  CB  ASP A  58     9003   7321   6435  -2839    656    459       C  
ATOM    438  CG  ASP A  58      43.525  16.821 -15.327  1.00 66.81           C  
ANISOU  438  CG  ASP A  58     9973   8242   7170  -2893    660    589       C  
ATOM    439  OD1 ASP A  58      42.305  16.682 -15.560  1.00 69.85           O  
ANISOU  439  OD1 ASP A  58    10322   8666   7553  -2605    638    737       O  
ATOM    440  OD2 ASP A  58      44.336  17.244 -16.178  1.00 70.10           O  
ANISOU  440  OD2 ASP A  58    10481   8698   7454  -3231    684    541       O  
ATOM    441  N   ALA A  59      44.552  16.505 -10.820  1.00 44.77           N  
ANISOU  441  N   ALA A  59     7154   5160   4696  -2615    642    328       N  
ATOM    442  CA  ALA A  59      44.635  15.682  -9.610  1.00 40.75           C  
ANISOU  442  CA  ALA A  59     6415   4708   4361  -2447    624    237       C  
ATOM    443  C   ALA A  59      45.664  16.141  -8.579  1.00 43.47           C  
ANISOU  443  C   ALA A  59     6838   5022   4658  -2614    644    124       C  
ATOM    444  O   ALA A  59      46.636  16.809  -8.910  1.00 48.29           O  
ANISOU  444  O   ALA A  59     7575   5677   5096  -2956    683     49       O  
ATOM    445  CB  ALA A  59      44.902  14.230 -10.000  1.00 39.09           C  
ANISOU  445  CB  ALA A  59     5799   4768   4286  -2435    626    119       C  
ATOM    446  N   VAL A  60      45.425  15.768  -7.321  1.00 46.82           N  
ANISOU  446  N   VAL A  60     7179   5401   5209  -2397    622    108       N  
ATOM    447  CA  VAL A  60      46.361  16.013  -6.208  1.00 47.63           C  
ANISOU  447  CA  VAL A  60     7279   5543   5277  -2527    641     -8       C  
ATOM    448  C   VAL A  60      46.032  15.092  -5.035  1.00 47.58           C  
ANISOU  448  C   VAL A  60     7048   5571   5460  -2234    603    -32       C  
ATOM    449  O   VAL A  60      44.869  14.770  -4.807  1.00 46.07           O  
ANISOU  449  O   VAL A  60     6868   5254   5384  -1949    568     74       O  
ATOM    450  CB  VAL A  60      46.293  17.458  -5.695  1.00 46.09           C  
ANISOU  450  CB  VAL A  60     7533   5062   4917  -2646    677     58       C  
ATOM    451  CG1 VAL A  60      44.910  17.759  -5.161  1.00 42.17           C  
ANISOU  451  CG1 VAL A  60     7239   4285   4498  -2274    646    223       C  
ATOM    452  CG2 VAL A  60      47.356  17.698  -4.619  1.00 47.42           C  
ANISOU  452  CG2 VAL A  60     7669   5341   5007  -2864    712    -84       C  
ATOM    453  N   THR A  61      47.064  14.698  -4.293  1.00 50.42           N  
ANISOU  453  N   THR A  61     7205   6135   5816  -2315    614   -172       N  
ATOM    454  CA  THR A  61      46.927  13.818  -3.131  1.00 52.51           C  
ANISOU  454  CA  THR A  61     7273   6446   6234  -2054    583   -201       C  
ATOM    455  C   THR A  61      46.666  14.605  -1.849  1.00 52.28           C  
ANISOU  455  C   THR A  61     7437   6231   6195  -2016    578   -161       C  
ATOM    456  O   THR A  61      47.382  15.560  -1.545  1.00 53.67           O  
ANISOU  456  O   THR A  61     7769   6414   6208  -2281    620   -211       O  
ATOM    457  CB  THR A  61      48.202  12.998  -2.942  1.00 56.50           C  
ANISOU  457  CB  THR A  61     7456   7305   6705  -2102    599   -364       C  
ATOM    458  OG1 THR A  61      49.276  13.641  -3.649  1.00 61.11           O  
ANISOU  458  OG1 THR A  61     8035   8104   7079  -2461    640   -460       O  
ATOM    459  CG2 THR A  61      48.016  11.602  -3.490  1.00 57.00           C  
ANISOU  459  CG2 THR A  61     7302   7466   6889  -1884    594   -388       C  
ATOM    460  N   LEU A  62      45.659  14.183  -1.085  1.00 48.50           N  
ANISOU  460  N   LEU A  62     6953   5608   5867  -1718    535    -83       N  
ATOM    461  CA  LEU A  62      45.214  14.938   0.084  1.00 45.38           C  
ANISOU  461  CA  LEU A  62     6756   5016   5473  -1646    527    -32       C  
ATOM    462  C   LEU A  62      44.995  14.082   1.309  1.00 44.36           C  
ANISOU  462  C   LEU A  62     6431   4935   5488  -1420    486    -56       C  
ATOM    463  O   LEU A  62      44.626  12.913   1.196  1.00 46.70           O  
ANISOU  463  O   LEU A  62     6533   5309   5901  -1237    456    -56       O  
ATOM    464  CB  LEU A  62      43.900  15.635  -0.238  1.00 42.47           C  
ANISOU  464  CB  LEU A  62     6667   4380   5090  -1482    512    122       C  
ATOM    465  CG  LEU A  62      43.929  16.550  -1.461  1.00 38.81           C  
ANISOU  465  CG  LEU A  62     6468   3813   4464  -1650    552    182       C  
ATOM    466  CD1 LEU A  62      42.553  17.157  -1.671  1.00 36.56           C  
ANISOU  466  CD1 LEU A  62     6436   3310   4143  -1381    533    350       C  
ATOM    467  CD2 LEU A  62      44.995  17.623  -1.306  1.00 32.85           C  
ANISOU  467  CD2 LEU A  62     5963   2998   3519  -2002    624    110       C  
ATOM    468  N   ASP A  63      45.210  14.683   2.480  1.00 44.56           N  
ANISOU  468  N   ASP A  63     6545   4902   5484  -1458    494    -76       N  
ATOM    469  CA  ASP A  63      44.853  14.059   3.753  1.00 42.87           C  
ANISOU  469  CA  ASP A  63     6198   4694   5396  -1245    450    -78       C  
ATOM    470  C   ASP A  63      43.345  14.131   3.915  1.00 40.81           C  
ANISOU  470  C   ASP A  63     6070   4218   5217  -1000    406     43       C  
ATOM    471  O   ASP A  63      42.690  14.975   3.308  1.00 45.07           O  
ANISOU  471  O   ASP A  63     6849   4594   5683   -988    417    130       O  
ATOM    472  CB  ASP A  63      45.520  14.765   4.936  1.00 46.42           C  
ANISOU  472  CB  ASP A  63     6700   5169   5768  -1390    479   -139       C  
ATOM    473  CG  ASP A  63      47.038  14.710   4.885  1.00 51.12           C  
ANISOU  473  CG  ASP A  63     7109   6091   6223  -1648    525   -273       C  
ATOM    474  OD1 ASP A  63      47.590  13.742   4.323  1.00 52.46           O  
ANISOU  474  OD1 ASP A  63     7021   6501   6410  -1590    514   -327       O  
ATOM    475  OD2 ASP A  63      47.685  15.641   5.422  1.00 54.59           O  
ANISOU  475  OD2 ASP A  63     7665   6575   6503  -1917    581   -333       O  
ATOM    476  N   ALA A  64      42.800  13.259   4.749  1.00 37.06           N  
ANISOU  476  N   ALA A  64     5448   3772   4861   -799    358     48       N  
ATOM    477  CA  ALA A  64      41.351  13.120   4.888  1.00 36.81           C  
ANISOU  477  CA  ALA A  64     5467   3643   4874   -582    312    141       C  
ATOM    478  C   ALA A  64      40.602  14.445   5.042  1.00 34.66           C  
ANISOU  478  C   ALA A  64     5470   3183   4514   -514    315    227       C  
ATOM    479  O   ALA A  64      39.522  14.614   4.490  1.00 34.54           O  
ANISOU  479  O   ALA A  64     5525   3147   4453   -356    294    318       O  
ATOM    480  CB  ALA A  64      41.021  12.194   6.064  1.00 34.63           C  
ANISOU  480  CB  ALA A  64     5041   3417   4701   -443    267    115       C  
ATOM    481  N   GLY A  65      41.167  15.370   5.806  1.00 35.51           N  
ANISOU  481  N   GLY A  65     5745   3177   4571   -620    350    197       N  
ATOM    482  CA  GLY A  65      40.484  16.624   6.119  1.00 36.74           C  
ANISOU  482  CA  GLY A  65     6229   3105   4626   -521    371    271       C  
ATOM    483  C   GLY A  65      40.242  17.448   4.874  1.00 38.97           C  
ANISOU  483  C   GLY A  65     6783   3259   4765   -526    411    356       C  
ATOM    484  O   GLY A  65      39.131  17.896   4.611  1.00 40.03           O  
ANISOU  484  O   GLY A  65     7071   3310   4828   -267    393    465       O  
ATOM    485  N   LEU A  66      41.296  17.637   4.095  1.00 40.87           N  
ANISOU  485  N   LEU A  66     7071   3520   4936   -812    464    304       N  
ATOM    486  CA  LEU A  66      41.199  18.407   2.874  1.00 42.83           C  
ANISOU  486  CA  LEU A  66     7597   3643   5035   -863    507    381       C  
ATOM    487  C   LEU A  66      40.300  17.698   1.853  1.00 41.90           C  
ANISOU  487  C   LEU A  66     7294   3668   4959   -656    451    466       C  
ATOM    488  O   LEU A  66      39.603  18.351   1.077  1.00 46.70           O  
ANISOU  488  O   LEU A  66     8127   4178   5440   -511    460    584       O  
ATOM    489  CB  LEU A  66      42.598  18.696   2.326  1.00 45.70           C  
ANISOU  489  CB  LEU A  66     8016   4052   5295  -1275    576    283       C  
ATOM    490  CG  LEU A  66      43.374  19.750   3.146  1.00 48.42           C  
ANISOU  490  CG  LEU A  66     8669   4240   5489  -1546    664    211       C  
ATOM    491  CD1 LEU A  66      44.888  19.531   3.107  1.00 49.14           C  
ANISOU  491  CD1 LEU A  66     8572   4593   5507  -1967    709     52       C  
ATOM    492  CD2 LEU A  66      43.038  21.162   2.672  1.00 51.07           C  
ANISOU  492  CD2 LEU A  66     9591   4214   5599  -1576    747    305       C  
ATOM    493  N   VAL A  67      40.279  16.368   1.883  1.00 36.91           N  
ANISOU  493  N   VAL A  67     6276   3271   4477   -633    401    410       N  
ATOM    494  CA  VAL A  67      39.340  15.609   1.059  1.00 33.54           C  
ANISOU  494  CA  VAL A  67     5668   3008   4067   -477    362    472       C  
ATOM    495  C   VAL A  67      37.901  16.067   1.304  1.00 35.84           C  
ANISOU  495  C   VAL A  67     6060   3284   4274   -154    326    592       C  
ATOM    496  O   VAL A  67      37.149  16.271   0.352  1.00 36.41           O  
ANISOU  496  O   VAL A  67     6168   3437   4229    -26    321    691       O  
ATOM    497  CB  VAL A  67      39.443  14.085   1.305  1.00 28.04           C  
ANISOU  497  CB  VAL A  67     4625   2513   3517   -500    334    384       C  
ATOM    498  CG1 VAL A  67      38.312  13.360   0.629  1.00 25.57           C  
ANISOU  498  CG1 VAL A  67     4168   2373   3176   -378    311    440       C  
ATOM    499  CG2 VAL A  67      40.760  13.556   0.805  1.00 27.58           C  
ANISOU  499  CG2 VAL A  67     4444   2535   3499   -738    372    278       C  
ATOM    500  N   TYR A  68      37.522  16.242   2.570  1.00 39.32           N  
ANISOU  500  N   TYR A  68     6528   3662   4749    -10    301    582       N  
ATOM    501  CA  TYR A  68      36.186  16.742   2.880  1.00 43.58           C  
ANISOU  501  CA  TYR A  68     7153   4229   5176    328    267    684       C  
ATOM    502  C   TYR A  68      35.954  18.101   2.224  1.00 48.52           C  
ANISOU  502  C   TYR A  68     8172   4658   5605    476    312    803       C  
ATOM    503  O   TYR A  68      35.046  18.248   1.395  1.00 51.29           O  
ANISOU  503  O   TYR A  68     8522   5155   5813    701    294    913       O  
ATOM    504  CB  TYR A  68      35.935  16.844   4.387  1.00 45.23           C  
ANISOU  504  CB  TYR A  68     7363   4378   5444    439    240    643       C  
ATOM    505  CG  TYR A  68      34.511  17.293   4.693  1.00 48.14           C  
ANISOU  505  CG  TYR A  68     7774   4848   5670    818    201    735       C  
ATOM    506  CD1 TYR A  68      33.423  16.501   4.330  1.00 47.98           C  
ANISOU  506  CD1 TYR A  68     7462   5184   5584    955    145    764       C  
ATOM    507  CD2 TYR A  68      34.254  18.513   5.306  1.00 50.04           C  
ANISOU  507  CD2 TYR A  68     8354   4860   5800   1033    230    785       C  
ATOM    508  CE1 TYR A  68      32.124  16.900   4.581  1.00 50.60           C  
ANISOU  508  CE1 TYR A  68     7778   5712   5736   1310    106    838       C  
ATOM    509  CE2 TYR A  68      32.952  18.923   5.563  1.00 53.48           C  
ANISOU  509  CE2 TYR A  68     8813   5434   6072   1437    194    867       C  
ATOM    510  CZ  TYR A  68      31.890  18.112   5.198  1.00 53.89           C  
ANISOU  510  CZ  TYR A  68     8512   5912   6052   1582    126    893       C  
ATOM    511  OH  TYR A  68      30.592  18.508   5.441  1.00 54.37           O  
ANISOU  511  OH  TYR A  68     8543   6212   5904   1993     87    964       O  
ATOM    512  N   ASP A  69      36.795  19.075   2.569  1.00 50.16           N  
ANISOU  512  N   ASP A  69     8733   4552   5774    336    379    781       N  
ATOM    513  CA  ASP A  69      36.696  20.423   1.998  1.00 56.73           C  
ANISOU  513  CA  ASP A  69    10058   5108   6386    443    447    890       C  
ATOM    514  C   ASP A  69      36.623  20.391   0.470  1.00 56.52           C  
ANISOU  514  C   ASP A  69    10036   5176   6262    419    451    973       C  
ATOM    515  O   ASP A  69      35.965  21.236  -0.141  1.00 60.08           O  
ANISOU  515  O   ASP A  69    10794   5528   6507    687    473   1114       O  
ATOM    516  CB  ASP A  69      37.878  21.304   2.443  1.00 62.87           C  
ANISOU  516  CB  ASP A  69    11218   5554   7115    122    544    814       C  
ATOM    517  CG  ASP A  69      37.902  21.558   3.960  1.00 66.62           C  
ANISOU  517  CG  ASP A  69    11761   5910   7642    154    558    745       C  
ATOM    518  OD1 ASP A  69      36.829  21.564   4.602  1.00 67.92           O  
ANISOU  518  OD1 ASP A  69    11879   6123   7806    523    510    798       O  
ATOM    519  OD2 ASP A  69      39.006  21.755   4.515  1.00 68.17           O  
ANISOU  519  OD2 ASP A  69    12037   6005   7858   -206    618    629       O  
ATOM    520  N   ALA A  70      37.287  19.413  -0.142  1.00 52.33           N  
ANISOU  520  N   ALA A  70     9176   4844   5864    124    434    889       N  
ATOM    521  CA  ALA A  70      37.305  19.292  -1.598  1.00 51.65           C  
ANISOU  521  CA  ALA A  70     9054   4871   5700     48    440    948       C  
ATOM    522  C   ALA A  70      35.987  18.772  -2.160  1.00 49.99           C  
ANISOU  522  C   ALA A  70     8593   4975   5427    356    382   1049       C  
ATOM    523  O   ALA A  70      35.594  19.138  -3.259  1.00 50.65           O  
ANISOU  523  O   ALA A  70     8773   5120   5353    454    392   1161       O  
ATOM    524  CB  ALA A  70      38.445  18.394  -2.038  1.00 49.19           C  
ANISOU  524  CB  ALA A  70     8469   4689   5533   -348    449    811       C  
ATOM    525  N   TYR A  71      35.309  17.904  -1.420  1.00 47.01           N  
ANISOU  525  N   TYR A  71     7887   4830   5143    480    326   1004       N  
ATOM    526  CA  TYR A  71      34.046  17.346  -1.909  1.00 44.82           C  
ANISOU  526  CA  TYR A  71     7335   4936   4759    704    280   1075       C  
ATOM    527  C   TYR A  71      32.932  18.400  -1.859  1.00 44.14           C  
ANISOU  527  C   TYR A  71     7471   4876   4425   1165    268   1231       C  
ATOM    528  O   TYR A  71      31.966  18.339  -2.617  1.00 39.63           O  
ANISOU  528  O   TYR A  71     6759   4634   3664   1384    246   1331       O  
ATOM    529  CB  TYR A  71      33.666  16.072  -1.135  1.00 39.25           C  
ANISOU  529  CB  TYR A  71     6248   4483   4182    638    237    966       C  
ATOM    530  CG  TYR A  71      32.225  16.029  -0.722  1.00 41.42           C  
ANISOU  530  CG  TYR A  71     6372   5073   4292    962    188   1027       C  
ATOM    531  CD1 TYR A  71      31.248  15.502  -1.558  1.00 44.56           C  
ANISOU  531  CD1 TYR A  71     6507   5909   4514   1023    173   1073       C  
ATOM    532  CD2 TYR A  71      31.833  16.542   0.506  1.00 44.46           C  
ANISOU  532  CD2 TYR A  71     6862   5365   4666   1195    160   1029       C  
ATOM    533  CE1 TYR A  71      29.905  15.481  -1.168  1.00 47.75           C  
ANISOU  533  CE1 TYR A  71     6732   6703   4710   1310    128   1116       C  
ATOM    534  CE2 TYR A  71      30.511  16.533   0.902  1.00 47.37           C  
ANISOU  534  CE2 TYR A  71     7067   6079   4851   1504    111   1073       C  
ATOM    535  CZ  TYR A  71      29.549  16.005   0.068  1.00 49.62           C  
ANISOU  535  CZ  TYR A  71     7068   6848   4939   1562     93   1115       C  
ATOM    536  OH  TYR A  71      28.242  16.008   0.498  1.00 52.17           O  
ANISOU  536  OH  TYR A  71     7192   7599   5032   1856     45   1145       O  
ATOM    537  N   LEU A  72      33.083  19.369  -0.966  1.00 44.71           N  
ANISOU  537  N   LEU A  72     7896   4619   4470   1322    291   1250       N  
ATOM    538  CA  LEU A  72      32.074  20.403  -0.784  1.00 50.11           C  
ANISOU  538  CA  LEU A  72     8850   5284   4905   1820    291   1391       C  
ATOM    539  C   LEU A  72      31.733  21.158  -2.055  1.00 53.32           C  
ANISOU  539  C   LEU A  72     9505   5695   5060   2040    320   1558       C  
ATOM    540  O   LEU A  72      32.581  21.336  -2.932  1.00 56.61           O  
ANISOU  540  O   LEU A  72    10093   5919   5497   1757    366   1565       O  
ATOM    541  CB  LEU A  72      32.555  21.423   0.244  1.00 50.86           C  
ANISOU  541  CB  LEU A  72     9405   4912   5005   1874    347   1373       C  
ATOM    542  CG  LEU A  72      32.483  20.956   1.683  1.00 47.29           C  
ANISOU  542  CG  LEU A  72     8752   4498   4717   1846    310   1253       C  
ATOM    543  CD1 LEU A  72      33.265  21.908   2.585  1.00 47.30           C  
ANISOU  543  CD1 LEU A  72     9213   4018   4742   1749    388   1207       C  
ATOM    544  CD2 LEU A  72      31.019  20.865   2.081  1.00 49.20           C  
ANISOU  544  CD2 LEU A  72     8783   5110   4802   2311    243   1315       C  
ATOM    545  N   ALA A  73      30.489  21.620  -2.136  1.00 54.48           N  
ANISOU  545  N   ALA A  73     9669   6090   4942   2565    293   1694       N  
ATOM    546  CA  ALA A  73      30.119  22.599  -3.145  1.00 59.28           C  
ANISOU  546  CA  ALA A  73    10635   6635   5256   2902    330   1883       C  
ATOM    547  C   ALA A  73      30.963  23.859  -2.906  1.00 60.78           C  
ANISOU  547  C   ALA A  73    11544   6148   5402   2875    429   1917       C  
ATOM    548  O   ALA A  73      31.165  24.247  -1.751  1.00 60.20           O  
ANISOU  548  O   ALA A  73    11694   5786   5394   2902    458   1848       O  
ATOM    549  CB  ALA A  73      28.635  22.921  -3.059  1.00 60.46           C  
ANISOU  549  CB  ALA A  73    10679   7200   5093   3548    286   2016       C  
ATOM    550  N   PRO A  74      31.479  24.489  -3.982  1.00 61.92           N  
ANISOU  550  N   PRO A  74    12070   6040   5418   2773    491   2012       N  
ATOM    551  CA  PRO A  74      31.328  24.203  -5.408  1.00 64.27           C  
ANISOU  551  CA  PRO A  74    12189   6619   5613   2730    470   2106       C  
ATOM    552  C   PRO A  74      32.495  23.405  -6.005  1.00 62.02           C  
ANISOU  552  C   PRO A  74    11665   6321   5581   2066    475   1965       C  
ATOM    553  O   PRO A  74      32.622  23.315  -7.231  1.00 59.37           O  
ANISOU  553  O   PRO A  74    11283   6108   5166   1943    479   2030       O  
ATOM    554  CB  PRO A  74      31.314  25.605  -6.018  1.00 68.35           C  
ANISOU  554  CB  PRO A  74    13430   6728   5812   3031    554   2294       C  
ATOM    555  CG  PRO A  74      32.283  26.380  -5.142  1.00 69.89           C  
ANISOU  555  CG  PRO A  74    14202   6284   6071   2779    652   2204       C  
ATOM    556  CD  PRO A  74      32.339  25.669  -3.785  1.00 65.94           C  
ANISOU  556  CD  PRO A  74    13317   5896   5842   2647    606   2026       C  
ATOM    557  N   ASN A  75      33.343  22.832  -5.157  1.00 60.39           N  
ANISOU  557  N   ASN A  75    11299   5992   5653   1663    476   1776       N  
ATOM    558  CA  ASN A  75      34.531  22.135  -5.648  1.00 59.35           C  
ANISOU  558  CA  ASN A  75    10971   5851   5730   1083    488   1635       C  
ATOM    559  C   ASN A  75      34.124  20.802  -6.243  1.00 56.30           C  
ANISOU  559  C   ASN A  75     9964   5973   5455    989    423   1589       C  
ATOM    560  O   ASN A  75      34.560  20.445  -7.331  1.00 58.64           O  
ANISOU  560  O   ASN A  75    10139   6378   5763    725    433   1578       O  
ATOM    561  CB  ASN A  75      35.541  21.918  -4.527  1.00 58.97           C  
ANISOU  561  CB  ASN A  75    10922   5580   5902    740    511   1453       C  
ATOM    562  CG  ASN A  75      35.719  23.144  -3.656  1.00 62.28           C  
ANISOU  562  CG  ASN A  75    11918   5547   6199    855    582   1480       C  
ATOM    563  OD1 ASN A  75      36.168  24.194  -4.123  1.00 61.99           O  
ANISOU  563  OD1 ASN A  75    12430   5156   5968    773    667   1545       O  
ATOM    564  ND2 ASN A  75      35.359  23.017  -2.374  1.00 61.80           N  
ANISOU  564  ND2 ASN A  75    11765   5485   6230   1024    559   1424       N  
ATOM    565  N   ASN A  76      33.280  20.078  -5.513  1.00 55.79           N  
ANISOU  565  N   ASN A  76     9533   6217   5449   1182    366   1553       N  
ATOM    566  CA  ASN A  76      32.679  18.834  -5.985  1.00 57.14           C  
ANISOU  566  CA  ASN A  76     9166   6889   5657   1108    322   1511       C  
ATOM    567  C   ASN A  76      33.690  17.789  -6.456  1.00 53.76           C  
ANISOU  567  C   ASN A  76     8489   6486   5451    606    341   1358       C  
ATOM    568  O   ASN A  76      33.424  17.037  -7.382  1.00 55.01           O  
ANISOU  568  O   ASN A  76     8357   6964   5578    479    341   1352       O  
ATOM    569  CB  ASN A  76      31.657  19.126  -7.097  1.00 62.96           C  
ANISOU  569  CB  ASN A  76     9844   7974   6104   1404    310   1681       C  
ATOM    570  CG  ASN A  76      30.567  20.098  -6.656  1.00 69.77           C  
ANISOU  570  CG  ASN A  76    10921   8893   6697   1994    290   1837       C  
ATOM    571  OD1 ASN A  76      30.125  20.949  -7.435  1.00 74.17           O  
ANISOU  571  OD1 ASN A  76    11724   9470   6987   2314    305   2013       O  
ATOM    572  ND2 ASN A  76      30.128  19.976  -5.403  1.00 68.50           N  
ANISOU  572  ND2 ASN A  76    10677   8764   6586   2166    259   1777       N  
ATOM    573  N   LEU A  77      34.849  17.729  -5.818  1.00 52.59           N  
ANISOU  573  N   LEU A  77     8446   6032   5502    331    364   1231       N  
ATOM    574  CA  LEU A  77      35.822  16.705  -6.165  1.00 50.21           C  
ANISOU  574  CA  LEU A  77     7900   5788   5390    -73    383   1079       C  
ATOM    575  C   LEU A  77      35.450  15.393  -5.484  1.00 50.49           C  
ANISOU  575  C   LEU A  77     7566   6055   5564   -102    356    970       C  
ATOM    576  O   LEU A  77      34.628  15.357  -4.567  1.00 50.70           O  
ANISOU  576  O   LEU A  77     7540   6157   5566    128    320    990       O  
ATOM    577  CB  LEU A  77      37.236  17.131  -5.777  1.00 47.09           C  
ANISOU  577  CB  LEU A  77     7725   5068   5098   -348    420    980       C  
ATOM    578  CG  LEU A  77      37.656  18.490  -6.331  1.00 48.87           C  
ANISOU  578  CG  LEU A  77     8407   5013   5147   -387    466   1072       C  
ATOM    579  CD1 LEU A  77      39.155  18.707  -6.183  1.00 48.38           C  
ANISOU  579  CD1 LEU A  77     8476   4763   5144   -791    514    936       C  
ATOM    580  CD2 LEU A  77      37.242  18.629  -7.784  1.00 52.73           C  
ANISOU  580  CD2 LEU A  77     8901   5653   5482   -361    470   1186       C  
ATOM    581  N   LYS A  78      36.047  14.310  -5.962  1.00 49.04           N  
ANISOU  581  N   LYS A  78     7153   5981   5498   -387    383    853       N  
ATOM    582  CA  LYS A  78      35.822  12.997  -5.385  1.00 45.42           C  
ANISOU  582  CA  LYS A  78     6429   5680   5150   -456    381    741       C  
ATOM    583  C   LYS A  78      37.125  12.200  -5.375  1.00 42.42           C  
ANISOU  583  C   LYS A  78     5981   5192   4947   -723    420    590       C  
ATOM    584  O   LYS A  78      37.983  12.393  -6.235  1.00 41.00           O  
ANISOU  584  O   LYS A  78     5841   4965   4770   -902    451    564       O  
ATOM    585  CB  LYS A  78      34.737  12.240  -6.153  1.00 46.73           C  
ANISOU  585  CB  LYS A  78     6360   6218   5175   -463    393    768       C  
ATOM    586  CG  LYS A  78      34.926  12.198  -7.662  1.00 47.77           C  
ANISOU  586  CG  LYS A  78     6444   6480   5225   -630    435    796       C  
ATOM    587  CD  LYS A  78      34.798  10.780  -8.210  1.00 48.17           C  
ANISOU  587  CD  LYS A  78     6256   6762   5284   -879    494    686       C  
ATOM    588  CE  LYS A  78      34.612  10.741  -9.718  1.00 47.29           C  
ANISOU  588  CE  LYS A  78     6051   6880   5036  -1021    535    730       C  
ATOM    589  NZ  LYS A  78      33.167  10.648 -10.056  1.00 50.36           N  
ANISOU  589  NZ  LYS A  78     6265   7694   5175   -918    531    817       N  
ATOM    590  N   PRO A  79      37.274  11.299  -4.393  1.00 39.38           N  
ANISOU  590  N   PRO A  79     5494   4787   4683   -732    418    490       N  
ATOM    591  CA  PRO A  79      38.518  10.575  -4.273  1.00 35.98           C  
ANISOU  591  CA  PRO A  79     5010   4274   4386   -897    454    356       C  
ATOM    592  C   PRO A  79      38.560   9.455  -5.303  1.00 35.43           C  
ANISOU  592  C   PRO A  79     4802   4360   4301  -1056    516    288       C  
ATOM    593  O   PRO A  79      37.581   8.732  -5.461  1.00 37.86           O  
ANISOU  593  O   PRO A  79     5027   4821   4537  -1059    536    296       O  
ATOM    594  CB  PRO A  79      38.453  10.031  -2.852  1.00 33.81           C  
ANISOU  594  CB  PRO A  79     4709   3931   4206   -792    431    302       C  
ATOM    595  CG  PRO A  79      36.997   9.877  -2.560  1.00 34.70           C  
ANISOU  595  CG  PRO A  79     4779   4181   4226   -665    403    370       C  
ATOM    596  CD  PRO A  79      36.230  10.729  -3.519  1.00 37.14           C  
ANISOU  596  CD  PRO A  79     5116   4618   4376   -602    392    491       C  
ATOM    597  N   VAL A  80      39.680   9.330  -6.003  1.00 35.05           N  
ANISOU  597  N   VAL A  80     4733   4296   4288  -1210    554    213       N  
ATOM    598  CA  VAL A  80      39.800   8.376  -7.101  1.00 34.52           C  
ANISOU  598  CA  VAL A  80     4562   4361   4194  -1365    625    145       C  
ATOM    599  C   VAL A  80      40.936   7.372  -6.945  1.00 37.00           C  
ANISOU  599  C   VAL A  80     4827   4638   4593  -1405    678     -5       C  
ATOM    600  O   VAL A  80      40.826   6.260  -7.436  1.00 44.04           O  
ANISOU  600  O   VAL A  80     5684   5584   5464  -1470    753    -76       O  
ATOM    601  CB  VAL A  80      39.956   9.106  -8.424  1.00 34.62           C  
ANISOU  601  CB  VAL A  80     4578   4456   4118  -1502    631    198       C  
ATOM    602  CG1 VAL A  80      38.731   9.993  -8.658  1.00 37.62           C  
ANISOU  602  CG1 VAL A  80     5019   4906   4369  -1392    588    362       C  
ATOM    603  CG2 VAL A  80      41.219   9.935  -8.420  1.00 37.41           C  
ANISOU  603  CG2 VAL A  80     5006   4712   4496  -1584    614    163       C  
ATOM    604  N   VAL A  81      42.020   7.747  -6.270  1.00 36.48           N  
ANISOU  604  N   VAL A  81     4768   4503   4589  -1360    651    -56       N  
ATOM    605  CA  VAL A  81      43.116   6.819  -6.023  1.00 33.56           C  
ANISOU  605  CA  VAL A  81     4331   4159   4262  -1319    696   -190       C  
ATOM    606  C   VAL A  81      43.569   6.929  -4.580  1.00 35.12           C  
ANISOU  606  C   VAL A  81     4540   4285   4520  -1161    654   -208       C  
ATOM    607  O   VAL A  81      43.532   8.012  -3.992  1.00 37.91           O  
ANISOU  607  O   VAL A  81     4940   4587   4875  -1167    595   -147       O  
ATOM    608  CB  VAL A  81      44.281   7.073  -6.994  1.00 34.80           C  
ANISOU  608  CB  VAL A  81     4395   4459   4367  -1468    722   -270       C  
ATOM    609  CG1 VAL A  81      45.488   6.208  -6.665  1.00 35.34           C  
ANISOU  609  CG1 VAL A  81     4365   4623   4439  -1358    762   -410       C  
ATOM    610  CG2 VAL A  81      43.823   6.803  -8.419  1.00 34.93           C  
ANISOU  610  CG2 VAL A  81     4390   4553   4328  -1626    772   -261       C  
ATOM    611  N   ALA A  82      43.983   5.796  -4.013  1.00 34.84           N  
ANISOU  611  N   ALA A  82     4488   4236   4513  -1012    693   -289       N  
ATOM    612  CA  ALA A  82      44.389   5.715  -2.615  1.00 31.87           C  
ANISOU  612  CA  ALA A  82     4109   3818   4181   -837    657   -303       C  
ATOM    613  C   ALA A  82      45.809   5.183  -2.472  1.00 31.91           C  
ANISOU  613  C   ALA A  82     4000   3978   4146   -721    690   -417       C  
ATOM    614  O   ALA A  82      46.166   4.191  -3.096  1.00 31.46           O  
ANISOU  614  O   ALA A  82     3944   3960   4048   -651    762   -491       O  
ATOM    615  CB  ALA A  82      43.441   4.821  -1.873  1.00 30.19           C  
ANISOU  615  CB  ALA A  82     4016   3455   4002   -713    670   -274       C  
ATOM    616  N   GLU A  83      46.615   5.840  -1.643  1.00 34.57           N  
ANISOU  616  N   GLU A  83     4239   4432   4463   -694    644   -437       N  
ATOM    617  CA  GLU A  83      47.904   5.290  -1.246  1.00 38.36           C  
ANISOU  617  CA  GLU A  83     4570   5139   4865   -523    667   -540       C  
ATOM    618  C   GLU A  83      47.664   4.173  -0.256  1.00 38.93           C  
ANISOU  618  C   GLU A  83     4737   5079   4975   -224    684   -529       C  
ATOM    619  O   GLU A  83      46.761   4.279   0.572  1.00 37.53           O  
ANISOU  619  O   GLU A  83     4677   4702   4881   -207    645   -449       O  
ATOM    620  CB  GLU A  83      48.757   6.339  -0.557  1.00 42.55           C  
ANISOU  620  CB  GLU A  83     4959   5885   5322   -626    621   -567       C  
ATOM    621  CG  GLU A  83      49.163   7.507  -1.425  1.00 46.01           C  
ANISOU  621  CG  GLU A  83     5355   6457   5669   -961    617   -591       C  
ATOM    622  CD  GLU A  83      50.085   8.479  -0.691  1.00 48.53           C  
ANISOU  622  CD  GLU A  83     5568   7015   5858  -1123    598   -643       C  
ATOM    623  OE1 GLU A  83      50.614   8.114   0.389  1.00 45.05           O  
ANISOU  623  OE1 GLU A  83     5002   6732   5384   -941    588   -679       O  
ATOM    624  OE2 GLU A  83      50.269   9.611  -1.198  1.00 49.29           O  
ANISOU  624  OE2 GLU A  83     5726   7142   5859  -1449    601   -648       O  
ATOM    625  N   PHE A  84      48.463   3.112  -0.341  1.00 41.01           N  
ANISOU  625  N   PHE A  84     4972   5454   5156     25    744   -608       N  
ATOM    626  CA  PHE A  84      48.428   2.041   0.659  1.00 40.94           C  
ANISOU  626  CA  PHE A  84     5097   5320   5139    351    769   -596       C  
ATOM    627  C   PHE A  84      49.818   1.825   1.251  1.00 45.27           C  
ANISOU  627  C   PHE A  84     5443   6204   5552    631    768   -664       C  
ATOM    628  O   PHE A  84      50.816   2.240   0.660  1.00 46.09           O  
ANISOU  628  O   PHE A  84     5309   6658   5544    574    771   -748       O  
ATOM    629  CB  PHE A  84      47.858   0.751   0.073  1.00 37.94           C  
ANISOU  629  CB  PHE A  84     4991   4683   4742    452    871   -609       C  
ATOM    630  CG  PHE A  84      48.786   0.032  -0.849  1.00 35.59           C  
ANISOU  630  CG  PHE A  84     4665   4534   4322    612    959   -711       C  
ATOM    631  CD1 PHE A  84      49.749  -0.823  -0.351  1.00 39.01           C  
ANISOU  631  CD1 PHE A  84     5113   5083   4627   1025   1005   -762       C  
ATOM    632  CD2 PHE A  84      48.672   0.181  -2.218  1.00 36.64           C  
ANISOU  632  CD2 PHE A  84     4768   4704   4451    380   1001   -755       C  
ATOM    633  CE1 PHE A  84      50.608  -1.513  -1.205  1.00 42.86           C  
ANISOU  633  CE1 PHE A  84     5582   5727   4975   1228   1093   -863       C  
ATOM    634  CE2 PHE A  84      49.512  -0.498  -3.084  1.00 39.68           C  
ANISOU  634  CE2 PHE A  84     5127   5234   4717    530   1088   -860       C  
ATOM    635  CZ  PHE A  84      50.488  -1.350  -2.576  1.00 44.58           C  
ANISOU  635  CZ  PHE A  84     5762   5974   5202    968   1136   -919       C  
ATOM    636  N   TYR A  85      49.871   1.164   2.406  1.00 46.08           N  
ANISOU  636  N   TYR A  85     5634   6238   5635    930    765   -631       N  
ATOM    637  CA  TYR A  85      51.011   1.307   3.313  1.00 48.78           C  
ANISOU  637  CA  TYR A  85     5730   6954   5850   1155    731   -663       C  
ATOM    638  C   TYR A  85      51.623   0.032   3.906  1.00 54.23           C  
ANISOU  638  C   TYR A  85     6510   7692   6401   1670    785   -671       C  
ATOM    639  O   TYR A  85      52.651   0.107   4.600  1.00 54.24           O  
ANISOU  639  O   TYR A  85     6261   8096   6251   1900    760   -700       O  
ATOM    640  CB  TYR A  85      50.588   2.223   4.456  1.00 46.02           C  
ANISOU  640  CB  TYR A  85     5322   6572   5592    984    645   -594       C  
ATOM    641  CG  TYR A  85      50.357   3.644   4.013  1.00 46.33           C  
ANISOU  641  CG  TYR A  85     5254   6661   5689    547    599   -595       C  
ATOM    642  CD1 TYR A  85      49.157   4.023   3.431  1.00 46.65           C  
ANISOU  642  CD1 TYR A  85     5486   6367   5873    303    590   -533       C  
ATOM    643  CD2 TYR A  85      51.336   4.618   4.184  1.00 48.48           C  
ANISOU  643  CD2 TYR A  85     5257   7331   5833    375    575   -660       C  
ATOM    644  CE1 TYR A  85      48.937   5.327   3.022  1.00 45.51           C  
ANISOU  644  CE1 TYR A  85     5305   6234   5754    -40    557   -519       C  
ATOM    645  CE2 TYR A  85      51.121   5.926   3.784  1.00 47.97           C  
ANISOU  645  CE2 TYR A  85     5189   7250   5787    -35    552   -658       C  
ATOM    646  CZ  TYR A  85      49.921   6.270   3.196  1.00 45.20           C  
ANISOU  646  CZ  TYR A  85     5069   6514   5591   -210    543   -580       C  
ATOM    647  OH  TYR A  85      49.700   7.559   2.788  1.00 43.65           O  
ANISOU  647  OH  TYR A  85     4927   6271   5388   -557    528   -564       O  
ATOM    648  N   GLY A  86      51.013  -1.121   3.641  1.00 54.91           N  
ANISOU  648  N   GLY A  86     6968   7392   6502   1847    868   -648       N  
ATOM    649  CA  GLY A  86      51.484  -2.383   4.206  1.00 59.22           C  
ANISOU  649  CA  GLY A  86     7722   7882   6896   2363    937   -639       C  
ATOM    650  C   GLY A  86      52.186  -3.220   3.158  1.00 64.25           C  
ANISOU  650  C   GLY A  86     8434   8604   7372   2634   1048   -728       C  
ATOM    651  O   GLY A  86      52.942  -2.695   2.341  1.00 63.91           O  
ANISOU  651  O   GLY A  86     8073   8945   7266   2543   1038   -817       O  
ATOM    652  N   SER A  87      51.944  -4.527   3.188  1.00 69.35           N  
ANISOU  652  N   SER A  87     9532   8887   7930   2958   1163   -711       N  
ATOM    653  CA  SER A  87      52.461  -5.419   2.157  1.00 74.00           C  
ANISOU  653  CA  SER A  87    10296   9459   8364   3220   1294   -798       C  
ATOM    654  C   SER A  87      51.543  -5.380   0.937  1.00 73.50           C  
ANISOU  654  C   SER A  87    10408   9094   8424   2762   1356   -835       C  
ATOM    655  O   SER A  87      50.370  -5.017   1.039  1.00 71.07           O  
ANISOU  655  O   SER A  87    10219   8502   8283   2350   1322   -775       O  
ATOM    656  CB  SER A  87      52.594  -6.853   2.688  1.00 78.30           C  
ANISOU  656  CB  SER A  87    11341   9690   8720   3770   1417   -764       C  
ATOM    657  OG  SER A  87      51.337  -7.500   2.795  1.00 77.75           O  
ANISOU  657  OG  SER A  87    11816   9006   8721   3553   1497   -711       O  
ATOM    658  N   LYS A  88      52.086  -5.759  -0.215  1.00 76.62           N  
ANISOU  658  N   LYS A  88    10797   9599   8714   2850   1447   -937       N  
ATOM    659  CA  LYS A  88      51.304  -5.868  -1.442  1.00 75.40           C  
ANISOU  659  CA  LYS A  88    10821   9190   8636   2454   1527   -981       C  
ATOM    660  C   LYS A  88      50.112  -6.812  -1.234  1.00 73.64           C  
ANISOU  660  C   LYS A  88    11185   8380   8416   2352   1642   -931       C  
ATOM    661  O   LYS A  88      49.079  -6.644  -1.876  1.00 70.49           O  
ANISOU  661  O   LYS A  88    10888   7782   8112   1886   1668   -929       O  
ATOM    662  CB  LYS A  88      52.192  -6.377  -2.589  1.00 81.48           C  
ANISOU  662  CB  LYS A  88    11556  10154   9247   2668   1632  -1107       C  
ATOM    663  CG  LYS A  88      51.704  -6.022  -4.004  1.00 81.97           C  
ANISOU  663  CG  LYS A  88    11552  10192   9399   2186   1667  -1170       C  
ATOM    664  CD  LYS A  88      52.383  -4.757  -4.542  1.00 81.56           C  
ANISOU  664  CD  LYS A  88    10925  10669   9395   1947   1539  -1216       C  
ATOM    665  CE  LYS A  88      51.710  -4.240  -5.812  1.00 79.43           C  
ANISOU  665  CE  LYS A  88    10598  10344   9237   1420   1548  -1240       C  
ATOM    666  NZ  LYS A  88      52.340  -2.982  -6.318  1.00 76.76           N  
ANISOU  666  NZ  LYS A  88     9772  10473   8921   1155   1431  -1278       N  
ATOM    667  N   GLU A  89      50.261  -7.777  -0.321  1.00 76.28           N  
ANISOU  667  N   GLU A  89    11899   8472   8613   2774   1711   -892       N  
ATOM    668  CA  GLU A  89      49.244  -8.814  -0.054  1.00 78.21           C  
ANISOU  668  CA  GLU A  89    12786   8146   8785   2691   1846   -860       C  
ATOM    669  C   GLU A  89      48.169  -8.467   1.008  1.00 73.64           C  
ANISOU  669  C   GLU A  89    12274   7379   8325   2396   1755   -756       C  
ATOM    670  O   GLU A  89      47.067  -9.020   0.972  1.00 73.65           O  
ANISOU  670  O   GLU A  89    12697   7000   8287   2085   1847   -749       O  
ATOM    671  CB  GLU A  89      49.936 -10.128   0.345  1.00 84.94           C  
ANISOU  671  CB  GLU A  89    14129   8766   9379   3315   1994   -868       C  
ATOM    672  CG  GLU A  89      50.656 -10.851  -0.804  1.00 90.13           C  
ANISOU  672  CG  GLU A  89    14958   9427   9860   3585   2155   -985       C  
ATOM    673  CD  GLU A  89      52.024 -10.266  -1.138  1.00 92.36           C  
ANISOU  673  CD  GLU A  89    14652  10331  10112   3930   2063  -1044       C  
ATOM    674  OE1 GLU A  89      52.285 -10.002  -2.335  1.00 93.47           O  
ANISOU  674  OE1 GLU A  89    14568  10676  10271   3747   2090  -1145       O  
ATOM    675  OE2 GLU A  89      52.840 -10.083  -0.208  1.00 92.91           O  
ANISOU  675  OE2 GLU A  89    14474  10719  10110   4365   1969   -995       O  
ATOM    676  N   ASP A  90      48.500  -7.590   1.957  1.00 68.69           N  
ANISOU  676  N   ASP A  90    11244   7044   7811   2480   1585   -688       N  
ATOM    677  CA  ASP A  90      47.542  -7.093   2.961  1.00 63.28           C  
ANISOU  677  CA  ASP A  90    10538   6252   7252   2204   1479   -598       C  
ATOM    678  C   ASP A  90      47.704  -5.564   3.048  1.00 59.52           C  
ANISOU  678  C   ASP A  90     9456   6189   6971   1979   1299   -577       C  
ATOM    679  O   ASP A  90      48.128  -5.021   4.077  1.00 57.54           O  
ANISOU  679  O   ASP A  90     8959   6141   6761   2131   1187   -525       O  
ATOM    680  CB  ASP A  90      47.778  -7.778   4.317  1.00 66.78           C  
ANISOU  680  CB  ASP A  90    11255   6533   7585   2602   1484   -526       C  
ATOM    681  CG  ASP A  90      46.921  -7.189   5.453  1.00 66.83           C  
ANISOU  681  CG  ASP A  90    11174   6498   7722   2346   1358   -440       C  
ATOM    682  OD1 ASP A  90      45.690  -7.026   5.278  1.00 63.98           O  
ANISOU  682  OD1 ASP A  90    10924   5957   7429   1882   1358   -436       O  
ATOM    683  OD2 ASP A  90      47.491  -6.896   6.533  1.00 65.86           O  
ANISOU  683  OD2 ASP A  90    10851   6561   7610   2619   1261   -382       O  
ATOM    684  N   PRO A  91      47.387  -4.864   1.944  1.00 56.01           N  
ANISOU  684  N   PRO A  91     8796   5863   6621   1610   1282   -617       N  
ATOM    685  CA  PRO A  91      47.607  -3.428   1.857  1.00 52.24           C  
ANISOU  685  CA  PRO A  91     7831   5733   6284   1396   1140   -604       C  
ATOM    686  C   PRO A  91      46.680  -2.614   2.744  1.00 47.23           C  
ANISOU  686  C   PRO A  91     7116   5044   5786   1148   1026   -517       C  
ATOM    687  O   PRO A  91      45.472  -2.786   2.676  1.00 40.90           O  
ANISOU  687  O   PRO A  91     6519   4008   5013    889   1047   -486       O  
ATOM    688  CB  PRO A  91      47.315  -3.125   0.383  1.00 51.58           C  
ANISOU  688  CB  PRO A  91     7675   5691   6230   1076   1181   -657       C  
ATOM    689  CG  PRO A  91      46.401  -4.195  -0.051  1.00 51.90           C  
ANISOU  689  CG  PRO A  91     8151   5373   6196    961   1317   -673       C  
ATOM    690  CD  PRO A  91      46.886  -5.407   0.666  1.00 56.15           C  
ANISOU  690  CD  PRO A  91     9044   5705   6587   1383   1411   -682       C  
ATOM    691  N   GLN A  92      47.264  -1.723   3.542  1.00 48.99           N  
ANISOU  691  N   GLN A  92     7029   5522   6062   1217    913   -489       N  
ATOM    692  CA  GLN A  92      46.522  -0.859   4.454  1.00 50.79           C  
ANISOU  692  CA  GLN A  92     7164   5722   6410   1022    806   -415       C  
ATOM    693  C   GLN A  92      46.392   0.560   3.887  1.00 49.07           C  
ANISOU  693  C   GLN A  92     6671   5686   6289    705    730   -411       C  
ATOM    694  O   GLN A  92      47.392   1.228   3.623  1.00 51.78           O  
ANISOU  694  O   GLN A  92     6756   6318   6601    708    704   -455       O  
ATOM    695  CB  GLN A  92      47.213  -0.809   5.822  1.00 54.64           C  
ANISOU  695  CB  GLN A  92     7541   6348   6870   1291    747   -386       C  
ATOM    696  CG  GLN A  92      47.485  -2.174   6.460  1.00 57.92           C  
ANISOU  696  CG  GLN A  92     8253   6597   7157   1678    820   -374       C  
ATOM    697  CD  GLN A  92      46.238  -3.028   6.580  1.00 60.42           C  
ANISOU  697  CD  GLN A  92     9000   6489   7466   1555    883   -340       C  
ATOM    698  OE1 GLN A  92      45.135  -2.516   6.761  1.00 61.01           O  
ANISOU  698  OE1 GLN A  92     9078   6465   7640   1232    830   -306       O  
ATOM    699  NE2 GLN A  92      46.409  -4.340   6.480  1.00 65.46           N  
ANISOU  699  NE2 GLN A  92    10026   6894   7951   1811   1006   -357       N  
ATOM    700  N   THR A  93      45.155   1.014   3.714  1.00 44.94           N  
ANISOU  700  N   THR A  93     6220   5010   5846    435    701   -360       N  
ATOM    701  CA  THR A  93      44.857   2.313   3.142  1.00 43.80           C  
ANISOU  701  CA  THR A  93     5906   4971   5767    172    641   -335       C  
ATOM    702  C   THR A  93      44.260   3.223   4.193  1.00 41.25           C  
ANISOU  702  C   THR A  93     5535   4619   5518    104    549   -267       C  
ATOM    703  O   THR A  93      44.678   4.360   4.339  1.00 42.66           O  
ANISOU  703  O   THR A  93     5564   4926   5719     15    497   -259       O  
ATOM    704  CB  THR A  93      43.850   2.193   1.992  1.00 46.63           C  
ANISOU  704  CB  THR A  93     6369   5231   6117    -46    685   -323       C  
ATOM    705  OG1 THR A  93      44.450   1.478   0.904  1.00 52.88           O  
ANISOU  705  OG1 THR A  93     7195   6060   6839    -19    778   -397       O  
ATOM    706  CG2 THR A  93      43.438   3.574   1.505  1.00 47.78           C  
ANISOU  706  CG2 THR A  93     6385   5463   6307   -261    620   -271       C  
ATOM    707  N   PHE A  94      43.262   2.720   4.905  1.00 41.03           N  
ANISOU  707  N   PHE A  94     5663   4422   5505    120    539   -225       N  
ATOM    708  CA  PHE A  94      42.612   3.468   5.964  1.00 41.82           C  
ANISOU  708  CA  PHE A  94     5727   4497   5665     80    455   -168       C  
ATOM    709  C   PHE A  94      43.330   3.220   7.266  1.00 47.51           C  
ANISOU  709  C   PHE A  94     6410   5249   6393    274    427   -174       C  
ATOM    710  O   PHE A  94      44.120   2.281   7.381  1.00 52.83           O  
ANISOU  710  O   PHE A  94     7130   5939   7006    475    477   -209       O  
ATOM    711  CB  PHE A  94      41.157   3.013   6.124  1.00 39.99           C  
ANISOU  711  CB  PHE A  94     5649   4140   5406    -18    455   -134       C  
ATOM    712  CG  PHE A  94      40.334   3.185   4.894  1.00 38.28           C  
ANISOU  712  CG  PHE A  94     5445   3957   5141   -204    485   -123       C  
ATOM    713  CD1 PHE A  94      40.246   2.174   3.963  1.00 40.13           C  
ANISOU  713  CD1 PHE A  94     5808   4148   5292   -272    583   -168       C  
ATOM    714  CD2 PHE A  94      39.652   4.361   4.659  1.00 40.40           C  
ANISOU  714  CD2 PHE A  94     5615   4309   5425   -297    425    -66       C  
ATOM    715  CE1 PHE A  94      39.487   2.330   2.819  1.00 40.59           C  
ANISOU  715  CE1 PHE A  94     5850   4288   5285   -463    614   -160       C  
ATOM    716  CE2 PHE A  94      38.890   4.526   3.515  1.00 40.45           C  
ANISOU  716  CE2 PHE A  94     5614   4398   5358   -436    450    -44       C  
ATOM    717  CZ  PHE A  94      38.810   3.512   2.597  1.00 40.91           C  
ANISOU  717  CZ  PHE A  94     5753   4454   5337   -536    541    -92       C  
ATOM    718  N   TYR A  95      43.045   4.070   8.247  1.00 49.62           N  
ANISOU  718  N   TYR A  95     6602   5536   6716    234    353   -137       N  
ATOM    719  CA  TYR A  95      43.365   3.778   9.635  1.00 49.51           C  
ANISOU  719  CA  TYR A  95     6570   5536   6707    386    320   -128       C  
ATOM    720  C   TYR A  95      42.230   4.211  10.523  1.00 51.23           C  
ANISOU  720  C   TYR A  95     6830   5659   6977    299    255    -82       C  
ATOM    721  O   TYR A  95      41.669   5.286  10.343  1.00 56.34           O  
ANISOU  721  O   TYR A  95     7432   6314   7660    163    219    -59       O  
ATOM    722  CB  TYR A  95      44.649   4.463  10.074  1.00 50.13           C  
ANISOU  722  CB  TYR A  95     6433   5851   6763    433    303   -160       C  
ATOM    723  CG  TYR A  95      44.683   5.959   9.914  1.00 46.55           C  
ANISOU  723  CG  TYR A  95     5880   5474   6335    210    275   -162       C  
ATOM    724  CD1 TYR A  95      44.337   6.802  10.962  1.00 49.36           C  
ANISOU  724  CD1 TYR A  95     6217   5807   6729    138    226   -137       C  
ATOM    725  CD2 TYR A  95      45.109   6.530   8.740  1.00 46.31           C  
ANISOU  725  CD2 TYR A  95     5808   5523   6265     69    308   -193       C  
ATOM    726  CE1 TYR A  95      44.399   8.187  10.825  1.00 48.13           C  
ANISOU  726  CE1 TYR A  95     6054   5671   6562    -62    224   -141       C  
ATOM    727  CE2 TYR A  95      45.173   7.906   8.594  1.00 47.22           C  
ANISOU  727  CE2 TYR A  95     5912   5664   6365   -145    299   -192       C  
ATOM    728  CZ  TYR A  95      44.811   8.722   9.630  1.00 46.44           C  
ANISOU  728  CZ  TYR A  95     5846   5505   6293   -204    264   -166       C  
ATOM    729  OH  TYR A  95      44.868  10.076   9.461  1.00 47.79           O  
ANISOU  729  OH  TYR A  95     6092   5648   6418   -412    278   -166       O  
ATOM    730  N   TYR A  96      41.904   3.363  11.488  1.00 52.85           N  
ANISOU  730  N   TYR A  96     7142   5775   7163    398    245    -67       N  
ATOM    731  CA  TYR A  96      40.821   3.608  12.431  1.00 48.26           C  
ANISOU  731  CA  TYR A  96     6593   5136   6606    320    182    -36       C  
ATOM    732  C   TYR A  96      41.309   4.543  13.538  1.00 43.30           C  
ANISOU  732  C   TYR A  96     5801   4611   6039    349    122    -28       C  
ATOM    733  O   TYR A  96      42.402   4.350  14.071  1.00 39.17           O  
ANISOU  733  O   TYR A  96     5191   4191   5499    479    129    -41       O  
ATOM    734  CB  TYR A  96      40.373   2.296  13.065  1.00 48.73           C  
ANISOU  734  CB  TYR A  96     6861   5062   6592    376    203    -32       C  
ATOM    735  CG  TYR A  96      39.787   1.264  12.123  1.00 51.36           C  
ANISOU  735  CG  TYR A  96     7425   5270   6819    289    286    -54       C  
ATOM    736  CD1 TYR A  96      40.574   0.597  11.182  1.00 52.75           C  
ANISOU  736  CD1 TYR A  96     7697   5397   6949    387    375    -82       C  
ATOM    737  CD2 TYR A  96      38.448   0.911  12.219  1.00 54.34           C  
ANISOU  737  CD2 TYR A  96     7932   5607   7109     90    286    -59       C  
ATOM    738  CE1 TYR A  96      40.023  -0.369  10.338  1.00 55.02           C  
ANISOU  738  CE1 TYR A  96     8235   5551   7120    274    472   -113       C  
ATOM    739  CE2 TYR A  96      37.891  -0.052  11.396  1.00 57.63           C  
ANISOU  739  CE2 TYR A  96     8577   5935   7384    -56    380    -93       C  
ATOM    740  CZ  TYR A  96      38.680  -0.693  10.456  1.00 58.44           C  
ANISOU  740  CZ  TYR A  96     8808   5941   7455     31    479   -119       C  
ATOM    741  OH  TYR A  96      38.103  -1.644   9.639  1.00 61.64           O  
ANISOU  741  OH  TYR A  96     9474   6245   7702   -150    591   -163       O  
ATOM    742  N   ALA A  97      40.508   5.553  13.879  1.00 39.45           N  
ANISOU  742  N   ALA A  97     5273   4123   5593    238     70    -10       N  
ATOM    743  CA  ALA A  97      40.814   6.411  15.025  1.00 38.21           C  
ANISOU  743  CA  ALA A  97     5010   4032   5478    234     27    -10       C  
ATOM    744  C   ALA A  97      40.330   5.739  16.314  1.00 35.17           C  
ANISOU  744  C   ALA A  97     4654   3616   5093    291    -19      2       C  
ATOM    745  O   ALA A  97      39.188   5.259  16.387  1.00 28.57           O  
ANISOU  745  O   ALA A  97     3920   2709   4226    246    -41     13       O  
ATOM    746  CB  ALA A  97      40.171   7.770  14.864  1.00 37.20           C  
ANISOU  746  CB  ALA A  97     4886   3879   5368    129      6      2       C  
ATOM    747  N   VAL A  98      41.198   5.709  17.325  1.00 32.61           N  
ANISOU  747  N   VAL A  98     4231   3386   4774    367    -32     -3       N  
ATOM    748  CA  VAL A  98      40.846   5.099  18.612  1.00 32.18           C  
ANISOU  748  CA  VAL A  98     4205   3311   4713    422    -77     15       C  
ATOM    749  C   VAL A  98      41.202   5.990  19.785  1.00 29.50           C  
ANISOU  749  C   VAL A  98     3707   3093   4407    382   -114      5       C  
ATOM    750  O   VAL A  98      42.027   6.892  19.663  1.00 34.48           O  
ANISOU  750  O   VAL A  98     4216   3850   5037    323    -86    -22       O  
ATOM    751  CB  VAL A  98      41.548   3.743  18.812  1.00 33.48           C  
ANISOU  751  CB  VAL A  98     4457   3460   4802    617    -46     34       C  
ATOM    752  CG1 VAL A  98      41.069   2.731  17.766  1.00 30.37           C  
ANISOU  752  CG1 VAL A  98     4295   2895   4347    628     10     35       C  
ATOM    753  CG2 VAL A  98      43.067   3.914  18.778  1.00 34.03           C  
ANISOU  753  CG2 VAL A  98     4349   3749   4834    756    -13     21       C  
ATOM    754  N   ALA A  99      40.553   5.733  20.917  1.00 25.23           N  
ANISOU  754  N   ALA A  99     3185   2526   3875    375   -168     19       N  
ATOM    755  CA  ALA A  99      40.894   6.379  22.184  1.00 22.88           C  
ANISOU  755  CA  ALA A  99     2742   2352   3600    339   -200      8       C  
ATOM    756  C   ALA A  99      41.421   5.278  23.095  1.00 26.42           C  
ANISOU  756  C   ALA A  99     3183   2862   3994    490   -217     42       C  
ATOM    757  O   ALA A  99      40.668   4.420  23.561  1.00 27.60           O  
ANISOU  757  O   ALA A  99     3474   2893   4118    513   -251     67       O  
ATOM    758  CB  ALA A  99      39.689   7.068  22.799  1.00 15.19           C  
ANISOU  758  CB  ALA A  99     1787   1319   2667    223   -252     -7       C  
ATOM    759  N   VAL A 100      42.727   5.287  23.316  1.00 29.60           N  
ANISOU  759  N   VAL A 100     3429   3476   4341    593   -186     41       N  
ATOM    760  CA  VAL A 100      43.371   4.257  24.112  1.00 33.38           C  
ANISOU  760  CA  VAL A 100     3896   4056   4731    813   -195     89       C  
ATOM    761  C   VAL A 100      43.305   4.684  25.573  1.00 33.69           C  
ANISOU  761  C   VAL A 100     3794   4226   4783    734   -246     91       C  
ATOM    762  O   VAL A 100      43.269   5.879  25.858  1.00 38.23           O  
ANISOU  762  O   VAL A 100     4228   4892   5406    530   -247     41       O  
ATOM    763  CB  VAL A 100      44.833   4.071  23.670  1.00 35.39           C  
ANISOU  763  CB  VAL A 100     3995   4579   4872   1001   -140     84       C  
ATOM    764  CG1 VAL A 100      45.492   2.945  24.454  1.00 38.45           C  
ANISOU  764  CG1 VAL A 100     4395   5087   5129   1320   -145    150       C  
ATOM    765  CG2 VAL A 100      44.908   3.800  22.164  1.00 32.61           C  
ANISOU  765  CG2 VAL A 100     3762   4112   4516   1044    -86     66       C  
ATOM    766  N   VAL A 101      43.256   3.719  26.488  1.00 29.77           N  
ANISOU  766  N   VAL A 101     3372   3712   4226    886   -281    149       N  
ATOM    767  CA  VAL A 101      43.405   4.011  27.914  1.00 29.17           C  
ANISOU  767  CA  VAL A 101     3129   3816   4138    841   -326    158       C  
ATOM    768  C   VAL A 101      44.022   2.868  28.673  1.00 34.30           C  
ANISOU  768  C   VAL A 101     3818   4561   4655   1127   -337    240       C  
ATOM    769  O   VAL A 101      44.020   1.724  28.224  1.00 36.47           O  
ANISOU  769  O   VAL A 101     4351   4654   4851   1352   -313    295       O  
ATOM    770  CB  VAL A 101      42.078   4.272  28.618  1.00 27.25           C  
ANISOU  770  CB  VAL A 101     2971   3400   3983    634   -390    140       C  
ATOM    771  CG1 VAL A 101      41.560   5.668  28.299  1.00 24.69           C  
ANISOU  771  CG1 VAL A 101     2561   3061   3761    392   -383     63       C  
ATOM    772  CG2 VAL A 101      41.085   3.175  28.276  1.00 27.57           C  
ANISOU  772  CG2 VAL A 101     3325   3154   3995    666   -407    171       C  
ATOM    773  N   LYS A 102      44.520   3.197  29.859  1.00 37.94           N  
ANISOU  773  N   LYS A 102     4046   5298   5070   1116   -365    251       N  
ATOM    774  CA  LYS A 102      45.032   2.200  30.779  1.00 42.56           C  
ANISOU  774  CA  LYS A 102     4657   6001   5513   1398   -386    343       C  
ATOM    775  C   LYS A 102      43.900   1.278  31.222  1.00 41.97           C  
ANISOU  775  C   LYS A 102     4938   5557   5453   1388   -432    394       C  
ATOM    776  O   LYS A 102      42.774   1.727  31.426  1.00 41.72           O  
ANISOU  776  O   LYS A 102     4959   5355   5537   1095   -475    343       O  
ATOM    777  CB  LYS A 102      45.666   2.873  31.997  1.00 44.29           C  
ANISOU  777  CB  LYS A 102     4523   6625   5680   1319   -408    334       C  
ATOM    778  CG  LYS A 102      46.966   3.631  31.715  1.00 45.49           C  
ANISOU  778  CG  LYS A 102     4314   7247   5722   1313   -348    281       C  
ATOM    779  CD  LYS A 102      48.173   2.703  31.638  1.00 49.87           C  
ANISOU  779  CD  LYS A 102     4780   8124   6045   1757   -320    358       C  
ATOM    780  CE  LYS A 102      49.480   3.457  31.899  1.00 53.38           C  
ANISOU  780  CE  LYS A 102     4760   9217   6303   1704   -276    302       C  
ATOM    781  NZ  LYS A 102      49.641   3.860  33.335  1.00 54.26           N  
ANISOU  781  NZ  LYS A 102     4618   9645   6351   1562   -305    308       N  
ATOM    782  N   LYS A 103      44.215  -0.007  31.360  1.00 43.72           N  
ANISOU  782  N   LYS A 103     5421   5673   5519   1714   -414    490       N  
ATOM    783  CA  LYS A 103      43.261  -1.006  31.809  1.00 43.23           C  
ANISOU  783  CA  LYS A 103     5765   5259   5403   1688   -438    540       C  
ATOM    784  C   LYS A 103      42.750  -0.684  33.210  1.00 41.24           C  
ANISOU  784  C   LYS A 103     5386   5101   5182   1485   -521    543       C  
ATOM    785  O   LYS A 103      43.535  -0.420  34.119  1.00 41.65           O  
ANISOU  785  O   LYS A 103     5162   5478   5185   1600   -545    581       O  
ATOM    786  CB  LYS A 103      43.915  -2.389  31.799  1.00 51.42           C  
ANISOU  786  CB  LYS A 103     7142   6175   6221   2127   -384    655       C  
ATOM    787  CG  LYS A 103      42.976  -3.524  32.207  1.00 57.20           C  
ANISOU  787  CG  LYS A 103     8404   6490   6839   2074   -382    706       C  
ATOM    788  CD  LYS A 103      43.099  -4.725  31.270  1.00 62.52           C  
ANISOU  788  CD  LYS A 103     9593   6814   7348   2332   -275    750       C  
ATOM    789  CE  LYS A 103      42.004  -5.755  31.512  1.00 65.27           C  
ANISOU  789  CE  LYS A 103    10527   6712   7559   2135   -248    766       C  
ATOM    790  NZ  LYS A 103      42.385  -6.719  32.584  1.00 70.07           N  
ANISOU  790  NZ  LYS A 103    11454   7223   7947   2438   -244    897       N  
ATOM    791  N   ASP A 104      41.428  -0.687  33.360  1.00 39.79           N  
ANISOU  791  N   ASP A 104     5379   4680   5060   1168   -562    494       N  
ATOM    792  CA  ASP A 104      40.758  -0.560  34.661  1.00 39.36           C  
ANISOU  792  CA  ASP A 104     5270   4673   5011    957   -643    489       C  
ATOM    793  C   ASP A 104      40.921   0.804  35.330  1.00 38.04           C  
ANISOU  793  C   ASP A 104     4646   4827   4983    777   -687    421       C  
ATOM    794  O   ASP A 104      41.080   0.906  36.539  1.00 39.90           O  
ANISOU  794  O   ASP A 104     4728   5242   5191    747   -735    446       O  
ATOM    795  CB  ASP A 104      41.170  -1.716  35.606  1.00 42.11           C  
ANISOU  795  CB  ASP A 104     5855   4975   5168   1203   -652    613       C  
ATOM    796  CG  ASP A 104      40.589  -3.076  35.172  1.00 45.22           C  
ANISOU  796  CG  ASP A 104     6842   4947   5394   1248   -603    659       C  
ATOM    797  OD1 ASP A 104      41.047  -4.115  35.697  1.00 47.25           O  
ANISOU  797  OD1 ASP A 104     7403   5092   5457   1528   -580    775       O  
ATOM    798  OD2 ASP A 104      39.673  -3.110  34.311  1.00 42.26           O  
ANISOU  798  OD2 ASP A 104     6650   4358   5050    999   -577    579       O  
ATOM    799  N   SER A 105      40.855   1.859  34.529  1.00 39.88           N  
ANISOU  799  N   SER A 105     4696   5111   5346    642   -660    333       N  
ATOM    800  CA  SER A 105      40.793   3.235  35.039  1.00 35.35           C  
ANISOU  800  CA  SER A 105     3797   4747   4887    416   -677    248       C  
ATOM    801  C   SER A 105      39.333   3.687  35.195  1.00 30.72           C  
ANISOU  801  C   SER A 105     3272   4018   4381    142   -730    166       C  
ATOM    802  O   SER A 105      39.055   4.839  35.510  1.00 26.81           O  
ANISOU  802  O   SER A 105     2588   3626   3974    -30   -736     87       O  
ATOM    803  CB  SER A 105      41.564   4.177  34.118  1.00 35.04           C  
ANISOU  803  CB  SER A 105     3581   4834   4900    421   -605    199       C  
ATOM    804  OG  SER A 105      41.373   3.835  32.756  1.00 36.86           O  
ANISOU  804  OG  SER A 105     4011   4851   5143    501   -566    200       O  
ATOM    805  N   GLY A 106      38.400   2.769  34.976  1.00 29.32           N  
ANISOU  805  N   GLY A 106     3376   3626   4137    103   -758    180       N  
ATOM    806  CA  GLY A 106      37.033   2.952  35.427  1.00 27.99           C  
ANISOU  806  CA  GLY A 106     3236   3432   3968   -148   -823    107       C  
ATOM    807  C   GLY A 106      36.347   4.169  34.867  1.00 29.40           C  
ANISOU  807  C   GLY A 106     3273   3653   4246   -272   -819      8       C  
ATOM    808  O   GLY A 106      35.714   4.906  35.606  1.00 34.19           O  
ANISOU  808  O   GLY A 106     3731   4375   4886   -413   -864    -60       O  
ATOM    809  N   PHE A 107      36.470   4.390  33.564  1.00 31.93           N  
ANISOU  809  N   PHE A 107     3654   3880   4599   -197   -761      3       N  
ATOM    810  CA  PHE A 107      35.645   5.384  32.903  1.00 29.25           C  
ANISOU  810  CA  PHE A 107     3257   3549   4308   -276   -757    -74       C  
ATOM    811  C   PHE A 107      35.412   5.063  31.437  1.00 33.17           C  
ANISOU  811  C   PHE A 107     3910   3920   4773   -225   -711    -64       C  
ATOM    812  O   PHE A 107      36.192   4.340  30.817  1.00 36.49           O  
ANISOU  812  O   PHE A 107     4452   4237   5176   -107   -662     -5       O  
ATOM    813  CB  PHE A 107      36.261   6.762  33.045  1.00 28.23           C  
ANISOU  813  CB  PHE A 107     2942   3500   4284   -264   -717   -109       C  
ATOM    814  CG  PHE A 107      37.533   6.927  32.306  1.00 28.94           C  
ANISOU  814  CG  PHE A 107     3013   3576   4407   -155   -639    -71       C  
ATOM    815  CD1 PHE A 107      37.533   7.350  30.988  1.00 34.46           C  
ANISOU  815  CD1 PHE A 107     3787   4176   5129   -112   -585    -81       C  
ATOM    816  CD2 PHE A 107      38.734   6.689  32.922  1.00 28.86           C  
ANISOU  816  CD2 PHE A 107     2888   3700   4379    -96   -618    -30       C  
ATOM    817  CE1 PHE A 107      38.728   7.516  30.300  1.00 33.49           C  
ANISOU  817  CE1 PHE A 107     3634   4078   5015    -40   -513    -59       C  
ATOM    818  CE2 PHE A 107      39.922   6.852  32.245  1.00 29.54           C  
ANISOU  818  CE2 PHE A 107     2915   3858   4451     -6   -546    -10       C  
ATOM    819  CZ  PHE A 107      39.922   7.261  30.936  1.00 30.73           C  
ANISOU  819  CZ  PHE A 107     3149   3898   4629      8   -494    -29       C  
ATOM    820  N   GLN A 108      34.335   5.628  30.899  1.00 31.52           N  
ANISOU  820  N   GLN A 108     3686   3750   4540   -294   -725   -123       N  
ATOM    821  CA  GLN A 108      33.917   5.396  29.531  1.00 30.36           C  
ANISOU  821  CA  GLN A 108     3658   3539   4340   -277   -687   -122       C  
ATOM    822  C   GLN A 108      33.931   6.681  28.704  1.00 30.73           C  
ANISOU  822  C   GLN A 108     3621   3592   4461   -190   -650   -142       C  
ATOM    823  O   GLN A 108      34.283   7.758  29.202  1.00 27.89           O  
ANISOU  823  O   GLN A 108     3155   3257   4184   -158   -641   -162       O  
ATOM    824  CB  GLN A 108      32.511   4.803  29.531  1.00 31.54           C  
ANISOU  824  CB  GLN A 108     3872   3795   4316   -444   -732   -172       C  
ATOM    825  CG  GLN A 108      32.400   3.472  30.232  1.00 32.16           C  
ANISOU  825  CG  GLN A 108     4127   3822   4269   -581   -751   -157       C  
ATOM    826  CD  GLN A 108      33.275   2.399  29.615  1.00 33.90           C  
ANISOU  826  CD  GLN A 108     4602   3810   4466   -497   -677    -84       C  
ATOM    827  OE1 GLN A 108      33.652   1.440  30.285  1.00 36.65           O  
ANISOU  827  OE1 GLN A 108     5133   4047   4746   -500   -675    -39       O  
ATOM    828  NE2 GLN A 108      33.608   2.556  28.338  1.00 30.85           N  
ANISOU  828  NE2 GLN A 108     4250   3349   4122   -400   -613    -70       N  
ATOM    829  N   MET A 109      33.554   6.545  27.432  1.00 31.34           N  
ANISOU  829  N   MET A 109     3782   3638   4487   -168   -616   -136       N  
ATOM    830  CA  MET A 109      33.518   7.661  26.497  1.00 34.47           C  
ANISOU  830  CA  MET A 109     4155   4020   4923    -72   -577   -139       C  
ATOM    831  C   MET A 109      32.706   8.807  27.080  1.00 33.42           C  
ANISOU  831  C   MET A 109     3930   4001   4769    -33   -612   -187       C  
ATOM    832  O   MET A 109      33.152   9.954  27.087  1.00 34.81           O  
ANISOU  832  O   MET A 109     4112   4100   5014     43   -570   -190       O  
ATOM    833  CB  MET A 109      32.903   7.226  25.157  1.00 40.01           C  
ANISOU  833  CB  MET A 109     4937   4739   5524    -77   -553   -129       C  
ATOM    834  CG  MET A 109      33.354   8.067  23.968  1.00 42.60           C  
ANISOU  834  CG  MET A 109     5296   4982   5909     33   -492   -101       C  
ATOM    835  SD  MET A 109      34.959   7.531  23.334  1.00 42.71           S  
ANISOU  835  SD  MET A 109     5382   4822   6022     55   -419    -57       S  
ATOM    836  CE  MET A 109      35.719   9.102  22.952  1.00 44.43           C  
ANISOU  836  CE  MET A 109     5584   4976   6322    113   -365    -55       C  
ATOM    837  N   ASN A 110      31.522   8.484  27.593  1.00 31.54           N  
ANISOU  837  N   ASN A 110     3626   3952   4404    -95   -679   -232       N  
ATOM    838  CA  ASN A 110      30.657   9.491  28.188  1.00 29.28           C  
ANISOU  838  CA  ASN A 110     3243   3819   4063    -16   -716   -287       C  
ATOM    839  C   ASN A 110      31.095   9.924  29.580  1.00 26.80           C  
ANISOU  839  C   ASN A 110     2865   3477   3843    -56   -734   -317       C  
ATOM    840  O   ASN A 110      30.317  10.527  30.300  1.00 31.14           O  
ANISOU  840  O   ASN A 110     3331   4170   4329    -17   -772   -376       O  
ATOM    841  CB  ASN A 110      29.198   9.030  28.203  1.00 30.80           C  
ANISOU  841  CB  ASN A 110     3341   4322   4039    -74   -783   -341       C  
ATOM    842  CG  ASN A 110      28.988   7.784  29.015  1.00 32.86           C  
ANISOU  842  CG  ASN A 110     3593   4666   4226   -316   -835   -369       C  
ATOM    843  OD1 ASN A 110      29.928   7.232  29.582  1.00 38.73           O  
ANISOU  843  OD1 ASN A 110     4409   5220   5086   -390   -825   -333       O  
ATOM    844  ND2 ASN A 110      27.751   7.322  29.070  1.00 29.74           N  
ANISOU  844  ND2 ASN A 110     3119   4584   3599   -443   -885   -434       N  
ATOM    845  N   GLN A 111      32.334   9.621  29.955  1.00 26.14           N  
ANISOU  845  N   GLN A 111     2803   3245   3883   -123   -702   -280       N  
ATOM    846  CA  GLN A 111      32.943  10.193  31.154  1.00 25.41           C  
ANISOU  846  CA  GLN A 111     2639   3143   3872   -171   -695   -305       C  
ATOM    847  C   GLN A 111      34.308  10.822  30.882  1.00 21.82           C  
ANISOU  847  C   GLN A 111     2229   2548   3514   -167   -602   -279       C  
ATOM    848  O   GLN A 111      35.046  11.130  31.807  1.00 21.19           O  
ANISOU  848  O   GLN A 111     2078   2496   3478   -253   -580   -296       O  
ATOM    849  CB  GLN A 111      33.051   9.135  32.254  1.00 27.12           C  
ANISOU  849  CB  GLN A 111     2780   3444   4079   -301   -760   -299       C  
ATOM    850  CG  GLN A 111      31.710   8.752  32.855  1.00 29.39           C  
ANISOU  850  CG  GLN A 111     3007   3919   4241   -382   -848   -356       C  
ATOM    851  CD  GLN A 111      31.799   7.526  33.729  1.00 31.74           C  
ANISOU  851  CD  GLN A 111     3310   4256   4493   -534   -904   -336       C  
ATOM    852  OE1 GLN A 111      32.500   6.568  33.399  1.00 30.73           O  
ANISOU  852  OE1 GLN A 111     3304   4002   4370   -535   -880   -266       O  
ATOM    853  NE2 GLN A 111      31.084   7.545  34.857  1.00 34.41           N  
ANISOU  853  NE2 GLN A 111     3541   4766   4768   -648   -975   -398       N  
ATOM    854  N   LEU A 112      34.629  11.072  29.623  1.00 22.35           N  
ANISOU  854  N   LEU A 112     2403   2504   3586    -95   -543   -247       N  
ATOM    855  CA  LEU A 112      35.851  11.812  29.310  1.00 24.99           C  
ANISOU  855  CA  LEU A 112     2787   2744   3964   -136   -446   -242       C  
ATOM    856  C   LEU A 112      35.943  13.194  29.964  1.00 28.39           C  
ANISOU  856  C   LEU A 112     3278   3125   4383   -195   -382   -303       C  
ATOM    857  O   LEU A 112      37.053  13.692  30.160  1.00 38.13           O  
ANISOU  857  O   LEU A 112     4518   4351   5618   -330   -300   -322       O  
ATOM    858  CB  LEU A 112      36.040  11.957  27.797  1.00 24.09           C  
ANISOU  858  CB  LEU A 112     2798   2518   3838    -63   -394   -206       C  
ATOM    859  CG  LEU A 112      36.485  10.687  27.072  1.00 22.46           C  
ANISOU  859  CG  LEU A 112     2564   2329   3642    -41   -410   -154       C  
ATOM    860  CD1 LEU A 112      36.645  10.957  25.593  1.00 20.65           C  
ANISOU  860  CD1 LEU A 112     2446   2001   3398     11   -355   -129       C  
ATOM    861  CD2 LEU A 112      37.794  10.158  27.663  1.00 26.20           C  
ANISOU  861  CD2 LEU A 112     2928   2887   4140    -95   -392   -141       C  
ATOM    862  N   ARG A 113      34.822  13.823  30.303  1.00 32.35           N  
ANISOU  862  N   ARG A 113     4143   4209   3941   -375    245  -1062       N  
ATOM    863  CA  ARG A 113      34.895  15.153  30.918  1.00 34.87           C  
ANISOU  863  CA  ARG A 113     4467   4410   4373   -326    416  -1230       C  
ATOM    864  C   ARG A 113      35.685  15.111  32.215  1.00 37.05           C  
ANISOU  864  C   ARG A 113     4895   4674   4508   -454    367  -1419       C  
ATOM    865  O   ARG A 113      35.496  14.208  33.021  1.00 43.66           O  
ANISOU  865  O   ARG A 113     5812   5651   5127   -553    309  -1439       O  
ATOM    866  CB  ARG A 113      33.513  15.729  31.195  1.00 35.29           C  
ANISOU  866  CB  ARG A 113     4417   4532   4460   -191    606  -1245       C  
ATOM    867  CG  ARG A 113      33.540  17.222  31.417  1.00 35.33           C  
ANISOU  867  CG  ARG A 113     4513   4319   4589    -31    738  -1405       C  
ATOM    868  CD  ARG A 113      32.138  17.809  31.457  1.00 39.95           C  
ANISOU  868  CD  ARG A 113     4962   4994   5223    230    924  -1411       C  
ATOM    869  NE  ARG A 113      31.455  17.524  32.714  1.00 43.27           N  
ANISOU  869  NE  ARG A 113     5342   5665   5434    256   1099  -1509       N  
ATOM    870  CZ  ARG A 113      30.225  17.934  33.013  1.00 48.74           C  
ANISOU  870  CZ  ARG A 113     5848   6554   6116    513   1323  -1526       C  
ATOM    871  NH1 ARG A 113      29.525  18.657  32.142  1.00 49.68           N  
ANISOU  871  NH1 ARG A 113     5814   6614   6447    788   1346  -1467       N  
ATOM    872  NH2 ARG A 113      29.691  17.622  34.194  1.00 51.37           N  
ANISOU  872  NH2 ARG A 113     6144   7167   6208    519   1533  -1596       N  
ATOM    873  N   GLY A 114      36.574  16.082  32.401  1.00 37.67           N  
ANISOU  873  N   GLY A 114     5048   4565   4702   -485    349  -1538       N  
ATOM    874  CA  GLY A 114      37.423  16.140  33.584  1.00 39.39           C  
ANISOU  874  CA  GLY A 114     5432   4729   4806   -623    227  -1718       C  
ATOM    875  C   GLY A 114      38.567  15.131  33.626  1.00 39.47           C  
ANISOU  875  C   GLY A 114     5404   4844   4749   -734     -9  -1686       C  
ATOM    876  O   GLY A 114      39.109  14.855  34.694  1.00 39.66           O  
ANISOU  876  O   GLY A 114     5579   4863   4625   -835   -165  -1821       O  
ATOM    877  N   LYS A 115      38.943  14.579  32.474  1.00 39.06           N  
ANISOU  877  N   LYS A 115     5182   4882   4777   -670    -50  -1517       N  
ATOM    878  CA  LYS A 115      40.115  13.715  32.385  1.00 38.73           C  
ANISOU  878  CA  LYS A 115     5075   4959   4680   -670   -259  -1495       C  
ATOM    879  C   LYS A 115      41.196  14.356  31.533  1.00 40.67           C  
ANISOU  879  C   LYS A 115     5075   5223   5154   -683   -232  -1407       C  
ATOM    880  O   LYS A 115      40.937  15.337  30.841  1.00 43.70           O  
ANISOU  880  O   LYS A 115     5400   5494   5712   -707    -64  -1328       O  
ATOM    881  CB  LYS A 115      39.721  12.345  31.860  1.00 36.88           C  
ANISOU  881  CB  LYS A 115     4914   4841   4257   -538   -348  -1380       C  
ATOM    882  CG  LYS A 115      39.304  11.408  32.987  1.00 38.68           C  
ANISOU  882  CG  LYS A 115     5395   5094   4208   -623   -502  -1456       C  
ATOM    883  CD  LYS A 115      37.936  10.817  32.760  1.00 37.35           C  
ANISOU  883  CD  LYS A 115     5322   4955   3913   -653   -444  -1327       C  
ATOM    884  CE  LYS A 115      37.301  10.418  34.063  1.00 37.15           C  
ANISOU  884  CE  LYS A 115     5498   4969   3648   -830   -457  -1387       C  
ATOM    885  NZ  LYS A 115      36.031  11.156  34.260  1.00 37.44           N  
ANISOU  885  NZ  LYS A 115     5412   5069   3744   -870   -162  -1362       N  
ATOM    886  N   LYS A 116      42.410  13.818  31.611  1.00 41.40           N  
ANISOU  886  N   LYS A 116     5018   5474   5238   -668   -402  -1409       N  
ATOM    887  CA  LYS A 116      43.584  14.473  31.023  1.00 43.79           C  
ANISOU  887  CA  LYS A 116     4997   5877   5765   -749   -369  -1308       C  
ATOM    888  C   LYS A 116      43.922  13.815  29.704  1.00 44.42           C  
ANISOU  888  C   LYS A 116     4902   6171   5805   -493   -253  -1130       C  
ATOM    889  O   LYS A 116      44.223  12.631  29.679  1.00 47.43           O  
ANISOU  889  O   LYS A 116     5314   6709   6000   -253   -387  -1151       O  
ATOM    890  CB  LYS A 116      44.781  14.407  31.980  1.00 44.51           C  
ANISOU  890  CB  LYS A 116     4943   6068   5900   -887   -635  -1410       C  
ATOM    891  CG  LYS A 116      44.575  15.190  33.281  1.00 45.03           C  
ANISOU  891  CG  LYS A 116     5257   5877   5975  -1147   -782  -1595       C  
ATOM    892  CD  LYS A 116      45.852  15.313  34.102  1.00 48.49           C  
ANISOU  892  CD  LYS A 116     5537   6383   6506  -1340  -1104  -1666       C  
ATOM    893  CE  LYS A 116      46.326  13.961  34.643  1.00 50.40           C  
ANISOU  893  CE  LYS A 116     5787   6818   6547  -1134  -1359  -1748       C  
ATOM    894  NZ  LYS A 116      47.557  14.069  35.503  1.00 53.23           N  
ANISOU  894  NZ  LYS A 116     5976   7246   7002  -1303  -1738  -1824       N  
ATOM    895  N   SER A 117      43.887  14.586  28.617  1.00 46.32           N  
ANISOU  895  N   SER A 117     5025   6391   6183   -520    -19   -959       N  
ATOM    896  CA  SER A 117      43.925  14.026  27.260  1.00 44.79           C  
ANISOU  896  CA  SER A 117     4793   6345   5882   -237    137   -789       C  
ATOM    897  C   SER A 117      45.253  14.180  26.543  1.00 47.91           C  
ANISOU  897  C   SER A 117     4796   7049   6357   -199    276   -629       C  
ATOM    898  O   SER A 117      45.914  15.210  26.649  1.00 50.83           O  
ANISOU  898  O   SER A 117     4907   7449   6957   -513    341   -546       O  
ATOM    899  CB  SER A 117      42.872  14.712  26.416  1.00 46.68           C  
ANISOU  899  CB  SER A 117     5218   6356   6161   -253    315   -681       C  
ATOM    900  OG  SER A 117      43.165  16.087  26.312  1.00 52.99           O  
ANISOU  900  OG  SER A 117     5907   7036   7190   -533    434   -604       O  
ATOM    901  N   CYS A 118      45.619  13.156  25.780  1.00 50.13           N  
ANISOU  901  N   CYS A 118     5055   7565   6428    191    322   -569       N  
ATOM    902  CA  CYS A 118      46.799  13.204  24.925  1.00 52.53           C  
ANISOU  902  CA  CYS A 118     4965   8248   6747    331    543   -390       C  
ATOM    903  C   CYS A 118      46.351  13.140  23.465  1.00 53.40           C  
ANISOU  903  C   CYS A 118     5283   8333   6673    580    805   -218       C  
ATOM    904  O   CYS A 118      45.583  12.266  23.082  1.00 51.47           O  
ANISOU  904  O   CYS A 118     5446   7938   6171    889    705   -277       O  
ATOM    905  CB  CYS A 118      47.748  12.054  25.266  1.00 54.39           C  
ANISOU  905  CB  CYS A 118     5007   8820   6837    694    384   -486       C  
ATOM    906  SG  CYS A 118      48.069  11.866  27.058  1.00 54.87           S  
ANISOU  906  SG  CYS A 118     5008   8819   7020    469    -39   -727       S  
ATOM    907  N   HIS A 119      46.824  14.087  22.662  1.00 58.72           N  
ANISOU  907  N   HIS A 119     5719   9129   7465    402   1108     13       N  
ATOM    908  CA  HIS A 119      46.435  14.203  21.256  1.00 59.37           C  
ANISOU  908  CA  HIS A 119     6039   9161   7358    592   1370    202       C  
ATOM    909  C   HIS A 119      47.649  14.193  20.351  1.00 61.58           C  
ANISOU  909  C   HIS A 119     5934   9922   7540    763   1723    427       C  
ATOM    910  O   HIS A 119      48.749  14.509  20.794  1.00 68.66           O  
ANISOU  910  O   HIS A 119     6280  11173   8634    563   1791    498       O  
ATOM    911  CB  HIS A 119      45.720  15.527  21.049  1.00 62.10           C  
ANISOU  911  CB  HIS A 119     6548   9147   7898    183   1438    311       C  
ATOM    912  CG  HIS A 119      44.532  15.713  21.935  1.00 59.93           C  
ANISOU  912  CG  HIS A 119     6574   8463   7733     35   1161    107       C  
ATOM    913  ND1 HIS A 119      43.240  15.525  21.494  1.00 58.01           N  
ANISOU  913  ND1 HIS A 119     6749   7920   7373    193   1079     78       N  
ATOM    914  CD2 HIS A 119      44.439  16.069  23.236  1.00 60.78           C  
ANISOU  914  CD2 HIS A 119     6612   8444   8039   -238    959    -69       C  
ATOM    915  CE1 HIS A 119      42.401  15.759  22.487  1.00 57.69           C  
ANISOU  915  CE1 HIS A 119     6815   7641   7464     34    882    -95       C  
ATOM    916  NE2 HIS A 119      43.103  16.097  23.554  1.00 59.39           N  
ANISOU  916  NE2 HIS A 119     6780   7938   7845   -211    820   -196       N  
ATOM    917  N   THR A 120      47.445  13.851  19.083  1.00 59.69           N  
ANISOU  917  N   THR A 120     5977   9714   6988   1125   1944    554       N  
ATOM    918  CA  THR A 120      48.522  13.895  18.095  1.00 64.44           C  
ANISOU  918  CA  THR A 120     6247  10806   7430   1326   2372    800       C  
ATOM    919  C   THR A 120      48.788  15.334  17.691  1.00 67.83           C  
ANISOU  919  C   THR A 120     6449  11238   8083    766   2650   1099       C  
ATOM    920  O   THR A 120      49.941  15.760  17.645  1.00 73.40           O  
ANISOU  920  O   THR A 120     6560  12410   8919    558   2909   1309       O  
ATOM    921  CB  THR A 120      48.191  13.103  16.817  1.00 64.33           C  
ANISOU  921  CB  THR A 120     6728  10782   6934   1919   2526    840       C  
ATOM    922  OG1 THR A 120      47.063  13.695  16.169  1.00 60.23           O  
ANISOU  922  OG1 THR A 120     6736   9780   6371   1741   2492    922       O  
ATOM    923  CG2 THR A 120      47.892  11.650  17.134  1.00 63.79           C  
ANISOU  923  CG2 THR A 120     7015  10627   6595   2461   2189    561       C  
ATOM    924  N   GLY A 121      47.718  16.068  17.388  1.00 65.91           N  
ANISOU  924  N   GLY A 121     6682  10480   7881    520   2570   1135       N  
ATOM    925  CA  GLY A 121      47.818  17.480  17.000  1.00 69.47           C  
ANISOU  925  CA  GLY A 121     7087  10794   8513    -21   2754   1411       C  
ATOM    926  C   GLY A 121      46.540  18.041  16.398  1.00 68.00           C  
ANISOU  926  C   GLY A 121     7544  10037   8254    -63   2657   1433       C  
ATOM    927  O   GLY A 121      45.632  17.293  16.031  1.00 63.81           O  
ANISOU  927  O   GLY A 121     7458   9292   7495    348   2509   1291       O  
ATOM    928  N   LEU A 122      46.468  19.366  16.296  1.00 70.75           N  
ANISOU  928  N   LEU A 122     7962  10121   8798   -569   2692   1620       N  
ATOM    929  CA  LEU A 122      45.301  20.028  15.710  1.00 69.80           C  
ANISOU  929  CA  LEU A 122     8443   9451   8626   -595   2577   1656       C  
ATOM    930  C   LEU A 122      45.195  19.757  14.212  1.00 73.89           C  
ANISOU  930  C   LEU A 122     9309  10021   8744   -271   2841   1874       C  
ATOM    931  O   LEU A 122      46.205  19.601  13.518  1.00 79.42           O  
ANISOU  931  O   LEU A 122     9763  11171   9241   -222   3233   2114       O  
ATOM    932  CB  LEU A 122      45.342  21.535  15.964  1.00 73.15           C  
ANISOU  932  CB  LEU A 122     8932   9540   9321  -1192   2516   1806       C  
ATOM    933  CG  LEU A 122      44.669  21.990  17.259  1.00 71.29           C  
ANISOU  933  CG  LEU A 122     8782   8913   9390  -1371   2126   1517       C  
ATOM    934  CD1 LEU A 122      45.171  21.182  18.438  1.00 69.57           C  
ANISOU  934  CD1 LEU A 122     8122   9014   9297  -1317   2006   1275       C  
ATOM    935  CD2 LEU A 122      44.909  23.476  17.480  1.00 76.07           C  
ANISOU  935  CD2 LEU A 122     9508   9179  10216  -1951   2045   1676       C  
ATOM    936  N   GLY A 123      43.960  19.686  13.721  1.00 71.65           N  
ANISOU  936  N   GLY A 123     9593   9300   8333    -29   2623   1793       N  
ATOM    937  CA  GLY A 123      43.705  19.410  12.309  1.00 72.20           C  
ANISOU  937  CA  GLY A 123    10124   9321   7988    304   2779   1970       C  
ATOM    938  C   GLY A 123      43.900  17.947  11.964  1.00 69.97           C  
ANISOU  938  C   GLY A 123     9882   9348   7354    875   2826   1852       C  
ATOM    939  O   GLY A 123      43.536  17.513  10.869  1.00 67.43           O  
ANISOU  939  O   GLY A 123    10055   8926   6641   1241   2857   1928       O  
ATOM    940  N   ARG A 124      44.456  17.186  12.908  1.00 69.03           N  
ANISOU  940  N   ARG A 124     9317   9558   7351    968   2782   1655       N  
ATOM    941  CA  ARG A 124      44.759  15.775  12.706  1.00 69.32           C  
ANISOU  941  CA  ARG A 124     9408   9879   7052   1534   2788   1520       C  
ATOM    942  C   ARG A 124      43.482  14.981  12.889  1.00 61.19           C  
ANISOU  942  C   ARG A 124     8860   8437   5954   1776   2304   1278       C  
ATOM    943  O   ARG A 124      42.632  15.360  13.690  1.00 60.37           O  
ANISOU  943  O   ARG A 124     8741   8024   6173   1491   1998   1149       O  
ATOM    944  CB  ARG A 124      45.804  15.296  13.716  1.00 71.31           C  
ANISOU  944  CB  ARG A 124     9026  10597   7473   1534   2851   1398       C  
ATOM    945  CG  ARG A 124      47.147  16.041  13.672  1.00 77.91           C  
ANISOU  945  CG  ARG A 124     9232  11928   8444   1225   3288   1659       C  
ATOM    946  CD  ARG A 124      48.073  15.485  12.613  1.00 85.18           C  
ANISOU  946  CD  ARG A 124    10062  13370   8933   1690   3750   1843       C  
ATOM    947  NE  ARG A 124      48.374  14.074  12.863  1.00 85.82           N  
ANISOU  947  NE  ARG A 124    10125  13705   8778   2326   3637   1592       N  
ATOM    948  CZ  ARG A 124      49.576  13.566  13.136  1.00 90.89           C  
ANISOU  948  CZ  ARG A 124    10174  14966   9395   2584   3862   1592       C  
ATOM    949  NH1 ARG A 124      50.672  14.320  13.175  1.00 96.26           N  
ANISOU  949  NH1 ARG A 124    10123  16165  10285   2228   4248   1863       N  
ATOM    950  NH2 ARG A 124      49.682  12.263  13.351  1.00 90.88           N  
ANISOU  950  NH2 ARG A 124    10322  15066   9144   3216   3668   1331       N  
ATOM    951  N   SER A 125      43.359  13.881  12.154  1.00 58.02           N  
ANISOU  951  N   SER A 125     8886   8043   5115   2300   2231   1229       N  
ATOM    952  CA  SER A 125      42.138  13.080  12.153  1.00 55.23           C  
ANISOU  952  CA  SER A 125     9049   7284   4652   2486   1731   1061       C  
ATOM    953  C   SER A 125      41.841  12.491  13.529  1.00 50.91           C  
ANISOU  953  C   SER A 125     8250   6721   4372   2357   1395    811       C  
ATOM    954  O   SER A 125      40.997  13.008  14.263  1.00 48.66           O  
ANISOU  954  O   SER A 125     7855   6199   4433   2000   1174    745       O  
ATOM    955  CB  SER A 125      42.221  11.952  11.110  1.00 60.41           C  
ANISOU  955  CB  SER A 125    10288   7933   4732   3081   1680   1054       C  
ATOM    956  OG  SER A 125      41.870  12.401   9.809  1.00 65.90           O  
ANISOU  956  OG  SER A 125    11482   8415   5141   3186   1779   1255       O  
ATOM    957  N   ALA A 126      42.549  11.415  13.865  1.00 51.53           N  
ANISOU  957  N   ALA A 126     8265   7060   4255   2686   1369    675       N  
ATOM    958  CA  ALA A 126      42.297  10.631  15.075  1.00 46.69           C  
ANISOU  958  CA  ALA A 126     7557   6406   3777   2628   1012    447       C  
ATOM    959  C   ALA A 126      42.617  11.381  16.364  1.00 45.45           C  
ANISOU  959  C   ALA A 126     6792   6395   4081   2179   1088    381       C  
ATOM    960  O   ALA A 126      41.955  11.184  17.387  1.00 42.34           O  
ANISOU  960  O   ALA A 126     6368   5838   3880   1955    791    232       O  
ATOM    961  CB  ALA A 126      43.096   9.335  15.026  1.00 45.19           C  
ANISOU  961  CB  ALA A 126     7516   6437   3217   3155    958    325       C  
ATOM    962  N   GLY A 127      43.633  12.230  16.315  1.00 47.83           N  
ANISOU  962  N   GLY A 127     6634   7004   4533   2029   1475    506       N  
ATOM    963  CA  GLY A 127      44.099  12.914  17.501  1.00 48.54           C  
ANISOU  963  CA  GLY A 127     6195   7227   5021   1614   1506    447       C  
ATOM    964  C   GLY A 127      43.292  14.145  17.847  1.00 50.95           C  
ANISOU  964  C   GLY A 127     6498   7206   5657   1141   1457    482       C  
ATOM    965  O   GLY A 127      43.472  14.708  18.928  1.00 50.59           O  
ANISOU  965  O   GLY A 127     6145   7162   5913    799   1399    393       O  
ATOM    966  N   TRP A 128      42.402  14.575  16.949  1.00 51.17           N  
ANISOU  966  N   TRP A 128     6904   6930   5607   1154   1447    599       N  
ATOM    967  CA  TRP A 128      41.651  15.800  17.187  1.00 49.92           C  
ANISOU  967  CA  TRP A 128     6776   6453   5739    793   1398    631       C  
ATOM    968  C   TRP A 128      40.291  15.861  16.493  1.00 49.94           C  
ANISOU  968  C   TRP A 128     7229   6082   5664    911   1191    664       C  
ATOM    969  O   TRP A 128      39.253  15.859  17.153  1.00 51.36           O  
ANISOU  969  O   TRP A 128     7447   6061   6006    836    931    530       O  
ATOM    970  CB  TRP A 128      42.506  16.985  16.770  1.00 53.25           C  
ANISOU  970  CB  TRP A 128     7005   6959   6270    508   1718    853       C  
ATOM    971  CG  TRP A 128      41.851  18.278  16.979  1.00 53.24           C  
ANISOU  971  CG  TRP A 128     7121   6581   6526    175   1639    884       C  
ATOM    972  CD1 TRP A 128      41.137  18.993  16.064  1.00 55.21           C  
ANISOU  972  CD1 TRP A 128     7755   6501   6722    179   1632   1032       C  
ATOM    973  CD2 TRP A 128      41.848  19.041  18.182  1.00 52.25           C  
ANISOU  973  CD2 TRP A 128     6799   6331   6720   -167   1523    752       C  
ATOM    974  NE1 TRP A 128      40.682  20.162  16.626  1.00 55.07           N  
ANISOU  974  NE1 TRP A 128     7786   6157   6980   -111   1516    993       N  
ATOM    975  CE2 TRP A 128      41.105  20.217  17.929  1.00 53.95           C  
ANISOU  975  CE2 TRP A 128     7311   6130   7058   -323   1455    816       C  
ATOM    976  CE3 TRP A 128      42.398  18.847  19.456  1.00 49.45           C  
ANISOU  976  CE3 TRP A 128     6106   6149   6532   -330   1439    575       C  
ATOM    977  CZ2 TRP A 128      40.896  21.194  18.905  1.00 51.89           C  
ANISOU  977  CZ2 TRP A 128     7045   5613   7059   -599   1318    694       C  
ATOM    978  CZ3 TRP A 128      42.192  19.818  20.427  1.00 47.99           C  
ANISOU  978  CZ3 TRP A 128     5919   5710   6603   -644   1303    463       C  
ATOM    979  CH2 TRP A 128      41.447  20.978  20.145  1.00 49.49           C  
ANISOU  979  CH2 TRP A 128     6434   5478   6890   -760   1250    516       C  
ATOM    980  N   ASN A 129      40.299  15.921  15.167  1.00 50.16           N  
ANISOU  980  N   ASN A 129     7581   6043   5433   1099   1307    855       N  
ATOM    981  CA  ASN A 129      39.070  16.130  14.404  1.00 48.28           C  
ANISOU  981  CA  ASN A 129     7777   5433   5134   1191   1079    919       C  
ATOM    982  C   ASN A 129      37.969  15.111  14.716  1.00 46.03           C  
ANISOU  982  C   ASN A 129     7658   5019   4812   1341    664    770       C  
ATOM    983  O   ASN A 129      36.792  15.474  14.784  1.00 43.96           O  
ANISOU  983  O   ASN A 129     7480   4504   4719   1269    415    757       O  
ATOM    984  CB  ASN A 129      39.368  16.155  12.898  1.00 49.78           C  
ANISOU  984  CB  ASN A 129     8370   5588   4957   1417   1252   1145       C  
ATOM    985  CG  ASN A 129      40.110  17.417  12.463  1.00 51.26           C  
ANISOU  985  CG  ASN A 129     8469   5805   5204   1158   1619   1370       C  
ATOM    986  OD1 ASN A 129      40.106  18.423  13.166  1.00 51.32           O  
ANISOU  986  OD1 ASN A 129     8241   5709   5551    801   1633   1358       O  
ATOM    987  ND2 ASN A 129      40.742  17.366  11.290  1.00 52.29           N  
ANISOU  987  ND2 ASN A 129     8839   6059   4968   1331   1908   1588       N  
ATOM    988  N   ILE A 130      38.344  13.847  14.909  1.00 45.03           N  
ANISOU  988  N   ILE A 130     7573   5072   4464   1544    571    673       N  
ATOM    989  CA  ILE A 130      37.368  12.812  15.292  1.00 44.76           C  
ANISOU  989  CA  ILE A 130     7711   4912   4382   1593    144    562       C  
ATOM    990  C   ILE A 130      36.901  12.914  16.770  1.00 44.16           C  
ANISOU  990  C   ILE A 130     7247   4893   4641   1299     40    405       C  
ATOM    991  O   ILE A 130      35.702  13.048  17.035  1.00 41.57           O  
ANISOU  991  O   ILE A 130     6903   4413   4478   1171   -193    399       O  
ATOM    992  CB  ILE A 130      37.880  11.374  14.991  1.00 44.36           C  
ANISOU  992  CB  ILE A 130     7975   4950   3928   1924      6    509       C  
ATOM    993  CG1 ILE A 130      37.747  11.032  13.501  1.00 50.01           C  
ANISOU  993  CG1 ILE A 130     9278   5483   4241   2258    -76    644       C  
ATOM    994  CG2 ILE A 130      37.076  10.362  15.756  1.00 42.80           C  
ANISOU  994  CG2 ILE A 130     7870   4654   3738   1829   -426    397       C  
ATOM    995  CD1 ILE A 130      38.929  11.421  12.652  1.00 53.56           C  
ANISOU  995  CD1 ILE A 130     9754   6145   4452   2504    388    755       C  
ATOM    996  N   PRO A 131      37.834  12.839  17.738  1.00 44.62           N  
ANISOU  996  N   PRO A 131     6983   5191   4780   1210    210    283       N  
ATOM    997  CA  PRO A 131      37.363  12.917  19.116  1.00 41.56           C  
ANISOU  997  CA  PRO A 131     6321   4833   4638    957    111    134       C  
ATOM    998  C   PRO A 131      36.544  14.174  19.405  1.00 39.53           C  
ANISOU  998  C   PRO A 131     5907   4425   4688    762    169    139       C  
ATOM    999  O   PRO A 131      35.426  14.078  19.925  1.00 34.98           O  
ANISOU  999  O   PRO A 131     5279   3789   4222    682    -10     94       O  
ATOM   1000  CB  PRO A 131      38.657  12.904  19.938  1.00 43.44           C  
ANISOU 1000  CB  PRO A 131     6267   5321   4915    899    297     27       C  
ATOM   1001  CG  PRO A 131      39.773  13.138  18.950  1.00 47.47           C  
ANISOU 1001  CG  PRO A 131     6771   5974   5290   1071    567    157       C  
ATOM   1002  CD  PRO A 131      39.281  12.575  17.675  1.00 47.93           C  
ANISOU 1002  CD  PRO A 131     7269   5888   5054   1357    458    275       C  
ATOM   1003  N   ILE A 132      37.086  15.333  19.045  1.00 39.62           N  
ANISOU 1003  N   ILE A 132     5857   4380   4818    698    412    209       N  
ATOM   1004  CA  ILE A 132      36.453  16.613  19.378  1.00 38.15           C  
ANISOU 1004  CA  ILE A 132     5596   4001   4899    558    450    186       C  
ATOM   1005  C   ILE A 132      35.162  16.817  18.585  1.00 36.34           C  
ANISOU 1005  C   ILE A 132     5574   3550   4685    700    260    282       C  
ATOM   1006  O   ILE A 132      34.178  17.334  19.114  1.00 33.88           O  
ANISOU 1006  O   ILE A 132     5155   3151   4568    689    172    209       O  
ATOM   1007  CB  ILE A 132      37.400  17.807  19.131  1.00 40.81           C  
ANISOU 1007  CB  ILE A 132     5905   4269   5332    401    695    271       C  
ATOM   1008  CG1 ILE A 132      38.738  17.602  19.849  1.00 42.12           C  
ANISOU 1008  CG1 ILE A 132     5796   4699   5509    238    843    210       C  
ATOM   1009  CG2 ILE A 132      36.751  19.106  19.593  1.00 39.90           C  
ANISOU 1009  CG2 ILE A 132     5816   3884   5459    292    670    209       C  
ATOM   1010  CD1 ILE A 132      38.597  17.214  21.310  1.00 43.08           C  
ANISOU 1010  CD1 ILE A 132     5726   4914   5728    146    724    -20       C  
ATOM   1011  N   GLY A 133      35.175  16.408  17.320  1.00 37.98           N  
ANISOU 1011  N   GLY A 133     6081   3680   4669    868    190    443       N  
ATOM   1012  CA  GLY A 133      33.975  16.426  16.489  1.00 39.92           C  
ANISOU 1012  CA  GLY A 133     6556   3712   4898   1008    -79    547       C  
ATOM   1013  C   GLY A 133      32.848  15.608  17.096  1.00 38.73           C  
ANISOU 1013  C   GLY A 133     6253   3641   4821    985   -378    482       C  
ATOM   1014  O   GLY A 133      31.717  16.085  17.199  1.00 36.63           O  
ANISOU 1014  O   GLY A 133     5863   3300   4755   1003   -530    492       O  
ATOM   1015  N   LEU A 134      33.167  14.383  17.516  1.00 40.41           N  
ANISOU 1015  N   LEU A 134     6466   4022   4867    942   -467    428       N  
ATOM   1016  CA  LEU A 134      32.185  13.492  18.146  1.00 39.56           C  
ANISOU 1016  CA  LEU A 134     6234   4007   4792    825   -756    408       C  
ATOM   1017  C   LEU A 134      31.875  13.866  19.603  1.00 38.46           C  
ANISOU 1017  C   LEU A 134     5668   4055   4890    649   -606    264       C  
ATOM   1018  O   LEU A 134      30.852  13.463  20.122  1.00 41.60           O  
ANISOU 1018  O   LEU A 134     5873   4562   5369    534   -775    286       O  
ATOM   1019  CB  LEU A 134      32.627  12.020  18.048  1.00 39.61           C  
ANISOU 1019  CB  LEU A 134     6517   4052   4482    840   -964    414       C  
ATOM   1020  CG  LEU A 134      32.712  11.396  16.634  1.00 44.54           C  
ANISOU 1020  CG  LEU A 134     7671   4468   4785   1063  -1203    545       C  
ATOM   1021  CD1 LEU A 134      32.993   9.890  16.726  1.00 45.79           C  
ANISOU 1021  CD1 LEU A 134     8159   4619   4620   1096  -1485    518       C  
ATOM   1022  CD2 LEU A 134      31.462  11.631  15.756  1.00 41.77           C  
ANISOU 1022  CD2 LEU A 134     7462   3906   4501   1072  -1534    705       C  
ATOM   1023  N   LEU A 135      32.740  14.632  20.262  1.00 39.81           N  
ANISOU 1023  N   LEU A 135     5703   4271   5153    614   -298    131       N  
ATOM   1024  CA  LEU A 135      32.425  15.173  21.595  1.00 42.25           C  
ANISOU 1024  CA  LEU A 135     5705   4698   5649    502   -152    -24       C  
ATOM   1025  C   LEU A 135      31.909  16.617  21.560  1.00 45.53           C  
ANISOU 1025  C   LEU A 135     6043   4965   6291    611    -31    -57       C  
ATOM   1026  O   LEU A 135      31.629  17.193  22.609  1.00 46.78           O  
ANISOU 1026  O   LEU A 135     6018   5187   6571    597    100   -205       O  
ATOM   1027  CB  LEU A 135      33.652  15.101  22.515  1.00 42.25           C  
ANISOU 1027  CB  LEU A 135     5655   4802   5597    383     26   -174       C  
ATOM   1028  CG  LEU A 135      34.108  13.711  22.977  1.00 41.34           C  
ANISOU 1028  CG  LEU A 135     5596   4847   5266    303   -106   -204       C  
ATOM   1029  CD1 LEU A 135      35.186  13.851  24.019  1.00 38.22           C  
ANISOU 1029  CD1 LEU A 135     5098   4550   4873    200     40   -367       C  
ATOM   1030  CD2 LEU A 135      32.949  12.884  23.525  1.00 41.85           C  
ANISOU 1030  CD2 LEU A 135     5593   5018   5290    184   -303   -170       C  
ATOM   1031  N   TYR A 136      31.761  17.182  20.362  1.00 47.98           N  
ANISOU 1031  N   TYR A 136     6556   5054   6620    752    -97     76       N  
ATOM   1032  CA  TYR A 136      31.449  18.606  20.183  1.00 49.27           C  
ANISOU 1032  CA  TYR A 136     6774   4987   6958    882    -23     54       C  
ATOM   1033  C   TYR A 136      30.261  19.109  21.000  1.00 48.59           C  
ANISOU 1033  C   TYR A 136     6423   4978   7059   1022    -35    -60       C  
ATOM   1034  O   TYR A 136      30.364  20.126  21.676  1.00 46.97           O  
ANISOU 1034  O   TYR A 136     6227   4667   6954   1087    114   -211       O  
ATOM   1035  CB  TYR A 136      31.205  18.900  18.707  1.00 53.52           C  
ANISOU 1035  CB  TYR A 136     7610   5280   7444   1028   -177    247       C  
ATOM   1036  CG  TYR A 136      30.946  20.356  18.407  1.00 60.14           C  
ANISOU 1036  CG  TYR A 136     8613   5813   8424   1169   -153    246       C  
ATOM   1037  CD1 TYR A 136      31.979  21.291  18.438  1.00 62.02           C  
ANISOU 1037  CD1 TYR A 136     9055   5853   8657   1038     42    233       C  
ATOM   1038  CD2 TYR A 136      29.671  20.798  18.075  1.00 64.52           C  
ANISOU 1038  CD2 TYR A 136     9133   6265   9115   1425   -368    276       C  
ATOM   1039  CE1 TYR A 136      31.745  22.632  18.156  1.00 64.92           C  
ANISOU 1039  CE1 TYR A 136     9681   5864   9122   1145      6    244       C  
ATOM   1040  CE2 TYR A 136      29.429  22.135  17.790  1.00 67.99           C  
ANISOU 1040  CE2 TYR A 136     9801   6374   9657   1612   -394    263       C  
ATOM   1041  CZ  TYR A 136      30.469  23.048  17.833  1.00 67.59           C  
ANISOU 1041  CZ  TYR A 136    10046   6066   9568   1463   -215    244       C  
ATOM   1042  OH  TYR A 136      30.228  24.378  17.554  1.00 72.59           O  
ANISOU 1042  OH  TYR A 136    11006   6301  10275   1626   -295    241       O  
ATOM   1043  N   CYS A 137      29.142  18.398  20.949  1.00 49.30           N  
ANISOU 1043  N   CYS A 137     6281   5265   7183   1072   -219     19       N  
ATOM   1044  CA  CYS A 137      27.921  18.877  21.603  1.00 52.21           C  
ANISOU 1044  CA  CYS A 137     6310   5794   7731   1262   -200    -51       C  
ATOM   1045  C   CYS A 137      27.877  18.666  23.126  1.00 52.60           C  
ANISOU 1045  C   CYS A 137     6087   6138   7761   1170     34   -224       C  
ATOM   1046  O   CYS A 137      26.915  19.070  23.776  1.00 56.06           O  
ANISOU 1046  O   CYS A 137     6223   6771   8304   1366    129   -294       O  
ATOM   1047  CB  CYS A 137      26.690  18.274  20.936  1.00 54.50           C  
ANISOU 1047  CB  CYS A 137     6379   6232   8099   1317   -501    145       C  
ATOM   1048  SG  CYS A 137      26.453  18.867  19.241  1.00 60.79           S  
ANISOU 1048  SG  CYS A 137     7532   6639   8929   1541   -803    315       S  
ATOM   1049  N   ASP A 138      28.907  18.057  23.702  1.00 48.71           N  
ANISOU 1049  N   ASP A 138     5704   5691   7112    913    132   -293       N  
