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***  tp-oleron  ***

elNémo ID: 22060918352777740

Job options:

ID        	=	 22060918352777740
JOBID     	=	 tp-oleron
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 tp-oleron

HEADER    HYDROLASE                               19-JAN-21   7BM6              
TITLE     STRUCTURE-FUNCTION ANALYSIS OF A NEW PL17 OLIGOALGINATE LYASE FROM THE
TITLE    2 MARINE BACTERIUM ZOBELLIA GALACTANIVORANS DSIJT                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALGINATE LYASE, FAMILY PL17;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 4.2.2.3;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: THE ACTIVE SITE TYROSINE Y274 WAS MUTATED TO ALANINE  
COMPND   7 Y247A THE N-TERMINAL PEPTIDE (1-23) WAS NOT INCLUDED IN RECOMBINANT  
COMPND   8 CONSTRUCTION DEFINED BY ELECTRON DENSITY                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ZOBELLIA GALACTANIVORANS (STRAIN DSM 12802 /    
SOURCE   3 CCUG 47099 / CIP 106680 / NCIMB 13871 / DSIJ);                       
SOURCE   4 ORGANISM_TAXID: 63186;                                               
SOURCE   5 STRAIN: DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / DSIJ;    
SOURCE   6 GENE: ALYA3, ZOBELLIA_2624;                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    ALGINATE LYASE, DELTA-GULURONATE COMPLEX, FAMILY PL17, EXO-ACTING     
KEYWDS   2 MARINE ENZYME, HYDROLASE                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.CZJZEK,T.RORET,D.JOUANNEAU,N.LE DUFF,A.JEUDY                        
REVDAT   2   01-DEC-21 7BM6    1       JRNL                                     
REVDAT   1   14-JUL-21 7BM6    0                                                
JRNL        AUTH   D.JOUANNEAU,L.J.KLAU,R.LAROCQUE,A.JAFFRENNOU,G.DUVAL,        
JRNL        AUTH 2 N.LE DUFF,T.RORET,A.JEUDY,F.L.AACHMANN,M.CZJZEK,F.THOMAS     
JRNL        TITL   STRUCTURE-FUNCTION ANALYSIS OF A NEW PL17 OLIGOALGINATE      
JRNL        TITL 2 LYASE FROM THE MARINE BACTERIUM ZOBELLIA GALACTANIVORANS     
JRNL        TITL 3 DSIJT.                                                       
JRNL        REF    GLYCOBIOLOGY                  V.  31  1364 2021              
JRNL        REFN                   ESSN 1460-2423                               
JRNL        PMID   34184062                                                     
JRNL        DOI    10.1093/GLYCOB/CWAB058                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.16 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0131                                      
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) : 2.16                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 130343                         
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) : 0.155                           
REMARK   3   R VALUE            (WORKING SET) : 0.153                           
REMARK   3   FREE R VALUE                     : 0.182                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6752                            
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) : 2.16                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.22                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9390                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.76                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2480                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 495                          
REMARK   3   BIN FREE R VALUE                    : 0.2890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11619                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 912                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
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): 0.134         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.125         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.090         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.495         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12030 ; 0.016 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 11180 ; 0.006 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 16299 ; 1.688 ; 1.952       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 25770 ; 1.013 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1482 ; 6.284 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   616 ;34.802 ;25.032       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2044 ;13.809 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    48 ;14.840 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1734 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 13895 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2879 ; 0.002 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    25        A   226                          
REMARK   3    RESIDUE RANGE :   A   253        A   400                          
REMARK   3    ORIGIN FOR THE GROUP (A): 103.8130  91.2880  17.2740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0049 T22:   0.0308                                     
REMARK   3      T33:   0.0362 T12:   0.0027                                     
REMARK   3      T13:  -0.0036 T23:   0.0055                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2689 L22:   0.1836                                     
REMARK   3      L33:   0.1869 L12:   0.0298                                     
REMARK   3      L13:  -0.1184 L23:  -0.0296                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0021 S12:  -0.0002 S13:   0.0169                       
REMARK   3      S21:   0.0248 S22:  -0.0063 S23:  -0.0004                       
REMARK   3      S31:  -0.0168 S32:  -0.0322 S33:   0.0041                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   401        A   672                          
REMARK   3    RESIDUE RANGE :   A   688        A   751                          
REMARK   3    ORIGIN FOR THE GROUP (A): 138.9970  87.4060   0.5700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0013 T22:   0.0301                                     
REMARK   3      T33:   0.0580 T12:  -0.0032                                     
REMARK   3      T13:  -0.0021 T23:   0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1333 L22:   0.0907                                     
REMARK   3      L33:   0.1614 L12:   0.0516                                     
REMARK   3      L13:   0.0039 L23:   0.0770                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0089 S12:  -0.0018 S13:  -0.0322                       
REMARK   3      S21:  -0.0011 S22:  -0.0056 S23:  -0.0298                       
REMARK   3      S31:  -0.0105 S32:   0.0410 S33:  -0.0032                       
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   227        A   252                          
REMARK   3    ORIGIN FOR THE GROUP (A): 120.7450  77.9300  29.4720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0236 T22:   0.0533                                     
REMARK   3      T33:   0.0304 T12:  -0.0094                                     
REMARK   3      T13:  -0.0142 T23:   0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3828 L22:   0.9067                                     
REMARK   3      L33:   0.8379 L12:  -0.6551                                     
REMARK   3      L13:  -0.0573 L23:  -0.6706                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0728 S12:  -0.0018 S13:  -0.0443                       
REMARK   3      S21:   0.0180 S22:   0.0251 S23:  -0.0078                       
REMARK   3      S31:   0.0253 S32:  -0.0024 S33:   0.0477                       
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   673        A   687                          
REMARK   3    ORIGIN FOR THE GROUP (A): 129.1940  95.9110 -23.7260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0222 T22:   0.0280                                     
REMARK   3      T33:   0.0574 T12:  -0.0199                                     
REMARK   3      T13:   0.0054 T23:  -0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3080 L22:   0.4328                                     
REMARK   3      L33:   3.6592 L12:   1.2985                                     
REMARK   3      L13:   3.9389 L23:   1.1400                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0651 S12:   0.1383 S13:   0.0132                       
REMARK   3      S21:  -0.0071 S22:   0.0485 S23:   0.0085                       
REMARK   3      S31:  -0.0795 S32:   0.1252 S33:   0.0166                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    25        B   226                          
REMARK   3    RESIDUE RANGE :   B   253        B   400                          
REMARK   3    ORIGIN FOR THE GROUP (A): 119.6770 101.1300 -42.1380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0377 T22:   0.0129                                     
REMARK   3      T33:   0.0319 T12:  -0.0167                                     
REMARK   3      T13:  -0.0009 T23:  -0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2166 L22:   0.2154                                     
REMARK   3      L33:   0.1733 L12:   0.0688                                     
REMARK   3      L13:  -0.0986 L23:  -0.0755                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0124 S12:   0.0099 S13:  -0.0091                       
REMARK   3      S21:  -0.0171 S22:   0.0067 S23:   0.0165                       
REMARK   3      S31:  -0.0400 S32:  -0.0008 S33:   0.0058                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   401        B   672                          
REMARK   3    RESIDUE RANGE :   B   688        B   751                          
REMARK   3    ORIGIN FOR THE GROUP (A): 108.5380  67.6750 -25.0880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0334 T22:   0.0214                                     
REMARK   3      T33:   0.0476 T12:  -0.0168                                     
REMARK   3      T13:   0.0345 T23:  -0.0162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3363 L22:   0.5076                                     
REMARK   3      L33:   0.4386 L12:   0.0186                                     
REMARK   3      L13:   0.3699 L23:   0.1325                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0071 S12:  -0.0497 S13:  -0.0338                       
REMARK   3      S21:   0.0754 S22:   0.0054 S23:   0.0358                       
REMARK   3      S31:   0.0361 S32:  -0.0621 S33:  -0.0125                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   227        B   252                          
REMARK   3    ORIGIN FOR THE GROUP (A): 125.6470  79.9910 -53.8900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0857 T22:   0.0420                                     
REMARK   3      T33:   0.0583 T12:  -0.0349                                     
REMARK   3      T13:   0.0186 T23:  -0.0302                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0579 L22:   3.5456                                     
REMARK   3      L33:   0.4249 L12:  -0.2566                                     
REMARK   3      L13:   0.0130 L23:  -1.0111                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0230 S12:   0.0306 S13:  -0.0005                       
REMARK   3      S21:  -0.0638 S22:  -0.0247 S23:  -0.1715                       
REMARK   3      S31:   0.0129 S32:  -0.0300 S33:   0.0477                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   673        B   687                          
REMARK   3    ORIGIN FOR THE GROUP (A): 104.7880  80.2350  -0.9220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0031 T22:   0.0363                                     
REMARK   3      T33:   0.0482 T12:  -0.0025                                     
REMARK   3      T13:  -0.0005 T23:   0.0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1135 L22:   2.7163                                     
REMARK   3      L33:   4.5229 L12:   1.9734                                     
REMARK   3      L13:   2.2895 L23:   3.4695                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0742 S12:  -0.0771 S13:  -0.0339                       
REMARK   3      S21:   0.0484 S22:  -0.0880 S23:  -0.0076                       
REMARK   3      S31:   0.0493 S32:  -0.1246 S33:   0.0138                       
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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED HYDROGENS       
REMARK   3  HAVE BEEN ADDED IN THE RIDING POSITIONS                             
REMARK   4                                                                      
REMARK   4 7BM6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JAN-21.                  
REMARK 100 THE DEPOSITION ID IS D_1292113395.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JAN-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 2                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER2 X 9M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 137171                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.160                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 21.16                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12000                            
REMARK 200   FOR THE DATA SET  : 16.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.16                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 18.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.57000                            
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: 7BJT                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION AT 13.4 MG.ML-1,        
REMARK 280  SUPPLEMENTED WITH 1.6 MM OF OLIGO-MANNURONATE OF DP3, WAS MIXED     
REMARK 280  WITH 0.2 MICRO-L OF CRYSTALLIZATION SOLUTION THAT CONTAINED 2.4     
REMARK 280  M SODIUM MALONATE (DIBASIC MONOHYDRATE) AND EQUILIBRATED AGAINST    
REMARK 280  A RESERVOIR CONTAINING 100 MICRO-L., PH 7.0, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 296.0K                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      112.24667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       56.12333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       84.18500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       28.06167            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      140.30833            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 49410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     MET A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     TYR A     6                                                      
REMARK 465     ILE A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     GLN A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     LEU A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     PHE A    15                                                      
REMARK 465     VAL A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     LEU A    18                                                      
REMARK 465     LEU A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     PHE A    21                                                      
REMARK 465     SER A    22                                                      
REMARK 465     GLY A    23                                                      
REMARK 465     HIS A    24                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     MET B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     TYR B     6                                                      
REMARK 465     ILE B     7                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     VAL B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     GLN B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     LEU B    13                                                      
REMARK 465     LEU B    14                                                      
REMARK 465     PHE B    15                                                      
REMARK 465     VAL B    16                                                      
REMARK 465     LEU B    17                                                      
REMARK 465     LEU B    18                                                      
REMARK 465     LEU B    19                                                      
REMARK 465     SER B    20                                                      
REMARK 465     PHE B    21                                                      
REMARK 465     SER B    22                                                      
REMARK 465     GLY B    23                                                      
REMARK 465     HIS B    24                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN A 413    CG   OD1  ND2                                       
REMARK 470     ASN B 413    CG   OD1  ND2                                       
REMARK 470     GLU B 504    CD   OE1  OE2                                       
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   311     O    HOH A   901              1.94            
REMARK 500   OG   SER B    79     O    GLY B   463              2.07            
REMARK 500   O4   MAV D     1     O5   MAW D     2              2.14            
REMARK 500   OG1  THR A   581     O    HOH A   902              2.14            
REMARK 500   OD2  ASP A   320     O    HOH A   903              2.16            
REMARK 500   O    HOH B  1189     O    HOH B  1194              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 449   N   -  CA  -  C   ANGL. DEV. = -16.7 DEGREES          
REMARK 500    ARG A 619   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ASP B 397   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG B 637   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  30       -1.86   -158.91                                   
REMARK 500    ILE A  32      -70.40   -118.80                                   
REMARK 500    LYS A  76      -37.47   -138.58                                   
REMARK 500    LYS A  76      -34.83   -140.12                                   
REMARK 500    THR A 133       75.50   -116.61                                   
REMARK 500    ARG A 134       33.42   -149.29                                   
REMARK 500    LEU A 178      -66.14   -121.91                                   
REMARK 500    SER A 187      -92.66   -128.00                                   
REMARK 500    HIS A 198      146.36    179.33                                   
REMARK 500    LEU A 316       30.22    -91.73                                   
REMARK 500    ASP A 318     -176.49    -69.28                                   
REMARK 500    ASN A 327     -152.83     58.43                                   
REMARK 500    GLN A 403       57.71   -113.19                                   
REMARK 500    ASN A 413       71.93   -101.44                                   
REMARK 500    LEU A 427     -157.62     65.32                                   
REMARK 500    ASP A 433       40.82   -145.42                                   
REMARK 500    ARG A 454      140.04   -179.04                                   
REMARK 500    TRP A 473      -71.95   -118.90                                   
REMARK 500    TYR A 506      -60.49    -92.59                                   
REMARK 500    LYS A 661      -74.06   -100.06                                   
REMARK 500    SER A 710       -9.75    -45.28                                   
REMARK 500    ASN A 711      -85.76     81.77                                   
REMARK 500    THR A 712       10.96    -54.14                                   
REMARK 500    ASN A 723      110.68   -165.80                                   
REMARK 500    SER B  30      -20.94   -153.14                                   
REMARK 500    ILE B  32      -70.07   -120.88                                   
REMARK 500    PRO B  75      156.39    -43.02                                   
REMARK 500    LYS B  76      -38.72   -171.12                                   
REMARK 500    SER B  79      155.60    -48.19                                   
REMARK 500    SER B 187      -92.69   -126.27                                   
REMARK 500    ASN B 195       30.25    -94.82                                   
REMARK 500    HIS B 198      147.60   -174.76                                   
REMARK 500    ASN B 327     -151.47     56.65                                   
REMARK 500    GLN B 403       57.28   -115.50                                   
REMARK 500    LEU B 427     -156.95     63.66                                   
REMARK 500    ASP B 433       43.60   -145.35                                   
REMARK 500    ARG B 454      143.56   -172.90                                   
REMARK 500    TRP B 473      -73.19   -119.90                                   
REMARK 500    LYS B 661      -77.53    -95.20                                   
REMARK 500    LYS B 709        5.12    -60.38                                   
REMARK 500    ASN B 711      -96.03     51.92                                   
REMARK 500    GLU B 713      107.86   -163.11                                   
REMARK 500    ASN B 723      117.94   -166.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 802  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  83   OG1                                                    
REMARK 620 2 LEU A 141   O   134.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 803  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 443   O                                                      
REMARK 620 2 HOH A 982   O    78.7                                              
REMARK 620 3 HOH A1031   O    91.3  82.7                                        
REMARK 620 4 HOH A1275   O   100.3 171.3 105.9                                  
REMARK 620 5 HOH A1315   O    92.0  87.1 168.5  84.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 801  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 449   OD1                                                    
REMARK 620 2 HOH A 945   O    91.8                                              
REMARK 620 3 HOH A 951   O    77.4  87.0                                        
REMARK 620 4 HOH A1205   O    90.9 176.0  90.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 801  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B 202   OG1                                                    
REMARK 620 2 ASN B 257   OD1  69.5                                              
REMARK 620 3 TYR B 268   OH  124.8 154.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 802  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 449   OD1                                                    
REMARK 620 2 HOH B 913   O    87.2                                              
REMARK 620 3 HOH B 997   O    76.5  86.8                                        
REMARK 620 4 HOH B1209   O    92.1 177.7  91.0                                  
REMARK 620 N                    1     2     3                                   
DBREF  7BM6 A    1   751  UNP    G0LCA3   G0LCA3_ZOBGA     1    751             
DBREF  7BM6 B    1   751  UNP    G0LCA3   G0LCA3_ZOBGA     1    751             
SEQADV 7BM6 ALA A  274  UNP  G0LCA3    TYR   274 ENGINEERED MUTATION            
SEQADV 7BM6 ALA B  274  UNP  G0LCA3    TYR   274 ENGINEERED MUTATION            
SEQRES   1 A  751  MET ASN MET THR LYS TYR ILE PRO VAL LEU GLN SER LEU          
SEQRES   2 A  751  LEU PHE VAL LEU LEU LEU SER PHE SER GLY HIS ALA GLN          
SEQRES   3 A  751  GLU HIS PRO SER LEU ILE LEU THR LYS ALA GLY VAL GLU          
SEQRES   4 A  751  LYS ILE ARG ALA GLU LEU GLY ASN ILE PRO ILE PHE ASP          
SEQRES   5 A  751  ALA THR LEU GLU LYS VAL LYS ALA GLU VAL ASP ALA GLU          
SEQRES   6 A  751  ILE ALA LEU GLY ILE ASP THR PRO LEU PRO LYS ASP TYR          
SEQRES   7 A  751  SER GLY GLY TYR THR HIS GLU ARG HIS LYS ARG ASN PHE          
SEQRES   8 A  751  PHE ILE LEU GLN LYS ALA GLY VAL LEU TYR GLN ILE LEU          
SEQRES   9 A  751  ASN ASP GLU LYS TYR ALA LEU TYR ILE LYS ASP MET LEU          
SEQRES  10 A  751  PHE GLN TYR GLU GLY MET TYR LYS ASP LEU PRO VAL HIS          
SEQRES  11 A  751  PRO GLN THR ARG SER TYR ALA ARG GLY LYS LEU PHE TRP          
SEQRES  12 A  751  GLN CYS LEU ASN ASP SER ASN TRP LEU VAL TYR VAL SER          
SEQRES  13 A  751  GLN ALA TYR ASP CYS VAL TYR ASP TYR LEU SER LYS LYS          
SEQRES  14 A  751  GLU ARG LYS GLN LEU GLU LYS ASN LEU PHE ARG PRO PHE          
SEQRES  15 A  751  ALA ASP TYR ILE SER ILE GLU ASN PRO GLN PHE TYR ASN          
SEQRES  16 A  751  ARG VAL HIS ASN HIS SER THR TRP GLY ASN ALA ALA VAL          
SEQRES  17 A  751  GLY MET ILE GLY LEU VAL MET GLY ASP GLU GLU LEU ILE          
SEQRES  18 A  751  GLN ARG ALA LEU TYR GLY ILE GLU ASP ASP GLY LEU PRO          
SEQRES  19 A  751  ILE GLY ALA LYS ASP ASN ASP GLY GLY PHE ILE LYS VAL          
SEQRES  20 A  751  GLU GLY GLN LYS ALA GLY PHE LEU ALA ASN ILE ASP GLU          
SEQRES  21 A  751  PRO PHE SER PRO ASP GLY TYR TYR THR GLU GLY PRO TYR          
SEQRES  22 A  751  ALA GLN ARG TYR ALA MET TYR PRO PHE LEU ILE PHE ALA          
SEQRES  23 A  751  GLU ALA LEU HIS ASN VAL ARG PRO GLN GLN LYS ILE PHE          
SEQRES  24 A  751  GLU HIS LYS ASP GLY VAL LEU LEU LYS SER VAL ASN THR          
SEQRES  25 A  751  LEU LEU SER LEU SER ASP ALA ASP GLY GLU PHE PHE PRO          
SEQRES  26 A  751  LEU ASN ASP ALA GLN LYS GLY MET SER TYR HIS SER ARG          
SEQRES  27 A  751  GLU LEU VAL THR ALA VAL ASP ILE ALA TYR HIS TYR GLY          
SEQRES  28 A  751  ASN HIS ASN PRO GLN LEU LEU SER ILE ALA GLU GLU GLN          
SEQRES  29 A  751  GLY GLN VAL LEU LEU ASP ASP SER GLY LEU ALA VAL ALA          
SEQRES  30 A  751  LEU GLY ILE ARG GLU GLY LYS SER GLU ASP PHE GLN LYS          
SEQRES  31 A  751  LYS SER ILE LYS LEU SER ASP GLY ALA ASN GLY ASP GLN          
SEQRES  32 A  751  GLY GLY VAL ALA ILE LEU ARG TYR GLY ASN GLU ALA MET          
SEQRES  33 A  751  THR LEU VAL TYR LYS TYR ALA ALA GLN GLY LEU SER HIS          
SEQRES  34 A  751  GLY HIS TYR ASP LYS LEU SER PHE SER LEU TYR GLU LYS          
SEQRES  35 A  751  GLY THR GLU ILE LEU GLN ASP TYR GLY LEU ALA ARG PHE          
SEQRES  36 A  751  VAL ASN ILE GLU GLN LYS GLY GLY GLY ASN TYR LEU LYS          
SEQRES  37 A  751  GLU ASN THR THR TRP ALA LYS GLN THR ILE ALA HIS ASN          
SEQRES  38 A  751  THR LEU VAL GLN ASN GLU THR SER HIS PHE GLU GLY LYS          
SEQRES  39 A  751  TYR GLU VAL GLY SER GLN HIS HIS SER GLU LEU TYR PHE          
SEQRES  40 A  751  PHE ASP ALA SER ASN PRO GLU VAL GLN VAL VAL SER ALA          
SEQRES  41 A  751  LYS GLU GLN ASN ALA TYR PRO GLY THR GLU MET HIS ARG          
SEQRES  42 A  751  THR MET ALA LEU ILE LYS THR ASP GLY PHE GLU LYS PRO          
SEQRES  43 A  751  PHE VAL LEU ASP ILE LEU ARG VAL GLY SER ASN ALA ALA          
SEQRES  44 A  751  ASN GLN TYR ASP LEU PRO PHE TYR PHE LYS GLY GLN VAL          
SEQRES  45 A  751  MET GLN THR ASN PHE ASP PHE THR THR PRO LYS SER LEU          
SEQRES  46 A  751  GLU PRO LEU GLY SER ASP ASN GLY TYR GLN HIS LEU TRP          
SEQRES  47 A  751  SER GLU GLY LEU GLY GLN PRO LYS GLY ASP ASN SER GLN          
SEQRES  48 A  751  LEU SER TRP LEU GLU ASN GLY ARG PHE TYR THR LEU THR          
SEQRES  49 A  751  THR ALA THR ASN ASN ASP ASP GLU LEU HIS PHE VAL ARG          
SEQRES  50 A  751  ILE GLY ALA ASN ASP PRO GLU PHE ASN LEU ARG ARG ASP          
SEQRES  51 A  751  ALA GLY LEU ILE ILE ARG ARG LYS ASN THR LYS ASN THR          
SEQRES  52 A  751  THR PHE VAL SER ILE LEU GLU SER HIS GLY HIS TYR SER          
SEQRES  53 A  751  PRO VAL SER GLU PHE SER VAL ASN ALA ASN SER SER ILE          
SEQRES  54 A  751  SER LYS ILE GLU LEU MET LEU ASP THR LYS GLU TYR THR          
SEQRES  55 A  751  ALA VAL LEU ILE ASP ALA LYS SER ASN THR GLU GLN THR          
SEQRES  56 A  751  LEU LEU ILE LEU ALA ASN GLU ASN LYS ASN VAL ASN LYS          
SEQRES  57 A  751  GLU HIS ILE ILE GLU ILE LYS GLY LYS GLU TYR ARG TRP          
SEQRES  58 A  751  THR GLY PRO TYR GLN PHE ILE LYS ILE ASN                      
SEQRES   1 B  751  MET ASN MET THR LYS TYR ILE PRO VAL LEU GLN SER LEU          
SEQRES   2 B  751  LEU PHE VAL LEU LEU LEU SER PHE SER GLY HIS ALA GLN          
SEQRES   3 B  751  GLU HIS PRO SER LEU ILE LEU THR LYS ALA GLY VAL GLU          
SEQRES   4 B  751  LYS ILE ARG ALA GLU LEU GLY ASN ILE PRO ILE PHE ASP          
SEQRES   5 B  751  ALA THR LEU GLU LYS VAL LYS ALA GLU VAL ASP ALA GLU          
SEQRES   6 B  751  ILE ALA LEU GLY ILE ASP THR PRO LEU PRO LYS ASP TYR          
SEQRES   7 B  751  SER GLY GLY TYR THR HIS GLU ARG HIS LYS ARG ASN PHE          
SEQRES   8 B  751  PHE ILE LEU GLN LYS ALA GLY VAL LEU TYR GLN ILE LEU          
SEQRES   9 B  751  ASN ASP GLU LYS TYR ALA LEU TYR ILE LYS ASP MET LEU          
SEQRES  10 B  751  PHE GLN TYR GLU GLY MET TYR LYS ASP LEU PRO VAL HIS          
SEQRES  11 B  751  PRO GLN THR ARG SER TYR ALA ARG GLY LYS LEU PHE TRP          
SEQRES  12 B  751  GLN CYS LEU ASN ASP SER ASN TRP LEU VAL TYR VAL SER          
SEQRES  13 B  751  GLN ALA TYR ASP CYS VAL TYR ASP TYR LEU SER LYS LYS          
SEQRES  14 B  751  GLU ARG LYS GLN LEU GLU LYS ASN LEU PHE ARG PRO PHE          
SEQRES  15 B  751  ALA ASP TYR ILE SER ILE GLU ASN PRO GLN PHE TYR ASN          
SEQRES  16 B  751  ARG VAL HIS ASN HIS SER THR TRP GLY ASN ALA ALA VAL          
SEQRES  17 B  751  GLY MET ILE GLY LEU VAL MET GLY ASP GLU GLU LEU ILE          
SEQRES  18 B  751  GLN ARG ALA LEU TYR GLY ILE GLU ASP ASP GLY LEU PRO          
SEQRES  19 B  751  ILE GLY ALA LYS ASP ASN ASP GLY GLY PHE ILE LYS VAL          
SEQRES  20 B  751  GLU GLY GLN LYS ALA GLY PHE LEU ALA ASN ILE ASP GLU          
SEQRES  21 B  751  PRO PHE SER PRO ASP GLY TYR TYR THR GLU GLY PRO TYR          
SEQRES  22 B  751  ALA GLN ARG TYR ALA MET TYR PRO PHE LEU ILE PHE ALA          
SEQRES  23 B  751  GLU ALA LEU HIS ASN VAL ARG PRO GLN GLN LYS ILE PHE          
SEQRES  24 B  751  GLU HIS LYS ASP GLY VAL LEU LEU LYS SER VAL ASN THR          
SEQRES  25 B  751  LEU LEU SER LEU SER ASP ALA ASP GLY GLU PHE PHE PRO          
SEQRES  26 B  751  LEU ASN ASP ALA GLN LYS GLY MET SER TYR HIS SER ARG          
SEQRES  27 B  751  GLU LEU VAL THR ALA VAL ASP ILE ALA TYR HIS TYR GLY          
SEQRES  28 B  751  ASN HIS ASN PRO GLN LEU LEU SER ILE ALA GLU GLU GLN          
SEQRES  29 B  751  GLY GLN VAL LEU LEU ASP ASP SER GLY LEU ALA VAL ALA          
SEQRES  30 B  751  LEU GLY ILE ARG GLU GLY LYS SER GLU ASP PHE GLN LYS          
SEQRES  31 B  751  LYS SER ILE LYS LEU SER ASP GLY ALA ASN GLY ASP GLN          
SEQRES  32 B  751  GLY GLY VAL ALA ILE LEU ARG TYR GLY ASN GLU ALA MET          
SEQRES  33 B  751  THR LEU VAL TYR LYS TYR ALA ALA GLN GLY LEU SER HIS          
SEQRES  34 B  751  GLY HIS TYR ASP LYS LEU SER PHE SER LEU TYR GLU LYS          
SEQRES  35 B  751  GLY THR GLU ILE LEU GLN ASP TYR GLY LEU ALA ARG PHE          
SEQRES  36 B  751  VAL ASN ILE GLU GLN LYS GLY GLY GLY ASN TYR LEU LYS          
SEQRES  37 B  751  GLU ASN THR THR TRP ALA LYS GLN THR ILE ALA HIS ASN          
SEQRES  38 B  751  THR LEU VAL GLN ASN GLU THR SER HIS PHE GLU GLY LYS          
SEQRES  39 B  751  TYR GLU VAL GLY SER GLN HIS HIS SER GLU LEU TYR PHE          
SEQRES  40 B  751  PHE ASP ALA SER ASN PRO GLU VAL GLN VAL VAL SER ALA          
SEQRES  41 B  751  LYS GLU GLN ASN ALA TYR PRO GLY THR GLU MET HIS ARG          
SEQRES  42 B  751  THR MET ALA LEU ILE LYS THR ASP GLY PHE GLU LYS PRO          
SEQRES  43 B  751  PHE VAL LEU ASP ILE LEU ARG VAL GLY SER ASN ALA ALA          
SEQRES  44 B  751  ASN GLN TYR ASP LEU PRO PHE TYR PHE LYS GLY GLN VAL          
SEQRES  45 B  751  MET GLN THR ASN PHE ASP PHE THR THR PRO LYS SER LEU          
SEQRES  46 B  751  GLU PRO LEU GLY SER ASP ASN GLY TYR GLN HIS LEU TRP          
SEQRES  47 B  751  SER GLU GLY LEU GLY GLN PRO LYS GLY ASP ASN SER GLN          
SEQRES  48 B  751  LEU SER TRP LEU GLU ASN GLY ARG PHE TYR THR LEU THR          
SEQRES  49 B  751  THR ALA THR ASN ASN ASP ASP GLU LEU HIS PHE VAL ARG          
SEQRES  50 B  751  ILE GLY ALA ASN ASP PRO GLU PHE ASN LEU ARG ARG ASP          
SEQRES  51 B  751  ALA GLY LEU ILE ILE ARG ARG LYS ASN THR LYS ASN THR          
SEQRES  52 B  751  THR PHE VAL SER ILE LEU GLU SER HIS GLY HIS TYR SER          
SEQRES  53 B  751  PRO VAL SER GLU PHE SER VAL ASN ALA ASN SER SER ILE          
SEQRES  54 B  751  SER LYS ILE GLU LEU MET LEU ASP THR LYS GLU TYR THR          
SEQRES  55 B  751  ALA VAL LEU ILE ASP ALA LYS SER ASN THR GLU GLN THR          
SEQRES  56 B  751  LEU LEU ILE LEU ALA ASN GLU ASN LYS ASN VAL ASN LYS          
SEQRES  57 B  751  GLU HIS ILE ILE GLU ILE LYS GLY LYS GLU TYR ARG TRP          
SEQRES  58 B  751  THR GLY PRO TYR GLN PHE ILE LYS ILE ASN                      
HET    MAV  C   1      13                                                       
HET    MAW  C   2      11                                                       
HET    MAV  D   1      13                                                       
HET    MAW  D   2      11                                                       
HET     CA  A 801       1                                                       
HET     MG  A 802       1                                                       
HET     MG  A 803       1                                                       
HET     MG  B 801       1                                                       
HET     CA  B 802       1                                                       
HET     MG  B 803       1                                                       
HET    GOL  B 804       6                                                       
HETNAM     MAV ALPHA-D-MANNOPYRANURONIC ACID                                    
HETNAM     MAW 4-DEOXY-ALPHA-L-ERYTHRO-HEX-4-ENOPYRANURONIC ACID                
HETNAM      CA CALCIUM ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     MAV ALPHA-D-MANNURONIC ACID; D-MANNURONIC ACID; MANNURONIC           
HETSYN   2 MAV  ACID                                                            
HETSYN     MAW 4-DEOXY-ALPHA-L-ERYTHRO-HEX-4-ENURONIC ACID; 4-DEOXY-L-          
HETSYN   2 MAW  ERYTHRO-HEX-4-ENURONIC ACID; 4-DEOXY-ERYTHRO-HEX-4-             
HETSYN   3 MAW  ENURONIC ACID                                                   
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  MAV    2(C6 H10 O7)                                                 
FORMUL   3  MAW    2(C6 H8 O6)                                                  
FORMUL   5   CA    2(CA 2+)                                                     
FORMUL   6   MG    4(MG 2+)                                                     
FORMUL  11  GOL    C3 H8 O3                                                     
FORMUL  12  HOH   *912(H2 O)                                                    
HELIX    1 AA1 THR A   34  LEU A   45  1                                  12    
HELIX    2 AA2 ILE A   48  GLY A   69  1                                  22    
HELIX    3 AA3 GLY A   81  ASN A  105  1                                  25    
HELIX    4 AA4 ASP A  106  TYR A  124  1                                  19    
HELIX    5 AA5 LYS A  125  LEU A  127  5                                   3    
HELIX    6 AA6 GLN A  144  TYR A  163  1                                  20    
HELIX    7 AA7 SER A  167  LEU A  178  1                                  12    
HELIX    8 AA8 LEU A  178  ILE A  186  1                                   9    
HELIX    9 AA9 ASN A  190  ASN A  195  1                                   6    
HELIX   10 AB1 HIS A  198  GLY A  216  1                                  19    
HELIX   11 AB2 ASP A  217  GLY A  227  1                                  11    
HELIX   12 AB3 GLY A  253  GLU A  260  1                                   8    
HELIX   13 AB4 GLY A  271  ARG A  293  1                                  23    
HELIX   14 AB5 PRO A  294  PHE A  299  5                                   6    
HELIX   15 AB6 GLU A  300  LEU A  316  1                                  17    
HELIX   16 AB7 SER A  337  GLY A  351  1                                  15    
HELIX   17 AB8 GLN A  356  GLY A  365  1                                  10    
HELIX   18 AB9 ASP A  370  GLU A  382  1                                  13    
HELIX   19 AC1 GLY A  426  GLY A  430  5                                   5    
HELIX   20 AC2 LYS A  461  ASN A  465  5                                   5    
HELIX   21 AC3 LEU A  467  TRP A  473  1                                   7    
HELIX   22 AC4 GLN A  476  HIS A  480  5                                   5    
HELIX   23 AC5 SER A  489  GLY A  493  5                                   5    
HELIX   24 AC6 LYS A  494  SER A  499  1                                   6    
HELIX   25 AC7 GLY A  593  GLN A  595  5                                   3    
HELIX   26 AC8 THR B   34  LEU B   45  1                                  12    
HELIX   27 AC9 ILE B   48  GLY B   69  1                                  22    
HELIX   28 AD1 GLY B   81  ASN B  105  1                                  25    
HELIX   29 AD2 ASP B  106  LYS B  125  1                                  20    
HELIX   30 AD3 GLN B  144  TYR B  163  1                                  20    
HELIX   31 AD4 SER B  167  LEU B  178  1                                  12    
HELIX   32 AD5 LEU B  178  ILE B  186  1                                   9    
HELIX   33 AD6 ASN B  190  ASN B  195  1                                   6    
HELIX   34 AD7 HIS B  198  GLY B  216  1                                  19    
HELIX   35 AD8 ASP B  217  GLY B  227  1                                  11    
HELIX   36 AD9 GLY B  253  GLU B  260  1                                   8    
HELIX   37 AE1 GLY B  271  ARG B  293  1                                  23    
HELIX   38 AE2 PRO B  294  PHE B  299  5                                   6    
HELIX   39 AE3 GLU B  300  LEU B  316  1                                  17    
HELIX   40 AE4 SER B  337  GLY B  351  1                                  15    
HELIX   41 AE5 GLN B  356  GLY B  365  1                                  10    
HELIX   42 AE6 ASP B  370  GLU B  382  1                                  13    
HELIX   43 AE7 LYS B  461  ASN B  465  5                                   5    
HELIX   44 AE8 LEU B  467  TRP B  473  1                                   7    
HELIX   45 AE9 GLN B  476  HIS B  480  5                                   5    
HELIX   46 AF1 SER B  489  GLY B  493  5                                   5    
HELIX   47 AF2 LYS B  494  SER B  499  1                                   6    
HELIX   48 AF3 GLY B  593  GLN B  595  5                                   3    
SHEET    1 AA1 5 ILE A 393  SER A 396  0                                        
SHEET    2 AA1 5 GLY A 405  TYR A 411 -1  O  VAL A 406   N  LEU A 395           
SHEET    3 AA1 5 MET A 416  TYR A 422 -1  O  TYR A 420   N  ALA A 407           
SHEET    4 AA1 5 SER A 436  GLU A 441 -1  O  SER A 436   N  LYS A 421           
SHEET    5 AA1 5 THR A 444  LEU A 447 -1  O  ILE A 446   N  LEU A 439           
SHEET    1 AA2 6 VAL A 484  GLN A 485  0                                        
SHEET    2 AA2 6 ASN A 560  PHE A 566 -1  O  ASP A 563   N  VAL A 484           
SHEET    3 AA2 6 ALA A 651  THR A 660 -1  O  THR A 660   N  ASN A 560           
SHEET    4 AA2 6 GLU A 632  ILE A 638 -1  N  HIS A 634   O  ILE A 654           
SHEET    5 AA2 6 LEU A 597  GLY A 603 -1  N  TRP A 598   O  ARG A 637           
SHEET    6 AA2 6 PHE A 579  THR A 580 -1  N  THR A 580   O  LEU A 602           
SHEET    1 AA3 6 VAL A 484  GLN A 485  0                                        
SHEET    2 AA3 6 ASN A 560  PHE A 566 -1  O  ASP A 563   N  VAL A 484           
SHEET    3 AA3 6 ALA A 651  THR A 660 -1  O  THR A 660   N  ASN A 560           
SHEET    4 AA3 6 GLU A 632  ILE A 638 -1  N  HIS A 634   O  ILE A 654           
SHEET    5 AA3 6 LEU A 597  GLY A 603 -1  N  TRP A 598   O  ARG A 637           
SHEET    6 AA3 6 GLU A 586  PRO A 587 -1  N  GLU A 586   O  SER A 599           
SHEET    1 AA4 8 GLU A 504  ASP A 509  0                                        
SHEET    2 AA4 8 VAL A 515  GLU A 522 -1  O  VAL A 517   N  ASP A 509           
SHEET    3 AA4 8 THR A 529  ILE A 538 -1  O  MET A 535   N  VAL A 518           
SHEET    4 AA4 8 PHE A 547  SER A 556 -1  O  GLY A 555   N  GLU A 530           
SHEET    5 AA4 8 THR A 663  HIS A 672 -1  O  THR A 663   N  VAL A 554           
SHEET    6 AA4 8 ARG A 619  ALA A 626 -1  N  THR A 624   O  ILE A 668           
SHEET    7 AA4 8 ASN A 609  GLU A 616 -1  N  LEU A 612   O  LEU A 623           
SHEET    8 AA4 8 GLN A 571  THR A 575 -1  N  MET A 573   O  SER A 613           
SHEET    1 AA5 2 HIS A 674  TYR A 675  0                                        
SHEET    2 AA5 2 SER A 682  VAL A 683 -1  O  VAL A 683   N  HIS A 674           
SHEET    1 AA6 4 ILE A 689  ASP A 697  0                                        
SHEET    2 AA6 4 TYR A 701  ALA A 708 -1  O  LEU A 705   N  GLU A 693           
SHEET    3 AA6 4 GLN A 714  ALA A 720 -1  O  LEU A 719   N  THR A 702           
SHEET    4 AA6 4 TYR A 745  LYS A 749 -1  O  GLN A 746   N  ILE A 718           
SHEET    1 AA7 2 GLU A 729  ILE A 734  0                                        
SHEET    2 AA7 2 LYS A 737  THR A 742 -1  O  TYR A 739   N  ILE A 732           
SHEET    1 AA8 5 ILE B 393  SER B 396  0                                        
SHEET    2 AA8 5 GLY B 405  TYR B 411 -1  O  VAL B 406   N  LEU B 395           
SHEET    3 AA8 5 MET B 416  TYR B 422 -1  O  TYR B 420   N  ALA B 407           
SHEET    4 AA8 5 SER B 436  GLU B 441 -1  O  SER B 436   N  LYS B 421           
SHEET    5 AA8 5 THR B 444  LEU B 447 -1  O  ILE B 446   N  LEU B 439           
SHEET    1 AA9 6 VAL B 484  GLN B 485  0                                        
SHEET    2 AA9 6 ASN B 560  PHE B 566 -1  O  ASP B 563   N  VAL B 484           
SHEET    3 AA9 6 ALA B 651  THR B 660 -1  O  THR B 660   N  ASN B 560           
SHEET    4 AA9 6 GLU B 632  ILE B 638 -1  N  HIS B 634   O  ILE B 654           
SHEET    5 AA9 6 LEU B 597  GLY B 603 -1  N  TRP B 598   O  ARG B 637           
SHEET    6 AA9 6 PHE B 579  THR B 580 -1  N  THR B 580   O  LEU B 602           
SHEET    1 AB1 8 GLU B 504  ASP B 509  0                                        
SHEET    2 AB1 8 VAL B 515  GLU B 522 -1  O  VAL B 517   N  ASP B 509           
SHEET    3 AB1 8 THR B 529  ILE B 538 -1  O  MET B 535   N  VAL B 518           
SHEET    4 AB1 8 PHE B 547  SER B 556 -1  O  ILE B 551   N  THR B 534           
SHEET    5 AB1 8 THR B 663  TYR B 675 -1  O  SER B 667   N  ASP B 550           
SHEET    6 AB1 8 ARG B 619  ALA B 626 -1  N  PHE B 620   O  HIS B 672           
SHEET    7 AB1 8 ASN B 609  GLU B 616 -1  N  LEU B 612   O  LEU B 623           
SHEET    8 AB1 8 GLN B 571  THR B 575 -1  N  GLN B 574   O  SER B 613           
SHEET    1 AB2 6 GLU B 504  ASP B 509  0                                        
SHEET    2 AB2 6 VAL B 515  GLU B 522 -1  O  VAL B 517   N  ASP B 509           
SHEET    3 AB2 6 THR B 529  ILE B 538 -1  O  MET B 535   N  VAL B 518           
SHEET    4 AB2 6 PHE B 547  SER B 556 -1  O  ILE B 551   N  THR B 534           
SHEET    5 AB2 6 THR B 663  TYR B 675 -1  O  SER B 667   N  ASP B 550           
SHEET    6 AB2 6 SER B 682  VAL B 683 -1  O  VAL B 683   N  HIS B 674           
SHEET    1 AB3 4 ILE B 689  ASP B 697  0                                        
SHEET    2 AB3 4 TYR B 701  ALA B 708 -1  O  ASP B 707   N  LYS B 691           
SHEET    3 AB3 4 GLN B 714  ALA B 720 -1  O  LEU B 719   N  THR B 702           
SHEET    4 AB3 4 TYR B 745  LYS B 749 -1  O  GLN B 746   N  ILE B 718           
SHEET    1 AB4 2 GLU B 729  ILE B 734  0                                        
SHEET    2 AB4 2 LYS B 737  THR B 742 -1  O  TRP B 741   N  HIS B 730           
LINK         O4  MAV C   1                 C1  MAW C   2     1555   1555  1.46  
LINK         O4  MAV D   1                 C1  MAW D   2     1555   1555  1.44  
LINK         OG1 THR A  83                MG    MG A 802     1555   1555  2.78  
LINK         O   LEU A 141                MG    MG A 802     1555   1555  2.86  
LINK         O   GLY A 443                MG    MG A 803     1555   1555  2.33  
LINK         OD1 ASP A 449                CA    CA A 801     1555   1555  2.23  
LINK        CA    CA A 801                 O   HOH A 945     1555   1555  2.12  
LINK        CA    CA A 801                 O   HOH A 951     1555   1555  2.13  
LINK        CA    CA A 801                 O   HOH A1205     1555   1555  2.14  
LINK        MG    MG A 803                 O   HOH A 982     1555   1555  2.55  
LINK        MG    MG A 803                 O   HOH A1031     1555   1555  2.46  
LINK        MG    MG A 803                 O   HOH A1275     1555   1555  2.43  
LINK        MG    MG A 803                 O   HOH A1315     1555   1555  2.12  
LINK         OG1 THR B 202                MG    MG B 801     1555   1555  2.83  
LINK         OD1 ASN B 257                MG    MG B 801     1555   1555  2.81  
LINK         OH  TYR B 268                MG    MG B 801     1555   1555  2.76  
LINK         OD1 ASP B 449                CA    CA B 802     1555   1555  2.24  
LINK        CA    CA B 802                 O   HOH B 913     1555   1555  2.11  
LINK        CA    CA B 802                 O   HOH B 997     1555   1555  2.16  
LINK        CA    CA B 802                 O   HOH B1209     1555   1555  2.09  
LINK        MG    MG B 803                 O   HOH B 908     1555   1555  2.86  
CISPEP   1 HIS A   28    PRO A   29          0        -1.81                     
CISPEP   2 HIS B   28    PRO B   29          0        -0.53                     
CRYST1  164.132  164.132  168.370  90.00  90.00 120.00 P 65         12          
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      0.006093  0.003518  0.000000        0.00000                         
SCALE2      0.000000  0.007035  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005939        0.00000                         
ATOM      1  N   ALA A  25      89.717 100.209  35.765  1.00 60.92           N  
ANISOU    1  N   ALA A  25     7639   7784   7723     96    221   -121       N  
ATOM      2  CA  ALA A  25      90.711 101.320  35.653  1.00 58.75           C  
ANISOU    2  CA  ALA A  25     7379   7490   7455     94    215   -133       C  
ATOM      3  C   ALA A  25      91.500 101.245  34.328  1.00 55.36           C  
ANISOU    3  C   ALA A  25     6939   7055   7041     95    192   -118       C  
ATOM      4  O   ALA A  25      91.553 102.244  33.584  1.00 55.20           O  
ANISOU    4  O   ALA A  25     6915   7017   7043    107    196   -118       O  
ATOM      5  CB  ALA A  25      91.660 101.309  36.845  1.00 61.68           C  
ANISOU    5  CB  ALA A  25     7775   7863   7798     76    210   -150       C  
ATOM      6  N   GLN A  26      92.099 100.079  34.037  1.00 48.68           N  
ANISOU    6  N   GLN A  26     6088   6222   6185     84    171   -105       N  
ATOM      7  CA  GLN A  26      92.836  99.880  32.778  1.00 43.44           C  
ANISOU    7  CA  GLN A  26     5414   5555   5536     84    150    -91       C  
ATOM      8  C   GLN A  26      91.868  99.938  31.599  1.00 40.46           C  
ANISOU    8  C   GLN A  26     5014   5179   5181    101    155    -76       C  
ATOM      9  O   GLN A  26      90.910  99.187  31.553  1.00 41.74           O  
ANISOU    9  O   GLN A  26     5161   5355   5342    104    161    -68       O  
ATOM     10  CB  GLN A  26      93.607  98.543  32.731  1.00 42.16           C  
ANISOU   10  CB  GLN A  26     5251   5407   5360     69    129    -79       C  
ATOM     11  CG  GLN A  26      94.568  98.465  31.533  1.00 42.44           C  
ANISOU   11  CG  GLN A  26     5280   5437   5409     68    108    -68       C  
ATOM     12  CD  GLN A  26      95.516  97.267  31.561  1.00 42.79           C  
ANISOU   12  CD  GLN A  26     5326   5492   5441     54     88    -59       C  
ATOM     13  OE1 GLN A  26      96.057  96.943  32.606  1.00 40.72           O  
ANISOU   13  OE1 GLN A  26     5078   5235   5160     42     84    -65       O  
ATOM     14  NE2 GLN A  26      95.752  96.631  30.381  1.00 41.98           N  
ANISOU   14  NE2 GLN A  26     5209   5391   5350     55     76    -44       N  
ATOM     15  N   GLU A  27      92.131 100.821  30.654  1.00 37.11           N  
ANISOU   15  N   GLU A  27     4584   4740   4776    110    152    -72       N  
ATOM     16  CA  GLU A  27      91.410 100.835  29.391  1.00 39.90           C  
ANISOU   16  CA  GLU A  27     4914   5097   5148    125    152    -55       C  
ATOM     17  C   GLU A  27      91.821  99.708  28.440  1.00 36.46           C  
ANISOU   17  C   GLU A  27     4466   4675   4711    117    130    -40       C  
ATOM     18  O   GLU A  27      92.971  99.280  28.428  1.00 30.93           O  
ANISOU   18  O   GLU A  27     3776   3974   4003    104    114    -40       O  
ATOM     19  CB  GLU A  27      91.646 102.151  28.682  1.00 44.12           C  
ANISOU   19  CB  GLU A  27     5449   5611   5703    138    155    -54       C  
ATOM     20  CG  GLU A  27      91.044 103.328  29.450  1.00 51.11           C  
ANISOU   20  CG  GLU A  27     6343   6481   6595    149    181    -69       C  
ATOM     21  CD  GLU A  27      91.128 104.635  28.694  1.00 55.47           C  
ANISOU   21  CD  GLU A  27     6894   7011   7171    165    188    -65       C  
ATOM     22  OE1 GLU A  27      92.085 104.819  27.905  1.00 56.54           O  
ANISOU   22  OE1 GLU A  27     7031   7139   7313    161    172    -58       O  
ATOM     23  OE2 GLU A  27      90.214 105.469  28.879  1.00 64.59           O  
ANISOU   23  OE2 GLU A  27     8045   8156   8340    182    210    -67       O  
ATOM     24  N   HIS A  28      90.859  99.280  27.631  1.00 33.18           N  
ANISOU   24  N   HIS A  28     4029   4273   4305    126    131    -27       N  
ATOM     25  CA  HIS A  28      91.086  98.312  26.566  1.00 33.71           C  
ANISOU   25  CA  HIS A  28     4082   4353   4372    120    114    -13       C  
ATOM     26  C   HIS A  28      90.413  98.793  25.277  1.00 35.64           C  
ANISOU   26  C   HIS A  28     4307   4602   4635    136    114      0       C  
ATOM     27  O   HIS A  28      89.231  99.093  25.306  1.00 37.84           O  
ANISOU   27  O   HIS A  28     4572   4887   4921    149    127      3       O  
ATOM     28  CB  HIS A  28      90.474  96.973  26.938  1.00 32.43           C  
ANISOU   28  CB  HIS A  28     3913   4210   4200    110    115    -11       C  
ATOM     29  CG  HIS A  28      91.158  96.290  28.066  1.00 31.61           C  
ANISOU   29  CG  HIS A  28     3827   4106   4078     95    112    -19       C  
ATOM     30  ND1 HIS A  28      90.818  96.516  29.381  1.00 32.49           N  
ANISOU   30  ND1 HIS A  28     3951   4215   4178     93    127    -31       N  
ATOM     31  CD2 HIS A  28      92.126  95.341  28.088  1.00 32.91           C  
ANISOU   31  CD2 HIS A  28     3999   4273   4233     80     97    -16       C  
ATOM     32  CE1 HIS A  28      91.549  95.747  30.165  1.00 32.65           C  
ANISOU   32  CE1 HIS A  28     3986   4239   4181     79    120    -34       C  
ATOM     33  NE2 HIS A  28      92.375  95.045  29.409  1.00 32.56           N  
ANISOU   33  NE2 HIS A  28     3972   4229   4172     71    102    -24       N  
ATOM     34  N   PRO A  29      91.124  98.862  24.163  1.00 33.56           N  
ANISOU   34  N   PRO A  29     4039   4336   4377    136     99     10       N  
ATOM     35  CA  PRO A  29      92.560  98.536  24.086  1.00 32.84           C  
ANISOU   35  CA  PRO A  29     3962   4236   4278    122     83      8       C  
ATOM     36  C   PRO A  29      93.437  99.665  24.636  1.00 33.71           C  
ANISOU   36  C   PRO A  29     4092   4325   4392    123     87     -2       C  
ATOM     37  O   PRO A  29      92.949 100.800  24.767  1.00 32.67           O  
ANISOU   37  O   PRO A  29     3961   4181   4271    137    101     -5       O  
ATOM     38  CB  PRO A  29      92.777  98.333  22.588  1.00 31.46           C  
ANISOU   38  CB  PRO A  29     3774   4069   4112    125     70     22       C  
ATOM     39  CG  PRO A  29      91.842  99.309  21.976  1.00 33.12           C  
ANISOU   39  CG  PRO A  29     3969   4279   4335    144     79     31       C  
ATOM     40  CD  PRO A  29      90.591  99.301  22.862  1.00 32.29           C  
ANISOU   40  CD  PRO A  29     3859   4181   4230    151     96     25       C  
ATOM     41  N   SER A  30      94.722  99.381  24.932  1.00 32.73           N  
ANISOU   41  N   SER A  30     3983   4194   4260    108     75     -7       N  
ATOM     42  CA  SER A  30      95.684 100.459  25.247  1.00 35.42           C  
ANISOU   42  CA  SER A  30     4339   4513   4605    107     75    -17       C  
ATOM     43  C   SER A  30      97.178 100.168  25.094  1.00 34.38           C  
ANISOU   43  C   SER A  30     4217   4377   4470     93     58    -17       C  
ATOM     44  O   SER A  30      98.022 101.007  25.283  1.00 41.14           O  
ANISOU   44  O   SER A  30     5084   5217   5330     89     57    -24       O  
ATOM     45  CB  SER A  30      95.450 100.895  26.679  1.00 37.27           C  
ANISOU   45  CB  SER A  30     4588   4742   4830    104     89    -34       C  
ATOM     46  OG  SER A  30      95.945  99.870  27.613  1.00 35.29           O  
ANISOU   46  OG  SER A  30     4347   4501   4559     87     81    -40       O  
ATOM     47  N   LEU A  31      97.460  98.931  24.720  1.00 34.22           N  
ANISOU   47  N   LEU A  31     4189   4371   4442     84     45     -9       N  
ATOM     48  CA  LEU A  31      98.862  98.442  24.575  1.00 33.59           C  
ANISOU   48  CA  LEU A  31     4116   4289   4359     71     29     -7       C  
ATOM     49  C   LEU A  31      99.514  98.932  23.291  1.00 30.04           C  
ANISOU   49  C   LEU A  31     3660   3831   3923     75     22      3       C  
ATOM     50  O   LEU A  31     100.585  99.501  23.331  1.00 27.68           O  
ANISOU   50  O   LEU A  31     3370   3519   3628     69     17     -1       O  
ATOM     51  CB  LEU A  31      98.896  96.936  24.618  1.00 34.58           C  
ANISOU   51  CB  LEU A  31     4235   4430   4473     62     21     -1       C  
ATOM     52  CG  LEU A  31      99.258  96.355  25.976  1.00 36.80           C  
ANISOU   52  CG  LEU A  31     4529   4715   4738     50     19     -9       C  
ATOM     53  CD1 LEU A  31      98.052  96.096  26.855  1.00 37.15           C  
ANISOU   53  CD1 LEU A  31     4573   4768   4772     53     32    -14       C  
ATOM     54  CD2 LEU A  31      99.952  95.005  25.741  1.00 40.06           C  
ANISOU   54  CD2 LEU A  31     4938   5136   5146     40      6      1       C  
ATOM     55  N   ILE A  32      98.833  98.676  22.167  1.00 30.08           N  
ANISOU   55  N   ILE A  32     3650   3844   3934     84     23     15       N  
ATOM     56  CA  ILE A  32      99.331  98.961  20.850  1.00 32.68           C  
ANISOU   56  CA  ILE A  32     3973   4171   4274     88     16     26       C  
ATOM     57  C   ILE A  32      98.379  99.983  20.149  1.00 35.11           C  
ANISOU   57  C   ILE A  32     4270   4475   4593    106     27     34       C  
ATOM     58  O   ILE A  32      98.721 101.126  19.925  1.00 35.22           O  
ANISOU   58  O   ILE A  32     4291   4473   4619    113     32     35       O  
ATOM     59  CB  ILE A  32      99.475  97.685  20.021  1.00 30.61           C  
ANISOU   59  CB  ILE A  32     3700   3924   4007     81      6     35       C  
ATOM     60  CG1 ILE A  32     100.237  96.597  20.763  1.00 30.78           C  
ANISOU   60  CG1 ILE A  32     3728   3949   4018     66     -2     30       C  
ATOM     61  CG2 ILE A  32     100.088  98.017  18.674  1.00 31.17           C  
ANISOU   61  CG2 ILE A  32     3765   3992   4087     85      0     46       C  
ATOM     62  CD1 ILE A  32     101.654  96.943  21.195  1.00 30.57           C  
ANISOU   62  CD1 ILE A  32     3713   3908   3993     58    -10     25       C  
ATOM     63  N   LEU A  33      97.187  99.554  19.791  1.00 36.03           N  
ANISOU   63  N   LEU A  33     4373   4608   4708    114     30     40       N  
ATOM     64  CA  LEU A  33      96.140 100.493  19.469  1.00 36.60           C  
ANISOU   64  CA  LEU A  33     4436   4679   4790    132     42     47       C  
ATOM     65  C   LEU A  33      95.597 101.065  20.785  1.00 37.25           C  
ANISOU   65  C   LEU A  33     4528   4752   4873    136     57     34       C  
ATOM     66  O   LEU A  33      95.333 100.308  21.726  1.00 37.56           O  
ANISOU   66  O   LEU A  33     4571   4799   4900    127     58     24       O  
ATOM     67  CB  LEU A  33      95.046  99.769  18.685  1.00 36.59           C  
ANISOU   67  CB  LEU A  33     4414   4702   4785    137     40     57       C  
ATOM     68  CG  LEU A  33      93.885 100.623  18.206  1.00 36.94           C  
ANISOU   68  CG  LEU A  33     4444   4751   4840    158     49     68       C  
ATOM     69  CD1 LEU A  33      94.347 101.721  17.261  1.00 37.72           C  
ANISOU   69  CD1 LEU A  33     4544   4838   4951    170     49     81       C  
ATOM     70  CD2 LEU A  33      92.862  99.720  17.540  1.00 35.89           C  
ANISOU   70  CD2 LEU A  33     4290   4645   4700    158     44     76       C  
ATOM     71  N   THR A  34      95.476 102.399  20.867  1.00 36.14           N  
ANISOU   71  N   THR A  34     4393   4594   4746    148     69     33       N  
ATOM     72  CA  THR A  34      94.901 103.081  22.038  1.00 36.64           C  
ANISOU   72  CA  THR A  34     4465   4645   4811    154     87     20       C  
ATOM     73  C   THR A  34      93.566 103.747  21.656  1.00 36.11           C  
ANISOU   73  C   THR A  34     4383   4580   4757    176    101     30       C  
ATOM     74  O   THR A  34      93.287 103.931  20.503  1.00 34.73           O  
ANISOU   74  O   THR A  34     4194   4413   4591    187     97     47       O  
ATOM     75  CB  THR A  34      95.869 104.144  22.680  1.00 35.78           C  
ANISOU   75  CB  THR A  34     4377   4510   4709    149     93      6       C  
ATOM     76  OG1 THR A  34      95.839 105.359  21.945  1.00 33.95           O  
ANISOU   76  OG1 THR A  34     4144   4260   4497    164    102     15       O  
ATOM     77  CG2 THR A  34      97.344 103.637  22.749  1.00 36.02           C  
ANISOU   77  CG2 THR A  34     4418   4538   4731    129     75      1       C  
ATOM     78  N   LYS A  35      92.773 104.125  22.647  1.00 39.74           N  
ANISOU   78  N   LYS A  35     4846   5036   5218    182    119     19       N  
ATOM     79  CA  LYS A  35      91.449 104.737  22.427  1.00 41.01           C  
ANISOU   79  CA  LYS A  35     4991   5199   5392    204    135     28       C  
ATOM     80  C   LYS A  35      91.554 106.129  21.865  1.00 40.14           C  
ANISOU   80  C   LYS A  35     4882   5065   5302    222    145     37       C  
ATOM     81  O   LYS A  35      90.792 106.468  20.953  1.00 39.88           O  
ANISOU   81  O   LYS A  35     4831   5040   5282    241    148     56       O  
ATOM     82  CB  LYS A  35      90.622 104.792  23.708  1.00 46.22           C  
ANISOU   82  CB  LYS A  35     5656   5858   6048    206    153     13       C  
ATOM     83  CG  LYS A  35      90.224 103.416  24.230  1.00 50.27           C  
ANISOU   83  CG  LYS A  35     6163   6394   6542    192    147      8       C  
ATOM     84  CD  LYS A  35      89.366 103.488  25.485  1.00 52.62           C  
ANISOU   84  CD  LYS A  35     6465   6692   6835    195    167     -6       C  
ATOM     85  CE  LYS A  35      87.917 103.104  25.229  1.00 54.96           C  
ANISOU   85  CE  LYS A  35     6736   7009   7137    207    175      4       C  
ATOM     86  NZ  LYS A  35      87.761 101.642  25.037  1.00 57.76           N  
ANISOU   86  NZ  LYS A  35     7080   7389   7477    192    160      9       N  
ATOM     87  N   ALA A  36      92.522 106.924  22.346  1.00 38.03           N  
ANISOU   87  N   ALA A  36     4637   4772   5041    215    150     24       N  
ATOM     88  CA  ALA A  36      92.775 108.205  21.714  1.00 36.90           C  
ANISOU   88  CA  ALA A  36     4497   4605   4919    230    160     34       C  
ATOM     89  C   ALA A  36      93.267 107.958  20.272  1.00 37.50           C  
ANISOU   89  C   ALA A  36     4561   4691   4997    231    142     56       C  
ATOM     90  O   ALA A  36      92.863 108.691  19.374  1.00 38.45           O  
ANISOU   90  O   ALA A  36     4671   4807   5133    251    148     76       O  
ATOM     91  CB  ALA A  36      93.720 109.109  22.522  1.00 35.84           C  
ANISOU   91  CB  ALA A  36     4388   4440   4791    220    170     13       C  
ATOM     92  N   GLY A  37      94.067 106.907  20.036  1.00 35.91           N  
ANISOU   92  N   GLY A  37     4361   4504   4779    212    121     54       N  
ATOM     93  CA  GLY A  37      94.444 106.539  18.675  1.00 35.30           C  
ANISOU   93  CA  GLY A  37     4272   4440   4701    213    105     74       C  
ATOM     94  C   GLY A  37      93.262 106.245  17.752  1.00 34.49           C  
ANISOU   94  C   GLY A  37     4145   4362   4598    229    103     95       C  
ATOM     95  O   GLY A  37      93.195 106.731  16.622  1.00 34.89           O  
ANISOU   95  O   GLY A  37     4185   4414   4657    242    101    115       O  
ATOM     96  N   VAL A  38      92.333 105.440  18.234  1.00 35.40           N  
ANISOU   96  N   VAL A  38     4249   4497   4703    227    103     89       N  
ATOM     97  CA  VAL A  38      91.127 105.128  17.485  1.00 36.70           C  
ANISOU   97  CA  VAL A  38     4389   4688   4868    241    101    106       C  
ATOM     98  C   VAL A  38      90.364 106.411  17.095  1.00 36.68           C  
ANISOU   98  C   VAL A  38     4377   4675   4886    268    116    123       C  
ATOM     99  O   VAL A  38      89.962 106.553  15.942  1.00 34.69           O  
ANISOU   99  O   VAL A  38     4107   4438   4637    281    110    145       O  
ATOM    100  CB  VAL A  38      90.183 104.198  18.281  1.00 38.51           C  
ANISOU  100  CB  VAL A  38     4610   4936   5087    235    103     95       C  
ATOM    101  CG1 VAL A  38      88.798 104.135  17.632  1.00 37.35           C  
ANISOU  101  CG1 VAL A  38     4435   4814   4944    251    105    112       C  
ATOM    102  CG2 VAL A  38      90.775 102.797  18.385  1.00 38.91           C  
ANISOU  102  CG2 VAL A  38     4664   5001   5118    210     87     85       C  
ATOM    103  N   GLU A  39      90.196 107.336  18.031  1.00 39.49           N  
ANISOU  103  N   GLU A  39     4744   5005   5255    277    137    112       N  
ATOM    104  CA  GLU A  39      89.509 108.628  17.713  1.00 44.14           C  
ANISOU  104  CA  GLU A  39     5326   5580   5867    305    155    128       C  
ATOM    105  C   GLU A  39      90.274 109.447  16.683  1.00 40.14           C  
ANISOU  105  C   GLU A  39     4824   5058   5372    313    152    146       C  
ATOM    106  O   GLU A  39      89.663 109.974  15.772  1.00 38.86           O  
ANISOU  106  O   GLU A  39     4644   4902   5220    334    154    171       O  