ATOM   1050  CA  ASP A 138      29.029  18.007  25.157  1.00 49.84           C  
ANISOU 1050  CA  ASP A 138     5710   6033   7194    833    347   -477       C  
ATOM   1051  C   ASP A 138      30.007  19.045  25.656  1.00 49.82           C  
ANISOU 1051  C   ASP A 138     5960   5779   7191    865    507   -675       C  
ATOM   1052  O   ASP A 138      30.124  19.255  26.865  1.00 55.92           O  
ANISOU 1052  O   ASP A 138     6715   6635   7899    852    666   -860       O  
ATOM   1053  CB  ASP A 138      29.478  16.627  25.624  1.00 50.99           C  
ANISOU 1053  CB  ASP A 138     5839   6380   7154    523    287   -433       C  
ATOM   1054  CG  ASP A 138      28.412  15.578  25.433  1.00 55.85           C  
ANISOU 1054  CG  ASP A 138     6219   7252   7750    405    102   -235       C  
ATOM   1055  OD1 ASP A 138      27.211  15.885  25.632  1.00 62.86           O  
ANISOU 1055  OD1 ASP A 138     6767   8349   8767    528    148   -187       O  
ATOM   1056  OD2 ASP A 138      28.782  14.440  25.085  1.00 56.44           O  
ANISOU 1056  OD2 ASP A 138     6450   7321   7673    192   -109   -120       O  
ATOM   1057  N   LEU A 139      30.714  19.695  24.738  1.00 45.64           N  
ANISOU 1057  N   LEU A 139     5698   4932   6710    874    449   -619       N  
ATOM   1058  CA  LEU A 139      31.603  20.772  25.118  1.00 43.39           C  
ANISOU 1058  CA  LEU A 139     5668   4371   6448    834    541   -759       C  
ATOM   1059  C   LEU A 139      30.760  21.896  25.721  1.00 47.00           C  
ANISOU 1059  C   LEU A 139     6175   4701   6980   1146    607   -931       C  
ATOM   1060  O   LEU A 139      29.653  22.157  25.260  1.00 47.05           O  
ANISOU 1060  O   LEU A 139     6067   4733   7078   1443    557   -878       O  
ATOM   1061  CB  LEU A 139      32.389  21.283  23.911  1.00 42.68           C  
ANISOU 1061  CB  LEU A 139     5838   3991   6389    751    476   -602       C  
ATOM   1062  CG  LEU A 139      33.273  20.267  23.179  1.00 40.86           C  
ANISOU 1062  CG  LEU A 139     5590   3892   6042    549    450   -434       C  
ATOM   1063  CD1 LEU A 139      34.058  20.931  22.055  1.00 42.26           C  
ANISOU 1063  CD1 LEU A 139     6016   3823   6218    475    468   -266       C  
ATOM   1064  CD2 LEU A 139      34.218  19.572  24.126  1.00 40.25           C  
ANISOU 1064  CD2 LEU A 139     5396   4020   5877    327    512   -539       C  
ATOM   1065  N   PRO A 140      31.276  22.559  26.769  1.00 52.02           N  
ANISOU 1065  N   PRO A 140     7003   5199   7564   1114    693  -1146       N  
ATOM   1066  CA  PRO A 140      30.513  23.640  27.382  1.00 57.97           C  
ANISOU 1066  CA  PRO A 140     7901   5799   8327   1489    752  -1346       C  
ATOM   1067  C   PRO A 140      30.338  24.842  26.447  1.00 60.52           C  
ANISOU 1067  C   PRO A 140     8548   5684   8764   1708    611  -1299       C  
ATOM   1068  O   PRO A 140      31.192  25.084  25.588  1.00 56.28           O  
ANISOU 1068  O   PRO A 140     8237   4880   8266   1446    497  -1144       O  
ATOM   1069  CB  PRO A 140      31.375  24.021  28.591  1.00 59.41           C  
ANISOU 1069  CB  PRO A 140     8354   5837   8382   1328    796  -1570       C  
ATOM   1070  CG  PRO A 140      32.768  23.607  28.211  1.00 54.05           C  
ANISOU 1070  CG  PRO A 140     7727   5088   7720    854    695  -1439       C  
ATOM   1071  CD  PRO A 140      32.593  22.376  27.412  1.00 50.95           C  
ANISOU 1071  CD  PRO A 140     6993   5021   7345    764    698  -1220       C  
ATOM   1072  N   GLU A 141      29.237  25.574  26.611  1.00 65.06           N  
ANISOU 1072  N   GLU A 141     9145   6204   9369   2202    624  -1419       N  
ATOM   1073  CA  GLU A 141      29.077  26.863  25.946  1.00 71.13           C  
ANISOU 1073  CA  GLU A 141    10350   6472  10204   2470    450  -1431       C  
ATOM   1074  C   GLU A 141      29.952  27.906  26.645  1.00 71.23           C  
ANISOU 1074  C   GLU A 141    10936   6011  10118   2359    389  -1624       C  
ATOM   1075  O   GLU A 141      30.057  27.904  27.872  1.00 71.78           O  
ANISOU 1075  O   GLU A 141    11047   6170  10057   2399    506  -1853       O  
ATOM   1076  CB  GLU A 141      27.619  27.340  25.967  1.00 80.72           C  
ANISOU 1076  CB  GLU A 141    11411   7785  11475   3123    457  -1527       C  
ATOM   1077  CG  GLU A 141      26.686  26.642  24.968  1.00 83.30           C  
ANISOU 1077  CG  GLU A 141    11270   8428  11950   3243    371  -1290       C  
ATOM   1078  CD  GLU A 141      25.953  25.444  25.556  1.00 83.78           C  
ANISOU 1078  CD  GLU A 141    10663   9154  12015   3217    557  -1249       C  
ATOM   1079  OE1 GLU A 141      26.465  24.830  26.517  1.00 82.66           O  
ANISOU 1079  OE1 GLU A 141    10432   9235  11742   2933    748  -1334       O  
ATOM   1080  OE2 GLU A 141      24.859  25.117  25.045  1.00 86.33           O  
ANISOU 1080  OE2 GLU A 141    10561   9770  12472   3451    477  -1112       O  
ATOM   1081  N   PRO A 142      30.589  28.800  25.874  1.00 71.45           N  
ANISOU 1081  N   PRO A 142    11449   5514  10184   2186    179  -1515       N  
ATOM   1082  CA  PRO A 142      30.595  28.851  24.413  1.00 68.82           C  
ANISOU 1082  CA  PRO A 142    11170   5032   9946   2099     47  -1229       C  
ATOM   1083  C   PRO A 142      31.579  27.852  23.803  1.00 63.21           C  
ANISOU 1083  C   PRO A 142    10203   4570   9244   1555    122   -975       C  
ATOM   1084  O   PRO A 142      32.650  27.606  24.373  1.00 58.06           O  
ANISOU 1084  O   PRO A 142     9532   3977   8550   1141    187   -995       O  
ATOM   1085  CB  PRO A 142      31.026  30.288  24.111  1.00 73.83           C  
ANISOU 1085  CB  PRO A 142    12524   4975  10554   2066   -186  -1232       C  
ATOM   1086  CG  PRO A 142      31.804  30.726  25.307  1.00 75.66           C  
ANISOU 1086  CG  PRO A 142    13039   5015  10693   1837   -197  -1442       C  
ATOM   1087  CD  PRO A 142      31.350  29.910  26.480  1.00 74.02           C  
ANISOU 1087  CD  PRO A 142    12395   5308  10423   2044     30  -1670       C  
ATOM   1088  N   ARG A 143      31.203  27.290  22.652  1.00 61.83           N  
ANISOU 1088  N   ARG A 143     9851   4536   9105   1601     88   -748       N  
ATOM   1089  CA  ARG A 143      32.073  26.392  21.883  1.00 59.21           C  
ANISOU 1089  CA  ARG A 143     9364   4404   8727   1201    154   -504       C  
ATOM   1090  C   ARG A 143      32.849  27.148  20.795  1.00 62.21           C  
ANISOU 1090  C   ARG A 143    10172   4394   9071    950     81   -266       C  
ATOM   1091  O   ARG A 143      33.374  26.540  19.859  1.00 62.20           O  
ANISOU 1091  O   ARG A 143    10109   4532   8994    749    144    -30       O  
ATOM   1092  CB  ARG A 143      31.253  25.266  21.244  1.00 56.93           C  
ANISOU 1092  CB  ARG A 143     8721   4470   8438   1378    131   -386       C  
ATOM   1093  CG  ARG A 143      30.318  24.553  22.199  1.00 54.26           C  
ANISOU 1093  CG  ARG A 143     7948   4532   8138   1592    191   -551       C  
ATOM   1094  CD  ARG A 143      29.664  23.344  21.558  1.00 51.61           C  
ANISOU 1094  CD  ARG A 143     7289   4527   7796   1620    106   -386       C  
ATOM   1095  NE  ARG A 143      28.558  22.845  22.381  1.00 51.85           N  
ANISOU 1095  NE  ARG A 143     6887   4929   7886   1817    141   -489       N  
ATOM   1096  CZ  ARG A 143      27.279  23.200  22.253  1.00 55.45           C  
ANISOU 1096  CZ  ARG A 143     7149   5454   8465   2199     43   -493       C  
ATOM   1097  NH1 ARG A 143      26.891  24.056  21.311  1.00 59.20           N  
ANISOU 1097  NH1 ARG A 143     7880   5597   9017   2466   -150   -420       N  
ATOM   1098  NH2 ARG A 143      26.371  22.683  23.072  1.00 56.95           N  
ANISOU 1098  NH2 ARG A 143     6867   6075   8696   2316    137   -552       N  
ATOM   1099  N   LYS A 144      32.880  28.475  20.910  1.00 67.60           N  
ANISOU 1099  N   LYS A 144    11335   4578   9773    983    -57   -321       N  
ATOM   1100  CA  LYS A 144      33.767  29.327  20.127  1.00 71.26           C  
ANISOU 1100  CA  LYS A 144    12256   4634  10187    614   -127    -86       C  
ATOM   1101  C   LYS A 144      34.550  30.199  21.123  1.00 73.91           C  
ANISOU 1101  C   LYS A 144    12871   4669  10541    303   -198   -216       C  
ATOM   1102  O   LYS A 144      33.942  30.885  21.947  1.00 75.23           O  
ANISOU 1102  O   LYS A 144    13296   4569  10721    618   -337   -485       O  
ATOM   1103  CB  LYS A 144      32.970  30.236  19.181  1.00 75.62           C  
ANISOU 1103  CB  LYS A 144    13299   4718  10714    929   -355     10       C  
ATOM   1104  CG  LYS A 144      31.977  29.533  18.238  1.00 75.04           C  
ANISOU 1104  CG  LYS A 144    13025   4855  10632   1307   -402    110       C  
ATOM   1105  CD  LYS A 144      32.591  29.161  16.882  1.00 74.42           C  
ANISOU 1105  CD  LYS A 144    13072   4794  10408   1023   -340    459       C  
ATOM   1106  CE  LYS A 144      32.796  30.378  15.968  1.00 78.01           C  
ANISOU 1106  CE  LYS A 144    14219   4658  10763    913   -510    675       C  
ATOM   1107  NZ  LYS A 144      31.537  30.858  15.332  1.00 78.93           N  
ANISOU 1107  NZ  LYS A 144    14644   4457  10888   1444   -821    656       N  
ATOM   1108  N   PRO A 145      35.893  30.168  21.072  1.00 74.44           N  
ANISOU 1108  N   PRO A 145    12887   4794  10601   -295   -117    -29       N  
ATOM   1109  CA  PRO A 145      36.736  29.373  20.197  1.00 72.12           C  
ANISOU 1109  CA  PRO A 145    12268   4873  10261   -625     98    272       C  
ATOM   1110  C   PRO A 145      36.799  27.949  20.700  1.00 67.49           C  
ANISOU 1110  C   PRO A 145    11076   4889   9678   -527    283    153       C  
ATOM   1111  O   PRO A 145      36.876  27.732  21.912  1.00 68.17           O  
ANISOU 1111  O   PRO A 145    10984   5100   9816   -531    267    -91       O  
ATOM   1112  CB  PRO A 145      38.101  30.038  20.333  1.00 76.48           C  
ANISOU 1112  CB  PRO A 145    12943   5275  10839  -1275     83    457       C  
ATOM   1113  CG  PRO A 145      38.116  30.550  21.721  1.00 78.29           C  
ANISOU 1113  CG  PRO A 145    13316   5286  11144  -1308   -110    156       C  
ATOM   1114  CD  PRO A 145      36.695  30.941  22.036  1.00 78.93           C  
ANISOU 1114  CD  PRO A 145    13706   5082  11203   -671   -255   -129       C  
ATOM   1115  N   LEU A 146      36.764  26.994  19.774  1.00 62.39           N  
ANISOU 1115  N   LEU A 146    10195   4569   8941   -430    429    325       N  
ATOM   1116  CA  LEU A 146      36.788  25.580  20.115  1.00 55.19           C  
ANISOU 1116  CA  LEU A 146     8807   4170   7992   -319    552    236       C  
ATOM   1117  C   LEU A 146      37.863  25.281  21.155  1.00 55.05           C  
ANISOU 1117  C   LEU A 146     8498   4394   8025   -644    622    140       C  
ATOM   1118  O   LEU A 146      37.587  24.640  22.170  1.00 55.82           O  
ANISOU 1118  O   LEU A 146     8370   4699   8141   -523    600    -92       O  
ATOM   1119  CB  LEU A 146      37.026  24.741  18.857  1.00 54.25           C  
ANISOU 1119  CB  LEU A 146     8610   4291   7710   -272    682    482       C  
ATOM   1120  CG  LEU A 146      36.962  23.219  18.983  1.00 49.69           C  
ANISOU 1120  CG  LEU A 146     7679   4162   7037   -102    742    414       C  
ATOM   1121  CD1 LEU A 146      35.589  22.773  19.461  1.00 49.74           C  
ANISOU 1121  CD1 LEU A 146     7614   4186   7098    231    573    220       C  
ATOM   1122  CD2 LEU A 146      37.298  22.578  17.652  1.00 49.73           C  
ANISOU 1122  CD2 LEU A 146     7761   4310   6822    -28    852    657       C  
ATOM   1123  N   GLU A 147      39.078  25.767  20.919  1.00 56.86           N  
ANISOU 1123  N   GLU A 147     8729   4603   8274  -1079    688    338       N  
ATOM   1124  CA  GLU A 147      40.202  25.447  21.797  1.00 57.41           C  
ANISOU 1124  CA  GLU A 147     8460   4945   8410  -1409    716    289       C  
ATOM   1125  C   GLU A 147      39.912  25.738  23.268  1.00 58.08           C  
ANISOU 1125  C   GLU A 147     8621   4868   8577  -1394    524    -35       C  
ATOM   1126  O   GLU A 147      40.323  24.964  24.130  1.00 54.50           O  
ANISOU 1126  O   GLU A 147     7863   4719   8125  -1429    522   -178       O  
ATOM   1127  CB  GLU A 147      41.484  26.166  21.364  1.00 61.89           C  
ANISOU 1127  CB  GLU A 147     9000   5485   9028  -1945    773    584       C  
ATOM   1128  CG  GLU A 147      42.208  25.535  20.164  1.00 61.99           C  
ANISOU 1128  CG  GLU A 147     8737   5903   8913  -1991   1067    901       C  
ATOM   1129  CD  GLU A 147      41.967  26.269  18.855  1.00 64.19           C  
ANISOU 1129  CD  GLU A 147     9409   5901   9079  -2035   1151   1191       C  
ATOM   1130  OE1 GLU A 147      40.807  26.646  18.581  1.00 65.32           O  
ANISOU 1130  OE1 GLU A 147     9975   5657   9186  -1730   1004   1097       O  
ATOM   1131  OE2 GLU A 147      42.942  26.467  18.098  1.00 67.65           O  
ANISOU 1131  OE2 GLU A 147     9721   6531   9454  -2370   1366   1527       O  
ATOM   1132  N   LYS A 148      39.201  26.831  23.552  1.00 64.13           N  
ANISOU 1132  N   LYS A 148     9842   5149   9376  -1298    355   -157       N  
ATOM   1133  CA  LYS A 148      38.861  27.190  24.941  1.00 66.68           C  
ANISOU 1133  CA  LYS A 148    10339   5285   9712  -1206    191   -485       C  
ATOM   1134  C   LYS A 148      37.921  26.166  25.581  1.00 62.68           C  
ANISOU 1134  C   LYS A 148     9583   5101   9130   -775    286   -721       C  
ATOM   1135  O   LYS A 148      38.151  25.721  26.714  1.00 58.69           O  
ANISOU 1135  O   LYS A 148     8952   4762   8588   -818    258   -918       O  
ATOM   1136  CB  LYS A 148      38.225  28.584  25.028  1.00 72.53           C  
ANISOU 1136  CB  LYS A 148    11691   5416  10452  -1077    -10   -581       C  
ATOM   1137  CG  LYS A 148      37.993  29.056  26.473  1.00 76.78           C  
ANISOU 1137  CG  LYS A 148    12510   5722  10942   -962   -179   -929       C  
ATOM   1138  CD  LYS A 148      37.380  30.450  26.560  1.00 84.22           C  
ANISOU 1138  CD  LYS A 148    14144   6017  11839   -748   -405  -1053       C  
ATOM   1139  CE  LYS A 148      37.029  30.794  28.014  1.00 88.11           C  
ANISOU 1139  CE  LYS A 148    14945   6324  12208   -497   -528  -1440       C  
ATOM   1140  NZ  LYS A 148      36.682  32.232  28.223  1.00 93.88           N  
ANISOU 1140  NZ  LYS A 148    16472   6345  12853   -318   -818  -1587       N  
ATOM   1141  N   ALA A 149      36.866  25.809  24.849  1.00 60.12           N  
ANISOU 1141  N   ALA A 149     9208   4858   8776   -398    370   -676       N  
ATOM   1142  CA  ALA A 149      35.852  24.892  25.343  1.00 56.82           C  
ANISOU 1142  CA  ALA A 149     8541   4748   8300    -43    444   -836       C  
ATOM   1143  C   ALA A 149      36.457  23.516  25.584  1.00 55.26           C  
ANISOU 1143  C   ALA A 149     7957   5000   8038   -199    524   -805       C  
ATOM   1144  O   ALA A 149      36.164  22.874  26.598  1.00 58.42           O  
ANISOU 1144  O   ALA A 149     8215   5613   8368   -122    541   -984       O  
ATOM   1145  CB  ALA A 149      34.691  24.810  24.366  1.00 56.84           C  
ANISOU 1145  CB  ALA A 149     8539   4743   8315    315    450   -734       C  
ATOM   1146  N   VAL A 150      37.311  23.075  24.662  1.00 51.94           N  
ANISOU 1146  N   VAL A 150     7404   4722   7611   -392    575   -575       N  
ATOM   1147  CA  VAL A 150      38.086  21.846  24.853  1.00 48.85           C  
ANISOU 1147  CA  VAL A 150     6699   4721   7142   -502    620   -550       C  
ATOM   1148  C   VAL A 150      38.965  21.944  26.106  1.00 50.69           C  
ANISOU 1148  C   VAL A 150     6864   4994   7403   -758    542   -710       C  
ATOM   1149  O   VAL A 150      38.971  21.039  26.938  1.00 47.98           O  
ANISOU 1149  O   VAL A 150     6376   4882   6972   -713    510   -849       O  
ATOM   1150  CB  VAL A 150      38.975  21.553  23.633  1.00 47.15           C  
ANISOU 1150  CB  VAL A 150     6379   4650   6888   -612    724   -280       C  
ATOM   1151  CG1 VAL A 150      39.969  20.442  23.943  1.00 41.79           C  
ANISOU 1151  CG1 VAL A 150     5388   4360   6132   -684    753   -283       C  
ATOM   1152  CG2 VAL A 150      38.108  21.202  22.422  1.00 45.66           C  
ANISOU 1152  CG2 VAL A 150     6306   4438   6606   -332    754   -138       C  
ATOM   1153  N   ALA A 151      39.699  23.049  26.229  1.00 55.63           N  
ANISOU 1153  N   ALA A 151     7639   5362   8138  -1055    469   -672       N  
ATOM   1154  CA  ALA A 151      40.456  23.362  27.446  1.00 56.88           C  
ANISOU 1154  CA  ALA A 151     7823   5456   8332  -1325    307   -830       C  
ATOM   1155  C   ALA A 151      39.579  23.262  28.691  1.00 57.27           C  
ANISOU 1155  C   ALA A 151     8057   5431   8272  -1090    248  -1139       C  
ATOM   1156  O   ALA A 151      39.968  22.618  29.659  1.00 59.06           O  
ANISOU 1156  O   ALA A 151     8178   5840   8423  -1156    172  -1278       O  
ATOM   1157  CB  ALA A 151      41.060  24.748  27.349  1.00 60.78           C  
ANISOU 1157  CB  ALA A 151     8585   5558   8950  -1682    168   -738       C  
ATOM   1158  N   ASN A 152      38.403  23.896  28.647  1.00 56.89           N  
ANISOU 1158  N   ASN A 152     8282   5138   8197   -791    290  -1235       N  
ATOM   1159  CA  ASN A 152      37.397  23.813  29.727  1.00 56.16           C  
ANISOU 1159  CA  ASN A 152     8321   5051   7967   -482    324  -1504       C  
ATOM   1160  C   ASN A 152      36.790  22.421  29.971  1.00 49.24           C  
ANISOU 1160  C   ASN A 152     7123   4613   6971   -309    456  -1521       C  
ATOM   1161  O   ASN A 152      36.214  22.183  31.027  1.00 48.01           O  
ANISOU 1161  O   ASN A 152     7021   4553   6668   -162    506  -1713       O  
ATOM   1162  CB  ASN A 152      36.232  24.787  29.455  1.00 61.30           C  
ANISOU 1162  CB  ASN A 152     9254   5411   8628   -115    365  -1573       C  
ATOM   1163  CG  ASN A 152      36.357  26.096  30.220  1.00 66.79           C  
ANISOU 1163  CG  ASN A 152    10469   5628   9279   -107    202  -1777       C  
ATOM   1164  OD1 ASN A 152      36.643  26.106  31.418  1.00 71.54           O  
ANISOU 1164  OD1 ASN A 152    11234   6197   9750   -165    130  -1991       O  
ATOM   1165  ND2 ASN A 152      36.113  27.210  29.532  1.00 68.33           N  
ANISOU 1165  ND2 ASN A 152    11008   5407   9548    -16    108  -1719       N  
ATOM   1166  N   PHE A 153      36.888  21.525  28.992  1.00 44.94           N  
ANISOU 1166  N   PHE A 153     6303   4313   6457   -328    504  -1311       N  
ATOM   1167  CA  PHE A 153      36.296  20.179  29.084  1.00 41.43           C  
ANISOU 1167  CA  PHE A 153     5631   4220   5891   -210    557  -1286       C  
ATOM   1168  C   PHE A 153      37.224  19.211  29.810  1.00 39.87           C  
ANISOU 1168  C   PHE A 153     5337   4232   5581   -408    468  -1337       C  
ATOM   1169  O   PHE A 153      36.823  18.579  30.788  1.00 42.64           O  
ANISOU 1169  O   PHE A 153     5698   4729   5773   -380    467  -1460       O  
ATOM   1170  CB  PHE A 153      35.984  19.658  27.676  1.00 39.57           C  
ANISOU 1170  CB  PHE A 153     5264   4076   5695   -115    576  -1051       C  
ATOM   1171  CG  PHE A 153      35.169  18.392  27.644  1.00 35.67           C  
ANISOU 1171  CG  PHE A 153     4614   3856   5083    -13    560   -998       C  
ATOM   1172  CD1 PHE A 153      33.818  18.407  27.970  1.00 37.15           C  
ANISOU 1172  CD1 PHE A 153     4728   4125   5262    163    615  -1034       C  
ATOM   1173  CD2 PHE A 153      35.738  17.195  27.234  1.00 30.12           C  
ANISOU 1173  CD2 PHE A 153     3843   3331   4268    -86    473   -890       C  
ATOM   1174  CE1 PHE A 153      33.065  17.233  27.916  1.00 35.72           C  
ANISOU 1174  CE1 PHE A 153     4389   4199   4983    160    561   -932       C  
ATOM   1175  CE2 PHE A 153      34.991  16.024  27.184  1.00 27.08           C  
ANISOU 1175  CE2 PHE A 153     3407   3128   3754    -45    385   -821       C  
ATOM   1176  CZ  PHE A 153      33.665  16.038  27.519  1.00 29.58           C  
ANISOU 1176  CZ  PHE A 153     3634   3522   4084     27    418   -823       C  
ATOM   1177  N   PHE A 154      38.461  19.106  29.328  1.00 39.02           N  
ANISOU 1177  N   PHE A 154     5128   4156   5541   -594    396  -1229       N  
ATOM   1178  CA  PHE A 154      39.494  18.271  29.959  1.00 40.18           C  
ANISOU 1178  CA  PHE A 154     5158   4501   5608   -739    266  -1277       C  
ATOM   1179  C   PHE A 154      40.125  18.970  31.158  1.00 45.42           C  
ANISOU 1179  C   PHE A 154     5960   5006   6290   -946    126  -1458       C  
ATOM   1180  O   PHE A 154      40.087  20.196  31.263  1.00 53.70           O  
ANISOU 1180  O   PHE A 154     7200   5763   7442  -1032    113  -1505       O  
ATOM   1181  CB  PHE A 154      40.576  17.922  28.939  1.00 41.53           C  
ANISOU 1181  CB  PHE A 154     5098   4836   5847   -797    270  -1080       C  
ATOM   1182  CG  PHE A 154      40.059  17.149  27.763  1.00 41.80           C  
ANISOU 1182  CG  PHE A 154     5094   4992   5798   -568    361   -918       C  
ATOM   1183  CD1 PHE A 154      39.783  15.792  27.872  1.00 41.51           C  
ANISOU 1183  CD1 PHE A 154     5068   5136   5567   -418    273   -935       C  
ATOM   1184  CD2 PHE A 154      39.818  17.777  26.557  1.00 43.13           C  
ANISOU 1184  CD2 PHE A 154     5296   5044   6048   -516    487   -745       C  
ATOM   1185  CE1 PHE A 154      39.288  15.076  26.799  1.00 39.29           C  
ANISOU 1185  CE1 PHE A 154     4840   4906   5181   -222    286   -792       C  
ATOM   1186  CE2 PHE A 154      39.330  17.057  25.469  1.00 42.96           C  
ANISOU 1186  CE2 PHE A 154     5312   5097   5913   -297    523   -603       C  
ATOM   1187  CZ  PHE A 154      39.062  15.708  25.598  1.00 39.39           C  
ANISOU 1187  CZ  PHE A 154     4881   4812   5272   -152    409   -632       C  
ATOM   1188  N   SER A 155      40.718  18.199  32.062  1.00 44.56           N  
ANISOU 1188  N   SER A 155     5821   5047   6063  -1023    -31  -1563       N  
ATOM   1189  CA  SER A 155      41.360  18.775  33.248  1.00 44.79           C  
ANISOU 1189  CA  SER A 155     6025   4912   6079  -1230   -235  -1740       C  
ATOM   1190  C   SER A 155      42.844  19.002  32.990  1.00 48.66           C  
ANISOU 1190  C   SER A 155     6263   5464   6761  -1505   -418  -1629       C  
ATOM   1191  O   SER A 155      43.661  18.930  33.908  1.00 55.24           O  
ANISOU 1191  O   SER A 155     7110   6300   7578  -1683   -679  -1734       O  
ATOM   1192  CB  SER A 155      41.149  17.861  34.468  1.00 46.60           C  
ANISOU 1192  CB  SER A 155     6411   5248   6045  -1172   -338  -1914       C  
ATOM   1193  OG  SER A 155      41.418  16.495  34.171  1.00 44.98           O  
ANISOU 1193  OG  SER A 155     6011   5330   5749  -1089   -388  -1820       O  
ATOM   1194  N   GLY A 156      43.190  19.298  31.740  1.00 49.03           N  
ANISOU 1194  N   GLY A 156     6066   5580   6983  -1551   -284  -1398       N  
ATOM   1195  CA  GLY A 156      44.585  19.378  31.319  1.00 51.09           C  
ANISOU 1195  CA  GLY A 156     5953   6037   7422  -1796   -375  -1223       C  
ATOM   1196  C   GLY A 156      44.829  18.480  30.126  1.00 48.12           C  
ANISOU 1196  C   GLY A 156     5245   6017   7022  -1572   -172  -1023       C  
ATOM   1197  O   GLY A 156      44.226  17.410  30.007  1.00 41.62           O  
ANISOU 1197  O   GLY A 156     4483   5320   6010  -1257   -114  -1074       O  
ATOM   1198  N   SER A 157      45.710  18.911  29.230  1.00 49.19           N  
ANISOU 1198  N   SER A 157     5062   6308   7319  -1743    -68   -780       N  
ATOM   1199  CA  SER A 157      45.912  18.179  27.995  1.00 47.56           C  
ANISOU 1199  CA  SER A 157     4611   6422   7037  -1478    175   -587       C  
ATOM   1200  C   SER A 157      47.246  18.478  27.365  1.00 52.31           C  
ANISOU 1200  C   SER A 157     4730   7351   7795  -1688    272   -332       C  
ATOM   1201  O   SER A 157      47.957  19.370  27.809  1.00 60.70           O  
ANISOU 1201  O   SER A 157     5643   8353   9066  -2124    129   -267       O  
ATOM   1202  CB  SER A 157      44.817  18.554  27.001  1.00 45.03           C  
ANISOU 1202  CB  SER A 157     4577   5876   6658  -1334    396   -494       C  
ATOM   1203  OG  SER A 157      43.534  18.432  27.581  1.00 42.20           O  
ANISOU 1203  OG  SER A 157     4580   5259   6197  -1176    327   -696       O  
ATOM   1204  N   CYS A 158      47.586  17.696  26.344  1.00 51.54           N  
ANISOU 1204  N   CYS A 158     4397   7615   7573  -1371    506   -180       N  
ATOM   1205  CA  CYS A 158      48.560  18.106  25.356  1.00 56.42           C  
ANISOU 1205  CA  CYS A 158     4598   8559   8281  -1515    762    134       C  
ATOM   1206  C   CYS A 158      47.880  18.215  24.010  1.00 57.56           C  
ANISOU 1206  C   CYS A 158     4997   8610   8263  -1314   1078    301       C  
ATOM   1207  O   CYS A 158      47.458  17.207  23.443  1.00 57.19           O  
ANISOU 1207  O   CYS A 158     5100   8665   7965   -836   1173    252       O  
ATOM   1208  CB  CYS A 158      49.698  17.119  25.218  1.00 60.79           C  
ANISOU 1208  CB  CYS A 158     4623   9695   8778  -1238    817    189       C  
ATOM   1209  SG  CYS A 158      50.834  17.646  23.910  1.00 68.97           S  
ANISOU 1209  SG  CYS A 158     5087  11233   9885  -1395   1247    625       S  
ATOM   1210  N   ALA A 159      47.794  19.440  23.500  1.00 62.24           N  
ANISOU 1210  N   ALA A 159     5699   8971   8980  -1689   1191    504       N  
ATOM   1211  CA  ALA A 159      47.284  19.702  22.163  1.00 61.25           C  
ANISOU 1211  CA  ALA A 159     5825   8747   8702  -1558   1475    710       C  
ATOM   1212  C   ALA A 159      48.399  20.324  21.337  1.00 67.05           C  
ANISOU 1212  C   ALA A 159     6176   9802   9498  -1880   1760   1088       C  
ATOM   1213  O   ALA A 159      48.706  21.505  21.504  1.00 71.74           O  
ANISOU 1213  O   ALA A 159     6763  10195  10301  -2436   1692   1247       O  
ATOM   1214  CB  ALA A 159      46.093  20.631  22.232  1.00 60.12           C  
ANISOU 1214  CB  ALA A 159     6223   8008   8610  -1690   1348    636       C  
ATOM   1215  N   PRO A 160      49.037  19.519  20.471  1.00 70.76           N  
ANISOU 1215  N   PRO A 160     6338  10784   9764  -1535   2076   1242       N  
ATOM   1216  CA  PRO A 160      50.064  20.034  19.560  1.00 78.97           C  
ANISOU 1216  CA  PRO A 160     6974  12227  10802  -1794   2448   1646       C  
ATOM   1217  C   PRO A 160      49.533  20.965  18.462  1.00 80.89           C  
ANISOU 1217  C   PRO A 160     7661  12140  10935  -1997   2659   1910       C  
ATOM   1218  O   PRO A 160      48.380  20.845  18.040  1.00 76.21           O  
ANISOU 1218  O   PRO A 160     7658  11134  10165  -1693   2601   1784       O  
ATOM   1219  CB  PRO A 160      50.664  18.758  18.956  1.00 79.54           C  
ANISOU 1219  CB  PRO A 160     6723  12904  10594  -1174   2733   1660       C  
ATOM   1220  CG  PRO A 160      50.433  17.722  19.992  1.00 74.33           C  
ANISOU 1220  CG  PRO A 160     6085  12219   9938   -811   2385   1278       C  
ATOM   1221  CD  PRO A 160      49.082  18.048  20.550  1.00 68.35           C  
ANISOU 1221  CD  PRO A 160     5950  10783   9236   -918   2063   1038       C  
ATOM   1222  N   CYS A 161      50.397  21.890  18.034  1.00 89.44           N  
ANISOU 1222  N   CYS A 161     8444  13412  12128  -2544   2869   2296       N  
ATOM   1223  CA  CYS A 161      50.084  22.941  17.046  1.00 93.66           C  
ANISOU 1223  CA  CYS A 161     9399  13620  12568  -2875   3044   2612       C  
ATOM   1224  C   CYS A 161      49.062  23.995  17.510  1.00 91.51           C  
ANISOU 1224  C   CYS A 161     9783  12533  12452  -3186   2650   2478       C  
ATOM   1225  O   CYS A 161      48.727  24.910  16.751  1.00 91.77           O  
ANISOU 1225  O   CYS A 161    10259  12202  12405  -3441   2715   2715       O  
ATOM   1226  CB  CYS A 161      49.668  22.326  15.704  1.00 94.65           C  
ANISOU 1226  CB  CYS A 161     9838  13859  12265  -2316   3408   2707       C  
ATOM   1227  SG  CYS A 161      50.732  20.956  15.159  1.00100.77           S  
ANISOU 1227  SG  CYS A 161     9984  15549  12757  -1726   3863   2778       S  
ATOM   1228  N   ALA A 162      48.602  23.880  18.759  1.00 87.55           N  
ANISOU 1228  N   ALA A 162     9365  11755  12146  -3141   2247   2105       N  
ATOM   1229  CA  ALA A 162      47.685  24.847  19.365  1.00 84.44           C  
ANISOU 1229  CA  ALA A 162     9554  10639  11888  -3350   1874   1930       C  
ATOM   1230  C   ALA A 162      48.474  26.047  19.884  1.00 87.92           C  
ANISOU 1230  C   ALA A 162     9920  10900  12586  -4122   1669   2126       C  
ATOM   1231  O   ALA A 162      49.664  26.176  19.597  1.00 91.18           O  
ANISOU 1231  O   ALA A 162     9804  11765  13075  -4543   1854   2464       O  
ATOM   1232  CB  ALA A 162      46.904  24.188  20.495  1.00 78.62           C  
ANISOU 1232  CB  ALA A 162     8930   9744  11197  -2965   1581   1467       C  
ATOM   1233  N   ASP A 163      47.812  26.917  20.647  1.00 87.01           N  
ANISOU 1233  N   ASP A 163    10335  10135  12591  -4300   1276   1924       N  
ATOM   1234  CA  ASP A 163      48.440  28.129  21.177  1.00 93.97           C  
ANISOU 1234  CA  ASP A 163    11334  10689  13683  -5041    971   2082       C  
ATOM   1235  C   ASP A 163      48.375  28.164  22.703  1.00 92.45           C  
ANISOU 1235  C   ASP A 163    11207  10267  13652  -5086    533   1706       C  
ATOM   1236  O   ASP A 163      47.297  28.088  23.281  1.00 88.25           O  
ANISOU 1236  O   ASP A 163    11129   9355  13048  -4649    365   1330       O  
ATOM   1237  CB  ASP A 163      47.764  29.369  20.588  1.00 97.52           C  
ANISOU 1237  CB  ASP A 163    12557  10437  14058  -5244    849   2222       C  
ATOM   1238  CG  ASP A 163      48.517  30.646  20.899  1.00106.68           C  
ANISOU 1238  CG  ASP A 163    13907  11236  15390  -6095    533   2482       C  
ATOM   1239  OD1 ASP A 163      48.251  31.232  21.970  1.00108.54           O  
ANISOU 1239  OD1 ASP A 163    14551  10958  15733  -6219     73   2210       O  
ATOM   1240  OD2 ASP A 163      49.366  31.065  20.074  1.00112.05           O  
ANISOU 1240  OD2 ASP A 163    14360  12139  16073  -6649    735   2968       O  
ATOM   1241  N   GLY A 164      49.533  28.297  23.346  1.00 98.57           N  
ANISOU 1241  N   GLY A 164    11523  11293  14634  -5621    348   1827       N  
ATOM   1242  CA  GLY A 164      49.637  28.228  24.807  1.00 99.14           C  
ANISOU 1242  CA  GLY A 164    11628  11209  14831  -5678    -84   1487       C  
ATOM   1243  C   GLY A 164      49.379  29.529  25.553  1.00103.13           C  
ANISOU 1243  C   GLY A 164    12854  10929  15402  -6099   -582   1382       C  
ATOM   1244  O   GLY A 164      49.043  29.504  26.740  1.00103.17           O  
ANISOU 1244  O   GLY A 164    13151  10650  15398  -5946   -918   1005       O  
ATOM   1245  N   THR A 165      49.543  30.662  24.869  1.00106.67           N  
ANISOU 1245  N   THR A 165    13653  11001  15877  -6620   -644   1717       N  
ATOM   1246  CA  THR A 165      49.324  31.979  25.474  1.00110.11           C  
ANISOU 1246  CA  THR A 165    14900  10602  16337  -7029  -1167   1644       C  
ATOM   1247  C   THR A 165      47.836  32.278  25.639  1.00104.86           C  
ANISOU 1247  C   THR A 165    15065   9316  15460  -6364  -1230   1252       C  
ATOM   1248  O   THR A 165      47.405  32.752  26.689  1.00103.83           O  
ANISOU 1248  O   THR A 165    15503   8662  15283  -6260  -1625    906       O  
ATOM   1249  CB  THR A 165      49.944  33.104  24.622  1.00119.05           C  
ANISOU 1249  CB  THR A 165    16219  11480  17532  -7824  -1238   2163       C  
ATOM   1250  OG1 THR A 165      49.341  33.111  23.322  1.00118.61           O  
ANISOU 1250  OG1 THR A 165    16333  11433  17300  -7523   -816   2355       O  
ATOM   1251  CG2 THR A 165      51.455  32.920  24.487  1.00123.95           C  
ANISOU 1251  CG2 THR A 165    15942  12765  18388  -8561  -1180   2605       C  
ATOM   1252  N   ASP A 166      47.064  32.007  24.589  1.00102.51           N  
ANISOU 1252  N   ASP A 166    14831   9097  15021  -5896   -845   1315       N  
ATOM   1253  CA  ASP A 166      45.606  32.162  24.625  1.00 98.87           C  
ANISOU 1253  CA  ASP A 166    14998   8183  14385  -5194   -858    975       C  
ATOM   1254  C   ASP A 166      44.968  31.111  25.539  1.00 91.35           C  
ANISOU 1254  C   ASP A 166    13814   7517  13377  -4556   -782    531       C  
ATOM   1255  O   ASP A 166      44.190  31.448  26.435  1.00 90.27           O  
ANISOU 1255  O   ASP A 166    14175   6967  13156  -4226  -1011    163       O  
ATOM   1256  CB  ASP A 166      45.012  32.045  23.213  1.00 97.03           C  
ANISOU 1256  CB  ASP A 166    14820   8020  14028  -4892   -501   1193       C  
ATOM   1257  CG  ASP A 166      45.577  33.078  22.242  1.00104.51           C  
ANISOU 1257  CG  ASP A 166    16066   8672  14973  -5521   -542   1664       C  
ATOM   1258  OD1 ASP A 166      46.338  33.975  22.672  1.00110.87           O  
ANISOU 1258  OD1 ASP A 166    17093   9148  15885  -6214   -889   1822       O  
ATOM   1259  OD2 ASP A 166      45.259  32.988  21.038  1.00103.48           O  
ANISOU 1259  OD2 ASP A 166    15982   8622  14713  -5351   -250   1895       O  
ATOM   1260  N   PHE A 167      45.319  29.845  25.310  1.00124.80           N  
ANISOU 1260  N   PHE A 167    14209   8332  24878  -1999   1446     84       N  
ATOM   1261  CA  PHE A 167      44.752  28.708  26.051  1.00118.11           C  
ANISOU 1261  CA  PHE A 167    13472   8191  23215  -1680   1518   -462       C  
ATOM   1262  C   PHE A 167      45.867  27.889  26.724  1.00114.93           C  
ANISOU 1262  C   PHE A 167    12996   8558  22112  -1989   1456   -787       C  
ATOM   1263  O   PHE A 167      46.497  27.042  26.082  1.00110.00           O  
ANISOU 1263  O   PHE A 167    12260   8602  20933  -2028   1459   -261       O  
ATOM   1264  CB  PHE A 167      43.927  27.815  25.110  1.00111.08           C  
ANISOU 1264  CB  PHE A 167    12611   7765  21830  -1236   1586    152       C  
ATOM   1265  CG  PHE A 167      43.312  28.558  23.953  1.00113.39           C  
ANISOU 1265  CG  PHE A 167    12886   7457  22740  -1075   1573    904       C  
ATOM   1266  CD1 PHE A 167      42.287  29.476  24.164  1.00117.14           C  
ANISOU 1266  CD1 PHE A 167    13409   7101  23997   -841   1587    690       C  
ATOM   1267  CD2 PHE A 167      43.770  28.352  22.655  1.00111.34           C  
ANISOU 1267  CD2 PHE A 167    12550   7474  22281  -1153   1551   1835       C  
ATOM   1268  CE1 PHE A 167      41.722  30.167  23.100  1.00119.65           C  
ANISOU 1268  CE1 PHE A 167    13686   6853  24924   -695   1533   1446       C  
ATOM   1269  CE2 PHE A 167      43.213  29.040  21.587  1.00114.41           C  
ANISOU 1269  CE2 PHE A 167    12926   7354  23191  -1032   1508   2587       C  
ATOM   1270  CZ  PHE A 167      42.185  29.948  21.809  1.00118.76           C  
ANISOU 1270  CZ  PHE A 167    13511   7053  24558   -807   1475   2419       C  
ATOM   1271  N   PRO A 168      46.117  28.139  28.023  1.00117.07           N  
ANISOU 1271  N   PRO A 168    13327   8747  22406  -2202   1392  -1664       N  
ATOM   1272  CA  PRO A 168      47.222  27.475  28.712  1.00113.85           C  
ANISOU 1272  CA  PRO A 168    12824   9016  21416  -2542   1272  -1951       C  
ATOM   1273  C   PRO A 168      46.918  26.023  29.058  1.00104.99           C  
ANISOU 1273  C   PRO A 168    11742   8819  19330  -2251   1317  -2061       C  
ATOM   1274  O   PRO A 168      47.832  25.200  29.162  1.00100.06           O  
ANISOU 1274  O   PRO A 168    10980   8872  18166  -2430   1227  -1941       O  
ATOM   1275  CB  PRO A 168      47.360  28.293  29.994  1.00119.81           C  
ANISOU 1275  CB  PRO A 168    13684   9324  22514  -2825   1168  -2892       C  
ATOM   1276  CG  PRO A 168      45.979  28.738  30.286  1.00121.93           C  
ANISOU 1276  CG  PRO A 168    14155   9081  23092  -2408   1330  -3311       C  
ATOM   1277  CD  PRO A 168      45.329  28.978  28.947  1.00121.64           C  
ANISOU 1277  CD  PRO A 168    14072   8660  23487  -2100   1432  -2467       C  
ATOM   1278  N   GLN A 169      45.634  25.718  29.219  1.00102.61           N  
ANISOU 1278  N   GLN A 169    11597   8517  18872  -1803   1447  -2253       N  
ATOM   1279  CA  GLN A 169      45.203  24.434  29.761  1.00 96.56           C  
ANISOU 1279  CA  GLN A 169    10884   8531  17275  -1549   1475  -2463       C  
ATOM   1280  C   GLN A 169      45.438  23.271  28.801  1.00 88.24           C  
ANISOU 1280  C   GLN A 169     9739   8108  15680  -1384   1462  -1750       C  
ATOM   1281  O   GLN A 169      45.525  22.121  29.228  1.00 83.28           O  
ANISOU 1281  O   GLN A 169     9102   8175  14366  -1300   1416  -1851       O  
ATOM   1282  CB  GLN A 169      43.724  24.506  30.152  1.00 97.66           C  
ANISOU 1282  CB  GLN A 169    11167   8454  17485  -1128   1636  -2817       C  
ATOM   1283  CG  GLN A 169      43.326  23.524  31.230  1.00 94.92           C  
ANISOU 1283  CG  GLN A 169    10881   8786  16399  -1002   1666  -3320       C  
ATOM   1284  CD  GLN A 169      44.102  23.731  32.514  1.00 98.74           C  
ANISOU 1284  CD  GLN A 169    11399   9449  16666  -1390   1566  -4050       C  
ATOM   1285  OE1 GLN A 169      44.443  24.859  32.876  1.00103.32           O  
ANISOU 1285  OE1 GLN A 169    12026   9444  17788  -1651   1536  -4471       O  
ATOM   1286  NE2 GLN A 169      44.387  22.636  33.212  1.00 96.21           N  
ANISOU 1286  NE2 GLN A 169    11061   9931  15562  -1445   1480  -4194       N  
ATOM   1287  N   LEU A 170      45.564  23.573  27.511  1.00 88.60           N  
ANISOU 1287  N   LEU A 170     9723   7910  16031  -1345   1495  -1032       N  
ATOM   1288  CA  LEU A 170      45.853  22.556  26.503  1.00 83.34           C  
ANISOU 1288  CA  LEU A 170     8992   7816  14857  -1196   1502   -384       C  
ATOM   1289  C   LEU A 170      47.306  22.093  26.551  1.00 84.14           C  
ANISOU 1289  C   LEU A 170     8896   8418  14655  -1520   1435   -274       C  
ATOM   1290  O   LEU A 170      47.714  21.275  25.728  1.00 81.78           O  
ANISOU 1290  O   LEU A 170     8519   8599  13954  -1409   1469    217       O  
ATOM   1291  CB  LEU A 170      45.557  23.088  25.096  1.00 84.01           C  
ANISOU 1291  CB  LEU A 170     9080   7527  15311  -1078   1565    359       C  
ATOM   1292  CG  LEU A 170      44.192  23.726  24.835  1.00 85.08           C  
ANISOU 1292  CG  LEU A 170     9347   7066  15914   -773   1602    414       C  
ATOM   1293  CD1 LEU A 170      44.016  23.988  23.347  1.00 86.31           C  
ANISOU 1293  CD1 LEU A 170     9496   7055  16241   -668   1612   1274       C  
ATOM   1294  CD2 LEU A 170      43.067  22.858  25.363  1.00 79.68           C  
ANISOU 1294  CD2 LEU A 170     8773   6692  14808   -392   1612     76       C  
ATOM   1295  N   CYS A 171      48.084  22.613  27.501  1.00 88.62           N  
ANISOU 1295  N   CYS A 171     9372   8877  15424  -1913   1334   -741       N  
ATOM   1296  CA  CYS A 171      49.519  22.372  27.542  1.00 88.69           C  
ANISOU 1296  CA  CYS A 171     9125   9273  15301  -2272   1246   -597       C  
ATOM   1297  C   CYS A 171      50.049  21.832  28.865  1.00 87.19           C  
ANISOU 1297  C   CYS A 171     8877   9535  14714  -2472   1067  -1194       C  
ATOM   1298  O   CYS A 171      51.230  21.546  28.960  1.00 88.62           O  
ANISOU 1298  O   CYS A 171     8807  10084  14780  -2752    962  -1071       O  
ATOM   1299  CB  CYS A 171      50.246  23.673  27.205  1.00 96.34           C  
ANISOU 1299  CB  CYS A 171     9948   9645  17013  -2690   1228   -394       C  
ATOM   1300  SG  CYS A 171      49.727  24.407  25.641  1.00100.26           S  
ANISOU 1300  SG  CYS A 171    10483   9607  18003  -2524   1404    419       S  
ATOM   1301  N   GLN A 172      49.208  21.662  29.880  1.00 87.56           N  
ANISOU 1301  N   GLN A 172     9129   9610  14531  -2334   1032  -1800       N  
ATOM   1302  CA  GLN A 172      49.697  21.173  31.177  1.00 90.57           C  
ANISOU 1302  CA  GLN A 172     9472  10466  14476  -2553    840  -2342       C  
ATOM   1303  C   GLN A 172      50.653  19.986  31.041  1.00 87.37           C  
ANISOU 1303  C   GLN A 172     8827  10801  13569  -2580    728  -1991       C  
ATOM   1304  O   GLN A 172      51.564  19.829  31.852  1.00 88.50           O  
ANISOU 1304  O   GLN A 172     8808  11268  13548  -2912    512  -2232       O  
ATOM   1305  CB  GLN A 172      48.539  20.795  32.106  1.00 90.97           C  
ANISOU 1305  CB  GLN A 172     9762  10657  14145  -2293    881  -2877       C  
ATOM   1306  CG  GLN A 172      47.855  21.995  32.769  1.00 97.73           C  
ANISOU 1306  CG  GLN A 172    10816  10873  15445  -2364    953  -3511       C  
ATOM   1307  CD  GLN A 172      47.052  21.618  34.009  1.00 98.24           C  
ANISOU 1307  CD  GLN A 172    11056  11253  15019  -2235    984  -4165       C  
ATOM   1308  OE1 GLN A 172      46.727  22.475  34.832  1.00102.98           O  
ANISOU 1308  OE1 GLN A 172    11804  11495  15828  -2352   1021  -4840       O  
ATOM   1309  NE2 GLN A 172      46.724  20.336  34.144  1.00 94.05           N  
ANISOU 1309  NE2 GLN A 172    10509  11388  13839  -1994    978  -3971       N  
ATOM   1310  N   LEU A 173      50.439  19.163  30.014  1.00 84.49           N  
ANISOU 1310  N   LEU A 173     8437  10686  12979  -2224    858  -1436       N  
ATOM   1311  CA  LEU A 173      51.293  18.001  29.726  1.00 81.97           C  
ANISOU 1311  CA  LEU A 173     7889  11010  12246  -2162    796  -1082       C  
ATOM   1312  C   LEU A 173      52.344  18.290  28.645  1.00 83.53           C  
ANISOU 1312  C   LEU A 173     7812  11185  12739  -2304    899   -519       C  
ATOM   1313  O   LEU A 173      53.349  17.589  28.567  1.00 84.61           O  
ANISOU 1313  O   LEU A 173     7669  11805  12676  -2362    844   -305       O  
ATOM   1314  CB  LEU A 173      50.430  16.805  29.299  1.00 75.59           C  
ANISOU 1314  CB  LEU A 173     7233  10522  10967  -1672    866   -882       C  
ATOM   1315  CG  LEU A 173      49.187  16.527  30.153  1.00 72.93           C  
ANISOU 1315  CG  LEU A 173     7152  10185  10374  -1479    832  -1309       C  
ATOM   1316  CD1 LEU A 173      48.275  15.534  29.454  1.00 68.03           C  
ANISOU 1316  CD1 LEU A 173     6667   9733   9448  -1022    903  -1003       C  
ATOM   1317  CD2 LEU A 173      49.579  16.038  31.538  1.00 72.08           C  
ANISOU 1317  CD2 LEU A 173     6979  10514   9894  -1690    614  -1737       C  
ATOM   1318  N   CYS A 174      52.094  19.293  27.803  1.00 85.80           N  
ANISOU 1318  N   CYS A 174     8160  10933  13508  -2343   1060   -245       N  
ATOM   1319  CA  CYS A 174      53.075  19.787  26.833  1.00 88.31           C  
ANISOU 1319  CA  CYS A 174     8206  11185  14164  -2555   1181    309       C  
ATOM   1320  C   CYS A 174      53.295  21.279  27.057  1.00 95.71           C  
ANISOU 1320  C   CYS A 174     9109  11443  15814  -2990   1125    190       C  
ATOM   1321  O   CYS A 174      52.900  22.092  26.215  1.00 98.63           O  
ANISOU 1321  O   CYS A 174     9561  11313  16602  -2969   1267    544       O  
ATOM   1322  CB  CYS A 174      52.574  19.559  25.408  1.00 85.37           C  
ANISOU 1322  CB  CYS A 174     7937  10817  13682  -2194   1426    901       C  
ATOM   1323  SG  CYS A 174      52.576  17.850  24.906  1.00 79.01           S  
ANISOU 1323  SG  CYS A 174     7131  10765  12123  -1728   1494   1098       S  
ATOM   1324  N   PRO A 175      53.924  21.648  28.193  1.00 98.99           N  
ANISOU 1324  N   PRO A 175     9409  11820  16383  -3400    887   -302       N  
ATOM   1325  CA  PRO A 175      54.025  23.050  28.628  1.00104.73           C  
ANISOU 1325  CA  PRO A 175    10165  11831  17795  -3823    772   -599       C  
ATOM   1326  C   PRO A 175      54.230  24.020  27.470  1.00107.68           C  
ANISOU 1326  C   PRO A 175    10430  11677  18806  -3964    932     24       C  
ATOM   1327  O   PRO A 175      53.569  25.058  27.405  1.00110.54           O  
ANISOU 1327  O   PRO A 175    10989  11294  19718  -4007    945    -88       O  
ATOM   1328  CB  PRO A 175      55.237  23.034  29.560  1.00107.97           C  
ANISOU 1328  CB  PRO A 175    10289  12531  18203  -4306    490   -891       C  
ATOM   1329  CG  PRO A 175      55.204  21.674  30.159  1.00102.51           C  
ANISOU 1329  CG  PRO A 175     9600  12600  16749  -4051    407  -1084       C  
ATOM   1330  CD  PRO A 175      54.691  20.752  29.081  1.00 97.18           C  
ANISOU 1330  CD  PRO A 175     8982  12232  15709  -3518    679   -559       C  
ATOM   1331  N   GLY A 176      55.145  23.669  26.571  1.00107.12           N  
ANISOU 1331  N   GLY A 176    10031  12004  18665  -4024   1063    691       N  
ATOM   1332  CA  GLY A 176      55.249  24.316  25.274  1.00110.37           C  
ANISOU 1332  CA  GLY A 176    10346  12115  19474  -4060   1282   1439       C  
ATOM   1333  C   GLY A 176      54.535  23.449  24.260  1.00105.42           C  
ANISOU 1333  C   GLY A 176     9890  11867  18299  -3509   1530   1858       C  
ATOM   1334  O   GLY A 176      55.124  22.518  23.715  1.00103.04           O  
ANISOU 1334  O   GLY A 176     9395  12234  17523  -3350   1673   2198       O  
ATOM   1335  N   CYS A 177      53.252  23.729  24.042  1.00105.11           N  
ANISOU 1335  N   CYS A 177    10208  11399  18330  -3205   1564   1792       N  
ATOM   1336  CA  CYS A 177      52.445  23.001  23.058  1.00101.05           C  
ANISOU 1336  CA  CYS A 177     9890  11169  17335  -2708   1739   2181       C  
ATOM   1337  C   CYS A 177      53.088  23.119  21.673  1.00104.64           C  
ANISOU 1337  C   CYS A 177    10144  11833  17780  -2762   1969   3031       C  
ATOM   1338  O   CYS A 177      52.639  23.900  20.833  1.00108.90           O  
ANISOU 1338  O   CYS A 177    10774  11944  18660  -2766   2048   3521       O  
ATOM   1339  CB  CYS A 177      51.008  23.552  23.031  1.00100.72           C  
ANISOU 1339  CB  CYS A 177    10194  10517  17559  -2455   1705   2045       C  
ATOM   1340  SG  CYS A 177      49.901  22.894  24.294  1.00 95.67           S  
ANISOU 1340  SG  CYS A 177     9834   9941  16576  -2139   1568   1191       S  
ATOM   1341  N   GLY A 178      54.137  22.332  21.445  1.00103.76           N  
ANISOU 1341  N   GLY A 178     9746  12404  17274  -2793   2084   3219       N  
ATOM   1342  CA  GLY A 178      54.973  22.461  20.252  1.00107.28           C  
ANISOU 1342  CA  GLY A 178     9919  13144  17699  -2904   2352   3983       C  
ATOM   1343  C   GLY A 178      54.543  21.589  19.085  1.00104.80           C  
ANISOU 1343  C   GLY A 178     9774  13335  16709  -2437   2581   4383       C  
ATOM   1344  O   GLY A 178      54.402  20.375  19.227  1.00 99.81           O  
ANISOU 1344  O   GLY A 178     9233  13214  15475  -2078   2583   4090       O  
ATOM   1345  N   CYS A 179      54.363  22.214  17.922  1.00109.72           N  
ANISOU 1345  N   CYS A 179    10440  13815  17434  -2463   2754   5067       N  
ATOM   1346  CA  CYS A 179      53.980  21.524  16.687  1.00109.29           C  
ANISOU 1346  CA  CYS A 179    10567  14244  16714  -2073   2965   5500       C  
ATOM   1347  C   CYS A 179      55.216  20.904  16.027  1.00110.71           C  
ANISOU 1347  C   CYS A 179    10401  15188  16477  -2081   3293   5844       C  
ATOM   1348  O   CYS A 179      55.525  21.193  14.870  1.00114.71           O  
ANISOU 1348  O   CYS A 179    10823  15931  16830  -2127   3566   6528       O  
ATOM   1349  CB  CYS A 179      53.314  22.528  15.732  1.00115.26           C  
ANISOU 1349  CB  CYS A 179    11492  14551  17752  -2140   2992   6146       C  
ATOM   1350  SG  CYS A 179      52.376  21.840  14.328  1.00115.27           S  
ANISOU 1350  SG  CYS A 179    11867  14980  16950  -1654   3098   6589       S  
ATOM   1351  N   SER A 180      55.913  20.038  16.760  1.00107.16           N  
ANISOU 1351  N   SER A 180     9737  15147  15833  -2021   3277   5388       N  
ATOM   1352  CA  SER A 180      57.209  19.527  16.313  1.00108.75           C  
ANISOU 1352  CA  SER A 180     9507  16020  15794  -2052   3589   5660       C  
ATOM   1353  C   SER A 180      57.637  18.263  17.055  1.00103.09           C  
ANISOU 1353  C   SER A 180     8666  15767  14739  -1796   3519   5103       C  
ATOM   1354  O   SER A 180      57.255  18.044  18.206  1.00 96.96           O  
ANISOU 1354  O   SER A 180     8006  14742  14093  -1800   3188   4523       O  
ATOM   1355  CB  SER A 180      58.279  20.609  16.483  1.00114.72           C  
ANISOU 1355  CB  SER A 180     9783  16569  17236  -2634   3648   6025       C  
ATOM   1356  OG  SER A 180      58.281  21.122  17.804  1.00113.80           O  
ANISOU 1356  OG  SER A 180     9620  15925  17695  -2959   3279   5515       O  
ATOM   1357  N   THR A 181      58.455  17.449  16.389  1.00104.04           N  
ANISOU 1357  N   THR A 181     8530  16567  14434  -1573   3843   5303       N  
ATOM   1358  CA  THR A 181      58.968  16.204  16.966  1.00 99.90           C  
ANISOU 1358  CA  THR A 181     7830  16494  13633  -1295   3803   4861       C  
ATOM   1359  C   THR A 181      59.920  16.460  18.143  1.00 98.62           C  
ANISOU 1359  C   THR A 181     7202  16266  14005  -1691   3596   4652       C  
ATOM   1360  O   THR A 181      60.181  15.552  18.933  1.00 91.38           O  
ANISOU 1360  O   THR A 181     6176  15576  12970  -1526   3417   4232       O  
ATOM   1361  CB  THR A 181      59.697  15.343  15.901  1.00103.49           C  
ANISOU 1361  CB  THR A 181     8076  17674  13572   -943   4251   5131       C  
ATOM   1362  OG1 THR A 181      58.986  15.406  14.659  1.00105.12           O  
ANISOU 1362  OG1 THR A 181     8665  17968  13308   -712   4472   5459       O  
ATOM   1363  CG2 THR A 181      59.797  13.890  16.352  1.00 97.93           C  
ANISOU 1363  CG2 THR A 181     7377  17318  12512   -494   4161   4620       C  
ATOM   1364  N   LEU A 182      60.446  17.685  18.243  1.00103.12           N  
ANISOU 1364  N   LEU A 182     7491  16521  15168  -2228   3592   4971       N  
ATOM   1365  CA  LEU A 182      61.211  18.115  19.424  1.00103.81           C  
ANISOU 1365  CA  LEU A 182     7200  16431  15812  -2691   3299   4734       C  
ATOM   1366  C   LEU A 182      60.477  17.762  20.724  1.00 97.12           C  
ANISOU 1366  C   LEU A 182     6673  15304  14923  -2631   2844   4013       C  
ATOM   1367  O   LEU A 182      60.968  16.955  21.513  1.00 94.21           O  
ANISOU 1367  O   LEU A 182     6096  15258  14441  -2560   2667   3688       O  
ATOM   1368  CB  LEU A 182      61.509  19.626  19.380  1.00109.21           C  
ANISOU 1368  CB  LEU A 182     7707  16592  17195  -3296   3262   5100       C  
ATOM   1369  CG  LEU A 182      62.885  20.094  18.878  1.00116.21           C  
ANISOU 1369  CG  LEU A 182     7934  17776  18447  -3675   3533   5710       C  
ATOM   1370  CD1 LEU A 182      63.997  19.545  19.772  1.00116.22           C  
ANISOU 1370  CD1 LEU A 182     7402  18155  18601  -3821   3369   5460       C  
ATOM   1371  CD2 LEU A 182      63.123  19.708  17.418  1.00118.20           C  
ANISOU 1371  CD2 LEU A 182     8088  18591  18232  -3355   4086   6319       C  
ATOM   1372  N   ASN A 183      59.307  18.366  20.936  1.00 94.40           N  
ANISOU 1372  N   ASN A 183     6810  14383  14676  -2652   2667   3799       N  
ATOM   1373  CA  ASN A 183      58.464  18.033  22.085  1.00 88.61           C  
ANISOU 1373  CA  ASN A 183     6414  13423  13830  -2551   2306   3136       C  
ATOM   1374  C   ASN A 183      58.153  16.537  22.075  1.00 86.92           C  
ANISOU 1374  C   ASN A 183     6342  13704  12978  -2016   2316   2920       C  
ATOM   1375  O   ASN A 183      57.704  15.986  21.063  1.00 85.65           O  
ANISOU 1375  O   ASN A 183     6386  13742  12415  -1613   2551   3149       O  
ATOM   1376  CB  ASN A 183      57.177  18.878  22.091  1.00 84.93           C  
ANISOU 1376  CB  ASN A 183     6422  12291  13555  -2561   2211   3008       C  
ATOM   1377  CG  ASN A 183      55.989  18.163  22.746  1.00 75.69           C  
ANISOU 1377  CG  ASN A 183     5679  11072  12007  -2203   2012   2474       C  
ATOM   1378  OD1 ASN A 183      55.987  17.879  23.948  1.00 72.90           O  
ANISOU 1378  OD1 ASN A 183     5326  10749  11622  -2294   1746   1958       O  
ATOM   1379  ND2 ASN A 183      54.968  17.886  21.947  1.00 68.10           N  
ANISOU 1379  ND2 ASN A 183     5069  10057  10750  -1818   2131   2632       N  
ATOM   1380  N   GLN A 184      58.407  15.896  23.212  1.00 87.02           N  
ANISOU 1380  N   GLN A 184     6250  13904  12912  -2039   2031   2488       N  
ATOM   1381  CA  GLN A 184      58.359  14.438  23.329  1.00 86.36           C  
ANISOU 1381  CA  GLN A 184     6192  14285  12335  -1592   1994   2319       C  
ATOM   1382  C   GLN A 184      57.014  13.799  22.974  1.00 81.44           C  
ANISOU 1382  C   GLN A 184     6093  13569  11280  -1135   1997   2172       C  
ATOM   1383  O   GLN A 184      56.979  12.704  22.409  1.00 81.65           O  
ANISOU 1383  O   GLN A 184     6168  13942  10913   -709   2112   2232       O  
ATOM   1384  CB  GLN A 184      58.761  14.015  24.747  1.00 88.87           C  
ANISOU 1384  CB  GLN A 184     6329  14749  12689  -1770   1615   1915       C  
ATOM   1385  CG  GLN A 184      57.817  14.500  25.853  1.00 89.65           C  
ANISOU 1385  CG  GLN A 184     6785  14449  12828  -1963   1299   1427       C  
ATOM   1386  CD  GLN A 184      58.345  14.191  27.239  1.00 92.08           C  
ANISOU 1386  CD  GLN A 184     6890  14971  13127  -2216    922   1075       C  
ATOM   1387  OE1 GLN A 184      58.847  13.096  27.493  1.00 91.60           O  
ANISOU 1387  OE1 GLN A 184     6611  15360  12832  -2020    821   1104       O  
ATOM   1388  NE2 GLN A 184      58.232  15.156  28.146  1.00 95.42           N  
ANISOU 1388  NE2 GLN A 184     7388  15064  13804  -2653    694    736       N  
ATOM   1389  N   TYR A 185      55.914  14.468  23.306  1.00 77.78           N  
ANISOU 1389  N   TYR A 185     6004  12627  10922  -1219   1864   1965       N  
ATOM   1390  CA  TYR A 185      54.592  13.866  23.143  1.00 71.99           C  
ANISOU 1390  CA  TYR A 185     5720  11799   9834   -828   1806   1804       C  
ATOM   1391  C   TYR A 185      53.887  14.217  21.830  1.00 70.51           C  
ANISOU 1391  C   TYR A 185     5798  11434   9557   -627   2033   2171       C  
ATOM   1392  O   TYR A 185      52.693  13.993  21.694  1.00 63.37           O  
ANISOU 1392  O   TYR A 185     5259  10348   8470   -381   1950   2069       O  
ATOM   1393  CB  TYR A 185      53.689  14.226  24.330  1.00 70.00           C  
ANISOU 1393  CB  TYR A 185     5704  11197   9695   -965   1534   1339       C  
ATOM   1394  CG  TYR A 185      54.107  13.642  25.668  1.00 69.38           C  
ANISOU 1394  CG  TYR A 185     5470  11376   9518  -1093   1259    952       C  
ATOM   1395  CD1 TYR A 185      54.689  12.374  25.766  1.00 67.60           C  
ANISOU 1395  CD1 TYR A 185     5057  11641   8987   -873   1193    985       C  
ATOM   1396  CD2 TYR A 185      53.879  14.350  26.847  1.00 71.61           C  
ANISOU 1396  CD2 TYR A 185     5806  11404   9999  -1423   1052    543       C  
ATOM   1397  CE1 TYR A 185      55.050  11.845  27.001  1.00 67.83           C  
ANISOU 1397  CE1 TYR A 185     4936  11913   8925  -1005    901    700       C  
ATOM   1398  CE2 TYR A 185      54.233  13.827  28.086  1.00 71.35           C  
ANISOU 1398  CE2 TYR A 185     5652  11661   9797  -1566    777    210       C  
ATOM   1399  CZ  TYR A 185      54.818  12.578  28.156  1.00 69.55           C  
ANISOU 1399  CZ  TYR A 185     5220  11932   9274  -1366    688    330       C  
ATOM   1400  OH  TYR A 185      55.169  12.068  29.379  1.00 68.38           O  
ANISOU 1400  OH  TYR A 185     4939  12081   8961  -1522    381     73       O  
ATOM   1401  N   PHE A 186      54.623  14.732  20.852  1.00 78.47           N  
ANISOU 1401  N   PHE A 186     6604  12535  10675   -738   2309   2636       N  
ATOM   1402  CA  PHE A 186      54.026  15.081  19.564  1.00 82.14           C  
ANISOU 1402  CA  PHE A 186     7310  12899  11000   -578   2512   3054       C  
ATOM   1403  C   PHE A 186      53.588  13.837  18.786  1.00 78.48           C  
ANISOU 1403  C   PHE A 186     7083  12821   9915    -80   2581   3060       C  
ATOM   1404  O   PHE A 186      54.177  12.766  18.920  1.00 76.10           O  
ANISOU 1404  O   PHE A 186     6634  12940   9343    130   2604   2894       O  
ATOM   1405  CB  PHE A 186      55.015  15.901  18.727  1.00 90.82           C  
ANISOU 1405  CB  PHE A 186     8097  14084  12327   -849   2812   3603       C  
ATOM   1406  CG  PHE A 186      54.474  16.339  17.385  1.00 94.48           C  
ANISOU 1406  CG  PHE A 186     8790  14488  12619   -736   3015   4119       C  
ATOM   1407  CD1 PHE A 186      53.725  17.501  17.269  1.00 96.35           C  
ANISOU 1407  CD1 PHE A 186     9211  14138  13262   -940   2923   4325       C  
ATOM   1408  CD2 PHE A 186      54.728  15.591  16.238  1.00 96.62           C  
ANISOU 1408  CD2 PHE A 186     9092  15299  12320   -422   3291   4398       C  
ATOM   1409  CE1 PHE A 186      53.231  17.908  16.035  1.00 99.86           C  
ANISOU 1409  CE1 PHE A 186     9851  14546  13546   -852   3067   4870       C  
ATOM   1410  CE2 PHE A 186      54.237  15.991  15.000  1.00 99.57           C  
ANISOU 1410  CE2 PHE A 186     9693  15683  12455   -343   3453   4893       C  
ATOM   1411  CZ  PHE A 186      53.488  17.151  14.899  1.00101.30           C  
ANISOU 1411  CZ  PHE A 186    10078  15328  13083   -569   3323   5166       C  
ATOM   1412  N   GLY A 187      52.534  13.991  17.988  1.00 78.19           N  
ANISOU 1412  N   GLY A 187     7412  12607   9689    105   2579   3244       N  
ATOM   1413  CA  GLY A 187      52.143  12.982  17.011  1.00 76.13           C  
ANISOU 1413  CA  GLY A 187     7401  12693   8832    526   2650   3313       C  
ATOM   1414  C   GLY A 187      51.694  11.659  17.585  1.00 70.75           C  
ANISOU 1414  C   GLY A 187     6872  12151   7859    844   2419   2851       C  
ATOM   1415  O   GLY A 187      51.634  11.479  18.799  1.00 69.90           O  
ANISOU 1415  O   GLY A 187     6679  11910   7971    746   2200   2494       O  
ATOM   1416  N   TYR A 188      51.384  10.730  16.688  1.00 70.18           N  
ANISOU 1416  N   TYR A 188     7034  12354   7276   1212   2458   2869       N  
ATOM   1417  CA  TYR A 188      50.846   9.423  17.058  1.00 64.54           C  
ANISOU 1417  CA  TYR A 188     6507  11718   6296   1531   2211   2481       C  
ATOM   1418  C   TYR A 188      51.619   8.817  18.224  1.00 62.05           C  
ANISOU 1418  C   TYR A 188     5883  11524   6169   1487   2116   2166       C  
ATOM   1419  O   TYR A 188      51.051   8.535  19.284  1.00 57.18           O  
ANISOU 1419  O   TYR A 188     5319  10715   5690   1446   1824   1883       O  
ATOM   1420  CB  TYR A 188      50.912   8.462  15.866  1.00 67.47           C  
ANISOU 1420  CB  TYR A 188     7074  12453   6109   1910   2340   2513       C  
ATOM   1421  CG  TYR A 188      50.006   8.804  14.693  1.00 70.00           C  
ANISOU 1421  CG  TYR A 188     7768  12721   6109   1996   2339   2793       C  
ATOM   1422  CD1 TYR A 188      50.535   9.117  13.439  1.00 74.64           C  
ANISOU 1422  CD1 TYR A 188     8366  13640   6353   2031   2675   3152       C  
ATOM   1423  CD2 TYR A 188      48.622   8.794  14.833  1.00 66.16           C  
ANISOU 1423  CD2 TYR A 188     7601  11894   5642   2039   1998   2728       C  
ATOM   1424  CE1 TYR A 188      49.699   9.413  12.357  1.00 77.37           C  
ANISOU 1424  CE1 TYR A 188     9066  13983   6349   2092   2630   3445       C  
ATOM   1425  CE2 TYR A 188      47.788   9.096  13.770  1.00 66.13           C  
ANISOU 1425  CE2 TYR A 188     7912  11853   5360   2107   1941   3018       C  
ATOM   1426  CZ  TYR A 188      48.324   9.398  12.534  1.00 72.44           C  
ANISOU 1426  CZ  TYR A 188     8751  12990   5784   2128   2237   3377       C  
ATOM   1427  OH  TYR A 188      47.482   9.689  11.485  1.00 74.23           O  
ANISOU 1427  OH  TYR A 188     9301  13216   5688   2176   2135   3698       O  
ATOM   1428  N   SER A 189      52.921   8.640  18.022  1.00 64.82           N  
ANISOU 1428  N   SER A 189     5883  12223   6523   1487   2368   2255       N  
ATOM   1429  CA  SER A 189      53.760   7.914  18.972  1.00 66.33           C  
ANISOU 1429  CA  SER A 189     5742  12598   6861   1501   2267   2015       C  
ATOM   1430  C   SER A 189      53.966   8.678  20.279  1.00 66.47           C  
ANISOU 1430  C   SER A 189     5532  12405   7317   1079   2079   1916       C  
ATOM   1431  O   SER A 189      53.995   8.075  21.353  1.00 64.95           O  
ANISOU 1431  O   SER A 189     5253  12233   7193   1068   1811   1650       O  
ATOM   1432  CB  SER A 189      55.107   7.551  18.340  1.00 70.42           C  
ANISOU 1432  CB  SER A 189     5892  13558   7306   1639   2612   2164       C  
ATOM   1433  OG  SER A 189      55.659   8.649  17.640  1.00 75.14           O  
ANISOU 1433  OG  SER A 189     6313  14232   8004   1393   2946   2554       O  
ATOM   1434  N   GLY A 190      54.095   9.997  20.193  1.00 68.43           N  
ANISOU 1434  N   GLY A 190     5700  12446   7855    723   2201   2129       N  
ATOM   1435  CA  GLY A 190      54.254  10.817  21.391  1.00 68.83           C  
ANISOU 1435  CA  GLY A 190     5582  12251   8320    302   2014   1973       C  
ATOM   1436  C   GLY A 190      52.985  10.847  22.226  1.00 65.30           C  
ANISOU 1436  C   GLY A 190     5467  11469   7874    296   1721   1655       C  
ATOM   1437  O   GLY A 190      53.026  10.670  23.452  1.00 64.89           O  
ANISOU 1437  O   GLY A 190     5329  11418   7908    146   1481   1351       O  
ATOM   1438  N   ALA A 191      51.855  11.068  21.558  1.00 61.66           N  
ANISOU 1438  N   ALA A 191     5367  10760   7301    457   1743   1747       N  
ATOM   1439  CA  ALA A 191      50.551  11.050  22.210  1.00 56.04           C  
ANISOU 1439  CA  ALA A 191     4947   9755   6592    507   1511   1490       C  
ATOM   1440  C   ALA A 191      50.391   9.804  23.074  1.00 52.65           C  
ANISOU 1440  C   ALA A 191     4523   9552   5931    672   1271   1191       C  
ATOM   1441  O   ALA A 191      49.898   9.888  24.192  1.00 53.21           O  
ANISOU 1441  O   ALA A 191     4627   9508   6082    538   1082    914       O  
ATOM   1442  CB  ALA A 191      49.456  11.105  21.177  1.00 56.02           C  
ANISOU 1442  CB  ALA A 191     5279   9572   6432    746   1546   1696       C  
ATOM   1443  N   PHE A 192      50.816   8.655  22.554  1.00 49.72           N  
ANISOU 1443  N   PHE A 192     4115   9499   5275    965   1285   1253       N  
ATOM   1444  CA  PHE A 192      50.740   7.397  23.292  1.00 45.49           C  
ANISOU 1444  CA  PHE A 192     3563   9149   4572   1134   1037   1041       C  
ATOM   1445  C   PHE A 192      51.720   7.356  24.453  1.00 49.89           C  
ANISOU 1445  C   PHE A 192     3767   9898   5289    885    921    910       C  
ATOM   1446  O   PHE A 192      51.412   6.800  25.509  1.00 47.31           O  
ANISOU 1446  O   PHE A 192     3443   9627   4905    848    658    720       O  
ATOM   1447  CB  PHE A 192      51.012   6.206  22.371  1.00 45.59           C  
ANISOU 1447  CB  PHE A 192     3623   9390   4310   1532   1086   1117       C  
ATOM   1448  CG  PHE A 192      51.017   4.884  23.085  1.00 44.54           C  
ANISOU 1448  CG  PHE A 192     3445   9388   4090   1711    812    946       C  
ATOM   1449  CD1 PHE A 192      49.836   4.325  23.540  1.00 41.90           C  
ANISOU 1449  CD1 PHE A 192     3368   8890   3661   1792    540    828       C  
ATOM   1450  CD2 PHE A 192      52.201   4.210  23.322  1.00 49.83           C  
ANISOU 1450  CD2 PHE A 192     3779  10333   4820   1788    815    946       C  
ATOM   1451  CE1 PHE A 192      49.824   3.109  24.215  1.00 40.88           C  
ANISOU 1451  CE1 PHE A 192     3188   8856   3488   1926    265    736       C  
ATOM   1452  CE2 PHE A 192      52.200   2.988  23.995  1.00 51.80           C  
ANISOU 1452  CE2 PHE A 192     3976  10659   5047   1953    527    842       C  
ATOM   1453  CZ  PHE A 192      51.001   2.437  24.440  1.00 44.37           C  
ANISOU 1453  CZ  PHE A 192     3320   9538   4002   2010    246    749       C  
ATOM   1454  N   LYS A 193      52.911   7.916  24.257  1.00 56.32           N  
ANISOU 1454  N   LYS A 193     4258  10847   6293    697   1099   1048       N  
ATOM   1455  CA  LYS A 193      53.898   7.974  25.339  1.00 58.27           C  
ANISOU 1455  CA  LYS A 193     4135  11285   6720    411    947    951       C  
ATOM   1456  C   LYS A 193      53.267   8.708  26.528  1.00 56.16           C  
ANISOU 1456  C   LYS A 193     3989  10803   6546     73    742    676       C  
ATOM   1457  O   LYS A 193      53.347   8.258  27.666  1.00 55.28           O  
ANISOU 1457  O   LYS A 193     3793  10856   6355    -41    474    488       O  
ATOM   1458  CB  LYS A 193      55.192   8.661  24.882  1.00 62.11           C  
ANISOU 1458  CB  LYS A 193     4232  11901   7464    203   1179   1178       C  
ATOM   1459  CG  LYS A 193      56.461   7.915  25.291  1.00 66.01           C  
ANISOU 1459  CG  LYS A 193     4263  12785   8032    220   1095   1232       C  
ATOM   1460  CD  LYS A 193      57.739   8.715  24.988  1.00 71.46           C  
ANISOU 1460  CD  LYS A 193     4497  13608   9046    -65   1303   1473       C  
ATOM   1461  CE  LYS A 193      58.204   9.533  26.196  1.00 74.12           C  
ANISOU 1461  CE  LYS A 193     4609  13884   9670   -599   1034   1330       C  
ATOM   1462  NZ  LYS A 193      59.058  10.695  25.809  1.00 79.42           N  
ANISOU 1462  NZ  LYS A 193     4967  14488  10722   -974   1229   1562       N  
ATOM   1463  N   CYS A 194      52.614   9.827  26.228  1.00 54.77           N  
ANISOU 1463  N   CYS A 194     4019  10262   6528    -67    876    660       N  
ATOM   1464  CA  CYS A 194      51.849  10.603  27.200  1.00 52.63           C  
ANISOU 1464  CA  CYS A 194     3916   9721   6362   -316    753    348       C  
ATOM   1465  C   CYS A 194      51.006   9.700  28.106  1.00 46.51           C  
ANISOU 1465  C   CYS A 194     3304   9080   5288   -178    521    118       C  
ATOM   1466  O   CYS A 194      51.082   9.796  29.330  1.00 42.26           O  
ANISOU 1466  O   CYS A 194     2704   8653   4698   -423    336   -154       O  
ATOM   1467  CB  CYS A 194      50.972  11.597  26.429  1.00 53.88           C  
ANISOU 1467  CB  CYS A 194     4328   9428   6714   -286    945    437       C  
ATOM   1468  SG  CYS A 194      49.909  12.661  27.370  1.00 53.25           S  
ANISOU 1468  SG  CYS A 194     4465   8916   6851   -493    887     48       S  
ATOM   1469  N   LEU A 195      50.223   8.816  27.491  1.00 44.48           N  
ANISOU 1469  N   LEU A 195     3249   8833   4817    193    520    244       N  
ATOM   1470  CA  LEU A 195      49.388   7.853  28.217  1.00 41.14           C  
ANISOU 1470  CA  LEU A 195     2959   8531   4139    335    302    120       C  
ATOM   1471  C   LEU A 195      50.242   6.828  28.937  1.00 43.54           C  
ANISOU 1471  C   LEU A 195     3020   9222   4300    317     75    134       C  
ATOM   1472  O   LEU A 195      50.034   6.546  30.113  1.00 47.07           O  
ANISOU 1472  O   LEU A 195     3443   9838   4602    166   -135    -23       O  
ATOM   1473  CB  LEU A 195      48.441   7.127  27.256  1.00 39.64           C  
ANISOU 1473  CB  LEU A 195     3020   8230   3814    714    319    288       C  
ATOM   1474  CG  LEU A 195      47.577   5.977  27.807  1.00 40.46           C  
ANISOU 1474  CG  LEU A 195     3239   8436   3699    882     79    251       C  
ATOM   1475  CD1 LEU A 195      46.791   6.407  29.062  1.00 39.07           C  
ANISOU 1475  CD1 LEU A 195     3107   8245   3491    664      8     15       C  
ATOM   1476  CD2 LEU A 195      46.619   5.445  26.729  1.00 37.24           C  
ANISOU 1476  CD2 LEU A 195     3087   7848   3216   1208     76    408       C  
ATOM   1477  N   LYS A 196      51.196   6.263  28.212  1.00 47.17           N  
ANISOU 1477  N   LYS A 196     3288   9838   4797    485    126    342       N  
ATOM   1478  CA  LYS A 196      52.104   5.277  28.764  1.00 52.09           C  
ANISOU 1478  CA  LYS A 196     3625  10793   5374    517    -86    410       C  
ATOM   1479  C   LYS A 196      52.796   5.831  30.009  1.00 54.23           C  
ANISOU 1479  C   LYS A 196     3649  11253   5701     91   -257    271       C  
ATOM   1480  O   LYS A 196      52.896   5.146  31.025  1.00 55.96           O  
ANISOU 1480  O   LYS A 196     3768  11720   5773     15   -549    246       O  
ATOM   1481  CB  LYS A 196      53.146   4.887  27.708  1.00 59.27           C  
ANISOU 1481  CB  LYS A 196     4308  11816   6395    751     93    621       C  
ATOM   1482  CG  LYS A 196      54.083   3.747  28.110  1.00 63.61           C  
ANISOU 1482  CG  LYS A 196     4529  12663   6977    888   -110    723       C  
ATOM   1483  CD  LYS A 196      55.261   3.634  27.145  1.00 68.91           C  
ANISOU 1483  CD  LYS A 196     4890  13476   7815   1073    147    895       C  
ATOM   1484  CE  LYS A 196      56.120   2.406  27.440  1.00 72.80           C  
ANISOU 1484  CE  LYS A 196     5046  14210   8406   1304    -41    998       C  
ATOM   1485  NZ  LYS A 196      56.442   2.265  28.894  1.00 75.34           N  
ANISOU 1485  NZ  LYS A 196     5137  14718   8771    996   -435    999       N  
ATOM   1486  N   ASP A 197      53.251   7.078  29.924  1.00 54.34           N  
ANISOU 1486  N   ASP A 197     3575  11142   5927   -207   -103    194       N  
ATOM   1487  CA  ASP A 197      54.051   7.685  30.980  1.00 58.45           C  
ANISOU 1487  CA  ASP A 197     3848  11825   6534   -647   -282     41       C  
ATOM   1488  C   ASP A 197      53.243   8.044  32.229  1.00 59.12           C  
ANISOU 1488  C   ASP A 197     4151  11907   6406   -898   -461   -305       C  
ATOM   1489  O   ASP A 197      53.800   8.128  33.320  1.00 61.24           O  
ANISOU 1489  O   ASP A 197     4252  12436   6582  -1221   -717   -449       O  
ATOM   1490  CB  ASP A 197      54.782   8.931  30.450  1.00 64.53           C  
ANISOU 1490  CB  ASP A 197     4456  12405   7657   -914    -75     74       C  
ATOM   1491  CG  ASP A 197      56.016   8.587  29.600  1.00 69.11           C  
ANISOU 1491  CG  ASP A 197     4644  13181   8432   -796     58    417       C  
ATOM   1492  OD1 ASP A 197      56.130   7.444  29.102  1.00 67.94           O  
ANISOU 1492  OD1 ASP A 197     4438  13216   8159   -403     81    601       O  
ATOM   1493  OD2 ASP A 197      56.883   9.472  29.433  1.00 74.16           O  
ANISOU 1493  OD2 ASP A 197     5017  13785   9377  -1098    148    496       O  
ATOM   1494  N   GLY A 198      51.940   8.256  32.072  1.00 57.37           N  
ANISOU 1494  N   GLY A 198     4284  11421   6092   -750   -324   -438       N  
ATOM   1495  CA  GLY A 198      51.090   8.652  33.190  1.00 56.70           C  
ANISOU 1495  CA  GLY A 198     4401  11338   5803   -944   -405   -792       C  
ATOM   1496  C   GLY A 198      50.634  10.095  33.099  1.00 57.65           C  
ANISOU 1496  C   GLY A 198     4694  11037   6172  -1122   -190  -1087       C  
ATOM   1497  O   GLY A 198      49.725  10.509  33.817  1.00 58.97           O  
ANISOU 1497  O   GLY A 198     5070  11122   6216  -1189   -158  -1417       O  
ATOM   1498  N   ALA A 199      51.262  10.869  32.222  1.00 58.82           N  
ANISOU 1498  N   ALA A 199     4742  10914   6695  -1192    -29   -958       N  
ATOM   1499  CA  ALA A 199      50.848  12.246  31.991  1.00 61.47           C  
ANISOU 1499  CA  ALA A 199     5229  10756   7370  -1339    164  -1162       C  
ATOM   1500  C   ALA A 199      49.332  12.323  31.844  1.00 59.64           C  
ANISOU 1500  C   ALA A 199     5315  10258   7086  -1065    314  -1265       C  
ATOM   1501  O   ALA A 199      48.669  13.044  32.591  1.00 60.27           O  
ANISOU 1501  O   ALA A 199     5548  10148   7205  -1190    353  -1666       O  
ATOM   1502  CB  ALA A 199      51.519  12.797  30.752  1.00 62.34           C  
ANISOU 1502  CB  ALA A 199     5204  10620   7861  -1338    350   -818       C  
ATOM   1503  N   GLY A 200      48.798  11.553  30.894  1.00 54.91           N  
ANISOU 1503  N   GLY A 200     4799   9661   6401   -688    391   -921       N  
ATOM   1504  CA  GLY A 200      47.368  11.559  30.589  1.00 50.84           C  
ANISOU 1504  CA  GLY A 200     4537   8899   5882   -414    505   -926       C  
ATOM   1505  C   GLY A 200      46.613  10.268  30.874  1.00 45.11           C  
ANISOU 1505  C   GLY A 200     3884   8469   4785   -164    374   -846       C  
ATOM   1506  O   GLY A 200      47.214   9.220  31.141  1.00 43.55           O  
ANISOU 1506  O   GLY A 200     3559   8651   4338   -143    189   -721       O  
ATOM   1507  N   ASP A 201      45.284  10.371  30.798  1.00 40.99           N  
ANISOU 1507  N   ASP A 201     3543   7741   4291     24    462   -889       N  
ATOM   1508  CA  ASP A 201      44.356   9.279  31.086  1.00 40.86           C  
ANISOU 1508  CA  ASP A 201     3592   7938   3995    231    349   -800       C  
ATOM   1509  C   ASP A 201      43.843   8.583  29.839  1.00 39.95           C  
ANISOU 1509  C   ASP A 201     3576   7701   3903    558    319   -428       C  
ATOM   1510  O   ASP A 201      43.488   7.404  29.889  1.00 41.93           O  
ANISOU 1510  O   ASP A 201     3840   8158   3934    712    145   -273       O  
ATOM   1511  CB  ASP A 201      43.130   9.827  31.806  1.00 45.20           C  
ANISOU 1511  CB  ASP A 201     4234   8361   4580    233    476  -1078       C  
ATOM   1512  CG  ASP A 201      43.468  10.491  33.094  1.00 49.11           C  
ANISOU 1512  CG  ASP A 201     4686   8996   4977    -73    514  -1531       C  
ATOM   1513  OD1 ASP A 201      44.158   9.847  33.907  1.00 51.26           O  
ANISOU 1513  OD1 ASP A 201     4859   9705   4914   -251    329  -1574       O  
ATOM   1514  OD2 ASP A 201      43.034  11.645  33.295  1.00 54.43           O  
ANISOU 1514  OD2 ASP A 201     5430   9338   5913   -131    711  -1849       O  
ATOM   1515  N   VAL A 202      43.740   9.342  28.750  1.00 39.97           N  
ANISOU 1515  N   VAL A 202     3658   7353   4174    647    467   -284       N  
ATOM   1516  CA  VAL A 202      43.285   8.840  27.457  1.00 38.13           C  
ANISOU 1516  CA  VAL A 202     3551   7008   3927    931    434     53       C  
ATOM   1517  C   VAL A 202      44.165   9.458  26.381  1.00 42.35           C  
ANISOU 1517  C   VAL A 202     4073   7414   4605    907    573    250       C  
ATOM   1518  O   VAL A 202      44.504  10.639  26.468  1.00 47.35           O  
ANISOU 1518  O   VAL A 202     4652   7819   5520    707    724    169       O  
ATOM   1519  CB  VAL A 202      41.789   9.211  27.173  1.00 36.39           C  
ANISOU 1519  CB  VAL A 202     3464   6485   3878   1091    469    109       C  
ATOM   1520  CG1 VAL A 202      41.487  10.663  27.539  1.00 36.37           C  
ANISOU 1520  CG1 VAL A 202     3444   6134   4241    953    673   -100       C  
ATOM   1521  CG2 VAL A 202      41.442   8.967  25.723  1.00 35.36           C  
ANISOU 1521  CG2 VAL A 202     3476   6214   3746   1323    418    463       C  
ATOM   1522  N   ALA A 203      44.543   8.659  25.383  1.00 42.12           N  
ANISOU 1522  N   ALA A 203     4088   7532   4385   1103    527    500       N  
ATOM   1523  CA  ALA A 203      45.281   9.161  24.225  1.00 42.73           C  
ANISOU 1523  CA  ALA A 203     4159   7558   4521   1114    697    747       C  
ATOM   1524  C   ALA A 203      44.507   8.841  22.960  1.00 45.00           C  
ANISOU 1524  C   ALA A 203     4674   7754   4670   1385    664   1015       C  
ATOM   1525  O   ALA A 203      43.898   7.776  22.859  1.00 48.34           O  
ANISOU 1525  O   ALA A 203     5217   8277   4872   1591    472   1006       O  
ATOM   1526  CB  ALA A 203      46.653   8.551  24.168  1.00 43.00           C  
ANISOU 1526  CB  ALA A 203     4002   7931   4407   1094    723    770       C  
ATOM   1527  N   PHE A 204      44.536   9.764  22.003  1.00 46.23           N  
ANISOU 1527  N   PHE A 204     4889   7720   4958   1358    822   1272       N  
ATOM   1528  CA  PHE A 204      43.767   9.636  20.770  1.00 46.38           C  
ANISOU 1528  CA  PHE A 204     5136   7660   4826   1574    768   1562       C  
ATOM   1529  C   PHE A 204      44.725   9.383  19.606  1.00 49.35           C  
ANISOU 1529  C   PHE A 204     5534   8306   4910   1657    917   1794       C  
ATOM   1530  O   PHE A 204      45.495  10.261  19.207  1.00 49.94           O  
ANISOU 1530  O   PHE A 204     5493   8365   5117   1494   1145   1994       O  
ATOM   1531  CB  PHE A 204      42.914  10.891  20.532  1.00 46.67           C  
ANISOU 1531  CB  PHE A 204     5227   7276   5228   1499    811   1744       C  
ATOM   1532  CG  PHE A 204      41.928  11.165  21.631  1.00 43.92           C  
ANISOU 1532  CG  PHE A 204     4841   6678   5170   1465    725   1487       C  
ATOM   1533  CD1 PHE A 204      40.688  10.557  21.635  1.00 43.25           C  
ANISOU 1533  CD1 PHE A 204     4862   6555   5017   1656    522   1495       C  
ATOM   1534  CD2 PHE A 204      42.248  12.012  22.676  1.00 46.86           C  
ANISOU 1534  CD2 PHE A 204     5057   6877   5871   1235    851   1217       C  
ATOM   1535  CE1 PHE A 204      39.777  10.796  22.661  1.00 41.85           C  
ANISOU 1535  CE1 PHE A 204     4606   6202   5093   1638    498   1268       C  
ATOM   1536  CE2 PHE A 204      41.334  12.256  23.707  1.00 45.49           C  
ANISOU 1536  CE2 PHE A 204     4852   6522   5910   1227    822    928       C  
ATOM   1537  CZ  PHE A 204      40.103  11.649  23.695  1.00 40.60           C  
ANISOU 1537  CZ  PHE A 204     4309   5901   5216   1439    671    969       C  
ATOM   1538  N   VAL A 205      44.659   8.169  19.064  1.00 48.58           N  
ANISOU 1538  N   VAL A 205     5582   8453   4422   1911    794   1760       N  
ATOM   1539  CA  VAL A 205      45.666   7.677  18.135  1.00 49.88           C  
ANISOU 1539  CA  VAL A 205     5745   8953   4252   2043    965   1852       C  
ATOM   1540  C   VAL A 205      45.042   6.744  17.090  1.00 50.31           C  
ANISOU 1540  C   VAL A 205     6114   9120   3881   2338    801   1885       C  
ATOM   1541  O   VAL A 205      43.820   6.539  17.089  1.00 50.15           O  
ANISOU 1541  O   VAL A 205     6287   8897   3872   2403    525   1885       O  
ATOM   1542  CB  VAL A 205      46.775   6.942  18.924  1.00 48.56           C  
ANISOU 1542  CB  VAL A 205     5324   9037   4092   2043   1009   1601       C  
ATOM   1543  CG1 VAL A 205      47.603   7.937  19.732  1.00 48.03           C  
ANISOU 1543  CG1 VAL A 205     4942   8923   4384   1716   1177   1601       C  
ATOM   1544  CG2 VAL A 205      46.174   5.889  19.846  1.00 43.60           C  
ANISOU 1544  CG2 VAL A 205     4737   8369   3461   2142    697   1329       C  
ATOM   1545  N   LYS A 206      45.866   6.201  16.192  1.00 50.17           N  
ANISOU 1545  N   LYS A 206     6139   9429   3494   2512    971   1902       N  
ATOM   1546  CA  LYS A 206      45.398   5.175  15.259  1.00 51.36           C  
ANISOU 1546  CA  LYS A 206     6610   9707   3199   2803    801   1816       C  
ATOM   1547  C   LYS A 206      45.357   3.857  15.992  1.00 48.16           C  
ANISOU 1547  C   LYS A 206     6192   9283   2823   2966    555   1454       C  
ATOM   1548  O   LYS A 206      46.048   3.678  16.989  1.00 46.35           O  
ANISOU 1548  O   LYS A 206     5682   9086   2845   2894    608   1311       O  
ATOM   1549  CB  LYS A 206      46.337   4.987  14.058  1.00 59.81           C  
ANISOU 1549  CB  LYS A 206     7737  11169   3818   2968   1111   1888       C  
ATOM   1550  CG  LYS A 206      46.772   6.244  13.351  1.00 64.44           C  
ANISOU 1550  CG  LYS A 206     8245  11872   4367   2781   1440   2310       C  
ATOM   1551  CD  LYS A 206      47.428   5.952  11.996  1.00 72.15           C  
ANISOU 1551  CD  LYS A 206     9355  13303   4755   2976   1728   2405       C  
ATOM   1552  CE  LYS A 206      48.844   5.409  12.125  1.00 75.73           C  
ANISOU 1552  CE  LYS A 206     9511  14098   5167   3108   2074   2207       C  
ATOM   1553  NZ  LYS A 206      49.687   6.215  13.048  1.00 75.12           N  
ANISOU 1553  NZ  LYS A 206     8978  13951   5614   2820   2269   2342       N  
ATOM   1554  N   HIS A 207      44.569   2.929  15.468  1.00 50.94           N  
ANISOU 1554  N   HIS A 207     6847   9583   2926   3171    260   1329       N  
ATOM   1555  CA  HIS A 207      44.544   1.543  15.944  1.00 52.47           C  
ANISOU 1555  CA  HIS A 207     7070   9731   3137   3357      0   1012       C  
ATOM   1556  C   HIS A 207      45.911   0.874  15.904  1.00 54.65           C  
ANISOU 1556  C   HIS A 207     7172  10258   3333   3549    236    810       C  
ATOM   1557  O   HIS A 207      46.203   0.023  16.733  1.00 53.96           O  
ANISOU 1557  O   HIS A 207     6932  10110   3459   3619     87    621       O  
ATOM   1558  CB  HIS A 207      43.596   0.708  15.084  1.00 55.87           C  
ANISOU 1558  CB  HIS A 207     7889  10069   3269   3545   -340    911       C  
ATOM   1559  CG  HIS A 207      44.075   0.512  13.677  1.00 60.39           C  
ANISOU 1559  CG  HIS A 207     8710  10914   3320   3761   -161    851       C  
ATOM   1560  ND1 HIS A 207      44.373  -0.729  13.159  1.00 64.60           N  
ANISOU 1560  ND1 HIS A 207     9438  11517   3590   4062   -257    497       N  
ATOM   1561  CD2 HIS A 207      44.331   1.403  12.692  1.00 62.36           C  
ANISOU 1561  CD2 HIS A 207     9044  11402   3248   3720    125   1098       C  
ATOM   1562  CE1 HIS A 207      44.771  -0.595  11.906  1.00 70.00           C  
ANISOU 1562  CE1 HIS A 207    10332  12507   3757   4209    -17    485       C  
ATOM   1563  NE2 HIS A 207      44.750   0.689  11.598  1.00 69.65           N  
ANISOU 1563  NE2 HIS A 207    10220  12592   3650   3993    215    883       N  
ATOM   1564  N   SER A 208      46.733   1.239  14.926  1.00 59.10           N  
ANISOU 1564  N   SER A 208     7738  11117   3600   3643    605    881       N  
ATOM   1565  CA  SER A 208      48.046   0.621  14.768  1.00 63.68           C  
ANISOU 1565  CA  SER A 208     8116  11972   4109   3870    885    695       C  
ATOM   1566  C   SER A 208      49.093   1.217  15.706  1.00 61.41           C  
ANISOU 1566  C   SER A 208     7345  11786   4201   3667   1125    814       C  
ATOM   1567  O   SER A 208      50.106   0.579  15.987  1.00 62.92           O  
ANISOU 1567  O   SER A 208     7269  12134   4504   3831   1246    664       O  
ATOM   1568  CB  SER A 208      48.522   0.754  13.321  1.00 69.79           C  
ANISOU 1568  CB  SER A 208     9060  13092   4366   4058   1233    728       C  
ATOM   1569  OG  SER A 208      48.885   2.091  13.032  1.00 71.88           O  
ANISOU 1569  OG  SER A 208     9166  13526   4619   3802   1569   1118       O  
ATOM   1570  N   THR A 209      48.848   2.433  16.189  1.00 59.26           N  
ANISOU 1570  N   THR A 209     6953  11407   4156   3315   1168   1073       N  
ATOM   1571  CA  THR A 209      49.833   3.162  16.996  1.00 59.58           C  
ANISOU 1571  CA  THR A 209     6560  11538   4540   3061   1378   1186       C  
ATOM   1572  C   THR A 209      50.403   2.366  18.167  1.00 54.30           C  
ANISOU 1572  C   THR A 209     5602  10878   4152   3087   1209    984       C  
ATOM   1573  O   THR A 209      51.599   2.433  18.443  1.00 54.80           O  
ANISOU 1573  O   THR A 209     5285  11161   4375   3053   1415   1014       O  
ATOM   1574  CB  THR A 209      49.247   4.458  17.570  1.00 58.60           C  
ANISOU 1574  CB  THR A 209     6408  11167   4692   2679   1331   1385       C  
ATOM   1575  OG1 THR A 209      48.607   5.208  16.528  1.00 61.85           O  
ANISOU 1575  OG1 THR A 209     7081  11517   4903   2650   1423   1636       O  
ATOM   1576  CG2 THR A 209      50.355   5.301  18.208  1.00 59.01           C  
ANISOU 1576  CG2 THR A 209     6037  11317   5067   2389   1556   1493       C  
ATOM   1577  N   ILE A 210      49.552   1.627  18.864  1.00 51.17           N  
ANISOU 1577  N   ILE A 210     5355  10256   3833   3127    821    828       N  
ATOM   1578  CA  ILE A 210      50.010   0.873  20.023  1.00 48.02           C  
ANISOU 1578  CA  ILE A 210     4691   9866   3687   3123    613    708       C  
ATOM   1579  C   ILE A 210      50.904  -0.270  19.582  1.00 51.38           C  
ANISOU 1579  C   ILE A 210     5004  10451   4069   3496    680    561       C  
ATOM   1580  O   ILE A 210      51.931  -0.535  20.211  1.00 55.10           O  
ANISOU 1580  O   ILE A 210     5089  11075   4772   3498    717    565       O  
ATOM   1581  CB  ILE A 210      48.848   0.322  20.875  1.00 41.70           C  
ANISOU 1581  CB  ILE A 210     4063   8808   2972   3061    189    638       C  
ATOM   1582  CG1 ILE A 210      49.365  -0.074  22.262  1.00 39.58           C  
ANISOU 1582  CG1 ILE A 210     3471   8607   2959   2921      1    620       C  
ATOM   1583  CG2 ILE A 210      48.174  -0.860  20.184  1.00 42.13           C  
ANISOU 1583  CG2 ILE A 210     4440   8712   2855   3386    -41    500       C  
ATOM   1584  CD1 ILE A 210      48.319  -0.614  23.183  1.00 35.84           C  
ANISOU 1584  CD1 ILE A 210     3111   7955   2549   2830   -377    607       C  
ATOM   1585  N   PHE A 211      50.524  -0.931  18.495  1.00 51.97           N  
ANISOU 1585  N   PHE A 211     5406  10486   3854   3817    687    419       N  
ATOM   1586  CA  PHE A 211      51.244  -2.113  18.034  1.00 55.81           C  
ANISOU 1586  CA  PHE A 211     5842  11056   4308   4233    739    192       C  
ATOM   1587  C   PHE A 211      52.663  -1.734  17.630  1.00 59.98           C  
ANISOU 1587  C   PHE A 211     5990  11955   4845   4318   1216    258       C  
ATOM   1588  O   PHE A 211      53.610  -2.495  17.846  1.00 60.05           O  
ANISOU 1588  O   PHE A 211     5690  12064   5061   4562   1274    150       O  
ATOM   1589  CB  PHE A 211      50.492  -2.790  16.878  1.00 57.08           C  
ANISOU 1589  CB  PHE A 211     6487  11101   4099   4533    652    -31       C  
ATOM   1590  CG  PHE A 211      49.239  -3.510  17.313  1.00 55.12           C  
ANISOU 1590  CG  PHE A 211     6533  10470   3938   4506    130   -118       C  
ATOM   1591  CD1 PHE A 211      49.263  -4.874  17.584  1.00 56.70           C  
ANISOU 1591  CD1 PHE A 211     6761  10448   4335   4769   -172   -344       C  
ATOM   1592  CD2 PHE A 211      48.039  -2.824  17.472  1.00 50.58           C  
ANISOU 1592  CD2 PHE A 211     6171   9737   3309   4216    -64     54       C  
ATOM   1593  CE1 PHE A 211      48.111  -5.542  18.000  1.00 52.35           C  
ANISOU 1593  CE1 PHE A 211     6445   9539   3907   4704   -664   -368       C  
ATOM   1594  CE2 PHE A 211      46.889  -3.490  17.883  1.00 47.13           C  
ANISOU 1594  CE2 PHE A 211     5944   8979   2982   4177   -527     15       C  
ATOM   1595  CZ  PHE A 211      46.931  -4.847  18.151  1.00 47.42           C  
ANISOU 1595  CZ  PHE A 211     6005   8813   3199   4400   -830   -181       C  
ATOM   1596  N   GLU A 212      52.797  -0.535  17.071  1.00 64.63           N  
ANISOU 1596  N   GLU A 212     6565  12732   5258   4104   1547    479       N  
ATOM   1597  CA  GLU A 212      54.095   0.000  16.668  1.00 70.92           C  
ANISOU 1597  CA  GLU A 212     6966  13905   6076   4106   2027    631       C  
ATOM   1598  C   GLU A 212      54.942   0.424  17.867  1.00 70.24           C  
ANISOU 1598  C   GLU A 212     6352  13877   6460   3813   1992    789       C  
ATOM   1599  O   GLU A 212      56.131   0.675  17.708  1.00 74.96           O  
ANISOU 1599  O   GLU A 212     6518  14779   7183   3823   2329    913       O  
ATOM   1600  CB  GLU A 212      53.913   1.192  15.720  1.00 72.64           C  
ANISOU 1600  CB  GLU A 212     7334  14276   5990   3912   2352    897       C  
ATOM   1601  CG  GLU A 212      53.325   0.831  14.356  1.00 75.54           C  
ANISOU 1601  CG  GLU A 212     8175  14729   5796   4203   2454    779       C  
ATOM   1602  CD  GLU A 212      52.630   2.009  13.680  1.00 75.72           C  
ANISOU 1602  CD  GLU A 212     8457  14753   5561   3930   2541   1105       C  
ATOM   1603  OE1 GLU A 212      53.118   2.473  12.626  1.00 74.22           O  
ANISOU 1603  OE1 GLU A 212     8262  14914   5023   3972   2956   1297       O  
ATOM   1604  OE2 GLU A 212      51.595   2.474  14.216  1.00 75.02           O  
ANISOU 1604  OE2 GLU A 212     8554  14319   5630   3678   2201   1194       O  
ATOM   1605  N   ASN A 213      54.335   0.510  19.051  1.00 66.82           N  
ANISOU 1605  N   ASN A 213     5940  13188   6262   3543   1587    790       N  
ATOM   1606  CA  ASN A 213      55.048   0.884  20.283  1.00 69.04           C  
ANISOU 1606  CA  ASN A 213     5772  13533   6927   3229   1473    903       C  
ATOM   1607  C   ASN A 213      55.143  -0.217  21.355  1.00 67.88           C  
ANISOU 1607  C   ASN A 213     5473  13304   7013   3332   1073    788       C  
ATOM   1608  O   ASN A 213      55.954  -0.105  22.276  1.00 70.19           O  
ANISOU 1608  O   ASN A 213     5341  13736   7593   3137    977    887       O  
ATOM   1609  CB  ASN A 213      54.405   2.129  20.900  1.00 68.88           C  
ANISOU 1609  CB  ASN A 213     5847  13345   6978   2749   1372   1022       C  
ATOM   1610  CG  ASN A 213      54.814   3.406  20.196  1.00 72.61           C  
ANISOU 1610  CG  ASN A 213     6226  13924   7438   2526   1754   1250       C  
ATOM   1611  OD1 ASN A 213      55.624   4.174  20.717  1.00 73.57           O  
ANISOU 1611  OD1 ASN A 213     5972  14146   7836   2205   1837   1387       O  
ATOM   1612  ND2 ASN A 213      54.260   3.639  19.005  1.00 73.90           N  
ANISOU 1612  ND2 ASN A 213     6726  14065   7286   2670   1959   1320       N  
ATOM   1613  N   LEU A 214      54.300  -1.247  21.257  1.00 63.84           N  
ANISOU 1613  N   LEU A 214     5301  12563   6393   3599    804    616       N  
ATOM   1614  CA  LEU A 214      54.403  -2.431  22.110  1.00 59.69           C  
ANISOU 1614  CA  LEU A 214     4642  11932   6105   3748    427    557       C  
ATOM   1615  C   LEU A 214      54.295  -3.704  21.263  1.00 62.04           C  
ANISOU 1615  C   LEU A 214     5151  12081   6340   4265    403    332       C  
ATOM   1616  O   LEU A 214      53.198  -4.146  20.918  1.00 58.51           O  
ANISOU 1616  O   LEU A 214     5147  11369   5716   4361    199    201       O  
ATOM   1617  CB  LEU A 214      53.310  -2.421  23.175  1.00 54.76           C  
ANISOU 1617  CB  LEU A 214     4215  11097   5494   3455      9    599       C  
ATOM   1618  CG  LEU A 214      53.208  -1.216  24.117  1.00 52.72           C  
ANISOU 1618  CG  LEU A 214     3833  10931   5267   2951    -14    722       C  
ATOM   1619  CD1 LEU A 214      51.980  -1.378  25.014  1.00 44.14           C  
ANISOU 1619  CD1 LEU A 214     2993   9656   4122   2758   -373    716       C  
ATOM   1620  CD2 LEU A 214      54.473  -1.034  24.954  1.00 54.87           C  
ANISOU 1620  CD2 LEU A 214     3585  11471   5792   2766    -32    841       C  
ATOM   1621  N   ALA A 215      55.438  -4.288  20.925  1.00 68.63           N  
ANISOU 1621  N   ALA A 215     5654  13076   7347   4601    607    270       N  
ATOM   1622  CA  ALA A 215      55.467  -5.511  20.118  1.00 74.60           C  
ANISOU 1622  CA  ALA A 215     6587  13672   8084   5136    617    -18       C  
ATOM   1623  C   ALA A 215      54.856  -6.718  20.848  1.00 75.88           C  
ANISOU 1623  C   ALA A 215     6880  13442   8508   5246     68    -78       C  
ATOM   1624  O   ALA A 215      54.251  -7.588  20.212  1.00 77.63           O  
ANISOU 1624  O   ALA A 215     7477  13374   8644   5553    -69   -340       O  
ATOM   1625  CB  ALA A 215      56.899  -5.822  19.674  1.00 79.62           C  
ANISOU 1625  CB  ALA A 215     6762  14582   8910   5492   1002    -72       C  
ATOM   1626  N   ASN A 216      55.001  -6.749  22.175  1.00 77.95           N  
ANISOU 1626  N   ASN A 216    10263  11388   7966   6311   2174   1637       N  
ATOM   1627  CA  ASN A 216      54.548  -7.871  23.004  1.00 78.58           C  
ANISOU 1627  CA  ASN A 216    10814  11125   7917   6567   2305   1710       C  
ATOM   1628  C   ASN A 216      53.121  -7.657  23.501  1.00 72.13           C  
ANISOU 1628  C   ASN A 216    10216   9886   7304   5978   2087   1433       C  
ATOM   1629  O   ASN A 216      52.776  -6.556  23.925  1.00 69.87           O  
ANISOU 1629  O   ASN A 216     9473   9840   7235   5501   1799   1291       O  
ATOM   1630  CB  ASN A 216      55.489  -8.023  24.199  1.00 83.87           C  
ANISOU 1630  CB  ASN A 216    11033  12409   8423   6989   2321   1997       C  
ATOM   1631  CG  ASN A 216      55.660  -9.464  24.633  1.00 89.01           C  
ANISOU 1631  CG  ASN A 216    12222  12799   8797   7629   2637   2225       C  
ATOM   1632  OD1 ASN A 216      54.926  -9.961  25.491  1.00 90.23           O  
ANISOU 1632  OD1 ASN A 216    12691  12640   8953   7542   2613   2168       O  
ATOM   1633  ND2 ASN A 216      56.651 -10.136  24.060  1.00 91.53           N  
ANISOU 1633  ND2 ASN A 216    12665  13253   8859   8298   2958   2497       N  
ATOM   1634  N   LYS A 217      52.299  -8.707  23.463  1.00 70.65           N  
ANISOU 1634  N   LYS A 217    10744   9081   7017   6005   2244   1364       N  
ATOM   1635  CA  LYS A 217      50.872  -8.592  23.832  1.00 65.77           C  
ANISOU 1635  CA  LYS A 217    10363   8071   6554   5430   2056   1102       C  
ATOM   1636  C   LYS A 217      50.625  -8.519  25.338  1.00 60.45           C  
ANISOU 1636  C   LYS A 217     9457   7580   5931   5359   1902   1128       C  
ATOM   1637  O   LYS A 217      49.612  -7.977  25.775  1.00 55.84           O  
ANISOU 1637  O   LYS A 217     8789   6891   5537   4844   1669    926       O  
ATOM   1638  CB  LYS A 217      50.048  -9.746  23.242  1.00 68.97           C  
ANISOU 1638  CB  LYS A 217    11637   7783   6786   5389   2285   1001       C  
ATOM   1639  CG  LYS A 217      48.566  -9.679  23.619  1.00 66.73           C  
ANISOU 1639  CG  LYS A 217    11569   7171   6613   4782   2095    746       C  
ATOM   1640  CD  LYS A 217      47.669 -10.477  22.687  1.00 69.16           C  
ANISOU 1640  CD  LYS A 217    12629   6893   6756   4520   2260    587       C  
ATOM   1641  CE  LYS A 217      46.247 -10.563  23.244  1.00 68.29           C  
ANISOU 1641  CE  LYS A 217    12717   6542   6686   3959   2095    375       C  
ATOM   1642  NZ  LYS A 217      46.211 -11.227  24.587  1.00 70.16           N  
ANISOU 1642  NZ  LYS A 217    13113   6721   6826   4150   2152    454       N  
ATOM   1643  N   ALA A 218      51.532  -9.084  26.128  1.00 62.09           N  
ANISOU 1643  N   ALA A 218     9568   8073   5952   5895   2042   1391       N  
ATOM   1644  CA  ALA A 218      51.458  -8.955  27.579  1.00 60.53           C  
ANISOU 1644  CA  ALA A 218     9078   8136   5786   5851   1891   1443       C  
ATOM   1645  C   ALA A 218      51.426  -7.479  27.976  1.00 55.28           C  
ANISOU 1645  C   ALA A 218     7695   7933   5375   5361   1556   1328       C  
ATOM   1646  O   ALA A 218      50.823  -7.128  28.985  1.00 55.22           O  
ANISOU 1646  O   ALA A 218     7540   7954   5485   5041   1369   1233       O  
ATOM   1647  CB  ALA A 218      52.629  -9.668  28.251  1.00 62.18           C  
ANISOU 1647  CB  ALA A 218     9179   8722   5725   6553   2093   1794       C  
ATOM   1648  N   ASP A 219      52.068  -6.629  27.177  1.00 52.63           N  
ANISOU 1648  N   ASP A 219     6964   7930   5103   5298   1507   1333       N  
ATOM   1649  CA  ASP A 219      52.038  -5.185  27.386  1.00 53.33           C  
ANISOU 1649  CA  ASP A 219     6477   8388   5397   4802   1241   1205       C  
ATOM   1650  C   ASP A 219      50.728  -4.578  26.893  1.00 51.98           C  
ANISOU 1650  C   ASP A 219     6505   7775   5469   4240   1090    909       C  
ATOM   1651  O   ASP A 219      50.202  -3.650  27.500  1.00 49.41           O  
ANISOU 1651  O   ASP A 219     5912   7546   5315   3810    887    778       O  
ATOM   1652  CB  ASP A 219      53.194  -4.499  26.651  1.00 56.36           C  
ANISOU 1652  CB  ASP A 219     6414   9275   5725   4910   1268   1310       C  
ATOM   1653  CG  ASP A 219      54.552  -4.971  27.113  1.00 62.34           C  
ANISOU 1653  CG  ASP A 219     6852  10622   6212   5462   1405   1636       C  
ATOM   1654  OD1 ASP A 219      54.638  -5.642  28.162  1.00 67.55           O  
ANISOU 1654  OD1 ASP A 219     7547  11373   6746   5726   1443   1785       O  
ATOM   1655  OD2 ASP A 219      55.542  -4.667  26.416  1.00 67.14           O  
ANISOU 1655  OD2 ASP A 219     7157  11638   6716   5644   1479   1756       O  
ATOM   1656  N   ARG A 220      50.219  -5.083  25.777  1.00 54.15           N  
ANISOU 1656  N   ARG A 220     7247   7594   5733   4249   1204    820       N  
ATOM   1657  CA  ARG A 220      48.986  -4.552  25.204  1.00 53.37           C  
ANISOU 1657  CA  ARG A 220     7310   7148   5820   3749   1069    574       C  
ATOM   1658  C   ARG A 220      47.777  -4.821  26.097  1.00 53.20           C  
ANISOU 1658  C   ARG A 220     7503   6848   5863   3466    964    451       C  
ATOM   1659  O   ARG A 220      46.863  -3.996  26.183  1.00 53.39           O  
ANISOU 1659  O   ARG A 220     7394   6823   6069   3031    784    289       O  
ATOM   1660  CB  ARG A 220      48.771  -5.099  23.790  1.00 54.28           C  
ANISOU 1660  CB  ARG A 220     7873   6894   5856   3807   1223    523       C  
ATOM   1661  CG  ARG A 220      49.757  -4.516  22.776  1.00 53.78           C  
ANISOU 1661  CG  ARG A 220     7543   7100   5791   3949   1276    589       C  
ATOM   1662  CD  ARG A 220      49.379  -4.819  21.331  1.00 54.10           C  
ANISOU 1662  CD  ARG A 220     7992   6771   5793   3883   1384    497       C  
ATOM   1663  NE  ARG A 220      50.373  -5.662  20.667  1.00 58.96           N  
ANISOU 1663  NE  ARG A 220     8845   7361   6195   4382   1659    665       N  
ATOM   1664  CZ  ARG A 220      50.257  -6.968  20.428  1.00 60.60           C  
ANISOU 1664  CZ  ARG A 220     9677   7163   6184   4652   1913    718       C  
ATOM   1665  NH1 ARG A 220      49.173  -7.653  20.786  1.00 59.42           N  
ANISOU 1665  NH1 ARG A 220     9999   6595   5981   4427   1921    603       N  
ATOM   1666  NH2 ARG A 220      51.248  -7.597  19.814  1.00 64.99           N  
ANISOU 1666  NH2 ARG A 220    10415   7733   6546   5147   2186    893       N  
ATOM   1667  N   ASP A 221      47.786  -5.955  26.787  1.00 55.55           N  
ANISOU 1667  N   ASP A 221     8133   6978   5994   3735   1094    541       N  
ATOM   1668  CA  ASP A 221      46.704  -6.290  27.714  1.00 54.81           C  
ANISOU 1668  CA  ASP A 221     8253   6640   5932   3477   1009    432       C  
ATOM   1669  C   ASP A 221      46.599  -5.306  28.889  1.00 52.64           C  
ANISOU 1669  C   ASP A 221     7470   6697   5834   3232    787    405       C  
ATOM   1670  O   ASP A 221      45.569  -5.266  29.558  1.00 55.06           O  
ANISOU 1670  O   ASP A 221     7866   6832   6224   2923    676    281       O  
ATOM   1671  CB  ASP A 221      46.855  -7.732  28.231  1.00 58.32           C  
ANISOU 1671  CB  ASP A 221     9203   6829   6126   3851   1229    550       C  
ATOM   1672  CG  ASP A 221      46.747  -8.780  27.120  1.00 59.58           C  
ANISOU 1672  CG  ASP A 221    10021   6543   6073   4013   1491    543       C  
ATOM   1673  OD1 ASP A 221      47.272  -9.903  27.308  1.00 60.54           O  
ANISOU 1673  OD1 ASP A 221    10564   6494   5943   4470   1755    700       O  
ATOM   1674  OD2 ASP A 221      46.142  -8.485  26.065  1.00 56.89           O  
ANISOU 1674  OD2 ASP A 221     9802   6022   5791   3690   1451    390       O  
ATOM   1675  N   GLN A 222      47.646  -4.511  29.130  1.00 52.24           N  
ANISOU 1675  N   GLN A 222     6904   7131   5815   3337    735    518       N  
ATOM   1676  CA  GLN A 222      47.613  -3.436  30.149  1.00 51.14           C  
ANISOU 1676  CA  GLN A 222     6302   7315   5815   3034    548    479       C  
ATOM   1677  C   GLN A 222      46.915  -2.153  29.643  1.00 48.26           C  
ANISOU 1677  C   GLN A 222     5766   6907   5663   2575    409    296       C  
ATOM   1678  O   GLN A 222      46.938  -1.108  30.306  1.00 44.84           O  
ANISOU 1678  O   GLN A 222     4994   6713   5330   2304    294    255       O  
ATOM   1679  CB  GLN A 222      49.037  -3.123  30.651  1.00 53.11           C  
ANISOU 1679  CB  GLN A 222     6084   8153   5943   3271    564    678       C  
ATOM   1680  CG  GLN A 222      49.533  -4.099  31.727  1.00 58.64           C  
ANISOU 1680  CG  GLN A 222     6821   9004   6454   3644    640    871       C  
ATOM   1681  CD  GLN A 222      51.031  -4.387  31.651  1.00 64.99           C  
ANISOU 1681  CD  GLN A 222     7334  10333   7027   4125    765   1145       C  
ATOM   1682  OE1 GLN A 222      51.829  -3.502  31.354  1.00 70.19           O  
ANISOU 1682  OE1 GLN A 222     7541  11456   7674   4025    716   1187       O  
ATOM   1683  NE2 GLN A 222      51.414  -5.633  31.923  1.00 66.46           N  
ANISOU 1683  NE2 GLN A 222     7791  10461   6999   4656    946   1346       N  
ATOM   1684  N   TYR A 223      46.304  -2.246  28.463  1.00 46.68           N  
ANISOU 1684  N   TYR A 223     5832   6402   5503   2497    441    198       N  
ATOM   1685  CA  TYR A 223      45.576  -1.148  27.856  1.00 43.15           C  
ANISOU 1685  CA  TYR A 223     5277   5891   5225   2138    338     55       C  
ATOM   1686  C   TYR A 223      44.267  -1.672  27.310  1.00 43.46           C  
ANISOU 1686  C   TYR A 223     5698   5538   5277   1971    327    -62       C  
ATOM   1687  O   TYR A 223      44.100  -2.878  27.099  1.00 49.22           O  
ANISOU 1687  O   TYR A 223     6819   6022   5858   2121    431    -46       O  
ATOM   1688  CB  TYR A 223      46.384  -0.537  26.709  1.00 43.78           C  
ANISOU 1688  CB  TYR A 223     5197   6136   5300   2206    390     83       C  
ATOM   1689  CG  TYR A 223      47.731  -0.011  27.140  1.00 44.19           C  
ANISOU 1689  CG  TYR A 223     4848   6656   5287   2322    408    202       C  
ATOM   1690  CD1 TYR A 223      48.814  -0.866  27.282  1.00 43.68           C  
ANISOU 1690  CD1 TYR A 223     4748   6811   5037   2729    522    381       C  
ATOM   1691  CD2 TYR A 223      47.914   1.339  27.425  1.00 44.55           C  
ANISOU 1691  CD2 TYR A 223     4563   6951   5415   2017    330    147       C  
ATOM   1692  CE1 TYR A 223      50.053  -0.397  27.699  1.00 46.14           C  
ANISOU 1692  CE1 TYR A 223     4629   7660   5242   2815    529    512       C  
ATOM   1693  CE2 TYR A 223      49.154   1.822  27.835  1.00 45.35           C  
ANISOU 1693  CE2 TYR A 223     4291   7540   5400   2039    348    249       C  
ATOM   1694  CZ  TYR A 223      50.218   0.948  27.973  1.00 45.72           C  
ANISOU 1694  CZ  TYR A 223     4234   7879   5257   2429    432    435       C  
ATOM   1695  OH  TYR A 223      51.446   1.419  28.381  1.00 47.78           O  
ANISOU 1695  OH  TYR A 223     4067   8726   5361   2431    441    557       O  
ATOM   1696  N   GLU A 224      43.344  -0.751  27.076  1.00 38.89           N  
ANISOU 1696  N   GLU A 224     5015   4921   4840   1654    220   -171       N  
ATOM   1697  CA  GLU A 224      42.058  -1.063  26.490  1.00 34.81           C  
ANISOU 1697  CA  GLU A 224     4760   4155   4313   1444    187   -267       C  
ATOM   1698  C   GLU A 224      41.721   0.053  25.508  1.00 31.51           C  
ANISOU 1698  C   GLU A 224     4174   3800   3998   1285    139   -309       C  
ATOM   1699  O   GLU A 224      42.477   1.023  25.380  1.00 26.67           O  
ANISOU 1699  O   GLU A 224     3296   3373   3464   1325    145   -279       O  
ATOM   1700  CB  GLU A 224      40.999  -1.147  27.589  1.00 36.40           C  
ANISOU 1700  CB  GLU A 224     4981   4293   4557   1230     96   -327       C  
ATOM   1701  CG  GLU A 224      41.059  -2.406  28.439  1.00 38.68           C  
ANISOU 1701  CG  GLU A 224     5544   4442   4710   1348    154   -305       C  
ATOM   1702  CD  GLU A 224      40.043  -2.393  29.572  1.00 39.78           C  
ANISOU 1702  CD  GLU A 224     5671   4544   4901   1115     58   -370       C  
ATOM   1703  OE1 GLU A 224      40.102  -1.464  30.417  1.00 38.11           O  
ANISOU 1703  OE1 GLU A 224     5139   4506   4835   1041    -20   -364       O  
ATOM   1704  OE2 GLU A 224      39.189  -3.315  29.620  1.00 40.47           O  
ANISOU 1704  OE2 GLU A 224     6091   4427   4860    979     75   -432       O  
ATOM   1705  N   LEU A 225      40.596  -0.096  24.813  1.00 32.09           N  
ANISOU 1705  N   LEU A 225     4412   3744   4038   1093    100   -371       N  
ATOM   1706  CA  LEU A 225      40.061   0.953  23.952  1.00 33.06           C  
ANISOU 1706  CA  LEU A 225     4380   3943   4240    955     51   -389       C  
ATOM   1707  C   LEU A 225      38.671   1.363  24.419  1.00 34.93           C  
ANISOU 1707  C   LEU A 225     4536   4214   4523    724    -47   -420       C  
ATOM   1708  O   LEU A 225      37.903   0.524  24.890  1.00 36.37           O  
ANISOU 1708  O   LEU A 225     4883   4322   4615    598    -79   -456       O  
ATOM   1709  CB  LEU A 225      39.978   0.472  22.505  1.00 32.90           C  
ANISOU 1709  CB  LEU A 225     4579   3826   4096    948     97   -399       C  
ATOM   1710  CG  LEU A 225      41.312   0.176  21.814  1.00 34.17           C  
ANISOU 1710  CG  LEU A 225     4815   3965   4205   1199    216   -355       C  
ATOM   1711  CD1 LEU A 225      41.069  -0.567  20.508  1.00 36.64           C  
ANISOU 1711  CD1 LEU A 225     5449   4116   4356   1155    282   -378       C  
ATOM   1712  CD2 LEU A 225      42.119   1.439  21.569  1.00 29.66           C  
ANISOU 1712  CD2 LEU A 225     3926   3580   3762   1270    217   -323       C  
ATOM   1713  N   LEU A 226      38.368   2.654  24.274  1.00 35.18           N  
ANISOU 1713  N   LEU A 226     4335   4361   4670    680    -70   -399       N  
ATOM   1714  CA  LEU A 226      37.038   3.208  24.553  1.00 34.49           C  
ANISOU 1714  CA  LEU A 226     4139   4352   4612    529   -133   -389       C  
ATOM   1715  C   LEU A 226      36.081   3.095  23.351  1.00 34.10           C  
ANISOU 1715  C   LEU A 226     4134   4377   4445    422   -172   -367       C  
ATOM   1716  O   LEU A 226      36.272   3.748  22.331  1.00 31.94           O  
ANISOU 1716  O   LEU A 226     3806   4150   4180    486   -144   -328       O  
ATOM   1717  CB  LEU A 226      37.156   4.683  24.954  1.00 32.70           C  
ANISOU 1717  CB  LEU A 226     3702   4195   4527    574    -88   -352       C  
ATOM   1718  CG  LEU A 226      37.857   5.030  26.273  1.00 29.17           C  
ANISOU 1718  CG  LEU A 226     3176   3738   4169    584    -53   -371       C  
ATOM   1719  CD1 LEU A 226      37.815   6.527  26.505  1.00 23.62           C  
ANISOU 1719  CD1 LEU A 226     2361   3064   3551    569     32   -343       C  
ATOM   1720  CD2 LEU A 226      37.224   4.290  27.435  1.00 27.98           C  
ANISOU 1720  CD2 LEU A 226     3063   3558   4009    497   -116   -398       C  
ATOM   1721  N   CYS A 227      35.042   2.280  23.496  1.00 35.82           N  
ANISOU 1721  N   CYS A 227     4447   4636   4527    231   -237   -389       N  
ATOM   1722  CA  CYS A 227      34.032   2.098  22.446  1.00 39.18           C  
ANISOU 1722  CA  CYS A 227     4884   5220   4781     57   -289   -361       C  
ATOM   1723  C   CYS A 227      32.935   3.155  22.577  1.00 37.54           C  
ANISOU 1723  C   CYS A 227     4379   5273   4610     49   -333   -262       C  
ATOM   1724  O   CYS A 227      32.688   3.680  23.668  1.00 36.52           O  
ANISOU 1724  O   CYS A 227     4115   5160   4600    106   -326   -243       O  
ATOM   1725  CB  CYS A 227      33.436   0.677  22.511  1.00 41.88           C  
ANISOU 1725  CB  CYS A 227     5496   5523   4891   -211   -318   -436       C  
ATOM   1726  SG  CYS A 227      34.670  -0.698  22.771  1.00 45.17           S  
ANISOU 1726  SG  CYS A 227     6350   5572   5239   -122   -204   -529       S  
ATOM   1727  N   LEU A 228      32.282   3.459  21.456  1.00 37.81           N  
ANISOU 1727  N   LEU A 228     4322   5523   4522     -1   -363   -184       N  
ATOM   1728  CA  LEU A 228      31.280   4.531  21.391  1.00 34.50           C  
ANISOU 1728  CA  LEU A 228     3613   5392   4104     81   -374    -39       C  
ATOM   1729  C   LEU A 228      30.019   4.232  22.191  1.00 36.12           C  
ANISOU 1729  C   LEU A 228     3677   5844   4202    -83   -444     -3       C  
ATOM   1730  O   LEU A 228      29.266   5.149  22.519  1.00 40.25           O  
ANISOU 1730  O   LEU A 228     3958   6579   4757     58   -419    128       O  
ATOM   1731  CB  LEU A 228      30.901   4.826  19.942  1.00 35.90           C  
ANISOU 1731  CB  LEU A 228     3715   5793   4134     76   -394     58       C  
ATOM   1732  CG  LEU A 228      31.966   5.588  19.144  1.00 35.13           C  
ANISOU 1732  CG  LEU A 228     3676   5509   4161    299   -304     68       C  
ATOM   1733  CD1 LEU A 228      31.627   5.662  17.650  1.00 33.08           C  
ANISOU 1733  CD1 LEU A 228     3386   5454   3730    254   -336    148       C  
ATOM   1734  CD2 LEU A 228      32.141   6.974  19.722  1.00 31.61           C  
ANISOU 1734  CD2 LEU A 228     3107   5004   3899    571   -193    147       C  
ATOM   1735  N   ASP A 229      29.802   2.962  22.520  1.00 35.25           N  
ANISOU 1735  N   ASP A 229     3746   5700   3949   -367   -507   -115       N  
ATOM   1736  CA  ASP A 229      28.684   2.559  23.372  1.00 38.28           C  
ANISOU 1736  CA  ASP A 229     4026   6304   4215   -574   -571   -109       C  
ATOM   1737  C   ASP A 229      29.066   2.611  24.848  1.00 39.54           C  
ANISOU 1737  C   ASP A 229     4227   6220   4575   -476   -534   -176       C  
ATOM   1738  O   ASP A 229      28.527   1.872  25.673  1.00 40.00           O  
ANISOU 1738  O   ASP A 229     4346   6306   4546   -686   -577   -240       O  
ATOM   1739  CB  ASP A 229      28.203   1.151  23.003  1.00 41.86           C  
ANISOU 1739  CB  ASP A 229     4709   6835   4362   -994   -636   -208       C  
ATOM   1740  CG  ASP A 229      29.312   0.113  23.077  1.00 42.05           C  
ANISOU 1740  CG  ASP A 229     5171   6412   4396  -1037   -571   -368       C  
ATOM   1741  OD1 ASP A 229      30.478   0.473  22.818  1.00 41.78           O  
ANISOU 1741  OD1 ASP A 229     5212   6116   4549   -760   -501   -376       O  
ATOM   1742  OD2 ASP A 229      29.020  -1.060  23.390  1.00 43.43           O  
ANISOU 1742  OD2 ASP A 229     5627   6508   4365  -1339   -573   -475       O  
ATOM   1743  N   ASN A 230      30.000   3.486  25.185  1.00 40.22           N  
ANISOU 1743  N   ASN A 230     4293   6084   4906   -191   -448   -164       N  
ATOM   1744  CA  ASN A 230      30.379   3.675  26.570  1.00 41.67           C  
ANISOU 1744  CA  ASN A 230     4491   6079   5263   -115   -408   -213       C  
ATOM   1745  C   ASN A 230      30.734   2.343  27.243  1.00 43.41           C  
ANISOU 1745  C   ASN A 230     4962   6107   5424   -291   -447   -349       C  
ATOM   1746  O   ASN A 230      30.239   2.007  28.319  1.00 47.16           O  
ANISOU 1746  O   ASN A 230     5437   6586   5895   -401   -473   -386       O  
ATOM   1747  CB  ASN A 230      29.268   4.423  27.301  1.00 38.30           C  
ANISOU 1747  CB  ASN A 230     3827   5871   4856    -78   -394   -112       C  
ATOM   1748  CG  ASN A 230      28.838   5.676  26.558  1.00 37.48           C  
ANISOU 1748  CG  ASN A 230     3521   5962   4759    148   -320     56       C  
ATOM   1749  OD1 ASN A 230      29.636   6.578  26.334  1.00 35.94           O  
ANISOU 1749  OD1 ASN A 230     3369   5589   4699    357   -212     79       O  
ATOM   1750  ND2 ASN A 230      27.577   5.732  26.168  1.00 39.97           N  
ANISOU 1750  ND2 ASN A 230     3622   6669   4897    105   -365    184       N  
ATOM   1751  N   THR A 231      31.607   1.597  26.574  1.00 41.34           N  
ANISOU 1751  N   THR A 231     4940   5666   5102   -292   -428   -414       N  
ATOM   1752  CA  THR A 231      32.135   0.337  27.078  1.00 40.32           C  
ANISOU 1752  CA  THR A 231     5121   5304   4893   -370   -412   -518       C  
ATOM   1753  C   THR A 231      33.559   0.205  26.568  1.00 37.41           C  
ANISOU 1753  C   THR A 231     4899   4731   4585   -150   -334   -527       C  
ATOM   1754  O   THR A 231      33.949   0.909  25.640  1.00 36.54           O  
ANISOU 1754  O   THR A 231     4681   4673   4529    -30   -312   -478       O  
ATOM   1755  CB  THR A 231      31.314  -0.850  26.569  1.00 44.09           C  
ANISOU 1755  CB  THR A 231     5844   5829   5078   -691   -441   -578       C  
ATOM   1756  OG1 THR A 231      31.102  -0.706  25.157  1.00 44.51           O  
ANISOU 1756  OG1 THR A 231     5879   6026   5008   -758   -451   -537       O  
ATOM   1757  CG2 THR A 231      29.959  -0.928  27.300  1.00 42.41           C  
ANISOU 1757  CG2 THR A 231     5494   5852   4767   -947   -519   -579       C  
ATOM   1758  N   ARG A 232      34.336  -0.688  27.170  1.00 36.35           N  
ANISOU 1758  N   ARG A 232     5002   4386   4422    -75   -281   -575       N  
ATOM   1759  CA  ARG A 232      35.740  -0.853  26.781  1.00 34.69           C  
ANISOU 1759  CA  ARG A 232     4894   4041   4244    182   -192   -555       C  
ATOM   1760  C   ARG A 232      35.983  -2.172  26.090  1.00 37.02           C  
ANISOU 1760  C   ARG A 232     5611   4142   4314    164   -103   -591       C  
ATOM   1761  O   ARG A 232      35.325  -3.171  26.391  1.00 39.62           O  
ANISOU 1761  O   ARG A 232     6230   4364   4461    -34    -88   -652       O  
ATOM   1762  CB  ARG A 232      36.659  -0.784  27.995  1.00 31.06           C  
ANISOU 1762  CB  ARG A 232     4360   3540   3902    370   -166   -534       C  
ATOM   1763  CG  ARG A 232      36.525   0.487  28.826  1.00 27.00           C  
ANISOU 1763  CG  ARG A 232     3505   3170   3582    357   -215   -510       C  
ATOM   1764  CD  ARG A 232      37.603   0.519  29.887  1.00 25.27           C  
ANISOU 1764  CD  ARG A 232     3213   2957   3430    507   -185   -485       C  
ATOM   1765  NE  ARG A 232      37.886   1.861  30.376  1.00 23.95           N  
ANISOU 1765  NE  ARG A 232     2766   2920   3414    493   -184   -462       N  
ATOM   1766  CZ  ARG A 232      39.030   2.219  30.944  1.00 26.98           C  
ANISOU 1766  CZ  ARG A 232     3019   3403   3831    584   -149   -429       C  
ATOM   1767  NH1 ARG A 232      40.010   1.337  31.096  1.00 28.19           N  
ANISOU 1767  NH1 ARG A 232     3244   3578   3889    762   -120   -386       N  
ATOM   1768  NH2 ARG A 232      39.200   3.467  31.358  1.00 29.45           N  
ANISOU 1768  NH2 ARG A 232     3142   3812   4236    493   -123   -426       N  
ATOM   1769  N   LYS A 233      36.950  -2.173  25.177  1.00 38.80           N  
ANISOU 1769  N   LYS A 233     5903   4308   4531    363    -21   -556       N  
ATOM   1770  CA  LYS A 233      37.423  -3.410  24.567  1.00 41.97           C  
ANISOU 1770  CA  LYS A 233     6755   4476   4716    429    120   -573       C  
ATOM   1771  C   LYS A 233      38.947  -3.451  24.508  1.00 42.72           C  
ANISOU 1771  C   LYS A 233     6844   4524   4866    828    235   -491       C  
ATOM   1772  O   LYS A 233      39.597  -2.401  24.587  1.00 39.65           O  
ANISOU 1772  O   LYS A 233     6078   4323   4665    972    188   -439       O  
ATOM   1773  CB  LYS A 233      36.851  -3.573  23.160  1.00 45.28           C  
ANISOU 1773  CB  LYS A 233     7339   4891   4974    209    131   -608       C  
ATOM   1774  CG  LYS A 233      35.456  -4.158  23.126  1.00 47.56           C  
ANISOU 1774  CG  LYS A 233     7814   5209   5047   -217     78   -686       C  
ATOM   1775  CD  LYS A 233      35.038  -4.465  21.699  1.00 51.60           C  
ANISOU 1775  CD  LYS A 233     8534   5734   5337   -458    110   -715       C  
ATOM   1776  CE  LYS A 233      33.536  -4.632  21.592  1.00 54.88           C  
ANISOU 1776  CE  LYS A 233     8930   6374   5547   -936      3   -764       C  
ATOM   1777  NZ  LYS A 233      33.052  -5.716  22.485  1.00 56.92           N  
ANISOU 1777  NZ  LYS A 233     9544   6476   5606  -1163     57   -850       N  
ATOM   1778  N   PRO A 234      39.518  -4.669  24.369  1.00 45.07           N  
ANISOU 1778  N   PRO A 234     7576   4583   4964   1005    409   -472       N  
ATOM   1779  CA  PRO A 234      40.958  -4.846  24.219  1.00 43.75           C  
ANISOU 1779  CA  PRO A 234     7415   4415   4793   1431    548   -361       C  
ATOM   1780  C   PRO A 234      41.495  -4.213  22.948  1.00 43.56           C  
ANISOU 1780  C   PRO A 234     7249   4482   4820   1503    566   -338       C  
ATOM   1781  O   PRO A 234      40.785  -4.148  21.949  1.00 43.79           O  
ANISOU 1781  O   PRO A 234     7400   4449   4789   1253    541   -407       O  
ATOM   1782  CB  PRO A 234      41.137  -6.367  24.175  1.00 46.97           C  
ANISOU 1782  CB  PRO A 234     8435   4491   4920   1575    769   -346       C  
ATOM   1783  CG  PRO A 234      39.798  -6.955  24.094  1.00 46.70           C  
ANISOU 1783  CG  PRO A 234     8749   4273   4724   1143    747   -478       C  
ATOM   1784  CD  PRO A 234      38.817  -5.954  24.543  1.00 45.93           C  
ANISOU 1784  CD  PRO A 234     8210   4426   4816    821    505   -541       C  
ATOM   1785  N   VAL A 235      42.754  -3.780  22.991  1.00 45.28           N  
ANISOU 1785  N   VAL A 235     7207   4878   5119   1827    611   -234       N  
ATOM   1786  CA  VAL A 235      43.376  -3.025  21.889  1.00 46.84           C  
ANISOU 1786  CA  VAL A 235     7208   5206   5383   1895    622   -212       C  
ATOM   1787  C   VAL A 235      43.397  -3.700  20.508  1.00 48.19           C  
ANISOU 1787  C   VAL A 235     7773   5151   5384   1914    763   -230       C  
ATOM   1788  O   VAL A 235      43.625  -3.023  19.501  1.00 46.23           O  
ANISOU 1788  O   VAL A 235     7383   4988   5194   1881    744   -238       O  
ATOM   1789  CB  VAL A 235      44.828  -2.621  22.223  1.00 47.07           C  
ANISOU 1789  CB  VAL A 235     6914   5511   5460   2232    674    -87       C  
ATOM   1790  CG1 VAL A 235      44.847  -1.696  23.422  1.00 46.40           C  
ANISOU 1790  CG1 VAL A 235     6407   5688   5534   2124    530    -84       C  
ATOM   1791  CG2 VAL A 235      45.679  -3.852  22.461  1.00 49.05           C  
ANISOU 1791  CG2 VAL A 235     7446   5675   5514   2638    874     37       C  
ATOM   1792  N   ASP A 236      43.181  -5.010  20.453  1.00 48.74           N  
ANISOU 1792  N   ASP A 236     8372   4920   5225   1953    922   -238       N  
ATOM   1793  CA  ASP A 236      43.142  -5.703  19.169  1.00 55.17           C  
ANISOU 1793  CA  ASP A 236     9642   5482   5838   1917   1085   -268       C  
ATOM   1794  C   ASP A 236      41.717  -5.984  18.680  1.00 56.75           C  
ANISOU 1794  C   ASP A 236    10119   5534   5907   1414   1016   -406       C  
ATOM   1795  O   ASP A 236      41.528  -6.775  17.756  1.00 59.27           O  
ANISOU 1795  O   ASP A 236    10927   5605   5987   1293   1171   -450       O  
ATOM   1796  CB  ASP A 236      43.991  -6.982  19.200  1.00 61.99           C  
ANISOU 1796  CB  ASP A 236    11001   6085   6465   2316   1382   -170       C  
ATOM   1797  CG  ASP A 236      43.572  -7.953  20.285  1.00 67.69           C  
ANISOU 1797  CG  ASP A 236    12076   6600   7042   2323   1460   -175       C  
ATOM   1798  OD1 ASP A 236      42.704  -7.607  21.122  1.00 67.07           O  
ANISOU 1798  OD1 ASP A 236    11795   6620   7071   2027   1265   -252       O  
ATOM   1799  OD2 ASP A 236      44.136  -9.070  20.300  1.00 72.94           O  
ANISOU 1799  OD2 ASP A 236    13247   6996   7471   2651   1741    -91       O  
ATOM   1800  N   GLU A 237      40.725  -5.329  19.287  1.00 54.99           N  
ANISOU 1800  N   GLU A 237     9584   5496   5814   1110    797   -466       N  
ATOM   1801  CA  GLU A 237      39.354  -5.304  18.748  1.00 53.92           C  
ANISOU 1801  CA  GLU A 237     9531   5391   5565    623    686   -566       C  
ATOM   1802  C   GLU A 237      39.000  -3.901  18.216  1.00 48.77           C  
ANISOU 1802  C   GLU A 237     8362   5050   5119    512    493   -552       C  
ATOM   1803  O   GLU A 237      37.845  -3.479  18.270  1.00 45.94           O  
ANISOU 1803  O   GLU A 237     7823   4874   4758    199    341   -585       O  
ATOM   1804  CB  GLU A 237      38.337  -5.711  19.813  1.00 55.40           C  
ANISOU 1804  CB  GLU A 237     9786   5577   5686    357    608   -626       C  
ATOM   1805  CG  GLU A 237      38.766  -6.853  20.712  1.00 58.82           C  
ANISOU 1805  CG  GLU A 237    10636   5733   5981    543    781   -618       C  
ATOM   1806  CD  GLU A 237      38.079  -8.154  20.398  1.00 63.51           C  
ANISOU 1806  CD  GLU A 237    11901   6029   6201    222    941   -713       C  
ATOM   1807  OE1 GLU A 237      38.049  -8.545  19.211  1.00 66.89           O  
ANISOU 1807  OE1 GLU A 237    12667   6324   6425     75   1059   -748       O  
ATOM   1808  OE2 GLU A 237      37.573  -8.784  21.352  1.00 65.11           O  
ANISOU 1808  OE2 GLU A 237    12321   6124   6295     89    961   -759       O  
ATOM   1809  N   TYR A 238      40.013  -3.182  17.740  1.00 45.69           N  
ANISOU 1809  N   TYR A 238     7740   4735   4883    792    518   -490       N  
ATOM   1810  CA  TYR A 238      39.851  -1.911  17.033  1.00 45.08           C  
ANISOU 1810  CA  TYR A 238     7287   4883   4959    730    397   -472       C  
ATOM   1811  C   TYR A 238      38.707  -1.897  16.013  1.00 49.11           C  
ANISOU 1811  C   TYR A 238     7881   5463   5315    371    325   -510       C  
ATOM   1812  O   TYR A 238      37.972  -0.913  15.926  1.00 49.20           O  
ANISOU 1812  O   TYR A 238     7555   5716   5423    249    182   -484       O  
ATOM   1813  CB  TYR A 238      41.166  -1.517  16.342  1.00 46.18           C  
ANISOU 1813  CB  TYR A 238     7348   5023   5176   1028    496   -421       C  
ATOM   1814  CG  TYR A 238      41.782  -2.618  15.482  1.00 54.34           C  
ANISOU 1814  CG  TYR A 238     8839   5810   5999   1145    696   -421       C  
ATOM   1815  CD1 TYR A 238      41.674  -2.600  14.090  1.00 54.17           C  
ANISOU 1815  CD1 TYR A 238     8974   5735   5872   1018    736   -445       C  
ATOM   1816  CD2 TYR A 238      42.474  -3.684  16.068  1.00 57.93           C  
ANISOU 1816  CD2 TYR A 238     9597   6075   6340   1403    870   -384       C  
ATOM   1817  CE1 TYR A 238      42.244  -3.612  13.311  1.00 57.03           C  
ANISOU 1817  CE1 TYR A 238     9806   5838   6026   1125    953   -445       C  
ATOM   1818  CE2 TYR A 238      43.034  -4.698  15.303  1.00 60.39           C  
ANISOU 1818  CE2 TYR A 238    10387   6124   6434   1556   1103   -366       C  
ATOM   1819  CZ  TYR A 238      42.921  -4.661  13.931  1.00 59.12           C  
ANISOU 1819  CZ  TYR A 238    10398   5889   6175   1406   1149   -403       C  
ATOM   1820  OH  TYR A 238      43.491  -5.682  13.204  1.00 57.38           O  
ANISOU 1820  OH  TYR A 238    10703   5376   5724   1564   1414   -385       O  
ATOM   1821  N   LYS A 239      38.553  -2.972  15.243  1.00 54.54           N  
ANISOU 1821  N   LYS A 239     9029   5960   5735    204    440   -559       N  
ATOM   1822  CA  LYS A 239      37.511  -3.017  14.203  1.00 58.93           C  
ANISOU 1822  CA  LYS A 239     9666   6638   6087   -190    374   -590       C  
ATOM   1823  C   LYS A 239      36.089  -2.896  14.768  1.00 56.38           C  
ANISOU 1823  C   LYS A 239     9160   6573   5689   -536    209   -602       C  
ATOM   1824  O   LYS A 239      35.200  -2.402  14.084  1.00 56.41           O  
ANISOU 1824  O   LYS A 239     8964   6863   5606   -782     91   -570       O  
ATOM   1825  CB  LYS A 239      37.623  -4.288  13.334  1.00 65.41           C  
ANISOU 1825  CB  LYS A 239    11098   7175   6578   -370    563   -656       C  
ATOM   1826  CG  LYS A 239      38.758  -4.267  12.307  1.00 67.56           C  
ANISOU 1826  CG  LYS A 239    11522   7278   6870   -106    714   -630       C  
ATOM   1827  CD  LYS A 239      38.608  -5.364  11.236  1.00 73.19           C  
ANISOU 1827  CD  LYS A 239    12848   7741   7219   -380    897   -697       C  
ATOM   1828  CE  LYS A 239      37.669  -4.943  10.090  1.00 75.92           C  
ANISOU 1828  CE  LYS A 239    13085   8346   7417   -807    763   -713       C  
ATOM   1829  NZ  LYS A 239      37.712  -5.849   8.897  1.00 77.81           N  
ANISOU 1829  NZ  LYS A 239    13903   8350   7311  -1070    953   -776       N  
ATOM   1830  N   ASP A 240      35.875  -3.360  15.999  1.00 56.13           N  
ANISOU 1830  N   ASP A 240     9186   6472   5669   -545    208   -632       N  
ATOM   1831  CA  ASP A 240      34.568  -3.230  16.668  1.00 57.17           C  
ANISOU 1831  CA  ASP A 240     9112   6870   5740   -847     58   -638       C  
ATOM   1832  C   ASP A 240      34.612  -2.272  17.871  1.00 51.91           C  
ANISOU 1832  C   ASP A 240     8006   6333   5386   -598    -42   -581       C  
ATOM   1833  O   ASP A 240      33.773  -2.370  18.772  1.00 50.96           O  
ANISOU 1833  O   ASP A 240     7787   6337   5239   -763   -121   -594       O  
ATOM   1834  CB  ASP A 240      34.055  -4.596  17.146  1.00 61.52           C  
ANISOU 1834  CB  ASP A 240    10135   7246   5995  -1165    141   -738       C  
ATOM   1835  CG  ASP A 240      34.377  -5.724  16.182  1.00 68.08           C  
ANISOU 1835  CG  ASP A 240    11577   7782   6510  -1337    336   -811       C  
ATOM   1836  OD1 ASP A 240      34.894  -5.450  15.073  1.00 71.12           O  
ANISOU 1836  OD1 ASP A 240    11982   8140   6901  -1241    382   -782       O  
ATOM   1837  OD2 ASP A 240      34.112  -6.893  16.544  1.00 68.78           O  
ANISOU 1837  OD2 ASP A 240    12167   7640   6324  -1574    464   -899       O  
ATOM   1838  N   CYS A 241      35.586  -1.360  17.889  1.00 46.11           N  
ANISOU 1838  N   CYS A 241     7033   5571   4918   -237    -26   -525       N  
ATOM   1839  CA  CYS A 241      35.748  -0.409  18.997  1.00 41.48           C  
ANISOU 1839  CA  CYS A 241     6088   5076   4598    -32    -87   -481       C  
ATOM   1840  C   CYS A 241      36.678   0.701  18.562  1.00 39.75           C  
ANISOU 1840  C   CYS A 241     5641   4882   4580    240    -59   -425       C  
ATOM   1841  O   CYS A 241      37.824   0.778  19.005  1.00 38.25           O  
ANISOU 1841  O   CYS A 241     5443   4579   4513    479     14   -425       O  
ATOM   1842  CB  CYS A 241      36.296  -1.098  20.254  1.00 41.04           C  
ANISOU 1842  CB  CYS A 241     6179   4828   4585     87    -30   -520       C  
ATOM   1843  SG  CYS A 241      36.331  -0.088  21.759  1.00 37.23           S  
ANISOU 1843  SG  CYS A 241     5312   4464   4371    230   -102   -483       S  
ATOM   1844  N   HIS A 242      36.170   1.540  17.665  1.00 40.56           N  
ANISOU 1844  N   HIS A 242     5563   5166   4681    190   -109   -370       N  
ATOM   1845  CA  HIS A 242      36.892   2.707  17.180  1.00 40.69           C  
ANISOU 1845  CA  HIS A 242     5390   5211   4859    402    -73   -320       C  
ATOM   1846  C   HIS A 242      35.928   3.878  17.137  1.00 40.84           C  
ANISOU 1846  C   HIS A 242     5127   5462   4927    389   -136   -229       C  
ATOM   1847  O   HIS A 242      34.726   3.707  17.366  1.00 40.92           O  
ANISOU 1847  O   HIS A 242     5058   5657   4833    225   -217   -193       O  
ATOM   1848  CB  HIS A 242      37.511   2.442  15.799  1.00 43.70           C  
ANISOU 1848  CB  HIS A 242     5948   5510   5146    424     -9   -332       C  
ATOM   1849  CG  HIS A 242      36.521   2.034  14.755  1.00 48.70           C  
ANISOU 1849  CG  HIS A 242     6685   6263   5557    169    -63   -319       C  
ATOM   1850  ND1 HIS A 242      36.130   0.724  14.569  1.00 52.54           N  
ANISOU 1850  ND1 HIS A 242     7495   6665   5805    -78    -46   -384       N  
ATOM   1851  CD2 HIS A 242      35.853   2.762  13.830  1.00 50.47           C  
ANISOU 1851  CD2 HIS A 242     6745   6707   5723    102   -122   -242       C  
ATOM   1852  CE1 HIS A 242      35.256   0.664  13.580  1.00 52.23           C  
ANISOU 1852  CE1 HIS A 242     7465   6819   5561   -336   -106   -357       C  
ATOM   1853  NE2 HIS A 242      35.069   1.886  13.116  1.00 53.38           N  
ANISOU 1853  NE2 HIS A 242     7292   7172   5817   -210   -161   -259       N  
ATOM   1854  N   LEU A 243      36.469   5.063  16.868  1.00 41.52           N  
ANISOU 1854  N   LEU A 243     5077   5550   5147    571    -79   -183       N  
ATOM   1855  CA  LEU A 243      35.681   6.284  16.771  1.00 44.60           C  
ANISOU 1855  CA  LEU A 243     5261   6113   5572    641    -79    -72       C  
ATOM   1856  C   LEU A 243      35.245   6.500  15.333  1.00 44.73           C  
ANISOU 1856  C   LEU A 243     5268   6274   5453    618    -99      3       C  
ATOM   1857  O   LEU A 243      34.069   6.672  15.056  1.00 46.63           O  
ANISOU 1857  O   LEU A 243     5371   6776   5570    559   -163    110       O  
ATOM   1858  CB  LEU A 243      36.508   7.481  17.244  1.00 48.65           C  
ANISOU 1858  CB  LEU A 243     5715   6513   6255    820     36    -68       C  
ATOM   1859  CG  LEU A 243      37.143   7.364  18.637  1.00 51.47           C  
ANISOU 1859  CG  LEU A 243     6069   6756   6730    824     64   -141       C  
ATOM   1860  CD1 LEU A 243      38.357   8.295  18.781  1.00 55.48           C  
ANISOU 1860  CD1 LEU A 243     6576   7169   7333    908    185   -171       C  
ATOM   1861  CD2 LEU A 243      36.123   7.633  19.718  1.00 48.84           C  
ANISOU 1861  CD2 LEU A 243     5629   6500   6427    798     40    -96       C  
ATOM   1862  N   ALA A 244      36.219   6.488  14.428  1.00 47.97           N  
ANISOU 1862  N   ALA A 244     5806   6549   5872    667    -43    -42       N  
ATOM   1863  CA  ALA A 244      35.991   6.682  12.996  1.00 49.06           C  
ANISOU 1863  CA  ALA A 244     5964   6791   5884    642    -53     17       C  
ATOM   1864  C   ALA A 244      37.106   6.022  12.175  1.00 48.14           C  
ANISOU 1864  C   ALA A 244     6071   6477   5742    620     -1    -80       C  
ATOM   1865  O   ALA A 244      38.161   5.676  12.715  1.00 45.57           O  
ANISOU 1865  O   ALA A 244     5837   5964   5515    699     63   -164       O  
ATOM   1866  CB  ALA A 244      35.909   8.164  12.679  1.00 49.80           C  
ANISOU 1866  CB  ALA A 244     5926   6947   6049    846     21    128       C  
ATOM   1867  N   GLN A 245      36.865   5.871  10.872  1.00 48.23           N  
ANISOU 1867  N   GLN A 245     6156   6566   5604    528    -20    -50       N  
ATOM   1868  CA  GLN A 245      37.722   5.082   9.989  1.00 47.91           C  
ANISOU 1868  CA  GLN A 245     6370   6346   5488    477     38   -133       C  
ATOM   1869  C   GLN A 245      38.294   5.962   8.886  1.00 48.03           C  
ANISOU 1869  C   GLN A 245     6365   6348   5538    598     97   -100       C  
ATOM   1870  O   GLN A 245      37.838   5.922   7.745  1.00 52.20           O  
ANISOU 1870  O   GLN A 245     6938   6983   5913    485     65    -56       O  
ATOM   1871  CB  GLN A 245      36.915   3.916   9.401  1.00 50.87           C  
ANISOU 1871  CB  GLN A 245     6936   6795   5596    171    -20   -154       C  
ATOM   1872  CG  GLN A 245      37.743   2.718   8.952  1.00 50.58           C  
ANISOU 1872  CG  GLN A 245     7280   6485   5454    105     86   -261       C  
ATOM   1873  CD  GLN A 245      36.906   1.633   8.287  1.00 53.97           C  
ANISOU 1873  CD  GLN A 245     7974   6967   5564   -270     62   -293       C  
ATOM   1874  OE1 GLN A 245      37.347   1.012   7.323  1.00 58.03           O  
ANISOU 1874  OE1 GLN A 245     8797   7320   5931   -363    156   -343       O  
ATOM   1875  NE2 GLN A 245      35.696   1.397   8.800  1.00 54.37           N  
ANISOU 1875  NE2 GLN A 245     7923   7256   5481   -516    -49   -265       N  
ATOM   1876  N   VAL A 246      39.297   6.752   9.253  1.00 45.24           N  
ANISOU 1876  N   VAL A 246     5947   5879   5361    796    187   -123       N  
ATOM   1877  CA  VAL A 246      39.969   7.704   8.360  1.00 45.21           C  
ANISOU 1877  CA  VAL A 246     5939   5840   5399    906    267   -108       C  
ATOM   1878  C   VAL A 246      40.618   7.001   7.151  1.00 44.04           C  
ANISOU 1878  C   VAL A 246     5994   5592   5149    854    309   -161       C  
ATOM   1879  O   VAL A 246      41.093   5.883   7.287  1.00 44.10           O  
ANISOU 1879  O   VAL A 246     6167   5479   5110    821    339   -230       O  
ATOM   1880  CB  VAL A 246      41.103   8.455   9.133  1.00 45.49           C  
ANISOU 1880  CB  VAL A 246     5907   5780   5596   1043    373   -157       C  
ATOM   1881  CG1 VAL A 246      41.727   9.570   8.299  1.00 44.47           C  
ANISOU 1881  CG1 VAL A 246     5793   5620   5483   1113    473   -148       C  
ATOM   1882  CG2 VAL A 246      40.578   9.011  10.432  1.00 44.57           C  
ANISOU 1882  CG2 VAL A 246     5653   5714   5569   1070    359   -125       C  
ATOM   1883  N   PRO A 247      40.620   7.650   5.966  1.00 41.54           N  
ANISOU 1883  N   PRO A 247     5694   5310   4780    862    330   -119       N  
ATOM   1884  CA  PRO A 247      41.528   7.283   4.870  1.00 40.19           C  
ANISOU 1884  CA  PRO A 247     5704   5013   4554    859    408   -178       C  
ATOM   1885  C   PRO A 247      42.858   8.010   5.008  1.00 39.57           C  
ANISOU 1885  C   PRO A 247     5577   4848   4609   1018    528   -227       C  
ATOM   1886  O   PRO A 247      42.891   9.116   5.535  1.00 44.64           O  
ANISOU 1886  O   PRO A 247     6082   5533   5346   1086    555   -202       O  
ATOM   1887  CB  PRO A 247      40.799   7.774   3.614  1.00 38.26           C  
ANISOU 1887  CB  PRO A 247     5465   4889   4183    779    363    -97       C  
ATOM   1888  CG  PRO A 247      39.547   8.426   4.083  1.00 39.18           C  
ANISOU 1888  CG  PRO A 247     5378   5227   4281    787    271     26       C  
ATOM   1889  CD  PRO A 247      39.659   8.675   5.535  1.00 38.80           C  
ANISOU 1889  CD  PRO A 247     5214   5140   4390    889    288      6       C  
ATOM   1890  N   SER A 248      43.940   7.415   4.523  1.00 39.77           N  
ANISOU 1890  N   SER A 248     5731   4769   4610   1065    619   -291       N  
ATOM   1891  CA  SER A 248      45.276   7.962   4.774  1.00 42.45           C  
ANISOU 1891  CA  SER A 248     5980   5112   5038   1187    730   -333       C  
ATOM   1892  C   SER A 248      45.666   9.100   3.857  1.00 44.23           C  
ANISOU 1892  C   SER A 248     6196   5346   5263   1181    794   -335       C  
ATOM   1893  O   SER A 248      46.069  10.171   4.308  1.00 45.60           O  
ANISOU 1893  O   SER A 248     6260   5568   5499   1189    849   -346       O  
ATOM   1894  CB  SER A 248      46.348   6.881   4.677  1.00 45.57           C  
ANISOU 1894  CB  SER A 248     6482   5449   5385   1297    827   -370       C  
ATOM   1895  OG  SER A 248      46.699   6.433   5.971  1.00 48.83           O  
ANISOU 1895  OG  SER A 248     6790   5916   5847   1389    832   -367       O  
ATOM   1896  N   HIS A 249      45.604   8.848   2.565  1.00 45.60           N  
ANISOU 1896  N   HIS A 249     6523   5460   5344   1142    805   -333       N  
ATOM   1897  CA  HIS A 249      46.097   9.817   1.619  1.00 44.83           C  
ANISOU 1897  CA  HIS A 249     6451   5351   5233   1142    881   -343       C  
ATOM   1898  C   HIS A 249      45.504   9.526   0.252  1.00 38.79           C  
ANISOU 1898  C   HIS A 249     5851   4541   4347   1063    844   -311       C  
ATOM   1899  O   HIS A 249      45.783   8.492  -0.347  1.00 35.07           O  
ANISOU 1899  O   HIS A 249     5542   3991   3793   1032    870   -345       O  
ATOM   1900  CB  HIS A 249      47.633   9.786   1.600  1.00 47.05           C  
ANISOU 1900  CB  HIS A 249     6699   5648   5528   1209   1010   -414       C  
ATOM   1901  CG  HIS A 249      48.251  11.110   1.282  1.00 46.76           C  
ANISOU 1901  CG  HIS A 249     6623   5647   5497   1167   1103   -445       C  
ATOM   1902  ND1 HIS A 249      49.356  11.242   0.472  1.00 45.95           N  
ANISOU 1902  ND1 HIS A 249     6555   5563   5342   1167   1212   -496       N  
ATOM   1903  CD2 HIS A 249      47.896  12.364   1.644  1.00 45.71           C  
ANISOU 1903  CD2 HIS A 249     6465   5515   5387   1114   1127   -430       C  
ATOM   1904  CE1 HIS A 249      49.666  12.520   0.360  1.00 46.67           C  
ANISOU 1904  CE1 HIS A 249     6642   5673   5418   1078   1291   -526       C  
ATOM   1905  NE2 HIS A 249      48.793  13.223   1.059  1.00 47.64           N  
ANISOU 1905  NE2 HIS A 249     6758   5763   5581   1051   1254   -486       N  
ATOM   1906  N   THR A 250      44.687  10.458  -0.222  1.00 35.72           N  
ANISOU 1906  N   THR A 250     5439   4209   3926   1041    802   -234       N  
ATOM   1907  CA  THR A 250      43.835  10.217  -1.363  1.00 37.30           C  
ANISOU 1907  CA  THR A 250     5735   4457   3980    942    729   -167       C  
ATOM   1908  C   THR A 250      44.038  11.220  -2.485  1.00 35.47           C  
ANISOU 1908  C   THR A 250     5566   4207   3703    973    792   -136       C  
ATOM   1909  O   THR A 250      44.006  12.429  -2.262  1.00 36.15           O  
ANISOU 1909  O   THR A 250     5601   4299   3835   1077    851    -92       O  
ATOM   1910  CB  THR A 250      42.371  10.272  -0.941  1.00 37.54           C  
ANISOU 1910  CB  THR A 250     5641   4673   3950    905    596    -46       C  
ATOM   1911  OG1 THR A 250      42.174   9.371   0.152  1.00 38.63           O  
ANISOU 1911  OG1 THR A 250     5737   4815   4126    859    543    -84       O  
ATOM   1912  CG2 THR A 250      41.478   9.866  -2.103  1.00 39.24           C  
ANISOU 1912  CG2 THR A 250     5920   5031   3957    745    504     33       C  
ATOM   1913  N   VAL A 251      44.250  10.702  -3.689  1.00 33.34           N  
ANISOU 1913  N   VAL A 251     5453   3890   3323    876    801   -162       N  
ATOM   1914  CA  VAL A 251      44.197  11.514  -4.888  1.00 35.49           C  
ANISOU 1914  CA  VAL A 251     5801   4170   3515    879    833   -113       C  
ATOM   1915  C   VAL A 251      42.737  11.706  -5.195  1.00 39.28           C  
ANISOU 1915  C   VAL A 251     6196   4872   3857    843    703     51       C  
ATOM   1916  O   VAL A 251      41.961  10.752  -5.172  1.00 40.41           O  
ANISOU 1916  O   VAL A 251     6322   5147   3887    685    587     81       O  
ATOM   1917  CB  VAL A 251      44.830  10.826  -6.109  1.00 37.81           C  
ANISOU 1917  CB  VAL A 251     6297   4355   3714    765    882   -187       C  
ATOM   1918  CG1 VAL A 251      44.731  11.717  -7.323  1.00 37.87           C  
ANISOU 1918  CG1 VAL A 251     6377   4378   3635    765    908   -131       C  
ATOM   1919  CG2 VAL A 251      46.276  10.454  -5.838  1.00 37.93           C  
ANISOU 1919  CG2 VAL A 251     6365   4217   3828    832   1019   -321       C  
ATOM   1920  N   VAL A 252      42.375  12.944  -5.493  1.00 43.74           N  
ANISOU 1920  N   VAL A 252     6722   5500   4399    988    739    166       N  
ATOM   1921  CA  VAL A 252      41.004  13.305  -5.796  1.00 44.19           C  
ANISOU 1921  CA  VAL A 252     6651   5839   4299   1036    638    372       C  
ATOM   1922  C   VAL A 252      40.941  13.801  -7.230  1.00 46.91           C  
ANISOU 1922  C   VAL A 252     7099   6230   4494   1038    659    451       C  
ATOM   1923  O   VAL A 252      41.952  14.241  -7.782  1.00 44.62           O  
ANISOU 1923  O   VAL A 252     6982   5710   4261   1062    785    349       O  
ATOM   1924  CB  VAL A 252      40.502  14.403  -4.844  1.00 43.15           C  
ANISOU 1924  CB  VAL A 252     6406   5755   4235   1292    699    494       C  
ATOM   1925  CG1 VAL A 252      40.698  13.975  -3.402  1.00 38.95           C  
ANISOU 1925  CG1 VAL A 252     5788   5149   3861   1277    690    398       C  
ATOM   1926  CG2 VAL A 252      41.235  15.714  -5.105  1.00 42.29           C  
ANISOU 1926  CG2 VAL A 252     6471   5422   4173   1467    896    480       C  
ATOM   1927  N   ALA A 253      39.751  13.723  -7.820  1.00 49.86           N  
ANISOU 1927  N   ALA A 253     7347   6942   4654    999    534    638       N  
ATOM   1928  CA  ALA A 253      39.523  14.135  -9.198  1.00 49.97           C  
ANISOU 1928  CA  ALA A 253     7424   7078   4484    993    529    749       C  
ATOM   1929  C   ALA A 253      38.184  14.852  -9.326  1.00 56.13           C  
ANISOU 1929  C   ALA A 253     7982   8270   5074   1195    465   1048       C  
ATOM   1930  O   ALA A 253      37.362  14.838  -8.404  1.00 56.62           O  
ANISOU 1930  O   ALA A 253     7830   8556   5128   1289    405   1161       O  
ATOM   1931  CB  ALA A 253      39.548  12.928 -10.098  1.00 50.11           C  
ANISOU 1931  CB  ALA A 253     7537   7156   4347    631    430    665       C  
ATOM   1932  N   ARG A 254      37.978  15.481 -10.479  1.00 61.01           N  
ANISOU 1932  N   ARG A 254     8647   9010   5525   1284    488   1189       N  
ATOM   1933  CA  ARG A 254      36.708  16.126 -10.808  1.00 65.59           C  
ANISOU 1933  CA  ARG A 254     9000  10058   5864   1511    434   1519       C  
ATOM   1934  C   ARG A 254      35.621  15.059 -10.810  1.00 66.41           C  
ANISOU 1934  C   ARG A 254     8817  10673   5742   1213    205   1616       C  
ATOM   1935  O   ARG A 254      35.820  13.968 -11.346  1.00 65.17           O  
ANISOU 1935  O   ARG A 254     8741  10522   5497    790    102   1467       O  
ATOM   1936  CB  ARG A 254      36.789  16.758 -12.199  1.00 69.99           C  
ANISOU 1936  CB  ARG A 254     9681  10661   6252   1593    483   1633       C  
ATOM   1937  CG  ARG A 254      36.440  18.225 -12.298  1.00 72.86           C  
ANISOU 1937  CG  ARG A 254    10082  11053   6548   2090    653   1884       C  
ATOM   1938  CD  ARG A 254      36.890  18.787 -13.658  1.00 74.42           C  
ANISOU 1938  CD  ARG A 254    10507  11136   6632   2128    736   1912       C  
ATOM   1939  NE  ARG A 254      38.352  18.841 -13.751  1.00 70.15           N  
ANISOU 1939  NE  ARG A 254    10313  10019   6322   1982    876   1593       N  
ATOM   1940  CZ  ARG A 254      39.119  18.095 -14.544  1.00 67.25           C  
ANISOU 1940  CZ  ARG A 254    10077   9497   5977   1633    820   1383       C  
ATOM   1941  NH1 ARG A 254      38.605  17.205 -15.387  1.00 68.48           N  
ANISOU 1941  NH1 ARG A 254    10111   9976   5932   1340    635   1431       N  
ATOM   1942  NH2 ARG A 254      40.431  18.259 -14.496  1.00 65.46           N  
ANISOU 1942  NH2 ARG A 254    10120   8802   5949   1563    970   1126       N  
ATOM   1943  N   SER A 255      34.474  15.364 -10.221  1.00 70.07           N  
ANISOU 1943  N   SER A 255     8972  11571   6082   1414    146   1866       N  
ATOM   1944  CA  SER A 255      33.398  14.384 -10.146  1.00 75.54           C  
ANISOU 1944  CA  SER A 255     9366  12814   6523   1090    -70   1961       C  
ATOM   1945  C   SER A 255      32.775  14.154 -11.510  1.00 79.67           C  
ANISOU 1945  C   SER A 255     9771  13824   6676    860   -200   2128       C  
ATOM   1946  O   SER A 255      32.329  13.049 -11.814  1.00 78.77           O  
ANISOU 1946  O   SER A 255     9581  14015   6333    364   -364   2078       O  
ATOM   1947  CB  SER A 255      32.332  14.815  -9.138  1.00 80.74           C  
ANISOU 1947  CB  SER A 255     9687  13862   7130   1386    -90   2203       C  
ATOM   1948  OG  SER A 255      31.638  13.691  -8.618  1.00 84.41           O  
ANISOU 1948  OG  SER A 255     9940  14672   7462    998   -269   2166       O  
ATOM   1949  N   MET A 256      32.760  15.201 -12.330  1.00 84.65           N  
ANISOU 1949  N   MET A 256    10422  14517   7223   1199   -112   2324       N  
ATOM   1950  CA  MET A 256      32.234  15.111 -13.682  1.00 89.75           C  
ANISOU 1950  CA  MET A 256    10959  15630   7512   1018   -225   2501       C  
ATOM   1951  C   MET A 256      33.354  14.967 -14.709  1.00 88.30           C  
ANISOU 1951  C   MET A 256    11166  14971   7412    811   -156   2271       C  
ATOM   1952  O   MET A 256      33.529  13.888 -15.270  1.00 91.77           O  
ANISOU 1952  O   MET A 256    11719  15419   7731    287   -258   2099       O  
ATOM   1953  CB  MET A 256      31.349  16.320 -13.995  1.00 96.87           C  
ANISOU 1953  CB  MET A 256    11598  17008   8199   1554   -176   2924       C  
ATOM   1954  CG  MET A 256      29.870  16.090 -13.688  1.00103.51           C  
ANISOU 1954  CG  MET A 256    11915  18713   8701   1550   -346   3248       C  
ATOM   1955  SD  MET A 256      29.041  15.025 -14.899  1.00110.43           S  
ANISOU 1955  SD  MET A 256    12516  20386   9056    879   -628   3350       S  
ATOM   1956  CE  MET A 256      29.232  15.977 -16.413  1.00110.06           C  
ANISOU 1956  CE  MET A 256    12572  20414   8833   1162   -553   3564       C  
ATOM   1957  N   GLY A 257      34.113  16.037 -14.950  1.00 84.85           N  
ANISOU 1957  N   GLY A 257    10969  14110   7159   1202     39   2261       N  
ATOM   1958  CA  GLY A 257      35.162  16.028 -15.980  1.00 81.75           C  
ANISOU 1958  CA  GLY A 257    10927  13304   6829   1042    117   2067       C  
ATOM   1959  C   GLY A 257      36.092  14.826 -15.892  1.00 77.30           C  
ANISOU 1959  C   GLY A 257    10610  12334   6427    581    100   1700       C  
ATOM   1960  O   GLY A 257      36.134  13.997 -16.801  1.00 76.46           O  
ANISOU 1960  O   GLY A 257    10602  12314   6135    162     14   1621       O  
ATOM   1961  N   GLY A 258      36.840  14.743 -14.793  1.00 72.94           N  
ANISOU 1961  N   GLY A 258    10173  11345   6195    673    202   1492       N  
ATOM   1962  CA  GLY A 258      37.631  13.563 -14.451  1.00 69.27           C  
ANISOU 1962  CA  GLY A 258     9902  10542   5876    327    203   1189       C  
ATOM   1963  C   GLY A 258      39.072  13.864 -14.031  1.00 64.29           C  
ANISOU 1963  C   GLY A 258     9530   9317   5579    481    393    946       C  
ATOM   1964  O   GLY A 258      39.313  14.727 -13.177  1.00 58.47           O  
ANISOU 1964  O   GLY A 258     8760   8423   5034    805    499    962       O  
ATOM   1965  N   LYS A 259      40.045  13.149 -14.597  1.00 63.37           N  
ANISOU 1965  N   LYS A 259     9677   8890   5509    241    452    725       N  
ATOM   1966  CA  LYS A 259      39.827  12.125 -15.631  1.00 64.58           C  
ANISOU 1966  CA  LYS A 259     9959   9162   5416   -168    371    688       C  
ATOM   1967  C   LYS A 259      39.977  10.708 -15.041  1.00 63.14           C  
ANISOU 1967  C   LYS A 259     9898   8855   5240   -468    356    513       C  
ATOM   1968  O   LYS A 259      40.354   9.768 -15.736  1.00 63.13           O  
ANISOU 1968  O   LYS A 259    10170   8700   5116   -779    397    382       O  
ATOM   1969  CB  LYS A 259      40.770  12.360 -16.829  1.00 65.20           C  
ANISOU 1969  CB  LYS A 259    10311   8964   5496   -205    487    586       C  
ATOM   1970  CG  LYS A 259      41.382  13.773 -16.884  1.00 64.02           C  
ANISOU 1970  CG  LYS A 259    10185   8622   5517    175    622    617       C  
ATOM   1971  CD  LYS A 259      41.648  14.253 -18.302  1.00 66.61           C  
ANISOU 1971  CD  LYS A 259    10683   8916   5709    137    668    649       C  
ATOM   1972  CE  LYS A 259      42.267  15.655 -18.271  1.00 67.77           C  
ANISOU 1972  CE  LYS A 259    10913   8835   6001    488    834    663       C  
ATOM   1973  NZ  LYS A 259      42.419  16.308 -19.598  1.00 69.14           N  
ANISOU 1973  NZ  LYS A 259    11251   8990   6030    506    887    727       N  
ATOM   1974  N   GLU A 260      39.702  10.592 -13.743  1.00 63.14           N  
ANISOU 1974  N   GLU A 260     9730   8889   5372   -352    324    515       N  
ATOM   1975  CA  GLU A 260      39.451   9.316 -13.051  1.00 65.43           C  
ANISOU 1975  CA  GLU A 260    10084   9172   5604   -624    282    414       C  
ATOM   1976  C   GLU A 260      40.254   8.095 -13.547  1.00 63.22           C  
ANISOU 1976  C   GLU A 260    10211   8547   5263   -910    399    205       C  
ATOM   1977  O   GLU A 260      41.165   7.633 -12.867  1.00 57.89           O  
ANISOU 1977  O   GLU A 260     9689   7520   4788   -793    526     50       O  
ATOM   1978  CB  GLU A 260      37.938   9.018 -13.065  1.00 70.46           C  
ANISOU 1978  CB  GLU A 260    10483  10360   5928   -880     91    597       C  
ATOM   1979  CG  GLU A 260      37.053  10.274 -13.207  1.00 73.74           C  
ANISOU 1979  CG  GLU A 260    10533  11213   6273   -599     -3    876       C  
ATOM   1980  CD  GLU A 260      35.575  10.012 -12.939  1.00 78.35           C  
ANISOU 1980  CD  GLU A 260    10787  12420   6564   -782   -188   1082       C  
ATOM   1981  OE1 GLU A 260      34.745  10.906 -13.233  1.00 81.63           O  
ANISOU 1981  OE1 GLU A 260    10895  13287   6835   -567   -262   1354       O  
ATOM   1982  OE2 GLU A 260      35.242   8.918 -12.433  1.00 78.37           O  
ANISOU 1982  OE2 GLU A 260    10839  12480   6457  -1132   -244    984       O  
ATOM   1983  N   ASP A 261      39.914   7.585 -14.728  1.00 51.78           N  
ANISOU 1983  N   ASP A 261     7951   6918   4805  -1270   -290    753       N  
ATOM   1984  CA  ASP A 261      40.528   6.363 -15.257  1.00 53.48           C  
ANISOU 1984  CA  ASP A 261     8043   7261   5018  -1410   -150    439       C  
ATOM   1985  C   ASP A 261      41.959   6.638 -15.700  1.00 52.64           C  
ANISOU 1985  C   ASP A 261     8030   7179   4793  -1529     70    510       C  
ATOM   1986  O   ASP A 261      42.877   5.892 -15.368  1.00 52.54           O  
ANISOU 1986  O   ASP A 261     7904   7092   4968  -1596    243    343       O  
ATOM   1987  CB  ASP A 261      39.716   5.818 -16.432  1.00 58.32           C  
ANISOU 1987  CB  ASP A 261     8590   8237   5333  -1414   -272    219       C  
ATOM   1988  CG  ASP A 261      38.226   5.825 -16.159  1.00 61.77           C  
ANISOU 1988  CG  ASP A 261     8900   8766   5805  -1305   -514    185       C  
ATOM   1989  OD1 ASP A 261      37.762   4.944 -15.406  1.00 62.38           O  
ANISOU 1989  OD1 ASP A 261     8805   8702   6195  -1364   -508    -31       O  
ATOM   1990  OD2 ASP A 261      37.528   6.724 -16.689  1.00 65.69           O  
ANISOU 1990  OD2 ASP A 261     9466   9484   6009  -1147   -698    393       O  
ATOM   1991  N   LEU A 262      42.136   7.718 -16.451  1.00 52.07           N  
ANISOU 1991  N   LEU A 262     8160   7222   4402  -1542     75    774       N  
ATOM   1992  CA  LEU A 262      43.464   8.195 -16.805  1.00 51.55           C  
ANISOU 1992  CA  LEU A 262     8186   7178   4222  -1706    309    892       C  
ATOM   1993  C   LEU A 262      44.386   8.292 -15.578  1.00 48.48           C  
ANISOU 1993  C   LEU A 262     7703   6520   4195  -1794    434    907       C  
ATOM   1994  O   LEU A 262      45.461   7.693 -15.545  1.00 48.12           O  
ANISOU 1994  O   LEU A 262     7498   6557   4229  -1890    619    744       O  
ATOM   1995  CB  LEU A 262      43.368   9.560 -17.481  1.00 51.56           C  
ANISOU 1995  CB  LEU A 262     8489   7204   3896  -1710    303   1269       C  
ATOM   1996  CG  LEU A 262      44.576   9.883 -18.341  1.00 54.82           C  
ANISOU 1996  CG  LEU A 262     8996   7785   4049  -1925    570   1357       C  
ATOM   1997  CD1 LEU A 262      44.617   8.941 -19.538  1.00 58.05           C  
ANISOU 1997  CD1 LEU A 262     9302   8618   4137  -1923    614   1099       C  
ATOM   1998  CD2 LEU A 262      44.524  11.325 -18.790  1.00 59.26           C  
ANISOU 1998  CD2 LEU A 262     9923   8239   4353  -1952    607   1795       C  
ATOM   1999  N   ILE A 263      43.948   9.036 -14.570  1.00 45.20           N  
ANISOU 1999  N   ILE A 263     7370   5827   3978  -1734    325   1084       N  
ATOM   2000  CA  ILE A 263      44.726   9.222 -13.353  1.00 42.90           C  
ANISOU 2000  CA  ILE A 263     6989   5327   3983  -1815    404   1087       C  
ATOM   2001  C   ILE A 263      45.253   7.885 -12.846  1.00 42.80           C  
ANISOU 2001  C   ILE A 263     6694   5377   4191  -1775    473    811       C  
ATOM   2002  O   ILE A 263      46.428   7.755 -12.481  1.00 43.94           O  
ANISOU 2002  O   ILE A 263     6692   5574   4429  -1868    620    754       O  
ATOM   2003  CB  ILE A 263      43.877   9.883 -12.256  1.00 42.48           C  
ANISOU 2003  CB  ILE A 263     7028   4991   4120  -1691    242   1216       C  
ATOM   2004  CG1 ILE A 263      43.655  11.368 -12.583  1.00 45.34           C  
ANISOU 2004  CG1 ILE A 263     7719   5192   4315  -1719    232   1515       C  
ATOM   2005  CG2 ILE A 263      44.551   9.731 -10.885  1.00 41.67           C  
ANISOU 2005  CG2 ILE A 263     6769   4750   4313  -1736    286   1134       C  
ATOM   2006  CD1 ILE A 263      42.482  12.007 -11.854  1.00 43.42           C  
ANISOU 2006  CD1 ILE A 263     7603   4716   4178  -1496     50   1634       C  
ATOM   2007  N   TRP A 264      44.369   6.897 -12.829  1.00 40.59           N  
ANISOU 2007  N   TRP A 264     6335   5094   3992  -1631    372    644       N  
ATOM   2008  CA  TRP A 264      44.721   5.557 -12.405  1.00 37.36           C  
ANISOU 2008  CA  TRP A 264     5734   4662   3800  -1558    454    404       C  
ATOM   2009  C   TRP A 264      45.800   4.996 -13.328  1.00 41.47           C  
ANISOU 2009  C   TRP A 264     6170   5406   4180  -1618    653    236       C  
ATOM   2010  O   TRP A 264      46.898   4.666 -12.878  1.00 43.39           O  
ANISOU 2010  O   TRP A 264     6259   5679   4550  -1596    793    181       O  
ATOM   2011  CB  TRP A 264      43.470   4.681 -12.391  1.00 35.13           C  
ANISOU 2011  CB  TRP A 264     5431   4310   3608  -1468    339    248       C  
ATOM   2012  CG  TRP A 264      43.732   3.243 -12.204  1.00 36.46           C  
ANISOU 2012  CG  TRP A 264     5486   4391   3974  -1408    460     -5       C  
ATOM   2013  CD1 TRP A 264      43.408   2.244 -13.063  1.00 40.07           C  
ANISOU 2013  CD1 TRP A 264     5937   4913   4374  -1437    511   -286       C  
ATOM   2014  CD2 TRP A 264      44.389   2.622 -11.093  1.00 34.21           C  
ANISOU 2014  CD2 TRP A 264     5106   3922   3968  -1290    557     -3       C  
ATOM   2015  NE1 TRP A 264      43.809   1.031 -12.556  1.00 39.33           N  
ANISOU 2015  NE1 TRP A 264     5788   4612   4543  -1344    659   -456       N  
ATOM   2016  CE2 TRP A 264      44.415   1.235 -11.348  1.00 35.44           C  
ANISOU 2016  CE2 TRP A 264     5239   3977   4248  -1226    684   -258       C  
ATOM   2017  CE3 TRP A 264      44.960   3.101  -9.911  1.00 29.80           C  
ANISOU 2017  CE3 TRP A 264     4489   3288   3546  -1222    547    181       C  
ATOM   2018  CZ2 TRP A 264      44.985   0.324 -10.467  1.00 34.47           C  
ANISOU 2018  CZ2 TRP A 264     5064   3650   4384  -1049    807   -278       C  
ATOM   2019  CZ3 TRP A 264      45.510   2.190  -9.024  1.00 29.58           C  
ANISOU 2019  CZ3 TRP A 264     4364   3137   3739  -1052    639    148       C  
ATOM   2020  CH2 TRP A 264      45.527   0.819  -9.311  1.00 32.69           C  
ANISOU 2020  CH2 TRP A 264     4762   3404   4255   -943    773    -53       C  
ATOM   2021  N   GLU A 265      45.508   4.925 -14.621  1.00 45.57           N  
ANISOU 2021  N   GLU A 265     6773   6135   4408  -1673    666    151       N  
ATOM   2022  CA  GLU A 265      46.477   4.402 -15.592  1.00 49.41           C  
ANISOU 2022  CA  GLU A 265     7186   6874   4712  -1723    877    -36       C  
ATOM   2023  C   GLU A 265      47.887   4.953 -15.315  1.00 49.59           C  
ANISOU 2023  C   GLU A 265     7097   6993   4753  -1819   1059     76       C  
ATOM   2024  O   GLU A 265      48.836   4.190 -15.171  1.00 51.33           O  
ANISOU 2024  O   GLU A 265     7117   7301   5086  -1743   1222   -103       O  
ATOM   2025  CB  GLU A 265      46.038   4.713 -17.028  1.00 52.45           C  
ANISOU 2025  CB  GLU A 265     7716   7540   4672  -1804    857    -46       C  
ATOM   2026  CG  GLU A 265      46.863   3.999 -18.101  1.00 60.27           C  
ANISOU 2026  CG  GLU A 265     8634   8826   5442  -1836   1079   -312       C  
ATOM   2027  CD  GLU A 265      46.384   4.275 -19.534  1.00 66.74           C  
ANISOU 2027  CD  GLU A 265     9602   9985   5772  -1905   1047   -330       C  
ATOM   2028  OE1 GLU A 265      45.296   4.870 -19.720  1.00 69.07           O  
ANISOU 2028  OE1 GLU A 265    10038  10294   5911  -1885    820   -160       O  
ATOM   2029  OE2 GLU A 265      47.100   3.883 -20.482  1.00 68.06           O  
ANISOU 2029  OE2 GLU A 265     9731  10446   5684  -1949   1250   -520       O  
ATOM   2030  N   LEU A 266      48.011   6.272 -15.216  1.00 48.15           N  
ANISOU 2030  N   LEU A 266     7036   6791   4468  -1981   1038    360       N  
ATOM   2031  CA  LEU A 266      49.296   6.909 -14.909  1.00 48.71           C  
ANISOU 2031  CA  LEU A 266     6983   6961   4562  -2160   1209    448       C  
ATOM   2032  C   LEU A 266      49.940   6.359 -13.644  1.00 47.69           C  
ANISOU 2032  C   LEU A 266     6586   6770   4762  -2045   1210    339       C  
ATOM   2033  O   LEU A 266      51.109   5.974 -13.645  1.00 47.81           O  
ANISOU 2033  O   LEU A 266     6342   7024   4799  -2051   1382    210       O  
ATOM   2034  CB  LEU A 266      49.119   8.418 -14.726  1.00 48.43           C  
ANISOU 2034  CB  LEU A 266     7180   6765   4455  -2364   1166    760       C  
ATOM   2035  CG  LEU A 266      50.388   9.202 -14.374  1.00 49.69           C  
ANISOU 2035  CG  LEU A 266     7225   7005   4650  -2647   1349    828       C  
ATOM   2036  CD1 LEU A 266      51.355   9.218 -15.558  1.00 54.37           C  
ANISOU 2036  CD1 LEU A 266     7743   7956   4961  -2847   1626    794       C  
ATOM   2037  CD2 LEU A 266      50.052  10.621 -13.945  1.00 50.30           C  
ANISOU 2037  CD2 LEU A 266     7588   6779   4746  -2832   1292   1096       C  
ATOM   2038  N   LEU A 267      49.177   6.354 -12.559  1.00 44.53           N  
ANISOU 2038  N   LEU A 267     6237   6093   4591  -1920   1018    404       N  
ATOM   2039  CA  LEU A 267      49.727   5.997 -11.263  1.00 41.24           C  
ANISOU 2039  CA  LEU A 267     5602   5635   4432  -1801    992    362       C  
ATOM   2040  C   LEU A 267      50.030   4.525 -11.177  1.00 41.35           C  
ANISOU 2040  C   LEU A 267     5438   5695   4580  -1528   1065    153       C  
ATOM   2041  O   LEU A 267      51.059   4.134 -10.632  1.00 42.23           O  
ANISOU 2041  O   LEU A 267     5291   5966   4788  -1415   1145     87       O  
ATOM   2042  CB  LEU A 267      48.778   6.408 -10.144  1.00 37.26           C  
ANISOU 2042  CB  LEU A 267     5225   4840   4091  -1736    788    494       C  
ATOM   2043  CG  LEU A 267      48.658   7.922  -9.992  1.00 36.15           C  
ANISOU 2043  CG  LEU A 267     5266   4600   3870  -1970    740    685       C  
ATOM   2044  CD1 LEU A 267      47.641   8.271  -8.929  1.00 33.55           C  
ANISOU 2044  CD1 LEU A 267     5062   3997   3687  -1857    553    778       C  
ATOM   2045  CD2 LEU A 267      50.009   8.532  -9.676  1.00 33.86           C  
ANISOU 2045  CD2 LEU A 267     4796   4499   3572  -2200    864    667       C  
ATOM   2046  N   ASN A 268      49.144   3.703 -11.717  1.00 43.88           N  
ANISOU 2046  N   ASN A 268     5893   5877   4903  -1413   1041     39       N  
ATOM   2047  CA  ASN A 268      49.379   2.271 -11.721  1.00 47.66           C  
ANISOU 2047  CA  ASN A 268     6279   6305   5526  -1165   1148   -178       C  
ATOM   2048  C   ASN A 268      50.621   1.945 -12.541  1.00 50.71           C  
ANISOU 2048  C   ASN A 268     6481   7009   5777  -1139   1372   -346       C  
ATOM   2049  O   ASN A 268      51.462   1.155 -12.130  1.00 52.43           O  
ANISOU 2049  O   ASN A 268     6502   7284   6134   -895   1483   -448       O  
ATOM   2050  CB  ASN A 268      48.171   1.524 -12.274  1.00 48.53           C  
ANISOU 2050  CB  ASN A 268     6579   6212   5647  -1142   1101   -325       C  
ATOM   2051  CG  ASN A 268      48.344   0.028 -12.198  1.00 51.98           C  
ANISOU 2051  CG  ASN A 268     6993   6477   6280   -907   1239   -558       C  
ATOM   2052  OD1 ASN A 268      48.518  -0.536 -11.115  1.00 52.47           O  
ANISOU 2052  OD1 ASN A 268     7007   6337   6592   -695   1247   -489       O  
ATOM   2053  ND2 ASN A 268      48.319  -0.626 -13.349  1.00 53.80           N  
ANISOU 2053  ND2 ASN A 268     7280   6778   6383   -927   1362   -834       N  
ATOM   2054  N   GLN A 269      50.742   2.581 -13.696  1.00 55.79           N  
ANISOU 2054  N   GLN A 269     7186   7885   6128  -1367   1448   -357       N  
ATOM   2055  CA  GLN A 269      51.906   2.384 -14.543  1.00 62.22           C  
ANISOU 2055  CA  GLN A 269     7813   9059   6767  -1381   1691   -513       C  
ATOM   2056  C   GLN A 269      53.151   2.989 -13.875  1.00 64.32           C  
ANISOU 2056  C   GLN A 269     7779   9577   7083  -1448   1765   -412       C  
ATOM   2057  O   GLN A 269      54.271   2.550 -14.128  1.00 70.89           O  
ANISOU 2057  O   GLN A 269     8329  10723   7883  -1344   1961   -567       O  
ATOM   2058  CB  GLN A 269      51.666   2.987 -15.929  1.00 66.87           C  
ANISOU 2058  CB  GLN A 269     8569   9857   6980  -1629   1762   -505       C  
ATOM   2059  CG  GLN A 269      52.396   2.260 -17.048  1.00 76.20           C  
ANISOU 2059  CG  GLN A 269     9639  11354   7958  -1563   2017   -786       C  
ATOM   2060  CD  GLN A 269      51.599   1.098 -17.619  1.00 80.75           C  
ANISOU 2060  CD  GLN A 269    10371  11777   8533  -1392   2001  -1085       C  
ATOM   2061  OE1 GLN A 269      50.640   1.299 -18.367  1.00 82.75           O  
ANISOU 2061  OE1 GLN A 269    10847  12033   8560  -1521   1893  -1098       O  
ATOM   2062  NE2 GLN A 269      52.005  -0.125 -17.283  1.00 83.57           N  
ANISOU 2062  NE2 GLN A 269    10614  12005   9133  -1096   2113  -1338       N  
ATOM   2063  N   ALA A 270      52.947   3.987 -13.016  1.00 61.93           N  
ANISOU 2063  N   ALA A 270     7517   9161   6854  -1619   1610   -185       N  
ATOM   2064  CA  ALA A 270      54.029   4.589 -12.232  1.00 60.68           C  
ANISOU 2064  CA  ALA A 270     7063   9237   6756  -1729   1641   -129       C  
ATOM   2065  C   ALA A 270      54.589   3.638 -11.170  1.00 61.51           C  
ANISOU 2065  C   ALA A 270     6881   9400   7090  -1356   1600   -222       C  
ATOM   2066  O   ALA A 270      55.798   3.519 -11.028  1.00 67.70           O  
ANISOU 2066  O   ALA A 270     7290  10570   7860  -1301   1717   -318       O  
ATOM   2067  CB  ALA A 270      53.552   5.876 -11.577  1.00 56.49           C  
ANISOU 2067  CB  ALA A 270     6708   8512   6246  -2008   1484     92       C  
ATOM   2068  N   GLN A 271      53.715   2.963 -10.429  1.00 60.27           N  
ANISOU 2068  N   GLN A 271     6888   8886   7126  -1089   1446   -180       N  
ATOM   2069  CA  GLN A 271      54.149   2.066  -9.348  1.00 60.19           C  
ANISOU 2069  CA  GLN A 271     6677   8880   7314   -693   1403   -196       C  
ATOM   2070  C   GLN A 271      54.734   0.765  -9.878  1.00 63.82           C  
ANISOU 2070  C   GLN A 271     7014   9418   7817   -327   1593   -394       C  
ATOM   2071  O   GLN A 271      55.479   0.079  -9.173  1.00 66.61           O  
ANISOU 2071  O   GLN A 271     7126   9903   8281     45   1613   -408       O  
ATOM   2072  CB  GLN A 271      52.989   1.741  -8.407  1.00 57.39           C  
ANISOU 2072  CB  GLN A 271     6576   8092   7136   -545   1223    -60       C  
ATOM   2073  CG  GLN A 271      52.150   0.532  -8.813  1.00 54.87           C  
ANISOU 2073  CG  GLN A 271     6503   7407   6938   -329   1285   -153       C  
ATOM   2074  CD  GLN A 271      50.939   0.375  -7.933  1.00 50.47           C  
ANISOU 2074  CD  GLN A 271     6180   6461   6537   -287   1134     -8       C  
ATOM   2075  OE1 GLN A 271      49.812   0.490  -8.396  1.00 53.73           O  
ANISOU 2075  OE1 GLN A 271     6828   6648   6937   -463   1082    -23       O  
ATOM   2076  NE2 GLN A 271      51.164   0.134  -6.650  1.00 44.27           N  
ANISOU 2076  NE2 GLN A 271     5305   5647   5870    -51   1060    136       N  
ATOM   2077  N   GLU A 272      54.360   0.411 -11.103  1.00 63.82           N  
ANISOU 2077  N   GLU A 272     7199   9334   7717   -398   1728   -550       N  
ATOM   2078  CA  GLU A 272      54.950  -0.723 -11.774  1.00 65.76           C  
ANISOU 2078  CA  GLU A 272     7353   9661   7974    -88   1947   -796       C  
ATOM   2079  C   GLU A 272      56.410  -0.402 -12.075  1.00 64.86           C  
ANISOU 2079  C   GLU A 272     6807  10122   7715    -89   2111   -882       C  
ATOM   2080  O   GLU A 272      57.272  -1.277 -12.010  1.00 69.79           O  
ANISOU 2080  O   GLU A 272     7187  10922   8410    312   2252  -1024       O  
ATOM   2081  CB  GLU A 272      54.190  -1.021 -13.065  1.00 71.47           C  
ANISOU 2081  CB  GLU A 272     8366  10230   8561   -238   2040   -984       C  
ATOM   2082  CG  GLU A 272      54.405  -2.430 -13.608  1.00 80.85           C  
ANISOU 2082  CG  GLU A 272     9599  11288   9832    116   2246  -1286       C  
ATOM   2083  CD  GLU A 272      53.781  -3.509 -12.730  1.00 84.74           C  
ANISOU 2083  CD  GLU A 272    10297  11250  10649    437   2194  -1266       C  
ATOM   2084  OE1 GLU A 272      54.160  -4.694 -12.896  1.00 90.64           O  
ANISOU 2084  OE1 GLU A 272    11075  11833  11530    809   2384  -1474       O  
ATOM   2085  OE2 GLU A 272      52.920  -3.174 -11.879  1.00 81.02           O  
ANISOU 2085  OE2 GLU A 272     9973  10513  10298    324   1990  -1040       O  
ATOM   2086  N   HIS A 273      56.682   0.868 -12.369  1.00 59.66           N  
ANISOU 2086  N   HIS A 273     6053   9752   6861   -537   2106   -788       N  
ATOM   2087  CA  HIS A 273      57.984   1.288 -12.892  1.00 60.61           C  
ANISOU 2087  CA  HIS A 273     5773  10451   6803   -679   2312   -891       C  
ATOM   2088  C   HIS A 273      58.933   1.879 -11.865  1.00 63.31           C  
ANISOU 2088  C   HIS A 273     5692  11163   7200   -737   2235   -813       C  
ATOM   2089  O   HIS A 273      60.085   1.460 -11.793  1.00 69.72           O  
ANISOU 2089  O   HIS A 273     6051  12437   8003   -504   2362   -955       O  
ATOM   2090  CB  HIS A 273      57.796   2.278 -14.038  1.00 55.17           C  
ANISOU 2090  CB  HIS A 273     5255   9878   5831  -1182   2429   -851       C  
ATOM   2091  CG  HIS A 273      57.553   1.612 -15.351  1.00 53.93           C  
ANISOU 2091  CG  HIS A 273     5273   9726   5494  -1100   2617  -1049       C  
ATOM   2092  ND1 HIS A 273      56.293   1.438 -15.876  1.00 50.14           N  
ANISOU 2092  ND1 HIS A 273     5228   8865   4956  -1142   2516  -1042       N  
ATOM   2093  CD2 HIS A 273      58.410   1.044 -16.231  1.00 56.45           C  
ANISOU 2093  CD2 HIS A 273     5365  10425   5660   -964   2898  -1297       C  
ATOM   2094  CE1 HIS A 273      56.384   0.804 -17.030  1.00 52.92           C  
ANISOU 2094  CE1 HIS A 273     5631   9362   5115  -1062   2715  -1290       C  
ATOM   2095  NE2 HIS A 273      57.658   0.553 -17.268  1.00 56.72           N  
ANISOU 2095  NE2 HIS A 273     5731  10284   5535   -944   2961  -1447       N  
ATOM   2096  N   PHE A 274      58.466   2.858 -11.096  1.00 61.20           N  
ANISOU 2096  N   PHE A 274     5548  10733   6971  -1041   2030   -619       N  
ATOM   2097  CA  PHE A 274      59.329   3.583 -10.161  1.00 66.70           C  
ANISOU 2097  CA  PHE A 274     5855  11805   7682  -1208   1947   -592       C  
ATOM   2098  C   PHE A 274      58.794   3.604  -8.738  1.00 63.40           C  
ANISOU 2098  C   PHE A 274     5523  11139   7430  -1042   1658   -452       C  
ATOM   2099  O   PHE A 274      59.137   4.494  -7.957  1.00 63.62           O  
ANISOU 2099  O   PHE A 274     5377  11355   7442  -1314   1540   -420       O  
ATOM   2100  CB  PHE A 274      59.525   5.015 -10.656  1.00 72.28           C  
ANISOU 2100  CB  PHE A 274     6598  12640   8226  -1868   2041   -537       C  
ATOM   2101  CG  PHE A 274      59.990   5.100 -12.086  1.00 78.73           C  
ANISOU 2101  CG  PHE A 274     7377  13711   8826  -2082   2349   -628       C  
ATOM   2102  CD1 PHE A 274      61.139   4.435 -12.495  1.00 83.08           C  
ANISOU 2102  CD1 PHE A 274     7453  14802   9312  -1876   2565   -841       C  
ATOM   2103  CD2 PHE A 274      59.281   5.839 -13.021  1.00 78.82           C  
ANISOU 2103  CD2 PHE A 274     7821  13456   8672  -2452   2429   -490       C  
ATOM   2104  CE1 PHE A 274      61.576   4.505 -13.812  1.00 86.43           C  
ANISOU 2104  CE1 PHE A 274     7833  15503   9504  -2072   2876   -936       C  
ATOM   2105  CE2 PHE A 274      59.714   5.918 -14.342  1.00 82.39           C  
ANISOU 2105  CE2 PHE A 274     8252  14182   8869  -2643   2725   -552       C  
ATOM   2106  CZ  PHE A 274      60.864   5.250 -14.736  1.00 85.69           C  
ANISOU 2106  CZ  PHE A 274     8193  15145   9219  -2471   2958   -785       C  
ATOM   2107  N   GLY A 275      57.985   2.603  -8.399  1.00 62.13           N  
ANISOU 2107  N   GLY A 275     5622  10569   7415   -612   1566   -390       N  
ATOM   2108  CA  GLY A 275      57.288   2.563  -7.123  1.00 62.65           C  
ANISOU 2108  CA  GLY A 275     5844  10347   7613   -453   1322   -228       C  
ATOM   2109  C   GLY A 275      58.180   2.279  -5.929  1.00 68.50           C  
ANISOU 2109  C   GLY A 275     6172  11478   8376   -135   1204   -221       C  
ATOM   2110  O   GLY A 275      58.884   3.174  -5.452  1.00 72.28           O  
ANISOU 2110  O   GLY A 275     6337  12368   8760   -417   1131   -267       O  
ATOM   2111  N   LYS A 276      58.135   1.037  -5.442  1.00 70.78           N  
ANISOU 2111  N   LYS A 276     6477  11636   8780    446   1188   -163       N  
ATOM   2112  CA  LYS A 276      58.851   0.625  -4.230  1.00 74.32           C  
ANISOU 2112  CA  LYS A 276     6586  12429   9222    872   1048    -94       C  
ATOM   2113  C   LYS A 276      59.832  -0.487  -4.577  1.00 79.75           C  
ANISOU 2113  C   LYS A 276     6968  13405   9929   1419   1208   -192       C  
ATOM   2114  O   LYS A 276      59.432  -1.513  -5.134  1.00 82.60           O  
ANISOU 2114  O   LYS A 276     7615  13353  10418   1736   1364   -201       O  
ATOM   2115  CB  LYS A 276      57.862   0.122  -3.176  1.00 71.42           C  
ANISOU 2115  CB  LYS A 276     6570  11603   8962   1156    893    142       C  
ATOM   2116  CG  LYS A 276      58.459  -0.092  -1.784  1.00 75.04           C  
ANISOU 2116  CG  LYS A 276     6733  12436   9342   1548    702    268       C  
ATOM   2117  CD  LYS A 276      58.579   1.221  -1.007  1.00 75.47           C  
ANISOU 2117  CD  LYS A 276     6604  12828   9245   1108    491    233       C  
ATOM   2118  CE  LYS A 276      58.877   0.991   0.481  1.00 77.29           C  
ANISOU 2118  CE  LYS A 276     6636  13377   9355   1496    265    375       C  
ATOM   2119  NZ  LYS A 276      58.490   2.177   1.314  1.00 74.61           N  
ANISOU 2119  NZ  LYS A 276     6336  13115   8899   1057     65    349       N  
ATOM   2120  N   ASP A 277      61.109  -0.285  -4.247  1.00 80.72           N  
ANISOU 2120  N   ASP A 277     6501  14243   9926   1530   1174   -292       N  
ATOM   2121  CA  ASP A 277      62.160  -1.238  -4.592  1.00 84.52           C  
ANISOU 2121  CA  ASP A 277     6604  15107  10403   2081   1330   -407       C  
ATOM   2122  C   ASP A 277      62.230  -1.457  -6.106  1.00 85.32           C  
ANISOU 2122  C   ASP A 277     6799  15103  10518   1933   1636   -616       C  
ATOM   2123  O   ASP A 277      62.820  -2.436  -6.568  1.00 90.03           O  
ANISOU 2123  O   ASP A 277     7247  15809  11153   2440   1821   -728       O  
ATOM   2124  CB  ASP A 277      61.933  -2.595  -3.892  1.00 85.71           C  
ANISOU 2124  CB  ASP A 277     6962  14916  10687   2870   1299   -208       C  
ATOM   2125  CG  ASP A 277      61.993  -2.504  -2.375  1.00 84.68           C  
ANISOU 2125  CG  ASP A 277     6701  14993  10479   3124   1009     20       C  
ATOM   2126  OD1 ASP A 277      60.935  -2.633  -1.726  1.00 78.56           O  
ANISOU 2126  OD1 ASP A 277     6394  13672   9783   3127    905    245       O  
ATOM   2127  OD2 ASP A 277      63.103  -2.329  -1.832  1.00 89.70           O  
ANISOU 2127  OD2 ASP A 277     6743  16384  10953   3330    890    -35       O  
ATOM   2128  N   LYS A 278      61.650  -0.543  -6.882  1.00 82.43           N  
ANISOU 2128  N   LYS A 278     6681  14544  10096   1273   1696   -668       N  
ATOM   2129  CA  LYS A 278      61.415  -0.812  -8.297  1.00 82.16           C  
ANISOU 2129  CA  LYS A 278     6873  14304  10041   1144   1960   -825       C  
ATOM   2130  C   LYS A 278      62.599  -0.451  -9.180  1.00 85.60           C  
ANISOU 2130  C   LYS A 278     6821  15405  10300    954   2191  -1052       C  
ATOM   2131  O   LYS A 278      63.169  -1.330  -9.826  1.00 86.04           O  
ANISOU 2131  O   LYS A 278     6718  15623  10352   1356   2410  -1228       O  
ATOM   2132  CB  LYS A 278      60.134  -0.133  -8.787  1.00 78.07           C  
ANISOU 2132  CB  LYS A 278     6895  13254   9513    619   1918   -741       C  
ATOM   2133  CG  LYS A 278      58.867  -0.951  -8.538  1.00 76.89           C  
ANISOU 2133  CG  LYS A 278     7277  12391   9546    872   1840   -628       C  
ATOM   2134  CD  LYS A 278      58.891  -2.302  -9.257  1.00 80.29           C  
ANISOU 2134  CD  LYS A 278     7847  12591  10069   1321   2059   -798       C  
ATOM   2135  CE  LYS A 278      57.710  -3.176  -8.859  1.00 79.75           C  
ANISOU 2135  CE  LYS A 278     8273  11813  10215   1547   2000   -695       C  
ATOM   2136  NZ  LYS A 278      57.985  -4.608  -9.190  1.00 85.21           N  
ANISOU 2136  NZ  LYS A 278     9055  12273  11048   2099   2215   -850       N  
ATOM   2137  N   SER A 279      62.959   0.831  -9.215  1.00 87.06           N  
ANISOU 2137  N   SER A 279     6783  15951  10344    336   2170  -1059       N  
ATOM   2138  CA  SER A 279      64.104   1.286 -10.009  1.00 93.54           C  
ANISOU 2138  CA  SER A 279     7111  17444  10987     53   2419  -1260       C  
ATOM   2139  C   SER A 279      65.055   2.145  -9.191  1.00 97.19           C  
ANISOU 2139  C   SER A 279     6997  18549  11383   -238   2305  -1299       C  
ATOM   2140  O   SER A 279      64.657   2.797  -8.227  1.00 96.78           O  
ANISOU 2140  O   SER A 279     7051  18345  11375   -465   2050  -1172       O  
ATOM   2141  CB  SER A 279      63.647   2.085 -11.228  1.00 92.84           C  
ANISOU 2141  CB  SER A 279     7356  17171  10748   -566   2616  -1263       C  
ATOM   2142  OG  SER A 279      63.874   3.473 -11.036  1.00 93.31           O  
ANISOU 2142  OG  SER A 279     7306  17431  10717  -1250   2587  -1200       O  
ATOM   2143  N   LYS A 280      66.310   2.170  -9.623  1.00102.47           N  
ANISOU 2143  N   LYS A 280     7041  19965  11928   -269   2514  -1511       N  
ATOM   2144  CA  LYS A 280      67.358   2.922  -8.941  1.00106.39           C  
ANISOU 2144  CA  LYS A 280     6874  21205  12344   -576   2437  -1625       C  
ATOM   2145  C   LYS A 280      67.654   4.208  -9.714  1.00105.41           C  
ANISOU 2145  C   LYS A 280     6693  21278  12082  -1482   2670  -1699       C  
ATOM   2146  O   LYS A 280      68.740   4.775  -9.604  1.00108.82           O  
ANISOU 2146  O   LYS A 280     6489  22441  12417  -1837   2760  -1881       O  
ATOM   2147  CB  LYS A 280      68.604   2.041  -8.794  1.00114.05           C  
ANISOU 2147  CB  LYS A 280     7102  22958  13273     45   2504  -1817       C  
ATOM   2148  CG  LYS A 280      68.230   0.591  -8.477  1.00115.07           C  
ANISOU 2148  CG  LYS A 280     7464  22714  13541   1002   2412  -1716       C  
ATOM   2149  CD  LYS A 280      69.359  -0.250  -7.893  1.00122.20           C  
ANISOU 2149  CD  LYS A 280     7671  24336  14422   1759   2359  -1820       C  
ATOM   2150  CE  LYS A 280      68.775  -1.434  -7.103  1.00121.28           C  
ANISOU 2150  CE  LYS A 280     7928  23687  14465   2622   2164  -1597       C  
ATOM   2151  NZ  LYS A 280      69.311  -2.753  -7.537  1.00125.15           N  
ANISOU 2151  NZ  LYS A 280     8271  24269  15012   3486   2367  -1689       N  
ATOM   2152  N   GLU A 281      66.671   4.654 -10.496  1.00 99.38           N  
ANISOU 2152  N   GLU A 281     6598  19864  11299  -1851   2773  -1548       N  
ATOM   2153  CA  GLU A 281      66.756   5.901 -11.232  1.00 97.86           C  
ANISOU 2153  CA  GLU A 281     6523  19686  10972  -2687   2998  -1526       C  
ATOM   2154  C   GLU A 281      65.835   6.908 -10.575  1.00 90.83           C  
ANISOU 2154  C   GLU A 281     6135  18208  10168  -3123   2770  -1331       C  
ATOM   2155  O   GLU A 281      66.285   7.940 -10.092  1.00 92.86           O  
ANISOU 2155  O   GLU A 281     6187  18678  10417  -3692   2753  -1387       O  
ATOM   2156  CB  GLU A 281      66.342   5.690 -12.688  1.00 98.77           C  
ANISOU 2156  CB  GLU A 281     7035  19548  10944  -2735   3297  -1477       C  
ATOM   2157  CG  GLU A 281      66.337   6.962 -13.525  1.00 99.85           C  
ANISOU 2157  CG  GLU A 281     7400  19631  10906  -3558   3554  -1374       C  
ATOM   2158  CD  GLU A 281      67.733   7.475 -13.821  1.00104.72           C  
ANISOU 2158  CD  GLU A 281     7341  21057  11391  -4019   3861  -1568       C  
ATOM   2159  OE1 GLU A 281      68.482   6.764 -14.520  1.00106.74           O  
ANISOU 2159  OE1 GLU A 281     7187  21846  11522  -3746   4116  -1751       O  
ATOM   2160  OE2 GLU A 281      68.075   8.588 -13.362  1.00105.49           O  
ANISOU 2160  OE2 GLU A 281     7314  21256  11510  -4671   3865  -1560       O  
ATOM   2161  N   PHE A 282      64.543   6.599 -10.559  1.00 83.70           N  
ANISOU 2161  N   PHE A 282     5880  16572   9351  -2858   2607  -1132       N  
ATOM   2162  CA  PHE A 282      63.552   7.492  -9.972  1.00 79.48           C  
ANISOU 2162  CA  PHE A 282     5853  15447   8898  -3181   2397   -944       C  
ATOM   2163  C   PHE A 282      62.724   6.809  -8.890  1.00 74.60           C  
ANISOU 2163  C   PHE A 282     5443  14454   8447  -2639   2056   -851       C  
ATOM   2164  O   PHE A 282      62.355   5.639  -9.002  1.00 70.36           O  
ANISOU 2164  O   PHE A 282     5005  13756   7971  -2050   2020   -829       O  
ATOM   2165  CB  PHE A 282      62.631   8.062 -11.043  1.00 77.31           C  
ANISOU 2165  CB  PHE A 282     6214  14631   8529  -3503   2543   -748       C  
ATOM   2166  CG  PHE A 282      61.660   9.074 -10.515  1.00 73.87           C  
ANISOU 2166  CG  PHE A 282     6289  13609   8170  -3821   2362   -557       C  
ATOM   2167  CD1 PHE A 282      62.108  10.293 -10.040  1.00 76.77           C  
ANISOU 2167  CD1 PHE A 282     6574  14047   8548  -4416   2388   -588       C  
ATOM   2168  CD2 PHE A 282      60.306   8.810 -10.483  1.00 68.94           C  
ANISOU 2168  CD2 PHE A 282     6211  12370   7611  -3533   2179   -376       C  
ATOM   2169  CE1 PHE A 282      61.223  11.231  -9.551  1.00 72.98           C  
ANISOU 2169  CE1 PHE A 282     6590  12993   8147  -4670   2244   -436       C  
ATOM   2170  CE2 PHE A 282      59.420   9.747  -9.995  1.00 66.39           C  
ANISOU 2170  CE2 PHE A 282     6328  11541   7355  -3774   2025   -212       C  
ATOM   2171  CZ  PHE A 282      59.880  10.957  -9.529  1.00 67.62           C  
ANISOU 2171  CZ  PHE A 282     6437  11731   7525  -4317   2061   -240       C  
ATOM   2172  N   GLN A 283      62.432   7.575  -7.849  1.00 75.57           N  
ANISOU 2172  N   GLN A 283     5654  14421   8638  -2874   1834   -806       N  
ATOM   2173  CA  GLN A 283      61.819   7.064  -6.642  1.00 76.16           C  
ANISOU 2173  CA  GLN A 283     5835  14270   8831  -2425   1521   -728       C  
ATOM   2174  C   GLN A 283      60.535   7.858  -6.396  1.00 74.70           C  
ANISOU 2174  C   GLN A 283     6272  13401   8708  -2682   1393   -549       C  
ATOM   2175  O   GLN A 283      60.577   9.040  -6.046  1.00 76.61           O  
ANISOU 2175  O   GLN A 283     6584  13588   8935  -3196   1368   -578       O  
ATOM   2176  CB  GLN A 283      62.790   7.211  -5.463  1.00 82.01           C  
ANISOU 2176  CB  GLN A 283     5996  15621   9544  -2409   1351   -893       C  
ATOM   2177  CG  GLN A 283      64.271   6.904  -5.783  1.00 90.34           C  
ANISOU 2177  CG  GLN A 283     6317  17511  10499  -2377   1512  -1120       C  
ATOM   2178  CD  GLN A 283      64.496   5.493  -6.315  1.00 93.02           C  
ANISOU 2178  CD  GLN A 283     6517  17973  10854  -1676   1617  -1111       C  
ATOM   2179  OE1 GLN A 283      63.746   4.570  -5.990  1.00 91.49           O  
ANISOU 2179  OE1 GLN A 283     6641  17361  10761  -1108   1489   -959       O  
ATOM   2180  NE2 GLN A 283      65.537   5.321  -7.134  1.00 96.34           N  
ANISOU 2180  NE2 GLN A 283     6468  18957  11179  -1725   1877  -1288       N  
ATOM   2181  N   LEU A 284      59.396   7.204  -6.598  1.00 71.12           N  
ANISOU 2181  N   LEU A 284     6262  12429   8329  -2325   1329   -387       N  
ATOM   2182  CA  LEU A 284      58.098   7.864  -6.536  1.00 68.12           C  
ANISOU 2182  CA  LEU A 284     6452  11433   7997  -2499   1228   -214       C  
ATOM   2183  C   LEU A 284      57.682   8.253  -5.113  1.00 67.12           C  
ANISOU 2183  C   LEU A 284     6383  11173   7945  -2464    971   -188       C  
ATOM   2184  O   LEU A 284      56.881   9.171  -4.931  1.00 66.98           O  
ANISOU 2184  O   LEU A 284     6747  10753   7951  -2730    908   -102       O  
ATOM   2185  CB  LEU A 284      57.042   6.948  -7.158  1.00 67.68           C  
ANISOU 2185  CB  LEU A 284     6761  10967   7989  -2129   1232    -98       C  
ATOM   2186  CG  LEU A 284      55.589   7.422  -7.271  1.00 66.01           C  
ANISOU 2186  CG  LEU A 284     7096  10174   7811  -2212   1131     77       C  
ATOM   2187  CD1 LEU A 284      55.486   8.838  -7.845  1.00 67.01           C  
ANISOU 2187  CD1 LEU A 284     7469  10157   7834  -2741   1223    154       C  
ATOM   2188  CD2 LEU A 284      54.801   6.422  -8.125  1.00 64.43           C  
ANISOU 2188  CD2 LEU A 284     7125   9735   7619  -1914   1179    107       C  
ATOM   2189  N   PHE A 285      58.221   7.559  -4.113  1.00 66.36           N  
ANISOU 2189  N   PHE A 285     5919  11431   7864  -2102    828   -257       N  
ATOM   2190  CA  PHE A 285      57.896   7.832  -2.716  1.00 62.51           C  
ANISOU 2190  CA  PHE A 285     5450  10911   7391  -2026    584   -244       C  
ATOM   2191  C   PHE A 285      59.110   8.286  -1.915  1.00 66.37           C  
ANISOU 2191  C   PHE A 285     5407  12036   7775  -2214    500   -459       C  
ATOM   2192  O   PHE A 285      59.121   8.184  -0.696  1.00 65.90           O  
ANISOU 2192  O   PHE A 285     5217  12155   7669  -2009    283   -480       O  
ATOM   2193  CB  PHE A 285      57.286   6.584  -2.082  1.00 60.73           C  
ANISOU 2193  CB  PHE A 285     5318  10524   7233  -1393    458    -92       C  
ATOM   2194  CG  PHE A 285      56.118   6.027  -2.853  1.00 54.31           C  
ANISOU 2194  CG  PHE A 285     4964   9144   6529  -1233    540     64       C  
ATOM   2195  CD1 PHE A 285      55.046   6.841  -3.192  1.00 49.85           C  
ANISOU 2195  CD1 PHE A 285     4834   8115   5991  -1533    535    144       C  
ATOM   2196  CD2 PHE A 285      56.089   4.695  -3.237  1.00 52.81           C  
ANISOU 2196  CD2 PHE A 285     4763   8894   6409   -777    623    110       C  
ATOM   2197  CE1 PHE A 285      53.966   6.338  -3.905  1.00 46.74           C  
ANISOU 2197  CE1 PHE A 285     4799   7292   5669  -1398    585    256       C  
ATOM   2198  CE2 PHE A 285      55.012   4.186  -3.948  1.00 49.15           C  
ANISOU 2198  CE2 PHE A 285     4696   7942   6038   -693    695    194       C  
ATOM   2199  CZ  PHE A 285      53.950   5.010  -4.284  1.00 44.75           C  
ANISOU 2199  CZ  PHE A 285     4511   7011   5483  -1013    663    262       C  
ATOM   2200  N   SER A 286      60.127   8.784  -2.617  1.00 72.64           N  
ANISOU 2200  N   SER A 286     5879  13213   8508  -2620    679   -627       N  
ATOM   2201  CA  SER A 286      61.340   9.338  -2.009  1.00 77.93           C  
ANISOU 2201  CA  SER A 286     5985  14551   9074  -2931    630   -890       C  
ATOM   2202  C   SER A 286      61.698  10.626  -2.768  1.00 81.93           C  
ANISOU 2202  C   SER A 286     6561  14995   9572  -3725    859  -1012       C  
ATOM   2203  O   SER A 286      60.899  11.086  -3.582  1.00 79.85           O  
ANISOU 2203  O   SER A 286     6835  14138   9367  -3937   1005   -846       O  
ATOM   2204  CB  SER A 286      62.469   8.313  -2.075  1.00 80.40           C  
ANISOU 2204  CB  SER A 286     5662  15572   9315  -2508    652   -984       C  
ATOM   2205  OG  SER A 286      63.516   8.661  -1.197  1.00 88.14           O  
ANISOU 2205  OG  SER A 286     6039  17280  10168  -2660    509  -1233       O  
ATOM   2206  N   SER A 287      62.868  11.213  -2.512  1.00 89.64           N  
ANISOU 2206  N   SER A 287     7011  16578  10469  -4168    899  -1290       N  
ATOM   2207  CA  SER A 287      63.232  12.496  -3.144  1.00 94.60           C  
ANISOU 2207  CA  SER A 287     7737  17104  11104  -5000   1152  -1406       C  
ATOM   2208  C   SER A 287      64.641  12.996  -2.792  1.00102.00           C  
ANISOU 2208  C   SER A 287     7964  18836  11954  -5502   1198  -1771       C  
ATOM   2209  O   SER A 287      65.305  12.445  -1.910  1.00104.85           O  
ANISOU 2209  O   SER A 287     7740  19873  12225  -5189    973  -1953       O  
ATOM   2210  CB  SER A 287      62.210  13.576  -2.744  1.00 93.34           C  
ANISOU 2210  CB  SER A 287     8233  16204  11029  -5337   1091  -1338       C  
ATOM   2211  OG  SER A 287      62.636  14.881  -3.095  1.00 97.84           O  
ANISOU 2211  OG  SER A 287     8905  16651  11617  -6157   1320  -1477       O  
ATOM   2212  N   PRO A 288      65.111  14.028  -3.513  1.00105.74           N  
ANISOU 2212  N   PRO A 288     8478  19260  12439  -6284   1503  -1869       N  
ATOM   2213  CA  PRO A 288      66.206  14.877  -3.048  1.00112.43           C  
ANISOU 2213  CA  PRO A 288     8807  20670  13243  -6991   1556  -2254       C  
ATOM   2214  C   PRO A 288      65.730  16.161  -2.359  1.00113.08           C  
ANISOU 2214  C   PRO A 288     9345  20216  13406  -7583   1502  -2385       C  
ATOM   2215  O   PRO A 288      66.356  16.596  -1.395  1.00118.62           O  
ANISOU 2215  O   PRO A 288     9628  21385  14057  -7915   1348  -2754       O  
ATOM   2216  CB  PRO A 288      66.946  15.224  -4.340  1.00117.38           C  
ANISOU 2216  CB  PRO A 288     9279  21474  13846  -7529   1992  -2254       C  
ATOM   2217  CG  PRO A 288      65.886  15.221  -5.383  1.00112.66           C  
ANISOU 2217  CG  PRO A 288     9465  20046  13296  -7372   2170  -1847       C  
ATOM   2218  CD  PRO A 288      64.880  14.181  -4.963  1.00105.43           C  
ANISOU 2218  CD  PRO A 288     8814  18835  12410  -6479   1856  -1633       C  
ATOM   2219  N   HIS A 289      64.639  16.755  -2.844  1.00109.39           N  
ANISOU 2219  N   HIS A 289     9714  18802  13048  -7690   1623  -2106       N  
ATOM   2220  CA  HIS A 289      64.203  18.083  -2.387  1.00112.25           C  
ANISOU 2220  CA  HIS A 289    10591  18549  13511  -8285   1659  -2218       C  
ATOM   2221  C   HIS A 289      63.169  18.044  -1.258  1.00107.80           C  
ANISOU 2221  C   HIS A 289    10389  17593  12977  -7843   1313  -2204       C  
ATOM   2222  O   HIS A 289      62.067  18.548  -1.419  1.00105.36           O  
ANISOU 2222  O   HIS A 289    10811  16454  12768  -7789   1348  -1977       O  
ATOM   2223  CB  HIS A 289      63.650  18.901  -3.572  1.00113.27           C  
ANISOU 2223  CB  HIS A 289    11447  17865  13727  -8670   2021  -1909       C  
ATOM   2224  CG  HIS A 289      64.679  19.745  -4.258  1.00121.38           C  
ANISOU 2224  CG  HIS A 289    12294  19071  14753  -9553   2418  -2056       C  
ATOM   2225  ND1 HIS A 289      65.244  19.397  -5.467  1.00123.76           N  
ANISOU 2225  ND1 HIS A 289    12386  19672  14967  -9644   2726  -1894       N  
ATOM   2226  CD2 HIS A 289      65.243  20.925  -3.904  1.00128.02           C  
ANISOU 2226  CD2 HIS A 289    13144  19829  15670 -10419   2585  -2366       C  
ATOM   2227  CE1 HIS A 289      66.115  20.324  -5.826  1.00131.50           C  
ANISOU 2227  CE1 HIS A 289    13237  20765  15962 -10533   3077  -2068       C  
ATOM   2228  NE2 HIS A 289      66.132  21.263  -4.895  1.00134.13           N  
ANISOU 2228  NE2 HIS A 289    13706  20848  16409 -11037   3001  -2360       N  
ATOM   2229  N   GLY A 290      63.526  17.467  -0.112  1.00108.74           N  
ANISOU 2229  N   GLY A 290     9989  18340  12986  -7515    988  -2441       N  
ATOM   2230  CA  GLY A 290      62.608  17.413   1.038  1.00106.91           C  
ANISOU 2230  CA  GLY A 290    10055  17829  12738  -7109    674  -2445       C  
ATOM   2231  C   GLY A 290      61.585  16.291   0.925  1.00100.81           C  
ANISOU 2231  C   GLY A 290     9552  16778  11974  -6239    533  -2041       C  
ATOM   2232  O   GLY A 290      61.502  15.625  -0.116  1.00 99.46           O  
ANISOU 2232  O   GLY A 290     9417  16534  11838  -5975    682  -1768       O  
ATOM   2233  N   LYS A 291      60.790  16.092   1.981  1.00 96.21           N  
ANISOU 2233  N   LYS A 291     9168  16036  11351  -5825    265  -2022       N  
ATOM   2234  CA  LYS A 291      59.986  14.858   2.129  1.00 88.98           C  
ANISOU 2234  CA  LYS A 291     8356  15033  10419  -4998    104  -1694       C  
ATOM   2235  C   LYS A 291      58.469  14.998   1.928  1.00 79.89           C  
ANISOU 2235  C   LYS A 291     7935  13029   9392  -4754    124  -1401       C  
ATOM   2236  O   LYS A 291      57.919  16.099   1.900  1.00 77.64           O  
ANISOU 2236  O   LYS A 291     8120  12189   9190  -5128    211  -1448       O  
ATOM   2237  CB  LYS A 291      60.293  14.195   3.479  1.00 90.89           C  
ANISOU 2237  CB  LYS A 291     8163  15898  10472  -4572   -213  -1827       C  
ATOM   2238  CG  LYS A 291      61.765  13.767   3.657  1.00 97.19           C  
ANISOU 2238  CG  LYS A 291     8145  17670  11114  -4605   -281  -2064       C  
ATOM   2239  CD  LYS A 291      62.206  12.582   2.763  1.00 96.88           C  
ANISOU 2239  CD  LYS A 291     7807  17902  11102  -4145   -174  -1835       C  
ATOM   2240  CE  LYS A 291      62.519  12.980   1.308  1.00 98.11           C  
ANISOU 2240  CE  LYS A 291     8045  17841  11392  -4605    174  -1804       C  
ATOM   2241  NZ  LYS A 291      63.352  11.979   0.580  1.00 99.10           N  
ANISOU 2241  NZ  LYS A 291     7677  18493  11485  -4274    282  -1747       N  
ATOM   2242  N   ASP A 292      57.816  13.848   1.769  1.00 73.93           N  
ANISOU 2242  N   ASP A 292     7254  12184   8652  -4113     54  -1106       N  
ATOM   2243  CA  ASP A 292      56.393  13.769   1.431  1.00 69.60           C  
ANISOU 2243  CA  ASP A 292     7293  10937   8214  -3838     77   -818       C  
ATOM   2244  C   ASP A 292      56.015  14.694   0.269  1.00 68.21           C  
ANISOU 2244  C   ASP A 292     7568  10204   8146  -4242    313   -716       C  
ATOM   2245  O   ASP A 292      54.968  15.346   0.292  1.00 65.17           O  
ANISOU 2245  O   ASP A 292     7693   9237   7832  -4251    319   -614       O  
ATOM   2246  CB  ASP A 292      55.520  14.067   2.655  1.00 70.40           C  
ANISOU 2246  CB  ASP A 292     7643  10822   8284  -3665   -109   -860       C  
ATOM   2247  CG  ASP A 292      55.603  12.985   3.720  1.00 71.60           C  
ANISOU 2247  CG  ASP A 292     7472  11432   8303  -3136   -328   -830       C  
ATOM   2248  OD1 ASP A 292      56.164  11.900   3.465  1.00 72.52           O  
ANISOU 2248  OD1 ASP A 292     7244  11924   8388  -2808   -336   -725       O  
ATOM   2249  OD2 ASP A 292      55.088  13.223   4.827  1.00 74.35           O  
ANISOU 2249  OD2 ASP A 292     7937  11750   8564  -3023   -477   -902       O  
ATOM   2250  N   LEU A 293      56.876  14.745  -0.745  1.00 68.18           N  
ANISOU 2250  N   LEU A 293     7368  10404   8134  -4544    517   -728       N  
ATOM   2251  CA  LEU A 293      56.580  15.503  -1.951  1.00 66.77           C  
ANISOU 2251  CA  LEU A 293     7615   9747   8007  -4882    763   -567       C  
ATOM   2252  C   LEU A 293      55.657  14.673  -2.837  1.00 60.89           C  
ANISOU 2252  C   LEU A 293     7123   8738   7276  -4414    778   -254       C  
ATOM   2253  O   LEU A 293      56.025  13.575  -3.243  1.00 59.63           O  
ANISOU 2253  O   LEU A 293     6649   8930   7076  -4117    787   -217       O  
ATOM   2254  CB  LEU A 293      57.863  15.844  -2.707  1.00 73.35           C  
ANISOU 2254  CB  LEU A 293     8128  10950   8793  -5405   1007   -694       C  
ATOM   2255  CG  LEU A 293      58.866  16.796  -2.046  1.00 80.39           C  
ANISOU 2255  CG  LEU A 293     8752  12115   9677  -6034   1051  -1047       C  
ATOM   2256  CD1 LEU A 293      59.964  17.112  -3.045  1.00 86.01           C  
ANISOU 2256  CD1 LEU A 293     9208  13123  10350  -6570   1360  -1105       C  
ATOM   2257  CD2 LEU A 293      58.218  18.083  -1.535  1.00 81.40           C  
ANISOU 2257  CD2 LEU A 293     9425  11609   9894  -6377   1059  -1115       C  
ATOM   2258  N   LEU A 294      54.459  15.200  -3.103  1.00 57.10           N  
ANISOU 2258  N   LEU A 294     7196   7655   6846  -4337    776    -57       N  
ATOM   2259  CA  LEU A 294      53.397  14.537  -3.888  1.00 51.65           C  
ANISOU 2259  CA  LEU A 294     6769   6702   6153  -3923    758    210       C  
ATOM   2260  C   LEU A 294      52.697  13.391  -3.177  1.00 47.30           C  
ANISOU 2260  C   LEU A 294     6102   6227   5644  -3373    548    240       C  
ATOM   2261  O   LEU A 294      51.481  13.255  -3.293  1.00 44.07           O  
ANISOU 2261  O   LEU A 294     6002   5472   5271  -3100    475    401       O  
ATOM   2262  CB  LEU A 294      53.892  14.026  -5.243  1.00 52.39           C  
ANISOU 2262  CB  LEU A 294     6751   6999   6156  -3966    945    305       C  
ATOM   2263  CG  LEU A 294      54.501  15.030  -6.216  1.00 56.07           C  
ANISOU 2263  CG  LEU A 294     7376   7385   6542  -4493   1214    358       C  
ATOM   2264  CD1 LEU A 294      54.737  14.320  -7.545  1.00 53.89           C  
ANISOU 2264  CD1 LEU A 294     7014   7330   6133  -4400   1374    471       C  
ATOM   2265  CD2 LEU A 294      53.611  16.262  -6.390  1.00 55.81           C  
ANISOU 2265  CD2 LEU A 294     7951   6722   6532  -4652   1253    542       C  
ATOM   2266  N   PHE A 295      53.460  12.551  -2.483  1.00 45.85           N  
ANISOU 2266  N   PHE A 295     5468   6508   5446  -3204    466    101       N  
ATOM   2267  CA  PHE A 295      52.906  11.391  -1.797  1.00 45.92           C  
ANISOU 2267  CA  PHE A 295     5381   6578   5488  -2689    309    164       C  
ATOM   2268  C   PHE A 295      53.676  11.164  -0.515  1.00 51.56           C  
ANISOU 2268  C   PHE A 295     5716   7726   6150  -2607    171     -1       C  
ATOM   2269  O   PHE A 295      54.778  11.694  -0.361  1.00 60.80           O  
ANISOU 2269  O   PHE A 295     6594   9252   7255  -2937    202   -197       O  
ATOM   2270  CB  PHE A 295      53.006  10.150  -2.691  1.00 44.70           C  
ANISOU 2270  CB  PHE A 295     5098   6543   5343  -2400    392    251       C  
ATOM   2271  CG  PHE A 295      52.456  10.357  -4.076  1.00 42.86           C  
ANISOU 2271  CG  PHE A 295     5167   6027   5092  -2515    529    373       C  
ATOM   2272  CD1 PHE A 295      51.088  10.367  -4.302  1.00 40.93           C  
ANISOU 2272  CD1 PHE A 295     5290   5377   4887  -2354    465    522       C  
ATOM   2273  CD2 PHE A 295      53.301  10.562  -5.149  1.00 44.62           C  
ANISOU 2273  CD2 PHE A 295     5282   6443   5227  -2782    720    337       C  
ATOM   2274  CE1 PHE A 295      50.578  10.566  -5.581  1.00 39.49           C  
ANISOU 2274  CE1 PHE A 295     5361   5010   4636  -2430    560    636       C  
ATOM   2275  CE2 PHE A 295      52.790  10.762  -6.433  1.00 45.13           C  