ATOM    107  CB  GLU A  39      89.242 109.500  18.957  1.00 47.23           C  
ANISOU  107  CB  GLU A  39     5731   5942   6271    312    181    110       C  
ATOM    108  CG  GLU A  39      88.331 108.870  19.994  1.00 54.49           C  
ANISOU  108  CG  GLU A  39     6646   6876   7182    308    189     95       C  
ATOM    109  CD  GLU A  39      86.843 108.821  19.610  1.00 64.63           C  
ANISOU  109  CD  GLU A  39     7901   8182   8473    330    195    113       C  
ATOM    110  OE1 GLU A  39      86.479 108.843  18.401  1.00 71.73           O  
ANISOU  110  OE1 GLU A  39     8779   9098   9376    343    184    138       O  
ATOM    111  OE2 GLU A  39      86.004 108.747  20.547  1.00 72.35           O  
ANISOU  111  OE2 GLU A  39     8875   9162   9452    333    211    101       O  
ATOM    112  N   LYS A  40      91.601 109.513  16.789  1.00 38.92           N  
ANISOU  112  N   LYS A  40     4690   4885   5214    295    146    135       N  
ATOM    113  CA  LYS A  40      92.361 110.320  15.835  1.00 40.58           C  
ANISOU  113  CA  LYS A  40     4904   5078   5435    302    146    152       C  
ATOM    114  C   LYS A  40      92.297 109.690  14.448  1.00 37.41           C  
ANISOU  114  C   LYS A  40     4485   4707   5023    304    126    176       C  
ATOM    115  O   LYS A  40      92.103 110.402  13.459  1.00 37.12           O  
ANISOU  115  O   LYS A  40     4438   4669   4997    323    129    201       O  
ATOM    116  CB  LYS A  40      93.803 110.492  16.252  1.00 45.28           C  
ANISOU  116  CB  LYS A  40     5523   5649   6030    281    144    135       C  
ATOM    117  CG  LYS A  40      93.992 111.392  17.443  1.00 52.17           C  
ANISOU  117  CG  LYS A  40     6416   6489   6917    280    164    113       C  
ATOM    118  CD  LYS A  40      95.457 111.412  17.880  1.00 58.79           C  
ANISOU  118  CD  LYS A  40     7276   7309   7752    255    158     94       C  
ATOM    119  CE  LYS A  40      95.600 111.671  19.372  1.00 63.25           C  
ANISOU  119  CE  LYS A  40     7860   7857   8316    244    171     63       C  
ATOM    120  NZ  LYS A  40      96.915 111.187  19.879  1.00 67.37           N  
ANISOU  120  NZ  LYS A  40     8397   8376   8824    216    157     44       N  
ATOM    121  N   ILE A  41      92.472 108.353  14.391  1.00 34.78           N  
ANISOU  121  N   ILE A  41     4147   4400   4668    285    107    167       N  
ATOM    122  CA  ILE A  41      92.376 107.618  13.136  1.00 33.62           C  
ANISOU  122  CA  ILE A  41     3983   4284   4507    283     89    185       C  
ATOM    123  C   ILE A  41      91.009 107.922  12.465  1.00 33.45           C  
ANISOU  123  C   ILE A  41     3936   4284   4491    308     91    208       C  
ATOM    124  O   ILE A  41      90.970 108.283  11.320  1.00 32.82           O  
ANISOU  124  O   ILE A  41     3846   4213   4412    320     86    232       O  
ATOM    125  CB  ILE A  41      92.543 106.094  13.344  1.00 32.22           C  
ANISOU  125  CB  ILE A  41     3804   4130   4308    260     72    169       C  
ATOM    126  CG1 ILE A  41      94.019 105.768  13.646  1.00 32.20           C  
ANISOU  126  CG1 ILE A  41     3823   4112   4300    238     65    153       C  
ATOM    127  CG2 ILE A  41      92.034 105.318  12.138  1.00 32.05           C  
ANISOU  127  CG2 ILE A  41     3761   4144   4272    260     56    185       C  
ATOM    128  CD1 ILE A  41      94.239 104.442  14.334  1.00 31.51           C  
ANISOU  128  CD1 ILE A  41     3739   4037   4197    216     56    134       C  
ATOM    129  N   ARG A  42      89.918 107.684  13.169  1.00 33.73           N  
ANISOU  129  N   ARG A  42     3961   4330   4527    313     98    201       N  
ATOM    130  CA  ARG A  42      88.549 107.901  12.595  1.00 37.13           C  
ANISOU  130  CA  ARG A  42     4362   4782   4961    336    100    223       C  
ATOM    131  C   ARG A  42      88.334 109.347  12.060  1.00 35.95           C  
ANISOU  131  C   ARG A  42     4210   4615   4834    365    114    249       C  
ATOM    132  O   ARG A  42      87.768 109.525  11.031  1.00 37.49           O  
ANISOU  132  O   ARG A  42     4385   4831   5029    381    107    275       O  
ATOM    133  CB  ARG A  42      87.461 107.580  13.615  1.00 37.38           C  
ANISOU  133  CB  ARG A  42     4384   4822   4995    338    110    210       C  
ATOM    134  CG  ARG A  42      87.293 106.131  13.967  1.00 38.96           C  
ANISOU  134  CG  ARG A  42     4581   5048   5175    315     97    192       C  
ATOM    135  CD  ARG A  42      86.139 106.017  14.962  1.00 40.29           C  
ANISOU  135  CD  ARG A  42     4738   5221   5349    321    111    183       C  
ATOM    136  NE  ARG A  42      86.002 104.663  15.478  1.00 42.63           N  
ANISOU  136  NE  ARG A  42     5033   5536   5627    298    102    165       N  
ATOM    137  CZ  ARG A  42      85.317 104.306  16.578  1.00 43.82           C  
ANISOU  137  CZ  ARG A  42     5183   5689   5779    295    114    149       C  
ATOM    138  NH1 ARG A  42      84.648 105.204  17.302  1.00 46.43           N  
ANISOU  138  NH1 ARG A  42     5512   6003   6125    313    136    149       N  
ATOM    139  NH2 ARG A  42      85.294 103.032  16.966  1.00 41.17           N  
ANISOU  139  NH2 ARG A  42     4846   5369   5426    272    106    135       N  
ATOM    140  N   ALA A  43      88.870 110.341  12.752  1.00 36.65           N  
ANISOU  140  N   ALA A  43     4320   4664   4942    370    133    240       N  
ATOM    141  CA  ALA A  43      88.858 111.729  12.311  1.00 38.60           C  
ANISOU  141  CA  ALA A  43     4568   4885   5212    395    149    262       C  
ATOM    142  C   ALA A  43      89.648 111.981  11.010  1.00 41.02           C  
ANISOU  142  C   ALA A  43     4876   5195   5516    396    138    285       C  
ATOM    143  O   ALA A  43      89.344 112.911  10.298  1.00 42.14           O  
ANISOU  143  O   ALA A  43     5009   5330   5672    420    146    313       O  
ATOM    144  CB  ALA A  43      89.411 112.622  13.442  1.00 38.63           C  
ANISOU  144  CB  ALA A  43     4598   4844   5235    393    173    241       C  
ATOM    145  N   GLU A  44      90.685 111.171  10.724  1.00 42.83           N  
ANISOU  145  N   GLU A  44     5116   5431   5726    371    121    274       N  
ATOM    146  CA  GLU A  44      91.549 111.373   9.567  1.00 39.23           C  
ANISOU  146  CA  GLU A  44     4663   4975   5266    369    111    293       C  
ATOM    147  C   GLU A  44      91.222 110.469   8.389  1.00 38.27           C  
ANISOU  147  C   GLU A  44     4521   4898   5121    366     89    309       C  
ATOM    148  O   GLU A  44      91.741 110.715   7.304  1.00 35.55           O  
ANISOU  148  O   GLU A  44     4176   4558   4772    370     83    329       O  
ATOM    149  CB  GLU A  44      93.015 111.164   9.951  1.00 41.14           C  
ANISOU  149  CB  GLU A  44     4931   5196   5505    344    109    271       C  
ATOM    150  CG  GLU A  44      93.595 112.176  10.920  1.00 42.96           C  
ANISOU  150  CG  GLU A  44     5184   5382   5759    344    130    255       C  
ATOM    151  CD  GLU A  44      93.684 113.599  10.396  1.00 44.47           C  
ANISOU  151  CD  GLU A  44     5379   5545   5974    366    148    279       C  
ATOM    152  OE1 GLU A  44      93.593 113.825   9.171  1.00 45.17           O  
ANISOU  152  OE1 GLU A  44     5455   5646   6061    379    142    309       O  
ATOM    153  OE2 GLU A  44      93.845 114.510  11.246  1.00 47.26           O  
ANISOU  153  OE2 GLU A  44     5747   5861   6349    369    169    266       O  
ATOM    154  N   LEU A  45      90.434 109.402   8.591  1.00 36.67           N  
ANISOU  154  N   LEU A  45     4303   4728   4902    358     77    299       N  
ATOM    155  CA  LEU A  45      90.176 108.434   7.509  1.00 37.62           C  
ANISOU  155  CA  LEU A  45     4406   4891   4999    351     55    309       C  
ATOM    156  C   LEU A  45      89.685 109.139   6.260  1.00 38.55           C  
ANISOU  156  C   LEU A  45     4506   5025   5118    374     52    345       C  
ATOM    157  O   LEU A  45      88.851 110.017   6.355  1.00 39.25           O  
ANISOU  157  O   LEU A  45     4584   5108   5223    400     65    363       O  
ATOM    158  CB  LEU A  45      89.129 107.359   7.885  1.00 37.56           C  
ANISOU  158  CB  LEU A  45     4379   4915   4978    342     46    296       C  
ATOM    159  CG  LEU A  45      89.574 106.230   8.810  1.00 38.68           C  
ANISOU  159  CG  LEU A  45     4534   5055   5109    315     42    263       C  
ATOM    160  CD1 LEU A  45      88.425 105.251   9.122  1.00 39.87           C  
ANISOU  160  CD1 LEU A  45     4664   5236   5249    309     36    254       C  
ATOM    161  CD2 LEU A  45      90.779 105.496   8.241  1.00 38.90           C  
ANISOU  161  CD2 LEU A  45     4575   5086   5121    292     28    255       C  
ATOM    162  N   GLY A  46      90.183 108.690   5.110  1.00 38.30           N  
ANISOU  162  N   GLY A  46     4471   5016   5066    366     36    356       N  
ATOM    163  CA  GLY A  46      89.938 109.297   3.827  1.00 39.62           C  
ANISOU  163  CA  GLY A  46     4624   5199   5229    385     32    392       C  
ATOM    164  C   GLY A  46      90.882 110.407   3.388  1.00 39.68           C  
ANISOU  164  C   GLY A  46     4649   5175   5251    396     44    410       C  
ATOM    165  O   GLY A  46      90.865 110.754   2.240  1.00 39.71           O  
ANISOU  165  O   GLY A  46     4645   5196   5248    407     38    439       O  
ATOM    166  N   ASN A  47      91.690 110.961   4.284  1.00 40.81           N  
ANISOU  166  N   ASN A  47     4817   5275   5415    391     60    394       N  
ATOM    167  CA  ASN A  47      92.726 111.939   3.922  1.00 41.98           C  
ANISOU  167  CA  ASN A  47     4983   5390   5577    395     72    406       C  
ATOM    168  C   ASN A  47      94.167 111.493   4.330  1.00 41.29           C  
ANISOU  168  C   ASN A  47     4920   5282   5488    367     71    379       C  
ATOM    169  O   ASN A  47      95.039 112.342   4.544  1.00 39.92           O  
ANISOU  169  O   ASN A  47     4764   5070   5332    367     85    379       O  
ATOM    170  CB  ASN A  47      92.357 113.301   4.541  1.00 45.16           C  
ANISOU  170  CB  ASN A  47     5390   5755   6013    420     97    417       C  
ATOM    171  CG  ASN A  47      93.140 114.488   3.927  1.00 50.74           C  
ANISOU  171  CG  ASN A  47     6110   6431   6737    432    112    440       C  
ATOM    172  OD1 ASN A  47      93.590 114.453   2.768  1.00 56.05           O  
ANISOU  172  OD1 ASN A  47     6781   7120   7397    432    103    462       O  
ATOM    173  ND2 ASN A  47      93.313 115.547   4.719  1.00 51.77           N  
ANISOU  173  ND2 ASN A  47     6255   6517   6898    441    136    435       N  
ATOM    174  N   ILE A  48      94.398 110.164   4.435  1.00 40.03           N  
ANISOU  174  N   ILE A  48     4759   5145   5305    342     54    357       N  
ATOM    175  CA  ILE A  48      95.743 109.588   4.746  1.00 38.17           C  
ANISOU  175  CA  ILE A  48     4543   4894   5064    315     50    333       C  
ATOM    176  C   ILE A  48      96.069 108.379   3.826  1.00 37.99           C  
ANISOU  176  C   ILE A  48     4514   4907   5014    298     31    331       C  
ATOM    177  O   ILE A  48      95.961 107.206   4.263  1.00 37.67           O  
ANISOU  177  O   ILE A  48     4472   4883   4960    280     20    308       O  
ATOM    178  CB  ILE A  48      95.853 109.233   6.260  1.00 37.34           C  
ANISOU  178  CB  ILE A  48     4450   4771   4968    301     55    299       C  
ATOM    179  CG1 ILE A  48      94.556 108.567   6.759  1.00 36.80           C  
ANISOU  179  CG1 ILE A  48     4364   4727   4890    304     50    292       C  
ATOM    180  CG2 ILE A  48      96.182 110.478   7.087  1.00 36.75           C  
ANISOU  180  CG2 ILE A  48     4390   4652   4919    310     76    296       C  
ATOM    181  CD1 ILE A  48      94.547 108.126   8.187  1.00 36.23           C  
ANISOU  181  CD1 ILE A  48     4302   4642   4821    291     54    261       C  
ATOM    182  N   PRO A  49      96.410 108.653   2.539  1.00 38.55           N  
ANISOU  182  N   PRO A  49     4581   4989   5076    304     27    355       N  
ATOM    183  CA  PRO A  49      96.425 107.594   1.466  1.00 36.88           C  
ANISOU  183  CA  PRO A  49     4360   4817   4835    292      9    358       C  
ATOM    184  C   PRO A  49      97.103 106.231   1.793  1.00 36.27           C  
ANISOU  184  C   PRO A  49     4290   4747   4744    263     -1    327       C  
ATOM    185  O   PRO A  49      96.489 105.174   1.532  1.00 34.36           O  
ANISOU  185  O   PRO A  49     4036   4538   4482    253    -14    319       O  
ATOM    186  CB  PRO A  49      97.111 108.298   0.290  1.00 36.47           C  
ANISOU  186  CB  PRO A  49     4312   4762   4781    300     13    384       C  
ATOM    187  CG  PRO A  49      96.690 109.764   0.447  1.00 36.81           C  
ANISOU  187  CG  PRO A  49     4356   4782   4850    327     29    409       C  
ATOM    188  CD  PRO A  49      96.668 110.010   1.953  1.00 38.33           C  
ANISOU  188  CD  PRO A  49     4558   4940   5064    324     41    384       C  
ATOM    189  N   ILE A  50      98.323 106.248   2.355  1.00 32.72           N  
ANISOU  189  N   ILE A  50     3859   4267   4305    249      6    311       N  
ATOM    190  CA  ILE A  50      99.002 105.020   2.716  1.00 30.80           C  
ANISOU  190  CA  ILE A  50     3623   4028   4051    224     -2    285       C  
ATOM    191  C   ILE A  50      98.201 104.202   3.791  1.00 30.45           C  
ANISOU  191  C   ILE A  50     3574   3992   4005    217     -7    263       C  
ATOM    192  O   ILE A  50      98.113 102.981   3.730  1.00 29.22           O  
ANISOU  192  O   ILE A  50     3413   3857   3834    201    -17    248       O  
ATOM    193  CB  ILE A  50     100.455 105.295   3.116  1.00 30.75           C  
ANISOU  193  CB  ILE A  50     3635   3988   4058    212      5    275       C  
ATOM    194  CG1 ILE A  50     101.261 103.999   3.201  1.00 32.12           C  
ANISOU  194  CG1 ILE A  50     3815   4170   4221    188     -4    254       C  
ATOM    195  CG2 ILE A  50     100.538 106.064   4.439  1.00 32.47           C  
ANISOU  195  CG2 ILE A  50     3864   4173   4300    216     16    264       C  
ATOM    196  CD1 ILE A  50     102.779 104.243   3.312  1.00 33.24           C  
ANISOU  196  CD1 ILE A  50     3972   4285   4375    177      2    248       C  
ATOM    197  N   PHE A  51      97.625 104.890   4.769  1.00 29.58           N  
ANISOU  197  N   PHE A  51     3464   3864   3911    228      3    260       N  
ATOM    198  CA  PHE A  51      96.779 104.262   5.781  1.00 29.04           C  
ANISOU  198  CA  PHE A  51     3390   3803   3842    224      1    243       C  
ATOM    199  C   PHE A  51      95.459 103.811   5.187  1.00 28.38           C  
ANISOU  199  C   PHE A  51     3283   3755   3743    231     -8    252       C  
ATOM    200  O   PHE A  51      95.040 102.673   5.413  1.00 27.26           O  
ANISOU  200  O   PHE A  51     3135   3634   3589    218    -16    237       O  
ATOM    201  CB  PHE A  51      96.580 105.211   6.950  1.00 29.29           C  
ANISOU  201  CB  PHE A  51     3430   3804   3894    234     15    237       C  
ATOM    202  CG  PHE A  51      96.028 104.584   8.212  1.00 29.08           C  
ANISOU  202  CG  PHE A  51     3404   3778   3868    226     16    215       C  
ATOM    203  CD1 PHE A  51      94.681 104.233   8.313  1.00 30.45           C  
ANISOU  203  CD1 PHE A  51     3560   3975   4035    234     14    217       C  
ATOM    204  CD2 PHE A  51      96.818 104.469   9.354  1.00 29.12           C  
ANISOU  204  CD2 PHE A  51     3427   3759   3879    213     21    193       C  
ATOM    205  CE1 PHE A  51      94.151 103.701   9.473  1.00 28.87           C  
ANISOU  205  CE1 PHE A  51     3359   3774   3835    227     17    198       C  
ATOM    206  CE2 PHE A  51      96.305 103.952  10.518  1.00 28.86           C  
ANISOU  206  CE2 PHE A  51     3395   3726   3844    206     23    175       C  
ATOM    207  CZ  PHE A  51      94.950 103.567  10.584  1.00 29.74           C  
ANISOU  207  CZ  PHE A  51     3489   3861   3950    214     22    177       C  
ATOM    208  N   ASP A  52      94.789 104.700   4.459  1.00 30.33           N  
ANISOU  208  N   ASP A  52     3519   4011   3993    253     -5    278       N  
ATOM    209  CA  ASP A  52      93.542 104.340   3.713  1.00 32.89           C  
ANISOU  209  CA  ASP A  52     3819   4376   4303    261    -16    291       C  
ATOM    210  C   ASP A  52      93.705 103.082   2.811  1.00 32.10           C  
ANISOU  210  C   ASP A  52     3712   4309   4177    241    -32    284       C  
ATOM    211  O   ASP A  52      92.853 102.197   2.847  1.00 34.13           O  
ANISOU  211  O   ASP A  52     3954   4593   4421    233    -40    275       O  
ATOM    212  CB  ASP A  52      93.007 105.510   2.873  1.00 34.39           C  
ANISOU  212  CB  ASP A  52     3996   4572   4498    288    -12    325       C  
ATOM    213  CG  ASP A  52      92.662 106.741   3.741  1.00 37.00           C  
ANISOU  213  CG  ASP A  52     4332   4871   4857    310      6    332       C  
ATOM    214  OD1 ASP A  52      92.051 106.539   4.838  1.00 38.42           O  
ANISOU  214  OD1 ASP A  52     4509   5044   5044    309     11    316       O  
ATOM    215  OD2 ASP A  52      93.010 107.902   3.363  1.00 37.33           O  
ANISOU  215  OD2 ASP A  52     4380   4892   4913    327     17    354       O  
ATOM    216  N   ALA A  53      94.797 103.006   2.059  1.00 30.04           N  
ANISOU  216  N   ALA A  53     3462   4044   3908    233    -34    287       N  
ATOM    217  CA  ALA A  53      95.086 101.883   1.209  1.00 31.69           C  
ANISOU  217  CA  ALA A  53     3668   4279   4093    214    -46    279       C  
ATOM    218  C   ALA A  53      95.321 100.597   2.008  1.00 32.20           C  
ANISOU  218  C   ALA A  53     3739   4341   4155    190    -48    247       C  
ATOM    219  O   ALA A  53      94.844  99.538   1.611  1.00 32.53           O  
ANISOU  219  O   ALA A  53     3770   4411   4179    176    -58    237       O  
ATOM    220  CB  ALA A  53      96.287 102.177   0.302  1.00 31.56           C  
ANISOU  220  CB  ALA A  53     3664   4255   4072    211    -44    289       C  
ATOM    221  N   THR A  54      96.066 100.695   3.123  1.00 30.80           N  
ANISOU  221  N   THR A  54     3579   4130   3995    185    -40    233       N  
ATOM    222  CA  THR A  54      96.300  99.541   3.971  1.00 29.28           C  
ANISOU  222  CA  THR A  54     3392   3932   3800    165    -41    207       C  
ATOM    223  C   THR A  54      94.975  99.017   4.611  1.00 30.02           C  
ANISOU  223  C   THR A  54     3471   4043   3892    164    -43    198       C  
ATOM    224  O   THR A  54      94.707  97.784   4.671  1.00 26.44           O  
ANISOU  224  O   THR A  54     3013   3607   3428    147    -49    182       O  
ATOM    225  CB  THR A  54      97.300  99.849   5.097  1.00 28.55           C  
ANISOU  225  CB  THR A  54     3319   3803   3725    161    -32    195       C  
ATOM    226  OG1 THR A  54      98.508 100.479   4.573  1.00 28.49           O  
ANISOU  226  OG1 THR A  54     3325   3778   3724    162    -29    204       O  
ATOM    227  CG2 THR A  54      97.622  98.553   5.843  1.00 27.75           C  
ANISOU  227  CG2 THR A  54     3224   3700   3620    140    -35    171       C  
ATOM    228  N   LEU A  55      94.182  99.941   5.134  1.00 29.81           N  
ANISOU  228  N   LEU A  55     3438   4011   3877    183    -37    208       N  
ATOM    229  CA  LEU A  55      92.880  99.579   5.738  1.00 31.25           C  
ANISOU  229  CA  LEU A  55     3605   4209   4060    185    -37    202       C  
ATOM    230  C   LEU A  55      91.963  98.819   4.763  1.00 31.80           C  
ANISOU  230  C   LEU A  55     3652   4319   4110    180    -49    206       C  
ATOM    231  O   LEU A  55      91.377  97.777   5.093  1.00 31.29           O  
ANISOU  231  O   LEU A  55     3579   4270   4039    165    -53    190       O  
ATOM    232  CB  LEU A  55      92.173 100.828   6.271  1.00 31.51           C  
ANISOU  232  CB  LEU A  55     3632   4229   4109    209    -26    216       C  
ATOM    233  CG  LEU A  55      90.740 100.683   6.804  1.00 33.25           C  
ANISOU  233  CG  LEU A  55     3835   4467   4333    217    -25    215       C  
ATOM    234  CD1 LEU A  55      90.731  99.769   8.027  1.00 33.99           C  
ANISOU  234  CD1 LEU A  55     3936   4552   4428    199    -21    189       C  
ATOM    235  CD2 LEU A  55      90.081 102.039   7.114  1.00 33.83           C  
ANISOU  235  CD2 LEU A  55     3902   4528   4425    244    -13    232       C  
ATOM    236  N   GLU A  56      91.879  99.333   3.549  1.00 32.63           N  
ANISOU  236  N   GLU A  56     3748   4444   4207    190    -56    226       N  
ATOM    237  CA  GLU A  56      91.127  98.666   2.484  1.00 36.25           C  
ANISOU  237  CA  GLU A  56     4186   4944   4644    183    -69    230       C  
ATOM    238  C   GLU A  56      91.613  97.240   2.124  1.00 33.64           C  
ANISOU  238  C   GLU A  56     3861   4626   4296    155    -76    208       C  
ATOM    239  O   GLU A  56      90.788  96.343   1.961  1.00 30.58           O  
ANISOU  239  O   GLU A  56     3457   4265   3897    142    -84    197       O  
ATOM    240  CB  GLU A  56      91.078  99.545   1.232  1.00 39.21           C  
ANISOU  240  CB  GLU A  56     4553   5336   5010    200    -75    259       C  
ATOM    241  CG  GLU A  56      90.299  98.904   0.103  1.00 44.92           C  
ANISOU  241  CG  GLU A  56     5254   6106   5708    193    -90    263       C  
ATOM    242  CD  GLU A  56      90.139  99.827  -1.088  1.00 50.65           C  
ANISOU  242  CD  GLU A  56     5969   6851   6423    212    -96    294       C  
ATOM    243  OE1 GLU A  56      89.255 100.721  -1.056  1.00 57.45           O  
ANISOU  243  OE1 GLU A  56     6815   7721   7294    236    -95    317       O  
ATOM    244  OE2 GLU A  56      90.879  99.634  -2.059  1.00 50.78           O  
ANISOU  244  OE2 GLU A  56     5994   6877   6423    203   -101    297       O  
ATOM    245  N   LYS A  57      92.921  97.069   1.965  1.00 33.24           N  
ANISOU  245  N   LYS A  57     3830   4554   4245    145    -73    201       N  
ATOM    246  CA  LYS A  57      93.528  95.753   1.743  1.00 36.70           C  
ANISOU  246  CA  LYS A  57     4276   4997   4672    120    -76    179       C  
ATOM    247  C   LYS A  57      93.268  94.759   2.912  1.00 33.27           C  
ANISOU  247  C   LYS A  57     3844   4553   4245    105    -72    156       C  
ATOM    248  O   LYS A  57      92.924  93.603   2.678  1.00 32.33           O  
ANISOU  248  O   LYS A  57     3718   4451   4115     86    -76    140       O  
ATOM    249  CB  LYS A  57      95.044  95.876   1.423  1.00 41.57           C  
ANISOU  249  CB  LYS A  57     4914   5591   5291    116    -72    179       C  
ATOM    250  CG  LYS A  57      95.772  94.537   1.336  1.00 50.45           C  
ANISOU  250  CG  LYS A  57     6047   6713   6408     91    -71    157       C  
ATOM    251  CD  LYS A  57      97.261  94.602   0.900  1.00 56.95           C  
ANISOU  251  CD  LYS A  57     6888   7517   7233     87    -67    157       C  
ATOM    252  CE  LYS A  57      98.273  94.568   2.060  1.00 59.25           C  
ANISOU  252  CE  LYS A  57     7197   7771   7544     84    -58    148       C  
ATOM    253  NZ  LYS A  57      98.679  95.924   2.532  1.00 59.29           N  
ANISOU  253  NZ  LYS A  57     7209   7752   7565    101    -53    163       N  
ATOM    254  N   VAL A  58      93.471  95.211   4.144  1.00 31.77           N  
ANISOU  254  N   VAL A  58     3664   4333   4073    112    -63    154       N  
ATOM    255  CA  VAL A  58      93.279  94.366   5.355  1.00 30.38           C  
ANISOU  255  CA  VAL A  58     3492   4146   3904    100    -58    134       C  
ATOM    256  C   VAL A  58      91.781  94.025   5.548  1.00 29.98           C  
ANISOU  256  C   VAL A  58     3421   4121   3851    100    -60    132       C  
ATOM    257  O   VAL A  58      91.434  92.899   5.864  1.00 28.15           O  
ANISOU  257  O   VAL A  58     3184   3896   3615     83    -60    115       O  
ATOM    258  CB  VAL A  58      93.873  95.050   6.577  1.00 29.80           C  
ANISOU  258  CB  VAL A  58     3436   4039   3849    109    -48    133       C  
ATOM    259  CG1 VAL A  58      93.400  94.417   7.884  1.00 32.14           C  
ANISOU  259  CG1 VAL A  58     3734   4327   4152    101    -42    118       C  
ATOM    260  CG2 VAL A  58      95.428  95.031   6.533  1.00 30.32           C  
ANISOU  260  CG2 VAL A  58     3522   4080   3919    102    -46    130       C  
ATOM    261  N   LYS A  59      90.905  95.017   5.375  1.00 29.06           N  
ANISOU  261  N   LYS A  59     3289   4016   3738    120    -61    149       N  
ATOM    262  CA  LYS A  59      89.470  94.755   5.420  1.00 30.71           C  
ANISOU  262  CA  LYS A  59     3473   4252   3943    121    -64    149       C  
ATOM    263  C   LYS A  59      89.059  93.623   4.455  1.00 29.19           C  
ANISOU  263  C   LYS A  59     3266   4092   3731    101    -75    140       C  
ATOM    264  O   LYS A  59      88.391  92.667   4.864  1.00 28.40           O  
ANISOU  264  O   LYS A  59     3157   4003   3630     85    -75    124       O  
ATOM    265  CB  LYS A  59      88.679  96.048   5.138  1.00 32.77           C  
ANISOU  265  CB  LYS A  59     3718   4522   4209    148    -65    174       C  
ATOM    266  CG  LYS A  59      87.190  95.874   5.366  1.00 35.77           C  
ANISOU  266  CG  LYS A  59     4073   4929   4591    151    -66    175       C  
ATOM    267  CD  LYS A  59      86.394  97.170   5.135  1.00 37.97           C  
ANISOU  267  CD  LYS A  59     4335   5216   4878    181    -65    201       C  
ATOM    268  CE  LYS A  59      84.956  96.964   5.623  1.00 38.97           C  
ANISOU  268  CE  LYS A  59     4436   5363   5010    184    -63    200       C  
ATOM    269  NZ  LYS A  59      84.274  95.822   4.936  1.00 39.71           N  
ANISOU  269  NZ  LYS A  59     4509   5496   5086    163    -77    190       N  
ATOM    270  N   ALA A  60      89.502  93.709   3.193  1.00 29.74           N  
ANISOU  270  N   ALA A  60     3336   4179   3787     99    -84    148       N  
ATOM    271  CA  ALA A  60      89.197  92.694   2.184  1.00 30.43           C  
ANISOU  271  CA  ALA A  60     3411   4299   3853     79    -95    137       C  
ATOM    272  C   ALA A  60      89.763  91.314   2.541  1.00 31.06           C  
ANISOU  272  C   ALA A  60     3504   4366   3932     52    -90    110       C  
ATOM    273  O   ALA A  60      89.103  90.249   2.387  1.00 28.90           O  
ANISOU  273  O   ALA A  60     3219   4113   3651     32    -93     93       O  
ATOM    274  CB  ALA A  60      89.675  93.145   0.792  1.00 30.53           C  
ANISOU  274  CB  ALA A  60     3423   4328   3848     83   -104    152       C  
ATOM    275  N   GLU A  61      90.968  91.324   3.075  1.00 30.96           N  
ANISOU  275  N   GLU A  61     3516   4319   3929     51    -81    106       N  
ATOM    276  CA  GLU A  61      91.575  90.080   3.566  1.00 32.49           C  
ANISOU  276  CA  GLU A  61     3723   4495   4126     30    -75     83       C  
ATOM    277  C   GLU A  61      90.804  89.426   4.731  1.00 30.47           C  
ANISOU  277  C   GLU A  61     3462   4235   3881     22    -68     71       C  
ATOM    278  O   GLU A  61      90.542  88.236   4.731  1.00 29.60           O  
ANISOU  278  O   GLU A  61     3349   4131   3767      1    -67     53       O  
ATOM    279  CB  GLU A  61      93.009  90.377   3.986  1.00 36.74           C  
ANISOU  279  CB  GLU A  61     4286   4999   4675     34    -68     85       C  
ATOM    280  CG  GLU A  61      93.946  89.249   3.822  1.00 40.05           C  
ANISOU  280  CG  GLU A  61     4719   5407   5093     14    -64     68       C  
ATOM    281  CD  GLU A  61      95.219  89.411   4.673  1.00 46.86           C  
ANISOU  281  CD  GLU A  61     5603   6233   5970     18    -56     68       C  
ATOM    282  OE1 GLU A  61      95.586  90.561   5.127  1.00 44.10           O  
ANISOU  282  OE1 GLU A  61     5260   5867   5630     36    -55     82       O  
ATOM    283  OE2 GLU A  61      95.847  88.338   4.862  1.00 49.52           O  
ANISOU  283  OE2 GLU A  61     5949   6558   6309      2    -51     53       O  
ATOM    284  N   VAL A  62      90.459  90.191   5.764  1.00 29.34           N  
ANISOU  284  N   VAL A  62     3319   4077   3751     38    -63     79       N  
ATOM    285  CA  VAL A  62      89.760  89.615   6.874  1.00 28.77           C  
ANISOU  285  CA  VAL A  62     3243   4000   3687     31    -55     69       C  
ATOM    286  C   VAL A  62      88.330  89.192   6.418  1.00 29.65           C  
ANISOU  286  C   VAL A  62     3327   4147   3791     24    -61     66       C  
ATOM    287  O   VAL A  62      87.826  88.135   6.840  1.00 29.59           O  
ANISOU  287  O   VAL A  62     3314   4144   3785      6    -56     50       O  
ATOM    288  CB  VAL A  62      89.726  90.578   8.085  1.00 30.00           C  
ANISOU  288  CB  VAL A  62     3407   4134   3858     50    -47     77       C  
ATOM    289  CG1 VAL A  62      88.808  90.093   9.184  1.00 28.98           C  
ANISOU  289  CG1 VAL A  62     3270   4004   3735     46    -38     69       C  
ATOM    290  CG2 VAL A  62      91.148  90.824   8.650  1.00 30.81           C  
ANISOU  290  CG2 VAL A  62     3536   4203   3968     53    -42     76       C  
ATOM    291  N   ASP A  63      87.673  90.011   5.601  1.00 29.13           N  
ANISOU  291  N   ASP A  63     3242   4106   3718     38    -70     81       N  
ATOM    292  CA  ASP A  63      86.313  89.671   5.130  1.00 30.48           C  
ANISOU  292  CA  ASP A  63     3384   4315   3881     31    -78     80       C  
ATOM    293  C   ASP A  63      86.327  88.329   4.368  1.00 30.44           C  
ANISOU  293  C   ASP A  63     3376   4328   3862      2    -83     60       C  
ATOM    294  O   ASP A  63      85.420  87.540   4.533  1.00 29.02           O  
ANISOU  294  O   ASP A  63     3180   4165   3682    -14    -82     47       O  
ATOM    295  CB  ASP A  63      85.697  90.772   4.275  1.00 30.89           C  
ANISOU  295  CB  ASP A  63     3417   4394   3926     52    -88    103       C  
ATOM    296  CG  ASP A  63      85.291  92.011   5.084  1.00 33.10           C  
ANISOU  296  CG  ASP A  63     3694   4659   4222     80    -81    121       C  
ATOM    297  OD1 ASP A  63      85.252  91.967   6.356  1.00 34.05           O  
ANISOU  297  OD1 ASP A  63     3824   4755   4358     82    -68    114       O  
ATOM    298  OD2 ASP A  63      84.979  93.044   4.426  1.00 35.37           O  
ANISOU  298  OD2 ASP A  63     3969   4962   4508    101    -87    143       O  
ATOM    299  N   ALA A  64      87.371  88.081   3.578  1.00 29.96           N  
ANISOU  299  N   ALA A  64     3331   4262   3791     -6    -86     55       N  
ATOM    300  CA  ALA A  64      87.513  86.794   2.899  1.00 32.49           C  
ANISOU  300  CA  ALA A  64     3652   4594   4100    -34    -87     34       C  
ATOM    301  C   ALA A  64      87.601  85.629   3.890  1.00 32.02           C  
ANISOU  301  C   ALA A  64     3602   4512   4053    -53    -74     14       C  
ATOM    302  O   ALA A  64      86.920  84.608   3.730  1.00 30.79           O  
ANISOU  302  O   ALA A  64     3434   4371   3893    -75    -73     -4       O  
ATOM    303  CB  ALA A  64      88.707  86.787   1.927  1.00 32.13           C  
ANISOU  303  CB  ALA A  64     3622   4543   4042    -37    -90     34       C  
ATOM    304  N   GLU A  65      88.411  85.778   4.932  1.00 34.00           N  
ANISOU  304  N   GLU A  65     3874   4726   4318    -45    -63     16       N  
ATOM    305  CA  GLU A  65      88.567  84.687   5.913  1.00 32.77           C  
ANISOU  305  CA  GLU A  65     3728   4547   4174    -60    -50      0       C  
ATOM    306  C   GLU A  65      87.312  84.442   6.720  1.00 33.08           C  
ANISOU  306  C   GLU A  65     3751   4596   4221    -64    -46     -3       C  
ATOM    307  O   GLU A  65      86.970  83.265   6.997  1.00 31.99           O  
ANISOU  307  O   GLU A  65     3612   4458   4087    -86    -38    -20       O  
ATOM    308  CB  GLU A  65      89.727  84.953   6.833  1.00 33.76           C  
ANISOU  308  CB  GLU A  65     3879   4636   4312    -50    -42      5       C  
ATOM    309  CG  GLU A  65      91.049  84.803   6.143  1.00 33.79           C  
ANISOU  309  CG  GLU A  65     3900   4627   4312    -53    -43      3       C  
ATOM    310  CD  GLU A  65      91.437  83.373   5.824  1.00 35.09           C  
ANISOU  310  CD  GLU A  65     4072   4786   4475    -78    -36    -16       C  
ATOM    311  OE1 GLU A  65      91.067  82.412   6.528  1.00 33.25           O  
ANISOU  311  OE1 GLU A  65     3839   4545   4251    -91    -27    -28       O  
ATOM    312  OE2 GLU A  65      92.174  83.222   4.840  1.00 39.87           O  
ANISOU  312  OE2 GLU A  65     4682   5393   5072    -83    -39    -20       O  
ATOM    313  N   ILE A  66      86.616  85.526   7.083  1.00 31.95           N  
ANISOU  313  N   ILE A  66     3596   4462   4082    -43    -48     13       N  
ATOM    314  CA  ILE A  66      85.301  85.406   7.739  1.00 32.50           C  
ANISOU  314  CA  ILE A  66     3645   4545   4157    -44    -44     11       C  
ATOM    315  C   ILE A  66      84.342  84.611   6.851  1.00 33.35           C  
ANISOU  315  C   ILE A  66     3729   4688   4256    -65    -51     -1       C  
ATOM    316  O   ILE A  66      83.601  83.786   7.370  1.00 34.72           O  
ANISOU  316  O   ILE A  66     3893   4865   4435    -81    -44    -13       O  
ATOM    317  CB  ILE A  66      84.686  86.766   8.144  1.00 33.45           C  
ANISOU  317  CB  ILE A  66     3754   4670   4283    -16    -45     31       C  
ATOM    318  CG1 ILE A  66      85.537  87.427   9.239  1.00 35.29           C  
ANISOU  318  CG1 ILE A  66     4013   4868   4529      0    -35     38       C  
ATOM    319  CG2 ILE A  66      83.204  86.644   8.572  1.00 32.04           C  
ANISOU  319  CG2 ILE A  66     3550   4513   4111    -18    -42     30       C  
ATOM    320  CD1 ILE A  66      85.103  88.851   9.600  1.00 36.07           C  
ANISOU  320  CD1 ILE A  66     4105   4966   4635     28    -34     57       C  
ATOM    321  N   ALA A  67      84.338  84.850   5.530  1.00 34.32           N  
ANISOU  321  N   ALA A  67     3841   4837   4362    -67    -66      2       N  
ATOM    322  CA  ALA A  67      83.478  84.049   4.612  1.00 33.05           C  
ANISOU  322  CA  ALA A  67     3658   4713   4189    -90    -75    -12       C  
ATOM    323  C   ALA A  67      83.870  82.593   4.603  1.00 32.75           C  
ANISOU  323  C   ALA A  67     3632   4662   4151   -121    -65    -38       C  
ATOM    324  O   ALA A  67      83.016  81.743   4.510  1.00 32.84           O  
ANISOU  324  O   ALA A  67     3625   4690   4161   -143    -64    -53       O  
ATOM    325  CB  ALA A  67      83.541  84.598   3.213  1.00 35.15           C  
ANISOU  325  CB  ALA A  67     3913   5008   4433    -85    -92     -3       C  
ATOM    326  N   LEU A  68      85.164  82.288   4.670  1.00 31.96           N  
ANISOU  326  N   LEU A  68     3560   4532   4054   -123    -58    -42       N  
ATOM    327  CA  LEU A  68      85.598  80.910   4.667  1.00 33.45           C  
ANISOU  327  CA  LEU A  68     3760   4704   4245   -149    -47    -65       C  
ATOM    328  C   LEU A  68      85.268  80.150   5.963  1.00 34.28           C  
ANISOU  328  C   LEU A  68     3869   4786   4369   -158    -31    -73       C  
ATOM    329  O   LEU A  68      85.137  78.956   5.928  1.00 33.21           O  
ANISOU  329  O   LEU A  68     3735   4647   4237   -183    -22    -92       O  
ATOM    330  CB  LEU A  68      87.097  80.844   4.380  1.00 36.88           C  
ANISOU  330  CB  LEU A  68     4222   5113   4679   -146    -44    -65       C  
ATOM    331  CG  LEU A  68      87.566  81.169   2.961  1.00 39.60           C  
ANISOU  331  CG  LEU A  68     4566   5477   5003   -147    -56    -65       C  
ATOM    332  CD1 LEU A  68      89.086  81.219   2.962  1.00 42.14           C  
ANISOU  332  CD1 LEU A  68     4915   5767   5329   -139    -49    -62       C  
ATOM    333  CD2 LEU A  68      87.096  80.117   1.958  1.00 39.80           C  
ANISOU  333  CD2 LEU A  68     4580   5527   5015   -177    -58    -89       C  
ATOM    334  N   GLY A  69      85.096  80.833   7.098  1.00 33.59           N  
ANISOU  334  N   GLY A  69     3784   4684   4293   -138    -26    -57       N  
ATOM    335  CA  GLY A  69      84.734  80.131   8.339  1.00 33.77           C  
ANISOU  335  CA  GLY A  69     3811   4689   4332   -146     -9    -63       C  
ATOM    336  C   GLY A  69      85.883  80.094   9.361  1.00 32.17           C  
ANISOU  336  C   GLY A  69     3638   4446   4140   -136      2    -57       C  
ATOM    337  O   GLY A  69      86.810  80.902   9.336  1.00 28.69           O  
ANISOU  337  O   GLY A  69     3211   3992   3697   -118     -3    -45       O  
ATOM    338  N   ILE A  70      85.784  79.178  10.298  1.00 31.71           N  
ANISOU  338  N   ILE A  70     3586   4368   4093   -148     17    -64       N  
ATOM    339  CA  ILE A  70      86.749  79.128  11.403  1.00 31.11           C  
ANISOU  339  CA  ILE A  70     3536   4259   4027   -139     28    -56       C  
ATOM    340  C   ILE A  70      87.249  77.709  11.446  1.00 29.38           C  
ANISOU  340  C   ILE A  70     3329   4019   3815   -161     40    -70       C  
ATOM    341  O   ILE A  70      86.494  76.824  11.767  1.00 26.65           O  
ANISOU  341  O   ILE A  70     2975   3675   3476   -178     51    -80       O  
ATOM    342  CB  ILE A  70      86.082  79.492  12.755  1.00 32.25           C  
ANISOU  342  CB  ILE A  70     3677   4397   4178   -128     37    -47       C  
ATOM    343  CG1 ILE A  70      85.589  80.952  12.723  1.00 32.20           C  
ANISOU  343  CG1 ILE A  70     3660   4408   4167   -105     26    -33       C  
ATOM    344  CG2 ILE A  70      87.083  79.294  13.907  1.00 33.60           C  
ANISOU  344  CG2 ILE A  70     3875   4535   4357   -121     47    -40       C  
ATOM    345  CD1 ILE A  70      84.776  81.350  13.917  1.00 32.50           C  
ANISOU  345  CD1 ILE A  70     3692   4445   4211    -95     36    -26       C  
ATOM    346  N   ASP A  71      88.544  77.522  11.198  1.00 28.38           N  
ANISOU  346  N   ASP A  71     3222   3872   3689   -158     40    -69       N  
ATOM    347  CA  ASP A  71      89.151  76.205  11.191  1.00 28.61           C  
ANISOU  347  CA  ASP A  71     3264   3878   3726   -176     54    -81       C  
ATOM    348  C   ASP A  71      90.319  76.166  12.205  1.00 27.18           C  
ANISOU  348  C   ASP A  71     3107   3665   3555   -163     61    -68       C  
ATOM    349  O   ASP A  71      91.289  76.981  12.144  1.00 25.55           O  
ANISOU  349  O   ASP A  71     2911   3451   3345   -146     52    -57       O  
ATOM    350  CB  ASP A  71      89.634  75.845   9.766  1.00 29.80           C  
ANISOU  350  CB  ASP A  71     3415   4038   3870   -188     49    -94       C  
ATOM    351  CG  ASP A  71      90.018  74.392   9.643  1.00 32.21           C  
ANISOU  351  CG  ASP A  71     3730   4322   4186   -210     65   -110       C  
ATOM    352  OD1 ASP A  71      89.462  73.554  10.339  1.00 40.22           O  
ANISOU  352  OD1 ASP A  71     4743   5328   5212   -223     79   -115       O  
ATOM    353  OD2 ASP A  71      90.868  74.037   8.854  1.00 36.22           O  
ANISOU  353  OD2 ASP A  71     4248   4823   4693   -215     66   -118       O  
ATOM    354  N   THR A  72      90.203  75.251  13.164  1.00 26.18           N  
ANISOU  354  N   THR A  72     2987   3521   3440   -172     77    -68       N  
ATOM    355  CA  THR A  72      91.225  75.051  14.207  1.00 26.04           C  
ANISOU  355  CA  THR A  72     2991   3474   3431   -162     84    -55       C  
ATOM    356  C   THR A  72      91.618  73.585  14.233  1.00 26.11           C  
ANISOU  356  C   THR A  72     3009   3460   3453   -179    101    -63       C  
ATOM    357  O   THR A  72      91.203  72.880  15.166  1.00 26.98           O  
ANISOU  357  O   THR A  72     3121   3558   3571   -185    115    -60       O  
ATOM    358  CB  THR A  72      90.722  75.492  15.630  1.00 26.68           C  
ANISOU  358  CB  THR A  72     3073   3553   3512   -150     88    -42       C  
ATOM    359  OG1 THR A  72      89.463  74.843  15.988  1.00 25.88           O  
ANISOU  359  OG1 THR A  72     2959   3460   3415   -165    100    -49       O  
ATOM    360  CG2 THR A  72      90.547  76.981  15.683  1.00 25.98           C  
ANISOU  360  CG2 THR A  72     2979   3480   3413   -131     73    -33       C  
ATOM    361  N   PRO A  73      92.389  73.114  13.209  1.00 26.45           N  
ANISOU  361  N   PRO A  73     3056   3496   3497   -186    101    -73       N  
ATOM    362  CA  PRO A  73      92.570  71.645  13.037  1.00 26.50           C  
ANISOU  362  CA  PRO A  73     3069   3482   3518   -206    120    -84       C  
ATOM    363  C   PRO A  73      93.501  71.041  14.100  1.00 27.24           C  
ANISOU  363  C   PRO A  73     3180   3543   3625   -198    132    -69       C  
ATOM    364  O   PRO A  73      94.390  71.724  14.619  1.00 26.90           O  
ANISOU  364  O   PRO A  73     3148   3494   3580   -178    124    -52       O  
ATOM    365  CB  PRO A  73      93.194  71.514  11.627  1.00 26.34           C  
ANISOU  365  CB  PRO A  73     3049   3465   3493   -213    116    -99       C  
ATOM    366  CG  PRO A  73      93.861  72.861  11.365  1.00 26.89           C  
ANISOU  366  CG  PRO A  73     3121   3546   3551   -191     97    -86       C  
ATOM    367  CD  PRO A  73      93.006  73.882  12.095  1.00 26.87           C  
ANISOU  367  CD  PRO A  73     3109   3561   3540   -179     86    -75       C  
ATOM    368  N   LEU A  74      93.315  69.748  14.373  1.00 27.60           N  
ANISOU  368  N   LEU A  74     3230   3570   3686   -214    153    -75       N  
ATOM    369  CA  LEU A  74      94.183  68.992  15.231  1.00 28.66           C  
ANISOU  369  CA  LEU A  74     3381   3673   3836   -208    167    -60       C  
ATOM    370  C   LEU A  74      95.613  69.127  14.688  1.00 27.91           C  
ANISOU  370  C   LEU A  74     3296   3565   3743   -196    161    -56       C  
ATOM    371  O   LEU A  74      95.848  68.785  13.573  1.00 27.88           O  
ANISOU  371  O   LEU A  74     3291   3561   3741   -207    164    -72       O  
ATOM    372  CB  LEU A  74      93.717  67.530  15.261  1.00 31.32           C  
ANISOU  372  CB  LEU A  74     3719   3992   4191   -230    191    -71       C  
ATOM    373  CG  LEU A  74      94.522  66.600  16.184  1.00 33.24           C  
ANISOU  373  CG  LEU A  74     3978   4201   4452   -224    209    -54       C  
ATOM    374  CD1 LEU A  74      94.325  66.966  17.668  1.00 33.05           C  
ANISOU  374  CD1 LEU A  74     3958   4177   4424   -210    207    -30       C  
ATOM    375  CD2 LEU A  74      94.148  65.129  15.940  1.00 34.04           C  
ANISOU  375  CD2 LEU A  74     4080   4280   4573   -248    235    -68       C  
ATOM    376  N   PRO A  75      96.557  69.689  15.441  1.00 27.47           N  
ANISOU  376  N   PRO A  75     3250   3501   3685   -175    153    -35       N  
ATOM    377  CA  PRO A  75      97.899  69.897  14.835  1.00 27.19           C  
ANISOU  377  CA  PRO A  75     3222   3455   3652   -165    148    -32       C  
ATOM    378  C   PRO A  75      98.655  68.598  14.439  1.00 27.56           C  
ANISOU  378  C   PRO A  75     3277   3474   3719   -173    167    -36       C  
ATOM    379  O   PRO A  75      98.653  67.659  15.257  1.00 26.49           O  
ANISOU  379  O   PRO A  75     3149   3319   3599   -176    184    -27       O  
ATOM    380  CB  PRO A  75      98.667  70.640  15.948  1.00 26.48           C  
ANISOU  380  CB  PRO A  75     3140   3362   3559   -143    136     -7       C  
ATOM    381  CG  PRO A  75      97.619  71.298  16.758  1.00 27.55           C  
ANISOU  381  CG  PRO A  75     3270   3515   3683   -141    130     -3       C  
ATOM    382  CD  PRO A  75      96.444  70.335  16.749  1.00 27.99           C  
ANISOU  382  CD  PRO A  75     3320   3571   3745   -161    147    -16       C  
ATOM    383  N   LYS A  76      99.281  68.584  13.235  1.00 27.62           N  
ANISOU  383  N   LYS A  76     3285   3482   3728   -176    167    -49       N  
ATOM    384  CA ALYS A  76     100.038  67.410  12.679  0.50 28.51           C  
ANISOU  384  CA ALYS A  76     3406   3568   3859   -184    187    -57       C  
ATOM    385  CA BLYS A  76     100.049  67.404  12.714  0.50 28.50           C  
ANISOU  385  CA BLYS A  76     3404   3566   3858   -183    187    -56       C  
ATOM    386  C   LYS A  76     101.335  67.776  11.992  1.00 27.02           C  
ANISOU  386  C   LYS A  76     3221   3374   3672   -172    181    -54       C  
ATOM    387  O   LYS A  76     102.293  67.005  12.040  1.00 24.33           O  
ANISOU  387  O   LYS A  76     2889   3008   3349   -167    196    -48       O  
ATOM    388  CB ALYS A  76      99.264  66.638  11.583  0.50 29.39           C  
ANISOU  388  CB ALYS A  76     3512   3683   3972   -210    200    -87       C  
ATOM    389  CB BLYS A  76      99.236  66.536  11.714  0.50 29.29           C  
ANISOU  389  CB BLYS A  76     3500   3668   3962   -210    202    -85       C  
ATOM    390  CG ALYS A  76      97.778  66.487  11.784  0.50 31.82           C  
ANISOU  390  CG ALYS A  76     3809   4006   4273   -227    201    -98       C  
ATOM    391  CG BLYS A  76      98.132  65.659  12.310  0.50 31.50           C  
ANISOU  391  CG BLYS A  76     3777   3941   4250   -227    217    -91       C  
ATOM    392  CD ALYS A  76      97.306  65.164  11.180  0.50 32.49           C  
ANISOU  392  CD ALYS A  76     3894   4077   4372   -253    225   -122       C  
ATOM    393  CD BLYS A  76      98.504  65.063  13.656  0.50 32.17           C  
ANISOU  393  CD BLYS A  76     3872   4000   4352   -216    230    -67       C  
ATOM    394  CE ALYS A  76      95.974  64.714  11.801  0.50 33.52           C  
ANISOU  394  CE ALYS A  76     4017   4212   4505   -269    233   -127       C  
ATOM    395  CE BLYS A  76      97.297  64.540  14.416  0.50 31.85           C  
ANISOU  395  CE BLYS A  76     3827   3959   4315   -229    241    -67       C  
ATOM    396  NZ ALYS A  76      96.196  63.676  12.840  0.50 33.91           N  
ANISOU  396  NZ ALYS A  76     4077   4228   4578   -268    255   -113       N  
ATOM    397  NZ BLYS A  76      97.699  63.621  15.498  0.50 32.22           N  
ANISOU  397  NZ BLYS A  76     3884   3975   4382   -223    259    -47       N  
ATOM    398  N   ASP A  77     101.310  68.912  11.286  1.00 25.80           N  
ANISOU  398  N   ASP A  77     3060   3244   3498   -167    162    -59       N  
ATOM    399  CA  ASP A  77     102.302  69.207  10.270  1.00 27.55           C  
ANISOU  399  CA  ASP A  77     3283   3465   3718   -163    160    -64       C  
ATOM    400  C   ASP A  77     103.495  70.067  10.654  1.00 26.67           C  
ANISOU  400  C   ASP A  77     3176   3351   3607   -140    147    -43       C  
ATOM    401  O   ASP A  77     103.452  70.797  11.629  1.00 27.79           O  
ANISOU  401  O   ASP A  77     3318   3499   3744   -128    133    -26       O  
ATOM    402  CB  ASP A  77     101.600  69.836   9.066  1.00 28.22           C  
ANISOU  402  CB  ASP A  77     3360   3580   3783   -173    149    -83       C  
ATOM    403  CG  ASP A  77     100.480  68.956   8.526  1.00 29.71           C  
ANISOU  403  CG  ASP A  77     3544   3775   3971   -198    161   -108       C  
ATOM    404  OD1 ASP A  77     100.779  67.755   8.241  1.00 30.73           O  
ANISOU  404  OD1 ASP A  77     3680   3881   4116   -210    183   -120       O  
ATOM    405  OD2 ASP A  77      99.347  69.485   8.348  1.00 27.93           O  
ANISOU  405  OD2 ASP A  77     3307   3576   3729   -206    150   -115       O  
ATOM    406  N   TYR A  78     104.548  69.942   9.849  1.00 27.03           N  
ANISOU  406  N   TYR A  78     3224   3387   3659   -137    152    -46       N  
ATOM    407  CA  TYR A  78     105.658  70.863   9.810  1.00 26.52           C  
ANISOU  407  CA  TYR A  78     3160   3323   3591   -120    139    -31       C  
ATOM    408  C   TYR A  78     105.271  72.109   9.009  1.00 25.76           C  
ANISOU  408  C   TYR A  78     3058   3256   3473   -119    121    -38       C  
ATOM    409  O   TYR A  78     104.186  72.182   8.387  1.00 25.73           O  
ANISOU  409  O   TYR A  78     3049   3272   3456   -132    119    -54       O  
ATOM    410  CB  TYR A  78     106.910  70.163   9.204  1.00 27.09           C  
ANISOU  410  CB  TYR A  78     3238   3375   3682   -117    155    -32       C  
ATOM    411  CG  TYR A  78     107.607  69.224  10.196  1.00 28.85           C  
ANISOU  411  CG  TYR A  78     3466   3569   3928   -109    168    -15       C  
ATOM    412  CD1 TYR A  78     108.041  69.710  11.437  1.00 27.36           C  
ANISOU  412  CD1 TYR A  78     3277   3378   3741    -92    155     10       C  
ATOM    413  CD2 TYR A  78     107.892  67.866   9.878  1.00 27.61           C  
ANISOU  413  CD2 TYR A  78     3313   3386   3792   -116    194    -24       C  
ATOM    414  CE1 TYR A  78     108.723  68.895  12.325  1.00 27.11           C  
ANISOU  414  CE1 TYR A  78     3249   3324   3730    -83    165     28       C  
ATOM    415  CE2 TYR A  78     108.574  67.032  10.787  1.00 27.65           C  
ANISOU  415  CE2 TYR A  78     3323   3364   3820   -106    206     -4       C  
ATOM    416  CZ  TYR A  78     108.970  67.554  12.016  1.00 28.37           C  
ANISOU  416  CZ  TYR A  78     3412   3457   3910    -89    191     23       C  
ATOM    417  OH  TYR A  78     109.600  66.781  13.014  1.00 28.09           O  
ANISOU  417  OH  TYR A  78     3379   3398   3894    -78    200     45       O  
ATOM    418  N   SER A  79     106.151  73.100   9.017  1.00 24.38           N  
ANISOU  418  N   SER A  79     2883   3085   3295   -104    108    -25       N  
ATOM    419  CA  SER A  79     105.921  74.326   8.302  1.00 24.37           C  
ANISOU  419  CA  SER A  79     2877   3107   3275   -101     93    -27       C  
ATOM    420  C   SER A  79     105.612  74.086   6.792  1.00 25.56           C  
ANISOU  420  C   SER A  79     3025   3271   3416   -115     99    -48       C  
ATOM    421  O   SER A  79     106.131  73.184   6.133  1.00 23.57           O  
ANISOU  421  O   SER A  79     2777   3005   3173   -123    116    -59       O  
ATOM    422  CB  SER A  79     107.124  75.285   8.459  1.00 24.77           C  
ANISOU  422  CB  SER A  79     2929   3155   3329    -85     82    -11       C  
ATOM    423  OG  SER A  79     108.230  74.868   7.673  1.00 25.28           O  
ANISOU  423  OG  SER A  79     2996   3206   3403    -84     93    -13       O  
ATOM    424  N   GLY A  80     104.680  74.881   6.273  1.00 25.18           N  
ANISOU  424  N   GLY A  80     2970   3249   3347   -119     87    -54       N  
ATOM    425  CA  GLY A  80     104.182  74.646   4.954  1.00 25.44           C  
ANISOU  425  CA  GLY A  80     2999   3299   3367   -133     91    -74       C  
ATOM    426  C   GLY A  80     103.067  73.656   4.829  1.00 25.43           C  
ANISOU  426  C   GLY A  80     2995   3303   3364   -153    100    -93       C  
ATOM    427  O   GLY A  80     102.303  73.725   3.843  1.00 26.37           O  
ANISOU  427  O   GLY A  80     3107   3446   3466   -166     97   -108       O  
ATOM    428  N   GLY A  81     102.936  72.777   5.824  1.00 25.82           N  
ANISOU  428  N   GLY A  81     3048   3332   3431   -156    111    -91       N  
ATOM    429  CA  GLY A  81     101.848  71.821   5.861  1.00 26.37           C  
ANISOU  429  CA  GLY A  81     3114   3404   3502   -176    121   -108       C  
ATOM    430  C   GLY A  81     100.575  72.502   6.376  1.00 27.45           C  
ANISOU  430  C   GLY A  81     3240   3564   3626   -176    106   -104       C  
ATOM    431  O   GLY A  81     100.619  73.507   7.105  1.00 25.20           O  
ANISOU  431  O   GLY A  81     2954   3284   3338   -159     92    -85       O  
ATOM    432  N   TYR A  82      99.433  71.933   5.994  1.00 28.21           N  
ANISOU  432  N   TYR A  82     3328   3674   3716   -195    110   -122       N  
ATOM    433  CA  TYR A  82      98.132  72.492   6.351  1.00 29.09           C  
ANISOU  433  CA  TYR A  82     3427   3810   3816   -197     98   -121       C  
ATOM    434  C   TYR A  82      97.940  72.968   7.812  1.00 27.17           C  
ANISOU  434  C   TYR A  82     3184   3559   3580   -182     92   -100       C  
ATOM    435  O   TYR A  82      97.550  74.123   8.001  1.00 27.23           O  
ANISOU  435  O   TYR A  82     3185   3585   3576   -169     76    -89       O  
ATOM    436  CB  TYR A  82      97.008  71.515   5.875  1.00 32.05           C  
ANISOU  436  CB  TYR A  82     3794   4196   4190   -224    107   -145       C  
ATOM    437  CG  TYR A  82      95.688  71.736   6.514  1.00 34.65           C  
ANISOU  437  CG  TYR A  82     4109   4542   4514   -228    100   -143       C  
ATOM    438  CD1 TYR A  82      94.922  72.877   6.266  1.00 35.71           C  
ANISOU  438  CD1 TYR A  82     4229   4708   4630   -220     81   -137       C  
ATOM    439  CD2 TYR A  82      95.191  70.787   7.398  1.00 39.89           C  
ANISOU  439  CD2 TYR A  82     4774   5188   5194   -239    116   -146       C  
ATOM    440  CE1 TYR A  82      93.666  73.057   6.920  1.00 36.42           C  
ANISOU  440  CE1 TYR A  82     4305   4813   4719   -223     77   -135       C  
ATOM    441  CE2 TYR A  82      93.963  70.941   8.022  1.00 41.55           C  
ANISOU  441  CE2 TYR A  82     4971   5413   5401   -243    112   -144       C  
ATOM    442  CZ  TYR A  82      93.216  72.087   7.795  1.00 39.04           C  
ANISOU  442  CZ  TYR A  82     4638   5127   5066   -235     92   -139       C  
ATOM    443  OH  TYR A  82      92.011  72.104   8.498  1.00 43.97           O  
ANISOU  443  OH  TYR A  82     5250   5764   5692   -239     92   -137       O  
ATOM    444  N   THR A  83      98.203  72.145   8.850  1.00 26.31           N  
ANISOU  444  N   THR A  83     3083   3423   3489   -182    106    -93       N  
ATOM    445  CA  THR A  83      97.864  72.573  10.220  1.00 25.61           C  
ANISOU  445  CA  THR A  83     2995   3332   3403   -170    102    -76       C  
ATOM    446  C   THR A  83      98.756  73.736  10.695  1.00 25.88           C  
ANISOU  446  C   THR A  83     3035   3364   3434   -146     87    -55       C  
ATOM    447  O   THR A  83      98.297  74.638  11.384  1.00 25.85           O  
ANISOU  447  O   THR A  83     3027   3371   3422   -136     77    -45       O  
ATOM    448  CB  THR A  83      97.858  71.442  11.297  1.00 26.17           C  
ANISOU  448  CB  THR A  83     3073   3377   3492   -175    119    -71       C  
ATOM    449  OG1 THR A  83      99.170  70.986  11.581  1.00 24.95           O  
ANISOU  449  OG1 THR A  83     2932   3195   3352   -166    127    -60       O  
ATOM    450  CG2 THR A  83      96.972  70.241  10.909  1.00 26.74           C  
ANISOU  450  CG2 THR A  83     3141   3447   3571   -200    136    -91       C  
ATOM    451  N   HIS A  84     100.022  73.717  10.300  1.00 24.03           N  
ANISOU  451  N   HIS A  84     2810   3116   3206   -139     89    -51       N  
ATOM    452  CA  HIS A  84     100.926  74.809  10.581  1.00 23.66           C  
ANISOU  452  CA  HIS A  84     2766   3068   3155   -120     76    -35       C  
ATOM    453  C   HIS A  84     100.460  76.093   9.892  1.00 23.75           C  
ANISOU  453  C   HIS A  84     2769   3105   3149   -114     59    -36       C  
ATOM    454  O   HIS A  84     100.301  77.118  10.563  1.00 25.24           O  
ANISOU  454  O   HIS A  84     2957   3301   3333   -101     48    -24       O  
ATOM    455  CB  HIS A  84     102.346  74.410  10.179  1.00 23.81           C  
ANISOU  455  CB  HIS A  84     2794   3068   3186   -116     82    -32       C  
ATOM    456  CG  HIS A  84     103.395  75.409  10.520  1.00 23.99           C  
ANISOU  456  CG  HIS A  84     2820   3086   3208    -98     70    -15       C  
ATOM    457  ND1 HIS A  84     104.258  75.244  11.589  1.00 24.74           N  
ANISOU  457  ND1 HIS A  84     2923   3163   3315    -88     71      1       N  
ATOM    458  CD2 HIS A  84     103.751  76.571   9.923  1.00 24.19           C  
ANISOU  458  CD2 HIS A  84     2843   3124   3224    -89     58    -12       C  
ATOM    459  CE1 HIS A  84     105.111  76.258  11.624  1.00 24.35           C  
ANISOU  459  CE1 HIS A  84     2874   3115   3263    -75     59     12       C  
ATOM    460  NE2 HIS A  84     104.846  77.067  10.617  1.00 23.71           N  
ANISOU  460  NE2 HIS A  84     2788   3051   3170    -75     52      4       N  
ATOM    461  N   GLU A  85     100.146  76.044   8.603  1.00 24.50           N  
ANISOU  461  N   GLU A  85     2858   3216   3234   -124     59    -50       N  
ATOM    462  CA  GLU A  85      99.749  77.258   7.854  1.00 25.16           C  
ANISOU  462  CA  GLU A  85     2933   3325   3301   -118     44    -48       C  
ATOM    463  C   GLU A  85      98.384  77.784   8.302  1.00 24.03           C  
ANISOU  463  C   GLU A  85     2778   3202   3150   -117     36    -47       C  
ATOM    464  O   GLU A  85      98.186  78.980   8.372  1.00 24.09           O  
ANISOU  464  O   GLU A  85     2782   3222   3150   -103     24    -36       O  
ATOM    465  CB  GLU A  85      99.785  77.039   6.321  1.00 26.46           C  
ANISOU  465  CB  GLU A  85     3094   3505   3455   -129     45    -63       C  
ATOM    466  CG  GLU A  85     101.187  76.569   5.843  1.00 29.13           C  
ANISOU  466  CG  GLU A  85     3443   3822   3802   -129     54    -64       C  
ATOM    467  CD  GLU A  85     102.274  77.559   6.118  1.00 30.17           C  
ANISOU  467  CD  GLU A  85     3581   3945   3937   -109     47    -46       C  
ATOM    468  OE1 GLU A  85     102.036  78.707   5.754  1.00 33.74           O  
ANISOU  468  OE1 GLU A  85     4028   4414   4377   -100     34    -38       O  
ATOM    469  OE2 GLU A  85     103.348  77.215   6.663  1.00 31.81           O  
ANISOU  469  OE2 GLU A  85     3797   4128   4160   -103     53    -38       O  
ATOM    470  N   ARG A  86      97.462  76.900   8.644  1.00 23.16           N  
ANISOU  470  N   ARG A  86     2663   3094   3043   -131     44    -57       N  
ATOM    471  CA  ARG A  86      96.132  77.332   9.106  1.00 23.27           C  
ANISOU  471  CA  ARG A  86     2664   3126   3051   -131     39    -55       C  
ATOM    472  C   ARG A  86      96.209  78.036  10.498  1.00 23.33           C  
ANISOU  472  C   ARG A  86     2677   3124   3064   -114     36    -38       C  
ATOM    473  O   ARG A  86      95.631  79.134  10.701  1.00 22.96           O  
ANISOU  473  O   ARG A  86     2623   3092   3009   -102     26    -30       O  
ATOM    474  CB  ARG A  86      95.190  76.143   9.156  1.00 23.95           C  
ANISOU  474  CB  ARG A  86     2743   3215   3141   -152     50    -71       C  
ATOM    475  CG  ARG A  86      93.716  76.449   9.362  1.00 25.29           C  
ANISOU  475  CG  ARG A  86     2896   3408   3304   -156     45    -73       C  
ATOM    476  CD  ARG A  86      93.165  77.338   8.249  1.00 26.37           C  
ANISOU  476  CD  ARG A  86     3018   3577   3424   -153     30    -75       C  
ATOM    477  NE  ARG A  86      93.256  78.717   8.648  1.00 28.91           N  
ANISOU  477  NE  ARG A  86     3340   3904   3742   -130     19    -57       N  
ATOM    478  CZ  ARG A  86      92.813  79.746   7.949  1.00 29.21           C  
ANISOU  478  CZ  ARG A  86     3365   3966   3767   -120      5    -51       C  
ATOM    479  NH1 ARG A  86      92.286  79.564   6.773  1.00 29.41           N  
ANISOU  479  NH1 ARG A  86     3377   4016   3779   -132      0    -61       N  
ATOM    480  NH2 ARG A  86      92.873  80.969   8.475  1.00 30.10           N  
ANISOU  480  NH2 ARG A  86     3479   4078   3879    -99     -2    -34       N  
ATOM    481  N   HIS A  87      96.923  77.447  11.452  1.00 22.99           N  
ANISOU  481  N   HIS A  87     2647   3056   3033   -112     44    -32       N  
ATOM    482  CA  HIS A  87      97.048  78.094  12.781  1.00 23.23           C  
ANISOU  482  CA  HIS A  87     2683   3078   3064    -97     41    -17       C  
ATOM    483  C   HIS A  87      97.850  79.404  12.715  1.00 24.12           C  
ANISOU  483  C   HIS A  87     2801   3191   3174    -80     29     -6       C  
ATOM    484  O   HIS A  87      97.576  80.349  13.484  1.00 23.71           O  
ANISOU  484  O   HIS A  87     2749   3142   3117    -68     23      2       O  
ATOM    485  CB  HIS A  87      97.636  77.129  13.813  1.00 23.72           C  
ANISOU  485  CB  HIS A  87     2757   3115   3139   -100     53    -12       C  
ATOM    486  CG  HIS A  87      96.645  76.127  14.303  1.00 23.35           C  
ANISOU  486  CG  HIS A  87     2706   3068   3097   -114     66    -18       C  
ATOM    487  ND1 HIS A  87      95.502  76.500  14.987  1.00 23.71           N  
ANISOU  487  ND1 HIS A  87     2745   3127   3138   -113     66    -17       N  
ATOM    488  CD2 HIS A  87      96.580  74.784  14.155  1.00 22.98           C  
ANISOU  488  CD2 HIS A  87     2661   3009   3060   -129     81    -27       C  
ATOM    489  CE1 HIS A  87      94.774  75.420  15.232  1.00 23.34           C  
ANISOU  489  CE1 HIS A  87     2694   3077   3097   -128     79    -24       C  
ATOM    490  NE2 HIS A  87      95.406  74.366  14.735  1.00 22.88           N  
ANISOU  490  NE2 HIS A  87     2642   3003   3049   -139     89    -30       N  
ATOM    491  N   LYS A  88      98.800  79.473  11.782  1.00 23.85           N  
ANISOU  491  N   LYS A  88     2770   3152   3139    -79     26     -7       N  
ATOM    492  CA  LYS A  88      99.607  80.683  11.593  1.00 25.44           C  
ANISOU  492  CA  LYS A  88     2975   3353   3337    -64     15      3       C  
ATOM    493  C   LYS A  88      98.737  81.737  10.974  1.00 25.58           C  
ANISOU  493  C   LYS A  88     2982   3393   3344    -58      6      3       C  
ATOM    494  O   LYS A  88      98.704  82.910  11.411  1.00 24.33           O  
ANISOU  494  O   LYS A  88     2824   3236   3183    -44     -1     13       O  
ATOM    495  CB  LYS A  88     100.815  80.353  10.727  1.00 26.51           C  
ANISOU  495  CB  LYS A  88     3116   3478   3477    -66     17      1       C  
ATOM    496  CG  LYS A  88     101.796  81.467  10.440  1.00 29.28           C  
ANISOU  496  CG  LYS A  88     3472   3827   3828    -53      8     11       C  
ATOM    497  CD  LYS A  88     102.890  80.928   9.505  1.00 31.17           C  
ANISOU  497  CD  LYS A  88     3715   4057   4072    -58     13      8       C  
ATOM    498  CE  LYS A  88     103.981  81.971   9.331  1.00 36.63           C  
ANISOU  498  CE  LYS A  88     4410   4742   4764    -46      6     19       C  
ATOM    499  NZ  LYS A  88     105.089  81.620   8.408  1.00 40.10           N  
ANISOU  499  NZ  LYS A  88     4852   5174   5209    -48     11     17       N  
ATOM    500  N   ARG A  89      97.995  81.347   9.949  1.00 25.94           N  
ANISOU  500  N   ARG A  89     3017   3457   3382    -69      6     -7       N  
ATOM    501  CA  ARG A  89      97.107  82.335   9.310  1.00 27.74           C  
ANISOU  501  CA  ARG A  89     3232   3710   3599    -62     -3     -5       C  
ATOM    502  C   ARG A  89      96.045  82.850  10.326  1.00 26.27           C  
ANISOU  502  C   ARG A  89     3039   3530   3413    -55     -4      0       C  
ATOM    503  O   ARG A  89      95.744  84.065  10.347  1.00 25.85           O  
ANISOU  503  O   ARG A  89     2981   3484   3356    -40    -11     10       O  
ATOM    504  CB  ARG A  89      96.486  81.744   8.033  1.00 31.43           C  
ANISOU  504  CB  ARG A  89     3688   4198   4056    -77     -4    -17       C  
ATOM    505  CG  ARG A  89      95.384  82.560   7.362  1.00 37.85           C  
ANISOU  505  CG  ARG A  89     4484   5041   4856    -72    -14    -14       C  
ATOM    506  CD  ARG A  89      95.810  83.813   6.616  1.00 42.34           C  
ANISOU  506  CD  ARG A  89     5052   5618   5417    -57    -24     -1       C  
ATOM    507  NE  ARG A  89      97.222  83.835   6.271  1.00 51.96           N  
ANISOU  507  NE  ARG A  89     6285   6818   6638    -55    -22      1       N  
ATOM    508  CZ  ARG A  89      97.777  83.630   5.068  1.00 56.75           C  
ANISOU  508  CZ  ARG A  89     6893   7432   7237    -61    -22     -3       C  
ATOM    509  NH1 ARG A  89      99.091  83.679   4.969  1.00 58.11           N  
ANISOU  509  NH1 ARG A  89     7078   7584   7415    -57    -18      1       N  
ATOM    510  NH2 ARG A  89      97.064  83.385   3.977  1.00 58.90           N  
ANISOU  510  NH2 ARG A  89     7154   7731   7494    -71    -26    -11       N  
ATOM    511  N   ASN A  90      95.496  81.967  11.166  1.00 23.90           N  
ANISOU  511  N   ASN A  90     2739   3224   3118    -65      5     -6       N  
ATOM    512  CA  ASN A  90      94.567  82.423  12.209  1.00 24.29           C  
ANISOU  512  CA  ASN A  90     2783   3277   3168    -58      6     -1       C  
ATOM    513  C   ASN A  90      95.137  83.547  13.118  1.00 24.23           C  
ANISOU  513  C   ASN A  90     2786   3257   3163    -40      3     11       C  
ATOM    514  O   ASN A  90      94.434  84.506  13.398  1.00 23.63           O  
ANISOU  514  O   ASN A  90     2704   3191   3085    -28      0     16       O  
ATOM    515  CB  ASN A  90      94.101  81.264  13.090  1.00 24.58           C  
ANISOU  515  CB  ASN A  90     2821   3307   3212    -71     18     -7       C  
ATOM    516  CG  ASN A  90      93.179  80.273  12.366  1.00 24.85           C  
ANISOU  516  CG  ASN A  90     2842   3357   3245    -90     23    -21       C  
ATOM    517  OD1 ASN A  90      92.709  80.517  11.256  1.00 24.38           O  
ANISOU  517  OD1 ASN A  90     2769   3317   3176    -93     16    -26       O  
ATOM    518  ND2 ASN A  90      92.964  79.121  12.997  1.00 24.78           N  
ANISOU  518  ND2 ASN A  90     2836   3337   3243   -103     36    -27       N  
ATOM    519  N   PHE A  91      96.396  83.439  13.575  1.00 23.08           N  
ANISOU  519  N   PHE A  91     2656   3090   3022    -37      3     15       N  
ATOM    520  CA  PHE A  91      96.930  84.481  14.421  1.00 23.30           C  
ANISOU  520  CA  PHE A  91     2694   3108   3052    -23      0     24       C  
ATOM    521  C   PHE A  91      97.071  85.842  13.739  1.00 23.84           C  
ANISOU  521  C   PHE A  91     2758   3181   3117    -10     -9     31       C  
ATOM    522  O   PHE A  91      96.721  86.863  14.348  1.00 24.64           O  
ANISOU  522  O   PHE A  91     2861   3283   3218      2    -10     35       O  
ATOM    523  CB  PHE A  91      98.119  84.047  15.311  1.00 22.63           C  
ANISOU  523  CB  PHE A  91     2624   3002   2972    -24      2     28       C  
ATOM    524  CG  PHE A  91      99.463  83.858  14.644  1.00 22.50           C  
ANISOU  524  CG  PHE A  91     2614   2974   2960    -25     -2     30       C  
ATOM    525  CD1 PHE A  91     100.198  84.948  14.166  1.00 22.49           C  
ANISOU  525  CD1 PHE A  91     2616   2971   2959    -16    -10     36       C  
ATOM    526  CD2 PHE A  91     100.071  82.624  14.675  1.00 21.86           C  
ANISOU  526  CD2 PHE A  91     2538   2882   2885    -35      4     28       C  
ATOM    527  CE1 PHE A  91     101.487  84.759  13.685  1.00 22.79           C  
ANISOU  527  CE1 PHE A  91     2660   2998   3003    -17    -12     38       C  
ATOM    528  CE2 PHE A  91     101.378  82.440  14.204  1.00 22.25           C  
ANISOU  528  CE2 PHE A  91     2594   2920   2941    -35      2     31       C  
ATOM    529  CZ  PHE A  91     102.064  83.518  13.695  1.00 22.48           C  
ANISOU  529  CZ  PHE A  91     2623   2948   2969    -26     -6     36       C  
ATOM    530  N   PHE A  92      97.516  85.848  12.489  1.00 24.32           N  
ANISOU  530  N   PHE A  92     2817   3248   3176    -12    -13     31       N  
ATOM    531  CA  PHE A  92      97.613  87.092  11.680  1.00 24.50           C  
ANISOU  531  CA  PHE A  92     2836   3278   3196      1    -21     38       C  
ATOM    532  C   PHE A  92      96.222  87.734  11.477  1.00 25.23           C  
ANISOU  532  C   PHE A  92     2913   3390   3283      8    -22     41       C  
ATOM    533  O   PHE A  92      96.027  88.977  11.610  1.00 24.22           O  
ANISOU  533  O   PHE A  92     2783   3261   3156     23    -24     50       O  
ATOM    534  CB  PHE A  92      98.275  86.858  10.318  1.00 22.58           C  
ANISOU  534  CB  PHE A  92     2592   3040   2949     -4    -24     38       C  
ATOM    535  CG  PHE A  92      99.766  86.580  10.358  1.00 22.25           C  
ANISOU  535  CG  PHE A  92     2563   2978   2913     -7    -23     39       C  
ATOM    536  CD1 PHE A  92     100.662  87.537  10.809  1.00 22.39           C  
ANISOU  536  CD1 PHE A  92     2589   2980   2937      4    -26     47       C  
ATOM    537  CD2 PHE A  92     100.270  85.412   9.852  1.00 22.20           C  
ANISOU  537  CD2 PHE A  92     2558   2968   2908    -20    -18     31       C  
ATOM    538  CE1 PHE A  92     102.011  87.295  10.796  1.00 23.24           C  
ANISOU  538  CE1 PHE A  92     2707   3073   3052      1    -25     49       C  
ATOM    539  CE2 PHE A  92     101.623  85.161   9.799  1.00 22.72           C  
ANISOU  539  CE2 PHE A  92     2633   3017   2981    -21    -17     33       C  
ATOM    540  CZ  PHE A  92     102.504  86.097  10.316  1.00 23.36           C  
ANISOU  540  CZ  PHE A  92     2723   3085   3068    -10    -21     42       C  
ATOM    541  N   ILE A  93      95.276  86.898  11.128  1.00 26.18           N  
ANISOU  541  N   ILE A  93     3021   3528   3399     -3    -20     34       N  
ATOM    542  CA  ILE A  93      93.899  87.366  10.892  1.00 27.98           C  
ANISOU  542  CA  ILE A  93     3231   3778   3623      3    -22     36       C  
ATOM    543  C   ILE A  93      93.231  87.877  12.162  1.00 26.92           C  
ANISOU  543  C   ILE A  93     3097   3639   3494     12    -16     39       C  
ATOM    544  O   ILE A  93      92.514  88.871  12.088  1.00 29.01           O  
ANISOU  544  O   ILE A  93     3352   3913   3758     26    -18     47       O  
ATOM    545  CB  ILE A  93      93.030  86.275  10.226  1.00 29.21           C  
ANISOU  545  CB  ILE A  93     3372   3956   3772    -14    -22     25       C  
ATOM    546  CG1 ILE A  93      93.553  85.949   8.844  1.00 32.16           C  
ANISOU  546  CG1 ILE A  93     3744   4338   4136    -22    -28     22       C  
ATOM    547  CG2 ILE A  93      91.553  86.692  10.168  1.00 30.08           C  
ANISOU  547  CG2 ILE A  93     3460   4089   3878     -9    -24     28       C  
ATOM    548  CD1 ILE A  93      93.409  87.041   7.772  1.00 33.67           C  
ANISOU  548  CD1 ILE A  93     3926   4547   4319     -9    -38     34       C  
ATOM    549  N   LEU A  94      93.448  87.235  13.322  1.00 26.25           N  
ANISOU  549  N   LEU A  94     3023   3538   3413      6     -9     33       N  
ATOM    550  CA  LEU A  94      92.837  87.707  14.582  1.00 25.91           C  
ANISOU  550  CA  LEU A  94     2981   3491   3374     14     -2     35       C  
ATOM    551  C   LEU A  94      93.325  89.102  14.925  1.00 26.42           C  
ANISOU  551  C   LEU A  94     3055   3543   3441     31     -3     43       C  
ATOM    552  O   LEU A  94      92.523  89.949  15.303  1.00 25.87           O  
ANISOU  552  O   LEU A  94     2979   3478   3374     44      1     46       O  
ATOM    553  CB  LEU A  94      93.129  86.794  15.767  1.00 26.82           C  
ANISOU  553  CB  LEU A  94     3109   3592   3491      4      6     29       C  
ATOM    554  CG  LEU A  94      92.283  85.534  15.732  1.00 28.00           C  
ANISOU  554  CG  LEU A  94     3247   3751   3639    -12     13     21       C  
ATOM    555  CD1 LEU A  94      92.870  84.470  16.598  1.00 28.34           C  
ANISOU  555  CD1 LEU A  94     3305   3779   3686    -23     20     18       C  
ATOM    556  CD2 LEU A  94      90.833  85.835  16.143  1.00 29.85           C  
ANISOU  556  CD2 LEU A  94     3466   4001   3874     -8     19     21       C  
ATOM    557  N   GLN A  95      94.640  89.314  14.837  1.00 24.00           N  
ANISOU  557  N   GLN A  95     2762   3219   3136     32     -8     45       N  
ATOM    558  CA  GLN A  95      95.182  90.631  15.077  1.00 24.82           C  
ANISOU  558  CA  GLN A  95     2875   3311   3244     46     -9     51       C  
ATOM    559  C   GLN A  95      94.663  91.688  14.087  1.00 25.53           C  
ANISOU  559  C   GLN A  95     2954   3412   3335     60    -12     60       C  
ATOM    560  O   GLN A  95      94.355  92.793  14.488  1.00 27.73           O  
ANISOU  560  O   GLN A  95     3233   3685   3618     74     -8     65       O  
ATOM    561  CB  GLN A  95      96.709  90.587  15.090  1.00 24.15           C  
ANISOU  561  CB  GLN A  95     2807   3209   3162     42    -14     51       C  
ATOM    562  CG  GLN A  95      97.355  91.925  15.488  1.00 25.99           C  
ANISOU  562  CG  GLN A  95     3050   3426   3400     54    -14     56       C  
ATOM    563  CD  GLN A  95      97.452  92.960  14.359  1.00 26.29           C  
ANISOU  563  CD  GLN A  95     3082   3466   3441     65    -18     65       C  
ATOM    564  OE1 GLN A  95      97.536  92.609  13.155  1.00 28.83           O  
ANISOU  564  OE1 GLN A  95     3396   3798   3759     62    -23     69       O  
ATOM    565  NE2 GLN A  95      97.362  94.222  14.722  1.00 26.76           N  
ANISOU  565  NE2 GLN A  95     3145   3515   3506     78    -14     69       N  
ATOM    566  N   LYS A  96      94.508  91.333  12.816  1.00 27.05           N  
ANISOU  566  N   LYS A  96     3135   3621   3523     56    -19     63       N  
ATOM    567  CA  LYS A  96      93.858  92.226  11.822  1.00 26.54           C  
ANISOU  567  CA  LYS A  96     3056   3571   3456     69    -23     74       C  
ATOM    568  C   LYS A  96      92.363  92.490  12.163  1.00 27.65           C  
ANISOU  568  C   LYS A  96     3180   3728   3598     77    -18     76       C  
ATOM    569  O   LYS A  96      91.936  93.671  12.193  1.00 26.76           O  
ANISOU  569  O   LYS A  96     3063   3614   3491     95    -15     87       O  
ATOM    570  CB  LYS A  96      94.064  91.684  10.425  1.00 27.61           C  
ANISOU  570  CB  LYS A  96     3184   3724   3583     61    -31     76       C  
ATOM    571  CG  LYS A  96      95.487  91.917   9.939  1.00 27.24           C  
ANISOU  571  CG  LYS A  96     3151   3661   3537     60    -34     79       C  
ATOM    572  CD  LYS A  96      95.848  91.139   8.703  1.00 28.59           C  
ANISOU  572  CD  LYS A  96     3318   3846   3698     48    -39     76       C  
ATOM    573  CE  LYS A  96      97.186  91.688   8.197  1.00 29.42           C  
ANISOU  573  CE  LYS A  96     3437   3936   3807     52    -40     83       C  
ATOM    574  NZ  LYS A  96      97.528  91.040   6.930  1.00 31.24           N  
ANISOU  574  NZ  LYS A  96     3663   4180   4027     42    -44     81       N  
ATOM    575  N   ALA A  97      91.616  91.436  12.520  1.00 26.25           N  
ANISOU  575  N   ALA A  97     2994   3562   3417     65    -15     67       N  
ATOM    576  CA  ALA A  97      90.218  91.615  12.926  1.00 27.88           C  
ANISOU  576  CA  ALA A  97     3184   3784   3626     71    -10     68       C  
ATOM    577  C   ALA A  97      90.065  92.556  14.120  1.00 28.97           C  
ANISOU  577  C   ALA A  97     3330   3905   3773     86      1     70       C  
ATOM    578  O   ALA A  97      89.117  93.338  14.199  1.00 30.19           O  
ANISOU  578  O   ALA A  97     3472   4067   3933    101      5     77       O  
ATOM    579  CB  ALA A  97      89.525  90.279  13.184  1.00 28.61           C  
ANISOU  579  CB  ALA A  97     3267   3889   3715     53     -7     56       C  
ATOM    580  N   GLY A  98      91.014  92.516  15.052  1.00 27.86           N  
ANISOU  580  N   GLY A  98     3211   3741   3635     82      5     64       N  
ATOM    581  CA  GLY A  98      90.939  93.347  16.217  1.00 26.01           C  
ANISOU  581  CA  GLY A  98     2987   3490   3405     92     15     62       C  
ATOM    582  C   GLY A  98      91.024  94.828  15.930  1.00 26.05           C  
ANISOU  582  C   GLY A  98     2994   3487   3419    112     17     72       C  
ATOM    583  O   GLY A  98      90.238  95.621  16.497  1.00 26.08           O  
ANISOU  583  O   GLY A  98     2992   3488   3429    126     27     74       O  
ATOM    584  N   VAL A  99      91.997  95.226  15.123  1.00 25.56           N  
ANISOU  584  N   VAL A  99     2938   3417   3358    114      9     78       N  
ATOM    585  CA  VAL A  99      92.109  96.648  14.759  1.00 26.52           C  
ANISOU  585  CA  VAL A  99     3060   3528   3487    132     11     90       C  
ATOM    586  C   VAL A  99      90.949  97.097  13.842  1.00 26.99           C  
ANISOU  586  C   VAL A  99     3096   3609   3549    147     10    104       C  
ATOM    587  O   VAL A  99      90.511  98.273  13.940  1.00 26.45           O  
ANISOU  587  O   VAL A  99     3025   3534   3492    166     18    113       O  
ATOM    588  CB  VAL A  99      93.501  97.055  14.183  1.00 27.20           C  
ANISOU  588  CB  VAL A  99     3161   3599   3576    131      5     94       C  
ATOM    589  CG1 VAL A  99      94.597  96.725  15.190  1.00 27.88           C  
ANISOU  589  CG1 VAL A  99     3268   3665   3661    118      6     81       C  
ATOM    590  CG2 VAL A  99      93.807  96.343  12.868  1.00 26.57           C  
ANISOU  590  CG2 VAL A  99     3072   3535   3487    122     -7     99       C  
ATOM    591  N   LEU A 100      90.428  96.196  13.003  1.00 27.17           N  
ANISOU  591  N   LEU A 100     3103   3658   3563    138      1    105       N  
ATOM    592  CA  LEU A 100      89.274  96.515  12.166  1.00 28.97           C  
ANISOU  592  CA  LEU A 100     3306   3911   3790    150     -2    119       C  
ATOM    593  C   LEU A 100      88.055  96.794  13.017  1.00 30.81           C  
ANISOU  593  C   LEU A 100     3526   4148   4031    161     10    118       C  
ATOM    594  O   LEU A 100      87.363  97.809  12.774  1.00 30.18           O  
ANISOU  594  O   LEU A 100     3435   4073   3960    182     14    132       O  
ATOM    595  CB  LEU A 100      88.958  95.456  11.092  1.00 29.86           C  
ANISOU  595  CB  LEU A 100     3403   4054   3890    136    -15    118       C  
ATOM    596  CG  LEU A 100      89.998  95.294   9.975  1.00 30.85           C  
ANISOU  596  CG  LEU A 100     3535   4180   4005    129    -25    122       C  
ATOM    597  CD1 LEU A 100      89.681  94.088   9.068  1.00 30.74           C  
ANISOU  597  CD1 LEU A 100     3508   4194   3977    110    -36    115       C  
ATOM    598  CD2 LEU A 100      90.253  96.571   9.160  1.00 31.37           C  
ANISOU  598  CD2 LEU A 100     3600   4243   4075    149    -27    142       C  
ATOM    599  N   TYR A 101      87.823  95.947  14.041  1.00 30.82           N  
ANISOU  599  N   TYR A 101     3533   4148   4031    147     16    102       N  
ATOM    600  CA  TYR A 101      86.733  96.147  14.974  1.00 30.85           C  
ANISOU  600  CA  TYR A 101     3527   4154   4041    155     29    100       C  
ATOM    601  C   TYR A 101      86.760  97.545  15.591  1.00 32.41           C  
ANISOU  601  C   TYR A 101     3734   4329   4252    176     42    105       C  
ATOM    602  O   TYR A 101      85.766  98.275  15.540  1.00 30.56           O  
ANISOU  602  O   TYR A 101     3483   4102   4026    195     50    115       O  
ATOM    603  CB  TYR A 101      86.735  95.088  16.072  1.00 30.96           C  
ANISOU  603  CB  TYR A 101     3551   4164   4050    137     36     83       C  
ATOM    604  CG  TYR A 101      85.766  95.378  17.202  1.00 31.47           C  
ANISOU  604  CG  TYR A 101     3610   4226   4121    145     53     79       C  
ATOM    605  CD1 TYR A 101      84.400  95.721  16.939  1.00 31.53           C  
ANISOU  605  CD1 TYR A 101     3591   4254   4136    158     58     87       C  
ATOM    606  CD2 TYR A 101      86.204  95.369  18.532  1.00 31.20           C  
ANISOU  606  CD2 TYR A 101     3598   4171   4087    141     64     67       C  
ATOM    607  CE1 TYR A 101      83.532  96.032  17.977  1.00 30.77           C  
ANISOU  607  CE1 TYR A 101     3491   4155   4047    167     75     84       C  
ATOM    608  CE2 TYR A 101      85.347  95.668  19.580  1.00 31.53           C  
ANISOU  608  CE2 TYR A 101     3636   4209   4132    148     81     62       C  
ATOM    609  CZ  TYR A 101      84.020  96.016  19.302  1.00 31.83           C  
ANISOU  609  CZ  TYR A 101     3648   4265   4179    162     88     71       C  
ATOM    610  OH  TYR A 101      83.200  96.301  20.350  1.00 31.96           O  
ANISOU  610  OH  TYR A 101     3664   4280   4202    169    106     66       O  
ATOM    611  N   GLN A 102      87.903  97.902  16.167  1.00 31.10           N  
ANISOU  611  N   GLN A 102     3594   4136   4087    173     45     98       N  
ATOM    612  CA  GLN A 102      88.099  99.187  16.789  1.00 31.52           C  
ANISOU  612  CA  GLN A 102     3660   4164   4152    190     58     98       C  
ATOM    613  C   GLN A 102      87.995 100.350  15.798  1.00 32.78           C  
ANISOU  613  C   GLN A 102     3810   4322   4322    211     58    118       C  
ATOM    614  O   GLN A 102      87.299 101.339  16.068  1.00 34.79           O  
ANISOU  614  O   GLN A 102     4060   4570   4590    231     71    124       O  
ATOM    615  CB  GLN A 102      89.450  99.206  17.509  1.00 31.37           C  
ANISOU  615  CB  GLN A 102     3670   4121   4130    178     58     86       C  
ATOM    616  CG  GLN A 102      89.434  98.317  18.777  1.00 31.86           C  
ANISOU  616  CG  GLN A 102     3742   4181   4183    162     64     69       C  
ATOM    617  CD  GLN A 102      88.557  98.907  19.894  1.00 32.66           C  
ANISOU  617  CD  GLN A 102     3844   4276   4290    173     83     62       C  
ATOM    618  OE1 GLN A 102      88.444 100.125  20.005  1.00 32.83           O  
ANISOU  618  OE1 GLN A 102     3868   4282   4323    189     93     65       O  
ATOM    619  NE2 GLN A 102      87.958  98.034  20.755  1.00 31.23           N  
ANISOU  619  NE2 GLN A 102     3660   4104   4101    163     89     53       N  
ATOM    620  N   ILE A 103      88.642 100.243  14.646  1.00 32.33           N  
ANISOU  620  N   ILE A 103     3753   4272   4260    207     43    128       N  
ATOM    621  CA  ILE A 103      88.708 101.381  13.736  1.00 33.84           C  
ANISOU  621  CA  ILE A 103     3938   4458   4460    227     43    147       C  
ATOM    622  C   ILE A 103      87.324 101.609  13.107  1.00 36.35           C  
ANISOU  622  C   ILE A 103     4227   4802   4782    244     43    164       C  
ATOM    623  O   ILE A 103      86.827 102.723  13.148  1.00 35.18           O  
ANISOU  623  O   ILE A 103     4073   4645   4648    267     55    177       O  
ATOM    624  CB  ILE A 103      89.834 101.257  12.689  1.00 33.75           C  
ANISOU  624  CB  ILE A 103     3935   4447   4442    219     30    154       C  
ATOM    625  CG1 ILE A 103      91.201 101.389  13.397  1.00 33.94           C  
ANISOU  625  CG1 ILE A 103     3987   4440   4468    207     33    140       C  
ATOM    626  CG2 ILE A 103      89.735 102.345  11.626  1.00 33.09           C  
ANISOU  626  CG2 ILE A 103     3843   4364   4367    240     29    178       C  
ATOM    627  CD1 ILE A 103      92.359 100.968  12.536  1.00 34.43           C  
ANISOU  627  CD1 ILE A 103     4056   4502   4522    195     20    142       C  
ATOM    628  N   LEU A 104      86.737 100.547  12.545  1.00 35.82           N  
ANISOU  628  N   LEU A 104     4141   4767   4701    233     31    164       N  
ATOM    629  CA  LEU A 104      85.463 100.629  11.854  1.00 36.27           C  
ANISOU  629  CA  LEU A 104     4167   4854   4758    245     27    180       C  
ATOM    630  C   LEU A 104      84.258 100.556  12.764  1.00 38.23           C  
ANISOU  630  C   LEU A 104     4402   5110   5016    251     40    175       C  
ATOM    631  O   LEU A 104      83.182 100.768  12.293  1.00 39.81           O  
ANISOU  631  O   LEU A 104     4575   5333   5219    265     39    189       O  
ATOM    632  CB  LEU A 104      85.353  99.529  10.795  1.00 36.24           C  
ANISOU  632  CB  LEU A 104     4148   4884   4736    228      8    181       C  
ATOM    633  CG  LEU A 104      86.443  99.517   9.743  1.00 36.28           C  
ANISOU  633  CG  LEU A 104     4164   4888   4731    222     -5    187       C  
ATOM    634  CD1 LEU A 104      86.234  98.301   8.865  1.00 37.41           C  
ANISOU  634  CD1 LEU A 104     4293   5064   4855    202    -21    182       C  
ATOM    635  CD2 LEU A 104      86.404 100.814   8.904  1.00 37.71           C  
ANISOU  635  CD2 LEU A 104     4339   5068   4920    248     -4    213       C  
ATOM    636  N   ASN A 105      84.430 100.228  14.047  1.00 38.96           N  
ANISOU  636  N   ASN A 105     4511   5184   5110    241     52    155       N  
ATOM    637  CA  ASN A 105      83.329 100.087  14.965  1.00 40.31           C  
ANISOU  637  CA  ASN A 105     4668   5360   5286    245     66    148       C  
ATOM    638  C   ASN A 105      82.303  99.101  14.434  1.00 40.83           C  
ANISOU  638  C   ASN A 105     4705   5464   5344    236     56    150       C  
ATOM    639  O   ASN A 105      81.132  99.418  14.357  1.00 39.72           O  
ANISOU  639  O   ASN A 105     4540   5341   5212    250     61    160       O  
ATOM    640  CB  ASN A 105      82.680 101.469  15.231  1.00 43.23           C  
ANISOU  640  CB  ASN A 105     5032   5718   5677    275     83    161       C  
ATOM    641  CG  ASN A 105      81.735 101.472  16.410  1.00 45.08           C  
ANISOU  641  CG  ASN A 105     5261   5950   5919    280    102    151       C  
ATOM    642  OD1 ASN A 105      81.757 100.600  17.268  1.00 47.20           O  
ANISOU  642  OD1 ASN A 105     5537   6217   6178    261    106    133       O  
ATOM    643  ND2 ASN A 105      80.890 102.482  16.465  1.00 49.32           N  
ANISOU  643  ND2 ASN A 105     5783   6484   6474    306    117    164       N  
ATOM    644  N   ASP A 106      82.750  97.919  14.030  1.00 39.11           N  
ANISOU  644  N   ASP A 106     4491   5259   5111    211     41    140       N  
ATOM    645  CA  ASP A 106      81.876  96.978  13.334  1.00 38.19           C  
ANISOU  645  CA  ASP A 106     4346   5178   4985    199     30    141       C  
ATOM    646  C   ASP A 106      82.030  95.612  13.995  1.00 38.18           C  
ANISOU  646  C   ASP A 106     4354   5177   4976    171     31    120       C  
ATOM    647  O   ASP A 106      83.078  94.948  13.893  1.00 35.79           O  
ANISOU  647  O   ASP A 106     4072   4864   4665    154     24    110       O  
ATOM    648  CB  ASP A 106      82.195  96.946  11.843  1.00 39.55           C  
ANISOU  648  CB  ASP A 106     4510   5371   5148    198     10    154       C  
ATOM    649  CG  ASP A 106      81.256  96.023  11.059  1.00 40.77           C  
ANISOU  649  CG  ASP A 106     4634   5566   5291    184     -3    153       C  
ATOM    650  OD1 ASP A 106      80.465  95.247  11.640  1.00 43.47           O  
ANISOU  650  OD1 ASP A 106     4964   5919   5634    172      2    142       O  
ATOM    651  OD2 ASP A 106      81.330  96.050   9.842  1.00 44.15           O  
ANISOU  651  OD2 ASP A 106     5051   6015   5709    184    -19    164       O  
ATOM    652  N   GLU A 107      80.965  95.218  14.682  1.00 38.37           N  
ANISOU  652  N   GLU A 107     4363   5212   5005    169     41    114       N  
ATOM    653  CA  GLU A 107      80.942  94.021  15.528  1.00 40.48           C  
ANISOU  653  CA  GLU A 107     4637   5476   5267    145     48     96       C  
ATOM    654  C   GLU A 107      81.071  92.691  14.825  1.00 36.97           C  
ANISOU  654  C   GLU A 107     4186   5050   4810    119     34     87       C  
ATOM    655  O   GLU A 107      81.292  91.698  15.492  1.00 36.65           O  
ANISOU  655  O   GLU A 107     4158   5001   4767    100     40     73       O  
ATOM    656  CB  GLU A 107      79.665  93.961  16.358  1.00 43.59           C  
ANISOU  656  CB  GLU A 107     5013   5880   5670    150     63     94       C  
ATOM    657  CG  GLU A 107      79.524  95.118  17.324  1.00 47.89           C  
ANISOU  657  CG  GLU A 107     5567   6403   6227    173     82     97       C  
ATOM    658  CD  GLU A 107      78.500  94.836  18.432  1.00 52.58           C  
ANISOU  658  CD  GLU A 107     6151   7000   6827    172    102     90       C  
ATOM    659  OE1 GLU A 107      77.546  94.048  18.181  1.00 49.34           O  
ANISOU  659  OE1 GLU A 107     5714   6616   6416    161    100     89       O  
ATOM    660  OE2 GLU A 107      78.694  95.387  19.551  1.00 49.94           O  
ANISOU  660  OE2 GLU A 107     5837   6642   6498    180    119     84       O  
ATOM    661  N   LYS A 108      80.906  92.669  13.510  1.00 35.71           N  
ANISOU  661  N   LYS A 108     4009   4915   4645    118     18     95       N  
ATOM    662  CA  LYS A 108      81.244  91.491  12.708  1.00 37.37           C  
ANISOU  662  CA  LYS A 108     4218   5139   4842     93      5     85       C  
ATOM    663  C   LYS A 108      82.701  90.990  13.021  1.00 35.08           C  
ANISOU  663  C   LYS A 108     3962   4820   4547     80      5     74       C  
ATOM    664  O   LYS A 108      82.939  89.783  13.128  1.00 34.01           O  
ANISOU  664  O   LYS A 108     3832   4683   4406     56      5     60       O  
ATOM    665  CB  LYS A 108      80.950  91.822  11.229  1.00 40.13           C  
ANISOU  665  CB  LYS A 108     4546   5518   5183     98    -13     98       C  
ATOM    666  CG  LYS A 108      81.708  91.172  10.085  1.00 45.74           C  
ANISOU  666  CG  LYS A 108     5262   6238   5878     81    -29     93       C  
ATOM    667  CD  LYS A 108      81.345  91.909   8.771  1.00 50.77           C  
ANISOU  667  CD  LYS A 108     5879   6905   6508     95    -44    111       C  
ATOM    668  CE  LYS A 108      82.284  91.648   7.586  1.00 53.24           C  
ANISOU  668  CE  LYS A 108     6201   7222   6804     85    -58    111       C  
ATOM    669  NZ  LYS A 108      82.242  90.237   7.065  1.00 54.80           N  
ANISOU  669  NZ  LYS A 108     6395   7438   6989     53    -65     91       N  
ATOM    670  N   TYR A 109      83.644  91.928  13.187  1.00 32.22           N  
ANISOU  670  N   TYR A 109     3621   4434   4188     95      6     81       N  
ATOM    671  CA  TYR A 109      85.048  91.596  13.455  1.00 30.27           C  
ANISOU  671  CA  TYR A 109     3404   4161   3937     85      6     73       C  
ATOM    672  C   TYR A 109      85.215  91.042  14.850  1.00 29.11           C  
ANISOU  672  C   TYR A 109     3272   3993   3793     76     19     62       C  
ATOM    673  O   TYR A 109      85.930  90.059  15.053  1.00 28.52           O  
ANISOU  673  O   TYR A 109     3212   3909   3714     58     19     51       O  
ATOM    674  CB  TYR A 109      85.948  92.825  13.182  1.00 29.08           C  
ANISOU  674  CB  TYR A 109     3268   3993   3790    104      3     85       C  
ATOM    675  CG  TYR A 109      85.810  93.203  11.753  1.00 29.08           C  
ANISOU  675  CG  TYR A 109     3252   4013   3783    110    -10     98       C  
ATOM    676  CD1 TYR A 109      86.227  92.321  10.738  1.00 28.90           C  
ANISOU  676  CD1 TYR A 109     3227   4005   3748     92    -23     93       C  
ATOM    677  CD2 TYR A 109      85.164  94.361  11.394  1.00 29.70           C  
ANISOU  677  CD2 TYR A 109     3315   4100   3868    134    -10    115       C  
ATOM    678  CE1 TYR A 109      86.040  92.616   9.421  1.00 28.58           C  
ANISOU  678  CE1 TYR A 109     3172   3988   3700     97    -35    104       C  
ATOM    679  CE2 TYR A 109      84.959  94.684  10.070  1.00 30.67           C  
ANISOU  679  CE2 TYR A 109     3422   4246   3983    140    -23    129       C  
ATOM    680  CZ  TYR A 109      85.400  93.816   9.083  1.00 30.31           C  
ANISOU  680  CZ  TYR A 109     3376   4217   3924    121    -36    124       C  
ATOM    681  OH  TYR A 109      85.177  94.167   7.776  1.00 30.06           O  
ANISOU  681  OH  TYR A 109     3328   4210   3881    128    -49    138       O  
ATOM    682  N   ALA A 110      84.523  91.655  15.811  1.00 30.69           N  
ANISOU  682  N   ALA A 110     3471   4190   4002     89     32     63       N  
ATOM    683  CA  ALA A 110      84.557  91.213  17.227  1.00 31.38           C  
ANISOU  683  CA  ALA A 110     3573   4261   4091     82     47     53       C  
ATOM    684  C   ALA A 110      83.938  89.828  17.402  1.00 32.78           C  
ANISOU  684  C   ALA A 110     3740   4451   4265     61     50     44       C  
ATOM    685  O   ALA A 110      84.439  89.006  18.157  1.00 30.75           O  
ANISOU  685  O   ALA A 110     3499   4180   4005     47     56     35       O  
ATOM    686  CB  ALA A 110      83.859  92.206  18.140  1.00 31.66           C  
ANISOU  686  CB  ALA A 110     3605   4290   4134    101     62     56       C  
ATOM    687  N   LEU A 111      82.849  89.593  16.696  1.00 32.63           N  
ANISOU  687  N   LEU A 111     3692   4459   4247     58     47     46       N  
ATOM    688  CA  LEU A 111      82.141  88.302  16.772  1.00 33.61           C  
ANISOU  688  CA  LEU A 111     3803   4597   4370     36     50     36       C  
ATOM    689  C   LEU A 111      83.017  87.205  16.195  1.00 31.57           C  
ANISOU  689  C   LEU A 111     3556   4335   4105     15     42     27       C  
ATOM    690  O   LEU A 111      83.072  86.143  16.742  1.00 30.15           O  
ANISOU  690  O   LEU A 111     3384   4148   3925     -3     50     18       O  
ATOM    691  CB  LEU A 111      80.800  88.385  16.047  1.00 34.12           C  
ANISOU  691  CB  LEU A 111     3832   4694   4437     38     46     40       C  
ATOM    692  CG  LEU A 111      79.871  87.145  15.938  1.00 37.86           C  
ANISOU  692  CG  LEU A 111     4285   5188   4911     14     49     30       C  
ATOM    693  CD1 LEU A 111      79.568  86.474  17.271  1.00 37.18           C  
ANISOU  693  CD1 LEU A 111     4207   5088   4830      5     68     22       C  
ATOM    694  CD2 LEU A 111      78.553  87.575  15.288  1.00 37.30           C  
ANISOU  694  CD2 LEU A 111     4178   5151   4844     22     44     37       C  
ATOM    695  N   TYR A 112      83.723  87.477  15.103  1.00 30.91           N  
ANISOU  695  N   TYR A 112     3475   4254   4015     17     27     31       N  
ATOM    696  CA  TYR A 112      84.674  86.518  14.553  1.00 30.72           C  
ANISOU  696  CA  TYR A 112     3464   4223   3986     -2     21     23       C  
ATOM    697  C   TYR A 112      85.793  86.192  15.552  1.00 28.44           C  
ANISOU  697  C   TYR A 112     3205   3903   3698     -5     28     19       C  
ATOM    698  O   TYR A 112      86.144  85.036  15.734  1.00 26.16           O  
ANISOU  698  O   TYR A 112     2925   3606   3410    -23     33     11       O  
ATOM    699  CB  TYR A 112      85.288  87.055  13.249  1.00 31.87           C  
ANISOU  699  CB  TYR A 112     3609   4375   4124      4      5     29       C  
ATOM    700  CG  TYR A 112      86.137  86.065  12.515  1.00 31.97           C  
ANISOU  700  CG  TYR A 112     3631   4384   4130    -15     -1     19       C  
ATOM    701  CD1 TYR A 112      85.559  85.009  11.844  1.00 34.85           C  
ANISOU  701  CD1 TYR A 112     3981   4769   4491    -36     -3      8       C  
ATOM    702  CD2 TYR A 112      87.508  86.149  12.509  1.00 34.38           C  
ANISOU  702  CD2 TYR A 112     3960   4667   4435    -13     -3     20       C  
ATOM    703  CE1 TYR A 112      86.330  84.090  11.135  1.00 35.49           C  
ANISOU  703  CE1 TYR A 112     4071   4846   4567    -54     -6     -3       C  
ATOM    704  CE2 TYR A 112      88.278  85.222  11.796  1.00 35.75           C  
ANISOU  704  CE2 TYR A 112     4141   4837   4603    -30     -6     11       C  
ATOM    705  CZ  TYR A 112      87.652  84.212  11.106  1.00 34.42           C  
ANISOU  705  CZ  TYR A 112     3958   4687   4431    -50     -7      0       C  
ATOM    706  OH  TYR A 112      88.340  83.275  10.401  1.00 42.75           O  
ANISOU  706  OH  TYR A 112     5022   5740   5483    -67     -8    -11       O  
ATOM    707  N   ILE A 113      86.358  87.227  16.187  1.00 28.39           N  
ANISOU  707  N   ILE A 113     3213   3879   3693     13     30     27       N  
ATOM    708  CA  ILE A 113      87.407  86.994  17.209  1.00 28.07           C  
ANISOU  708  CA  ILE A 113     3200   3813   3654     11     36     24       C  
ATOM    709  C   ILE A 113      86.857  86.135  18.358  1.00 28.37           C  
ANISOU  709  C   ILE A 113     3240   3847   3693      0     51     19       C  
ATOM    710  O   ILE A 113      87.479  85.160  18.789  1.00 25.53           O  
ANISOU  710  O   ILE A 113     2894   3475   3332    -13     54     14       O  
ATOM    711  CB  ILE A 113      88.006  88.323  17.744  1.00 28.55           C  
ANISOU  711  CB  ILE A 113     3275   3857   3715     30     36     31       C  
ATOM    712  CG1 ILE A 113      88.757  89.032  16.626  1.00 28.77           C  
ANISOU  712  CG1 ILE A 113     3305   3885   3743     39     23     38       C  
ATOM    713  CG2 ILE A 113      88.955  88.083  18.919  1.00 28.03           C  
ANISOU  713  CG2 ILE A 113     3234   3768   3647     27     42     28       C  
ATOM    714  CD1 ILE A 113      89.072  90.475  16.967  1.00 29.19           C  
ANISOU  714  CD1 ILE A 113     3367   3925   3800     59     25     45       C  
ATOM    715  N   LYS A 114      85.675  86.498  18.856  1.00 27.69           N  
ANISOU  715  N   LYS A 114     3139   3772   3610      7     60     20       N  
ATOM    716  CA  LYS A 114      85.059  85.727  19.926  1.00 29.60           C  
ANISOU  716  CA  LYS A 114     3382   4012   3853     -3     75     15       C  
ATOM    717  C   LYS A 114      84.846  84.271  19.577  1.00 28.49           C  
ANISOU  717  C   LYS A 114     3234   3877   3713    -27     77      8       C  
ATOM    718  O   LYS A 114      85.236  83.407  20.329  1.00 27.11           O  
ANISOU  718  O   LYS A 114     3073   3688   3538    -38     86      5       O  
ATOM    719  CB  LYS A 114      83.740  86.354  20.358  1.00 33.38           C  
ANISOU  719  CB  LYS A 114     3841   4504   4335      7     85     17       C  
ATOM    720  CG  LYS A 114      83.088  85.581  21.492  1.00 37.30           C  
ANISOU  720  CG  LYS A 114     4339   5000   4834     -3    103     13       C  
ATOM    721  CD  LYS A 114      82.050  86.394  22.229  1.00 42.81           C  
ANISOU  721  CD  LYS A 114     5026   5704   5535     12    117     15       C  
ATOM    722  CE  LYS A 114      80.641  86.056  21.825  1.00 48.35           C  
ANISOU  722  CE  LYS A 114     5696   6431   6244      6    122     14       C  
ATOM    723  NZ  LYS A 114      80.243  86.867  20.634  1.00 52.66           N  
ANISOU  723  NZ  LYS A 114     6220   6994   6793     18    108     20       N  
ATOM    724  N   ASP A 115      84.200  84.004  18.438  1.00 27.92           N  
ANISOU  724  N   ASP A 115     3140   3826   3643    -34     70      4       N  
ATOM    725  CA  ASP A 115      83.968  82.665  17.971  1.00 27.77           C  
ANISOU  725  CA  ASP A 115     3113   3813   3626    -58     71     -5       C  
ATOM    726  C   ASP A 115      85.268  81.847  17.762  1.00 26.78           C  
ANISOU  726  C   ASP A 115     3009   3667   3498    -70     69     -9       C  
ATOM    727  O   ASP A 115      85.320  80.663  18.086  1.00 25.30           O  
ANISOU  727  O   ASP A 115     2827   3470   3315    -87     78    -15       O  
ATOM    728  CB  ASP A 115      83.142  82.695  16.683  1.00 29.97           C  
ANISOU  728  CB  ASP A 115     3364   4120   3903    -64     61     -9       C  
ATOM    729  CG  ASP A 115      81.641  83.132  16.921  1.00 33.00           C  
ANISOU  729  CG  ASP A 115     3721   4527   4292    -58     66     -6       C  
ATOM    730  OD1 ASP A 115      81.175  83.192  18.059  1.00 33.59           O  
ANISOU  730  OD1 ASP A 115     3798   4595   4371    -54     81     -4       O  
ATOM    731  OD2 ASP A 115      80.971  83.483  15.941  1.00 37.08           O  
ANISOU  731  OD2 ASP A 115     4214   5070   4807    -56     55     -5       O  
ATOM    732  N   MET A 116      86.285  82.480  17.222  1.00 24.74           N  
ANISOU  732  N   MET A 116     2763   3402   3237    -59     57     -5       N  
ATOM    733  CA  MET A 116      87.566  81.782  17.013  1.00 25.93           C  
ANISOU  733  CA  MET A 116     2932   3533   3386    -68     54     -7       C  
ATOM    734  C   MET A 116      88.239  81.474  18.335  1.00 24.96           C  
ANISOU  734  C   MET A 116     2830   3386   3265    -66     64     -2       C  
ATOM    735  O   MET A 116      88.674  80.329  18.538  1.00 25.41           O  
ANISOU  735  O   MET A 116     2897   3431   3326    -80     71     -5       O  
ATOM    736  CB  MET A 116      88.503  82.515  16.012  1.00 26.11           C  
ANISOU  736  CB  MET A 116     2960   3556   3405    -58     39     -3       C  
ATOM    737  CG  MET A 116      89.837  81.755  15.791  1.00 26.72           C  
ANISOU  737  CG  MET A 116     3056   3614   3484    -66     38     -6       C  
ATOM    738  SD  MET A 116      90.822  82.408  14.453  1.00 29.77           S  
ANISOU  738  SD  MET A 116     3445   4001   3864    -59     23     -4       S  
ATOM    739  CE  MET A 116      89.964  81.701  13.040  1.00 30.93           C  
ANISOU  739  CE  MET A 116     3571   4175   4007    -77     20    -16       C  
ATOM    740  N   LEU A 117      88.254  82.452  19.252  1.00 25.97           N  
ANISOU  740  N   LEU A 117     2967   3511   3391    -49     66      5       N  
ATOM    741  CA  LEU A 117      88.834  82.247  20.609  1.00 25.88           C  
ANISOU  741  CA  LEU A 117     2975   3480   3377    -48     74     10       C  
ATOM    742  C   LEU A 117      88.157  81.138  21.364  1.00 26.11           C  
ANISOU  742  C   LEU A 117     3002   3508   3409    -61     90      8       C  
ATOM    743  O   LEU A 117      88.825  80.284  21.973  1.00 25.89           O  
ANISOU  743  O   LEU A 117     2990   3465   3383    -69     96     11       O  
ATOM    744  CB  LEU A 117      88.871  83.533  21.425  1.00 25.16           C  
ANISOU  744  CB  LEU A 117     2892   3387   3281    -29     74     15       C  
ATOM    745  CG  LEU A 117      89.847  84.593  20.919  1.00 26.54           C  
ANISOU  745  CG  LEU A 117     3074   3555   3454    -16     61     18       C  
ATOM    746  CD1 LEU A 117      89.722  85.835  21.772  1.00 26.85           C  
ANISOU  746  CD1 LEU A 117     3121   3591   3490      0     64     21       C  
ATOM    747  CD2 LEU A 117      91.292  84.114  20.863  1.00 28.00           C  
ANISOU  747  CD2 LEU A 117     3277   3723   3638    -21     54     21       C  
ATOM    748  N   PHE A 118      86.822  81.123  21.315  1.00 26.73           N  
ANISOU  748  N   PHE A 118     3061   3604   3491    -65     97      4       N  
ATOM    749  CA  PHE A 118      86.053  80.015  21.919  1.00 26.33           C  
ANISOU  749  CA  PHE A 118     3006   3554   3445    -81    114      1       C  
ATOM    750  C   PHE A 118      86.248  78.656  21.262  1.00 26.79           C  
ANISOU  750  C   PHE A 118     3062   3606   3510   -102    116     -6       C  
ATOM    751  O   PHE A 118      86.317  77.652  21.941  1.00 28.46           O  
ANISOU  751  O   PHE A 118     3282   3804   3726   -113    130     -4       O  
ATOM    752  CB  PHE A 118      84.593  80.423  22.148  1.00 27.27           C  
ANISOU  752  CB  PHE A 118     3104   3692   3566    -78    122     -1       C  
ATOM    753  CG  PHE A 118      84.423  81.165  23.431  1.00 27.31           C  
ANISOU  753  CG  PHE A 118     3118   3692   3565    -64    131      5       C  
ATOM    754  CD1 PHE A 118      84.654  80.511  24.658  1.00 29.19           C  
ANISOU  754  CD1 PHE A 118     3373   3916   3800    -69    145     10       C  
ATOM    755  CD2 PHE A 118      84.178  82.520  23.437  1.00 28.17           C  
ANISOU  755  CD2 PHE A 118     3223   3809   3672    -45    127      7       C  
ATOM    756  CE1 PHE A 118      84.589  81.214  25.881  1.00 28.92           C  
ANISOU  756  CE1 PHE A 118     3351   3879   3758    -57    154     15       C  
ATOM    757  CE2 PHE A 118      84.122  83.223  24.642  1.00 29.50           C  
ANISOU  757  CE2 PHE A 118     3404   3972   3835    -32    136     11       C  
ATOM    758  CZ  PHE A 118      84.337  82.579  25.855  1.00 28.52           C  
ANISOU  758  CZ  PHE A 118     3295   3836   3704    -39    149     14       C  
ATOM    759  N   GLN A 119      86.441  78.615  19.953  1.00 27.54           N  
ANISOU  759  N   GLN A 119     3148   3709   3606   -107    104    -13       N  
ATOM    760  CA  GLN A 119      86.803  77.379  19.302  1.00 27.77           C  
ANISOU  760  CA  GLN A 119     3180   3730   3643   -126    108    -21       C  
ATOM    761  C   GLN A 119      88.191  76.885  19.719  1.00 27.43           C  
ANISOU  761  C   GLN A 119     3161   3660   3600   -124    109    -14       C  
ATOM    762  O   GLN A 119      88.389  75.710  20.011  1.00 26.01           O  
ANISOU  762  O   GLN A 119     2988   3465   3429   -138    122    -15       O  
ATOM    763  CB  GLN A 119      86.668  77.502  17.778  1.00 28.90           C  
ANISOU  763  CB  GLN A 119     3308   3890   3784   -132     94    -31       C  
ATOM    764  CG  GLN A 119      86.627  76.148  17.103  1.00 30.01           C  
ANISOU  764  CG  GLN A 119     3445   4026   3931   -157    101    -44       C  
ATOM    765  CD  GLN A 119      86.165  76.209  15.647  1.00 31.02           C  
ANISOU  765  CD  GLN A 119     3553   4178   4054   -167     90    -57       C  
ATOM    766  OE1 GLN A 119      85.051  76.642  15.376  1.00 31.89           O  
ANISOU  766  OE1 GLN A 119     3641   4313   4161   -168     86    -60       O  
ATOM    767  NE2 GLN A 119      87.008  75.766  14.713  1.00 30.04           N  
ANISOU  767  NE2 GLN A 119     3438   4048   3930   -175     85    -65       N  
ATOM    768  N   TYR A 120      89.162  77.788  19.780  1.00 26.78           N  
ANISOU  768  N   TYR A 120     3091   3572   3512   -107     97     -6       N  
ATOM    769  CA  TYR A 120      90.454  77.416  20.400  1.00 25.85           C  
ANISOU  769  CA  TYR A 120     2995   3431   3395   -103     99      3       C  
ATOM    770  C   TYR A 120      90.273  76.910  21.818  1.00 25.50           C  
ANISOU  770  C   TYR A 120     2961   3377   3351   -104    113     12       C  
ATOM    771  O   TYR A 120      90.852  75.886  22.197  1.00 25.57           O  
ANISOU  771  O   TYR A 120     2981   3368   3366   -112    121     17       O  
ATOM    772  CB  TYR A 120      91.434  78.621  20.358  1.00 24.64           C  
ANISOU  772  CB  TYR A 120     2852   3276   3235    -85     83     10       C  
ATOM    773  CG  TYR A 120      92.196  78.697  19.099  1.00 23.96           C  
ANISOU  773  CG  TYR A 120     2764   3188   3150    -86     72      5       C  
ATOM    774  CD1 TYR A 120      93.221  77.757  18.845  1.00 25.72           C  
ANISOU  774  CD1 TYR A 120     2998   3394   3380    -93     75      6       C  
ATOM    775  CD2 TYR A 120      91.993  79.717  18.173  1.00 24.24           C  
ANISOU  775  CD2 TYR A 120     2789   3239   3181    -78     60      2       C  
ATOM    776  CE1 TYR A 120      93.978  77.809  17.693  1.00 24.42           C  
ANISOU  776  CE1 TYR A 120     2833   3228   3217    -94     67      2       C  
ATOM    777  CE2 TYR A 120      92.770  79.802  17.000  1.00 24.20           C  
ANISOU  777  CE2 TYR A 120     2786   3234   3177    -78     51     -1       C  
ATOM    778  CZ  TYR A 120      93.761  78.828  16.786  1.00 24.10           C  
ANISOU  778  CZ  TYR A 120     2783   3204   3170    -87     54     -2       C  
ATOM    779  OH  TYR A 120      94.540  78.855  15.688  1.00 24.02           O  
ANISOU  779  OH  TYR A 120     2775   3193   3160    -88     48     -5       O  
ATOM    780  N   GLU A 121      89.503  77.638  22.629  1.00 26.90           N  
ANISOU  780  N   GLU A 121     3135   3565   3522    -96    116     15       N  
ATOM    781  CA  GLU A 121      89.293  77.268  24.047  1.00 27.41           C  
ANISOU  781  CA  GLU A 121     3210   3622   3583    -96    130     24       C  
ATOM    782  C   GLU A 121      88.724  75.854  24.209  1.00 27.60           C  
ANISOU  782  C   GLU A 121     3229   3639   3617   -115    148     22       C  
ATOM    783  O   GLU A 121      88.941  75.196  25.228  1.00 26.43           O  
ANISOU  783  O   GLU A 121     3095   3480   3469   -117    160     33       O  
ATOM    784  CB  GLU A 121      88.397  78.301  24.752  1.00 29.66           C  
ANISOU  784  CB  GLU A 121     3488   3921   3859    -85    133     24       C  
ATOM    785  CG  GLU A 121      88.157  78.093  26.234  1.00 31.04           C  
ANISOU  785  CG  GLU A 121     3675   4092   4027    -84    148     32       C  
ATOM    786  CD  GLU A 121      87.068  77.043  26.559  1.00 34.40           C  
ANISOU  786  CD  GLU A 121     4090   4520   4460    -99    167     31       C  
ATOM    787  OE1 GLU A 121      86.152  76.772  25.747  1.00 33.90           O  
ANISOU  787  OE1 GLU A 121     4006   4467   4406   -110    170     21       O  
ATOM    788  OE2 GLU A 121      87.149  76.459  27.651  1.00 37.06           O  
ANISOU  788  OE2 GLU A 121     4440   4848   4793   -102    180     41       O  
ATOM    789  N   GLY A 122      87.923  75.442  23.241  1.00 27.12           N  
ANISOU  789  N   GLY A 122     3151   3589   3565   -128    150     10       N  
ATOM    790  CA  GLY A 122      87.305  74.136  23.234  1.00 28.37           C  
ANISOU  790  CA  GLY A 122     3304   3742   3735   -148    167      5       C  
ATOM    791  C   GLY A 122      88.242  73.001  22.893  1.00 28.63           C  
ANISOU  791  C   GLY A 122     3347   3752   3777   -158    172      6       C  
ATOM    792  O   GLY A 122      87.860  71.868  23.088  1.00 30.80           O  
ANISOU  792  O   GLY A 122     3622   4017   4064   -174    189      5       O  
ATOM    793  N   MET A 123      89.396  73.288  22.287  1.00 28.26           N  
ANISOU  793  N   MET A 123     3310   3698   3729   -150    158      7       N  
ATOM    794  CA  MET A 123      90.332  72.244  21.835  1.00 29.78           C  
ANISOU  794  CA  MET A 123     3513   3869   3933   -158    163      7       C  
ATOM    795  C   MET A 123      91.674  72.280  22.559  1.00 29.75           C  
ANISOU  795  C   MET A 123     3529   3848   3927   -144    159     25       C  
ATOM    796  O   MET A 123      92.278  71.199  22.739  1.00 30.36           O  
ANISOU  796  O   MET A 123     3616   3904   4016   -149    171     31       O  
ATOM    797  CB  MET A 123      90.514  72.241  20.291  1.00 30.77           C  
ANISOU  797  CB  MET A 123     3629   4001   4062   -166    153     -9       C  
ATOM    798  CG  MET A 123      90.885  73.560  19.595  1.00 31.69           C  
ANISOU  798  CG  MET A 123     3742   4133   4167   -152    132    -11       C  
ATOM    799  SD  MET A 123      92.673  73.840  19.564  1.00 34.12           S  
ANISOU  799  SD  MET A 123     4068   4422   4474   -136    121      0       S  
ATOM    800  CE  MET A 123      93.080  72.730  18.199  1.00 34.82           C  
ANISOU  800  CE  MET A 123     4155   4501   4575   -154    127    -15       C  
ATOM    801  N   TYR A 124      92.139  73.482  22.956  1.00 28.30           N  
ANISOU  801  N   TYR A 124     3351   3672   3730   -126    144     32       N  
ATOM    802  CA  TYR A 124      93.531  73.666  23.358  1.00 29.57           C  
ANISOU  802  CA  TYR A 124     3528   3821   3888   -113    135     45       C  
ATOM    803  C   TYR A 124      93.933  72.843  24.576  1.00 31.49           C  
ANISOU  803  C   TYR A 124     3784   4047   4132   -112    147     63       C  
ATOM    804  O   TYR A 124      94.917  72.107  24.506  1.00 29.37           O  
ANISOU  804  O   TYR A 124     3525   3762   3874   -111    149     72       O  
ATOM    805  CB  TYR A 124      93.903  75.145  23.548  1.00 29.34           C  
ANISOU  805  CB  TYR A 124     3501   3803   3845    -96    117     48       C  
ATOM    806  CG  TYR A 124      95.333  75.327  24.049  1.00 27.76           C  
ANISOU  806  CG  TYR A 124     3315   3591   3641    -85    108     61       C  
ATOM    807  CD1 TYR A 124      96.394  75.304  23.174  1.00 26.97           C  
ANISOU  807  CD1 TYR A 124     3217   3483   3548    -82     99     60       C  
ATOM    808  CD2 TYR A 124      95.604  75.437  25.421  1.00 28.94           C  
ANISOU  808  CD2 TYR A 124     3476   3738   3780    -77    109     75       C  
ATOM    809  CE1 TYR A 124      97.701  75.433  23.627  1.00 27.33           C  
ANISOU  809  CE1 TYR A 124     3274   3519   3592    -73     90     73       C  
ATOM    810  CE2 TYR A 124      96.920  75.588  25.895  1.00 28.83           C  
ANISOU  810  CE2 TYR A 124     3474   3716   3763    -68     99     88       C  
ATOM    811  CZ  TYR A 124      97.966  75.587  24.990  1.00 27.56           C  
ANISOU  811  CZ  TYR A 124     3313   3547   3610    -65     89     87       C  
ATOM    812  OH  TYR A 124      99.271  75.637  25.464  1.00 27.90           O  
ANISOU  812  OH  TYR A 124     3366   3583   3652    -57     80    101       O  
ATOM    813  N   LYS A 125      93.182  72.981  25.670  1.00 34.75           N  
ANISOU  813  N   LYS A 125     4199   4468   4537   -111    155     69       N  
ATOM    814  CA  LYS A 125      93.362  72.158  26.895  1.00 40.03           C  
ANISOU  814  CA  LYS A 125     4880   5125   5205   -111    169     88       C  
ATOM    815  C   LYS A 125      93.467  70.634  26.710  1.00 38.54           C  
ANISOU  815  C   LYS A 125     4694   4915   5036   -123    187     92       C  
ATOM    816  O   LYS A 125      94.185  70.014  27.448  1.00 38.78           O  
ANISOU  816  O   LYS A 125     4736   4931   5067   -118    192    111       O  
ATOM    817  CB  LYS A 125      92.248  72.422  27.925  1.00 45.71           C  
ANISOU  817  CB  LYS A 125     5598   5856   5913   -112    179     90       C  
ATOM    818  CG  LYS A 125      90.866  72.371  27.277  1.00 53.48           C  
ANISOU  818  CG  LYS A 125     6564   6852   6905   -125    188     73       C  
ATOM    819  CD  LYS A 125      89.713  71.970  28.195  1.00 57.54           C  
ANISOU  819  CD  LYS A 125     7075   7371   7417   -132    208     76       C  
ATOM    820  CE  LYS A 125      88.391  72.254  27.496  1.00 56.93           C  
ANISOU  820  CE  LYS A 125     6976   7309   7344   -142    211     58       C  
ATOM    821  NZ  LYS A 125      88.061  73.697  27.536  1.00 61.43           N  
ANISOU  821  NZ  LYS A 125     7540   7899   7901   -128    198     52       N  
ATOM    822  N   ASP A 126      92.750  70.063  25.756  1.00 35.85           N  
ANISOU  822  N   ASP A 126     4340   4572   4708   -139    196     76       N  
ATOM    823  CA  ASP A 126      92.762  68.626  25.511  1.00 35.87           C  
ANISOU  823  CA  ASP A 126     4345   4553   4731   -153    216     77       C  
ATOM    824  C   ASP A 126      93.852  68.153  24.550  1.00 34.67           C  
ANISOU  824  C   ASP A 126     4196   4384   4592   -153    212     73       C  
ATOM    825  O   ASP A 126      93.999  66.982  24.337  1.00 31.16           O  
ANISOU  825  O   ASP A 126     3755   3918   4166   -163    229     74       O  
ATOM    826  CB  ASP A 126      91.402  68.136  24.998  1.00 39.05           C  
ANISOU  826  CB  ASP A 126     4733   4962   5143   -174    230     59       C  
ATOM    827  CG  ASP A 126      90.285  68.205  26.058  1.00 42.03           C  
ANISOU  827  CG  ASP A 126     5107   5350   5514   -177    242     65       C  
ATOM    828  OD1 ASP A 126      90.586  68.200  27.250  1.00 46.33           O  
ANISOU  828  OD1 ASP A 126     5664   5889   6049   -167    246     85       O  
ATOM    829  OD2 ASP A 126      89.124  68.281  25.690  1.00 39.27           O  
ANISOU  829  OD2 ASP A 126     4741   5013   5165   -189    247     49       O  
ATOM    830  N   LEU A 127      94.590  69.073  23.965  1.00 32.36           N  
ANISOU  830  N   LEU A 127     3903   4100   4292   -142    192     69       N  
ATOM    831  CA  LEU A 127      95.628  68.712  23.044  1.00 32.27           C  
ANISOU  831  CA  LEU A 127     3894   4074   4292   -141    189     66       C  
ATOM    832  C   LEU A 127      96.848  68.107  23.701  1.00 32.10           C  
ANISOU  832  C   LEU A 127     3887   4032   4278   -130    193     88       C  
ATOM    833  O   LEU A 127      97.244  68.497  24.763  1.00 33.45           O  
ANISOU  833  O   LEU A 127     4066   4207   4438   -117    186    107       O  
ATOM    834  CB  LEU A 127      96.108  69.930  22.267  1.00 31.86           C  
ANISOU  834  CB  LEU A 127     3839   4039   4229   -132    166     57       C  
ATOM    835  CG  LEU A 127      95.267  70.620  21.216  1.00 32.39           C  
ANISOU  835  CG  LEU A 127     3891   4126   4289   -139    158     35       C  
ATOM    836  CD1 LEU A 127      95.921  71.903  20.793  1.00 34.54           C  
ANISOU  836  CD1 LEU A 127     4163   4411   4550   -125    136     35       C  
ATOM    837  CD2 LEU A 127      94.989  69.737  20.034  1.00 31.44           C  
ANISOU  837  CD2 LEU A 127     3763   3999   4182   -158    168     17       C  
ATOM    838  N   PRO A 128      97.475  67.167  23.005  1.00 30.79           N  
ANISOU  838  N   PRO A 128     3723   3844   4131   -135    203     86       N  
ATOM    839  CA  PRO A 128      98.707  66.543  23.495  1.00 30.22           C  
ANISOU  839  CA  PRO A 128     3662   3751   4070   -123    208    108       C  
ATOM    840  C   PRO A 128      99.883  67.245  22.820  1.00 32.67           C  
ANISOU  840  C   PRO A 128     3971   4064   4378   -111    189    107       C  
ATOM    841  O   PRO A 128      99.658  67.928  21.820  1.00 32.70           O  
ANISOU  841  O   PRO A 128     3968   4082   4376   -116    179     87       O  
ATOM    842  CB  PRO A 128      98.588  65.104  22.996  1.00 31.32           C  
ANISOU  842  CB  PRO A 128     3802   3863   4234   -137    233    103       C  
ATOM    843  CG  PRO A 128      97.748  65.205  21.770  1.00 31.81           C  
ANISOU  843  CG  PRO A 128     3854   3935   4298   -156    235     71       C  
ATOM    844  CD  PRO A 128      96.768  66.313  22.035  1.00 32.15           C  
ANISOU  844  CD  PRO A 128     3888   4008   4319   -156    220     64       C  
ATOM    845  N   VAL A 129     101.098  67.093  23.344  1.00 30.36           N  
ANISOU  845  N   VAL A 129     3686   3761   4090    -96    185    129       N  
ATOM    846  CA  VAL A 129     102.270  67.734  22.746  1.00 29.23           C  
ANISOU  846  CA  VAL A 129     3542   3619   3946    -85    168    129       C  
ATOM    847  C   VAL A 129     102.261  67.499  21.239  1.00 28.19           C  
ANISOU  847  C   VAL A 129     3404   3482   3826    -96    174    105       C  
ATOM    848  O   VAL A 129     101.921  66.406  20.788  1.00 26.99           O  
ANISOU  848  O   VAL A 129     3252   3312   3691   -108    195     96       O  
ATOM    849  CB  VAL A 129     103.580  67.188  23.339  1.00 32.10           C  
ANISOU  849  CB  VAL A 129     3911   3966   4321    -70    169    155       C  
ATOM    850  CG1 VAL A 129     104.779  67.811  22.640  1.00 31.17           C  
ANISOU  850  CG1 VAL A 129     3790   3850   4204    -60    154    154       C  
ATOM    851  CG2 VAL A 129     103.633  67.448  24.837  1.00 34.15           C  
ANISOU  851  CG2 VAL A 129     4176   4235   4564    -60    162    179       C  
ATOM    852  N   HIS A 130     102.620  68.513  20.455  1.00 27.46           N  
ANISOU  852  N   HIS A 130     3306   3403   3723    -92    157     94       N  
ATOM    853  CA  HIS A 130     102.598  68.334  18.996  1.00 26.76           C  
ANISOU  853  CA  HIS A 130     3213   3313   3643   -103    162     71       C  
ATOM    854  C   HIS A 130     103.256  66.981  18.649  1.00 28.66           C  
ANISOU  854  C   HIS A 130     3458   3524   3908   -106    184     73       C  
ATOM    855  O   HIS A 130     104.329  66.671  19.193  1.00 27.49           O  
ANISOU  855  O   HIS A 130     3315   3361   3771    -92    185     95       O  
ATOM    856  CB  HIS A 130     103.362  69.454  18.308  1.00 26.61           C  
ANISOU  856  CB  HIS A 130     3191   3307   3615    -93    143     67       C  
ATOM    857  CG  HIS A 130     102.986  69.647  16.874  1.00 26.53           C  
ANISOU  857  CG  HIS A 130     3173   3304   3601   -105    143     42       C  
ATOM    858  ND1 HIS A 130     103.502  68.868  15.862  1.00 24.83           N  
ANISOU  858  ND1 HIS A 130     2959   3074   3401   -112    157     31       N  
ATOM    859  CD2 HIS A 130     102.150  70.543  16.281  1.00 25.96           C  
ANISOU  859  CD2 HIS A 130     3094   3256   3513   -111    132     27       C  
ATOM    860  CE1 HIS A 130     102.994  69.263  14.715  1.00 26.44           C  
ANISOU  860  CE1 HIS A 130     3156   3293   3595   -122    153      9       C  
ATOM    861  NE2 HIS A 130     102.192  70.295  14.939  1.00 26.10           N  
ANISOU  861  NE2 HIS A 130     3108   3274   3534   -121    137      8       N  
ATOM    862  N   PRO A 131     102.640  66.193  17.754  1.00 28.54           N  
ANISOU  862  N   PRO A 131     3440   3499   3903   -124    202     52       N  
ATOM    863  CA  PRO A 131     103.215  64.870  17.452  1.00 30.78           C  
ANISOU  863  CA  PRO A 131     3729   3752   4212   -127    226     52       C  
ATOM    864  C   PRO A 131     104.541  64.869  16.683  1.00 29.28           C  
ANISOU  864  C   PRO A 131     3540   3551   4033   -117    225     53       C  
ATOM    865  O   PRO A 131     105.236  63.892  16.754  1.00 29.73           O  
ANISOU  865  O   PRO A 131     3603   3582   4113   -113    243     63       O  
ATOM    866  CB  PRO A 131     102.126  64.155  16.624  1.00 30.57           C  
ANISOU  866  CB  PRO A 131     3700   3723   4191   -152    243     24       C  
ATOM    867  CG  PRO A 131     101.400  65.279  15.999  1.00 32.60           C  
ANISOU  867  CG  PRO A 131     3948   4012   4425   -158    223      6       C  
ATOM    868  CD  PRO A 131     101.457  66.477  16.946  1.00 30.13           C  
ANISOU  868  CD  PRO A 131     3634   3720   4094   -141    200     25       C  
ATOM    869  N   GLN A 132     104.891  65.921  15.961  1.00 28.65           N  
ANISOU  869  N   GLN A 132     3456   3491   3939   -113    207     44       N  
ATOM    870  CA  GLN A 132     106.265  65.996  15.398  1.00 29.72           C  
ANISOU  870  CA  GLN A 132     3591   3615   4084   -101    206     49       C  
ATOM    871  C   GLN A 132     107.308  66.123  16.525  1.00 28.83           C  
ANISOU  871  C   GLN A 132     3481   3496   3978    -80    197     82       C  
ATOM    872  O   GLN A 132     107.147  66.933  17.469  1.00 28.03           O  
ANISOU  872  O   GLN A 132     3379   3412   3860    -72    179     96       O  
ATOM    873  CB  GLN A 132     106.435  67.120  14.387  1.00 29.84           C  
ANISOU  873  CB  GLN A 132     3601   3653   4083   -101    188     35       C  
ATOM    874  CG  GLN A 132     105.520  67.063  13.170  1.00 30.49           C  
ANISOU  874  CG  GLN A 132     3680   3746   4157   -121    194      4       C  
ATOM    875  CD  GLN A 132     105.722  65.821  12.284  1.00 30.20           C  
ANISOU  875  CD  GLN A 132     3648   3687   4140   -134    220    -13       C  
ATOM    876  OE1 GLN A 132     106.609  64.998  12.505  1.00 28.29           O  
ANISOU  876  OE1 GLN A 132     3411   3418   3919   -126    236     -2       O  
ATOM    877  NE2 GLN A 132     104.845  65.679  11.301  1.00 29.20           N  
ANISOU  877  NE2 GLN A 132     3519   3573   4005   -154    225    -41       N  
ATOM    878  N   THR A 133     108.370  65.329  16.428  1.00 28.88           N  
ANISOU  878  N   THR A 133     3489   3478   4006    -71    211     93       N  
ATOM    879  CA  THR A 133     109.433  65.347  17.426  1.00 28.62           C  
ANISOU  879  CA  THR A 133     3456   3439   3980    -51    204    124       C  
ATOM    880  C   THR A 133     110.755  65.798  16.815  1.00 28.48           C  
ANISOU  880  C   THR A 133     3433   3420   3969    -39    196    128       C  
ATOM    881  O   THR A 133     111.647  64.985  16.573  1.00 31.48           O  
ANISOU  881  O   THR A 133     3812   3777   4372    -32    212    136       O  
ATOM    882  CB  THR A 133     109.623  63.962  18.073  1.00 29.27           C  
ANISOU  882  CB  THR A 133     3543   3492   4087    -47    227    143       C  
ATOM    883  OG1 THR A 133     110.205  63.063  17.121  1.00 29.78           O  
ANISOU  883  OG1 THR A 133     3608   3530   4176    -49    251    133       O  
ATOM    884  CG2 THR A 133     108.287  63.405  18.540  1.00 30.48           C  
ANISOU  884  CG2 THR A 133     3701   3642   4236    -62    240    137       C  
ATOM    885  N   ARG A 134     110.874  67.099  16.568  1.00 28.82           N  
ANISOU  885  N   ARG A 134     3471   3487   3992    -37    173    122       N  
ATOM    886  CA  ARG A 134     112.087  67.660  15.985  1.00 30.68           C  
ANISOU  886  CA  ARG A 134     3700   3724   4231    -27    164    125       C  
ATOM    887  C   ARG A 134     112.319  69.089  16.465  1.00 29.80           C  
ANISOU  887  C   ARG A 134     3585   3638   4100    -20    135    133       C  
ATOM    888  O   ARG A 134     112.911  69.903  15.757  1.00 29.44           O  
ANISOU  888  O   ARG A 134     3534   3601   4050    -18    125    127       O  
ATOM    889  CB  ARG A 134     112.014  67.624  14.458  1.00 32.74           C  
ANISOU  889  CB  ARG A 134     3961   3984   4495    -38    175     98       C  
ATOM    890  CG  ARG A 134     113.332  67.928  13.765  1.00 34.00           C  
ANISOU  890  CG  ARG A 134     4115   4139   4664    -28    174    102       C  