ANISOU 2275  CE2 PHE A 295     5639   6292   5215  -2869    841    468       C  
ATOM   2276  CZ  PHE A 295      51.435  10.767  -6.644  1.00 39.99           C  
ANISOU 2276  CZ  PHE A 295     5352   5261   4583  -2681    745    618       C  
ATOM   2277  N   LYS A 296      53.107  10.386   0.405  1.00 48.88           N  
ANISOU 2277  N   LYS A 296     5367   7391   5815  -2183     24     76       N  
ATOM   2278  CA  LYS A 296      53.822  10.032   1.634  1.00 52.53           C  
ANISOU 2278  CA  LYS A 296     5464   8325   6169  -2011   -125    -35       C  
ATOM   2279  C   LYS A 296      54.984   9.085   1.302  1.00 53.95           C  
ANISOU 2279  C   LYS A 296     5191   8999   6308  -1816    -82    -63       C  
ATOM   2280  O   LYS A 296      54.900   8.292   0.364  1.00 50.77           O  
ANISOU 2280  O   LYS A 296     4826   8481   5984  -1627     43     52       O  
ATOM   2281  CB  LYS A 296      52.887   9.402   2.682  1.00 52.08           C  
ANISOU 2281  CB  LYS A 296     5552   8140   6098  -1586   -258    110       C  
ATOM   2282  CG  LYS A 296      52.255  10.387   3.678  1.00 52.95           C  
ANISOU 2282  CG  LYS A 296     5875   8098   6146  -1736   -364     14       C  
ATOM   2283  CD  LYS A 296      50.904  10.911   3.206  1.00 52.44           C  
ANISOU 2283  CD  LYS A 296     6280   7439   6206  -1794   -297    126       C  
ATOM   2284  CE  LYS A 296      50.097  11.593   4.332  1.00 52.43           C  
ANISOU 2284  CE  LYS A 296     6490   7288   6145  -1771   -393     59       C  
ATOM   2285  NZ  LYS A 296      50.464  13.025   4.561  1.00 51.88           N  
ANISOU 2285  NZ  LYS A 296     6519   7155   6038  -2208   -392   -203       N  
ATOM   2286  N   ASP A 297      56.067   9.179   2.069  1.00 58.97           N  
ANISOU 2286  N   ASP A 297     5385  10212   6807  -1849   -188   -241       N  
ATOM   2287  CA  ASP A 297      57.261   8.364   1.813  1.00 63.60           C  
ANISOU 2287  CA  ASP A 297     5472  11355   7337  -1630   -157   -292       C  
ATOM   2288  C   ASP A 297      57.130   6.944   2.367  1.00 63.21           C  
ANISOU 2288  C   ASP A 297     5348  11398   7272   -934   -239    -85       C  
ATOM   2289  O   ASP A 297      57.927   6.067   2.031  1.00 66.79           O  
ANISOU 2289  O   ASP A 297     5480  12182   7717   -613   -183    -71       O  
ATOM   2290  CB  ASP A 297      58.520   9.039   2.378  1.00 69.96           C  
ANISOU 2290  CB  ASP A 297     5763  12833   7984  -1948   -246   -587       C  
ATOM   2291  CG  ASP A 297      58.760  10.430   1.794  1.00 72.48           C  
ANISOU 2291  CG  ASP A 297     6172  13026   8342  -2697   -109   -797       C  
ATOM   2292  OD1 ASP A 297      58.395  10.678   0.624  1.00 72.54           O  
ANISOU 2292  OD1 ASP A 297     6483  12612   8468  -2913    100   -697       O  
ATOM   2293  OD2 ASP A 297      59.306  11.286   2.514  1.00 74.13           O  
ANISOU 2293  OD2 ASP A 297     6167  13549   8449  -3079   -204  -1063       O  
ATOM   2294  N   SER A 298      56.123   6.724   3.212  1.00 58.91           N  
ANISOU 2294  N   SER A 298     5115  10545   6724   -693   -347     80       N  
ATOM   2295  CA  SER A 298      55.802   5.392   3.708  1.00 57.47           C  
ANISOU 2295  CA  SER A 298     4990  10298   6550    -72   -374    334       C  
ATOM   2296  C   SER A 298      54.845   4.659   2.768  1.00 53.33           C  
ANISOU 2296  C   SER A 298     4859   9161   6243     60   -194    510       C  
ATOM   2297  O   SER A 298      54.527   3.495   2.989  1.00 53.53           O  
ANISOU 2297  O   SER A 298     4995   9016   6329    520   -154    714       O  
ATOM   2298  CB  SER A 298      55.157   5.508   5.080  1.00 58.93           C  
ANISOU 2298  CB  SER A 298     5322  10470   6601     82   -542    432       C  
ATOM   2299  OG  SER A 298      54.070   6.415   5.024  1.00 59.16           O  
ANISOU 2299  OG  SER A 298     5740  10035   6704   -280   -522    396       O  
ATOM   2300  N   ALA A 299      54.371   5.350   1.735  1.00 50.41           N  
ANISOU 2300  N   ALA A 299     4714   8461   5978   -353    -82    431       N  
ATOM   2301  CA  ALA A 299      53.424   4.774   0.789  1.00 47.61           C  
ANISOU 2301  CA  ALA A 299     4706   7593   5791   -291     62    544       C  
ATOM   2302  C   ALA A 299      54.093   3.690  -0.025  1.00 48.67           C  
ANISOU 2302  C   ALA A 299     4680   7826   5987    -15    209    535       C  
ATOM   2303  O   ALA A 299      55.197   3.883  -0.532  1.00 53.61           O  
ANISOU 2303  O   ALA A 299     4977   8845   6548   -118    267    385       O  
ATOM   2304  CB  ALA A 299      52.865   5.851  -0.138  1.00 46.36           C  
ANISOU 2304  CB  ALA A 299     4793   7155   5666   -765    124    470       C  
ATOM   2305  N   HIS A 300      53.410   2.559  -0.152  1.00 46.57           N  
ANISOU 2305  N   HIS A 300     4648   7195   5852    316    291    673       N  
ATOM   2306  CA  HIS A 300      53.944   1.395  -0.847  1.00 49.46           C  
ANISOU 2306  CA  HIS A 300     4932   7560   6300    645    452    651       C  
ATOM   2307  C   HIS A 300      53.379   1.243  -2.257  1.00 43.96           C  
ANISOU 2307  C   HIS A 300     4474   6529   5701    438    617    549       C  
ATOM   2308  O   HIS A 300      53.859   0.417  -3.024  1.00 48.26           O  
ANISOU 2308  O   HIS A 300     4956   7084   6296    639    775    459       O  
ATOM   2309  CB  HIS A 300      53.671   0.127  -0.028  1.00 53.01           C  
ANISOU 2309  CB  HIS A 300     5510   7798   6834   1173    469    859       C  
ATOM   2310  CG  HIS A 300      54.564  -0.025   1.165  1.00 57.07           C  
ANISOU 2310  CG  HIS A 300     5714   8773   7199   1532    331    963       C  
ATOM   2311  ND1 HIS A 300      54.731   0.971   2.102  1.00 57.62           N  
ANISOU 2311  ND1 HIS A 300     5611   9196   7086   1340    127    947       N  
ATOM   2312  CD2 HIS A 300      55.336  -1.060   1.575  1.00 62.30           C  
ANISOU 2312  CD2 HIS A 300     6207   9620   7844   2101    360   1077       C  
ATOM   2313  CE1 HIS A 300      55.566   0.558   3.039  1.00 62.70           C  
ANISOU 2313  CE1 HIS A 300     5963  10283   7578   1755     15   1037       C  
ATOM   2314  NE2 HIS A 300      55.946  -0.672   2.744  1.00 66.21           N  
ANISOU 2314  NE2 HIS A 300     6403  10635   8118   2249    151   1143       N  
ATOM   2315  N   GLY A 301      52.371   2.037  -2.599  1.00 37.26           N  
ANISOU 2315  N   GLY A 301     3888   5414   4855     69    577    553       N  
ATOM   2316  CA  GLY A 301      51.757   1.961  -3.917  1.00 36.51           C  
ANISOU 2316  CA  GLY A 301     4011   5068   4794   -124    694    462       C  
ATOM   2317  C   GLY A 301      50.378   2.578  -3.943  1.00 36.17           C  
ANISOU 2317  C   GLY A 301     4276   4696   4770   -365    606    534       C  
ATOM   2318  O   GLY A 301      49.985   3.283  -3.017  1.00 37.14           O  
ANISOU 2318  O   GLY A 301     4441   4798   4873   -439    471    631       O  
ATOM   2319  N   PHE A 302      49.633   2.293  -5.006  1.00 38.87           N  
ANISOU 2319  N   PHE A 302     4816   4818   5134   -464    679    465       N  
ATOM   2320  CA  PHE A 302      48.273   2.796  -5.161  1.00 34.71           C  
ANISOU 2320  CA  PHE A 302     4538   4038   4611   -646    590    518       C  
ATOM   2321  C   PHE A 302      47.228   1.700  -5.355  1.00 33.89           C  
ANISOU 2321  C   PHE A 302     4603   3628   4646   -535    640    482       C  
ATOM   2322  O   PHE A 302      47.532   0.589  -5.781  1.00 36.45           O  
ANISOU 2322  O   PHE A 302     4924   3875   5051   -381    779    370       O  
ATOM   2323  CB  PHE A 302      48.215   3.729  -6.349  1.00 35.39           C  
ANISOU 2323  CB  PHE A 302     4699   4214   4533   -937    598    468       C  
ATOM   2324  CG  PHE A 302      49.172   4.872  -6.263  1.00 36.66           C  
ANISOU 2324  CG  PHE A 302     4739   4617   4574  -1142    592    494       C  
ATOM   2325  CD1 PHE A 302      48.922   5.938  -5.408  1.00 36.45           C  
ANISOU 2325  CD1 PHE A 302     4774   4536   4540  -1267    470    593       C  
ATOM   2326  CD2 PHE A 302      50.319   4.895  -7.050  1.00 38.96           C  
ANISOU 2326  CD2 PHE A 302     4854   5192   4759  -1238    733    394       C  
ATOM   2327  CE1 PHE A 302      49.808   7.016  -5.331  1.00 38.06           C  
ANISOU 2327  CE1 PHE A 302     4888   4924   4651  -1525    487    578       C  
ATOM   2328  CE2 PHE A 302      51.204   5.960  -6.985  1.00 40.82           C  
ANISOU 2328  CE2 PHE A 302     4962   5655   4893  -1503    759    401       C  
ATOM   2329  CZ  PHE A 302      50.949   7.024  -6.120  1.00 41.31           C  
ANISOU 2329  CZ  PHE A 302     5109   5618   4967  -1667    635    487       C  
ATOM   2330  N   LEU A 303      45.993   2.046  -5.011  1.00 33.59           N  
ANISOU 2330  N   LEU A 303     4707   3416   4641   -626    540    558       N  
ATOM   2331  CA  LEU A 303      44.819   1.229  -5.261  1.00 33.18           C  
ANISOU 2331  CA  LEU A 303     4787   3116   4702   -637    575    496       C  
ATOM   2332  C   LEU A 303      43.739   2.149  -5.825  1.00 36.07           C  
ANISOU 2332  C   LEU A 303     5232   3514   4957   -844    445    491       C  
ATOM   2333  O   LEU A 303      43.565   3.273  -5.355  1.00 36.05           O  
ANISOU 2333  O   LEU A 303     5243   3575   4880   -890    328    616       O  
ATOM   2334  CB  LEU A 303      44.312   0.622  -3.965  1.00 31.47           C  
ANISOU 2334  CB  LEU A 303     4609   2702   4647   -482    593    634       C  
ATOM   2335  CG  LEU A 303      45.154  -0.441  -3.256  1.00 32.97           C  
ANISOU 2335  CG  LEU A 303     4772   2805   4950   -192    722    706       C  
ATOM   2336  CD1 LEU A 303      44.609  -0.685  -1.838  1.00 30.68           C  
ANISOU 2336  CD1 LEU A 303     4540   2381   4736    -60    715    921       C  
ATOM   2337  CD2 LEU A 303      45.183  -1.730  -4.044  1.00 33.06           C  
ANISOU 2337  CD2 LEU A 303     4882   2581   5097   -132    907    542       C  
ATOM   2338  N   LYS A 304      43.020   1.681  -6.836  1.00 39.57           N  
ANISOU 2338  N   LYS A 304     5731   3926   5379   -948    462    332       N  
ATOM   2339  CA  LYS A 304      41.933   2.460  -7.397  1.00 38.86           C  
ANISOU 2339  CA  LYS A 304     5686   3923   5158  -1080    318    334       C  
ATOM   2340  C   LYS A 304      40.764   2.428  -6.410  1.00 36.81           C  
ANISOU 2340  C   LYS A 304     5414   3539   5031  -1052    254    415       C  
ATOM   2341  O   LYS A 304      40.543   1.426  -5.720  1.00 33.70           O  
ANISOU 2341  O   LYS A 304     5011   2964   4830  -1008    360    397       O  
ATOM   2342  CB  LYS A 304      41.519   1.896  -8.756  1.00 42.54           C  
ANISOU 2342  CB  LYS A 304     6168   4477   5518  -1197    337    104       C  
ATOM   2343  CG  LYS A 304      40.511   2.749  -9.514  1.00 46.26           C  
ANISOU 2343  CG  LYS A 304     6659   5141   5776  -1282    161    118       C  
ATOM   2344  CD  LYS A 304      40.116   2.082 -10.828  1.00 52.67           C  
ANISOU 2344  CD  LYS A 304     7458   6110   6443  -1399    165   -152       C  
ATOM   2345  CE  LYS A 304      38.983   2.831 -11.520  1.00 56.79           C  
ANISOU 2345  CE  LYS A 304     7958   6889   6728  -1431    -43   -131       C  
ATOM   2346  NZ  LYS A 304      37.677   2.699 -10.803  1.00 57.53           N  
ANISOU 2346  NZ  LYS A 304     7935   6949   6975  -1431   -143   -139       N  
ATOM   2347  N   VAL A 305      40.041   3.540  -6.337  1.00 33.81           N  
ANISOU 2347  N   VAL A 305     5049   3252   4546  -1061    104    519       N  
ATOM   2348  CA  VAL A 305      38.862   3.641  -5.499  1.00 32.20           C  
ANISOU 2348  CA  VAL A 305     4798   3003   4433  -1022     46    578       C  
ATOM   2349  C   VAL A 305      37.676   3.195  -6.328  1.00 33.83           C  
ANISOU 2349  C   VAL A 305     4924   3318   4613  -1131     -6    411       C  
ATOM   2350  O   VAL A 305      37.455   3.733  -7.404  1.00 41.15           O  
ANISOU 2350  O   VAL A 305     5861   4434   5341  -1159   -120    365       O  
ATOM   2351  CB  VAL A 305      38.601   5.089  -5.051  1.00 30.57           C  
ANISOU 2351  CB  VAL A 305     4644   2848   4123   -934    -84    738       C  
ATOM   2352  CG1 VAL A 305      37.360   5.152  -4.206  1.00 26.67           C  
ANISOU 2352  CG1 VAL A 305     4069   2353   3710   -864   -122    771       C  
ATOM   2353  CG2 VAL A 305      39.798   5.648  -4.296  1.00 29.42           C  
ANISOU 2353  CG2 VAL A 305     4561   2642   3975   -892    -48    845       C  
ATOM   2354  N   PRO A 306      36.896   2.229  -5.833  1.00 32.66           N  
ANISOU 2354  N   PRO A 306     4690   3076   4645  -1205     80    323       N  
ATOM   2355  CA  PRO A 306      35.737   1.811  -6.580  1.00 34.84           C  
ANISOU 2355  CA  PRO A 306     4834   3509   4896  -1362     24    117       C  
ATOM   2356  C   PRO A 306      34.846   2.987  -6.967  1.00 36.20           C  
ANISOU 2356  C   PRO A 306     4910   3978   4866  -1272   -198    175       C  
ATOM   2357  O   PRO A 306      34.579   3.836  -6.133  1.00 32.17           O  
ANISOU 2357  O   PRO A 306     4401   3463   4361  -1113   -251    359       O  
ATOM   2358  CB  PRO A 306      35.012   0.894  -5.596  1.00 36.71           C  
ANISOU 2358  CB  PRO A 306     4994   3578   5377  -1462    174     92       C  
ATOM   2359  CG  PRO A 306      36.082   0.318  -4.785  1.00 35.45           C  
ANISOU 2359  CG  PRO A 306     4992   3115   5364  -1370    352    224       C  
ATOM   2360  CD  PRO A 306      37.066   1.427  -4.610  1.00 34.80           C  
ANISOU 2360  CD  PRO A 306     4984   3107   5132  -1171    248    407       C  
ATOM   2361  N   PRO A 307      34.359   3.011  -8.221  1.00 41.34           N  
ANISOU 2361  N   PRO A 307     5482   4902   5323  -1345   -326      9       N  
ATOM   2362  CA  PRO A 307      33.602   4.142  -8.764  1.00 43.93           C  
ANISOU 2362  CA  PRO A 307     5743   5541   5405  -1183   -554     98       C  
ATOM   2363  C   PRO A 307      32.320   4.491  -8.007  1.00 43.77           C  
ANISOU 2363  C   PRO A 307     5512   5664   5454  -1082   -634    138       C  
ATOM   2364  O   PRO A 307      31.799   5.590  -8.166  1.00 47.25           O  
ANISOU 2364  O   PRO A 307     5936   6291   5727   -841   -803    281       O  
ATOM   2365  CB  PRO A 307      33.259   3.682 -10.191  1.00 47.29           C  
ANISOU 2365  CB  PRO A 307     6073   6283   5614  -1320   -654   -153       C  
ATOM   2366  CG  PRO A 307      33.281   2.204 -10.127  1.00 48.01           C  
ANISOU 2366  CG  PRO A 307     6096   6224   5922  -1606   -477   -447       C  
ATOM   2367  CD  PRO A 307      34.362   1.864  -9.149  1.00 44.49           C  
ANISOU 2367  CD  PRO A 307     5839   5344   5721  -1576   -259   -302       C  
ATOM   2368  N   ARG A 308      31.806   3.567  -7.208  1.00 43.65           N  
ANISOU 2368  N   ARG A 308     5345   5562   5679  -1249   -493     22       N  
ATOM   2369  CA  ARG A 308      30.623   3.839  -6.409  1.00 44.73           C  
ANISOU 2369  CA  ARG A 308     5248   5862   5886  -1174   -522     51       C  
ATOM   2370  C   ARG A 308      30.959   4.704  -5.202  1.00 43.73           C  
ANISOU 2370  C   ARG A 308     5267   5532   5818   -929   -474    316       C  
ATOM   2371  O   ARG A 308      30.073   5.261  -4.567  1.00 47.06           O  
ANISOU 2371  O   ARG A 308     5535   6105   6242   -769   -514    371       O  
ATOM   2372  CB  ARG A 308      30.003   2.522  -5.938  1.00 45.90           C  
ANISOU 2372  CB  ARG A 308     5208   5963   6270  -1495   -334   -151       C  
ATOM   2373  CG  ARG A 308      28.584   2.620  -5.386  1.00 46.55           C  
ANISOU 2373  CG  ARG A 308     4940   6350   6398  -1509   -352   -208       C  
ATOM   2374  CD  ARG A 308      27.599   3.153  -6.419  1.00 49.75           C  
ANISOU 2374  CD  ARG A 308     5048   7290   6565  -1423   -622   -357       C  
ATOM   2375  NE  ARG A 308      26.235   3.211  -5.903  1.00 50.84           N  
ANISOU 2375  NE  ARG A 308     4778   7793   6747  -1429   -635   -441       N  
ATOM   2376  CZ  ARG A 308      25.789   4.137  -5.056  1.00 49.80           C  
ANISOU 2376  CZ  ARG A 308     4576   7746   6598  -1101   -658   -246       C  
ATOM   2377  NH1 ARG A 308      26.586   5.097  -4.594  1.00 45.54           N  
ANISOU 2377  NH1 ARG A 308     4373   6918   6013   -771   -673     30       N  
ATOM   2378  NH2 ARG A 308      24.535   4.099  -4.654  1.00 54.94           N  
ANISOU 2378  NH2 ARG A 308     4806   8786   7282  -1120   -649   -358       N  
ATOM   2379  N   MET A 309      32.241   4.826  -4.892  1.00 41.47           N  
ANISOU 2379  N   MET A 309     5253   4940   5563   -898   -389    448       N  
ATOM   2380  CA  MET A 309      32.666   5.467  -3.660  1.00 41.09           C  
ANISOU 2380  CA  MET A 309     5335   4704   5573   -733   -326    638       C  
ATOM   2381  C   MET A 309      32.790   6.971  -3.782  1.00 38.66           C  
ANISOU 2381  C   MET A 309     5176   4410   5104   -480   -470    781       C  
ATOM   2382  O   MET A 309      33.848   7.479  -4.136  1.00 40.87           O  
ANISOU 2382  O   MET A 309     5679   4544   5308   -473   -484    863       O  
ATOM   2383  CB  MET A 309      34.003   4.877  -3.217  1.00 39.56           C  
ANISOU 2383  CB  MET A 309     5321   4235   5477   -816   -177    691       C  
ATOM   2384  CG  MET A 309      34.426   5.274  -1.830  1.00 37.68           C  
ANISOU 2384  CG  MET A 309     5169   3864   5284   -688   -105    842       C  
ATOM   2385  SD  MET A 309      34.743   3.812  -0.844  1.00 39.25           S  
ANISOU 2385  SD  MET A 309     5359   3886   5668   -793    128    873       S  
ATOM   2386  CE  MET A 309      33.088   3.182  -0.658  1.00 42.96           C  
ANISOU 2386  CE  MET A 309     5593   4489   6242   -928    209    779       C  
ATOM   2387  N   ASP A 310      31.712   7.683  -3.465  1.00 40.37           N  
ANISOU 2387  N   ASP A 310     5273   4789   5279   -273   -554    809       N  
ATOM   2388  CA  ASP A 310      31.778   9.138  -3.331  1.00 41.41           C  
ANISOU 2388  CA  ASP A 310     5601   4833   5300      9   -645    954       C  
ATOM   2389  C   ASP A 310      32.429   9.461  -1.990  1.00 38.94           C  
ANISOU 2389  C   ASP A 310     5441   4274   5081     34   -522   1012       C  
ATOM   2390  O   ASP A 310      32.674   8.555  -1.191  1.00 35.62           O  
ANISOU 2390  O   ASP A 310     4938   3817   4779   -114   -387    974       O  
ATOM   2391  CB  ASP A 310      30.393   9.789  -3.489  1.00 45.43           C  
ANISOU 2391  CB  ASP A 310     5926   5613   5722    295   -777    953       C  
ATOM   2392  CG  ASP A 310      29.465   9.534  -2.309  1.00 47.74           C  
ANISOU 2392  CG  ASP A 310     5967   6037   6136    357   -681    883       C  
ATOM   2393  OD1 ASP A 310      29.092  10.517  -1.628  1.00 51.36           O  
ANISOU 2393  OD1 ASP A 310     6489   6453   6571    652   -686    944       O  
ATOM   2394  OD2 ASP A 310      29.095   8.366  -2.071  1.00 45.51           O  
ANISOU 2394  OD2 ASP A 310     5439   5887   5966    108   -577    762       O  
ATOM   2395  N   ALA A 311      32.724  10.737  -1.750  1.00 39.46           N  
ANISOU 2395  N   ALA A 311     5747   4166   5080    219   -561   1101       N  
ATOM   2396  CA  ALA A 311      33.529  11.134  -0.580  1.00 36.95           C  
ANISOU 2396  CA  ALA A 311     5596   3634   4809    199   -465   1108       C  
ATOM   2397  C   ALA A 311      32.829  10.849   0.736  1.00 37.77           C  
ANISOU 2397  C   ALA A 311     5534   3842   4975    290   -374   1053       C  
ATOM   2398  O   ALA A 311      33.465  10.418   1.705  1.00 34.01           O  
ANISOU 2398  O   ALA A 311     5072   3319   4532    188   -273   1042       O  
ATOM   2399  CB  ALA A 311      33.897  12.595  -0.657  1.00 34.62           C  
ANISOU 2399  CB  ALA A 311     5615   3097   4441    335   -507   1168       C  
ATOM   2400  N   LYS A 312      31.520  11.100   0.774  1.00 42.13           N  
ANISOU 2400  N   LYS A 312     5912   4581   5515    503   -408   1027       N  
ATOM   2401  CA  LYS A 312      30.729  10.827   1.973  1.00 42.43           C  
ANISOU 2401  CA  LYS A 312     5754   4776   5591    586   -292    973       C  
ATOM   2402  C   LYS A 312      31.000   9.395   2.409  1.00 38.89           C  
ANISOU 2402  C   LYS A 312     5163   4384   5231    306   -152    975       C  
ATOM   2403  O   LYS A 312      31.305   9.140   3.575  1.00 38.50           O  
ANISOU 2403  O   LYS A 312     5144   4307   5178    285    -24    998       O  
ATOM   2404  CB  LYS A 312      29.229  11.042   1.718  1.00 48.15           C  
ANISOU 2404  CB  LYS A 312     6200   5797   6297    814   -343    925       C  
ATOM   2405  CG  LYS A 312      28.714  12.470   1.997  1.00 53.60           C  
ANISOU 2405  CG  LYS A 312     7018   6435   6912   1225   -397    923       C  
ATOM   2406  CD  LYS A 312      27.188  12.590   1.755  1.00 58.37           C  
ANISOU 2406  CD  LYS A 312     7262   7427   7489   1502   -452    871       C  
ATOM   2407  CE  LYS A 312      26.840  13.478   0.552  1.00 63.76           C  
ANISOU 2407  CE  LYS A 312     8031   8125   8070   1814   -657    953       C  
ATOM   2408  NZ  LYS A 312      25.553  13.151  -0.164  1.00 65.76           N  
ANISOU 2408  NZ  LYS A 312     7835   8885   8266   1960   -781    902       N  
ATOM   2409  N   MET A 313      30.924   8.475   1.449  1.00 36.45           N  
ANISOU 2409  N   MET A 313     4729   4137   4982    104   -171    952       N  
ATOM   2410  CA  MET A 313      31.105   7.046   1.706  1.00 33.85           C  
ANISOU 2410  CA  MET A 313     4305   3788   4768   -160    -15    951       C  
ATOM   2411  C   MET A 313      32.543   6.715   2.089  1.00 35.03           C  
ANISOU 2411  C   MET A 313     4682   3703   4926   -238     43   1034       C  
ATOM   2412  O   MET A 313      32.787   5.991   3.057  1.00 38.96           O  
ANISOU 2412  O   MET A 313     5186   4156   5461   -285    196   1108       O  
ATOM   2413  CB  MET A 313      30.725   6.253   0.466  1.00 33.85           C  
ANISOU 2413  CB  MET A 313     4155   3881   4824   -360    -59    847       C  
ATOM   2414  CG  MET A 313      30.433   4.810   0.734  1.00 36.16           C  
ANISOU 2414  CG  MET A 313     4316   4153   5269   -636    136    801       C  
ATOM   2415  SD  MET A 313      29.747   3.999  -0.716  1.00 44.26           S  
ANISOU 2415  SD  MET A 313     5125   5347   6345   -904     73    577       S  
ATOM   2416  CE  MET A 313      28.171   4.829  -0.894  1.00 45.91           C  
ANISOU 2416  CE  MET A 313     4971   6021   6452   -735    -74    482       C  
ATOM   2417  N   TYR A 314      33.483   7.256   1.318  1.00 32.99           N  
ANISOU 2417  N   TYR A 314     4595   3328   4611   -238    -74   1036       N  
ATOM   2418  CA  TYR A 314      34.912   7.064   1.531  1.00 31.14           C  
ANISOU 2418  CA  TYR A 314     4519   2946   4368   -302    -45   1085       C  
ATOM   2419  C   TYR A 314      35.331   7.514   2.929  1.00 28.98           C  
ANISOU 2419  C   TYR A 314     4317   2670   4024   -191     -4   1133       C  
ATOM   2420  O   TYR A 314      35.808   6.710   3.726  1.00 31.43           O  
ANISOU 2420  O   TYR A 314     4613   2983   4344   -206    100   1205       O  
ATOM   2421  CB  TYR A 314      35.679   7.834   0.456  1.00 33.98           C  
ANISOU 2421  CB  TYR A 314     5022   3234   4654   -334   -165   1067       C  
ATOM   2422  CG  TYR A 314      37.153   7.518   0.346  1.00 35.06           C  
ANISOU 2422  CG  TYR A 314     5241   3294   4785   -441   -133   1081       C  
ATOM   2423  CD1 TYR A 314      37.591   6.295  -0.143  1.00 37.24           C  
ANISOU 2423  CD1 TYR A 314     5455   3554   5139   -544    -53   1061       C  
ATOM   2424  CD2 TYR A 314      38.104   8.465   0.686  1.00 36.52           C  
ANISOU 2424  CD2 TYR A 314     5554   3432   4890   -444   -172   1085       C  
ATOM   2425  CE1 TYR A 314      38.945   6.012  -0.261  1.00 41.49           C  
ANISOU 2425  CE1 TYR A 314     6029   4071   5666   -587    -19   1066       C  
ATOM   2426  CE2 TYR A 314      39.449   8.206   0.566  1.00 39.39           C  
ANISOU 2426  CE2 TYR A 314     5921   3806   5237   -547   -146   1076       C  
ATOM   2427  CZ  TYR A 314      39.877   6.977   0.092  1.00 43.80           C  
ANISOU 2427  CZ  TYR A 314     6388   4391   5864   -590    -73   1076       C  
ATOM   2428  OH  TYR A 314      41.238   6.722  -0.020  1.00 47.79           O  
ANISOU 2428  OH  TYR A 314     6856   4954   6346   -640    -42   1059       O  
ATOM   2429  N   LEU A 315      35.118   8.784   3.242  1.00 29.30           N  
ANISOU 2429  N   LEU A 315     4448   2705   3978    -60    -79   1091       N  
ATOM   2430  CA  LEU A 315      35.382   9.288   4.595  1.00 32.66           C  
ANISOU 2430  CA  LEU A 315     4938   3166   4307     40    -43   1073       C  
ATOM   2431  C   LEU A 315      34.546   8.505   5.629  1.00 34.66           C  
ANISOU 2431  C   LEU A 315     5039   3574   4556    104     99   1129       C  
ATOM   2432  O   LEU A 315      35.054   8.088   6.683  1.00 34.35           O  
ANISOU 2432  O   LEU A 315     5014   3607   4432    124    175   1190       O  
ATOM   2433  CB  LEU A 315      35.072  10.785   4.679  1.00 32.73           C  
ANISOU 2433  CB  LEU A 315     5097   3091   4250    180   -119    978       C  
ATOM   2434  CG  LEU A 315      35.909  11.711   3.787  1.00 31.98           C  
ANISOU 2434  CG  LEU A 315     5215   2790   4145     91   -215    950       C  
ATOM   2435  CD1 LEU A 315      35.163  13.008   3.459  1.00 30.64           C  
ANISOU 2435  CD1 LEU A 315     5215   2468   3960    281   -266    916       C  
ATOM   2436  CD2 LEU A 315      37.273  11.995   4.432  1.00 31.97           C  
ANISOU 2436  CD2 LEU A 315     5313   2760   4074    -55   -216    878       C  
ATOM   2437  N   GLY A 316      33.270   8.297   5.305  1.00 33.59           N  
ANISOU 2437  N   GLY A 316     4744   3526   4491    132    141   1116       N  
ATOM   2438  CA  GLY A 316      32.378   7.508   6.140  1.00 35.11           C  
ANISOU 2438  CA  GLY A 316     4766   3876   4699    127    317   1171       C  
ATOM   2439  C   GLY A 316      31.584   8.348   7.119  1.00 38.94           C  
ANISOU 2439  C   GLY A 316     5205   4525   5067    335    363   1107       C  
ATOM   2440  O   GLY A 316      32.030   9.418   7.547  1.00 43.42           O  
ANISOU 2440  O   GLY A 316     5935   5042   5519    481    285   1027       O  
ATOM   2441  N   TYR A 317      30.415   7.835   7.491  1.00 38.80           N  
ANISOU 2441  N   TYR A 317     4958   4706   5079    325    516   1121       N  
ATOM   2442  CA  TYR A 317      29.484   8.533   8.366  1.00 40.55           C  
ANISOU 2442  CA  TYR A 317     5071   5145   5190    539    597   1043       C  
ATOM   2443  C   TYR A 317      30.132   9.219   9.571  1.00 39.08           C  
ANISOU 2443  C   TYR A 317     5086   4958   4802    697    616   1012       C  
ATOM   2444  O   TYR A 317      29.994  10.428   9.749  1.00 41.05           O  
ANISOU 2444  O   TYR A 317     5431   5190   4975    917    539    860       O  
ATOM   2445  CB  TYR A 317      28.410   7.557   8.858  1.00 44.88           C  
ANISOU 2445  CB  TYR A 317     5341   5934   5778    414    835   1103       C  
ATOM   2446  CG  TYR A 317      27.272   8.215   9.615  1.00 50.71           C  
ANISOU 2446  CG  TYR A 317     5881   6977   6412    635    943   1001       C  
ATOM   2447  CD1 TYR A 317      26.578   9.285   9.062  1.00 53.24           C  
ANISOU 2447  CD1 TYR A 317     6094   7391   6742    897    801    841       C  
ATOM   2448  CD2 TYR A 317      26.879   7.759  10.873  1.00 54.82           C  
ANISOU 2448  CD2 TYR A 317     6320   7703   6804    616   1202   1077       C  
ATOM   2449  CE1 TYR A 317      25.533   9.893   9.735  1.00 56.94           C  
ANISOU 2449  CE1 TYR A 317     6361   8154   7118   1157    910    728       C  
ATOM   2450  CE2 TYR A 317      25.827   8.364  11.557  1.00 59.26           C  
ANISOU 2450  CE2 TYR A 317     6674   8587   7255    831   1326    959       C  
ATOM   2451  CZ  TYR A 317      25.158   9.436  10.975  1.00 59.14           C  
ANISOU 2451  CZ  TYR A 317     6534   8663   7276   1113   1176    768       C  
ATOM   2452  OH  TYR A 317      24.113  10.060  11.618  1.00 61.33           O  
ANISOU 2452  OH  TYR A 317     6586   9269   7449   1388   1302    632       O  
ATOM   2453  N   GLU A 318      30.829   8.449  10.401  1.00 39.67           N  
ANISOU 2453  N   GLU A 318     5238   5055   4779    601    720   1147       N  
ATOM   2454  CA  GLU A 318      31.288   8.959  11.698  1.00 41.37           C  
ANISOU 2454  CA  GLU A 318     5583   5395   4741    744    754   1104       C  
ATOM   2455  C   GLU A 318      32.300  10.074  11.529  1.00 38.07           C  
ANISOU 2455  C   GLU A 318     5388   4815   4264    799    547    934       C  
ATOM   2456  O   GLU A 318      32.373  10.975  12.370  1.00 28.89           O  
ANISOU 2456  O   GLU A 318     4327   3731   2919    942    540    763       O  
ATOM   2457  CB  GLU A 318      31.901   7.856  12.564  1.00 44.08           C  
ANISOU 2457  CB  GLU A 318     5968   5830   4952    667    883   1328       C  
ATOM   2458  CG  GLU A 318      30.928   6.775  13.000  1.00 49.63           C  
ANISOU 2458  CG  GLU A 318     6511   6668   5677    582   1158   1518       C  
ATOM   2459  CD  GLU A 318      30.776   5.649  11.987  1.00 51.97           C  
ANISOU 2459  CD  GLU A 318     6737   6756   6252    340   1215   1648       C  
ATOM   2460  OE1 GLU A 318      31.573   5.580  11.020  1.00 49.23           O  
ANISOU 2460  OE1 GLU A 318     6480   6183   6044    269   1042   1623       O  
ATOM   2461  OE2 GLU A 318      29.852   4.825  12.168  1.00 56.92           O  
ANISOU 2461  OE2 GLU A 318     7218   7454   6954    196   1454   1755       O  
ATOM   2462  N   TYR A 319      33.088   9.998  10.451  1.00 40.13           N  
ANISOU 2462  N   TYR A 319     5725   4851   4671    658    401    961       N  
ATOM   2463  CA  TYR A 319      34.051  11.052  10.132  1.00 38.16           C  
ANISOU 2463  CA  TYR A 319     5680   4422   4398    636    233    806       C  
ATOM   2464  C   TYR A 319      33.288  12.294   9.721  1.00 37.39           C  
ANISOU 2464  C   TYR A 319     5669   4182   4355    795    190    645       C  
ATOM   2465  O   TYR A 319      33.432  13.346  10.339  1.00 39.73           O  
ANISOU 2465  O   TYR A 319     6133   4422   4542    899    176    453       O  
ATOM   2466  CB  TYR A 319      35.034  10.643   9.030  1.00 34.01           C  
ANISOU 2466  CB  TYR A 319     5192   3727   4004    441    126    886       C  
ATOM   2467  CG  TYR A 319      36.131  11.672   8.836  1.00 36.63           C  
ANISOU 2467  CG  TYR A 319     5713   3913   4292    351     -4    732       C  
ATOM   2468  CD1 TYR A 319      37.331  11.577   9.518  1.00 38.64           C  
ANISOU 2468  CD1 TYR A 319     5981   4297   4402    258    -50    685       C  
ATOM   2469  CD2 TYR A 319      35.954  12.753   7.992  1.00 41.43           C  
ANISOU 2469  CD2 TYR A 319     6482   4269   4990    355    -72    636       C  
ATOM   2470  CE1 TYR A 319      38.332  12.521   9.357  1.00 40.98           C  
ANISOU 2470  CE1 TYR A 319     6411   4493   4667    105   -150    505       C  
ATOM   2471  CE2 TYR A 319      36.947  13.705   7.822  1.00 44.58           C  
ANISOU 2471  CE2 TYR A 319     7083   4491   5366    211   -145    497       C  
ATOM   2472  CZ  TYR A 319      38.135  13.592   8.509  1.00 44.52           C  
ANISOU 2472  CZ  TYR A 319     7051   4631   5233     53   -180    409       C  
ATOM   2473  OH  TYR A 319      39.120  14.555   8.339  1.00 46.08           O  
ANISOU 2473  OH  TYR A 319     7413   4677   5417   -160   -236    231       O  
ATOM   2474  N   VAL A 320      32.460  12.150   8.692  1.00 34.67           N  
ANISOU 2474  N   VAL A 320     5214   3789   4169    834    173    714       N  
ATOM   2475  CA  VAL A 320      31.679  13.261   8.156  1.00 34.58           C  
ANISOU 2475  CA  VAL A 320     5275   3657   4206   1060    117    618       C  
ATOM   2476  C   VAL A 320      30.882  13.956   9.256  1.00 37.71           C  
ANISOU 2476  C   VAL A 320     5663   4177   4486   1333    224    463       C  
ATOM   2477  O   VAL A 320      30.958  15.171   9.399  1.00 36.82           O  
ANISOU 2477  O   VAL A 320     5792   3854   4342   1501    192    303       O  
ATOM   2478  CB  VAL A 320      30.727  12.779   7.049  1.00 35.10           C  
ANISOU 2478  CB  VAL A 320     5117   3818   4401   1094     81    719       C  
ATOM   2479  CG1 VAL A 320      29.647  13.816   6.772  1.00 40.66           C  
ANISOU 2479  CG1 VAL A 320     5811   4530   5110   1445     45    643       C  
ATOM   2480  CG2 VAL A 320      31.515  12.464   5.778  1.00 32.45           C  
ANISOU 2480  CG2 VAL A 320     4866   3311   4151    881    -42    816       C  
ATOM   2481  N   THR A 321      30.135  13.177  10.035  1.00 38.03           N  
ANISOU 2481  N   THR A 321     5445   4541   4462   1363    376    504       N  
ATOM   2482  CA  THR A 321      29.434  13.695  11.202  1.00 39.83           C  
ANISOU 2482  CA  THR A 321     5634   4963   4535   1606    516    353       C  
ATOM   2483  C   THR A 321      30.373  14.466  12.125  1.00 41.59           C  
ANISOU 2483  C   THR A 321     6149   5072   4581   1610    499    168       C  
ATOM   2484  O   THR A 321      30.016  15.522  12.661  1.00 43.96           O  
ANISOU 2484  O   THR A 321     6585   5320   4799   1853    541    -60       O  
ATOM   2485  CB  THR A 321      28.801  12.558  12.004  1.00 42.32           C  
ANISOU 2485  CB  THR A 321     5659   5652   4768   1531    720    471       C  
ATOM   2486  OG1 THR A 321      27.747  11.969  11.236  1.00 47.36           O  
ANISOU 2486  OG1 THR A 321     5987   6440   5569   1510    759    562       O  
ATOM   2487  CG2 THR A 321      28.243  13.069  13.324  1.00 44.99           C  
ANISOU 2487  CG2 THR A 321     5975   6236   4884   1762    889    311       C  
ATOM   2488  N   ALA A 322      31.575  13.931  12.314  1.00 39.97           N  
ANISOU 2488  N   ALA A 322     6026   4850   4310   1350    439    238       N  
ATOM   2489  CA  ALA A 322      32.540  14.552  13.202  1.00 42.64           C  
ANISOU 2489  CA  ALA A 322     6576   5175   4450   1300    399     37       C  
ATOM   2490  C   ALA A 322      32.897  15.938  12.683  1.00 46.01           C  
ANISOU 2490  C   ALA A 322     7303   5207   4970   1324    297   -189       C  
ATOM   2491  O   ALA A 322      32.661  16.951  13.348  1.00 49.85           O  
ANISOU 2491  O   ALA A 322     7964   5619   5357   1488    348   -460       O  
ATOM   2492  CB  ALA A 322      33.779  13.688  13.318  1.00 40.27           C  
ANISOU 2492  CB  ALA A 322     6251   4973   4078   1044    323    174       C  
ATOM   2493  N   ILE A 323      33.422  15.970  11.464  1.00 44.81           N  
ANISOU 2493  N   ILE A 323     7234   4783   5011   1163    180    -74       N  
ATOM   2494  CA  ILE A 323      33.975  17.185  10.884  1.00 47.07           C  
ANISOU 2494  CA  ILE A 323     7848   4648   5388   1101    106   -226       C  
ATOM   2495  C   ILE A 323      32.881  18.207  10.549  1.00 48.81           C  
ANISOU 2495  C   ILE A 323     8227   4614   5705   1450    155   -298       C  
ATOM   2496  O   ILE A 323      33.154  19.402  10.518  1.00 50.77           O  
ANISOU 2496  O   ILE A 323     8822   4483   5986   1481    161   -488       O  
ATOM   2497  CB  ILE A 323      34.860  16.860   9.640  1.00 47.02           C  
ANISOU 2497  CB  ILE A 323     7871   4467   5527    824     -4    -46       C  
ATOM   2498  CG1 ILE A 323      36.214  17.592   9.717  1.00 50.98           C  
ANISOU 2498  CG1 ILE A 323     8609   4763   5998    519    -57   -235       C  
ATOM   2499  CG2 ILE A 323      34.120  17.135   8.352  1.00 45.08           C  
ANISOU 2499  CG2 ILE A 323     7680   3996   5453    979    -34    117       C  
ATOM   2500  CD1 ILE A 323      36.119  19.098   9.867  1.00 56.79           C  
ANISOU 2500  CD1 ILE A 323     9723   5094   6762    581    -10   -491       C  
ATOM   2501  N   ARG A 324      31.654  17.735  10.320  1.00 49.90           N  
ANISOU 2501  N   ARG A 324     8108   4965   5887   1713    200   -156       N  
ATOM   2502  CA  ARG A 324      30.495  18.615  10.174  1.00 54.75           C  
ANISOU 2502  CA  ARG A 324     8785   5466   6553   2141    250   -228       C  
ATOM   2503  C   ARG A 324      30.374  19.448  11.426  1.00 60.10           C  
ANISOU 2503  C   ARG A 324     9636   6111   7089   2318    371   -547       C  
ATOM   2504  O   ARG A 324      30.528  20.667  11.390  1.00 63.20           O  
ANISOU 2504  O   ARG A 324    10407   6081   7526   2449    386   -735       O  
ATOM   2505  CB  ARG A 324      29.201  17.812   9.994  1.00 59.87           C  
ANISOU 2505  CB  ARG A 324     9004   6521   7224   2351    294    -79       C  
ATOM   2506  CG  ARG A 324      29.019  17.165   8.624  1.00 62.97           C  
ANISOU 2506  CG  ARG A 324     9223   6948   7754   2258    169    175       C  
ATOM   2507  CD  ARG A 324      28.186  18.019   7.675  1.00 70.28           C  
ANISOU 2507  CD  ARG A 324    10213   7730   8760   2646     90    225       C  
ATOM   2508  NE  ARG A 324      26.795  18.181   8.108  1.00 76.59           N  
ANISOU 2508  NE  ARG A 324    10725   8850   9526   3063    176    145       N  
ATOM   2509  CZ  ARG A 324      25.832  17.269   7.965  1.00 79.12           C  
ANISOU 2509  CZ  ARG A 324    10555   9653   9852   3079    198    216       C  
ATOM   2510  NH1 ARG A 324      26.083  16.084   7.411  1.00 77.74           N  
ANISOU 2510  NH1 ARG A 324    10160   9651   9727   2696    146    363       N  
ATOM   2511  NH2 ARG A 324      24.604  17.544   8.392  1.00 83.08           N  
ANISOU 2511  NH2 ARG A 324    10779  10473  10316   3470    290    114       N  
ATOM   2512  N   ASN A 325      30.145  18.765  12.548  1.00 63.19           N  
ANISOU 2512  N   ASN A 325     9780   6934   7295   2302    476   -611       N  
ATOM   2513  CA  ASN A 325      29.874  19.426  13.822  1.00 65.08           C  
ANISOU 2513  CA  ASN A 325    10122   7265   7340   2501    614   -931       C  
ATOM   2514  C   ASN A 325      30.914  20.492  14.151  1.00 68.04           C  
ANISOU 2514  C   ASN A 325    10934   7247   7673   2342    575  -1239       C  
ATOM   2515  O   ASN A 325      30.597  21.497  14.787  1.00 72.15           O  
ANISOU 2515  O   ASN A 325    11687   7602   8126   2578    677  -1560       O  
ATOM   2516  CB  ASN A 325      29.790  18.398  14.954  1.00 63.75           C  
ANISOU 2516  CB  ASN A 325     9658   7642   6923   2403    722   -898       C  
ATOM   2517  CG  ASN A 325      28.597  17.451  14.810  1.00 64.71           C  
ANISOU 2517  CG  ASN A 325     9357   8147   7084   2542    834   -659       C  
ATOM   2518  OD1 ASN A 325      27.809  17.556  13.870  1.00 66.26           O  
ANISOU 2518  OD1 ASN A 325     9430   8268   7479   2722    802   -551       O  
ATOM   2519  ND2 ASN A 325      28.470  16.515  15.747  1.00 62.26           N  
ANISOU 2519  ND2 ASN A 325     8819   8271   6566   2442    971   -574       N  
ATOM   2520  N   LEU A 326      32.151  20.286  13.706  1.00 67.09           N  
ANISOU 2520  N   LEU A 326    10917   6978   7598   1932    442  -1170       N  
ATOM   2521  CA  LEU A 326      33.217  21.247  13.980  1.00 72.32           C  
ANISOU 2521  CA  LEU A 326    11947   7303   8228   1680    408  -1484       C  
ATOM   2522  C   LEU A 326      32.952  22.604  13.335  1.00 77.30           C  
ANISOU 2522  C   LEU A 326    13011   7296   9066   1858    455  -1610       C  
ATOM   2523  O   LEU A 326      33.322  23.643  13.886  1.00 77.40           O  
ANISOU 2523  O   LEU A 326    13375   6993   9042   1801    521  -1983       O  
ATOM   2524  CB  LEU A 326      34.579  20.697  13.538  1.00 68.89           C  
ANISOU 2524  CB  LEU A 326    11462   6903   7811   1204    265  -1366       C  
ATOM   2525  CG  LEU A 326      35.158  19.596  14.440  1.00 66.80           C  
ANISOU 2525  CG  LEU A 326    10882   7211   7289   1030    219  -1328       C  
ATOM   2526  CD1 LEU A 326      36.436  19.018  13.837  1.00 64.67           C  
ANISOU 2526  CD1 LEU A 326    10521   6981   7068    643     77  -1179       C  
ATOM   2527  CD2 LEU A 326      35.418  20.102  15.860  1.00 67.01           C  
ANISOU 2527  CD2 LEU A 326    10990   7459   7012   1021    260  -1732       C  
ATOM   2528  N   ARG A 327      32.279  22.595  12.190  1.00 80.51           N  
ANISOU 2528  N   ARG A 327    13404   7513   9673   2090    429  -1306       N  
ATOM   2529  CA  ARG A 327      32.059  23.820  11.431  1.00 85.87           C  
ANISOU 2529  CA  ARG A 327    14525   7561  10542   2299    467  -1323       C  
ATOM   2530  C   ARG A 327      30.689  24.399  11.796  1.00 89.84           C  
ANISOU 2530  C   ARG A 327    15047   8045  11041   2918    588  -1426       C  
ATOM   2531  O   ARG A 327      30.607  25.478  12.390  1.00 92.93           O  
ANISOU 2531  O   ARG A 327    15809   8073  11428   3094    713  -1759       O  
ATOM   2532  CB  ARG A 327      32.195  23.556   9.928  1.00 84.36           C  
ANISOU 2532  CB  ARG A 327    14336   7199  10519   2224    354   -923       C  
ATOM   2533  CG  ARG A 327      33.005  22.308   9.587  1.00 80.15           C  
ANISOU 2533  CG  ARG A 327    13469   7037   9948   1787    235   -720       C  
ATOM   2534  CD  ARG A 327      33.961  22.488   8.424  1.00 81.92           C  
ANISOU 2534  CD  ARG A 327    13908   6926  10293   1448    167   -540       C  
ATOM   2535  NE  ARG A 327      35.332  22.677   8.902  1.00 84.27           N  
ANISOU 2535  NE  ARG A 327    14333   7143  10543    945    172   -771       N  
ATOM   2536  CZ  ARG A 327      36.431  22.240   8.281  1.00 83.80           C  
ANISOU 2536  CZ  ARG A 327    14207   7124  10509    516    105   -654       C  
ATOM   2537  NH1 ARG A 327      37.621  22.466   8.825  1.00 85.83           N  
ANISOU 2537  NH1 ARG A 327    14521   7387  10705     83    108   -912       N  
ATOM   2538  NH2 ARG A 327      36.359  21.571   7.132  1.00 80.69           N  
ANISOU 2538  NH2 ARG A 327    13661   6813  10183    515     36   -312       N  
ATOM   2539  N   GLU A 328      29.628  23.660  11.475  1.00 88.65           N  
ANISOU 2539  N   GLU A 328    14477   8315  10890   3233    562  -1176       N  
ATOM   2540  CA  GLU A 328      28.258  24.038  11.859  1.00 93.78           C  
ANISOU 2540  CA  GLU A 328    15001   9116  11514   3837    677  -1268       C  
ATOM   2541  C   GLU A 328      27.885  23.558  13.274  1.00 94.10           C  
ANISOU 2541  C   GLU A 328    14741   9689  11325   3870    813  -1516       C  
ATOM   2542  O   GLU A 328      27.799  22.354  13.538  1.00 91.11           O  
ANISOU 2542  O   GLU A 328    13925   9853  10838   3663    798  -1360       O  
ATOM   2543  CB  GLU A 328      27.248  23.524  10.825  1.00 93.31           C  
ANISOU 2543  CB  GLU A 328    14583   9325  11547   4147    586   -916       C  
ATOM   2544  CG  GLU A 328      27.255  22.013  10.583  1.00 88.81           C  
ANISOU 2544  CG  GLU A 328    13493   9316  10935   3809    498   -673       C  
ATOM   2545  CD  GLU A 328      27.258  21.650   9.105  1.00 87.35           C  
ANISOU 2545  CD  GLU A 328    13231   9079  10878   3747    323   -331       C  
ATOM   2546  OE1 GLU A 328      26.475  20.761   8.711  1.00 86.96           O  
ANISOU 2546  OE1 GLU A 328    12713   9500  10828   3805    275   -166       O  
ATOM   2547  OE2 GLU A 328      28.047  22.247   8.338  1.00 86.85           O  
ANISOU 2547  OE2 GLU A 328    13574   8524  10902   3611    246   -242       O  
ATOM   2548  N   GLY A 329      27.633  24.507  14.173  1.00 97.91           N  
ANISOU 2548  N   GLY A 329    15482   9997  11721   4145    969  -1896       N  
ATOM   2549  CA  GLY A 329      27.464  24.204  15.591  1.00 99.16           C  
ANISOU 2549  CA  GLY A 329    15446  10626  11602   4138   1112  -2181       C  
ATOM   2550  C   GLY A 329      26.168  23.528  16.015  1.00100.65           C  
ANISOU 2550  C   GLY A 329    15111  11454  11677   4489   1240  -2094       C  
ATOM   2551  O   GLY A 329      25.871  23.472  17.208  1.00102.85           O  
ANISOU 2551  O   GLY A 329    15274  12098  11705   4580   1409  -2349       O  
ATOM   2552  N   THR A 330      25.404  23.006  15.055  1.00101.13           N  
ANISOU 2552  N   THR A 330    14835  11693  11897   4656   1170  -1753       N  
ATOM   2553  CA  THR A 330      24.091  22.408  15.333  1.00102.68           C  
ANISOU 2553  CA  THR A 330    14484  12510  12020   4965   1301  -1682       C  
ATOM   2554  C   THR A 330      24.151  21.311  16.382  1.00 98.95           C  
ANISOU 2554  C   THR A 330    13674  12624  11297   4642   1432  -1674       C  
ATOM   2555  O   THR A 330      24.724  20.244  16.150  1.00 95.56           O  
ANISOU 2555  O   THR A 330    13092  12347  10869   4186   1344  -1412       O  
ATOM   2556  CB  THR A 330      23.434  21.816  14.058  1.00101.94           C  
ANISOU 2556  CB  THR A 330    14026  12587  12121   5037   1160  -1318       C  
ATOM   2557  OG1 THR A 330      22.755  22.854  13.343  1.00106.86           O  
ANISOU 2557  OG1 THR A 330    14796  12918  12889   5608   1116  -1334       O  
ATOM   2558  CG2 THR A 330      22.428  20.715  14.413  1.00101.32           C  
ANISOU 2558  CG2 THR A 330    13295  13253  11950   5021   1290  -1213       C  
ATOM   2559  N   CYS A 331      23.573  21.607  17.540  1.00 99.90           N  
ANISOU 2559  N   CYS A 331    13716  13051  11190   4907   1661  -1958       N  
ATOM   2560  CA  CYS A 331      23.281  20.609  18.551  1.00 98.87           C  
ANISOU 2560  CA  CYS A 331    13215  13564  10789   4726   1849  -1912       C  
ATOM   2561  C   CYS A 331      21.806  20.779  18.901  1.00104.22           C  
ANISOU 2561  C   CYS A 331    13497  14690  11413   5215   2085  -2025       C  
ATOM   2562  O   CYS A 331      21.210  21.806  18.563  1.00104.68           O  
ANISOU 2562  O   CYS A 331    13659  14516  11599   5726   2091  -2210       O  
ATOM   2563  CB  CYS A 331      24.161  20.822  19.783  1.00 99.36           C  
ANISOU 2563  CB  CYS A 331    13577  13648  10527   4536   1917  -2188       C  
ATOM   2564  SG  CYS A 331      25.938  20.839  19.442  1.00 95.69           S  
ANISOU 2564  SG  CYS A 331    13548  12701  10107   4007   1637  -2153       S  
ATOM   2565  N   PRO A 332      21.202  19.778  19.571  1.00106.86           N  
ANISOU 2565  N   PRO A 332    13375  15670  11557   5076   2299  -1903       N  
ATOM   2566  CA  PRO A 332      19.788  19.917  19.928  1.00112.21           C  
ANISOU 2566  CA  PRO A 332    13609  16855  12172   5511   2552  -2028       C  
ATOM   2567  C   PRO A 332      19.569  21.147  20.807  1.00119.42           C  
ANISOU 2567  C   PRO A 332    14792  17684  12898   6008   2714  -2492       C  
ATOM   2568  O   PRO A 332      20.466  21.509  21.568  1.00121.11           O  
ANISOU 2568  O   PRO A 332    15431  17685  12902   5861   2716  -2714       O  
ATOM   2569  CB  PRO A 332      19.483  18.624  20.701  1.00111.62           C  
ANISOU 2569  CB  PRO A 332    13125  17418  11868   5140   2796  -1825       C  
ATOM   2570  CG  PRO A 332      20.592  17.685  20.377  1.00106.28           C  
ANISOU 2570  CG  PRO A 332    12622  16520  11239   4558   2617  -1503       C  
ATOM   2571  CD  PRO A 332      21.785  18.522  20.078  1.00104.14           C  
ANISOU 2571  CD  PRO A 332    12921  15611  11034   4543   2348  -1648       C  
ATOM   2572  N   GLU A 333      18.407  21.791  20.689  1.00124.28           N  
ANISOU 2572  N   GLU A 333    15158  18477  13585   6601   2842  -2664       N  
ATOM   2573  CA  GLU A 333      18.117  23.002  21.466  1.00130.85           C  
ANISOU 2573  CA  GLU A 333    16260  19187  14269   7150   3020  -3137       C  
ATOM   2574  C   GLU A 333      16.911  22.815  22.413  1.00138.64           C  
ANISOU 2574  C   GLU A 333    16725  20957  14996   7471   3393  -3311       C  
ATOM   2575  O   GLU A 333      15.792  23.206  22.077  1.00142.39           O  
ANISOU 2575  O   GLU A 333    16842  21669  15592   8019   3483  -3382       O  
ATOM   2576  CB  GLU A 333      17.931  24.225  20.540  1.00132.00           C  
ANISOU 2576  CB  GLU A 333    16728  18704  14724   7706   2861  -3249       C  
ATOM   2577  CG  GLU A 333      16.740  24.193  19.556  1.00132.30           C  
ANISOU 2577  CG  GLU A 333    16259  19014  14994   8165   2808  -3044       C  
ATOM   2578  CD  GLU A 333      17.090  23.702  18.159  1.00125.98           C  
ANISOU 2578  CD  GLU A 333    15422  17970  14475   7870   2476  -2618       C  
ATOM   2579  OE1 GLU A 333      18.289  23.588  17.818  1.00119.96           O  
ANISOU 2579  OE1 GLU A 333    15106  16688  13783   7391   2280  -2489       O  
ATOM   2580  OE2 GLU A 333      16.142  23.442  17.386  1.00127.05           O  
ANISOU 2580  OE2 GLU A 333    15048  18481  14743   8130   2411  -2435       O  
ATOM   2581  N   ALA A 334      17.116  22.240  23.604  1.00141.50           N  
ANISOU 2581  N   ALA A 334    17024  21765  14976   7164   3622  -3378       N  
ATOM   2582  CA  ALA A 334      18.428  21.831  24.134  1.00139.50           C  
ANISOU 2582  CA  ALA A 334    17173  21320  14509   6603   3517  -3323       C  
ATOM   2583  C   ALA A 334      18.676  20.312  24.089  1.00136.16           C  
ANISOU 2583  C   ALA A 334    16439  21266  14030   5988   3514  -2835       C  
ATOM   2584  O   ALA A 334      19.737  19.879  23.631  1.00130.97           O  
ANISOU 2584  O   ALA A 334    16043  20246  13476   5552   3256  -2601       O  
ATOM   2585  CB  ALA A 334      18.604  22.355  25.562  1.00144.30           C  
ANISOU 2585  CB  ALA A 334    18025  22141  14662   6742   3754  -3766       C  
ATOM   2586  N   PRO A 335      17.726  19.496  24.598  1.00139.09           N  
ANISOU 2586  N   PRO A 335    16271  22348  14231   5943   3827  -2688       N  
ATOM   2587  CA  PRO A 335      17.899  18.045  24.491  1.00135.54           C  
ANISOU 2587  CA  PRO A 335    15567  22157  13775   5360   3859  -2209       C  
ATOM   2588  C   PRO A 335      17.068  17.416  23.365  1.00133.67           C  
ANISOU 2588  C   PRO A 335    14822  22047  13919   5267   3817  -1928       C  
ATOM   2589  O   PRO A 335      15.988  17.916  23.040  1.00138.31           O  
ANISOU 2589  O   PRO A 335    15042  22872  14639   5693   3899  -2096       O  
ATOM   2590  CB  PRO A 335      17.415  17.542  25.860  1.00139.97           C  
ANISOU 2590  CB  PRO A 335    15902  23414  13866   5309   4280  -2227       C  
ATOM   2591  CG  PRO A 335      16.528  18.653  26.420  1.00146.24           C  
ANISOU 2591  CG  PRO A 335    16588  24465  14512   5936   4503  -2713       C  
ATOM   2592  CD  PRO A 335      16.587  19.825  25.474  1.00145.70           C  
ANISOU 2592  CD  PRO A 335    16763  23785  14812   6367   4211  -2968       C  
ATOM   2593  N   THR A 336      17.578  16.334  22.775  1.00127.00           N  
ANISOU 2593  N   THR A 336    13953  21064  13237   4732   3683  -1529       N  
ATOM   2594  CA  THR A 336      16.797  15.529  21.834  1.00125.17           C  
ANISOU 2594  CA  THR A 336    13211  21038  13309   4521   3685  -1280       C  
ATOM   2595  C   THR A 336      15.738  14.765  22.619  1.00129.98           C  
ANISOU 2595  C   THR A 336    13285  22381  13722   4382   4129  -1209       C  
ATOM   2596  O   THR A 336      16.073  13.997  23.522  1.00130.60           O  
ANISOU 2596  O   THR A 336    13461  22642  13521   4039   4364  -1017       O  
ATOM   2597  CB  THR A 336      17.664  14.514  21.073  1.00119.48           C  
ANISOU 2597  CB  THR A 336    12648  19953  12796   3958   3467   -905       C  
ATOM   2598  OG1 THR A 336      18.566  13.876  21.985  1.00118.56           O  
ANISOU 2598  OG1 THR A 336    12850  19803  12395   3626   3571   -726       O  
ATOM   2599  CG2 THR A 336      18.461  15.194  19.974  1.00115.19           C  
ANISOU 2599  CG2 THR A 336    12477  18767  12523   4070   3041   -947       C  
ATOM   2600  N   ASP A 337      14.470  14.979  22.263  1.00133.59           N  
ANISOU 2600  N   ASP A 337    13169  23277  14311   4655   4249  -1350       N  
ATOM   2601  CA  ASP A 337      13.321  14.491  23.044  1.00137.71           C  
ANISOU 2601  CA  ASP A 337    13112  24575  14636   4604   4713  -1373       C  
ATOM   2602  C   ASP A 337      13.399  12.995  23.380  1.00137.51           C  
ANISOU 2602  C   ASP A 337    12957  24747  14546   3879   4975   -977       C  
ATOM   2603  O   ASP A 337      13.766  12.628  24.499  1.00138.30           O  
ANISOU 2603  O   ASP A 337    13288  24977  14284   3709   5243   -861       O  
ATOM   2604  CB  ASP A 337      12.004  14.816  22.319  1.00139.87           C  
ANISOU 2604  CB  ASP A 337    12706  25299  15141   4940   4722  -1551       C  
ATOM   2605  CG  ASP A 337      11.708  16.307  22.284  1.00141.20           C  
ANISOU 2605  CG  ASP A 337    12972  25384  15296   5771   4599  -1943       C  
ATOM   2606  OD1 ASP A 337      12.618  17.083  21.923  1.00137.39           O  
ANISOU 2606  OD1 ASP A 337    13094  24214  14896   5999   4272  -2014       O  
ATOM   2607  OD2 ASP A 337      10.567  16.700  22.610  1.00143.99           O  
ANISOU 2607  OD2 ASP A 337    12800  26346  15565   6195   4848  -2183       O  
ATOM   2608  N   GLU A 338      13.049  12.139  22.420  1.00136.02           N  
ANISOU 2608  N   GLU A 338    12420  24574  14688   3462   4909   -772       N  
ATOM   2609  CA  GLU A 338      13.151  10.688  22.606  1.00134.64           C  
ANISOU 2609  CA  GLU A 338    12185  24450  14521   2744   5159   -390       C  
ATOM   2610  C   GLU A 338      13.304   9.941  21.278  1.00129.36           C  
ANISOU 2610  C   GLU A 338    11422  23453  14276   2315   4895   -215       C  
ATOM   2611  O   GLU A 338      14.199   9.104  21.146  1.00127.23           O  
ANISOU 2611  O   GLU A 338    11541  22730  14069   1880   4833     89       O  
ATOM   2612  CB  GLU A 338      11.975  10.136  23.440  1.00142.72           C  
ANISOU 2612  CB  GLU A 338    12641  26235  15352   2547   5716   -375       C  
ATOM   2613  CG  GLU A 338      10.582  10.154  22.788  1.00147.93           C  
ANISOU 2613  CG  GLU A 338    12473  27486  16249   2578   5809   -585       C  
ATOM   2614  CD  GLU A 338      10.003  11.549  22.636  1.00150.55           C  
ANISOU 2614  CD  GLU A 338    12570  28073  16559   3383   5643  -1007       C  
ATOM   2615  OE1 GLU A 338       9.986  12.298  23.635  1.00153.01           O  
ANISOU 2615  OE1 GLU A 338    13042  28556  16538   3831   5825  -1198       O  
ATOM   2616  OE2 GLU A 338       9.552  11.889  21.521  1.00150.12           O  
ANISOU 2616  OE2 GLU A 338    12178  28056  16804   3588   5340  -1150       O  
ATOM   2617  N   CYS A 339      12.455  10.254  20.298  1.00127.50           N  
ANISOU 2617  N   CYS A 339    10676  23461  14305   2473   4730   -418       N  
ATOM   2618  CA  CYS A 339      12.526   9.625  18.977  1.00121.22           C  
ANISOU 2618  CA  CYS A 339     9752  22430  13878   2099   4457   -320       C  
ATOM   2619  C   CYS A 339      11.937  10.510  17.881  1.00120.82           C  
ANISOU 2619  C   CYS A 339     9354  22532  14022   2574   4101   -588       C  
ATOM   2620  O   CYS A 339      10.739  10.477  17.601  1.00125.23           O  
ANISOU 2620  O   CYS A 339     9207  23727  14650   2623   4206   -758       O  
ATOM   2621  CB  CYS A 339      11.830   8.257  18.974  1.00122.64           C  
ANISOU 2621  CB  CYS A 339     9475  22950  14173   1381   4812   -161       C  
ATOM   2622  SG  CYS A 339      12.877   6.835  19.397  1.00116.80           S  
ANISOU 2622  SG  CYS A 339     9306  21647  13426    660   5020    298       S  
ATOM   2623  N   LYS A 340      12.805  11.313  17.281  1.00116.61           N  
ANISOU 2623  N   LYS A 340     9322  21430  13554   2934   3687   -613       N  
ATOM   2624  CA  LYS A 340      12.511  12.022  16.038  1.00116.66           C  
ANISOU 2624  CA  LYS A 340     9157  21411  13757   3326   3290   -755       C  
ATOM   2625  C   LYS A 340      12.151  11.046  14.889  1.00114.33           C  
ANISOU 2625  C   LYS A 340     8451  21272  13717   2813   3156   -679       C  
ATOM   2626  O   LYS A 340      12.391   9.841  14.996  1.00113.05           O  
ANISOU 2626  O   LYS A 340     8304  21023  13624   2130   3340   -500       O  
ATOM   2627  CB  LYS A 340      13.708  12.922  15.676  1.00112.57           C  
ANISOU 2627  CB  LYS A 340     9373  20144  13254   3665   2930   -729       C  
ATOM   2628  CG  LYS A 340      14.900  12.227  15.003  1.00107.14           C  
ANISOU 2628  CG  LYS A 340     9144  18851  12714   3169   2702   -484       C  
ATOM   2629  CD  LYS A 340      15.818  11.499  15.993  1.00105.49           C  
ANISOU 2629  CD  LYS A 340     9351  18369  12360   2744   2924   -287       C  
ATOM   2630  CE  LYS A 340      15.472  10.018  16.151  1.00107.23           C  
ANISOU 2630  CE  LYS A 340     9268  18832  12644   2079   3214    -93       C  
ATOM   2631  NZ  LYS A 340      16.582   9.273  16.807  1.00104.92           N  
ANISOU 2631  NZ  LYS A 340     9486  18133  12247   1710   3329    177       N  
ATOM   2632  N   PRO A 341      11.592  11.571  13.780  1.00 67.59           N  
ANISOU 2632  N   PRO A 341     8907   9848   6927   1339   -283  -2162       N  
ATOM   2633  CA  PRO A 341      10.960  10.738  12.757  1.00 64.04           C  
ANISOU 2633  CA  PRO A 341     8317   9400   6617   1351   -223  -1916       C  
ATOM   2634  C   PRO A 341      11.934  10.027  11.831  1.00 58.59           C  
ANISOU 2634  C   PRO A 341     7665   8569   6026   1160   -309  -1592       C  
ATOM   2635  O   PRO A 341      12.995  10.575  11.505  1.00 60.27           O  
ANISOU 2635  O   PRO A 341     8027   8546   6328   1063   -447  -1576       O  
ATOM   2636  CB  PRO A 341      10.145  11.746  11.956  1.00 66.19           C  
ANISOU 2636  CB  PRO A 341     8609   9403   7138   1573   -288  -2071       C  
ATOM   2637  CG  PRO A 341      10.931  12.994  12.037  1.00 67.96           C  
ANISOU 2637  CG  PRO A 341     9056   9330   7437   1578   -450  -2248       C  
ATOM   2638  CD  PRO A 341      11.646  12.983  13.357  1.00 69.28           C  
ANISOU 2638  CD  PRO A 341     9275   9702   7347   1465   -426  -2378       C  
ATOM   2639  N   VAL A 342      11.545   8.829  11.393  1.00 52.27           N  
ANISOU 2639  N   VAL A 342     6726   7912   5223   1106   -220  -1352       N  
ATOM   2640  CA  VAL A 342      12.406   7.963  10.577  1.00 47.43           C  
ANISOU 2640  CA  VAL A 342     6125   7212   4684    936   -275  -1055       C  
ATOM   2641  C   VAL A 342      12.271   8.229   9.073  1.00 45.11           C  
ANISOU 2641  C   VAL A 342     5876   6625   4640    977   -350   -951       C  
ATOM   2642  O   VAL A 342      11.163   8.282   8.530  1.00 43.26           O  
ANISOU 2642  O   VAL A 342     5565   6369   4504   1119   -320   -974       O  
ATOM   2643  CB  VAL A 342      12.102   6.466  10.831  1.00 45.73           C  
ANISOU 2643  CB  VAL A 342     5763   7269   4341    846   -158   -840       C  
ATOM   2644  CG1 VAL A 342      12.562   5.600   9.638  1.00 40.96           C  
ANISOU 2644  CG1 VAL A 342     5145   6530   3886    744   -202   -564       C  
ATOM   2645  CG2 VAL A 342      12.736   6.005  12.139  1.00 42.20           C  
ANISOU 2645  CG2 VAL A 342     5337   7062   3634    732   -137   -836       C  
ATOM   2646  N   LYS A 343      13.413   8.378   8.411  1.00 43.12           N  
ANISOU 2646  N   LYS A 343     5741   6161   4480    846   -449   -836       N  
ATOM   2647  CA  LYS A 343      13.447   8.544   6.966  1.00 45.02           C  
ANISOU 2647  CA  LYS A 343     6056   6139   4912    843   -511   -705       C  
ATOM   2648  C   LYS A 343      13.449   7.177   6.252  1.00 42.31           C  
ANISOU 2648  C   LYS A 343     5608   5888   4579    757   -453   -448       C  
ATOM   2649  O   LYS A 343      14.488   6.495   6.177  1.00 39.89           O  
ANISOU 2649  O   LYS A 343     5295   5610   4250    599   -453   -303       O  
ATOM   2650  CB  LYS A 343      14.666   9.374   6.570  1.00 45.69           C  
ANISOU 2650  CB  LYS A 343     6315   5961   5083    717   -614   -710       C  
ATOM   2651  CG  LYS A 343      14.701  10.757   7.218  1.00 50.57           C  
ANISOU 2651  CG  LYS A 343     7063   6438   5714    789   -694   -971       C  
ATOM   2652  CD  LYS A 343      16.004  11.492   6.896  1.00 52.65           C  
ANISOU 2652  CD  LYS A 343     7484   6455   6065    611   -790   -963       C  
ATOM   2653  CE  LYS A 343      16.480  12.332   8.068  1.00 56.59           C  
ANISOU 2653  CE  LYS A 343     8048   6958   6495    592   -855  -1207       C  
ATOM   2654  NZ  LYS A 343      17.763  13.026   7.763  1.00 60.46           N  
ANISOU 2654  NZ  LYS A 343     8668   7213   7091    389   -950  -1201       N  
ATOM   2655  N   TRP A 344      12.279   6.777   5.748  1.00 38.83           N  
ANISOU 2655  N   TRP A 344     5075   5494   4186    868   -414   -409       N  
ATOM   2656  CA  TRP A 344      12.151   5.530   4.989  1.00 38.67           C  
ANISOU 2656  CA  TRP A 344     4969   5531   4193    797   -376   -188       C  
ATOM   2657  C   TRP A 344      12.562   5.767   3.552  1.00 39.76           C  
ANISOU 2657  C   TRP A 344     5241   5402   4462    761   -456    -75       C  
ATOM   2658  O   TRP A 344      12.228   6.809   2.981  1.00 44.68           O  
ANISOU 2658  O   TRP A 344     5986   5815   5176    859   -540   -157       O  
ATOM   2659  CB  TRP A 344      10.721   4.974   5.017  1.00 37.96           C  
ANISOU 2659  CB  TRP A 344     4710   5605   4106    907   -309   -198       C  
ATOM   2660  CG  TRP A 344      10.688   3.497   4.753  1.00 38.27           C  
ANISOU 2660  CG  TRP A 344     4644   5774   4122    794   -249      9       C  
ATOM   2661  CD1 TRP A 344      10.500   2.867   3.548  1.00 36.77           C  
ANISOU 2661  CD1 TRP A 344     4454   5482   4035    769   -286    156       C  
ATOM   2662  CD2 TRP A 344      10.889   2.462   5.714  1.00 40.81           C  
ANISOU 2662  CD2 TRP A 344     4872   6330   4304    684   -158     95       C  
ATOM   2663  NE1 TRP A 344      10.555   1.502   3.709  1.00 34.16           N  
ANISOU 2663  NE1 TRP A 344     4026   5296   3656    656   -222    311       N  
ATOM   2664  CE2 TRP A 344      10.789   1.229   5.030  1.00 38.70           C  
ANISOU 2664  CE2 TRP A 344     4548   6071   4087    602   -146    290       C  
ATOM   2665  CE3 TRP A 344      11.131   2.457   7.093  1.00 43.73           C  
ANISOU 2665  CE3 TRP A 344     5221   6897   4497    647    -97     26       C  
ATOM   2666  CZ2 TRP A 344      10.927   0.006   5.680  1.00 41.50           C  
ANISOU 2666  CZ2 TRP A 344     4830   6597   4340    485    -82    429       C  
ATOM   2667  CZ3 TRP A 344      11.270   1.246   7.735  1.00 45.56           C  
ANISOU 2667  CZ3 TRP A 344     5389   7317   4605    528    -33    178       C  
ATOM   2668  CH2 TRP A 344      11.170   0.032   7.027  1.00 44.98           C  
ANISOU 2668  CH2 TRP A 344     5264   7222   4606    448    -29    384       C  
ATOM   2669  N   CYS A 345      13.275   4.805   2.964  1.00 40.44           N  
ANISOU 2669  N   CYS A 345     5318   5493   4554    625   -432    109       N  
ATOM   2670  CA  CYS A 345      13.778   4.969   1.607  1.00 41.83           C  
ANISOU 2670  CA  CYS A 345     5630   5445   4818    564   -478    215       C  
ATOM   2671  C   CYS A 345      12.879   4.296   0.603  1.00 40.88           C  
ANISOU 2671  C   CYS A 345     5478   5313   4742    621   -489    317       C  
ATOM   2672  O   CYS A 345      12.856   3.072   0.496  1.00 45.03           O  
ANISOU 2672  O   CYS A 345     5897   5964   5247    564   -436    429       O  
ATOM   2673  CB  CYS A 345      15.213   4.468   1.445  1.00 42.95           C  
ANISOU 2673  CB  CYS A 345     5787   5577   4954    386   -444    318       C  
ATOM   2674  SG  CYS A 345      16.031   5.350   0.090  1.00 44.27           S  
ANISOU 2674  SG  CYS A 345     6169   5450   5202    286   -478    367       S  
ATOM   2675  N   ALA A 346      12.135   5.103  -0.136  1.00 40.90           N  
ANISOU 2675  N   ALA A 346     5583   5148   4810    738   -579    273       N  
ATOM   2676  CA  ALA A 346      11.288   4.590  -1.192  1.00 42.03           C  
ANISOU 2676  CA  ALA A 346     5716   5257   4995    797   -628    358       C  
ATOM   2677  C   ALA A 346      12.123   4.295  -2.441  1.00 41.14           C  
ANISOU 2677  C   ALA A 346     5762   4997   4875    666   -634    508       C  
ATOM   2678  O   ALA A 346      13.027   5.042  -2.802  1.00 40.69           O  
ANISOU 2678  O   ALA A 346     5876   4771   4812    582   -642    523       O  
ATOM   2679  CB  ALA A 346      10.170   5.582  -1.506  1.00 43.63           C  
ANISOU 2679  CB  ALA A 346     5969   5335   5272    992   -755    250       C  
ATOM   2680  N   LEU A 347      11.807   3.186  -3.090  1.00 42.29           N  
ANISOU 2680  N   LEU A 347     5843   5211   5015    640   -621    609       N  
ATOM   2681  CA  LEU A 347      12.462   2.785  -4.321  1.00 42.24           C  
ANISOU 2681  CA  LEU A 347     5974   5093   4982    532   -612    730       C  
ATOM   2682  C   LEU A 347      11.662   3.387  -5.463  1.00 41.79           C  
ANISOU 2682  C   LEU A 347     6082   4864   4932    626   -750    748       C  
ATOM   2683  O   LEU A 347      10.657   2.825  -5.886  1.00 48.18           O  
ANISOU 2683  O   LEU A 347     6820   5725   5763    708   -822    760       O  
ATOM   2684  CB  LEU A 347      12.490   1.242  -4.413  1.00 40.78           C  
ANISOU 2684  CB  LEU A 347     5649   5058   4790    468   -545    809       C  
ATOM   2685  CG  LEU A 347      13.679   0.535  -5.066  1.00 40.02           C  
ANISOU 2685  CG  LEU A 347     5609   4932   4665    326   -461    894       C  
ATOM   2686  CD1 LEU A 347      13.206  -0.740  -5.750  1.00 33.60           C  
ANISOU 2686  CD1 LEU A 347     4745   4165   3855    322   -470    956       C  
ATOM   2687  CD2 LEU A 347      14.422   1.446  -6.063  1.00 44.81           C  
ANISOU 2687  CD2 LEU A 347     6444   5350   5230    255   -458    919       C  
ATOM   2688  N   SER A 348      12.080   4.558  -5.931  1.00 43.68           N  
ANISOU 2688  N   SER A 348     6547   4892   5157    612   -805    752       N  
ATOM   2689  CA  SER A 348      11.414   5.250  -7.052  1.00 45.76           C  
ANISOU 2689  CA  SER A 348     7025   4953   5409    700   -966    793       C  
ATOM   2690  C   SER A 348       9.947   5.582  -6.750  1.00 46.71           C  
ANISOU 2690  C   SER A 348     7037   5094   5618    930  -1118    690       C  
ATOM   2691  O   SER A 348       9.439   5.265  -5.672  1.00 48.71           O  
ANISOU 2691  O   SER A 348     7043   5535   5930   1005  -1067    585       O  
ATOM   2692  CB  SER A 348      11.559   4.436  -8.351  1.00 46.87           C  
ANISOU 2692  CB  SER A 348     7271   5076   5460    612   -962    918       C  
ATOM   2693  OG  SER A 348      10.716   4.912  -9.379  1.00 50.01           O  
ANISOU 2693  OG  SER A 348     7853   5319   5829    717  -1149    959       O  
ATOM   2694  N   HIS A 349       9.268   6.215  -7.703  1.00 46.47           N  
ANISOU 2694  N   HIS A 349     7186   4877   5593   1043  -1306    720       N  
ATOM   2695  CA  HIS A 349       7.977   6.822  -7.419  1.00 44.37           C  
ANISOU 2695  CA  HIS A 349     6829   4587   5442   1288  -1475    598       C  
ATOM   2696  C   HIS A 349       6.894   5.832  -6.979  1.00 38.50           C  
ANISOU 2696  C   HIS A 349     5752   4103   4771   1381  -1464    521       C  
ATOM   2697  O   HIS A 349       6.175   6.114  -6.039  1.00 42.11           O  
ANISOU 2697  O   HIS A 349     6004   4670   5326   1524  -1461    370       O  
ATOM   2698  CB  HIS A 349       7.515   7.725  -8.562  1.00 49.13           C  
ANISOU 2698  CB  HIS A 349     7714   4913   6040   1400  -1717    658       C  
ATOM   2699  CG  HIS A 349       6.968   6.994  -9.741  1.00 52.19           C  
ANISOU 2699  CG  HIS A 349     8148   5315   6365   1405  -1834    760       C  
ATOM   2700  ND1 HIS A 349       7.772   6.463 -10.724  1.00 52.36           N  
ANISOU 2700  ND1 HIS A 349     8370   5297   6228   1209  -1768    915       N  
ATOM   2701  CD2 HIS A 349       5.692   6.736 -10.114  1.00 55.09           C  
ANISOU 2701  CD2 HIS A 349     8389   5734   6810   1583  -2023    713       C  
ATOM   2702  CE1 HIS A 349       7.015   5.893 -11.644  1.00 54.27           C  
ANISOU 2702  CE1 HIS A 349     8626   5561   6433   1265  -1916    958       C  
ATOM   2703  NE2 HIS A 349       5.749   6.043 -11.296  1.00 55.19           N  
ANISOU 2703  NE2 HIS A 349     8541   5730   6698   1487  -2082    842       N  
ATOM   2704  N   HIS A 350       6.800   4.669  -7.608  1.00 36.58           N  
ANISOU 2704  N   HIS A 350     5451   3966   4481   1287  -1442    615       N  
ATOM   2705  CA  HIS A 350       5.831   3.643  -7.172  1.00 36.95           C  
ANISOU 2705  CA  HIS A 350     5179   4255   4604   1327  -1416    556       C  
ATOM   2706  C   HIS A 350       5.844   3.427  -5.648  1.00 36.51           C  
ANISOU 2706  C   HIS A 350     4870   4416   4586   1313  -1235    454       C  
ATOM   2707  O   HIS A 350       4.799   3.425  -5.001  1.00 36.25           O  
ANISOU 2707  O   HIS A 350     4594   4533   4647   1437  -1243    331       O  
ATOM   2708  CB  HIS A 350       6.095   2.302  -7.858  1.00 36.02           C  
ANISOU 2708  CB  HIS A 350     5054   4212   4420   1168  -1366    673       C  
ATOM   2709  CG  HIS A 350       5.659   2.244  -9.288  1.00 40.51           C  
ANISOU 2709  CG  HIS A 350     5796   4648   4950   1203  -1561    739       C  
ATOM   2710  ND1 HIS A 350       6.472   2.634 -10.331  1.00 43.60           N  
ANISOU 2710  ND1 HIS A 350     6518   4844   5204   1125  -1598    848       N  
ATOM   2711  CD2 HIS A 350       4.507   1.809  -9.852  1.00 44.38           C  
ANISOU 2711  CD2 HIS A 350     6174   5184   5503   1292  -1730    710       C  
ATOM   2712  CE1 HIS A 350       5.834   2.461 -11.475  1.00 46.12           C  
ANISOU 2712  CE1 HIS A 350     6949   5092   5482   1175  -1789    887       C  
ATOM   2713  NE2 HIS A 350       4.638   1.963 -11.212  1.00 47.40           N  
ANISOU 2713  NE2 HIS A 350     6842   5395   5775   1281  -1887    800       N  
ATOM   2714  N   GLU A 351       7.023   3.240  -5.073  1.00 34.31           N  
ANISOU 2714  N   GLU A 351     4643   4167   4226   1161  -1071    500       N  
ATOM   2715  CA  GLU A 351       7.111   3.097  -3.631  1.00 37.41           C  
ANISOU 2715  CA  GLU A 351     4842   4755   4615   1142   -919    414       C  
ATOM   2716  C   GLU A 351       6.909   4.446  -2.941  1.00 39.31           C  
ANISOU 2716  C   GLU A 351     5112   4930   4895   1293   -957    253       C  
ATOM   2717  O   GLU A 351       6.208   4.531  -1.938  1.00 40.31           O  
ANISOU 2717  O   GLU A 351     5033   5231   5053   1385   -897    115       O  
ATOM   2718  CB  GLU A 351       8.447   2.471  -3.218  1.00 40.75           C  
ANISOU 2718  CB  GLU A 351     5309   5229   4947    948   -770    508       C  
ATOM   2719  CG  GLU A 351       8.571   0.960  -3.523  1.00 40.33           C  
ANISOU 2719  CG  GLU A 351     5167   5284   4873    817   -707    632       C  
ATOM   2720  CD  GLU A 351       9.575   0.238  -2.622  1.00 40.01           C  
ANISOU 2720  CD  GLU A 351     5068   5363   4771    678   -565    685       C  
ATOM   2721  OE1 GLU A 351      10.404   0.899  -1.964  1.00 40.98           O  
ANISOU 2721  OE1 GLU A 351     5250   5468   4853    654   -520    643       O  
ATOM   2722  OE2 GLU A 351       9.529  -1.010  -2.556  1.00 43.32           O  
ANISOU 2722  OE2 GLU A 351     5385   5885   5190    592   -515    768       O  
ATOM   2723  N   ARG A 352       7.515   5.498  -3.482  1.00 40.58           N  
ANISOU 2723  N   ARG A 352     5535   4835   5050   1309  -1049    266       N  
ATOM   2724  CA  ARG A 352       7.375   6.837  -2.914  1.00 44.66           C  
ANISOU 2724  CA  ARG A 352     6121   5230   5618   1453  -1111    108       C  
ATOM   2725  C   ARG A 352       5.953   7.155  -2.530  1.00 45.87           C  
ANISOU 2725  C   ARG A 352     6072   5473   5883   1692  -1185    -65       C  
ATOM   2726  O   ARG A 352       5.683   7.543  -1.403  1.00 45.70           O  
ANISOU 2726  O   ARG A 352     5913   5573   5877   1778  -1107   -240       O  
ATOM   2727  CB  ARG A 352       7.843   7.901  -3.902  1.00 49.45           C  
ANISOU 2727  CB  ARG A 352     7057   5496   6234   1463  -1263    172       C  
ATOM   2728  CG  ARG A 352       9.037   8.681  -3.439  1.00 51.53           C  
ANISOU 2728  CG  ARG A 352     7494   5626   6458   1343  -1203    154       C  
ATOM   2729  CD  ARG A 352       8.714   9.647  -2.318  1.00 52.73           C  
ANISOU 2729  CD  ARG A 352     7595   5767   6675   1493  -1220    -67       C  
ATOM   2730  NE  ARG A 352       9.836  10.565  -2.124  1.00 56.08           N  
ANISOU 2730  NE  ARG A 352     8242   5986   7081   1374  -1218    -78       N  
ATOM   2731  CZ  ARG A 352       9.840  11.612  -1.300  1.00 59.76           C  
ANISOU 2731  CZ  ARG A 352     8756   6352   7597   1468  -1258   -267       C  
ATOM   2732  NH1 ARG A 352       8.780  11.907  -0.554  1.00 61.26           N  
ANISOU 2732  NH1 ARG A 352     8781   6642   7852   1704  -1286   -477       N  
ATOM   2733  NH2 ARG A 352      10.919  12.379  -1.228  1.00 62.31           N  
ANISOU 2733  NH2 ARG A 352     9288   6474   7912   1320  -1265   -260       N  
ATOM   2734  N   LEU A 353       5.053   6.989  -3.487  1.00 48.80           N  
ANISOU 2734  N   LEU A 353     6420   5793   6331   1799  -1339    -28       N  
ATOM   2735  CA  LEU A 353       3.662   7.379  -3.316  1.00 53.64           C  
ANISOU 2735  CA  LEU A 353     6829   6465   7087   2051  -1449   -202       C  
ATOM   2736  C   LEU A 353       3.000   6.590  -2.184  1.00 51.08           C  
ANISOU 2736  C   LEU A 353     6134   6499   6774   2043  -1258   -318       C  
ATOM   2737  O   LEU A 353       2.202   7.144  -1.423  1.00 51.89           O  
ANISOU 2737  O   LEU A 353     6051   6704   6962   2226  -1241   -532       O  
ATOM   2738  CB  LEU A 353       2.883   7.215  -4.633  1.00 58.66           C  
ANISOU 2738  CB  LEU A 353     7504   6991   7795   2144  -1674   -121       C  
ATOM   2739  CG  LEU A 353       3.413   7.978  -5.863  1.00 63.86           C  
ANISOU 2739  CG  LEU A 353     8557   7294   8411   2148  -1878     17       C  
ATOM   2740  CD1 LEU A 353       2.463   7.805  -7.059  1.00 68.59           C  
ANISOU 2740  CD1 LEU A 353     9172   7821   9069   2271  -2129     71       C  
ATOM   2741  CD2 LEU A 353       3.661   9.468  -5.578  1.00 65.23           C  
ANISOU 2741  CD2 LEU A 353     8941   7206   8636   2287  -1975    -83       C  
ATOM   2742  N   LYS A 354       3.329   5.306  -2.064  1.00 44.79           N  
ANISOU 2742  N   LYS A 354     5239   5891   5889   1828  -1110   -182       N  
ATOM   2743  CA  LYS A 354       2.866   4.542  -0.919  1.00 43.08           C  
ANISOU 2743  CA  LYS A 354     4723   6000   5645   1769   -908   -254       C  
ATOM   2744  C   LYS A 354       3.513   5.128   0.317  1.00 45.49           C  
ANISOU 2744  C   LYS A 354     5067   6365   5852   1758   -767   -364       C  
ATOM   2745  O   LYS A 354       2.841   5.390   1.307  1.00 48.18           O  
ANISOU 2745  O   LYS A 354     5207   6898   6202   1859   -664   -550       O  
ATOM   2746  CB  LYS A 354       3.209   3.061  -1.035  1.00 38.25           C  
ANISOU 2746  CB  LYS A 354     4051   5526   4957   1532   -798    -64       C  
ATOM   2747  CG  LYS A 354       2.592   2.221   0.065  1.00 37.69           C  
ANISOU 2747  CG  LYS A 354     3684   5779   4859   1453   -604   -109       C  
ATOM   2748  CD  LYS A 354       2.974   0.761  -0.067  1.00 38.69           C  
ANISOU 2748  CD  LYS A 354     3790   5989   4922   1217   -522     92       C  
ATOM   2749  CE  LYS A 354       2.657  -0.025   1.208  1.00 39.50           C  
ANISOU 2749  CE  LYS A 354     3675   6388   4945   1091   -307     89       C  
ATOM   2750  NZ  LYS A 354       2.664  -1.506   0.986  1.00 37.01           N  
ANISOU 2750  NZ  LYS A 354     3303   6138   4621    882   -261    274       N  
ATOM   2751  N   CYS A 355       4.819   5.356   0.249  1.00 46.23           N  
ANISOU 2751  N   CYS A 355     5413   6301   5849   1633   -761   -264       N  
ATOM   2752  CA  CYS A 355       5.537   5.914   1.385  1.00 47.83           C  
ANISOU 2752  CA  CYS A 355     5672   6546   5954   1605   -657   -369       C  
ATOM   2753  C   CYS A 355       4.880   7.210   1.815  1.00 47.53           C  
ANISOU 2753  C   CYS A 355     5621   6439   6000   1845   -722   -621       C  
ATOM   2754  O   CYS A 355       4.480   7.347   2.956  1.00 50.48           O  
ANISOU 2754  O   CYS A 355     5834   7023   6325   1905   -596   -798       O  
ATOM   2755  CB  CYS A 355       7.013   6.136   1.048  1.00 48.98           C  
ANISOU 2755  CB  CYS A 355     6088   6491   6031   1449   -685   -241       C  
ATOM   2756  SG  CYS A 355       8.028   6.634   2.453  1.00 50.84           S  
ANISOU 2756  SG  CYS A 355     6379   6798   6138   1370   -577   -353       S  
ATOM   2757  N   ASP A 356       4.746   8.146   0.885  1.00 49.45           N  
ANISOU 2757  N   ASP A 356     6043   6383   6363   1986   -924   -639       N  
ATOM   2758  CA  ASP A 356       4.144   9.450   1.172  1.00 53.79           C  
ANISOU 2758  CA  ASP A 356     6614   6798   7024   2244  -1030   -881       C  
ATOM   2759  C   ASP A 356       2.812   9.351   1.895  1.00 56.25           C  
ANISOU 2759  C   ASP A 356     6586   7379   7408   2432   -950  -1103       C  
ATOM   2760  O   ASP A 356       2.497  10.204   2.725  1.00 61.52           O  
ANISOU 2760  O   ASP A 356     7204   8067   8103   2602   -922  -1356       O  
ATOM   2761  CB  ASP A 356       3.939  10.256  -0.117  1.00 55.52           C  
ANISOU 2761  CB  ASP A 356     7057   6660   7379   2382  -1294   -825       C  
ATOM   2762  CG  ASP A 356       5.205  10.940  -0.597  1.00 57.75           C  
ANISOU 2762  CG  ASP A 356     7710   6624   7610   2247  -1371   -702       C  
ATOM   2763  OD1 ASP A 356       6.273  10.777   0.031  1.00 57.58           O  
ANISOU 2763  OD1 ASP A 356     7749   6660   7467   2050  -1230   -668       O  
ATOM   2764  OD2 ASP A 356       5.128  11.653  -1.618  1.00 63.06           O  
ANISOU 2764  OD2 ASP A 356     8615   6983   8360   2332  -1581   -634       O  
ATOM   2765  N   GLU A 357       2.021   8.335   1.567  1.00 55.02           N  
ANISOU 2765  N   GLU A 357     6190   7427   7289   2400   -911  -1024       N  
ATOM   2766  CA  GLU A 357       0.722   8.160   2.208  1.00 58.73           C  
ANISOU 2766  CA  GLU A 357     6294   8182   7839   2548   -812  -1229       C  
ATOM   2767  C   GLU A 357       0.956   7.642   3.609  1.00 57.61           C  
ANISOU 2767  C   GLU A 357     6011   8364   7513   2402   -527  -1292       C  
ATOM   2768  O   GLU A 357       0.356   8.134   4.564  1.00 63.24           O  
ANISOU 2768  O   GLU A 357     6553   9252   8224   2545   -411  -1550       O  
ATOM   2769  CB  GLU A 357      -0.177   7.195   1.429  1.00 62.54           C  
ANISOU 2769  CB  GLU A 357     6553   8784   8424   2522   -860  -1121       C  
ATOM   2770  CG  GLU A 357      -1.669   7.312   1.786  1.00 68.87           C  
ANISOU 2770  CG  GLU A 357     6966   9812   9390   2735   -832  -1366       C  
ATOM   2771  CD  GLU A 357      -2.531   6.192   1.198  1.00 70.76           C  
ANISOU 2771  CD  GLU A 357     6937  10226   9720   2648   -844  -1263       C  
ATOM   2772  OE1 GLU A 357      -2.038   5.434   0.330  1.00 69.52           O  
ANISOU 2772  OE1 GLU A 357     6935   9960   9518   2467   -927  -1013       O  
ATOM   2773  OE2 GLU A 357      -3.706   6.070   1.614  1.00 72.51           O  
ANISOU 2773  OE2 GLU A 357     6784  10702  10065   2756   -764  -1450       O  
ATOM   2774  N   TRP A 358       1.841   6.655   3.728  1.00 53.06           N  
ANISOU 2774  N   TRP A 358     5520   7865   6774   2125   -420  -1062       N  
ATOM   2775  CA  TRP A 358       2.240   6.130   5.029  1.00 50.56           C  
ANISOU 2775  CA  TRP A 358     5138   7825   6249   1963   -184  -1074       C  
ATOM   2776  C   TRP A 358       2.653   7.279   5.935  1.00 49.63           C  
ANISOU 2776  C   TRP A 358     5141   7661   6054   2075   -160  -1301       C  
ATOM   2777  O   TRP A 358       2.234   7.342   7.086  1.00 51.12           O  
ANISOU 2777  O   TRP A 358     5176   8115   6132   2107     19  -1485       O  
ATOM   2778  CB  TRP A 358       3.384   5.120   4.884  1.00 48.82           C  
ANISOU 2778  CB  TRP A 358     5071   7587   5892   1686   -150   -788       C  
ATOM   2779  CG  TRP A 358       3.865   4.528   6.181  1.00 50.31           C  
ANISOU 2779  CG  TRP A 358     5228   8034   5854   1516     49   -764       C  
ATOM   2780  CD1 TRP A 358       3.201   4.518   7.375  1.00 52.45           C  
ANISOU 2780  CD1 TRP A 358     5314   8607   6009   1540    239   -930       C  
ATOM   2781  CD2 TRP A 358       5.101   3.831   6.405  1.00 46.93           C  
ANISOU 2781  CD2 TRP A 358     4959   7593   5278   1297     72   -558       C  
ATOM   2782  NE1 TRP A 358       3.951   3.880   8.324  1.00 53.13           N  
ANISOU 2782  NE1 TRP A 358     5468   8858   5862   1344    364   -824       N  
ATOM   2783  CE2 TRP A 358       5.120   3.443   7.759  1.00 48.92           C  
ANISOU 2783  CE2 TRP A 358     5137   8130   5319   1203    251   -596       C  
ATOM   2784  CE3 TRP A 358       6.191   3.505   5.596  1.00 42.99           C  
ANISOU 2784  CE3 TRP A 358     4653   6878   4804   1179    -41   -355       C  
ATOM   2785  CZ2 TRP A 358       6.186   2.745   8.323  1.00 45.50           C  
ANISOU 2785  CZ2 TRP A 358     4823   7753   4710   1009    284   -428       C  
ATOM   2786  CZ3 TRP A 358       7.250   2.809   6.158  1.00 43.78           C  
ANISOU 2786  CZ3 TRP A 358     4837   7044   4752    995     11   -210       C  
ATOM   2787  CH2 TRP A 358       7.238   2.436   7.507  1.00 43.82           C  
ANISOU 2787  CH2 TRP A 358     4773   7316   4560    918    154   -241       C  
ATOM   2788  N   SER A 359       3.446   8.202   5.396  1.00 49.03           N  
ANISOU 2788  N   SER A 359     5348   7247   6035   2128   -339  -1297       N  
ATOM   2789  CA  SER A 359       3.889   9.371   6.152  1.00 51.72           C  
ANISOU 2789  CA  SER A 359     5836   7485   6331   2229   -355  -1520       C  
ATOM   2790  C   SER A 359       2.730  10.174   6.713  1.00 55.65           C  
ANISOU 2790  C   SER A 359     6151   8075   6920   2511   -324  -1855       C  
ATOM   2791  O   SER A 359       2.695  10.472   7.906  1.00 60.07           O  
ANISOU 2791  O   SER A 359     6654   8826   7344   2542   -176  -2070       O  
ATOM   2792  CB  SER A 359       4.734  10.289   5.283  1.00 50.64           C  
ANISOU 2792  CB  SER A 359     6020   6927   6292   2246   -575  -1457       C  
ATOM   2793  OG  SER A 359       5.080  11.451   6.007  1.00 51.59           O  
ANISOU 2793  OG  SER A 359     6281   6925   6395   2346   -606  -1693       O  
ATOM   2794  N   VAL A 360       1.783  10.521   5.851  1.00 57.18           N  
ANISOU 2794  N   VAL A 360     6248   8138   7338   2724   -470  -1911       N  
ATOM   2795  CA  VAL A 360       0.636  11.333   6.264  1.00 62.62           C  
ANISOU 2795  CA  VAL A 360     6738   8890   8166   3035   -470  -2250       C  
ATOM   2796  C   VAL A 360      -0.059  10.735   7.489  1.00 63.06           C  
ANISOU 2796  C   VAL A 360     6465   9413   8083   3006   -169  -2417       C  
ATOM   2797  O   VAL A 360      -0.340  11.443   8.447  1.00 65.48           O  
ANISOU 2797  O   VAL A 360     6711   9826   8343   3159    -66  -2724       O  
ATOM   2798  CB  VAL A 360      -0.397  11.503   5.121  1.00 63.77           C  
ANISOU 2798  CB  VAL A 360     6759   8891   8581   3255   -678  -2252       C  
ATOM   2799  CG1 VAL A 360      -1.567  12.365   5.587  1.00 67.58           C  
ANISOU 2799  CG1 VAL A 360     7004   9439   9233   3606   -686  -2632       C  
ATOM   2800  CG2 VAL A 360       0.258  12.112   3.887  1.00 61.35           C  
ANISOU 2800  CG2 VAL A 360     6811   8123   8377   3273   -974  -2071       C  
ATOM   2801  N   ASN A 361      -0.310   9.429   7.450  1.00 61.49           N  
ANISOU 2801  N   ASN A 361     6075   9482   7806   2795    -24  -2212       N  
ATOM   2802  CA  ASN A 361      -1.017   8.734   8.525  1.00 64.39           C  
ANISOU 2802  CA  ASN A 361     6133  10301   8032   2718    277  -2319       C  
ATOM   2803  C   ASN A 361      -0.250   8.635   9.831  1.00 65.11           C  
ANISOU 2803  C   ASN A 361     6343  10587   7811   2554    479  -2357       C  
ATOM   2804  O   ASN A 361      -0.856   8.469  10.886  1.00 67.38           O  
ANISOU 2804  O   ASN A 361     6420  11227   7956   2553    729  -2537       O  
ATOM   2805  CB  ASN A 361      -1.391   7.317   8.088  1.00 64.61           C  
ANISOU 2805  CB  ASN A 361     5971  10516   8061   2495    356  -2051       C  
ATOM   2806  CG  ASN A 361      -2.717   7.262   7.387  1.00 67.54           C  
ANISOU 2806  CG  ASN A 361     6025  10939   8698   2667    288  -2146       C  
ATOM   2807  OD1 ASN A 361      -2.783   7.032   6.183  1.00 68.24           O  
ANISOU 2807  OD1 ASN A 361     6160  10815   8953   2676     71  -1976       O  
ATOM   2808  ND2 ASN A 361      -3.790   7.480   8.138  1.00 71.92           N  
ANISOU 2808  ND2 ASN A 361     6243  11791   9291   2808    472  -2433       N  
ATOM   2809  N   SER A 362       1.073   8.727   9.761  1.00 64.65           N  
ANISOU 2809  N   SER A 362     6612  10312   7638   2410    372  -2191       N  
ATOM   2810  CA  SER A 362       1.923   8.494  10.925  1.00 67.22           C  
ANISOU 2810  CA  SER A 362     7069  10813   7659   2225    519  -2178       C  
ATOM   2811  C   SER A 362       2.037   9.695  11.859  1.00 73.07           C  
ANISOU 2811  C   SER A 362     7904  11545   8312   2396    543  -2527       C  
ATOM   2812  O   SER A 362       2.748   9.616  12.859  1.00 76.00           O  
ANISOU 2812  O   SER A 362     8403  12058   8417   2259    638  -2549       O  
ATOM   2813  CB  SER A 362       3.325   8.092  10.468  1.00 63.57           C  
ANISOU 2813  CB  SER A 362     6887  10133   7134   2006    381  -1877       C  
ATOM   2814  OG  SER A 362       3.982   9.180   9.849  1.00 64.06           O  
ANISOU 2814  OG  SER A 362     7193   9810   7337   2117    156  -1936       O  
ATOM   2815  N   VAL A 363       1.342  10.789  11.537  1.00 77.39           N  
ANISOU 2815  N   VAL A 363     8400  11921   9084   2699    438  -2804       N  
ATOM   2816  CA  VAL A 363       1.447  12.072  12.261  1.00 82.76           C  
ANISOU 2816  CA  VAL A 363     9201  12505   9738   2901    412  -3166       C  
ATOM   2817  C   VAL A 363       2.894  12.447  12.626  1.00 84.27           C  
ANISOU 2817  C   VAL A 363     9744  12508   9768   2742    309  -3105       C  
ATOM   2818  O   VAL A 363       3.261  12.529  13.803  1.00 85.71           O  
ANISOU 2818  O   VAL A 363     9982  12895   9687   2671    441  -3253       O  
ATOM   2819  CB  VAL A 363       0.504  12.154  13.510  1.00 85.52           C  
ANISOU 2819  CB  VAL A 363     9293  13269   9931   3016    696  -3507       C  
ATOM   2820  CG1 VAL A 363      -0.921  12.469  13.078  1.00 87.35           C  
ANISOU 2820  CG1 VAL A 363     9200  13550  10438   3308    712  -3725       C  
ATOM   2821  CG2 VAL A 363       0.552  10.878  14.343  1.00 84.52           C  
ANISOU 2821  CG2 VAL A 363     9050  13580   9486   2724    972  -3328       C  
ATOM   2822  N   GLY A 364       3.705  12.654  11.590  1.00 82.77           N  
ANISOU 2822  N   GLY A 364     9781  11938   9731   2675     73  -2886       N  
ATOM   2823  CA  GLY A 364       5.068  13.152  11.743  1.00 80.69           C  
ANISOU 2823  CA  GLY A 364     9831  11440   9387   2535    -58  -2842       C  
ATOM   2824  C   GLY A 364       6.097  12.173  12.285  1.00 77.16           C  
ANISOU 2824  C   GLY A 364     9447  11191   8680   2222     28  -2607       C  
ATOM   2825  O   GLY A 364       7.183  12.595  12.674  1.00 77.34           O  
ANISOU 2825  O   GLY A 364     9684  11093   8610   2111    -59  -2629       O  
ATOM   2826  N   LYS A 365       5.781  10.877  12.304  1.00 72.80           N  
ANISOU 2826  N   LYS A 365     8711  10924   8024   2080    178  -2382       N  
ATOM   2827  CA  LYS A 365       6.733   9.862  12.789  1.00 68.44           C  
ANISOU 2827  CA  LYS A 365     8221  10543   7239   1800    235  -2137       C  
ATOM   2828  C   LYS A 365       7.505   9.141  11.676  1.00 58.85           C  
ANISOU 2828  C   LYS A 365     7084   9133   6144   1629    111  -1781       C  
ATOM   2829  O   LYS A 365       8.478   8.445  11.961  1.00 56.00           O  
ANISOU 2829  O   LYS A 365     6801   8836   5640   1421    106  -1589       O  
ATOM   2830  CB  LYS A 365       6.028   8.832  13.682  1.00 72.21           C  
ANISOU 2830  CB  LYS A 365     8492  11460   7484   1715    485  -2104       C  
ATOM   2831  CG  LYS A 365       5.581   9.380  15.046  1.00 78.83           C  
ANISOU 2831  CG  LYS A 365     9294  12568   8091   1809    648  -2437       C  
ATOM   2832  CD  LYS A 365       5.998   8.449  16.191  1.00 81.16           C  
ANISOU 2832  CD  LYS A 365     9617  13207   8015   1581    798  -2313       C  
ATOM   2833  CE  LYS A 365       5.217   8.690  17.484  1.00 85.06           C  
ANISOU 2833  CE  LYS A 365    10013  14067   8240   1651   1039  -2608       C  
ATOM   2834  NZ  LYS A 365       5.626   7.724  18.555  1.00 84.82           N  
ANISOU 2834  NZ  LYS A 365    10047  14364   7818   1408   1172  -2441       N  
ATOM   2835  N   ILE A 366       7.070   9.295  10.425  1.00 54.87           N  
ANISOU 2835  N   ILE A 366     6556   8399   5893   1725      8  -1702       N  
ATOM   2836  CA  ILE A 366       7.750   8.687   9.272  1.00 50.67           C  
ANISOU 2836  CA  ILE A 366     6107   7672   5471   1580   -101  -1395       C  
ATOM   2837  C   ILE A 366       7.902   9.687   8.116  1.00 51.51           C  
ANISOU 2837  C   ILE A 366     6382   7380   5810   1689   -298  -1411       C  
ATOM   2838  O   ILE A 366       6.911  10.169   7.561  1.00 50.65           O  
ANISOU 2838  O   ILE A 366     6209   7172   5864   1891   -354  -1513       O  
ATOM   2839  CB  ILE A 366       6.995   7.430   8.757  1.00 48.56           C  
ANISOU 2839  CB  ILE A 366     5639   7576   5237   1525    -13  -1190       C  
ATOM   2840  CG1 ILE A 366       7.024   6.305   9.798  1.00 51.54           C  
ANISOU 2840  CG1 ILE A 366     5902   8304   5377   1359    167  -1096       C  
ATOM   2841  CG2 ILE A 366       7.610   6.913   7.458  1.00 42.60           C  
ANISOU 2841  CG2 ILE A 366     4983   6596   4607   1412   -133   -919       C  
ATOM   2842  CD1 ILE A 366       8.423   5.733  10.070  1.00 49.44           C  
ANISOU 2842  CD1 ILE A 366     5789   8021   4976   1145    124   -902       C  
ATOM   2843  N   GLU A 367       9.147   9.992   7.755  1.00 52.08           N  
ANISOU 2843  N   GLU A 367     6667   7224   5898   1549   -407  -1307       N  
ATOM   2844  CA  GLU A 367       9.426  10.819   6.578  1.00 55.19           C  
ANISOU 2844  CA  GLU A 367     7254   7232   6483   1589   -580  -1259       C  
ATOM   2845  C   GLU A 367       9.844   9.937   5.412  1.00 51.60           C  
ANISOU 2845  C   GLU A 367     6821   6707   6077   1439   -603   -955       C  
ATOM   2846  O   GLU A 367      10.327   8.819   5.604  1.00 49.14           O  
ANISOU 2846  O   GLU A 367     6423   6589   5660   1273   -511   -790       O  
ATOM   2847  CB  GLU A 367      10.509  11.862   6.877  1.00 60.18           C  
ANISOU 2847  CB  GLU A 367     8114   7636   7117   1516   -677  -1363       C  
ATOM   2848  CG  GLU A 367       9.969  13.162   7.490  1.00 64.87           C  
ANISOU 2848  CG  GLU A 367     8776   8110   7761   1730   -739  -1689       C  
ATOM   2849  CD  GLU A 367      10.994  13.885   8.352  1.00 66.75           C  
ANISOU 2849  CD  GLU A 367     9169   8275   7919   1625   -780  -1843       C  
ATOM   2850  OE1 GLU A 367      12.206  13.844   8.026  1.00 64.99           O  
ANISOU 2850  OE1 GLU A 367     9073   7921   7701   1402   -836  -1689       O  
ATOM   2851  OE2 GLU A 367      10.575  14.491   9.360  1.00 69.81           O  
ANISOU 2851  OE2 GLU A 367     9537   8748   8238   1766   -753  -2135       O  
ATOM   2852  N   CYS A 368       9.647  10.449   4.203  1.00 51.73           N  
ANISOU 2852  N   CYS A 368     6969   6439   6247   1505   -736   -886       N  
ATOM   2853  CA  CYS A 368       9.929   9.697   2.992  1.00 51.56           C  
ANISOU 2853  CA  CYS A 368     6987   6342   6261   1385   -761   -625       C  
ATOM   2854  C   CYS A 368      11.041  10.359   2.204  1.00 51.44           C  
ANISOU 2854  C   CYS A 368     7235   6017   6291   1250   -854   -523       C  
ATOM   2855  O   CYS A 368      11.135  11.592   2.125  1.00 48.86           O  
ANISOU 2855  O   CYS A 368     7094   5430   6042   1317   -966   -636       O  
ATOM   2856  CB  CYS A 368       8.679   9.591   2.120  1.00 54.72           C  
ANISOU 2856  CB  CYS A 368     7318   6702   6772   1559   -837   -602       C  
ATOM   2857  SG  CYS A 368       7.382   8.541   2.818  1.00 61.93           S  
ANISOU 2857  SG  CYS A 368     7875   8006   7650   1652   -699   -668       S  
ATOM   2858  N   VAL A 369      11.883   9.514   1.626  1.00 48.30           N  
ANISOU 2858  N   VAL A 369     6852   5649   5851   1051   -800   -314       N  
ATOM   2859  CA  VAL A 369      12.971   9.948   0.782  1.00 47.48           C  
ANISOU 2859  CA  VAL A 369     6962   5300   5779    883   -843   -193       C  
ATOM   2860  C   VAL A 369      13.188   8.809  -0.193  1.00 44.75           C  
ANISOU 2860  C   VAL A 369     6578   5020   5406    772   -787     25       C  
ATOM   2861  O   VAL A 369      13.175   7.658   0.209  1.00 44.13           O  
ANISOU 2861  O   VAL A 369     6310   5188   5268    733   -691     76       O  
ATOM   2862  CB  VAL A 369      14.233  10.205   1.623  1.00 49.76           C  
ANISOU 2862  CB  VAL A 369     7268   5615   6023    712   -798   -253       C  
ATOM   2863  CG1 VAL A 369      15.494  10.064   0.791  1.00 48.84           C  
ANISOU 2863  CG1 VAL A 369     7256   5378   5922    478   -769    -87       C  
ATOM   2864  CG2 VAL A 369      14.162  11.587   2.274  1.00 55.38           C  
ANISOU 2864  CG2 VAL A 369     8108   6152   6781    797   -890   -469       C  
ATOM   2865  N   SER A 370      13.367   9.116  -1.472  1.00 44.43           N  
ANISOU 2865  N   SER A 370     6732   4753   5398    721   -848    151       N  
ATOM   2866  CA  SER A 370      13.514   8.067  -2.473  1.00 41.25           C  
ANISOU 2866  CA  SER A 370     6311   4405   4956    630   -797    333       C  
ATOM   2867  C   SER A 370      14.834   8.084  -3.216  1.00 40.55           C  
ANISOU 2867  C   SER A 370     6364   4203   4841    403   -732    457       C  
ATOM   2868  O   SER A 370      15.482   9.121  -3.345  1.00 43.72           O  
ANISOU 2868  O   SER A 370     6946   4400   5267    311   -761    440       O  
ATOM   2869  CB  SER A 370      12.388   8.147  -3.490  1.00 41.65           C  
ANISOU 2869  CB  SER A 370     6445   4347   5034    778   -918    383       C  
ATOM   2870  OG  SER A 370      12.144   9.488  -3.863  1.00 43.40           O  
ANISOU 2870  OG  SER A 370     6898   4284   5310    863  -1062    341       O  
ATOM   2871  N   ALA A 371      15.204   6.902  -3.697  1.00 37.57           N  
ANISOU 2871  N   ALA A 371     5893   3962   4419    310   -636    571       N  
ATOM   2872  CA  ALA A 371      16.300   6.708  -4.627  1.00 38.61           C  
ANISOU 2872  CA  ALA A 371     6130   4022   4519    114   -550    688       C  
ATOM   2873  C   ALA A 371      15.780   5.768  -5.712  1.00 39.33           C  
ANISOU 2873  C   ALA A 371     6236   4149   4558    144   -544    799       C  
ATOM   2874  O   ALA A 371      14.733   5.150  -5.536  1.00 38.75           O  
ANISOU 2874  O   ALA A 371     6043   4186   4493    288   -598    781       O  
ATOM   2875  CB  ALA A 371      17.497   6.105  -3.919  1.00 35.82           C  
ANISOU 2875  CB  ALA A 371     5602   3830   4177    -27   -429    668       C  
ATOM   2876  N   GLU A 372      16.507   5.659  -6.824  1.00 41.34           N  
ANISOU 2876  N   GLU A 372     6633   4320   4754     -4   -473    901       N  
ATOM   2877  CA  GLU A 372      16.021   4.921  -7.997  1.00 38.13           C  
ANISOU 2877  CA  GLU A 372     6300   3915   4272     19   -485    994       C  
ATOM   2878  C   GLU A 372      16.503   3.468  -8.049  1.00 35.77           C  
ANISOU 2878  C   GLU A 372     5815   3810   3965    -37   -360   1012       C  
ATOM   2879  O   GLU A 372      15.944   2.664  -8.796  1.00 33.54           O  
ANISOU 2879  O   GLU A 372     5546   3561   3636      9   -385   1055       O  
ATOM   2880  CB  GLU A 372      16.395   5.652  -9.291  1.00 37.65           C  
ANISOU 2880  CB  GLU A 372     6547   3646   4112    -99   -484   1095       C  
ATOM   2881  CG  GLU A 372      15.616   6.916  -9.530  1.00 41.52           C  
ANISOU 2881  CG  GLU A 372     7270   3903   4602      1   -666   1109       C  
ATOM   2882  CD  GLU A 372      14.142   6.661  -9.820  1.00 48.54           C  
ANISOU 2882  CD  GLU A 372     8152   4798   5495    224   -849   1102       C  
ATOM   2883  OE1 GLU A 372      13.315   6.941  -8.920  1.00 52.24           O  
ANISOU 2883  OE1 GLU A 372     8482   5299   6068    401   -950    995       O  
ATOM   2884  OE2 GLU A 372      13.809   6.192 -10.941  1.00 49.72           O  
ANISOU 2884  OE2 GLU A 372     8425   4928   5539    222   -892   1190       O  
ATOM   2885  N   THR A 373      17.545   3.140  -7.289  1.00 35.32           N  
ANISOU 2885  N   THR A 373     5594   3864   3961   -131   -247    972       N  
ATOM   2886  CA  THR A 373      17.890   1.731  -7.023  1.00 37.83           C  
ANISOU 2886  CA  THR A 373     5703   4361   4308   -134   -169    972       C  
ATOM   2887  C   THR A 373      17.993   1.502  -5.525  1.00 38.28           C  
ANISOU 2887  C   THR A 373     5551   4559   4435    -89   -185    910       C  
ATOM   2888  O   THR A 373      17.963   2.444  -4.744  1.00 44.43           O  
ANISOU 2888  O   THR A 373     6343   5308   5231    -75   -232    849       O  
ATOM   2889  CB  THR A 373      19.218   1.269  -7.682  1.00 36.16           C  
ANISOU 2889  CB  THR A 373     5478   4171   4089   -287    -14    989       C  
ATOM   2890  OG1 THR A 373      20.339   1.914  -7.051  1.00 35.58           O  
ANISOU 2890  OG1 THR A 373     5339   4103   4076   -404     50    942       O  
ATOM   2891  CG2 THR A 373      19.201   1.544  -9.182  1.00 35.02           C  
ANISOU 2891  CG2 THR A 373     5571   3903   3831   -359     28   1052       C  
ATOM   2892  N   THR A 374      18.117   0.246  -5.122  1.00 35.25           N  
ANISOU 2892  N   THR A 374     4995   4318   4082    -68   -156    925       N  
ATOM   2893  CA  THR A 374      18.159  -0.064  -3.705  1.00 33.66           C  
ANISOU 2893  CA  THR A 374     4622   4256   3911    -29   -183    890       C  
ATOM   2894  C   THR A 374      19.579   0.218  -3.173  1.00 31.17           C  
ANISOU 2894  C   THR A 374     4235   3970   3639   -135   -135    847       C  
ATOM   2895  O   THR A 374      19.742   0.913  -2.181  1.00 27.79           O  
ANISOU 2895  O   THR A 374     3777   3573   3209   -138   -178    783       O  
ATOM   2896  CB  THR A 374      17.563  -1.487  -3.382  1.00 32.96           C  
ANISOU 2896  CB  THR A 374     4402   4288   3833     35   -200    944       C  
ATOM   2897  OG1 THR A 374      18.452  -2.221  -2.544  1.00 36.20           O  
ANISOU 2897  OG1 THR A 374     4671   4802   4279      3   -182    954       O  
ATOM   2898  CG2 THR A 374      17.287  -2.290  -4.635  1.00 34.23           C  
ANISOU 2898  CG2 THR A 374     4622   4390   3996     36   -181    996       C  
ATOM   2899  N   GLU A 375      20.603  -0.238  -3.877  1.00 32.38           N  
ANISOU 2899  N   GLU A 375     4358   4112   3833   -224    -48    864       N  
ATOM   2900  CA  GLU A 375      21.972   0.175  -3.562  1.00 33.48           C  
ANISOU 2900  CA  GLU A 375     4415   4270   4035   -341      1    808       C  
ATOM   2901  C   GLU A 375      22.081   1.685  -3.267  1.00 35.25           C  
ANISOU 2901  C   GLU A 375     4750   4396   4247   -413    -28    750       C  
ATOM   2902  O   GLU A 375      22.738   2.090  -2.296  1.00 37.07           O  
ANISOU 2902  O   GLU A 375     4887   4679   4519   -458    -67    680       O  
ATOM   2903  CB  GLU A 375      22.927  -0.226  -4.694  1.00 36.03           C  
ANISOU 2903  CB  GLU A 375     4724   4571   4397   -439    136    814       C  
ATOM   2904  CG  GLU A 375      23.237  -1.734  -4.745  1.00 38.24           C  
ANISOU 2904  CG  GLU A 375     4845   4947   4735   -371    156    827       C  
ATOM   2905  CD  GLU A 375      24.289  -2.109  -5.798  1.00 44.43           C  
ANISOU 2905  CD  GLU A 375     5583   5732   5567   -456    309    790       C  
ATOM   2906  OE1 GLU A 375      24.138  -1.749  -6.983  1.00 50.20           O  
ANISOU 2906  OE1 GLU A 375     6479   6380   6215   -524    408    806       O  
ATOM   2907  OE2 GLU A 375      25.274  -2.780  -5.451  1.00 48.47           O  
ANISOU 2907  OE2 GLU A 375     5892   6332   6194   -450    330    738       O  
ATOM   2908  N   ASP A 376      21.433   2.517  -4.083  1.00 35.83           N  
ANISOU 2908  N   ASP A 376     5035   4314   4267   -420    -30    777       N  
ATOM   2909  CA  ASP A 376      21.403   3.969  -3.825  1.00 35.78           C  
ANISOU 2909  CA  ASP A 376     5169   4167   4260   -470    -83    725       C  
ATOM   2910  C   ASP A 376      20.717   4.279  -2.496  1.00 39.04           C  
ANISOU 2910  C   ASP A 376     5526   4642   4665   -345   -198    642       C  
ATOM   2911  O   ASP A 376      21.158   5.149  -1.759  1.00 40.87           O  
ANISOU 2911  O   ASP A 376     5766   4838   4924   -398   -241    551       O  
ATOM   2912  CB  ASP A 376      20.704   4.732  -4.951  1.00 34.55           C  
ANISOU 2912  CB  ASP A 376     5274   3810   4042   -468   -101    786       C  
ATOM   2913  CG  ASP A 376      21.518   4.781  -6.245  1.00 35.68           C  
ANISOU 2913  CG  ASP A 376     5530   3872   4154   -642     31    859       C  
ATOM   2914  OD1 ASP A 376      22.700   4.389  -6.253  1.00 36.60           O  
ANISOU 2914  OD1 ASP A 376     5503   4082   4323   -775    152    837       O  
ATOM   2915  OD2 ASP A 376      20.957   5.225  -7.274  1.00 35.09           O  
ANISOU 2915  OD2 ASP A 376     5691   3646   3996   -643     12    936       O  
ATOM   2916  N   CYS A 377      19.638   3.568  -2.193  1.00 39.98           N  
ANISOU 2916  N   CYS A 377     5589   4860   4743   -191   -242    662       N  
ATOM   2917  CA  CYS A 377      18.972   3.731  -0.910  1.00 40.67           C  
ANISOU 2917  CA  CYS A 377     5603   5050   4799    -80   -314    579       C  
ATOM   2918  C   CYS A 377      19.888   3.258   0.211  1.00 40.92           C  
ANISOU 2918  C   CYS A 377     5471   5244   4832   -134   -315    542       C  
ATOM   2919  O   CYS A 377      20.065   3.950   1.221  1.00 45.02           O  
ANISOU 2919  O   CYS A 377     5984   5793   5329   -136   -370    435       O  
ATOM   2920  CB  CYS A 377      17.630   2.988  -0.871  1.00 40.67           C  
ANISOU 2920  CB  CYS A 377     5552   5142   4759     67   -335    617       C  
ATOM   2921  SG  CYS A 377      16.225   3.982  -1.417  1.00 43.15           S  
ANISOU 2921  SG  CYS A 377     6016   5305   5072    208   -414    572       S  
ATOM   2922  N   ILE A 378      20.493   2.090   0.038  1.00 36.77           N  
ANISOU 2922  N   ILE A 378     4822   4814   4333   -171   -272    621       N  
ATOM   2923  CA  ILE A 378      21.400   1.595   1.059  1.00 33.62           C  
ANISOU 2923  CA  ILE A 378     4271   4558   3945   -207   -308    598       C  
ATOM   2924  C   ILE A 378      22.426   2.658   1.371  1.00 35.90           C  
ANISOU 2924  C   ILE A 378     4570   4791   4281   -324   -333    494       C  
ATOM   2925  O   ILE A 378      22.641   2.985   2.529  1.00 38.76           O  
ANISOU 2925  O   ILE A 378     4888   5236   4602   -321   -415    410       O  
ATOM   2926  CB  ILE A 378      22.137   0.333   0.651  1.00 29.43           C  
ANISOU 2926  CB  ILE A 378     3614   4087   3482   -230   -270    680       C  
ATOM   2927  CG1 ILE A 378      21.179  -0.856   0.619  1.00 31.79           C  
ANISOU 2927  CG1 ILE A 378     3891   4450   3739   -127   -273    779       C  
ATOM   2928  CG2 ILE A 378      23.199   0.044   1.641  1.00 26.96           C  
ANISOU 2928  CG2 ILE A 378     3154   3890   3201   -265   -340    644       C  
ATOM   2929  CD1 ILE A 378      21.883  -2.208   0.553  1.00 30.93           C  
ANISOU 2929  CD1 ILE A 378     3654   4397   3699   -121   -276    849       C  
ATOM   2930  N   ALA A 379      23.033   3.220   0.332  1.00 34.44           N  
ANISOU 2930  N   ALA A 379     4452   4463   4171   -443   -262    497       N  
ATOM   2931  CA  ALA A 379      24.069   4.221   0.533  1.00 34.57           C  
ANISOU 2931  CA  ALA A 379     4468   4411   4255   -595   -274    404       C  
ATOM   2932  C   ALA A 379      23.513   5.441   1.257  1.00 37.08           C  
ANISOU 2932  C   ALA A 379     4922   4642   4525   -568   -366    296       C  
ATOM   2933  O   ALA A 379      24.175   5.994   2.137  1.00 41.21           O  
ANISOU 2933  O   ALA A 379     5397   5193   5070   -638   -440    184       O  
ATOM   2934  CB  ALA A 379      24.681   4.617  -0.783  1.00 35.58           C  
ANISOU 2934  CB  ALA A 379     4671   4398   4449   -748   -154    445       C  
ATOM   2935  N   LYS A 380      22.295   5.849   0.898  1.00 36.97           N  
ANISOU 2935  N   LYS A 380     5069   4522   4455   -455   -374    312       N  
ATOM   2936  CA  LYS A 380      21.604   6.940   1.591  1.00 38.94           C  
ANISOU 2936  CA  LYS A 380     5440   4687   4667   -378   -463    187       C  
ATOM   2937  C   LYS A 380      21.415   6.635   3.085  1.00 38.74           C  
ANISOU 2937  C   LYS A 380     5297   4868   4554   -289   -531     89       C  
ATOM   2938  O   LYS A 380      21.495   7.529   3.929  1.00 38.64           O  
ANISOU 2938  O   LYS A 380     5335   4827   4519   -291   -607    -62       O  
ATOM   2939  CB  LYS A 380      20.242   7.227   0.950  1.00 43.09           C  
ANISOU 2939  CB  LYS A 380     6113   5096   5164   -229   -472    220       C  
ATOM   2940  CG  LYS A 380      20.264   8.206  -0.244  1.00 48.85           C  
ANISOU 2940  CG  LYS A 380     7068   5544   5949   -303   -473    265       C  
ATOM   2941  CD  LYS A 380      18.827   8.551  -0.709  1.00 51.08           C  
ANISOU 2941  CD  LYS A 380     7487   5714   6208   -113   -537    274       C  
ATOM   2942  CE  LYS A 380      18.746   9.816  -1.569  1.00 54.09           C  
ANISOU 2942  CE  LYS A 380     8142   5777   6634   -154   -600    291       C  
ATOM   2943  NZ  LYS A 380      19.113   9.575  -2.995  1.00 54.88           N  
ANISOU 2943  NZ  LYS A 380     8363   5773   6716   -282   -531    465       N  
ATOM   2944  N   ILE A 381      21.156   5.379   3.420  1.00 36.97           N  
ANISOU 2944  N   ILE A 381     4935   4844   4267   -217   -507    173       N  
ATOM   2945  CA  ILE A 381      21.029   5.022   4.822  1.00 38.30           C  
ANISOU 2945  CA  ILE A 381     5016   5218   4319   -157   -565    109       C  
ATOM   2946  C   ILE A 381      22.386   5.135   5.500  1.00 37.66           C  
ANISOU 2946  C   ILE A 381     4853   5195   4263   -282   -641     46       C  
ATOM   2947  O   ILE A 381      22.479   5.615   6.626  1.00 41.73           O  
ANISOU 2947  O   ILE A 381     5379   5788   4688   -274   -726    -84       O  
ATOM   2948  CB  ILE A 381      20.447   3.614   5.023  1.00 38.26           C  
ANISOU 2948  CB  ILE A 381     4905   5393   4238    -76   -527    240       C  
ATOM   2949  CG1 ILE A 381      18.979   3.592   4.603  1.00 38.72           C  
ANISOU 2949  CG1 ILE A 381     5016   5429   4265     49   -471    262       C  
ATOM   2950  CG2 ILE A 381      20.547   3.205   6.472  1.00 36.19           C  
ANISOU 2950  CG2 ILE A 381     4575   5344   3833    -55   -590    204       C  
ATOM   2951  CD1 ILE A 381      18.397   2.196   4.457  1.00 36.56           C  
ANISOU 2951  CD1 ILE A 381     4649   5280   3961     91   -423    412       C  
ATOM   2952  N   MET A 382      23.437   4.727   4.801  1.00 35.88           N  
ANISOU 2952  N   MET A 382     4538   4936   4160   -396   -614    120       N  
ATOM   2953  CA  MET A 382      24.785   4.777   5.362  1.00 37.73           C  
ANISOU 2953  CA  MET A 382     4647   5234   4454   -515   -697     56       C  
ATOM   2954  C   MET A 382      25.217   6.195   5.692  1.00 39.63           C  
ANISOU 2954  C   MET A 382     4974   5351   4731   -624   -761   -111       C  
ATOM   2955  O   MET A 382      25.876   6.419   6.701  1.00 38.70           O  
ANISOU 2955  O   MET A 382     4792   5325   4587   -671   -883   -222       O  
ATOM   2956  CB  MET A 382      25.812   4.228   4.382  1.00 38.19           C  
ANISOU 2956  CB  MET A 382     4576   5264   4671   -620   -625    136       C  
ATOM   2957  CG  MET A 382      25.645   2.800   3.985  1.00 38.11           C  
ANISOU 2957  CG  MET A 382     4468   5347   4663   -529   -575    279       C  
ATOM   2958  SD  MET A 382      26.832   2.478   2.675  1.00 44.24           S  
ANISOU 2958  SD  MET A 382     5117   6062   5631   -657   -454    313       S  
ATOM   2959  CE  MET A 382      25.967   1.175   1.831  1.00 38.00           C  
ANISOU 2959  CE  MET A 382     4353   5279   4806   -522   -362    465       C  
ATOM   2960  N   ASN A 383      24.860   7.140   4.821  1.00 42.67           N  
ANISOU 2960  N   ASN A 383     5522   5514   5178   -668   -696   -126       N  
ATOM   2961  CA  ASN A 383      25.404   8.497   4.882  1.00 42.62           C  
ANISOU 2961  CA  ASN A 383     5617   5326   5249   -812   -749   -262       C  
ATOM   2962  C   ASN A 383      24.553   9.499   5.654  1.00 43.98           C  
ANISOU 2962  C   ASN A 383     5960   5417   5334   -711   -835   -420       C  
ATOM   2963  O   ASN A 383      24.951  10.649   5.797  1.00 46.85           O  
ANISOU 2963  O   ASN A 383     6430   5607   5765   -821   -901   -551       O  
ATOM   2964  CB  ASN A 383      25.652   9.013   3.469  1.00 41.62           C  
ANISOU 2964  CB  ASN A 383     5597   4974   5243   -949   -638   -176       C  
ATOM   2965  CG  ASN A 383      24.377   9.288   2.719  1.00 42.57           C  
ANISOU 2965  CG  ASN A 383     5920   4941   5312   -817   -593   -106       C  
ATOM   2966  OD1 ASN A 383      23.334   9.527   3.320  1.00 44.39           O  
ANISOU 2966  OD1 ASN A 383     6231   5181   5455   -642   -655   -178       O  
ATOM   2967  ND2 ASN A 383      24.450   9.265   1.395  1.00 41.24           N  
ANISOU 2967  ND2 ASN A 383     5834   4643   5193   -897   -485     26       N  
ATOM   2968  N   GLY A 384      23.382   9.076   6.127  1.00 44.77           N  
ANISOU 2968  N   GLY A 384     6082   5634   5295   -508   -828   -419       N  
ATOM   2969  CA  GLY A 384      22.530   9.932   6.958  1.00 47.04           C  
ANISOU 2969  CA  GLY A 384     6497   5889   5488   -382   -892   -601       C  
ATOM   2970  C   GLY A 384      21.284  10.475   6.280  1.00 47.18           C  
ANISOU 2970  C   GLY A 384     6668   5731   5527   -235   -849   -601       C  
ATOM   2971  O   GLY A 384      20.288  10.761   6.945  1.00 45.44           O  
ANISOU 2971  O   GLY A 384     6489   5565   5213    -63   -864   -728       O  
ATOM   2972  N   GLU A 385      21.339  10.622   4.957  1.00 49.43           N  
ANISOU 2972  N   GLU A 385     7035   5817   5930   -298   -797   -465       N  
ATOM   2973  CA  GLU A 385      20.204  11.119   4.169  1.00 48.87           C  
ANISOU 2973  CA  GLU A 385     7120   5558   5890   -157   -790   -441       C  
ATOM   2974  C   GLU A 385      18.934  10.296   4.400  1.00 47.05           C  
ANISOU 2974  C   GLU A 385     6792   5524   5562     58   -745   -414       C  
ATOM   2975  O   GLU A 385      17.822  10.822   4.306  1.00 50.14           O  
ANISOU 2975  O   GLU A 385     7265   5826   5961    233   -774   -490       O  
ATOM   2976  CB  GLU A 385      20.548  11.118   2.677  1.00 48.90           C  
ANISOU 2976  CB  GLU A 385     7220   5373   5988   -278   -736   -256       C  
ATOM   2977  CG  GLU A 385      21.652  12.107   2.278  1.00 53.32           C  
ANISOU 2977  CG  GLU A 385     7909   5694   6655   -512   -759   -272       C  
ATOM   2978  CD  GLU A 385      21.806  12.263   0.764  1.00 54.97           C  
ANISOU 2978  CD  GLU A 385     8270   5698   6920   -628   -693    -90       C  
ATOM   2979  OE1 GLU A 385      22.940  12.503   0.297  1.00 56.65           O  
ANISOU 2979  OE1 GLU A 385     8495   5831   7200   -876   -635    -38       O  
ATOM   2980  OE2 GLU A 385      20.794  12.150   0.038  1.00 55.19           O  
ANISOU 2980  OE2 GLU A 385     8403   5653   6915   -479   -697     -2       O  
ATOM   2981  N   ALA A 386      19.115   9.011   4.694  1.00 43.07           N  
ANISOU 2981  N   ALA A 386     6107   5276   4981     40   -681   -309       N  
ATOM   2982  CA  ALA A 386      18.016   8.103   4.986  1.00 43.73           C  
ANISOU 2982  CA  ALA A 386     6080   5565   4971    193   -625   -266       C  
ATOM   2983  C   ALA A 386      18.328   7.295   6.230  1.00 46.84           C  
ANISOU 2983  C   ALA A 386     6332   6240   5225    172   -615   -283       C  
ATOM   2984  O   ALA A 386      19.450   7.350   6.750  1.00 50.78           O  
ANISOU 2984  O   ALA A 386     6806   6774   5714     49   -668   -314       O  
ATOM   2985  CB  ALA A 386      17.785   7.176   3.827  1.00 43.95           C  
ANISOU 2985  CB  ALA A 386     6069   5582   5047    184   -563    -65       C  
ATOM   2986  N   ASP A 387      17.330   6.548   6.698  1.00 44.49           N  
ANISOU 2986  N   ASP A 387     5943   6141   4821    285   -554   -257       N  
ATOM   2987  CA  ASP A 387      17.438   5.797   7.942  1.00 45.08           C  
ANISOU 2987  CA  ASP A 387     5920   6486   4723    271   -542   -258       C  
ATOM   2988  C   ASP A 387      17.092   4.313   7.783  1.00 43.26           C  
ANISOU 2988  C   ASP A 387     5572   6413   4451    264   -474    -54       C  
ATOM   2989  O   ASP A 387      17.809   3.456   8.300  1.00 42.79           O  
ANISOU 2989  O   ASP A 387     5452   6480   4324    185   -502     45       O  
ATOM   2990  CB  ASP A 387      16.534   6.414   9.018  1.00 47.72           C  
ANISOU 2990  CB  ASP A 387     6273   6944   4914    392   -519   -461       C  
ATOM   2991  CG  ASP A 387      16.899   7.854   9.346  1.00 50.94           C  
ANISOU 2991  CG  ASP A 387     6811   7192   5353    404   -605   -691       C  
ATOM   2992  OD1 ASP A 387      18.081   8.226   9.264  1.00 51.26           O  
ANISOU 2992  OD1 ASP A 387     6903   7116   5459    272   -694   -699       O  
ATOM   2993  OD2 ASP A 387      15.992   8.626   9.700  1.00 57.10           O  
ANISOU 2993  OD2 ASP A 387     7632   7959   6103    547   -584   -880       O  
ATOM   2994  N   ALA A 388      15.999   4.000   7.089  1.00 39.00           N  
ANISOU 2994  N   ALA A 388     5002   5856   3962    347   -404      6       N  
ATOM   2995  CA  ALA A 388      15.494   2.632   7.097  1.00 35.91           C  
ANISOU 2995  CA  ALA A 388     4503   5619   3523    335   -339    174       C  
ATOM   2996  C   ALA A 388      14.803   2.224   5.810  1.00 37.25           C  
ANISOU 2996  C   ALA A 388     4653   5677   3825    372   -307    277       C  
ATOM   2997  O   ALA A 388      14.165   3.036   5.141  1.00 39.34           O  
ANISOU 2997  O   ALA A 388     4967   5806   4173    461   -319    195       O  
ATOM   2998  CB  ALA A 388      14.541   2.446   8.259  1.00 35.37           C  
ANISOU 2998  CB  ALA A 388     4372   5790   3279    390   -264    107       C  
ATOM   2999  N   MET A 389      14.937   0.943   5.484  1.00 35.03           N  
ANISOU 2999  N   MET A 389     4307   5443   3559    309   -287    454       N  
ATOM   3000  CA  MET A 389      14.195   0.325   4.393  1.00 33.78           C  
ANISOU 3000  CA  MET A 389     4119   5218   3499    333   -261    553       C  
ATOM   3001  C   MET A 389      14.189  -1.180   4.638  1.00 34.48           C  
ANISOU 3001  C   MET A 389     4124   5424   3553    262   -233    720       C  
ATOM   3002  O   MET A 389      15.000  -1.677   5.415  1.00 36.59           O  
ANISOU 3002  O   MET A 389     4383   5772   3746    198   -256    777       O  
ATOM   3003  CB  MET A 389      14.835   0.646   3.044  1.00 32.20           C  
ANISOU 3003  CB  MET A 389     4013   4793   3427    309   -302    585       C  
ATOM   3004  CG  MET A 389      15.992  -0.258   2.670  1.00 30.50           C  
ANISOU 3004  CG  MET A 389     3785   4549   3254    207   -307    707       C  
ATOM   3005  SD  MET A 389      17.016   0.468   1.404  1.00 35.26           S  
ANISOU 3005  SD  MET A 389     4504   4930   3962    145   -317    692       S  
ATOM   3006  CE  MET A 389      15.978   0.310  -0.045  1.00 34.49           C  
ANISOU 3006  CE  MET A 389     4479   4711   3915    202   -310    748       C  
ATOM   3007  N   SER A 390      13.282  -1.899   3.987  1.00 33.11           N  
ANISOU 3007  N   SER A 390     3896   5246   3437    273   -204    797       N  
ATOM   3008  CA  SER A 390      13.212  -3.348   4.138  1.00 31.40           C  
ANISOU 3008  CA  SER A 390     3621   5100   3209    195   -187    960       C  
ATOM   3009  C   SER A 390      13.832  -3.975   2.912  1.00 27.38           C  
ANISOU 3009  C   SER A 390     3154   4419   2829    167   -231   1047       C  
ATOM   3010  O   SER A 390      13.667  -3.476   1.817  1.00 36.39           O  
ANISOU 3010  O   SER A 390     4345   5428   4052    208   -247   1000       O  
ATOM   3011  CB  SER A 390      11.766  -3.813   4.307  1.00 33.53           C  
ANISOU 3011  CB  SER A 390     3786   5491   3462    198   -120    979       C  
ATOM   3012  OG  SER A 390      11.686  -5.229   4.351  1.00 34.27           O  
ANISOU 3012  OG  SER A 390     3845   5611   3565    101   -113   1148       O  
ATOM   3013  N   LEU A 391      14.523  -5.085   3.088  1.00 24.07           N  
ANISOU 3013  N   LEU A 391     2726   4000   2422    105   -256   1170       N  
ATOM   3014  CA  LEU A 391      15.363  -5.614   2.040  1.00 21.14           C  
ANISOU 3014  CA  LEU A 391     2389   3475   2166     91   -288   1214       C  
ATOM   3015  C   LEU A 391      15.334  -7.131   1.966  1.00 26.01           C  
ANISOU 3015  C   LEU A 391     2980   4071   2832     49   -311   1353       C  
ATOM   3016  O   LEU A 391      15.353  -7.827   2.980  1.00 25.06           O  
ANISOU 3016  O   LEU A 391     2835   4040   2646     10   -332   1448       O  
ATOM   3017  CB  LEU A 391      16.798  -5.208   2.307  1.00 21.35           C  
ANISOU 3017  CB  LEU A 391     2431   3478   2203     79   -321   1175       C  
ATOM   3018  CG  LEU A 391      17.186  -3.747   2.166  1.00 21.69           C  
ANISOU 3018  CG  LEU A 391     2524   3479   2238     91   -312   1041       C  
ATOM   3019  CD1 LEU A 391      18.550  -3.517   2.823  1.00 20.51           C  
ANISOU 3019  CD1 LEU A 391     2347   3358   2089     53   -359   1008       C  
ATOM   3020  CD2 LEU A 391      17.217  -3.350   0.690  1.00 20.05           C  
ANISOU 3020  CD2 LEU A 391     2390   3110   2117     94   -282   1011       C  
ATOM   3021  N   ASP A 392      15.313  -7.632   0.740  1.00 30.57           N  
ANISOU 3021  N   ASP A 392     3585   4515   3515     54   -316   1363       N  
ATOM   3022  CA  ASP A 392      15.661  -9.003   0.464  1.00 32.10           C  
ANISOU 3022  CA  ASP A 392     3777   4629   3791     30   -354   1460       C  
ATOM   3023  C   ASP A 392      16.905  -9.378   1.246  1.00 30.79           C  
ANISOU 3023  C   ASP A 392     3591   4477   3630     34   -407   1504       C  
ATOM   3024  O   ASP A 392      17.762  -8.521   1.524  1.00 30.89           O  
ANISOU 3024  O   ASP A 392     3591   4525   3619     53   -408   1428       O  
ATOM   3025  CB  ASP A 392      15.944  -9.180  -1.024  1.00 35.30           C  
ANISOU 3025  CB  ASP A 392     4233   4885   4294     52   -346   1406       C  
ATOM   3026  CG  ASP A 392      16.215 -10.610  -1.385  1.00 38.25           C  
ANISOU 3026  CG  ASP A 392     4612   5156   4767     44   -388   1475       C  
ATOM   3027  OD1 ASP A 392      15.229 -11.371  -1.525  1.00 41.32           O  
ANISOU 3027  OD1 ASP A 392     5004   5517   5177      5   -412   1535       O  
ATOM   3028  OD2 ASP A 392      17.409 -10.973  -1.501  1.00 36.88           O  
ANISOU 3028  OD2 ASP A 392     4427   4924   4662     76   -403   1459       O  
ATOM   3029  N   GLY A 393      16.998 -10.658   1.596  1.00 28.89           N  
ANISOU 3029  N   GLY A 393     3349   4198   3429     15   -469   1627       N  
ATOM   3030  CA  GLY A 393      18.134 -11.173   2.343  1.00 31.00           C  
ANISOU 3030  CA  GLY A 393     3600   4462   3716     40   -561   1685       C  
ATOM   3031  C   GLY A 393      19.453 -10.893   1.653  1.00 32.04           C  
ANISOU 3031  C   GLY A 393     3688   4523   3965    103   -568   1574       C  
ATOM   3032  O   GLY A 393      20.423 -10.482   2.290  1.00 34.84           O  
ANISOU 3032  O   GLY A 393     3991   4937   4308    124   -620   1541       O  
ATOM   3033  N   GLY A 394      19.479 -11.093   0.341  1.00 31.34           N  
ANISOU 3033  N   GLY A 394     3613   4318   3978    122   -511   1506       N  
ATOM   3034  CA  GLY A 394      20.682 -10.891  -0.438  1.00 30.20           C  
ANISOU 3034  CA  GLY A 394     3418   4118   3940    165   -477   1392       C  
ATOM   3035  C   GLY A 394      21.160  -9.458  -0.412  1.00 31.49           C  
ANISOU 3035  C   GLY A 394     3557   4359   4048    133   -414   1289       C  
ATOM   3036  O   GLY A 394      22.341  -9.199  -0.647  1.00 36.84           O  
ANISOU 3036  O   GLY A 394     4155   5035   4807    141   -394   1205       O  
ATOM   3037  N   PHE A 395      20.256  -8.524  -0.134  1.00 28.35           N  
ANISOU 3037  N   PHE A 395     3219   4024   3530     94   -382   1285       N  
ATOM   3038  CA  PHE A 395      20.646  -7.127  -0.011  1.00 29.72           C  
ANISOU 3038  CA  PHE A 395     3395   4242   3655     60   -343   1189       C  
ATOM   3039  C   PHE A 395      20.833  -6.700   1.423  1.00 33.47           C  
ANISOU 3039  C   PHE A 395     3832   4838   4046     53   -418   1197       C  
ATOM   3040  O   PHE A 395      21.580  -5.756   1.683  1.00 39.87           O  
ANISOU 3040  O   PHE A 395     4617   5678   4855     22   -421   1108       O  
ATOM   3041  CB  PHE A 395      19.662  -6.212  -0.720  1.00 30.39           C  
ANISOU 3041  CB  PHE A 395     3583   4288   3675     44   -276   1147       C  
ATOM   3042  CG  PHE A 395      19.910  -6.117  -2.187  1.00 32.69           C  
ANISOU 3042  CG  PHE A 395     3936   4467   4016     27   -199   1101       C  
ATOM   3043  CD1 PHE A 395      20.667  -5.075  -2.707  1.00 35.22           C  
ANISOU 3043  CD1 PHE A 395     4291   4749   4340    -29   -132   1022       C  
ATOM   3044  CD2 PHE A 395      19.438  -7.094  -3.046  1.00 31.40           C  
ANISOU 3044  CD2 PHE A 395     3809   4236   3886     51   -190   1136       C  
ATOM   3045  CE1 PHE A 395      20.921  -4.995  -4.058  1.00 33.61           C  
ANISOU 3045  CE1 PHE A 395     4167   4458   4147    -64    -43    991       C  
ATOM   3046  CE2 PHE A 395      19.687  -7.021  -4.396  1.00 32.27           C  
ANISOU 3046  CE2 PHE A 395     3996   4258   4006     33   -116   1085       C  
ATOM   3047  CZ  PHE A 395      20.432  -5.969  -4.906  1.00 33.52           C  
ANISOU 3047  CZ  PHE A 395     4199   4396   4143    -27    -34   1018       C  
ATOM   3048  N   VAL A 396      20.189  -7.379   2.365  1.00 29.65           N  
ANISOU 3048  N   VAL A 396     3355   4428   3482     65   -478   1300       N  
ATOM   3049  CA  VAL A 396      20.576  -7.182   3.754  1.00 30.23           C  
ANISOU 3049  CA  VAL A 396     3405   4626   3455     58   -566   1315       C  
ATOM   3050  C   VAL A 396      22.046  -7.558   3.906  1.00 30.56           C  
ANISOU 3050  C   VAL A 396     3356   4649   3606     81   -662   1302       C  
ATOM   3051  O   VAL A 396      22.792  -6.906   4.625  1.00 34.07           O  
ANISOU 3051  O   VAL A 396     3758   5169   4017     66   -729   1235       O  
ATOM   3052  CB  VAL A 396      19.762  -8.019   4.717  1.00 31.23           C  
ANISOU 3052  CB  VAL A 396     3568   4834   3462     47   -608   1455       C  
ATOM   3053  CG1 VAL A 396      20.272  -7.799   6.116  1.00 32.94           C  
ANISOU 3053  CG1 VAL A 396     3787   5185   3542     37   -708   1469       C  
ATOM   3054  CG2 VAL A 396      18.289  -7.660   4.620  1.00 30.69           C  
ANISOU 3054  CG2 VAL A 396     3542   4815   3306     24   -505   1449       C  
ATOM   3055  N   TYR A 397      22.449  -8.610   3.206  1.00 30.73           N  
ANISOU 3055  N   TYR A 397     3338   4568   3770    123   -676   1346       N  
ATOM   3056  CA  TYR A 397      23.836  -9.063   3.198  1.00 34.57           C  
ANISOU 3056  CA  TYR A 397     3703   5028   4403    173   -763   1311       C  
ATOM   3057  C   TYR A 397      24.785  -7.938   2.824  1.00 36.80           C  
ANISOU 3057  C   TYR A 397     3895   5337   4751    130   -706   1153       C  
ATOM   3058  O   TYR A 397      25.745  -7.653   3.531  1.00 39.77           O  
ANISOU 3058  O   TYR A 397     4170   5784   5157    129   -808   1103       O  
ATOM   3059  CB  TYR A 397      23.984 -10.227   2.217  1.00 36.47           C  
ANISOU 3059  CB  TYR A 397     3923   5133   4801    236   -743   1335       C  
ATOM   3060  CG  TYR A 397      25.398 -10.683   1.992  1.00 39.95           C  
ANISOU 3060  CG  TYR A 397     4208   5541   5430    311   -804   1259       C  
ATOM   3061  CD1 TYR A 397      26.040 -11.509   2.907  1.00 42.39           C  
ANISOU 3061  CD1 TYR A 397     4458   5853   5797    395   -998   1333       C  
ATOM   3062  CD2 TYR A 397      26.093 -10.302   0.858  1.00 41.54           C  
ANISOU 3062  CD2 TYR A 397     4319   5713   5751    300   -668   1111       C  
ATOM   3063  CE1 TYR A 397      27.340 -11.934   2.699  1.00 43.81           C  
ANISOU 3063  CE1 TYR A 397     4462   6006   6179    490  -1070   1243       C  
ATOM   3064  CE2 TYR A 397      27.393 -10.720   0.645  1.00 44.49           C  
ANISOU 3064  CE2 TYR A 397     4511   6080   6314    373   -702   1015       C  
ATOM   3065  CZ  TYR A 397      28.012 -11.537   1.569  1.00 44.06           C  
ANISOU 3065  CZ  TYR A 397     4368   6027   6344    480   -910   1072       C  
ATOM   3066  OH  TYR A 397      29.303 -11.953   1.341  1.00 47.27           O  
ANISOU 3066  OH  TYR A 397     4563   6430   6968    576   -957    957       O  
ATOM   3067  N   ILE A 398      24.501  -7.290   1.703  1.00 38.62           N  
ANISOU 3067  N   ILE A 398     4169   5505   4998     80   -550   1079       N  
ATOM   3068  CA  ILE A 398      25.293  -6.149   1.248  1.00 33.30           C  
ANISOU 3068  CA  ILE A 398     3443   4836   4374      0   -470    947       C  
ATOM   3069  C   ILE A 398      25.223  -5.012   2.277  1.00 33.26           C  
ANISOU 3069  C   ILE A 398     3469   4911   4257    -56   -532    903       C  
ATOM   3070  O   ILE A 398      26.250  -4.473   2.705  1.00 29.75           O  
ANISOU 3070  O   ILE A 398     2918   4516   3869   -104   -586    816       O  
ATOM   3071  CB  ILE A 398      24.794  -5.664  -0.127  1.00 28.13           C  
ANISOU 3071  CB  ILE A 398     2894   4085   3710    -50   -302    912       C  
ATOM   3072  CG1 ILE A 398      25.107  -6.724  -1.200  1.00 25.82           C  
ANISOU 3072  CG1 ILE A 398     2560   3723   3527     -3   -232    910       C  
ATOM   3073  CG2 ILE A 398      25.413  -4.315  -0.490  1.00 25.56           C  
ANISOU 3073  CG2 ILE A 398     2569   3747   3396   -167   -218    806       C  
ATOM   3074  CD1 ILE A 398      24.450  -6.471  -2.533  1.00 19.90           C  
ANISOU 3074  CD1 ILE A 398     1952   2885   2726    -41    -95    898       C  
ATOM   3075  N   ALA A 399      24.010  -4.664   2.692  1.00 30.70           N  
ANISOU 3075  N   ALA A 399     3278   4606   3781    -49   -528    946       N  
ATOM   3076  CA  ALA A 399      23.835  -3.642   3.724  1.00 31.36           C  
ANISOU 3076  CA  ALA A 399     3405   4768   3742    -81   -584    884       C  
ATOM   3077  C   ALA A 399      24.738  -3.944   4.913  1.00 31.38           C  
ANISOU 3077  C   ALA A 399     3310   4881   3731    -71   -744    881       C  
ATOM   3078  O   ALA A 399      25.317  -3.039   5.524  1.00 31.94           O  
ANISOU 3078  O   ALA A 399     3357   5000   3779   -125   -806    775       O  
ATOM   3079  CB  ALA A 399      22.376  -3.573   4.177  1.00 28.16           C  
ANISOU 3079  CB  ALA A 399     3116   4405   3177    -43   -563    933       C  
ATOM   3080  N   GLY A 400      24.851  -5.228   5.227  1.00 28.65           N  
ANISOU 3080  N   GLY A 400     2921   4561   3404     -2   -829   1000       N  
ATOM   3081  CA  GLY A 400      25.629  -5.677   6.359  1.00 31.95           C  
ANISOU 3081  CA  GLY A 400     3270   5073   3797     29  -1017   1030       C  
ATOM   3082  C   GLY A 400      27.118  -5.602   6.138  1.00 32.99           C  
ANISOU 3082  C   GLY A 400     3217   5198   4120     23  -1090    931       C  
ATOM   3083  O   GLY A 400      27.860  -5.355   7.075  1.00 35.72           O  
ANISOU 3083  O   GLY A 400     3495   5634   4442     16  -1251    885       O  
ATOM   3084  N   LYS A 401      27.562  -5.829   4.907  1.00 35.53           N  
ANISOU 3084  N   LYS A 401     3447   5425   4628     24   -971    888       N  
ATOM   3085  CA  LYS A 401      28.949  -5.537   4.544  1.00 39.80           C  
ANISOU 3085  CA  LYS A 401     3782   5976   5363    -12   -979    757       C  
ATOM   3086  C   LYS A 401      29.202  -4.022   4.616  1.00 39.00           C  
ANISOU 3086  C   LYS A 401     3688   5898   5231   -156   -927    624       C  
ATOM   3087  O   LYS A 401      30.327  -3.577   4.843  1.00 42.79           O  
ANISOU 3087  O   LYS A 401     4000   6429   5828   -218   -994    510       O  
ATOM   3088  CB  LYS A 401      29.267  -6.052   3.140  1.00 40.94           C  
ANISOU 3088  CB  LYS A 401     3846   6031   5680      5   -816    726       C  
ATOM   3089  CG  LYS A 401      29.257  -7.566   3.002  1.00 44.49           C  
ANISOU 3089  CG  LYS A 401     4262   6429   6214    153   -884    818       C  
ATOM   3090  CD  LYS A 401      30.567  -8.227   3.452  1.00 47.41           C  
ANISOU 3090  CD  LYS A 401     4399   6842   6771    249  -1057    768       C  
ATOM   3091  CE  LYS A 401      30.542  -9.713   3.092  1.00 48.13           C  
ANISOU 3091  CE  LYS A 401     4476   6832   6978    407  -1107    842       C  
ATOM   3092  NZ  LYS A 401      31.756 -10.487   3.484  1.00 49.54           N  
ANISOU 3092  NZ  LYS A 401     4431   7026   7366    546  -1300    794       N  
ATOM   3093  N   CYS A 402      28.148  -3.240   4.431  1.00 34.19           N  
ANISOU 3093  N   CYS A 402     3270   5241   4480   -207   -820    632       N  
ATOM   3094  CA  CYS A 402      28.246  -1.797   4.487  1.00 37.82           C  
ANISOU 3094  CA  CYS A 402     3783   5678   4910   -333   -781    513       C  
ATOM   3095  C   CYS A 402      28.061  -1.268   5.917  1.00 38.45           C  
ANISOU 3095  C   CYS A 402     3922   5854   4832   -330   -944    471       C  
ATOM   3096  O   CYS A 402      28.029  -0.051   6.150  1.00 35.20           O  
ANISOU 3096  O   CYS A 402     3583   5414   4378   -420   -941    358       O  
ATOM   3097  CB  CYS A 402      27.241  -1.170   3.508  1.00 39.49           C  
ANISOU 3097  CB  CYS A 402     4176   5764   5065   -368   -606    529       C  
ATOM   3098  SG  CYS A 402      27.584  -1.554   1.732  1.00 41.21           S  
ANISOU 3098  SG  CYS A 402     4356   5875   5429   -410   -403    548       S  
ATOM   3099  N   GLY A 403      27.966  -2.184   6.876  1.00 39.85           N  
ANISOU 3099  N   GLY A 403     4087   6137   4917   -232  -1093    559       N  
ATOM   3100  CA  GLY A 403      27.914  -1.821   8.289  1.00 43.51           C  
ANISOU 3100  CA  GLY A 403     4609   6722   5201   -229  -1260    521       C  
ATOM   3101  C   GLY A 403      26.559  -1.328   8.755  1.00 44.95           C  
ANISOU 3101  C   GLY A 403     4993   6928   5156   -212  -1191    528       C  
ATOM   3102  O   GLY A 403      26.476  -0.417   9.576  1.00 47.10           O  
ANISOU 3102  O   GLY A 403     5338   7258   5300   -249  -1253    410       O  
ATOM   3103  N   LEU A 404      25.498  -1.933   8.230  1.00 45.30           N  
ANISOU 3103  N   LEU A 404     5117   6934   5161   -153  -1066    647       N  
ATOM   3104  CA  LEU A 404      24.146  -1.640   8.661  1.00 45.11           C  
ANISOU 3104  CA  LEU A 404     5241   6957   4941   -123   -991    657       C  
ATOM   3105  C   LEU A 404      23.588  -2.869   9.338  1.00 47.09           C  
ANISOU 3105  C   LEU A 404     5524   7315   5053    -66  -1034    828       C  
ATOM   3106  O   LEU A 404      24.046  -3.981   9.092  1.00 50.09           O  
ANISOU 3106  O   LEU A 404     5837   7665   5530    -36  -1092    955       O  
ATOM   3107  CB  LEU A 404      23.281  -1.247   7.471  1.00 44.76           C  
ANISOU 3107  CB  LEU A 404     5255   6781   4972   -117   -816    649       C  
ATOM   3108  CG  LEU A 404      23.762  -0.010   6.699  1.00 45.08           C  
ANISOU 3108  CG  LEU A 404     5309   6682   5138   -190   -765    511       C  
ATOM   3109  CD1 LEU A 404      22.951   0.151   5.427  1.00 43.77           C  
ANISOU 3109  CD1 LEU A 404     5217   6377   5037   -173   -622    546       C  
ATOM   3110  CD2 LEU A 404      23.682   1.257   7.543  1.00 44.09           C  
ANISOU 3110  CD2 LEU A 404     5264   6579   4910   -219   -819    347       C  
ATOM   3111  N   VAL A 405      22.585  -2.662  10.180  1.00 49.10           N  
ANISOU 3111  N   VAL A 405     5885   7687   5085    -56   -998    826       N  
ATOM   3112  CA  VAL A 405      22.074  -3.720  11.042  1.00 48.78           C  
ANISOU 3112  CA  VAL A 405     5898   7772   4863    -41  -1037    991       C  
ATOM   3113  C   VAL A 405      20.618  -4.055  10.760  1.00 48.10           C  
ANISOU 3113  C   VAL A 405     5861   7703   4711    -33   -866   1067       C  
ATOM   3114  O   VAL A 405      19.804  -3.149  10.570  1.00 47.85           O  
ANISOU 3114  O   VAL A 405     5855   7679   4649    -20   -744    940       O  
ATOM   3115  CB  VAL A 405      22.191  -3.327  12.515  1.00 51.92           C  
ANISOU 3115  CB  VAL A 405     6377   8352   4998    -61  -1142    933       C  
ATOM   3116  CG1 VAL A 405      23.613  -3.540  12.998  1.00 54.48           C  
ANISOU 3116  CG1 VAL A 405     6644   8689   5365    -66  -1373    935       C  
ATOM   3117  CG2 VAL A 405      21.743  -1.880  12.726  1.00 52.22           C  
ANISOU 3117  CG2 VAL A 405     6465   8422   4955    -67  -1060    705       C  
ATOM   3118  N   PRO A 406      20.288  -5.361  10.732  1.00 47.67           N  
ANISOU 3118  N   PRO A 406     5816   7645   4653    -39   -869   1269       N  
ATOM   3119  CA  PRO A 406      18.907  -5.809  10.668  1.00 45.89           C  
ANISOU 3119  CA  PRO A 406     5621   7466   4348    -61   -723   1355       C  
ATOM   3120  C   PRO A 406      18.213  -5.604  11.997  1.00 47.63           C  
ANISOU 3120  C   PRO A 406     5920   7907   4272   -101   -680   1351       C  
ATOM   3121  O   PRO A 406      18.698  -6.086  13.025  1.00 49.12           O  
ANISOU 3121  O   PRO A 406     6179   8195   4287   -134   -798   1449       O  
ATOM   3122  CB  PRO A 406      19.030  -7.302  10.362  1.00 48.24           C  
ANISOU 3122  CB  PRO A 406     5919   7673   4736    -76   -781   1575       C  
ATOM   3123  CG  PRO A 406      20.375  -7.681  10.807  1.00 49.60           C  
ANISOU 3123  CG  PRO A 406     6089   7820   4937    -50   -980   1621       C  
ATOM   3124  CD  PRO A 406      21.225  -6.488  10.576  1.00 49.73           C  
ANISOU 3124  CD  PRO A 406     6039   7820   5036    -22  -1013   1415       C  
ATOM   3125  N   VAL A 407      17.081  -4.907  11.960  1.00 46.81           N  
ANISOU 3125  N   VAL A 407     5800   7880   4104    -92   -514   1233       N  
ATOM   3126  CA  VAL A 407      16.372  -4.470  13.167  1.00 45.42           C  
ANISOU 3126  CA  VAL A 407     5678   7935   3644   -117   -430   1159       C  
ATOM   3127  C   VAL A 407      15.083  -5.254  13.424  1.00 43.30           C  
ANISOU 3127  C   VAL A 407     5394   7794   3264   -187   -268   1288       C  
ATOM   3128  O   VAL A 407      14.696  -5.469  14.573  1.00 43.60           O  
ANISOU 3128  O   VAL A 407     5499   8042   3024   -257   -213   1334       O  
ATOM   3129  CB  VAL A 407      16.070  -2.953  13.077  1.00 44.57           C  
ANISOU 3129  CB  VAL A 407     5551   7836   3548    -39   -361    879       C  
ATOM   3130  CG1 VAL A 407      14.683  -2.624  13.575  1.00 45.52           C  
ANISOU 3130  CG1 VAL A 407     5645   8139   3513    -28   -171    783       C  
ATOM   3131  CG2 VAL A 407      17.104  -2.174  13.851  1.00 49.13           C  
ANISOU 3131  CG2 VAL A 407     6200   8450   4018    -32   -500    743       C  
ATOM   3132  N   LEU A 408      14.419  -5.663  12.349  1.00 39.61           N  
ANISOU 3132  N   LEU A 408     4838   7208   3003   -183   -191   1340       N  
ATOM   3133  CA  LEU A 408      13.179  -6.422  12.430  1.00 38.57           C  
ANISOU 3133  CA  LEU A 408     4657   7176   2821   -267    -41   1455       C  
ATOM   3134  C   LEU A 408      13.004  -7.209  11.135  1.00 40.46           C  
ANISOU 3134  C   LEU A 408     4834   7209   3329   -273    -62   1566       C  
ATOM   3135  O   LEU A 408      13.236  -6.675  10.047  1.00 43.30           O  
ANISOU 3135  O   LEU A 408     5150   7406   3897   -182    -98   1457       O  
ATOM   3136  CB  LEU A 408      11.976  -5.490  12.587  1.00 37.04           C  
ANISOU 3136  CB  LEU A 408     4365   7140   2567   -223    143   1250       C  
ATOM   3137  CG  LEU A 408      11.763  -4.654  13.848  1.00 37.32           C  
ANISOU 3137  CG  LEU A 408     4440   7417   2323   -210    227   1085       C  
ATOM   3138  CD1 LEU A 408      10.610  -3.697  13.631  1.00 32.38           C  
ANISOU 3138  CD1 LEU A 408     3679   6876   1747   -114    389    846       C  
ATOM   3139  CD2 LEU A 408      11.514  -5.532  15.071  1.00 40.89           C  
ANISOU 3139  CD2 LEU A 408     4971   8091   2472   -363    298   1260       C  
ATOM   3140  N   ALA A 409      12.594  -8.467  11.246  1.00 39.87           N  
ANISOU 3140  N   ALA A 409     4774   7134   3240   -390    -43   1781       N  
ATOM   3141  CA  ALA A 409      12.359  -9.289  10.073  1.00 38.75           C  
ANISOU 3141  CA  ALA A 409     4585   6797   3340   -406    -68   1876       C  
ATOM   3142  C   ALA A 409      10.922  -9.137   9.627  1.00 41.10           C  
ANISOU 3142  C   ALA A 409     4747   7171   3700   -435     90   1803       C  
ATOM   3143  O   ALA A 409      10.057  -8.812  10.432  1.00 45.78           O  
ANISOU 3143  O   ALA A 409     5281   7985   4126   -485    236   1751       O  
ATOM   3144  CB  ALA A 409      12.643 -10.739  10.389  1.00 40.43           C  
ANISOU 3144  CB  ALA A 409     4892   6934   3534   -520   -150   2138       C  
ATOM   3145  N   GLU A 410      10.673  -9.366   8.344  1.00 38.84           N  
ANISOU 3145  N   GLU A 410     4401   6709   3647   -400     58   1786       N  
ATOM   3146  CA  GLU A 410       9.323  -9.627   7.866  1.00 43.82           C  
ANISOU 3146  CA  GLU A 410     4898   7385   4368   -457    162   1772       C  
ATOM   3147  C   GLU A 410       8.975 -11.083   8.202  1.00 46.99           C  
ANISOU 3147  C   GLU A 410     5326   7778   4751   -644    177   2007       C  
ATOM   3148  O   GLU A 410       9.853 -11.954   8.159  1.00 48.56           O  
ANISOU 3148  O   GLU A 410     5653   7816   4983   -675     52   2166       O  
ATOM   3149  CB  GLU A 410       9.240  -9.412   6.355  1.00 46.40           C  
ANISOU 3149  CB  GLU A 410     5183   7516   4931   -360     89   1680       C  
ATOM   3150  CG  GLU A 410       9.519  -7.974   5.896  1.00 48.00           C  
ANISOU 3150  CG  GLU A 410     5385   7688   5166   -193     66   1470       C  
ATOM   3151  CD  GLU A 410       9.424  -7.795   4.386  1.00 46.76           C  
ANISOU 3151  CD  GLU A 410     5223   7338   5205   -114    -11   1406       C  
ATOM   3152  OE1 GLU A 410       9.060  -8.767   3.697  1.00 48.14           O  
ANISOU 3152  OE1 GLU A 410     5378   7421   5490   -181    -43   1498       O  
ATOM   3153  OE2 GLU A 410       9.712  -6.684   3.884  1.00 46.21           O  
ANISOU 3153  OE2 GLU A 410     5189   7200   5169      6    -46   1266       O  
ATOM   3154  N   ASN A 411       7.712 -11.341   8.551  1.00 45.75           N  
ANISOU 3154  N   ASN A 411     5044   7788   4552   -769    326   2026       N  
ATOM   3155  CA  ASN A 411       7.216 -12.711   8.767  1.00 44.44           C  
ANISOU 3155  CA  ASN A 411     4895   7596   4394   -983    354   2251       C  
ATOM   3156  C   ASN A 411       6.005 -13.033   7.872  1.00 43.10           C  
ANISOU 3156  C   ASN A 411     4545   7405   4428  -1051    405   2204       C  
ATOM   3157  O   ASN A 411       5.104 -12.209   7.709  1.00 39.68           O  
ANISOU 3157  O   ASN A 411     3924   7127   4026   -990    508   2017       O  
ATOM   3158  CB  ASN A 411       6.877 -12.935  10.247  1.00 46.69           C  
ANISOU 3158  CB  ASN A 411     5217   8127   4396  -1146    499   2371       C  
ATOM   3159  CG  ASN A 411       8.071 -13.452  11.067  1.00 47.17           C  
ANISOU 3159  CG  ASN A 411     5517   8120   4285  -1172    374   2562       C  
ATOM   3160  OD1 ASN A 411       9.113 -13.832  10.526  1.00 45.87           O  
ANISOU 3160  OD1 ASN A 411     5466   7712   4249  -1083    180   2622       O  
ATOM   3161  ND2 ASN A 411       7.908 -13.474  12.381  1.00 47.87           N  
ANISOU 3161  ND2 ASN A 411     5678   8434   4078  -1291    482   2651       N  
ATOM   3162  N   TYR A 412       5.998 -14.234   7.295  1.00 42.84           N  
ANISOU 3162  N   TYR A 412     4566   7169   4542  -1167    315   2361       N  
ATOM   3163  CA  TYR A 412       5.001 -14.621   6.289  1.00 46.49           C  
ANISOU 3163  CA  TYR A 412     4877   7563   5223  -1228    309   2309       C  
ATOM   3164  C   TYR A 412       4.073 -15.753   6.725  1.00 53.80           C  
ANISOU 3164  C   TYR A 412     5743   8539   6159  -1509    400   2485       C  
ATOM   3165  O   TYR A 412       3.200 -16.165   5.958  1.00 52.68           O  
ANISOU 3165  O   TYR A 412     5462   8347   6206  -1593    388   2447       O  
ATOM   3166  CB  TYR A 412       5.720 -14.996   4.983  1.00 44.69           C  
ANISOU 3166  CB  TYR A 412     4756   7029   5196  -1120    113   2292       C  
ATOM   3167  CG  TYR A 412       6.776 -13.981   4.624  1.00 40.33           C  
ANISOU 3167  CG  TYR A 412     4285   6419   4618   -887     38   2156       C  
ATOM   3168  CD1 TYR A 412       6.443 -12.640   4.485  1.00 39.15           C  
ANISOU 3168  CD1 TYR A 412     4028   6406   4441   -743     93   1953       C  
ATOM   3169  CD2 TYR A 412       8.106 -14.347   4.472  1.00 38.72           C  
ANISOU 3169  CD2 TYR A 412     4258   6026   4427   -816    -87   2228       C  
ATOM   3170  CE1 TYR A 412       7.395 -11.698   4.190  1.00 37.60           C  
ANISOU 3170  CE1 TYR A 412     3918   6146   4223   -564     31   1841       C  
ATOM   3171  CE2 TYR A 412       9.068 -13.409   4.174  1.00 36.56           C  
ANISOU 3171  CE2 TYR A 412     4037   5718   4136   -636   -136   2103       C  
ATOM   3172  CZ  TYR A 412       8.701 -12.086   4.031  1.00 36.41           C  
ANISOU 3172  CZ  TYR A 412     3928   5825   4082   -525    -74   1918       C  
ATOM   3173  OH  TYR A 412       9.638 -11.139   3.739  1.00 35.32           O  
ANISOU 3173  OH  TYR A 412     3853   5636   3931   -376   -120   1804       O  
ATOM   3174  N   ASN A 413       4.249 -16.223   7.960  1.00 62.57           N  
ANISOU 3174  N   ASN A 413     6964   9752   7058  -1665    487   2675       N  
ATOM   3175  CA  ASN A 413       3.496 -17.346   8.514  1.00 70.16           C  
ANISOU 3175  CA  ASN A 413     7919  10748   7991  -1971    584   2890       C  
ATOM   3176  C   ASN A 413       2.443 -16.834   9.503  1.00 70.25           C  
ANISOU 3176  C   ASN A 413     7739  11138   7816  -2103    856   2837       C  
ATOM   3177  O   ASN A 413       2.779 -16.204  10.500  1.00 67.10           O  
ANISOU 3177  O   ASN A 413     7402  10937   7157  -2054    954   2820       O  
ATOM   3178  CB  ASN A 413       4.478 -18.289   9.217  1.00 77.14           C  
ANISOU 3178  CB  ASN A 413     9101  11464   8746  -2061    477   3169       C  
ATOM   3179  CG  ASN A 413       3.993 -19.724   9.290  1.00 87.50           C  
ANISOU 3179  CG  ASN A 413    10490  12619  10137  -2352    464   3420       C  
ATOM   3180  OD1 ASN A 413       3.357 -20.234   8.370  1.00 87.35           O  
ANISOU 3180  OD1 ASN A 413    10362  12465  10364  -2431    424   3381       O  
ATOM   3181  ND2 ASN A 413       4.319 -20.389  10.397  1.00 98.88           N  
ANISOU 3181  ND2 ASN A 413    12143  14064  11363  -2520    479   3687       N  
ATOM   3182  N   LYS A 414       1.171 -17.095   9.220  1.00 74.24           N  
ANISOU 3182  N   LYS A 414     7999  11753   8457  -2269    979   2790       N  
ATOM   3183  CA  LYS A 414       0.081 -16.665  10.103  1.00 79.29           C  
ANISOU 3183  CA  LYS A 414     8406  12772   8947  -2406   1266   2715       C  
ATOM   3184  C   LYS A 414       0.238 -17.318  11.477  1.00 82.57           C  
ANISOU 3184  C   LYS A 414     9007  13312   9055  -2661   1412   2981       C  
ATOM   3185  O   LYS A 414       0.446 -18.529  11.568  1.00 84.38           O  
ANISOU 3185  O   LYS A 414     9423  13338   9298  -2880   1336   3259       O  
ATOM   3186  CB  LYS A 414      -1.283 -17.034   9.502  1.00 82.40           C  
ANISOU 3186  CB  LYS A 414     8487  13238   9582  -2575   1350   2641       C  
ATOM   3187  CG  LYS A 414      -2.509 -16.375  10.179  1.00 87.35           C  
ANISOU 3187  CG  LYS A 414     8775  14286  10128  -2650   1651   2469       C  
ATOM   3188  CD  LYS A 414      -2.956 -15.064   9.499  1.00 86.41           C  
ANISOU 3188  CD  LYS A 414     8388  14278  10164  -2335   1624   2111       C  
ATOM   3189  CE  LYS A 414      -2.296 -13.828  10.115  1.00 85.40           C  
ANISOU 3189  CE  LYS A 414     8355  14280   9813  -2068   1667   1955       C  
ATOM   3190  NZ  LYS A 414      -2.358 -12.633   9.215  1.00 81.71           N  
ANISOU 3190  NZ  LYS A 414     7756  13764   9527  -1724   1533   1658       N  
ATOM   3191  N   SER A 415       0.157 -16.512  12.537  1.00 83.14           N  
ANISOU 3191  N   SER A 415     9051  13702   8837  -2627   1609   2895       N  
ATOM   3192  CA  SER A 415       0.284 -17.019  13.904  1.00 85.16           C  
ANISOU 3192  CA  SER A 415     9500  14117   8738  -2866   1760   3137       C  
ATOM   3193  C   SER A 415      -0.154 -16.018  14.969  1.00 85.51           C  
ANISOU 3193  C   SER A 415     9425  14584   8480  -2838   2037   2959       C  
ATOM   3194  O   SER A 415       0.088 -14.818  14.864  1.00 79.92           O  
ANISOU 3194  O   SER A 415     8638  13967   7762  -2548   2019   2682       O  
ATOM   3195  CB  SER A 415       1.721 -17.468  14.185  1.00 84.47           C  
ANISOU 3195  CB  SER A 415     9807  13768   8522  -2796   1513   3360       C  
ATOM   3196  OG  SER A 415       1.955 -18.772  13.676  1.00 84.94           O  
ANISOU 3196  OG  SER A 415    10023  13487   8763  -2950   1336   3618       O  
ATOM   3197  N   ASP A 416      -0.789 -16.545  16.009  1.00 92.36           N  
ANISOU 3197  N   ASP A 416    10300  15702   9091  -3154   2295   3125       N  
ATOM   3198  CA  ASP A 416      -1.203 -15.752  17.167  1.00 95.92           C  
ANISOU 3198  CA  ASP A 416    10673  16579   9193  -3173   2592   2980       C  
ATOM   3199  C   ASP A 416      -0.024 -15.124  17.928  1.00 94.57           C  
ANISOU 3199  C   ASP A 416    10806  16423   8703  -2979   2479   2969       C  
ATOM   3200  O   ASP A 416      -0.230 -14.300  18.818  1.00 97.38           O  
ANISOU 3200  O   ASP A 416    11119  17111   8769  -2931   2686   2792       O  
ATOM   3201  CB  ASP A 416      -2.041 -16.612  18.121  1.00100.06           C  
ANISOU 3201  CB  ASP A 416    11192  17350   9477  -3602   2895   3212       C  
ATOM   3202  CG  ASP A 416      -1.338 -17.901  18.524  1.00101.72           C  
ANISOU 3202  CG  ASP A 416    11808  17302   9538  -3853   2742   3660       C  
ATOM   3203  OD1 ASP A 416      -0.302 -18.242  17.913  1.00 98.94           O  
ANISOU 3203  OD1 ASP A 416    11686  16563   9344  -3693   2394   3774       O  
ATOM   3204  OD2 ASP A 416      -1.827 -18.581  19.449  1.00106.28           O  
ANISOU 3204  OD2 ASP A 416    12477  18062   9843  -4213   2970   3897       O  
ATOM   3205  N   ASN A 417       1.200 -15.519  17.585  1.00 89.81           N  
ANISOU 3205  N   ASN A 417    10495  15469   8159  -2869   2150   3141       N  
ATOM   3206  CA  ASN A 417       2.398 -14.967  18.205  1.00 87.41           C  
ANISOU 3206  CA  ASN A 417    10460  15149   7602  -2681   1993   3129       C  
ATOM   3207  C   ASN A 417       3.420 -14.603  17.123  1.00 78.68           C  
ANISOU 3207  C   ASN A 417     9398  13700   6798  -2372   1665   3024       C  
ATOM   3208  O   ASN A 417       4.565 -15.039  17.155  1.00 74.71           O  
ANISOU 3208  O   ASN A 417     9160  12959   6268  -2317   1409   3201       O  
ATOM   3209  CB  ASN A 417       2.963 -15.986  19.209  1.00 91.45           C  
ANISOU 3209  CB  ASN A 417    11337  15621   7789  -2919   1934   3515       C  
ATOM   3210  CG  ASN A 417       3.920 -15.365  20.222  1.00 92.91           C  
ANISOU 3210  CG  ASN A 417    11773  15930   7598  -2792   1850   3489       C  
ATOM   3211  OD1 ASN A 417       3.881 -14.164  20.488  1.00 93.41           O  
ANISOU 3211  OD1 ASN A 417    11723  16216   7553  -2604   1949   3177       O  
ATOM   3212  ND2 ASN A 417       4.780 -16.195  20.801  1.00 94.28           N  
ANISOU 3212  ND2 ASN A 417    12299  15948   7577  -2891   1649   3815       N  
ATOM   3213  N   CYS A 418       2.985 -13.794  16.161  1.00 76.28           N  
ANISOU 3213  N   CYS A 418     8824  13380   6779  -2172   1676   2731       N  
ATOM   3214  CA  CYS A 418       3.789 -13.491  14.966  1.00 71.05           C  
ANISOU 3214  CA  CYS A 418     8177  12395   6424  -1916   1401   2632       C  
ATOM   3215  C   CYS A 418       5.028 -12.646  15.262  1.00 67.07           C  
ANISOU 3215  C   CYS A 418     7848  11844   5791  -1684   1236   2528       C  
ATOM   3216  O   CYS A 418       6.091 -12.894  14.699  1.00 64.02           O  
ANISOU 3216  O   CYS A 418     7608  11175   5543  -1573    984   2606       O  
ATOM   3217  CB  CYS A 418       2.932 -12.780  13.909  1.00 68.80           C  
ANISOU 3217  CB  CYS A 418     7579  12122   6440  -1771   1454   2353       C  
ATOM   3218  SG  CYS A 418       3.803 -12.410  12.356  1.00 66.56           S  
ANISOU 3218  SG  CYS A 418     7324  11459   6506  -1491   1148   2241       S  
ATOM   3219  N   GLU A 419       4.882 -11.648  16.133  1.00 66.44           N  
ANISOU 3219  N   GLU A 419     7741  12044   5458  -1615   1383   2334       N  
ATOM   3220  CA  GLU A 419       5.947 -10.673  16.386  1.00 63.53           C  
ANISOU 3220  CA  GLU A 419     7502  11647   4990  -1395   1235   2178       C  
ATOM   3221  C   GLU A 419       7.120 -11.222  17.200  1.00 65.57           C  
ANISOU 3221  C   GLU A 419     8067  11841   5006  -1454   1057   2409       C  
ATOM   3222  O   GLU A 419       8.200 -10.632  17.197  1.00 66.81           O  
ANISOU 3222  O   GLU A 419     8331  11896   5158  -1282    865   2320       O  
ATOM   3223  CB  GLU A 419       5.384  -9.426  17.078  1.00 64.11           C  
ANISOU 3223  CB  GLU A 419     7458  12030   4873  -1297   1440   1870       C  
ATOM   3224  CG  GLU A 419       4.367  -8.646  16.233  1.00 64.33           C  
ANISOU 3224  CG  GLU A 419     7177  12093   5170  -1158   1557   1589       C  
ATOM   3225  CD  GLU A 419       3.783  -7.445  16.969  1.00 67.88           C  
ANISOU 3225  CD  GLU A 419     7508  12842   5443  -1043   1760   1267       C  
ATOM   3226  OE1 GLU A 419       4.571  -6.627  17.491  1.00 69.82           O  
ANISOU 3226  OE1 GLU A 419     7904  13100   5522   -909   1676   1132       O  
ATOM   3227  OE2 GLU A 419       2.538  -7.316  17.027  1.00 68.64           O  
ANISOU 3227  OE2 GLU A 419     7347  13157   5575  -1084   1999   1133       O  
ATOM   3228  N   ASP A 420       6.916 -12.345  17.882  1.00 68.99           N  
ANISOU 3228  N   ASP A 420     8640  12324   5249  -1700   1107   2709       N  
ATOM   3229  CA  ASP A 420       7.931 -12.906  18.774  1.00 71.72           C  
ANISOU 3229  CA  ASP A 420     9294  12627   5330  -1763    927   2949       C  
ATOM   3230  C   ASP A 420       8.278 -14.338  18.359  1.00 69.57           C  
ANISOU 3230  C   ASP A 420     9161  12055   5219  -1887    747   3290       C  
ATOM   3231  O   ASP A 420       8.569 -15.186  19.203  1.00 67.57           O  
ANISOU 3231  O   ASP A 420     9153  11799   4724  -2051    679   3579       O  
ATOM   3232  CB  ASP A 420       7.408 -12.864  20.221  1.00 78.11           C  
ANISOU 3232  CB  ASP A 420    10214  13797   5667  -1950   1148   3007       C  
ATOM   3233  CG  ASP A 420       8.515 -12.715  21.253  1.00 81.65           C  
ANISOU 3233  CG  ASP A 420    10952  14294   5777  -1908    958   3082       C  
ATOM   3234  OD1 ASP A 420       8.378 -13.286  22.358  1.00 87.88           O  
ANISOU 3234  OD1 ASP A 420    11953  15255   6182  -2117   1028   3305       O  
ATOM   3235  OD2 ASP A 420       9.513 -12.019  20.974  1.00 81.55           O  
ANISOU 3235  OD2 ASP A 420    10958  14157   5871  -1678    737   2920       O  
ATOM   3236  N   THR A 421       8.250 -14.593  17.051  1.00 66.37           N  
ANISOU 3236  N   THR A 421     8617  11386   5216  -1803    658   3249       N  
ATOM   3237  CA  THR A 421       8.473 -15.930  16.508  1.00 66.71           C  
ANISOU 3237  CA  THR A 421     8765  11120   5461  -1904    498   3522       C  
ATOM   3238  C   THR A 421       9.409 -15.880  15.307  1.00 64.59           C  
ANISOU 3238  C   THR A 421     8464  10534   5543  -1671    253   3427       C  
ATOM   3239  O   THR A 421       8.985 -15.514  14.214  1.00 64.10           O  
ANISOU 3239  O   THR A 421     8201  10400   5752  -1583    301   3242       O  
ATOM   3240  CB  THR A 421       7.159 -16.569  16.031  1.00 66.76           C  
ANISOU 3240  CB  THR A 421     8611  11137   5620  -2116    694   3584       C  
ATOM   3241  OG1 THR A 421       6.244 -16.670  17.125  1.00 70.05           O  
ANISOU 3241  OG1 THR A 421     9034  11867   5717  -2364    959   3676       O  
ATOM   3242  CG2 THR A 421       7.419 -17.955  15.461  1.00 67.55           C  
ANISOU 3242  CG2 THR A 421     8842  10884   5939  -2219    509   3851       C  
ATOM   3243  N   PRO A 422      10.682 -16.264  15.492  1.00 64.82           N  
ANISOU 3243  N   PRO A 422     8685  10377   5565  -1572    -13   3551       N  
ATOM   3244  CA  PRO A 422      11.586 -16.302  14.332  1.00 60.67           C  
ANISOU 3244  CA  PRO A 422     8114   9561   5379  -1365   -220   3458       C  
ATOM   3245  C   PRO A 422      11.196 -17.403  13.339  1.00 57.40           C  
ANISOU 3245  C   PRO A 422     7676   8877   5258  -1441   -258   3576       C  
ATOM   3246  O   PRO A 422      10.982 -18.547  13.748  1.00 57.87           O  
ANISOU 3246  O   PRO A 422     7888   8831   5270  -1619   -299   3847       O  
ATOM   3247  CB  PRO A 422      12.943 -16.619  14.963  1.00 63.72           C  
ANISOU 3247  CB  PRO A 422     8701   9843   5667  -1273   -487   3590       C  
ATOM   3248  CG  PRO A 422      12.595 -17.381  16.227  1.00 66.61           C  
ANISOU 3248  CG  PRO A 422     9283  10316   5708  -1492   -467   3882       C  
ATOM   3249  CD  PRO A 422      11.330 -16.754  16.725  1.00 66.36           C  
ANISOU 3249  CD  PRO A 422     9146  10615   5455  -1647   -144   3787       C  
ATOM   3250  N   GLU A 423      11.099 -17.053  12.057  1.00 53.21           N  
ANISOU 3250  N   GLU A 423     6976   8226   5014  -1316   -250   3375       N  
ATOM   3251  CA  GLU A 423      10.731 -18.014  11.015  1.00 51.18           C  
ANISOU 3251  CA  GLU A 423     6694   7715   5039  -1373   -295   3439       C  
ATOM   3252  C   GLU A 423      11.984 -18.546  10.348  1.00 49.35           C  
ANISOU 3252  C   GLU A 423     6554   7178   5019  -1202   -542   3456       C  
ATOM   3253  O   GLU A 423      12.949 -17.812  10.158  1.00 47.39           O  
ANISOU 3253  O   GLU A 423     6275   6933   4797  -1005   -626   3304       O  
ATOM   3254  CB  GLU A 423       9.847 -17.366   9.955  1.00 48.95           C  
ANISOU 3254  CB  GLU A 423     6185   7484   4931  -1336   -156   3206       C  
ATOM   3255  CG  GLU A 423       8.403 -17.146  10.358  1.00 49.73           C  
ANISOU 3255  CG  GLU A 423     6140   7834   4921  -1520     84   3188       C  
ATOM   3256  CD  GLU A 423       7.607 -16.386   9.293  1.00 49.52           C  
ANISOU 3256  CD  GLU A 423     5880   7856   5080  -1435    174   2934       C  
ATOM   3257  OE1 GLU A 423       6.405 -16.113   9.531  1.00 50.88           O  
ANISOU 3257  OE1 GLU A 423     5883   8245   5204  -1552    365   2874       O  
ATOM   3258  OE2 GLU A 423       8.177 -16.047   8.220  1.00 44.54           O  
ANISOU 3258  OE2 GLU A 423     5231   7054   4639  -1251     55   2792       O  
ATOM   3259  N   ALA A 424      11.957 -19.823   9.983  1.00 51.63           N  
ANISOU 3259  N   ALA A 424     6944   7201   5470  -1282   -652   3628       N  
ATOM   3260  CA  ALA A 424      13.117 -20.474   9.380  1.00 52.11           C  
ANISOU 3260  CA  ALA A 424     7092   6961   5748  -1114   -886   3640       C  
ATOM   3261  C   ALA A 424      13.450 -19.834   8.046  1.00 50.36           C  
ANISOU 3261  C   ALA A 424     6712   6675   5748   -926   -874   3362       C  
ATOM   3262  O   ALA A 424      14.611 -19.793   7.639  1.00 47.14           O  
ANISOU 3262  O   ALA A 424     6311   6139   5463   -735  -1014   3277       O  
ATOM   3263  CB  ALA A 424      12.866 -21.956   9.205  1.00 54.48           C  
ANISOU 3263  CB  ALA A 424     7536   6972   6193  -1244   -994   3856       C  
ATOM   3264  N   GLY A 425      12.424 -19.337   7.366  1.00 53.89           N  
ANISOU 3264  N   GLY A 425     7015   7220   6242   -986   -708   3221       N  
ATOM   3265  CA  GLY A 425      12.619 -18.575   6.134  1.00 51.71           C  
ANISOU 3265  CA  GLY A 425     6611   6916   6121   -826   -682   2965       C  
ATOM   3266  C   GLY A 425      11.747 -19.092   5.018  1.00 50.14           C  
ANISOU 3266  C   GLY A 425     6358   6584   6110   -896   -652   2912       C  
ATOM   3267  O   GLY A 425      11.127 -20.148   5.136  1.00 53.69           O  
ANISOU 3267  O   GLY A 425     6868   6920   6612  -1062   -674   3069       O  
ATOM   3268  N   TYR A 426      11.717 -18.346   3.925  1.00 47.54           N  
ANISOU 3268  N   TYR A 426     5928   6259   5875   -779   -616   2693       N  
ATOM   3269  CA  TYR A 426      10.896 -18.703   2.781  1.00 45.64           C  
ANISOU 3269  CA  TYR A 426     5636   5911   5795   -827   -607   2611       C  
ATOM   3270  C   TYR A 426      11.685 -19.582   1.817  1.00 46.85           C  
ANISOU 3270  C   TYR A 426     5887   5773   6140   -736   -746   2579       C  
ATOM   3271  O   TYR A 426      12.878 -19.812   2.024  1.00 48.52           O  
ANISOU 3271  O   TYR A 426     6176   5884   6374   -617   -837   2604       O  
ATOM   3272  CB  TYR A 426      10.303 -17.456   2.110  1.00 41.39           C  
ANISOU 3272  CB  TYR A 426     4960   5531   5235   -758   -509   2405       C  
ATOM   3273  CG  TYR A 426      11.258 -16.472   1.474  1.00 39.13           C  
ANISOU 3273  CG  TYR A 426     4679   5239   4951   -563   -522   2235       C  
ATOM   3274  CD1 TYR A 426      11.961 -15.547   2.239  1.00 38.54           C  
ANISOU 3274  CD1 TYR A 426     4598   5303   4742   -482   -488   2209       C  
ATOM   3275  CD2 TYR A 426      11.392 -16.406   0.091  1.00 40.23           C  
ANISOU 3275  CD2 TYR A 426     4831   5245   5211   -478   -561   2094       C  
ATOM   3276  CE1 TYR A 426      12.806 -14.615   1.647  1.00 35.97           C  
ANISOU 3276  CE1 TYR A 426     4271   4967   4427   -337   -490   2057       C  
ATOM   3277  CE2 TYR A 426      12.231 -15.473  -0.513  1.00 37.77           C  
ANISOU 3277  CE2 TYR A 426     4532   4936   4885   -332   -549   1951       C  
ATOM   3278  CZ  TYR A 426      12.937 -14.582   0.267  1.00 37.63           C  
ANISOU 3278  CZ  TYR A 426     4498   5043   4756   -270   -511   1937       C  
ATOM   3279  OH  TYR A 426      13.771 -13.662  -0.353  1.00 38.17           O  
ANISOU 3279  OH  TYR A 426     4578   5102   4823   -157   -493   1801       O  
ATOM   3280  N   PHE A 427      11.006 -20.085   0.786  1.00 46.62           N  
ANISOU 3280  N   PHE A 427     5846   5616   6252   -789   -768   2509       N  
ATOM   3281  CA  PHE A 427      11.571 -21.078  -0.126  1.00 47.20           C  
ANISOU 3281  CA  PHE A 427     6023   5401   6508   -726   -894   2467       C  
ATOM   3282  C   PHE A 427      11.737 -20.555  -1.551  1.00 45.97           C  
ANISOU 3282  C   PHE A 427     5840   5212   6415   -596   -884   2231       C  
ATOM   3283  O   PHE A 427      10.753 -20.327  -2.260  1.00 46.38           O  
ANISOU 3283  O   PHE A 427     5834   5306   6483   -660   -858   2143       O  
ATOM   3284  CB  PHE A 427      10.678 -22.319  -0.171  1.00 51.00           C  
ANISOU 3284  CB  PHE A 427     6559   5713   7104   -921   -956   2587       C  
ATOM   3285  CG  PHE A 427      10.896 -23.281   0.966  1.00 52.71           C  
ANISOU 3285  CG  PHE A 427     6897   5821   7310  -1030  -1026   2839       C  
ATOM   3286  CD1 PHE A 427      12.117 -23.919   1.124  1.00 53.94           C  
ANISOU 3286  CD1 PHE A 427     7185   5768   7540   -891  -1164   2891       C  
ATOM   3287  CD2 PHE A 427       9.865 -23.581   1.848  1.00 54.78           C  
ANISOU 3287  CD2 PHE A 427     7142   6182   7491  -1275   -958   3026       C  
ATOM   3288  CE1 PHE A 427      12.321 -24.816   2.154  1.00 57.16           C  
ANISOU 3288  CE1 PHE A 427     7734   6049   7934   -981  -1263   3141       C  
ATOM   3289  CE2 PHE A 427      10.060 -24.480   2.883  1.00 58.82           C  
ANISOU 3289  CE2 PHE A 427     7803   6579   7965  -1396  -1027   3285       C  
ATOM   3290  CZ  PHE A 427      11.291 -25.100   3.037  1.00 59.70           C  
ANISOU 3290  CZ  PHE A 427     8076   6462   8146  -1243  -1196   3352       C  
ATOM   3291  N   ALA A 428      12.990 -20.395  -1.968  1.00 44.13           N  
ANISOU 3291  N   ALA A 428     5648   4905   6214   -420   -910   2131       N  
ATOM   3292  CA  ALA A 428      13.331 -20.127  -3.367  1.00 40.24           C  
ANISOU 3292  CA  ALA A 428     5171   4345   5773   -307   -899   1921       C  
ATOM   3293  C   ALA A 428      13.002 -21.327  -4.256  1.00 41.01           C  
ANISOU 3293  C   ALA A 428     5358   4202   6022   -345   -994   1872       C  
ATOM   3294  O   ALA A 428      13.441 -22.453  -3.988  1.00 45.41           O  
ANISOU 3294  O   ALA A 428     5996   4554   6703   -339  -1093   1948       O  
ATOM   3295  CB  ALA A 428      14.805 -19.816  -3.484  1.00 41.20           C  
ANISOU 3295  CB  ALA A 428     5296   4451   5906   -134   -886   1835       C  
ATOM   3296  N   VAL A 429      12.239 -21.073  -5.314  1.00 36.56           N  
ANISOU 3296  N   VAL A 429     4790   3651   5449   -377   -983   1741       N  
ATOM   3297  CA  VAL A 429      11.870 -22.104  -6.278  1.00 37.10           C  
ANISOU 3297  CA  VAL A 429     4948   3504   5644   -416  -1081   1656       C  
ATOM   3298  C   VAL A 429      12.139 -21.630  -7.696  1.00 34.17           C  
ANISOU 3298  C   VAL A 429     4628   3130   5224   -306  -1056   1430       C  
ATOM   3299  O   VAL A 429      12.507 -20.473  -7.923  1.00 33.53           O  
ANISOU 3299  O   VAL A 429     4512   3213   5014   -223   -960   1364       O  
ATOM   3300  CB  VAL A 429      10.387 -22.479  -6.170  1.00 39.51           C  
ANISOU 3300  CB  VAL A 429     5207   3819   5986   -620  -1130   1730       C  
ATOM   3301  CG1 VAL A 429      10.066 -22.945  -4.760  1.00 42.74           C  
ANISOU 3301  CG1 VAL A 429     5579   4247   6411   -764  -1126   1967       C  
ATOM   3302  CG2 VAL A 429       9.510 -21.298  -6.585  1.00 37.33           C  
ANISOU 3302  CG2 VAL A 429     4822   3767   5594   -635  -1072   1647       C  
ATOM   3303  N   ALA A 430      11.966 -22.553  -8.636  1.00 33.54           N  
ANISOU 3303  N   ALA A 430     4650   2854   5240   -318  -1146   1316       N  
ATOM   3304  CA  ALA A 430      12.232 -22.323 -10.041  1.00 32.22           C  
ANISOU 3304  CA  ALA A 430     4572   2662   5010   -226  -1131   1096       C  
ATOM   3305  C   ALA A 430      11.012 -22.808 -10.799  1.00 35.83           C  
ANISOU 3305  C   ALA A 430     5074   3042   5498   -349  -1251   1031       C  
ATOM   3306  O   ALA A 430      10.725 -24.010 -10.822  1.00 39.21           O  
ANISOU 3306  O   ALA A 430     5561   3260   6079   -427  -1363   1037       O  
ATOM   3307  CB  ALA A 430      13.477 -23.089 -10.472  1.00 27.95           C  
ANISOU 3307  CB  ALA A 430     4120   1941   4559    -82  -1126    972       C  
ATOM   3308  N   VAL A 431      10.290 -21.874 -11.413  1.00 36.20           N  
ANISOU 3308  N   VAL A 431     5096   3247   5411   -369  -1246    970       N  
ATOM   3309  CA  VAL A 431       8.998 -22.193 -12.005  1.00 34.33           C  
ANISOU 3309  CA  VAL A 431     4857   2981   5206   -495  -1383    920       C  
ATOM   3310  C   VAL A 431       9.039 -22.200 -13.515  1.00 37.27           C  
ANISOU 3310  C   VAL A 431     5386   3293   5482   -433  -1446    704       C  
ATOM   3311  O   VAL A 431       9.655 -21.340 -14.129  1.00 42.45           O  
ANISOU 3311  O   VAL A 431     6116   4045   5970   -316  -1359    621       O  
ATOM   3312  CB  VAL A 431       7.939 -21.206 -11.558  1.00 30.54           C  
ANISOU 3312  CB  VAL A 431     4217   2723   4666   -565  -1378   1006       C  
ATOM   3313  CG1 VAL A 431       6.567 -21.744 -11.910  1.00 30.85           C  
ANISOU 3313  CG1 VAL A 431     4193   2727   4801   -721  -1533    977       C  
ATOM   3314  CG2 VAL A 431       8.058 -20.949 -10.049  1.00 29.04           C  
ANISOU 3314  CG2 VAL A 431     3886   2644   4503   -602  -1272   1201       C  
ATOM   3315  N   VAL A 432       8.372 -23.180 -14.105  1.00 39.41           N  
ANISOU 3315  N   VAL A 432     5720   3403   5850   -528  -1599    616       N  
ATOM   3316  CA  VAL A 432       8.263 -23.291 -15.551  1.00 42.08           C  
ANISOU 3316  CA  VAL A 432     6225   3682   6082   -489  -1690    399       C  
ATOM   3317  C   VAL A 432       6.820 -23.620 -15.905  1.00 44.24           C  
ANISOU 3317  C   VAL A 432     6447   3938   6422   -646  -1890    370       C  
ATOM   3318  O   VAL A 432       5.961 -23.687 -15.031  1.00 46.03           O  
ANISOU 3318  O   VAL A 432     6492   4220   6778   -782  -1926    516       O  
ATOM   3319  CB  VAL A 432       9.210 -24.387 -16.096  1.00 45.51           C  
ANISOU 3319  CB  VAL A 432     6828   3884   6581   -413  -1685    242       C  
ATOM   3320  CG1 VAL A 432      10.651 -24.011 -15.820  1.00 44.93           C  
ANISOU 3320  CG1 VAL A 432     6766   3853   6453   -248  -1489    244       C  
ATOM   3321  CG2 VAL A 432       8.890 -25.740 -15.475  1.00 47.15           C  
ANISOU 3321  CG2 VAL A 432     7015   3854   7046   -530  -1798    306       C  
ATOM   3322  N   LYS A 433       6.546 -23.817 -17.183  1.00 46.29           N  
ANISOU 3322  N   LYS A 433     6861   4138   6588   -636  -2019    174       N  
ATOM   3323  CA  LYS A 433       5.198 -24.122 -17.614  1.00 50.72           C  
ANISOU 3323  CA  LYS A 433     7369   4687   7216   -782  -2240    120       C  
ATOM   3324  C   LYS A 433       5.053 -25.631 -17.759  1.00 56.55           C  
ANISOU 3324  C   LYS A 433     8182   5153   8153   -901  -2364     34       C  
ATOM   3325  O   LYS A 433       5.995 -26.306 -18.183  1.00 57.34           O  
ANISOU 3325  O   LYS A 433     8465   5073   8248   -811  -2323    -90       O  
ATOM   3326  CB  LYS A 433       4.915 -23.434 -18.944  1.00 51.69           C  
ANISOU 3326  CB  LYS A 433     7637   4902   7103   -707  -2351    -43       C  
ATOM   3327  CG  LYS A 433       5.313 -21.972 -18.970  1.00 51.40           C  
ANISOU 3327  CG  LYS A 433     7607   5075   6847   -569  -2223     26       C  
ATOM   3328  CD  LYS A 433       4.814 -21.286 -20.237  1.00 52.89           C  
ANISOU 3328  CD  LYS A 433     7948   5345   6804   -521  -2381    -96       C  
ATOM   3329  CE  LYS A 433       5.653 -20.068 -20.562  1.00 50.48           C  
ANISOU 3329  CE  LYS A 433     7777   5164   6240   -378  -2224    -65       C  
ATOM   3330  NZ  LYS A 433       7.061 -20.436 -20.925  1.00 48.97           N  
ANISOU 3330  NZ  LYS A 433     7770   4890   5945   -302  -2022   -157       N  
ATOM   3331  N   LYS A 434       3.886 -26.162 -17.393  1.00 59.59           N  
ANISOU 3331  N   LYS A 434     8416   5500   8726  -1106  -2510     92       N  
ATOM   3332  CA  LYS A 434       3.563 -27.562 -17.682  1.00 64.09           C  
ANISOU 3332  CA  LYS A 434     9072   5791   9488  -1253  -2672     -7       C  
ATOM   3333  C   LYS A 434       3.802 -27.823 -19.160  1.00 67.04           C  
ANISOU 3333  C   LYS A 434     9695   6062   9716  -1161  -2798   -291       C  
ATOM   3334  O   LYS A 434       4.429 -28.821 -19.533  1.00 69.65           O  
ANISOU 3334  O   LYS A 434    10211   6139  10112  -1129  -2822   -428       O  
ATOM   3335  CB  LYS A 434       2.099 -27.890 -17.351  1.00 66.74           C  
ANISOU 3335  CB  LYS A 434     9195   6152  10012  -1511  -2833     58       C  
ATOM   3336  CG  LYS A 434       1.886 -28.489 -15.971  1.00 68.66           C  
ANISOU 3336  CG  LYS A 434     9281   6327  10481  -1695  -2747    296       C  
ATOM   3337  CD  LYS A 434       0.520 -29.156 -15.821  1.00 71.73           C  
ANISOU 3337  CD  LYS A 434     9497   6670  11089  -1996  -2911    317       C  
ATOM   3338  CE  LYS A 434       0.441 -30.500 -16.539  1.00 73.91           C  
ANISOU 3338  CE  LYS A 434     9965   6600  11517  -2116  -3111    152       C  
ATOM   3339  NZ  LYS A 434      -0.780 -31.245 -16.143  1.00 74.84           N  
ANISOU 3339  NZ  LYS A 434     9902   6646  11888  -2454  -3237    221       N  
ATOM   3340  N   SER A 435       3.295 -26.903 -19.982  1.00 65.19           N  
ANISOU 3340  N   SER A 435     9471   6025   9274  -1109  -2883   -379       N  
ATOM   3341  CA  SER A 435       3.388 -26.976 -21.439  1.00 64.96           C  
ANISOU 3341  CA  SER A 435     9691   5953   9039  -1033  -3015   -639       C  
ATOM   3342  C   SER A 435       4.788 -27.354 -21.940  1.00 64.26           C  
ANISOU 3342  C   SER A 435     9854   5732   8830   -864  -2859   -786       C  
ATOM   3343  O   SER A 435       4.926 -28.181 -22.846  1.00 68.33           O  
ANISOU 3343  O   SER A 435    10576   6069   9317   -859  -2967  -1023       O  
ATOM   3344  CB  SER A 435       2.950 -25.639 -22.037  1.00 63.21           C  
ANISOU 3344  CB  SER A 435     9464   5994   8560   -950  -3068   -638       C  
ATOM   3345  OG  SER A 435       3.118 -25.627 -23.439  1.00 67.43           O  
ANISOU 3345  OG  SER A 435    10275   6507   8839   -874  -3181   -869       O  
ATOM   3346  N   ALA A 436       5.814 -26.755 -21.340  1.00 60.32           N  
ANISOU 3346  N   ALA A 436     9322   5327   8269   -726  -2605   -663       N  
ATOM   3347  CA  ALA A 436       7.202 -27.018 -21.710  1.00 60.97           C  
ANISOU 3347  CA  ALA A 436     9581   5325   8260   -555  -2424   -798       C  
ATOM   3348  C   ALA A 436       7.705 -28.234 -20.956  1.00 63.69           C  
ANISOU 3348  C   ALA A 436     9899   5404   8896   -568  -2401   -776       C  
ATOM   3349  O   ALA A 436       8.433 -28.106 -19.967  1.00 60.88           O  
ANISOU 3349  O   ALA A 436     9433   5062   8638   -502  -2238   -611       O  
ATOM   3350  CB  ALA A 436       8.080 -25.805 -21.402  1.00 57.81           C  
ANISOU 3350  CB  ALA A 436     9136   5148   7682   -416  -2177   -680       C  
ATOM   3351  N   SER A 437       7.309 -29.414 -21.433  1.00 67.74           N  
ANISOU 3351  N   SER A 437    10528   5662   9548   -652  -2587   -944       N  
ATOM   3352  CA  SER A 437       7.687 -30.691 -20.815  1.00 67.46           C  
ANISOU 3352  CA  SER A 437    10512   5310   9810   -674  -2618   -934       C  
ATOM   3353  C   SER A 437       9.200 -30.947 -20.851  1.00 66.77           C  
ANISOU 3353  C   SER A 437    10520   5132   9715   -437  -2429  -1046       C  
ATOM   3354  O   SER A 437       9.745 -31.620 -19.978  1.00 64.66           O  
ANISOU 3354  O   SER A 437    10211   4676   9683   -400  -2401   -942       O  
ATOM   3355  CB  SER A 437       6.947 -31.836 -21.514  1.00 70.18           C  
ANISOU 3355  CB  SER A 437    10996   5387  10283   -811  -2873  -1136       C  
ATOM   3356  OG  SER A 437       6.921 -31.634 -22.916  1.00 70.15           O  
ANISOU 3356  OG  SER A 437    11184   5450  10019   -740  -2933  -1424       O  
ATOM   3357  N   ASP A 438       9.862 -30.367 -21.847  1.00 68.69           N  
ANISOU 3357  N   ASP A 438    10886   5527   9685   -281  -2300  -1249       N  
ATOM   3358  CA  ASP A 438      11.265 -30.646 -22.160  1.00 69.96           C  
ANISOU 3358  CA  ASP A 438    11136   5624   9820    -55  -2116  -1437       C  
ATOM   3359  C   ASP A 438      12.273 -30.250 -21.071  1.00 63.93           C  
ANISOU 3359  C   ASP A 438    10197   4937   9155     66  -1915  -1243       C  
ATOM   3360  O   ASP A 438      13.345 -30.835 -20.985  1.00 67.08           O  
ANISOU 3360  O   ASP A 438    10613   5197   9676    238  -1824  -1363       O  
ATOM   3361  CB  ASP A 438      11.642 -29.928 -23.467  1.00 75.12           C  
ANISOU 3361  CB  ASP A 438    11947   6489  10106     39  -1991  -1669       C  
ATOM   3362  CG  ASP A 438      10.549 -30.031 -24.539  1.00 82.09           C  
ANISOU 3362  CG  ASP A 438    13002   7369  10820    -90  -2209  -1825       C  
ATOM   3363  OD1 ASP A 438      10.027 -31.149 -24.787  1.00 85.88           O  
ANISOU 3363  OD1 ASP A 438    13576   7583  11469   -166  -2421  -1970       O  
ATOM   3364  OD2 ASP A 438      10.213 -28.982 -25.129  1.00 82.67           O  
ANISOU 3364  OD2 ASP A 438    13124   7696  10593   -117  -2187  -1801       O  
ATOM   3365  N   LEU A 439      11.933 -29.266 -20.246  1.00 57.85           N  
ANISOU 3365  N   LEU A 439     9253   4386   8339    -12  -1859   -961       N  
ATOM   3366  CA  LEU A 439      12.912 -28.620 -19.373  1.00 56.11           C  
ANISOU 3366  CA  LEU A 439     8880   4306   8134    103  -1659   -803       C  
ATOM   3367  C   LEU A 439      13.168 -29.364 -18.076  1.00 56.75           C  
ANISOU 3367  C   LEU A 439     8853   4196   8515    105  -1713   -613       C  
ATOM   3368  O   LEU A 439      12.241 -29.843 -17.433  1.00 58.29           O  
ANISOU 3368  O   LEU A 439     9014   4271   8863    -65  -1874   -442       O  
ATOM   3369  CB  LEU A 439      12.450 -27.205 -19.009  1.00 54.16           C  
ANISOU 3369  CB  LEU A 439     8509   4366   7702     25  -1583   -593       C  
ATOM   3370  CG  LEU A 439      12.128 -26.243 -20.150  1.00 53.74           C  
ANISOU 3370  CG  LEU A 439     8567   4522   7330     13  -1546   -707       C  
ATOM   3371  CD1 LEU A 439      11.602 -24.946 -19.567  1.00 51.00           C  
ANISOU 3371  CD1 LEU A 439     8084   4419   6876    -56  -1511   -472       C  
ATOM   3372  CD2 LEU A 439      13.341 -25.998 -21.034  1.00 54.13           C  
ANISOU 3372  CD2 LEU A 439     8731   4645   7192    172  -1339   -925       C  
ATOM   3373  N   THR A 440      14.436 -29.425 -17.685  1.00 58.41           N  
ANISOU 3373  N   THR A 440     9003   4390   8800    291  -1579   -635       N  
ATOM   3374  CA  THR A 440      14.823 -29.908 -16.360  1.00 59.55           C  
ANISOU 3374  CA  THR A 440     9042   4399   9187    318  -1625   -419       C  
ATOM   3375  C   THR A 440      16.008 -29.118 -15.824  1.00 58.08           C  
ANISOU 3375  C   THR A 440     8704   4409   8953    477  -1434   -362       C  
ATOM   3376  O   THR A 440      16.739 -28.469 -16.575  1.00 54.98           O  
ANISOU 3376  O   THR A 440     8302   4193   8395    591  -1255   -543       O  
ATOM   3377  CB  THR A 440      15.177 -31.414 -16.354  1.00 62.33           C  
ANISOU 3377  CB  THR A 440     9508   4359   9816    404  -1776   -536       C  
ATOM   3378  OG1 THR A 440      16.092 -31.706 -17.421  1.00 63.25           O  
ANISOU 3378  OG1 THR A 440     9708   4425   9899    613  -1684   -883       O  
ATOM   3379  CG2 THR A 440      13.919 -32.260 -16.509  1.00 64.88           C  
ANISOU 3379  CG2 THR A 440     9955   4451  10246    191  -1998   -511       C  
ATOM   3380  N   TRP A 441      16.188 -29.201 -14.511  1.00 59.54           N  
ANISOU 3380  N   TRP A 441     8780   4562   9281    466  -1479   -109       N  
ATOM   3381  CA  TRP A 441      17.213 -28.444 -13.797  1.00 57.50           C  
ANISOU 3381  CA  TRP A 441     8360   4491   8997    589  -1339    -19       C  
ATOM   3382  C   TRP A 441      18.617 -28.666 -14.379  1.00 59.47           C  
ANISOU 3382  C   TRP A 441     8579   4711   9305    836  -1223   -283       C  
ATOM   3383  O   TRP A 441      19.463 -27.771 -14.332  1.00 59.40           O  
ANISOU 3383  O   TRP A 441     8437   4934   9198    922  -1046   -311       O  
ATOM   3384  CB  TRP A 441      17.139 -28.802 -12.311  1.00 55.87           C  
ANISOU 3384  CB  TRP A 441     8089   4190   8950    539  -1461    279       C  
ATOM   3385  CG  TRP A 441      18.188 -28.220 -11.480  1.00 56.33           C  
ANISOU 3385  CG  TRP A 441     7993   4395   9014    667  -1375    370       C  
ATOM   3386  CD1 TRP A 441      19.062 -28.894 -10.688  1.00 60.66           C  
ANISOU 3386  CD1 TRP A 441     8504   4781   9764    813  -1471    434       C  
ATOM   3387  CD2 TRP A 441      18.501 -26.833 -11.341  1.00 57.64           C  
ANISOU 3387  CD2 TRP A 441     8024   4891   8985    663  -1198    406       C  
ATOM   3388  NE1 TRP A 441      19.907 -28.014 -10.058  1.00 61.10           N  
ANISOU 3388  NE1 TRP A 441     8392   5063   9760    897  -1368    499       N  
ATOM   3389  CE2 TRP A 441      19.584 -26.740 -10.442  1.00 58.01           C  
ANISOU 3389  CE2 TRP A 441     7941   4971   9129    799  -1193    480       C  
ATOM   3390  CE3 TRP A 441      17.969 -25.657 -11.881  1.00 57.96           C  
ANISOU 3390  CE3 TRP A 441     8050   5185   8787    559  -1065    385       C  
ATOM   3391  CZ2 TRP A 441      20.146 -25.517 -10.069  1.00 56.72           C  
ANISOU 3391  CZ2 TRP A 441     7629   5089   8834    815  -1048    523       C  
ATOM   3392  CZ3 TRP A 441      18.531 -24.437 -11.511  1.00 55.82           C  
ANISOU 3392  CZ3 TRP A 441     7649   5174   8388    582   -919    437       C  
ATOM   3393  CH2 TRP A 441      19.608 -24.380 -10.614  1.00 55.81           C  
ANISOU 3393  CH2 TRP A 441     7514   5202   8491    700   -907    500       C  
ATOM   3394  N   ASP A 442      18.848 -29.841 -14.953  1.00 62.44           N  
ANISOU 3394  N   ASP A 442     9070   4807   9845    945  -1316   -492       N  
ATOM   3395  CA  ASP A 442      20.101 -30.124 -15.641  1.00 71.06           C  
ANISOU 3395  CA  ASP A 442    10127   5874  10998   1189  -1193   -797       C  
ATOM   3396  C   ASP A 442      20.173 -29.436 -17.009  1.00 75.03           C  
ANISOU 3396  C   ASP A 442    10686   6596  11225   1182   -983  -1054       C  
ATOM   3397  O   ASP A 442      21.212 -28.894 -17.387  1.00 77.98           O  
ANISOU 3397  O   ASP A 442    10950   7158  11522   1309   -766  -1212       O  
ATOM   3398  CB  ASP A 442      20.260 -31.632 -15.830  1.00 78.59           C  
ANISOU 3398  CB  ASP A 442    11205   6433  12223   1318  -1373   -960       C  
ATOM   3399  CG  ASP A 442      20.266 -32.393 -14.512  1.00 83.00           C  
ANISOU 3399  CG  ASP A 442    11748   6736  13052   1332  -1596   -696       C  
ATOM   3400  OD1 ASP A 442      21.211 -32.191 -13.710  1.00 84.23           O  
ANISOU 3400  OD1 ASP A 442    11742   6953  13309   1479  -1574   -607       O  
ATOM   3401  OD2 ASP A 442      19.327 -33.193 -14.286  1.00 83.51           O  
ANISOU 3401  OD2 ASP A 442    11969   6539  13222   1184  -1800   -575       O  
ATOM   3402  N   ASN A 443      19.052 -29.436 -17.728  1.00 75.99           N  
ANISOU 3402  N   ASN A 443    10981   6703  11191   1017  -1052  -1084       N  
ATOM   3403  CA  ASN A 443      19.007 -29.092 -19.156  1.00 75.39           C  
ANISOU 3403  CA  ASN A 443    11036   6757  10851   1011   -916  -1353       C  
ATOM   3404  C   ASN A 443      18.935 -27.590 -19.472  1.00 70.14           C  
ANISOU 3404  C   ASN A 443    10336   6449   9867    911   -727  -1270       C  
ATOM   3405  O   ASN A 443      18.658 -27.213 -20.611  1.00 70.98           O  
ANISOU 3405  O   ASN A 443    10592   6666   9709    859   -651  -1428       O  
ATOM   3406  CB  ASN A 443      17.785 -29.791 -19.790  1.00 79.37           C  
ANISOU 3406  CB  ASN A 443    11754   7072  11332    875  -1123  -1424       C  
ATOM   3407  CG  ASN A 443      18.114 -30.513 -21.094  1.00 84.13           C  
ANISOU 3407  CG  ASN A 443    12533   7557  11874    988  -1089  -1816       C  
ATOM   3408  OD1 ASN A 443      19.135 -31.194 -21.202  1.00 87.53           O  
ANISOU 3408  OD1 ASN A 443    12931   7860  12466   1197  -1020  -2030       O  
ATOM   3409  ND2 ASN A 443      17.223 -30.396 -22.078  1.00 83.63           N  
ANISOU 3409  ND2 ASN A 443    12658   7534  11585    858  -1154  -1925       N  
ATOM   3410  N   LEU A 444      19.193 -26.730 -18.490  1.00 57.70           N  
ANISOU 3410  N   LEU A 444     8179   5185   8560   1432   -358   -610       N  
ATOM   3411  CA  LEU A 444      18.884 -25.296 -18.645  1.00 50.58           C  
ANISOU 3411  CA  LEU A 444     7127   4619   7472   1277   -268   -526       C  
ATOM   3412  C   LEU A 444      19.776 -24.519 -19.605  1.00 48.24           C  
ANISOU 3412  C   LEU A 444     6700   4613   7016   1415    -98   -641       C  
ATOM   3413  O   LEU A 444      19.372 -23.463 -20.072  1.00 46.71           O  
ANISOU 3413  O   LEU A 444     6453   4643   6651   1286    -31   -615       O  
ATOM   3414  CB  LEU A 444      18.864 -24.590 -17.288  1.00 44.77           C  
ANISOU 3414  CB  LEU A 444     6262   3975   6775   1160   -294   -250       C  
ATOM   3415  CG  LEU A 444      17.615 -24.900 -16.465  1.00 40.94           C  
ANISOU 3415  CG  LEU A 444     5877   3324   6354    930   -417   -106       C  
ATOM   3416  CD1 LEU A 444      17.686 -24.263 -15.097  1.00 38.13           C  
ANISOU 3416  CD1 LEU A 444     5407   3072   6007    852   -432    147       C  
ATOM   3417  CD2 LEU A 444      16.381 -24.429 -17.193  1.00 39.48           C  
ANISOU 3417  CD2 LEU A 444     5730   3226   6044    734   -423   -179       C  
ATOM   3418  N   LYS A 445      20.972 -25.027 -19.896  1.00 50.69           N  
ANISOU 3418  N   LYS A 445     6955   4925   7380   1677    -22   -757       N  
ATOM   3419  CA  LYS A 445      21.880 -24.364 -20.833  1.00 49.09           C  
ANISOU 3419  CA  LYS A 445     6608   5019   7023   1805    170   -863       C  
ATOM   3420  C   LYS A 445      21.105 -23.943 -22.066  1.00 46.82           C  
ANISOU 3420  C   LYS A 445     6435   4847   6506   1699    222   -997       C  
ATOM   3421  O   LYS A 445      20.361 -24.739 -22.635  1.00 50.19           O  
ANISOU 3421  O   LYS A 445     7066   5088   6917   1691    132  -1167       O  
ATOM   3422  CB  LYS A 445      23.028 -25.296 -21.250  1.00 52.97           C  
ANISOU 3422  CB  LYS A 445     7071   5459   7596   2132    239  -1052       C  
ATOM   3423  CG  LYS A 445      23.874 -24.780 -22.430  1.00 55.34           C  
ANISOU 3423  CG  LYS A 445     7242   6078   7707   2269    467  -1204       C  
ATOM   3424  CD  LYS A 445      25.100 -25.670 -22.720  1.00 61.43           C  
ANISOU 3424  CD  LYS A 445     7931   6837   8573   2628    553  -1388       C  
ATOM   3425  CE  LYS A 445      24.743 -26.963 -23.500  1.00 64.28           C  
ANISOU 3425  CE  LYS A 445     8565   6918   8941   2806    493  -1683       C  
ATOM   3426  NZ  LYS A 445      24.480 -26.748 -24.968  1.00 61.40           N  
ANISOU 3426  NZ  LYS A 445     8303   6733   8293   2812    629  -1912       N  
ATOM   3427  N   GLY A 446      21.273 -22.685 -22.461  1.00 41.25           N  
ANISOU 3427  N   GLY A 446     5606   4441   5625   1611    354   -914       N  
ATOM   3428  CA  GLY A 446      20.698 -22.176 -23.696  1.00 41.10           C  
ANISOU 3428  CA  GLY A 446     5687   4578   5353   1543    417  -1017       C  
ATOM   3429  C   GLY A 446      19.209 -21.902 -23.636  1.00 41.44           C  
ANISOU 3429  C   GLY A 446     5861   4543   5343   1318    263   -959       C  
ATOM   3430  O   GLY A 446      18.575 -21.710 -24.680  1.00 44.77           O  
ANISOU 3430  O   GLY A 446     6398   5053   5561   1278    259  -1071       O  
ATOM   3431  N   LYS A 447      18.650 -21.883 -22.428  1.00 38.06           N  
ANISOU 3431  N   LYS A 447     5404   3974   5082   1179    136   -787       N  
ATOM   3432  CA  LYS A 447      17.257 -21.538 -22.235  1.00 40.18           C  
ANISOU 3432  CA  LYS A 447     5740   4209   5317    967      6   -711       C  
ATOM   3433  C   LYS A 447      17.160 -20.085 -21.808  1.00 39.53           C  
ANISOU 3433  C   LYS A 447     5534   4328   5159    851     61   -502       C  
ATOM   3434  O   LYS A 447      18.185 -19.451 -21.596  1.00 43.32           O  
ANISOU 3434  O   LYS A 447     5886   4938   5635    909    184   -418       O  
ATOM   3435  CB  LYS A 447      16.621 -22.465 -21.201  1.00 43.34           C  
ANISOU 3435  CB  LYS A 447     6195   4337   5934    879   -150   -655       C  
ATOM   3436  CG  LYS A 447      16.621 -23.931 -21.618  1.00 49.54           C  
ANISOU 3436  CG  LYS A 447     7144   4858   6820    972   -229   -863       C  
ATOM   3437  CD  LYS A 447      15.768 -24.168 -22.854  1.00 52.60           C  
ANISOU 3437  CD  LYS A 447     7674   5255   7056    918   -292  -1079       C  
ATOM   3438  CE  LYS A 447      16.007 -25.548 -23.440  1.00 58.50           C  
ANISOU 3438  CE  LYS A 447     8600   5749   7877   1052   -348  -1339       C  
ATOM   3439  NZ  LYS A 447      15.220 -25.735 -24.700  1.00 61.49           N  
ANISOU 3439  NZ  LYS A 447     9122   6166   8076   1000   -423  -1579       N  
ATOM   3440  N   LYS A 448      15.931 -19.570 -21.693  1.00 39.03           N  
ANISOU 3440  N   LYS A 448     5502   4285   5043    691    -35   -430       N  
ATOM   3441  CA  LYS A 448      15.665 -18.153 -21.367  1.00 39.34           C  
ANISOU 3441  CA  LYS A 448     5460   4486   5002    596     -2   -255       C  
ATOM   3442  C   LYS A 448      15.205 -17.974 -19.919  1.00 34.37           C  
ANISOU 3442  C   LYS A 448     4756   3781   4520    489    -78    -91       C  
ATOM   3443  O   LYS A 448      14.376 -18.743 -19.459  1.00 32.46           O  
ANISOU 3443  O   LYS A 448     4553   3405   4377    413   -190   -100       O  
ATOM   3444  CB  LYS A 448      14.579 -17.588 -22.302  1.00 41.29           C  
ANISOU 3444  CB  LYS A 448     5786   4840   5063    533    -58   -292       C  
ATOM   3445  CG  LYS A 448      14.832 -17.809 -23.799  1.00 45.03           C  
ANISOU 3445  CG  LYS A 448     6367   5407   5336    632     -5   -464       C  
ATOM   3446  CD  LYS A 448      13.879 -16.970 -24.643  1.00 47.24           C  
ANISOU 3446  CD  LYS A 448     6713   5834   5402    584    -63   -446       C  
ATOM   3447  CE  LYS A 448      13.927 -17.325 -26.114  1.00 51.22           C  
ANISOU 3447  CE  LYS A 448     7352   6435   5674    673    -47   -632       C  
ATOM   3448  NZ  LYS A 448      13.120 -18.547 -26.408  1.00 54.91           N  
ANISOU 3448  NZ  LYS A 448     7908   6771   6184    648   -216   -842       N  
ATOM   3449  N   SER A 449      15.690 -16.945 -19.215  1.00 32.65           N  
ANISOU 3449  N   SER A 449     4440   3658   4309    466    -18     56       N  
ATOM   3450  CA  SER A 449      15.410 -16.833 -17.769  1.00 31.89           C  
ANISOU 3450  CA  SER A 449     4281   3506   4331    390    -80    193       C  
ATOM   3451  C   SER A 449      14.831 -15.519 -17.281  1.00 32.35           C  
ANISOU 3451  C   SER A 449     4300   3668   4323    306    -84    309       C  
ATOM   3452  O   SER A 449      15.009 -14.460 -17.888  1.00 31.08           O  
ANISOU 3452  O   SER A 449     4144   3613   4052    311    -23    326       O  
ATOM   3453  CB  SER A 449      16.656 -17.152 -16.940  1.00 33.39           C  
ANISOU 3453  CB  SER A 449     4388   3659   4639    464    -48    245       C  
ATOM   3454  OG  SER A 449      17.656 -16.165 -17.083  1.00 34.45           O  
ANISOU 3454  OG  SER A 449     4430   3933   4726    490     53    281       O  
ATOM   3455  N   CYS A 450      14.144 -15.614 -16.144  1.00 31.05           N  
ANISOU 3455  N   CYS A 450     4108   3463   4227    234   -153    393       N  
ATOM   3456  CA  CYS A 450      13.501 -14.477 -15.522  1.00 27.56           C  
ANISOU 3456  CA  CYS A 450     3632   3107   3733    178   -163    481       C  
ATOM   3457  C   CYS A 450      13.857 -14.446 -14.042  1.00 24.60           C  
ANISOU 3457  C   CYS A 450     3202   2717   3429    156   -176    581       C  
ATOM   3458  O   CYS A 450      13.638 -15.411 -13.323  1.00 25.11           O  
ANISOU 3458  O   CYS A 450     3266   2704   3570    128   -220    618       O  
ATOM   3459  CB  CYS A 450      11.987 -14.555 -15.718  1.00 27.90           C  
ANISOU 3459  CB  CYS A 450     3685   3175   3741    117   -233    462       C  
ATOM   3460  SG  CYS A 450      11.482 -14.826 -17.437  1.00 29.23           S  
ANISOU 3460  SG  CYS A 450     3928   3369   3810    143   -266    326       S  
ATOM   3461  N   HIS A 451      14.418 -13.322 -13.611  1.00 25.49           N  
ANISOU 3461  N   HIS A 451     3282   2896   3508    161   -143    626       N  
ATOM   3462  CA  HIS A 451      14.875 -13.136 -12.247  1.00 25.53           C  
ANISOU 3462  CA  HIS A 451     3241   2913   3547    147   -167    700       C  
ATOM   3463  C   HIS A 451      14.195 -11.921 -11.664  1.00 23.93           C  
ANISOU 3463  C   HIS A 451     3047   2778   3269    115   -174    727       C  
ATOM   3464  O   HIS A 451      13.985 -10.939 -12.368  1.00 21.91           O  
ANISOU 3464  O   HIS A 451     2824   2544   2956    121   -146    700       O  
ATOM   3465  CB  HIS A 451      16.374 -12.856 -12.229  1.00 28.54           C  
ANISOU 3465  CB  HIS A 451     3563   3314   3968    180   -137    698       C  
ATOM   3466  CG  HIS A 451      17.183 -13.834 -13.008  1.00 29.90           C  
ANISOU 3466  CG  HIS A 451     3712   3446   4204    253   -105    644       C  
ATOM   3467  ND1 HIS A 451      17.876 -14.863 -12.413  1.00 33.11           N  
ANISOU 3467  ND1 HIS A 451     4078   3796   4705    319   -148    664       N  
ATOM   3468  CD2 HIS A 451      17.409 -13.945 -14.336  1.00 31.22           C  
ANISOU 3468  CD2 HIS A 451     3900   3623   4341    293    -33    565       C  
ATOM   3469  CE1 HIS A 451      18.499 -15.566 -13.340  1.00 33.83           C  
ANISOU 3469  CE1 HIS A 451     4158   3855   4839    409   -101    584       C  
ATOM   3470  NE2 HIS A 451      18.225 -15.035 -14.516  1.00 35.06           N  
ANISOU 3470  NE2 HIS A 451     4350   4060   4910    389    -24    517       N  
ATOM   3471  N   THR A 452      13.891 -11.977 -10.370  1.00 26.11           N  
ANISOU 3471  N   THR A 452     3305   3082   3533     94   -208    781       N  
ATOM   3472  CA  THR A 452      13.426 -10.799  -9.630  1.00 25.51           C  
ANISOU 3472  CA  THR A 452     3240   3072   3379     91   -212    781       C  
ATOM   3473  C   THR A 452      14.385  -9.627  -9.838  1.00 23.05           C  
ANISOU 3473  C   THR A 452     2946   2746   3064     91   -202    749       C  
ATOM   3474  O   THR A 452      13.948  -8.519 -10.168  1.00 19.46           O  
ANISOU 3474  O   THR A 452     2544   2284   2564    103   -190    720       O  
ATOM   3475  CB  THR A 452      13.324 -11.072  -8.113  1.00 24.52           C  
ANISOU 3475  CB  THR A 452     3100   3002   3216     77   -242    839       C  
ATOM   3476  OG1 THR A 452      14.608 -11.465  -7.622  1.00 27.58           O  
ANISOU 3476  OG1 THR A 452     3465   3367   3646     82   -284    869       O  
ATOM   3477  CG2 THR A 452      12.308 -12.165  -7.815  1.00 21.87           C  
ANISOU 3477  CG2 THR A 452     2747   2680   2883     41   -235    901       C  
ATOM   3478  N   ALA A 453      15.682  -9.897  -9.636  1.00 21.53           N  
ANISOU 3478  N   ALA A 453     2705   2545   2931     77   -215    759       N  
ATOM   3479  CA  ALA A 453      16.759  -8.910  -9.788  1.00 20.61           C  
ANISOU 3479  CA  ALA A 453     2570   2424   2839     35   -206    736       C  
ATOM   3480  C   ALA A 453      18.101  -9.526  -9.410  1.00 24.76           C  
ANISOU 3480  C   ALA A 453     2985   2980   3440     33   -236    750       C  
ATOM   3481  O   ALA A 453      18.150 -10.470  -8.619  1.00 27.30           O  
ANISOU 3481  O   ALA A 453     3279   3319   3773     75   -293    786       O  
ATOM   3482  CB  ALA A 453      16.500  -7.657  -8.917  1.00 12.07           C  
ANISOU 3482  CB  ALA A 453     1546   1341   1700      6   -249    707       C  
ATOM   3483  N   VAL A 454      19.191  -8.973  -9.943  1.00 27.21           N  
ANISOU 3483  N   VAL A 454     3228   3306   3805    -16   -200    732       N  
ATOM   3484  CA  VAL A 454      20.524  -9.416  -9.545  1.00 30.94           C  
ANISOU 3484  CA  VAL A 454     3552   3843   4361    -11   -238    735       C  
ATOM   3485  C   VAL A 454      20.763  -9.109  -8.054  1.00 31.99           C  
ANISOU 3485  C   VAL A 454     3667   4019   4469    -39   -367    737       C  
ATOM   3486  O   VAL A 454      20.425  -8.021  -7.561  1.00 25.93           O  
ANISOU 3486  O   VAL A 454     2975   3233   3644   -110   -400    703       O  
ATOM   3487  CB  VAL A 454      21.645  -8.763 -10.395  1.00 34.05           C  
ANISOU 3487  CB  VAL A 454     3840   4279   4819    -89   -158    719       C  
ATOM   3488  CG1 VAL A 454      21.338  -8.892 -11.872  1.00 33.89           C  
ANISOU 3488  CG1 VAL A 454     3871   4236   4769    -64    -24    718       C  
ATOM   3489  CG2 VAL A 454      21.838  -7.309 -10.024  1.00 38.19           C  
ANISOU 3489  CG2 VAL A 454     4396   4778   5335   -232   -188    706       C  
ATOM   3490  N   GLY A 455      21.322 -10.084  -7.341  1.00 33.49           N  
ANISOU 3490  N   GLY A 455     3774   4260   4689     35   -448    771       N  
ATOM   3491  CA  GLY A 455      21.679  -9.920  -5.934  1.00 35.64           C  
ANISOU 3491  CA  GLY A 455     4025   4604   4913     25   -588    778       C  
ATOM   3492  C   GLY A 455      20.570 -10.254  -4.949  1.00 36.54           C  
ANISOU 3492  C   GLY A 455     4274   4714   4897     64   -632    825       C  
ATOM   3493  O   GLY A 455      20.772 -10.143  -3.738  1.00 37.75           O  
ANISOU 3493  O   GLY A 455     4435   4944   4965     66   -745    834       O  
ATOM   3494  N   ARG A 456      19.399 -10.638  -5.460  1.00 33.87           N  
ANISOU 3494  N   ARG A 456     4033   4306   4532     87   -543    852       N  
ATOM   3495  CA  ARG A 456      18.304 -11.088  -4.612  1.00 33.40           C  
ANISOU 3495  CA  ARG A 456     4069   4262   4360    109   -554    914       C  
ATOM   3496  C   ARG A 456      18.337 -12.604  -4.415  1.00 37.38           C  
ANISOU 3496  C   ARG A 456     4572   4726   4905    174   -580   1027       C  
ATOM   3497  O   ARG A 456      18.836 -13.355  -5.266  1.00 39.24           O  
ANISOU 3497  O   ARG A 456     4762   4884   5263    222   -560   1030       O  
ATOM   3498  CB  ARG A 456      16.961 -10.651  -5.193  1.00 31.43           C  
ANISOU 3498  CB  ARG A 456     3896   3977   4068     85   -456    882       C  
ATOM   3499  CG  ARG A 456      16.728  -9.158  -5.044  1.00 30.05           C  
ANISOU 3499  CG  ARG A 456     3768   3822   3829     51   -451    787       C  
ATOM   3500  CD  ARG A 456      15.449  -8.691  -5.694  1.00 24.87           C  