ATOM    891  CD  ARG A 134     113.137  68.886  12.601  1.00 37.78           C  
ANISOU  891  CD  ARG A 134     4591   4636   5126    -36    165     80       C  
ATOM    892  NE  ARG A 134     114.289  69.763  12.415  1.00 42.19           N  
ANISOU  892  NE  ARG A 134     5144   5202   5686    -24    152     90       N  
ATOM    893  CZ  ARG A 134     115.082  69.739  11.349  1.00 40.19           C  
ANISOU  893  CZ  ARG A 134     4887   4943   5441    -23    161     82       C  
ATOM    894  NH1 ARG A 134     114.849  68.880  10.366  1.00 43.06           N  
ANISOU  894  NH1 ARG A 134     5255   5294   5813    -34    185     63       N  
ATOM    895  NH2 ARG A 134     116.108  70.575  11.264  1.00 42.44           N  
ANISOU  895  NH2 ARG A 134     5165   5234   5726    -13    149     93       N  
ATOM    896  N   SER A 135     111.914  69.275  17.676  1.00 26.50           N  
ANISOU  896  N   SER A 135     3169   3228   3671    -17    125    147       N  
ATOM    897  CA  SER A 135     112.150  70.498  18.303  1.00 26.37           C  
ANISOU  897  CA  SER A 135     3150   3232   3636    -10    100    155       C  
ATOM    898  C   SER A 135     112.592  70.115  19.699  1.00 27.08           C  
ANISOU  898  C   SER A 135     3241   3320   3728      1     95    183       C  
ATOM    899  O   SER A 135     112.089  69.186  20.273  1.00 26.93           O  
ANISOU  899  O   SER A 135     3227   3290   3715     -1    108    191       O  
ATOM    900  CB  SER A 135     110.900  71.331  18.332  1.00 25.24           C  
ANISOU  900  CB  SER A 135     3011   3109   3471    -20     91    139       C  
ATOM    901  OG  SER A 135     111.102  72.377  19.180  1.00 25.48           O  
ANISOU  901  OG  SER A 135     3040   3156   3486    -14     69    149       O  
ATOM    902  N   TYR A 136     113.520  70.885  20.225  1.00 27.16           N  
ANISOU  902  N   TYR A 136     3246   3340   3733     11     75    196       N  
ATOM    903  CA  TYR A 136     113.979  70.741  21.572  1.00 28.47           C  
ANISOU  903  CA  TYR A 136     3411   3510   3894     21     66    222       C  
ATOM    904  C   TYR A 136     112.870  71.256  22.511  1.00 28.31           C  
ANISOU  904  C   TYR A 136     3400   3508   3851     15     56    220       C  
ATOM    905  O   TYR A 136     112.950  71.066  23.681  1.00 30.20           O  
ANISOU  905  O   TYR A 136     3640   3751   4081     20     51    239       O  
ATOM    906  CB  TYR A 136     115.275  71.523  21.774  1.00 28.29           C  
ANISOU  906  CB  TYR A 136     3380   3498   3872     30     45    234       C  
ATOM    907  CG  TYR A 136     115.126  73.036  21.876  1.00 29.74           C  
ANISOU  907  CG  TYR A 136     3564   3704   4033     26     23    222       C  
ATOM    908  CD1 TYR A 136     114.711  73.784  20.806  1.00 29.71           C  
ANISOU  908  CD1 TYR A 136     3559   3703   4024     18     23    199       C  
ATOM    909  CD2 TYR A 136     115.422  73.697  23.038  1.00 30.28           C  
ANISOU  909  CD2 TYR A 136     3631   3789   4085     29      3    235       C  
ATOM    910  CE1 TYR A 136     114.585  75.151  20.895  1.00 31.89           C  
ANISOU  910  CE1 TYR A 136     3837   3998   4284     15      5    189       C  
ATOM    911  CE2 TYR A 136     115.302  75.065  23.138  1.00 31.60           C  
ANISOU  911  CE2 TYR A 136     3799   3974   4234     25    -15    222       C  
ATOM    912  CZ  TYR A 136     114.882  75.792  22.064  1.00 30.19           C  
ANISOU  912  CZ  TYR A 136     3621   3796   4054     18    -13    200       C  
ATOM    913  OH  TYR A 136     114.765  77.141  22.161  1.00 30.35           O  
ANISOU  913  OH  TYR A 136     3643   3831   4059     14    -29    189       O  
ATOM    914  N   ALA A 137     111.853  71.919  21.978  1.00 26.57           N  
ANISOU  914  N   ALA A 137     3182   3297   3617      4     56    196       N  
ATOM    915  CA  ALA A 137     110.762  72.432  22.767  1.00 25.91           C  
ANISOU  915  CA  ALA A 137     3105   3228   3512     -2     49    192       C  
ATOM    916  C   ALA A 137     109.501  72.352  21.945  1.00 26.54           C  
ANISOU  916  C   ALA A 137     3187   3308   3590    -14     62    169       C  
ATOM    917  O   ALA A 137     109.038  73.335  21.331  1.00 27.87           O  
ANISOU  917  O   ALA A 137     3353   3488   3747    -19     54    151       O  
ATOM    918  CB  ALA A 137     111.052  73.872  23.154  1.00 27.11           C  
ANISOU  918  CB  ALA A 137     3255   3400   3645      1     26    189       C  
ATOM    919  N   ARG A 138     108.976  71.157  21.836  1.00 26.11           N  
ANISOU  919  N   ARG A 138     3135   3238   3548    -20     82    169       N  
ATOM    920  CA  ARG A 138     107.797  70.912  21.014  1.00 26.21           C  
ANISOU  920  CA  ARG A 138     3147   3250   3561    -34     95    146       C  
ATOM    921  C   ARG A 138     106.616  71.760  21.506  1.00 25.87           C  
ANISOU  921  C   ARG A 138     3106   3228   3497    -39     87    138       C  
ATOM    922  O   ARG A 138     106.438  71.939  22.703  1.00 28.27           O  
ANISOU  922  O   ARG A 138     3414   3538   3789    -35     81    151       O  
ATOM    923  CB  ARG A 138     107.460  69.432  21.064  1.00 26.62           C  
ANISOU  923  CB  ARG A 138     3203   3280   3631    -39    120    150       C  
ATOM    924  CG  ARG A 138     108.509  68.580  20.359  1.00 27.48           C  
ANISOU  924  CG  ARG A 138     3310   3368   3764    -35    133    154       C  
ATOM    925  CD  ARG A 138     108.485  67.162  20.864  1.00 28.87           C  
ANISOU  925  CD  ARG A 138     3491   3520   3959    -35    155    169       C  
ATOM    926  NE  ARG A 138     107.232  66.492  20.507  1.00 29.92           N  
ANISOU  926  NE  ARG A 138     3627   3647   4095    -52    174    151       N  
ATOM    927  CZ  ARG A 138     106.850  65.293  20.969  1.00 31.70           C  
ANISOU  927  CZ  ARG A 138     3857   3852   4336    -56    196    160       C  
ATOM    928  NH1 ARG A 138     107.592  64.636  21.824  1.00 32.22           N  
ANISOU  928  NH1 ARG A 138     3926   3903   4413    -43    201    188       N  
ATOM    929  NH2 ARG A 138     105.720  64.735  20.549  1.00 31.51           N  
ANISOU  929  NH2 ARG A 138     3834   3823   4315    -74    212    140       N  
ATOM    930  N   GLY A 139     105.890  72.375  20.585  1.00 25.48           N  
ANISOU  930  N   GLY A 139     3053   3189   3441    -47     84    116       N  
ATOM    931  CA  GLY A 139     104.746  73.233  20.939  1.00 25.58           C  
ANISOU  931  CA  GLY A 139     3064   3220   3434    -51     77    107       C  
ATOM    932  C   GLY A 139     103.479  72.387  21.163  1.00 25.98           C  
ANISOU  932  C   GLY A 139     3115   3268   3487    -62     94    101       C  
ATOM    933  O   GLY A 139     103.565  71.154  21.243  1.00 23.70           O  
ANISOU  933  O   GLY A 139     2830   2963   3214    -67    111    107       O  
ATOM    934  N   LYS A 140     102.318  73.061  21.219  1.00 25.97           N  
ANISOU  934  N   LYS A 140     3111   3285   3472    -67     91     90       N  
ATOM    935  CA  LYS A 140     101.038  72.415  21.141  1.00 28.92           C  
ANISOU  935  CA  LYS A 140     3480   3659   3848    -80    105     80       C  
ATOM    936  C   LYS A 140     100.298  72.645  19.842  1.00 27.47           C  
ANISOU  936  C   LYS A 140     3287   3486   3663    -91    106     58       C  
ATOM    937  O   LYS A 140      99.955  71.680  19.179  1.00 25.59           O  
ANISOU  937  O   LYS A 140     3046   3239   3437   -104    120     47       O  
ATOM    938  CB  LYS A 140     100.115  72.819  22.298  1.00 32.02           C  
ANISOU  938  CB  LYS A 140     3875   4064   4227    -79    105     85       C  
ATOM    939  CG  LYS A 140     100.590  72.213  23.575  1.00 34.45           C  
ANISOU  939  CG  LYS A 140     4193   4362   4535    -73    110    107       C  
ATOM    940  CD  LYS A 140      99.486  71.569  24.360  1.00 38.51           C  
ANISOU  940  CD  LYS A 140     4709   4877   5048    -81    126    110       C  
ATOM    941  CE  LYS A 140     100.067  70.578  25.350  1.00 40.64           C  
ANISOU  941  CE  LYS A 140     4987   5130   5324    -77    136    133       C  
ATOM    942  NZ  LYS A 140      99.669  70.998  26.711  1.00 45.10           N  
ANISOU  942  NZ  LYS A 140     5558   5706   5870    -72    134    145       N  
ATOM    943  N   LEU A 141     100.036  73.903  19.521  1.00 24.93           N  
ANISOU  943  N   LEU A 141     2960   3182   3328    -86     91     51       N  
ATOM    944  CA  LEU A 141      99.513  74.266  18.217  1.00 26.09           C  
ANISOU  944  CA  LEU A 141     3097   3342   3473    -93     87     33       C  
ATOM    945  C   LEU A 141     100.482  73.984  17.024  1.00 25.38           C  
ANISOU  945  C   LEU A 141     3008   3244   3392    -95     87     27       C  
ATOM    946  O   LEU A 141     100.037  73.648  15.945  1.00 23.46           O  
ANISOU  946  O   LEU A 141     2758   3005   3150   -106     92     11       O  
ATOM    947  CB  LEU A 141      99.110  75.765  18.219  1.00 26.14           C  
ANISOU  947  CB  LEU A 141     3099   3369   3464    -84     71     31       C  
ATOM    948  CG  LEU A 141      97.947  76.120  19.132  1.00 26.06           C  
ANISOU  948  CG  LEU A 141     3085   3370   3445    -84     73     33       C  
ATOM    949  CD1 LEU A 141      97.543  77.556  18.840  1.00 26.98           C  
ANISOU  949  CD1 LEU A 141     3196   3505   3550    -75     60     29       C  
ATOM    950  CD2 LEU A 141      96.748  75.194  18.923  1.00 26.41           C  
ANISOU  950  CD2 LEU A 141     3122   3419   3495   -100     87     22       C  
ATOM    951  N   PHE A 142     101.799  74.109  17.277  1.00 24.81           N  
ANISOU  951  N   PHE A 142     2943   3160   3325    -83     82     40       N  
ATOM    952  CA  PHE A 142     102.836  73.981  16.266  1.00 24.11           C  
ANISOU  952  CA  PHE A 142     2854   3062   3243    -82     82     37       C  
ATOM    953  C   PHE A 142     103.928  73.032  16.710  1.00 23.84           C  
ANISOU  953  C   PHE A 142     2827   3005   3225    -78     91     50       C  
ATOM    954  O   PHE A 142     103.991  72.680  17.858  1.00 24.25           O  
ANISOU  954  O   PHE A 142     2884   3050   3280    -73     94     64       O  
ATOM    955  CB  PHE A 142     103.457  75.331  16.009  1.00 24.35           C  
ANISOU  955  CB  PHE A 142     2884   3104   3266    -70     64     40       C  
ATOM    956  CG  PHE A 142     102.489  76.381  15.551  1.00 23.92           C  
ANISOU  956  CG  PHE A 142     2821   3070   3195    -71     54     30       C  
ATOM    957  CD1 PHE A 142     102.266  76.583  14.185  1.00 23.83           C  
ANISOU  957  CD1 PHE A 142     2805   3070   3181    -77     53     17       C  
ATOM    958  CD2 PHE A 142     101.860  77.232  16.454  1.00 24.36           C  
ANISOU  958  CD2 PHE A 142     2877   3137   3241    -65     46     36       C  
ATOM    959  CE1 PHE A 142     101.418  77.563  13.726  1.00 23.32           C  
ANISOU  959  CE1 PHE A 142     2732   3025   3103    -76     44     11       C  
ATOM    960  CE2 PHE A 142     101.018  78.263  15.985  1.00 24.31           C  
ANISOU  960  CE2 PHE A 142     2864   3149   3223    -63     38     28       C  
ATOM    961  CZ  PHE A 142     100.769  78.400  14.620  1.00 23.54           C  
ANISOU  961  CZ  PHE A 142     2759   3063   3124    -69     37     17       C  
ATOM    962  N   TRP A 143     104.772  72.609  15.765  1.00 24.86           N  
ANISOU  962  N   TRP A 143     2956   3123   3366    -79     97     45       N  
ATOM    963  CA  TRP A 143     105.892  71.725  16.031  1.00 24.32           C  
ANISOU  963  CA  TRP A 143     2892   3032   3316    -73    107     58       C  
ATOM    964  C   TRP A 143     106.877  72.273  17.062  1.00 23.93           C  
ANISOU  964  C   TRP A 143     2845   2981   3265    -57     94     80       C  
ATOM    965  O   TRP A 143     107.578  71.500  17.725  1.00 24.20           O  
ANISOU  965  O   TRP A 143     2883   2999   3312    -50    101     97       O  
ATOM    966  CB  TRP A 143     106.602  71.374  14.689  1.00 25.40           C  
ANISOU  966  CB  TRP A 143     3027   3160   3463    -76    116     46       C  
ATOM    967  CG  TRP A 143     107.490  72.441  14.116  1.00 23.65           C  
ANISOU  967  CG  TRP A 143     2803   2948   3236    -67    101     48       C  
ATOM    968  CD1 TRP A 143     107.110  73.590  13.492  1.00 23.40           C  
ANISOU  968  CD1 TRP A 143     2767   2935   3187    -68     87     39       C  
ATOM    969  CD2 TRP A 143     108.914  72.456  14.176  1.00 23.17           C  
ANISOU  969  CD2 TRP A 143     2742   2875   3187    -55     99     62       C  
ATOM    970  NE1 TRP A 143     108.219  74.327  13.161  1.00 23.58           N  
ANISOU  970  NE1 TRP A 143     2789   2959   3211    -58     78     46       N  
ATOM    971  CE2 TRP A 143     109.345  73.631  13.531  1.00 22.89           C  
ANISOU  971  CE2 TRP A 143     2703   2852   3141    -51     85     59       C  
ATOM    972  CE3 TRP A 143     109.871  71.579  14.706  1.00 23.24           C  
ANISOU  972  CE3 TRP A 143     2753   2863   3215    -47    109     78       C  
ATOM    973  CZ2 TRP A 143     110.690  73.961  13.404  1.00 21.99           C  
ANISOU  973  CZ2 TRP A 143     2586   2732   3036    -40     81     69       C  
ATOM    974  CZ3 TRP A 143     111.211  71.891  14.564  1.00 23.12           C  
ANISOU  974  CZ3 TRP A 143     2735   2842   3209    -36    104     89       C  
ATOM    975  CH2 TRP A 143     111.611  73.071  13.895  1.00 21.91           C  
ANISOU  975  CH2 TRP A 143     2578   2703   3046    -33     90     84       C  
ATOM    976  N   GLN A 144     106.900  73.589  17.239  1.00 22.10           N  
ANISOU  976  N   GLN A 144     2612   2767   3019    -51     75     81       N  
ATOM    977  CA  GLN A 144     107.808  74.169  18.192  1.00 24.04           C  
ANISOU  977  CA  GLN A 144     2859   3014   3261    -38     61     99       C  
ATOM    978  C   GLN A 144     107.159  75.352  18.964  1.00 24.38           C  
ANISOU  978  C   GLN A 144     2903   3075   3284    -36     46     99       C  
ATOM    979  O   GLN A 144     106.260  76.091  18.463  1.00 24.09           O  
ANISOU  979  O   GLN A 144     2864   3052   3237    -40     42     85       O  
ATOM    980  CB  GLN A 144     109.122  74.608  17.482  1.00 23.39           C  
ANISOU  980  CB  GLN A 144     2773   2927   3186    -31     54    102       C  
ATOM    981  CG  GLN A 144     108.843  75.631  16.411  1.00 24.69           C  
ANISOU  981  CG  GLN A 144     2934   3105   3342    -34     47     86       C  
ATOM    982  CD  GLN A 144     110.089  76.212  15.735  1.00 24.99           C  
ANISOU  982  CD  GLN A 144     2969   3141   3386    -28     40     89       C  
ATOM    983  OE1 GLN A 144     111.214  75.987  16.135  1.00 23.48           O  
ANISOU  983  OE1 GLN A 144     2775   2940   3205    -20     38    103       O  
ATOM    984  NE2 GLN A 144     109.852  76.920  14.681  1.00 26.29           N  
ANISOU  984  NE2 GLN A 144     3130   3315   3543    -31     37     77       N  
ATOM    985  N   CYS A 145     107.653  75.540  20.173  1.00 24.38           N  
ANISOU  985  N   CYS A 145     2907   3076   3280    -28     37    116       N  
ATOM    986  CA  CYS A 145     107.228  76.637  21.051  1.00 24.48           C  
ANISOU  986  CA  CYS A 145     2923   3104   3274    -25     24    116       C  
ATOM    987  C   CYS A 145     107.449  78.017  20.475  1.00 23.72           C  
ANISOU  987  C   CYS A 145     2824   3018   3171    -22     10    107       C  
ATOM    988  O   CYS A 145     106.668  78.955  20.766  1.00 24.32           O  
ANISOU  988  O   CYS A 145     2900   3106   3233    -22      4    100       O  
ATOM    989  CB  CYS A 145     107.911  76.496  22.425  1.00 26.80           C  
ANISOU  989  CB  CYS A 145     3222   3398   3564    -18     17    135       C  
ATOM    990  SG  CYS A 145     107.099  75.360  23.613  1.00 26.50           S  
ANISOU  990  SG  CYS A 145     3190   3356   3523    -21     30    147       S  
ATOM    991  N   LEU A 146     108.476  78.183  19.647  1.00 23.00           N  
ANISOU  991  N   LEU A 146     2729   2921   3090    -19      7    107       N  
ATOM    992  CA  LEU A 146     108.653  79.437  18.909  1.00 22.50           C  
ANISOU  992  CA  LEU A 146     2662   2865   3021    -18     -3     99       C  
ATOM    993  C   LEU A 146     107.336  79.880  18.256  1.00 22.87           C  
ANISOU  993  C   LEU A 146     2706   2922   3059    -22      0     84       C  
ATOM    994  O   LEU A 146     106.935  81.056  18.361  1.00 21.59           O  
ANISOU  994  O   LEU A 146     2545   2771   2888    -19     -8     80       O  
ATOM    995  CB  LEU A 146     109.745  79.343  17.869  1.00 22.53           C  
ANISOU  995  CB  LEU A 146     2661   2861   3038    -16     -2     99       C  
ATOM    996  CG  LEU A 146     109.956  80.561  16.983  1.00 22.85           C  
ANISOU  996  CG  LEU A 146     2698   2907   3075    -14    -10     92       C  
ATOM    997  CD1 LEU A 146     110.211  81.822  17.802  1.00 22.64           C  
ANISOU  997  CD1 LEU A 146     2674   2888   3040    -10    -25     95       C  
ATOM    998  CD2 LEU A 146     111.049  80.291  15.936  1.00 22.34           C  
ANISOU  998  CD2 LEU A 146     2629   2835   3025    -13     -6     93       C  
ATOM    999  N   ASN A 147     106.691  78.959  17.556  1.00 22.78           N  
ANISOU  999  N   ASN A 147     2693   2909   3053    -30     13     76       N  
ATOM   1000  CA  ASN A 147     105.504  79.316  16.775  1.00 23.68           C  
ANISOU 1000  CA  ASN A 147     2803   3036   3160    -35     15     63       C  
ATOM   1001  C   ASN A 147     104.239  79.449  17.667  1.00 24.50           C  
ANISOU 1001  C   ASN A 147     2907   3148   3253    -37     17     61       C  
ATOM   1002  O   ASN A 147     103.412  80.303  17.394  1.00 23.51           O  
ANISOU 1002  O   ASN A 147     2777   3036   3118    -36     13     54       O  
ATOM   1003  CB  ASN A 147     105.266  78.336  15.592  1.00 24.53           C  
ANISOU 1003  CB  ASN A 147     2907   3140   3275    -45     28     52       C  
ATOM   1004  CG  ASN A 147     106.410  78.290  14.587  1.00 23.79           C  
ANISOU 1004  CG  ASN A 147     2811   3038   3189    -43     29     52       C  
ATOM   1005  OD1 ASN A 147     106.844  77.222  14.226  1.00 25.17           O  
ANISOU 1005  OD1 ASN A 147     2986   3200   3375    -48     40     50       O  
ATOM   1006  ND2 ASN A 147     106.854  79.421  14.105  1.00 23.88           N  
ANISOU 1006  ND2 ASN A 147     2821   3056   3196    -37     18     52       N  
ATOM   1007  N   ASP A 148     104.124  78.655  18.756  1.00 23.65           N  
ANISOU 1007  N   ASP A 148     2805   3035   3147    -38     23     68       N  
ATOM   1008  CA  ASP A 148     103.119  78.928  19.760  1.00 24.29           C  
ANISOU 1008  CA  ASP A 148     2887   3124   3217    -38     24     69       C  
ATOM   1009  C   ASP A 148     103.277  80.345  20.343  1.00 24.22           C  
ANISOU 1009  C   ASP A 148     2882   3124   3197    -29     10     71       C  
ATOM   1010  O   ASP A 148     102.262  81.046  20.576  1.00 22.66           O  
ANISOU 1010  O   ASP A 148     2682   2937   2991    -28     10     65       O  
ATOM   1011  CB  ASP A 148     103.118  77.929  20.888  1.00 24.43           C  
ANISOU 1011  CB  ASP A 148     2911   3134   3237    -40     32     80       C  
ATOM   1012  CG  ASP A 148     102.589  76.528  20.465  1.00 25.12           C  
ANISOU 1012  CG  ASP A 148     2996   3213   3336    -51     49     76       C  
ATOM   1013  OD1 ASP A 148     102.979  76.006  19.423  1.00 25.45           O  
ANISOU 1013  OD1 ASP A 148     3035   3247   3388    -55     54     70       O  
ATOM   1014  OD2 ASP A 148     101.818  75.909  21.213  1.00 24.73           O  
ANISOU 1014  OD2 ASP A 148     2948   3163   3284    -56     59     78       O  
ATOM   1015  N   SER A 149     104.529  80.753  20.597  1.00 22.92           N  
ANISOU 1015  N   SER A 149     2721   2953   3034    -23      1     79       N  
ATOM   1016  CA  SER A 149     104.788  82.085  21.066  1.00 22.14           C  
ANISOU 1016  CA  SER A 149     2625   2859   2926    -17    -11     78       C  
ATOM   1017  C   SER A 149     104.381  83.195  20.063  1.00 22.19           C  
ANISOU 1017  C   SER A 149     2627   2873   2932    -14    -15     68       C  
ATOM   1018  O   SER A 149     103.817  84.233  20.502  1.00 23.18           O  
ANISOU 1018  O   SER A 149     2753   3004   3049    -10    -18     64       O  
ATOM   1019  CB  SER A 149     106.240  82.204  21.539  1.00 23.49           C  
ANISOU 1019  CB  SER A 149     2801   3025   3102    -13    -21     88       C  
ATOM   1020  OG  SER A 149     106.518  81.195  22.554  1.00 25.07           O  
ANISOU 1020  OG  SER A 149     3005   3221   3301    -14    -18    100       O  
ATOM   1021  N   ASN A 150     104.686  83.014  18.770  1.00 22.11           N  
ANISOU 1021  N   ASN A 150     2610   2860   2929    -16    -14     65       N  
ATOM   1022  CA  ASN A 150     104.211  83.924  17.681  1.00 21.96           C  
ANISOU 1022  CA  ASN A 150     2585   2850   2909    -13    -16     58       C  
ATOM   1023  C   ASN A 150     102.703  84.104  17.813  1.00 22.20           C  
ANISOU 1023  C   ASN A 150     2611   2892   2932    -14    -11     52       C  
ATOM   1024  O   ASN A 150     102.176  85.216  17.803  1.00 23.10           O  
ANISOU 1024  O   ASN A 150     2724   3013   3041     -8    -14     50       O  
ATOM   1025  CB  ASN A 150     104.416  83.379  16.254  1.00 22.80           C  
ANISOU 1025  CB  ASN A 150     2686   2956   3022    -18    -12     54       C  
ATOM   1026  CG  ASN A 150     105.849  83.099  15.837  1.00 23.35           C  
ANISOU 1026  CG  ASN A 150     2757   3014   3101    -18    -13     60       C  
ATOM   1027  OD1 ASN A 150     106.055  82.146  15.063  1.00 23.95           O  
ANISOU 1027  OD1 ASN A 150     2830   3086   3184    -23     -6     57       O  
ATOM   1028  ND2 ASN A 150     106.814  83.837  16.325  1.00 23.51           N  
ANISOU 1028  ND2 ASN A 150     2781   3029   3124    -12    -22     66       N  
ATOM   1029  N   TRP A 151     102.009  82.986  17.891  1.00 21.70           N  
ANISOU 1029  N   TRP A 151     2546   2831   2870    -22     -2     49       N  
ATOM   1030  CA  TRP A 151     100.566  82.963  18.025  1.00 23.17           C  
ANISOU 1030  CA  TRP A 151     2725   3029   3050    -24      4     43       C  
ATOM   1031  C   TRP A 151     100.054  83.809  19.182  1.00 23.53           C  
ANISOU 1031  C   TRP A 151     2775   3078   3088    -17      3     45       C  
ATOM   1032  O   TRP A 151      99.204  84.712  18.951  1.00 22.91           O  
ANISOU 1032  O   TRP A 151     2690   3009   3005    -12      2     41       O  
ATOM   1033  CB  TRP A 151     100.106  81.517  18.194  1.00 23.99           C  
ANISOU 1033  CB  TRP A 151     2828   3131   3158    -36     16     41       C  
ATOM   1034  CG  TRP A 151      98.615  81.266  18.127  1.00 25.09           C  
ANISOU 1034  CG  TRP A 151     2957   3282   3293    -42     23     34       C  
ATOM   1035  CD1 TRP A 151      97.934  80.768  17.062  1.00 25.99           C  
ANISOU 1035  CD1 TRP A 151     3061   3406   3410    -51     27     24       C  
ATOM   1036  CD2 TRP A 151      97.667  81.374  19.187  1.00 26.29           C  
ANISOU 1036  CD2 TRP A 151     3109   3440   3440    -41     29     34       C  
ATOM   1037  NE1 TRP A 151      96.623  80.605  17.364  1.00 26.67           N  
ANISOU 1037  NE1 TRP A 151     3137   3503   3492    -55     33     20       N  
ATOM   1038  CE2 TRP A 151      96.415  80.984  18.662  1.00 26.88           C  
ANISOU 1038  CE2 TRP A 151     3170   3527   3514    -49     35     26       C  
ATOM   1039  CE3 TRP A 151      97.732  81.811  20.519  1.00 26.85           C  
ANISOU 1039  CE3 TRP A 151     3189   3508   3505    -34     29     41       C  
ATOM   1040  CZ2 TRP A 151      95.244  81.004  19.419  1.00 26.96           C  
ANISOU 1040  CZ2 TRP A 151     3175   3546   3521    -50     43     25       C  
ATOM   1041  CZ3 TRP A 151      96.540  81.825  21.281  1.00 27.10           C  
ANISOU 1041  CZ3 TRP A 151     3217   3548   3531    -35     37     39       C  
ATOM   1042  CH2 TRP A 151      95.338  81.419  20.736  1.00 27.14           C  
ANISOU 1042  CH2 TRP A 151     3209   3565   3539    -42     45     31       C  
ATOM   1043  N   LEU A 152     100.621  83.597  20.391  1.00 22.28           N  
ANISOU 1043  N   LEU A 152     2627   2912   2927    -17      3     51       N  
ATOM   1044  CA  LEU A 152     100.251  84.406  21.536  1.00 22.92           C  
ANISOU 1044  CA  LEU A 152     2714   2996   2999    -11      2     51       C  
ATOM   1045  C   LEU A 152     100.579  85.895  21.486  1.00 23.32           C  
ANISOU 1045  C   LEU A 152     2768   3047   3048     -2     -6     49       C  
ATOM   1046  O   LEU A 152      99.729  86.719  21.897  1.00 23.22           O  
ANISOU 1046  O   LEU A 152     2755   3040   3030      3     -3     44       O  
ATOM   1047  CB  LEU A 152     100.653  83.751  22.868  1.00 24.49           C  
ANISOU 1047  CB  LEU A 152     2922   3189   3192    -14      4     58       C  
ATOM   1048  CG  LEU A 152     100.194  84.405  24.155  1.00 24.73           C  
ANISOU 1048  CG  LEU A 152     2960   3225   3210    -10      6     57       C  
ATOM   1049  CD1 LEU A 152      98.665  84.487  24.202  1.00 25.57           C  
ANISOU 1049  CD1 LEU A 152     3060   3341   3313    -10     17     51       C  
ATOM   1050  CD2 LEU A 152     100.757  83.627  25.330  1.00 25.88           C  
ANISOU 1050  CD2 LEU A 152     3116   3368   3349    -14      7     67       C  
ATOM   1051  N   VAL A 153     101.731  86.287  20.932  1.00 22.56           N  
ANISOU 1051  N   VAL A 153     2672   2942   2956      0    -15     52       N  
ATOM   1052  CA  VAL A 153     101.989  87.727  20.708  1.00 22.59           C  
ANISOU 1052  CA  VAL A 153     2678   2945   2961      8    -21     49       C  
ATOM   1053  C   VAL A 153     100.853  88.380  19.850  1.00 24.19           C  
ANISOU 1053  C   VAL A 153     2871   3156   3164     13    -16     45       C  
ATOM   1054  O   VAL A 153     100.365  89.479  20.143  1.00 25.87           O  
ANISOU 1054  O   VAL A 153     3084   3369   3375     21    -15     43       O  
ATOM   1055  CB  VAL A 153     103.358  87.968  20.019  1.00 21.79           C  
ANISOU 1055  CB  VAL A 153     2577   2834   2867      8    -29     53       C  
ATOM   1056  CG1 VAL A 153     103.523  89.427  19.644  1.00 23.38           C  
ANISOU 1056  CG1 VAL A 153     2780   3032   3070     15    -33     51       C  
ATOM   1057  CG2 VAL A 153     104.479  87.531  20.943  1.00 21.03           C  
ANISOU 1057  CG2 VAL A 153     2490   2732   2770      4    -35     58       C  
ATOM   1058  N   TYR A 154     100.468  87.707  18.778  1.00 23.81           N  
ANISOU 1058  N   TYR A 154     2813   3115   3120     10    -15     45       N  
ATOM   1059  CA  TYR A 154      99.480  88.246  17.877  1.00 25.50           C  
ANISOU 1059  CA  TYR A 154     3015   3340   3333     15    -13     44       C  
ATOM   1060  C   TYR A 154      98.071  88.226  18.482  1.00 25.81           C  
ANISOU 1060  C   TYR A 154     3049   3389   3368     17     -5     40       C  
ATOM   1061  O   TYR A 154      97.389  89.209  18.453  1.00 26.45           O  
ANISOU 1061  O   TYR A 154     3126   3476   3449     26     -3     40       O  
ATOM   1062  CB  TYR A 154      99.520  87.567  16.488  1.00 24.72           C  
ANISOU 1062  CB  TYR A 154     2908   3248   3237      9    -14     43       C  
ATOM   1063  CG  TYR A 154     100.566  88.126  15.566  1.00 24.86           C  
ANISOU 1063  CG  TYR A 154     2927   3260   3258     13    -21     48       C  
ATOM   1064  CD1 TYR A 154     101.896  87.697  15.621  1.00 24.28           C  
ANISOU 1064  CD1 TYR A 154     2862   3174   3190      8    -24     50       C  
ATOM   1065  CD2 TYR A 154     100.223  89.099  14.608  1.00 25.30           C  
ANISOU 1065  CD2 TYR A 154     2976   3323   3313     21    -23     51       C  
ATOM   1066  CE1 TYR A 154     102.862  88.215  14.750  1.00 24.83           C  
ANISOU 1066  CE1 TYR A 154     2932   3239   3264     11    -28     54       C  
ATOM   1067  CE2 TYR A 154     101.176  89.635  13.750  1.00 25.75           C  
ANISOU 1067  CE2 TYR A 154     3035   3375   3374     24    -28     56       C  
ATOM   1068  CZ  TYR A 154     102.490  89.186  13.823  1.00 25.46           C  
ANISOU 1068  CZ  TYR A 154     3006   3326   3342     18    -30     56       C  
ATOM   1069  OH  TYR A 154     103.369  89.717  12.961  1.00 25.36           O  
ANISOU 1069  OH  TYR A 154     2994   3308   3334     21    -33     61       O  
ATOM   1070  N   VAL A 155      97.685  87.114  19.068  1.00 26.54           N  
ANISOU 1070  N   VAL A 155     3142   3485   3459      8      1     38       N  
ATOM   1071  CA  VAL A 155      96.381  86.970  19.689  1.00 25.56           C  
ANISOU 1071  CA  VAL A 155     3011   3370   3331      8     10     35       C  
ATOM   1072  C   VAL A 155      96.139  87.915  20.898  1.00 27.16           C  
ANISOU 1072  C   VAL A 155     3222   3569   3528     16     14     34       C  
ATOM   1073  O   VAL A 155      94.989  88.369  21.100  1.00 25.93           O  
ANISOU 1073  O   VAL A 155     3059   3422   3372     22     22     32       O  
ATOM   1074  CB  VAL A 155      96.100  85.519  20.033  1.00 25.17           C  
ANISOU 1074  CB  VAL A 155     2961   3321   3281     -5     18     33       C  
ATOM   1075  CG1 VAL A 155      94.757  85.351  20.708  1.00 26.32           C  
ANISOU 1075  CG1 VAL A 155     3100   3477   3424     -6     28     31       C  
ATOM   1076  CG2 VAL A 155      96.044  84.701  18.761  1.00 26.17           C  
ANISOU 1076  CG2 VAL A 155     3078   3454   3413    -14     16     31       C  
ATOM   1077  N   SER A 156      97.185  88.192  21.676  1.00 25.87           N  
ANISOU 1077  N   SER A 156     3073   3393   3362     17     10     35       N  
ATOM   1078  CA  SER A 156      97.141  89.129  22.769  1.00 26.59           C  
ANISOU 1078  CA  SER A 156     3175   3481   3448     23     13     32       C  
ATOM   1079  C   SER A 156      96.615  90.475  22.329  1.00 26.24           C  
ANISOU 1079  C   SER A 156     3125   3437   3408     35     15     30       C  
ATOM   1080  O   SER A 156      95.860  91.138  23.073  1.00 24.20           O  
ANISOU 1080  O   SER A 156     2869   3180   3147     42     24     25       O  
ATOM   1081  CB  SER A 156      98.533  89.368  23.350  1.00 27.34           C  
ANISOU 1081  CB  SER A 156     3284   3563   3539     21      4     33       C  
ATOM   1082  OG  SER A 156      98.843  88.284  24.185  1.00 32.70           O  
ANISOU 1082  OG  SER A 156     3970   4243   4212     12      5     36       O  
ATOM   1083  N   GLN A 157      97.087  90.900  21.162  1.00 25.70           N  
ANISOU 1083  N   GLN A 157     3052   3367   3347     39      7     33       N  
ATOM   1084  CA  GLN A 157      96.667  92.190  20.591  1.00 26.23           C  
ANISOU 1084  CA  GLN A 157     3113   3433   3420     52      9     35       C  
ATOM   1085  C   GLN A 157      95.164  92.163  20.269  1.00 25.38           C  
ANISOU 1085  C   GLN A 157     2990   3341   3314     58     17     35       C  
ATOM   1086  O   GLN A 157      94.445  93.146  20.526  1.00 25.02           O  
ANISOU 1086  O   GLN A 157     2942   3295   3271     70     24     35       O  
ATOM   1087  CB  GLN A 157      97.499  92.517  19.358  1.00 25.73           C  
ANISOU 1087  CB  GLN A 157     3048   3366   3363     54      0     40       C  
ATOM   1088  CG  GLN A 157      98.931  92.774  19.727  1.00 26.73           C  
ANISOU 1088  CG  GLN A 157     3188   3477   3491     49     -7     40       C  
ATOM   1089  CD  GLN A 157      99.794  92.970  18.518  1.00 26.96           C  
ANISOU 1089  CD  GLN A 157     3215   3502   3526     50    -15     46       C  
ATOM   1090  OE1 GLN A 157      99.656  93.956  17.793  1.00 25.70           O  
ANISOU 1090  OE1 GLN A 157     3051   3341   3372     59    -14     50       O  
ATOM   1091  NE2 GLN A 157     100.685  92.015  18.272  1.00 27.97           N  
ANISOU 1091  NE2 GLN A 157     3344   3629   3654     40    -21     47       N  
ATOM   1092  N   ALA A 158      94.712  91.057  19.684  1.00 25.23           N  
ANISOU 1092  N   ALA A 158     2959   3334   3293     49     15     37       N  
ATOM   1093  CA  ALA A 158      93.300  90.866  19.393  1.00 26.20           C  
ANISOU 1093  CA  ALA A 158     3064   3473   3416     52     22     37       C  
ATOM   1094  C   ALA A 158      92.465  90.864  20.663  1.00 27.83           C  
ANISOU 1094  C   ALA A 158     3272   3681   3620     53     34     32       C  
ATOM   1095  O   ALA A 158      91.406  91.503  20.696  1.00 27.27           O  
ANISOU 1095  O   ALA A 158     3191   3619   3552     64     41     33       O  
ATOM   1096  CB  ALA A 158      93.017  89.573  18.602  1.00 26.03           C  
ANISOU 1096  CB  ALA A 158     3032   3466   3393     38     18     36       C  
ATOM   1097  N   TYR A 159      92.912  90.114  21.681  1.00 28.06           N  
ANISOU 1097  N   TYR A 159     3316   3704   3643     43     37     28       N  
ATOM   1098  CA  TYR A 159      92.209  90.080  22.955  1.00 27.56           C  
ANISOU 1098  CA  TYR A 159     3256   3642   3575     43     50     24       C  
ATOM   1099  C   TYR A 159      92.071  91.504  23.543  1.00 28.41           C  
ANISOU 1099  C   TYR A 159     3370   3742   3683     57     56     21       C  
ATOM   1100  O   TYR A 159      90.979  91.878  24.058  1.00 27.17           O  
ANISOU 1100  O   TYR A 159     3207   3590   3526     65     69     18       O  
ATOM   1101  CB  TYR A 159      92.873  89.106  23.945  1.00 27.83           C  
ANISOU 1101  CB  TYR A 159     3304   3669   3599     31     51     23       C  
ATOM   1102  CG  TYR A 159      92.109  88.834  25.230  1.00 27.77           C  
ANISOU 1102  CG  TYR A 159     3301   3665   3585     29     65     20       C  
ATOM   1103  CD1 TYR A 159      90.711  88.569  25.232  1.00 28.91           C  
ANISOU 1103  CD1 TYR A 159     3429   3822   3731     30     77     19       C  
ATOM   1104  CD2 TYR A 159      92.775  88.801  26.447  1.00 28.97           C  
ANISOU 1104  CD2 TYR A 159     3472   3810   3726     26     66     19       C  
ATOM   1105  CE1 TYR A 159      90.034  88.282  26.408  1.00 29.34           C  
ANISOU 1105  CE1 TYR A 159     3488   3880   3779     27     91     16       C  
ATOM   1106  CE2 TYR A 159      92.118  88.514  27.633  1.00 31.01           C  
ANISOU 1106  CE2 TYR A 159     3735   4072   3975     24     80     16       C  
ATOM   1107  CZ  TYR A 159      90.727  88.288  27.615  1.00 31.77           C  
ANISOU 1107  CZ  TYR A 159     3816   4179   4075     25     94     15       C  
ATOM   1108  OH  TYR A 159      90.097  88.026  28.801  1.00 32.02           O  
ANISOU 1108  OH  TYR A 159     3853   4215   4097     22    109     13       O  
ATOM   1109  N   ASP A 160      93.139  92.292  23.471  1.00 26.24           N  
ANISOU 1109  N   ASP A 160     3108   3453   3409     61     48     20       N  
ATOM   1110  CA  ASP A 160      93.074  93.694  23.900  1.00 27.44           C  
ANISOU 1110  CA  ASP A 160     3267   3595   3564     74     55     16       C  
ATOM   1111  C   ASP A 160      91.941  94.502  23.190  1.00 28.61           C  
ANISOU 1111  C   ASP A 160     3398   3750   3723     89     62     20       C  
ATOM   1112  O   ASP A 160      91.286  95.389  23.783  1.00 28.87           O  
ANISOU 1112  O   ASP A 160     3431   3778   3759    100     75     16       O  
ATOM   1113  CB  ASP A 160      94.427  94.392  23.695  1.00 28.05           C  
ANISOU 1113  CB  ASP A 160     3357   3656   3643     74     45     16       C  
ATOM   1114  CG  ASP A 160      94.588  95.645  24.559  1.00 29.29           C  
ANISOU 1114  CG  ASP A 160     3527   3799   3800     81     53      7       C  
ATOM   1115  OD1 ASP A 160      94.026  95.702  25.671  1.00 30.50           O  
ANISOU 1115  OD1 ASP A 160     3688   3955   3947     80     64     -1       O  
ATOM   1116  OD2 ASP A 160      95.275  96.586  24.116  1.00 28.20           O  
ANISOU 1116  OD2 ASP A 160     3395   3649   3671     85     49      7       O  
ATOM   1117  N   CYS A 161      91.762  94.213  21.918  1.00 30.37           N  
ANISOU 1117  N   CYS A 161     3605   3983   3951     90     54     29       N  
ATOM   1118  CA  CYS A 161      90.790  94.909  21.071  1.00 30.88           C  
ANISOU 1118  CA  CYS A 161     3651   4057   4025    105     57     37       C  
ATOM   1119  C   CYS A 161      89.329  94.478  21.336  1.00 32.18           C  
ANISOU 1119  C   CYS A 161     3798   4240   4191    107     67     36       C  
ATOM   1120  O   CYS A 161      88.436  95.275  21.115  1.00 30.38           O  
ANISOU 1120  O   CYS A 161     3557   4016   3971    122     75     41       O  
ATOM   1121  CB  CYS A 161      91.142  94.764  19.621  1.00 29.73           C  
ANISOU 1121  CB  CYS A 161     3495   3919   3883    105     43     46       C  
ATOM   1122  SG  CYS A 161      92.550  95.806  19.079  1.00 31.82           S  
ANISOU 1122  SG  CYS A 161     3774   4163   4152    110     35     50       S  
ATOM   1123  N   VAL A 162      89.107  93.252  21.811  1.00 30.51           N  
ANISOU 1123  N   VAL A 162     3585   4036   3971     92     69     31       N  
ATOM   1124  CA  VAL A 162      87.763  92.792  22.147  1.00 31.44           C  
ANISOU 1124  CA  VAL A 162     3686   4169   4089     91     80     30       C  
ATOM   1125  C   VAL A 162      87.472  92.663  23.624  1.00 32.05           C  
ANISOU 1125  C   VAL A 162     3776   4241   4161     89     95     22       C  
ATOM   1126  O   VAL A 162      86.375  92.228  23.953  1.00 31.22           O  
ANISOU 1126  O   VAL A 162     3657   4148   4057     87    106     21       O  
ATOM   1127  CB  VAL A 162      87.392  91.448  21.475  1.00 32.74           C  
ANISOU 1127  CB  VAL A 162     3836   4351   4252     76     74     31       C  
ATOM   1128  CG1 VAL A 162      87.392  91.640  19.975  1.00 34.36           C  
ANISOU 1128  CG1 VAL A 162     4026   4568   4461     79     60     39       C  
ATOM   1129  CG2 VAL A 162      88.265  90.267  21.954  1.00 31.56           C  
ANISOU 1129  CG2 VAL A 162     3703   4193   4094     57     71     26       C  
ATOM   1130  N   TYR A 163      88.406  93.069  24.499  1.00 30.67           N  
ANISOU 1130  N   TYR A 163     3624   4048   3980     88     97     16       N  
ATOM   1131  CA  TYR A 163      88.260  92.865  25.931  1.00 33.19           C  
ANISOU 1131  CA  TYR A 163     3957   4363   4289     83    110      8       C  
ATOM   1132  C   TYR A 163      86.887  93.370  26.468  1.00 34.07           C  
ANISOU 1132  C   TYR A 163     4057   4482   4405     94    129      6       C  
ATOM   1133  O   TYR A 163      86.177  92.612  27.134  1.00 33.18           O  
ANISOU 1133  O   TYR A 163     3940   4378   4287     87    140      4       O  
ATOM   1134  CB  TYR A 163      89.392  93.547  26.680  1.00 33.54           C  
ANISOU 1134  CB  TYR A 163     4026   4390   4326     83    108      2       C  
ATOM   1135  CG  TYR A 163      89.574  93.132  28.108  1.00 35.44           C  
ANISOU 1135  CG  TYR A 163     4285   4630   4552     74    116     -5       C  
ATOM   1136  CD1 TYR A 163      90.456  92.133  28.458  1.00 37.17           C  
ANISOU 1136  CD1 TYR A 163     4515   4847   4760     60    106     -3       C  
ATOM   1137  CD2 TYR A 163      88.938  93.838  29.137  1.00 37.74           C  
ANISOU 1137  CD2 TYR A 163     4582   4918   4839     81    134    -14       C  
ATOM   1138  CE1 TYR A 163      90.653  91.796  29.788  1.00 38.62           C  
ANISOU 1138  CE1 TYR A 163     4715   5031   4927     52    113     -8       C  
ATOM   1139  CE2 TYR A 163      89.105  93.503  30.459  1.00 37.43           C  
ANISOU 1139  CE2 TYR A 163     4560   4878   4782     73    142    -21       C  
ATOM   1140  CZ  TYR A 163      89.974  92.504  30.784  1.00 38.53           C  
ANISOU 1140  CZ  TYR A 163     4711   5020   4910     59    131    -17       C  
ATOM   1141  OH  TYR A 163      90.146  92.208  32.102  1.00 38.50           O  
ANISOU 1141  OH  TYR A 163     4724   5018   4888     51    138    -22       O  
ATOM   1142  N   ASP A 164      86.508  94.606  26.119  1.00 33.79           N  
ANISOU 1142  N   ASP A 164     4015   4442   4381    112    135      7       N  
ATOM   1143  CA  ASP A 164      85.212  95.160  26.572  1.00 34.76           C  
ANISOU 1143  CA  ASP A 164     4125   4570   4511    125    154      6       C  
ATOM   1144  C   ASP A 164      83.994  94.583  25.866  1.00 34.86           C  
ANISOU 1144  C   ASP A 164     4108   4605   4531    127    156     14       C  
ATOM   1145  O   ASP A 164      82.921  94.627  26.400  1.00 33.53           O  
ANISOU 1145  O   ASP A 164     3928   4445   4367    132    172     12       O  
ATOM   1146  CB  ASP A 164      85.197  96.695  26.467  1.00 36.49           C  
ANISOU 1146  CB  ASP A 164     4348   4776   4742    146    162      5       C  
ATOM   1147  CG  ASP A 164      86.146  97.366  27.462  1.00 37.78           C  
ANISOU 1147  CG  ASP A 164     4540   4917   4897    144    167     -8       C  
ATOM   1148  OD1 ASP A 164      86.572  96.719  28.422  1.00 41.72           O  
ANISOU 1148  OD1 ASP A 164     5056   5416   5380    129    168    -16       O  
ATOM   1149  OD2 ASP A 164      86.480  98.557  27.311  1.00 42.26           O  
ANISOU 1149  OD2 ASP A 164     5115   5468   5473    156    170     -9       O  
ATOM   1150  N   TYR A 165      84.153  94.044  24.659  1.00 35.91           N  
ANISOU 1150  N   TYR A 165     4227   4749   4667    121    138     22       N  
ATOM   1151  CA  TYR A 165      83.050  93.472  23.924  1.00 34.19           C  
ANISOU 1151  CA  TYR A 165     3981   4555   4456    119    137     28       C  
ATOM   1152  C   TYR A 165      82.604  92.175  24.572  1.00 34.36           C  
ANISOU 1152  C   TYR A 165     3999   4585   4470    101    144     23       C  
ATOM   1153  O   TYR A 165      81.412  91.842  24.567  1.00 35.18           O  
ANISOU 1153  O   TYR A 165     4081   4707   4580    101    153     24       O  
ATOM   1154  CB  TYR A 165      83.459  93.250  22.463  1.00 34.83           C  
ANISOU 1154  CB  TYR A 165     4051   4645   4539    116    116     37       C  
ATOM   1155  CG  TYR A 165      82.523  92.356  21.653  1.00 34.25           C  
ANISOU 1155  CG  TYR A 165     3949   4598   4468    107    111     40       C  
ATOM   1156  CD1 TYR A 165      81.359  92.859  21.079  1.00 34.62           C  
ANISOU 1156  CD1 TYR A 165     3967   4663   4524    120    113     48       C  
ATOM   1157  CD2 TYR A 165      82.827  91.008  21.450  1.00 34.22           C  
ANISOU 1157  CD2 TYR A 165     3947   4600   4457     84    103     35       C  
ATOM   1158  CE1 TYR A 165      80.518  92.029  20.330  1.00 35.31           C  
ANISOU 1158  CE1 TYR A 165     4027   4777   4612    110    106     51       C  
ATOM   1159  CE2 TYR A 165      81.985  90.177  20.760  1.00 35.20           C  
ANISOU 1159  CE2 TYR A 165     4046   4747   4582     73     99     36       C  
ATOM   1160  CZ  TYR A 165      80.852  90.699  20.172  1.00 35.76           C  
ANISOU 1160  CZ  TYR A 165     4088   4838   4660     85     99     43       C  
ATOM   1161  OH  TYR A 165      80.072  89.863  19.437  1.00 39.28           O  
ANISOU 1161  OH  TYR A 165     4509   5309   5108     71     93     42       O  
ATOM   1162  N   LEU A 166      83.565  91.419  25.079  1.00 32.48           N  
ANISOU 1162  N   LEU A 166     3783   4337   4221     86    140     18       N  
ATOM   1163  CA  LEU A 166      83.313  90.182  25.819  1.00 31.11           C  
ANISOU 1163  CA  LEU A 166     3613   4168   4041     68    148     14       C  
ATOM   1164  C   LEU A 166      82.689  90.512  27.163  1.00 31.62           C  
ANISOU 1164  C   LEU A 166     3683   4229   4101     73    170      9       C  
ATOM   1165  O   LEU A 166      82.949  91.565  27.767  1.00 31.32           O  
ANISOU 1165  O   LEU A 166     3660   4180   4062     86    177      5       O  
ATOM   1166  CB  LEU A 166      84.629  89.395  26.085  1.00 29.13           C  
ANISOU 1166  CB  LEU A 166     3385   3904   3779     53    138     13       C  
ATOM   1167  CG  LEU A 166      85.377  88.972  24.816  1.00 29.45           C  
ANISOU 1167  CG  LEU A 166     3422   3945   3822     46    118     16       C  
ATOM   1168  CD1 LEU A 166      86.795  88.475  25.144  1.00 28.63           C  
ANISOU 1168  CD1 LEU A 166     3343   3826   3710     37    110     16       C  
ATOM   1169  CD2 LEU A 166      84.512  87.940  24.039  1.00 29.82           C  
ANISOU 1169  CD2 LEU A 166     3445   4010   3875     34    117     17       C  
ATOM   1170  N   SER A 167      81.959  89.543  27.673  1.00 30.52           N  
ANISOU 1170  N   SER A 167     3536   4100   3960     62    182      8       N  
ATOM   1171  CA  SER A 167      81.425  89.639  29.025  1.00 31.58           C  
ANISOU 1171  CA  SER A 167     3679   4232   4088     63    204      4       C  
ATOM   1172  C   SER A 167      82.499  89.177  29.996  1.00 32.53           C  
ANISOU 1172  C   SER A 167     3829   4338   4190     53    203      1       C  
ATOM   1173  O   SER A 167      83.449  88.454  29.622  1.00 30.90           O  
ANISOU 1173  O   SER A 167     3632   4127   3980     41    187      4       O  
ATOM   1174  CB  SER A 167      80.180  88.739  29.162  1.00 30.72           C  
ANISOU 1174  CB  SER A 167     3548   4139   3984     54    218      5       C  
ATOM   1175  OG  SER A 167      80.556  87.367  29.183  1.00 29.61           O  
ANISOU 1175  OG  SER A 167     3413   3999   3838     33    213      7       O  
ATOM   1176  N   LYS A 168      82.326  89.550  31.256  1.00 33.64           N  
ANISOU 1176  N   LYS A 168     3985   4475   4321     57    220     -4       N  
ATOM   1177  CA  LYS A 168      83.230  89.080  32.311  1.00 35.08           C  
ANISOU 1177  CA  LYS A 168     4195   4649   4485     46    221     -6       C  
ATOM   1178  C   LYS A 168      83.280  87.536  32.475  1.00 32.67           C  
ANISOU 1178  C   LYS A 168     3890   4349   4175     28    221      2       C  
ATOM   1179  O   LYS A 168      84.363  86.948  32.693  1.00 29.74           O  
ANISOU 1179  O   LYS A 168     3537   3970   3794     19    209      6       O  
ATOM   1180  CB  LYS A 168      82.864  89.717  33.630  1.00 39.82           C  
ANISOU 1180  CB  LYS A 168     4809   5247   5072     53    241    -14       C  
ATOM   1181  CG  LYS A 168      83.746  89.201  34.747  1.00 44.79           C  
ANISOU 1181  CG  LYS A 168     5466   5873   5680     42    241    -14       C  
ATOM   1182  CD  LYS A 168      83.612  89.982  36.035  1.00 52.24           C  
ANISOU 1182  CD  LYS A 168     6428   6815   6607     47    259    -24       C  
ATOM   1183  CE  LYS A 168      84.806  89.635  36.919  1.00 59.26           C  
ANISOU 1183  CE  LYS A 168     7345   7700   7472     37    250    -23       C  
ATOM   1184  NZ  LYS A 168      84.414  89.708  38.356  1.00 64.53           N  
ANISOU 1184  NZ  LYS A 168     8027   8372   8118     35    271    -29       N  
ATOM   1185  N   LYS A 169      82.119  86.881  32.403  1.00 29.80           N  
ANISOU 1185  N   LYS A 169     3506   3996   3819     22    234      4       N  
ATOM   1186  CA  LYS A 169      82.096  85.434  32.398  1.00 29.88           C  
ANISOU 1186  CA  LYS A 169     3514   4009   3830      4    236     11       C  
ATOM   1187  C   LYS A 169      82.922  84.803  31.228  1.00 28.91           C  
ANISOU 1187  C   LYS A 169     3388   3881   3714     -5    213     14       C  
ATOM   1188  O   LYS A 169      83.620  83.794  31.422  1.00 28.08           O  
ANISOU 1188  O   LYS A 169     3296   3769   3605    -17    210     20       O  
ATOM   1189  CB  LYS A 169      80.654  84.963  32.371  1.00 30.65           C  
ANISOU 1189  CB  LYS A 169     3586   4120   3938     -1    253     11       C  
ATOM   1190  CG  LYS A 169      80.448  83.460  32.354  1.00 31.14           C  
ANISOU 1190  CG  LYS A 169     3643   4184   4004    -21    259     16       C  
ATOM   1191  CD  LYS A 169      78.916  83.237  32.238  1.00 32.11           C  
ANISOU 1191  CD  LYS A 169     3738   4323   4141    -25    276     14       C  
ATOM   1192  CE  LYS A 169      78.641  81.753  32.330  1.00 31.96           C  
ANISOU 1192  CE  LYS A 169     3715   4304   4126    -46    285     19       C  
ATOM   1193  NZ  LYS A 169      77.206  81.449  32.581  1.00 33.01           N  
ANISOU 1193  NZ  LYS A 169     3824   4450   4269    -52    307     18       N  
ATOM   1194  N   GLU A 170      82.823  85.394  30.036  1.00 29.70           N  
ANISOU 1194  N   GLU A 170     3472   3986   3827      3    200     12       N  
ATOM   1195  CA  GLU A 170      83.571  84.935  28.853  1.00 29.55           C  
ANISOU 1195  CA  GLU A 170     3450   3964   3814     -4    180     14       C  
ATOM   1196  C   GLU A 170      85.082  85.122  29.011  1.00 28.77           C  
ANISOU 1196  C   GLU A 170     3377   3850   3706     -2    166     16       C  
ATOM   1197  O   GLU A 170      85.844  84.199  28.746  1.00 29.23           O  
ANISOU 1197  O   GLU A 170     3442   3901   3764    -14    158     20       O  
ATOM   1198  CB  GLU A 170      83.083  85.648  27.611  1.00 31.25           C  
ANISOU 1198  CB  GLU A 170     3643   4190   4041      5    170     12       C  
ATOM   1199  CG  GLU A 170      81.681  85.195  27.178  1.00 31.81           C  
ANISOU 1199  CG  GLU A 170     3684   4278   4122     -1    180     11       C  
ATOM   1200  CD  GLU A 170      81.019  86.152  26.186  1.00 32.51           C  
ANISOU 1200  CD  GLU A 170     3749   4381   4221     13    172     11       C  
ATOM   1201  OE1 GLU A 170      81.455  87.286  26.001  1.00 34.14           O  
ANISOU 1201  OE1 GLU A 170     3963   4582   4428     30    165     13       O  
ATOM   1202  OE2 GLU A 170      80.071  85.750  25.551  1.00 36.41           O  
ANISOU 1202  OE2 GLU A 170     4218   4893   4724      7    173     11       O  
ATOM   1203  N   ARG A 171      85.487  86.292  29.481  1.00 28.44           N  
ANISOU 1203  N   ARG A 171     3347   3801   3656     11    165     13       N  
ATOM   1204  CA  ARG A 171      86.905  86.568  29.746  1.00 30.12           C  
ANISOU 1204  CA  ARG A 171     3582   4001   3859     12    151     14       C  
ATOM   1205  C   ARG A 171      87.456  85.600  30.776  1.00 30.48           C  
ANISOU 1205  C   ARG A 171     3646   4042   3892      1    156     19       C  
ATOM   1206  O   ARG A 171      88.511  85.023  30.557  1.00 29.30           O  
ANISOU 1206  O   ARG A 171     3506   3885   3741     -5    143     25       O  
ATOM   1207  CB  ARG A 171      87.127  88.008  30.227  1.00 28.95           C  
ANISOU 1207  CB  ARG A 171     3446   3848   3707     27    152      7       C  
ATOM   1208  CG  ARG A 171      86.748  89.028  29.197  1.00 30.37           C  
ANISOU 1208  CG  ARG A 171     3610   4029   3899     40    148      5       C  
ATOM   1209  CD  ARG A 171      87.412  90.356  29.460  1.00 31.69           C  
ANISOU 1209  CD  ARG A 171     3792   4185   4064     52    144     -1       C  
ATOM   1210  NE  ARG A 171      86.907  90.876  30.720  1.00 33.84           N  
ANISOU 1210  NE  ARG A 171     4074   4457   4327     57    162     -8       N  
ATOM   1211  CZ  ARG A 171      85.820  91.636  30.848  1.00 35.76           C  
ANISOU 1211  CZ  ARG A 171     4306   4704   4578     69    178    -12       C  
ATOM   1212  NH1 ARG A 171      85.112  92.031  29.779  1.00 36.30           N  
ANISOU 1212  NH1 ARG A 171     4352   4779   4663     79    177     -8       N  
ATOM   1213  NH2 ARG A 171      85.450  92.025  32.067  1.00 36.29           N  
ANISOU 1213  NH2 ARG A 171     4385   4770   4635     72    197    -20       N  
ATOM   1214  N   LYS A 172      86.715  85.375  31.867  1.00 30.45           N  
ANISOU 1214  N   LYS A 172     3646   4044   3880     -1    174     19       N  
ATOM   1215  CA  LYS A 172      87.180  84.446  32.883  1.00 32.83           C  
ANISOU 1215  CA  LYS A 172     3964   4343   4168    -11    179     27       C  
ATOM   1216  C   LYS A 172      87.467  83.043  32.320  1.00 31.32           C  
ANISOU 1216  C   LYS A 172     3768   4147   3986    -24    175     36       C  
ATOM   1217  O   LYS A 172      88.509  82.463  32.615  1.00 30.38           O  
ANISOU 1217  O   LYS A 172     3663   4019   3860    -28    167     44       O  
ATOM   1218  CB  LYS A 172      86.224  84.374  34.096  1.00 38.45           C  
ANISOU 1218  CB  LYS A 172     4679   5062   4869    -11    203     26       C  
ATOM   1219  CG  LYS A 172      86.840  83.581  35.240  1.00 45.47           C  
ANISOU 1219  CG  LYS A 172     5588   5948   5740    -19    207     36       C  
ATOM   1220  CD  LYS A 172      85.932  83.267  36.419  1.00 52.06           C  
ANISOU 1220  CD  LYS A 172     6427   6791   6563    -22    231     38       C  
ATOM   1221  CE  LYS A 172      85.637  84.491  37.281  1.00 56.79           C  
ANISOU 1221  CE  LYS A 172     7036   7395   7147    -12    240     27       C  
ATOM   1222  NZ  LYS A 172      85.085  84.054  38.603  1.00 60.19           N  
ANISOU 1222  NZ  LYS A 172     7477   7833   7560    -17    262     31       N  
ATOM   1223  N   GLN A 173      86.551  82.490  31.520  1.00 28.41           N  
ANISOU 1223  N   GLN A 173     3378   3783   3632    -30    181     34       N  
ATOM   1224  CA  GLN A 173      86.782  81.170  30.923  1.00 28.17           C  
ANISOU 1224  CA  GLN A 173     3343   3748   3613    -44    179     40       C  
ATOM   1225  C   GLN A 173      87.984  81.162  29.925  1.00 27.45           C  
ANISOU 1225  C   GLN A 173     3256   3648   3527    -44    158     41       C  
ATOM   1226  O   GLN A 173      88.839  80.273  29.944  1.00 27.12           O  
ANISOU 1226  O   GLN A 173     3223   3595   3485    -51    154     49       O  
ATOM   1227  CB  GLN A 173      85.510  80.712  30.228  1.00 27.58           C  
ANISOU 1227  CB  GLN A 173     3244   3684   3553    -52    189     35       C  
ATOM   1228  CG  GLN A 173      85.585  79.308  29.669  1.00 27.48           C  
ANISOU 1228  CG  GLN A 173     3226   3665   3552    -69    191     38       C  
ATOM   1229  CD  GLN A 173      85.610  78.217  30.715  1.00 27.00           C  
ANISOU 1229  CD  GLN A 173     3177   3596   3486    -79    207     49       C  
ATOM   1230  OE1 GLN A 173      85.269  78.419  31.912  1.00 29.36           O  
ANISOU 1230  OE1 GLN A 173     3485   3897   3772    -75    221     53       O  
ATOM   1231  NE2 GLN A 173      85.949  77.025  30.263  1.00 26.05           N  
ANISOU 1231  NE2 GLN A 173     3057   3465   3377    -92    209     52       N  
ATOM   1232  N   LEU A 174      88.068  82.163  29.063  1.00 27.20           N  
ANISOU 1232  N   LEU A 174     3216   3620   3500    -34    146     34       N  
ATOM   1233  CA  LEU A 174      89.224  82.239  28.142  1.00 27.71           C  
ANISOU 1233  CA  LEU A 174     3284   3675   3568    -33    127     35       C  
ATOM   1234  C   LEU A 174      90.540  82.297  28.890  1.00 28.02           C  
ANISOU 1234  C   LEU A 174     3346   3704   3596    -30    119     41       C  
ATOM   1235  O   LEU A 174      91.503  81.615  28.525  1.00 28.24           O  
ANISOU 1235  O   LEU A 174     3379   3722   3628    -35    110     47       O  
ATOM   1236  CB  LEU A 174      89.114  83.452  27.197  1.00 27.10           C  
ANISOU 1236  CB  LEU A 174     3197   3604   3496    -22    116     28       C  
ATOM   1237  CG  LEU A 174      87.981  83.297  26.215  1.00 27.85           C  
ANISOU 1237  CG  LEU A 174     3267   3712   3602    -25    119     23       C  
ATOM   1238  CD1 LEU A 174      87.866  84.585  25.424  1.00 28.89           C  
ANISOU 1238  CD1 LEU A 174     3391   3851   3737    -11    109     20       C  
ATOM   1239  CD2 LEU A 174      88.095  82.118  25.249  1.00 28.12           C  
ANISOU 1239  CD2 LEU A 174     3293   3746   3645    -40    115     22       C  
ATOM   1240  N   GLU A 175      90.579  83.130  29.932  1.00 28.43           N  
ANISOU 1240  N   GLU A 175     3410   3758   3635    -22    122     40       N  
ATOM   1241  CA  GLU A 175      91.792  83.295  30.739  1.00 29.11           C  
ANISOU 1241  CA  GLU A 175     3516   3837   3708    -20    113     46       C  
ATOM   1242  C   GLU A 175      92.192  82.035  31.509  1.00 29.69           C  
ANISOU 1242  C   GLU A 175     3600   3907   3776    -29    118     59       C  
ATOM   1243  O   GLU A 175      93.379  81.649  31.523  1.00 27.40           O  
ANISOU 1243  O   GLU A 175     3319   3608   3484    -30    107     67       O  
ATOM   1244  CB  GLU A 175      91.644  84.498  31.671  1.00 29.75           C  
ANISOU 1244  CB  GLU A 175     3607   3922   3774    -11    116     38       C  
ATOM   1245  CG  GLU A 175      91.617  85.785  30.867  1.00 29.45           C  
ANISOU 1245  CG  GLU A 175     3562   3883   3744     -1    109     28       C  
ATOM   1246  CD  GLU A 175      91.540  87.040  31.691  1.00 30.70           C  
ANISOU 1246  CD  GLU A 175     3731   4042   3891      7    113     19       C  
ATOM   1247  OE1 GLU A 175      91.657  86.957  32.894  1.00 33.47           O  
ANISOU 1247  OE1 GLU A 175     4096   4395   4225      5    119     20       O  
ATOM   1248  OE2 GLU A 175      91.389  88.142  31.119  1.00 32.43           O  
ANISOU 1248  OE2 GLU A 175     3945   4259   4118     17    110     12       O  
ATOM   1249  N   LYS A 176      91.208  81.395  32.129  1.00 29.55           N  
ANISOU 1249  N   LYS A 176     3579   3894   3755    -35    136     61       N  
ATOM   1250  CA  LYS A 176      91.445  80.176  32.865  1.00 31.74           C  
ANISOU 1250  CA  LYS A 176     3865   4167   4028    -42    145     76       C  
ATOM   1251  C   LYS A 176      91.791  78.964  31.997  1.00 29.96           C  
ANISOU 1251  C   LYS A 176     3633   3930   3820    -51    143     82       C  
ATOM   1252  O   LYS A 176      92.633  78.135  32.351  1.00 28.67           O  
ANISOU 1252  O   LYS A 176     3480   3758   3656    -54    141     96       O  
ATOM   1253  CB  LYS A 176      90.241  79.870  33.795  1.00 35.76           C  
ANISOU 1253  CB  LYS A 176     4373   4684   4530    -46    167     77       C  
ATOM   1254  CG  LYS A 176      90.383  78.563  34.584  1.00 39.23           C  
ANISOU 1254  CG  LYS A 176     4821   5118   4965    -55    178     94       C  
ATOM   1255  CD  LYS A 176      89.299  78.354  35.645  1.00 44.41           C  
ANISOU 1255  CD  LYS A 176     5480   5783   5611    -58    201     97       C  
ATOM   1256  CE  LYS A 176      87.902  78.103  35.106  1.00 45.66           C  
ANISOU 1256  CE  LYS A 176     5618   5945   5785    -65    217     88       C  
ATOM   1257  NZ  LYS A 176      87.589  76.665  34.931  1.00 49.55           N  
ANISOU 1257  NZ  LYS A 176     6105   6430   6293    -78    231     98       N  
ATOM   1258  N   ASN A 177      91.115  78.806  30.882  1.00 31.43           N  
ANISOU 1258  N   ASN A 177     3801   4117   4022    -56    145     73       N  
ATOM   1259  CA  ASN A 177      91.273  77.588  30.084  1.00 33.30           C  
ANISOU 1259  CA  ASN A 177     4032   4344   4276    -67    148     76       C  
ATOM   1260  C   ASN A 177      92.063  77.694  28.803  1.00 30.10           C  
ANISOU 1260  C   ASN A 177     3622   3932   3882    -66    133     71       C  
ATOM   1261  O   ASN A 177      92.321  76.671  28.197  1.00 26.76           O  
ANISOU 1261  O   ASN A 177     3196   3499   3471    -75    136     73       O  
ATOM   1262  CB  ASN A 177      89.909  77.027  29.754  1.00 39.34           C  
ANISOU 1262  CB  ASN A 177     4781   5114   5051    -78    165     69       C  
ATOM   1263  CG  ASN A 177      89.495  75.981  30.725  1.00 47.16           C  
ANISOU 1263  CG  ASN A 177     5777   6100   6041    -86    184     80       C  
ATOM   1264  OD1 ASN A 177      89.307  74.821  30.359  1.00 59.22           O  
ANISOU 1264  OD1 ASN A 177     7300   7618   7582    -99    194     83       O  
ATOM   1265  ND2 ASN A 177      89.418  76.356  31.982  1.00 48.94           N  
ANISOU 1265  ND2 ASN A 177     6015   6332   6250    -80    190     88       N  
ATOM   1266  N   LEU A 178      92.366  78.910  28.355  1.00 26.47           N  
ANISOU 1266  N   LEU A 178     3161   3478   3418    -56    118     64       N  
ATOM   1267  CA  LEU A 178      93.184  79.090  27.172  1.00 27.18           C  
ANISOU 1267  CA  LEU A 178     3247   3563   3516    -55    103     60       C  
ATOM   1268  C   LEU A 178      94.444  79.922  27.501  1.00 26.75           C  
ANISOU 1268  C   LEU A 178     3206   3505   3454    -44     88     64       C  
ATOM   1269  O   LEU A 178      95.534  79.394  27.442  1.00 25.26           O  
ANISOU 1269  O   LEU A 178     3025   3306   3268    -45     82     72       O  
ATOM   1270  CB  LEU A 178      92.374  79.726  26.039  1.00 27.27           C  
ANISOU 1270  CB  LEU A 178     3242   3586   3535    -54    100     47       C  
ATOM   1271  CG  LEU A 178      93.116  80.087  24.737  1.00 27.49           C  
ANISOU 1271  CG  LEU A 178     3265   3611   3569    -51     85     42       C  
ATOM   1272  CD1 LEU A 178      93.638  78.833  24.052  1.00 28.05           C  
ANISOU 1272  CD1 LEU A 178     3335   3671   3651    -63     87     43       C  
ATOM   1273  CD2 LEU A 178      92.178  80.886  23.835  1.00 27.63           C  
ANISOU 1273  CD2 LEU A 178     3265   3644   3589    -48     82     32       C  
ATOM   1274  N   PHE A 179      94.287  81.195  27.855  1.00 27.18           N  
ANISOU 1274  N   PHE A 179     3263   3567   3498    -35     83     59       N  
ATOM   1275  CA  PHE A 179      95.491  82.090  27.988  1.00 27.74           C  
ANISOU 1275  CA  PHE A 179     3344   3633   3562    -26     67     60       C  
ATOM   1276  C   PHE A 179      96.502  81.758  29.069  1.00 28.12           C  
ANISOU 1276  C   PHE A 179     3407   3676   3599    -26     63     71       C  
ATOM   1277  O   PHE A 179      97.729  81.755  28.768  1.00 27.32           O  
ANISOU 1277  O   PHE A 179     3310   3568   3501    -25     50     76       O  
ATOM   1278  CB  PHE A 179      95.094  83.546  28.082  1.00 27.48           C  
ANISOU 1278  CB  PHE A 179     3311   3607   3524    -17     64     50       C  
ATOM   1279  CG  PHE A 179      94.369  84.045  26.859  1.00 27.93           C  
ANISOU 1279  CG  PHE A 179     3351   3668   3591    -14     64     42       C  
ATOM   1280  CD1 PHE A 179      94.918  83.865  25.583  1.00 28.96           C  
ANISOU 1280  CD1 PHE A 179     3475   3795   3733    -16     54     42       C  
ATOM   1281  CD2 PHE A 179      93.134  84.687  26.965  1.00 28.77           C  
ANISOU 1281  CD2 PHE A 179     3449   3785   3697     -9     73     35       C  
ATOM   1282  CE1 PHE A 179      94.266  84.302  24.448  1.00 30.51           C  
ANISOU 1282  CE1 PHE A 179     3656   3999   3937    -13     53     36       C  
ATOM   1283  CE2 PHE A 179      92.468  85.154  25.818  1.00 28.82           C  