ANISOU 3500  CD  ARG A 456     3171   3135   3141     65   -369    757       C  
ATOM   3501  NE  ARG A 456      14.285  -9.114  -4.940  1.00 23.90           N  
ANISOU 3501  NE  ARG A 456     3070   3089   2920     93   -346    796       N  
ATOM   3502  CZ  ARG A 456      13.063  -8.612  -5.075  1.00 23.02           C  
ANISOU 3502  CZ  ARG A 456     2982   3010   2753    125   -291    761       C  
ATOM   3503  NH1 ARG A 456      12.801  -7.640  -5.951  1.00 23.05           N  
ANISOU 3503  NH1 ARG A 456     3021   2951   2786    151   -270    690       N  
ATOM   3504  NH2 ARG A 456      12.089  -9.100  -4.317  1.00 24.72           N  
ANISOU 3504  NH2 ARG A 456     3181   3331   2882    135   -254    808       N  
ATOM   3505  N   THR A 457      17.780 -13.046  -3.291  1.00 36.75           N  
ANISOU 3505  N   THR A 457     4560   4692   4713    179   -620   1120       N  
ATOM   3506  CA  THR A 457      17.931 -14.423  -2.843  1.00 33.68           C  
ANISOU 3506  CA  THR A 457     4200   4248   4351    233   -672   1260       C  
ATOM   3507  C   THR A 457      17.415 -15.419  -3.865  1.00 31.24           C  
ANISOU 3507  C   THR A 457     3921   3783   4168    235   -602   1283       C  
ATOM   3508  O   THR A 457      18.191 -16.165  -4.470  1.00 32.23           O  
ANISOU 3508  O   THR A 457     4012   3808   4425    313   -628   1278       O  
ATOM   3509  CB  THR A 457      17.209 -14.666  -1.510  1.00 32.43           C  
ANISOU 3509  CB  THR A 457     4131   4172   4018    210   -693   1382       C  
ATOM   3510  OG1 THR A 457      17.616 -13.687  -0.547  1.00 31.37           O  
ANISOU 3510  OG1 THR A 457     3990   4192   3737    212   -765   1327       O  
ATOM   3511  CG2 THR A 457      17.529 -16.052  -0.992  1.00 32.68           C  
ANISOU 3511  CG2 THR A 457     4215   4124   4078    267   -767   1557       C  
ATOM   3512  N   ALA A 458      16.104 -15.426  -4.053  1.00 30.31           N  
ANISOU 3512  N   ALA A 458     3856   3652   4008    155   -518   1293       N  
ATOM   3513  CA  ALA A 458      15.449 -16.474  -4.841  1.00 29.60           C  
ANISOU 3513  CA  ALA A 458     3808   3416   4023    124   -477   1320       C  
ATOM   3514  C   ALA A 458      15.596 -16.233  -6.336  1.00 29.37           C  
ANISOU 3514  C   ALA A 458     3742   3326   4091    143   -429   1176       C  
ATOM   3515  O   ALA A 458      15.504 -17.164  -7.122  1.00 33.79           O  
ANISOU 3515  O   ALA A 458     4337   3749   4755    154   -424   1157       O  
ATOM   3516  CB  ALA A 458      13.980 -16.574  -4.471  1.00 23.78           C  
ANISOU 3516  CB  ALA A 458     3104   2721   3209     12   -412   1383       C  
ATOM   3517  N   GLY A 459      15.818 -14.981  -6.718  1.00 25.96           N  
ANISOU 3517  N   GLY A 459     3260   2990   3615    144   -396   1076       N  
ATOM   3518  CA  GLY A 459      15.933 -14.618  -8.110  1.00 22.31           C  
ANISOU 3518  CA  GLY A 459     2776   2497   3202    155   -340    964       C  
ATOM   3519  C   GLY A 459      17.345 -14.655  -8.622  1.00 21.88           C  
ANISOU 3519  C   GLY A 459     2655   2434   3226    230   -344    916       C  
ATOM   3520  O   GLY A 459      17.552 -14.645  -9.821  1.00 22.72           O  
ANISOU 3520  O   GLY A 459     2750   2514   3368    254   -284    836       O  
ATOM   3521  N   TRP A 460      18.330 -14.684  -7.735  1.00 25.06           N  
ANISOU 3521  N   TRP A 460     2998   2882   3644    273   -412    962       N  
ATOM   3522  CA  TRP A 460      19.713 -14.676  -8.191  1.00 29.65           C  
ANISOU 3522  CA  TRP A 460     3464   3493   4310    345   -412    913       C  
ATOM   3523  C   TRP A 460      20.647 -15.516  -7.335  1.00 34.09           C  
ANISOU 3523  C   TRP A 460     3968   4054   4933    449   -518    982       C  
ATOM   3524  O   TRP A 460      21.178 -16.528  -7.807  1.00 37.72           O  
ANISOU 3524  O   TRP A 460     4405   4432   5496    569   -521    972       O  
ATOM   3525  CB  TRP A 460      20.236 -13.242  -8.254  1.00 32.86           C  
ANISOU 3525  CB  TRP A 460     3794   4010   4680    268   -388    859       C  
ATOM   3526  CG  TRP A 460      21.523 -13.140  -8.989  1.00 33.55           C  
ANISOU 3526  CG  TRP A 460     3737   4153   4856    304   -344    806       C  
ATOM   3527  CD1 TRP A 460      22.779 -13.113  -8.456  1.00 32.49           C  
ANISOU 3527  CD1 TRP A 460     3445   4112   4787    336   -412    810       C  
ATOM   3528  CD2 TRP A 460      21.680 -13.066 -10.404  1.00 31.53           C  
ANISOU 3528  CD2 TRP A 460     3462   3892   4623    312   -216    740       C  
ATOM   3529  NE1 TRP A 460      23.713 -13.012  -9.463  1.00 34.53           N  
ANISOU 3529  NE1 TRP A 460     3564   4434   5123    357   -315    751       N  
ATOM   3530  CE2 TRP A 460      23.064 -12.989 -10.668  1.00 32.05           C  
ANISOU 3530  CE2 TRP A 460     3345   4060   4771    345   -186    711       C  
ATOM   3531  CE3 TRP A 460      20.784 -13.054 -11.475  1.00 32.08           C  
ANISOU 3531  CE3 TRP A 460     3646   3905   4639    297   -128    702       C  
ATOM   3532  CZ2 TRP A 460      23.573 -12.897 -11.961  1.00 31.50           C  
ANISOU 3532  CZ2 TRP A 460     3211   4042   4717    360    -43    652       C  
ATOM   3533  CZ3 TRP A 460      21.287 -12.970 -12.763  1.00 32.76           C  
ANISOU 3533  CZ3 TRP A 460     3691   4031   4725    319     -9    641       C  
ATOM   3534  CH2 TRP A 460      22.672 -12.893 -12.994  1.00 33.11           C  
ANISOU 3534  CH2 TRP A 460     3559   4183   4839    349     46    620       C  
ATOM   3535  N   ASN A 461      20.834 -15.105  -6.082  1.00 32.68           N  
ANISOU 3535  N   ASN A 461     3775   3964   4679    423   -615   1046       N  
ATOM   3536  CA  ASN A 461      21.878 -15.682  -5.249  1.00 35.39           C  
ANISOU 3536  CA  ASN A 461     4038   4347   5059    531   -744   1111       C  
ATOM   3537  C   ASN A 461      21.740 -17.189  -5.133  1.00 36.03           C  
ANISOU 3537  C   ASN A 461     4208   4275   5208    651   -787   1210       C  
ATOM   3538  O   ASN A 461      22.726 -17.921  -5.297  1.00 39.29           O  
ANISOU 3538  O   ASN A 461     4538   4655   5735    805   -841   1212       O  
ATOM   3539  CB  ASN A 461      21.911 -15.012  -3.873  1.00 38.31           C  
ANISOU 3539  CB  ASN A 461     4418   4845   5292    476   -854   1160       C  
ATOM   3540  CG  ASN A 461      22.371 -13.550  -3.941  1.00 38.61           C  
ANISOU 3540  CG  ASN A 461     4360   5006   5304    369   -848   1044       C  
ATOM   3541  OD1 ASN A 461      23.123 -13.159  -4.833  1.00 38.87           O  
ANISOU 3541  OD1 ASN A 461     4264   5062   5443    353   -792    962       O  
ATOM   3542  ND2 ASN A 461      21.928 -12.747  -2.986  1.00 40.07           N  
ANISOU 3542  ND2 ASN A 461     4617   5265   5344    290   -901   1035       N  
ATOM   3543  N   ILE A 462      20.519 -17.658  -4.892  1.00 35.00           N  
ANISOU 3543  N   ILE A 462     4239   4041   5020    582   -760   1290       N  
ATOM   3544  CA  ILE A 462      20.266 -19.103  -4.831  1.00 34.74           C  
ANISOU 3544  CA  ILE A 462     4323   3810   5066    655   -797   1394       C  
ATOM   3545  C   ILE A 462      20.382 -19.779  -6.213  1.00 33.51           C  
ANISOU 3545  C   ILE A 462     4175   3499   5061    727   -727   1277       C  
ATOM   3546  O   ILE A 462      21.220 -20.652  -6.396  1.00 31.68           O  
ANISOU 3546  O   ILE A 462     3926   3165   4948    896   -781   1274       O  
ATOM   3547  CB  ILE A 462      18.918 -19.426  -4.141  1.00 31.86           C  
ANISOU 3547  CB  ILE A 462     4111   3391   4602    523   -778   1527       C  
ATOM   3548  CG1 ILE A 462      18.990 -19.101  -2.642  1.00 33.64           C  
ANISOU 3548  CG1 ILE A 462     4356   3762   4662    508   -862   1664       C  
ATOM   3549  CG2 ILE A 462      18.539 -20.868  -4.348  1.00 32.46           C  
ANISOU 3549  CG2 ILE A 462     4324   3216   4794    546   -796   1617       C  
ATOM   3550  CD1 ILE A 462      20.164 -19.702  -1.899  1.00 31.41           C  
ANISOU 3550  CD1 ILE A 462     4056   3477   4402    670  -1017   1766       C  
ATOM   3551  N   PRO A 463      19.564 -19.376  -7.194  1.00 35.26           N  
ANISOU 3551  N   PRO A 463     4423   3710   5266    621   -616   1170       N  
ATOM   3552  CA  PRO A 463      19.692 -20.091  -8.467  1.00 39.61           C  
ANISOU 3552  CA  PRO A 463     5001   4121   5929    701   -564   1046       C  
ATOM   3553  C   PRO A 463      21.099 -20.045  -9.052  1.00 41.85           C  
ANISOU 3553  C   PRO A 463     5139   4473   6289    871   -545    943       C  
ATOM   3554  O   PRO A 463      21.636 -21.083  -9.444  1.00 47.08           O  
ANISOU 3554  O   PRO A 463     5825   4997   7067   1035   -567    900       O  
ATOM   3555  CB  PRO A 463      18.716 -19.359  -9.392  1.00 38.51           C  
ANISOU 3555  CB  PRO A 463     4882   4034   5716    564   -462    944       C  
ATOM   3556  CG  PRO A 463      17.734 -18.746  -8.498  1.00 37.84           C  
ANISOU 3556  CG  PRO A 463     4827   4029   5522    417   -472   1045       C  
ATOM   3557  CD  PRO A 463      18.452 -18.415  -7.214  1.00 36.47           C  
ANISOU 3557  CD  PRO A 463     4598   3960   5301    455   -547   1152       C  
ATOM   3558  N   MET A 464      21.692 -18.858  -9.099  1.00 37.81           N  
ANISOU 3558  N   MET A 464     4475   4170   5721    832   -502    902       N  
ATOM   3559  CA  MET A 464      22.998 -18.706  -9.719  1.00 38.41           C  
ANISOU 3559  CA  MET A 464     4373   4356   5867    957   -455    806       C  
ATOM   3560  C   MET A 464      24.099 -19.336  -8.877  1.00 43.94           C  
ANISOU 3560  C   MET A 464     4965   5072   6660   1130   -579    872       C  
ATOM   3561  O   MET A 464      25.039 -19.920  -9.428  1.00 47.78           O  
ANISOU 3561  O   MET A 464     5342   5561   7253   1316   -557    795       O  
ATOM   3562  CB  MET A 464      23.293 -17.234 -10.002  1.00 36.84           C  
ANISOU 3562  CB  MET A 464     4045   4357   5595    825   -374    762       C  
ATOM   3563  CG  MET A 464      22.225 -16.558 -10.856  1.00 34.77           C  
ANISOU 3563  CG  MET A 464     3897   4080   5235    684   -268    711       C  
ATOM   3564  SD  MET A 464      21.451 -17.707 -12.022  1.00 36.13           S  
ANISOU 3564  SD  MET A 464     4226   4075   5427    755   -213    619       S  
ATOM   3565  CE  MET A 464      22.650 -17.689 -13.328  1.00 36.45           C  
ANISOU 3565  CE  MET A 464     4129   4226   5494    882    -74    480       C  
ATOM   3566  N   GLY A 465      23.983 -19.241  -7.553  1.00 44.15           N  
ANISOU 3566  N   GLY A 465     5020   5123   6632   1089   -711   1012       N  
ATOM   3567  CA  GLY A 465      24.948 -19.881  -6.664  1.00 45.57           C  
ANISOU 3567  CA  GLY A 465     5119   5319   6877   1266   -863   1100       C  
ATOM   3568  C   GLY A 465      25.143 -21.330  -7.075  1.00 46.85           C  
ANISOU 3568  C   GLY A 465     5367   5258   7177   1482   -888   1096       C  
ATOM   3569  O   GLY A 465      26.263 -21.781  -7.342  1.00 49.08           O  
ANISOU 3569  O   GLY A 465     5496   5575   7575   1699   -914   1038       O  
ATOM   3570  N   LEU A 466      24.029 -22.046  -7.154  1.00 44.25           N  
ANISOU 3570  N   LEU A 466     5277   4695   6841   1419   -876   1147       N  
ATOM   3571  CA  LEU A 466      24.026 -23.423  -7.598  1.00 42.62           C  
ANISOU 3571  CA  LEU A 466     5210   4213   6771   1587   -901   1129       C  
ATOM   3572  C   LEU A 466      24.654 -23.525  -8.972  1.00 42.40           C  
ANISOU 3572  C   LEU A 466     5075   4206   6829   1726   -781    908       C  
ATOM   3573  O   LEU A 466      25.613 -24.260  -9.150  1.00 43.11           O  
ANISOU 3573  O   LEU A 466     5094   4243   7043   1986   -820    857       O  
ATOM   3574  CB  LEU A 466      22.603 -23.966  -7.636  1.00 41.97           C  
ANISOU 3574  CB  LEU A 466     5382   3899   6667   1417   -884   1189       C  
ATOM   3575  CG  LEU A 466      21.913 -24.005  -6.271  1.00 43.22           C  
ANISOU 3575  CG  LEU A 466     5656   4038   6727   1281   -975   1425       C  
ATOM   3576  CD1 LEU A 466      20.425 -24.319  -6.414  1.00 43.66           C  
ANISOU 3576  CD1 LEU A 466     5900   3935   6756   1058   -920   1468       C  
ATOM   3577  CD2 LEU A 466      22.606 -25.007  -5.364  1.00 44.43           C  
ANISOU 3577  CD2 LEU A 466     5878   4049   6953   1478  -1137   1595       C  
ATOM   3578  N   LEU A 467      24.139 -22.764  -9.935  1.00 42.01           N  
ANISOU 3578  N   LEU A 467     5010   4252   6699   1572   -633    780       N  
ATOM   3579  CA  LEU A 467      24.631 -22.847 -11.317  1.00 42.98           C  
ANISOU 3579  CA  LEU A 467     5059   4416   6857   1689   -495    571       C  
ATOM   3580  C   LEU A 467      26.150 -22.702 -11.399  1.00 47.48           C  
ANISOU 3580  C   LEU A 467     5356   5185   7499   1896   -472    513       C  
ATOM   3581  O   LEU A 467      26.810 -23.474 -12.099  1.00 52.25           O  
ANISOU 3581  O   LEU A 467     5921   5734   8197   2134   -427    381       O  
ATOM   3582  CB  LEU A 467      23.947 -21.811 -12.216  1.00 39.34           C  
ANISOU 3582  CB  LEU A 467     4600   4087   6259   1482   -351    483       C  
ATOM   3583  CG  LEU A 467      24.327 -21.836 -13.709  1.00 39.06           C  
ANISOU 3583  CG  LEU A 467     4521   4119   6203   1577   -192    278       C  
ATOM   3584  CD1 LEU A 467      24.213 -23.220 -14.332  1.00 40.60           C  
ANISOU 3584  CD1 LEU A 467     4879   4060   6485   1762   -211    146       C  
ATOM   3585  CD2 LEU A 467      23.467 -20.872 -14.477  1.00 35.16           C  
ANISOU 3585  CD2 LEU A 467     4083   3723   5554   1366    -88    238       C  
ATOM   3586  N   TYR A 468      26.697 -21.731 -10.668  1.00 48.46           N  
ANISOU 3586  N   TYR A 468     5285   5544   7582   1808   -508    601       N  
ATOM   3587  CA  TYR A 468      28.148 -21.512 -10.610  1.00 48.80           C  
ANISOU 3587  CA  TYR A 468     5020   5816   7704   1966   -507    562       C  
ATOM   3588  C   TYR A 468      28.903 -22.712 -10.037  1.00 47.88           C  
ANISOU 3588  C   TYR A 468     4872   5587   7733   2275   -658    602       C  
ATOM   3589  O   TYR A 468      29.940 -23.099 -10.562  1.00 48.37           O  
ANISOU 3589  O   TYR A 468     4737   5741   7899   2515   -608    490       O  
ATOM   3590  CB  TYR A 468      28.450 -20.264  -9.791  1.00 50.28           C  
ANISOU 3590  CB  TYR A 468     5040   6239   7824   1771   -561    652       C  
ATOM   3591  CG  TYR A 468      29.924 -19.946  -9.656  1.00 55.57           C  
ANISOU 3591  CG  TYR A 468     5357   7175   8584   1881   -580    618       C  
ATOM   3592  CD1 TYR A 468      30.720 -19.725 -10.778  1.00 55.50           C  
ANISOU 3592  CD1 TYR A 468     5126   7339   8621   1943   -394    477       C  
ATOM   3593  CD2 TYR A 468      30.516 -19.843  -8.397  1.00 58.87           C  
ANISOU 3593  CD2 TYR A 468     5647   7695   9025   1914   -784    727       C  
ATOM   3594  CE1 TYR A 468      32.073 -19.426 -10.650  1.00 59.91           C  
ANISOU 3594  CE1 TYR A 468     5317   8172   9276   2024   -402    448       C  
ATOM   3595  CE2 TYR A 468      31.867 -19.546  -8.257  1.00 61.93           C  
ANISOU 3595  CE2 TYR A 468     5675   8348   9506   2002   -822    689       C  
ATOM   3596  CZ  TYR A 468      32.643 -19.340  -9.381  1.00 62.29           C  
ANISOU 3596  CZ  TYR A 468     5476   8568   9624   2051   -627    551       C  
ATOM   3597  OH  TYR A 468      33.984 -19.049  -9.217  1.00 60.76           O  
ANISOU 3597  OH  TYR A 468     4885   8666   9535   2122   -661    517       O  
ATOM   3598  N   ASN A 469      28.370 -23.311  -8.976  1.00 48.28           N  
ANISOU 3598  N   ASN A 469     5120   5440   7785   2280   -834    770       N  
ATOM   3599  CA  ASN A 469      28.926 -24.555  -8.433  1.00 52.33           C  
ANISOU 3599  CA  ASN A 469     5678   5775   8432   2582   -995    840       C  
ATOM   3600  C   ASN A 469      28.960 -25.702  -9.439  1.00 54.10           C  
ANISOU 3600  C   ASN A 469     6026   5748   8780   2817   -926    688       C  
ATOM   3601  O   ASN A 469      29.620 -26.709  -9.201  1.00 60.78           O  
ANISOU 3601  O   ASN A 469     6876   6451   9765   3125  -1039    703       O  
ATOM   3602  CB  ASN A 469      28.145 -25.014  -7.197  1.00 55.35           C  
ANISOU 3602  CB  ASN A 469     6313   5955   8761   2502  -1171   1074       C  
ATOM   3603  CG  ASN A 469      28.427 -24.170  -5.972  1.00 59.02           C  
ANISOU 3603  CG  ASN A 469     6650   6664   9112   2390  -1300   1222       C  
ATOM   3604  OD1 ASN A 469      29.348 -23.347  -5.952  1.00 62.12           O  
ANISOU 3604  OD1 ASN A 469     6747   7353   9501   2396  -1298   1154       O  
ATOM   3605  ND2 ASN A 469      27.631 -24.377  -4.931  1.00 59.29           N  
ANISOU 3605  ND2 ASN A 469     6905   6578   9043   2275  -1412   1423       N  
ATOM   3606  N   LYS A 470      28.251 -25.554 -10.553  1.00 53.08           N  
ANISOU 3606  N   LYS A 470     6009   5561   8597   2687   -756    536       N  
ATOM   3607  CA  LYS A 470      28.241 -26.561 -11.603  1.00 57.55           C  
ANISOU 3607  CA  LYS A 470     6709   5905   9254   2891   -683    346       C  
ATOM   3608  C   LYS A 470      29.142 -26.112 -12.745  1.00 54.58           C  
ANISOU 3608  C   LYS A 470     6070   5805   8863   3016   -486    126       C  
ATOM   3609  O   LYS A 470      30.150 -26.744 -13.015  1.00 54.52           O  
ANISOU 3609  O   LYS A 470     5923   5820   8974   3343   -478     18       O  
ATOM   3610  CB  LYS A 470      26.821 -26.809 -12.141  1.00 62.47           C  
ANISOU 3610  CB  LYS A 470     7645   6280   9812   2670   -641    303       C  
ATOM   3611  CG  LYS A 470      25.679 -26.657 -11.124  1.00 65.37           C  
ANISOU 3611  CG  LYS A 470     8199   6523  10116   2390   -752    530       C  
ATOM   3612  CD  LYS A 470      25.195 -27.979 -10.517  1.00 69.32           C  
ANISOU 3612  CD  LYS A 470     8984   6619  10737   2458   -909    654       C  
ATOM   3613  CE  LYS A 470      23.895 -27.769  -9.728  1.00 67.61           C  
ANISOU 3613  CE  LYS A 470     8942   6320  10428   2131   -959    856       C  
ATOM   3614  NZ  LYS A 470      22.847 -27.062 -10.536  1.00 65.57           N  
ANISOU 3614  NZ  LYS A 470     8711   6151  10052   1858   -828    741       N  
ATOM   3615  N   ILE A 471      28.791 -25.010 -13.404  1.00 51.30           N  
ANISOU 3615  N   ILE A 471     5584   5610   8298   2766   -323     70       N  
ATOM   3616  CA  ILE A 471      29.446 -24.662 -14.666  1.00 53.53           C  
ANISOU 3616  CA  ILE A 471     5683   6126   8531   2852   -102   -134       C  
ATOM   3617  C   ILE A 471      30.871 -24.112 -14.516  1.00 58.28           C  
ANISOU 3617  C   ILE A 471     5876   7082   9187   2971    -43   -135       C  
ATOM   3618  O   ILE A 471      31.661 -24.206 -15.463  1.00 60.87           O  
ANISOU 3618  O   ILE A 471     6021   7586   9520   3151    132   -307       O  
ATOM   3619  CB  ILE A 471      28.573 -23.744 -15.550  1.00 50.62           C  
ANISOU 3619  CB  ILE A 471     5409   5851   7971   2562     55   -185       C  
ATOM   3620  CG1 ILE A 471      28.253 -22.412 -14.859  1.00 48.98           C  
ANISOU 3620  CG1 ILE A 471     5118   5817   7674   2246     31     -7       C  
ATOM   3621  CG2 ILE A 471      27.294 -24.465 -15.912  1.00 48.83           C  
ANISOU 3621  CG2 ILE A 471     5540   5302   7711   2497      2   -242       C  
ATOM   3622  CD1 ILE A 471      27.676 -21.359 -15.798  1.00 42.21           C  
ANISOU 3622  CD1 ILE A 471     4295   5102   6639   2007    199    -51       C  
ATOM   3623  N   ASN A 472      31.187 -23.558 -13.339  1.00 58.65           N  
ANISOU 3623  N   ASN A 472     5774   7244   9266   2869   -188     47       N  
ATOM   3624  CA  ASN A 472      32.548 -23.090 -12.975  1.00 62.08           C  
ANISOU 3624  CA  ASN A 472     5798   8008   9781   2964   -194     64       C  
ATOM   3625  C   ASN A 472      33.012 -21.751 -13.578  1.00 60.77           C  
ANISOU 3625  C   ASN A 472     5362   8200   9529   2729      5     28       C  
ATOM   3626  O   ASN A 472      34.214 -21.448 -13.561  1.00 61.71           O  
ANISOU 3626  O   ASN A 472     5104   8614   9729   2813     49      0       O  
ATOM   3627  CB  ASN A 472      33.617 -24.178 -13.238  1.00 69.80           C  
ANISOU 3627  CB  ASN A 472     6605   8995  10920   3400   -198    -60       C  
ATOM   3628  CG  ASN A 472      33.711 -25.194 -12.116  1.00 73.82           C  
ANISOU 3628  CG  ASN A 472     7226   9261  11561   3637   -472     64       C  
ATOM   3629  OD1 ASN A 472      33.683 -24.835 -10.933  1.00 74.94           O  
ANISOU 3629  OD1 ASN A 472     7343   9437  11694   3516   -665    254       O  
ATOM   3630  ND2 ASN A 472      33.841 -26.472 -12.480  1.00 74.97           N  
ANISOU 3630  ND2 ASN A 472     7511   9153  11820   3986   -496    -44       N  
ATOM   3631  N   HIS A 473      32.072 -20.955 -14.093  1.00 57.25           N  
ANISOU 3631  N   HIS A 473     5100   7726   8928   2434    119     39       N  
ATOM   3632  CA  HIS A 473      32.362 -19.587 -14.534  1.00 55.71           C  
ANISOU 3632  CA  HIS A 473     4714   7808   8644   2162    280     54       C  
ATOM   3633  C   HIS A 473      31.206 -18.658 -14.192  1.00 55.90           C  
ANISOU 3633  C   HIS A 473     4976   7724   8541   1828    231    169       C  
ATOM   3634  O   HIS A 473      30.085 -19.121 -13.962  1.00 56.62           O  
ANISOU 3634  O   HIS A 473     5376   7553   8584   1810    137    200       O  
ATOM   3635  CB  HIS A 473      32.659 -19.541 -16.037  1.00 56.55           C  
ANISOU 3635  CB  HIS A 473     4752   8064   8669   2218    564    -99       C  
ATOM   3636  CG  HIS A 473      31.551 -20.063 -16.904  1.00 55.91           C  
ANISOU 3636  CG  HIS A 473     5029   7752   8462   2243    631   -193       C  
ATOM   3637  ND1 HIS A 473      30.539 -19.260 -17.386  1.00 51.97           N  
ANISOU 3637  ND1 HIS A 473     4742   7211   7794   1973    698   -151       N  
ATOM   3638  CD2 HIS A 473      31.316 -21.301 -17.403  1.00 56.91           C  
ANISOU 3638  CD2 HIS A 473     5334   7680   8611   2510    628   -340       C  
ATOM   3639  CE1 HIS A 473      29.725 -19.982 -18.136  1.00 51.23           C  
ANISOU 3639  CE1 HIS A 473     4921   6928   7617   2062    726   -267       C  
ATOM   3640  NE2 HIS A 473      30.173 -21.224 -18.162  1.00 53.41           N  
ANISOU 3640  NE2 HIS A 473     5191   7094   8007   2375    686   -390       N  
ATOM   3641  N   CYS A 474      31.479 -17.352 -14.170  1.00 55.89           N  
ANISOU 3641  N   CYS A 474     4823   7919   8494   1565    298    228       N  
ATOM   3642  CA  CYS A 474      30.474 -16.344 -13.791  1.00 52.40           C  
ANISOU 3642  CA  CYS A 474     4584   7384   7942   1268    246    328       C  
ATOM   3643  C   CYS A 474      29.600 -15.864 -14.942  1.00 49.20           C  
ANISOU 3643  C   CYS A 474     4386   6926   7382   1135    421    296       C  
ATOM   3644  O   CYS A 474      28.624 -15.154 -14.710  1.00 40.88           O  
ANISOU 3644  O   CYS A 474     3530   5766   6238    939    375    366       O  
ATOM   3645  CB  CYS A 474      31.151 -15.117 -13.169  1.00 56.09           C  
ANISOU 3645  CB  CYS A 474     4827   8041   8442   1040    207    400       C  
ATOM   3646  SG  CYS A 474      31.900 -15.405 -11.556  1.00 62.88           S  
ANISOU 3646  SG  CYS A 474     5498   8962   9430   1126    -73    461       S  
ATOM   3647  N   ARG A 475      29.946 -16.236 -16.174  1.00 54.29           N  
ANISOU 3647  N   ARG A 475     4986   7659   7984   1257    617    185       N  
ATOM   3648  CA  ARG A 475      29.286 -15.689 -17.373  1.00 55.42           C  
ANISOU 3648  CA  ARG A 475     5297   7811   7950   1134    792    161       C  
ATOM   3649  C   ARG A 475      27.877 -16.245 -17.580  1.00 48.84           C  
ANISOU 3649  C   ARG A 475     4808   6724   7023   1160    713    128       C  
ATOM   3650  O   ARG A 475      27.559 -16.762 -18.646  1.00 48.23           O  
ANISOU 3650  O   ARG A 475     4856   6624   6846   1263    818     13       O  
ATOM   3651  CB  ARG A 475      30.141 -15.963 -18.621  1.00 60.88           C  
ANISOU 3651  CB  ARG A 475     5830   8711   8591   1272   1035     43       C  
ATOM   3652  CG  ARG A 475      31.481 -15.219 -18.654  1.00 65.97           C  
ANISOU 3652  CG  ARG A 475     6104   9658   9305   1182   1170     87       C  
ATOM   3653  CD  ARG A 475      32.662 -16.160 -18.984  1.00 72.87           C  
ANISOU 3653  CD  ARG A 475     6695  10718  10277   1479   1274    -47       C  
ATOM   3654  NE  ARG A 475      32.385 -17.037 -20.127  1.00 74.90           N  
ANISOU 3654  NE  ARG A 475     7109  10940  10410   1707   1417   -211       N  
ATOM   3655  CZ  ARG A 475      32.896 -18.256 -20.308  1.00 76.42           C  
ANISOU 3655  CZ  ARG A 475     7229  11127  10682   2052   1428   -374       C  
ATOM   3656  NH1 ARG A 475      32.552 -18.951 -21.389  1.00 77.08           N  
ANISOU 3656  NH1 ARG A 475     7497  11162  10627   2230   1554   -544       N  
ATOM   3657  NH2 ARG A 475      33.738 -18.792 -19.424  1.00 77.95           N  
ANISOU 3657  NH2 ARG A 475     7178  11355  11086   2236   1301   -377       N  
ATOM   3658  N   PHE A 476      27.028 -16.101 -16.567  1.00 44.25           N  
ANISOU 3658  N   PHE A 476     4370   5976   6466   1056    530    222       N  
ATOM   3659  CA  PHE A 476      25.669 -16.656 -16.591  1.00 39.37           C  
ANISOU 3659  CA  PHE A 476     4036   5132   5789   1057    437    206       C  
ATOM   3660  C   PHE A 476      24.896 -16.224 -17.827  1.00 38.94           C  
ANISOU 3660  C   PHE A 476     4143   5092   5559    975    556    156       C  
ATOM   3661  O   PHE A 476      24.080 -16.976 -18.345  1.00 41.41           O  
ANISOU 3661  O   PHE A 476     4642   5271   5821   1041    528     68       O  
ATOM   3662  CB  PHE A 476      24.881 -16.246 -15.342  1.00 34.23           C  
ANISOU 3662  CB  PHE A 476     3478   4372   5157    913    268    335       C  
ATOM   3663  CG  PHE A 476      25.560 -16.605 -14.028  1.00 35.17           C  
ANISOU 3663  CG  PHE A 476     3467   4488   5408    982    123    405       C  
ATOM   3664  CD1 PHE A 476      26.110 -17.861 -13.820  1.00 37.25           C  
ANISOU 3664  CD1 PHE A 476     3690   4678   5787   1210     63    363       C  
ATOM   3665  CD2 PHE A 476      25.621 -15.676 -12.989  1.00 34.81           C  
ANISOU 3665  CD2 PHE A 476     3360   4506   5360    830     33    508       C  
ATOM   3666  CE1 PHE A 476      26.725 -18.177 -12.603  1.00 40.64           C  
ANISOU 3666  CE1 PHE A 476     4009   5113   6319   1289    -92    448       C  
ATOM   3667  CE2 PHE A 476      26.221 -15.980 -11.782  1.00 32.79           C  
ANISOU 3667  CE2 PHE A 476     2997   4272   5191    894   -119    570       C  
ATOM   3668  CZ  PHE A 476      26.778 -17.229 -11.586  1.00 38.14           C  
ANISOU 3668  CZ  PHE A 476     3625   4892   5974   1125   -184    553       C  
ATOM   3669  N   ASP A 477      25.176 -15.013 -18.303  1.00 42.20           N  
ANISOU 3669  N   ASP A 477     4489   5666   5882    825    679    216       N  
ATOM   3670  CA  ASP A 477      24.531 -14.459 -19.498  1.00 39.68           C  
ANISOU 3670  CA  ASP A 477     4321   5386   5370    749    791    201       C  
ATOM   3671  C   ASP A 477      24.920 -15.173 -20.792  1.00 38.79           C  
ANISOU 3671  C   ASP A 477     4218   5368   5154    912    946     52       C  
ATOM   3672  O   ASP A 477      24.373 -14.876 -21.837  1.00 37.52           O  
ANISOU 3672  O   ASP A 477     4202   5248   4804    879   1026     25       O  
ATOM   3673  CB  ASP A 477      24.833 -12.958 -19.620  1.00 39.14           C  
ANISOU 3673  CB  ASP A 477     4191   5440   5241    543    882    333       C  
ATOM   3674  CG  ASP A 477      26.254 -12.677 -20.060  1.00 41.84           C  
ANISOU 3674  CG  ASP A 477     4286   6003   5608    539   1066    336       C  
ATOM   3675  OD1 ASP A 477      27.188 -13.171 -19.384  1.00 41.81           O  
ANISOU 3675  OD1 ASP A 477     4062   6058   5765    626   1036    305       O  
ATOM   3676  OD2 ASP A 477      26.426 -11.963 -21.084  1.00 42.32           O  
ANISOU 3676  OD2 ASP A 477     4367   6191   5523    450   1241    379       O  
ATOM   3677  N   GLU A 478      25.869 -16.098 -20.723  1.00 44.75           N  
ANISOU 3677  N   GLU A 478     4820   6164   6019   1106    984    -51       N  
ATOM   3678  CA  GLU A 478      26.213 -16.943 -21.871  1.00 52.65           C  
ANISOU 3678  CA  GLU A 478     5844   7234   6927   1310   1121   -235       C  
ATOM   3679  C   GLU A 478      25.661 -18.365 -21.726  1.00 53.21           C  
ANISOU 3679  C   GLU A 478     6081   7059   7077   1495    976   -383       C  
ATOM   3680  O   GLU A 478      25.444 -19.045 -22.728  1.00 59.17           O  
ANISOU 3680  O   GLU A 478     6971   7794   7718   1627   1035   -560       O  
ATOM   3681  CB  GLU A 478      27.732 -16.974 -22.073  1.00 55.83           C  
ANISOU 3681  CB  GLU A 478     5944   7878   7391   1429   1299   -272       C  
ATOM   3682  CG  GLU A 478      28.319 -15.609 -22.452  1.00 56.40           C  
ANISOU 3682  CG  GLU A 478     5857   8201   7371   1217   1481   -134       C  
ATOM   3683  CD  GLU A 478      29.835 -15.621 -22.605  1.00 59.59           C  
ANISOU 3683  CD  GLU A 478     5907   8880   7853   1305   1665   -162       C  
ATOM   3684  OE1 GLU A 478      30.463 -16.695 -22.461  1.00 61.46           O  
ANISOU 3684  OE1 GLU A 478     6016   9127   8210   1572   1655   -303       O  
ATOM   3685  OE2 GLU A 478      30.405 -14.542 -22.866  1.00 60.77           O  
ANISOU 3685  OE2 GLU A 478     5900   9234   7956   1105   1819    -38       O  
ATOM   3686  N   PHE A 479      25.438 -18.802 -20.485  1.00 49.54           N  
ANISOU 3686  N   PHE A 479     5621   6405   6797   1496    785   -309       N  
ATOM   3687  CA  PHE A 479      24.815 -20.102 -20.203  1.00 48.89           C  
ANISOU 3687  CA  PHE A 479     5723   6042   6813   1619    628   -402       C  
ATOM   3688  C   PHE A 479      23.359 -20.078 -20.606  1.00 45.19           C  
ANISOU 3688  C   PHE A 479     5507   5438   6226   1473    548   -423       C  
ATOM   3689  O   PHE A 479      22.856 -21.017 -21.219  1.00 45.08           O  
ANISOU 3689  O   PHE A 479     5668   5272   6188   1562    507   -586       O  
ATOM   3690  CB  PHE A 479      24.900 -20.428 -18.713  1.00 49.20           C  
ANISOU 3690  CB  PHE A 479     5711   5936   7049   1619    452   -265       C  
ATOM   3691  CG  PHE A 479      24.172 -21.684 -18.320  1.00 48.77           C  
ANISOU 3691  CG  PHE A 479     5866   5564   7099   1693    287   -306       C  
ATOM   3692  CD1 PHE A 479      22.860 -21.630 -17.882  1.00 46.93           C  
ANISOU 3692  CD1 PHE A 479     5811   5174   6845   1498    164   -219       C  
ATOM   3693  CD2 PHE A 479      24.803 -22.918 -18.382  1.00 51.23           C  
ANISOU 3693  CD2 PHE A 479     6194   5731   7542   1957    259   -427       C  
ATOM   3694  CE1 PHE A 479      22.187 -22.784 -17.518  1.00 48.27           C  
ANISOU 3694  CE1 PHE A 479     6168   5049   7122   1525     23   -238       C  
ATOM   3695  CE2 PHE A 479      24.136 -24.073 -18.019  1.00 52.67           C  
ANISOU 3695  CE2 PHE A 479     6596   5579   7836   2003    103   -449       C  
ATOM   3696  CZ  PHE A 479      22.825 -24.005 -17.585  1.00 51.55           C  
ANISOU 3696  CZ  PHE A 479     6627   5286   7673   1766    -11   -346       C  
ATOM   3697  N   PHE A 480      22.674 -19.012 -20.213  1.00 43.12           N  
ANISOU 3697  N   PHE A 480     5258   5224   5901   1251    510   -266       N  
ATOM   3698  CA  PHE A 480      21.356 -18.726 -20.759  1.00 41.67           C  
ANISOU 3698  CA  PHE A 480     5263   4994   5577   1116    458   -279       C  
ATOM   3699  C   PHE A 480      21.526 -18.095 -22.138  1.00 41.18           C  
ANISOU 3699  C   PHE A 480     5223   5135   5290   1121    620   -349       C  
ATOM   3700  O   PHE A 480      22.572 -17.520 -22.448  1.00 45.57           O  
ANISOU 3700  O   PHE A 480     5627   5886   5803   1151    784   -318       O  
ATOM   3701  CB  PHE A 480      20.562 -17.822 -19.819  1.00 37.17           C  
ANISOU 3701  CB  PHE A 480     4693   4405   5024    919    361    -96       C  
ATOM   3702  CG  PHE A 480      20.201 -18.484 -18.522  1.00 37.85           C  
ANISOU 3702  CG  PHE A 480     4793   4308   5281    900    207    -21       C  
ATOM   3703  CD1 PHE A 480      19.400 -19.610 -18.508  1.00 39.90           C  
ANISOU 3703  CD1 PHE A 480     5199   4359   5600    915     96    -94       C  
ATOM   3704  CD2 PHE A 480      20.677 -18.000 -17.314  1.00 39.11           C  
ANISOU 3704  CD2 PHE A 480     4827   4501   5531    856    170    126       C  
ATOM   3705  CE1 PHE A 480      19.076 -20.235 -17.309  1.00 39.65           C  
ANISOU 3705  CE1 PHE A 480     5193   4158   5715    881    -29      7       C  
ATOM   3706  CE2 PHE A 480      20.357 -18.620 -16.109  1.00 35.31           C  
ANISOU 3706  CE2 PHE A 480     4375   3872   5171    844     36    213       C  
ATOM   3707  CZ  PHE A 480      19.562 -19.734 -16.110  1.00 37.70           C  
ANISOU 3707  CZ  PHE A 480     4827   3969   5529    855    -54    168       C  
ATOM   3708  N   SER A 481      20.517 -18.252 -22.980  1.00 38.59           N  
ANISOU 3708  N   SER A 481     5078   4772   4812   1090    573   -443       N  
ATOM   3709  CA  SER A 481      20.540 -17.661 -24.310  1.00 39.55           C  
ANISOU 3709  CA  SER A 481     5261   5089   4677   1095    705   -494       C  
ATOM   3710  C   SER A 481      20.269 -16.164 -24.171  1.00 40.32           C  
ANISOU 3710  C   SER A 481     5329   5303   4689    919    734   -282       C  
ATOM   3711  O   SER A 481      20.952 -15.328 -24.769  1.00 42.88           O  
ANISOU 3711  O   SER A 481     5595   5814   4882    897    903   -211       O  
ATOM   3712  CB  SER A 481      19.491 -18.328 -25.198  1.00 37.80           C  
ANISOU 3712  CB  SER A 481     5251   4793   4317   1118    602   -668       C  
ATOM   3713  OG  SER A 481      18.264 -18.510 -24.500  1.00 34.69           O  
ANISOU 3713  OG  SER A 481     4930   4222   4030    991    397   -621       O  
ATOM   3714  N   GLU A 482      19.270 -15.852 -23.355  1.00 37.85           N  
ANISOU 3714  N   GLU A 482     5058   4867   4456    798    574   -180       N  
ATOM   3715  CA  GLU A 482      18.888 -14.482 -23.044  1.00 37.37           C  
ANISOU 3715  CA  GLU A 482     4990   4860   4350    654    566      6       C  
ATOM   3716  C   GLU A 482      17.988 -14.535 -21.811  1.00 34.74           C  
ANISOU 3716  C   GLU A 482     4655   4376   4170    573    394     74       C  
ATOM   3717  O   GLU A 482      17.604 -15.629 -21.382  1.00 32.02           O  
ANISOU 3717  O   GLU A 482     4331   3897   3937    608    291     -9       O  
ATOM   3718  CB  GLU A 482      18.172 -13.830 -24.237  1.00 40.04           C  
ANISOU 3718  CB  GLU A 482     5477   5299   4437    630    580     14       C  
ATOM   3719  CG  GLU A 482      17.168 -14.732 -24.953  1.00 43.25           C  
ANISOU 3719  CG  GLU A 482     6026   5661   4745    687    458   -156       C  
ATOM   3720  CD  GLU A 482      16.659 -14.143 -26.256  1.00 48.71           C  
ANISOU 3720  CD  GLU A 482     6861   6498   5151    696    474   -159       C  
ATOM   3721  OE1 GLU A 482      17.038 -14.650 -27.337  1.00 55.00           O  
ANISOU 3721  OE1 GLU A 482     7730   7396   5770    794    559   -301       O  
ATOM   3722  OE2 GLU A 482      15.883 -13.172 -26.201  1.00 49.51           O  
ANISOU 3722  OE2 GLU A 482     7008   6614   5190    622    399    -22       O  
ATOM   3723  N   GLY A 483      17.666 -13.377 -21.232  1.00 30.87           N  
ANISOU 3723  N   GLY A 483     4147   3899   3684    467    369    224       N  
ATOM   3724  CA  GLY A 483      16.740 -13.334 -20.104  1.00 28.34           C  
ANISOU 3724  CA  GLY A 483     3823   3475   3470    402    228    283       C  
ATOM   3725  C   GLY A 483      16.333 -11.953 -19.639  1.00 26.83           C  
ANISOU 3725  C   GLY A 483     3639   3305   3250    317    210    416       C  
ATOM   3726  O   GLY A 483      16.530 -10.969 -20.350  1.00 27.04           O  
ANISOU 3726  O   GLY A 483     3714   3399   3160    296    282    476       O  
ATOM   3727  N   CYS A 484      15.736 -11.895 -18.445  1.00 27.20           N  
ANISOU 3727  N   CYS A 484     3653   3286   3397    275    114    463       N  
ATOM   3728  CA  CYS A 484      15.504 -10.624 -17.757  1.00 27.81           C  
ANISOU 3728  CA  CYS A 484     3731   3362   3473    217     97    564       C  
ATOM   3729  C   CYS A 484      15.922 -10.727 -16.288  1.00 27.64           C  
ANISOU 3729  C   CYS A 484     3620   3301   3581    184     60    600       C  
ATOM   3730  O   CYS A 484      15.346 -11.503 -15.513  1.00 28.61           O  
ANISOU 3730  O   CYS A 484     3723   3386   3764    188    -13    589       O  
ATOM   3731  CB  CYS A 484      14.051 -10.166 -17.861  1.00 27.40           C  
ANISOU 3731  CB  CYS A 484     3748   3311   3351    224      9    576       C  
ATOM   3732  SG  CYS A 484      13.780  -8.551 -17.071  1.00 25.42           S  
ANISOU 3732  SG  CYS A 484     3526   3032   3099    198    -10    672       S  
ATOM   3733  N   ALA A 485      16.930  -9.936 -15.934  1.00 23.59           N  
ANISOU 3733  N   ALA A 485     3057   2806   3102    138    109    648       N  
ATOM   3734  CA  ALA A 485      17.509  -9.909 -14.597  1.00 22.72           C  
ANISOU 3734  CA  ALA A 485     2859   2684   3089    107     62    674       C  
ATOM   3735  C   ALA A 485      17.762  -8.452 -14.270  1.00 24.42           C  
ANISOU 3735  C   ALA A 485     3098   2889   3291     24     68    720       C  
ATOM   3736  O   ALA A 485      18.890  -7.967 -14.387  1.00 19.63           O  
ANISOU 3736  O   ALA A 485     2423   2310   2726    -41    122    739       O  
ATOM   3737  CB  ALA A 485      18.808 -10.678 -14.563  1.00 19.80           C  
ANISOU 3737  CB  ALA A 485     2366   2351   2805    139    100    651       C  
ATOM   3738  N   PRO A 486      16.700  -7.730 -13.898  1.00 28.24           N  
ANISOU 3738  N   PRO A 486     3675   3330   3726     26     12    732       N  
ATOM   3739  CA  PRO A 486      16.874  -6.308 -13.663  1.00 30.76           C  
ANISOU 3739  CA  PRO A 486     4057   3593   4038    -39      8    761       C  
ATOM   3740  C   PRO A 486      18.096  -6.080 -12.809  1.00 27.32           C  
ANISOU 3740  C   PRO A 486     3524   3167   3689   -127     -8    756       C  
ATOM   3741  O   PRO A 486      18.341  -6.870 -11.901  1.00 27.81           O  
ANISOU 3741  O   PRO A 486     3498   3276   3792   -101    -63    732       O  
ATOM   3742  CB  PRO A 486      15.583  -5.917 -12.939  1.00 30.82           C  
ANISOU 3742  CB  PRO A 486     4138   3570   4003     21    -69    741       C  
ATOM   3743  CG  PRO A 486      14.567  -6.844 -13.522  1.00 28.64           C  
ANISOU 3743  CG  PRO A 486     3858   3342   3681     97    -74    728       C  
ATOM   3744  CD  PRO A 486      15.301  -8.151 -13.711  1.00 27.66           C  
ANISOU 3744  CD  PRO A 486     3645   3256   3609     88    -46    714       C  
ATOM   3745  N   GLY A 487      18.864  -5.040 -13.136  1.00 26.68           N  
ANISOU 3745  N   GLY A 487     3458   3044   3635   -236     33    787       N  
ATOM   3746  CA  GLY A 487      20.163  -4.786 -12.515  1.00 28.62           C  
ANISOU 3746  CA  GLY A 487     3576   3321   3977   -352     17    777       C  
ATOM   3747  C   GLY A 487      21.372  -5.334 -13.265  1.00 32.55           C  
ANISOU 3747  C   GLY A 487     3909   3929   4530   -391    121    800       C  
ATOM   3748  O   GLY A 487      22.506  -5.110 -12.855  1.00 34.31           O  
ANISOU 3748  O   GLY A 487     3984   4207   4844   -494    112    794       O  
ATOM   3749  N   SER A 488      21.141  -6.066 -14.350  1.00 37.16           N  
ANISOU 3749  N   SER A 488     4504   4562   5055   -303    216    810       N  
ATOM   3750  CA  SER A 488      22.229  -6.505 -15.225  1.00 41.28           C  
ANISOU 3750  CA  SER A 488     4882   5203   5600   -316    348    819       C  
ATOM   3751  C   SER A 488      22.728  -5.360 -16.113  1.00 43.86           C  
ANISOU 3751  C   SER A 488     5241   5526   5896   -468    472    904       C  
ATOM   3752  O   SER A 488      21.997  -4.393 -16.360  1.00 44.23           O  
ANISOU 3752  O   SER A 488     5477   5450   5878   -518    457    963       O  
ATOM   3753  CB  SER A 488      21.780  -7.686 -16.085  1.00 42.15           C  
ANISOU 3753  CB  SER A 488     5020   5358   5636   -160    403    774       C  
ATOM   3754  OG  SER A 488      21.546  -8.829 -15.277  1.00 45.06           O  
ANISOU 3754  OG  SER A 488     5343   5714   6063    -45    301    714       O  
ATOM   3755  N   LYS A 489      23.976  -5.471 -16.576  1.00 45.28           N  
ANISOU 3755  N   LYS A 489     5234   5844   6127   -538    596    921       N  
ATOM   3756  CA  LYS A 489      24.544  -4.491 -17.505  1.00 47.68           C  
ANISOU 3756  CA  LYS A 489     5550   6171   6394   -706    750   1027       C  
ATOM   3757  C   LYS A 489      23.647  -4.354 -18.724  1.00 44.10           C  
ANISOU 3757  C   LYS A 489     5320   5682   5755   -638    832   1087       C  
ATOM   3758  O   LYS A 489      23.253  -5.348 -19.339  1.00 43.09           O  
ANISOU 3758  O   LYS A 489     5211   5632   5529   -470    866   1024       O  
ATOM   3759  CB  LYS A 489      25.958  -4.890 -17.954  1.00 54.32           C  
ANISOU 3759  CB  LYS A 489     6115   7228   7296   -756    907   1025       C  
ATOM   3760  CG  LYS A 489      27.030  -4.679 -16.893  1.00 59.08           C  
ANISOU 3760  CG  LYS A 489     6471   7890   8087   -883    829    997       C  
ATOM   3761  CD  LYS A 489      28.426  -4.508 -17.493  1.00 64.74           C  
ANISOU 3761  CD  LYS A 489     6913   8815   8868  -1022   1014   1042       C  
ATOM   3762  CE  LYS A 489      28.633  -3.142 -18.145  1.00 68.53           C  
ANISOU 3762  CE  LYS A 489     7485   9231   9322  -1298   1138   1191       C  
ATOM   3763  NZ  LYS A 489      28.297  -3.149 -19.598  1.00 72.42           N  
ANISOU 3763  NZ  LYS A 489     8124   9775   9617  -1252   1345   1282       N  
ATOM   3764  N   LYS A 490      23.345  -3.118 -19.086  1.00 43.36           N  
ANISOU 3764  N   LYS A 490     5403   5461   5611   -766    851   1207       N  
ATOM   3765  CA  LYS A 490      22.321  -2.855 -20.096  1.00 48.33           C  
ANISOU 3765  CA  LYS A 490     6275   6033   6054   -682    873   1278       C  
ATOM   3766  C   LYS A 490      22.447  -3.693 -21.374  1.00 47.29           C  
ANISOU 3766  C   LYS A 490     6126   6088   5754   -575   1023   1267       C  
ATOM   3767  O   LYS A 490      21.439  -4.007 -22.001  1.00 45.24           O  
ANISOU 3767  O   LYS A 490     6027   5820   5341   -434    980   1248       O  
ATOM   3768  CB  LYS A 490      22.285  -1.365 -20.448  1.00 53.25           C  
ANISOU 3768  CB  LYS A 490     7084   6496   6652   -849    902   1444       C  
ATOM   3769  CG  LYS A 490      21.755  -0.476 -19.324  1.00 53.12           C  
ANISOU 3769  CG  LYS A 490     7181   6245   6756   -892    726   1427       C  
ATOM   3770  CD  LYS A 490      20.296  -0.752 -19.007  1.00 50.57           C  
ANISOU 3770  CD  LYS A 490     7000   5848   6368   -676    573   1351       C  
ATOM   3771  CE  LYS A 490      19.650   0.459 -18.345  1.00 53.02           C  
ANISOU 3771  CE  LYS A 490     7499   5912   6734   -696    444   1374       C  
ATOM   3772  NZ  LYS A 490      18.279   0.188 -17.840  1.00 52.44           N  
ANISOU 3772  NZ  LYS A 490     7503   5802   6621   -484    302   1280       N  
ATOM   3773  N   ASP A 491      23.659  -4.064 -21.764  1.00 50.11           N  
ANISOU 3773  N   ASP A 491     6280   6627   6131   -632   1193   1262       N  
ATOM   3774  CA  ASP A 491      23.818  -4.843 -22.987  1.00 55.10           C  
ANISOU 3774  CA  ASP A 491     6905   7450   6582   -514   1350   1227       C  
ATOM   3775  C   ASP A 491      24.267  -6.292 -22.780  1.00 50.15           C  
ANISOU 3775  C   ASP A 491     6079   6956   6019   -343   1360   1042       C  
ATOM   3776  O   ASP A 491      24.944  -6.860 -23.639  1.00 49.07           O  
ANISOU 3776  O   ASP A 491     5843   7014   5788   -277   1538    997       O  
ATOM   3777  CB  ASP A 491      24.710  -4.086 -23.979  1.00 64.56           C  
ANISOU 3777  CB  ASP A 491     8079   8777   7675   -680   1587   1384       C  
ATOM   3778  CG  ASP A 491      23.950  -2.953 -24.687  1.00 70.87           C  
ANISOU 3778  CG  ASP A 491     9179   9444   8306   -758   1584   1571       C  
ATOM   3779  OD1 ASP A 491      23.597  -3.118 -25.878  1.00 73.43           O  
ANISOU 3779  OD1 ASP A 491     9649   9874   8377   -669   1678   1612       O  
ATOM   3780  OD2 ASP A 491      23.674  -1.914 -24.042  1.00 72.04           O  
ANISOU 3780  OD2 ASP A 491     9433   9374   8566   -889   1473   1669       O  
ATOM   3781  N   SER A 492      23.870  -6.891 -21.655  1.00 45.34           N  
ANISOU 3781  N   SER A 492     5427   6240   5560   -260   1175    940       N  
ATOM   3782  CA  SER A 492      23.930  -8.353 -21.517  1.00 44.31           C  
ANISOU 3782  CA  SER A 492     5202   6163   5470    -63   1141    775       C  
ATOM   3783  C   SER A 492      22.670  -8.965 -22.102  1.00 43.51           C  
ANISOU 3783  C   SER A 492     5315   5994   5222     75   1061    699       C  
ATOM   3784  O   SER A 492      21.688  -8.269 -22.371  1.00 47.06           O  
ANISOU 3784  O   SER A 492     5957   6359   5565     33    996    773       O  
ATOM   3785  CB  SER A 492      24.118  -8.827 -20.061  1.00 39.29           C  
ANISOU 3785  CB  SER A 492     4431   5449   5048    -36    980    720       C  
ATOM   3786  OG  SER A 492      23.477  -7.989 -19.130  1.00 34.95           O  
ANISOU 3786  OG  SER A 492     3975   4749   4555   -146    833    790       O  
ATOM   3787  N   SER A 493      22.711 -10.274 -22.297  1.00 40.46           N  
ANISOU 3787  N   SER A 493     4892   5640   4842    244   1056    545       N  
ATOM   3788  CA  SER A 493      21.572 -10.988 -22.828  1.00 40.74           C  
ANISOU 3788  CA  SER A 493     5109   5610   4761    356    963    445       C  
ATOM   3789  C   SER A 493      20.455 -10.967 -21.790  1.00 38.31           C  
ANISOU 3789  C   SER A 493     4876   5126   4554    325    754    466       C  
ATOM   3790  O   SER A 493      19.278 -10.886 -22.139  1.00 39.70           O  
ANISOU 3790  O   SER A 493     5208   5249   4627    335    660    458       O  
ATOM   3791  CB  SER A 493      21.970 -12.424 -23.215  1.00 42.87           C  
ANISOU 3791  CB  SER A 493     5329   5917   5042    536   1001    258       C  
ATOM   3792  OG  SER A 493      22.356 -13.203 -22.091  1.00 40.74           O  
ANISOU 3792  OG  SER A 493     4928   5556   4995    597    909    210       O  
ATOM   3793  N   LEU A 494      20.838 -10.990 -20.514  1.00 35.89           N  
ANISOU 3793  N   LEU A 494     4444   4756   4436    288    683    495       N  
ATOM   3794  CA  LEU A 494      19.889 -11.009 -19.406  1.00 33.13           C  
ANISOU 3794  CA  LEU A 494     4144   4272   4173    262    511    518       C  
ATOM   3795  C   LEU A 494      19.129  -9.693 -19.241  1.00 34.53           C  
ANISOU 3795  C   LEU A 494     4426   4403   4291    159    464    625       C  
ATOM   3796  O   LEU A 494      18.372  -9.538 -18.281  1.00 32.52           O  
ANISOU 3796  O   LEU A 494     4197   4064   4096    141    342    644       O  
ATOM   3797  CB  LEU A 494      20.601 -11.332 -18.086  1.00 33.99           C  
ANISOU 3797  CB  LEU A 494     4101   4352   4461    258    451    529       C  
ATOM   3798  CG  LEU A 494      21.438 -12.612 -17.961  1.00 35.35           C  
ANISOU 3798  CG  LEU A 494     4155   4542   4736    389    466    441       C  
ATOM   3799  CD1 LEU A 494      22.020 -12.696 -16.567  1.00 32.79           C  
ANISOU 3799  CD1 LEU A 494     3700   4197   4563    376    372    488       C  
ATOM   3800  CD2 LEU A 494      20.630 -13.859 -18.249  1.00 37.90           C  
ANISOU 3800  CD2 LEU A 494     4593   4759   5049    498    398    340       C  
ATOM   3801  N   CYS A 495      19.340  -8.737 -20.144  1.00 37.00           N  
ANISOU 3801  N   CYS A 495     4804   4767   4485    101    564    701       N  
ATOM   3802  CA  CYS A 495      18.441  -7.591 -20.236  1.00 36.38           C  
ANISOU 3802  CA  CYS A 495     4876   4616   4330     52    506    795       C  
ATOM   3803  C   CYS A 495      17.521  -7.660 -21.467  1.00 35.36           C  
ANISOU 3803  C   CYS A 495     4903   4527   4007    129    495    786       C  
ATOM   3804  O   CYS A 495      16.591  -6.877 -21.570  1.00 38.46           O  
ANISOU 3804  O   CYS A 495     5417   4862   4333    136    415    851       O  
ATOM   3805  CB  CYS A 495      19.237  -6.287 -20.241  1.00 37.01           C  
ANISOU 3805  CB  CYS A 495     4958   4677   4426    -87    592    923       C  
ATOM   3806  SG  CYS A 495      19.816  -5.728 -18.611  1.00 40.05           S  
ANISOU 3806  SG  CYS A 495     5226   4973   5019   -200    515    935       S  
ATOM   3807  N   LYS A 496      17.748  -8.597 -22.383  1.00 35.44           N  
ANISOU 3807  N   LYS A 496     4910   4637   3920    205    560    692       N  
ATOM   3808  CA  LYS A 496      17.031  -8.578 -23.673  1.00 40.05           C  
ANISOU 3808  CA  LYS A 496     5649   5290   4277    270    553    679       C  
ATOM   3809  C   LYS A 496      15.523  -8.849 -23.557  1.00 36.51           C  
ANISOU 3809  C   LYS A 496     5275   4789   3808    329    362    623       C  
ATOM   3810  O   LYS A 496      14.750  -8.409 -24.410  1.00 37.84           O  
ANISOU 3810  O   LYS A 496     5574   5002   3802    371    306    658       O  
ATOM   3811  CB  LYS A 496      17.648  -9.565 -24.677  1.00 43.67           C  
ANISOU 3811  CB  LYS A 496     6096   5878   4618    348    667    554       C  
ATOM   3812  CG  LYS A 496      18.930  -9.102 -25.349  1.00 47.71           C  
ANISOU 3812  CG  LYS A 496     6564   6522   5042    305    890    630       C  
ATOM   3813  CD  LYS A 496      19.410 -10.170 -26.349  1.00 54.67           C  
ANISOU 3813  CD  LYS A 496     7440   7549   5784    426   1002    466       C  
ATOM   3814  CE  LYS A 496      20.639  -9.740 -27.171  1.00 58.28           C  
ANISOU 3814  CE  LYS A 496     7839   8195   6108    392   1261    539       C  
ATOM   3815  NZ  LYS A 496      21.926  -9.982 -26.444  1.00 58.73           N  
ANISOU 3815  NZ  LYS A 496     7646   8290   6379    364   1378    524       N  
ATOM   3816  N   LEU A 497      15.115  -9.574 -22.518  1.00 31.32           N  
ANISOU 3816  N   LEU A 497     4525   4054   3321    330    261    547       N  
ATOM   3817  CA  LEU A 497      13.718  -9.971 -22.356  1.00 28.23           C  
ANISOU 3817  CA  LEU A 497     4156   3637   2934    361     96    487       C  
ATOM   3818  C   LEU A 497      12.924  -9.048 -21.446  1.00 27.34           C  
ANISOU 3818  C   LEU A 497     4029   3467   2890    340     10    580       C  
ATOM   3819  O   LEU A 497      11.700  -9.181 -21.353  1.00 24.97           O  
ANISOU 3819  O   LEU A 497     3723   3182   2584    370   -116    548       O  
ATOM   3820  CB  LEU A 497      13.615 -11.401 -21.821  1.00 26.58           C  
ANISOU 3820  CB  LEU A 497     3867   3374   2858    361     43    357       C  
ATOM   3821  CG  LEU A 497      14.150 -12.518 -22.724  1.00 29.21           C  
ANISOU 3821  CG  LEU A 497     4234   3734   3133    418     92    212       C  
ATOM   3822  CD1 LEU A 497      13.739 -13.855 -22.160  1.00 32.55           C  
ANISOU 3822  CD1 LEU A 497     4618   4046   3703    409     -5     98       C  
ATOM   3823  CD2 LEU A 497      13.674 -12.403 -24.159  1.00 24.16           C  
ANISOU 3823  CD2 LEU A 497     3721   3201   2257    469     72    152       C  
ATOM   3824  N   CYS A 498      13.600  -8.115 -20.783  1.00 25.83           N  
ANISOU 3824  N   CYS A 498     3825   3220   2768    292     74    681       N  
ATOM   3825  CA  CYS A 498      12.912  -7.154 -19.937  1.00 25.70           C  
ANISOU 3825  CA  CYS A 498     3820   3138   2805    295      1    746       C  
ATOM   3826  C   CYS A 498      11.964  -6.280 -20.758  1.00 27.33           C  
ANISOU 3826  C   CYS A 498     4151   3361   2873    374    -69    806       C  
ATOM   3827  O   CYS A 498      12.049  -6.245 -21.994  1.00 27.46           O  
ANISOU 3827  O   CYS A 498     4263   3439   2732    403    -44    829       O  
ATOM   3828  CB  CYS A 498      13.925  -6.320 -19.168  1.00 28.76           C  
ANISOU 3828  CB  CYS A 498     4193   3447   3285    215     73    818       C  
ATOM   3829  SG  CYS A 498      15.013  -7.315 -18.111  1.00 33.77           S  
ANISOU 3829  SG  CYS A 498     4665   4086   4079    152    116    757       S  
ATOM   3830  N   MET A 499      11.044  -5.600 -20.077  1.00 28.30           N  
ANISOU 3830  N   MET A 499     4272   3441   3038    428   -159    828       N  
ATOM   3831  CA  MET A 499       9.929  -4.934 -20.762  1.00 28.79           C  
ANISOU 3831  CA  MET A 499     4420   3533   2987    547   -263    868       C  
ATOM   3832  C   MET A 499       9.884  -3.430 -20.614  1.00 29.19           C  
ANISOU 3832  C   MET A 499     4601   3458   3033    602   -273    982       C  
ATOM   3833  O   MET A 499       9.000  -2.799 -21.177  1.00 37.75           O  
ANISOU 3833  O   MET A 499     5768   4550   4025    730   -369   1031       O  
ATOM   3834  CB  MET A 499       8.575  -5.534 -20.330  1.00 27.30           C  
ANISOU 3834  CB  MET A 499     4099   3436   2840    611   -387    776       C  
ATOM   3835  CG  MET A 499       8.139  -5.270 -18.903  1.00 27.80           C  
ANISOU 3835  CG  MET A 499     4060   3466   3037    623   -399    755       C  
ATOM   3836  SD  MET A 499       6.332  -5.391 -18.705  1.00 31.44           S  
ANISOU 3836  SD  MET A 499     4376   4069   3499    740   -537    696       S  
ATOM   3837  CE  MET A 499       5.797  -3.768 -19.237  1.00 27.86           C  
ANISOU 3837  CE  MET A 499     4067   3560   2958    937   -611    784       C  
ATOM   3838  N   GLY A 500      10.828  -2.844 -19.890  1.00 29.79           N  
ANISOU 3838  N   GLY A 500     4702   3408   3207    510   -190   1022       N  
ATOM   3839  CA  GLY A 500      10.824  -1.395 -19.662  1.00 29.79           C  
ANISOU 3839  CA  GLY A 500     4852   3238   3229    544   -209   1114       C  
ATOM   3840  C   GLY A 500      11.164  -0.609 -20.910  1.00 31.85           C  
ANISOU 3840  C   GLY A 500     5307   3435   3358    540   -175   1269       C  
ATOM   3841  O   GLY A 500      11.741  -1.138 -21.858  1.00 32.85           O  
ANISOU 3841  O   GLY A 500     5444   3662   3377    475    -94   1305       O  
ATOM   3842  N   SER A 501      10.813   0.665 -20.913  1.00 36.71           N  
ANISOU 3842  N   SER A 501     6093   3879   3975    617   -232   1364       N  
ATOM   3843  CA  SER A 501      11.128   1.526 -22.037  1.00 43.70           C  
ANISOU 3843  CA  SER A 501     7200   4669   4735    605   -202   1552       C  
ATOM   3844  C   SER A 501      11.545   2.908 -21.542  1.00 48.94           C  
ANISOU 3844  C   SER A 501     8040   5048   5509    550   -196   1648       C  
ATOM   3845  O   SER A 501      10.996   3.372 -20.550  1.00 51.87           O  
ANISOU 3845  O   SER A 501     8406   5304   5998    645   -282   1558       O  
ATOM   3846  CB  SER A 501       9.894   1.662 -22.932  1.00 46.27           C  
ANISOU 3846  CB  SER A 501     7611   5069   4899    823   -341   1600       C  
ATOM   3847  OG  SER A 501       8.805   2.225 -22.212  1.00 46.44           O  
ANISOU 3847  OG  SER A 501     7627   5012   5007   1012   -480   1543       O  
ATOM   3848  N   GLY A 502      12.526   3.565 -22.163  1.00 52.71           N  
ANISOU 3848  N   GLY A 502     8670   5405   5954    386    -89   1817       N  
ATOM   3849  CA  GLY A 502      13.589   2.958 -22.962  1.00 53.42           C  
ANISOU 3849  CA  GLY A 502     8700   5647   5950    208     78   1884       C  
ATOM   3850  C   GLY A 502      14.832   2.944 -22.091  1.00 53.25           C  
ANISOU 3850  C   GLY A 502     8549   5572   6111    -24    187   1832       C  
ATOM   3851  O   GLY A 502      15.586   1.975 -22.088  1.00 53.67           O  
ANISOU 3851  O   GLY A 502     8407   5811   6173   -122    292   1758       O  
ATOM   3852  N   LEU A 503      15.044   4.040 -21.362  1.00 53.50           N  
ANISOU 3852  N   LEU A 503     8694   5344   6291   -102    147   1863       N  
ATOM   3853  CA  LEU A 503      16.046   4.106 -20.297  1.00 51.04           C  
ANISOU 3853  CA  LEU A 503     8251   4971   6170   -303    189   1773       C  
ATOM   3854  C   LEU A 503      15.684   3.158 -19.160  1.00 45.57           C  
ANISOU 3854  C   LEU A 503     7343   4415   5556   -207    115   1550       C  
ATOM   3855  O   LEU A 503      16.574   2.606 -18.511  1.00 43.30           O  
ANISOU 3855  O   LEU A 503     6869   4218   5366   -344    166   1465       O  
ATOM   3856  CB  LEU A 503      16.168   5.528 -19.722  1.00 52.48           C  
ANISOU 3856  CB  LEU A 503     8636   4814   6488   -386    121   1820       C  
ATOM   3857  CG  LEU A 503      16.545   6.691 -20.648  1.00 57.45           C  
ANISOU 3857  CG  LEU A 503     9530   5215   7083   -516    179   2068       C  
ATOM   3858  CD1 LEU A 503      16.573   7.995 -19.869  1.00 56.69           C  
ANISOU 3858  CD1 LEU A 503     9637   4744   7158   -582     78   2059       C  
ATOM   3859  CD2 LEU A 503      17.886   6.452 -21.330  1.00 60.23           C  
ANISOU 3859  CD2 LEU A 503     9774   5699   7413   -798    379   2197       C  
ATOM   3860  N   ASN A 504      14.382   2.981 -18.919  1.00 42.34           N  
ANISOU 3860  N   ASN A 504     6954   4030   5101     26     -5   1469       N  
ATOM   3861  CA  ASN A 504      13.904   2.150 -17.797  1.00 37.86           C  
ANISOU 3861  CA  ASN A 504     6202   3587   4596    113    -69   1282       C  
ATOM   3862  C   ASN A 504      14.139   0.639 -17.986  1.00 33.27           C  
ANISOU 3862  C   ASN A 504     5406   3259   3975     93     -9   1218       C  
ATOM   3863  O   ASN A 504      14.187  -0.112 -17.018  1.00 29.90           O  
ANISOU 3863  O   ASN A 504     4822   2920   3620     89    -29   1098       O  
ATOM   3864  CB  ASN A 504      12.420   2.423 -17.522  1.00 36.04           C  
ANISOU 3864  CB  ASN A 504     6028   3334   4331    358   -195   1222       C  
ATOM   3865  CG  ASN A 504      12.156   3.864 -17.103  1.00 35.84           C  
ANISOU 3865  CG  ASN A 504     6213   3034   4369    421   -268   1239       C  
ATOM   3866  OD1 ASN A 504      12.997   4.502 -16.487  1.00 36.75           O  
ANISOU 3866  OD1 ASN A 504     6390   2981   4591    268   -251   1222       O  
ATOM   3867  ND2 ASN A 504      10.981   4.374 -17.436  1.00 34.60           N  
ANISOU 3867  ND2 ASN A 504     6165   2826   4154    654   -363   1261       N  
ATOM   3868  N   LEU A 505      14.292   0.212 -19.237  1.00 34.51           N  
ANISOU 3868  N   LEU A 505     5580   3523   4009     89     62   1300       N  
ATOM   3869  CA  LEU A 505      14.566  -1.181 -19.579  1.00 30.86           C  
ANISOU 3869  CA  LEU A 505     4953   3267   3504     82    120   1229       C  
ATOM   3870  C   LEU A 505      15.614  -1.780 -18.642  1.00 34.76           C  
ANISOU 3870  C   LEU A 505     5267   3802   4137    -41    173   1149       C  
ATOM   3871  O   LEU A 505      16.698  -1.230 -18.492  1.00 38.04           O  
ANISOU 3871  O   LEU A 505     5670   4160   4625   -194    245   1202       O  
ATOM   3872  CB  LEU A 505      15.062  -1.262 -21.029  1.00 28.66           C  
ANISOU 3872  CB  LEU A 505     4746   3072   3072     44    231   1335       C  
ATOM   3873  CG  LEU A 505      15.370  -2.619 -21.663  1.00 25.49           C  
ANISOU 3873  CG  LEU A 505     4222   2872   2593     63    302   1253       C  
ATOM   3874  CD1 LEU A 505      14.179  -3.562 -21.531  1.00 21.88           C  
ANISOU 3874  CD1 LEU A 505     3710   2493   2111    206    175   1125       C  
ATOM   3875  CD2 LEU A 505      15.772  -2.456 -23.132  1.00 22.52           C  
ANISOU 3875  CD2 LEU A 505     3956   2582   2017     45    418   1363       C  
ATOM   3876  N   CYS A 506      15.265  -2.890 -17.994  1.00 32.67           N  
ANISOU 3876  N   CYS A 506     4864   3637   3914     21    126   1032       N  
ATOM   3877  CA  CYS A 506      16.178  -3.645 -17.143  1.00 32.48           C  
ANISOU 3877  CA  CYS A 506     4670   3667   4002    -54    153    964       C  
ATOM   3878  C   CYS A 506      16.605  -2.899 -15.875  1.00 34.74           C  
ANISOU 3878  C   CYS A 506     4940   3857   4403   -135    104    945       C  
ATOM   3879  O   CYS A 506      17.461  -3.377 -15.124  1.00 33.60           O  
ANISOU 3879  O   CYS A 506     4658   3762   4346   -203    107    900       O  
ATOM   3880  CB  CYS A 506      17.407  -4.073 -17.936  1.00 35.48           C  
ANISOU 3880  CB  CYS A 506     4970   4138   4374   -136    286    994       C  
ATOM   3881  SG  CYS A 506      18.147  -5.646 -17.413  1.00 37.46           S  
ANISOU 3881  SG  CYS A 506     5007   4512   4715   -111    304    888       S  
ATOM   3882  N   GLU A 507      15.995  -1.746 -15.616  1.00 34.89           N  
ANISOU 3882  N   GLU A 507     5105   3736   4415   -112     43    965       N  
ATOM   3883  CA  GLU A 507      16.354  -0.970 -14.450  1.00 34.97           C  
ANISOU 3883  CA  GLU A 507     5132   3638   4516   -184    -17    917       C  
ATOM   3884  C   GLU A 507      15.750  -1.716 -13.256  1.00 35.08           C  
ANISOU 3884  C   GLU A 507     5051   3740   4536    -90    -91    809       C  
ATOM   3885  O   GLU A 507      14.654  -2.263 -13.365  1.00 34.06           O  
ANISOU 3885  O   GLU A 507     4914   3681   4346     41   -114    790       O  
ATOM   3886  CB  GLU A 507      15.832   0.464 -14.590  1.00 36.43           C  
ANISOU 3886  CB  GLU A 507     5532   3618   4692   -158    -61    958       C  
ATOM   3887  CG  GLU A 507      16.689   1.532 -13.930  1.00 39.62           C  
ANISOU 3887  CG  GLU A 507     6002   3851   5201   -318    -89    942       C  
ATOM   3888  CD  GLU A 507      18.121   1.542 -14.426  1.00 41.83           C  
ANISOU 3888  CD  GLU A 507     6192   4155   5545   -543      7   1022       C  
ATOM   3889  OE1 GLU A 507      18.336   1.557 -15.653  1.00 41.99           O  
ANISOU 3889  OE1 GLU A 507     6248   4197   5509   -581    111   1151       O  
ATOM   3890  OE2 GLU A 507      19.039   1.542 -13.581  1.00 46.98           O  
ANISOU 3890  OE2 GLU A 507     6727   4827   6297   -681    -23    955       O  
ATOM   3891  N   PRO A 508      16.463  -1.768 -12.116  1.00 35.82           N  
ANISOU 3891  N   PRO A 508     5066   3849   4696   -168   -132    746       N  
ATOM   3892  CA  PRO A 508      16.023  -2.626 -11.010  1.00 34.40           C  
ANISOU 3892  CA  PRO A 508     4794   3780   4495    -93   -186    675       C  
ATOM   3893  C   PRO A 508      15.003  -1.967 -10.078  1.00 35.61           C  
ANISOU 3893  C   PRO A 508     5040   3893   4597      8   -252    599       C  
ATOM   3894  O   PRO A 508      15.165  -1.969  -8.855  1.00 42.84           O  
ANISOU 3894  O   PRO A 508     5931   4847   5500      0   -307    526       O  
ATOM   3895  CB  PRO A 508      17.334  -2.942 -10.283  1.00 31.35           C  
ANISOU 3895  CB  PRO A 508     4286   3446   4181   -210   -212    653       C  
ATOM   3896  CG  PRO A 508      18.157  -1.747 -10.487  1.00 33.89           C  
ANISOU 3896  CG  PRO A 508     4667   3643   4565   -351   -212    660       C  
ATOM   3897  CD  PRO A 508      17.728  -1.089 -11.791  1.00 35.83           C  
ANISOU 3897  CD  PRO A 508     5046   3781   4785   -341   -138    744       C  
ATOM   3898  N   ASN A 509      13.950  -1.426 -10.672  1.00 31.79           N  
ANISOU 3898  N   ASN A 509     4657   3352   4069    121   -247    611       N  
ATOM   3899  CA  ASN A 509      12.838  -0.863  -9.938  1.00 26.26           C  
ANISOU 3899  CA  ASN A 509     4021   2641   3315    264   -291    532       C  
ATOM   3900  C   ASN A 509      11.552  -1.075 -10.738  1.00 25.88           C  
ANISOU 3900  C   ASN A 509     3964   2653   3217    410   -279    566       C  
ATOM   3901  O   ASN A 509      11.562  -1.672 -11.825  1.00 16.49           O  
ANISOU 3901  O   ASN A 509     2738   1506   2022    388   -249    643       O  
ATOM   3902  CB  ASN A 509      13.084   0.619  -9.658  1.00 28.82           C  
ANISOU 3902  CB  ASN A 509     4521   2759   3670    257   -339    477       C  
ATOM   3903  CG  ASN A 509      13.186   1.468 -10.941  1.00 32.86           C  
ANISOU 3903  CG  ASN A 509     5178   3091   4215    241   -324    577       C  
ATOM   3904  OD1 ASN A 509      12.348   1.372 -11.844  1.00 27.81           O  
ANISOU 3904  OD1 ASN A 509     4559   2478   3528    360   -311    643       O  
ATOM   3905  ND2 ASN A 509      14.217   2.318 -11.005  1.00 34.99           N  
ANISOU 3905  ND2 ASN A 509     5550   3182   4562     82   -334    596       N  
ATOM   3906  N   ASN A 510      10.449  -0.562 -10.210  1.00 30.31           N  
ANISOU 3906  N   ASN A 510     4551   3231   3734    570   -307    496       N  
ATOM   3907  CA  ASN A 510       9.133  -0.888 -10.738  1.00 32.24           C  
ANISOU 3907  CA  ASN A 510     4723   3593   3935    714   -310    511       C  
ATOM   3908  C   ASN A 510       8.819  -0.296 -12.096  1.00 32.60           C  
ANISOU 3908  C   ASN A 510     4872   3542   3973    788   -341    587       C  
ATOM   3909  O   ASN A 510       7.969  -0.831 -12.801  1.00 32.53           O  
ANISOU 3909  O   ASN A 510     4778   3656   3928    861   -359    616       O  
ATOM   3910  CB  ASN A 510       8.061  -0.504  -9.729  1.00 34.64           C  
ANISOU 3910  CB  ASN A 510     4988   3981   4192    879   -317    407       C  
ATOM   3911  CG  ASN A 510       8.103  -1.380  -8.500  1.00 31.95           C  
ANISOU 3911  CG  ASN A 510     4518   3807   3813    813   -272    365       C  
ATOM   3912  OD1 ASN A 510       8.126  -2.606  -8.610  1.00 28.65           O  
ANISOU 3912  OD1 ASN A 510     3971   3514   3402    715   -243    428       O  
ATOM   3913  ND2 ASN A 510       8.126  -0.758  -7.324  1.00 32.19           N  
ANISOU 3913  ND2 ASN A 510     4604   3832   3795    870   -273    259       N  
ATOM   3914  N   LYS A 511       9.512   0.778 -12.473  1.00 34.81           N  
ANISOU 3914  N   LYS A 511     5338   3606   4282    755   -356    627       N  
ATOM   3915  CA  LYS A 511       9.430   1.305 -13.837  1.00 35.32           C  
ANISOU 3915  CA  LYS A 511     5532   3570   4319    794   -376    743       C  
ATOM   3916  C   LYS A 511       9.750   0.201 -14.840  1.00 33.15           C  
ANISOU 3916  C   LYS A 511     5163   3433   4001    694   -333    819       C  
ATOM   3917  O   LYS A 511       9.358   0.290 -16.003  1.00 40.02           O  
ANISOU 3917  O   LYS A 511     6094   4314   4798    759   -357    900       O  
ATOM   3918  CB  LYS A 511      10.402   2.464 -14.066  1.00 41.27           C  
ANISOU 3918  CB  LYS A 511     6498   4062   5123    693   -372    808       C  
ATOM   3919  CG  LYS A 511      10.229   3.687 -13.160  1.00 45.17           C  
ANISOU 3919  CG  LYS A 511     7141   4349   5671    778   -430    716       C  
ATOM   3920  CD  LYS A 511      11.332   4.700 -13.433  1.00 48.65           C  
ANISOU 3920  CD  LYS A 511     7784   4514   6185    607   -425    791       C  
ATOM   3921  CE  LYS A 511      11.065   6.022 -12.747  1.00 54.76           C  
ANISOU 3921  CE  LYS A 511     8766   5020   7019    711   -504    699       C  
ATOM   3922  NZ  LYS A 511      12.068   7.062 -13.127  1.00 58.44           N  
ANISOU 3922  NZ  LYS A 511     9453   5178   7574    518   -509    793       N  
ATOM   3923  N   GLU A 512      10.476  -0.824 -14.397  1.00 26.42           N  
ANISOU 3923  N   GLU A 512     4178   2679   3182    551   -277    787       N  
ATOM   3924  CA  GLU A 512      10.667  -2.033 -15.190  1.00 24.12           C  
ANISOU 3924  CA  GLU A 512     3786   2520   2857    488   -240    815       C  
ATOM   3925  C   GLU A 512       9.662  -3.107 -14.762  1.00 23.74           C  
ANISOU 3925  C   GLU A 512     3575   2640   2803    545   -272    746       C  
ATOM   3926  O   GLU A 512       9.713  -3.602 -13.651  1.00 22.14           O  
ANISOU 3926  O   GLU A 512     3277   2489   2646    506   -258    694       O  
ATOM   3927  CB  GLU A 512      12.096  -2.547 -15.031  1.00 22.66           C  
ANISOU 3927  CB  GLU A 512     3553   2329   2729    319   -165    826       C  
ATOM   3928  CG  GLU A 512      12.319  -3.968 -15.501  1.00 22.55           C  
ANISOU 3928  CG  GLU A 512     3421   2444   2704    279   -129    811       C  
ATOM   3929  CD  GLU A 512      11.973  -4.153 -16.957  1.00 24.14           C  
ANISOU 3929  CD  GLU A 512     3680   2690   2802    324   -123    850       C  
ATOM   3930  OE1 GLU A 512      12.776  -3.736 -17.815  1.00 24.99           O  
ANISOU 3930  OE1 GLU A 512     3870   2760   2864    270    -55    921       O  
ATOM   3931  OE2 GLU A 512      10.900  -4.717 -17.254  1.00 26.82           O  
ANISOU 3931  OE2 GLU A 512     3977   3118   3096    404   -186    810       O  
ATOM   3932  N   GLY A 513       8.783  -3.496 -15.676  1.00 28.69           N  
ANISOU 3932  N   GLY A 513     4173   3359   3368    618   -317    753       N  
ATOM   3933  CA  GLY A 513       7.670  -4.383 -15.362  1.00 29.33           C  
ANISOU 3933  CA  GLY A 513     4093   3596   3456    654   -359    693       C  
ATOM   3934  C   GLY A 513       7.984  -5.822 -15.001  1.00 31.12           C  
ANISOU 3934  C   GLY A 513     4201   3890   3734    524   -324    663       C  
ATOM   3935  O   GLY A 513       7.112  -6.516 -14.482  1.00 36.53           O  
ANISOU 3935  O   GLY A 513     4752   4683   4444    516   -344    628       O  
ATOM   3936  N   TYR A 514       9.204  -6.289 -15.263  1.00 29.90           N  
ANISOU 3936  N   TYR A 514     4088   3672   3601    424   -269    680       N  
ATOM   3937  CA  TYR A 514       9.592  -7.655 -14.883  1.00 26.88           C  
ANISOU 3937  CA  TYR A 514     3617   3315   3281    328   -246    655       C  
ATOM   3938  C   TYR A 514      10.433  -7.703 -13.592  1.00 27.10           C  
ANISOU 3938  C   TYR A 514     3619   3305   3374    272   -206    670       C  
ATOM   3939  O   TYR A 514      11.094  -8.706 -13.294  1.00 27.23           O  
ANISOU 3939  O   TYR A 514     3591   3309   3446    209   -187    672       O  
ATOM   3940  CB  TYR A 514      10.316  -8.347 -16.037  1.00 28.41           C  
ANISOU 3940  CB  TYR A 514     3852   3489   3453    292   -221    641       C  
ATOM   3941  CG  TYR A 514       9.449  -8.718 -17.234  1.00 27.20           C  
ANISOU 3941  CG  TYR A 514     3713   3401   3220    330   -284    599       C  
ATOM   3942  CD1 TYR A 514       8.058  -8.735 -17.163  1.00 30.43           C  
ANISOU 3942  CD1 TYR A 514     4048   3896   3618    368   -371    575       C  
ATOM   3943  CD2 TYR A 514      10.033  -9.088 -18.426  1.00 26.42           C  
ANISOU 3943  CD2 TYR A 514     3687   3303   3050    329   -259    573       C  
ATOM   3944  CE1 TYR A 514       7.290  -9.083 -18.263  1.00 31.38           C  
ANISOU 3944  CE1 TYR A 514     4168   4093   3663    395   -456    525       C  
ATOM   3945  CE2 TYR A 514       9.268  -9.448 -19.519  1.00 30.75           C  
ANISOU 3945  CE2 TYR A 514     4261   3922   3500    363   -335    516       C  
ATOM   3946  CZ  TYR A 514       7.905  -9.441 -19.434  1.00 31.05           C  
ANISOU 3946  CZ  TYR A 514     4226   4037   3535    391   -446    492       C  
ATOM   3947  OH  TYR A 514       7.171  -9.793 -20.538  1.00 34.14           O  
ANISOU 3947  OH  TYR A 514     4633   4515   3824    418   -548    425       O  
ATOM   3948  N   TYR A 515      10.353  -6.629 -12.811  1.00 26.36           N  
ANISOU 3948  N   TYR A 515     3559   3190   3268    312   -208    672       N  
ATOM   3949  CA  TYR A 515      11.065  -6.513 -11.550  1.00 24.11           C  
ANISOU 3949  CA  TYR A 515     3262   2887   3013    268   -196    668       C  
ATOM   3950  C   TYR A 515      10.277  -7.171 -10.411  1.00 24.14           C  
ANISOU 3950  C   TYR A 515     3175   2993   3003    272   -200    663       C  
ATOM   3951  O   TYR A 515       9.063  -7.023 -10.302  1.00 28.02           O  
ANISOU 3951  O   TYR A 515     3621   3567   3458    335   -205    644       O  
ATOM   3952  CB  TYR A 515      11.326  -5.033 -11.253  1.00 23.35           C  
ANISOU 3952  CB  TYR A 515     3268   2705   2900    302   -206    649       C  
ATOM   3953  CG  TYR A 515      11.999  -4.786  -9.942  1.00 24.63           C  
ANISOU 3953  CG  TYR A 515     3428   2858   3072    259   -219    617       C  
ATOM   3954  CD1 TYR A 515      13.359  -4.971  -9.789  1.00 28.47           C  
ANISOU 3954  CD1 TYR A 515     3896   3308   3612    156   -219    632       C  
ATOM   3955  CD2 TYR A 515      11.270  -4.374  -8.839  1.00 30.12           C  
ANISOU 3955  CD2 TYR A 515     4128   3607   3711    330   -235    560       C  
ATOM   3956  CE1 TYR A 515      13.978  -4.751  -8.553  1.00 29.28           C  
ANISOU 3956  CE1 TYR A 515     3990   3423   3710    116   -261    594       C  
ATOM   3957  CE2 TYR A 515      11.875  -4.150  -7.614  1.00 29.74           C  
ANISOU 3957  CE2 TYR A 515     4094   3568   3637    295   -261    516       C  
ATOM   3958  CZ  TYR A 515      13.222  -4.342  -7.480  1.00 27.11           C  
ANISOU 3958  CZ  TYR A 515     3748   3194   3357    185   -286    534       C  
ATOM   3959  OH  TYR A 515      13.794  -4.117  -6.262  1.00 27.58           O  
ANISOU 3959  OH  TYR A 515     3818   3283   3380    153   -339    482       O  
ATOM   3960  N   GLY A 516      10.977  -7.900  -9.556  1.00 21.60           N  
ANISOU 3960  N   GLY A 516     2820   2681   2706    207   -196    689       N  
ATOM   3961  CA  GLY A 516      10.346  -8.500  -8.407  1.00 20.74           C  
ANISOU 3961  CA  GLY A 516     2648   2670   2561    195   -187    715       C  
ATOM   3962  C   GLY A 516       9.642  -9.796  -8.739  1.00 24.63           C  
ANISOU 3962  C   GLY A 516     3067   3196   3095    139   -180    760       C  
ATOM   3963  O   GLY A 516       9.679 -10.276  -9.876  1.00 27.49           O  
ANISOU 3963  O   GLY A 516     3433   3501   3510    121   -195    748       O  
ATOM   3964  N   TYR A 517       8.990 -10.363  -7.731  1.00 26.74           N  
ANISOU 3964  N   TYR A 517     3275   3557   3328    102   -154    812       N  
ATOM   3965  CA  TYR A 517       8.450 -11.706  -7.839  1.00 25.39           C  
ANISOU 3965  CA  TYR A 517     3046   3386   3216      3   -150    877       C  
ATOM   3966  C   TYR A 517       7.356 -11.775  -8.906  1.00 28.12           C  
ANISOU 3966  C   TYR A 517     3321   3769   3595     -6   -164    827       C  
ATOM   3967  O   TYR A 517       7.346 -12.681  -9.734  1.00 30.29           O  
ANISOU 3967  O   TYR A 517     3599   3963   3947    -73   -201    820       O  
ATOM   3968  CB  TYR A 517       7.891 -12.162  -6.496  1.00 23.73           C  
ANISOU 3968  CB  TYR A 517     2785   3288   2942    -52   -101    967       C  
ATOM   3969  CG  TYR A 517       8.885 -12.233  -5.351  1.00 21.46           C  
ANISOU 3969  CG  TYR A 517     2570   2991   2593    -43   -110   1029       C  
ATOM   3970  CD1 TYR A 517       9.928 -13.144  -5.359  1.00 24.71           C  
ANISOU 3970  CD1 TYR A 517     3040   3271   3076    -77   -162   1095       C  
ATOM   3971  CD2 TYR A 517       8.741 -11.432  -4.241  1.00 22.74           C  
ANISOU 3971  CD2 TYR A 517     2739   3286   2614     13    -77   1014       C  
ATOM   3972  CE1 TYR A 517      10.820 -13.231  -4.295  1.00 27.38           C  
ANISOU 3972  CE1 TYR A 517     3430   3623   3351    -55   -196   1159       C  
ATOM   3973  CE2 TYR A 517       9.617 -11.506  -3.175  1.00 26.07           C  
ANISOU 3973  CE2 TYR A 517     3229   3723   2955     20   -108   1063       C  
ATOM   3974  CZ  TYR A 517      10.660 -12.403  -3.196  1.00 28.19           C  
ANISOU 3974  CZ  TYR A 517     3541   3871   3297    -16   -175   1144       C  
ATOM   3975  OH  TYR A 517      11.537 -12.464  -2.119  1.00 27.84           O  
ANISOU 3975  OH  TYR A 517     3552   3863   3163      7   -232   1197       O  
ATOM   3976  N   THR A 518       6.434 -10.821  -8.888  1.00 27.69           N  
ANISOU 3976  N   THR A 518     3203   3837   3479     76   -149    779       N  
ATOM   3977  CA  THR A 518       5.383 -10.803  -9.884  1.00 29.69           C  
ANISOU 3977  CA  THR A 518     3371   4155   3756     88   -187    730       C  
ATOM   3978  C   THR A 518       5.988 -10.636 -11.277  1.00 30.12           C  
ANISOU 3978  C   THR A 518     3525   4089   3828    126   -251    679       C  
ATOM   3979  O   THR A 518       5.639 -11.359 -12.207  1.00 30.02           O  
ANISOU 3979  O   THR A 518     3489   4063   3855     68   -304    650       O  
ATOM   3980  CB  THR A 518       4.378  -9.676  -9.631  1.00 31.46           C  
ANISOU 3980  CB  THR A 518     3510   4531   3911    222   -169    683       C  
ATOM   3981  OG1 THR A 518       3.626  -9.959  -8.446  1.00 32.81           O  
ANISOU 3981  OG1 THR A 518     3553   4865   4049    182    -89    724       O  
ATOM   3982  CG2 THR A 518       3.435  -9.564 -10.790  1.00 33.30           C  
ANISOU 3982  CG2 THR A 518     3658   4830   4164    265   -243    632       C  
ATOM   3983  N   GLY A 519       6.908  -9.686 -11.402  1.00 29.69           N  
ANISOU 3983  N   GLY A 519     3588   3955   3738    209   -243    666       N  
ATOM   3984  CA  GLY A 519       7.548  -9.393 -12.671  1.00 28.60           C  
ANISOU 3984  CA  GLY A 519     3550   3727   3591    242   -273    640       C  
ATOM   3985  C   GLY A 519       8.303 -10.581 -13.228  1.00 29.85           C  
ANISOU 3985  C   GLY A 519     3738   3801   3802    157   -276    635       C  
ATOM   3986  O   GLY A 519       8.176 -10.915 -14.408  1.00 31.77           O  
ANISOU 3986  O   GLY A 519     4009   4032   4029    158   -313    589       O  
ATOM   3987  N   ALA A 520       9.094 -11.227 -12.379  1.00 29.40           N  
ANISOU 3987  N   ALA A 520     3683   3688   3800    100   -245    675       N  
ATOM   3988  CA  ALA A 520       9.805 -12.429 -12.795  1.00 26.92           C  
ANISOU 3988  CA  ALA A 520     3398   3277   3556     50   -251    664       C  
ATOM   3989  C   ALA A 520       8.820 -13.458 -13.323  1.00 25.00           C  
ANISOU 3989  C   ALA A 520     3119   3031   3351    -21   -301    627       C  
ATOM   3990  O   ALA A 520       9.021 -14.015 -14.392  1.00 28.40           O  
ANISOU 3990  O   ALA A 520     3598   3402   3789    -20   -330    554       O  
ATOM   3991  CB  ALA A 520      10.605 -12.996 -11.659  1.00 26.02           C  
ANISOU 3991  CB  ALA A 520     3281   3111   3496     21   -234    731       C  
ATOM   3992  N   PHE A 521       7.741 -13.687 -12.585  1.00 25.37           N  
ANISOU 3992  N   PHE A 521     3072   3153   3413    -89   -309    669       N  
ATOM   3993  CA  PHE A 521       6.703 -14.628 -13.019  1.00 27.90           C  
ANISOU 3993  CA  PHE A 521     3329   3482   3788   -198   -365    636       C  
ATOM   3994  C   PHE A 521       6.075 -14.190 -14.351  1.00 31.02           C  
ANISOU 3994  C   PHE A 521     3713   3950   4125   -149   -436    533       C  
ATOM   3995  O   PHE A 521       5.956 -14.997 -15.274  1.00 33.54           O  
ANISOU 3995  O   PHE A 521     4066   4207   4470   -202   -503    450       O  
ATOM   3996  CB  PHE A 521       5.633 -14.796 -11.923  1.00 26.00           C  
ANISOU 3996  CB  PHE A 521     2954   3357   3566   -292   -336    717       C  
ATOM   3997  CG  PHE A 521       4.428 -15.597 -12.352  1.00 25.84           C  
ANISOU 3997  CG  PHE A 521     2824   3381   3613   -435   -395    685       C  
ATOM   3998  CD1 PHE A 521       4.550 -16.939 -12.698  1.00 27.02           C  
ANISOU 3998  CD1 PHE A 521     3034   3362   3872   -573   -447    669       C  
ATOM   3999  CD2 PHE A 521       3.173 -15.013 -12.404  1.00 27.79           C  
ANISOU 3999  CD2 PHE A 521     2901   3833   3826   -429   -408    663       C  
ATOM   4000  CE1 PHE A 521       3.446 -17.684 -13.103  1.00 26.02           C  
ANISOU 4000  CE1 PHE A 521     2804   3260   3821   -739   -518    627       C  
ATOM   4001  CE2 PHE A 521       2.059 -15.754 -12.802  1.00 30.15           C  
ANISOU 4001  CE2 PHE A 521     3061   4196   4198   -583   -476    628       C  
ATOM   4002  CZ  PHE A 521       2.203 -17.094 -13.149  1.00 29.16           C  
ANISOU 4002  CZ  PHE A 521     3004   3890   4185   -757   -533    610       C  
ATOM   4003  N   ARG A 522       5.694 -12.916 -14.451  1.00 28.82           N  
ANISOU 4003  N   ARG A 522     3403   3789   3757    -36   -432    535       N  
ATOM   4004  CA  ARG A 522       5.101 -12.391 -15.681  1.00 28.67           C  
ANISOU 4004  CA  ARG A 522     3387   3849   3660     39   -514    464       C  
ATOM   4005  C   ARG A 522       6.027 -12.590 -16.866  1.00 28.18           C  
ANISOU 4005  C   ARG A 522     3474   3690   3542     72   -528    406       C  
ATOM   4006  O   ARG A 522       5.588 -12.956 -17.959  1.00 31.37           O  
ANISOU 4006  O   ARG A 522     3895   4127   3897     66   -616    320       O  
ATOM   4007  CB  ARG A 522       4.786 -10.902 -15.568  1.00 26.74           C  
ANISOU 4007  CB  ARG A 522     3135   3693   3333    191   -505    496       C  
ATOM   4008  CG  ARG A 522       4.240 -10.352 -16.859  1.00 28.07           C  
ANISOU 4008  CG  ARG A 522     3330   3930   3405    291   -604    450       C  
ATOM   4009  CD  ARG A 522       3.971  -8.884 -16.800  1.00 28.67           C  
ANISOU 4009  CD  ARG A 522     3434   4046   3412    461   -607    492       C  
ATOM   4010  NE  ARG A 522       3.477  -8.392 -18.080  1.00 25.82           N  
ANISOU 4010  NE  ARG A 522     3121   3746   2944    570   -718    474       N  
ATOM   4011  CZ  ARG A 522       2.989  -7.174 -18.263  1.00 27.69           C  
ANISOU 4011  CZ  ARG A 522     3386   4018   3119    745   -764    512       C  
ATOM   4012  NH1 ARG A 522       2.946  -6.321 -17.252  1.00 31.16           N  
ANISOU 4012  NH1 ARG A 522     3814   4427   3599    830   -701    545       N  
ATOM   4013  NH2 ARG A 522       2.559  -6.801 -19.462  1.00 27.47           N  
ANISOU 4013  NH2 ARG A 522     3414   4047   2976    849   -882    514       N  
ATOM   4014  N   CYS A 523       7.306 -12.316 -16.649  1.00 27.46           N  
ANISOU 4014  N   CYS A 523     3480   3504   3448    110   -441    444       N  
ATOM   4015  CA  CYS A 523       8.329 -12.622 -17.641  1.00 27.37           C  
ANISOU 4015  CA  CYS A 523     3586   3422   3392    138   -416    392       C  
ATOM   4016  C   CYS A 523       8.229 -14.062 -18.117  1.00 27.52           C  
ANISOU 4016  C   CYS A 523     3619   3371   3466     64   -468    291       C  
ATOM   4017  O   CYS A 523       8.340 -14.312 -19.313  1.00 33.95           O  
ANISOU 4017  O   CYS A 523     4512   4193   4193     97   -500    194       O  
ATOM   4018  CB  CYS A 523       9.719 -12.390 -17.075  1.00 25.69           C  
ANISOU 4018  CB  CYS A 523     3413   3132   3217    156   -313    448       C  
ATOM   4019  SG  CYS A 523      10.982 -12.972 -18.171  1.00 25.97           S  
ANISOU 4019  SG  CYS A 523     3538   3112   3217    194   -253    374       S  
ATOM   4020  N   LEU A 524       8.027 -14.995 -17.181  1.00 25.23           N  
ANISOU 4020  N   LEU A 524     3272   3004   3310    -37   -476    315       N  
ATOM   4021  CA  LEU A 524       7.895 -16.424 -17.504  1.00 26.96           C  
ANISOU 4021  CA  LEU A 524     3526   3100   3617   -126   -536    225       C  
ATOM   4022  C   LEU A 524       6.695 -16.687 -18.376  1.00 26.72           C  
ANISOU 4022  C   LEU A 524     3460   3143   3548   -191   -658    120       C  
ATOM   4023  O   LEU A 524       6.768 -17.493 -19.293  1.00 29.40           O  
ANISOU 4023  O   LEU A 524     3886   3408   3878   -210   -723    -17       O  
ATOM   4024  CB  LEU A 524       7.763 -17.276 -16.236  1.00 28.69           C  
ANISOU 4024  CB  LEU A 524     3699   3215   3985   -241   -526    316       C  
ATOM   4025  CG  LEU A 524       7.525 -18.784 -16.413  1.00 28.35           C  
ANISOU 4025  CG  LEU A 524     3711   2993   4068   -362   -598    247       C  
ATOM   4026  CD1 LEU A 524       8.784 -19.447 -16.909  1.00 29.35           C  
ANISOU 4026  CD1 LEU A 524     3979   2951   4222   -259   -576    165       C  
ATOM   4027  CD2 LEU A 524       7.052 -19.439 -15.115  1.00 27.77           C  
ANISOU 4027  CD2 LEU A 524     3579   2851   4121   -510   -589    388       C  
ATOM   4028  N   VAL A 525       5.587 -16.026 -18.068  1.00 26.67           N  
ANISOU 4028  N   VAL A 525     3320   3293   3521   -218   -698    171       N  
ATOM   4029  CA  VAL A 525       4.383 -16.150 -18.871  1.00 32.55           C  
ANISOU 4029  CA  VAL A 525     3987   4152   4227   -271   -834     76       C  
ATOM   4030  C   VAL A 525       4.611 -15.692 -20.304  1.00 36.42           C  
ANISOU 4030  C   VAL A 525     4591   4705   4542   -147   -894    -25       C  
ATOM   4031  O   VAL A 525       4.348 -16.436 -21.249  1.00 39.20           O  
ANISOU 4031  O   VAL A 525     4996   5039   4859   -195  -1003   -171       O  
ATOM   4032  CB  VAL A 525       3.255 -15.301 -18.306  1.00 33.21           C  
ANISOU 4032  CB  VAL A 525     3883   4430   4304   -261   -851    154       C  
ATOM   4033  CG1 VAL A 525       2.183 -15.088 -19.357  1.00 33.08           C  
ANISOU 4033  CG1 VAL A 525     3786   4576   4205   -243  -1008     56       C  
ATOM   4034  CG2 VAL A 525       2.699 -15.953 -17.064  1.00 36.18           C  
ANISOU 4034  CG2 VAL A 525     4120   4798   4830   -424   -808    234       C  
ATOM   4035  N   GLU A 526       5.116 -14.474 -20.459  1.00 34.58           N  
ANISOU 4035  N   GLU A 526     4413   4536   4189      5   -824     53       N  
ATOM   4036  CA  GLU A 526       5.145 -13.824 -21.765  1.00 36.15           C  
ANISOU 4036  CA  GLU A 526     4714   4831   4190    125   -878      8       C  
ATOM   4037  C   GLU A 526       6.354 -14.193 -22.623  1.00 35.35           C  
ANISOU 4037  C   GLU A 526     4790   4649   3991    173   -805    -64       C  
ATOM   4038  O   GLU A 526       6.221 -14.347 -23.831  1.00 35.17           O  
ANISOU 4038  O   GLU A 526     4858   4694   3810    215   -881   -170       O  
ATOM   4039  CB  GLU A 526       5.061 -12.305 -21.583  1.00 35.56           C  
ANISOU 4039  CB  GLU A 526     4635   4840   4034    257   -840    142       C  
ATOM   4040  CG  GLU A 526       3.763 -11.881 -20.938  1.00 36.41           C  
ANISOU 4040  CG  GLU A 526     4561   5068   4205    262   -919    181       C  
ATOM   4041  CD  GLU A 526       3.707 -10.418 -20.569  1.00 35.49           C  
ANISOU 4041  CD  GLU A 526     4456   4988   4042    412   -877    299       C  
ATOM   4042  OE1 GLU A 526       4.765  -9.842 -20.237  1.00 36.42           O  
ANISOU 4042  OE1 GLU A 526     4689   4995   4153    446   -754    375       O  
ATOM   4043  OE2 GLU A 526       2.593  -9.843 -20.579  1.00 31.41           O  
ANISOU 4043  OE2 GLU A 526     3823   4606   3506    496   -974    309       O  
ATOM   4044  N   LYS A 527       7.522 -14.345 -22.002  1.00 34.52           N  
ANISOU 4044  N   LYS A 527     4722   4424   3970    176   -662    -14       N  
ATOM   4045  CA  LYS A 527       8.782 -14.375 -22.748  1.00 33.61           C  
ANISOU 4045  CA  LYS A 527     4736   4281   3753    256   -552    -51       C  
ATOM   4046  C   LYS A 527       9.743 -15.528 -22.411  1.00 33.38           C  
ANISOU 4046  C   LYS A 527     4730   4099   3853    236   -480   -126       C  
ATOM   4047  O   LYS A 527      10.272 -16.163 -23.319  1.00 33.43           O  
ANISOU 4047  O   LYS A 527     4835   4088   3780    289   -460   -263       O  
ATOM   4048  CB  LYS A 527       9.514 -13.052 -22.537  1.00 33.24           C  
ANISOU 4048  CB  LYS A 527     4709   4274   3648    323   -429    104       C  
ATOM   4049  CG  LYS A 527       8.762 -11.814 -23.009  1.00 32.86           C  
ANISOU 4049  CG  LYS A 527     4688   4339   3457    385   -490    190       C  
ATOM   4050  CD  LYS A 527       9.764 -10.758 -23.444  1.00 33.54           C  
ANISOU 4050  CD  LYS A 527     4879   4438   3427    444   -359    303       C  
ATOM   4051  CE  LYS A 527       9.168  -9.372 -23.561  1.00 33.86           C  
ANISOU 4051  CE  LYS A 527     4965   4519   3380    509   -406    437       C  
ATOM   4052  NZ  LYS A 527      10.230  -8.412 -23.981  1.00 32.48           N  
ANISOU 4052  NZ  LYS A 527     4908   4323   3110    524   -267    562       N  
ATOM   4053  N   GLY A 528       9.983 -15.782 -21.125  1.00 33.17           N  
ANISOU 4053  N   GLY A 528     4623   3970   4009    182   -444    -40       N  
ATOM   4054  CA  GLY A 528      10.995 -16.765 -20.695  1.00 36.00           C  
ANISOU 4054  CA  GLY A 528     5003   4179   4497    198   -382    -76       C  
ATOM   4055  C   GLY A 528      10.612 -18.246 -20.608  1.00 37.66           C  
ANISOU 4055  C   GLY A 528     5251   4218   4839    128   -475   -189       C  
ATOM   4056  O   GLY A 528       9.477 -18.640 -20.914  1.00 37.10           O  
ANISOU 4056  O   GLY A 528     5178   4147   4770     28   -599   -260       O  
ATOM   4057  N   ASP A 529      11.594 -19.058 -20.196  1.00 34.60           N  
ANISOU 4057  N   ASP A 529     4898   3678   4572    181   -423   -205       N  
ATOM   4058  CA  ASP A 529      11.432 -20.504 -19.984  1.00 35.05           C  
ANISOU 4058  CA  ASP A 529     5025   3507   4787    130   -504   -289       C  
ATOM   4059  C   ASP A 529      11.457 -20.911 -18.511  1.00 33.71           C  
ANISOU 4059  C   ASP A 529     4804   3208   4797     56   -510   -121       C  
ATOM   4060  O   ASP A 529      11.129 -22.055 -18.185  1.00 34.13           O  
ANISOU 4060  O   ASP A 529     4921   3052   4993    -27   -587   -141       O  
ATOM   4061  CB  ASP A 529      12.537 -21.279 -20.695  1.00 36.12           C  
ANISOU 4061  CB  ASP A 529     5267   3534   4924    289   -454   -450       C  
ATOM   4062  CG  ASP A 529      12.558 -21.028 -22.173  1.00 41.92           C  
ANISOU 4062  CG  ASP A 529     6077   4401   5450    369   -437   -628       C  
ATOM   4063  OD1 ASP A 529      11.456 -20.899 -22.757  1.00 45.19           O  
ANISOU 4063  OD1 ASP A 529     6514   4883   5772    270   -545   -693       O  
ATOM   4064  OD2 ASP A 529      13.675 -20.968 -22.747  1.00 41.73           O  
ANISOU 4064  OD2 ASP A 529     6078   4433   5346    533   -315   -700       O  
ATOM   4065  N   VAL A 530      11.868 -20.000 -17.632  1.00 29.80           N  
ANISOU 4065  N   VAL A 530     4212   2825   4287     81   -435     43       N  
ATOM   4066  CA  VAL A 530      11.892 -20.282 -16.210  1.00 32.04           C  
ANISOU 4066  CA  VAL A 530     4454   3029   4691     21   -441    210       C  
ATOM   4067  C   VAL A 530      11.997 -19.020 -15.374  1.00 31.80           C  
ANISOU 4067  C   VAL A 530     4316   3175   4590     25   -380    354       C  
ATOM   4068  O   VAL A 530      12.845 -18.167 -15.621  1.00 31.80           O  
ANISOU 4068  O   VAL A 530     4287   3279   4517    124   -310    349       O  
ATOM   4069  CB  VAL A 530      13.067 -21.185 -15.822  1.00 36.65           C  
ANISOU 4069  CB  VAL A 530     5097   3434   5393    137   -430    219       C  
ATOM   4070  CG1 VAL A 530      14.400 -20.515 -16.147  1.00 35.48           C  
ANISOU 4070  CG1 VAL A 530     4896   3403   5181    309   -333    189       C  
ATOM   4071  CG2 VAL A 530      12.982 -21.537 -14.334  1.00 38.26           C  
ANISOU 4071  CG2 VAL A 530     5283   3558   5695     68   -458    415       C  
ATOM   4072  N   ALA A 531      11.138 -18.918 -14.372  1.00 32.25           N  
ANISOU 4072  N   ALA A 531     4317   3265   4670    -92   -403    476       N  
ATOM   4073  CA  ALA A 531      11.214 -17.833 -13.423  1.00 31.42           C  
ANISOU 4073  CA  ALA A 531     4132   3305   4501    -81   -354    594       C  
ATOM   4074  C   ALA A 531      11.939 -18.341 -12.187  1.00 32.68           C  
ANISOU 4074  C   ALA A 531     4302   3384   4730    -65   -353    719       C  
ATOM   4075  O   ALA A 531      11.781 -19.506 -11.802  1.00 31.75           O  
ANISOU 4075  O   ALA A 531     4242   3111   4712   -122   -395    770       O  
ATOM   4076  CB  ALA A 531       9.822 -17.347 -13.069  1.00 30.13           C  
ANISOU 4076  CB  ALA A 531     3890   3268   4292   -187   -366    637       C  
ATOM   4077  N   PHE A 532      12.743 -17.466 -11.584  1.00 32.68           N  
ANISOU 4077  N   PHE A 532     4259   3481   4676      7   -316    771       N  
ATOM   4078  CA  PHE A 532      13.362 -17.731 -10.283  1.00 33.87           C  
ANISOU 4078  CA  PHE A 532     4406   3611   4851     27   -335    899       C  
ATOM   4079  C   PHE A 532      12.728 -16.847  -9.221  1.00 32.30           C  
ANISOU 4079  C   PHE A 532     4159   3565   4549    -32   -315    985       C  
ATOM   4080  O   PHE A 532      13.094 -15.680  -9.077  1.00 30.25           O  
ANISOU 4080  O   PHE A 532     3860   3419   4213     12   -292    957       O  
ATOM   4081  CB  PHE A 532      14.858 -17.473 -10.345  1.00 32.87           C  
ANISOU 4081  CB  PHE A 532     4250   3495   4745    155   -330    872       C  
ATOM   4082  CG  PHE A 532      15.571 -18.369 -11.297  1.00 33.30           C  
ANISOU 4082  CG  PHE A 532     4340   3421   4893    251   -332    778       C  
ATOM   4083  CD1 PHE A 532      15.616 -19.726 -11.072  1.00 33.73           C  
ANISOU 4083  CD1 PHE A 532     4475   3285   5057    276   -390    812       C  
ATOM   4084  CD2 PHE A 532      16.185 -17.857 -12.429  1.00 32.32           C  
ANISOU 4084  CD2 PHE A 532     4181   3359   4739    321   -269    655       C  
ATOM   4085  CE1 PHE A 532      16.268 -20.558 -11.953  1.00 36.34           C  
ANISOU 4085  CE1 PHE A 532     4851   3483   5475    395   -392    696       C  
ATOM   4086  CE2 PHE A 532      16.836 -18.681 -13.309  1.00 31.54           C  
ANISOU 4086  CE2 PHE A 532     4112   3169   4705    431   -252    548       C  
ATOM   4087  CZ  PHE A 532      16.878 -20.031 -13.077  1.00 34.38           C  
ANISOU 4087  CZ  PHE A 532     4552   3332   5181    480   -317    553       C  
ATOM   4088  N   VAL A 533      11.783 -17.415  -8.481  1.00 30.59           N  
ANISOU 4088  N   VAL A 533     3949   3345   4329   -135   -319   1085       N  
ATOM   4089  CA  VAL A 533      10.955 -16.648  -7.560  1.00 33.55           C  
ANISOU 4089  CA  VAL A 533     4267   3891   4588   -186   -276   1145       C  
ATOM   4090  C   VAL A 533      10.792 -17.399  -6.255  1.00 34.97           C  
ANISOU 4090  C   VAL A 533     4478   4066   4743   -251   -277   1316       C  
ATOM   4091  O   VAL A 533      11.341 -18.476  -6.096  1.00 39.20           O  
ANISOU 4091  O   VAL A 533     5090   4439   5363   -252   -325   1396       O  
ATOM   4092  CB  VAL A 533       9.551 -16.382  -8.166  1.00 35.18           C  
ANISOU 4092  CB  VAL A 533     4402   4182   4781   -264   -246   1087       C  
ATOM   4093  CG1 VAL A 533       9.647 -15.383  -9.303  1.00 29.76           C  
ANISOU 4093  CG1 VAL A 533     3702   3539   4068   -180   -248    947       C  
ATOM   4094  CG2 VAL A 533       8.895 -17.695  -8.624  1.00 33.64           C  
ANISOU 4094  CG2 VAL A 533     4223   3856   4701   -392   -276   1106       C  
ATOM   4095  N   LYS A 534      10.051 -16.811  -5.320  1.00 37.02           N  
ANISOU 4095  N   LYS A 534     4688   4504   4874   -291   -220   1374       N  
ATOM   4096  CA  LYS A 534       9.675 -17.488  -4.070  1.00 37.93           C  
ANISOU 4096  CA  LYS A 534     4831   4658   4923   -376   -192   1557       C  
ATOM   4097  C   LYS A 534       8.562 -18.510  -4.310  1.00 38.38           C  
ANISOU 4097  C   LYS A 534     4865   4648   5071   -552   -158   1636       C  
ATOM   4098  O   LYS A 534       7.942 -18.523  -5.376  1.00 38.90           O  
ANISOU 4098  O   LYS A 534     4870   4684   5228   -601   -163   1522       O  
ATOM   4099  CB  LYS A 534       9.241 -16.471  -3.015  1.00 37.33           C  
ANISOU 4099  CB  LYS A 534     4706   4826   4652   -348   -123   1569       C  
ATOM   4100  CG  LYS A 534       8.056 -15.601  -3.426  1.00 37.98           C  
ANISOU 4100  CG  LYS A 534     4665   5068   4697   -358    -45   1458       C  
ATOM   4101  CD  LYS A 534       7.701 -14.595  -2.344  1.00 40.59           C  
ANISOU 4101  CD  LYS A 534     4964   5628   4830   -292     25   1442       C  
ATOM   4102  CE  LYS A 534       6.517 -13.748  -2.759  1.00 42.11           C  
ANISOU 4102  CE  LYS A 534     5026   5974   5001   -261     97   1327       C  
ATOM   4103  NZ  LYS A 534       6.056 -12.851  -1.674  1.00 43.41           N  
ANISOU 4103  NZ  LYS A 534     5158   6365   4971   -178    182   1296       N  
ATOM   4104  N   HIS A 535       8.309 -19.356  -3.314  1.00 39.87           N  
ANISOU 4104  N   HIS A 535     5104   4816   5229   -659   -131   1836       N  
ATOM   4105  CA  HIS A 535       7.396 -20.499  -3.479  1.00 43.83           C  
ANISOU 4105  CA  HIS A 535     5605   5201   5848   -867   -110   1941       C  
ATOM   4106  C   HIS A 535       5.923 -20.124  -3.565  1.00 43.68           C  
ANISOU 4106  C   HIS A 535     5405   5394   5797  -1007     -9   1913       C  
ATOM   4107  O   HIS A 535       5.109 -20.936  -4.000  1.00 44.13           O  
ANISOU 4107  O   HIS A 535     5418   5365   5983  -1198     -8   1944       O  
ATOM   4108  CB  HIS A 535       7.589 -21.532  -2.362  1.00 46.73           C  
ANISOU 4108  CB  HIS A 535     6101   5465   6190   -955   -106   2202       C  
ATOM   4109  CG  HIS A 535       7.169 -21.057  -1.005  1.00 50.13           C  
ANISOU 4109  CG  HIS A 535     6492   6165   6391   -980      2   2349       C  
ATOM   4110  ND1 HIS A 535       7.951 -20.227  -0.230  1.00 51.03           N  
ANISOU 4110  ND1 HIS A 535     6639   6430   6319   -805    -13   2335       N  
ATOM   4111  CD2 HIS A 535       6.058 -21.315  -0.275  1.00 54.62           C  
ANISOU 4111  CD2 HIS A 535     6988   6892   6874  -1165    133   2508       C  
ATOM   4112  CE1 HIS A 535       7.335 -19.984   0.913  1.00 53.59           C  
ANISOU 4112  CE1 HIS A 535     6933   6994   6435   -861    100   2463       C  