ANISOU 1283  CE2 PHE A 179     3439   3799   3714     -5     71     30       C  
ATOM   1284  CZ  PHE A 179      93.040  84.959  24.558  1.00 29.73           C  
ANISOU 1284  CZ  PHE A 179     3548   3911   3837     -8     60     31       C  
ATOM   1285  N   ARG A 180      96.041  81.497  30.305  1.00 29.00           N  
ANISOU 1285  N   ARG A 180     3528   3793   3698    -28     73     76       N  
ATOM   1286  CA  ARG A 180      96.991  81.156  31.406  1.00 30.55           C  
ANISOU 1286  CA  ARG A 180     3738   3988   3880    -28     68     89       C  
ATOM   1287  C   ARG A 180      97.699  79.837  31.191  1.00 28.36           C  
ANISOU 1287  C   ARG A 180     3461   3701   3613    -32     68    104       C  
ATOM   1288  O   ARG A 180      98.892  79.769  31.387  1.00 26.12           O  
ANISOU 1288  O   ARG A 180     3183   3413   3327    -29     55    113       O  
ATOM   1289  CB  ARG A 180      96.415  81.215  32.815  1.00 32.16           C  
ANISOU 1289  CB  ARG A 180     3953   4202   4066    -28     78     92       C  
ATOM   1290  CG  ARG A 180      96.064  82.605  33.233  1.00 36.36           C  
ANISOU 1290  CG  ARG A 180     4489   4742   4585    -23     77     78       C  
ATOM   1291  CD  ARG A 180      95.252  82.635  34.536  1.00 39.72           C  
ANISOU 1291  CD  ARG A 180     4922   5177   4991    -24     92     78       C  
ATOM   1292  NE  ARG A 180      94.772  83.997  34.726  1.00 43.24           N  
ANISOU 1292  NE  ARG A 180     5371   5629   5431    -18     94     61       N  
ATOM   1293  CZ  ARG A 180      95.538  84.999  35.135  1.00 43.72           C  
ANISOU 1293  CZ  ARG A 180     5441   5690   5479    -15     83     54       C  
ATOM   1294  NH1 ARG A 180      96.783  84.770  35.476  1.00 45.13           N  
ANISOU 1294  NH1 ARG A 180     5629   5868   5649    -18     67     62       N  
ATOM   1295  NH2 ARG A 180      95.055  86.226  35.250  1.00 45.66           N  
ANISOU 1295  NH2 ARG A 180     5690   5938   5723    -10     87     37       N  
ATOM   1296  N   PRO A 181      96.970  78.793  30.794  1.00 28.16           N  
ANISOU 1296  N   PRO A 181     3429   3671   3601    -39     82    106       N  
ATOM   1297  CA  PRO A 181      97.673  77.554  30.481  1.00 28.97           C  
ANISOU 1297  CA  PRO A 181     3531   3760   3717    -43     84    120       C  
ATOM   1298  C   PRO A 181      98.641  77.672  29.285  1.00 27.89           C  
ANISOU 1298  C   PRO A 181     3389   3614   3594    -41     71    116       C  
ATOM   1299  O   PRO A 181      99.658  77.011  29.278  1.00 25.95           O  
ANISOU 1299  O   PRO A 181     3147   3359   3355    -39     67    129       O  
ATOM   1300  CB  PRO A 181      96.534  76.563  30.140  1.00 29.40           C  
ANISOU 1300  CB  PRO A 181     3577   3810   3783    -53    103    117       C  
ATOM   1301  CG  PRO A 181      95.361  77.099  30.874  1.00 29.96           C  
ANISOU 1301  CG  PRO A 181     3648   3895   3842    -53    113    111       C  
ATOM   1302  CD  PRO A 181      95.516  78.599  30.877  1.00 29.79           C  
ANISOU 1302  CD  PRO A 181     3628   3883   3809    -44     99    100       C  
ATOM   1303  N   PHE A 182      98.241  78.424  28.252  1.00 26.63           N  
ANISOU 1303  N   PHE A 182     3219   3458   3440    -40     66    100       N  
ATOM   1304  CA  PHE A 182      99.096  78.668  27.088  1.00 26.23           C  
ANISOU 1304  CA  PHE A 182     3164   3401   3400    -38     55     96       C  
ATOM   1305  C   PHE A 182     100.392  79.351  27.557  1.00 24.89           C  
ANISOU 1305  C   PHE A 182     3003   3232   3224    -31     38    103       C  
ATOM   1306  O   PHE A 182     101.494  78.895  27.251  1.00 23.76           O  
ANISOU 1306  O   PHE A 182     2860   3079   3088    -29     32    111       O  
ATOM   1307  CB  PHE A 182      98.315  79.510  26.042  1.00 26.36           C  
ANISOU 1307  CB  PHE A 182     3170   3426   3421    -38     53     79       C  
ATOM   1308  CG  PHE A 182      98.814  79.395  24.630  1.00 26.82           C  
ANISOU 1308  CG  PHE A 182     3219   3478   3492    -40     48     74       C  
ATOM   1309  CD1 PHE A 182     100.014  79.961  24.265  1.00 27.24           C  
ANISOU 1309  CD1 PHE A 182     3276   3528   3547    -34     34     76       C  
ATOM   1310  CD2 PHE A 182      98.029  78.797  23.625  1.00 27.02           C  
ANISOU 1310  CD2 PHE A 182     3235   3506   3528    -48     56     65       C  
ATOM   1311  CE1 PHE A 182     100.472  79.912  22.963  1.00 26.82           C  
ANISOU 1311  CE1 PHE A 182     3216   3469   3504    -35     30     71       C  
ATOM   1312  CE2 PHE A 182      98.493  78.711  22.319  1.00 27.46           C  
ANISOU 1312  CE2 PHE A 182     3283   3557   3592    -51     51     59       C  
ATOM   1313  CZ  PHE A 182      99.718  79.291  21.969  1.00 27.75           C  
ANISOU 1313  CZ  PHE A 182     3324   3589   3630    -43     39     62       C  
ATOM   1314  N   ALA A 183     100.250  80.424  28.331  1.00 24.27           N  
ANISOU 1314  N   ALA A 183     2929   3162   3129    -26     33     98       N  
ATOM   1315  CA  ALA A 183     101.416  81.186  28.757  1.00 24.94           C  
ANISOU 1315  CA  ALA A 183     3022   3249   3206    -21     17    101       C  
ATOM   1316  C   ALA A 183     102.368  80.334  29.609  1.00 25.80           C  
ANISOU 1316  C   ALA A 183     3137   3355   3311    -21     13    120       C  
ATOM   1317  O   ALA A 183     103.566  80.443  29.455  1.00 25.36           O  
ANISOU 1317  O   ALA A 183     3082   3296   3259    -18      0    126       O  
ATOM   1318  CB  ALA A 183     101.003  82.449  29.475  1.00 24.39           C  
ANISOU 1318  CB  ALA A 183     2958   3189   3120    -18     14     91       C  
ATOM   1319  N   ASP A 184     101.817  79.431  30.427  1.00 25.45           N  
ANISOU 1319  N   ASP A 184     3098   3312   3261    -24     25    130       N  
ATOM   1320  CA  ASP A 184     102.621  78.534  31.215  1.00 27.11           C  
ANISOU 1320  CA  ASP A 184     3314   3520   3468    -22     23    151       C  
ATOM   1321  C   ASP A 184     103.336  77.521  30.405  1.00 27.40           C  
ANISOU 1321  C   ASP A 184     3344   3541   3525    -22     25    161       C  
ATOM   1322  O   ASP A 184     104.497  77.185  30.737  1.00 26.12           O  
ANISOU 1322  O   ASP A 184     3184   3377   3364    -17     15    177       O  
ATOM   1323  CB  ASP A 184     101.783  77.803  32.300  1.00 29.25           C  
ANISOU 1323  CB  ASP A 184     3591   3795   3726    -25     38    161       C  
ATOM   1324  CG  ASP A 184     101.476  78.703  33.495  1.00 31.70           C  
ANISOU 1324  CG  ASP A 184     3912   4122   4011    -24     35    157       C  
ATOM   1325  OD1 ASP A 184     101.991  79.857  33.594  1.00 30.49           O  
ANISOU 1325  OD1 ASP A 184     3760   3976   3847    -22     20    147       O  
ATOM   1326  OD2 ASP A 184     100.715  78.230  34.344  1.00 34.62           O  
ANISOU 1326  OD2 ASP A 184     4288   4498   4370    -27     48    164       O  
ATOM   1327  N   TYR A 185     102.657  77.014  29.370  1.00 27.32           N  
ANISOU 1327  N   TYR A 185     3327   3523   3533    -27     37    152       N  
ATOM   1328  CA  TYR A 185     103.223  75.973  28.500  1.00 26.59           C  
ANISOU 1328  CA  TYR A 185     3228   3413   3461    -28     43    158       C  
ATOM   1329  C   TYR A 185     104.482  76.466  27.784  1.00 25.62           C  
ANISOU 1329  C   TYR A 185     3102   3287   3347    -23     28    158       C  
ATOM   1330  O   TYR A 185     105.455  75.724  27.706  1.00 24.41           O  
ANISOU 1330  O   TYR A 185     2947   3123   3204    -19     27    172       O  
ATOM   1331  CB  TYR A 185     102.206  75.413  27.508  1.00 26.78           C  
ANISOU 1331  CB  TYR A 185     3245   3430   3500    -36     59    145       C  
ATOM   1332  CG  TYR A 185     102.771  74.274  26.705  1.00 28.06           C  
ANISOU 1332  CG  TYR A 185     3404   3575   3684    -39     68    150       C  
ATOM   1333  CD1 TYR A 185     102.783  72.955  27.217  1.00 29.31           C  
ANISOU 1333  CD1 TYR A 185     3566   3719   3851    -41     83    166       C  
ATOM   1334  CD2 TYR A 185     103.371  74.500  25.449  1.00 28.28           C  
ANISOU 1334  CD2 TYR A 185     3425   3597   3723    -39     62    140       C  
ATOM   1335  CE1 TYR A 185     103.372  71.898  26.483  1.00 29.44           C  
ANISOU 1335  CE1 TYR A 185     3580   3716   3890    -42     93    171       C  
ATOM   1336  CE2 TYR A 185     103.968  73.469  24.726  1.00 28.95           C  
ANISOU 1336  CE2 TYR A 185     3508   3664   3828    -40     71    144       C  
ATOM   1337  CZ  TYR A 185     103.961  72.159  25.235  1.00 29.74           C  
ANISOU 1337  CZ  TYR A 185     3611   3749   3939    -42     87    158       C  
ATOM   1338  OH  TYR A 185     104.555  71.123  24.506  1.00 28.65           O  
ANISOU 1338  OH  TYR A 185     3471   3591   3823    -43     99    161       O  
ATOM   1339  N   ILE A 186     104.448  77.704  27.274  1.00 24.42           N  
ANISOU 1339  N   ILE A 186     2947   3143   3190    -22     17    142       N  
ATOM   1340  CA  ILE A 186     105.598  78.267  26.556  1.00 25.23           C  
ANISOU 1340  CA  ILE A 186     3045   3242   3299    -18      3    140       C  
ATOM   1341  C   ILE A 186     106.664  78.842  27.490  1.00 25.69           C  
ANISOU 1341  C   ILE A 186     3107   3307   3346    -12    -13    151       C  
ATOM   1342  O   ILE A 186     107.654  79.365  27.015  1.00 27.22           O  
ANISOU 1342  O   ILE A 186     3297   3499   3546    -10    -25    150       O  
ATOM   1343  CB  ILE A 186     105.202  79.311  25.486  1.00 24.20           C  
ANISOU 1343  CB  ILE A 186     2909   3115   3170    -19      0    121       C  
ATOM   1344  CG1 ILE A 186     104.550  80.509  26.130  1.00 23.47           C  
ANISOU 1344  CG1 ILE A 186     2821   3036   3061    -17     -6    112       C  
ATOM   1345  CG2 ILE A 186     104.322  78.638  24.434  1.00 25.70           C  
ANISOU 1345  CG2 ILE A 186     3092   3300   3372    -25     14    112       C  
ATOM   1346  CD1 ILE A 186     104.288  81.654  25.177  1.00 23.90           C  
ANISOU 1346  CD1 ILE A 186     2871   3093   3118    -16    -10     97       C  
ATOM   1347  N   SER A 187     106.460  78.753  28.806  1.00 26.07           N  
ANISOU 1347  N   SER A 187     3164   3365   3378    -12    -14    160       N  
ATOM   1348  CA  SER A 187     107.393  79.326  29.786  1.00 26.80           C  
ANISOU 1348  CA  SER A 187     3260   3467   3455     -9    -31    168       C  
ATOM   1349  C   SER A 187     107.805  78.288  30.834  1.00 27.39           C  
ANISOU 1349  C   SER A 187     3339   3544   3524     -6    -30    192       C  
ATOM   1350  O   SER A 187     108.808  77.554  30.638  1.00 26.99           O  
ANISOU 1350  O   SER A 187     3283   3486   3487     -1    -34    209       O  
ATOM   1351  CB  SER A 187     106.814  80.623  30.376  1.00 27.21           C  
ANISOU 1351  CB  SER A 187     3319   3533   3487    -11    -37    153       C  
ATOM   1352  OG  SER A 187     105.639  80.437  31.168  1.00 27.19           O  
ANISOU 1352  OG  SER A 187     3323   3537   3470    -14    -25    151       O  
ATOM   1353  N   ILE A 188     107.086  78.239  31.954  1.00 28.01           N  
ANISOU 1353  N   ILE A 188     3426   3633   3582     -8    -26    196       N  
ATOM   1354  CA  ILE A 188     107.500  77.402  33.086  1.00 29.54           C  
ANISOU 1354  CA  ILE A 188     3625   3833   3766     -5    -27    220       C  
ATOM   1355  C   ILE A 188     107.533  75.901  32.753  1.00 28.19           C  
ANISOU 1355  C   ILE A 188     3451   3645   3616     -2    -11    239       C  
ATOM   1356  O   ILE A 188     108.348  75.201  33.316  1.00 26.46           O  
ANISOU 1356  O   ILE A 188     3231   3426   3397      4    -15    263       O  
ATOM   1357  CB  ILE A 188     106.721  77.630  34.427  1.00 31.03           C  
ANISOU 1357  CB  ILE A 188     3825   4037   3926     -8    -23    222       C  
ATOM   1358  CG1 ILE A 188     105.214  77.379  34.259  1.00 32.67           C  
ANISOU 1358  CG1 ILE A 188     4037   4241   4136    -12     -2    211       C  
ATOM   1359  CG2 ILE A 188     107.050  79.006  34.987  1.00 32.45           C  
ANISOU 1359  CG2 ILE A 188     4010   4235   4084    -10    -41    208       C  
ATOM   1360  CD1 ILE A 188     104.416  77.631  35.525  1.00 32.34           C  
ANISOU 1360  CD1 ILE A 188     4006   4215   4067    -15      4    211       C  
ATOM   1361  N   GLU A 189     106.742  75.456  31.797  1.00 28.18           N  
ANISOU 1361  N   GLU A 189     3446   3629   3632     -6      6    228       N  
ATOM   1362  CA  GLU A 189     106.809  74.055  31.316  1.00 31.63           C  
ANISOU 1362  CA  GLU A 189     3879   4046   4093     -4     22    241       C  
ATOM   1363  C   GLU A 189     107.871  73.769  30.270  1.00 30.24           C  
ANISOU 1363  C   GLU A 189     3694   3856   3940      0     19    243       C  
ATOM   1364  O   GLU A 189     108.140  72.605  30.027  1.00 31.15           O  
ANISOU 1364  O   GLU A 189     3807   3955   4074      3     32    257       O  
ATOM   1365  CB  GLU A 189     105.443  73.604  30.789  1.00 33.61           C  
ANISOU 1365  CB  GLU A 189     4131   4289   4352    -13     44    227       C  
ATOM   1366  CG  GLU A 189     104.415  73.552  31.917  1.00 38.32           C  
ANISOU 1366  CG  GLU A 189     4735   4896   4929    -16     52    231       C  
ATOM   1367  CD  GLU A 189     102.951  73.366  31.442  1.00 43.16           C  
ANISOU 1367  CD  GLU A 189     5346   5505   5547    -26     71    214       C  
ATOM   1368  OE1 GLU A 189     102.709  72.656  30.463  1.00 47.06           O  
ANISOU 1368  OE1 GLU A 189     5834   5984   6063    -31     84    207       O  
ATOM   1369  OE2 GLU A 189     102.036  73.915  32.076  1.00 46.09           O  
ANISOU 1369  OE2 GLU A 189     5721   5889   5901    -29     74    206       O  
ATOM   1370  N   ASN A 190     108.424  74.816  29.642  1.00 27.88           N  
ANISOU 1370  N   ASN A 190     3390   3563   3640      0      3    229       N  
ATOM   1371  CA  ASN A 190     109.528  74.701  28.649  1.00 28.97           C  
ANISOU 1371  CA  ASN A 190     3519   3690   3800      5     -1    230       C  
ATOM   1372  C   ASN A 190     110.584  75.799  28.899  1.00 27.78           C  
ANISOU 1372  C   ASN A 190     3364   3552   3639      8    -25    230       C  
ATOM   1373  O   ASN A 190     110.778  76.688  28.050  1.00 26.83           O  
ANISOU 1373  O   ASN A 190     3239   3432   3521      6    -32    213       O  
ATOM   1374  CB  ASN A 190     109.000  74.724  27.212  1.00 27.35           C  
ANISOU 1374  CB  ASN A 190     3309   3473   3609     -1     10    209       C  
ATOM   1375  CG  ASN A 190     108.306  73.438  26.857  1.00 28.53           C  
ANISOU 1375  CG  ASN A 190     3460   3607   3775     -5     33    210       C  
ATOM   1376  OD1 ASN A 190     108.985  72.452  26.642  1.00 29.50           O  
ANISOU 1376  OD1 ASN A 190     3580   3714   3916     -1     41    224       O  
ATOM   1377  ND2 ASN A 190     106.945  73.422  26.843  1.00 25.66           N  
ANISOU 1377  ND2 ASN A 190     3099   3246   3404    -14     44    197       N  
ATOM   1378  N   PRO A 191     111.210  75.747  30.092  1.00 28.53           N  
ANISOU 1378  N   PRO A 191     3462   3659   3720     13    -37    249       N  
ATOM   1379  CA  PRO A 191     112.212  76.744  30.471  1.00 28.11           C  
ANISOU 1379  CA  PRO A 191     3405   3621   3656     14    -60    250       C  
ATOM   1380  C   PRO A 191     113.421  76.723  29.519  1.00 27.39           C  
ANISOU 1380  C   PRO A 191     3301   3520   3587     19    -66    252       C  
ATOM   1381  O   PRO A 191     114.007  77.760  29.327  1.00 23.96           O  
ANISOU 1381  O   PRO A 191     2862   3093   3148     16    -81    242       O  
ATOM   1382  CB  PRO A 191     112.597  76.336  31.904  1.00 28.74           C  
ANISOU 1382  CB  PRO A 191     3488   3715   3718     18    -69    273       C  
ATOM   1383  CG  PRO A 191     112.363  74.838  31.944  1.00 29.97           C  
ANISOU 1383  CG  PRO A 191     3644   3855   3888     24    -50    294       C  
ATOM   1384  CD  PRO A 191     111.124  74.643  31.097  1.00 29.14           C  
ANISOU 1384  CD  PRO A 191     3543   3735   3792     18    -29    274       C  
ATOM   1385  N   GLN A 192     113.749  75.550  28.934  1.00 26.32           N  
ANISOU 1385  N   GLN A 192     3160   3366   3475     25    -52    265       N  
ATOM   1386  CA  GLN A 192     114.826  75.416  27.945  1.00 26.92           C  
ANISOU 1386  CA  GLN A 192     3224   3431   3575     30    -53    267       C  
ATOM   1387  C   GLN A 192     114.607  76.294  26.679  1.00 27.83           C  
ANISOU 1387  C   GLN A 192     3337   3542   3696     23    -52    241       C  
ATOM   1388  O   GLN A 192     115.576  76.681  26.020  1.00 26.61           O  
ANISOU 1388  O   GLN A 192     3173   3385   3554     25    -59    239       O  
ATOM   1389  CB  GLN A 192     115.083  73.945  27.557  1.00 27.27           C  
ANISOU 1389  CB  GLN A 192     3264   3454   3644     37    -34    284       C  
ATOM   1390  CG  GLN A 192     114.126  73.280  26.553  1.00 26.60           C  
ANISOU 1390  CG  GLN A 192     3184   3350   3573     32    -10    269       C  
ATOM   1391  CD  GLN A 192     112.759  72.926  27.129  1.00 27.42           C  
ANISOU 1391  CD  GLN A 192     3299   3455   3664     25      2    266       C  
ATOM   1392  OE1 GLN A 192     112.454  73.265  28.252  1.00 28.35           O  
ANISOU 1392  OE1 GLN A 192     3423   3589   3761     25     -8    273       O  
ATOM   1393  NE2 GLN A 192     111.921  72.245  26.331  1.00 27.51           N  
ANISOU 1393  NE2 GLN A 192     3313   3451   3689     19     23    253       N  
ATOM   1394  N   PHE A 193     113.337  76.576  26.358  1.00 25.61           N  
ANISOU 1394  N   PHE A 193     3064   3261   3408     16    -43    222       N  
ATOM   1395  CA  PHE A 193     112.969  77.500  25.327  1.00 25.16           C  
ANISOU 1395  CA  PHE A 193     3006   3203   3351     10    -43    199       C  
ATOM   1396  C   PHE A 193     112.919  78.946  25.820  1.00 25.53           C  
ANISOU 1396  C   PHE A 193     3056   3266   3379      7    -60    188       C  
ATOM   1397  O   PHE A 193     113.401  79.891  25.144  1.00 26.03           O  
ANISOU 1397  O   PHE A 193     3114   3330   3445      5    -68    178       O  
ATOM   1398  CB  PHE A 193     111.588  77.090  24.735  1.00 25.23           C  
ANISOU 1398  CB  PHE A 193     3019   3205   3361      4    -25    185       C  
ATOM   1399  CG  PHE A 193     110.884  78.196  23.989  1.00 24.16           C  
ANISOU 1399  CG  PHE A 193     2884   3076   3218     -1    -27    163       C  
ATOM   1400  CD1 PHE A 193     111.223  78.503  22.666  1.00 24.77           C  
ANISOU 1400  CD1 PHE A 193     2956   3147   3308     -2    -25    152       C  
ATOM   1401  CD2 PHE A 193     109.871  78.909  24.594  1.00 24.78           C  
ANISOU 1401  CD2 PHE A 193     2970   3167   3279     -5    -29    153       C  
ATOM   1402  CE1 PHE A 193     110.586  79.556  21.984  1.00 25.58           C  
ANISOU 1402  CE1 PHE A 193     3059   3257   3404     -5    -28    135       C  
ATOM   1403  CE2 PHE A 193     109.180  79.938  23.919  1.00 24.33           C  
ANISOU 1403  CE2 PHE A 193     2913   3115   3217     -8    -31    135       C  
ATOM   1404  CZ  PHE A 193     109.542  80.267  22.610  1.00 24.95           C  
ANISOU 1404  CZ  PHE A 193     2985   3188   3307     -8    -30    127       C  
ATOM   1405  N   TYR A 194     112.256  79.122  26.971  1.00 25.54           N  
ANISOU 1405  N   TYR A 194     3066   3279   3360      5    -63    190       N  
ATOM   1406  CA  TYR A 194     111.925  80.413  27.486  1.00 25.22           C  
ANISOU 1406  CA  TYR A 194     3030   3251   3300      0    -74    176       C  
ATOM   1407  C   TYR A 194     113.006  81.235  28.156  1.00 25.56           C  
ANISOU 1407  C   TYR A 194     3072   3307   3335      0    -94    180       C  
ATOM   1408  O   TYR A 194     112.931  82.490  28.088  1.00 24.92           O  
ANISOU 1408  O   TYR A 194     2992   3230   3245     -5   -102    163       O  
ATOM   1409  CB  TYR A 194     110.766  80.254  28.423  1.00 25.52           C  
ANISOU 1409  CB  TYR A 194     3079   3297   3320     -2    -67    175       C  
ATOM   1410  CG  TYR A 194     110.173  81.535  28.923  1.00 25.49           C  
ANISOU 1410  CG  TYR A 194     3082   3305   3297     -6    -73    158       C  
ATOM   1411  CD1 TYR A 194     109.158  82.153  28.242  1.00 26.17           C  
ANISOU 1411  CD1 TYR A 194     3170   3388   3385     -8    -64    140       C  
ATOM   1412  CD2 TYR A 194     110.639  82.119  30.110  1.00 26.22           C  
ANISOU 1412  CD2 TYR A 194     3180   3412   3370     -8    -87    161       C  
ATOM   1413  CE1 TYR A 194     108.597  83.334  28.691  1.00 25.93           C  
ANISOU 1413  CE1 TYR A 194     3146   3366   3340    -11    -67    125       C  
ATOM   1414  CE2 TYR A 194     110.099  83.301  30.577  1.00 26.59           C  
ANISOU 1414  CE2 TYR A 194     3235   3468   3401    -13    -90    144       C  
ATOM   1415  CZ  TYR A 194     109.068  83.911  29.831  1.00 27.81           C  
ANISOU 1415  CZ  TYR A 194     3391   3616   3560    -13    -79    126       C  
ATOM   1416  OH  TYR A 194     108.480  85.119  30.275  1.00 27.33           O  
ANISOU 1416  OH  TYR A 194     3338   3562   3485    -16    -80    109       O  
ATOM   1417  N   ASN A 195     113.986  80.589  28.791  1.00 25.63           N  
ANISOU 1417  N   ASN A 195     3076   3319   3344      4   -103    200       N  
ATOM   1418  CA  ASN A 195     114.929  81.302  29.678  1.00 28.70           C  
ANISOU 1418  CA  ASN A 195     3462   3723   3719      2   -124    204       C  
ATOM   1419  C   ASN A 195     116.394  81.572  29.174  1.00 30.68           C  
ANISOU 1419  C   ASN A 195     3699   3973   3986      3   -137    210       C  
ATOM   1420  O   ASN A 195     117.317  81.634  29.956  1.00 34.82           O  
ANISOU 1420  O   ASN A 195     4216   4510   4502      3   -153    222       O  
ATOM   1421  CB  ASN A 195     114.942  80.600  31.052  1.00 28.26           C  
ANISOU 1421  CB  ASN A 195     3411   3682   3646      4   -129    224       C  
ATOM   1422  CG  ASN A 195     114.427  81.499  32.180  1.00 29.75           C  
ANISOU 1422  CG  ASN A 195     3612   3889   3805     -4   -137    212       C  
ATOM   1423  OD1 ASN A 195     113.479  82.233  32.033  1.00 31.27           O  
ANISOU 1423  OD1 ASN A 195     3812   4079   3989     -8   -130    192       O  
ATOM   1424  ND2 ASN A 195     115.104  81.450  33.327  1.00 32.09           N  
ANISOU 1424  ND2 ASN A 195     3907   4202   4082     -4   -153    226       N  
ATOM   1425  N   ARG A 196     116.532  81.771  27.875  1.00 31.02           N  
ANISOU 1425  N   ARG A 196     3736   4002   4049      4   -129    200       N  
ATOM   1426  CA  ARG A 196     117.792  82.042  27.220  1.00 31.06           C  
ANISOU 1426  CA  ARG A 196     3727   4003   4071      5   -138    204       C  
ATOM   1427  C   ARG A 196     117.946  83.463  26.744  1.00 31.50           C  
ANISOU 1427  C   ARG A 196     3783   4060   4126     -3   -145    184       C  
ATOM   1428  O   ARG A 196     117.060  84.252  26.864  1.00 31.33           O  
ANISOU 1428  O   ARG A 196     3772   4040   4091     -8   -142    167       O  
ATOM   1429  CB  ARG A 196     117.909  81.196  25.959  1.00 31.18           C  
ANISOU 1429  CB  ARG A 196     3736   4000   4112     11   -121    207       C  
ATOM   1430  CG  ARG A 196     117.267  79.836  26.015  1.00 31.58           C  
ANISOU 1430  CG  ARG A 196     3790   4041   4167     17   -105    219       C  
ATOM   1431  CD  ARG A 196     117.147  79.171  24.662  1.00 31.08           C  
ANISOU 1431  CD  ARG A 196     3724   3960   4126     19    -86    214       C  
ATOM   1432  NE  ARG A 196     118.440  78.835  24.099  1.00 31.70           N  
ANISOU 1432  NE  ARG A 196     3789   4031   4225     25    -87    226       N  
ATOM   1433  CZ  ARG A 196     118.646  78.287  22.916  1.00 32.34           C  
ANISOU 1433  CZ  ARG A 196     3865   4096   4326     28    -71    223       C  
ATOM   1434  NH1 ARG A 196     117.658  77.990  22.128  1.00 32.71           N  
ANISOU 1434  NH1 ARG A 196     3920   4134   4376     24    -55    209       N  
ATOM   1435  NH2 ARG A 196     119.863  78.033  22.524  1.00 33.73           N  
ANISOU 1435  NH2 ARG A 196     4028   4266   4521     34    -72    234       N  
ATOM   1436  N   VAL A 197     119.107  83.741  26.184  1.00 29.74           N  
ANISOU 1436  N   VAL A 197     3547   3834   3919     -3   -152    187       N  
ATOM   1437  CA  VAL A 197     119.400  84.983  25.519  1.00 30.81           C  
ANISOU 1437  CA  VAL A 197     3681   3966   4060     -9   -155    171       C  
ATOM   1438  C   VAL A 197     119.455  84.413  24.102  1.00 29.49           C  
ANISOU 1438  C   VAL A 197     3508   3783   3914     -3   -139    172       C  
ATOM   1439  O   VAL A 197     120.385  83.746  23.733  1.00 27.80           O  
ANISOU 1439  O   VAL A 197     3282   3564   3717      2   -138    186       O  
ATOM   1440  CB  VAL A 197     120.688  85.658  25.974  1.00 30.59           C  
ANISOU 1440  CB  VAL A 197     3642   3948   4033    -15   -174    174       C  
ATOM   1441  CG1 VAL A 197     121.121  86.640  24.926  1.00 32.02           C  
ANISOU 1441  CG1 VAL A 197     3819   4120   4229    -20   -172    161       C  
ATOM   1442  CG2 VAL A 197     120.452  86.364  27.286  1.00 30.84           C  
ANISOU 1442  CG2 VAL A 197     3682   3996   4039    -24   -189    166       C  
ATOM   1443  N   HIS A 198     118.407  84.684  23.347  1.00 27.43           N  
ANISOU 1443  N   HIS A 198     3256   3515   3652     -4   -126    159       N  
ATOM   1444  CA  HIS A 198     118.143  84.067  22.077  1.00 29.07           C  
ANISOU 1444  CA  HIS A 198     3461   3709   3874      0   -109    158       C  
ATOM   1445  C   HIS A 198     116.842  84.621  21.519  1.00 27.99           C  
ANISOU 1445  C   HIS A 198     3334   3571   3729     -2   -100    141       C  
ATOM   1446  O   HIS A 198     115.942  84.941  22.323  1.00 30.23           O  
ANISOU 1446  O   HIS A 198     3628   3862   3997     -4   -102    135       O  
ATOM   1447  CB  HIS A 198     117.987  82.571  22.309  1.00 31.68           C  
ANISOU 1447  CB  HIS A 198     3792   4036   4210      7   -100    171       C  
ATOM   1448  CG  HIS A 198     118.120  81.737  21.075  1.00 33.82           C  
ANISOU 1448  CG  HIS A 198     4057   4293   4500     10    -83    173       C  
ATOM   1449  ND1 HIS A 198     117.044  81.414  20.293  1.00 36.48           N  
ANISOU 1449  ND1 HIS A 198     4401   4624   4836      9    -68    161       N  
ATOM   1450  CD2 HIS A 198     119.169  81.077  20.544  1.00 36.92           C  
ANISOU 1450  CD2 HIS A 198     4439   4677   4912     16    -79    183       C  
ATOM   1451  CE1 HIS A 198     117.423  80.646  19.289  1.00 37.89           C  
ANISOU 1451  CE1 HIS A 198     4574   4791   5031     12    -55    163       C  
ATOM   1452  NE2 HIS A 198     118.710  80.409  19.426  1.00 37.91           N  
ANISOU 1452  NE2 HIS A 198     4566   4790   5047     16    -60    177       N  
ATOM   1453  N   ASN A 199     116.731  84.758  20.198  1.00 27.55           N  
ANISOU 1453  N   ASN A 199     3276   3507   3683     -1    -90    135       N  
ATOM   1454  CA  ASN A 199     115.495  85.199  19.562  1.00 28.87           C  
ANISOU 1454  CA  ASN A 199     3451   3675   3844     -2    -81    121       C  
ATOM   1455  C   ASN A 199     114.244  84.379  19.952  1.00 27.42           C  
ANISOU 1455  C   ASN A 199     3274   3493   3650     -2    -73    120       C  
ATOM   1456  O   ASN A 199     113.162  84.937  20.098  1.00 25.89           O  
ANISOU 1456  O   ASN A 199     3087   3305   3446     -3    -71    110       O  
ATOM   1457  CB  ASN A 199     115.614  85.382  18.029  1.00 32.41           C  
ANISOU 1457  CB  ASN A 199     3896   4117   4303     -1    -72    117       C  
ATOM   1458  CG  ASN A 199     115.489  84.084  17.235  1.00 34.35           C  
ANISOU 1458  CG  ASN A 199     4138   4356   4557      0    -57    119       C  
ATOM   1459  OD1 ASN A 199     114.386  83.570  17.011  1.00 38.18           O  
ANISOU 1459  OD1 ASN A 199     4628   4843   5036     -1    -48    113       O  
ATOM   1460  ND2 ASN A 199     116.612  83.558  16.795  1.00 35.70           N  
ANISOU 1460  ND2 ASN A 199     4301   4520   4744      2    -54    127       N  
ATOM   1461  N   HIS A 200     114.405  83.077  20.124  1.00 25.56           N  
ANISOU 1461  N   HIS A 200     3037   3254   3421      0    -66    129       N  
ATOM   1462  CA  HIS A 200     113.334  82.251  20.675  1.00 26.73           C  
ANISOU 1462  CA  HIS A 200     3191   3404   3561     -1    -58    130       C  
ATOM   1463  C   HIS A 200     112.769  82.800  21.973  1.00 24.89           C  
ANISOU 1463  C   HIS A 200     2966   3182   3311     -2    -66    129       C  
ATOM   1464  O   HIS A 200     111.555  82.885  22.121  1.00 24.82           O  
ANISOU 1464  O   HIS A 200     2963   3177   3292     -4    -60    121       O  
ATOM   1465  CB  HIS A 200     113.772  80.805  20.934  1.00 27.17           C  
ANISOU 1465  CB  HIS A 200     3244   3451   3627      2    -51    144       C  
ATOM   1466  CG  HIS A 200     113.960  80.008  19.690  1.00 28.67           C  
ANISOU 1466  CG  HIS A 200     3430   3630   3834      3    -36    142       C  
ATOM   1467  ND1 HIS A 200     113.966  78.625  19.683  1.00 31.05           N  
ANISOU 1467  ND1 HIS A 200     3730   3920   4146      4    -23    150       N  
ATOM   1468  CD2 HIS A 200     114.133  80.394  18.411  1.00 29.71           C  
ANISOU 1468  CD2 HIS A 200     3558   3759   3973      1    -32    132       C  
ATOM   1469  CE1 HIS A 200     114.123  78.199  18.442  1.00 31.47           C  
ANISOU 1469  CE1 HIS A 200     3780   3965   4213      3    -10    143       C  
ATOM   1470  NE2 HIS A 200     114.283  79.250  17.660  1.00 31.12           N  
ANISOU 1470  NE2 HIS A 200     3734   3926   4166      1    -16    133       N  
ATOM   1471  N   SER A 201     113.653  83.087  22.932  1.00 23.29           N  
ANISOU 1471  N   SER A 201     2762   2984   3104     -1    -80    137       N  
ATOM   1472  CA  SER A 201     113.228  83.550  24.247  1.00 22.37           C  
ANISOU 1472  CA  SER A 201     2654   2878   2968     -4    -88    136       C  
ATOM   1473  C   SER A 201     112.658  84.952  24.171  1.00 24.31           C  
ANISOU 1473  C   SER A 201     2905   3128   3204     -7    -91    120       C  
ATOM   1474  O   SER A 201     111.716  85.251  24.889  1.00 24.16           O  
ANISOU 1474  O   SER A 201     2894   3116   3171     -8    -89    113       O  
ATOM   1475  CB  SER A 201     114.312  83.433  25.279  1.00 22.74           C  
ANISOU 1475  CB  SER A 201     2698   2932   3010     -3   -102    150       C  
ATOM   1476  OG  SER A 201     114.747  82.063  25.393  1.00 23.39           O  
ANISOU 1476  OG  SER A 201     2775   3010   3102      2    -97    168       O  
ATOM   1477  N   THR A 202     113.151  85.790  23.258  1.00 24.41           N  
ANISOU 1477  N   THR A 202     2913   3136   3227     -7    -94    113       N  
ATOM   1478  CA  THR A 202     112.548  87.099  23.081  1.00 25.22           C  
ANISOU 1478  CA  THR A 202     3020   3238   3323     -9    -94     98       C  
ATOM   1479  C   THR A 202     111.066  86.949  22.666  1.00 25.61           C  
ANISOU 1479  C   THR A 202     3073   3289   3368     -6    -81     91       C  
ATOM   1480  O   THR A 202     110.240  87.636  23.198  1.00 24.95           O  
ANISOU 1480  O   THR A 202     2996   3210   3274     -7    -79     83       O  
ATOM   1481  CB  THR A 202     113.317  87.907  22.078  1.00 26.23           C  
ANISOU 1481  CB  THR A 202     3142   3360   3464     -9    -96     95       C  
ATOM   1482  OG1 THR A 202     114.674  88.051  22.572  1.00 26.20           O  
ANISOU 1482  OG1 THR A 202     3134   3358   3465    -12   -109    102       O  
ATOM   1483  CG2 THR A 202     112.675  89.316  21.858  1.00 26.37           C  
ANISOU 1483  CG2 THR A 202     3166   3376   3478     -9    -95     82       C  
ATOM   1484  N   TRP A 203     110.763  86.011  21.765  1.00 24.07           N  
ANISOU 1484  N   TRP A 203     2874   3091   3182     -5    -71     94       N  
ATOM   1485  CA  TRP A 203     109.370  85.737  21.377  1.00 23.55           C  
ANISOU 1485  CA  TRP A 203     2809   3028   3113     -4    -59     88       C  
ATOM   1486  C   TRP A 203     108.531  85.178  22.526  1.00 23.18           C  
ANISOU 1486  C   TRP A 203     2768   2987   3054     -6    -55     89       C  
ATOM   1487  O   TRP A 203     107.429  85.640  22.766  1.00 23.61           O  
ANISOU 1487  O   TRP A 203     2825   3046   3098     -5    -51     81       O  
ATOM   1488  CB  TRP A 203     109.293  84.799  20.195  1.00 22.07           C  
ANISOU 1488  CB  TRP A 203     2615   2836   2936     -5    -50     89       C  
ATOM   1489  CG  TRP A 203     109.435  85.455  18.853  1.00 23.06           C  
ANISOU 1489  CG  TRP A 203     2735   2959   3067     -4    -49     84       C  
ATOM   1490  CD1 TRP A 203     110.585  85.490  18.073  1.00 22.35           C  
ANISOU 1490  CD1 TRP A 203     2641   2863   2989     -3    -51     88       C  
ATOM   1491  CD2 TRP A 203     108.402  86.092  18.074  1.00 22.46           C  
ANISOU 1491  CD2 TRP A 203     2657   2888   2987     -2    -45     75       C  
ATOM   1492  NE1 TRP A 203     110.310  86.148  16.895  1.00 24.63           N  
ANISOU 1492  NE1 TRP A 203     2926   3153   3279     -2    -48     82       N  
ATOM   1493  CE2 TRP A 203     108.985  86.495  16.848  1.00 22.69           C  
ANISOU 1493  CE2 TRP A 203     2682   2914   3024     -1    -45     75       C  
ATOM   1494  CE3 TRP A 203     107.037  86.363  18.295  1.00 22.75           C  
ANISOU 1494  CE3 TRP A 203     2696   2934   3015     -1    -40     69       C  
ATOM   1495  CZ2 TRP A 203     108.254  87.131  15.827  1.00 23.53           C  
ANISOU 1495  CZ2 TRP A 203     2785   3027   3128      1    -42     70       C  
ATOM   1496  CZ3 TRP A 203     106.299  86.993  17.283  1.00 23.46           C  
ANISOU 1496  CZ3 TRP A 203     2780   3029   3103      2    -38     64       C  
ATOM   1497  CH2 TRP A 203     106.909  87.390  16.067  1.00 23.82           C  
ANISOU 1497  CH2 TRP A 203     2822   3074   3156      3    -39     65       C  
ATOM   1498  N   GLY A 204     109.077  84.204  23.239  1.00 23.65           N  
ANISOU 1498  N   GLY A 204     2828   3045   3112     -7    -57    101       N  
ATOM   1499  CA  GLY A 204     108.451  83.653  24.431  1.00 24.82           C  
ANISOU 1499  CA  GLY A 204     2983   3199   3249     -8    -53    105       C  
ATOM   1500  C   GLY A 204     108.179  84.688  25.527  1.00 24.68           C  
ANISOU 1500  C   GLY A 204     2973   3190   3214     -8    -60     99       C  
ATOM   1501  O   GLY A 204     107.061  84.741  26.027  1.00 24.79           O  
ANISOU 1501  O   GLY A 204     2992   3210   3217     -9    -52     93       O  
ATOM   1502  N   ASN A 205     109.169  85.533  25.832  1.00 23.39           N  
ANISOU 1502  N   ASN A 205     2811   3029   3049     -9    -73     98       N  
ATOM   1503  CA  ASN A 205     109.049  86.593  26.826  1.00 23.47           C  
ANISOU 1503  CA  ASN A 205     2829   3046   3043    -11    -80     89       C  
ATOM   1504  C   ASN A 205     107.975  87.601  26.422  1.00 23.68           C  
ANISOU 1504  C   ASN A 205     2858   3070   3067     -9    -71     74       C  
ATOM   1505  O   ASN A 205     107.157  87.997  27.273  1.00 23.29           O  
ANISOU 1505  O   ASN A 205     2817   3028   3005    -10    -67     67       O  
ATOM   1506  CB  ASN A 205     110.339  87.397  27.042  1.00 24.04           C  
ANISOU 1506  CB  ASN A 205     2900   3118   3115    -15    -95     88       C  
ATOM   1507  CG  ASN A 205     111.584  86.550  27.437  1.00 26.06           C  
ANISOU 1507  CG  ASN A 205     3151   3377   3374    -15   -106    105       C  
ATOM   1508  OD1 ASN A 205     112.688  87.049  27.264  1.00 30.39           O  
ANISOU 1508  OD1 ASN A 205     3694   3924   3929    -18   -117    105       O  
ATOM   1509  ND2 ASN A 205     111.427  85.384  28.035  1.00 25.78           N  
ANISOU 1509  ND2 ASN A 205     3116   3346   3333    -14   -103    118       N  
ATOM   1510  N   ALA A 206     107.980  88.024  25.144  1.00 23.12           N  
ANISOU 1510  N   ALA A 206     2781   2993   3011     -7    -69     70       N  
ATOM   1511  CA  ALA A 206     106.997  88.982  24.669  1.00 24.05           C  
ANISOU 1511  CA  ALA A 206     2899   3109   3129     -3    -62     59       C  
ATOM   1512  C   ALA A 206     105.559  88.370  24.669  1.00 24.00           C  
ANISOU 1512  C   ALA A 206     2891   3108   3118     -1    -49     57       C  
ATOM   1513  O   ALA A 206     104.593  89.029  25.012  1.00 24.59           O  
ANISOU 1513  O   ALA A 206     2969   3187   3187      2    -42     49       O  
ATOM   1514  CB  ALA A 206     107.393  89.478  23.302  1.00 24.05           C  
ANISOU 1514  CB  ALA A 206     2892   3102   3144      0    -63     58       C  
ATOM   1515  N   ALA A 207     105.439  87.076  24.353  1.00 24.66           N  
ANISOU 1515  N   ALA A 207     2971   3193   3207     -3    -44     65       N  
ATOM   1516  CA  ALA A 207     104.134  86.398  24.355  1.00 23.94           C  
ANISOU 1516  CA  ALA A 207     2877   3107   3113     -3    -32     64       C  
ATOM   1517  C   ALA A 207     103.525  86.418  25.746  1.00 25.12           C  
ANISOU 1517  C   ALA A 207     3034   3263   3246     -4    -28     63       C  
ATOM   1518  O   ALA A 207     102.351  86.810  25.936  1.00 24.01           O  
ANISOU 1518  O   ALA A 207     2894   3128   3101     -2    -19     55       O  
ATOM   1519  CB  ALA A 207     104.282  84.990  23.896  1.00 24.01           C  
ANISOU 1519  CB  ALA A 207     2880   3113   3129     -7    -27     72       C  
ATOM   1520  N   VAL A 208     104.335  86.027  26.735  1.00 25.50           N  
ANISOU 1520  N   VAL A 208     3089   3312   3286     -7    -34     70       N  
ATOM   1521  CA  VAL A 208     103.902  85.976  28.129  1.00 25.53           C  
ANISOU 1521  CA  VAL A 208     3103   3324   3273     -9    -31     71       C  
ATOM   1522  C   VAL A 208     103.600  87.376  28.685  1.00 26.45           C  
ANISOU 1522  C   VAL A 208     3227   3444   3380     -7    -32     57       C  
ATOM   1523  O   VAL A 208     102.626  87.586  29.480  1.00 26.81           O  
ANISOU 1523  O   VAL A 208     3277   3496   3412     -7    -22     51       O  
ATOM   1524  CB  VAL A 208     104.949  85.256  29.000  1.00 25.81           C  
ANISOU 1524  CB  VAL A 208     3143   3362   3302    -12    -40     84       C  
ATOM   1525  CG1 VAL A 208     104.641  85.411  30.477  1.00 26.46           C  
ANISOU 1525  CG1 VAL A 208     3236   3455   3361    -14    -39     84       C  
ATOM   1526  CG2 VAL A 208     104.986  83.787  28.655  1.00 25.99           C  
ANISOU 1526  CG2 VAL A 208     3160   3380   3334    -12    -33     98       C  
ATOM   1527  N   GLY A 209     104.421  88.324  28.260  1.00 24.93           N  
ANISOU 1527  N   GLY A 209     3034   3247   3193     -6    -42     52       N  
ATOM   1528  CA  GLY A 209     104.340  89.672  28.720  1.00 26.15           C  
ANISOU 1528  CA  GLY A 209     3195   3400   3340     -6    -43     38       C  
ATOM   1529  C   GLY A 209     103.131  90.397  28.122  1.00 26.98           C  
ANISOU 1529  C   GLY A 209     3296   3502   3452      1    -30     29       C  
ATOM   1530  O   GLY A 209     102.516  91.205  28.797  1.00 28.53           O  
ANISOU 1530  O   GLY A 209     3500   3700   3640      3    -23     18       O  
ATOM   1531  N   MET A 210     102.853  90.179  26.839  1.00 27.37           N  
ANISOU 1531  N   MET A 210     3335   3548   3517      5    -28     33       N  
ATOM   1532  CA  MET A 210     101.736  90.848  26.168  1.00 26.39           C  
ANISOU 1532  CA  MET A 210     3204   3423   3399     13    -18     27       C  
ATOM   1533  C   MET A 210     100.428  90.371  26.811  1.00 26.30           C  
ANISOU 1533  C   MET A 210     3193   3421   3379     14     -4     25       C  
ATOM   1534  O   MET A 210      99.551  91.195  27.165  1.00 25.73           O  
ANISOU 1534  O   MET A 210     3122   3350   3304     19      5     17       O  
ATOM   1535  CB  MET A 210     101.743  90.584  24.653  1.00 26.39           C  
ANISOU 1535  CB  MET A 210     3192   3421   3414     16    -19     32       C  
ATOM   1536  CG  MET A 210     102.849  91.250  23.841  1.00 26.57           C  
ANISOU 1536  CG  MET A 210     3214   3435   3446     17    -29     34       C  
ATOM   1537  SD  MET A 210     102.616  93.022  23.821  1.00 29.19           S  
ANISOU 1537  SD  MET A 210     3551   3759   3783     25    -25     24       S  
ATOM   1538  CE  MET A 210     101.245  93.060  22.631  1.00 27.75           C  
ANISOU 1538  CE  MET A 210     3354   3583   3608     34    -16     28       C  
ATOM   1539  N   ILE A 211     100.284  89.063  26.972  1.00 25.54           N  
ANISOU 1539  N   ILE A 211     3093   3330   3280      8     -2     33       N  
ATOM   1540  CA  ILE A 211      99.068  88.530  27.593  1.00 25.71           C  
ANISOU 1540  CA  ILE A 211     3114   3360   3295      8     11     32       C  
ATOM   1541  C   ILE A 211      98.959  88.938  29.080  1.00 28.41           C  
ANISOU 1541  C   ILE A 211     3470   3706   3619      7     16     27       C  
ATOM   1542  O   ILE A 211      97.852  89.297  29.548  1.00 27.96           O  
ANISOU 1542  O   ILE A 211     3412   3653   3557     10     29     20       O  
ATOM   1543  CB  ILE A 211      98.869  87.001  27.395  1.00 26.49           C  
ANISOU 1543  CB  ILE A 211     3207   3462   3397      1     15     42       C  
ATOM   1544  CG1 ILE A 211      97.396  86.614  27.644  1.00 27.32           C  
ANISOU 1544  CG1 ILE A 211     3306   3575   3500      1     31     39       C  
ATOM   1545  CG2 ILE A 211      99.730  86.146  28.305  1.00 25.88           C  
ANISOU 1545  CG2 ILE A 211     3139   3384   3311     -5     10     52       C  
ATOM   1546  CD1 ILE A 211      96.434  87.232  26.657  1.00 28.96           C  
ANISOU 1546  CD1 ILE A 211     3499   3786   3717      7     35     33       C  
ATOM   1547  N   GLY A 212     100.091  88.942  29.813  1.00 27.01           N  
ANISOU 1547  N   GLY A 212     3303   3528   3432      2      5     29       N  
ATOM   1548  CA  GLY A 212     100.137  89.523  31.133  1.00 26.30           C  
ANISOU 1548  CA  GLY A 212     3227   3442   3324      0      6     22       C  
ATOM   1549  C   GLY A 212      99.656  90.955  31.222  1.00 27.17           C  
ANISOU 1549  C   GLY A 212     3341   3548   3434      5     13      6       C  
ATOM   1550  O   GLY A 212      98.866  91.289  32.109  1.00 28.82           O  
ANISOU 1550  O   GLY A 212     3557   3762   3631      6     25     -2       O  
ATOM   1551  N   LEU A 213     100.156  91.823  30.362  1.00 26.57           N  
ANISOU 1551  N   LEU A 213     3262   3463   3372      9      6      2       N  
ATOM   1552  CA  LEU A 213      99.706  93.222  30.361  1.00 27.39           C  
ANISOU 1552  CA  LEU A 213     3369   3559   3480     15     15    -12       C  
ATOM   1553  C   LEU A 213      98.182  93.405  30.057  1.00 28.07           C  
ANISOU 1553  C   LEU A 213     3446   3647   3572     25     32    -15       C  
ATOM   1554  O   LEU A 213      97.518  94.258  30.655  1.00 28.95           O  
ANISOU 1554  O   LEU A 213     3563   3757   3680     30     45    -26       O  
ATOM   1555  CB  LEU A 213     100.515  94.019  29.368  1.00 27.19           C  
ANISOU 1555  CB  LEU A 213     3339   3521   3469     18      5    -13       C  
ATOM   1556  CG  LEU A 213     101.978  94.305  29.702  1.00 27.19           C  
ANISOU 1556  CG  LEU A 213     3348   3517   3465      9    -10    -16       C  
ATOM   1557  CD1 LEU A 213     102.601  95.035  28.518  1.00 27.08           C  
ANISOU 1557  CD1 LEU A 213     3328   3491   3471     12    -16    -14       C  
ATOM   1558  CD2 LEU A 213     102.157  95.113  30.990  1.00 27.52           C  
ANISOU 1558  CD2 LEU A 213     3406   3560   3492      3     -8    -31       C  
ATOM   1559  N   VAL A 214      97.632  92.643  29.131  1.00 28.40           N  
ANISOU 1559  N   VAL A 214     3473   3693   3624     28     33     -5       N  
ATOM   1560  CA  VAL A 214      96.194  92.778  28.798  1.00 29.15           C  
ANISOU 1560  CA  VAL A 214     3557   3794   3727     37     48     -6       C  
ATOM   1561  C   VAL A 214      95.377  92.391  30.041  1.00 31.11           C  
ANISOU 1561  C   VAL A 214     3810   4050   3960     34     62    -10       C  
ATOM   1562  O   VAL A 214      94.383  93.077  30.360  1.00 28.88           O  
ANISOU 1562  O   VAL A 214     3526   3768   3678     42     77    -17       O  
ATOM   1563  CB  VAL A 214      95.712  91.881  27.626  1.00 29.05           C  
ANISOU 1563  CB  VAL A 214     3525   3786   3724     37     46      5       C  
ATOM   1564  CG1 VAL A 214      94.195  92.064  27.330  1.00 28.12           C  
ANISOU 1564  CG1 VAL A 214     3393   3677   3613     46     60      4       C  
ATOM   1565  CG2 VAL A 214      96.479  92.185  26.381  1.00 28.52           C  
ANISOU 1565  CG2 VAL A 214     3453   3713   3670     39     34      9       C  
ATOM   1566  N   MET A 215      95.794  91.292  30.697  1.00 29.97           N  
ANISOU 1566  N   MET A 215     3672   3911   3803     24     58     -3       N  
ATOM   1567  CA  MET A 215      95.118  90.732  31.863  1.00 33.30           C  
ANISOU 1567  CA  MET A 215     4099   4342   4209     20     71     -4       C  
ATOM   1568  C   MET A 215      95.373  91.435  33.213  1.00 33.69           C  
ANISOU 1568  C   MET A 215     4168   4393   4239     18     75    -15       C  
ATOM   1569  O   MET A 215      94.629  91.216  34.106  1.00 32.96           O  
ANISOU 1569  O   MET A 215     4080   4308   4135     17     89    -17       O  
ATOM   1570  CB  MET A 215      95.457  89.241  32.054  1.00 32.47           C  
ANISOU 1570  CB  MET A 215     3995   4243   4099     11     66     10       C  
ATOM   1571  CG  MET A 215      94.946  88.361  30.942  1.00 33.30           C  
ANISOU 1571  CG  MET A 215     4082   4349   4220     10     67     18       C  
ATOM   1572  SD  MET A 215      95.093  86.586  31.207  1.00 34.29           S  
ANISOU 1572  SD  MET A 215     4208   4478   4343     -1     69     33       S  
ATOM   1573  CE  MET A 215      96.831  86.430  31.665  1.00 36.02           C  
ANISOU 1573  CE  MET A 215     4441   4692   4552     -5     50     40       C  
ATOM   1574  N   GLY A 216      96.394  92.272  33.337  1.00 33.40           N  
ANISOU 1574  N   GLY A 216     4141   4349   4199     17     64    -22       N  
ATOM   1575  CA  GLY A 216      96.777  92.864  34.626  1.00 33.14           C  
ANISOU 1575  CA  GLY A 216     4127   4319   4146     11     65    -34       C  
ATOM   1576  C   GLY A 216      97.369  91.827  35.577  1.00 33.89           C  
ANISOU 1576  C   GLY A 216     4231   4426   4220      1     58    -24       C  
ATOM   1577  O   GLY A 216      97.185  91.916  36.771  1.00 36.67           O  
ANISOU 1577  O   GLY A 216     4596   4786   4550     -4     65    -31       O  
ATOM   1578  N   ASP A 217      98.097  90.857  35.039  1.00 33.55           N  
ANISOU 1578  N   ASP A 217     4181   4383   4183     -3     44     -9       N  
ATOM   1579  CA  ASP A 217      98.685  89.809  35.816  1.00 33.64           C  
ANISOU 1579  CA  ASP A 217     4199   4405   4177    -11     36      5       C  
ATOM   1580  C   ASP A 217     100.169  90.098  36.103  1.00 34.56           C  
ANISOU 1580  C   ASP A 217     4324   4522   4286    -17     15      5       C  
ATOM   1581  O   ASP A 217     101.066  89.826  35.263  1.00 32.23           O  
ANISOU 1581  O   ASP A 217     4020   4220   4005    -17      1     13       O  
ATOM   1582  CB  ASP A 217      98.556  88.522  35.076  1.00 33.37           C  
ANISOU 1582  CB  ASP A 217     4153   4369   4157    -10     36     22       C  
ATOM   1583  CG  ASP A 217      98.980  87.361  35.900  1.00 35.95           C  
ANISOU 1583  CG  ASP A 217     4485   4705   4469    -16     33     38       C  
ATOM   1584  OD1 ASP A 217     100.094  87.308  36.447  1.00 36.04           O  
ANISOU 1584  OD1 ASP A 217     4505   4721   4468    -20     17     44       O  
ATOM   1585  OD2 ASP A 217      98.157  86.458  35.988  1.00 39.41           O  
ANISOU 1585  OD2 ASP A 217     4920   5146   4909    -16     46     47       O  
ATOM   1586  N   GLU A 218     100.410  90.551  37.329  1.00 33.81           N  
ANISOU 1586  N   GLU A 218     4243   4437   4166    -23     14     -4       N  
ATOM   1587  CA  GLU A 218     101.722  90.968  37.751  1.00 35.25           C  
ANISOU 1587  CA  GLU A 218     4433   4624   4338    -31     -5     -8       C  
ATOM   1588  C   GLU A 218     102.774  89.848  37.687  1.00 34.27           C  
ANISOU 1588  C   GLU A 218     4304   4506   4213    -34    -23     15       C  
ATOM   1589  O   GLU A 218     103.929  90.098  37.347  1.00 32.50           O  
ANISOU 1589  O   GLU A 218     4076   4279   3995    -38    -40     16       O  
ATOM   1590  CB  GLU A 218     101.637  91.584  39.159  1.00 36.59           C  
ANISOU 1590  CB  GLU A 218     4620   4806   4477    -38     -1    -22       C  
ATOM   1591  CG  GLU A 218     102.884  92.323  39.590  1.00 39.19           C  
ANISOU 1591  CG  GLU A 218     4957   5139   4795    -48    -20    -33       C  
ATOM   1592  CD  GLU A 218     103.259  93.472  38.649  1.00 42.69           C  
ANISOU 1592  CD  GLU A 218     5396   5564   5262    -47    -23    -48       C  
ATOM   1593  OE1 GLU A 218     102.361  93.998  37.926  1.00 42.78           O  
ANISOU 1593  OE1 GLU A 218     5403   5561   5292    -38     -7    -56       O  
ATOM   1594  OE2 GLU A 218     104.475  93.848  38.634  1.00 44.27           O  
ANISOU 1594  OE2 GLU A 218     5595   5764   5460    -55    -42    -51       O  
ATOM   1595  N   GLU A 219     102.357  88.632  37.990  1.00 34.43           N  
ANISOU 1595  N   GLU A 219     4322   4532   4228    -33    -16     32       N  
ATOM   1596  CA  GLU A 219     103.214  87.479  37.931  1.00 35.52           C  
ANISOU 1596  CA  GLU A 219     4454   4673   4367    -33    -29     56       C  
ATOM   1597  C   GLU A 219     103.795  87.244  36.526  1.00 33.32           C  
ANISOU 1597  C   GLU A 219     4161   4380   4118    -29    -37     62       C  
ATOM   1598  O   GLU A 219     105.027  87.068  36.366  1.00 31.00           O  
ANISOU 1598  O   GLU A 219     3864   4087   3829    -31    -55     71       O  
ATOM   1599  CB  GLU A 219     102.477  86.229  38.452  1.00 38.86           C  
ANISOU 1599  CB  GLU A 219     4879   5103   4783    -32    -15     73       C  
ATOM   1600  CG  GLU A 219     103.411  85.022  38.530  1.00 45.36           C  
ANISOU 1600  CG  GLU A 219     5698   5929   5608    -32    -27     99       C  
ATOM   1601  CD  GLU A 219     102.775  83.731  39.037  1.00 52.92           C  
ANISOU 1601  CD  GLU A 219     6658   6891   6560    -30    -13    119       C  
ATOM   1602  OE1 GLU A 219     101.531  83.634  39.190  1.00 58.48           O  
ANISOU 1602  OE1 GLU A 219     7364   7594   7263    -30      7    114       O  
ATOM   1603  OE2 GLU A 219     103.554  82.784  39.288  1.00 61.39           O  
ANISOU 1603  OE2 GLU A 219     7729   7966   7632    -30    -21    142       O  
ATOM   1604  N   LEU A 220     102.918  87.263  35.522  1.00 30.96           N  
ANISOU 1604  N   LEU A 220     3855   4070   3840    -24    -24     57       N  
ATOM   1605  CA  LEU A 220     103.309  87.055  34.141  1.00 29.77           C  
ANISOU 1605  CA  LEU A 220     3690   3906   3715    -21    -29     61       C  
ATOM   1606  C   LEU A 220     104.131  88.214  33.646  1.00 27.91           C  
ANISOU 1606  C   LEU A 220     3454   3664   3487    -21    -41     49       C  
ATOM   1607  O   LEU A 220     105.073  88.014  32.905  1.00 27.12           O  
ANISOU 1607  O   LEU A 220     3346   3557   3401    -21    -53     57       O  
ATOM   1608  CB  LEU A 220     102.094  86.818  33.196  1.00 29.71           C  
ANISOU 1608  CB  LEU A 220     3674   3891   3725    -16    -13     58       C  
ATOM   1609  CG  LEU A 220     101.258  85.535  33.492  1.00 29.72           C  
ANISOU 1609  CG  LEU A 220     3672   3895   3723    -16      1     71       C  
ATOM   1610  CD1 LEU A 220     100.176  85.375  32.431  1.00 28.98           C  
ANISOU 1610  CD1 LEU A 220     3567   3795   3648    -14     14     66       C  
ATOM   1611  CD2 LEU A 220     102.087  84.250  33.524  1.00 29.41           C  
ANISOU 1611  CD2 LEU A 220     3632   3855   3689    -18     -5     91       C  
ATOM   1612  N   ILE A 221     103.749  89.422  34.012  1.00 27.32           N  
ANISOU 1612  N   ILE A 221     3387   3590   3405    -22    -37     31       N  
ATOM   1613  CA  ILE A 221     104.518  90.579  33.637  1.00 28.02           C  
ANISOU 1613  CA  ILE A 221     3475   3670   3500    -24    -47     19       C  
ATOM   1614  C   ILE A 221     105.974  90.462  34.161  1.00 28.21           C  
ANISOU 1614  C   ILE A 221     3501   3701   3515    -32    -68     25       C  
ATOM   1615  O   ILE A 221     106.893  90.701  33.395  1.00 27.91           O  
ANISOU 1615  O   ILE A 221     3456   3656   3492    -33    -79     27       O  
ATOM   1616  CB  ILE A 221     103.863  91.873  34.111  1.00 27.97           C  
ANISOU 1616  CB  ILE A 221     3479   3662   3486    -24    -37     -3       C  
ATOM   1617  CG1 ILE A 221     102.538  92.106  33.368  1.00 28.68           C  
ANISOU 1617  CG1 ILE A 221     3563   3744   3590    -14    -19     -7       C  
ATOM   1618  CG2 ILE A 221     104.755  93.071  33.821  1.00 28.20           C  
ANISOU 1618  CG2 ILE A 221     3510   3682   3523    -28    -47    -15       C  
ATOM   1619  CD1 ILE A 221     101.655  93.150  34.031  1.00 28.35           C  
ANISOU 1619  CD1 ILE A 221     3531   3701   3540    -12     -4    -25       C  
ATOM   1620  N   GLN A 222     106.161  90.070  35.425  1.00 29.30           N  
ANISOU 1620  N   GLN A 222     3649   3855   3629    -37    -72     29       N  
ATOM   1621  CA  GLN A 222     107.497  89.905  36.015  1.00 30.60           C  
ANISOU 1621  CA  GLN A 222     3813   4030   3781    -45    -93     37       C  
ATOM   1622  C   GLN A 222     108.280  88.782  35.334  1.00 28.49           C  
ANISOU 1622  C   GLN A 222     3533   3761   3531    -41   -102     60       C  
ATOM   1623  O   GLN A 222     109.471  88.901  35.164  1.00 26.75           O  
ANISOU 1623  O   GLN A 222     3307   3541   3316    -44   -118     65       O  
ATOM   1624  CB  GLN A 222     107.450  89.598  37.533  1.00 34.04           C  
ANISOU 1624  CB  GLN A 222     4262   4488   4186    -51    -95     40       C  
ATOM   1625  CG  GLN A 222     106.961  90.740  38.423  1.00 38.71           C  
ANISOU 1625  CG  GLN A 222     4868   5085   4756    -58    -89     15       C  
ATOM   1626  CD  GLN A 222     107.860  91.935  38.341  1.00 41.36           C  
ANISOU 1626  CD  GLN A 222     5204   5416   5093    -66   -102     -3       C  
ATOM   1627  OE1 GLN A 222     109.064  91.814  38.550  1.00 47.92           O  
ANISOU 1627  OE1 GLN A 222     6030   6256   5919    -73   -122      4       O  
ATOM   1628  NE2 GLN A 222     107.319  93.066  37.937  1.00 43.74           N  
ANISOU 1628  NE2 GLN A 222     5510   5703   5406    -66    -90    -24       N  
ATOM   1629  N   ARG A 223     107.595  87.675  35.045  1.00 26.80           N  
ANISOU 1629  N   ARG A 223     3315   3543   3323    -34    -90     74       N  
ATOM   1630  CA  ARG A 223     108.165  86.533  34.348  1.00 26.95           C  
ANISOU 1630  CA  ARG A 223     3323   3556   3360    -30    -93     95       C  
ATOM   1631  C   ARG A 223     108.649  86.942  32.966  1.00 26.58           C  
ANISOU 1631  C   ARG A 223     3266   3494   3339    -27    -96     90       C  
ATOM   1632  O   ARG A 223     109.650  86.423  32.491  1.00 25.58           O  
ANISOU 1632  O   ARG A 223     3129   3364   3225    -26   -106    103       O  
ATOM   1633  CB  ARG A 223     107.156  85.368  34.256  1.00 26.61           C  
ANISOU 1633  CB  ARG A 223     3279   3510   3321    -25    -76    107       C  
ATOM   1634  CG  ARG A 223     107.816  84.017  33.947  1.00 28.60           C  
ANISOU 1634  CG  ARG A 223     3522   3757   3585    -21    -79    131       C  
ATOM   1635  CD  ARG A 223     106.790  82.954  33.590  1.00 29.51           C  
ANISOU 1635  CD  ARG A 223     3636   3865   3711    -18    -59    138       C  
ATOM   1636  NE  ARG A 223     105.959  82.612  34.738  1.00 31.41           N  
ANISOU 1636  NE  ARG A 223     3887   4116   3930    -19    -49    142       N  
ATOM   1637  CZ  ARG A 223     104.821  81.901  34.718  1.00 33.50           C  
ANISOU 1637  CZ  ARG A 223     4153   4378   4199    -19    -30    145       C  
ATOM   1638  NH1 ARG A 223     104.252  81.465  33.595  1.00 34.19           N  
ANISOU 1638  NH1 ARG A 223     4231   4451   4308    -18    -19    142       N  
ATOM   1639  NH2 ARG A 223     104.197  81.686  35.850  1.00 36.11           N  
ANISOU 1639  NH2 ARG A 223     4493   4719   4508    -21    -22    149       N  
ATOM   1640  N   ALA A 224     107.904  87.850  32.310  1.00 25.43           N  
ANISOU 1640  N   ALA A 224     3121   3340   3202    -26    -87     73       N  
ATOM   1641  CA  ALA A 224     108.307  88.357  31.034  1.00 25.35           C  
ANISOU 1641  CA  ALA A 224     3102   3317   3213    -24    -89     68       C  
ATOM   1642  C   ALA A 224     109.549  89.215  31.119  1.00 24.96           C  
ANISOU 1642  C   ALA A 224     3051   3268   3165    -29   -105     63       C  
ATOM   1643  O   ALA A 224     110.426  89.090  30.280  1.00 24.69           O  
ANISOU 1643  O   ALA A 224     3007   3226   3147    -28   -112     69       O  
ATOM   1644  CB  ALA A 224     107.190  89.132  30.378  1.00 25.15           C  
ANISOU 1644  CB  ALA A 224     3077   3283   3194    -19    -76     53       C  
ATOM   1645  N   LEU A 225     109.588  90.107  32.102  1.00 25.66           N  
ANISOU 1645  N   LEU A 225     3150   3364   3235    -36   -110     49       N  
ATOM   1646  CA  LEU A 225     110.675  91.075  32.229  1.00 27.54           C  
ANISOU 1646  CA  LEU A 225     3388   3602   3475    -44   -124     40       C  
ATOM   1647  C   LEU A 225     111.981  90.456  32.737  1.00 27.68           C  
ANISOU 1647  C   LEU A 225     3399   3631   3486    -49   -143     55       C  
ATOM   1648  O   LEU A 225     113.060  90.849  32.294  1.00 26.05           O  
ANISOU 1648  O   LEU A 225     3184   3421   3292    -53   -155     55       O  
ATOM   1649  CB  LEU A 225     110.250  92.219  33.149  1.00 28.07           C  
ANISOU 1649  CB  LEU A 225     3468   3673   3523    -51   -121     19       C  
ATOM   1650  CG  LEU A 225     109.175  93.165  32.584  1.00 28.90           C  
ANISOU 1650  CG  LEU A 225     3578   3764   3638    -45   -104      2       C  
ATOM   1651  CD1 LEU A 225     108.742  94.129  33.686  1.00 30.37           C  
ANISOU 1651  CD1 LEU A 225     3780   3955   3805    -52    -99    -18       C  
ATOM   1652  CD2 LEU A 225     109.684  93.978  31.408  1.00 29.13           C  
ANISOU 1652  CD2 LEU A 225     3600   3777   3691    -44   -105     -2       C  
ATOM   1653  N   TYR A 226     111.838  89.541  33.699  1.00 28.01           N  
ANISOU 1653  N   TYR A 226     3444   3687   3510    -48   -145     68       N  
ATOM   1654  CA  TYR A 226     112.946  89.036  34.514  1.00 30.20           C  
ANISOU 1654  CA  TYR A 226     3717   3981   3775    -53   -164     82       C  
ATOM   1655  C   TYR A 226     113.202  87.551  34.407  1.00 28.30           C  
ANISOU 1655  C   TYR A 226     3468   3742   3540    -45   -164    109       C  
ATOM   1656  O   TYR A 226     114.134  87.087  34.990  1.00 28.94           O  
ANISOU 1656  O   TYR A 226     3544   3837   3615    -46   -179    124       O  
ATOM   1657  CB  TYR A 226     112.778  89.472  35.994  1.00 31.37           C  
ANISOU 1657  CB  TYR A 226     3879   4149   3890    -62   -170     72       C  
ATOM   1658  CG  TYR A 226     112.874  90.973  36.135  1.00 33.07           C  
ANISOU 1658  CG  TYR A 226     4102   4362   4101    -73   -172     45       C  
ATOM   1659  CD1 TYR A 226     114.096  91.628  35.985  1.00 33.97           C  
ANISOU 1659  CD1 TYR A 226     4208   4478   4222    -82   -189     39       C  
ATOM   1660  CD2 TYR A 226     111.745  91.738  36.411  1.00 35.34           C  
ANISOU 1660  CD2 TYR A 226     4403   4645   4380    -74   -156     24       C  
ATOM   1661  CE1 TYR A 226     114.181  93.019  36.078  1.00 36.06           C  
ANISOU 1661  CE1 TYR A 226     4480   4737   4486    -93   -189     13       C  
ATOM   1662  CE2 TYR A 226     111.814  93.146  36.477  1.00 36.13           C  
ANISOU 1662  CE2 TYR A 226     4510   4738   4479    -83   -155     -2       C  
ATOM   1663  CZ  TYR A 226     113.032  93.762  36.325  1.00 37.16           C  
ANISOU 1663  CZ  TYR A 226     4634   4869   4617    -93   -172     -8       C  
ATOM   1664  OH  TYR A 226     113.093  95.142  36.405  1.00 44.39           O  
ANISOU 1664  OH  TYR A 226     5558   5776   5534   -103   -169    -34       O  
ATOM   1665  N   GLY A 227     112.417  86.848  33.613  1.00 29.01           N  
ANISOU 1665  N   GLY A 227     3666   3882   3476    217   -136    232       N  
ATOM   1666  CA  GLY A 227     112.572  85.430  33.378  1.00 29.69           C  
ANISOU 1666  CA  GLY A 227     3712   3998   3574    173   -129    251       C  
ATOM   1667  C   GLY A 227     112.075  84.571  34.524  1.00 29.81           C  
ANISOU 1667  C   GLY A 227     3726   4042   3556    224    -96    280       C  
ATOM   1668  O   GLY A 227     111.566  85.066  35.518  1.00 29.65           O  
ANISOU 1668  O   GLY A 227     3740   4032   3494    304    -75    288       O  
ATOM   1669  N   ILE A 228     112.214  83.271  34.357  1.00 29.71           N  
ANISOU 1669  N   ILE A 228     3678   4045   3567    185    -87    300       N  
ATOM   1670  CA  ILE A 228     111.852  82.320  35.380  1.00 31.15           C  
ANISOU 1670  CA  ILE A 228     3849   4252   3733    228    -51    340       C  
ATOM   1671  C   ILE A 228     113.017  82.342  36.357  1.00 35.12           C  
ANISOU 1671  C   ILE A 228     4402   4748   4195    263    -74    294       C  
ATOM   1672  O   ILE A 228     114.211  82.225  35.956  1.00 33.68           O  
ANISOU 1672  O   ILE A 228     4228   4541   4028    215   -113    249       O  
ATOM   1673  CB  ILE A 228     111.686  80.893  34.809  1.00 31.13           C  
ANISOU 1673  CB  ILE A 228     3791   4252   3785    167    -38    374       C  
ATOM   1674  CG1 ILE A 228     110.535  80.876  33.771  1.00 31.18           C  
ANISOU 1674  CG1 ILE A 228     3744   4269   3832    123    -32    412       C  
ATOM   1675  CG2 ILE A 228     111.503  79.864  35.932  1.00 31.10           C  
ANISOU 1675  CG2 ILE A 228     3772   4266   3777    212      2    424       C  
ATOM   1676  CD1 ILE A 228     110.566  79.681  32.835  1.00 30.64           C  
ANISOU 1676  CD1 ILE A 228     3634   4187   3821     43    -45    411       C  
ATOM   1677  N   GLU A 229     112.650  82.433  37.632  1.00 38.07           N  
ANISOU 1677  N   GLU A 229     4801   5150   4513    353    -48    314       N  
ATOM   1678  CA  GLU A 229     113.595  82.395  38.732  1.00 43.94           C  
ANISOU 1678  CA  GLU A 229     5590   5903   5202    403    -70    276       C  
ATOM   1679  C   GLU A 229     114.008  80.940  39.015  1.00 43.51           C  
ANISOU 1679  C   GLU A 229     5498   5869   5167    388    -47    316       C  
ATOM   1680  O   GLU A 229     113.157  80.035  39.042  1.00 40.46           O  
ANISOU 1680  O   GLU A 229     5062   5501   4811    393      6    390       O  
ATOM   1681  CB  GLU A 229     112.949  82.996  39.961  1.00 48.88           C  
ANISOU 1681  CB  GLU A 229     6260   6563   5749    518    -46    286       C  
ATOM   1682  CG  GLU A 229     113.942  83.484  41.003  1.00 56.18           C  
ANISOU 1682  CG  GLU A 229     7252   7492   6601    574    -94    215       C  
ATOM   1683  CD  GLU A 229     113.262  84.120  42.224  1.00 64.66           C  
ANISOU 1683  CD  GLU A 229     8383   8603   7581    705    -71    214       C  
ATOM   1684  OE1 GLU A 229     111.998  84.112  42.329  1.00 63.14           O  
ANISOU 1684  OE1 GLU A 229     8170   8438   7381    760     -4    285       O  
ATOM   1685  OE2 GLU A 229     114.013  84.640  43.082  1.00 72.51           O  
ANISOU 1685  OE2 GLU A 229     9443   9601   8506    755   -122    141       O  
ATOM   1686  N   ASP A 230     115.301  80.727  39.209  1.00 42.92           N  
ANISOU 1686  N   ASP A 230     5440   5786   5082    370    -86    273       N  
ATOM   1687  CA  ASP A 230     115.846  79.388  39.476  1.00 45.51           C  
ANISOU 1687  CA  ASP A 230     5735   6127   5428    361    -63    310       C  
ATOM   1688  C   ASP A 230     115.343  78.346  38.449  1.00 42.52           C  
ANISOU 1688  C   ASP A 230     5299   5722   5133    290    -28    355       C  
ATOM   1689  O   ASP A 230     114.629  77.418  38.782  1.00 42.44           O  
ANISOU 1689  O   ASP A 230     5251   5724   5148    309     23    424       O  
ATOM   1690  CB  ASP A 230     115.555  78.961  40.941  1.00 50.87           C  
ANISOU 1690  CB  ASP A 230     6422   6863   6044    464    -24    359       C  
ATOM   1691  CG  ASP A 230     116.457  77.788  41.432  1.00 59.76           C  
ANISOU 1691  CG  ASP A 230     7525   8007   7174    470    -11    388       C  
ATOM   1692  OD1 ASP A 230     117.518  77.454  40.819  1.00 61.50           O  
ANISOU 1692  OD1 ASP A 230     7738   8199   7432    404    -42    358       O  
ATOM   1693  OD2 ASP A 230     116.111  77.195  42.474  1.00 66.44           O  
ANISOU 1693  OD2 ASP A 230     8359   8902   7984    551     37    452       O  
ATOM   1694  N   ASP A 231     115.745  78.514  37.191  1.00 39.80           N  
ANISOU 1694  N   ASP A 231     4949   5341   4833    210    -60    316       N  
ATOM   1695  CA  ASP A 231     115.191  77.705  36.088  1.00 36.55           C  
ANISOU 1695  CA  ASP A 231     4494   4903   4489    143    -41    338       C  
ATOM   1696  C   ASP A 231     115.665  76.239  36.065  1.00 35.47           C  
ANISOU 1696  C   ASP A 231     4333   4748   4398    120    -16    363       C  
ATOM   1697  O   ASP A 231     115.039  75.412  35.412  1.00 31.83           O  
ANISOU 1697  O   ASP A 231     3837   4261   3995     76      2    385       O  
ATOM   1698  CB  ASP A 231     115.456  78.356  34.735  1.00 36.19           C  
ANISOU 1698  CB  ASP A 231     4453   4834   4462     79    -79    290       C  
ATOM   1699  CG  ASP A 231     116.960  78.595  34.437  1.00 36.96           C  
ANISOU 1699  CG  ASP A 231     4573   4917   4552     57   -116    243       C  
ATOM   1700  OD1 ASP A 231     117.821  77.747  34.762  1.00 34.05           O  
ANISOU 1700  OD1 ASP A 231     4202   4545   4189     60   -108    248       O  
ATOM   1701  OD2 ASP A 231     117.241  79.646  33.803  1.00 36.63           O  
ANISOU 1701  OD2 ASP A 231     4544   4866   4506     37   -149    211       O  
ATOM   1702  N   GLY A 232     116.771  75.939  36.761  1.00 34.58           N  
ANISOU 1702  N   GLY A 232     4236   4644   4258    150    -18    357       N  
ATOM   1703  CA  GLY A 232     117.259  74.551  36.870  1.00 34.13           C  
ANISOU 1703  CA  GLY A 232     4156   4568   4242    142     15    390       C  
ATOM   1704  C   GLY A 232     117.877  73.989  35.610  1.00 33.25           C  
ANISOU 1704  C   GLY A 232     4042   4411   4179     74      3    355       C  
ATOM   1705  O   GLY A 232     118.168  72.788  35.572  1.00 33.76           O  
ANISOU 1705  O   GLY A 232     4092   4447   4289     66     35    380       O  
ATOM   1706  N   LEU A 233     118.162  74.841  34.613  1.00 31.65           N  
ANISOU 1706  N   LEU A 233     3856   4202   3966     34    -38    303       N  
ATOM   1707  CA  LEU A 233     118.636  74.378  33.318  1.00 32.11           C  
ANISOU 1707  CA  LEU A 233     3914   4227   4057    -19    -45    271       C  
ATOM   1708  C   LEU A 233     120.127  73.978  33.337  1.00 31.38           C  
ANISOU 1708  C   LEU A 233     3832   4131   3960    -10    -44    265       C  
ATOM   1709  O   LEU A 233     120.921  74.629  33.994  1.00 30.76           O  
ANISOU 1709  O   LEU A 233     3762   4081   3846     17    -65    265       O  
ATOM   1710  CB  LEU A 233     118.435  75.465  32.256  1.00 34.44           C  
ANISOU 1710  CB  LEU A 233     4217   4529   4338    -52    -82    232       C  
ATOM   1711  CG  LEU A 233     116.978  75.814  31.907  1.00 35.98           C  
ANISOU 1711  CG  LEU A 233     4397   4731   4544    -69    -85    239       C  
ATOM   1712  CD1 LEU A 233     117.003  77.027  31.013  1.00 36.13           C  
ANISOU 1712  CD1 LEU A 233     4423   4765   4539    -87   -118    210       C  
ATOM   1713  CD2 LEU A 233     116.299  74.631  31.238  1.00 36.00           C  
ANISOU 1713  CD2 LEU A 233     4378   4702   4598   -109    -72    242       C  
ATOM   1714  N   PRO A 234     120.497  72.938  32.573  1.00 30.69           N  
ANISOU 1714  N   PRO A 234     3744   4007   3909    -32    -23    258       N  
ATOM   1715  CA  PRO A 234     121.883  72.509  32.469  1.00 30.98           C  
ANISOU 1715  CA  PRO A 234     3787   4041   3944    -18    -12    262       C  
ATOM   1716  C   PRO A 234     122.706  73.439  31.627  1.00 30.66           C  
ANISOU 1716  C   PRO A 234     3753   4018   3879    -33    -46    235       C  
ATOM   1717  O   PRO A 234     122.294  73.852  30.559  1.00 31.67           O  
ANISOU 1717  O   PRO A 234     3886   4141   4004    -62    -61    205       O  
ATOM   1718  CB  PRO A 234     121.799  71.111  31.797  1.00 30.33           C  
ANISOU 1718  CB  PRO A 234     3709   3903   3910    -33     25    257       C  
ATOM   1719  CG  PRO A 234     120.474  71.088  31.104  1.00 30.55           C  
ANISOU 1719  CG  PRO A 234     3737   3909   3963    -75     11    229       C  
ATOM   1720  CD  PRO A 234     119.596  72.162  31.683  1.00 30.11           C  
ANISOU 1720  CD  PRO A 234     3667   3892   3881    -72    -12    242       C  
ATOM   1721  N   ILE A 235     123.904  73.729  32.101  1.00 31.76           N  
ANISOU 1721  N   ILE A 235     3885   4181   4002    -11    -57    255       N  
ATOM   1722  CA  ILE A 235     124.845  74.572  31.435  1.00 31.31           C  
ANISOU 1722  CA  ILE A 235     3821   4141   3936    -23    -85    249       C  
ATOM   1723  C   ILE A 235     125.659  73.618  30.605  1.00 33.28           C  
ANISOU 1723  C   ILE A 235     4069   4374   4201    -15    -47    261       C  
ATOM   1724  O   ILE A 235     126.164  72.594  31.097  1.00 35.60           O  
ANISOU 1724  O   ILE A 235     4361   4658   4507     12    -12    288       O  
ATOM   1725  CB  ILE A 235     125.685  75.335  32.482  1.00 34.20           C  
ANISOU 1725  CB  ILE A 235     4172   4538   4286     -7   -125    267       C  
ATOM   1726  CG1 ILE A 235     124.803  76.361  33.210  1.00 33.25           C  
ANISOU 1726  CG1 ILE A 235     4066   4427   4142     -6   -163    243       C  
ATOM   1727  CG2 ILE A 235     126.894  76.064  31.849  1.00 34.77           C  
ANISOU 1727  CG2 ILE A 235     4221   4621   4370    -22   -153    281       C  
ATOM   1728  CD1 ILE A 235     125.320  76.661  34.590  1.00 34.95           C  
ANISOU 1728  CD1 ILE A 235     4280   4671   4328     26   -195    250       C  
ATOM   1729  N   GLY A 236     125.808  73.928  29.329  1.00 33.66           N  
ANISOU 1729  N   GLY A 236     4121   4421   4245    -29    -49    244       N  
ATOM   1730  CA  GLY A 236     126.459  72.991  28.421  1.00 34.12           C  
ANISOU 1730  CA  GLY A 236     4191   4465   4307     -9     -8    247       C  
ATOM   1731  C   GLY A 236     125.524  72.162  27.571  1.00 33.44           C  
ANISOU 1731  C   GLY A 236     4140   4343   4225    -20     11    198       C  
ATOM   1732  O   GLY A 236     125.976  71.517  26.635  1.00 34.81           O  
ANISOU 1732  O   GLY A 236     4334   4503   4390      1     39    185       O  
ATOM   1733  N   ALA A 237     124.232  72.128  27.873  1.00 32.73           N  
ANISOU 1733  N   ALA A 237     4055   4235   4146    -49     -5    172       N  
ATOM   1734  CA  ALA A 237     123.253  71.479  26.946  1.00 32.26           C  
ANISOU 1734  CA  ALA A 237     4021   4142   4093    -72     -6    121       C  
ATOM   1735  C   ALA A 237     123.021  72.334  25.687  1.00 32.53           C  
ANISOU 1735  C   ALA A 237     4059   4212   4088    -83    -34     91       C  
ATOM   1736  O   ALA A 237     123.132  73.577  25.743  1.00 31.37           O  
ANISOU 1736  O   ALA A 237     3890   4106   3923    -87    -57    114       O  
ATOM   1737  CB  ALA A 237     121.933  71.237  27.650  1.00 33.19           C  
ANISOU 1737  CB  ALA A 237     4129   4237   4245   -101    -16    118       C  
ATOM   1738  N   LYS A 238     122.727  71.662  24.572  1.00 32.92           N  
ANISOU 1738  N   LYS A 238     4139   4244   4124    -85    -33     41       N  
ATOM   1739  CA  LYS A 238     122.563  72.280  23.241  1.00 35.45           C  
ANISOU 1739  CA  LYS A 238     4468   4607   4394    -81    -54     13       C  
ATOM   1740  C   LYS A 238     121.156  72.167  22.692  1.00 36.01           C  
ANISOU 1740  C   LYS A 238     4545   4675   4463   -121    -94    -38       C  
ATOM   1741  O   LYS A 238     120.435  71.237  23.024  1.00 36.65           O  
ANISOU 1741  O   LYS A 238     4635   4703   4586   -150   -100    -66       O  
ATOM   1742  CB  LYS A 238     123.532  71.644  22.241  1.00 37.06           C  
ANISOU 1742  CB  LYS A 238     4707   4813   4563    -32    -23     -6       C  
ATOM   1743  CG  LYS A 238     124.965  72.019  22.568  1.00 36.40           C  
ANISOU 1743  CG  LYS A 238     4600   4753   4476      9     12     62       C  
ATOM   1744  CD  LYS A 238     125.965  71.248  21.753  1.00 37.73           C  
ANISOU 1744  CD  LYS A 238     4801   4920   4615     70     56     58       C  
ATOM   1745  CE  LYS A 238     127.360  71.738  22.081  1.00 39.17           C  
ANISOU 1745  CE  LYS A 238     4944   5137   4803    107     87    143       C  
ATOM   1746  NZ  LYS A 238     128.329  71.251  21.075  1.00 41.91           N  
ANISOU 1746  NZ  LYS A 238     5313   5502   5108    179    136    156       N  
ATOM   1747  N   ASP A 239     120.768  73.166  21.908  1.00 35.43           N  
ANISOU 1747  N   ASP A 239     4457   4658   4347   -124   -120    -39       N  
ATOM   1748  CA  ASP A 239     119.563  73.150  21.062  1.00 36.24           C  
ANISOU 1748  CA  ASP A 239     4563   4779   4429   -154   -163    -87       C  
ATOM   1749  C   ASP A 239     119.841  72.317  19.794  1.00 37.78           C  
ANISOU 1749  C   ASP A 239     4805   4973   4575   -127   -167   -153       C  
ATOM   1750  O   ASP A 239     120.911  71.775  19.664  1.00 37.17           O  
ANISOU 1750  O   ASP A 239     4758   4879   4487    -83   -129   -155       O  
ATOM   1751  CB  ASP A 239     119.084  74.583  20.744  1.00 35.24           C  
ANISOU 1751  CB  ASP A 239     4398   4719   4272   -157   -183    -51       C  
ATOM   1752  CG  ASP A 239     120.051  75.378  19.911  1.00 37.34           C  
ANISOU 1752  CG  ASP A 239     4661   5039   4487   -110   -165    -22       C  
ATOM   1753  OD1 ASP A 239     120.945  74.807  19.259  1.00 37.06           O  
ANISOU 1753  OD1 ASP A 239     4655   5007   4419    -68   -141    -38       O  
ATOM   1754  OD2 ASP A 239     119.926  76.631  19.900  1.00 41.19           O  
ANISOU 1754  OD2 ASP A 239     5114   5567   4971   -108   -170     26       O  
ATOM   1755  N   ASN A 240     118.867  72.183  18.889  1.00 40.69           N  
ANISOU 1755  N   ASN A 240     5183   5364   4915   -149   -215   -209       N  
ATOM   1756  CA  ASN A 240     119.015  71.370  17.638  1.00 41.84           C  
ANISOU 1756  CA  ASN A 240     5386   5512   5002   -120   -232   -291       C  
ATOM   1757  C   ASN A 240     119.974  72.004  16.637  1.00 41.03           C  
ANISOU 1757  C   ASN A 240     5294   5486   4808    -43   -203   -270       C  
ATOM   1758  O   ASN A 240     120.444  71.342  15.764  1.00 42.51           O  
ANISOU 1758  O   ASN A 240     5535   5677   4940      6   -195   -324       O  
ATOM   1759  CB  ASN A 240     117.693  71.295  16.846  1.00 44.73           C  
ANISOU 1759  CB  ASN A 240     5748   5902   5344   -161   -305   -353       C  
ATOM   1760  CG  ASN A 240     116.521  70.825  17.658  1.00 45.37           C  
ANISOU 1760  CG  ASN A 240     5799   5924   5517   -241   -342   -359       C  
ATOM   1761  OD1 ASN A 240     115.546  71.570  17.854  1.00 45.12           O  
ANISOU 1761  OD1 ASN A 240     5713   5931   5498   -279   -371   -322       O  
ATOM   1762  ND2 ASN A 240     116.592  69.600  18.123  1.00 46.22           N  
ANISOU 1762  ND2 ASN A 240     5936   5936   5691   -263   -336   -396       N  
ATOM   1763  N   ASP A 241     120.158  73.314  16.697  1.00 38.80           N  
ANISOU 1763  N   ASP A 241     4963   5268   4512    -31   -189   -193       N  
ATOM   1764  CA  ASP A 241     121.076  73.991  15.812  1.00 41.30           C  
ANISOU 1764  CA  ASP A 241     5276   5658   4760     41   -155   -150       C  
ATOM   1765  C   ASP A 241     122.534  74.072  16.374  1.00 40.49           C  
ANISOU 1765  C   ASP A 241     5163   5536   4686     81    -93    -81       C  
ATOM   1766  O   ASP A 241     123.371  74.796  15.824  1.00 41.47           O  
ANISOU 1766  O   ASP A 241     5263   5717   4775    135    -59    -16       O  
ATOM   1767  CB  ASP A 241     120.490  75.358  15.491  1.00 43.69           C  
ANISOU 1767  CB  ASP A 241     5523   6033   5043     32   -174    -97       C  
ATOM   1768  CG  ASP A 241     119.012  75.277  15.002  1.00 46.59           C  
ANISOU 1768  CG  ASP A 241     5889   6426   5386    -10   -238   -154       C  
ATOM   1769  OD1 ASP A 241     118.609  74.305  14.313  1.00 54.33           O  
ANISOU 1769  OD1 ASP A 241     6916   7401   6325     -9   -274   -243       O  
ATOM   1770  OD2 ASP A 241     118.219  76.164  15.333  1.00 45.38           O  
ANISOU 1770  OD2 ASP A 241     5688   6295   5259    -46   -258   -113       O  
ATOM   1771  N   GLY A 242     122.805  73.374  17.484  1.00 38.93           N  
ANISOU 1771  N   GLY A 242     4975   5263   4556     54    -79    -83       N  
ATOM   1772  CA  GLY A 242     124.168  73.232  18.039  1.00 39.05           C  
ANISOU 1772  CA  GLY A 242     4980   5258   4597     90    -26    -24       C  
ATOM   1773  C   GLY A 242     124.660  74.264  19.064  1.00 36.57           C  
ANISOU 1773  C   GLY A 242     4606   4949   4339     67    -20     61       C  
ATOM   1774  O   GLY A 242     125.798  74.185  19.503  1.00 36.89           O  
ANISOU 1774  O   GLY A 242     4632   4981   4402     94     15    114       O  
ATOM   1775  N   GLY A 243     123.830  75.230  19.428  1.00 35.22           N  
ANISOU 1775  N   GLY A 243     4403   4791   4189     22    -56     74       N  
ATOM   1776  CA  GLY A 243     124.210  76.254  20.409  1.00 36.61           C  
ANISOU 1776  CA  GLY A 243     4531   4962   4416      0    -61    139       C  
ATOM   1777  C   GLY A 243     123.748  75.952  21.847  1.00 34.68           C  
ANISOU 1777  C   GLY A 243     4288   4665   4223    -43    -77    125       C  
ATOM   1778  O   GLY A 243     122.773  75.231  22.071  1.00 35.86           O  
ANISOU 1778  O   GLY A 243     4461   4786   4379    -69    -90     76       O  
ATOM   1779  N   PHE A 244     124.396  76.583  22.808  1.00 31.31           N  
ANISOU 1779  N   PHE A 244     3834   4230   3834    -50    -80    172       N  
ATOM   1780  CA  PHE A 244     124.087  76.366  24.228  1.00 29.47           C  
ANISOU 1780  CA  PHE A 244     3602   3960   3636    -74    -92    167       C  
ATOM   1781  C   PHE A 244     122.722  76.931  24.587  1.00 29.55           C  
ANISOU 1781  C   PHE A 244     3609   3968   3650   -105   -121    147       C  
ATOM   1782  O   PHE A 244     122.347  78.023  24.153  1.00 26.49           O  
ANISOU 1782  O   PHE A 244     3205   3605   3254   -112   -139    159       O  
ATOM   1783  CB  PHE A 244     125.159  76.957  25.148  1.00 29.10           C  
ANISOU 1783  CB  PHE A 244     3526   3912   3618    -69    -99    215       C  
ATOM   1784  CG  PHE A 244     126.525  76.307  25.020  1.00 29.58           C  
ANISOU 1784  CG  PHE A 244     3579   3977   3683    -36    -67    250       C  
ATOM   1785  CD1 PHE A 244     126.661  74.936  25.011  1.00 31.68           C  
ANISOU 1785  CD1 PHE A 244     3873   4220   3941    -15    -31    231       C  
ATOM   1786  CD2 PHE A 244     127.673  77.087  24.946  1.00 30.26           C  
ANISOU 1786  CD2 PHE A 244     3624   4084   3790    -27    -73    309       C  
ATOM   1787  CE1 PHE A 244     127.923  74.329  24.930  1.00 34.13           C  
ANISOU 1787  CE1 PHE A 244     4177   4536   4256     24      6    271       C  
ATOM   1788  CE2 PHE A 244     128.925  76.515  24.864  1.00 31.36           C  
ANISOU 1788  CE2 PHE A 244     3747   4234   3937      6    -41    354       C  
ATOM   1789  CZ  PHE A 244     129.052  75.135  24.866  1.00 33.80           C  
ANISOU 1789  CZ  PHE A 244     4088   4526   4229     36      1    336       C  
ATOM   1790  N   ILE A 245     121.960  76.135  25.340  1.00 29.40           N  
ANISOU 1790  N   ILE A 245     3605   3921   3647   -119   -119    124       N  
ATOM   1791  CA  ILE A 245     120.685  76.565  25.888  1.00 31.14           C  
ANISOU 1791  CA  ILE A 245     3817   4140   3875   -141   -139    120       C  
ATOM   1792  C   ILE A 245     120.876  77.739  26.841  1.00 31.23           C  
ANISOU 1792  C   ILE A 245     3815   4157   3892   -133   -155    147       C  
ATOM   1793  O   ILE A 245     120.181  78.773  26.703  1.00 30.85           O  
ANISOU 1793  O   ILE A 245     3759   4124   3839   -139   -173    152       O  
ATOM   1794  CB  ILE A 245     120.017  75.404  26.686  1.00 31.71           C  
ANISOU 1794  CB  ILE A 245     3896   4177   3975   -149   -125    112       C  
ATOM   1795  CG1 ILE A 245     119.610  74.247  25.763  1.00 33.07           C  
ANISOU 1795  CG1 ILE A 245     4084   4326   4155   -167   -120     72       C  
ATOM   1796  CG2 ILE A 245     118.855  75.910  27.526  1.00 32.76           C  
ANISOU 1796  CG2 ILE A 245     4013   4315   4117   -156   -135    129       C  
ATOM   1797  CD1 ILE A 245     118.641  74.634  24.639  1.00 34.97           C  
ANISOU 1797  CD1 ILE A 245     4319   4595   4373   -191   -151     44       C  
ATOM   1798  N   LYS A 246     121.793  77.534  27.802  1.00 30.44           N  
ANISOU 1798  N   LYS A 246     3718   4046   3802   -116   -150    163       N  
ATOM   1799  CA  LYS A 246     121.999  78.418  28.934  1.00 33.39           C  
ANISOU 1799  CA  LYS A 246     4089   4420   4178   -106   -174    175       C  
ATOM   1800  C   LYS A 246     123.476  78.744  29.152  1.00 32.95           C  
ANISOU 1800  C   LYS A 246     4021   4366   4133    -99   -189    194       C  
ATOM   1801  O   LYS A 246     124.330  77.877  29.023  1.00 34.14           O  
ANISOU 1801  O   LYS A 246     4167   4517   4288    -89   -168    209       O  
ATOM   1802  CB  LYS A 246     121.427  77.737  30.193  1.00 34.56           C  
ANISOU 1802  CB  LYS A 246     4248   4561   4322    -87   -161    177       C  
ATOM   1803  CG  LYS A 246     121.485  78.563  31.458  1.00 38.22           C  
ANISOU 1803  CG  LYS A 246     4721   5033   4769    -62   -186    179       C  
ATOM   1804  CD  LYS A 246     120.389  79.620  31.529  1.00 41.17           C  
ANISOU 1804  CD  LYS A 246     5103   5409   5132    -58   -201    169       C  
ATOM   1805  CE  LYS A 246     120.579  80.429  32.820  1.00 44.49           C  
ANISOU 1805  CE  LYS A 246     5545   5831   5528    -23   -230    158       C  
ATOM   1806  NZ  LYS A 246     119.510  81.418  33.025  1.00 43.48           N  
ANISOU 1806  NZ  LYS A 246     5433   5701   5385     -4   -235    149       N  
ATOM   1807  N   VAL A 247     123.757  79.998  29.496  1.00 31.65           N  
ANISOU 1807  N   VAL A 247     3850   4198   3978   -103   -228    197       N  
ATOM   1808  CA  VAL A 247     125.123  80.451  29.763  1.00 31.23           C  
ANISOU 1808  CA  VAL A 247     3774   4143   3948   -107   -257    219       C  
ATOM   1809  C   VAL A 247     125.232  80.691  31.267  1.00 30.32           C  
ANISOU 1809  C   VAL A 247     3675   4025   3822    -92   -294    201       C  
ATOM   1810  O   VAL A 247     124.413  81.393  31.853  1.00 28.85           O  
ANISOU 1810  O   VAL A 247     3513   3828   3619    -84   -314    173       O  
ATOM   1811  CB  VAL A 247     125.511  81.709  28.938  1.00 31.60           C  
ANISOU 1811  CB  VAL A 247     3795   4180   4030   -128   -281    240       C  
ATOM   1812  CG1 VAL A 247     126.905  82.201  29.270  1.00 32.70           C  
ANISOU 1812  CG1 VAL A 247     3902   4312   4212   -140   -319    270       C  
ATOM   1813  CG2 VAL A 247     125.504  81.368  27.475  1.00 32.61           C  
ANISOU 1813  CG2 VAL A 247     3908   4329   4155   -126   -241    263       C  
ATOM   1814  N   GLU A 248     126.269  80.130  31.884  1.00 30.19           N  
ANISOU 1814  N   GLU A 248     3644   4021   3805    -82   -301    220       N  
ATOM   1815  CA  GLU A 248     126.493  80.347  33.322  1.00 30.96           C  
ANISOU 1815  CA  GLU A 248     3755   4128   3880    -62   -344    202       C  
ATOM   1816  C   GLU A 248     126.556  81.840  33.700  1.00 30.07           C  
ANISOU 1816  C   GLU A 248     3652   3991   3781    -77   -413    169       C  
ATOM   1817  O   GLU A 248     127.283  82.577  33.085  1.00 28.82           O  
ANISOU 1817  O   GLU A 248     3465   3812   3673   -111   -444    185       O  
ATOM   1818  CB  GLU A 248     127.800  79.712  33.756  1.00 32.49           C  
ANISOU 1818  CB  GLU A 248     3919   4346   4080    -54   -352    236       C  
ATOM   1819  CG  GLU A 248     128.058  79.798  35.276  1.00 34.59           C  
ANISOU 1819  CG  GLU A 248     4198   4638   4308    -25   -399    218       C  
ATOM   1820  CD  GLU A 248     129.248  78.951  35.709  1.00 36.04           C  
ANISOU 1820  CD  GLU A 248     4346   4858   4491     -9   -396    264       C  
ATOM   1821  OE1 GLU A 248     129.755  78.157  34.871  1.00 36.21           O  
ANISOU 1821  OE1 GLU A 248     4339   4879   4540    -14   -344    309       O  
ATOM   1822  OE2 GLU A 248     129.685  79.123  36.865  1.00 34.34           O  
ANISOU 1822  OE2 GLU A 248     4131   4673   4244     12   -447    253       O  
ATOM   1823  N   GLY A 249     125.807  82.240  34.723  1.00 30.43           N  
ANISOU 1823  N   GLY A 249     3740   4036   3785    -47   -435    128       N  
ATOM   1824  CA  GLY A 249     125.807  83.612  35.223  1.00 32.29           C  
ANISOU 1824  CA  GLY A 249     4000   4239   4029    -52   -504     82       C  
ATOM   1825  C   GLY A 249     124.994  84.597  34.377  1.00 33.62           C  
ANISOU 1825  C   GLY A 249     4178   4367   4228    -70   -495     73       C  
ATOM   1826  O   GLY A 249     124.934  85.780  34.655  1.00 34.37           O  
ANISOU 1826  O   GLY A 249     4296   4421   4343    -74   -545     38       O  
ATOM   1827  N   GLN A 250     124.350  84.120  33.333  1.00 34.28           N  
ANISOU 1827  N   GLN A 250     4247   4461   4319    -78   -434    105       N  
ATOM   1828  CA  GLN A 250     123.631  85.007  32.450  1.00 35.05           C  
ANISOU 1828  CA  GLN A 250     4344   4532   4443    -92   -423    108       C  
ATOM   1829  C   GLN A 250     122.190  85.076  32.940  1.00 34.14           C  
ANISOU 1829  C   GLN A 250     4268   4424   4281    -52   -396     86       C  
ATOM   1830  O   GLN A 250     121.595  84.083  33.236  1.00 31.31           O  
ANISOU 1830  O   GLN A 250     3915   4098   3884    -29   -357     95       O  
ATOM   1831  CB  GLN A 250     123.702  84.505  31.031  1.00 35.66           C  
ANISOU 1831  CB  GLN A 250     4381   4626   4542   -116   -378    152       C  
ATOM   1832  CG  GLN A 250     123.266  85.542  30.009  1.00 37.47           C  
ANISOU 1832  CG  GLN A 250     4596   4835   4806   -131   -373    170       C  
ATOM   1833  CD  GLN A 250     123.585  85.111  28.585  1.00 39.27           C  
ANISOU 1833  CD  GLN A 250     4784   5091   5047   -147   -335    216       C  
ATOM   1834  OE1 GLN A 250     123.152  84.062  28.141  1.00 40.07           O  
ANISOU 1834  OE1 GLN A 250     4887   5226   5112   -138   -297    216       O  
ATOM   1835  NE2 GLN A 250     124.338  85.927  27.866  1.00 42.43           N  
ANISOU 1835  NE2 GLN A 250     5145   5474   5500   -165   -348    256       N  
ATOM   1836  N   LYS A 251     121.646  86.277  32.973  1.00 33.10           N  
ANISOU 1836  N   LYS A 251     4158   4256   4161    -43   -414     67       N  
ATOM   1837  CA  LYS A 251     120.250  86.512  33.294  1.00 32.94           C  
ANISOU 1837  CA  LYS A 251     4169   4244   4102      0   -383     60       C  
ATOM   1838  C   LYS A 251     119.318  86.013  32.188  1.00 30.96           C  
ANISOU 1838  C   LYS A 251     3886   4023   3855    -13   -327    102       C  
ATOM   1839  O   LYS A 251     119.750  85.685  31.092  1.00 31.55           O  
ANISOU 1839  O   LYS A 251     3923   4107   3958    -52   -317    128       O  
ATOM   1840  CB  LYS A 251     120.040  88.014  33.549  1.00 34.40           C  
ANISOU 1840  CB  LYS A 251     4389   4374   4308     16   -417     28       C  
ATOM   1841  CG  LYS A 251     120.888  88.499  34.728  1.00 37.23           C  
ANISOU 1841  CG  LYS A 251     4788   4701   4658     30   -487    -30       C  
ATOM   1842  CD  LYS A 251     120.726  89.978  34.953  1.00 40.48           C  
ANISOU 1842  CD  LYS A 251     5240   5041   5099     43   -527    -71       C  
ATOM   1843  CE  LYS A 251     121.514  90.397  36.168  1.00 43.70           C  
ANISOU 1843  CE  LYS A 251     5695   5419   5490     58   -607   -144       C  
ATOM   1844  NZ  LYS A 251     121.188  91.819  36.424  1.00 47.23           N  
ANISOU 1844  NZ  LYS A 251     6195   5785   5964     79   -643   -194       N  
ATOM   1845  N   ALA A 252     118.020  86.029  32.502  1.00 29.23           N  
ANISOU 1845  N   ALA A 252     3682   3821   3603     25   -295    110       N  
ATOM   1846  CA  ALA A 252     116.934  85.650  31.602  1.00 26.72           C  
ANISOU 1846  CA  ALA A 252     3333   3535   3287     15   -252    149       C  
ATOM   1847  C   ALA A 252     115.868  86.747  31.598  1.00 26.20           C  
ANISOU 1847  C   ALA A 252     3279   3459   3217     48   -239    160       C  
ATOM   1848  O   ALA A 252     115.858  87.646  32.444  1.00 27.46           O  
ANISOU 1848  O   ALA A 252     3482   3587   3366     90   -255    133       O  
ATOM   1849  CB  ALA A 252     116.323  84.316  32.064  1.00 25.74           C  
ANISOU 1849  CB  ALA A 252     3199   3447   3136     27   -219    166       C  
ATOM   1850  N   GLY A 253     114.944  86.640  30.649  1.00 25.85           N  
ANISOU 1850  N   GLY A 253     3120   3390   3314    -29   -160    130       N  
ATOM   1851  CA  GLY A 253     113.877  87.613  30.438  1.00 25.19           C  
ANISOU 1851  CA  GLY A 253     3046   3300   3225    -32   -149    109       C  
ATOM   1852  C   GLY A 253     114.126  88.672  29.385  1.00 25.84           C  
ANISOU 1852  C   GLY A 253     3124   3369   3323    -33   -148     95       C  
ATOM   1853  O   GLY A 253     115.218  88.789  28.780  1.00 25.50           O  
ANISOU 1853  O   GLY A 253     3071   3323   3297    -35   -156     99       O  
ATOM   1854  N   PHE A 254     113.077  89.443  29.160  1.00 25.95           N  
ANISOU 1854  N   PHE A 254     3148   3378   3336    -33   -137     79       N  
ATOM   1855  CA  PHE A 254     113.073  90.448  28.142  1.00 25.68           C  
ANISOU 1855  CA  PHE A 254     3111   3331   3316    -33   -133     67       C  
ATOM   1856  C   PHE A 254     114.207  91.439  28.261  1.00 26.08           C  
ANISOU 1856  C   PHE A 254     3159   3381   3370    -41   -146     60       C  
ATOM   1857  O   PHE A 254     114.882  91.722  27.257  1.00 25.76           O  
ANISOU 1857  O   PHE A 254     3109   3330   3348    -41   -147     61       O  
ATOM   1858  CB  PHE A 254     111.733  91.159  28.125  1.00 25.86           C  
ANISOU 1858  CB  PHE A 254     3144   3350   3333    -30   -119     52       C  
ATOM   1859  CG  PHE A 254     111.511  92.008  26.915  1.00 26.36           C  
ANISOU 1859  CG  PHE A 254     3203   3399   3413    -26   -111     45       C  
ATOM   1860  CD1 PHE A 254     111.414  91.441  25.673  1.00 26.74           C  
ANISOU 1860  CD1 PHE A 254     3242   3440   3476    -20   -105     54       C  
ATOM   1861  CD2 PHE A 254     111.322  93.395  27.039  1.00 27.15           C  
ANISOU 1861  CD2 PHE A 254     3311   3493   3513    -29   -109     29       C  
ATOM   1862  CE1 PHE A 254     111.151  92.227  24.528  1.00 27.92           C  
ANISOU 1862  CE1 PHE A 254     3389   3579   3639    -16    -98     49       C  
ATOM   1863  CE2 PHE A 254     111.074  94.180  25.904  1.00 28.19           C  
ANISOU 1863  CE2 PHE A 254     3439   3611   3660    -24   -101     25       C  
ATOM   1864  CZ  PHE A 254     110.977  93.597  24.649  1.00 27.40           C  
ANISOU 1864  CZ  PHE A 254     3330   3507   3574    -17    -96     36       C  
ATOM   1865  N   LEU A 255     114.420  91.971  29.469  1.00 28.13           N  
ANISOU 1865  N   LEU A 255     3425   3650   3611    -50   -155     51       N  
ATOM   1866  CA  LEU A 255     115.494  92.963  29.667  1.00 27.87           C  
ANISOU 1866  CA  LEU A 255     3389   3618   3581    -62   -168     41       C  
ATOM   1867  C   LEU A 255     116.866  92.392  29.370  1.00 26.75           C  
ANISOU 1867  C   LEU A 255     3233   3481   3452    -63   -182     57       C  
ATOM   1868  O   LEU A 255     117.715  93.093  28.770  1.00 26.44           O  
ANISOU 1868  O   LEU A 255     3186   3433   3428    -69   -186     52       O  
ATOM   1869  CB  LEU A 255     115.441  93.577  31.065  1.00 29.15           C  
ANISOU 1869  CB  LEU A 255     3563   3793   3719    -73   -175     27       C  
ATOM   1870  CG  LEU A 255     114.102  94.238  31.417  1.00 30.70           C  
ANISOU 1870  CG  LEU A 255     3776   3985   3904    -71   -160      9       C  
ATOM   1871  CD1 LEU A 255     114.188  94.854  32.803  1.00 31.39           C  
ANISOU 1871  CD1 LEU A 255     3875   4086   3967    -84   -167     -6       C  
ATOM   1872  CD2 LEU A 255     113.663  95.291  30.390  1.00 30.96           C  
ANISOU 1872  CD2 LEU A 255     3810   3997   3957    -67   -146     -3       C  
ATOM   1873  N   ALA A 256     117.099  91.134  29.741  1.00 26.40           N  
ANISOU 1873  N   ALA A 256     3182   3446   3402    -58   -187     76       N  
ATOM   1874  CA  ALA A 256     118.417  90.475  29.456  1.00 26.97           C  
ANISOU 1874  CA  ALA A 256     3238   3523   3488    -57   -199     93       C  
ATOM   1875  C   ALA A 256     118.615  90.320  27.929  1.00 28.06           C  
ANISOU 1875  C   ALA A 256     3367   3643   3653    -50   -188     98       C  
ATOM   1876  O   ALA A 256     119.734  90.441  27.419  1.00 28.41           O  
ANISOU 1876  O   ALA A 256     3398   3684   3713    -52   -195    103       O  
ATOM   1877  CB  ALA A 256     118.496  89.100  30.148  1.00 26.13           C  
ANISOU 1877  CB  ALA A 256     3128   3429   3372    -51   -203    115       C  
ATOM   1878  N   ASN A 257     117.499  90.038  27.220  1.00 26.35           N  
ANISOU 1878  N   ASN A 257     3157   3416   3441    -42   -171     96       N  
ATOM   1879  CA  ASN A 257     117.496  89.927  25.771  1.00 26.37           C  
ANISOU 1879  CA  ASN A 257     3153   3404   3465    -35   -159     98       C  
ATOM   1880  C   ASN A 257     117.700  91.244  25.045  1.00 26.91           C  
ANISOU 1880  C   ASN A 257     3221   3461   3543    -40   -157     85       C  
ATOM   1881  O   ASN A 257     117.996  91.235  23.876  1.00 27.78           O  
ANISOU 1881  O   ASN A 257     3324   3561   3670    -36   -150     88       O  
ATOM   1882  CB  ASN A 257     116.270  89.165  25.254  1.00 25.05           C  
ANISOU 1882  CB  ASN A 257     2990   3230   3296    -27   -143    101       C  
ATOM   1883  CG  ASN A 257     116.465  87.644  25.318  1.00 26.53           C  
ANISOU 1883  CG  ASN A 257     3173   3421   3488    -21   -141    119       C  
ATOM   1884  OD1 ASN A 257     117.163  87.044  24.494  1.00 27.29           O  
ANISOU 1884  OD1 ASN A 257     3258   3509   3601    -17   -138    128       O  
ATOM   1885  ND2 ASN A 257     115.884  87.031  26.300  1.00 26.62           N  
ANISOU 1885  ND2 ASN A 257     3191   3441   3484    -20   -141    123       N  
ATOM   1886  N   ILE A 258     117.518  92.375  25.715  1.00 27.43           N  
ANISOU 1886  N   ILE A 258     3295   3528   3598    -48   -161     69       N  
ATOM   1887  CA  ILE A 258     117.932  93.665  25.195  1.00 29.31           C  
ANISOU 1887  CA  ILE A 258     3533   3755   3848    -54   -160     58       C  
ATOM   1888  C   ILE A 258     119.413  93.970  25.544  1.00 30.54           C  
ANISOU 1888  C   ILE A 258     3678   3916   4010    -65   -176     59       C  
ATOM   1889  O   ILE A 258     120.134  94.523  24.726  1.00 31.67           O  
ANISOU 1889  O   ILE A 258     3814   4050   4171    -68   -175     59       O  
ATOM   1890  CB  ILE A 258     117.085  94.777  25.819  1.00 30.35           C  
ANISOU 1890  CB  ILE A 258     3679   3884   3967    -59   -156     39       C  
ATOM   1891  CG1 ILE A 258     115.647  94.602  25.369  1.00 30.16           C  
ANISOU 1891  CG1 ILE A 258     3664   3856   3941    -48   -140     38       C  
ATOM   1892  CG2 ILE A 258     117.616  96.167  25.440  1.00 31.76           C  
ANISOU 1892  CG2 ILE A 258     3859   4050   4159    -67   -155     26       C  
ATOM   1893  CD1 ILE A 258     114.713  95.588  25.993  1.00 31.07           C  
ANISOU 1893  CD1 ILE A 258     3792   3968   4045    -49   -133     21       C  
ATOM   1894  N   ASP A 259     119.819  93.684  26.782  1.00 31.55           N  
ANISOU 1894  N   ASP A 259     3805   4060   4121    -72   -191     60       N  
ATOM   1895  CA  ASP A 259     121.177  94.015  27.262  1.00 32.04           C  
ANISOU 1895  CA  ASP A 259     3856   4132   4187    -85   -209     61       C  
ATOM   1896  C   ASP A 259     122.263  93.188  26.617  1.00 31.37           C  
ANISOU 1896  C   ASP A 259     3751   4047   4119    -80   -214     80       C  
ATOM   1897  O   ASP A 259     123.293  93.746  26.311  1.00 29.79           O  
ANISOU 1897  O   ASP A 259     3541   3846   3934    -88   -220     78       O  
ATOM   1898  CB  ASP A 259     121.318  93.908  28.795  1.00 32.79           C  
ANISOU 1898  CB  ASP A 259     3955   4248   4256    -94   -225     57       C  
ATOM   1899  CG  ASP A 259     120.540  94.996  29.516  1.00 36.66           C  
ANISOU 1899  CG  ASP A 259     4462   4736   4729   -103   -222     33       C  
ATOM   1900  OD1 ASP A 259     120.617  96.176  29.071  1.00 37.24           O  
ANISOU 1900  OD1 ASP A 259     4540   4796   4814   -110   -216     17       O  
ATOM   1901  OD2 ASP A 259     119.856  94.698  30.517  1.00 36.32           O  
ANISOU 1901  OD2 ASP A 259     4430   4706   4662   -103   -223     31       O  
ATOM   1902  N   GLU A 260     122.038  91.883  26.454  1.00 28.93           N  
ANISOU 1902  N   GLU A 260     3439   3741   3811    -67   -210     98       N  
ATOM   1903  CA  GLU A 260     123.122  90.984  26.058  1.00 30.80           C  
ANISOU 1903  CA  GLU A 260     3658   3981   4064    -62   -215    117       C  
ATOM   1904  C   GLU A 260     123.459  90.796  24.565  1.00 28.49           C  
ANISOU 1904  C   GLU A 260     3355   3671   3797    -55   -201    123       C  
ATOM   1905  O   GLU A 260     124.633  90.813  24.216  1.00 28.43           O  
ANISOU 1905  O   GLU A 260     3332   3664   3806    -57   -207    131       O  
ATOM   1906  CB  GLU A 260     122.979  89.625  26.757  1.00 32.58           C  
ANISOU 1906  CB  GLU A 260     3881   4218   4279    -53   -218    136       C  
ATOM   1907  CG  GLU A 260     123.051  89.722  28.280  1.00 35.33           C  
ANISOU 1907  CG  GLU A 260     4234   4588   4602    -61   -236    135       C  
ATOM   1908  CD  GLU A 260     124.288  90.508  28.814  1.00 39.56           C  
ANISOU 1908  CD  GLU A 260     4757   5136   5137    -75   -256    131       C  
ATOM   1909  OE1 GLU A 260     125.389  90.248  28.311  1.00 37.64           O  
ANISOU 1909  OE1 GLU A 260     4495   4893   4914    -74   -262    143       O  
ATOM   1910  OE2 GLU A 260     124.150  91.410  29.713  1.00 41.01           O  
ANISOU 1910  OE2 GLU A 260     4949   5330   5302    -89   -267    113       O  
ATOM   1911  N   PRO A 261     122.453  90.604  23.685  1.00 26.71           N  
ANISOU 1911  N   PRO A 261     3140   3433   3574    -47   -183    120       N  
ATOM   1912  CA  PRO A 261     122.781  90.289  22.314  1.00 26.74           C  
ANISOU 1912  CA  PRO A 261     3135   3424   3599    -40   -170    127       C  
ATOM   1913  C   PRO A 261     122.804  91.531  21.391  1.00 26.52           C  
ANISOU 1913  C   PRO A 261     3110   3385   3581    -45   -163    114       C  
ATOM   1914  O   PRO A 261     122.994  91.404  20.209  1.00 26.51           O  
ANISOU 1914  O   PRO A 261     3104   3374   3595    -40   -151    118       O  
ATOM   1915  CB  PRO A 261     121.660  89.307  21.945  1.00 26.68           C  
ANISOU 1915  CB  PRO A 261     3137   3413   3587    -29   -156    130       C  
ATOM   1916  CG  PRO A 261     120.446  89.881  22.660  1.00 27.35           C  
ANISOU 1916  CG  PRO A 261     3238   3502   3651    -32   -156    117       C  
ATOM   1917  CD  PRO A 261     121.002  90.501  23.926  1.00 26.74           C  
ANISOU 1917  CD  PRO A 261     3161   3437   3563    -42   -174    113       C  
ATOM   1918  N   PHE A 262     122.601  92.718  21.942  1.00 26.62           N  
ANISOU 1918  N   PHE A 262     3130   3397   3585    -54   -168    100       N  
ATOM   1919  CA  PHE A 262     122.759  93.971  21.194  1.00 27.28           C  
ANISOU 1919  CA  PHE A 262     3216   3469   3681    -60   -162     90       C  
ATOM   1920  C   PHE A 262     124.019  94.653  21.686  1.00 27.49           C  
ANISOU 1920  C   PHE A 262     3231   3498   3714    -74   -176     87       C  
ATOM   1921  O   PHE A 262     124.252  94.712  22.910  1.00 27.40           O  
ANISOU 1921  O   PHE A 262     3221   3501   3691    -82   -191     82       O  
ATOM   1922  CB  PHE A 262     121.635  94.962  21.474  1.00 26.70           C  
ANISOU 1922  CB  PHE A 262     3159   3389   3595    -62   -156     74       C  
ATOM   1923  CG  PHE A 262     120.390  94.706  20.736  1.00 26.92           C  
ANISOU 1923  CG  PHE A 262     3197   3412   3620    -50   -141     75       C  
ATOM   1924  CD1 PHE A 262     120.275  95.011  19.393  1.00 27.43           C  
ANISOU 1924  CD1 PHE A 262     3260   3465   3697    -45   -128     78       C  
ATOM   1925  CD2 PHE A 262     119.278  94.161  21.391  1.00 28.47           C  
ANISOU 1925  CD2 PHE A 262     3403   3616   3799    -45   -140     72       C  
ATOM   1926  CE1 PHE A 262     119.082  94.772  18.686  1.00 27.42           C  
ANISOU 1926  CE1 PHE A 262     3266   3462   3691    -34   -115     78       C  
ATOM   1927  CE2 PHE A 262     118.110  93.905  20.701  1.00 28.97           C  
ANISOU 1927  CE2 PHE A 262     3472   3675   3859    -35   -127     73       C  
ATOM   1928  CZ  PHE A 262     117.986  94.245  19.346  1.00 28.93           C  
ANISOU 1928  CZ  PHE A 262     3465   3661   3866    -30   -115     75       C  
ATOM   1929  N   SER A 263     124.815  95.156  20.742  1.00 27.37           N  
ANISOU 1929  N   SER A 263     3207   3473   3720    -77   -170     89       N  
ATOM   1930  CA  SER A 263     125.939  95.996  21.049  1.00 26.26           C  
ANISOU 1930  CA  SER A 263     3056   3333   3589    -91   -180     83       C  
ATOM   1931  C   SER A 263     125.494  97.421  21.328  1.00 27.17           C  
ANISOU 1931  C   SER A 263     3185   3439   3700   -102   -178     64       C  
ATOM   1932  O   SER A 263     124.330  97.804  21.030  1.00 28.07           O  
ANISOU 1932  O   SER A 263     3315   3543   3808    -95   -165     58       O  
ATOM   1933  CB  SER A 263     126.908  95.954  19.854  1.00 28.45           C  
ANISOU 1933  CB  SER A 263     3317   3601   3890    -90   -172     94       C  
ATOM   1934  OG  SER A 263     126.466  96.773  18.794  1.00 27.32           O  
ANISOU 1934  OG  SER A 263     3183   3441   3755    -88   -155     89       O  
ATOM   1935  N   PRO A 264     126.423  98.272  21.805  1.00 27.77           N  
ANISOU 1935  N   PRO A 264     3253   3515   3782   -119   -188     55       N  
ATOM   1936  CA  PRO A 264     126.068  99.707  21.899  1.00 28.33           C  
ANISOU 1936  CA  PRO A 264     3337   3572   3856   -130   -181     36       C  
ATOM   1937  C   PRO A 264     125.791 100.399  20.536  1.00 29.33           C  
ANISOU 1937  C   PRO A 264     3468   3676   4000   -123   -160     38       C  
ATOM   1938  O   PRO A 264     125.266 101.474  20.531  1.00 28.58           O  
ANISOU 1938  O   PRO A 264     3387   3567   3907   -127   -151     26       O  
ATOM   1939  CB  PRO A 264     127.280 100.356  22.682  1.00 28.61           C  
ANISOU 1939  CB  PRO A 264     3361   3613   3895   -152   -197     26       C  
ATOM   1940  CG  PRO A 264     128.054  99.191  23.222  1.00 28.07           C  
ANISOU 1940  CG  PRO A 264     3276   3568   3822   -151   -215     40       C  
ATOM   1941  CD  PRO A 264     127.807  98.013  22.275  1.00 27.34           C  
ANISOU 1941  CD  PRO A 264     3178   3474   3735   -130   -205     61       C  
ATOM   1942  N   ASP A 265     126.073  99.762  19.387  1.00 30.24           N  
ANISOU 1942  N   ASP A 265     3574   3788   4128   -112   -151     55       N  
ATOM   1943  CA  ASP A 265     125.699 100.317  18.057  1.00 29.47           C  
ANISOU 1943  CA  ASP A 265     3483   3673   4043   -104   -131     60       C  
ATOM   1944  C   ASP A 265     124.355  99.818  17.509  1.00 29.78           C  
ANISOU 1944  C   ASP A 265     3533   3711   4069    -87   -120     65       C  
ATOM   1945  O   ASP A 265     124.000 100.074  16.353  1.00 30.92           O  
ANISOU 1945  O   ASP A 265     3680   3845   4221    -78   -105     72       O  
ATOM   1946  CB  ASP A 265     126.807  99.970  17.052  1.00 30.47           C  
ANISOU 1946  CB  ASP A 265     3592   3798   4189   -104   -127     74       C  
ATOM   1947  CG  ASP A 265     128.130 100.672  17.380  1.00 32.06           C  
ANISOU 1947  CG  ASP A 265     3779   3997   4406   -122   -135     69       C  
ATOM   1948  OD1 ASP A 265     128.060 101.813  17.834  1.00 34.17           O  
ANISOU 1948  OD1 ASP A 265     4054   4255   4675   -134   -135     54       O  
ATOM   1949  OD2 ASP A 265     129.231 100.091  17.203  1.00 33.10           O  
ANISOU 1949  OD2 ASP A 265     3892   4136   4549   -125   -140     79       O  
ATOM   1950  N   GLY A 266     123.632  99.059  18.322  1.00 28.24           N  
ANISOU 1950  N   GLY A 266     3344   3529   3856    -82   -128     63       N  
ATOM   1951  CA  GLY A 266     122.368  98.489  17.935  1.00 27.19           C  
ANISOU 1951  CA  GLY A 266     3222   3399   3712    -67   -119     67       C  
ATOM   1952  C   GLY A 266     122.517  97.323  16.981  1.00 26.54           C  
ANISOU 1952  C   GLY A 266     3131   3321   3633    -57   -113     81       C  
ATOM   1953  O   GLY A 266     121.561  96.994  16.337  1.00 28.43           O  
ANISOU 1953  O   GLY A 266     3376   3561   3867    -46   -103     85       O  
ATOM   1954  N   TYR A 267     123.696  96.705  16.916  1.00 26.17           N  
ANISOU 1954  N   TYR A 267     3068   3278   3596    -60   -119     90       N  
ATOM   1955  CA  TYR A 267     123.913  95.503  16.133  1.00 25.83           C  
ANISOU 1955  CA  TYR A 267     3017   3240   3558    -51   -113    102       C  
ATOM   1956  C   TYR A 267     123.524  94.266  16.955  1.00 26.76           C  
ANISOU 1956  C   TYR A 267     3135   3369   3662    -46   -121    106       C  
ATOM   1957  O   TYR A 267     124.132  93.979  17.994  1.00 27.39           O  
ANISOU 1957  O   TYR A 267     3208   3458   3740    -52   -135    107       O  
ATOM   1958  CB  TYR A 267     125.382  95.389  15.675  1.00 25.71           C  
ANISOU 1958  CB  TYR A 267     2985   3223   3563    -56   -114    111       C  
ATOM   1959  CG  TYR A 267     125.707  94.082  14.992  1.00 25.73           C  
ANISOU 1959  CG  TYR A 267     2977   3229   3571    -47   -107    123       C  
ATOM   1960  CD1 TYR A 267     125.132  93.747  13.743  1.00 27.81           C  
ANISOU 1960  CD1 TYR A 267     3246   3487   3833    -38    -90    126       C  
ATOM   1961  CD2 TYR A 267     126.573  93.172  15.559  1.00 26.08           C  
ANISOU 1961  CD2 TYR A 267     3008   3281   3621    -47   -116    132       C  
ATOM   1962  CE1 TYR A 267     125.416  92.515  13.120  1.00 26.99           C  
ANISOU 1962  CE1 TYR A 267     3135   3385   3735    -30    -82    135       C  
ATOM   1963  CE2 TYR A 267     126.866  91.967  14.935  1.00 25.77           C  
ANISOU 1963  CE2 TYR A 267     2960   3241   3588    -37   -107    142       C  
ATOM   1964  CZ  TYR A 267     126.270  91.632  13.759  1.00 25.89           C  
ANISOU 1964  CZ  TYR A 267     2982   3250   3603    -30    -90    143       C  
ATOM   1965  OH  TYR A 267     126.599  90.452  13.175  1.00 27.36           O  
ANISOU 1965  OH  TYR A 267     3161   3436   3797    -22    -80    151       O  
ATOM   1966  N   TYR A 268     122.579  93.498  16.427  1.00 26.26           N  
ANISOU 1966  N   TYR A 268     3078   3307   3592    -36   -111    108       N  
ATOM   1967  CA  TYR A 268     122.084  92.248  17.040  1.00 26.61           C  
ANISOU 1967  CA  TYR A 268     3124   3361   3626    -30   -114    112       C  
ATOM   1968  C   TYR A 268     122.996  91.105  16.622  1.00 25.69           C  
ANISOU 1968  C   TYR A 268     2995   3245   3522    -26   -112    125       C  
ATOM   1969  O   TYR A 268     123.207  90.891  15.457  1.00 25.58           O  
ANISOU 1969  O   TYR A 268     2976   3225   3518    -22    -99    128       O  
ATOM   1970  CB  TYR A 268     120.650  91.978  16.594  1.00 26.38           C  
ANISOU 1970  CB  TYR A 268     3108   3332   3585    -23   -104    108       C  
ATOM   1971  CG  TYR A 268     119.950  90.860  17.301  1.00 27.39           C  
ANISOU 1971  CG  TYR A 268     3238   3467   3700    -19   -105    110       C  
ATOM   1972  CD1 TYR A 268     119.607  90.959  18.654  1.00 28.12           C  
ANISOU 1972  CD1 TYR A 268     3338   3568   3781    -22   -116    106       C  
ATOM   1973  CD2 TYR A 268     119.628  89.694  16.630  1.00 28.73           C  
ANISOU 1973  CD2 TYR A 268     3407   3637   3873    -13    -95    116       C  
ATOM   1974  CE1 TYR A 268     118.970  89.925  19.326  1.00 28.42           C  
ANISOU 1974  CE1 TYR A 268     3379   3611   3807    -19   -116    110       C  
ATOM   1975  CE2 TYR A 268     118.964  88.643  17.272  1.00 30.91           C  
ANISOU 1975  CE2 TYR A 268     3688   3918   4140     -9    -95    118       C  
ATOM   1976  CZ  TYR A 268     118.655  88.752  18.623  1.00 31.56           C  
ANISOU 1976  CZ  TYR A 268     3775   4007   4209    -12   -105    116       C  
ATOM   1977  OH  TYR A 268     117.984  87.724  19.240  1.00 33.59           O  
ANISOU 1977  OH  TYR A 268     4036   4270   4458     -9   -103    120       O  
ATOM   1978  N   THR A 269     123.568  90.396  17.597  1.00 26.23           N  
ANISOU 1978  N   THR A 269     3055   3321   3590    -27   -123    132       N  
ATOM   1979  CA  THR A 269     124.714  89.527  17.363  1.00 25.76           C  
ANISOU 1979  CA  THR A 269     2979   3261   3546    -23   -122    146       C  
ATOM   1980  C   THR A 269     124.434  88.355  16.419  1.00 25.66           C  
ANISOU 1980  C   THR A 269     2967   3243   3540    -14   -106    152       C  
ATOM   1981  O   THR A 269     125.327  87.815  15.820  1.00 26.67           O  
ANISOU 1981  O   THR A 269     3082   3366   3684    -10    -99    160       O  
ATOM   1982  CB  THR A 269     125.301  89.028  18.720  1.00 25.29           C  
ANISOU 1982  CB  THR A 269     2912   3213   3483    -25   -140    154       C  
ATOM   1983  OG1 THR A 269     126.613  88.499  18.516  1.00 25.41           O  
ANISOU 1983  OG1 THR A 269     2908   3229   3517    -23   -141    168       O  
ATOM   1984  CG2 THR A 269     124.434  87.954  19.389  1.00 25.71           C  
ANISOU 1984  CG2 THR A 269     2973   3272   3523    -18   -139    159       C  
ATOM   1985  N   GLU A 270     123.191  87.930  16.334  1.00 26.02           N  
ANISOU 1985  N   GLU A 270     3025   3288   3573    -10    -98    146       N  
ATOM   1986  CA  GLU A 270     122.849  86.833  15.454  1.00 27.39           C  
ANISOU 1986  CA  GLU A 270     3199   3456   3750     -3    -82    149       C  
ATOM   1987  C   GLU A 270     122.853  87.229  13.965  1.00 26.49           C  
ANISOU 1987  C   GLU A 270     3087   3336   3644     -3    -67    143       C  
ATOM   1988  O   GLU A 270     122.893  86.362  13.106  1.00 27.25           O  
ANISOU 1988  O   GLU A 270     3181   3427   3746      1    -53    145       O  
ATOM   1989  CB  GLU A 270     121.486  86.241  15.812  1.00 29.65           C  
ANISOU 1989  CB  GLU A 270     3499   3746   4022     -1    -78    144       C  
ATOM   1990  CG  GLU A 270     121.311  85.719  17.234  1.00 29.50           C  
ANISOU 1990  CG  GLU A 270     3481   3733   3993      0    -89    150       C  
ATOM   1991  CD  GLU A 270     119.992  84.899  17.387  1.00 34.10           C  
ANISOU 1991  CD  GLU A 270     4076   4317   4565      2    -81    146       C  
ATOM   1992  OE1 GLU A 270     119.848  83.866  16.710  1.00 38.24           O  
ANISOU 1992  OE1 GLU A 270     4599   4834   5097      6    -67    148       O  
ATOM   1993  OE2 GLU A 270     119.096  85.244  18.182  1.00 34.55           O  
ANISOU 1993  OE2 GLU A 270     4141   4380   4606      0    -87    140       O  
ATOM   1994  N   GLY A 271     122.850  88.523  13.641  1.00 23.88           N  
ANISOU 1994  N   GLY A 271     2758   3004   3310     -8    -70    138       N  
ATOM   1995  CA  GLY A 271     122.987  88.920  12.260  1.00 23.58           C  
ANISOU 1995  CA  GLY A 271     2720   2962   3278     -7    -57    136       C  
ATOM   1996  C   GLY A 271     121.639  89.404  11.777  1.00 24.48           C  
ANISOU 1996  C   GLY A 271     2847   3078   3376     -6    -52    127       C  
ATOM   1997  O   GLY A 271     120.667  89.296  12.524  1.00 25.71           O  
ANISOU 1997  O   GLY A 271     3011   3239   3519     -6    -58    122       O  
ATOM   1998  N   PRO A 272     121.575  89.990  10.558  1.00 25.29           N  
ANISOU 1998  N   PRO A 272     2952   3179   3480     -6    -42    126       N  
ATOM   1999  CA  PRO A 272     120.393  90.776  10.229  1.00 24.56           C  
ANISOU 1999  CA  PRO A 272     2870   3090   3373     -5    -41    120       C  
ATOM   2000  C   PRO A 272     119.138  89.998   9.894  1.00 23.38           C  
ANISOU 2000  C   PRO A 272     2726   2947   3208     -1    -35    115       C  
ATOM   2001  O   PRO A 272     118.030  90.501  10.085  1.00 23.89           O  
ANISOU 2001  O   PRO A 272     2799   3018   3261      0    -38    110       O  
ATOM   2002  CB  PRO A 272     120.834  91.641   9.037  1.00 23.98           C  
ANISOU 2002  CB  PRO A 272     2795   3013   3305     -5    -32    124       C  
ATOM   2003  CG  PRO A 272     122.091  91.084   8.606  1.00 25.16           C  
ANISOU 2003  CG  PRO A 272     2933   3157   3469     -6    -25    129       C  
ATOM   2004  CD  PRO A 272     122.737  90.428   9.776  1.00 25.74           C  
ANISOU 2004  CD  PRO A 272     3000   3230   3551     -8    -35    131       C  
ATOM   2005  N   TYR A 273     119.290  88.803   9.382  1.00 23.47           N  
ANISOU 2005  N   TYR A 273     2735   2960   3222     -1    -26    115       N  
ATOM   2006  CA  TYR A 273     118.132  87.979   9.086  1.00 23.43           C  
ANISOU 2006  CA  TYR A 273     2735   2962   3205      0    -20    108       C  
ATOM   2007  C   TYR A 273     117.375  87.692  10.383  1.00 23.06           C  
ANISOU 2007  C   TYR A 273     2693   2918   3151      0    -29    105       C  
ATOM   2008  O   TYR A 273     116.138  87.874  10.461  1.00 23.82           O  
ANISOU 2008  O   TYR A 273     2796   3022   3235      1    -31    100       O  
ATOM   2009  CB  TYR A 273     118.541  86.711   8.351  1.00 24.30           C  
ANISOU 2009  CB  TYR A 273     2842   3069   3321     -1     -7    107       C  
ATOM   2010  CG  TYR A 273     117.400  85.753   8.121  1.00 26.30           C  
ANISOU 2010  CG  TYR A 273     3101   3329   3564     -2      0     98       C  
ATOM   2011  CD1 TYR A 273     116.522  85.903   7.014  1.00 25.75           C  
ANISOU 2011  CD1 TYR A 273     3035   3269   3479     -4      6     91       C  
ATOM   2012  CD2 TYR A 273     117.196  84.655   9.001  1.00 25.56           C  
ANISOU 2012  CD2 TYR A 273     3007   3230   3472     -3      0     97       C  
ATOM   2013  CE1 TYR A 273     115.475  84.980   6.802  1.00 25.84           C  
ANISOU 2013  CE1 TYR A 273     3049   3287   3480     -8     12     81       C  
ATOM   2014  CE2 TYR A 273     116.139  83.755   8.794  1.00 26.92           C  
ANISOU 2014  CE2 TYR A 273     3184   3408   3636     -6      7     88       C  
ATOM   2015  CZ  TYR A 273     115.287  83.910   7.707  1.00 26.15           C  
ANISOU 2015  CZ  TYR A 273     3089   3320   3525    -10     13     79       C  
ATOM   2016  OH  TYR A 273     114.241  82.985   7.576  1.00 26.12           O  
ANISOU 2016  OH  TYR A 273     3089   3322   3514    -15     19     69       O  
ATOM   2017  N   ALA A 274     118.107  87.304  11.418  1.00 23.16           N  
ANISOU 2017  N   ALA A 274     2701   2925   3172      0    -36    111       N  
ATOM   2018  CA  ALA A 274     117.523  87.058  12.742  1.00 22.51           C  
ANISOU 2018  CA  ALA A 274     2624   2847   3083      0    -45    110       C  
ATOM   2019  C   ALA A 274     117.120  88.375  13.446  1.00 23.34           C  
ANISOU 2019  C   ALA A 274     2734   2955   3180     -1    -56    107       C  
ATOM   2020  O   ALA A 274     116.109  88.446  14.096  1.00 23.31           O  
ANISOU 2020  O   ALA A 274     2737   2956   3165     -1    -59    102       O  
ATOM   2021  CB  ALA A 274     118.476  86.228  13.596  1.00 22.09           C  
ANISOU 2021  CB  ALA A 274     2564   2788   3040      0    -50    119       C  
ATOM   2022  N   GLN A 275     117.904  89.444  13.304  1.00 23.35           N  
ANISOU 2022  N   GLN A 275     2733   2952   3188     -3    -61    109       N  
ATOM   2023  CA  GLN A 275     117.497  90.689  13.881  1.00 22.97           C  
ANISOU 2023  CA  GLN A 275     2690   2904   3134     -4    -68    104       C  
ATOM   2024  C   GLN A 275     116.117  91.120  13.370  1.00 23.95           C  
ANISOU 2024  C   GLN A 275     2822   3032   3247      0    -62     98       C  
ATOM   2025  O   GLN A 275     115.256  91.579  14.153  1.00 23.99           O  
ANISOU 2025  O   GLN A 275     2833   3040   3242      0    -66     93       O  
ATOM   2026  CB  GLN A 275     118.499  91.788  13.598  1.00 23.41           C  
ANISOU 2026  CB  GLN A 275     2742   2952   3201     -8    -70    106       C  
ATOM   2027  CG  GLN A 275     118.148  93.044  14.375  1.00 24.07           C  
ANISOU 2027  CG  GLN A 275     2832   3033   3280    -10    -77     99       C  
ATOM   2028  CD  GLN A 275     119.159  94.162  14.210  1.00 25.89           C  
ANISOU 2028  CD  GLN A 275     3059   3255   3523    -16    -79    100       C  
ATOM   2029  OE1 GLN A 275     120.321  93.953  13.827  1.00 25.74           O  
ANISOU 2029  OE1 GLN A 275     3030   3232   3517    -19    -79    106       O  
ATOM   2030  NE2 GLN A 275     118.750  95.352  14.631  1.00 27.58           N  
ANISOU 2030  NE2 GLN A 275     3281   3464   3735    -18    -80     93       N  
ATOM   2031  N   ARG A 276     115.933  91.037  12.063  1.00 23.11           N  
ANISOU 2031  N   ARG A 276     2713   2927   3140      2    -52    100       N  
ATOM   2032  CA  ARG A 276     114.658  91.304  11.437  1.00 22.81           C  
ANISOU 2032  CA  ARG A 276     2680   2897   3092      6    -47     97       C  
ATOM   2033  C   ARG A 276     113.490  90.564  12.159  1.00 23.54           C  
ANISOU 2033  C   ARG A 276     2775   2996   3172      7    -48     91       C  
ATOM   2034  O   ARG A 276     112.401  91.104  12.367  1.00 21.95           O  
ANISOU 2034  O   ARG A 276     2577   2801   2962     10    -49     88       O  
ATOM   2035  CB  ARG A 276     114.739  90.889   9.947  1.00 22.60           C  
ANISOU 2035  CB  ARG A 276     2649   2874   3064      7    -37     99       C  
ATOM   2036  CG  ARG A 276     113.424  90.853   9.170  1.00 21.81           C  
ANISOU 2036  CG  ARG A 276     2551   2786   2950     10    -33     96       C  
ATOM   2037  CD  ARG A 276     112.579  89.575   9.308  1.00 21.58           C  
ANISOU 2037  CD  ARG A 276     2521   2766   2913      8    -30     89       C  
ATOM   2038  NE  ARG A 276     113.376  88.367   9.300  1.00 20.64           N  
ANISOU 2038  NE  ARG A 276     2400   2642   2802      3    -25     88       N  
ATOM   2039  CZ  ARG A 276     112.895  87.111   9.352  1.00 21.12           C  
ANISOU 2039  CZ  ARG A 276     2460   2705   2859     -1    -20     82       C  
ATOM   2040  NH1 ARG A 276     111.598  86.850   9.402  1.00 20.62           N  
ANISOU 2040  NH1 ARG A 276     2398   2652   2784     -2    -20     76       N  
ATOM   2041  NH2 ARG A 276     113.734  86.078   9.360  1.00 20.96           N  
ANISOU 2041  NH2 ARG A 276     2438   2677   2850     -4    -14     83       N  
ATOM   2042  N   TYR A 277     113.710  89.305  12.479  1.00 24.11           N  
ANISOU 2042  N   TYR A 277     2846   3070   3246      4    -47     91       N  
ATOM   2043  CA  TYR A 277     112.649  88.476  13.059  1.00 24.20           C  
ANISOU 2043  CA  TYR A 277     2860   3088   3248      3    -46     86       C  
ATOM   2044  C   TYR A 277     112.398  88.972  14.503  1.00 26.04           C  
ANISOU 2044  C   TYR A 277     3098   3320   3476      3    -55     85       C  
ATOM   2045  O   TYR A 277     111.250  89.109  14.926  1.00 25.16           O  
ANISOU 2045  O   TYR A 277     2990   3215   3355      5    -54     81       O  
ATOM   2046  CB  TYR A 277     113.122  87.026  13.060  1.00 23.79           C  
ANISOU 2046  CB  TYR A 277     2805   3033   3203      0    -41     88       C  
ATOM   2047  CG  TYR A 277     112.111  85.999  13.445  1.00 23.22           C  
ANISOU 2047  CG  TYR A 277     2734   2964   3123     -2    -36     84       C  
ATOM   2048  CD1 TYR A 277     110.804  86.056  12.959  1.00 23.72           C  
ANISOU 2048  CD1 TYR A 277     2799   3038   3176     -3    -32     77       C  
ATOM   2049  CD2 TYR A 277     112.443  84.982  14.341  1.00 23.30           C  
ANISOU 2049  CD2 TYR A 277     2745   2970   3138     -4    -36     88       C  
ATOM   2050  CE1 TYR A 277     109.855  85.093  13.319  1.00 24.95           C  
ANISOU 2050  CE1 TYR A 277     2956   3198   3327     -7    -27     72       C  
ATOM   2051  CE2 TYR A 277     111.490  84.021  14.708  1.00 24.55           C  
ANISOU 2051  CE2 TYR A 277     2906   3131   3292     -6    -30     85       C  
ATOM   2052  CZ  TYR A 277     110.214  84.084  14.204  1.00 23.84           C  
ANISOU 2052  CZ  TYR A 277     2817   3050   3192     -9    -25     76       C  
ATOM   2053  OH  TYR A 277     109.278  83.150  14.573  1.00 27.32           O  
ANISOU 2053  OH  TYR A 277     3258   3493   3628    -13    -18     73       O  
ATOM   2054  N   ALA A 278     113.482  89.253  15.244  1.00 25.76           N  
ANISOU 2054  N   ALA A 278     3062   3279   3448      1    -62     89       N  
ATOM   2055  CA  ALA A 278     113.359  89.642  16.652  1.00 25.98           C  
ANISOU 2055  CA  ALA A 278     3095   3307   3468      0    -71     87       C  
ATOM   2056  C   ALA A 278     112.766  91.033  16.875  1.00 26.67           C  
ANISOU 2056  C   ALA A 278     3188   3394   3551      1    -72     80       C  
ATOM   2057  O   ALA A 278     112.212  91.305  17.940  1.00 24.44           O  
ANISOU 2057  O   ALA A 278     2912   3115   3260      1    -76     75       O  
ATOM   2058  CB  ALA A 278     114.710  89.544  17.332  1.00 26.35           C  
ANISOU 2058  CB  ALA A 278     3138   3350   3522     -4    -80     92       C  
ATOM   2059  N   MET A 279     112.881  91.920  15.897  1.00 26.61           N  
ANISOU 2059  N   MET A 279     3179   3382   3549      4    -69     80       N  
ATOM   2060  CA  MET A 279     112.378  93.296  16.079  1.00 28.41           C  
ANISOU 2060  CA  MET A 279     3412   3606   3775      7    -68     75       C  
ATOM   2061  C   MET A 279     110.882  93.286  16.349  1.00 27.41           C  
ANISOU 2061  C   MET A 279     3290   3488   3638     12    -64     71       C  
ATOM   2062  O   MET A 279     110.381  94.185  17.016  1.00 26.30           O  
ANISOU 2062  O   MET A 279     3155   3344   3494     14    -63     65       O  
ATOM   2063  CB  MET A 279     112.610  94.132  14.847  1.00 31.37           C  
ANISOU 2063  CB  MET A 279     3785   3976   4159     10    -63     80       C  
ATOM   2064  CG  MET A 279     114.066  94.291  14.484  1.00 37.40           C  
ANISOU 2064  CG  MET A 279     4544   4732   4935      5    -66     84       C  
ATOM   2065  SD  MET A 279     114.873  95.412  15.584  1.00 48.41           S  
ANISOU 2065  SD  MET A 279     5943   6116   6336     -2    -73     79       S  
ATOM   2066  CE  MET A 279     115.435  94.441  16.845  1.00 34.47           C  
ANISOU 2066  CE  MET A 279     4175   4357   4565     -9    -84     77       C  
ATOM   2067  N   TYR A 280     110.160  92.310  15.804  1.00 24.20           N  