ATOM   4113  NE2 HIS A 535       6.185 -20.634   0.913  1.00 55.53           N  
ANISOU 4113  NE2 HIS A 535     7107   7259   6733  -1077    204   2579       N  
ATOM   4114  N   GLN A 536       5.581 -18.908  -3.155  1.00 46.16           N  
ANISOU 4114  N   GLN A 536     5608   5980   5950   -910     67   1845       N  
ATOM   4115  CA  GLN A 536       4.183 -18.484  -3.113  1.00 48.92           C  
ANISOU 4115  CA  GLN A 536     5757   6575   6257  -1000    171   1818       C  
ATOM   4116  C   GLN A 536       3.744 -17.634  -4.315  1.00 44.29           C  
ANISOU 4116  C   GLN A 536     5051   6052   5726   -909    129   1597       C  
ATOM   4117  O   GLN A 536       2.552 -17.399  -4.485  1.00 45.37           O  
ANISOU 4117  O   GLN A 536     4997   6375   5867   -977    185   1561       O  
ATOM   4118  CB  GLN A 536       3.896 -17.748  -1.797  1.00 52.87           C  
ANISOU 4118  CB  GLN A 536     6205   7355   6528   -938    299   1888       C  
ATOM   4119  CG  GLN A 536       2.469 -17.947  -1.251  1.00 59.47           C  
ANISOU 4119  CG  GLN A 536     6846   8439   7312  -1105    453   1986       C  
ATOM   4120  CD  GLN A 536       2.171 -19.387  -0.766  1.00 62.91           C  
ANISOU 4120  CD  GLN A 536     7326   8763   7815  -1374    495   2238       C  
ATOM   4121  OE1 GLN A 536       2.065 -20.328  -1.563  1.00 61.91           O  
ANISOU 4121  OE1 GLN A 536     7224   8401   7898  -1532    412   2255       O  
ATOM   4122  NE2 GLN A 536       2.008 -19.542   0.545  1.00 61.98           N  
ANISOU 4122  NE2 GLN A 536     7230   8812   7508  -1428    624   2433       N  
ATOM   4123  N   THR A 537       4.681 -17.236  -5.175  1.00 39.59           N  
ANISOU 4123  N   THR A 537     4556   5310   5176   -764     29   1464       N  
ATOM   4124  CA  THR A 537       4.396 -16.236  -6.222  1.00 37.68           C  
ANISOU 4124  CA  THR A 537     4240   5139   4938   -644     -9   1279       C  
ATOM   4125  C   THR A 537       3.321 -16.644  -7.227  1.00 35.96           C  
ANISOU 4125  C   THR A 537     3891   4943   4829   -760    -50   1210       C  
ATOM   4126  O   THR A 537       2.555 -15.800  -7.702  1.00 33.97           O  
ANISOU 4126  O   THR A 537     3505   4858   4542   -683    -53   1108       O  
ATOM   4127  CB  THR A 537       5.666 -15.843  -7.017  1.00 35.17           C  
ANISOU 4127  CB  THR A 537     4063   4654   4645   -500    -93   1175       C  
ATOM   4128  OG1 THR A 537       6.672 -15.356  -6.115  1.00 34.08           O  
ANISOU 4128  OG1 THR A 537     4016   4519   4413   -398    -76   1217       O  
ATOM   4129  CG2 THR A 537       5.334 -14.767  -8.050  1.00 29.69           C  
ANISOU 4129  CG2 THR A 537     3316   4034   3930   -382   -124   1022       C  
ATOM   4130  N   VAL A 538       3.265 -17.928  -7.555  1.00 36.37           N  
ANISOU 4130  N   VAL A 538     3987   4818   5016   -938   -100   1259       N  
ATOM   4131  CA  VAL A 538       2.254 -18.409  -8.495  1.00 35.50           C  
ANISOU 4131  CA  VAL A 538     3754   4720   5015  -1080   -165   1180       C  
ATOM   4132  C   VAL A 538       0.856 -18.271  -7.869  1.00 36.53           C  
ANISOU 4132  C   VAL A 538     3635   5123   5121  -1206    -73   1246       C  
ATOM   4133  O   VAL A 538       0.054 -17.478  -8.355  1.00 38.00           O  
ANISOU 4133  O   VAL A 538     3647   5515   5275  -1129    -88   1137       O  
ATOM   4134  CB  VAL A 538       2.557 -19.839  -8.992  1.00 35.58           C  
ANISOU 4134  CB  VAL A 538     3896   4436   5185  -1248   -253   1193       C  
ATOM   4135  CG1 VAL A 538       1.527 -20.283 -10.022  1.00 36.66           C  
ANISOU 4135  CG1 VAL A 538     3911   4589   5429  -1404   -349   1074       C  
ATOM   4136  CG2 VAL A 538       3.963 -19.892  -9.569  1.00 33.32           C  
ANISOU 4136  CG2 VAL A 538     3824   3929   4908  -1080   -319   1114       C  
ATOM   4137  N   PRO A 539       0.579 -18.980  -6.757  1.00 36.30           N  
ANISOU 4137  N   PRO A 539     3582   5116   5093  -1382     30   1434       N  
ATOM   4138  CA  PRO A 539      -0.712 -18.780  -6.112  1.00 38.01           C  
ANISOU 4138  CA  PRO A 539     3536   5640   5267  -1492    152   1500       C  
ATOM   4139  C   PRO A 539      -1.090 -17.315  -6.037  1.00 41.53           C  
ANISOU 4139  C   PRO A 539     3839   6368   5571  -1245    204   1383       C  
ATOM   4140  O   PRO A 539      -2.219 -16.943  -6.336  1.00 47.18           O  
ANISOU 4140  O   PRO A 539     4301   7321   6305  -1255    218   1313       O  
ATOM   4141  CB  PRO A 539      -0.479 -19.306  -4.699  1.00 38.61           C  
ANISOU 4141  CB  PRO A 539     3689   5722   5261  -1597    289   1731       C  
ATOM   4142  CG  PRO A 539       0.560 -20.295  -4.828  1.00 39.33           C  
ANISOU 4142  CG  PRO A 539     4044   5454   5447  -1657    197   1806       C  
ATOM   4143  CD  PRO A 539       1.415 -19.926  -6.001  1.00 37.10           C  
ANISOU 4143  CD  PRO A 539     3888   4992   5216  -1467     49   1606       C  
ATOM   4144  N   GLN A 540      -0.129 -16.483  -5.673  1.00 41.07           N  
ANISOU 4144  N   GLN A 540     3945   6272   5386  -1017    217   1352       N  
ATOM   4145  CA  GLN A 540      -0.403 -15.086  -5.450  1.00 45.03           C  
ANISOU 4145  CA  GLN A 540     4362   6993   5755   -777    269   1246       C  
ATOM   4146  C   GLN A 540      -0.776 -14.325  -6.713  1.00 43.06           C  
ANISOU 4146  C   GLN A 540     4036   6769   5555   -632    153   1071       C  
ATOM   4147  O   GLN A 540      -1.301 -13.227  -6.620  1.00 46.16           O  
ANISOU 4147  O   GLN A 540     4319   7352   5866   -441    187    985       O  
ATOM   4148  CB  GLN A 540       0.796 -14.443  -4.771  1.00 47.05           C  
ANISOU 4148  CB  GLN A 540     4835   7162   5881   -605    286   1249       C  
ATOM   4149  CG  GLN A 540       1.058 -15.058  -3.418  1.00 50.95           C  
ANISOU 4149  CG  GLN A 540     5392   7690   6276   -711    395   1427       C  
ATOM   4150  CD  GLN A 540       2.029 -14.272  -2.592  1.00 53.67           C  
ANISOU 4150  CD  GLN A 540     5901   8033   6457   -533    410   1407       C  
ATOM   4151  OE1 GLN A 540       1.693 -13.826  -1.497  1.00 61.35           O  
ANISOU 4151  OE1 GLN A 540     6831   9222   7256   -478    529   1435       O  
ATOM   4152  NE2 GLN A 540       3.245 -14.101  -3.099  1.00 51.22           N  
ANISOU 4152  NE2 GLN A 540     5772   7495   6194   -447    290   1348       N  
ATOM   4153  N   ASN A 541      -0.526 -14.909  -7.880  1.00 40.82           N  
ANISOU 4153  N   ASN A 541     3822   6296   5392   -710     15   1017       N  
ATOM   4154  CA  ASN A 541      -0.784 -14.239  -9.153  1.00 40.96           C  
ANISOU 4154  CA  ASN A 541     3808   6330   5427   -572   -111    866       C  
ATOM   4155  C   ASN A 541      -1.620 -15.067 -10.122  1.00 42.87           C  
ANISOU 4155  C   ASN A 541     3909   6587   5792   -749   -225    816       C  
ATOM   4156  O   ASN A 541      -1.595 -14.823 -11.329  1.00 42.71           O  
ANISOU 4156  O   ASN A 541     3928   6519   5781   -668   -363    699       O  
ATOM   4157  CB  ASN A 541       0.545 -13.877  -9.819  1.00 39.93           C  
ANISOU 4157  CB  ASN A 541     3941   5962   5271   -438   -186    810       C  
ATOM   4158  CG  ASN A 541       1.271 -12.765  -9.102  1.00 38.57           C  
ANISOU 4158  CG  ASN A 541     3882   5792   4982   -244   -116    814       C  
ATOM   4159  OD1 ASN A 541       0.725 -11.680  -8.908  1.00 42.47           O  
ANISOU 4159  OD1 ASN A 541     4294   6442   5403    -78    -88    761       O  
ATOM   4160  ND2 ASN A 541       2.509 -13.022  -8.712  1.00 33.33           N  
ANISOU 4160  ND2 ASN A 541     3406   4951   4308   -257   -100    865       N  
ATOM   4161  N   THR A 542      -2.366 -16.034  -9.598  1.00 44.24           N  
ANISOU 4161  N   THR A 542     3924   6833   6051  -1001   -171    905       N  
ATOM   4162  CA  THR A 542      -3.210 -16.882 -10.426  1.00 47.68           C  
ANISOU 4162  CA  THR A 542     4211   7283   6623  -1217   -289    851       C  
ATOM   4163  C   THR A 542      -4.584 -17.003  -9.803  1.00 49.49           C  
ANISOU 4163  C   THR A 542     4092   7820   6891  -1368   -199    911       C  
ATOM   4164  O   THR A 542      -4.826 -16.469  -8.723  1.00 46.60           O  
ANISOU 4164  O   THR A 542     3624   7651   6431  -1290    -30    996       O  
ATOM   4165  CB  THR A 542      -2.593 -18.281 -10.609  1.00 49.07           C  
ANISOU 4165  CB  THR A 542     4581   7140   6923  -1455   -344    897       C  
ATOM   4166  OG1 THR A 542      -2.126 -18.759  -9.349  1.00 51.23           O  
ANISOU 4166  OG1 THR A 542     4949   7331   7185  -1547   -197   1082       O  
ATOM   4167  CG2 THR A 542      -1.427 -18.228 -11.575  1.00 48.74           C  
ANISOU 4167  CG2 THR A 542     4818   6843   6860  -1305   -458    785       C  
ATOM   4168  N   GLY A 543      -5.488 -17.691 -10.497  1.00 53.19           N  
ANISOU 4168  N   GLY A 543     4368   8349   7492  -1584   -313    854       N  
ATOM   4169  CA  GLY A 543      -6.844 -17.872 -10.008  1.00 57.83           C  
ANISOU 4169  CA  GLY A 543     4573   9256   8142  -1764   -233    907       C  
ATOM   4170  C   GLY A 543      -7.497 -16.536  -9.697  1.00 58.59           C  
ANISOU 4170  C   GLY A 543     4434   9709   8118  -1471   -154    856       C  
ATOM   4171  O   GLY A 543      -8.188 -16.394  -8.685  1.00 61.70           O  
ANISOU 4171  O   GLY A 543     4590  10375   8478  -1511     32    949       O  
ATOM   4172  N   GLY A 544      -7.251 -15.551 -10.559  1.00 56.09           N  
ANISOU 4172  N   GLY A 544     4202   9384   7727  -1165   -288    714       N  
ATOM   4173  CA  GLY A 544      -7.911 -14.252 -10.470  1.00 56.37           C  
ANISOU 4173  CA  GLY A 544     4035   9715   7669   -851   -260    642       C  
ATOM   4174  C   GLY A 544      -7.402 -13.293  -9.405  1.00 54.03           C  
ANISOU 4174  C   GLY A 544     3857   9448   7222   -600    -77    687       C  
ATOM   4175  O   GLY A 544      -7.814 -12.135  -9.378  1.00 53.48           O  
ANISOU 4175  O   GLY A 544     3685   9561   7076   -296    -68    606       O  
ATOM   4176  N   LYS A 545      -6.509 -13.751  -8.532  1.00 52.53           N  
ANISOU 4176  N   LYS A 545     3893   9076   6989   -710     52    804       N  
ATOM   4177  CA  LYS A 545      -6.125 -12.952  -7.366  1.00 53.61           C  
ANISOU 4177  CA  LYS A 545     4116   9281   6971   -514    229    842       C  
ATOM   4178  C   LYS A 545      -5.278 -11.746  -7.749  1.00 52.22           C  
ANISOU 4178  C   LYS A 545     4195   8944   6702   -187    150    736       C  
ATOM   4179  O   LYS A 545      -5.288 -10.741  -7.043  1.00 53.43           O  
ANISOU 4179  O   LYS A 545     4358   9206   6738     50    249    695       O  
ATOM   4180  CB  LYS A 545      -5.422 -13.813  -6.313  1.00 53.70           C  
ANISOU 4180  CB  LYS A 545     4295   9163   6947   -726    366   1009       C  
ATOM   4181  CG  LYS A 545      -6.363 -14.789  -5.631  1.00 59.69           C  
ANISOU 4181  CG  LYS A 545     4792  10128   7760  -1032    504   1149       C  
ATOM   4182  CD  LYS A 545      -5.752 -15.446  -4.395  1.00 61.90           C  
ANISOU 4182  CD  LYS A 545     5241  10326   7951  -1188    665   1343       C  
ATOM   4183  CE  LYS A 545      -4.636 -16.416  -4.751  1.00 60.70           C  
ANISOU 4183  CE  LYS A 545     5408   9765   7890  -1349    545   1420       C  
ATOM   4184  NZ  LYS A 545      -5.061 -17.505  -5.692  1.00 61.73           N  
ANISOU 4184  NZ  LYS A 545     5466   9755   8234  -1631    413   1421       N  
ATOM   4185  N   ASN A 546      -4.547 -11.855  -8.856  1.00 48.96           N  
ANISOU 4185  N   ASN A 546     3993   8270   6340   -183    -20    690       N  
ATOM   4186  CA  ASN A 546      -3.920 -10.698  -9.483  1.00 46.16           C  
ANISOU 4186  CA  ASN A 546     3840   7781   5917     99   -112    599       C  
ATOM   4187  C   ASN A 546      -4.798 -10.291 -10.662  1.00 46.89           C  
ANISOU 4187  C   ASN A 546     3772   7995   6049    218   -274    503       C  
ATOM   4188  O   ASN A 546      -4.875 -11.024 -11.644  1.00 52.11           O  
ANISOU 4188  O   ASN A 546     4426   8591   6782     68   -411    483       O  
ATOM   4189  CB  ASN A 546      -2.497 -11.039  -9.952  1.00 42.98           C  
ANISOU 4189  CB  ASN A 546     3767   7044   5520     36   -177    622       C  
ATOM   4190  CG  ASN A 546      -1.795  -9.866 -10.629  1.00 39.68           C  
ANISOU 4190  CG  ASN A 546     3560   6480   5035    283   -257    553       C  
ATOM   4191  OD1 ASN A 546      -2.432  -8.902 -11.068  1.00 36.90           O  
ANISOU 4191  OD1 ASN A 546     3134   6236   4652    496   -317    486       O  
ATOM   4192  ND2 ASN A 546      -0.470  -9.945 -10.713  1.00 37.46           N  
ANISOU 4192  ND2 ASN A 546     3540   5953   4738    255   -259    580       N  
ATOM   4193  N   PRO A 547      -5.456  -9.120 -10.579  1.00 46.57           N  
ANISOU 4193  N   PRO A 547     3613   8128   5953    505   -272    435       N  
ATOM   4194  CA  PRO A 547      -6.465  -8.731 -11.566  1.00 48.51           C  
ANISOU 4194  CA  PRO A 547     3653   8547   6231    645   -431    358       C  
ATOM   4195  C   PRO A 547      -5.936  -8.133 -12.883  1.00 49.55           C  
ANISOU 4195  C   PRO A 547     4025   8481   6322    806   -624    317       C  
ATOM   4196  O   PRO A 547      -6.729  -7.838 -13.774  1.00 55.47           O  
ANISOU 4196  O   PRO A 547     4630   9370   7078    930   -785    264       O  
ATOM   4197  CB  PRO A 547      -7.270  -7.678 -10.811  1.00 50.66           C  
ANISOU 4197  CB  PRO A 547     3734   9060   6455    930   -334    307       C  
ATOM   4198  CG  PRO A 547      -6.258  -7.001  -9.965  1.00 48.50           C  
ANISOU 4198  CG  PRO A 547     3752   8590   6087   1049   -210    318       C  
ATOM   4199  CD  PRO A 547      -5.288  -8.078  -9.548  1.00 46.71           C  
ANISOU 4199  CD  PRO A 547     3694   8182   5871    737   -135    414       C  
ATOM   4200  N   ASP A 548      -4.627  -7.948 -13.017  1.00 48.73           N  
ANISOU 4200  N   ASP A 548     4269   8079   6167    807   -610    350       N  
ATOM   4201  CA  ASP A 548      -4.070  -7.333 -14.230  1.00 46.43           C  
ANISOU 4201  CA  ASP A 548     4216   7610   5814    949   -759    336       C  
ATOM   4202  C   ASP A 548      -4.277  -8.226 -15.440  1.00 44.10           C  
ANISOU 4202  C   ASP A 548     3885   7331   5540    791   -921    309       C  
ATOM   4203  O   ASP A 548      -4.162  -9.446 -15.320  1.00 41.18           O  
ANISOU 4203  O   ASP A 548     3468   6939   5241    516   -896    312       O  
ATOM   4204  CB  ASP A 548      -2.574  -7.054 -14.079  1.00 43.48           C  
ANISOU 4204  CB  ASP A 548     4187   6939   5395    935   -687    382       C  
ATOM   4205  CG  ASP A 548      -2.277  -6.044 -13.006  1.00 42.24           C  
ANISOU 4205  CG  ASP A 548     4114   6733   5203   1101   -565    384       C  
ATOM   4206  OD1 ASP A 548      -3.205  -5.688 -12.245  1.00 46.64           O  
ANISOU 4206  OD1 ASP A 548     4464   7493   5765   1219   -505    346       O  
ATOM   4207  OD2 ASP A 548      -1.108  -5.618 -12.919  1.00 38.80           O  
ANISOU 4207  OD2 ASP A 548     3942   6065   4735   1108   -529    411       O  
ATOM   4208  N   PRO A 549      -4.569  -7.617 -16.610  1.00 44.92           N  
ANISOU 4208  N   PRO A 549     4036   7461   5571    970  -1096    280       N  
ATOM   4209  CA  PRO A 549      -4.811  -8.329 -17.859  1.00 42.18           C  
ANISOU 4209  CA  PRO A 549     3674   7154   5201    859  -1280    230       C  
ATOM   4210  C   PRO A 549      -3.933  -9.557 -18.032  1.00 37.53           C  
ANISOU 4210  C   PRO A 549     3234   6384   4643    574  -1242    218       C  
ATOM   4211  O   PRO A 549      -4.429 -10.655 -18.255  1.00 41.01           O  
ANISOU 4211  O   PRO A 549     3525   6898   5158    353  -1312    159       O  
ATOM   4212  CB  PRO A 549      -4.470  -7.281 -18.917  1.00 41.90           C  
ANISOU 4212  CB  PRO A 549     3873   7027   5021   1111  -1401    255       C  
ATOM   4213  CG  PRO A 549      -4.840  -5.988 -18.287  1.00 43.31           C  
ANISOU 4213  CG  PRO A 549     4018   7242   5195   1396  -1353    291       C  
ATOM   4214  CD  PRO A 549      -4.739  -6.161 -16.792  1.00 45.15           C  
ANISOU 4214  CD  PRO A 549     4149   7481   5525   1309  -1143    295       C  
ATOM   4215  N   TRP A 550      -2.633  -9.377 -17.902  1.00 34.66           N  
ANISOU 4215  N   TRP A 550     3156   5778   4237    580  -1134    270       N  
ATOM   4216  CA  TRP A 550      -1.708 -10.456 -18.217  1.00 35.36           C  
ANISOU 4216  CA  TRP A 550     3406   5686   4343    371  -1111    249       C  
ATOM   4217  C   TRP A 550      -1.883 -11.670 -17.289  1.00 36.71           C  
ANISOU 4217  C   TRP A 550     3437   5850   4661    113  -1027    253       C  
ATOM   4218  O   TRP A 550      -1.652 -12.794 -17.711  1.00 37.55           O  
ANISOU 4218  O   TRP A 550     3591   5858   4816    -77  -1075    200       O  
ATOM   4219  CB  TRP A 550      -0.270  -9.930 -18.203  1.00 33.11           C  
ANISOU 4219  CB  TRP A 550     3412   5177   3991    446  -1004    309       C  
ATOM   4220  CG  TRP A 550       0.209  -9.522 -16.844  1.00 33.47           C  
ANISOU 4220  CG  TRP A 550     3469   5156   4092    462   -838    381       C  
ATOM   4221  CD1 TRP A 550       0.197  -8.272 -16.305  1.00 33.54           C  
ANISOU 4221  CD1 TRP A 550     3509   5170   4064    650   -786    423       C  
ATOM   4222  CD2 TRP A 550       0.764 -10.383 -15.851  1.00 33.59           C  
ANISOU 4222  CD2 TRP A 550     3482   5083   4197    287   -719    413       C  
ATOM   4223  NE1 TRP A 550       0.714  -8.299 -15.033  1.00 32.47           N  
ANISOU 4223  NE1 TRP A 550     3386   4975   3977    597   -644    460       N  
ATOM   4224  CE2 TRP A 550       1.071  -9.587 -14.733  1.00 33.03           C  
ANISOU 4224  CE2 TRP A 550     3434   4998   4119    378   -602    468       C  
ATOM   4225  CE3 TRP A 550       1.031 -11.755 -15.801  1.00 33.53           C  
ANISOU 4225  CE3 TRP A 550     3473   4993   4272     72   -712    399       C  
ATOM   4226  CZ2 TRP A 550       1.629 -10.113 -13.580  1.00 34.05           C  
ANISOU 4226  CZ2 TRP A 550     3575   5066   4298    262   -485    520       C  
ATOM   4227  CZ3 TRP A 550       1.582 -12.274 -14.658  1.00 34.83           C  
ANISOU 4227  CZ3 TRP A 550     3656   5073   4504    -33   -593    468       C  
ATOM   4228  CH2 TRP A 550       1.879 -11.457 -13.562  1.00 34.30           C  
ANISOU 4228  CH2 TRP A 550     3602   5025   4405     62   -483    532       C  
ATOM   4229  N   ALA A 551      -2.320 -11.427 -16.049  1.00 38.10           N  
ANISOU 4229  N   ALA A 551     3452   6129   4896    114   -905    315       N  
ATOM   4230  CA  ALA A 551      -2.460 -12.464 -15.006  1.00 38.73           C  
ANISOU 4230  CA  ALA A 551     3416   6206   5091   -125   -794    366       C  
ATOM   4231  C   ALA A 551      -3.884 -12.996 -14.797  1.00 43.02           C  
ANISOU 4231  C   ALA A 551     3621   6997   5728   -273   -831    348       C  
ATOM   4232  O   ALA A 551      -4.084 -14.002 -14.123  1.00 42.65           O  
ANISOU 4232  O   ALA A 551     3481   6939   5784   -522   -758    401       O  
ATOM   4233  CB  ALA A 551      -1.966 -11.907 -13.692  1.00 37.72           C  
ANISOU 4233  CB  ALA A 551     3337   6056   4938    -48   -615    455       C  
ATOM   4234  N   LYS A 552      -4.866 -12.319 -15.373  1.00 47.68           N  
ANISOU 4234  N   LYS A 552     4019   7811   6285   -124   -946    284       N  
ATOM   4235  CA  LYS A 552      -6.269 -12.504 -15.004  1.00 53.61           C  
ANISOU 4235  CA  LYS A 552     4384   8866   7118   -204   -954    272       C  
ATOM   4236  C   LYS A 552      -6.737 -13.958 -14.999  1.00 55.47           C  
ANISOU 4236  C   LYS A 552     4471   9107   7498   -579   -987    267       C  
ATOM   4237  O   LYS A 552      -7.488 -14.364 -14.116  1.00 56.19           O  
ANISOU 4237  O   LYS A 552     4299   9372   7677   -746   -874    330       O  
ATOM   4238  CB  LYS A 552      -7.161 -11.680 -15.947  1.00 58.65           C  
ANISOU 4238  CB  LYS A 552     4858   9722   7703     23  -1140    185       C  
ATOM   4239  CG  LYS A 552      -8.476 -11.215 -15.338  1.00 64.66           C  
ANISOU 4239  CG  LYS A 552     5217  10840   8511    118  -1099    180       C  
ATOM   4240  CD  LYS A 552      -8.896  -9.863 -15.907  1.00 67.64           C  
ANISOU 4240  CD  LYS A 552     5564  11344   8791    511  -1218    134       C  
ATOM   4241  CE  LYS A 552     -10.256  -9.419 -15.384  1.00 71.24           C  
ANISOU 4241  CE  LYS A 552     5585  12182   9302    644  -1191    107       C  
ATOM   4242  NZ  LYS A 552     -10.525  -7.984 -15.691  1.00 71.29           N  
ANISOU 4242  NZ  LYS A 552     5614  12254   9218   1087  -1271     77       N  
ATOM   4243  N   ASN A 553      -6.287 -14.735 -15.978  1.00 56.40           N  
ANISOU 4243  N   ASN A 553     4767   9027   7635   -716  -1134    191       N  
ATOM   4244  CA  ASN A 553      -6.875 -16.043 -16.247  1.00 60.32           C  
ANISOU 4244  CA  ASN A 553     5127   9515   8277  -1061  -1231    142       C  
ATOM   4245  C   ASN A 553      -5.892 -17.201 -16.169  1.00 58.92           C  
ANISOU 4245  C   ASN A 553     5233   8984   8171  -1280  -1195    163       C  
ATOM   4246  O   ASN A 553      -6.206 -18.320 -16.589  1.00 62.26           O  
ANISOU 4246  O   ASN A 553     5630   9313   8714  -1557  -1308     94       O  
ATOM   4247  CB  ASN A 553      -7.535 -16.015 -17.626  1.00 63.48           C  
ANISOU 4247  CB  ASN A 553     5434  10042   8645  -1032  -1499    -20       C  
ATOM   4248  CG  ASN A 553      -8.697 -15.050 -17.688  1.00 67.70           C  
ANISOU 4248  CG  ASN A 553     5627  10950   9146   -837  -1564    -38       C  
ATOM   4249  OD1 ASN A 553      -8.635 -14.029 -18.369  1.00 67.69           O  
ANISOU 4249  OD1 ASN A 553     5701  11016   9003   -527  -1665    -77       O  
ATOM   4250  ND2 ASN A 553      -9.764 -15.361 -16.957  1.00 72.94           N  
ANISOU 4250  ND2 ASN A 553     5910  11864   9941  -1012  -1500      0       N  
ATOM   4251  N   LEU A 554      -4.712 -16.941 -15.624  1.00 53.24           N  
ANISOU 4251  N   LEU A 554     4778   8064   7388  -1155  -1050    250       N  
ATOM   4252  CA  LEU A 554      -3.710 -17.977 -15.487  1.00 55.40           C  
ANISOU 4252  CA  LEU A 554     5315   8007   7729  -1308  -1014    278       C  
ATOM   4253  C   LEU A 554      -4.116 -18.847 -14.299  1.00 60.81           C  
ANISOU 4253  C   LEU A 554     5875   8675   8553  -1585   -886    424       C  
ATOM   4254  O   LEU A 554      -4.718 -18.358 -13.336  1.00 62.11           O  
ANISOU 4254  O   LEU A 554     5828   9070   8701  -1571   -749    534       O  
ATOM   4255  CB  LEU A 554      -2.327 -17.370 -15.263  1.00 54.37           C  
ANISOU 4255  CB  LEU A 554     5464   7706   7488  -1079   -909    328       C  
ATOM   4256  CG  LEU A 554      -1.887 -16.251 -16.221  1.00 53.07           C  
ANISOU 4256  CG  LEU A 554     5418   7582   7163   -792   -979    242       C  
ATOM   4257  CD1 LEU A 554      -0.638 -15.567 -15.674  1.00 50.25           C  
ANISOU 4257  CD1 LEU A 554     5269   7098   6727   -614   -841    326       C  
ATOM   4258  CD2 LEU A 554      -1.653 -16.773 -17.643  1.00 50.53           C  
ANISOU 4258  CD2 LEU A 554     5240   7150   6807   -813  -1150     85       C  
ATOM   4259  N   ASN A 555      -3.794 -20.134 -14.385  1.00 62.91           N  
ANISOU 4259  N   ASN A 555     6286   8666   8949  -1828   -928    425       N  
ATOM   4260  CA  ASN A 555      -4.188 -21.107 -13.382  1.00 65.64           C  
ANISOU 4260  CA  ASN A 555     6552   8949   9439  -2133   -828    583       C  
ATOM   4261  C   ASN A 555      -2.953 -21.728 -12.736  1.00 62.57           C  
ANISOU 4261  C   ASN A 555     6474   8228   9070  -2134   -735    704       C  
ATOM   4262  O   ASN A 555      -1.975 -22.021 -13.419  1.00 59.45           O  
ANISOU 4262  O   ASN A 555     6345   7573   8670  -2030   -818    605       O  
ATOM   4263  CB  ASN A 555      -5.038 -22.194 -14.038  1.00 72.81           C  
ANISOU 4263  CB  ASN A 555     7350   9793  10520  -2464   -989    486       C  
ATOM   4264  CG  ASN A 555      -6.338 -22.448 -13.297  1.00 80.44           C  
ANISOU 4264  CG  ASN A 555     7955  11014  11595  -2744   -911    604       C  
ATOM   4265  OD1 ASN A 555      -6.552 -23.533 -12.752  1.00 85.22           O  
ANISOU 4265  OD1 ASN A 555     8568  11455  12356  -3074   -866    725       O  
ATOM   4266  ND2 ASN A 555      -7.216 -21.447 -13.277  1.00 81.52           N  
ANISOU 4266  ND2 ASN A 555     7770  11553  11652  -2609   -889    576       N  
ATOM   4267  N   GLU A 556      -2.995 -21.914 -11.419  1.00 61.01           N  
ANISOU 4267  N   GLU A 556     6238   8061   8882  -2233   -562    921       N  
ATOM   4268  CA  GLU A 556      -1.936 -22.625 -10.708  1.00 59.65           C  
ANISOU 4268  CA  GLU A 556     6342   7584   8738  -2256   -493   1066       C  
ATOM   4269  C   GLU A 556      -1.580 -23.914 -11.431  1.00 60.13           C  
ANISOU 4269  C   GLU A 556     6615   7264   8968  -2425   -639    988       C  
ATOM   4270  O   GLU A 556      -0.411 -24.206 -11.653  1.00 59.61           O  
ANISOU 4270  O   GLU A 556     6823   6925   8899  -2278   -674    954       O  
ATOM   4271  CB  GLU A 556      -2.382 -22.993  -9.294  1.00 64.48           C  
ANISOU 4271  CB  GLU A 556     6857   8282   9360  -2451   -319   1324       C  
ATOM   4272  CG  GLU A 556      -2.286 -21.888  -8.265  1.00 64.07           C  
ANISOU 4272  CG  GLU A 556     6718   8512   9113  -2244   -146   1427       C  
ATOM   4273  CD  GLU A 556      -2.418 -22.418  -6.846  1.00 68.40           C  
ANISOU 4273  CD  GLU A 556     7266   9089   9633  -2418     27   1697       C  
ATOM   4274  OE1 GLU A 556      -1.868 -23.506  -6.553  1.00 69.43           O  
ANISOU 4274  OE1 GLU A 556     7618   8903   9858  -2570      6   1834       O  
ATOM   4275  OE2 GLU A 556      -3.067 -21.745  -6.020  1.00 72.36           O  
ANISOU 4275  OE2 GLU A 556     7558   9928  10007  -2389    185   1776       O  
ATOM   4276  N   LYS A 557      -2.609 -24.684 -11.779  1.00 64.34           N  
ANISOU 4276  N   LYS A 557     7007   7785   9655  -2736   -724    950       N  
ATOM   4277  CA  LYS A 557      -2.461 -25.927 -12.535  1.00 66.74           C  
ANISOU 4277  CA  LYS A 557     7502   7719  10135  -2927   -887    835       C  
ATOM   4278  C   LYS A 557      -1.448 -25.827 -13.667  1.00 64.08           C  
ANISOU 4278  C   LYS A 557     7414   7196   9737  -2663  -1014    604       C  
ATOM   4279  O   LYS A 557      -0.730 -26.785 -13.926  1.00 64.87           O  
ANISOU 4279  O   LYS A 557     7785   6921   9941  -2689  -1083    557       O  
ATOM   4280  CB  LYS A 557      -3.808 -26.351 -13.136  1.00 73.07           C  
ANISOU 4280  CB  LYS A 557     8057   8637  11069  -3241  -1015    724       C  
ATOM   4281  CG  LYS A 557      -4.705 -27.155 -12.203  1.00 79.52           C  
ANISOU 4281  CG  LYS A 557     8714   9451  12050  -3647   -926    943       C  
ATOM   4282  CD  LYS A 557      -5.826 -27.868 -12.978  1.00 83.12           C  
ANISOU 4282  CD  LYS A 557     8987   9902  12691  -4006  -1105    793       C  
ATOM   4283  CE  LYS A 557      -6.576 -28.873 -12.106  1.00 86.12           C  
ANISOU 4283  CE  LYS A 557     9264  10186  13272  -4468  -1020   1025       C  
ATOM   4284  NZ  LYS A 557      -7.578 -29.670 -12.881  1.00 89.95           N  
ANISOU 4284  NZ  LYS A 557     9595  10611  13970  -4859  -1218    866       N  
ATOM   4285  N   ASP A 558      -1.399 -24.671 -14.333  1.00 62.17           N  
ANISOU 4285  N   ASP A 558     7083   7214   9323  -2404  -1038    468       N  
ATOM   4286  CA  ASP A 558      -0.589 -24.489 -15.545  1.00 61.42           C  
ANISOU 4286  CA  ASP A 558     7186   7012   9139  -2173  -1149    244       C  
ATOM   4287  C   ASP A 558       0.922 -24.474 -15.306  1.00 56.47           C  
ANISOU 4287  C   ASP A 558     6827   6172   8459  -1930  -1064    288       C  
ATOM   4288  O   ASP A 558       1.694 -24.465 -16.265  1.00 57.28           O  
ANISOU 4288  O   ASP A 558     7101   6168   8496  -1751  -1129    112       O  
ATOM   4289  CB  ASP A 558      -0.979 -23.184 -16.270  1.00 61.90           C  
ANISOU 4289  CB  ASP A 558     7083   7419   9016  -1967  -1189    132       C  
ATOM   4290  CG  ASP A 558      -2.415 -23.200 -16.814  1.00 65.36           C  
ANISOU 4290  CG  ASP A 558     7252   8086   9496  -2158  -1329     30       C  
ATOM   4291  OD1 ASP A 558      -2.876 -24.261 -17.290  1.00 63.55           O  
ANISOU 4291  OD1 ASP A 558     7041   7696   9408  -2413  -1470    -83       O  
ATOM   4292  OD2 ASP A 558      -3.074 -22.134 -16.781  1.00 65.60           O  
ANISOU 4292  OD2 ASP A 558     7048   8454   9422  -2042  -1310     51       O  
ATOM   4293  N   TYR A 559       1.352 -24.466 -14.048  1.00 52.95           N  
ANISOU 4293  N   TYR A 559     6404   5687   8028  -1919   -919    517       N  
ATOM   4294  CA  TYR A 559       2.773 -24.282 -13.744  1.00 50.41           C  
ANISOU 4294  CA  TYR A 559     6280   5230   7643  -1670   -846    566       C  
ATOM   4295  C   TYR A 559       3.353 -25.389 -12.851  1.00 48.88           C  
ANISOU 4295  C   TYR A 559     6263   4722   7585  -1757   -814    733       C  
ATOM   4296  O   TYR A 559       2.621 -26.071 -12.134  1.00 48.14           O  
ANISOU 4296  O   TYR A 559     6122   4566   7604  -2017   -796    888       O  
ATOM   4297  CB  TYR A 559       2.991 -22.876 -13.170  1.00 48.36           C  
ANISOU 4297  CB  TYR A 559     5901   5264   7210  -1471   -724    657       C  
ATOM   4298  CG  TYR A 559       2.400 -21.815 -14.076  1.00 46.36           C  
ANISOU 4298  CG  TYR A 559     5501   5278   6834  -1371   -770    509       C  
ATOM   4299  CD1 TYR A 559       3.091 -21.367 -15.189  1.00 46.91           C  
ANISOU 4299  CD1 TYR A 559     5684   5334   6806  -1171   -824    344       C  
ATOM   4300  CD2 TYR A 559       1.132 -21.312 -13.852  1.00 48.70           C  
ANISOU 4300  CD2 TYR A 559     5548   5845   7111  -1473   -763    541       C  
ATOM   4301  CE1 TYR A 559       2.548 -20.419 -16.041  1.00 47.17           C  
ANISOU 4301  CE1 TYR A 559     5614   5596   6714  -1075   -880    236       C  
ATOM   4302  CE2 TYR A 559       0.577 -20.368 -14.694  1.00 50.82           C  
ANISOU 4302  CE2 TYR A 559     5692   6346   7273  -1356   -829    416       C  
ATOM   4303  CZ  TYR A 559       1.290 -19.924 -15.792  1.00 49.17           C  
ANISOU 4303  CZ  TYR A 559     5628   6096   6957  -1158   -895    272       C  
ATOM   4304  OH  TYR A 559       0.740 -18.985 -16.640  1.00 47.47           O  
ANISOU 4304  OH  TYR A 559     5316   6100   6619  -1033   -971    175       O  
ATOM   4305  N   GLU A 560       4.669 -25.583 -12.959  1.00 47.90           N  
ANISOU 4305  N   GLU A 560     6340   4404   7455  -1538   -813    703       N  
ATOM   4306  CA  GLU A 560       5.397 -26.647 -12.252  1.00 49.13           C  
ANISOU 4306  CA  GLU A 560     6698   4231   7740  -1548   -814    842       C  
ATOM   4307  C   GLU A 560       6.726 -26.111 -11.708  1.00 44.50           C  
ANISOU 4307  C   GLU A 560     6175   3678   7055  -1263   -740    923       C  
ATOM   4308  O   GLU A 560       7.187 -25.032 -12.087  1.00 42.40           O  
ANISOU 4308  O   GLU A 560     5831   3633   6648  -1070   -698    831       O  
ATOM   4309  CB  GLU A 560       5.671 -27.848 -13.176  1.00 50.94           C  
ANISOU 4309  CB  GLU A 560     7139   4089   8126  -1574   -945    658       C  
ATOM   4310  CG  GLU A 560       4.432 -28.634 -13.599  1.00 54.84           C  
ANISOU 4310  CG  GLU A 560     7606   4469   8761  -1904  -1050    586       C  
ATOM   4311  CD  GLU A 560       4.762 -29.975 -14.273  1.00 59.46           C  
ANISOU 4311  CD  GLU A 560     8457   4608   9529  -1944  -1186    424       C  
ATOM   4312  OE1 GLU A 560       5.624 -30.002 -15.178  1.00 60.27           O  
ANISOU 4312  OE1 GLU A 560     8693   4620   9586  -1693  -1230    198       O  
ATOM   4313  OE2 GLU A 560       4.148 -31.004 -13.906  1.00 61.25           O  
ANISOU 4313  OE2 GLU A 560     8761   4568   9945  -2231  -1245    517       O  
ATOM   4314  N   LEU A 561       7.333 -26.882 -10.819  1.00 41.64           N  
ANISOU 4314  N   LEU A 561     5956   3090   6775  -1249   -736   1104       N  
ATOM   4315  CA  LEU A 561       8.578 -26.499 -10.184  1.00 41.11           C  
ANISOU 4315  CA  LEU A 561     5934   3054   6632   -999   -693   1196       C  
ATOM   4316  C   LEU A 561       9.654 -27.476 -10.614  1.00 44.37           C  
ANISOU 4316  C   LEU A 561     6553   3129   7176   -827   -774   1113       C  
ATOM   4317  O   LEU A 561       9.399 -28.668 -10.732  1.00 49.40           O  
ANISOU 4317  O   LEU A 561     7350   3441   7981   -945   -852   1121       O  
ATOM   4318  CB  LEU A 561       8.428 -26.532  -8.655  1.00 41.92           C  
ANISOU 4318  CB  LEU A 561     6024   3217   6686  -1086   -630   1498       C  
ATOM   4319  CG  LEU A 561       7.372 -25.589  -8.056  1.00 39.29           C  
ANISOU 4319  CG  LEU A 561     5482   3234   6210  -1232   -527   1588       C  
ATOM   4320  CD1 LEU A 561       7.149 -25.861  -6.577  1.00 36.27           C  
ANISOU 4320  CD1 LEU A 561     5121   2888   5772  -1344   -458   1887       C  
ATOM   4321  CD2 LEU A 561       7.757 -24.136  -8.289  1.00 33.87           C  
ANISOU 4321  CD2 LEU A 561     4663   2850   5357  -1032   -476   1466       C  
ATOM   4322  N   LEU A 562      10.856 -26.976 -10.858  1.00 42.53           N  
ANISOU 4322  N   LEU A 562     6311   2969   6878   -548   -755   1028       N  
ATOM   4323  CA  LEU A 562      11.978 -27.858 -11.108  1.00 45.84           C  
ANISOU 4323  CA  LEU A 562     6894   3107   7417   -336   -817    966       C  
ATOM   4324  C   LEU A 562      12.627 -28.158  -9.763  1.00 44.53           C  
ANISOU 4324  C   LEU A 562     6782   2870   7268   -256   -830   1233       C  
ATOM   4325  O   LEU A 562      12.890 -27.236  -8.984  1.00 38.57           O  
ANISOU 4325  O   LEU A 562     5898   2385   6371   -211   -773   1355       O  
ATOM   4326  CB  LEU A 562      12.976 -27.205 -12.070  1.00 46.94           C  
ANISOU 4326  CB  LEU A 562     6966   3391   7478    -78   -779    744       C  
ATOM   4327  CG  LEU A 562      12.432 -26.657 -13.399  1.00 45.70           C  
ANISOU 4327  CG  LEU A 562     6747   3382   7234   -123   -756    499       C  
ATOM   4328  CD1 LEU A 562      13.576 -26.345 -14.351  1.00 45.42           C  
ANISOU 4328  CD1 LEU A 562     6698   3419   7140    143   -710    300       C  
ATOM   4329  CD2 LEU A 562      11.458 -27.619 -14.062  1.00 48.66           C  
ANISOU 4329  CD2 LEU A 562     7246   3524   7718   -310   -848    376       C  
ATOM   4330  N   CYS A 563      12.841 -29.441  -9.477  1.00 48.69           N  
ANISOU 4330  N   CYS A 563     7514   3026   7962   -244   -917   1323       N  
ATOM   4331  CA  CYS A 563      13.530 -29.866  -8.251  1.00 53.30           C  
ANISOU 4331  CA  CYS A 563     8184   3506   8562   -134   -958   1588       C  
ATOM   4332  C   CYS A 563      14.978 -30.124  -8.580  1.00 53.78           C  
ANISOU 4332  C   CYS A 563     8281   3466   8687    225  -1013   1475       C  
ATOM   4333  O   CYS A 563      15.331 -30.290  -9.742  1.00 57.09           O  
ANISOU 4333  O   CYS A 563     8714   3807   9171    356  -1015   1206       O  
ATOM   4334  CB  CYS A 563      12.936 -31.153  -7.667  1.00 58.31           C  
ANISOU 4334  CB  CYS A 563     9043   3764   9348   -322  -1029   1798       C  
ATOM   4335  SG  CYS A 563      11.149 -31.293  -7.718  1.00 61.94           S  
ANISOU 4335  SG  CYS A 563     9473   4231   9829   -780   -979   1853       S  
ATOM   4336  N   LEU A 564      15.807 -30.194  -7.548  1.00 55.66           N  
ANISOU 4336  N   LEU A 564     8530   3719   8898    389  -1059   1680       N  
ATOM   4337  CA  LEU A 564      17.236 -30.431  -7.730  1.00 57.73           C  
ANISOU 4337  CA  LEU A 564     8783   3924   9228    750  -1119   1595       C  
ATOM   4338  C   LEU A 564      17.512 -31.818  -8.300  1.00 60.60           C  
ANISOU 4338  C   LEU A 564     9379   3829   9816    891  -1213   1502       C  
ATOM   4339  O   LEU A 564      18.411 -31.985  -9.129  1.00 59.50           O  
ANISOU 4339  O   LEU A 564     9211   3649   9749   1166  -1219   1272       O  
ATOM   4340  CB  LEU A 564      17.966 -30.237  -6.406  1.00 57.90           C  
ANISOU 4340  CB  LEU A 564     8762   4071   9166    879  -1180   1854       C  
ATOM   4341  CG  LEU A 564      17.899 -28.775  -5.954  1.00 55.12           C  
ANISOU 4341  CG  LEU A 564     8177   4174   8591    792  -1096   1875       C  
ATOM   4342  CD1 LEU A 564      17.803 -28.666  -4.433  1.00 56.16           C  
ANISOU 4342  CD1 LEU A 564     8341   4409   8587    728  -1143   2187       C  
ATOM   4343  CD2 LEU A 564      19.087 -27.992  -6.510  1.00 53.18           C  
ANISOU 4343  CD2 LEU A 564     7720   4166   8321   1033  -1073   1675       C  
ATOM   4344  N   ASP A 565      16.714 -32.798  -7.882  1.00 65.32           N  
ANISOU 4344  N   ASP A 565    10208   4084  10526    693  -1278   1672       N  
ATOM   4345  CA  ASP A 565      16.870 -34.181  -8.353  1.00 70.72           C  
ANISOU 4345  CA  ASP A 565    11163   4261  11445    796  -1386   1595       C  
ATOM   4346  C   ASP A 565      16.599 -34.374  -9.852  1.00 68.93           C  
ANISOU 4346  C   ASP A 565    10968   3927  11295    788  -1361   1215       C  
ATOM   4347  O   ASP A 565      16.743 -35.482 -10.365  1.00 70.78           O  
ANISOU 4347  O   ASP A 565    11435   3736  11721    889  -1451   1087       O  
ATOM   4348  CB  ASP A 565      15.986 -35.133  -7.535  1.00 76.45           C  
ANISOU 4348  CB  ASP A 565    12139   4634  12275    521  -1455   1890       C  
ATOM   4349  CG  ASP A 565      14.498 -34.818  -7.649  1.00 79.34           C  
ANISOU 4349  CG  ASP A 565    12452   5110  12586     74  -1372   1911       C  
ATOM   4350  OD1 ASP A 565      14.088 -34.104  -8.590  1.00 78.48           O  
ANISOU 4350  OD1 ASP A 565    12174   5240  12404     -5  -1297   1645       O  
ATOM   4351  OD2 ASP A 565      13.732 -35.300  -6.785  1.00 85.31           O  
ANISOU 4351  OD2 ASP A 565    13328   5718  13367   -198  -1382   2206       O  
ATOM   4352  N   GLY A 566      16.189 -33.309 -10.543  1.00 65.38           N  
ANISOU 4352  N   GLY A 566    10306   3848  10689    673  -1250   1034       N  
ATOM   4353  CA  GLY A 566      15.964 -33.359 -11.989  1.00 66.64           C  
ANISOU 4353  CA  GLY A 566    10479   3977  10862    679  -1226    673       C  
ATOM   4354  C   GLY A 566      14.514 -33.615 -12.375  1.00 67.79           C  
ANISOU 4354  C   GLY A 566    10705   4010  11041    296  -1251    626       C  
ATOM   4355  O   GLY A 566      14.120 -33.388 -13.524  1.00 66.01           O  
ANISOU 4355  O   GLY A 566    10447   3869  10763    244  -1232    343       O  
ATOM   4356  N   THR A 567      13.715 -34.093 -11.422  1.00 69.09           N  
ANISOU 4356  N   THR A 567    10966   4002  11282     20  -1294    906       N  
ATOM   4357  CA  THR A 567      12.282 -34.287 -11.642  1.00 67.40           C  
ANISOU 4357  CA  THR A 567    10772   3730  11108   -387  -1311    900       C  
ATOM   4358  C   THR A 567      11.557 -32.963 -11.389  1.00 63.45           C  
ANISOU 4358  C   THR A 567     9982   3730  10396   -570  -1194    978       C  
ATOM   4359  O   THR A 567      12.186 -31.968 -11.016  1.00 56.44           O  
ANISOU 4359  O   THR A 567     8922   3178   9345   -392  -1110   1039       O  
ATOM   4360  CB  THR A 567      11.713 -35.410 -10.744  1.00 67.87           C  
ANISOU 4360  CB  THR A 567    11053   3384  11351   -632  -1390   1182       C  
ATOM   4361  OG1 THR A 567      11.670 -34.976  -9.379  1.00 65.28           O  
ANISOU 4361  OG1 THR A 567    10634   3257  10913   -700  -1321   1554       O  
ATOM   4362  CG2 THR A 567      12.572 -36.662 -10.856  1.00 71.15           C  
ANISOU 4362  CG2 THR A 567    11776   3279  11979   -387  -1514   1137       C  
ATOM   4363  N   ARG A 568      10.242 -32.949 -11.603  1.00 65.92           N  
ANISOU 4363  N   ARG A 568    10236   4089  10721   -920  -1197    963       N  
ATOM   4364  CA  ARG A 568       9.458 -31.714 -11.492  1.00 65.03           C  
ANISOU 4364  CA  ARG A 568     9846   4442  10420  -1071  -1096    998       C  
ATOM   4365  C   ARG A 568       8.047 -31.955 -10.946  1.00 64.69           C  
ANISOU 4365  C   ARG A 568     9739   4411  10430  -1482  -1086   1176       C  
ATOM   4366  O   ARG A 568       7.353 -32.867 -11.391  1.00 66.33           O  
ANISOU 4366  O   ARG A 568    10059   4337  10806  -1717  -1178   1099       O  
ATOM   4367  CB  ARG A 568       9.405 -30.987 -12.849  1.00 65.95           C  
ANISOU 4367  CB  ARG A 568     9847   4784  10427   -976  -1092    664       C  
ATOM   4368  CG  ARG A 568       9.227 -31.897 -14.071  1.00 70.78           C  
ANISOU 4368  CG  ARG A 568    10631   5096  11164  -1007  -1214    365       C  
ATOM   4369  CD  ARG A 568       9.450 -31.148 -15.392  1.00 69.46           C  
ANISOU 4369  CD  ARG A 568    10380   5178  10835   -836  -1199     50       C  
ATOM   4370  NE  ARG A 568       8.390 -30.180 -15.671  1.00 68.81           N  
ANISOU 4370  NE  ARG A 568    10075   5460  10612  -1024  -1174     31       N  
ATOM   4371  CZ  ARG A 568       8.297 -29.453 -16.784  1.00 68.88           C  
ANISOU 4371  CZ  ARG A 568    10000   5713  10458   -937  -1175   -198       C  
ATOM   4372  NH1 ARG A 568       9.199 -29.574 -17.755  1.00 71.24           N  
ANISOU 4372  NH1 ARG A 568    10416   5956  10696   -681  -1178   -437       N  
ATOM   4373  NH2 ARG A 568       7.287 -28.600 -16.934  1.00 66.44           N  
ANISOU 4373  NH2 ARG A 568     9490   5718  10036  -1095  -1169   -184       N  
ATOM   4374  N   LYS A 569       7.638 -31.120  -9.988  1.00 63.39           N  
ANISOU 4374  N   LYS A 569     9384   4584  10117  -1567   -971   1401       N  
ATOM   4375  CA  LYS A 569       6.383 -31.306  -9.247  1.00 67.05           C  
ANISOU 4375  CA  LYS A 569     9754   5115  10607  -1936   -919   1621       C  
ATOM   4376  C   LYS A 569       5.501 -30.056  -9.311  1.00 66.59           C  
ANISOU 4376  C   LYS A 569     9382   5543  10376  -2022   -821   1574       C  
ATOM   4377  O   LYS A 569       5.971 -28.988  -9.698  1.00 64.91           O  
ANISOU 4377  O   LYS A 569     9057   5598  10009  -1783   -786   1432       O  
ATOM   4378  CB  LYS A 569       6.682 -31.657  -7.782  1.00 67.76           C  
ANISOU 4378  CB  LYS A 569     9943   5131  10673  -1958   -859   1993       C  
ATOM   4379  CG  LYS A 569       7.713 -32.768  -7.615  1.00 70.42           C  
ANISOU 4379  CG  LYS A 569    10591   5004  11160  -1790   -965   2067       C  
ATOM   4380  CD  LYS A 569       7.433 -33.644  -6.398  1.00 75.40           C  
ANISOU 4380  CD  LYS A 569    11385   5408  11856  -1996   -951   2452       C  
ATOM   4381  CE  LYS A 569       8.503 -34.719  -6.223  1.00 78.06           C  
ANISOU 4381  CE  LYS A 569    12046   5268  12344  -1780  -1076   2536       C  
ATOM   4382  NZ  LYS A 569       8.646 -35.579  -7.433  1.00 79.35           N  
ANISOU 4382  NZ  LYS A 569    12390   5020  12741  -1747  -1212   2243       N  
ATOM   4383  N   PRO A 570       4.212 -30.182  -8.934  1.00 70.22           N  
ANISOU 4383  N   PRO A 570     9695   6117  10870  -2364   -774   1697       N  
ATOM   4384  CA  PRO A 570       3.324 -29.013  -8.923  1.00 67.57           C  
ANISOU 4384  CA  PRO A 570     9046   6250  10380  -2419   -680   1659       C  
ATOM   4385  C   PRO A 570       3.747 -27.952  -7.917  1.00 64.26           C  
ANISOU 4385  C   PRO A 570     8530   6147   9740  -2223   -541   1815       C  
ATOM   4386  O   PRO A 570       4.644 -28.188  -7.109  1.00 62.17           O  
ANISOU 4386  O   PRO A 570     8426   5759   9437  -2089   -520   1987       O  
ATOM   4387  CB  PRO A 570       1.968 -29.600  -8.524  1.00 70.23           C  
ANISOU 4387  CB  PRO A 570     9253   6605  10826  -2835   -646   1807       C  
ATOM   4388  CG  PRO A 570       2.050 -31.025  -8.886  1.00 74.18           C  
ANISOU 4388  CG  PRO A 570    10003   6614  11569  -3017   -776   1796       C  
ATOM   4389  CD  PRO A 570       3.469 -31.422  -8.654  1.00 73.66           C  
ANISOU 4389  CD  PRO A 570    10233   6246  11510  -2724   -815   1844       C  
ATOM   4390  N   VAL A 571       3.078 -26.803  -7.963  1.00 62.29           N  
ANISOU 4390  N   VAL A 571     8022   6298   9346  -2202   -463   1748       N  
ATOM   4391  CA  VAL A 571       3.486 -25.639  -7.180  1.00 58.69           C  
ANISOU 4391  CA  VAL A 571     7482   6143   8674  -1988   -350   1822       C  
ATOM   4392  C   VAL A 571       3.368 -25.854  -5.671  1.00 58.14           C  
ANISOU 4392  C   VAL A 571     7429   6144   8517  -2087   -228   2132       C  
ATOM   4393  O   VAL A 571       4.284 -25.521  -4.928  1.00 56.78           O  
ANISOU 4393  O   VAL A 571     7357   5998   8218  -1891   -199   2229       O  
ATOM   4394  CB  VAL A 571       2.702 -24.383  -7.596  1.00 58.11           C  
ANISOU 4394  CB  VAL A 571     7146   6451   8482  -1935   -303   1673       C  
ATOM   4395  CG1 VAL A 571       2.976 -23.222  -6.636  1.00 58.78           C  
ANISOU 4395  CG1 VAL A 571     7155   6827   8354  -1750   -180   1756       C  
ATOM   4396  CG2 VAL A 571       3.078 -23.990  -9.007  1.00 57.06           C  
ANISOU 4396  CG2 VAL A 571     7038   6274   8369  -1769   -418   1395       C  
ATOM   4397  N   GLU A 572       2.258 -26.424  -5.221  1.00 61.05           N  
ANISOU 4397  N   GLU A 572     7697   6555   8946  -2401   -158   2289       N  
ATOM   4398  CA  GLU A 572       2.069 -26.689  -3.793  1.00 64.52           C  
ANISOU 4398  CA  GLU A 572     8159   7078   9277  -2522    -21   2607       C  
ATOM   4399  C   GLU A 572       3.111 -27.646  -3.194  1.00 66.79           C  
ANISOU 4399  C   GLU A 572     8764   7008   9606  -2471    -83   2812       C  
ATOM   4400  O   GLU A 572       3.300 -27.663  -1.974  1.00 68.11           O  
ANISOU 4400  O   GLU A 572     8995   7269   9617  -2465     10   3069       O  
ATOM   4401  CB  GLU A 572       0.656 -27.214  -3.519  1.00 67.72           C  
ANISOU 4401  CB  GLU A 572     8382   7588   9760  -2908     77   2746       C  
ATOM   4402  CG  GLU A 572       0.330 -28.566  -4.148  1.00 69.95           C  
ANISOU 4402  CG  GLU A 572     8783   7472  10323  -3203    -40   2759       C  
ATOM   4403  CD  GLU A 572      -1.168 -28.824  -4.239  1.00 73.66           C  
ANISOU 4403  CD  GLU A 572     8978   8115  10895  -3588     30   2794       C  
ATOM   4404  OE1 GLU A 572      -1.573 -29.808  -4.896  1.00 74.39           O  
ANISOU 4404  OE1 GLU A 572     9125   7911  11228  -3858    -85   2747       O  
ATOM   4405  OE2 GLU A 572      -1.947 -28.039  -3.658  1.00 75.38           O  
ANISOU 4405  OE2 GLU A 572     8914   8772  10956  -3620    197   2853       O  
ATOM   4406  N   GLU A 573       3.795 -28.415  -4.042  1.00 66.65           N  
ANISOU 4406  N   GLU A 573     8946   6597   9782  -2408   -243   2693       N  
ATOM   4407  CA  GLU A 573       4.809 -29.375  -3.586  1.00 68.98           C  
ANISOU 4407  CA  GLU A 573     9545   6518  10148  -2318   -327   2866       C  
ATOM   4408  C   GLU A 573       6.204 -28.756  -3.373  1.00 63.38           C  
ANISOU 4408  C   GLU A 573     8917   5859   9304  -1928   -374   2813       C  
ATOM   4409  O   GLU A 573       7.216 -29.444  -3.510  1.00 67.95           O  
ANISOU 4409  O   GLU A 573     9713   6117   9988  -1761   -492   2822       O  
ATOM   4410  CB  GLU A 573       4.908 -30.546  -4.580  1.00 73.42           C  
ANISOU 4410  CB  GLU A 573    10294   6612  10992  -2409   -479   2744       C  
ATOM   4411  CG  GLU A 573       3.674 -31.443  -4.634  1.00 79.11           C  
ANISOU 4411  CG  GLU A 573    10993   7177  11886  -2839   -465   2847       C  
ATOM   4412  CD  GLU A 573       3.667 -32.524  -3.562  1.00 86.30           C  
ANISOU 4412  CD  GLU A 573    12126   7806  12856  -3032   -440   3228       C  
ATOM   4413  OE1 GLU A 573       4.678 -33.252  -3.425  1.00 89.37           O  
ANISOU 4413  OE1 GLU A 573    12810   7819  13326  -2854   -550   3308       O  
ATOM   4414  OE2 GLU A 573       2.636 -32.660  -2.867  1.00 89.94           O  
ANISOU 4414  OE2 GLU A 573    12465   8423  13284  -3361   -307   3457       O  
ATOM   4415  N   TYR A 574       6.265 -27.477  -3.016  1.00 56.05           N  
ANISOU 4415  N   TYR A 574     7814   5326   8156  -1783   -288   2755       N  
ATOM   4416  CA  TYR A 574       7.558 -26.774  -2.884  1.00 51.90           C  
ANISOU 4416  CA  TYR A 574     7329   4877   7515  -1447   -340   2674       C  
ATOM   4417  C   TYR A 574       8.461 -27.324  -1.765  1.00 52.76           C  
ANISOU 4417  C   TYR A 574     7633   4860   7554  -1334   -387   2934       C  
ATOM   4418  O   TYR A 574       9.689 -27.289  -1.874  1.00 50.91           O  
ANISOU 4418  O   TYR A 574     7482   4528   7332  -1070   -492   2871       O  
ATOM   4419  CB  TYR A 574       7.342 -25.264  -2.685  1.00 45.15           C  
ANISOU 4419  CB  TYR A 574     6261   4447   6446  -1348   -244   2558       C  
ATOM   4420  CG  TYR A 574       6.387 -24.944  -1.565  1.00 42.95           C  
ANISOU 4420  CG  TYR A 574     5877   4455   5987  -1510    -94   2749       C  
ATOM   4421  CD1 TYR A 574       5.051 -24.671  -1.828  1.00 41.57           C  
ANISOU 4421  CD1 TYR A 574     5499   4474   5820  -1712     11   2699       C  
ATOM   4422  CD2 TYR A 574       6.814 -24.941  -0.238  1.00 43.15           C  
ANISOU 4422  CD2 TYR A 574     5997   4579   5820  -1453    -59   2979       C  
ATOM   4423  CE1 TYR A 574       4.166 -24.394  -0.803  1.00 45.09           C  
ANISOU 4423  CE1 TYR A 574     5824   5212   6095  -1849    172   2867       C  
ATOM   4424  CE2 TYR A 574       5.940 -24.669   0.795  1.00 43.99           C  
ANISOU 4424  CE2 TYR A 574     6014   4972   5730  -1594     99   3150       C  
ATOM   4425  CZ  TYR A 574       4.620 -24.396   0.506  1.00 46.33           C  
ANISOU 4425  CZ  TYR A 574     6094   5464   6046  -1789    226   3090       C  
ATOM   4426  OH  TYR A 574       3.745 -24.119   1.519  1.00 49.70           O  
ANISOU 4426  OH  TYR A 574     6404   6208   6273  -1914    406   3248       O  
ATOM   4427  N   ALA A 575       7.859 -27.827  -0.693  1.00 57.14           N  
ANISOU 4427  N   ALA A 575     8248   5435   8026  -1529   -311   3234       N  
ATOM   4428  CA  ALA A 575       8.629 -28.377   0.427  1.00 60.15           C  
ANISOU 4428  CA  ALA A 575     8832   5710   8310  -1429   -365   3518       C  
ATOM   4429  C   ALA A 575       9.521 -29.524  -0.047  1.00 60.46           C  
ANISOU 4429  C   ALA A 575     9108   5281   8585  -1306   -536   3535       C  
ATOM   4430  O   ALA A 575      10.628 -29.710   0.470  1.00 57.76           O  
ANISOU 4430  O   ALA A 575     8895   4858   8194  -1063   -645   3634       O  
ATOM   4431  CB  ALA A 575       7.698 -28.849   1.534  1.00 61.43           C  
ANISOU 4431  CB  ALA A 575     9039   5950   8350  -1704   -237   3857       C  
ATOM   4432  N   ASN A 576       9.022 -30.267  -1.040  1.00 59.66           N  
ANISOU 4432  N   ASN A 576     9052   4882   8735  -1463   -569   3419       N  
ATOM   4433  CA  ASN A 576       9.735 -31.378  -1.660  1.00 60.43           C  
ANISOU 4433  CA  ASN A 576     9377   4503   9082  -1348   -725   3375       C  
ATOM   4434  C   ASN A 576      10.450 -30.968  -2.947  1.00 56.56           C  
ANISOU 4434  C   ASN A 576     8809   3991   8691  -1103   -797   2995       C  
ATOM   4435  O   ASN A 576      11.046 -31.803  -3.619  1.00 59.77           O  
ANISOU 4435  O   ASN A 576     9379   4033   9298   -973   -914   2890       O  
ATOM   4436  CB  ASN A 576       8.753 -32.515  -1.993  1.00 64.94           C  
ANISOU 4436  CB  ASN A 576    10076   4723   9875  -1687   -729   3458       C  
ATOM   4437  CG  ASN A 576       7.846 -32.886  -0.822  1.00 67.93           C  
ANISOU 4437  CG  ASN A 576    10494   5160  10157  -2005   -615   3839       C  
ATOM   4438  OD1 ASN A 576       8.273 -32.892   0.332  1.00 68.03           O  
ANISOU 4438  OD1 ASN A 576    10602   5255   9989  -1917   -598   4123       O  
ATOM   4439  ND2 ASN A 576       6.587 -33.202  -1.123  1.00 67.81           N  
ANISOU 4439  ND2 ASN A 576    10394   5119  10250  -2384   -535   3848       N  
ATOM   4440  N   CYS A 577      10.390 -29.692  -3.305  1.00 55.08           N  
ANISOU 4440  N   CYS A 577     8383   4185   8360  -1033   -723   2791       N  
ATOM   4441  CA  CYS A 577      10.892 -29.259  -4.608  1.00 54.36           C  
ANISOU 4441  CA  CYS A 577     8209   4102   8343   -855   -762   2445       C  
ATOM   4442  C   CYS A 577      11.319 -27.793  -4.654  1.00 48.72           C  
ANISOU 4442  C   CYS A 577     7283   3789   7438   -689   -701   2304       C  
ATOM   4443  O   CYS A 577      10.895 -27.048  -5.522  1.00 48.80           O  
ANISOU 4443  O   CYS A 577     7148   3969   7427   -720   -652   2084       O  
ATOM   4444  CB  CYS A 577       9.834 -29.517  -5.679  1.00 55.69           C  
ANISOU 4444  CB  CYS A 577     8337   4180   8641  -1084   -749   2261       C  
ATOM   4445  SG  CYS A 577      10.482 -29.402  -7.360  1.00 57.26           S  
ANISOU 4445  SG  CYS A 577     8529   4285   8942   -869   -818   1859       S  
ATOM   4446  N   HIS A 578      12.184 -27.392  -3.735  1.00 46.45           N  
ANISOU 4446  N   HIS A 578     6992   3639   7018   -512   -721   2429       N  
ATOM   4447  CA  HIS A 578      12.731 -26.046  -3.749  1.00 42.08           C  
ANISOU 4447  CA  HIS A 578     6263   3418   6309   -358   -685   2291       C  
ATOM   4448  C   HIS A 578      14.238 -26.093  -3.986  1.00 41.65           C  
ANISOU 4448  C   HIS A 578     6223   3292   6310    -62   -784   2204       C  
ATOM   4449  O   HIS A 578      14.850 -27.159  -3.933  1.00 45.32           O  
ANISOU 4449  O   HIS A 578     6837   3473   6909     53   -882   2281       O  
ATOM   4450  CB  HIS A 578      12.418 -25.336  -2.438  1.00 42.04           C  
ANISOU 4450  CB  HIS A 578     6200   3703   6071   -419   -624   2473       C  
ATOM   4451  CG  HIS A 578      13.022 -25.996  -1.243  1.00 45.53           C  
ANISOU 4451  CG  HIS A 578     6788   4061   6450   -344   -702   2741       C  
ATOM   4452  ND1 HIS A 578      12.397 -27.020  -0.568  1.00 51.98           N  
ANISOU 4452  ND1 HIS A 578     7763   4700   7285   -514   -693   3009       N  
ATOM   4453  CD2 HIS A 578      14.199 -25.789  -0.611  1.00 45.75           C  
ANISOU 4453  CD2 HIS A 578     6830   4160   6394   -121   -801   2792       C  
ATOM   4454  CE1 HIS A 578      13.164 -27.412   0.434  1.00 54.11           C  
ANISOU 4454  CE1 HIS A 578     8160   4931   7469   -381   -785   3228       C  
ATOM   4455  NE2 HIS A 578      14.260 -26.678   0.432  1.00 51.17           N  
ANISOU 4455  NE2 HIS A 578     7693   4719   7032   -135   -861   3092       N  
ATOM   4456  N   LEU A 579      14.827 -24.930  -4.245  1.00 38.76           N  
ANISOU 4456  N   LEU A 579     5695   3182   5850     59   -758   2046       N  
ATOM   4457  CA  LEU A 579      16.260 -24.828  -4.496  1.00 40.13           C  
ANISOU 4457  CA  LEU A 579     5820   3355   6073    319   -832   1951       C  
ATOM   4458  C   LEU A 579      17.048 -24.569  -3.209  1.00 42.77           C  
ANISOU 4458  C   LEU A 579     6135   3834   6281    432   -913   2120       C  
ATOM   4459  O   LEU A 579      18.135 -25.127  -3.017  1.00 44.81           O  
ANISOU 4459  O   LEU A 579     6418   3990   6615    641  -1025   2162       O  
ATOM   4460  CB  LEU A 579      16.542 -23.735  -5.524  1.00 36.16           C  
ANISOU 4460  CB  LEU A 579     5151   3040   5547    365   -762   1699       C  
ATOM   4461  CG  LEU A 579      15.898 -23.955  -6.897  1.00 35.20           C  
ANISOU 4461  CG  LEU A 579     5050   2804   5521    291   -703   1511       C  
ATOM   4462  CD1 LEU A 579      16.237 -22.792  -7.819  1.00 36.22           C  
ANISOU 4462  CD1 LEU A 579     5031   3141   5589    344   -631   1307       C  
ATOM   4463  CD2 LEU A 579      16.329 -25.264  -7.532  1.00 33.37           C  
ANISOU 4463  CD2 LEU A 579     4952   2252   5474    406   -768   1453       C  
ATOM   4464  N   ALA A 580      16.505 -23.731  -2.330  1.00 39.90           N  
ANISOU 4464  N   ALA A 580     5724   3718   5718    312   -865   2205       N  
ATOM   4465  CA  ALA A 580      17.118 -23.510  -1.020  1.00 41.13           C  
ANISOU 4465  CA  ALA A 580     5887   4027   5713    396   -953   2367       C  
ATOM   4466  C   ALA A 580      16.192 -22.719  -0.117  1.00 41.47           C  
ANISOU 4466  C   ALA A 580     5916   4317   5522    232   -868   2445       C  
ATOM   4467  O   ALA A 580      15.205 -22.154  -0.572  1.00 44.33           O  
ANISOU 4467  O   ALA A 580     6218   4763   5861     84   -743   2344       O  
ATOM   4468  CB  ALA A 580      18.438 -22.785  -1.172  1.00 38.94           C  
ANISOU 4468  CB  ALA A 580     5457   3899   5440    585  -1032   2221       C  
ATOM   4469  N   ARG A 581      16.507 -22.689   1.168  1.00 43.95           N  
ANISOU 4469  N   ARG A 581     6284   4761   5652    276   -941   2621       N  
ATOM   4470  CA  ARG A 581      15.792 -21.833   2.094  1.00 45.18           C  
ANISOU 4470  CA  ARG A 581     6422   5194   5550    164   -862   2661       C  
ATOM   4471  C   ARG A 581      16.259 -20.410   1.852  1.00 42.21           C  
ANISOU 4471  C   ARG A 581     5889   5037   5112    223   -864   2416       C  
ATOM   4472  O   ARG A 581      17.412 -20.179   1.507  1.00 44.09           O  
ANISOU 4472  O   ARG A 581     6048   5267   5439    363   -971   2305       O  
ATOM   4473  CB  ARG A 581      16.090 -22.208   3.542  1.00 50.96           C  
ANISOU 4473  CB  ARG A 581     7277   6018   6068    212   -954   2911       C  
ATOM   4474  CG  ARG A 581      14.966 -21.856   4.504  1.00 54.75           C  
ANISOU 4474  CG  ARG A 581     7801   6719   6283     53   -820   3031       C  
ATOM   4475  CD  ARG A 581      14.176 -23.101   4.918  1.00 59.82           C  
ANISOU 4475  CD  ARG A 581     8604   7196   6928    -91   -757   3332       C  
ATOM   4476  NE  ARG A 581      12.843 -22.768   5.411  1.00 61.44           N  
ANISOU 4476  NE  ARG A 581     8785   7606   6953   -291   -560   3397       N  
ATOM   4477  CZ  ARG A 581      12.011 -23.627   5.993  1.00 63.92           C  
ANISOU 4477  CZ  ARG A 581     9212   7875   7201   -465   -463   3676       C  
ATOM   4478  NH1 ARG A 581      10.819 -23.211   6.397  1.00 66.53           N  
ANISOU 4478  NH1 ARG A 581     9467   8446   7366   -636   -265   3704       N  
ATOM   4479  NH2 ARG A 581      12.358 -24.893   6.174  1.00 66.69           N  
ANISOU 4479  NH2 ARG A 581     9747   7938   7655   -468   -557   3931       N  
ATOM   4480  N   ALA A 582      15.361 -19.462   2.056  1.00 37.20           N  
ANISOU 4480  N   ALA A 582     5208   4596   4330    115   -745   2335       N  
ATOM   4481  CA  ALA A 582      15.661 -18.073   1.852  1.00 34.90           C  
ANISOU 4481  CA  ALA A 582     4803   4473   3983    151   -741   2109       C  
ATOM   4482  C   ALA A 582      15.370 -17.336   3.141  1.00 39.07           C  
ANISOU 4482  C   ALA A 582     5366   5255   4223    138   -734   2136       C  
ATOM   4483  O   ALA A 582      14.233 -17.346   3.603  1.00 44.57           O  
ANISOU 4483  O   ALA A 582     6100   6050   4786     41   -606   2211       O  
ATOM   4484  CB  ALA A 582      14.792 -17.532   0.743  1.00 33.10           C  
ANISOU 4484  CB  ALA A 582     4500   4218   3857     66   -608   1949       C  
ATOM   4485  N   PRO A 583      16.387 -16.701   3.741  1.00 39.23           N  
ANISOU 4485  N   PRO A 583     5367   5398   4140    234   -872   2064       N  
ATOM   4486  CA  PRO A 583      16.112 -15.859   4.902  1.00 38.79           C  
ANISOU 4486  CA  PRO A 583     5355   5590   3793    229   -871   2030       C  
ATOM   4487  C   PRO A 583      15.029 -14.829   4.604  1.00 39.56           C  
ANISOU 4487  C   PRO A 583     5412   5778   3839    161   -708   1862       C  
ATOM   4488  O   PRO A 583      15.105 -14.129   3.593  1.00 37.67           O  
ANISOU 4488  O   PRO A 583     5090   5459   3765    156   -682   1680       O  
ATOM   4489  CB  PRO A 583      17.445 -15.152   5.153  1.00 40.36           C  
ANISOU 4489  CB  PRO A 583     5496   5862   3976    319  -1058   1892       C  
ATOM   4490  CG  PRO A 583      18.474 -16.059   4.576  1.00 41.78           C  
ANISOU 4490  CG  PRO A 583     5622   5873   4380    399  -1175   1970       C  
ATOM   4491  CD  PRO A 583      17.827 -16.794   3.439  1.00 40.07           C  
ANISOU 4491  CD  PRO A 583     5402   5439   4384    349  -1039   2011       C  
ATOM   4492  N   ASN A 584      14.026 -14.751   5.475  1.00 41.80           N  
ANISOU 4492  N   ASN A 584     5755   6236   3891    119   -593   1933       N  
ATOM   4493  CA  ASN A 584      12.982 -13.745   5.369  1.00 37.21           C  
ANISOU 4493  CA  ASN A 584     5128   5778   3233     97   -443   1769       C  
ATOM   4494  C   ASN A 584      13.604 -12.402   5.093  1.00 37.79           C  
ANISOU 4494  C   ASN A 584     5172   5855   3330    164   -526   1504       C  
ATOM   4495  O   ASN A 584      14.661 -12.095   5.630  1.00 42.95           O  
ANISOU 4495  O   ASN A 584     5860   6547   3913    213   -686   1453       O  
ATOM   4496  CB  ASN A 584      12.194 -13.640   6.682  1.00 39.47           C  
ANISOU 4496  CB  ASN A 584     5483   6325   3189     94   -342   1845       C  
ATOM   4497  CG  ASN A 584      11.093 -14.691   6.813  1.00 37.96           C  
ANISOU 4497  CG  ASN A 584     5284   6159   2979    -23   -175   2083       C  
ATOM   4498  OD1 ASN A 584      10.943 -15.578   5.971  1.00 35.20           O  
ANISOU 4498  OD1 ASN A 584     4899   5606   2868   -108   -160   2192       O  
ATOM   4499  ND2 ASN A 584      10.308 -14.579   7.880  1.00 35.77           N  
ANISOU 4499  ND2 ASN A 584     5040   6141   2410    -37    -44   2154       N  
ATOM   4500  N   HIS A 585      12.944 -11.594   4.268  1.00 36.25           N  
ANISOU 4500  N   HIS A 585     4916   5619   3238    159   -428   1342       N  
ATOM   4501  CA  HIS A 585      13.322 -10.196   4.096  1.00 32.76           C  
ANISOU 4501  CA  HIS A 585     4480   5169   2799    210   -483   1097       C  
ATOM   4502  C   HIS A 585      13.358  -9.505   5.462  1.00 31.87           C  
ANISOU 4502  C   HIS A 585     4460   5257   2391    269   -524   1006       C  
ATOM   4503  O   HIS A 585      12.751  -9.983   6.414  1.00 33.75           O  
ANISOU 4503  O   HIS A 585     4744   5675   2405    279   -449   1122       O  
ATOM   4504  CB  HIS A 585      12.319  -9.494   3.183  1.00 34.43           C  
ANISOU 4504  CB  HIS A 585     4639   5329   3113    221   -354    976       C  
ATOM   4505  CG  HIS A 585      12.406  -9.909   1.746  1.00 33.25           C  
ANISOU 4505  CG  HIS A 585     4415   4987   3231    173   -342   1009       C  
ATOM   4506  ND1 HIS A 585      12.009  -9.089   0.714  1.00 30.67           N  
ANISOU 4506  ND1 HIS A 585     4058   4570   3026    194   -299    880       N  
ATOM   4507  CD2 HIS A 585      12.864 -11.048   1.170  1.00 33.72           C  
ANISOU 4507  CD2 HIS A 585     4441   4927   3443    121   -374   1148       C  
ATOM   4508  CE1 HIS A 585      12.224  -9.706  -0.437  1.00 34.05           C  
ANISOU 4508  CE1 HIS A 585     4434   4854   3648    148   -301    937       C  
ATOM   4509  NE2 HIS A 585      12.741 -10.895  -0.189  1.00 30.34           N  
ANISOU 4509  NE2 HIS A 585     3960   4359   3207    107   -343   1085       N  
ATOM   4510  N   ALA A 586      14.065  -8.388   5.566  1.00 37.49           N  
ANISOU 4510  N   ALA A 586     5989   3346   4909    652   -908    954       N  
ATOM   4511  CA  ALA A 586      14.184  -7.690   6.850  1.00 35.07           C  
ANISOU 4511  CA  ALA A 586     5660   3333   4333    602   -789   1284       C  
ATOM   4512  C   ALA A 586      14.479  -6.213   6.699  1.00 30.73           C  
ANISOU 4512  C   ALA A 586     5216   3074   3388    734   -730   1130       C  
ATOM   4513  O   ALA A 586      14.931  -5.761   5.662  1.00 27.85           O  
ANISOU 4513  O   ALA A 586     4964   2673   2947    887   -754    910       O  
ATOM   4514  CB  ALA A 586      15.260  -8.335   7.687  1.00 36.62           C  
ANISOU 4514  CB  ALA A 586     5851   3443   4622    610   -769   1631       C  
ATOM   4515  N   VAL A 587      14.227  -5.474   7.769  1.00 32.66           N  
ANISOU 4515  N   VAL A 587     5400   3609   3402    678   -635   1253       N  
ATOM   4516  CA  VAL A 587      14.475  -4.045   7.817  1.00 29.73           C  
ANISOU 4516  CA  VAL A 587     5091   3427   2780    775   -564   1083       C  
ATOM   4517  C   VAL A 587      15.856  -3.808   8.386  1.00 29.31           C  
ANISOU 4517  C   VAL A 587     5077   3441   2618    797   -555   1147       C  
ATOM   4518  O   VAL A 587      16.268  -4.479   9.328  1.00 38.73           O  
ANISOU 4518  O   VAL A 587     6193   4753   3767    727   -578   1386       O  
ATOM   4519  CB  VAL A 587      13.456  -3.349   8.730  1.00 32.62           C  
ANISOU 4519  CB  VAL A 587     5328   4085   2982    717   -463   1056       C  
ATOM   4520  CG1 VAL A 587      13.641  -1.831   8.692  1.00 33.91           C  
ANISOU 4520  CG1 VAL A 587     5538   4315   3030    833   -386    806       C  
ATOM   4521  CG2 VAL A 587      12.052  -3.732   8.329  1.00 33.56           C  
ANISOU 4521  CG2 VAL A 587     5321   4185   3243    668   -478   1039       C  
ATOM   4522  N   VAL A 588      16.563  -2.837   7.830  1.00 28.88           N  
ANISOU 4522  N   VAL A 588     5105   3335   2534    893   -521    974       N  
ATOM   4523  CA  VAL A 588      17.917  -2.523   8.263  1.00 28.76           C  
ANISOU 4523  CA  VAL A 588     5072   3381   2475    890   -524    980       C  
ATOM   4524  C   VAL A 588      18.070  -1.034   8.480  1.00 29.76           C  
ANISOU 4524  C   VAL A 588     5181   3567   2560    882   -440    746       C  
ATOM   4525  O   VAL A 588      17.322  -0.233   7.916  1.00 24.04           O  
ANISOU 4525  O   VAL A 588     4501   2729   1905    945   -364    631       O  
ATOM   4526  CB  VAL A 588      18.979  -2.931   7.215  1.00 26.92           C  
ANISOU 4526  CB  VAL A 588     4902   2934   2394    997   -538   1006       C  
ATOM   4527  CG1 VAL A 588      18.888  -4.418   6.909  1.00 27.54           C  
ANISOU 4527  CG1 VAL A 588     4987   2848   2628   1030   -619   1139       C  
ATOM   4528  CG2 VAL A 588      18.819  -2.088   5.943  1.00 20.00           C  
ANISOU 4528  CG2 VAL A 588     4120   1933   1547   1108   -448    878       C  
ATOM   4529  N   THR A 589      19.077  -0.690   9.278  1.00 32.58           N  
ANISOU 4529  N   THR A 589     5443   4082   2855    813   -470    674       N  
ATOM   4530  CA  THR A 589      19.422   0.690   9.580  1.00 30.89           C  
ANISOU 4530  CA  THR A 589     5165   3861   2712    761   -407    371       C  
ATOM   4531  C   THR A 589      20.852   0.767  10.117  1.00 35.17           C  
ANISOU 4531  C   THR A 589     5565   4544   3255    676   -493    305       C  
ATOM   4532  O   THR A 589      21.561  -0.248  10.186  1.00 38.16           O  
ANISOU 4532  O   THR A 589     5904   5027   3569    703   -594    544       O  
ATOM   4533  CB  THR A 589      18.476   1.239  10.627  1.00 32.57           C  
ANISOU 4533  CB  THR A 589     5300   4328   2745    717   -377    132       C  
ATOM   4534  OG1 THR A 589      18.822   2.599  10.912  1.00 38.33           O  
ANISOU 4534  OG1 THR A 589     5951   4967   3646    668   -319   -263       O  
ATOM   4535  CG2 THR A 589      18.552   0.392  11.893  1.00 31.51           C  
ANISOU 4535  CG2 THR A 589     5049   4688   2237    651   -479    247       C  
ATOM   4536  N   ARG A 590      21.282   1.958  10.515  1.00 36.91           N  
ANISOU 4536  N   ARG A 590     5672   4749   3602    577   -466    -41       N  
ATOM   4537  CA  ARG A 590      22.596   2.091  11.159  1.00 43.54           C  
ANISOU 4537  CA  ARG A 590     6302   5802   4438    462   -590   -188       C  
ATOM   4538  C   ARG A 590      22.444   2.033  12.682  1.00 48.14           C  
ANISOU 4538  C   ARG A 590     6728   6957   4604    395   -739   -420       C  
ATOM   4539  O   ARG A 590      21.371   2.324  13.220  1.00 50.33           O  
ANISOU 4539  O   ARG A 590     7042   7392   4689    411   -681   -598       O  
ATOM   4540  CB  ARG A 590      23.332   3.354  10.705  1.00 46.04           C  
ANISOU 4540  CB  ARG A 590     6516   5772   5204    347   -492   -453       C  
ATOM   4541  CG  ARG A 590      22.437   4.523  10.434  1.00 47.46           C  
ANISOU 4541  CG  ARG A 590     6775   5594   5663    351   -326   -684       C  
ATOM   4542  CD  ARG A 590      23.201   5.735  10.015  1.00 50.34           C  
ANISOU 4542  CD  ARG A 590     7009   5529   6589    218   -208   -868       C  
ATOM   4543  NE  ARG A 590      22.258   6.728   9.523  1.00 54.25           N  
ANISOU 4543  NE  ARG A 590     7607   5576   7427    297    -22   -919       N  
ATOM   4544  CZ  ARG A 590      21.497   7.491  10.299  1.00 62.79           C  
ANISOU 4544  CZ  ARG A 590     8643   6625   8590    289    -12  -1374       C  
ATOM   4545  NH1 ARG A 590      21.571   7.397  11.623  1.00 68.65           N  
ANISOU 4545  NH1 ARG A 590     9239   7835   9011    189   -174  -1855       N  
ATOM   4546  NH2 ARG A 590      20.664   8.369   9.754  1.00 66.67           N  
ANISOU 4546  NH2 ARG A 590     9208   6652   9470    412    165  -1351       N  
ATOM   4547  N   LYS A 591      23.515   1.633  13.364  1.00 50.74           N  
ANISOU 4547  N   LYS A 591     6853   7669   4755    349   -929   -401       N  
ATOM   4548  CA  LYS A 591      23.462   1.349  14.802  1.00 54.15           C  
ANISOU 4548  CA  LYS A 591     7114   8815   4646    334  -1103   -495       C  
ATOM   4549  C   LYS A 591      22.780   2.435  15.628  1.00 55.26           C  
ANISOU 4549  C   LYS A 591     7181   9205   4610    255  -1063  -1102       C  
ATOM   4550  O   LYS A 591      21.953   2.124  16.481  1.00 55.41           O  
ANISOU 4550  O   LYS A 591     7188   9718   4149    312  -1054  -1074       O  
ATOM   4551  CB  LYS A 591      24.865   1.065  15.364  1.00 59.43           C  
ANISOU 4551  CB  LYS A 591     7502   9887   5192    300  -1351   -480       C  
ATOM   4552  CG  LYS A 591      25.152  -0.419  15.616  1.00 61.12           C  
ANISOU 4552  CG  LYS A 591     7689  10385   5148    463  -1478    179       C  
ATOM   4553  CD  LYS A 591      24.477  -0.907  16.899  1.00 65.70           C  
ANISOU 4553  CD  LYS A 591     8200  11676   5086    520  -1561    357       C  
ATOM   4554  CE  LYS A 591      24.539  -2.424  17.030  1.00 66.84           C  
ANISOU 4554  CE  LYS A 591     8352  11920   5126    692  -1621   1151       C  
ATOM   4555  NZ  LYS A 591      23.620  -2.930  18.086  1.00 68.62           N  
ANISOU 4555  NZ  LYS A 591     8548  12727   4799    738  -1596   1477       N  
ATOM   4556  N   ASP A 592      23.105   3.698  15.354  1.00 54.99           N  
ANISOU 4556  N   ASP A 592     7078   8806   5011    130  -1009  -1638       N  
ATOM   4557  CA  ASP A 592      22.585   4.820  16.149  1.00 60.40           C  
ANISOU 4557  CA  ASP A 592     7651   9651   5646     63   -976  -2356       C  
ATOM   4558  C   ASP A 592      21.068   5.043  16.037  1.00 61.56           C  
ANISOU 4558  C   ASP A 592     7979   9646   5765    193   -752  -2379       C  
ATOM   4559  O   ASP A 592      20.523   5.902  16.738  1.00 65.99           O  
ANISOU 4559  O   ASP A 592     8437  10371   6266    189   -695  -2992       O  
ATOM   4560  CB  ASP A 592      23.331   6.129  15.823  1.00 63.39           C  
ANISOU 4560  CB  ASP A 592     7883   9514   6687   -121   -957  -2916       C  
ATOM   4561  CG  ASP A 592      23.165   6.565  14.371  1.00 61.61           C  
ANISOU 4561  CG  ASP A 592     7857   8398   7155    -96   -715  -2605       C  
ATOM   4562  OD1 ASP A 592      23.199   5.688  13.477  1.00 58.47           O  
ANISOU 4562  OD1 ASP A 592     7637   7847   6732     12   -662  -1956       O  
ATOM   4563  OD2 ASP A 592      23.013   7.783  14.119  1.00 61.15           O  
ANISOU 4563  OD2 ASP A 592     7759   7803   7673   -170   -576  -3006       O  
ATOM   4564  N   LYS A 593      20.386   4.288  15.175  1.00 58.17           N  
ANISOU 4564  N   LYS A 593     7777   8928   5396    314   -632  -1780       N  
ATOM   4565  CA  LYS A 593      18.925   4.395  15.070  1.00 62.89           C  
ANISOU 4565  CA  LYS A 593     8488   9451   5958    438   -447  -1760       C  
ATOM   4566  C   LYS A 593      18.146   3.100  15.320  1.00 62.40           C  
ANISOU 4566  C   LYS A 593     8482   9777   5451    514   -435  -1222       C  
ATOM   4567  O   LYS A 593      16.927   3.148  15.472  1.00 62.53           O  
ANISOU 4567  O   LYS A 593     8505   9886   5366    592   -289  -1240       O  
ATOM   4568  CB  LYS A 593      18.517   5.016  13.721  1.00 62.94           C  
ANISOU 4568  CB  LYS A 593     8660   8679   6576    511   -286  -1657       C  
ATOM   4569  CG  LYS A 593      18.526   6.559  13.727  1.00 67.46           C  
ANISOU 4569  CG  LYS A 593     9145   8833   7652    488   -182  -2247       C  
ATOM   4570  CD  LYS A 593      17.292   7.169  13.052  1.00 66.29           C  
ANISOU 4570  CD  LYS A 593     9093   8248   7847    673     14  -2210       C  
ATOM   4571  CE  LYS A 593      17.249   8.696  13.229  1.00 70.21           C  
ANISOU 4571  CE  LYS A 593     9469   8287   8922    679    130  -2817       C  
ATOM   4572  NZ  LYS A 593      15.978   9.318  12.727  1.00 67.67           N  
ANISOU 4572  NZ  LYS A 593     9188   7588   8935    919    313  -2787       N  
ATOM   4573  N   GLU A 594      18.837   1.961  15.387  1.00 63.84           N  
ANISOU 4573  N   GLU A 594     8664  10158   5432    492   -576   -740       N  
ATOM   4574  CA  GLU A 594      18.218   0.674  15.761  1.00 63.83           C  
ANISOU 4574  CA  GLU A 594     8670  10490   5095    534   -566   -181       C  
ATOM   4575  C   GLU A 594      17.188   0.833  16.882  1.00 65.98           C  
ANISOU 4575  C   GLU A 594     8802  11380   4887    553   -448   -333       C  
ATOM   4576  O   GLU A 594      16.098   0.261  16.823  1.00 64.38           O  
ANISOU 4576  O   GLU A 594     8617  11201   4644    579   -307    -11       O  
ATOM   4577  CB  GLU A 594      19.309  -0.322  16.177  1.00 68.64           C  
ANISOU 4577  CB  GLU A 594     9193  11391   5494    528   -759    236       C  
ATOM   4578  CG  GLU A 594      18.828  -1.583  16.898  1.00 73.69           C  
ANISOU 4578  CG  GLU A 594     9766  12461   5772    564   -753    855       C  
ATOM   4579  CD  GLU A 594      19.943  -2.603  17.079  1.00 76.21           C  
ANISOU 4579  CD  GLU A 594    10010  12888   6057    615   -945   1359       C  
ATOM   4580  OE1 GLU A 594      20.991  -2.248  17.662  1.00 77.64           O  
ANISOU 4580  OE1 GLU A 594    10028  13473   5999    621  -1129   1159       O  
ATOM   4581  OE2 GLU A 594      19.771  -3.758  16.634  1.00 77.62           O  
ANISOU 4581  OE2 GLU A 594    10262  12731   6498    655   -921   1927       O  
ATOM   4582  N   ALA A 595      17.544   1.613  17.899  1.00 70.68           N  
ANISOU 4582  N   ALA A 595     9222  12511   5123    536   -500   -866       N  
ATOM   4583  CA  ALA A 595      16.625   1.930  18.985  1.00 76.16           C  
ANISOU 4583  CA  ALA A 595     9751  13883   5302    586   -360  -1153       C  
ATOM   4584  C   ALA A 595      15.312   2.498  18.442  1.00 74.09           C  
ANISOU 4584  C   ALA A 595     9554  13221   5376    657   -114  -1355       C  
ATOM   4585  O   ALA A 595      14.275   1.841  18.501  1.00 73.71           O  
ANISOU 4585  O   ALA A 595     9480  13329   5197    689     42   -952       O  
ATOM   4586  CB  ALA A 595      17.271   2.917  19.958  1.00 80.53           C  
ANISOU 4586  CB  ALA A 595    10104  14968   5524    563   -473  -1936       C  
ATOM   4587  N   CYS A 596      15.368   3.707  17.895  1.00 72.89           N  
ANISOU 4587  N   CYS A 596     9452  12527   5717    682    -80  -1934       N  
ATOM   4588  CA  CYS A 596      14.158   4.418  17.481  1.00 72.69           C  
ANISOU 4588  CA  CYS A 596     9434  12164   6022    807    137  -2183       C  
ATOM   4589  C   CYS A 596      13.371   3.697  16.385  1.00 69.44           C  
ANISOU 4589  C   CYS A 596     9162  11307   5914    846    199  -1568       C  
ATOM   4590  O   CYS A 596      12.141   3.799  16.333  1.00 70.36           O  
ANISOU 4590  O   CYS A 596     9199  11461   6072    948    370  -1572       O  
ATOM   4591  CB  CYS A 596      14.487   5.845  17.015  1.00 74.42           C  
ANISOU 4591  CB  CYS A 596     9674  11758   6845    841    154  -2814       C  
ATOM   4592  SG  CYS A 596      14.597   7.083  18.331  1.00 82.07           S  
ANISOU 4592  SG  CYS A 596    10387  13170   7626    862    194  -3887       S  
ATOM   4593  N   VAL A 597      14.068   2.979  15.506  1.00 62.70           N  
ANISOU 4593  N   VAL A 597     8480  10067   5277    775     56  -1099       N  
ATOM   4594  CA  VAL A 597      13.400   2.319  14.392  1.00 56.66           C  
ANISOU 4594  CA  VAL A 597     7833   8894   4803    809     74   -642       C  
ATOM   4595  C   VAL A 597      12.553   1.163  14.907  1.00 57.81           C  
ANISOU 4595  C   VAL A 597     7866   9453   4645    753    137   -213       C  
ATOM   4596  O   VAL A 597      11.387   1.026  14.526  1.00 58.09           O  
ANISOU 4596  O   VAL A 597     7838   9407   4828    794    241   -110       O  
ATOM   4597  CB  VAL A 597      14.399   1.833  13.316  1.00 52.31           C  
ANISOU 4597  CB  VAL A 597     7471   7873   4533    769    -77   -337       C  
ATOM   4598  CG1 VAL A 597      13.680   1.057  12.221  1.00 46.14           C  
ANISOU 4598  CG1 VAL A 597     6779   6783   3970    805    -86     37       C  
ATOM   4599  CG2 VAL A 597      15.129   3.013  12.719  1.00 52.05           C  
ANISOU 4599  CG2 VAL A 597     7508   7404   4865    807    -81   -665       C  
ATOM   4600  N   HIS A 598      13.135   0.341  15.775  1.00 59.02           N  
ANISOU 4600  N   HIS A 598     7958  10059   4410    661     76     76       N  
ATOM   4601  CA  HIS A 598      12.388  -0.747  16.410  1.00 63.99           C  
ANISOU 4601  CA  HIS A 598     8439  11099   4774    591    177    580       C  
ATOM   4602  C   HIS A 598      11.138  -0.202  17.130  1.00 67.61           C  
ANISOU 4602  C   HIS A 598     8677  12033   4978    647    420    330       C  
ATOM   4603  O   HIS A 598      10.044  -0.743  16.991  1.00 68.85           O  
ANISOU 4603  O   HIS A 598     8711  12200   5247    606    557    625       O  
ATOM   4604  CB  HIS A 598      13.290  -1.493  17.391  1.00 67.80           C  
ANISOU 4604  CB  HIS A 598     8853  12090   4819    539     83    943       C  
ATOM   4605  CG  HIS A 598      12.759  -2.826  17.819  1.00 70.71           C  
ANISOU 4605  CG  HIS A 598     9099  12680   5089    452    171   1681       C  
ATOM   4606  ND1 HIS A 598      13.518  -3.975  17.766  1.00 72.48           N  
ANISOU 4606  ND1 HIS A 598     9366  12739   5435    408     36   2276       N  
ATOM   4607  CD2 HIS A 598      11.555  -3.194  18.318  1.00 72.91           C  
ANISOU 4607  CD2 HIS A 598     9177  13296   5229    397    402   1953       C  
ATOM   4608  CE1 HIS A 598      12.806  -4.993  18.215  1.00 74.79           C  
ANISOU 4608  CE1 HIS A 598     9503  13199   5714    320    179   2910       C  
ATOM   4609  NE2 HIS A 598      11.611  -4.546  18.553  1.00 76.23           N  
ANISOU 4609  NE2 HIS A 598     9529  13711   5726    293    409   2738       N  
ATOM   4610  N   LYS A 599      11.308   0.888  17.870  1.00 69.29           N  
ANISOU 4610  N   LYS A 599     8808  12623   4897    741    475   -274       N  
ATOM   4611  CA  LYS A 599      10.217   1.484  18.639  1.00 74.86           C  
ANISOU 4611  CA  LYS A 599     9275  13847   5322    841    729   -626       C  
ATOM   4612  C   LYS A 599       9.103   1.999  17.731  1.00 72.37           C  
ANISOU 4612  C   LYS A 599     8940  13023   5534    946    844   -788       C  
ATOM   4613  O   LYS A 599       7.942   1.616  17.881  1.00 75.03           O  
ANISOU 4613  O   LYS A 599     9072  13604   5832    949   1033   -567       O  
ATOM   4614  CB  LYS A 599      10.761   2.627  19.504  1.00 78.91           C  
ANISOU 4614  CB  LYS A 599     9711  14766   5507    935    727  -1407       C  
ATOM   4615  CG  LYS A 599       9.852   3.086  20.626  1.00 83.96           C  
ANISOU 4615  CG  LYS A 599    10060  16206   5635   1057    996  -1814       C  
ATOM   4616  CD  LYS A 599      10.538   4.164  21.464  1.00 90.90           C  
ANISOU 4616  CD  LYS A 599    10857  17478   6202   1134    940  -2707       C  
ATOM   4617  CE  LYS A 599      11.673   3.598  22.342  1.00 94.14           C  
ANISOU 4617  CE  LYS A 599    11233  18601   5936   1030    731  -2536       C  
ATOM   4618  NZ  LYS A 599      12.399   4.650  23.114  1.00 97.80           N  
ANISOU 4618  NZ  LYS A 599    11578  19462   6118   1074    615  -3508       N  
ATOM   4619  N   ILE A 600       9.470   2.863  16.791  1.00 67.72           N  
ANISOU 4619  N   ILE A 600     8527  11756   5446   1036    733  -1123       N  
ATOM   4620  CA  ILE A 600       8.504   3.496  15.901  1.00 65.93           C  
ANISOU 4620  CA  ILE A 600     8270  11066   5714   1196    808  -1263       C  
ATOM   4621  C   ILE A 600       7.737   2.450  15.097  1.00 63.47           C  
ANISOU 4621  C   ILE A 600     7936  10589   5593   1118    771   -687       C  
ATOM   4622  O   ILE A 600       6.523   2.550  14.964  1.00 68.05           O  
ANISOU 4622  O   ILE A 600     8304  11249   6303   1207    901   -694       O  
ATOM   4623  CB  ILE A 600       9.194   4.475  14.920  1.00 64.06           C  
ANISOU 4623  CB  ILE A 600     8243  10099   5999   1295    683  -1522       C  
ATOM   4624  CG1 ILE A 600       9.742   5.693  15.663  1.00 68.28           C  
ANISOU 4624  CG1 ILE A 600     8729  10670   6543   1367    741  -2224       C  
ATOM   4625  CG2 ILE A 600       8.229   4.935  13.838  1.00 61.74           C  
ANISOU 4625  CG2 ILE A 600     7922   9346   6191   1487    715  -1454       C  
ATOM   4626  CD1 ILE A 600       8.688   6.675  16.073  1.00 73.26           C  
ANISOU 4626  CD1 ILE A 600     9137  11379   7319   1597    964  -2747       C  
ATOM   4627  N   LEU A 601       8.444   1.443  14.587  1.00 58.17           N  
ANISOU 4627  N   LEU A 601     7441   9695   4966    953    589   -242       N  
ATOM   4628  CA  LEU A 601       7.843   0.453  13.683  1.00 56.12           C  
ANISOU 4628  CA  LEU A 601     7169   9172   4983    861    505    184       C  
ATOM   4629  C   LEU A 601       6.827  -0.465  14.347  1.00 59.73           C  
ANISOU 4629  C   LEU A 601     7341  10051   5304    716    661    523       C  
ATOM   4630  O   LEU A 601       5.896  -0.912  13.688  1.00 60.91           O  
ANISOU 4630  O   LEU A 601     7349  10038   5754    668    642    676       O  
ATOM   4631  CB  LEU A 601       8.915  -0.407  12.996  1.00 53.06           C  
ANISOU 4631  CB  LEU A 601     7025   8413   4722    744    289    487       C  
ATOM   4632  CG  LEU A 601       9.671   0.195  11.805  1.00 49.13           C  
ANISOU 4632  CG  LEU A 601     6772   7397   4497    864    134    321       C  
ATOM   4633  CD1 LEU A 601      10.650  -0.830  11.291  1.00 48.84           C  
ANISOU 4633  CD1 LEU A 601     6908   7119   4531    755    -29    611       C  
ATOM   4634  CD2 LEU A 601       8.737   0.635  10.678  1.00 44.74           C  
ANISOU 4634  CD2 LEU A 601     6178   6582   4241   1014     99    244       C  
ATOM   4635  N   ARG A 602       7.002  -0.776  15.628  1.00 63.01           N  
ANISOU 4635  N   ARG A 602     7636  11040   5265    636    812    669       N  
ATOM   4636  CA  ARG A 602       5.981  -1.548  16.328  1.00 67.14           C  
ANISOU 4636  CA  ARG A 602     7837  12023   5652    501   1033   1056       C  
ATOM   4637  C   ARG A 602       4.806  -0.639  16.667  1.00 70.27           C  
ANISOU 4637  C   ARG A 602     7947  12776   5976    665   1274    663       C  
ATOM   4638  O   ARG A 602       3.651  -1.007  16.433  1.00 72.46           O  
ANISOU 4638  O   ARG A 602     7947  13088   6495    601   1385    843       O  
ATOM   4639  CB  ARG A 602       6.539  -2.280  17.556  1.00 71.39           C  
ANISOU 4639  CB  ARG A 602     8312  13132   5682    382   1132   1493       C  
ATOM   4640  CG  ARG A 602       7.370  -3.520  17.168  1.00 71.01           C  
ANISOU 4640  CG  ARG A 602     8437  12661   5882    210    932   2065       C  
ATOM   4641  CD  ARG A 602       7.046  -4.774  17.977  1.00 74.91           C  
ANISOU 4641  CD  ARG A 602     8699  13487   6277     13   1101   2844       C  
ATOM   4642  NE  ARG A 602       7.908  -4.916  19.149  1.00 78.92           N  
ANISOU 4642  NE  ARG A 602     9205  14628   6155     64   1132   3128       N  
ATOM   4643  CZ  ARG A 602       7.599  -4.542  20.392  1.00 85.69           C  
ANISOU 4643  CZ  ARG A 602     9834  16417   6308    138   1372   3134       C  
ATOM   4644  NH1 ARG A 602       6.425  -3.983  20.684  1.00 88.58           N  
ANISOU 4644  NH1 ARG A 602     9942  17180   6536    175   1648   2858       N  
ATOM   4645  NH2 ARG A 602       8.482  -4.731  21.366  1.00 89.87           N  
ANISOU 4645  NH2 ARG A 602    10359  17560   6226    200   1332   3403       N  
ATOM   4646  N   GLN A 603       5.100   0.554  17.184  1.00 71.57           N  
ANISOU 4646  N   GLN A 603     8145  13171   5877    879   1347     82       N  
ATOM   4647  CA  GLN A 603       4.087   1.615  17.300  1.00 75.19           C  
ANISOU 4647  CA  GLN A 603     8365  13785   6418   1117   1548   -427       C  
ATOM   4648  C   GLN A 603       3.279   1.705  16.004  1.00 71.24           C  
ANISOU 4648  C   GLN A 603     7820  12716   6532   1188   1433   -373       C  
ATOM   4649  O   GLN A 603       2.055   1.829  16.026  1.00 75.93           O  
ANISOU 4649  O   GLN A 603     8074  13520   7258   1272   1603   -409       O  
ATOM   4650  CB  GLN A 603       4.746   2.972  17.631  1.00 76.40           C  
ANISOU 4650  CB  GLN A 603     8647  13899   6484   1343   1544  -1159       C  
ATOM   4651  CG  GLN A 603       4.162   4.222  16.924  1.00 76.47           C  
ANISOU 4651  CG  GLN A 603     8613  13416   7024   1636   1567  -1661       C  
ATOM   4652  CD  GLN A 603       2.758   4.604  17.399  1.00 82.11           C  
ANISOU 4652  CD  GLN A 603     8912  14562   7725   1830   1872  -1892       C  
ATOM   4653  OE1 GLN A 603       2.124   3.871  18.161  1.00 85.32           O  
ANISOU 4653  OE1 GLN A 603     9042  15640   7736   1713   2085  -1621       O  
ATOM   4654  NE2 GLN A 603       2.269   5.760  16.941  1.00 80.77           N  
ANISOU 4654  NE2 GLN A 603     8666  13996   8029   2144   1913  -2351       N  
ATOM   4655  N   GLN A 604       3.981   1.602  14.883  1.00 62.64           N  
ANISOU 4655  N   GLN A 604     7041  10985   5773   1162   1141   -271       N  
ATOM   4656  CA  GLN A 604       3.409   1.847  13.575  1.00 59.00           C  
ANISOU 4656  CA  GLN A 604     6575  10045   5796   1287    979   -272       C  
ATOM   4657  C   GLN A 604       2.596   0.673  13.013  1.00 59.41           C  
ANISOU 4657  C   GLN A 604     6430  10088   6056   1079    892    142       C  
ATOM   4658  O   GLN A 604       1.516   0.884  12.463  1.00 63.18           O  
ANISOU 4658  O   GLN A 604     6642  10562   6803   1191    878     86       O  
ATOM   4659  CB  GLN A 604       4.537   2.226  12.611  1.00 54.69           C  
ANISOU 4659  CB  GLN A 604     6418   8921   5440   1353    732   -324       C  
ATOM   4660  CG  GLN A 604       4.148   3.191  11.539  1.00 54.52           C  
ANISOU 4660  CG  GLN A 604     6408   8502   5804   1638    641   -481       C  
ATOM   4661  CD  GLN A 604       3.613   4.508  12.060  1.00 58.82           C  
ANISOU 4661  CD  GLN A 604     6776   9101   6471   1930    848   -917       C  
ATOM   4662  OE1 GLN A 604       2.820   5.159  11.389  1.00 62.45           O  
ANISOU 4662  OE1 GLN A 604     7086   9376   7267   2195    831   -961       O  
ATOM   4663  NE2 GLN A 604       4.037   4.907  13.254  1.00 61.84           N  
ANISOU 4663  NE2 GLN A 604     7149   9758   6589   1909   1034  -1266       N  
ATOM   4664  N   GLN A 605       3.104  -0.553  13.144  1.00 58.53           N  
ANISOU 4664  N   GLN A 605     6409   9949   5880    785    822    537       N  
ATOM   4665  CA  GLN A 605       2.421  -1.737  12.582  1.00 58.18           C  
ANISOU 4665  CA  GLN A 605     6170   9774   6160    539    720    872       C  
ATOM   4666  C   GLN A 605       1.178  -2.150  13.376  1.00 60.64           C  
ANISOU 4666  C   GLN A 605     6002  10563   6477    394    993   1070       C  
ATOM   4667  O   GLN A 605       0.276  -2.787  12.834  1.00 58.44           O  
ANISOU 4667  O   GLN A 605     5434  10194   6575    233    924   1200       O  
ATOM   4668  CB  GLN A 605       3.380  -2.936  12.439  1.00 57.97           C  
ANISOU 4668  CB  GLN A 605     6378   9445   6205    287    571   1223       C  
ATOM   4669  CG  GLN A 605       3.565  -3.809  13.689  1.00 63.04           C  
ANISOU 4669  CG  GLN A 605     6904  10416   6630     59    787   1687       C  
ATOM   4670  CD  GLN A 605       4.365  -5.080  13.409  1.00 62.78           C  
ANISOU 4670  CD  GLN A 605     7043   9959   6850   -160    625   2077       C  
ATOM   4671  OE1 GLN A 605       4.099  -5.797  12.444  1.00 62.10           O  
ANISOU 4671  OE1 GLN A 605     6928   9420   7248   -294    438   2083       O  
ATOM   4672  NE2 GLN A 605       5.341  -5.368  14.266  1.00 62.69           N  
ANISOU 4672  NE2 GLN A 605     7178  10117   6523   -178    687   2371       N  
ATOM   4673  N   HIS A 606       1.138  -1.812  14.660  1.00 63.87           N  
ANISOU 4673  N   HIS A 606     6286  11525   6456    440   1306   1076       N  
ATOM   4674  CA  HIS A 606      -0.066  -2.043  15.438  1.00 73.27           C  
ANISOU 4674  CA  HIS A 606     6980  13270   7589    351   1632   1249       C  
ATOM   4675  C   HIS A 606      -1.212  -1.232  14.838  1.00 72.97           C  
ANISOU 4675  C   HIS A 606     6642  13240   7845    581   1634    873       C  
ATOM   4676  O   HIS A 606      -2.360  -1.684  14.836  1.00 76.95           O  
ANISOU 4676  O   HIS A 606     6684  13955   8599    445   1754   1048       O  
ATOM   4677  CB  HIS A 606       0.139  -1.690  16.917  1.00 82.22           C  
ANISOU 4677  CB  HIS A 606     8034  15130   8076    430   1980   1238       C  
ATOM   4678  CG  HIS A 606       0.981  -2.679  17.670  1.00 87.03           C  
ANISOU 4678  CG  HIS A 606     8775  15923   8368    193   2023   1795       C  
ATOM   4679  ND1 HIS A 606       1.445  -2.441  18.948  1.00 92.60           N  
ANISOU 4679  ND1 HIS A 606     9472  17340   8371    274   2247   1817       N  
ATOM   4680  CD2 HIS A 606       1.450  -3.902  17.322  1.00 86.41           C  
ANISOU 4680  CD2 HIS A 606     8818  15422   8590    -91   1858   2347       C  
ATOM   4681  CE1 HIS A 606       2.150  -3.480  19.360  1.00 93.63           C  
ANISOU 4681  CE1 HIS A 606     9705  17510   8359     61   2213   2449       C  
ATOM   4682  NE2 HIS A 606       2.172  -4.378  18.390  1.00 91.05           N  
ANISOU 4682  NE2 HIS A 606     9464  16444   8687   -159   1991   2780       N  
ATOM   4683  N   LEU A 607      -0.897  -0.051  14.306  1.00 67.36           N  
ANISOU 4683  N   LEU A 607     6157  12274   7164    929   1497    401       N  
ATOM   4684  CA  LEU A 607      -1.912   0.791  13.669  1.00 67.84           C  
ANISOU 4684  CA  LEU A 607     5943  12291   7541   1222   1467     99       C  
ATOM   4685  C   LEU A 607      -2.314   0.303  12.269  1.00 63.10           C  
ANISOU 4685  C   LEU A 607     5290  11296   7388   1151   1103    232       C  
ATOM   4686  O   LEU A 607      -3.495   0.348  11.918  1.00 64.74           O  
ANISOU 4686  O   LEU A 607     5056  11672   7869   1214   1093    202       O  
ATOM   4687  CB  LEU A 607      -1.454   2.260  13.608  1.00 67.79           C  
ANISOU 4687  CB  LEU A 607     6165  12087   7504   1639   1471   -392       C  
ATOM   4688  CG  LEU A 607      -1.598   3.085  14.900  1.00 71.62           C  
ANISOU 4688  CG  LEU A 607     6493  13058   7663   1838   1850   -791       C  
ATOM   4689  CD1 LEU A 607      -0.973   4.474  14.742  1.00 69.18           C  
ANISOU 4689  CD1 LEU A 607     6447  12354   7485   2194   1807  -1312       C  
ATOM   4690  CD2 LEU A 607      -3.060   3.200  15.313  1.00 74.42           C  
ANISOU 4690  CD2 LEU A 607     6257  13919   8101   1958   2135   -858       C  
ATOM   4691  N   PHE A 608      -1.349  -0.166  11.480  1.00 56.46           N  
ANISOU 4691  N   PHE A 608     4857   9999   6596   1033    801    341       N  
ATOM   4692  CA  PHE A 608      -1.590  -0.425  10.057  1.00 56.79           C  
ANISOU 4692  CA  PHE A 608     4899   9728   6950   1051    425    334       C  
ATOM   4693  C   PHE A 608      -1.094  -1.789   9.542  1.00 59.07           C  
ANISOU 4693  C   PHE A 608     5333   9735   7377    680    198    549       C  
ATOM   4694  O   PHE A 608      -0.854  -1.950   8.338  1.00 57.12           O  
ANISOU 4694  O   PHE A 608     5236   9216   7252    728   -135    453       O  
ATOM   4695  CB  PHE A 608      -0.953   0.694   9.231  1.00 51.85           C  
ANISOU 4695  CB  PHE A 608     4614   8792   6293   1433    250    134       C  
ATOM   4696  CG  PHE A 608      -1.197   2.068   9.785  1.00 51.49           C  
ANISOU 4696  CG  PHE A 608     4496   8847   6220   1804    484   -115       C  
ATOM   4697  CD1 PHE A 608      -2.464   2.620   9.767  1.00 59.15           C  
ANISOU 4697  CD1 PHE A 608     5009  10068   7396   2046    565   -229       C  
ATOM   4698  CD2 PHE A 608      -0.164   2.804  10.331  1.00 48.78           C  
ANISOU 4698  CD2 PHE A 608     4499   8331   5703   1913    618   -282       C  
ATOM   4699  CE1 PHE A 608      -2.692   3.885  10.279  1.00 61.71           C  
ANISOU 4699  CE1 PHE A 608     5248  10418   7782   2422    796   -516       C  
ATOM   4700  CE2 PHE A 608      -0.386   4.069  10.837  1.00 52.05           C  
ANISOU 4700  CE2 PHE A 608     4826   8760   6189   2247    830   -612       C  
ATOM   4701  CZ  PHE A 608      -1.645   4.608  10.815  1.00 58.24           C  
ANISOU 4701  CZ  PHE A 608     5178   9745   7207   2515    930   -734       C  
ATOM   4702  N   GLY A 609      -0.972  -2.765  10.443  1.00 61.71           N  
ANISOU 4702  N   GLY A 609     5592  10153   7702    334    389    843       N  
ATOM   4703  CA  GLY A 609      -0.534  -4.118  10.084  1.00 60.35           C  
ANISOU 4703  CA  GLY A 609     5514   9628   7790    -19    219   1062       C  
ATOM   4704  C   GLY A 609      -1.676  -4.955   9.551  1.00 65.09           C  
ANISOU 4704  C   GLY A 609     5645  10205   8880   -287     88   1066       C  
ATOM   4705  O   GLY A 609      -2.782  -4.447   9.371  1.00 67.84           O  
ANISOU 4705  O   GLY A 609     5598  10855   9323   -172     94    908       O  
ATOM   4706  N   SER A 610      -1.426  -6.241   9.307  1.00 69.29           N  
ANISOU 4706  N   SER A 610     6179  10359   9789   -643    -35   1220       N  
ATOM   4707  CA  SER A 610      -2.435  -7.125   8.698  1.00 77.80           C  
ANISOU 4707  CA  SER A 610     6796  11317  11448   -957   -215   1123       C  
ATOM   4708  C   SER A 610      -3.698  -7.352   9.561  1.00 87.67           C  
ANISOU 4708  C   SER A 610     7431  12933  12947  -1202     96   1397       C  
ATOM   4709  O   SER A 610      -4.687  -7.904   9.076  1.00 88.61           O  
ANISOU 4709  O   SER A 610     7066  13027  13573  -1455    -47   1270       O  
ATOM   4710  CB  SER A 610      -1.809  -8.463   8.278  1.00 77.37           C  
ANISOU 4710  CB  SER A 610     6884  10667  11848  -1285   -398   1166       C  
ATOM   4711  OG  SER A 610      -1.521  -9.281   9.393  1.00 79.27           O  
ANISOU 4711  OG  SER A 610     7091  10754  12273  -1574    -82   1731       O  
ATOM   4712  N   ASN A 611      -3.649  -6.938  10.829  1.00 95.30           N  
ANISOU 4712  N   ASN A 611     8383  14284  13542  -1131    520   1742       N  
ATOM   4713  CA  ASN A 611      -4.831  -6.861  11.691  1.00107.23           C  
ANISOU 4713  CA  ASN A 611     9310  16317  15116  -1246    887   1971       C  
ATOM   4714  C   ASN A 611      -5.953  -6.100  10.987  1.00106.65           C  
ANISOU 4714  C   ASN A 611     8834  16526  15163  -1029    728   1542       C  
ATOM   4715  O   ASN A 611      -7.092  -6.563  10.932  1.00110.58           O  
ANISOU 4715  O   ASN A 611     8722  17181  16114  -1287    765   1590       O  
ATOM   4716  CB  ASN A 611      -4.450  -6.183  13.024  1.00115.13           C  
ANISOU 4716  CB  ASN A 611    10450  17826  15468  -1034   1321   2209       C  
ATOM   4717  CG  ASN A 611      -5.662  -5.860  13.919  1.00130.16           C  
ANISOU 4717  CG  ASN A 611    11750  20417  17288  -1035   1750   2348       C  
ATOM   4718  OD1 ASN A 611      -6.802  -6.150  13.565  1.00134.11           O  
ANISOU 4718  OD1 ASN A 611    11699  20994  18264  -1214   1733   2319       O  
ATOM   4719  ND2 ASN A 611      -5.414  -5.247  15.083  1.00141.14           N  
ANISOU 4719  ND2 ASN A 611    13209  22364  18054   -827   2134   2450       N  
ATOM   4720  N   VAL A 612      -5.610  -4.947  10.423  1.00101.63           N  
ANISOU 4720  N   VAL A 612     8512  15932  14172   -556    540   1159       N  
ATOM   4721  CA  VAL A 612      -6.596  -4.056   9.813  1.00103.14           C  
ANISOU 4721  CA  VAL A 612     8347  16419  14424   -234    401    824       C  
ATOM   4722  C   VAL A 612      -7.228  -4.631   8.537  1.00106.11           C  
ANISOU 4722  C   VAL A 612     8417  16646  15253   -391    -66    585       C  
ATOM   4723  O   VAL A 612      -6.533  -5.186   7.685  1.00104.26           O  
ANISOU 4723  O   VAL A 612     8513  16007  15093   -499   -412    449       O  
ATOM   4724  CB  VAL A 612      -5.962  -2.688   9.490  1.00 97.14           C  
ANISOU 4724  CB  VAL A 612     8029  15631  13250    320    318    560       C  
ATOM   4725  CG1 VAL A 612      -6.948  -1.799   8.755  1.00 99.42           C  