ANISOU 2067  N   TYR A 280     2880   3090   3227     14    -59     72       N  
ATOM   2068  CA  TYR A 280     108.718  92.337  16.029  1.00 25.06           C  
ANISOU 2068  CA  TYR A 280     2989   3207   3326     18    -54     68       C  
ATOM   2069  C   TYR A 280     108.398  92.219  17.540  1.00 23.58           C  
ANISOU 2069  C   TYR A 280     2808   3020   3131     16    -57     63       C  
ATOM   2070  O   TYR A 280     107.864  93.191  18.114  1.00 22.91           O  
ANISOU 2070  O   TYR A 280     2729   2933   3043     19    -55     58       O  
ATOM   2071  CB  TYR A 280     107.936  91.356  15.151  1.00 24.19           C  
ANISOU 2071  CB  TYR A 280     2872   3107   3211     19    -49     69       C  
ATOM   2072  CG  TYR A 280     106.442  91.564  15.278  1.00 23.40           C  
ANISOU 2072  CG  TYR A 280     2771   3017   3103     24    -44     66       C  
ATOM   2073  CD1 TYR A 280     105.760  92.473  14.453  1.00 23.65           C  
ANISOU 2073  CD1 TYR A 280     2798   3053   3134     32    -42     69       C  
ATOM   2074  CD2 TYR A 280     105.729  90.847  16.211  1.00 23.34           C  
ANISOU 2074  CD2 TYR A 280     2765   3015   3089     21    -43     62       C  
ATOM   2075  CE1 TYR A 280     104.381  92.662  14.572  1.00 24.09           C  
ANISOU 2075  CE1 TYR A 280     2850   3118   3183     37    -38     67       C  
ATOM   2076  CE2 TYR A 280     104.359  91.014  16.364  1.00 24.56           C  
ANISOU 2076  CE2 TYR A 280     2916   3179   3237     25    -38     59       C  
ATOM   2077  CZ  TYR A 280     103.680  91.940  15.554  1.00 25.22           C  
ANISOU 2077  CZ  TYR A 280     2994   3267   3321     34    -36     61       C  
ATOM   2078  OH  TYR A 280     102.322  92.085  15.747  1.00 26.26           O  
ANISOU 2078  OH  TYR A 280     3121   3408   3447     39    -31     59       O  
ATOM   2079  N   PRO A 281     108.833  91.127  18.191  1.00 22.68           N  
ANISOU 2079  N   PRO A 281     2695   2908   3014     10    -60     65       N  
ATOM   2080  CA  PRO A 281     108.550  91.031  19.639  1.00 22.67           C  
ANISOU 2080  CA  PRO A 281     2700   2910   3003      8    -63     61       C  
ATOM   2081  C   PRO A 281     109.262  92.110  20.483  1.00 23.43           C  
ANISOU 2081  C   PRO A 281     2804   3000   3099      5    -70     56       C  
ATOM   2082  O   PRO A 281     108.682  92.588  21.457  1.00 22.75           O  
ANISOU 2082  O   PRO A 281     2725   2917   3004      5    -69     49       O  
ATOM   2083  CB  PRO A 281     109.032  89.626  20.000  1.00 22.45           C  
ANISOU 2083  CB  PRO A 281     2670   2884   2975      3    -65     67       C  
ATOM   2084  CG  PRO A 281     110.036  89.285  18.922  1.00 22.62           C  
ANISOU 2084  CG  PRO A 281     2685   2900   3009      2    -66     73       C  
ATOM   2085  CD  PRO A 281     109.448  89.886  17.685  1.00 21.93           C  
ANISOU 2085  CD  PRO A 281     2595   2814   2925      6    -60     70       C  
ATOM   2086  N   PHE A 282     110.482  92.513  20.107  1.00 23.99           N  
ANISOU 2086  N   PHE A 282     2872   3064   3180      2    -76     59       N  
ATOM   2087  CA  PHE A 282     111.145  93.579  20.843  1.00 25.05           C  
ANISOU 2087  CA  PHE A 282     3012   3192   3315     -3    -82     52       C  
ATOM   2088  C   PHE A 282     110.323  94.882  20.826  1.00 25.37           C  
ANISOU 2088  C   PHE A 282     3058   3227   3355      2    -75     43       C  
ATOM   2089  O   PHE A 282     110.098  95.467  21.873  1.00 25.32           O  
ANISOU 2089  O   PHE A 282     3060   3220   3341     -1    -75     34       O  
ATOM   2090  CB  PHE A 282     112.557  93.874  20.318  1.00 25.60           C  
ANISOU 2090  CB  PHE A 282     3075   3254   3396     -8    -89     57       C  
ATOM   2091  CG  PHE A 282     113.628  92.938  20.849  1.00 25.89           C  
ANISOU 2091  CG  PHE A 282     3107   3297   3434    -13    -99     63       C  
ATOM   2092  CD1 PHE A 282     113.909  92.865  22.222  1.00 26.35           C  
ANISOU 2092  CD1 PHE A 282     3170   3361   3481    -20   -108     60       C  
ATOM   2093  CD2 PHE A 282     114.441  92.260  19.978  1.00 26.11           C  
ANISOU 2093  CD2 PHE A 282     3125   3322   3473    -13    -99     73       C  
ATOM   2094  CE1 PHE A 282     114.935  92.053  22.710  1.00 27.31           C  
ANISOU 2094  CE1 PHE A 282     3284   3488   3602    -24   -119     69       C  
ATOM   2095  CE2 PHE A 282     115.487  91.438  20.453  1.00 26.39           C  
ANISOU 2095  CE2 PHE A 282     3154   3361   3512    -16   -108     81       C  
ATOM   2096  CZ  PHE A 282     115.726  91.331  21.818  1.00 26.86           C  
ANISOU 2096  CZ  PHE A 282     3217   3428   3560    -21   -118     81       C  
ATOM   2097  N   LEU A 283     109.919  95.359  19.645  1.00 25.75           N  
ANISOU 2097  N   LEU A 283     3102   3270   3411      9    -68     47       N  
ATOM   2098  CA  LEU A 283     109.291  96.677  19.552  1.00 25.04           C  
ANISOU 2098  CA  LEU A 283     3017   3172   3325     15    -60     41       C  
ATOM   2099  C   LEU A 283     107.818  96.642  19.967  1.00 25.43           C  
ANISOU 2099  C   LEU A 283     3069   3228   3365     22    -52     37       C  
ATOM   2100  O   LEU A 283     107.333  97.583  20.560  1.00 24.67           O  
ANISOU 2100  O   LEU A 283     2980   3126   3268     25    -46     29       O  
ATOM   2101  CB  LEU A 283     109.523  97.269  18.183  1.00 26.95           C  
ANISOU 2101  CB  LEU A 283     3253   3407   3579     21    -55     49       C  
ATOM   2102  CG  LEU A 283     111.012  97.638  17.943  1.00 28.36           C  
ANISOU 2102  CG  LEU A 283     3430   3575   3769     13    -61     51       C  
ATOM   2103  CD1 LEU A 283     111.149  98.027  16.510  1.00 29.42           C  
ANISOU 2103  CD1 LEU A 283     3560   3705   3914     19    -55     61       C  
ATOM   2104  CD2 LEU A 283     111.416  98.840  18.797  1.00 29.75           C  
ANISOU 2104  CD2 LEU A 283     3615   3739   3949      7    -62     40       C  
ATOM   2105  N   ILE A 284     107.121  95.542  19.691  1.00 25.60           N  
ANISOU 2105  N   ILE A 284     3084   3262   3380     25    -50     42       N  
ATOM   2106  CA  ILE A 284     105.737  95.390  20.114  1.00 27.23           C  
ANISOU 2106  CA  ILE A 284     3292   3477   3579     30    -43     38       C  
ATOM   2107  C   ILE A 284     105.608  95.346  21.624  1.00 27.16           C  
ANISOU 2107  C   ILE A 284     3292   3470   3559     25    -43     29       C  
ATOM   2108  O   ILE A 284     104.837  96.130  22.221  1.00 27.16           O  
ANISOU 2108  O   ILE A 284     3298   3467   3556     30    -35     21       O  
ATOM   2109  CB  ILE A 284     105.084  94.156  19.486  1.00 27.93           C  
ANISOU 2109  CB  ILE A 284     3371   3579   3664     31    -41     45       C  
ATOM   2110  CG1 ILE A 284     104.781  94.414  18.007  1.00 29.32           C  
ANISOU 2110  CG1 ILE A 284     3538   3756   3846     38    -38     52       C  
ATOM   2111  CG2 ILE A 284     103.801  93.767  20.215  1.00 28.21           C  
ANISOU 2111  CG2 ILE A 284     3407   3624   3690     33    -34     40       C  
ATOM   2112  CD1 ILE A 284     103.615  95.349  17.693  1.00 29.68           C  
ANISOU 2112  CD1 ILE A 284     3579   3803   3893     50    -30     52       C  
ATOM   2113  N   PHE A 285     106.395  94.476  22.251  1.00 26.13           N  
ANISOU 2113  N   PHE A 285     3164   3343   3422     16    -51     31       N  
ATOM   2114  CA  PHE A 285     106.395  94.424  23.676  1.00 25.79           C  
ANISOU 2114  CA  PHE A 285     3130   3304   3366     11    -53     23       C  
ATOM   2115  C   PHE A 285     106.938  95.699  24.268  1.00 25.52           C  
ANISOU 2115  C   PHE A 285     3104   3259   3332      7    -55     13       C  
ATOM   2116  O   PHE A 285     106.387  96.135  25.266  1.00 25.23           O  
ANISOU 2116  O   PHE A 285     3076   3224   3285      6    -50      2       O  
ATOM   2117  CB  PHE A 285     107.126  93.201  24.213  1.00 26.43           C  
ANISOU 2117  CB  PHE A 285     3210   3392   3440      3    -62     30       C  
ATOM   2118  CG  PHE A 285     106.952  92.967  25.685  1.00 26.78           C  
ANISOU 2118  CG  PHE A 285     3263   3444   3467     -2    -64     26       C  
ATOM   2119  CD1 PHE A 285     105.751  93.166  26.327  1.00 27.71           C  
ANISOU 2119  CD1 PHE A 285     3387   3567   3576      1    -53     18       C  
ATOM   2120  CD2 PHE A 285     108.017  92.454  26.429  1.00 28.53           C  
ANISOU 2120  CD2 PHE A 285     3488   3671   3683    -10    -76     30       C  
ATOM   2121  CE1 PHE A 285     105.611  92.897  27.686  1.00 27.43           C  
ANISOU 2121  CE1 PHE A 285     3361   3540   3522     -4    -53     15       C  
ATOM   2122  CE2 PHE A 285     107.898  92.186  27.758  1.00 28.58           C  
ANISOU 2122  CE2 PHE A 285     3502   3686   3670    -15    -78     28       C  
ATOM   2123  CZ  PHE A 285     106.697  92.445  28.410  1.00 28.88           C  
ANISOU 2123  CZ  PHE A 285     3548   3729   3698    -12    -66     19       C  
ATOM   2124  N   ALA A 286     107.951  96.337  23.660  1.00 24.48           N  
ANISOU 2124  N   ALA A 286     2971   3118   3213      4    -61     13       N  
ATOM   2125  CA  ALA A 286     108.421  97.611  24.200  1.00 25.25           C  
ANISOU 2125  CA  ALA A 286     3077   3205   3313     -1    -61      1       C  
ATOM   2126  C   ALA A 286     107.299  98.681  24.105  1.00 27.54           C  
ANISOU 2126  C   ALA A 286     3371   3485   3607      9    -45     -6       C  
ATOM   2127  O   ALA A 286     107.145  99.506  24.991  1.00 28.89           O  
ANISOU 2127  O   ALA A 286     3553   3650   3773      6    -41    -20       O  
ATOM   2128  CB  ALA A 286     109.668  98.082  23.469  1.00 24.86           C  
ANISOU 2128  CB  ALA A 286     3023   3145   3278     -6    -68      5       C  
ATOM   2129  N   GLU A 287     106.535  98.674  23.008  1.00 28.15           N  
ANISOU 2129  N   GLU A 287     3441   3562   3693     21    -38      3       N  
ATOM   2130  CA  GLU A 287     105.507  99.668  22.825  1.00 30.10           C  
ANISOU 2130  CA  GLU A 287     3690   3801   3946     32    -24     -1       C  
ATOM   2131  C   GLU A 287     104.427  99.474  23.915  1.00 29.63           C  
ANISOU 2131  C   GLU A 287     3635   3749   3873     35    -16    -10       C  
ATOM   2132  O   GLU A 287     104.005 100.441  24.534  1.00 24.76           O  
ANISOU 2132  O   GLU A 287     3027   3123   3257     37     -5    -21       O  
ATOM   2133  CB  GLU A 287     104.870  99.552  21.437  1.00 32.67           C  
ANISOU 2133  CB  GLU A 287     4003   4129   4281     45    -19     14       C  
ATOM   2134  CG  GLU A 287     103.793 100.613  21.228  1.00 36.47           C  
ANISOU 2134  CG  GLU A 287     4485   4603   4770     59     -5     13       C  
ATOM   2135  CD  GLU A 287     103.126 100.579  19.894  1.00 39.22           C  
ANISOU 2135  CD  GLU A 287     4820   4957   5126     72     -2     28       C  
ATOM   2136  OE1 GLU A 287     103.352  99.639  19.106  1.00 39.08           O  
ANISOU 2136  OE1 GLU A 287     4794   4951   5105     69    -10     37       O  
ATOM   2137  OE2 GLU A 287     102.320 101.499  19.675  1.00 45.13           O  
ANISOU 2137  OE2 GLU A 287     5567   5698   5881     85     10     30       O  
ATOM   2138  N   ALA A 288     103.992  98.212  24.103  1.00 27.90           N  
ANISOU 2138  N   ALA A 288     3411   3546   3642     33    -19     -4       N  
ATOM   2139  CA  ALA A 288     102.998  97.893  25.142  1.00 28.65           C  
ANISOU 2139  CA  ALA A 288     3511   3651   3725     34    -11    -11       C  
ATOM   2140  C   ALA A 288     103.476  98.306  26.555  1.00 29.86           C  
ANISOU 2140  C   ALA A 288     3679   3802   3865     24    -12    -26       C  
ATOM   2141  O   ALA A 288     102.669  98.839  27.348  1.00 29.60           O  
ANISOU 2141  O   ALA A 288     3654   3767   3826     27      0    -37       O  
ATOM   2142  CB  ALA A 288     102.634  96.409  25.133  1.00 27.80           C  
ANISOU 2142  CB  ALA A 288     3397   3559   3608     32    -14     -2       C  
ATOM   2143  N   LEU A 289     104.755  98.029  26.866  1.00 28.55           N  
ANISOU 2143  N   LEU A 289     3517   3637   3695     12    -26    -26       N  
ATOM   2144  CA  LEU A 289     105.338  98.436  28.123  1.00 28.73           C  
ANISOU 2144  CA  LEU A 289     3552   3660   3704      0    -31    -40       C  
ATOM   2145  C   LEU A 289     105.336  99.952  28.244  1.00 30.64           C  
ANISOU 2145  C   LEU A 289     3802   3884   3954      1    -21    -56       C  
ATOM   2146  O   LEU A 289     104.987 100.463  29.296  1.00 28.55           O  
ANISOU 2146  O   LEU A 289     3550   3619   3678     -3    -14    -71       O  
ATOM   2147  CB  LEU A 289     106.745  97.889  28.306  1.00 28.45           C  
ANISOU 2147  CB  LEU A 289     3515   3630   3664    -12    -49    -35       C  
ATOM   2148  CG  LEU A 289     106.830  96.385  28.566  1.00 28.12           C  
ANISOU 2148  CG  LEU A 289     3469   3604   3611    -14    -57    -22       C  
ATOM   2149  CD1 LEU A 289     108.272  95.929  28.394  1.00 29.54           C  
ANISOU 2149  CD1 LEU A 289     3642   3786   3794    -22    -75    -13       C  
ATOM   2150  CD2 LEU A 289     106.329  96.052  29.968  1.00 28.50           C  
ANISOU 2150  CD2 LEU A 289     3527   3665   3636    -18    -55    -28       C  
ATOM   2151  N   HIS A 290     105.662 100.669  27.166  1.00 29.93           N  
ANISOU 2151  N   HIS A 290     3708   3780   3885      6    -20    -51       N  
ATOM   2152  CA  HIS A 290     105.651 102.124  27.234  1.00 30.73           C  
ANISOU 2152  CA  HIS A 290     3817   3861   3997      7     -8    -65       C  
ATOM   2153  C   HIS A 290     104.236 102.638  27.602  1.00 31.19           C  
ANISOU 2153  C   HIS A 290     3880   3916   4055     19     12    -72       C  
ATOM   2154  O   HIS A 290     104.089 103.500  28.464  1.00 29.86           O  
ANISOU 2154  O   HIS A 290     3724   3738   3883     16     22    -91       O  
ATOM   2155  CB  HIS A 290     106.152 102.747  25.933  1.00 31.36           C  
ANISOU 2155  CB  HIS A 290     3890   3925   4100     12     -8    -55       C  
ATOM   2156  CG  HIS A 290     105.933 104.227  25.836  1.00 33.53           C  
ANISOU 2156  CG  HIS A 290     4173   4178   4391     17      8    -65       C  
ATOM   2157  ND1 HIS A 290     106.843 105.145  26.315  1.00 34.75           N  
ANISOU 2157  ND1 HIS A 290     4336   4317   4549      4      7    -81       N  
ATOM   2158  CD2 HIS A 290     104.906 104.954  25.341  1.00 34.33           C  
ANISOU 2158  CD2 HIS A 290     4273   4268   4505     34     25    -62       C  
ATOM   2159  CE1 HIS A 290     106.404 106.373  26.095  1.00 33.44           C  
ANISOU 2159  CE1 HIS A 290     4176   4129   4400     12     25    -87       C  
ATOM   2160  NE2 HIS A 290     105.225 106.289  25.525  1.00 33.81           N  
ANISOU 2160  NE2 HIS A 290     4217   4178   4452     31     36    -75       N  
ATOM   2161  N   ASN A 291     103.216 102.089  26.965  1.00 30.83           N  
ANISOU 2161  N   ASN A 291     3823   3878   4012     33     18    -59       N  
ATOM   2162  CA  ASN A 291     101.841 102.567  27.167  1.00 33.48           C  
ANISOU 2162  CA  ASN A 291     4160   4211   4351     47     37    -63       C  
ATOM   2163  C   ASN A 291     101.220 102.111  28.481  1.00 34.34           C  
ANISOU 2163  C   ASN A 291     4277   4332   4439     42     43    -74       C  
ATOM   2164  O   ASN A 291     100.465 102.846  29.070  1.00 34.83           O  
ANISOU 2164  O   ASN A 291     4346   4387   4501     48     60    -87       O  
ATOM   2165  CB  ASN A 291     100.919 102.140  26.014  1.00 33.13           C  
ANISOU 2165  CB  ASN A 291     4098   4173   4316     63     40    -44       C  
ATOM   2166  CG  ASN A 291     101.237 102.847  24.707  1.00 32.78           C  
ANISOU 2166  CG  ASN A 291     4047   4117   4292     71     40    -33       C  
ATOM   2167  OD1 ASN A 291     101.709 103.951  24.706  1.00 34.45           O  
ANISOU 2167  OD1 ASN A 291     4267   4309   4515     71     46    -40       O  
ATOM   2168  ND2 ASN A 291     101.039 102.174  23.593  1.00 32.37           N  
ANISOU 2168  ND2 ASN A 291     3981   4075   4244     77     33    -15       N  
ATOM   2169  N   VAL A 292     101.547 100.903  28.942  1.00 34.92           N  
ANISOU 2169  N   VAL A 292     4350   4424   4496     33     30    -70       N  
ATOM   2170  CA  VAL A 292     100.943 100.368  30.160  1.00 34.73           C  
ANISOU 2170  CA  VAL A 292     4333   4413   4450     28     36    -78       C  
ATOM   2171  C   VAL A 292     101.832 100.537  31.408  1.00 35.87           C  
ANISOU 2171  C   VAL A 292     4493   4560   4575     12     28    -93       C  
ATOM   2172  O   VAL A 292     101.298 100.725  32.473  1.00 35.77           O  
ANISOU 2172  O   VAL A 292     4491   4552   4547      9     39   -107       O  
ATOM   2173  CB  VAL A 292     100.537  98.876  30.000  1.00 34.70           C  
ANISOU 2173  CB  VAL A 292     4319   4429   4438     29     30    -62       C  
ATOM   2174  CG1 VAL A 292      99.799  98.400  31.247  1.00 34.24           C  
ANISOU 2174  CG1 VAL A 292     4267   4382   4359     26     39    -68       C  
ATOM   2175  CG2 VAL A 292      99.641  98.676  28.775  1.00 35.04           C  
ANISOU 2175  CG2 VAL A 292     4345   4472   4498     43     36    -48       C  
ATOM   2176  N   ARG A 293     103.158 100.429  31.286  1.00 36.89           N  
ANISOU 2176  N   ARG A 293     4623   4690   4704      0     10    -91       N  
ATOM   2177  CA  ARG A 293     104.103 100.563  32.421  1.00 37.24           C  
ANISOU 2177  CA  ARG A 293     4680   4740   4730    -17      0   -105       C  
ATOM   2178  C   ARG A 293     105.192 101.567  32.110  1.00 35.48           C  
ANISOU 2178  C   ARG A 293     4460   4501   4519    -26     -7   -115       C  
ATOM   2179  O   ARG A 293     106.354 101.191  31.969  1.00 35.39           O  
ANISOU 2179  O   ARG A 293     4444   4495   4507    -36    -26   -108       O  
ATOM   2180  CB  ARG A 293     104.764  99.228  32.685  1.00 40.74           C  
ANISOU 2180  CB  ARG A 293     5119   5203   5159    -25    -19    -91       C  
ATOM   2181  CG  ARG A 293     103.847  98.239  33.329  1.00 46.72           C  
ANISOU 2181  CG  ARG A 293     5877   5976   5899    -21    -12    -84       C  
ATOM   2182  CD  ARG A 293     104.586  96.937  33.511  1.00 49.00           C  
ANISOU 2182  CD  ARG A 293     6160   6281   6176    -28    -30    -67       C  
ATOM   2183  NE  ARG A 293     105.261  96.704  34.797  1.00 50.03           N  
ANISOU 2183  NE  ARG A 293     6301   6427   6281    -41    -41    -72       N  
ATOM   2184  CZ  ARG A 293     104.675  96.243  35.924  1.00 44.65           C  
ANISOU 2184  CZ  ARG A 293     5630   5761   5576    -44    -35    -74       C  
ATOM   2185  NH1 ARG A 293     103.362  96.042  36.030  1.00 43.36           N  
ANISOU 2185  NH1 ARG A 293     5466   5598   5410    -35    -16    -74       N  
ATOM   2186  NH2 ARG A 293     105.425  95.973  36.949  1.00 42.62           N  
ANISOU 2186  NH2 ARG A 293     5380   5520   5295    -56    -48    -75       N  
ATOM   2187  N   PRO A 294     104.834 102.853  31.985  1.00 37.58           N  
ANISOU 2187  N   PRO A 294     4733   4747   4799    -22      9   -129       N  
ATOM   2188  CA  PRO A 294     105.843 103.845  31.601  1.00 36.28           C  
ANISOU 2188  CA  PRO A 294     4571   4565   4650    -30      4   -138       C  
ATOM   2189  C   PRO A 294     107.045 103.966  32.547  1.00 38.19           C  
ANISOU 2189  C   PRO A 294     4821   4814   4876    -52    -11   -153       C  
ATOM   2190  O   PRO A 294     108.131 104.344  32.102  1.00 37.94           O  
ANISOU 2190  O   PRO A 294     4786   4774   4856    -62    -22   -153       O  
ATOM   2191  CB  PRO A 294     105.042 105.159  31.496  1.00 36.52           C  
ANISOU 2191  CB  PRO A 294     4609   4572   4697    -20     29   -151       C  
ATOM   2192  CG  PRO A 294     103.776 104.938  32.247  1.00 36.46           C  
ANISOU 2192  CG  PRO A 294     4606   4572   4675    -12     44   -157       C  
ATOM   2193  CD  PRO A 294     103.481 103.463  32.129  1.00 36.89           C  
ANISOU 2193  CD  PRO A 294     4650   4651   4716     -8     33   -137       C  
ATOM   2194  N   GLN A 295     106.870 103.586  33.811  1.00 40.41           N  
ANISOU 2194  N   GLN A 295     5112   5113   5129    -61    -13   -163       N  
ATOM   2195  CA  GLN A 295     107.954 103.556  34.813  1.00 42.43           C  
ANISOU 2195  CA  GLN A 295     5374   5382   5364    -83    -31   -176       C  
ATOM   2196  C   GLN A 295     109.107 102.613  34.467  1.00 40.11           C  
ANISOU 2196  C   GLN A 295     5068   5104   5070    -89    -56   -157       C  
ATOM   2197  O   GLN A 295     110.188 102.742  35.007  1.00 39.09           O  
ANISOU 2197  O   GLN A 295     4939   4982   4930   -107    -73   -165       O  
ATOM   2198  CB  GLN A 295     107.392 103.220  36.209  1.00 45.59           C  
ANISOU 2198  CB  GLN A 295     5788   5802   5731    -89    -27   -188       C  
ATOM   2199  CG  GLN A 295     106.887 101.765  36.389  1.00 49.57           C  
ANISOU 2199  CG  GLN A 295     6286   6329   6221    -80    -32   -166       C  
ATOM   2200  CD  GLN A 295     105.409 101.527  35.985  1.00 49.37           C  
ANISOU 2200  CD  GLN A 295     6258   6298   6204    -60    -11   -158       C  
ATOM   2201  OE1 GLN A 295     104.763 102.342  35.301  1.00 45.42           O  
ANISOU 2201  OE1 GLN A 295     5756   5777   5725    -49      6   -162       O  
ATOM   2202  NE2 GLN A 295     104.876 100.401  36.429  1.00 51.69           N  
ANISOU 2202  NE2 GLN A 295     6549   6610   6480    -57    -12   -144       N  
ATOM   2203  N   GLN A 296     108.869 101.655  33.578  1.00 38.26           N  
ANISOU 2203  N   GLN A 296     4820   4873   4846    -76    -59   -132       N  
ATOM   2204  CA  GLN A 296     109.933 100.768  33.084  1.00 38.23           C  
ANISOU 2204  CA  GLN A 296     4802   4879   4846    -79    -80   -112       C  
ATOM   2205  C   GLN A 296     110.980 101.473  32.194  1.00 36.39           C  
ANISOU 2205  C   GLN A 296     4561   4630   4636    -85    -87   -113       C  
ATOM   2206  O   GLN A 296     112.104 101.000  32.059  1.00 35.36           O  
ANISOU 2206  O   GLN A 296     4422   4508   4507    -93   -105   -103       O  
ATOM   2207  CB  GLN A 296     109.279  99.637  32.303  1.00 41.93           C  
ANISOU 2207  CB  GLN A 296     5260   5352   5321    -63    -77    -89       C  
ATOM   2208  CG  GLN A 296     110.090  98.390  32.261  1.00 46.02           C  
ANISOU 2208  CG  GLN A 296     5766   5885   5833    -66    -95    -69       C  
ATOM   2209  CD  GLN A 296     110.187  97.730  33.631  1.00 46.19           C  
ANISOU 2209  CD  GLN A 296     5796   5930   5825    -75   -104    -70       C  
ATOM   2210  OE1 GLN A 296     109.193  97.596  34.358  1.00 51.03           O  
ANISOU 2210  OE1 GLN A 296     6418   6550   6422    -71    -93    -75       O  
ATOM   2211  NE2 GLN A 296     111.355  97.324  33.975  1.00 45.39           N  
ANISOU 2211  NE2 GLN A 296     5689   5841   5717    -85   -124    -63       N  
ATOM   2212  N   LYS A 297     110.591 102.590  31.576  1.00 36.28           N  
ANISOU 2212  N   LYS A 297     4551   4592   4642    -80    -71   -122       N  
ATOM   2213  CA  LYS A 297     111.430 103.358  30.673  1.00 39.08           C  
ANISOU 2213  CA  LYS A 297     4900   4929   5021    -83    -72   -122       C  
ATOM   2214  C   LYS A 297     112.072 102.482  29.588  1.00 36.34           C  
ANISOU 2214  C   LYS A 297     4535   4585   4686    -78    -84    -98       C  
ATOM   2215  O   LYS A 297     113.246 102.595  29.313  1.00 32.87           O  
ANISOU 2215  O   LYS A 297     4089   4145   4256    -88    -96    -95       O  
ATOM   2216  CB  LYS A 297     112.511 104.125  31.454  1.00 43.94           C  
ANISOU 2216  CB  LYS A 297     5522   5544   5632   -106    -82   -143       C  
ATOM   2217  CG  LYS A 297     111.973 105.207  32.395  1.00 48.52           C  
ANISOU 2217  CG  LYS A 297     6119   6113   6202   -113    -68   -171       C  
ATOM   2218  CD  LYS A 297     113.099 105.597  33.349  1.00 56.12           C  
ANISOU 2218  CD  LYS A 297     7087   7086   7152   -139    -83   -191       C  
ATOM   2219  CE  LYS A 297     112.658 106.394  34.561  1.00 60.56           C  
ANISOU 2219  CE  LYS A 297     7668   7646   7696   -151    -72   -222       C  
ATOM   2220  NZ  LYS A 297     112.499 107.824  34.210  1.00 64.14           N  
ANISOU 2220  NZ  LYS A 297     8130   8067   8172   -152    -52   -241       N  
ATOM   2221  N   ILE A 298     111.265 101.616  28.965  1.00 33.78           N  
ANISOU 2221  N   ILE A 298     4205   4266   4363    -62    -79    -80       N  
ATOM   2222  CA  ILE A 298     111.793 100.595  28.070  1.00 30.58           C  
ANISOU 2222  CA  ILE A 298     3785   3868   3966    -57    -89    -58       C  
ATOM   2223  C   ILE A 298     112.538 101.194  26.863  1.00 30.69           C  
ANISOU 2223  C   ILE A 298     3790   3865   4004    -56    -88    -52       C  
ATOM   2224  O   ILE A 298     113.574 100.693  26.477  1.00 30.31           O  
ANISOU 2224  O   ILE A 298     3732   3822   3963    -62   -101    -42       O  
ATOM   2225  CB  ILE A 298     110.675  99.639  27.634  1.00 29.97           C  
ANISOU 2225  CB  ILE A 298     3704   3798   3886    -41    -81    -44       C  
ATOM   2226  CG1 ILE A 298     111.252  98.385  26.978  1.00 29.64           C  
ANISOU 2226  CG1 ILE A 298     3649   3766   3848    -39    -92    -24       C  
ATOM   2227  CG2 ILE A 298     109.685 100.366  26.688  1.00 30.22           C  
ANISOU 2227  CG2 ILE A 298     3735   3815   3933    -27    -63    -44       C  
ATOM   2228  CD1 ILE A 298     112.045  97.511  27.942  1.00 30.35           C  
ANISOU 2228  CD1 ILE A 298     3737   3873   3922    -49   -108    -21       C  
ATOM   2229  N   PHE A 299     112.044 102.305  26.312  1.00 30.42           N  
ANISOU 2229  N   PHE A 299     3761   3811   3985    -50    -73    -59       N  
ATOM   2230  CA  PHE A 299     112.720 102.966  25.201  1.00 31.01           C  
ANISOU 2230  CA  PHE A 299     3829   3869   4083    -50    -70    -52       C  
ATOM   2231  C   PHE A 299     114.024 103.702  25.566  1.00 32.20           C  
ANISOU 2231  C   PHE A 299     3981   4013   4241    -69    -79    -64       C  
ATOM   2232  O   PHE A 299     114.746 104.150  24.664  1.00 35.61           O  
ANISOU 2232  O   PHE A 299     4406   4432   4692    -70    -78    -58       O  
ATOM   2233  CB  PHE A 299     111.756 103.859  24.404  1.00 29.49           C  
ANISOU 2233  CB  PHE A 299     3641   3660   3906    -35    -51    -51       C  
ATOM   2234  CG  PHE A 299     110.706 103.095  23.635  1.00 28.47           C  
ANISOU 2234  CG  PHE A 299     3505   3538   3774    -17    -45    -34       C  
ATOM   2235  CD1 PHE A 299     111.072 102.104  22.709  1.00 27.75           C  
ANISOU 2235  CD1 PHE A 299     3400   3457   3685    -14    -53    -16       C  
ATOM   2236  CD2 PHE A 299     109.369 103.399  23.781  1.00 28.26           C  
ANISOU 2236  CD2 PHE A 299     3483   3510   3745     -5    -31    -37       C  
ATOM   2237  CE1 PHE A 299     110.139 101.408  21.984  1.00 26.76           C  
ANISOU 2237  CE1 PHE A 299     3269   3341   3558      0    -48     -4       C  
ATOM   2238  CE2 PHE A 299     108.402 102.701  23.048  1.00 28.85           C  
ANISOU 2238  CE2 PHE A 299     3550   3594   3818     10    -27    -23       C  
ATOM   2239  CZ  PHE A 299     108.794 101.699  22.153  1.00 27.92           C  
ANISOU 2239  CZ  PHE A 299     3420   3488   3701     12    -36     -7       C  
ATOM   2240  N   GLU A 300     114.338 103.797  26.857  1.00 33.86           N  
ANISOU 2240  N   GLU A 300     4199   4233   4435    -83    -88    -81       N  
ATOM   2241  CA  GLU A 300     115.661 104.271  27.353  1.00 34.53           C  
ANISOU 2241  CA  GLU A 300     4281   4317   4521   -104   -101    -93       C  
ATOM   2242  C   GLU A 300     116.615 103.143  27.709  1.00 32.10           C  
ANISOU 2242  C   GLU A 300     3961   4033   4202   -112   -123    -82       C  
ATOM   2243  O   GLU A 300     117.810 103.361  27.935  1.00 31.67           O  
ANISOU 2243  O   GLU A 300     3900   3982   4152   -128   -136    -87       O  
ATOM   2244  CB  GLU A 300     115.457 105.164  28.567  1.00 35.63           C  
ANISOU 2244  CB  GLU A 300     4436   4453   4648   -118    -96   -120       C  
ATOM   2245  CG  GLU A 300     114.665 106.398  28.193  1.00 40.69           C  
ANISOU 2245  CG  GLU A 300     5088   5066   5305   -110    -73   -131       C  
ATOM   2246  CD  GLU A 300     114.367 107.312  29.380  1.00 46.00           C  
ANISOU 2246  CD  GLU A 300     5778   5733   5967   -123    -65   -160       C  
ATOM   2247  OE1 GLU A 300     114.797 107.048  30.517  1.00 52.56           O  
ANISOU 2247  OE1 GLU A 300     6612   6582   6775   -139    -78   -174       O  
ATOM   2248  OE2 GLU A 300     113.666 108.307  29.169  1.00 52.87           O  
ANISOU 2248  OE2 GLU A 300     6658   6580   6851   -116    -43   -170       O  
ATOM   2249  N   HIS A 301     116.107 101.931  27.742  1.00 29.74           N  
ANISOU 2249  N   HIS A 301     3659   3750   3891   -101   -126    -67       N  
ATOM   2250  CA  HIS A 301     116.922 100.829  28.163  1.00 30.64           C  
ANISOU 2250  CA  HIS A 301     3762   3885   3994   -106   -146    -55       C  
ATOM   2251  C   HIS A 301     118.164 100.646  27.273  1.00 29.54           C  
ANISOU 2251  C   HIS A 301     3606   3743   3875   -109   -154    -42       C  
ATOM   2252  O   HIS A 301     118.073 100.724  26.039  1.00 29.21           O  
ANISOU 2252  O   HIS A 301     3559   3687   3852    -99   -144    -32       O  
ATOM   2253  CB  HIS A 301     116.106  99.562  28.216  1.00 30.92           C  
ANISOU 2253  CB  HIS A 301     3797   3935   4018    -92   -144    -40       C  
ATOM   2254  CG  HIS A 301     116.731  98.508  29.048  1.00 32.79           C  
ANISOU 2254  CG  HIS A 301     4028   4194   4238    -98   -162    -31       C  
ATOM   2255  ND1 HIS A 301     116.505  98.411  30.400  1.00 34.93           N  
ANISOU 2255  ND1 HIS A 301     4308   4481   4483   -105   -169    -40       N  
ATOM   2256  CD2 HIS A 301     117.646  97.559  28.746  1.00 35.33           C  
ANISOU 2256  CD2 HIS A 301     4334   4525   4565    -97   -175    -13       C  
ATOM   2257  CE1 HIS A 301     117.214  97.411  30.889  1.00 35.83           C  
ANISOU 2257  CE1 HIS A 301     4413   4615   4587   -108   -185    -26       C  
ATOM   2258  NE2 HIS A 301     117.898  96.861  29.896  1.00 37.04           N  
ANISOU 2258  NE2 HIS A 301     4551   4763   4759   -102   -189     -9       N  
ATOM   2259  N   LYS A 302     119.294 100.376  27.935  1.00 30.70           N  
ANISOU 2259  N   LYS A 302     3745   3905   4016   -123   -173    -42       N  
ATOM   2260  CA  LYS A 302     120.642 100.287  27.356  1.00 30.32           C  
ANISOU 2260  CA  LYS A 302     3679   3857   3985   -130   -184    -33       C  
ATOM   2261  C   LYS A 302     120.933 101.420  26.388  1.00 31.78           C  
ANISOU 2261  C   LYS A 302     3863   4018   4195   -133   -172    -39       C  
ATOM   2262  O   LYS A 302     121.219 101.207  25.201  1.00 28.73           O  
ANISOU 2262  O   LYS A 302     3466   3622   3827   -125   -165    -24       O  
ATOM   2263  CB  LYS A 302     120.842  98.924  26.674  1.00 30.61           C  
ANISOU 2263  CB  LYS A 302     3702   3901   4027   -116   -187     -7       C  
ATOM   2264  CG  LYS A 302     122.334  98.585  26.416  1.00 29.95           C  
ANISOU 2264  CG  LYS A 302     3599   3825   3957   -124   -201      4       C  
ATOM   2265  CD  LYS A 302     122.402  97.497  25.350  1.00 30.26           C  
ANISOU 2265  CD  LYS A 302     3627   3862   4009   -108   -195     27       C  
ATOM   2266  CE  LYS A 302     123.807  97.374  24.754  1.00 30.40           C  
ANISOU 2266  CE  LYS A 302     3625   3880   4047   -113   -202     37       C  
ATOM   2267  NZ  LYS A 302     124.493  96.263  25.400  1.00 28.99           N  
ANISOU 2267  NZ  LYS A 302     3433   3721   3861   -112   -218     52       N  
ATOM   2268  N   ASP A 303     120.762 102.643  26.883  1.00 34.38           N  
ANISOU 2268  N   ASP A 303     4204   4335   4523   -145   -166    -61       N  
ATOM   2269  CA  ASP A 303     121.000 103.849  26.089  1.00 36.12           C  
ANISOU 2269  CA  ASP A 303     4427   4531   4768   -149   -153    -68       C  
ATOM   2270  C   ASP A 303     120.152 103.943  24.780  1.00 33.88           C  
ANISOU 2270  C   ASP A 303     4145   4229   4499   -129   -133    -55       C  
ATOM   2271  O   ASP A 303     120.624 104.232  23.706  1.00 32.91           O  
ANISOU 2271  O   ASP A 303     4015   4093   4397   -126   -126    -45       O  
ATOM   2272  CB  ASP A 303     122.521 103.975  25.833  1.00 39.80           C  
ANISOU 2272  CB  ASP A 303     4875   4998   5249   -164   -165    -65       C  
ATOM   2273  CG  ASP A 303     122.900 105.312  25.242  1.00 46.65           C  
ANISOU 2273  CG  ASP A 303     5744   5839   6140   -174   -152    -76       C  
ATOM   2274  OD1 ASP A 303     122.216 106.342  25.558  1.00 53.08           O  
ANISOU 2274  OD1 ASP A 303     6576   6638   6955   -177   -139    -94       O  
ATOM   2275  OD2 ASP A 303     123.858 105.336  24.427  1.00 53.56           O  
ANISOU 2275  OD2 ASP A 303     6605   6710   7036   -177   -153    -65       O  
ATOM   2276  N   GLY A 304     118.867 103.688  24.889  1.00 33.33           N  
ANISOU 2276  N   GLY A 304     4086   4160   4418   -115   -123    -54       N  
ATOM   2277  CA  GLY A 304     117.982 103.679  23.732  1.00 30.41           C  
ANISOU 2277  CA  GLY A 304     3717   3778   4058    -95   -106    -41       C  
ATOM   2278  C   GLY A 304     118.291 102.670  22.601  1.00 28.82           C  
ANISOU 2278  C   GLY A 304     3502   3584   3864    -85   -109    -18       C  
ATOM   2279  O   GLY A 304     118.058 102.978  21.469  1.00 28.45           O  
ANISOU 2279  O   GLY A 304     3453   3524   3831    -75    -97     -8       O  
ATOM   2280  N   VAL A 305     118.775 101.467  22.909  1.00 27.38           N  
ANISOU 2280  N   VAL A 305     3311   3421   3673    -86   -123     -9       N  
ATOM   2281  CA  VAL A 305     119.317 100.586  21.875  1.00 28.32           C  
ANISOU 2281  CA  VAL A 305     3415   3543   3801    -79   -125     10       C  
ATOM   2282  C   VAL A 305     118.238 100.074  20.907  1.00 28.46           C  
ANISOU 2282  C   VAL A 305     3435   3559   3819    -61   -112     22       C  
ATOM   2283  O   VAL A 305     118.524  99.866  19.745  1.00 28.49           O  
ANISOU 2283  O   VAL A 305     3431   3559   3834    -55   -106     34       O  
ATOM   2284  CB  VAL A 305     120.164  99.405  22.490  1.00 28.09           C  
ANISOU 2284  CB  VAL A 305     3375   3533   3764    -84   -142     18       C  
ATOM   2285  CG1 VAL A 305     119.263  98.310  23.070  1.00 27.10           C  
ANISOU 2285  CG1 VAL A 305     3254   3423   3620    -75   -144     23       C  
ATOM   2286  CG2 VAL A 305     121.111  98.807  21.453  1.00 28.73           C  
ANISOU 2286  CG2 VAL A 305     3441   3614   3863    -81   -143     35       C  
ATOM   2287  N   LEU A 306     117.013  99.859  21.380  1.00 27.64           N  
ANISOU 2287  N   LEU A 306     3341   3461   3700    -53   -107     18       N  
ATOM   2288  CA  LEU A 306     115.975  99.290  20.503  1.00 27.53           C  
ANISOU 2288  CA  LEU A 306     3327   3449   3685    -38    -97     28       C  
ATOM   2289  C   LEU A 306     115.619 100.204  19.309  1.00 29.18           C  
ANISOU 2289  C   LEU A 306     3537   3643   3908    -30    -83     32       C  
ATOM   2290  O   LEU A 306     115.504  99.741  18.167  1.00 27.88           O  
ANISOU 2290  O   LEU A 306     3366   3480   3747    -21    -78     45       O  
ATOM   2291  CB  LEU A 306     114.687  98.937  21.285  1.00 27.20           C  
ANISOU 2291  CB  LEU A 306     3295   3416   3626    -32    -94     22       C  
ATOM   2292  CG  LEU A 306     114.773  97.756  22.243  1.00 29.24           C  
ANISOU 2292  CG  LEU A 306     3551   3691   3868    -35   -105     24       C  
ATOM   2293  CD1 LEU A 306     113.418  97.471  22.889  1.00 31.75           C  
ANISOU 2293  CD1 LEU A 306     3878   4016   4170    -29    -99     19       C  
ATOM   2294  CD2 LEU A 306     115.298  96.500  21.602  1.00 28.43           C  
ANISOU 2294  CD2 LEU A 306     3437   3596   3770    -32   -109     39       C  
ATOM   2295  N   LEU A 307     115.443 101.485  19.582  1.00 29.93           N  
ANISOU 2295  N   LEU A 307     3640   3723   4008    -32    -76     22       N  
ATOM   2296  CA  LEU A 307     115.189 102.476  18.528  1.00 31.11           C  
ANISOU 2296  CA  LEU A 307     3791   3856   4172    -24    -62     27       C  
ATOM   2297  C   LEU A 307     116.391 102.649  17.637  1.00 30.49           C  
ANISOU 2297  C   LEU A 307     3704   3771   4110    -30    -63     36       C  
ATOM   2298  O   LEU A 307     116.255 102.739  16.418  1.00 31.98           O  
ANISOU 2298  O   LEU A 307     3889   3956   4306    -21    -54     49       O  
ATOM   2299  CB  LEU A 307     114.852 103.843  19.126  1.00 32.72           C  
ANISOU 2299  CB  LEU A 307     4006   4043   4381    -27    -53     13       C  
ATOM   2300  CG  LEU A 307     113.599 103.854  19.990  1.00 34.81           C  
ANISOU 2300  CG  LEU A 307     4281   4313   4633    -20    -49      3       C  
ATOM   2301  CD1 LEU A 307     113.514 105.080  20.901  1.00 36.39           C  
ANISOU 2301  CD1 LEU A 307     4493   4496   4836    -28    -42    -16       C  
ATOM   2302  CD2 LEU A 307     112.408 103.787  19.059  1.00 35.94           C  
ANISOU 2302  CD2 LEU A 307     4422   4457   4776     -1    -38     16       C  
ATOM   2303  N   LYS A 308     117.567 102.689  18.235  1.00 29.70           N  
ANISOU 2303  N   LYS A 308     3600   3671   4014    -45    -73     29       N  
ATOM   2304  CA  LYS A 308     118.774 102.774  17.465  1.00 29.70           C  
ANISOU 2304  CA  LYS A 308     3589   3665   4029    -51    -74     38       C  
ATOM   2305  C   LYS A 308     118.938 101.558  16.525  1.00 28.63           C  
ANISOU 2305  C   LYS A 308     3443   3542   3892    -43    -75     54       C  
ATOM   2306  O   LYS A 308     119.433 101.699  15.420  1.00 27.56           O  
ANISOU 2306  O   LYS A 308     3301   3400   3769    -41    -68     65       O  
ATOM   2307  CB  LYS A 308     119.986 102.919  18.389  1.00 30.78           C  
ANISOU 2307  CB  LYS A 308     3721   3804   4170    -70    -87     27       C  
ATOM   2308  CG  LYS A 308     121.284 102.884  17.628  1.00 34.89           C  
ANISOU 2308  CG  LYS A 308     4229   4321   4708    -77    -89     37       C  
ATOM   2309  CD  LYS A 308     122.516 102.907  18.506  1.00 37.33           C  
ANISOU 2309  CD  LYS A 308     4528   4635   5020    -95   -104     28       C  
ATOM   2310  CE  LYS A 308     122.730 104.268  19.129  1.00 37.85           C  
ANISOU 2310  CE  LYS A 308     4601   4685   5093   -110   -101     11       C  
ATOM   2311  NZ  LYS A 308     123.960 104.124  19.936  1.00 40.27           N  
ANISOU 2311  NZ  LYS A 308     4897   5003   5401   -129   -119      3       N  
ATOM   2312  N   SER A 309     118.549 100.368  16.985  1.00 28.39           N  
ANISOU 2312  N   SER A 309     3411   3528   3847    -40    -83     55       N  
ATOM   2313  CA  SER A 309     118.792  99.136  16.239  1.00 27.65           C  
ANISOU 2313  CA  SER A 309     3308   3445   3753    -34    -84     68       C  
ATOM   2314  C   SER A 309     117.986  99.061  14.923  1.00 27.70           C  
ANISOU 2314  C   SER A 309     3315   3450   3758    -21    -71     78       C  
ATOM   2315  O   SER A 309     118.352  98.344  13.998  1.00 27.91           O  
ANISOU 2315  O   SER A 309     3334   3481   3788    -18    -68     87       O  
ATOM   2316  CB  SER A 309     118.494  97.915  17.129  1.00 27.59           C  
ANISOU 2316  CB  SER A 309     3299   3452   3730    -33    -94     67       C  
ATOM   2317  OG  SER A 309     117.084  97.728  17.266  1.00 26.96           O  
ANISOU 2317  OG  SER A 309     3228   3377   3637    -24    -88     64       O  
ATOM   2318  N   VAL A 310     116.886  99.812  14.837  1.00 27.46           N  
ANISOU 2318  N   VAL A 310     3294   3415   3724    -13    -63     75       N  
ATOM   2319  CA  VAL A 310     116.110  99.872  13.630  1.00 26.72           C  
ANISOU 2319  CA  VAL A 310     3201   3323   3629     -1    -53     85       C  
ATOM   2320  C   VAL A 310     116.944 100.535  12.487  1.00 26.84           C  
ANISOU 2320  C   VAL A 310     3212   3328   3659     -2    -45     95       C  
ATOM   2321  O   VAL A 310     117.009  99.990  11.352  1.00 24.64           O  
ANISOU 2321  O   VAL A 310     2928   3056   3379      3    -40    106       O  
ATOM   2322  CB  VAL A 310     114.739 100.585  13.874  1.00 26.67           C  
ANISOU 2322  CB  VAL A 310     3203   3314   3616      8    -46     81       C  
ATOM   2323  CG1 VAL A 310     113.946 100.681  12.589  1.00 26.42           C  
ANISOU 2323  CG1 VAL A 310     3169   3287   3582     21    -37     94       C  
ATOM   2324  CG2 VAL A 310     113.920  99.834  14.908  1.00 26.28           C  
ANISOU 2324  CG2 VAL A 310     3157   3277   3552      9    -52     72       C  
ATOM   2325  N   ASN A 311     117.613 101.648  12.797  1.00 26.57           N  
ANISOU 2325  N   ASN A 311     3180   3278   3638    -10    -43     91       N  
ATOM   2326  CA AASN A 311     118.499 102.303  11.833  0.50 26.64           C  
ANISOU 2326  CA AASN A 311     3185   3275   3663    -12    -35    100       C  
ATOM   2327  CA BASN A 311     118.499 102.313  11.837  0.50 28.79           C  
ANISOU 2327  CA BASN A 311     3457   3548   3936    -12    -35    100       C  
ATOM   2328  C   ASN A 311     119.626 101.367  11.457  1.00 27.19           C  
ANISOU 2328  C   ASN A 311     3242   3352   3736    -19    -39    105       C  
ATOM   2329  O   ASN A 311     119.953 101.239  10.305  1.00 29.68           O  
ANISOU 2329  O   ASN A 311     3553   3668   4055    -15    -31    117       O  
ATOM   2330  CB AASN A 311     119.074 103.614  12.391  0.50 26.25           C  
ANISOU 2330  CB AASN A 311     3139   3206   3629    -22    -32     92       C  
ATOM   2331  CB BASN A 311     119.044 103.631  12.426  0.50 31.25           C  
ANISOU 2331  CB BASN A 311     3773   3839   4262    -22    -32     92       C  
ATOM   2332  CG AASN A 311     117.989 104.601  12.803  0.50 26.27           C  
ANISOU 2332  CG AASN A 311     3153   3197   3629    -15    -25     87       C  
ATOM   2333  CG BASN A 311     119.917 104.413  11.456  0.50 34.80           C  
ANISOU 2333  CG BASN A 311     4219   4275   4730    -25    -21    102       C  
ATOM   2334  OD1AASN A 311     116.851 104.542  12.304  0.50 25.93           O  
ANISOU 2334  OD1AASN A 311     3114   3160   3578      0    -19     94       O  
ATOM   2335  OD1BASN A 311     119.465 105.364  10.797  0.50 39.11           O  
ANISOU 2335  OD1BASN A 311     4770   4807   5281    -18     -8    110       O  
ATOM   2336  ND2AASN A 311     118.329 105.502  13.720  0.50 26.06           N  
ANISOU 2336  ND2AASN A 311     3133   3156   3612    -26    -25     73       N  
ATOM   2337  ND2BASN A 311     121.184 104.036  11.374  0.50 36.68           N  
ANISOU 2337  ND2BASN A 311     4447   4514   4977    -37    -26    103       N  
ATOM   2338  N   THR A 312     120.215 100.716  12.447  1.00 26.92           N  
ANISOU 2338  N   THR A 312     3203   3324   3700    -28    -52     97       N  
ATOM   2339  CA  THR A 312     121.311  99.794  12.191  1.00 26.27           C  
ANISOU 2339  CA  THR A 312     3109   3249   3625    -33    -56    103       C  
ATOM   2340  C   THR A 312     120.828  98.693  11.263  1.00 25.32           C  
ANISOU 2340  C   THR A 312     2987   3140   3495    -22    -50    111       C  
ATOM   2341  O   THR A 312     121.521  98.338  10.339  1.00 24.58           O  
ANISOU 2341  O   THR A 312     2885   3046   3407    -22    -44    119       O  
ATOM   2342  CB  THR A 312     121.840  99.193  13.504  1.00 25.25           C  
ANISOU 2342  CB  THR A 312     2975   3126   3492    -41    -72     95       C  
ATOM   2343  OG1 THR A 312     122.330 100.256  14.320  1.00 25.62           O  
ANISOU 2343  OG1 THR A 312     3023   3164   3547    -53    -77     85       O  
ATOM   2344  CG2 THR A 312     123.000  98.195  13.263  1.00 24.28           C  
ANISOU 2344  CG2 THR A 312     2837   3010   3377    -45    -75    103       C  
ATOM   2345  N   LEU A 313     119.637  98.123  11.525  1.00 24.45           N  
ANISOU 2345  N   LEU A 313     2883   3039   3369    -15    -52    108       N  
ATOM   2346  CA  LEU A 313     119.184  97.036  10.678  1.00 23.80           C  
ANISOU 2346  CA  LEU A 313     2798   2967   3277     -8    -47    113       C  
ATOM   2347  C   LEU A 313     118.929  97.506   9.212  1.00 23.46           C  
ANISOU 2347  C   LEU A 313     2756   2924   3235     -1    -34    123       C  
ATOM   2348  O   LEU A 313     119.290  96.827   8.219  1.00 21.76           O  
ANISOU 2348  O   LEU A 313     2536   2714   3019      0    -27    129       O  
ATOM   2349  CB  LEU A 313     117.940  96.399  11.278  1.00 24.14           C  
ANISOU 2349  CB  LEU A 313     2847   3021   3304     -3    -51    108       C  
ATOM   2350  CG  LEU A 313     117.341  95.288  10.441  1.00 23.66           C  
ANISOU 2350  CG  LEU A 313     2784   2972   3234      3    -45    111       C  
ATOM   2351  CD1 LEU A 313     118.279  94.123  10.259  1.00 24.30           C  
ANISOU 2351  CD1 LEU A 313     2858   3055   3321     -1    -45    113       C  
ATOM   2352  CD2 LEU A 313     116.077  94.844  11.125  1.00 24.59           C  
ANISOU 2352  CD2 LEU A 313     2907   3098   3337      6    -49    104       C  
ATOM   2353  N   LEU A 314     118.280  98.652   9.077  1.00 23.33           N  
ANISOU 2353  N   LEU A 314     2746   2901   3217      4    -30    124       N  
ATOM   2354  CA  LEU A 314     118.113  99.233   7.768  1.00 24.77           C  
ANISOU 2354  CA  LEU A 314     2929   3082   3400     10    -18    136       C  
ATOM   2355  C   LEU A 314     119.473  99.443   7.057  1.00 24.94           C  
ANISOU 2355  C   LEU A 314     2944   3096   3435      4    -12    143       C  
ATOM   2356  O   LEU A 314     119.567  99.265   5.837  1.00 24.24           O  
ANISOU 2356  O   LEU A 314     2853   3012   3343      8     -2    152       O  
ATOM   2357  CB  LEU A 314     117.344 100.542   7.856  1.00 26.00           C  
ANISOU 2357  CB  LEU A 314     3093   3229   3557     17    -14    138       C  
ATOM   2358  CG  LEU A 314     115.872 100.367   8.263  1.00 26.79           C  
ANISOU 2358  CG  LEU A 314     3198   3339   3643     25    -18    134       C  
ATOM   2359  CD1 LEU A 314     115.259 101.729   8.655  1.00 27.51           C  
ANISOU 2359  CD1 LEU A 314     3297   3417   3740     31    -13    134       C  
ATOM   2360  CD2 LEU A 314     115.045  99.711   7.168  1.00 26.70           C  
ANISOU 2360  CD2 LEU A 314     3183   3345   3615     34    -14    142       C  
ATOM   2361  N   SER A 315     120.519  99.773   7.808  1.00 25.11           N  
ANISOU 2361  N   SER A 315     2962   3106   3472     -6    -16    138       N  
ATOM   2362  CA  SER A 315     121.832  99.952   7.194  1.00 27.22           C  
ANISOU 2362  CA  SER A 315     3221   3366   3755    -13    -10    145       C  
ATOM   2363  C   SER A 315     122.467  98.665   6.748  1.00 25.62           C  
ANISOU 2363  C   SER A 315     3010   3174   3552    -13     -9    147       C  
ATOM   2364  O   SER A 315     123.447  98.703   6.021  1.00 25.08           O  
ANISOU 2364  O   SER A 315     2933   3101   3494    -17      0    154       O  
ATOM   2365  CB  SER A 315     122.765 100.688   8.154  1.00 28.27           C  
ANISOU 2365  CB  SER A 315     3350   3486   3905    -25    -16    139       C  
ATOM   2366  OG  SER A 315     122.188 101.956   8.383  1.00 31.84           O  
ANISOU 2366  OG  SER A 315     3812   3926   4360    -24    -13    137       O  
ATOM   2367  N   LEU A 316     121.966  97.530   7.252  1.00 25.44           N  
ANISOU 2367  N   LEU A 316     2987   3162   3518    -11    -16    141       N  
ATOM   2368  CA  LEU A 316     122.448  96.208   6.851  1.00 26.03           C  
ANISOU 2368  CA  LEU A 316     3053   3245   3591    -11    -13    142       C  
ATOM   2369  C   LEU A 316     121.667  95.595   5.676  1.00 26.48           C  
ANISOU 2369  C   LEU A 316     3114   3313   3633     -3     -3    145       C  
ATOM   2370  O   LEU A 316     121.575  94.346   5.527  1.00 24.87           O  
ANISOU 2370  O   LEU A 316     2909   3117   3424     -2     -1    141       O  
ATOM   2371  CB  LEU A 316     122.447  95.257   8.076  1.00 26.14           C  
ANISOU 2371  CB  LEU A 316     3064   3263   3604    -13    -26    135       C  
ATOM   2372  CG  LEU A 316     123.577  95.525   9.070  1.00 26.18           C  
ANISOU 2372  CG  LEU A 316     3061   3263   3625    -22    -36    134       C  
ATOM   2373  CD1 LEU A 316     123.228  95.057  10.455  1.00 26.83           C  
ANISOU 2373  CD1 LEU A 316     3144   3349   3699    -23    -51    127       C  
ATOM   2374  CD2 LEU A 316     124.850  94.832   8.628  1.00 27.19           C  
ANISOU 2374  CD2 LEU A 316     3174   3389   3766    -24    -31    140       C  
ATOM   2375  N   SER A 317     121.150  96.465   4.804  1.00 26.88           N  
ANISOU 2375  N   SER A 317     3171   3364   3678      1      5    151       N  
ATOM   2376  CA  SER A 317     120.484  96.032   3.601  1.00 26.71           C  
ANISOU 2376  CA  SER A 317     3153   3356   3641      7     14    154       C  
ATOM   2377  C   SER A 317     121.199  96.607   2.365  1.00 27.40           C  
ANISOU 2377  C   SER A 317     3238   3440   3732      7     28    166       C  
ATOM   2378  O   SER A 317     121.753  97.730   2.421  1.00 25.06           O  
ANISOU 2378  O   SER A 317     2941   3131   3449      5     30    173       O  
ATOM   2379  CB  SER A 317     119.019  96.424   3.661  1.00 26.81           C  
ANISOU 2379  CB  SER A 317     3173   3376   3637     14      9    154       C  
ATOM   2380  OG  SER A 317     118.813  97.841   3.612  1.00 25.76           O  
ANISOU 2380  OG  SER A 317     3044   3234   3508     18     11    162       O  
ATOM   2381  N   ASP A 318     121.192  95.822   1.277  1.00 25.92           N  
ANISOU 2381  N   ASP A 318     3050   3264   3534      8     38    167       N  
ATOM   2382  CA  ASP A 318     121.676  96.272  -0.013  1.00 26.16           C  
ANISOU 2382  CA  ASP A 318     3081   3296   3563      9     52    177       C  
ATOM   2383  C   ASP A 318     120.767  97.352  -0.670  1.00 26.70           C  
ANISOU 2383  C   ASP A 318     3157   3370   3618     17     54    189       C  
ATOM   2384  O   ASP A 318     119.742  97.799  -0.081  1.00 24.38           O  
ANISOU 2384  O   ASP A 318     2868   3078   3319     22     44    188       O  
ATOM   2385  CB  ASP A 318     121.947  95.081  -0.946  1.00 26.21           C  
ANISOU 2385  CB  ASP A 318     3085   3314   3560      7     63    173       C  
ATOM   2386  CG  ASP A 318     120.683  94.409  -1.512  1.00 27.18           C  
ANISOU 2386  CG  ASP A 318     3214   3456   3657     10     62    167       C  
ATOM   2387  OD1 ASP A 318     119.546  94.975  -1.458  1.00 25.85           O  
ANISOU 2387  OD1 ASP A 318     3051   3297   3476     16     54    170       O  
ATOM   2388  OD2 ASP A 318     120.860  93.243  -2.011  1.00 26.43           O  
ANISOU 2388  OD2 ASP A 318     3118   3369   3556      7     70    158       O  
ATOM   2389  N   ALA A 319     121.104  97.760  -1.880  1.00 26.27           N  
ANISOU 2389  N   ALA A 319     3103   3319   3559     18     67    201       N  
ATOM   2390  CA  ALA A 319     120.324  98.872  -2.560  1.00 27.89           C  
ANISOU 2390  CA  ALA A 319     3315   3530   3753     27     70    216       C  
ATOM   2391  C   ALA A 319     118.830  98.571  -2.805  1.00 27.99           C  
ANISOU 2391  C   ALA A 319     3331   3563   3741     34     62    215       C  
ATOM   2392  O   ALA A 319     118.062  99.482  -3.012  1.00 26.72           O  
ANISOU 2392  O   ALA A 319     3174   3405   3574     43     61    227       O  
ATOM   2393  CB  ALA A 319     120.974  99.262  -3.879  1.00 27.01           C  
ANISOU 2393  CB  ALA A 319     3203   3421   3638     28     87    231       C  
ATOM   2394  N   ASP A 320     118.433  97.299  -2.805  1.00 28.71           N  
ANISOU 2394  N   ASP A 320     3421   3669   3819     31     58    200       N  
ATOM   2395  CA  ASP A 320     117.069  96.917  -2.954  1.00 28.85           C  
ANISOU 2395  CA  ASP A 320     3440   3706   3815     35     50    196       C  
ATOM   2396  C   ASP A 320     116.372  96.676  -1.638  1.00 28.08           C  
ANISOU 2396  C   ASP A 320     3342   3604   3722     35     37    185       C  
ATOM   2397  O   ASP A 320     115.276  96.130  -1.663  1.00 26.64           O  
ANISOU 2397  O   ASP A 320     3159   3438   3523     37     31    179       O  
ATOM   2398  CB  ASP A 320     116.956  95.587  -3.741  1.00 32.77           C  
ANISOU 2398  CB  ASP A 320     3936   4222   4293     29     55    185       C  
ATOM   2399  CG  ASP A 320     117.429  95.694  -5.170  1.00 35.31           C  
ANISOU 2399  CG  ASP A 320     4259   4555   4602     28     69    194       C  
ATOM   2400  OD1 ASP A 320     117.106  96.682  -5.839  1.00 36.82           O  
ANISOU 2400  OD1 ASP A 320     4453   4753   4785     36     71    211       O  
ATOM   2401  OD2 ASP A 320     118.171  94.784  -5.600  1.00 41.25           O  
ANISOU 2401  OD2 ASP A 320     5010   5307   5354     20     79    185       O  
ATOM   2402  N   GLY A 321     117.010  96.986  -0.498  1.00 26.51           N  
ANISOU 2402  N   GLY A 321     3143   3384   3545     33     33    181       N  
ATOM   2403  CA  GLY A 321     116.458  96.726   0.799  1.00 25.52           C  
ANISOU 2403  CA  GLY A 321     3018   3255   3424     32     21    170       C  
ATOM   2404  C   GLY A 321     116.544  95.268   1.255  1.00 27.65           C  
ANISOU 2404  C   GLY A 321     3285   3530   3692     25     18    155       C  
ATOM   2405  O   GLY A 321     115.887  94.942   2.260  1.00 27.27           O  
ANISOU 2405  O   GLY A 321     3237   3481   3642     25      9    147       O  
ATOM   2406  N   GLU A 322     117.348  94.412   0.585  1.00 25.77           N  
ANISOU 2406  N   GLU A 322     3043   3293   3454     19     27    152       N  
ATOM   2407  CA  GLU A 322     117.541  93.020   1.012  1.00 26.62           C  
ANISOU 2407  CA  GLU A 322     3149   3402   3564     13     26    139       C  
ATOM   2408  C   GLU A 322     118.687  92.899   2.037  1.00 25.65           C  
ANISOU 2408  C   GLU A 322     3022   3261   3464      9     23    138       C  
ATOM   2409  O   GLU A 322     119.789  93.389   1.801  1.00 23.40           O  
ANISOU 2409  O   GLU A 322     2733   2965   3192      8     29    145       O  
ATOM   2410  CB  GLU A 322     117.798  92.072  -0.190  1.00 27.39           C  
ANISOU 2410  CB  GLU A 322     3246   3510   3652      9     39    135       C  
ATOM   2411  CG  GLU A 322     116.533  91.930  -0.986  1.00 31.27           C  
ANISOU 2411  CG  GLU A 322     3741   4023   4118     10     38    132       C  
ATOM   2412  CD  GLU A 322     116.601  91.089  -2.248  1.00 33.56           C  
ANISOU 2412  CD  GLU A 322     4032   4327   4393      5     50    126       C  
ATOM   2413  OE1 GLU A 322     117.589  90.427  -2.550  1.00 40.25           O  
ANISOU 2413  OE1 GLU A 322     4877   5166   5249      0     62    121       O  
ATOM   2414  OE2 GLU A 322     115.594  91.059  -2.923  1.00 36.98           O  
ANISOU 2414  OE2 GLU A 322     4466   4780   4805      5     48    124       O  
ATOM   2415  N   PHE A 323     118.450  92.165   3.118  1.00 23.97           N  
ANISOU 2415  N   PHE A 323     2808   3045   3253      7     15    129       N  
ATOM   2416  CA  PHE A 323     119.467  92.066   4.189  1.00 24.66           C  
ANISOU 2416  CA  PHE A 323     2891   3119   3360      4     10    129       C  
ATOM   2417  C   PHE A 323     120.650  91.250   3.756  1.00 23.62           C  
ANISOU 2417  C   PHE A 323     2752   2983   3241      1     19    130       C  
ATOM   2418  O   PHE A 323     120.473  90.273   3.076  1.00 24.50           O  
ANISOU 2418  O   PHE A 323     2864   3100   3346      1     29    125       O  
ATOM   2419  CB  PHE A 323     118.839  91.549   5.498  1.00 23.45           C  
ANISOU 2419  CB  PHE A 323     2739   2966   3204      4     -2    122       C  
ATOM   2420  CG  PHE A 323     117.783  92.471   6.021  1.00 22.23           C  
ANISOU 2420  CG  PHE A 323     2591   2815   3042      7    -10    122       C  
ATOM   2421  CD1 PHE A 323     118.109  93.774   6.370  1.00 21.76           C  
ANISOU 2421  CD1 PHE A 323     2532   2745   2989      8    -14    127       C  
ATOM   2422  CD2 PHE A 323     116.477  92.056   6.122  1.00 21.76           C  
ANISOU 2422  CD2 PHE A 323     2536   2766   2967     10    -13    116       C  
ATOM   2423  CE1 PHE A 323     117.154  94.670   6.803  1.00 22.06           C  
ANISOU 2423  CE1 PHE A 323     2576   2785   3021     12    -19    126       C  
ATOM   2424  CE2 PHE A 323     115.484  92.947   6.560  1.00 22.50           C  
ANISOU 2424  CE2 PHE A 323     2634   2863   3054     14    -19    116       C  
ATOM   2425  CZ  PHE A 323     115.812  94.265   6.882  1.00 22.37           C  
ANISOU 2425  CZ  PHE A 323     2619   2835   3045     16    -21    121       C  
ATOM   2426  N   PHE A 324     121.857  91.704   4.098  1.00 24.14           N  
ANISOU 2426  N   PHE A 324     2810   3037   3324     -1     19    136       N  
ATOM   2427  CA  PHE A 324     123.082  90.980   3.737  1.00 24.39           C  
ANISOU 2427  CA  PHE A 324     2832   3063   3371     -3     28    138       C  
ATOM   2428  C   PHE A 324     123.029  89.583   4.341  1.00 23.60           C  
ANISOU 2428  C   PHE A 324     2730   2963   3273     -2     27    133       C  
ATOM   2429  O   PHE A 324     122.720  89.433   5.504  1.00 24.13           O  
ANISOU 2429  O   PHE A 324     2798   3030   3342     -2     14    131       O  
ATOM   2430  CB  PHE A 324     124.332  91.716   4.221  1.00 24.31           C  
ANISOU 2430  CB  PHE A 324     2813   3043   3381     -6     25    146       C  
ATOM   2431  CG  PHE A 324     124.501  93.088   3.603  1.00 25.24           C  
ANISOU 2431  CG  PHE A 324     2933   3157   3501     -7     29    152       C  
ATOM   2432  CD1 PHE A 324     124.525  93.254   2.253  1.00 24.47           C  
ANISOU 2432  CD1 PHE A 324     2837   3063   3396     -6     44    157       C  
ATOM   2433  CD2 PHE A 324     124.586  94.225   4.416  1.00 25.77           C  
ANISOU 2433  CD2 PHE A 324     3000   3217   3574    -11     18    154       C  
ATOM   2434  CE1 PHE A 324     124.630  94.510   1.682  1.00 26.48           C  
ANISOU 2434  CE1 PHE A 324     3095   3314   3652     -6     49    165       C  
ATOM   2435  CE2 PHE A 324     124.703  95.500   3.852  1.00 27.08           C  
ANISOU 2435  CE2 PHE A 324     3169   3377   3743    -12     23    161       C  
ATOM   2436  CZ  PHE A 324     124.703  95.651   2.489  1.00 26.94           C  
ANISOU 2436  CZ  PHE A 324     3153   3362   3719     -9     39    168       C  
ATOM   2437  N   PRO A 325     123.338  88.546   3.567  1.00 24.42           N  
ANISOU 2437  N   PRO A 325     2832   3067   3379     -2     42    130       N  
ATOM   2438  CA  PRO A 325     123.083  87.188   4.107  1.00 24.55           C  
ANISOU 2438  CA  PRO A 325     2848   3081   3397     -1     43    124       C  
ATOM   2439  C   PRO A 325     124.207  86.575   4.971  1.00 25.37           C  
ANISOU 2439  C   PRO A 325     2941   3176   3523      1     40    130       C  
ATOM   2440  O   PRO A 325     124.796  85.520   4.642  1.00 27.04           O  
ANISOU 2440  O   PRO A 325     3147   3381   3746      4     54    130       O  
ATOM   2441  CB  PRO A 325     122.827  86.390   2.841  1.00 24.71           C  
ANISOU 2441  CB  PRO A 325     2873   3106   3409     -2     61    116       C  
ATOM   2442  CG  PRO A 325     123.659  87.053   1.803  1.00 23.57           C  
ANISOU 2442  CG  PRO A 325     2725   2961   3269     -2     72    121       C  
ATOM   2443  CD  PRO A 325     123.499  88.528   2.116  1.00 23.62           C  
ANISOU 2443  CD  PRO A 325     2732   2969   3271     -2     59    129       C  
ATOM   2444  N   LEU A 326     124.431  87.223   6.100  1.00 26.20           N  
ANISOU 2444  N   LEU A 326     3042   3279   3633      1     23    136       N  
ATOM   2445  CA  LEU A 326     125.412  86.847   7.121  1.00 27.21           C  
ANISOU 2445  CA  LEU A 326     3158   3402   3779      2     15    144       C  
ATOM   2446  C   LEU A 326     124.841  85.748   8.034  1.00 27.19           C  
ANISOU 2446  C   LEU A 326     3158   3400   3773      5     10    143       C  
ATOM   2447  O   LEU A 326     123.658  85.765   8.373  1.00 24.98           O  
ANISOU 2447  O   LEU A 326     2889   3125   3476      4      5    136       O  
ATOM   2448  CB  LEU A 326     125.739  88.065   7.941  1.00 28.16           C  
ANISOU 2448  CB  LEU A 326     3274   3523   3901     -2     -2    148       C  
ATOM   2449  CG  LEU A 326     126.200  89.308   7.171  1.00 31.25           C  
ANISOU 2449  CG  LEU A 326     3664   3913   4296     -6      2    150       C  
ATOM   2450  CD1 LEU A 326     126.677  90.352   8.152  1.00 31.56           C  
ANISOU 2450  CD1 LEU A 326     3699   3951   4342    -12    -14    152       C  
ATOM   2451  CD2 LEU A 326     127.298  88.936   6.142  1.00 33.15           C  
ANISOU 2451  CD2 LEU A 326     3894   4148   4552     -4     20    155       C  
ATOM   2452  N   ASN A 327     125.663  84.754   8.365  1.00 26.63           N  
ANISOU 2452  N   ASN A 327     3076   3322   3718     10     15    150       N  
ATOM   2453  CA  ASN A 327     125.243  83.650   9.203  1.00 26.22           C  
ANISOU 2453  CA  ASN A 327     3027   3268   3666     14     13    152       C  
ATOM   2454  C   ASN A 327     124.032  82.935   8.533  1.00 27.58           C  
ANISOU 2454  C   ASN A 327     3213   3441   3825     12     26    140       C  
ATOM   2455  O   ASN A 327     123.921  82.961   7.314  1.00 25.73           O  
ANISOU 2455  O   ASN A 327     2982   3207   3588     10     40    132       O  
ATOM   2456  CB  ASN A 327     124.983  84.124  10.655  1.00 25.63           C  
ANISOU 2456  CB  ASN A 327     2953   3200   3584     12    -10    157       C  
ATOM   2457  CG  ASN A 327     126.240  84.654  11.360  1.00 25.69           C  
ANISOU 2457  CG  ASN A 327     2945   3209   3605     12    -23    168       C  
ATOM   2458  OD1 ASN A 327     127.370  84.255  11.080  1.00 24.49           O  
ANISOU 2458  OD1 ASN A 327     2779   3052   3472     16    -17    177       O  
ATOM   2459  ND2 ASN A 327     126.019  85.551  12.325  1.00 26.21           N  