ANISOU 4725  CG1 VAL A 612     7949  16160  13666    700    135    299       C  
ATOM   4726  CG2 VAL A 612      -5.482  -2.017  10.771  1.00 96.59           C  
ANISOU 4726  CG2 VAL A 612     8157  15780  12761    485    757    637       C  
ATOM   4727  N   THR A 613      -8.550  -4.497   8.426  1.00111.12           N  
ANISOU 4727  N   THR A 613     8382  17665  16173   -393    -73    492       N  
ATOM   4728  CA  THR A 613      -9.282  -4.830   7.201  1.00114.25           C  
ANISOU 4728  CA  THR A 613     8393  18088  16929   -464   -563    174       C  
ATOM   4729  C   THR A 613     -10.058  -3.593   6.728  1.00116.59           C  
ANISOU 4729  C   THR A 613     8399  18828  17073     81   -695    -31       C  
ATOM   4730  O   THR A 613      -9.906  -2.510   7.302  1.00114.94           O  
ANISOU 4730  O   THR A 613     8361  18764  16545    503   -406     38       O  
ATOM   4731  CB  THR A 613     -10.224  -6.040   7.408  1.00120.16           C  
ANISOU 4731  CB  THR A 613     8469  18852  18335  -1064   -524    260       C  
ATOM   4732  OG1 THR A 613     -11.226  -5.720   8.383  1.00123.01           O  
ANISOU 4732  OG1 THR A 613     8249  19700  18789  -1071    -81    494       O  
ATOM   4733  CG2 THR A 613      -9.432  -7.256   7.868  1.00119.61           C  
ANISOU 4733  CG2 THR A 613     8686  18245  18515  -1565   -382    542       C  
ATOM   4734  N   ASP A 614     -10.888  -3.756   5.696  1.00120.97           N  
ANISOU 4734  N   ASP A 614     8486  19594  17884     87  -1141   -299       N  
ATOM   4735  CA  ASP A 614     -11.457  -2.626   4.951  1.00121.34           C  
ANISOU 4735  CA  ASP A 614     8326  20016  17761    673  -1403   -453       C  
ATOM   4736  C   ASP A 614     -10.323  -1.648   4.657  1.00114.06           C  
ANISOU 4736  C   ASP A 614     8156  18842  16339   1165  -1421   -395       C  
ATOM   4737  O   ASP A 614     -10.357  -0.472   5.032  1.00112.02           O  
ANISOU 4737  O   ASP A 614     7974  18667  15924   1645  -1188   -302       O  
ATOM   4738  CB  ASP A 614     -12.616  -1.954   5.707  1.00125.77           C  
ANISOU 4738  CB  ASP A 614     8245  21042  18501    889  -1064   -363       C  
ATOM   4739  CG  ASP A 614     -13.560  -1.176   4.777  1.00129.37           C  
ANISOU 4739  CG  ASP A 614     8203  21936  19018   1376  -1450   -523       C  
ATOM   4740  OD1 ASP A 614     -13.155  -0.825   3.646  1.00127.16           O  
ANISOU 4740  OD1 ASP A 614     8216  21619  18480   1691  -1910   -617       O  
ATOM   4741  OD2 ASP A 614     -14.716  -0.917   5.177  1.00133.77           O  
ANISOU 4741  OD2 ASP A 614     8039  22923  19862   1466  -1286   -518       O  
ATOM   4742  N   CYS A 615      -9.306  -2.177   3.990  1.00109.63           N  
ANISOU 4742  N   CYS A 615     8122  17938  15594   1022  -1681   -473       N  
ATOM   4743  CA  CYS A 615      -8.085  -1.439   3.723  1.00105.51           C  
ANISOU 4743  CA  CYS A 615     8319  17125  14644   1375  -1670   -382       C  
ATOM   4744  C   CYS A 615      -8.283  -0.280   2.763  1.00106.77           C  
ANISOU 4744  C   CYS A 615     8471  17511  14585   1990  -1940   -364       C  
ATOM   4745  O   CYS A 615      -7.529   0.685   2.797  1.00104.95           O  
ANISOU 4745  O   CYS A 615     8696  17057  14124   2365  -1796   -202       O  
ATOM   4746  CB  CYS A 615      -7.013  -2.386   3.195  1.00103.59           C  
ANISOU 4746  CB  CYS A 615     8552  16518  14291   1066  -1875   -484       C  
ATOM   4747  SG  CYS A 615      -6.354  -3.412   4.508  1.00103.37           S  
ANISOU 4747  SG  CYS A 615     8747  16073  14454    512  -1450   -299       S  
ATOM   4748  N   SER A 616      -9.283  -0.385   1.896  1.00111.54           N  
ANISOU 4748  N   SER A 616     8531  18558  15289   2089  -2344   -506       N  
ATOM   4749  CA  SER A 616      -9.690   0.742   1.075  1.00113.71           C  
ANISOU 4749  CA  SER A 616     8661  19145  15398   2724  -2587   -378       C  
ATOM   4750  C   SER A 616     -10.307   1.787   1.997  1.00114.05           C  
ANISOU 4750  C   SER A 616     8441  19213  15679   3074  -2184   -211       C  
ATOM   4751  O   SER A 616     -11.083   1.449   2.891  1.00116.67           O  
ANISOU 4751  O   SER A 616     8313  19696  16322   2824  -1918   -297       O  
ATOM   4752  CB  SER A 616     -10.698   0.295   0.019  1.00120.36           C  
ANISOU 4752  CB  SER A 616     8885  20570  16276   2727  -3142   -595       C  
ATOM   4753  OG  SER A 616     -10.979   1.339  -0.893  1.00123.79           O  
ANISOU 4753  OG  SER A 616     9215  21357  16464   3382  -3429   -378       O  
ATOM   4754  N   GLY A 617      -9.942   3.049   1.797  1.00111.40           N  
ANISOU 4754  N   GLY A 617     8385  18710  15233   3651  -2106     22       N  
ATOM   4755  CA  GLY A 617     -10.343   4.113   2.708  1.00111.70           C  
ANISOU 4755  CA  GLY A 617     8261  18640  15540   4019  -1684     91       C  
ATOM   4756  C   GLY A 617      -9.350   4.213   3.846  1.00106.36           C  
ANISOU 4756  C   GLY A 617     8119  17491  14803   3810  -1197     31       C  
ATOM   4757  O   GLY A 617      -8.801   5.285   4.107  1.00106.37           O  
ANISOU 4757  O   GLY A 617     8447  17128  14839   4181   -970    102       O  
ATOM   4758  N   ASN A 618      -9.117   3.094   4.527  1.00102.67           N  
ANISOU 4758  N   ASN A 618     7710  17025  14274   3217  -1046    -93       N  
ATOM   4759  CA  ASN A 618      -8.030   3.006   5.499  1.00 96.90           C  
ANISOU 4759  CA  ASN A 618     7516  15929  13374   2980   -674   -113       C  
ATOM   4760  C   ASN A 618      -6.668   2.932   4.799  1.00 90.18           C  
ANISOU 4760  C   ASN A 618     7347  14673  12246   2946   -875    -18       C  
ATOM   4761  O   ASN A 618      -6.580   2.710   3.589  1.00 87.46           O  
ANISOU 4761  O   ASN A 618     7055  14386  11791   3016  -1287     46       O  
ATOM   4762  CB  ASN A 618      -8.216   1.785   6.411  1.00 96.37           C  
ANISOU 4762  CB  ASN A 618     7263  16016  13336   2383   -457   -146       C  
ATOM   4763  CG  ASN A 618      -9.520   1.826   7.193  1.00100.05           C  
ANISOU 4763  CG  ASN A 618     7023  16938  14052   2380   -175   -199       C  
ATOM   4764  OD1 ASN A 618     -10.011   2.895   7.551  1.00100.80           O  
ANISOU 4764  OD1 ASN A 618     6904  17160  14236   2834     40   -290       O  
ATOM   4765  ND2 ASN A 618     -10.083   0.655   7.464  1.00101.72           N  
ANISOU 4765  ND2 ASN A 618     6842  17370  14436   1868   -151   -144       N  
ATOM   4766  N   PHE A 619      -5.605   3.144   5.564  1.00 86.35           N  
ANISOU 4766  N   PHE A 619     7347  13846  11616   2858   -582    -30       N  
ATOM   4767  CA  PHE A 619      -4.264   2.871   5.082  1.00 79.84           C  
ANISOU 4767  CA  PHE A 619     7119  12667  10550   2727   -714     51       C  
ATOM   4768  C   PHE A 619      -3.811   1.545   5.657  1.00 76.28           C  
ANISOU 4768  C   PHE A 619     6787  12189  10005   2169   -646     28       C  
ATOM   4769  O   PHE A 619      -3.800   1.370   6.871  1.00 75.64           O  
ANISOU 4769  O   PHE A 619     6659  12168   9911   1974   -306     10       O  
ATOM   4770  CB  PHE A 619      -3.278   3.954   5.500  1.00 76.76           C  
ANISOU 4770  CB  PHE A 619     7164  11885  10117   2975   -471     56       C  
ATOM   4771  CG  PHE A 619      -1.865   3.640   5.113  1.00 71.02           C  
ANISOU 4771  CG  PHE A 619     6995  10828   9161   2807   -562    146       C  
ATOM   4772  CD1 PHE A 619      -1.460   3.757   3.792  1.00 69.11           C  
ANISOU 4772  CD1 PHE A 619     6943  10506   8810   2986   -863    325       C  
ATOM   4773  CD2 PHE A 619      -0.952   3.185   6.057  1.00 67.84           C  
ANISOU 4773  CD2 PHE A 619     6885  10277   8613   2485   -348     73       C  
ATOM   4774  CE1 PHE A 619      -0.167   3.449   3.421  1.00 65.50           C  
ANISOU 4774  CE1 PHE A 619     6952   9794   8141   2843   -912    398       C  
ATOM   4775  CE2 PHE A 619       0.344   2.876   5.694  1.00 63.06           C  
ANISOU 4775  CE2 PHE A 619     6737   9391   7832   2348   -434    154       C  
ATOM   4776  CZ  PHE A 619       0.738   3.009   4.374  1.00 62.17           C  
ANISOU 4776  CZ  PHE A 619     6804   9170   7650   2523   -699    301       C  
ATOM   4777  N   CYS A 620      -3.435   0.622   4.777  1.00 75.27           N  
ANISOU 4777  N   CYS A 620     6798  11989   9812   1943   -966     33       N  
ATOM   4778  CA  CYS A 620      -2.938  -0.680   5.178  1.00 74.30           C  
ANISOU 4778  CA  CYS A 620     6799  11719   9711   1446   -935     40       C  
ATOM   4779  C   CYS A 620      -1.504  -0.855   4.696  1.00 67.39           C  
ANISOU 4779  C   CYS A 620     6501  10492   8611   1431  -1036     67       C  
ATOM   4780  O   CYS A 620      -1.218  -0.745   3.506  1.00 62.49           O  
ANISOU 4780  O   CYS A 620     6022   9860   7859   1612  -1330     12       O  
ATOM   4781  CB  CYS A 620      -3.838  -1.775   4.622  1.00 81.34           C  
ANISOU 4781  CB  CYS A 620     7253  12787  10867   1143  -1208    -80       C  
ATOM   4782  SG  CYS A 620      -5.306  -2.080   5.629  1.00 90.85           S  
ANISOU 4782  SG  CYS A 620     7749  14346  12426    907   -951    -31       S  
ATOM   4783  N   LEU A 621      -0.608  -1.143   5.632  1.00 64.94           N  
ANISOU 4783  N   LEU A 621     6484   9968   8223   1230   -786    166       N  
ATOM   4784  CA  LEU A 621       0.820  -1.069   5.363  1.00 62.70           C  
ANISOU 4784  CA  LEU A 621     6718   9371   7734   1273   -813    205       C  
ATOM   4785  C   LEU A 621       1.325  -2.210   4.485  1.00 62.87           C  
ANISOU 4785  C   LEU A 621     6876   9222   7790   1066  -1084    133       C  
ATOM   4786  O   LEU A 621       2.018  -1.970   3.502  1.00 64.42           O  
ANISOU 4786  O   LEU A 621     7337   9337   7804   1257  -1257     80       O  
ATOM   4787  CB  LEU A 621       1.597  -1.032   6.683  1.00 61.76           C  
ANISOU 4787  CB  LEU A 621     6804   9160   7502   1138   -497    313       C  
ATOM   4788  CG  LEU A 621       3.107  -0.787   6.634  1.00 57.11           C  
ANISOU 4788  CG  LEU A 621     6690   8285   6723   1192   -481    346       C  
ATOM   4789  CD1 LEU A 621       3.423   0.520   5.932  1.00 55.84           C  
ANISOU 4789  CD1 LEU A 621     6698   8014   6505   1567   -518    290       C  
ATOM   4790  CD2 LEU A 621       3.682  -0.797   8.045  1.00 53.03           C  
ANISOU 4790  CD2 LEU A 621     6261   7826   6061   1051   -210    420       C  
ATOM   4791  N   PHE A 622       0.974  -3.444   4.827  1.00 63.82           N  
ANISOU 4791  N   PHE A 622     6791   9282   8175    685  -1100    128       N  
ATOM   4792  CA  PHE A 622       1.576  -4.605   4.169  1.00 64.67           C  
ANISOU 4792  CA  PHE A 622     7042   9112   8418    471  -1310      0       C  
ATOM   4793  C   PHE A 622       0.863  -5.071   2.913  1.00 69.06           C  
ANISOU 4793  C   PHE A 622     7341   9806   9092    460  -1685   -346       C  
ATOM   4794  O   PHE A 622       1.306  -6.028   2.288  1.00 70.82           O  
ANISOU 4794  O   PHE A 622     7650   9810   9449    303  -1877   -579       O  
ATOM   4795  CB  PHE A 622       1.693  -5.777   5.141  1.00 66.63           C  
ANISOU 4795  CB  PHE A 622     7212   9103   9001     61  -1140    197       C  
ATOM   4796  CG  PHE A 622       2.297  -5.408   6.456  1.00 66.50           C  
ANISOU 4796  CG  PHE A 622     7373   9104   8789     64   -798    537       C  
ATOM   4797  CD1 PHE A 622       3.386  -4.541   6.523  1.00 64.49           C  
ANISOU 4797  CD1 PHE A 622     7513   8822   8170    326   -730    553       C  
ATOM   4798  CD2 PHE A 622       1.786  -5.927   7.632  1.00 69.47           C  
ANISOU 4798  CD2 PHE A 622     7487   9577   9331   -202   -542    843       C  
ATOM   4799  CE1 PHE A 622       3.942  -4.194   7.735  1.00 62.65           C  
ANISOU 4799  CE1 PHE A 622     7401   8676   7726    323   -463    770       C  
ATOM   4800  CE2 PHE A 622       2.345  -5.586   8.850  1.00 69.94           C  
ANISOU 4800  CE2 PHE A 622     7686   9793   9095   -172   -250   1126       C  
ATOM   4801  CZ  PHE A 622       3.426  -4.715   8.900  1.00 65.10           C  
ANISOU 4801  CZ  PHE A 622     7461   9172   8103     92   -235   1041       C  
ATOM   4802  N   ARG A 623      -0.232  -4.423   2.535  1.00 73.10           N  
ANISOU 4802  N   ARG A 623     7509  10702   9562    641  -1808   -424       N  
ATOM   4803  CA  ARG A 623      -0.855  -4.744   1.253  1.00 79.36           C  
ANISOU 4803  CA  ARG A 623     8045  11761  10348    692  -2226   -784       C  
ATOM   4804  C   ARG A 623      -0.491  -3.665   0.250  1.00 76.52           C  
ANISOU 4804  C   ARG A 623     7906  11683   9484   1187  -2377   -752       C  
ATOM   4805  O   ARG A 623      -0.730  -2.482   0.467  1.00 74.27           O  
ANISOU 4805  O   ARG A 623     7616  11547   9058   1511  -2241   -490       O  
ATOM   4806  CB  ARG A 623      -2.385  -4.981   1.319  1.00 87.45           C  
ANISOU 4806  CB  ARG A 623     8429  13090  11709    528  -2354   -915       C  
ATOM   4807  CG  ARG A 623      -3.074  -4.697   2.641  1.00 91.08           C  
ANISOU 4807  CG  ARG A 623     8616  13582  12408    407  -1983   -610       C  
ATOM   4808  CD  ARG A 623      -2.730  -5.739   3.711  1.00 93.63           C  
ANISOU 4808  CD  ARG A 623     8979  13510  13084    -58  -1700   -421       C  
ATOM   4809  NE  ARG A 623      -2.411  -5.074   4.974  1.00 92.86           N  
ANISOU 4809  NE  ARG A 623     9052  13431  12800     36  -1265    -47       N  
ATOM   4810  CZ  ARG A 623      -3.244  -4.905   6.000  1.00 96.93           C  
ANISOU 4810  CZ  ARG A 623     9199  14189  13441    -60   -960    159       C  
ATOM   4811  NH1 ARG A 623      -4.492  -5.377   5.984  1.00101.12           N  
ANISOU 4811  NH1 ARG A 623     9132  14928  14362   -292  -1007    102       N  
ATOM   4812  NH2 ARG A 623      -2.809  -4.253   7.068  1.00 96.20           N  
ANISOU 4812  NH2 ARG A 623     9309  14176  13068     74   -595    392       N  
ATOM   4813  N   SER A 624       0.159  -4.099  -0.819  1.00 77.34           N  
ANISOU 4813  N   SER A 624     8211  11830   9344   1250  -2624  -1001       N  
ATOM   4814  CA  SER A 624       0.307  -3.313  -2.025  1.00 79.56           C  
ANISOU 4814  CA  SER A 624     8582  12533   9114   1694  -2840   -981       C  
ATOM   4815  C   SER A 624      -0.468  -4.070  -3.114  1.00 84.16           C  
ANISOU 4815  C   SER A 624     8787  13563   9628   1636  -3307  -1482       C  
ATOM   4816  O   SER A 624      -1.055  -5.128  -2.848  1.00 84.26           O  
ANISOU 4816  O   SER A 624     8489  13435  10090   1226  -3423  -1841       O  
ATOM   4817  CB  SER A 624       1.800  -3.157  -2.354  1.00 76.85           C  
ANISOU 4817  CB  SER A 624     8767  11981   8451   1835  -2699   -863       C  
ATOM   4818  OG  SER A 624       2.046  -3.083  -3.746  1.00 81.89           O  
ANISOU 4818  OG  SER A 624     9453  13069   8591   2119  -2971  -1015       O  
ATOM   4819  N   GLU A 625      -0.498  -3.533  -4.325  1.00 86.40           N  
ANISOU 4819  N   GLU A 625     9056  14405   9367   2035  -3579  -1504       N  
ATOM   4820  CA  GLU A 625      -1.108  -4.264  -5.426  1.00 95.77           C  
ANISOU 4820  CA  GLU A 625     9894  16126  10370   2002  -4064  -2076       C  
ATOM   4821  C   GLU A 625      -0.038  -4.953  -6.279  1.00 96.23           C  
ANISOU 4821  C   GLU A 625    10270  16218  10074   2009  -4166  -2470       C  
ATOM   4822  O   GLU A 625       0.577  -4.339  -7.155  1.00 96.42           O  
ANISOU 4822  O   GLU A 625    10525  16660   9448   2416  -4198  -2287       O  
ATOM   4823  CB  GLU A 625      -2.069  -3.379  -6.246  1.00104.03           C  
ANISOU 4823  CB  GLU A 625    10571  17951  11004   2441  -4381  -1915       C  
ATOM   4824  CG  GLU A 625      -1.484  -2.486  -7.362  1.00107.20           C  
ANISOU 4824  CG  GLU A 625    11215  18895  10622   3004  -4467  -1575       C  
ATOM   4825  CD  GLU A 625      -0.529  -1.422  -6.859  1.00103.20           C  
ANISOU 4825  CD  GLU A 625    11189  17943  10079   3243  -3998   -877       C  
ATOM   4826  OE1 GLU A 625       0.475  -1.161  -7.556  1.00103.70           O  
ANISOU 4826  OE1 GLU A 625    11601  18145   9654   3478  -3924   -695       O  
ATOM   4827  OE2 GLU A 625      -0.782  -0.847  -5.776  1.00100.32           O  
ANISOU 4827  OE2 GLU A 625    10821  17117  10178   3190  -3699   -546       O  
ATOM   4828  N   THR A 626       0.208  -6.227  -5.972  1.00 49.85           N  
ANISOU 4828  N   THR A 626     6021   6163   6757  -1046   -390   1190       N  
ATOM   4829  CA  THR A 626       1.091  -7.097  -6.784  1.00 48.31           C  
ANISOU 4829  CA  THR A 626     6003   5901   6452  -1121   -479   1138       C  
ATOM   4830  C   THR A 626       2.570  -6.665  -6.923  1.00 40.95           C  
ANISOU 4830  C   THR A 626     5194   4923   5444  -1043   -442   1008       C  
ATOM   4831  O   THR A 626       3.321  -7.321  -7.652  1.00 39.54           O  
ANISOU 4831  O   THR A 626     5142   4701   5181  -1092   -497    946       O  
ATOM   4832  CB  THR A 626       0.520  -7.308  -8.236  1.00 47.38           C  
ANISOU 4832  CB  THR A 626     5886   5784   6333  -1245   -628   1208       C  
ATOM   4833  OG1 THR A 626       0.750  -6.138  -9.022  1.00 44.62           O  
ANISOU 4833  OG1 THR A 626     5504   5448   5999  -1207   -654   1227       O  
ATOM   4834  CG2 THR A 626      -0.970  -7.608  -8.215  1.00 47.79           C  
ANISOU 4834  CG2 THR A 626     5791   5885   6483  -1332   -685   1354       C  
ATOM   4835  N   LYS A 627       2.985  -5.596  -6.236  1.00 33.54           N  
ANISOU 4835  N   LYS A 627     4209   3992   4543   -927   -349    952       N  
ATOM   4836  CA  LYS A 627       4.305  -4.996  -6.464  1.00 31.87           C  
ANISOU 4836  CA  LYS A 627     4081   3737   4290   -866   -329    854       C  
ATOM   4837  C   LYS A 627       5.171  -4.854  -5.209  1.00 34.89           C  
ANISOU 4837  C   LYS A 627     4494   4127   4635   -778   -232    746       C  
ATOM   4838  O   LYS A 627       6.211  -4.199  -5.251  1.00 37.35           O  
ANISOU 4838  O   LYS A 627     4846   4405   4940   -723   -213    667       O  
ATOM   4839  CB  LYS A 627       4.150  -3.632  -7.132  1.00 31.47           C  
ANISOU 4839  CB  LYS A 627     3944   3662   4349   -833   -353    899       C  
ATOM   4840  CG  LYS A 627       4.053  -3.694  -8.640  1.00 34.08           C  
ANISOU 4840  CG  LYS A 627     4300   4010   4640   -932   -468    992       C  
ATOM   4841  CD  LYS A 627       3.650  -2.336  -9.232  1.00 37.00           C  
ANISOU 4841  CD  LYS A 627     4543   4359   5157   -912   -514   1111       C  
ATOM   4842  CE  LYS A 627       3.038  -2.468 -10.635  1.00 38.23           C  
ANISOU 4842  CE  LYS A 627     4673   4587   5266  -1041   -653   1267       C  
ATOM   4843  NZ  LYS A 627       4.076  -2.389 -11.713  1.00 38.38           N  
ANISOU 4843  NZ  LYS A 627     4788   4659   5134  -1104   -697   1269       N  
ATOM   4844  N   ASP A 628       4.758  -5.459  -4.102  1.00 33.89           N  
ANISOU 4844  N   ASP A 628     4340   4064   4473   -778   -179    757       N  
ATOM   4845  CA  ASP A 628       5.591  -5.512  -2.912  1.00 32.89           C  
ANISOU 4845  CA  ASP A 628     4247   3985   4265   -723   -110    676       C  
ATOM   4846  C   ASP A 628       6.188  -4.167  -2.556  1.00 29.52           C  
ANISOU 4846  C   ASP A 628     3789   3552   3874   -631    -53    550       C  
ATOM   4847  O   ASP A 628       7.391  -4.059  -2.362  1.00 30.41           O  
ANISOU 4847  O   ASP A 628     3975   3644   3936   -602    -55    473       O  
ATOM   4848  CB  ASP A 628       6.740  -6.483  -3.130  1.00 33.73           C  
ANISOU 4848  CB  ASP A 628     4484   4032   4299   -748   -161    664       C  
ATOM   4849  CG  ASP A 628       6.279  -7.835  -3.536  1.00 34.55           C  
ANISOU 4849  CG  ASP A 628     4628   4091   4408   -839   -230    756       C  
ATOM   4850  OD1 ASP A 628       5.338  -8.354  -2.903  1.00 32.86           O  
ANISOU 4850  OD1 ASP A 628     4348   3937   4201   -887   -220    855       O  
ATOM   4851  OD2 ASP A 628       6.878  -8.378  -4.488  1.00 39.37           O  
ANISOU 4851  OD2 ASP A 628     5327   4609   5021   -865   -291    719       O  
ATOM   4852  N   LEU A 629       5.352  -3.148  -2.463  1.00 29.60           N  
ANISOU 4852  N   LEU A 629     3677   3567   4001   -584     -9    526       N  
ATOM   4853  CA  LEU A 629       5.847  -1.801  -2.246  1.00 29.33           C  
ANISOU 4853  CA  LEU A 629     3603   3478   4065   -500     28    396       C  
ATOM   4854  C   LEU A 629       6.147  -1.588  -0.770  1.00 28.64           C  
ANISOU 4854  C   LEU A 629     3497   3499   3884   -450    125    243       C  
ATOM   4855  O   LEU A 629       5.295  -1.793   0.082  1.00 22.53           O  
ANISOU 4855  O   LEU A 629     2643   2858   3061   -445    206    229       O  
ATOM   4856  CB  LEU A 629       4.850  -0.761  -2.765  1.00 31.18           C  
ANISOU 4856  CB  LEU A 629     3696   3636   4514   -459     26    428       C  
ATOM   4857  CG  LEU A 629       4.432  -0.896  -4.235  1.00 28.68           C  
ANISOU 4857  CG  LEU A 629     3376   3254   4268   -528    -87    606       C  
ATOM   4858  CD1 LEU A 629       3.157  -0.109  -4.451  1.00 31.19           C  
ANISOU 4858  CD1 LEU A 629     3516   3534   4799   -490    -88    677       C  
ATOM   4859  CD2 LEU A 629       5.524  -0.436  -5.188  1.00 25.50           C  
ANISOU 4859  CD2 LEU A 629     3051   2762   3876   -547   -161    627       C  
ATOM   4860  N   LEU A 630       7.385  -1.171  -0.503  1.00 36.40           N  
ANISOU 4860  N   LEU A 630     4548   4451   4832   -426    113    132       N  
ATOM   4861  CA  LEU A 630       7.942  -0.946   0.836  1.00 35.17           C  
ANISOU 4861  CA  LEU A 630     4395   4413   4554   -399    175    -28       C  
ATOM   4862  C   LEU A 630       8.147  -2.254   1.565  1.00 36.53           C  
ANISOU 4862  C   LEU A 630     4626   4745   4508   -461    173     60       C  
ATOM   4863  O   LEU A 630       9.226  -2.496   2.089  1.00 44.15           O  
ANISOU 4863  O   LEU A 630     5657   5758   5359   -474    143     26       O  
ATOM   4864  CB  LEU A 630       7.115   0.050   1.653  1.00 34.28           C  
ANISOU 4864  CB  LEU A 630     4154   4358   4515   -331    283   -201       C  
ATOM   4865  CG  LEU A 630       7.017   1.453   1.037  1.00 35.45           C  
ANISOU 4865  CG  LEU A 630     4226   4301   4942   -259    270   -295       C  
ATOM   4866  CD1 LEU A 630       6.299   2.412   1.963  1.00 36.39           C  
ANISOU 4866  CD1 LEU A 630     4212   4458   5158   -173    388   -522       C  
ATOM   4867  CD2 LEU A 630       8.382   2.024   0.683  1.00 34.63           C  
ANISOU 4867  CD2 LEU A 630     4199   4064   4894   -265    190   -348       C  
ATOM   4868  N   PHE A 631       7.125  -3.098   1.571  1.00 35.77           N  
ANISOU 4868  N   PHE A 631     4493   4720   4377   -505    191    198       N  
ATOM   4869  CA  PHE A 631       7.206  -4.433   2.134  1.00 38.45           C  
ANISOU 4869  CA  PHE A 631     4874   5173   4560   -579    168    340       C  
ATOM   4870  C   PHE A 631       6.643  -5.464   1.176  1.00 39.75           C  
ANISOU 4870  C   PHE A 631     5066   5237   4799   -643     98    521       C  
ATOM   4871  O   PHE A 631       5.831  -5.147   0.311  1.00 43.01           O  
ANISOU 4871  O   PHE A 631     5434   5570   5339   -642     89    546       O  
ATOM   4872  CB  PHE A 631       6.410  -4.477   3.424  1.00 41.69           C  
ANISOU 4872  CB  PHE A 631     5185   5826   4830   -596    274    327       C  
ATOM   4873  CG  PHE A 631       6.946  -3.570   4.478  1.00 47.56           C  
ANISOU 4873  CG  PHE A 631     5905   6709   5458   -551    344    115       C  
ATOM   4874  CD1 PHE A 631       7.897  -4.022   5.379  1.00 49.12           C  
ANISOU 4874  CD1 PHE A 631     6157   7049   5456   -595    310    128       C  
ATOM   4875  CD2 PHE A 631       6.521  -2.256   4.559  1.00 52.03           C  
ANISOU 4875  CD2 PHE A 631     6386   7251   6132   -467    431   -103       C  
ATOM   4876  CE1 PHE A 631       8.405  -3.181   6.354  1.00 51.10           C  
ANISOU 4876  CE1 PHE A 631     6388   7449   5577   -572    359    -88       C  
ATOM   4877  CE2 PHE A 631       7.025  -1.407   5.533  1.00 53.63           C  
ANISOU 4877  CE2 PHE A 631     6571   7570   6237   -432    490   -344       C  
ATOM   4878  CZ  PHE A 631       7.972  -1.874   6.432  1.00 53.31           C  
ANISOU 4878  CZ  PHE A 631     6596   7703   5958   -492    452   -344       C  
ATOM   4879  N   ARG A 632       7.065  -6.710   1.332  1.00 39.47           N  
ANISOU 4879  N   ARG A 632     5097   5200   4701   -705     34    650       N  
ATOM   4880  CA  ARG A 632       6.423  -7.793   0.598  1.00 40.92           C  
ANISOU 4880  CA  ARG A 632     5296   5290   4961   -781    -34    801       C  
ATOM   4881  C   ARG A 632       4.922  -7.832   0.892  1.00 44.52           C  
ANISOU 4881  C   ARG A 632     5629   5855   5432   -828     20    890       C  
ATOM   4882  O   ARG A 632       4.498  -7.588   2.021  1.00 46.94           O  
ANISOU 4882  O   ARG A 632     5845   6356   5634   -824    114    891       O  
ATOM   4883  CB  ARG A 632       7.046  -9.139   0.940  1.00 38.41           C  
ANISOU 4883  CB  ARG A 632     5043   4937   4616   -837   -109    930       C  
ATOM   4884  CG  ARG A 632       8.072  -9.583  -0.059  1.00 37.86           C  
ANISOU 4884  CG  ARG A 632     5081   4672   4631   -816   -191    883       C  
ATOM   4885  CD  ARG A 632       8.827 -10.804   0.401  1.00 38.54           C  
ANISOU 4885  CD  ARG A 632     5208   4700   4736   -842   -262    993       C  
ATOM   4886  NE  ARG A 632       7.931 -11.886   0.807  1.00 39.12           N  
ANISOU 4886  NE  ARG A 632     5237   4778   4848   -940   -302   1185       N  
ATOM   4887  CZ  ARG A 632       8.263 -13.171   0.824  1.00 40.49           C  
ANISOU 4887  CZ  ARG A 632     5439   4811   5134   -984   -395   1310       C  
ATOM   4888  NH1 ARG A 632       9.470 -13.581   0.450  1.00 41.81           N  
ANISOU 4888  NH1 ARG A 632     5674   4824   5387   -925   -449   1249       N  
ATOM   4889  NH2 ARG A 632       7.370 -14.055   1.217  1.00 44.40           N  
ANISOU 4889  NH2 ARG A 632     5878   5310   5683  -1089   -436   1505       N  
ATOM   4890  N   ASP A 633       4.134  -8.163  -0.129  1.00 44.41           N  
ANISOU 4890  N   ASP A 633     5601   5736   5535   -879    -39    962       N  
ATOM   4891  CA  ASP A 633       2.674  -8.125  -0.034  1.00 45.02           C  
ANISOU 4891  CA  ASP A 633     5539   5902   5665   -923      1   1054       C  
ATOM   4892  C   ASP A 633       2.111  -9.129   0.951  1.00 43.61           C  
ANISOU 4892  C   ASP A 633     5294   5859   5415  -1014     23   1225       C  
ATOM   4893  O   ASP A 633       0.995  -8.957   1.431  1.00 46.36           O  
ANISOU 4893  O   ASP A 633     5494   6356   5764  -1037    103   1290       O  
ATOM   4894  CB  ASP A 633       2.030  -8.381  -1.399  1.00 45.95           C  
ANISOU 4894  CB  ASP A 633     5662   5883   5915   -984   -103   1113       C  
ATOM   4895  CG  ASP A 633       2.320  -7.286  -2.398  1.00 45.55           C  
ANISOU 4895  CG  ASP A 633     5632   5745   5931   -914   -124   1002       C  
ATOM   4896  OD1 ASP A 633       2.500  -6.120  -1.971  1.00 42.34           O  
ANISOU 4896  OD1 ASP A 633     5170   5380   5535   -813    -39    895       O  
ATOM   4897  OD2 ASP A 633       2.363  -7.609  -3.612  1.00 46.68           O  
ANISOU 4897  OD2 ASP A 633     5840   5780   6115   -972   -231   1023       O  
ATOM   4898  N   ASP A 634       2.866 -10.181   1.237  1.00 40.72           N  
ANISOU 4898  N   ASP A 634     5021   5442   5009  -1068    -49   1315       N  
ATOM   4899  CA  ASP A 634       2.370 -11.240   2.102  1.00 36.98           C  
ANISOU 4899  CA  ASP A 634     4481   5074   4495  -1177    -57   1534       C  
ATOM   4900  C   ASP A 634       2.971 -11.202   3.505  1.00 39.00           C  
ANISOU 4900  C   ASP A 634     4716   5545   4556  -1166     13   1568       C  
ATOM   4901  O   ASP A 634       2.768 -12.132   4.289  1.00 41.57           O  
ANISOU 4901  O   ASP A 634     4993   5973   4829  -1268     -9   1788       O  
ATOM   4902  CB  ASP A 634       2.563 -12.608   1.439  1.00 35.36           C  
ANISOU 4902  CB  ASP A 634     4360   4641   4434  -1273   -211   1663       C  
ATOM   4903  CG  ASP A 634       3.996 -12.875   1.014  1.00 35.76           C  
ANISOU 4903  CG  ASP A 634     4562   4510   4515  -1211   -286   1559       C  
ATOM   4904  OD1 ASP A 634       4.921 -12.175   1.489  1.00 32.55           O  
ANISOU 4904  OD1 ASP A 634     4190   4183   3996  -1118   -231   1450       O  
ATOM   4905  OD2 ASP A 634       4.190 -13.804   0.190  1.00 37.90           O  
ANISOU 4905  OD2 ASP A 634     4908   4556   4935  -1259   -400   1575       O  
ATOM   4906  N   THR A 635       3.691 -10.122   3.822  1.00 39.54           N  
ANISOU 4906  N   THR A 635     4815   5691   4519  -1057     85   1362       N  
ATOM   4907  CA  THR A 635       4.110  -9.842   5.198  1.00 42.48           C  
ANISOU 4907  CA  THR A 635     5147   6328   4664  -1052    165   1346       C  
ATOM   4908  C   THR A 635       2.932  -9.912   6.153  1.00 44.95           C  
ANISOU 4908  C   THR A 635     5297   6935   4849  -1121    285   1457       C  
ATOM   4909  O   THR A 635       1.943  -9.217   5.967  1.00 52.07           O  
ANISOU 4909  O   THR A 635     6092   7893   5801  -1082    389   1363       O  
ATOM   4910  CB  THR A 635       4.704  -8.429   5.343  1.00 43.15           C  
ANISOU 4910  CB  THR A 635     5253   6459   4684   -930    245   1056       C  
ATOM   4911  OG1 THR A 635       5.869  -8.308   4.524  1.00 45.08           O  
ANISOU 4911  OG1 THR A 635     5631   6469   5029   -873    146    967       O  
ATOM   4912  CG2 THR A 635       5.078  -8.144   6.802  1.00 43.39           C  
ANISOU 4912  CG2 THR A 635     5239   6799   4447   -943    324   1009       C  
ATOM   4913  N   VAL A 636       3.037 -10.746   7.176  1.00 46.11           N  
ANISOU 4913  N   VAL A 636     5406   7279   4836  -1226    271   1674       N  
ATOM   4914  CA  VAL A 636       1.992 -10.829   8.192  1.00 48.92           C  
ANISOU 4914  CA  VAL A 636     5591   7978   5019  -1307    401   1797       C  
ATOM   4915  C   VAL A 636       2.290  -9.855   9.332  1.00 50.86           C  
ANISOU 4915  C   VAL A 636     5790   8561   4975  -1256    548   1588       C  
ATOM   4916  O   VAL A 636       1.380  -9.274   9.914  1.00 51.33           O  
ANISOU 4916  O   VAL A 636     5702   8886   4914  -1245    721   1495       O  
ATOM   4917  CB  VAL A 636       1.876 -12.252   8.750  1.00 50.53           C  
ANISOU 4917  CB  VAL A 636     5756   8256   5188  -1474    308   2182       C  
ATOM   4918  CG1 VAL A 636       0.708 -12.340   9.694  1.00 56.05           C  
ANISOU 4918  CG1 VAL A 636     6257   9328   5711  -1574    453   2334       C  
ATOM   4919  CG2 VAL A 636       1.719 -13.252   7.618  1.00 48.50           C  
ANISOU 4919  CG2 VAL A 636     5562   7624   5243  -1527    144   2341       C  
ATOM   4920  N   CYS A 637       3.572  -9.690   9.645  1.00 52.94           N  
ANISOU 4920  N   CYS A 637     6169   8816   5132  -1226    476   1502       N  
ATOM   4921  CA  CYS A 637       4.006  -8.800  10.719  1.00 55.96           C  
ANISOU 4921  CA  CYS A 637     6525   9509   5228  -1194    583   1280       C  
ATOM   4922  C   CYS A 637       5.521  -8.597  10.653  1.00 54.76           C  
ANISOU 4922  C   CYS A 637     6519   9224   5063  -1149    456   1178       C  
ATOM   4923  O   CYS A 637       6.209  -9.251   9.866  1.00 56.05           O  
ANISOU 4923  O   CYS A 637     6787   9086   5423  -1145    301   1307       O  
ATOM   4924  CB  CYS A 637       3.624  -9.378  12.091  1.00 59.76           C  
ANISOU 4924  CB  CYS A 637     6887  10439   5381  -1337    650   1494       C  
ATOM   4925  SG  CYS A 637       4.755 -10.653  12.711  1.00 61.92           S  
ANISOU 4925  SG  CYS A 637     7230  10768   5529  -1476    443   1869       S  
ATOM   4926  N   LEU A 638       6.032  -7.695  11.487  1.00 53.69           N  
ANISOU 4926  N   LEU A 638     6380   9321   4700  -1120    524    931       N  
ATOM   4927  CA  LEU A 638       7.471  -7.508  11.640  1.00 51.86           C  
ANISOU 4927  CA  LEU A 638     6257   9033   4415  -1104    401    854       C  
ATOM   4928  C   LEU A 638       7.945  -8.143  12.953  1.00 55.55           C  
ANISOU 4928  C   LEU A 638     6689   9872   4546  -1239    348   1057       C  
ATOM   4929  O   LEU A 638       7.402  -7.858  14.023  1.00 53.73           O  
ANISOU 4929  O   LEU A 638     6359  10050   4006  -1304    475    996       O  
ATOM   4930  CB  LEU A 638       7.832  -6.022  11.589  1.00 50.66           C  
ANISOU 4930  CB  LEU A 638     6129   8844   4274   -991    476    432       C  
ATOM   4931  CG  LEU A 638       7.531  -5.347  10.244  1.00 47.87           C  
ANISOU 4931  CG  LEU A 638     5809   8109   4270   -865    493    275       C  
ATOM   4932  CD1 LEU A 638       7.773  -3.848  10.310  1.00 44.14           C  
ANISOU 4932  CD1 LEU A 638     5331   7602   3837   -764    569   -119       C  
ATOM   4933  CD2 LEU A 638       8.354  -5.978   9.122  1.00 45.39           C  
ANISOU 4933  CD2 LEU A 638     5612   7447   4189   -849    328    438       C  
ATOM   4934  N   ALA A 639       8.955  -9.010  12.861  1.00 57.08           N  
ANISOU 4934  N   ALA A 639     6951   9936   4802  -1283    161   1303       N  
ATOM   4935  CA  ALA A 639       9.412  -9.784  14.008  1.00 59.05           C  
ANISOU 4935  CA  ALA A 639     7152  10503   4779  -1425     68   1591       C  
ATOM   4936  C   ALA A 639      10.586  -9.106  14.682  1.00 58.96           C  
ANISOU 4936  C   ALA A 639     7180  10665   4557  -1426      5   1407       C  
ATOM   4937  O   ALA A 639      11.405  -8.462  14.030  1.00 48.91           O  
ANISOU 4937  O   ALA A 639     5994   9131   3460  -1321    -44   1178       O  
ATOM   4938  CB  ALA A 639       9.792 -11.193  13.587  1.00 59.92           C  
ANISOU 4938  CB  ALA A 639     7284  10361   5121  -1475   -115   1999       C  
ATOM   4939  N   LYS A 640      10.648  -9.269  16.000  1.00 64.18           N  
ANISOU 4939  N   LYS A 640     7766  11792   4828  -1562      2   1524       N  
ATOM   4940  CA  LYS A 640      11.743  -8.764  16.802  1.00 64.89           C  
ANISOU 4940  CA  LYS A 640     7877  12118   4662  -1606    -86   1396       C  
ATOM   4941  C   LYS A 640      12.960  -9.623  16.546  1.00 64.81           C  
ANISOU 4941  C   LYS A 640     7908  11884   4834  -1620   -328   1702       C  
ATOM   4942  O   LYS A 640      12.837 -10.807  16.220  1.00 59.13           O  
ANISOU 4942  O   LYS A 640     7168  10986   4313  -1651   -423   2085       O  
ATOM   4943  CB  LYS A 640      11.376  -8.806  18.289  1.00 71.27           C  
ANISOU 4943  CB  LYS A 640     8579  13541   4960  -1773    -25   1472       C  
ATOM   4944  CG  LYS A 640      10.205  -7.888  18.671  1.00 73.47           C  
ANISOU 4944  CG  LYS A 640     8791  14094   5031  -1750    242   1116       C  
ATOM   4945  CD  LYS A 640       9.436  -8.371  19.908  1.00 77.88           C  
ANISOU 4945  CD  LYS A 640     9210  15240   5139  -1927    339   1332       C  
ATOM   4946  CE  LYS A 640      10.146  -8.037  21.217  1.00 82.15           C  
ANISOU 4946  CE  LYS A 640     9727  16309   5178  -2065    290   1245       C  
ATOM   4947  NZ  LYS A 640       9.242  -8.209  22.399  1.00 86.46           N  
ANISOU 4947  NZ  LYS A 640    10126  17492   5232  -2225    452   1334       N  
ATOM   4948  N   LEU A 641      14.134  -9.009  16.673  1.00 70.06           N  
ANISOU 4948  N   LEU A 641     8619  12538   5462  -1593   -428   1518       N  
ATOM   4949  CA  LEU A 641      15.405  -9.718  16.580  1.00 72.50           C  
ANISOU 4949  CA  LEU A 641     8937  12690   5919  -1605   -658   1786       C  
ATOM   4950  C   LEU A 641      16.170  -9.475  17.876  1.00 80.81           C  
ANISOU 4950  C   LEU A 641     9939  14194   6572  -1741   -768   1811       C  
ATOM   4951  O   LEU A 641      16.796  -8.430  18.056  1.00 84.17           O  
ANISOU 4951  O   LEU A 641    10399  14691   6890  -1721   -770   1465       O  
ATOM   4952  CB  LEU A 641      16.218  -9.225  15.375  1.00 66.60           C  
ANISOU 4952  CB  LEU A 641     8277  11483   5544  -1446   -694   1561       C  
ATOM   4953  CG  LEU A 641      15.489  -9.070  14.036  1.00 61.38           C  
ANISOU 4953  CG  LEU A 641     7678  10423   5220  -1311   -566   1413       C  
ATOM   4954  CD1 LEU A 641      16.317  -8.242  13.068  1.00 57.61           C  
ANISOU 4954  CD1 LEU A 641     7272   9627   4989  -1184   -578   1133       C  
ATOM   4955  CD2 LEU A 641      15.154 -10.421  13.439  1.00 61.07           C  
ANISOU 4955  CD2 LEU A 641     7629  10135   5439  -1308   -626   1769       C  
ATOM   4956  N   HIS A 642      16.100 -10.427  18.794  1.00 86.73           N  
ANISOU 4956  N   HIS A 642    10598  15260   7095  -1896   -870   2230       N  
ATOM   4957  CA  HIS A 642      16.861 -10.323  20.031  1.00 94.27           C  
ANISOU 4957  CA  HIS A 642    11493  16677   7649  -2050  -1009   2320       C  
ATOM   4958  C   HIS A 642      18.211 -10.964  19.759  1.00 93.66           C  
ANISOU 4958  C   HIS A 642    11400  16343   7843  -2025  -1267   2600       C  
ATOM   4959  O   HIS A 642      18.267 -12.121  19.345  1.00 95.64           O  
ANISOU 4959  O   HIS A 642    11614  16325   8398  -2004  -1372   3002       O  
ATOM   4960  CB  HIS A 642      16.166 -11.040  21.203  1.00101.75           C  
ANISOU 4960  CB  HIS A 642    12328  18142   8192  -2252  -1008   2686       C  
ATOM   4961  CG  HIS A 642      14.677 -11.142  21.068  1.00105.10           C  
ANISOU 4961  CG  HIS A 642    12729  18624   8582  -2251   -778   2664       C  
ATOM   4962  ND1 HIS A 642      14.039 -12.333  20.786  1.00106.19           N  
ANISOU 4962  ND1 HIS A 642    12811  18603   8934  -2286   -806   3109       N  
ATOM   4963  CD2 HIS A 642      13.702 -10.207  21.171  1.00107.15           C  
ANISOU 4963  CD2 HIS A 642    12996  19068   8648  -2218   -523   2252       C  
ATOM   4964  CE1 HIS A 642      12.735 -12.127  20.726  1.00106.85           C  
ANISOU 4964  CE1 HIS A 642    12867  18794   8939  -2285   -579   2987       C  
ATOM   4965  NE2 HIS A 642      12.504 -10.846  20.956  1.00107.59           N  
ANISOU 4965  NE2 HIS A 642    12992  19097   8789  -2235   -399   2470       N  
ATOM   4966  N   ASP A 643      19.293 -10.210  19.949  1.00 92.86           N  
ANISOU 4966  N   ASP A 643    11317  16296   7671  -2020  -1367   2374       N  
ATOM   4967  CA  ASP A 643      20.651 -10.762  19.851  1.00 91.61           C  
ANISOU 4967  CA  ASP A 643    11108  15968   7731  -2009  -1620   2645       C  
ATOM   4968  C   ASP A 643      20.923 -11.428  18.496  1.00 83.49           C  
ANISOU 4968  C   ASP A 643    10108  14327   7286  -1826  -1640   2762       C  
ATOM   4969  O   ASP A 643      21.897 -12.159  18.334  1.00 83.48           O  
ANISOU 4969  O   ASP A 643    10040  14137   7542  -1796  -1832   3052       O  
ATOM   4970  CB  ASP A 643      20.888 -11.756  21.002  1.00 98.34           C  
ANISOU 4970  CB  ASP A 643    11832  17208   8325  -2198  -1822   3174       C  
ATOM   4971  CG  ASP A 643      22.253 -12.427  20.937  1.00101.15           C  
ANISOU 4971  CG  ASP A 643    12103  17379   8951  -2181  -2097   3509       C  
ATOM   4972  OD1 ASP A 643      23.258 -11.727  20.675  1.00102.61           O  
ANISOU 4972  OD1 ASP A 643    12305  17455   9228  -2117  -2166   3260       O  
ATOM   4973  OD2 ASP A 643      22.315 -13.659  21.151  1.00102.84           O  
ANISOU 4973  OD2 ASP A 643    12217  17548   9310  -2231  -2249   4034       O  
ATOM   4974  N   ARG A 644      20.057 -11.166  17.526  1.00 75.34           N  
ANISOU 4974  N   ARG A 644     9165  13002   6460  -1705  -1440   2524       N  
ATOM   4975  CA  ARG A 644      20.201 -11.713  16.192  1.00 71.35           C  
ANISOU 4975  CA  ARG A 644     8698  11956   6456  -1542  -1432   2567       C  
ATOM   4976  C   ARG A 644      20.345 -10.500  15.256  1.00 65.19           C  
ANISOU 4976  C   ARG A 644     8015  10946   5808  -1409  -1296   2085       C  
ATOM   4977  O   ARG A 644      19.808 -10.475  14.152  1.00 58.43           O  
ANISOU 4977  O   ARG A 644     7226   9759   5217  -1294  -1172   1954       O  
ATOM   4978  CB  ARG A 644      18.975 -12.588  15.871  1.00 72.38           C  
ANISOU 4978  CB  ARG A 644     8833  11964   6705  -1547  -1341   2772       C  
ATOM   4979  CG  ARG A 644      19.302 -13.913  15.181  1.00 73.20           C  
ANISOU 4979  CG  ARG A 644     8901  11660   7251  -1480  -1465   3109       C  
ATOM   4980  CD  ARG A 644      18.162 -14.939  15.286  1.00 75.37           C  
ANISOU 4980  CD  ARG A 644     9142  11915   7579  -1557  -1442   3422       C  
ATOM   4981  NE  ARG A 644      17.264 -14.922  14.121  1.00 75.69           N  
ANISOU 4981  NE  ARG A 644     9269  11623   7865  -1457  -1284   3216       N  
ATOM   4982  CZ  ARG A 644      15.987 -14.521  14.112  1.00 75.52           C  
ANISOU 4982  CZ  ARG A 644     9277  11738   7678  -1496  -1110   3079       C  
ATOM   4983  NH1 ARG A 644      15.378 -14.073  15.215  1.00 77.13           N  
ANISOU 4983  NH1 ARG A 644     9432  12418   7455  -1626  -1036   3090       N  
ATOM   4984  NH2 ARG A 644      15.305 -14.571  12.972  1.00 72.34           N  
ANISOU 4984  NH2 ARG A 644     8942  11005   7538  -1405  -1005   2922       N  
ATOM   4985  N   ASN A 645      21.109  -9.508  15.721  1.00 65.01           N  
ANISOU 4985  N   ASN A 645     7990  11109   5603  -1443  -1340   1846       N  
ATOM   4986  CA  ASN A 645      21.108  -8.155  15.153  1.00 61.47           C  
ANISOU 4986  CA  ASN A 645     7618  10543   5197  -1365  -1213   1381       C  
ATOM   4987  C   ASN A 645      22.365  -7.853  14.352  1.00 58.48           C  
ANISOU 4987  C   ASN A 645     7235   9865   5119  -1270  -1301   1299       C  
ATOM   4988  O   ASN A 645      23.007  -6.815  14.537  1.00 58.06           O  
ANISOU 4988  O   ASN A 645     7184   9882   4993  -1291  -1328   1036       O  
ATOM   4989  CB  ASN A 645      20.911  -7.109  16.267  1.00 63.68           C  
ANISOU 4989  CB  ASN A 645     7895  11245   5054  -1482  -1174   1099       C  
ATOM   4990  CG  ASN A 645      21.950  -7.215  17.385  1.00 64.79           C  
ANISOU 4990  CG  ASN A 645     7959  11728   4931  -1623  -1383   1242       C  
ATOM   4991  OD1 ASN A 645      22.625  -8.234  17.536  1.00 64.71           O  
ANISOU 4991  OD1 ASN A 645     7875  11701   5010  -1651  -1559   1639       O  
ATOM   4992  ND2 ASN A 645      22.068  -6.156  18.179  1.00 65.12           N  
ANISOU 4992  ND2 ASN A 645     8007  12079   4656  -1715  -1373    913       N  
ATOM   4993  N   THR A 646      22.688  -8.771  13.445  1.00 56.80           N  
ANISOU 4993  N   THR A 646     7008   9316   5255  -1168  -1337   1515       N  
ATOM   4994  CA  THR A 646      23.883  -8.693  12.612  1.00 54.46           C  
ANISOU 4994  CA  THR A 646     6683   8741   5269  -1067  -1404   1484       C  
ATOM   4995  C   THR A 646      23.673  -9.557  11.382  1.00 53.27           C  
ANISOU 4995  C   THR A 646     6555   8206   5479   -935  -1341   1590       C  
ATOM   4996  O   THR A 646      23.222 -10.693  11.496  1.00 55.36           O  
ANISOU 4996  O   THR A 646     6800   8425   5811   -943  -1375   1863       O  
ATOM   4997  CB  THR A 646      25.108  -9.205  13.372  1.00 58.04           C  
ANISOU 4997  CB  THR A 646     7014   9336   5701  -1127  -1627   1746       C  
ATOM   4998  OG1 THR A 646      25.570  -8.187  14.262  1.00 59.57           O  
ANISOU 4998  OG1 THR A 646     7191   9841   5602  -1241  -1695   1562       O  
ATOM   4999  CG2 THR A 646      26.225  -9.577  12.426  1.00 60.22           C  
ANISOU 4999  CG2 THR A 646     7226   9285   6371   -998  -1684   1815       C  
ATOM   5000  N   TYR A 647      24.017  -9.025  10.212  1.00 50.79           N  
ANISOU 5000  N   TYR A 647     6277   7625   5396   -826  -1256   1376       N  
ATOM   5001  CA  TYR A 647      23.689  -9.678   8.944  1.00 49.38           C  
ANISOU 5001  CA  TYR A 647     6138   7115   5510   -710  -1166   1393       C  
ATOM   5002  C   TYR A 647      24.088 -11.160   8.913  1.00 52.75           C  
ANISOU 5002  C   TYR A 647     6491   7392   6160   -668  -1274   1707       C  
ATOM   5003  O   TYR A 647      23.321 -11.991   8.421  1.00 50.25           O  
ANISOU 5003  O   TYR A 647     6213   6903   5979   -636  -1225   1792       O  
ATOM   5004  CB  TYR A 647      24.285  -8.906   7.744  1.00 48.33           C  
ANISOU 5004  CB  TYR A 647     6022   6772   5568   -616  -1083   1156       C  
ATOM   5005  CG  TYR A 647      25.762  -9.142   7.468  1.00 48.76           C  
ANISOU 5005  CG  TYR A 647     5970   6729   5828   -554  -1176   1228       C  
ATOM   5006  CD1 TYR A 647      26.751  -8.352   8.063  1.00 49.94           C  
ANISOU 5006  CD1 TYR A 647     6046   7037   5893   -608  -1272   1176       C  
ATOM   5007  CD2 TYR A 647      26.166 -10.145   6.598  1.00 48.21           C  
ANISOU 5007  CD2 TYR A 647     5859   6409   6052   -441  -1165   1328       C  
ATOM   5008  CE1 TYR A 647      28.104  -8.572   7.799  1.00 49.58           C  
ANISOU 5008  CE1 TYR A 647     5876   6910   6054   -551  -1355   1258       C  
ATOM   5009  CE2 TYR A 647      27.508 -10.375   6.338  1.00 49.90           C  
ANISOU 5009  CE2 TYR A 647     5948   6539   6473   -370  -1232   1386       C  
ATOM   5010  CZ  TYR A 647      28.471  -9.591   6.935  1.00 49.56           C  
ANISOU 5010  CZ  TYR A 647     5821   6664   6347   -424  -1326   1367       C  
ATOM   5011  OH  TYR A 647      29.793  -9.849   6.651  1.00 49.84           O  
ANISOU 5011  OH  TYR A 647     5708   6618   6611   -351  -1389   1440       O  
ATOM   5012  N   GLU A 648      25.268 -11.480   9.451  1.00 56.47           N  
ANISOU 5012  N   GLU A 648     6845   7919   6693   -672  -1431   1880       N  
ATOM   5013  CA  GLU A 648      25.741 -12.871   9.547  1.00 59.96           C  
ANISOU 5013  CA  GLU A 648     7183   8208   7389   -627  -1559   2204       C  
ATOM   5014  C   GLU A 648      24.834 -13.641  10.493  1.00 59.33           C  
ANISOU 5014  C   GLU A 648     7103   8284   7156   -741  -1629   2487       C  
ATOM   5015  O   GLU A 648      24.308 -14.711  10.166  1.00 56.62           O  
ANISOU 5015  O   GLU A 648     6760   7728   7025   -709  -1632   2658       O  
ATOM   5016  CB  GLU A 648      27.163 -12.933  10.113  1.00 66.73           C  
ANISOU 5016  CB  GLU A 648     7890   9150   8314   -626  -1735   2360       C  
ATOM   5017  CG  GLU A 648      28.193 -12.080   9.388  1.00 70.82           C  
ANISOU 5017  CG  GLU A 648     8373   9585   8949   -546  -1688   2119       C  
ATOM   5018  CD  GLU A 648      29.090 -11.307  10.347  1.00 75.79           C  
ANISOU 5018  CD  GLU A 648     8916  10502   9377   -648  -1831   2135       C  
ATOM   5019  OE1 GLU A 648      28.572 -10.400  11.037  1.00 75.31           O  
ANISOU 5019  OE1 GLU A 648     8934  10710   8973   -774  -1817   1992       O  
ATOM   5020  OE2 GLU A 648      30.308 -11.597  10.403  1.00 80.11           O  
ANISOU 5020  OE2 GLU A 648     9311  11009  10120   -603  -1957   2275       O  
ATOM   5021  N   LYS A 649      24.666 -13.059  11.675  1.00 58.42           N  
ANISOU 5021  N   LYS A 649     6979   8556   6662   -884  -1683   2525       N  
ATOM   5022  CA  LYS A 649      23.873 -13.637  12.742  1.00 58.43           C  
ANISOU 5022  CA  LYS A 649     6959   8813   6429  -1025  -1747   2806       C  
ATOM   5023  C   LYS A 649      22.418 -13.802  12.301  1.00 57.20           C  
ANISOU 5023  C   LYS A 649     6903   8575   6254  -1030  -1583   2732       C  
ATOM   5024  O   LYS A 649      21.781 -14.796  12.631  1.00 57.94           O  
ANISOU 5024  O   LYS A 649     6964   8661   6390  -1092  -1631   3030       O  
ATOM   5025  CB  LYS A 649      23.968 -12.732  13.970  1.00 60.07           C  
ANISOU 5025  CB  LYS A 649     7152   9493   6179  -1175  -1794   2744       C  
ATOM   5026  CG  LYS A 649      23.990 -13.443  15.301  1.00 65.99           C  
ANISOU 5026  CG  LYS A 649     7797  10581   6695  -1335  -1970   3151       C  
ATOM   5027  CD  LYS A 649      24.751 -12.630  16.365  1.00 70.02           C  
ANISOU 5027  CD  LYS A 649     8255  11508   6841  -1461  -2089   3091       C  
ATOM   5028  CE  LYS A 649      24.257 -11.184  16.461  1.00 69.54           C  
ANISOU 5028  CE  LYS A 649     8304  11651   6465  -1495  -1919   2612       C  
ATOM   5029  NZ  LYS A 649      24.681 -10.512  17.726  1.00 73.88           N  
ANISOU 5029  NZ  LYS A 649     8810  12687   6573  -1663  -2029   2558       N  
ATOM   5030  N   TYR A 650      21.898 -12.837  11.540  1.00 56.19           N  
ANISOU 5030  N   TYR A 650     6884   8376   6089   -973  -1403   2359       N  
ATOM   5031  CA  TYR A 650      20.488 -12.871  11.131  1.00 55.23           C  
ANISOU 5031  CA  TYR A 650     6844   8203   5937   -983  -1251   2277       C  
ATOM   5032  C   TYR A 650      20.232 -13.812   9.975  1.00 54.83           C  
ANISOU 5032  C   TYR A 650     6820   7748   6264   -886  -1228   2333       C  
ATOM   5033  O   TYR A 650      19.330 -14.640  10.031  1.00 53.80           O  
ANISOU 5033  O   TYR A 650     6687   7565   6188   -937  -1227   2521       O  
ATOM   5034  CB  TYR A 650      19.972 -11.501  10.709  1.00 50.60           C  
ANISOU 5034  CB  TYR A 650     6347   7671   5210   -955  -1080   1879       C  
ATOM   5035  CG  TYR A 650      18.594 -11.626  10.104  1.00 47.33           C  
ANISOU 5035  CG  TYR A 650     5993   7149   4839   -945   -940   1818       C  
ATOM   5036  CD1 TYR A 650      17.491 -11.851  10.908  1.00 49.29           C  
ANISOU 5036  CD1 TYR A 650     6219   7644   4866  -1054   -896   1947       C  
ATOM   5037  CD2 TYR A 650      18.400 -11.580   8.725  1.00 43.88           C  
ANISOU 5037  CD2 TYR A 650     5623   6386   4662   -839   -858   1656       C  
ATOM   5038  CE1 TYR A 650      16.217 -11.994  10.362  1.00 47.45           C  
ANISOU 5038  CE1 TYR A 650     6019   7317   4692  -1051   -777   1912       C  
ATOM   5039  CE2 TYR A 650      17.125 -11.720   8.172  1.00 41.19           C  
ANISOU 5039  CE2 TYR A 650     5327   5960   4362   -844   -752   1619       C  
ATOM   5040  CZ  TYR A 650      16.043 -11.925   9.001  1.00 41.58           C  
ANISOU 5040  CZ  TYR A 650     5345   6240   4215   -948   -716   1750       C  
ATOM   5041  OH  TYR A 650      14.783 -12.069   8.484  1.00 41.38           O  
ANISOU 5041  OH  TYR A 650     5341   6139   4242   -960   -620   1730       O  
ATOM   5042  N   LEU A 651      21.005 -13.637   8.908  1.00 55.33           N  
ANISOU 5042  N   LEU A 651     6906   7541   6577   -756  -1203   2148       N  
ATOM   5043  CA  LEU A 651      20.836 -14.432   7.700  1.00 54.48           C  
ANISOU 5043  CA  LEU A 651     6831   7062   6808   -659  -1165   2121       C  
ATOM   5044  C   LEU A 651      21.135 -15.896   7.951  1.00 57.62           C  
ANISOU 5044  C   LEU A 651     7141   7281   7472   -655  -1312   2451       C  
ATOM   5045  O   LEU A 651      20.673 -16.759   7.206  1.00 60.41           O  
ANISOU 5045  O   LEU A 651     7519   7349   8086   -615  -1297   2472       O  
ATOM   5046  CB  LEU A 651      21.739 -13.910   6.580  1.00 51.98           C  
ANISOU 5046  CB  LEU A 651     6532   6557   6662   -529  -1102   1859       C  
ATOM   5047  CG  LEU A 651      21.395 -12.515   6.061  1.00 47.83           C  
ANISOU 5047  CG  LEU A 651     6090   6121   5963   -525   -960   1545       C  
ATOM   5048  CD1 LEU A 651      22.484 -11.997   5.148  1.00 44.81           C  
ANISOU 5048  CD1 LEU A 651     5691   5609   5726   -424   -923   1360       C  
ATOM   5049  CD2 LEU A 651      20.054 -12.545   5.343  1.00 46.78           C  
ANISOU 5049  CD2 LEU A 651     6048   5895   5831   -538   -846   1448       C  
ATOM   5050  N   GLY A 652      21.907 -16.171   8.998  1.00 60.49           N  
ANISOU 5050  N   GLY A 652     7395   7804   7783   -702  -1466   2711       N  
ATOM   5051  CA  GLY A 652      22.312 -17.526   9.315  1.00 62.86           C  
ANISOU 5051  CA  GLY A 652     7583   7925   8376   -696  -1634   3069       C  
ATOM   5052  C   GLY A 652      23.606 -17.860   8.609  1.00 63.38           C  
ANISOU 5052  C   GLY A 652     7574   7706   8801   -535  -1680   3004       C  
ATOM   5053  O   GLY A 652      24.161 -17.043   7.873  1.00 58.18           O  
ANISOU 5053  O   GLY A 652     6952   7018   8135   -443  -1575   2695       O  
ATOM   5054  N   GLU A 653      24.061 -19.088   8.811  1.00 68.83           N  
ANISOU 5054  N   GLU A 653     8144   8175   9833   -499  -1834   3306       N  
ATOM   5055  CA  GLU A 653      25.400 -19.495   8.423  1.00 73.09           C  
ANISOU 5055  CA  GLU A 653     8558   8485  10729   -347  -1906   3313       C  
ATOM   5056  C   GLU A 653      25.410 -20.119   7.020  1.00 72.68           C  
ANISOU 5056  C   GLU A 653     8538   7997  11078   -186  -1797   3067       C  
ATOM   5057  O   GLU A 653      26.390 -19.976   6.285  1.00 72.93           O  
ANISOU 5057  O   GLU A 653     8516   7889  11307    -38  -1740   2864       O  
ATOM   5058  CB  GLU A 653      25.967 -20.449   9.480  1.00 80.80           C  
ANISOU 5058  CB  GLU A 653     9355   9464  11880   -391  -2151   3793       C  
ATOM   5059  CG  GLU A 653      26.044 -19.843  10.912  1.00 84.90           C  
ANISOU 5059  CG  GLU A 653     9831  10475  11952   -570  -2274   4039       C  
ATOM   5060  CD  GLU A 653      24.674 -19.673  11.601  1.00 85.64           C  
ANISOU 5060  CD  GLU A 653    10024  10856  11660   -758  -2233   4140       C  
ATOM   5061  OE1 GLU A 653      23.829 -20.592  11.509  1.00 84.91           O  
ANISOU 5061  OE1 GLU A 653     9941  10578  11744   -795  -2249   4323       O  
ATOM   5062  OE2 GLU A 653      24.443 -18.617  12.239  1.00 84.60           O  
ANISOU 5062  OE2 GLU A 653     9950  11135  11059   -869  -2181   4025       O  
ATOM   5063  N   GLU A 654      24.316 -20.785   6.646  1.00 71.50           N  
ANISOU 5063  N   GLU A 654     8471   7660  11035   -224  -1762   3071       N  
ATOM   5064  CA  GLU A 654      24.129 -21.282   5.276  1.00 68.66           C  
ANISOU 5064  CA  GLU A 654     8172   6933  10981   -102  -1645   2775       C  
ATOM   5065  C   GLU A 654      24.185 -20.146   4.260  1.00 64.02           C  
ANISOU 5065  C   GLU A 654     7699   6447  10179    -45  -1440   2344       C  
ATOM   5066  O   GLU A 654      25.020 -20.145   3.356  1.00 63.71           O  
ANISOU 5066  O   GLU A 654     7623   6249  10335    100  -1360   2109       O  
ATOM   5067  CB  GLU A 654      22.779 -21.985   5.125  1.00 69.67           C  
ANISOU 5067  CB  GLU A 654     8387   6913  11173   -200  -1649   2840       C  
ATOM   5068  CG  GLU A 654      22.670 -23.316   5.857  1.00 78.42           C  
ANISOU 5068  CG  GLU A 654     9375   7811  12609   -249  -1850   3260       C  
ATOM   5069  CD  GLU A 654      22.233 -23.185   7.317  1.00 80.65           C  
ANISOU 5069  CD  GLU A 654     9610   8447  12586   -436  -1976   3682       C  
ATOM   5070  OE1 GLU A 654      21.653 -24.166   7.833  1.00 83.44           O  
ANISOU 5070  OE1 GLU A 654     9904   8679  13120   -536  -2109   4029       O  
ATOM   5071  OE2 GLU A 654      22.465 -22.120   7.943  1.00 77.99           O  
ANISOU 5071  OE2 GLU A 654     9287   8512  11833   -491  -1942   3665       O  
ATOM   5072  N   TYR A 655      23.293 -19.175   4.415  1.00 57.15           N  
ANISOU 5072  N   TYR A 655     6951   5848   8915   -161  -1354   2253       N  
ATOM   5073  CA  TYR A 655      23.112 -18.156   3.394  1.00 50.31           C  
ANISOU 5073  CA  TYR A 655     6196   5046   7875   -127  -1174   1885       C  
ATOM   5074  C   TYR A 655      24.368 -17.322   3.200  1.00 47.05           C  
ANISOU 5074  C   TYR A 655     5720   4739   7420    -42  -1131   1745       C  
ATOM   5075  O   TYR A 655      24.785 -17.070   2.067  1.00 47.36           O  
ANISOU 5075  O   TYR A 655     5776   4676   7544     54  -1008   1478       O  
ATOM   5076  CB  TYR A 655      21.933 -17.253   3.738  1.00 49.70           C  
ANISOU 5076  CB  TYR A 655     6230   5231   7424   -262  -1108   1850       C  
ATOM   5077  CG  TYR A 655      21.515 -16.349   2.593  1.00 47.96           C  
ANISOU 5077  CG  TYR A 655     6120   5025   7078   -239   -942   1516       C  
ATOM   5078  CD1 TYR A 655      21.115 -16.885   1.374  1.00 45.39           C  
ANISOU 5078  CD1 TYR A 655     5855   4465   6927   -192   -871   1336       C  
ATOM   5079  CD2 TYR A 655      21.508 -14.965   2.729  1.00 46.40           C  
ANISOU 5079  CD2 TYR A 655     5959   5074   6595   -274   -868   1386       C  
ATOM   5080  CE1 TYR A 655      20.725 -16.079   0.327  1.00 42.71           C  
ANISOU 5080  CE1 TYR A 655     5605   4168   6454   -189   -738   1072       C  
ATOM   5081  CE2 TYR A 655      21.110 -14.145   1.673  1.00 44.77           C  
ANISOU 5081  CE2 TYR A 655     5837   4870   6303   -260   -734   1129       C  
ATOM   5082  CZ  TYR A 655      20.722 -14.714   0.477  1.00 42.72           C  
ANISOU 5082  CZ  TYR A 655     5632   4407   6193   -222   -673    992       C  
ATOM   5083  OH  TYR A 655      20.336 -13.925  -0.579  1.00 41.73           O  
ANISOU 5083  OH  TYR A 655     5578   4311   5964   -225   -559    775       O  
ATOM   5084  N   VAL A 656      24.972 -16.902   4.307  1.00 48.02           N  
ANISOU 5084  N   VAL A 656     5760   5086   7401    -91  -1237   1934       N  
ATOM   5085  CA  VAL A 656      26.213 -16.116   4.272  1.00 43.92           C  
ANISOU 5085  CA  VAL A 656     5156   4677   6852    -32  -1229   1841       C  
ATOM   5086  C   VAL A 656      27.296 -16.866   3.495  1.00 45.46           C  
ANISOU 5086  C   VAL A 656     5229   4606   7436    135  -1218   1787       C  
ATOM   5087  O   VAL A 656      28.062 -16.260   2.748  1.00 39.96           O  
ANISOU 5087  O   VAL A 656     4499   3923   6763    213  -1114   1577       O  
ATOM   5088  CB  VAL A 656      26.731 -15.805   5.692  1.00 43.53           C  
ANISOU 5088  CB  VAL A 656     5016   4896   6628   -124  -1391   2092       C  
ATOM   5089  CG1 VAL A 656      28.008 -14.982   5.635  1.00 44.22           C  
ANISOU 5089  CG1 VAL A 656     5007   5089   6704    -79  -1396   1994       C  
ATOM   5090  CG2 VAL A 656      25.682 -15.069   6.485  1.00 42.96           C  
ANISOU 5090  CG2 VAL A 656     5050   5110   6162   -282  -1381   2105       C  
ATOM   5091  N   LYS A 657      27.339 -18.187   3.672  1.00 51.33           N  
ANISOU 5091  N   LYS A 657     5895   5107   8502    189  -1321   1979       N  
ATOM   5092  CA  LYS A 657      28.241 -19.041   2.907  1.00 55.85           C  
ANISOU 5092  CA  LYS A 657     6344   5379   9500    366  -1298   1898       C  
ATOM   5093  C   LYS A 657      27.924 -18.936   1.407  1.00 53.38           C  
ANISOU 5093  C   LYS A 657     6134   4928   9220    441  -1088   1506       C  
ATOM   5094  O   LYS A 657      28.752 -18.452   0.622  1.00 50.42           O  
ANISOU 5094  O   LYS A 657     5705   4582   8869    536   -964   1285       O  
ATOM   5095  CB  LYS A 657      28.156 -20.503   3.395  1.00 62.14           C  
ANISOU 5095  CB  LYS A 657     7044   5893  10671    398  -1460   2181       C  
ATOM   5096  CG  LYS A 657      29.328 -21.401   2.935  1.00 68.48           C  
ANISOU 5096  CG  LYS A 657     7655   6388  11975    599  -1481   2159       C  
ATOM   5097  CD  LYS A 657      29.283 -22.845   3.513  1.00 73.17           C  
ANISOU 5097  CD  LYS A 657     8129   6666  13004    630  -1674   2486       C  
ATOM   5098  CE  LYS A 657      27.963 -23.580   3.217  1.00 74.01           C  
ANISOU 5098  CE  LYS A 657     8378   6558  13186    557  -1668   2460       C  
ATOM   5099  NZ  LYS A 657      27.304 -23.178   1.921  1.00 69.54           N  
ANISOU 5099  NZ  LYS A 657     7991   5962  12470    572  -1444   2005       N  
ATOM   5100  N   ALA A 658      26.715 -19.352   1.029  1.00 51.25           N  
ANISOU 5100  N   ALA A 658     6003   4544   8924    381  -1054   1437       N  
ATOM   5101  CA  ALA A 658      26.304 -19.421  -0.378  1.00 50.69           C  
ANISOU 5101  CA  ALA A 658     6033   4344   8884    431   -884   1084       C  
ATOM   5102  C   ALA A 658      26.563 -18.107  -1.109  1.00 48.06           C  
ANISOU 5102  C   ALA A 658     5751   4252   8257    423   -723    842       C  
ATOM   5103  O   ALA A 658      27.100 -18.085  -2.226  1.00 43.58           O  
ANISOU 5103  O   ALA A 658     5157   3631   7769    521   -583    578       O  
ATOM   5104  CB  ALA A 658      24.829 -19.801  -0.479  1.00 49.80           C  
ANISOU 5104  CB  ALA A 658     6068   4157   8696    315   -899   1090       C  
ATOM   5105  N   VAL A 659      26.182 -17.010  -0.468  1.00 45.77           N  
ANISOU 5105  N   VAL A 659     5523   4232   7634    302   -744    933       N  
ATOM   5106  CA  VAL A 659      26.431 -15.700  -1.036  1.00 45.85           C  
ANISOU 5106  CA  VAL A 659     5568   4452   7401    280   -621    753       C  
ATOM   5107  C   VAL A 659      27.925 -15.473  -1.173  1.00 48.27           C  
ANISOU 5107  C   VAL A 659     5713   4790   7837    384   -597    725       C  
ATOM   5108  O   VAL A 659      28.383 -14.980  -2.195  1.00 51.11           O  
ANISOU 5108  O   VAL A 659     6055   5196   8167    430   -454    516       O  
ATOM   5109  CB  VAL A 659      25.840 -14.591  -0.178  1.00 43.16           C  
ANISOU 5109  CB  VAL A 659     5298   4360   6740    144   -666    854       C  
ATOM   5110  CG1 VAL A 659      26.234 -13.240  -0.751  1.00 42.25           C  
ANISOU 5110  CG1 VAL A 659     5192   4414   6447    126   -560    688       C  
ATOM   5111  CG2 VAL A 659      24.327 -14.738  -0.104  1.00 35.66           C  
ANISOU 5111  CG2 VAL A 659     4487   3403   5659     45   -666    872       C  
ATOM   5112  N   GLY A 660      28.673 -15.844  -0.136  1.00 52.29           N  
ANISOU 5112  N   GLY A 660     6089   5293   8485    411   -743    958       N  
ATOM   5113  CA  GLY A 660      30.135 -15.745  -0.142  1.00 53.49           C  
ANISOU 5113  CA  GLY A 660     6051   5466   8807    512   -748    976       C  
ATOM   5114  C   GLY A 660      30.746 -16.510  -1.296  1.00 54.52           C  
ANISOU 5114  C   GLY A 660     6091   5390   9234    678   -615    771       C  
ATOM   5115  O   GLY A 660      31.602 -15.985  -2.001  1.00 53.11           O  
ANISOU 5115  O   GLY A 660     5821   5298   9059    739   -492    619       O  
ATOM   5116  N   ASN A 661      30.288 -17.746  -1.496  1.00 56.81           N  
ANISOU 5116  N   ASN A 661     6400   5411   9773    744   -636    755       N  
ATOM   5117  CA  ASN A 661      30.690 -18.562  -2.653  1.00 58.47           C  
ANISOU 5117  CA  ASN A 661     6547   5403  10267    901   -496    490       C  
ATOM   5118  C   ASN A 661      30.571 -17.830  -3.993  1.00 55.22           C  
ANISOU 5118  C   ASN A 661     6218   5139   9624    890   -274    159       C  
ATOM   5119  O   ASN A 661      31.388 -18.047  -4.889  1.00 54.11           O  
ANISOU 5119  O   ASN A 661     5963   4967   9630   1018   -127    -60       O  
ATOM   5120  CB  ASN A 661      29.869 -19.864  -2.717  1.00 61.56           C  
ANISOU 5120  CB  ASN A 661     7003   5478  10909    925   -558    483       C  
ATOM   5121  CG  ASN A 661      30.324 -20.914  -1.692  1.00 66.52           C  
ANISOU 5121  CG  ASN A 661     7475   5874  11925    995   -757    790       C  
ATOM   5122  OD1 ASN A 661      31.395 -20.799  -1.072  1.00 67.74           O  
ANISOU 5122  OD1 ASN A 661     7448   6087  12203   1059   -836    974       O  
ATOM   5123  ND2 ASN A 661      29.507 -21.955  -1.525  1.00 65.56           N  
ANISOU 5123  ND2 ASN A 661     7412   5485  12013    974   -853    867       N  
ATOM   5124  N   LEU A 662      29.560 -16.966  -4.114  1.00 51.48           N  
ANISOU 5124  N   LEU A 662     5926   4840   8794    736   -252    136       N  
ATOM   5125  CA  LEU A 662      29.352 -16.153  -5.314  1.00 50.84           C  
ANISOU 5125  CA  LEU A 662     5924   4932   8460    692    -73   -110       C  
ATOM   5126  C   LEU A 662      30.247 -14.908  -5.391  1.00 52.96           C  
ANISOU 5126  C   LEU A 662     6099   5454   8569    668    -10    -84       C  
ATOM   5127  O   LEU A 662      30.221 -14.203  -6.401  1.00 51.59           O  
ANISOU 5127  O   LEU A 662     5959   5440   8205    628    135   -247       O  
ATOM   5128  CB  LEU A 662      27.878 -15.707  -5.427  1.00 49.57           C  
ANISOU 5128  CB  LEU A 662     5974   4841   8021    538    -90   -117       C  
ATOM   5129  CG  LEU A 662      26.910 -16.453  -6.363  1.00 50.02           C  
ANISOU 5129  CG  LEU A 662     6155   4764   8087    523    -31   -326       C  
ATOM   5130  CD1 LEU A 662      25.571 -15.736  -6.387  1.00 45.88           C  
ANISOU 5130  CD1 LEU A 662     5799   4364   7267    362    -56   -283       C  
ATOM   5131  CD2 LEU A 662      27.444 -16.593  -7.788  1.00 49.54           C  
ANISOU 5131  CD2 LEU A 662     6054   4741   8027    599    157   -641       C  
ATOM   5132  N   ARG A 663      31.032 -14.631  -4.352  1.00 56.89           N  
ANISOU 5132  N   ARG A 663     6474   6000   9143    676   -129    131       N  
ATOM   5133  CA  ARG A 663      31.789 -13.372  -4.282  1.00 61.77           C  
ANISOU 5133  CA  ARG A 663     7010   6847   9613    620   -105    177       C  
ATOM   5134  C   ARG A 663      32.509 -13.040  -5.598  1.00 61.62           C  
ANISOU 5134  C   ARG A 663     6898   6934   9582    675    101    -28       C  
ATOM   5135  O   ARG A 663      32.397 -11.922  -6.112  1.00 56.32           O  
ANISOU 5135  O   ARG A 663     6270   6451   8680    572    175    -65       O  
ATOM   5136  CB  ARG A 663      32.788 -13.394  -3.109  1.00 66.43           C  
ANISOU 5136  CB  ARG A 663     7431   7452  10358    648   -262    405       C  
ATOM   5137  CG  ARG A 663      33.502 -12.063  -2.846  1.00 69.75           C  
ANISOU 5137  CG  ARG A 663     7773   8096  10632    559   -282    470       C  
ATOM   5138  CD  ARG A 663      32.527 -10.951  -2.427  1.00 71.67           C  
ANISOU 5138  CD  ARG A 663     8195   8470  10568    387   -336    496       C  
ATOM   5139  NE  ARG A 663      33.186  -9.646  -2.266  1.00 74.05           N  
ANISOU 5139  NE  ARG A 663     8423   8945  10766    295   -355    526       N  
ATOM   5140  CZ  ARG A 663      33.187  -8.655  -3.164  1.00 74.70           C  
ANISOU 5140  CZ  ARG A 663     8524   9127  10732    234   -234    421       C  
ATOM   5141  NH1 ARG A 663      32.564  -8.777  -4.332  1.00 76.25           N  
ANISOU 5141  NH1 ARG A 663     8811   9305  10856    249    -78    277       N  
ATOM   5142  NH2 ARG A 663      33.822  -7.519  -2.890  1.00 75.45           N  
ANISOU 5142  NH2 ARG A 663     8538   9345  10785    142   -282    474       N  
ATOM   5143  N   LYS A 664      33.229 -14.023  -6.132  1.00 65.03           N  
ANISOU 5143  N   LYS A 664     7191   7243  10273    835    194   -156       N  
ATOM   5144  CA  LYS A 664      33.923 -13.907  -7.422  1.00 67.38           C  
ANISOU 5144  CA  LYS A 664     7380   7659  10560    902    418   -382       C  
ATOM   5145  C   LYS A 664      33.013 -13.383  -8.544  1.00 65.87           C  
ANISOU 5145  C   LYS A 664     7361   7613  10054    792    551   -559       C  
ATOM   5146  O   LYS A 664      33.442 -12.590  -9.382  1.00 66.73           O  
ANISOU 5146  O   LYS A 664     7410   7949   9996    745    693   -624       O  
ATOM   5147  CB  LYS A 664      34.513 -15.280  -7.803  1.00 71.82           C  
ANISOU 5147  CB  LYS A 664     7804   8014  11471   1105    500   -553       C  
ATOM   5148  CG  LYS A 664      35.169 -15.395  -9.196  1.00 75.59           C  
ANISOU 5148  CG  LYS A 664     8163   8615  11942   1197    765   -853       C  
ATOM   5149  CD  LYS A 664      36.648 -14.982  -9.220  1.00 77.07           C  
ANISOU 5149  CD  LYS A 664     8072   8955  12257   1277    847   -793       C  
ATOM   5150  CE  LYS A 664      37.290 -15.330 -10.572  1.00 80.15           C  
ANISOU 5150  CE  LYS A 664     8320   9463  12671   1393   1132  -1116       C  
ATOM   5151  NZ  LYS A 664      38.707 -14.882 -10.711  1.00 80.99           N  
ANISOU 5151  NZ  LYS A 664     8133   9756  12882   1461   1243  -1061       N  
ATOM   5152  N   CYS A 665      31.759 -13.820  -8.552  1.00 64.48           N  
ANISOU 5152  N   CYS A 665     7383   7316   9800    738    495   -607       N  
ATOM   5153  CA  CYS A 665      30.817 -13.439  -9.605  1.00 61.88           C  
ANISOU 5153  CA  CYS A 665     7211   7114   9187    630    593   -760       C  
ATOM   5154  C   CYS A 665      30.157 -12.085  -9.422  1.00 58.52           C  
ANISOU 5154  C   CYS A 665     6893   6861   8482    457    532   -598       C  
ATOM   5155  O   CYS A 665      29.499 -11.602 -10.339  1.00 58.09           O  
ANISOU 5155  O   CYS A 665     6934   6944   8194    360    608   -681       O  
ATOM   5156  CB  CYS A 665      29.728 -14.507  -9.738  1.00 61.43           C  
ANISOU 5156  CB  CYS A 665     7305   6847   9188    639    549   -885       C  
ATOM   5157  SG  CYS A 665      30.342 -16.028 -10.415  1.00 66.72           S  
ANISOU 5157  SG  CYS A 665     7869   7312  10171    830    667  -1186       S  
ATOM   5158  N   SER A 666      30.318 -11.470  -8.257  1.00 57.94           N  
ANISOU 5158  N   SER A 666     6798   6781   8436    416    390   -376       N  
ATOM   5159  CA  SER A 666      29.584 -10.243  -7.951  1.00 56.00           C  
ANISOU 5159  CA  SER A 666     6657   6644   7975    264    318   -249       C  
ATOM   5160  C   SER A 666      29.773  -9.160  -9.021  1.00 55.77           C  
ANISOU 5160  C   SER A 666     6599   6829   7761    177    438   -281       C  
ATOM   5161  O   SER A 666      30.840  -9.015  -9.616  1.00 53.22           O  
ANISOU 5161  O   SER A 666     6124   6624   7473    216    552   -321       O  
ATOM   5162  CB  SER A 666      29.972  -9.692  -6.578  1.00 54.74           C  
ANISOU 5162  CB  SER A 666     6447   6478   7874    236    166    -54       C  
ATOM   5163  OG  SER A 666      29.042  -8.706  -6.169  1.00 51.52           O  
ANISOU 5163  OG  SER A 666     6161   6122   7293    108     91     23       O  
ATOM   5164  N   THR A 667      28.702  -8.421  -9.268  1.00 56.56           N  
ANISOU 5164  N   THR A 667     6833   6983   7674     54    410   -242       N  
ATOM   5165  CA  THR A 667      28.695  -7.357 -10.257  1.00 56.66           C  
ANISOU 5165  CA  THR A 667     6826   7187   7515    -52    491   -217       C  
ATOM   5166  C   THR A 667      28.492  -5.984  -9.574  1.00 52.46           C  
ANISOU 5166  C   THR A 667     6302   6670   6961   -160    380    -40       C  
ATOM   5167  O   THR A 667      28.675  -4.929 -10.203  1.00 47.53           O  
ANISOU 5167  O   THR A 667     5626   6175   6260   -255    416     40       O  
ATOM   5168  CB  THR A 667      27.578  -7.645 -11.295  1.00 58.40           C  
ANISOU 5168  CB  THR A 667     7178   7457   7555   -110    545   -322       C  
ATOM   5169  OG1 THR A 667      28.022  -7.284 -12.607  1.00 59.83           O  
ANISOU 5169  OG1 THR A 667     7285   7864   7582   -161    688   -370       O  
ATOM   5170  CG2 THR A 667      26.279  -6.910 -10.945  1.00 58.83           C  
ANISOU 5170  CG2 THR A 667     7364   7472   7518   -219    429   -205       C  
ATOM   5171  N   SER A 668      28.172  -6.027  -8.275  1.00 47.96           N  
ANISOU 5171  N   SER A 668     5783   5968   6471   -145    245     18       N  
ATOM   5172  CA  SER A 668      27.667  -4.882  -7.511  1.00 44.83           C  
ANISOU 5172  CA  SER A 668     5429   5553   6050   -237    135    120       C  
ATOM   5173  C   SER A 668      28.712  -3.836  -7.137  1.00 43.39           C  
ANISOU 5173  C   SER A 668     5116   5423   5948   -284     95    204       C  
ATOM   5174  O   SER A 668      29.643  -4.116  -6.380  1.00 46.32           O  
ANISOU 5174  O   SER A 668     5392   5780   6426   -235     45    224       O  
ATOM   5175  CB  SER A 668      27.011  -5.382  -6.223  1.00 46.18           C  
ANISOU 5175  CB  SER A 668     5688   5612   6247   -209     20    130       C  
ATOM   5176  OG  SER A 668      26.951  -4.356  -5.255  1.00 47.51           O  
ANISOU 5176  OG  SER A 668     5851   5781   6418   -274    -79    188       O  
ATOM   5177  N   SER A 669      28.514  -2.619  -7.631  1.00 40.34           N  
ANISOU 5177  N   SER A 669     4717   5083   5529   -389     97    271       N  
ATOM   5178  CA  SER A 669      29.400  -1.495  -7.351  1.00 39.76           C  
ANISOU 5178  CA  SER A 669     4519   5032   5554   -462     45    357       C  
ATOM   5179  C   SER A 669      29.411  -1.040  -5.883  1.00 40.01           C  
ANISOU 5179  C   SER A 669     4567   4973   5661   -481   -105    347       C  
ATOM   5180  O   SER A 669      30.388  -0.445  -5.432  1.00 46.08           O  
ANISOU 5180  O   SER A 669     5219   5758   6533   -522   -167    387       O  
ATOM   5181  CB  SER A 669      29.025  -0.310  -8.244  1.00 40.70           C  
ANISOU 5181  CB  SER A 669     4625   5187   5651   -580     64    454       C  
ATOM   5182  OG  SER A 669      27.731   0.180  -7.930  1.00 39.07           O  
ANISOU 5182  OG  SER A 669     4545   4877   5424   -616     -6    447       O  
ATOM   5183  N   LEU A 670      28.342  -1.302  -5.137  1.00 39.18           N  
ANISOU 5183  N   LEU A 670     4597   4796   5495   -462   -162    290       N  
ATOM   5184  CA  LEU A 670      28.311  -0.945  -3.711  1.00 35.83           C  
ANISOU 5184  CA  LEU A 670     4190   4335   5090   -484   -290    254       C  
ATOM   5185  C   LEU A 670      29.076  -1.966  -2.877  1.00 36.10           C  
ANISOU 5185  C   LEU A 670     4174   4406   5136   -416   -343    266       C  
ATOM   5186  O   LEU A 670      29.834  -1.590  -1.982  1.00 38.75           O  
ANISOU 5186  O   LEU A 670     4433   4775   5515   -453   -447    277       O  
ATOM   5187  CB  LEU A 670      26.876  -0.803  -3.202  1.00 32.71           C  
ANISOU 5187  CB  LEU A 670     3932   3885   4611   -495   -316    193       C  
ATOM   5188  CG  LEU A 670      26.682  -0.465  -1.718  1.00 32.35           C  
ANISOU 5188  CG  LEU A 670     3913   3846   4532   -522   -424    121       C  
ATOM   5189  CD1 LEU A 670      27.420   0.821  -1.331  1.00 35.89           C  
ANISOU 5189  CD1 LEU A 670     4275   4275   5085   -606   -505     83       C  
ATOM   5190  CD2 LEU A 670      25.181  -0.366  -1.383  1.00 26.37           C  
ANISOU 5190  CD2 LEU A 670     3273   3057   3691   -521   -409     57       C  
ATOM   5191  N   LEU A 671      28.897  -3.255  -3.165  1.00 34.10           N  
ANISOU 5191  N   LEU A 671     3954   4141   4862   -323   -285    271       N  
ATOM   5192  CA  LEU A 671      29.624  -4.280  -2.417  1.00 34.90           C  
ANISOU 5192  CA  LEU A 671     3987   4249   5023   -250   -347    318       C  
ATOM   5193  C   LEU A 671      31.126  -4.094  -2.579  1.00 40.22           C  
ANISOU 5193  C   LEU A 671     4477   4976   5828   -238   -352    366       C  
ATOM   5194  O   LEU A 671      31.884  -4.291  -1.633  1.00 44.24           O  
ANISOU 5194  O   LEU A 671     4897   5518   6395   -232   -466    430       O  
ATOM   5195  CB  LEU A 671      29.232  -5.690  -2.846  1.00 32.69           C  
ANISOU 5195  CB  LEU A 671     3755   3900   4765   -149   -282    308       C  
ATOM   5196  CG  LEU A 671      29.901  -6.804  -2.023  1.00 31.51           C  
ANISOU 5196  CG  LEU A 671     3526   3719   4728    -68   -367    392       C  
ATOM   5197  CD1 LEU A 671      29.539  -6.671  -0.547  1.00 29.04           C  
ANISOU 5197  CD1 LEU A 671     3255   3455   4322   -133   -520    471       C  
ATOM   5198  CD2 LEU A 671      29.537  -8.184  -2.540  1.00 25.26           C  
ANISOU 5198  CD2 LEU A 671     2770   2808   4019     34   -305    366       C  
ATOM   5199  N   GLU A 672      31.541  -3.713  -3.783  1.00 43.16           N  
ANISOU 5199  N   GLU A 672     4781   5381   6236   -243   -231    352       N  
ATOM   5200  CA  GLU A 672      32.947  -3.462  -4.091  1.00 44.97           C  
ANISOU 5200  CA  GLU A 672     4812   5683   6591   -239   -207    406       C  
ATOM   5201  C   GLU A 672      33.473  -2.359  -3.173  1.00 45.20           C  
ANISOU 5201  C   GLU A 672     4776   5738   6661   -352   -356    456       C  
ATOM   5202  O   GLU A 672      34.502  -2.523  -2.508  1.00 47.08           O  
ANISOU 5202  O   GLU A 672     4874   6017   6998   -342   -447    516       O  
ATOM   5203  CB  GLU A 672      33.070  -3.057  -5.562  1.00 47.79           C  
ANISOU 5203  CB  GLU A 672     5123   6111   6924   -263    -44    394       C  
ATOM   5204  CG  GLU A 672      34.474  -2.988  -6.137  1.00 54.34           C  
ANISOU 5204  CG  GLU A 672     5728   7048   7868   -245     37    446       C  
ATOM   5205  CD  GLU A 672      34.461  -2.817  -7.666  1.00 60.34           C  
ANISOU 5205  CD  GLU A 672     6453   7928   8544   -266    226    429       C  
ATOM   5206  OE1 GLU A 672      35.412  -3.292  -8.336  1.00 63.67           O  
ANISOU 5206  OE1 GLU A 672     6710   8460   9023   -197    358    413       O  
ATOM   5207  OE2 GLU A 672      33.489  -2.222  -8.199  1.00 60.95           O  
ANISOU 5207  OE2 GLU A 672     6658   8007   8492   -351    244    433       O  
ATOM   5208  N   ALA A 673      32.726  -1.260  -3.110  1.00 39.91           N  
ANISOU 5208  N   ALA A 673     4202   5034   5929   -459   -391    421       N  
ATOM   5209  CA  ALA A 673      33.133  -0.075  -2.355  1.00 38.24           C  
ANISOU 5209  CA  ALA A 673     3938   4818   5774   -579   -526    422       C  
ATOM   5210  C   ALA A 673      33.101  -0.284  -0.840  1.00 39.73           C  
ANISOU 5210  C   ALA A 673     4163   5027   5904   -593   -687    381       C  
ATOM   5211  O   ALA A 673      33.939   0.260  -0.113  1.00 38.95           O  
ANISOU 5211  O   ALA A 673     3961   4971   5866   -671   -817    392       O  
ATOM   5212  CB  ALA A 673      32.247   1.093  -2.729  1.00 36.05           C  
ANISOU 5212  CB  ALA A 673     3751   4462   5487   -671   -515    380       C  
ATOM   5213  N   CYS A 674      32.128  -1.055  -0.365  1.00 38.03           N  
ANISOU 5213  N   CYS A 674     4087   4801   5560   -534   -685    344       N  
ATOM   5214  CA  CYS A 674      32.002  -1.312   1.063  1.00 37.29           C  
ANISOU 5214  CA  CYS A 674     4030   4775   5364   -560   -828    328       C  
ATOM   5215  C   CYS A 674      33.097  -2.266   1.526  1.00 35.50           C  
ANISOU 5215  C   CYS A 674     3666   4619   5205   -506   -907    457       C  
ATOM   5216  O   CYS A 674      33.720  -2.031   2.553  1.00 36.27           O  
ANISOU 5216  O   CYS A 674     3690   4810   5279   -577  -1063    483       O  
ATOM   5217  CB  CYS A 674      30.607  -1.851   1.407  1.00 38.80           C  
ANISOU 5217  CB  CYS A 674     4391   4952   5400   -526   -794    283       C  
ATOM   5218  SG  CYS A 674      29.335  -0.567   1.393  1.00 38.40           S  
ANISOU 5218  SG  CYS A 674     4470   4842   5279   -603   -758    121       S  
ATOM   5219  N   THR A 675      33.349  -3.326   0.765  1.00 33.40           N  
ANISOU 5219  N   THR A 675     3351   4305   5035   -383   -807    531       N  
ATOM   5220  CA  THR A 675      34.423  -4.255   1.115  1.00 37.46           C  
ANISOU 5220  CA  THR A 675     3703   4851   5678   -308   -876    662       C  
ATOM   5221  C   THR A 675      35.792  -3.638   0.855  1.00 38.36           C  
ANISOU 5221  C   THR A 675     3612   5019   5944   -343   -901    706       C  
ATOM   5222  O   THR A 675      36.809  -4.129   1.348  1.00 35.29           O  
ANISOU 5222  O   THR A 675     3054   4680   5673   -311  -1001    824       O  
ATOM   5223  CB  THR A 675      34.322  -5.611   0.361  1.00 38.60           C  
ANISOU 5223  CB  THR A 675     3838   4895   5933   -150   -755    694       C  
ATOM   5224  OG1 THR A 675      34.363  -5.393  -1.054  1.00 39.31           O  
ANISOU 5224  OG1 THR A 675     3915   4948   6073   -110   -568    605       O  
ATOM   5225  CG2 THR A 675      33.039  -6.335   0.733  1.00 36.05           C  
ANISOU 5225  CG2 THR A 675     3693   4513   5491   -128   -761    687       C  
ATOM   5226  N   PHE A 676      35.824  -2.575   0.060  1.00 40.58           N  
ANISOU 5226  N   PHE A 676     3889   5291   6241   -414   -817    637       N  
ATOM   5227  CA  PHE A 676      37.045  -1.798  -0.082  1.00 40.87           C  
ANISOU 5227  CA  PHE A 676     3729   5385   6413   -489   -860    690       C  
ATOM   5228  C   PHE A 676      37.316  -1.090   1.225  1.00 42.89           C  
ANISOU 5228  C   PHE A 676     3971   5702   6622   -624  -1080    682       C  
ATOM   5229  O   PHE A 676      38.436  -1.145   1.735  1.00 44.29           O  
ANISOU 5229  O   PHE A 676     3968   5959   6902   -652  -1204    778       O  
ATOM   5230  CB  PHE A 676      36.932  -0.778  -1.203  1.00 38.54           C  
ANISOU 5230  CB  PHE A 676     3433   5062   6147   -558   -735    653       C  
ATOM   5231  CG  PHE A 676      38.213  -0.088  -1.503  1.00 37.95           C  
ANISOU 5231  CG  PHE A 676     3132   5050   6236   -634   -757    741       C  
ATOM   5232  CD1 PHE A 676      38.556   1.075  -0.843  1.00 38.22           C  
ANISOU 5232  CD1 PHE A 676     3125   5080   6317   -796   -918    732       C  
ATOM   5233  CD2 PHE A 676      39.086  -0.608  -2.440  1.00 38.96           C  
ANISOU 5233  CD2 PHE A 676     3077   5245   6480   -548   -612    819       C  
ATOM   5234  CE1 PHE A 676      39.751   1.717  -1.114  1.00 39.99           C  
ANISOU 5234  CE1 PHE A 676     3126   5356   6714   -884   -951    832       C  
ATOM   5235  CE2 PHE A 676      40.281   0.025  -2.719  1.00 40.95           C  
ANISOU 5235  CE2 PHE A 676     3095   5575   6887   -626   -624    921       C  
ATOM   5236  CZ  PHE A 676      40.615   1.192  -2.054  1.00 40.40           C  
ANISOU 5236  CZ  PHE A 676     2984   5491   6876   -801   -801    943       C  
ATOM   5237  N   ARG A 677      36.291  -0.420   1.757  1.00 44.04           N  
ANISOU 5237  N   ARG A 677     4297   5822   6615   -708  -1128    554       N  
ATOM   5238  CA  ARG A 677      36.394   0.218   3.066  1.00 47.21           C  
ANISOU 5238  CA  ARG A 677     4712   6301   6924   -839  -1328    486       C  
ATOM   5239  C   ARG A 677      36.901  -0.831   4.024  1.00 54.15           C  
ANISOU 5239  C   ARG A 677     5517   7306   7751   -800  -1460    614       C  
ATOM   5240  O   ARG A 677      37.962  -0.648   4.607  1.00 57.81           O  
ANISOU 5240  O   ARG A 677     5822   7866   8279   -873  -1617    686       O  
ATOM   5241  CB  ARG A 677      35.063   0.800   3.526  1.00 46.09           C  
ANISOU 5241  CB  ARG A 677     4778   6125   6609   -892  -1323    307       C  
ATOM   5242  CG  ARG A 677      34.748   2.152   2.894  1.00 46.60           C  
ANISOU 5242  CG  ARG A 677     4875   6058   6775   -974  -1272    186       C  
ATOM   5243  CD  ARG A 677      35.190   3.302   3.789  1.00 46.78           C  
ANISOU 5243  CD  ARG A 677     4854   6097   6825  -1134  -1447     53       C  
ATOM   5244  NE  ARG A 677      34.373   3.379   4.994  1.00 43.72           N  
ANISOU 5244  NE  ARG A 677     4601   5792   6218  -1173  -1526   -123       N  
ATOM   5245  CZ  ARG A 677      34.623   4.169   6.031  1.00 46.00           C  
ANISOU 5245  CZ  ARG A 677     4879   6146   6452  -1308  -1687   -293       C  
ATOM   5246  NH1 ARG A 677      35.681   4.980   6.033  1.00 50.13           N  
ANISOU 5246  NH1 ARG A 677     5262   6633   7153  -1427  -1809   -301       N  
ATOM   5247  NH2 ARG A 677      33.806   4.145   7.078  1.00 45.54           N  
ANISOU 5247  NH2 ARG A 677     4944   6205   6153  -1334  -1725   -464       N  
ATOM   5248  N   ARG A 678      36.144  -1.919   4.182  1.00 57.64           N  
ANISOU 5248  N   ARG A 678     6063   7744   8093   -697  -1412    663       N  
ATOM   5249  CA  ARG A 678      36.709  -3.224   4.571  1.00 65.44           C  
ANISOU 5249  CA  ARG A 678     6941   8780   9145   -602  -1482    858       C  
ATOM   5250  C   ARG A 678      35.690  -4.281   4.930  1.00 67.65           C  
ANISOU 5250  C   ARG A 678     7358   9044   9303   -529  -1461    911       C  
ATOM   5251  O   ARG A 678      34.691  -3.975   5.575  1.00 68.93           O  
ANISOU 5251  O   ARG A 678     7679   9269   9243   -604  -1485    821       O  
ATOM   5252  CB  ARG A 678      37.760  -3.133   5.685  1.00 71.54           C  
ANISOU 5252  CB  ARG A 678     7553   9715   9916   -697  -1718    973       C  
ATOM   5253  CG  ARG A 678      39.170  -3.316   5.133  1.00 74.70           C  
ANISOU 5253  CG  ARG A 678     7697  10096  10591   -640  -1724   1105       C  
ATOM   5254  CD  ARG A 678      40.184  -2.335   5.684  1.00 78.49           C  
ANISOU 5254  CD  ARG A 678     8028  10693  11103   -799  -1901   1105       C  
ATOM   5255  NE  ARG A 678      41.146  -2.028   4.632  1.00 80.00           N  
ANISOU 5255  NE  ARG A 678     8028  10819  11550   -760  -1796   1142       N  
ATOM   5256  CZ  ARG A 678      42.395  -1.621   4.822  1.00 82.80           C  
ANISOU 5256  CZ  ARG A 678     8149  11253  12057   -838  -1922   1236       C  
ATOM   5257  NH1 ARG A 678      42.897  -1.434   6.042  1.00 84.53           N  
ANISOU 5257  NH1 ARG A 678     8295  11623  12199   -969  -2183   1296       N  
ATOM   5258  NH2 ARG A 678      43.147  -1.403   3.758  1.00 84.90           N  
ANISOU 5258  NH2 ARG A 678     8243  11472  12544   -793  -1784   1275       N  
ATOM   5259  N   PRO A 679      35.980  -5.544   4.551  1.00 70.68           N  
ANISOU 5259  N   PRO A 679     7660   9342   9854   -384  -1419   1059       N  
ATOM   5260  CA  PRO A 679      35.029  -6.656   4.612  1.00 71.62           C  
ANISOU 5260  CA  PRO A 679     7895   9383   9935   -300  -1376   1120       C  
ATOM   5261  C   PRO A 679      34.740  -7.146   6.039  1.00 74.72           C  
ANISOU 5261  C   PRO A 679     8309   9922  10160   -376  -1566   1279       C  
ATOM   5262  O   PRO A 679      33.667  -7.707   6.302  1.00 73.47           O  
ANISOU 5262  O   PRO A 679     8285   9747   9881   -371  -1541   1307       O  
ATOM   5263  CB  PRO A 679      35.732  -7.748   3.801  1.00 72.30           C  
ANISOU 5263  CB  PRO A 679     7835   9317  10318   -128  -1298   1215       C  
ATOM   5264  CG  PRO A 679      37.185  -7.501   4.034  1.00 73.74           C  
ANISOU 5264  CG  PRO A 679     7781   9579  10657   -137  -1405   1316       C  
ATOM   5265  CD  PRO A 679      37.343  -6.015   4.217  1.00 72.28           C  
ANISOU 5265  CD  PRO A 679     7621   9520  10321   -297  -1443   1191       C  
TER    5266      PRO A 679                                                      
HETATM 5267 FE    FE A 680      13.378 -12.316  -1.571  1.00 30.30          FE  
HETATM 5268  C   CO3 A 681      13.935 -12.577  -4.080  1.00 24.78           C  
HETATM 5269  O1  CO3 A 681      14.316 -12.832  -5.299  1.00 22.30           O  
HETATM 5270  O2  CO3 A 681      13.434 -11.415  -3.783  1.00 22.34           O  
HETATM 5271  O3  CO3 A 681      14.031 -13.476  -3.137  1.00 26.68           O  
HETATM 5272 FE    FE A 682      46.250  10.879  10.728  1.00 60.32          FE  
HETATM 5273  C   CO3 A 683      45.830  11.588  13.408  1.00 55.02           C  
HETATM 5274  O1  CO3 A 683      45.470  11.909  14.614  1.00 53.14           O  
HETATM 5275  O2  CO3 A 683      46.875  12.142  12.878  1.00 51.14           O  
HETATM 5276  O3  CO3 A 683      45.160  10.704  12.719  1.00 58.48           O  
HETATM 5277  C1  NAG A 684       3.972 -21.771  10.645  1.00 68.54           C  
HETATM 5278  C2  NAG A 684       5.439 -22.263  10.606  1.00 72.74           C  
HETATM 5279  C3  NAG A 684       5.785 -23.456  11.522  1.00 73.50           C  
HETATM 5280  C4  NAG A 684       4.824 -23.673  12.690  1.00 73.01           C  
HETATM 5281  C5  NAG A 684       3.388 -23.306  12.326  1.00 70.81           C  
HETATM 5282  C6  NAG A 684       2.408 -23.458  13.498  1.00 70.85           C  
HETATM 5283  C7  NAG A 684       5.391 -23.408   8.406  1.00 73.67           C  
HETATM 5284  C8  NAG A 684       6.000 -23.481   7.031  1.00 72.40           C  
HETATM 5285  N2  NAG A 684       5.901 -22.485   9.232  1.00 73.81           N  
HETATM 5286  O3  NAG A 684       7.080 -23.274  12.067  1.00 73.14           O  
HETATM 5287  O4  NAG A 684       4.923 -25.016  13.119  1.00 75.76           O  
HETATM 5288  O5  NAG A 684       3.392 -21.955  11.917  1.00 69.72           O  
HETATM 5289  O6  NAG A 684       2.844 -24.399  14.461  1.00 68.58           O  
HETATM 5290  O7  NAG A 684       4.475 -24.171   8.723  1.00 72.54           O  
HETATM 5291  C1  NAG A 685      -4.104  -4.893  15.586  1.00 79.99           C  
HETATM 5292  C2  NAG A 685      -4.277  -3.846  16.709  1.00 85.62           C  
HETATM 5293  C3  NAG A 685      -3.083  -3.830  17.666  1.00 86.07           C  
HETATM 5294  C4  NAG A 685      -2.800  -5.249  18.147  1.00 86.39           C  
HETATM 5295  C5  NAG A 685      -2.446  -6.125  16.947  1.00 87.13           C  
HETATM 5296  C6  NAG A 685      -2.183  -7.590  17.329  1.00 88.99           C  
HETATM 5297  C7  NAG A 685      -4.701  -1.383  16.752  1.00 92.24           C  
HETATM 5298  C8  NAG A 685      -5.000  -0.177  15.902  1.00 93.35           C  
HETATM 5299  N2  NAG A 685      -4.558  -2.545  16.095  1.00 89.27           N  
HETATM 5300  O3  NAG A 685      -3.336  -3.003  18.782  1.00 86.36           O  
HETATM 5301  O4  NAG A 685      -1.740  -5.269  19.087  1.00 84.80           O  
HETATM 5302  O5  NAG A 685      -3.488  -6.114  15.983  1.00 84.24           O  
HETATM 5303  O6  NAG A 685      -2.342  -7.783  18.722  1.00 93.20           O  
HETATM 5304  O7  NAG A 685      -4.594  -1.250  17.973  1.00 92.73           O  
HETATM 5305  S   SO4 A 686      46.509  13.088   9.723  1.00117.44           S  
HETATM 5306  O1  SO4 A 686      47.559  12.196  10.210  1.00117.14           O  
HETATM 5307  O2  SO4 A 686      46.044  12.610   8.425  1.00118.53           O  
HETATM 5308  O3  SO4 A 686      45.381  13.096  10.648  1.00116.49           O  
HETATM 5309  O4  SO4 A 686      47.037  14.447   9.587  1.00117.71           O  
HETATM 5310  O   HOH A 687      15.700 -13.208   1.218  1.00 14.47           O  
HETATM 5311  O   HOH A 688       8.662   3.350 -10.012  1.00 23.71           O  
HETATM 5312  O   HOH A 689      10.533  -5.717   1.112  1.00  6.83           O  
HETATM 5313  O   HOH A 690      55.418  12.215 -18.340  1.00 31.82           O  
HETATM 5314  O   HOH A 691      33.699   3.824  26.316  1.00 25.00           O  
HETATM 5315  O   HOH A 692      50.464  23.146  20.154  1.00 68.41           O  
HETATM 5316  O   HOH A 693      37.517   0.494  33.588  1.00 19.45           O  
HETATM 5317  O   HOH A 694      29.703  18.334  -3.577  1.00  8.63           O  
CONECT   76  368                                                                
CONECT  149  298                                                                
CONECT  298  149                                                                
CONECT  368   76                                                                
CONECT  729 5272                                                                
CONECT  906 1468                                                                
CONECT 1048 2564                                                                
CONECT 1209 1323                                                                
CONECT 1227 1350                                                                
CONECT 1300 1340                                                                
CONECT 1323 1209                                                                
CONECT 1340 1300                                                                
CONECT 1350 1227                                                                
CONECT 1427 5272                                                                
CONECT 1468  906                                                                
CONECT 1726 1843                                                                
CONECT 1843 1726                                                                
CONECT 2564 1048                                                                
CONECT 2622 4592                                                                
CONECT 2674 2921                                                                
CONECT 2756 2857                                                                
CONECT 2857 2756                                                                
CONECT 2921 2674                                                                
CONECT 3027 5267                                                                
CONECT 3098 5218                                                                
CONECT 3181 5277                                                                
CONECT 3218 4925                                                                
CONECT 3279 5267                                                                
CONECT 3460 4019                                                                
CONECT 3646 5157                                                                
CONECT 3732 3829                                                                
CONECT 3806 3881                                                                
CONECT 3829 3732                                                                
CONECT 3881 3806                                                                
CONECT 3975 5267                                                                
CONECT 4019 3460                                                                
CONECT 4335 4445                                                                
CONECT 4445 4335                                                                
CONECT 4509 5267                                                                
CONECT 4592 2622                                                                
CONECT 4719 5291                                                                
CONECT 4747 4782                                                                
CONECT 4782 4747                                                                
CONECT 4925 3218                                                                
CONECT 5157 3646                                                                
CONECT 5218 3098                                                                
CONECT 5267 3027 3279 3975 4509                                                 
CONECT 5267 5270 5271                                                           
CONECT 5268 5269 5270 5271                                                      
CONECT 5269 5268                                                                
CONECT 5270 5267 5268                                                           
CONECT 5271 5267 5268                                                           
CONECT 5272  729 1427 5275 5276                                                 
CONECT 5272 5306 5308                                                           
CONECT 5273 5274 5275 5276                                                      
CONECT 5274 5273                                                                
CONECT 5275 5272 5273                                                           
CONECT 5276 5272 5273                                                           
CONECT 5277 3181 5278 5288                                                      
CONECT 5278 5277 5279 5285                                                      
CONECT 5279 5278 5280 5286                                                      
CONECT 5280 5279 5281 5287                                                      
CONECT 5281 5280 5282 5288                                                      
CONECT 5282 5281 5289                                                           
CONECT 5283 5284 5285 5290                                                      
CONECT 5284 5283                                                                
CONECT 5285 5278 5283                                                           
CONECT 5286 5279                                                                
CONECT 5287 5280                                                                
CONECT 5288 5277 5281                                                           
CONECT 5289 5282                                                                
CONECT 5290 5283                                                                
CONECT 5291 4719 5292 5302                                                      
CONECT 5292 5291 5293 5299                                                      
CONECT 5293 5292 5294 5300                                                      
CONECT 5294 5293 5295 5301                                                      
CONECT 5295 5294 5296 5302                                                      
CONECT 5296 5295 5303                                                           
CONECT 5297 5298 5299 5304                                                      
CONECT 5298 5297                                                                
CONECT 5299 5292 5297                                                           
CONECT 5300 5293                                                                
CONECT 5301 5294                                                                
CONECT 5302 5291 5295                                                           
CONECT 5303 5296                                                                
CONECT 5304 5297                                                                
CONECT 5305 5306 5307 5308 5309                                                 
CONECT 5306 5272 5305                                                           
CONECT 5307 5305                                                                
CONECT 5308 5272 5305                                                           
CONECT 5309 5305                                                                
MASTER      505    0    7   31   34    0    0    6 5316    1   91   53          
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.