ANISOU 2459  ND2 ASN A 327     3014   3284   3661      7    -42    167       N  
ATOM   2460  N   ASP A 328     123.140  82.280   9.302  1.00 30.00           N  
ANISOU 2460  N   ASP A 328     3526   3748   4123     13     22    138       N  
ATOM   2461  CA  ASP A 328     122.013  81.520   8.692  1.00 28.53           C  
ANISOU 2461  CA  ASP A 328     3351   3562   3926     10     35    125       C  
ATOM   2462  C   ASP A 328     120.963  82.538   8.185  1.00 28.86           C  
ANISOU 2462  C   ASP A 328     3402   3616   3946      4     29    115       C  
ATOM   2463  O   ASP A 328     120.217  83.094   8.958  1.00 33.37           O  
ANISOU 2463  O   ASP A 328     3979   4195   4506      3     15    114       O  
ATOM   2464  CB  ASP A 328     121.365  80.608   9.733  1.00 27.56           C  
ANISOU 2464  CB  ASP A 328     3233   3437   3802     11     32    127       C  
ATOM   2465  CG  ASP A 328     122.150  79.313   9.983  1.00 28.61           C  
ANISOU 2465  CG  ASP A 328     3359   3556   3955     17     44    136       C  
ATOM   2466  OD1 ASP A 328     123.126  78.982   9.236  1.00 26.50           O  
ANISOU 2466  OD1 ASP A 328     3085   3281   3705     21     57    138       O  
ATOM   2467  OD2 ASP A 328     121.765  78.634  10.978  1.00 30.56           O  
ANISOU 2467  OD2 ASP A 328     3608   3800   4203     20     40    142       O  
ATOM   2468  N   ALA A 329     120.927  82.791   6.898  1.00 28.52           N  
ANISOU 2468  N   ALA A 329     3361   3576   3898      2     40    107       N  
ATOM   2469  CA  ALA A 329     120.124  83.880   6.341  1.00 27.35           C  
ANISOU 2469  CA  ALA A 329     3219   3440   3732     -2     35    102       C  
ATOM   2470  C   ALA A 329     119.586  83.432   5.014  1.00 25.93           C  
ANISOU 2470  C   ALA A 329     3045   3267   3542     -6     50     91       C  
ATOM   2471  O   ALA A 329     120.334  82.914   4.180  1.00 25.65           O  
ANISOU 2471  O   ALA A 329     3006   3225   3514     -6     65     89       O  
ATOM   2472  CB  ALA A 329     120.976  85.140   6.162  1.00 26.84           C  
ANISOU 2472  CB  ALA A 329     3149   3375   3673      0     29    110       C  
ATOM   2473  N   GLN A 330     118.277  83.573   4.831  1.00 24.09           N  
ANISOU 2473  N   GLN A 330     2819   3046   3290     -9     46     82       N  
ATOM   2474  CA  GLN A 330     117.662  83.302   3.536  1.00 24.07           C  
ANISOU 2474  CA  GLN A 330     2820   3053   3271    -15     57     71       C  
ATOM   2475  C   GLN A 330     117.702  84.545   2.692  1.00 23.82           C  
ANISOU 2475  C   GLN A 330     2789   3032   3230    -13     54     76       C  
ATOM   2476  O   GLN A 330     117.191  85.553   3.124  1.00 23.34           O  
ANISOU 2476  O   GLN A 330     2730   2977   3162    -10     41     81       O  
ATOM   2477  CB  GLN A 330     116.190  82.848   3.639  1.00 23.57           C  
ANISOU 2477  CB  GLN A 330     2762   3001   3192    -20     54     60       C  
ATOM   2478  CG  GLN A 330     115.682  82.409   2.288  1.00 24.23           C  
ANISOU 2478  CG  GLN A 330     2849   3097   3261    -28     66     47       C  
ATOM   2479  CD  GLN A 330     114.419  81.578   2.305  1.00 25.14           C  
ANISOU 2479  CD  GLN A 330     2967   3220   3364    -37     68     33       C  
ATOM   2480  OE1 GLN A 330     114.457  80.344   2.099  1.00 24.11           O  
ANISOU 2480  OE1 GLN A 330     2839   3082   3240    -43     82     21       O  
ATOM   2481  NE2 GLN A 330     113.286  82.249   2.466  1.00 25.17           N  
ANISOU 2481  NE2 GLN A 330     2972   3240   3353    -37     55     33       N  
ATOM   2482  N   LYS A 331     118.235  84.443   1.467  1.00 24.98           N  
ANISOU 2482  N   LYS A 331     2935   3181   3374    -16     68     73       N  
ATOM   2483  CA  LYS A 331     118.327  85.604   0.530  1.00 24.63           C  
ANISOU 2483  CA  LYS A 331     2892   3147   3319    -14     68     80       C  
ATOM   2484  C   LYS A 331     116.923  86.032   0.048  1.00 25.85           C  
ANISOU 2484  C   LYS A 331     3051   3321   3448    -16     61     75       C  
ATOM   2485  O   LYS A 331     116.011  85.178  -0.160  1.00 24.10           O  
ANISOU 2485  O   LYS A 331     2832   3110   3215    -22     63     63       O  
ATOM   2486  CB  LYS A 331     119.154  85.246  -0.677  1.00 25.60           C  
ANISOU 2486  CB  LYS A 331     3015   3269   3443    -16     86     77       C  
ATOM   2487  CG  LYS A 331     120.580  84.871  -0.259  1.00 26.91           C  
ANISOU 2487  CG  LYS A 331     3173   3416   3635    -13     94     83       C  
ATOM   2488  CD  LYS A 331     121.554  84.770  -1.412  1.00 26.61           C  
ANISOU 2488  CD  LYS A 331     3134   3377   3601    -14    113     83       C  
ATOM   2489  CE  LYS A 331     122.936  84.296  -0.942  1.00 26.00           C  
ANISOU 2489  CE  LYS A 331     3047   3280   3552    -10    121     89       C  
ATOM   2490  NZ  LYS A 331     123.773  84.153  -2.165  1.00 28.54           N  
ANISOU 2490  NZ  LYS A 331     3367   3601   3876    -11    142     87       N  
ATOM   2491  N   GLY A 332     116.738  87.337  -0.032  1.00 24.01           N  
ANISOU 2491  N   GLY A 332     2818   3094   3209    -10     52     87       N  
ATOM   2492  CA  GLY A 332     115.471  87.916  -0.392  1.00 25.29           C  
ANISOU 2492  CA  GLY A 332     2982   3274   3350     -9     44     87       C  
ATOM   2493  C   GLY A 332     114.689  88.457   0.791  1.00 26.15           C  
ANISOU 2493  C   GLY A 332     3092   3382   3462     -4     29     91       C  
ATOM   2494  O   GLY A 332     113.823  89.289   0.588  1.00 28.44           O  
ANISOU 2494  O   GLY A 332     3381   3684   3739      0     22     96       O  
ATOM   2495  N   MET A 333     115.006  88.085   2.045  1.00 25.50           N  
ANISOU 2495  N   MET A 333     3009   3286   3396     -4     24     89       N  
ATOM   2496  CA  MET A 333     114.425  88.763   3.157  1.00 23.24           C  
ANISOU 2496  CA  MET A 333     2722   2996   3110      0     12     93       C  
ATOM   2497  C   MET A 333     114.852  90.250   3.093  1.00 24.32           C  
ANISOU 2497  C   MET A 333     2860   3128   3253      7      8    106       C  
ATOM   2498  O   MET A 333     115.993  90.581   2.792  1.00 22.71           O  
ANISOU 2498  O   MET A 333     2654   2914   3060      7     13    112       O  
ATOM   2499  CB  MET A 333     114.766  88.120   4.494  1.00 24.46           C  
ANISOU 2499  CB  MET A 333     2876   3137   3279     -1      7     90       C  
ATOM   2500  CG  MET A 333     114.172  88.774   5.788  1.00 23.59           C  
ANISOU 2500  CG  MET A 333     2768   3025   3169      3     -5     92       C  
ATOM   2501  SD  MET A 333     112.346  89.039   5.818  1.00 25.45           S  
ANISOU 2501  SD  MET A 333     3005   3277   3386      5    -11     88       S  
ATOM   2502  CE  MET A 333     111.773  87.346   5.834  1.00 25.44           C  
ANISOU 2502  CE  MET A 333     3003   3282   3380     -4     -5     75       C  
ATOM   2503  N   SER A 334     113.885  91.135   3.329  1.00 24.96           N  
ANISOU 2503  N   SER A 334     2942   3215   3325     12      0    110       N  
ATOM   2504  CA  SER A 334     114.037  92.575   3.055  1.00 24.96           C  
ANISOU 2504  CA  SER A 334     2943   3211   3328     19     -1    122       C  
ATOM   2505  C   SER A 334     113.259  93.440   4.024  1.00 25.41           C  
ANISOU 2505  C   SER A 334     3002   3265   3386     25     -9    124       C  
ATOM   2506  O   SER A 334     112.440  92.973   4.831  1.00 24.39           O  
ANISOU 2506  O   SER A 334     2874   3140   3253     24    -15    116       O  
ATOM   2507  CB  SER A 334     113.525  92.901   1.637  1.00 25.81           C  
ANISOU 2507  CB  SER A 334     3051   3336   3419     22      5    128       C  
ATOM   2508  OG  SER A 334     112.087  92.957   1.584  1.00 24.44           O  
ANISOU 2508  OG  SER A 334     2877   3180   3230     26     -1    127       O  
ATOM   2509  N   TYR A 335     113.483  94.739   3.923  1.00 26.33           N  
ANISOU 2509  N   TYR A 335     3121   3373   3508     31     -9    134       N  
ATOM   2510  CA  TYR A 335     112.771  95.685   4.752  1.00 27.71           C  
ANISOU 2510  CA  TYR A 335     3299   3543   3686     37    -14    136       C  
ATOM   2511  C   TYR A 335     111.290  95.907   4.369  1.00 28.27           C  
ANISOU 2511  C   TYR A 335     3368   3631   3742     45    -16    139       C  
ATOM   2512  O   TYR A 335     110.619  96.691   4.938  1.00 30.01           O  
ANISOU 2512  O   TYR A 335     3590   3847   3964     52    -18    141       O  
ATOM   2513  CB  TYR A 335     113.568  96.957   5.049  1.00 28.19           C  
ANISOU 2513  CB  TYR A 335     3363   3585   3763     39    -12    143       C  
ATOM   2514  CG  TYR A 335     113.930  97.868   3.927  1.00 29.22           C  
ANISOU 2514  CG  TYR A 335     3494   3713   3896     44     -4    157       C  
ATOM   2515  CD1 TYR A 335     112.987  98.321   3.035  1.00 30.11           C  
ANISOU 2515  CD1 TYR A 335     3606   3840   3996     53     -1    168       C  
ATOM   2516  CD2 TYR A 335     115.230  98.344   3.816  1.00 30.62           C  
ANISOU 2516  CD2 TYR A 335     3671   3875   4089     39      1    162       C  
ATOM   2517  CE1 TYR A 335     113.329  99.200   2.042  1.00 31.75           C  
ANISOU 2517  CE1 TYR A 335     3814   4044   4205     59      7    183       C  
ATOM   2518  CE2 TYR A 335     115.583  99.230   2.843  1.00 30.83           C  
ANISOU 2518  CE2 TYR A 335     3698   3897   4118     43     10    176       C  
ATOM   2519  CZ  TYR A 335     114.637  99.651   1.955  1.00 31.00           C  
ANISOU 2519  CZ  TYR A 335     3720   3932   4126     53     13    187       C  
ATOM   2520  OH  TYR A 335     115.012 100.503   0.988  1.00 31.02           O  
ANISOU 2520  OH  TYR A 335     3725   3931   4132     58     23    204       O  
ATOM   2521  N   HIS A 336     110.812  95.148   3.413  1.00 28.25           N  
ANISOU 2521  N   HIS A 336     3362   3648   3725     44    -14    138       N  
ATOM   2522  CA  HIS A 336     109.430  95.163   3.032  1.00 27.99           C  
ANISOU 2522  CA  HIS A 336     3324   3634   3675     50    -17    140       C  
ATOM   2523  C   HIS A 336     108.684  94.151   3.898  1.00 27.06           C  
ANISOU 2523  C   HIS A 336     3205   3523   3554     44    -22    126       C  
ATOM   2524  O   HIS A 336     107.497  94.081   3.816  1.00 23.26           O  
ANISOU 2524  O   HIS A 336     2719   3057   3062     47    -26    125       O  
ATOM   2525  CB  HIS A 336     109.240  94.786   1.571  1.00 28.97           C  
ANISOU 2525  CB  HIS A 336     3445   3780   3783     48    -14    144       C  
ATOM   2526  CG  HIS A 336     109.703  95.820   0.613  1.00 33.13           C  
ANISOU 2526  CG  HIS A 336     3973   4305   4309     55     -9    161       C  
ATOM   2527  ND1 HIS A 336     108.875  96.785   0.099  1.00 35.77           N  
ANISOU 2527  ND1 HIS A 336     4305   4651   4637     68    -10    176       N  
ATOM   2528  CD2 HIS A 336     110.920  96.049   0.081  1.00 35.43           C  
ANISOU 2528  CD2 HIS A 336     4267   4585   4607     53     -1    167       C  
ATOM   2529  CE1 HIS A 336     109.561  97.562  -0.706  1.00 35.16           C  
ANISOU 2529  CE1 HIS A 336     4230   4569   4561     72     -3    191       C  
ATOM   2530  NE2 HIS A 336     110.805  97.141  -0.730  1.00 34.57           N  
ANISOU 2530  NE2 HIS A 336     4160   4481   4496     62      2    185       N  
ATOM   2531  N   SER A 337     109.394  93.386   4.723  1.00 25.55           N  
ANISOU 2531  N   SER A 337     3017   3319   3373     36    -23    116       N  
ATOM   2532  CA  SER A 337     108.744  92.363   5.545  1.00 25.23           C  
ANISOU 2532  CA  SER A 337     2975   3282   3329     30    -26    104       C  
ATOM   2533  C   SER A 337     107.837  93.000   6.606  1.00 25.60           C  
ANISOU 2533  C   SER A 337     3023   3328   3377     37    -30    104       C  
ATOM   2534  O   SER A 337     108.018  94.174   6.993  1.00 26.09           O  
ANISOU 2534  O   SER A 337     3088   3378   3446     44    -31    110       O  
ATOM   2535  CB  SER A 337     109.801  91.482   6.217  1.00 25.08           C  
ANISOU 2535  CB  SER A 337     2959   3250   3321     22    -24     97       C  
ATOM   2536  OG  SER A 337     110.333  92.107   7.366  1.00 26.05           O  
ANISOU 2536  OG  SER A 337     3086   3356   3455     24    -29     99       O  
ATOM   2537  N   ARG A 338     106.891  92.215   7.107  1.00 24.27           N  
ANISOU 2537  N   ARG A 338     2851   3168   3202     33    -32     95       N  
ATOM   2538  CA  ARG A 338     105.919  92.691   8.121  1.00 24.28           C  
ANISOU 2538  CA  ARG A 338     2853   3170   3204     39    -35     94       C  
ATOM   2539  C   ARG A 338     106.646  93.197   9.386  1.00 24.97           C  
ANISOU 2539  C   ARG A 338     2948   3237   3302     40    -36     92       C  
ATOM   2540  O   ARG A 338     106.238  94.209   9.996  1.00 24.77           O  
ANISOU 2540  O   ARG A 338     2925   3206   3280     47    -37     95       O  
ATOM   2541  CB  ARG A 338     104.875  91.603   8.428  1.00 23.50           C  
ANISOU 2541  CB  ARG A 338     2748   3084   3095     33    -35     84       C  
ATOM   2542  CG  ARG A 338     105.446  90.406   9.220  1.00 23.83           C  
ANISOU 2542  CG  ARG A 338     2795   3117   3142     23    -34     75       C  
ATOM   2543  CD  ARG A 338     104.377  89.335   9.443  1.00 23.29           C  
ANISOU 2543  CD  ARG A 338     2722   3061   3067     16    -32     67       C  
ATOM   2544  NE  ARG A 338     104.070  88.639   8.225  1.00 22.61           N  
ANISOU 2544  NE  ARG A 338     2628   2989   2971      9    -29     63       N  
ATOM   2545  CZ  ARG A 338     104.704  87.556   7.805  1.00 24.97           C  
ANISOU 2545  CZ  ARG A 338     2930   3286   3273     -1    -25     56       C  
ATOM   2546  NH1 ARG A 338     105.705  87.015   8.500  1.00 25.18           N  
ANISOU 2546  NH1 ARG A 338     2963   3294   3310     -4    -22     55       N  
ATOM   2547  NH2 ARG A 338     104.340  86.983   6.676  1.00 27.92           N  
ANISOU 2547  NH2 ARG A 338     3298   3674   3636     -8    -22     50       N  
ATOM   2548  N   GLU A 339     107.772  92.579   9.738  1.00 24.46           N  
ANISOU 2548  N   GLU A 339     2887   3162   3244     32    -37     89       N  
ATOM   2549  CA  GLU A 339     108.518  93.028  10.918  1.00 25.06           C  
ANISOU 2549  CA  GLU A 339     2970   3222   3330     31    -40     88       C  
ATOM   2550  C   GLU A 339     109.077  94.472  10.797  1.00 24.54           C  
ANISOU 2550  C   GLU A 339     2907   3144   3272     36    -40     94       C  
ATOM   2551  O   GLU A 339     109.114  95.211  11.779  1.00 24.48           O  
ANISOU 2551  O   GLU A 339     2905   3126   3269     37    -42     91       O  
ATOM   2552  CB  GLU A 339     109.681  92.048  11.286  1.00 27.42           C  
ANISOU 2552  CB  GLU A 339     3270   3514   3635     22    -42     85       C  
ATOM   2553  CG  GLU A 339     109.260  90.603  11.544  1.00 28.51           C  
ANISOU 2553  CG  GLU A 339     3406   3659   3768     16    -41     80       C  
ATOM   2554  CD  GLU A 339     109.314  89.713  10.301  1.00 31.61           C  
ANISOU 2554  CD  GLU A 339     3794   4059   4158     12    -35     79       C  
ATOM   2555  OE1 GLU A 339     109.147  90.219   9.142  1.00 31.36           O  
ANISOU 2555  OE1 GLU A 339     3759   4034   4122     15    -32     82       O  
ATOM   2556  OE2 GLU A 339     109.553  88.478  10.489  1.00 34.21           O  
ANISOU 2556  OE2 GLU A 339     4122   4386   4489      6    -32     75       O  
ATOM   2557  N   LEU A 340     109.543  94.831   9.623  1.00 24.13           N  
ANISOU 2557  N   LEU A 340     2853   3092   3223     38    -37    102       N  
ATOM   2558  CA  LEU A 340     110.148  96.132   9.380  1.00 24.92           C  
ANISOU 2558  CA  LEU A 340     2956   3179   3333     42    -34    109       C  
ATOM   2559  C   LEU A 340     109.081  97.191   9.154  1.00 24.44           C  
ANISOU 2559  C   LEU A 340     2896   3122   3270     54    -31    115       C  
ATOM   2560  O   LEU A 340     109.304  98.337   9.462  1.00 24.08           O  
ANISOU 2560  O   LEU A 340     2854   3061   3234     58    -28    118       O  
ATOM   2561  CB  LEU A 340     111.142  96.090   8.198  1.00 25.43           C  
ANISOU 2561  CB  LEU A 340     3017   3243   3401     40    -30    117       C  
ATOM   2562  CG  LEU A 340     112.595  95.782   8.541  1.00 26.14           C  
ANISOU 2562  CG  LEU A 340     3108   3321   3503     31    -32    114       C  
ATOM   2563  CD1 LEU A 340     113.175  96.830   9.486  1.00 24.86           C  
ANISOU 2563  CD1 LEU A 340     2950   3142   3353     29    -35    113       C  
ATOM   2564  CD2 LEU A 340     112.668  94.362   9.084  1.00 26.67           C  
ANISOU 2564  CD2 LEU A 340     3173   3394   3566     24    -36    106       C  
ATOM   2565  N   VAL A 341     107.906  96.806   8.654  1.00 25.49           N  
ANISOU 2565  N   VAL A 341     3022   3271   3390     59    -31    117       N  
ATOM   2566  CA  VAL A 341     106.756  97.732   8.643  1.00 25.58           C  
ANISOU 2566  CA  VAL A 341     3032   3287   3401     72    -28    123       C  
ATOM   2567  C   VAL A 341     106.481  98.183  10.055  1.00 27.15           C  
ANISOU 2567  C   VAL A 341     3237   3473   3605     73    -28    114       C  
ATOM   2568  O   VAL A 341     106.358  99.403  10.330  1.00 25.44           O  
ANISOU 2568  O   VAL A 341     3025   3244   3399     81    -23    118       O  
ATOM   2569  CB  VAL A 341     105.447  97.124   8.043  1.00 26.03           C  
ANISOU 2569  CB  VAL A 341     3079   3368   3442     76    -29    125       C  
ATOM   2570  CG1 VAL A 341     104.264  98.091   8.089  1.00 26.28           C  
ANISOU 2570  CG1 VAL A 341     3106   3403   3474     91    -27    132       C  
ATOM   2571  CG2 VAL A 341     105.630  96.790   6.599  1.00 25.29           C  
ANISOU 2571  CG2 VAL A 341     2980   3289   3340     75    -30    133       C  
ATOM   2572  N   THR A 342     106.391  97.175  10.948  1.00 28.14           N  
ANISOU 2572  N   THR A 342     3363   3603   3726     64    -32    102       N  
ATOM   2573  CA  THR A 342     106.198  97.352  12.358  1.00 28.06           C  
ANISOU 2573  CA  THR A 342     3360   3585   3718     63    -32     92       C  
ATOM   2574  C   THR A 342     107.308  98.170  13.035  1.00 28.43           C  
ANISOU 2574  C   THR A 342     3415   3610   3775     58    -33     89       C  
ATOM   2575  O   THR A 342     107.000  99.149  13.764  1.00 26.96           O  
ANISOU 2575  O   THR A 342     3235   3413   3594     63    -29     84       O  
ATOM   2576  CB  THR A 342     106.087  95.974  13.061  1.00 30.72           C  
ANISOU 2576  CB  THR A 342     3696   3930   4046     53    -37     83       C  
ATOM   2577  OG1 THR A 342     104.992  95.255  12.529  1.00 29.42           O  
ANISOU 2577  OG1 THR A 342     3523   3784   3872     55    -35     84       O  
ATOM   2578  CG2 THR A 342     105.869  96.146  14.540  1.00 31.21           C  
ANISOU 2578  CG2 THR A 342     3766   3986   4108     51    -37     74       C  
ATOM   2579  N   ALA A 343     108.575  97.802  12.774  1.00 26.60           N  
ANISOU 2579  N   ALA A 343     3184   3374   3548     49    -37     90       N  
ATOM   2580  CA  ALA A 343     109.708  98.487  13.415  1.00 26.94           C  
ANISOU 2580  CA  ALA A 343     3234   3401   3603     42    -39     85       C  
ATOM   2581  C   ALA A 343     109.827  99.953  13.007  1.00 25.41           C  
ANISOU 2581  C   ALA A 343     3044   3192   3421     49    -31     91       C  
ATOM   2582  O   ALA A 343     110.123 100.806  13.821  1.00 27.11           O  
ANISOU 2582  O   ALA A 343     3266   3392   3643     46    -30     83       O  
ATOM   2583  CB  ALA A 343     111.024  97.763  13.086  1.00 26.68           C  
ANISOU 2583  CB  ALA A 343     3198   3367   3574     33    -44     88       C  
ATOM   2584  N   VAL A 344     109.665 100.210  11.732  1.00 25.79           N  
ANISOU 2584  N   VAL A 344     3087   3243   3470     56    -26    103       N  
ATOM   2585  CA  VAL A 344     109.782 101.550  11.175  1.00 26.90           C  
ANISOU 2585  CA  VAL A 344     3230   3369   3623     64    -18    113       C  
ATOM   2586  C   VAL A 344     108.699 102.468  11.815  1.00 26.83           C  
ANISOU 2586  C   VAL A 344     3226   3353   3616     74    -11    110       C  
ATOM   2587  O   VAL A 344     109.005 103.585  12.287  1.00 27.60           O  
ANISOU 2587  O   VAL A 344     3331   3430   3726     74     -5    106       O  
ATOM   2588  CB  VAL A 344     109.754 101.466   9.631  1.00 27.60           C  
ANISOU 2588  CB  VAL A 344     3312   3467   3708     70    -14    129       C  
ATOM   2589  CG1 VAL A 344     109.532 102.803   8.951  1.00 29.39           C  
ANISOU 2589  CG1 VAL A 344     3539   3682   3944     82     -4    143       C  
ATOM   2590  CG2 VAL A 344     111.044 100.879   9.104  1.00 27.84           C  
ANISOU 2590  CG2 VAL A 344     3340   3498   3741     60    -17    130       C  
ATOM   2591  N   ASP A 345     107.472 101.971  11.892  1.00 26.07           N  
ANISOU 2591  N   ASP A 345     3125   3273   3508     82    -12    110       N  
ATOM   2592  CA  ASP A 345     106.349 102.802  12.340  1.00 27.11           C  
ANISOU 2592  CA  ASP A 345     3258   3399   3643     94     -4    109       C  
ATOM   2593  C   ASP A 345     106.431 103.086  13.848  1.00 27.77           C  
ANISOU 2593  C   ASP A 345     3352   3471   3729     87     -2     91       C  
ATOM   2594  O   ASP A 345     106.241 104.204  14.294  1.00 27.24           O  
ANISOU 2594  O   ASP A 345     3291   3385   3672     93      7     88       O  
ATOM   2595  CB  ASP A 345     105.015 102.152  11.979  1.00 27.60           C  
ANISOU 2595  CB  ASP A 345     3311   3485   3693    104     -5    114       C  
ATOM   2596  CG  ASP A 345     104.750 102.084  10.467  1.00 28.99           C  
ANISOU 2596  CG  ASP A 345     3476   3674   3864    112     -5    132       C  
ATOM   2597  OD1 ASP A 345     105.644 102.380   9.607  1.00 28.24           O  
ANISOU 2597  OD1 ASP A 345     3383   3574   3774    110     -5    142       O  
ATOM   2598  OD2 ASP A 345     103.614 101.667  10.110  1.00 30.53           O  
ANISOU 2598  OD2 ASP A 345     3662   3890   4049    120     -7    137       O  
ATOM   2599  N   ILE A 346     106.814 102.074  14.634  1.00 27.64           N  
ANISOU 2599  N   ILE A 346     3337   3462   3703     75    -12     80       N  
ATOM   2600  CA  ILE A 346     107.034 102.235  16.027  1.00 26.41           C  
ANISOU 2600  CA  ILE A 346     3191   3298   3546     66    -13     63       C  
ATOM   2601  C   ILE A 346     108.220 103.176  16.324  1.00 28.26           C  
ANISOU 2601  C   ILE A 346     3433   3511   3793     57    -12     57       C  
ATOM   2602  O   ILE A 346     108.113 103.989  17.249  1.00 27.45           O  
ANISOU 2602  O   ILE A 346     3340   3395   3695     55     -6     45       O  
ATOM   2603  CB  ILE A 346     107.195 100.856  16.707  1.00 26.74           C  
ANISOU 2603  CB  ILE A 346     3232   3356   3575     55    -23     56       C  
ATOM   2604  CG1 ILE A 346     105.825 100.128  16.723  1.00 27.15           C  
ANISOU 2604  CG1 ILE A 346     3277   3424   3615     63    -21     58       C  
ATOM   2605  CG2 ILE A 346     107.723 101.010  18.102  1.00 27.37           C  
ANISOU 2605  CG2 ILE A 346     3321   3428   3651     44    -27     41       C  
ATOM   2606  CD1 ILE A 346     105.818  98.692  17.198  1.00 27.33           C  
ANISOU 2606  CD1 ILE A 346     3297   3462   3624     55    -29     54       C  
ATOM   2607  N   ALA A 347     109.344 103.005  15.619  1.00 26.96           N  
ANISOU 2607  N   ALA A 347     3265   3344   3635     50    -17     64       N  
ATOM   2608  CA  ALA A 347     110.515 103.839  15.845  1.00 28.40           C  
ANISOU 2608  CA  ALA A 347     3453   3508   3831     39    -16     58       C  
ATOM   2609  C   ALA A 347     110.204 105.299  15.479  1.00 28.65           C  
ANISOU 2609  C   ALA A 347     3490   3519   3878     48     -2     62       C  
ATOM   2610  O   ALA A 347     110.665 106.177  16.150  1.00 28.90           O  
ANISOU 2610  O   ALA A 347     3529   3532   3919     41      3     51       O  
ATOM   2611  CB  ALA A 347     111.724 103.328  15.069  1.00 28.14           C  
ANISOU 2611  CB  ALA A 347     3412   3477   3801     31    -23     67       C  
ATOM   2612  N   TYR A 348     109.419 105.520  14.429  1.00 28.85           N  
ANISOU 2612  N   TYR A 348     3510   3547   3905     65      6     79       N  
ATOM   2613  CA  TYR A 348     109.036 106.877  14.048  1.00 30.38           C  
ANISOU 2613  CA  TYR A 348     3708   3721   4114     76     21     86       C  
ATOM   2614  C   TYR A 348     108.197 107.518  15.148  1.00 31.46           C  
ANISOU 2614  C   TYR A 348     3852   3847   4252     81     30     72       C  
ATOM   2615  O   TYR A 348     108.461 108.637  15.579  1.00 29.58           O  
ANISOU 2615  O   TYR A 348     3625   3585   4030     79     41     64       O  
ATOM   2616  CB  TYR A 348     108.220 106.929  12.752  1.00 29.72           C  
ANISOU 2616  CB  TYR A 348     3615   3647   4029     95     27    109       C  
ATOM   2617  CG  TYR A 348     107.961 108.346  12.347  1.00 29.05           C  
ANISOU 2617  CG  TYR A 348     3534   3540   3962    108     43    119       C  
ATOM   2618  CD1 TYR A 348     108.983 109.128  11.857  1.00 28.65           C  
ANISOU 2618  CD1 TYR A 348     3489   3470   3929    102     49    126       C  
ATOM   2619  CD2 TYR A 348     106.682 108.927  12.489  1.00 29.32           C  
ANISOU 2619  CD2 TYR A 348     3569   3572   4000    126     53    124       C  
ATOM   2620  CE1 TYR A 348     108.774 110.455  11.514  1.00 29.94           C  
ANISOU 2620  CE1 TYR A 348     3657   3610   4110    114     66    136       C  
ATOM   2621  CE2 TYR A 348     106.463 110.261  12.149  1.00 30.11           C  
ANISOU 2621  CE2 TYR A 348     3673   3649   4119    139     70    135       C  
ATOM   2622  CZ  TYR A 348     107.503 111.014  11.672  1.00 30.32           C  
ANISOU 2622  CZ  TYR A 348     3704   3654   4161    133     77    141       C  
ATOM   2623  OH  TYR A 348     107.275 112.321  11.313  1.00 32.11           O  
ANISOU 2623  OH  TYR A 348     3936   3856   4409    146     95    154       O  
ATOM   2624  N   HIS A 349     107.166 106.803  15.551  1.00 30.87           N  
ANISOU 2624  N   HIS A 349     3775   3791   4164     87     27     69       N  
ATOM   2625  CA  HIS A 349     106.230 107.307  16.567  1.00 33.09           C  
ANISOU 2625  CA  HIS A 349     4063   4065   4445     93     37     57       C  
ATOM   2626  C   HIS A 349     106.788 107.500  17.988  1.00 34.25           C  
ANISOU 2626  C   HIS A 349     4222   4201   4589     76     36     32       C  
ATOM   2627  O   HIS A 349     106.451 108.489  18.618  1.00 30.07           O  
ANISOU 2627  O   HIS A 349     3703   3654   4070     79     49     21       O  
ATOM   2628  CB  HIS A 349     104.993 106.398  16.620  1.00 33.53           C  
ANISOU 2628  CB  HIS A 349     4109   4144   4485    103     34     60       C  
ATOM   2629  CG  HIS A 349     103.857 106.948  17.426  1.00 34.79           C  
ANISOU 2629  CG  HIS A 349     4273   4298   4646    113     47     52       C  
ATOM   2630  ND1 HIS A 349     103.475 108.273  17.384  1.00 35.26           N  
ANISOU 2630  ND1 HIS A 349     4338   4336   4723    126     64     54       N  
ATOM   2631  CD2 HIS A 349     102.990 106.340  18.273  1.00 36.29           C  
ANISOU 2631  CD2 HIS A 349     4463   4502   4823    114     47     42       C  
ATOM   2632  CE1 HIS A 349     102.425 108.460  18.162  1.00 35.22           C  
ANISOU 2632  CE1 HIS A 349     4334   4331   4716    134     75     45       C  
ATOM   2633  NE2 HIS A 349     102.111 107.304  18.717  1.00 36.72           N  
ANISOU 2633  NE2 HIS A 349     4522   4544   4888    127     64     38       N  
ATOM   2634  N   TYR A 350     107.624 106.570  18.480  1.00 34.38           N  
ANISOU 2634  N   TYR A 350     4239   4231   4594     60     20     23       N  
ATOM   2635  CA  TYR A 350     108.101 106.600  19.860  1.00 35.93           C  
ANISOU 2635  CA  TYR A 350     4446   4424   4784     43     16      1       C  
ATOM   2636  C   TYR A 350     109.505 107.088  19.981  1.00 37.24           C  
ANISOU 2636  C   TYR A 350     4615   4576   4958     26     11     -6       C  
ATOM   2637  O   TYR A 350     109.984 107.207  21.090  1.00 41.02           O  
ANISOU 2637  O   TYR A 350     5102   5053   5431     11      6    -25       O  
ATOM   2638  CB  TYR A 350     107.988 105.206  20.544  1.00 37.11           C  
ANISOU 2638  CB  TYR A 350     4592   4599   4911     36      2     -3       C  
ATOM   2639  CG  TYR A 350     106.559 104.804  20.721  1.00 38.15           C  
ANISOU 2639  CG  TYR A 350     4720   4741   5032     50      9     -1       C  
ATOM   2640  CD1 TYR A 350     105.780 105.307  21.783  1.00 38.85           C  
ANISOU 2640  CD1 TYR A 350     4819   4825   5117     52     19    -16       C  
ATOM   2641  CD2 TYR A 350     105.922 104.017  19.767  1.00 38.26           C  
ANISOU 2641  CD2 TYR A 350     4723   4772   5044     61      6     16       C  
ATOM   2642  CE1 TYR A 350     104.422 104.984  21.887  1.00 37.20           C  
ANISOU 2642  CE1 TYR A 350     4605   4627   4901     66     27    -12       C  
ATOM   2643  CE2 TYR A 350     104.569 103.699  19.878  1.00 38.24           C  
ANISOU 2643  CE2 TYR A 350     4715   4780   5033     73     13     19       C  
ATOM   2644  CZ  TYR A 350     103.824 104.185  20.938  1.00 38.61           C  
ANISOU 2644  CZ  TYR A 350     4771   4823   5078     76     23      5       C  
ATOM   2645  OH  TYR A 350     102.468 103.834  21.026  1.00 40.31           O  
ANISOU 2645  OH  TYR A 350     4979   5050   5287     88     31      8       O  
ATOM   2646  N   GLY A 351     110.188 107.327  18.867  1.00 36.40           N  
ANISOU 2646  N   GLY A 351     4503   4462   4866     28     11      8       N  
ATOM   2647  CA  GLY A 351     111.569 107.750  18.891  1.00 36.59           C  
ANISOU 2647  CA  GLY A 351     4527   4474   4900     11      6      2       C  
ATOM   2648  C   GLY A 351     111.561 109.246  18.654  1.00 40.81           C  
ANISOU 2648  C   GLY A 351     5071   4980   5457     14     24      0       C  
ATOM   2649  O   GLY A 351     110.564 109.916  18.948  1.00 41.97           O  
ANISOU 2649  O   GLY A 351     5224   5116   5607     25     38     -4       O  
ATOM   2650  N   ASN A 352     112.615 109.793  18.074  1.00 40.81           N  
ANISOU 2650  N   ASN A 352     5069   4965   5473      5     26      5       N  
ATOM   2651  CA  ASN A 352     112.598 111.240  17.848  1.00 46.03           C  
ANISOU 2651  CA  ASN A 352     5738   5596   6157      8     45      3       C  
ATOM   2652  C   ASN A 352     111.920 111.717  16.542  1.00 44.82           C  
ANISOU 2652  C   ASN A 352     5580   5433   6015     31     59     29       C  
ATOM   2653  O   ASN A 352     112.129 112.851  16.126  1.00 42.20           O  
ANISOU 2653  O   ASN A 352     5254   5076   5705     33     75     34       O  
ATOM   2654  CB  ASN A 352     113.987 111.876  18.067  1.00 51.16           C  
ANISOU 2654  CB  ASN A 352     6390   6228   6821    -14     44     -8       C  
ATOM   2655  CG  ASN A 352     115.090 111.186  17.305  1.00 57.56           C  
ANISOU 2655  CG  ASN A 352     7188   7050   7632    -22     31      5       C  
ATOM   2656  OD1 ASN A 352     114.916 110.802  16.147  1.00 61.97           O  
ANISOU 2656  OD1 ASN A 352     7738   7616   8191     -9     32     28       O  
ATOM   2657  ND2 ASN A 352     116.238 110.990  17.966  1.00 63.66           N  
ANISOU 2657  ND2 ASN A 352     7958   7827   8403    -45     18    -10       N  
ATOM   2658  N   HIS A 353     111.076 110.878  15.923  1.00 42.11           N  
ANISOU 2658  N   HIS A 353     5229   5113   5659     47     54     46       N  
ATOM   2659  CA  HIS A 353     110.411 111.217  14.677  1.00 39.72           C  
ANISOU 2659  CA  HIS A 353     4921   4809   5363     68     65     71       C  
ATOM   2660  C   HIS A 353     111.406 111.477  13.539  1.00 38.04           C  
ANISOU 2660  C   HIS A 353     4703   4588   5162     65     67     88       C  
ATOM   2661  O   HIS A 353     111.316 112.475  12.799  1.00 35.72           O  
ANISOU 2661  O   HIS A 353     4412   4275   4886     76     82    103       O  
ATOM   2662  CB  HIS A 353     109.454 112.403  14.916  1.00 43.42           C  
ANISOU 2662  CB  HIS A 353     5397   5254   5845     83     85     71       C  
ATOM   2663  CG  HIS A 353     108.683 112.261  16.192  1.00 48.36           C  
ANISOU 2663  CG  HIS A 353     6029   5883   6461     83     86     50       C  
ATOM   2664  ND1 HIS A 353     107.754 111.261  16.390  1.00 49.65           N  
ANISOU 2664  ND1 HIS A 353     6186   6074   6605     91     77     51       N  
ATOM   2665  CD2 HIS A 353     108.754 112.943  17.363  1.00 50.87           C  
ANISOU 2665  CD2 HIS A 353     6360   6183   6785     72     94     25       C  
ATOM   2666  CE1 HIS A 353     107.272 111.342  17.616  1.00 48.15           C  
ANISOU 2666  CE1 HIS A 353     6004   5881   6409     87     81     30       C  
ATOM   2667  NE2 HIS A 353     107.845 112.367  18.220  1.00 51.36           N  
ANISOU 2667  NE2 HIS A 353     6423   6261   6830     76     91     14       N  
ATOM   2668  N   ASN A 354     112.333 110.541  13.373  1.00 34.81           N  
ANISOU 2668  N   ASN A 354     4287   4195   4744     51     51     87       N  
ATOM   2669  CA  ASN A 354     113.311 110.621  12.325  1.00 33.63           C  
ANISOU 2669  CA  ASN A 354     4132   4042   4604     47     52    102       C  
ATOM   2670  C   ASN A 354     112.647 110.596  10.952  1.00 34.46           C  
ANISOU 2670  C   ASN A 354     4231   4156   4706     67     59    129       C  
ATOM   2671  O   ASN A 354     112.084 109.565  10.548  1.00 34.29           O  
ANISOU 2671  O   ASN A 354     4202   4161   4666     75     49    137       O  
ATOM   2672  CB  ASN A 354     114.289 109.479  12.440  1.00 34.64           C  
ANISOU 2672  CB  ASN A 354     4252   4188   4721     31     35     96       C  
ATOM   2673  CG  ASN A 354     115.362 109.523  11.392  1.00 35.42           C  
ANISOU 2673  CG  ASN A 354     4345   4283   4830     26     37    110       C  
ATOM   2674  OD1 ASN A 354     115.356 110.348  10.471  1.00 34.71           O  
ANISOU 2674  OD1 ASN A 354     4256   4180   4753     35     51    127       O  
ATOM   2675  ND2 ASN A 354     116.259 108.580  11.485  1.00 37.42           N  
ANISOU 2675  ND2 ASN A 354     4590   4550   5077     13     24    106       N  
ATOM   2676  N   PRO A 355     112.732 111.731  10.214  1.00 33.12           N  
ANISOU 2676  N   PRO A 355     4065   3965   4555     75     75    145       N  
ATOM   2677  CA  PRO A 355     112.039 111.800   8.930  1.00 32.60           C  
ANISOU 2677  CA  PRO A 355     3993   3910   4485     96     81    173       C  
ATOM   2678  C   PRO A 355     112.593 110.884   7.848  1.00 31.70           C  
ANISOU 2678  C   PRO A 355     3870   3818   4358     93     72    187       C  
ATOM   2679  O   PRO A 355     111.867 110.625   6.872  1.00 27.92           O  
ANISOU 2679  O   PRO A 355     3385   3357   3867    109     73    206       O  
ATOM   2680  CB  PRO A 355     112.212 113.285   8.501  1.00 33.66           C  
ANISOU 2680  CB  PRO A 355     4135   4012   4644    103    102    186       C  
ATOM   2681  CG  PRO A 355     113.413 113.761   9.282  1.00 34.09           C  
ANISOU 2681  CG  PRO A 355     4196   4042   4715     80    104    166       C  
ATOM   2682  CD  PRO A 355     113.410 113.008  10.565  1.00 32.73           C  
ANISOU 2682  CD  PRO A 355     4024   3881   4530     66     89    138       C  
ATOM   2683  N   GLN A 356     113.837 110.386   8.022  1.00 29.66           N  
ANISOU 2683  N   GLN A 356     3609   3559   4101     74     65    176       N  
ATOM   2684  CA  GLN A 356     114.373 109.386   7.119  1.00 29.95           C  
ANISOU 2684  CA  GLN A 356     3637   3618   4125     70     57    185       C  
ATOM   2685  C   GLN A 356     113.567 108.065   7.111  1.00 30.25           C  
ANISOU 2685  C   GLN A 356     3669   3687   4139     75     43    182       C  
ATOM   2686  O   GLN A 356     113.555 107.351   6.111  1.00 30.15           O  
ANISOU 2686  O   GLN A 356     3649   3694   4112     79     40    194       O  
ATOM   2687  CB  GLN A 356     115.836 109.136   7.387  1.00 30.52           C  
ANISOU 2687  CB  GLN A 356     3707   3684   4207     50     52    175       C  
ATOM   2688  CG  GLN A 356     116.723 110.340   7.051  1.00 31.50           C  
ANISOU 2688  CG  GLN A 356     3835   3780   4354     44     67    182       C  
ATOM   2689  CD  GLN A 356     118.208 110.043   7.168  1.00 33.49           C  
ANISOU 2689  CD  GLN A 356     4080   4028   4615     24     63    174       C  
ATOM   2690  OE1 GLN A 356     118.616 108.905   7.129  1.00 35.28           O  
ANISOU 2690  OE1 GLN A 356     4299   4274   4830     18     51    170       O  
ATOM   2691  NE2 GLN A 356     119.019 111.079   7.290  1.00 35.10           N  
ANISOU 2691  NE2 GLN A 356     4287   4206   4842     13     73    172       N  
ATOM   2692  N   LEU A 357     112.911 107.744   8.224  1.00 29.91           N  
ANISOU 2692  N   LEU A 357     3628   3648   4089     75     36    166       N  
ATOM   2693  CA  LEU A 357     112.095 106.520   8.319  1.00 30.21           C  
ANISOU 2693  CA  LEU A 357     3661   3713   4106     78     25    162       C  
ATOM   2694  C   LEU A 357     110.835 106.589   7.463  1.00 30.27           C  
ANISOU 2694  C   LEU A 357     3664   3736   4103     97     29    179       C  
ATOM   2695  O   LEU A 357     110.300 105.573   7.032  1.00 31.00           O  
ANISOU 2695  O   LEU A 357     3749   3853   4177    100     21    181       O  
ATOM   2696  CB  LEU A 357     111.715 106.249   9.752  1.00 29.25           C  
ANISOU 2696  CB  LEU A 357     3543   3590   3980     72     18    141       C  
ATOM   2697  CG  LEU A 357     112.860 105.942  10.713  1.00 30.80           C  
ANISOU 2697  CG  LEU A 357     3742   3780   4182     53     10    123       C  
ATOM   2698  CD1 LEU A 357     112.306 105.894  12.146  1.00 30.71           C  
ANISOU 2698  CD1 LEU A 357     3736   3767   4165     50      6    104       C  
ATOM   2699  CD2 LEU A 357     113.562 104.655  10.352  1.00 31.13           C  
ANISOU 2699  CD2 LEU A 357     3775   3838   4214     45      0    124       C  
ATOM   2700  N   LEU A 358     110.360 107.803   7.229  1.00 30.67           N  
ANISOU 2700  N   LEU A 358     3717   3770   4165    110     41    191       N  
ATOM   2701  CA  LEU A 358     109.203 108.029   6.377  1.00 31.84           C  
ANISOU 2701  CA  LEU A 358     3861   3933   4306    130     45    211       C  
ATOM   2702  C   LEU A 358     109.448 107.635   4.936  1.00 31.39           C  
ANISOU 2702  C   LEU A 358     3797   3894   4237    133     43    230       C  
ATOM   2703  O   LEU A 358     108.515 107.183   4.275  1.00 31.74           O  
ANISOU 2703  O   LEU A 358     3833   3963   4264    144     39    240       O  
ATOM   2704  CB  LEU A 358     108.769 109.497   6.433  1.00 31.98           C  
ANISOU 2704  CB  LEU A 358     3884   3926   4342    145     61    222       C  
ATOM   2705  CG  LEU A 358     108.383 110.026   7.809  1.00 31.96           C  
ANISOU 2705  CG  LEU A 358     3889   3904   4351    144     65    203       C  
ATOM   2706  CD1 LEU A 358     108.038 111.517   7.757  1.00 33.28           C  
ANISOU 2706  CD1 LEU A 358     4062   4043   4539    158     84    215       C  
ATOM   2707  CD2 LEU A 358     107.241 109.189   8.393  1.00 32.64           C  
ANISOU 2707  CD2 LEU A 358     3969   4013   4420    149     56    193       C  
ATOM   2708  N   SER A 359     110.674 107.801   4.437  1.00 31.13           N  
ANISOU 2708  N   SER A 359     3766   3850   4212    123     48    234       N  
ATOM   2709  CA  SER A 359     110.974 107.345   3.070  1.00 30.89           C  
ANISOU 2709  CA  SER A 359     3730   3839   4168    125     47    250       C  
ATOM   2710  C   SER A 359     110.949 105.812   2.953  1.00 30.28           C  
ANISOU 2710  C   SER A 359     3646   3789   4070    115     34    238       C  
ATOM   2711  O   SER A 359     110.584 105.291   1.919  1.00 32.10           O  
ANISOU 2711  O   SER A 359     3871   4043   4282    120     32    249       O  
ATOM   2712  CB  SER A 359     112.321 107.879   2.562  1.00 30.84           C  
ANISOU 2712  CB  SER A 359     3728   3815   4177    116     57    257       C  
ATOM   2713  OG  SER A 359     113.369 107.344   3.347  1.00 31.76           O  
ANISOU 2713  OG  SER A 359     3845   3922   4299     97     51    237       O  
ATOM   2714  N   ILE A 360     111.340 105.105   4.002  1.00 28.65           N  
ANISOU 2714  N   ILE A 360     3442   3579   3866    102     26    216       N  
ATOM   2715  CA  ILE A 360     111.255 103.664   4.013  1.00 28.68           C  
ANISOU 2715  CA  ILE A 360     3439   3604   3852     94     16    204       C  
ATOM   2716  C   ILE A 360     109.779 103.285   4.042  1.00 28.40           C  
ANISOU 2716  C   ILE A 360     3400   3590   3802    104     10    205       C  
ATOM   2717  O   ILE A 360     109.356 102.409   3.315  1.00 28.11           O  
ANISOU 2717  O   ILE A 360     3357   3578   3748    104      5    207       O  
ATOM   2718  CB  ILE A 360     112.003 103.054   5.241  1.00 28.94           C  
ANISOU 2718  CB  ILE A 360     3475   3628   3893     79      9    183       C  
ATOM   2719  CG1 ILE A 360     113.471 103.525   5.271  1.00 29.38           C  
ANISOU 2719  CG1 ILE A 360     3534   3664   3967     68     14    183       C  
ATOM   2720  CG2 ILE A 360     111.862 101.506   5.266  1.00 27.18           C  
ANISOU 2720  CG2 ILE A 360     3247   3426   3655     71      0    173       C  
ATOM   2721  CD1 ILE A 360     114.338 102.997   4.127  1.00 29.02           C  
ANISOU 2721  CD1 ILE A 360     3483   3626   3917     63     17    192       C  
ATOM   2722  N   ALA A 361     108.990 103.936   4.891  1.00 29.85           N  
ANISOU 2722  N   ALA A 361     3585   3764   3992    112     11    202       N  
ATOM   2723  CA  ALA A 361     107.550 103.678   4.922  1.00 29.29           C  
ANISOU 2723  CA  ALA A 361     3507   3712   3908    123      7    204       C  
ATOM   2724  C   ALA A 361     106.879 103.894   3.567  1.00 30.53           C  
ANISOU 2724  C   ALA A 361     3657   3889   4053    136      9    225       C  
ATOM   2725  O   ALA A 361     106.029 103.080   3.149  1.00 28.38           O  
ANISOU 2725  O   ALA A 361     3376   3645   3763    137      1    225       O  
ATOM   2726  CB  ALA A 361     106.848 104.456   6.022  1.00 30.45           C  
ANISOU 2726  CB  ALA A 361     3658   3844   4067    131     12    198       C  
ATOM   2727  N   GLU A 362     107.332 104.910   2.823  1.00 33.25           N  
ANISOU 2727  N   GLU A 362     4004   4222   4407    144     18    244       N  
ATOM   2728  CA  GLU A 362     106.843 105.105   1.438  1.00 35.45           C  
ANISOU 2728  CA  GLU A 362     4276   4522   4671    156     19    267       C  
ATOM   2729  C   GLU A 362     107.201 103.978   0.459  1.00 33.49           C  
ANISOU 2729  C   GLU A 362     4023   4300   4402    145     13    265       C  
ATOM   2730  O   GLU A 362     106.363 103.613  -0.372  1.00 32.51           O  
ANISOU 2730  O   GLU A 362     3891   4205   4258    151      7    275       O  
ATOM   2731  CB  GLU A 362     107.298 106.443   0.848  1.00 37.06           C  
ANISOU 2731  CB  GLU A 362     4485   4707   4890    166     32    290       C  
ATOM   2732  CG  GLU A 362     106.665 107.635   1.513  1.00 38.52           C  
ANISOU 2732  CG  GLU A 362     4672   4869   5093    181     41    297       C  
ATOM   2733  CD  GLU A 362     107.270 108.951   0.988  1.00 42.93           C  
ANISOU 2733  CD  GLU A 362     5238   5404   5670    190     56    318       C  
ATOM   2734  OE1 GLU A 362     108.481 109.231   1.177  1.00 42.95           O  
ANISOU 2734  OE1 GLU A 362     5249   5383   5688    177     63    312       O  
ATOM   2735  OE2 GLU A 362     106.518 109.717   0.368  1.00 45.59           O  
ANISOU 2735  OE2 GLU A 362     5570   5744   6007    210     62    343       O  
ATOM   2736  N   GLU A 363     108.415 103.450   0.540  1.00 32.27           N  
ANISOU 2736  N   GLU A 363     3874   4135   4252    129     14    254       N  
ATOM   2737  CA  GLU A 363     108.793 102.255  -0.230  1.00 32.68           C  
ANISOU 2737  CA  GLU A 363     3922   4208   4285    118     10    247       C  
ATOM   2738  C   GLU A 363     107.973 101.036   0.171  1.00 30.47           C  
ANISOU 2738  C   GLU A 363     3636   3949   3991    112     -1    230       C  
ATOM   2739  O   GLU A 363     107.609 100.243  -0.654  1.00 30.97           O  
ANISOU 2739  O   GLU A 363     3694   4038   4034    108     -5    229       O  
ATOM   2740  CB  GLU A 363     110.277 101.931  -0.037  1.00 35.72           C  
ANISOU 2740  CB  GLU A 363     4313   4576   4682    103     14    237       C  
ATOM   2741  CG  GLU A 363     111.192 102.943  -0.716  1.00 43.28           C  
ANISOU 2741  CG  GLU A 363     5276   5518   5652    106     26    255       C  
ATOM   2742  CD  GLU A 363     112.689 102.736  -0.431  1.00 49.29           C  
ANISOU 2742  CD  GLU A 363     6040   6259   6428     92     30    245       C  
ATOM   2743  OE1 GLU A 363     113.072 101.722   0.168  1.00 52.48           O  
ANISOU 2743  OE1 GLU A 363     6444   6665   6833     81     24    227       O  
ATOM   2744  OE2 GLU A 363     113.501 103.604  -0.805  1.00 57.21           O  
ANISOU 2744  OE2 GLU A 363     7047   7246   7444     93     41    257       O  
ATOM   2745  N   GLN A 364     107.730 100.859   1.453  1.00 29.85           N  
ANISOU 2745  N   GLN A 364     3560   3859   3923    109     -5    215       N  
ATOM   2746  CA  GLN A 364     106.925  99.719   1.916  1.00 30.28           C  
ANISOU 2746  CA  GLN A 364     3609   3931   3965    102    -13    199       C  
ATOM   2747  C   GLN A 364     105.479  99.835   1.398  1.00 30.81           C  
ANISOU 2747  C   GLN A 364     3666   4023   4018    114    -18    208       C  
ATOM   2748  O   GLN A 364     104.875  98.850   1.044  1.00 31.12           O  
ANISOU 2748  O   GLN A 364     3697   4086   4040    108    -24    201       O  
ATOM   2749  CB  GLN A 364     106.935  99.623   3.431  1.00 28.45           C  
ANISOU 2749  CB  GLN A 364     3382   3681   3747     98    -15    183       C  
ATOM   2750  CG  GLN A 364     108.286  99.315   4.032  1.00 27.73           C  
ANISOU 2750  CG  GLN A 364     3298   3570   3668     86    -14    172       C  
ATOM   2751  CD  GLN A 364     108.332  99.537   5.536  1.00 27.42           C  
ANISOU 2751  CD  GLN A 364     3264   3513   3642     83    -16    160       C  
ATOM   2752  OE1 GLN A 364     107.621 100.405   6.082  1.00 27.11           O  
ANISOU 2752  OE1 GLN A 364     3227   3466   3608     93    -13    163       O  
ATOM   2753  NE2 GLN A 364     109.221  98.806   6.217  1.00 27.20           N  
ANISOU 2753  NE2 GLN A 364     3239   3476   3619     71    -19    148       N  
ATOM   2754  N   GLY A 365     104.934 101.041   1.365  1.00 30.43           N  
ANISOU 2754  N   GLY A 365     3617   3970   3977    130    -14    225       N  
ATOM   2755  CA  GLY A 365     103.598 101.246   0.754  1.00 30.98           C  
ANISOU 2755  CA  GLY A 365     3674   4065   4032    143    -18    239       C  
ATOM   2756  C   GLY A 365     102.464 100.785   1.681  1.00 31.56           C  
ANISOU 2756  C   GLY A 365     3740   4147   4105    144    -24    226       C  
ATOM   2757  O   GLY A 365     101.339 100.660   1.270  1.00 29.59           O  
ANISOU 2757  O   GLY A 365     3478   3923   3843    151    -29    233       O  
ATOM   2758  N   GLN A 366     102.773 100.566   2.956  1.00 31.44           N  
ANISOU 2758  N   GLN A 366     3733   4111   4103    137    -22    209       N  
ATOM   2759  CA  GLN A 366     101.781 100.228   3.939  1.00 31.01           C  
ANISOU 2759  CA  GLN A 366     3672   4060   4048    138    -25    197       C  
ATOM   2760  C   GLN A 366     102.274 100.665   5.304  1.00 30.39           C  
ANISOU 2760  C   GLN A 366     3606   3952   3989    136    -19    186       C  
ATOM   2761  O   GLN A 366     103.497 100.880   5.523  1.00 27.92           O  
ANISOU 2761  O   GLN A 366     3304   3618   3686    129    -16    183       O  
ATOM   2762  CB  GLN A 366     101.482  98.711   3.947  1.00 31.75           C  
ANISOU 2762  CB  GLN A 366     3760   4175   4127    122    -32    180       C  
ATOM   2763  CG  GLN A 366     102.683  97.830   4.194  1.00 33.09           C  
ANISOU 2763  CG  GLN A 366     3940   4333   4299    104    -32    166       C  
ATOM   2764  CD  GLN A 366     102.360  96.323   4.043  1.00 35.85           C  
ANISOU 2764  CD  GLN A 366     4284   4702   4635     90    -38    150       C  
ATOM   2765  OE1 GLN A 366     101.228  95.905   4.178  1.00 42.01           O  
ANISOU 2765  OE1 GLN A 366     5055   5500   5407     90    -41    146       O  
ATOM   2766  NE2 GLN A 366     103.350  95.537   3.751  1.00 33.96           N  
ANISOU 2766  NE2 GLN A 366     4051   4459   4394     77    -37    142       N  
ATOM   2767  N   VAL A 367     101.303 100.757   6.206  1.00 27.83           N  
ANISOU 2767  N   VAL A 367     3278   3628   3668    142    -18    180       N  
ATOM   2768  CA  VAL A 367     101.517 101.102   7.588  1.00 28.36           C  
ANISOU 2768  CA  VAL A 367     3355   3671   3748    140    -13    168       C  
ATOM   2769  C   VAL A 367     100.690 100.225   8.526  1.00 29.03           C  
ANISOU 2769  C   VAL A 367     3436   3766   3826    134    -16    152       C  
ATOM   2770  O   VAL A 367      99.689  99.638   8.122  1.00 28.12           O  
ANISOU 2770  O   VAL A 367     3308   3676   3701    136    -20    154       O  
ATOM   2771  CB  VAL A 367     101.197 102.589   7.872  1.00 27.67           C  
ANISOU 2771  CB  VAL A 367     3271   3565   3677    157     -3    178       C  
ATOM   2772  CG1 VAL A 367     102.212 103.478   7.171  1.00 28.25           C  
ANISOU 2772  CG1 VAL A 367     3352   3621   3760    160      3    191       C  
ATOM   2773  CG2 VAL A 367      99.786 102.960   7.457  1.00 28.02           C  
ANISOU 2773  CG2 VAL A 367     3302   3628   3718    175     -1    192       C  
ATOM   2774  N   LEU A 368     101.120 100.164   9.787  1.00 29.81           N  
ANISOU 2774  N   LEU A 368     3547   3849   3933    126    -14    137       N  
ATOM   2775  CA  LEU A 368     100.335  99.569  10.857  1.00 29.91           C  
ANISOU 2775  CA  LEU A 368     3557   3866   3941    123    -13    124       C  
ATOM   2776  C   LEU A 368      99.019 100.340  11.015  1.00 29.74           C  
ANISOU 2776  C   LEU A 368     3527   3849   3923    140     -6    131       C  
ATOM   2777  O   LEU A 368      98.948 101.581  10.822  1.00 28.04           O  
ANISOU 2777  O   LEU A 368     3313   3620   3719    154      1    142       O  
ATOM   2778  CB  LEU A 368     101.057  99.628  12.181  1.00 30.91           C  
ANISOU 2778  CB  LEU A 368     3698   3972   4074    114    -11    110       C  
ATOM   2779  CG  LEU A 368     102.371  98.832  12.271  1.00 32.30           C  
ANISOU 2779  CG  LEU A 368     3881   4143   4248     98    -18    103       C  
ATOM   2780  CD1 LEU A 368     102.994  99.161  13.618  1.00 32.95           C  
ANISOU 2780  CD1 LEU A 368     3977   4206   4336     92    -16     90       C  
ATOM   2781  CD2 LEU A 368     102.113  97.323  12.092  1.00 31.33           C  
ANISOU 2781  CD2 LEU A 368     3751   4039   4112     87    -24     97       C  
ATOM   2782  N   LEU A 369      97.980  99.588  11.309  1.00 28.05           N  
ANISOU 2782  N   LEU A 369     3303   3654   3701    139     -8    126       N  
ATOM   2783  CA  LEU A 369      96.647 100.152  11.456  1.00 30.90           C  
ANISOU 2783  CA  LEU A 369     3652   4023   4065    154     -2    132       C  
ATOM   2784  C   LEU A 369      96.466 100.520  12.905  1.00 31.27           C  
ANISOU 2784  C   LEU A 369     3709   4052   4120    155      8    120       C  
ATOM   2785  O   LEU A 369      95.694  99.903  13.619  1.00 32.77           O  
ANISOU 2785  O   LEU A 369     3895   4252   4305    152     10    110       O  
ATOM   2786  CB  LEU A 369      95.608  99.167  10.962  1.00 29.60           C  
ANISOU 2786  CB  LEU A 369     3470   3888   3888    151     -8    133       C  
ATOM   2787  CG  LEU A 369      95.620  98.920   9.463  1.00 30.33           C  
ANISOU 2787  CG  LEU A 369     3550   4002   3970    151    -17    146       C  
ATOM   2788  CD1 LEU A 369      94.584  97.869   9.071  1.00 31.20           C  
ANISOU 2788  CD1 LEU A 369     3643   4143   4068    144    -24    143       C  
ATOM   2789  CD2 LEU A 369      95.323 100.191   8.686  1.00 31.51           C  
ANISOU 2789  CD2 LEU A 369     3694   4151   4127    172    -14    168       C  
ATOM   2790  N   ASP A 370      97.250 101.500  13.347  1.00 30.66           N  
ANISOU 2790  N   ASP A 370     3646   3948   4054    158     15    118       N  
ATOM   2791  CA  ASP A 370      97.289 101.876  14.738  1.00 30.47           C  
ANISOU 2791  CA  ASP A 370     3636   3907   4036    156     24    103       C  
ATOM   2792  C   ASP A 370      97.923 103.278  14.904  1.00 29.01           C  
ANISOU 2792  C   ASP A 370     3463   3693   3866    164     33    104       C  
ATOM   2793  O   ASP A 370      98.189 103.947  13.903  1.00 29.82           O  
ANISOU 2793  O   ASP A 370     3563   3791   3977    173     34    119       O  
ATOM   2794  CB  ASP A 370      97.959 100.768  15.597  1.00 31.60           C  
ANISOU 2794  CB  ASP A 370     3788   4050   4168    136     17     86       C  
ATOM   2795  CG  ASP A 370      99.463 100.669  15.380  1.00 34.08           C  
ANISOU 2795  CG  ASP A 370     4113   4353   4484    124      9     84       C  
ATOM   2796  OD1 ASP A 370     100.092 101.615  14.786  1.00 35.46           O  
ANISOU 2796  OD1 ASP A 370     4292   4513   4669    129     11     92       O  
ATOM   2797  OD2 ASP A 370      99.999  99.620  15.807  1.00 33.07           O  
ANISOU 2797  OD2 ASP A 370     3989   4230   4347    109      1     75       O  
ATOM   2798  N   ASP A 371      98.118 103.717  16.150  1.00 28.08           N  
ANISOU 2798  N   ASP A 371     3360   3557   3753    160     42     88       N  
ATOM   2799  CA  ASP A 371      98.605 105.083  16.459  1.00 29.76           C  
ANISOU 2799  CA  ASP A 371     3585   3741   3982    166     54     85       C  
ATOM   2800  C   ASP A 371      99.906 105.361  15.754  1.00 30.35           C  
ANISOU 2800  C   ASP A 371     3666   3804   4063    158     47     91       C  
ATOM   2801  O   ASP A 371     100.105 106.442  15.218  1.00 31.17           O  
ANISOU 2801  O   ASP A 371     3772   3891   4182    168     56    102       O  
ATOM   2802  CB  ASP A 371      98.868 105.316  17.959  1.00 31.53           C  
ANISOU 2802  CB  ASP A 371     3825   3950   4206    156     60     63       C  
ATOM   2803  CG  ASP A 371      97.705 104.950  18.870  1.00 32.22           C  
ANISOU 2803  CG  ASP A 371     3910   4048   4286    160     68     53       C  
ATOM   2804  OD1 ASP A 371      96.930 103.968  18.609  1.00 32.40           O  
ANISOU 2804  OD1 ASP A 371     3919   4095   4298    161     62     59       O  
ATOM   2805  OD2 ASP A 371      97.618 105.639  19.911  1.00 32.62           O  
ANISOU 2805  OD2 ASP A 371     3972   4082   4340    160     80     39       O  
ATOM   2806  N   SER A 372     100.816 104.385  15.752  1.00 29.79           N  
ANISOU 2806  N   SER A 372     3597   3741   3981    141     34     85       N  
ATOM   2807  CA  SER A 372     102.117 104.610  15.146  1.00 30.47           C  
ANISOU 2807  CA  SER A 372     3689   3817   4073    132     28     90       C  
ATOM   2808  C   SER A 372     102.007 104.734  13.604  1.00 30.29           C  
ANISOU 2808  C   SER A 372     3654   3802   4052    143     27    112       C  
ATOM   2809  O   SER A 372     102.673 105.572  12.973  1.00 32.08           O  
ANISOU 2809  O   SER A 372     3885   4014   4291    146     31    122       O  
ATOM   2810  CB  SER A 372     103.098 103.538  15.611  1.00 31.63           C  
ANISOU 2810  CB  SER A 372     3840   3969   4209    112     15     78       C  
ATOM   2811  OG  SER A 372     102.798 102.335  14.912  1.00 36.15           O  
ANISOU 2811  OG  SER A 372     4400   4565   4769    111      6     85       O  
ATOM   2812  N   GLY A 373     101.149 103.924  12.989  1.00 29.84           N  
ANISOU 2812  N   GLY A 373     3583   3771   3983    148     21    121       N  
ATOM   2813  CA  GLY A 373     100.944 103.968  11.554  1.00 28.41           C  
ANISOU 2813  CA  GLY A 373     3391   3604   3800    157     18    141       C  
ATOM   2814  C   GLY A 373     100.255 105.254  11.108  1.00 29.94           C  
ANISOU 2814  C   GLY A 373     3581   3788   4006    179     30    158       C  
ATOM   2815  O   GLY A 373     100.558 105.778  10.027  1.00 30.25           O  
ANISOU 2815  O   GLY A 373     3617   3826   4049    186     31    176       O  
ATOM   2816  N   LEU A 374      99.356 105.769  11.955  1.00 30.05           N  
ANISOU 2816  N   LEU A 374     3595   3795   4027    189     40    152       N  
ATOM   2817  CA  LEU A 374      98.741 107.077  11.751  1.00 30.84           C  
ANISOU 2817  CA  LEU A 374     3693   3881   4144    210     54    167       C  
ATOM   2818  C   LEU A 374      99.809 108.185  11.766  1.00 30.73           C  
ANISOU 2818  C   LEU A 374     3694   3833   4147    209     64    167       C  
ATOM   2819  O   LEU A 374      99.761 109.088  10.904  1.00 34.56           O  
ANISOU 2819  O   LEU A 374     4177   4310   4644    224     72    189       O  
ATOM   2820  CB  LEU A 374      97.679 107.423  12.810  1.00 29.64           C  
ANISOU 2820  CB  LEU A 374     3540   3723   3998    220     66    157       C  
ATOM   2821  CG  LEU A 374      97.068 108.865  12.659  1.00 30.58           C  
ANISOU 2821  CG  LEU A 374     3658   3822   4138    244     85    172       C  
ATOM   2822  CD1 LEU A 374      96.317 109.057  11.336  1.00 30.82           C  
ANISOU 2822  CD1 LEU A 374     3670   3873   4168    264     82    202       C  
ATOM   2823  CD2 LEU A 374      96.128 109.197  13.813  1.00 31.23           C  
ANISOU 2823  CD2 LEU A 374     3742   3897   4227    252     99    159       C  
ATOM   2824  N   ALA A 375     100.724 108.126  12.719  1.00 28.60           N  
ANISOU 2824  N   ALA A 375     3440   3548   3881    191     64    146       N  
ATOM   2825  CA  ALA A 375     101.781 109.145  12.827  1.00 29.91           C  
ANISOU 2825  CA  ALA A 375     3619   3681   4063    187     73    143       C  
ATOM   2826  C   ALA A 375     102.698 109.146  11.600  1.00 30.52           C  
ANISOU 2826  C   ALA A 375     3694   3760   4141    183     67    160       C  
ATOM   2827  O   ALA A 375     103.020 110.211  11.117  1.00 30.93           O  
ANISOU 2827  O   ALA A 375     3751   3791   4210    191     78    172       O  
ATOM   2828  CB  ALA A 375     102.581 108.985  14.103  1.00 29.25           C  
ANISOU 2828  CB  ALA A 375     3550   3585   3979    166     71    116       C  
ATOM   2829  N   VAL A 376     103.033 107.961  11.058  1.00 29.30           N  
ANISOU 2829  N   VAL A 376     3533   3631   3970    173     51    161       N  
ATOM   2830  CA  VAL A 376     103.764 107.864   9.808  1.00 28.75           C  
ANISOU 2830  CA  VAL A 376     3460   3567   3898    171     47    178       C  
ATOM   2831  C   VAL A 376     102.934 108.454   8.630  1.00 29.64           C  
ANISOU 2831  C   VAL A 376     3562   3689   4012    193     52    206       C  
ATOM   2832  O   VAL A 376     103.442 109.228   7.834  1.00 27.54           O  
ANISOU 2832  O   VAL A 376     3298   3410   3756    199     59    223       O  
ATOM   2833  CB  VAL A 376     104.147 106.389   9.482  1.00 28.68           C  
ANISOU 2833  CB  VAL A 376     3445   3584   3869    157     30    172       C  
ATOM   2834  CG1 VAL A 376     104.650 106.244   8.051  1.00 28.47           C  
ANISOU 2834  CG1 VAL A 376     3412   3568   3837    158     27    191       C  
ATOM   2835  CG2 VAL A 376     105.185 105.866  10.473  1.00 29.50           C  
ANISOU 2835  CG2 VAL A 376     3558   3678   3973    136     25    150       C  
ATOM   2836  N   ALA A 377     101.681 108.034   8.480  1.00 29.65           N  
ANISOU 2836  N   ALA A 377     3550   3714   4002    205     49    212       N  
ATOM   2837  CA  ALA A 377     100.856 108.589   7.402  1.00 31.30           C  
ANISOU 2837  CA  ALA A 377     3747   3934   4211    227     52    240       C  
ATOM   2838  C   ALA A 377     100.768 110.142   7.454  1.00 32.24           C  
ANISOU 2838  C   ALA A 377     3873   4023   4355    244     71    254       C  
ATOM   2839  O   ALA A 377     100.821 110.820   6.427  1.00 31.86           O  
ANISOU 2839  O   ALA A 377     3821   3973   4312    258     76    279       O  
ATOM   2840  CB  ALA A 377      99.477 108.012   7.448  1.00 30.94           C  
ANISOU 2840  CB  ALA A 377     3685   3916   4153    236     46    242       C  
ATOM   2841  N   LEU A 378     100.602 110.679   8.651  1.00 33.31           N  
ANISOU 2841  N   LEU A 378     4017   4134   4504    245     82    237       N  
ATOM   2842  CA  LEU A 378     100.537 112.130   8.812  1.00 34.85           C  
ANISOU 2842  CA  LEU A 378     4220   4296   4725    260    103    246       C  
ATOM   2843  C   LEU A 378     101.872 112.809   8.522  1.00 34.81           C  
ANISOU 2843  C   LEU A 378     4229   4263   4734    250    110    248       C  
ATOM   2844  O   LEU A 378     101.880 113.908   7.953  1.00 35.66           O  
ANISOU 2844  O   LEU A 378     4338   4350   4859    265    124    269       O  
ATOM   2845  CB  LEU A 378     100.021 112.522  10.204  1.00 34.77           C  
ANISOU 2845  CB  LEU A 378     4218   4266   4726    261    115    224       C  
ATOM   2846  CG  LEU A 378      98.562 112.123  10.504  1.00 36.61           C  
ANISOU 2846  CG  LEU A 378     4437   4522   4952    275    114    225       C  
ATOM   2847  CD1 LEU A 378      98.272 112.344  11.994  1.00 35.46           C  
ANISOU 2847  CD1 LEU A 378     4301   4358   4813    271    125    198       C  
ATOM   2848  CD2 LEU A 378      97.580 112.936   9.633  1.00 38.41           C  
ANISOU 2848  CD2 LEU A 378     4650   4753   5190    305    123    257       C  
ATOM   2849  N   GLY A 379     102.981 112.190   8.939  1.00 33.87           N  
ANISOU 2849  N   GLY A 379     4118   4142   4609    225    100    227       N  
ATOM   2850  CA  GLY A 379     104.310 112.701   8.612  1.00 35.05           C  
ANISOU 2850  CA  GLY A 379     4278   4269   4771    213    105    228       C  
ATOM   2851  C   GLY A 379     104.467 112.795   7.107  1.00 35.82           C  
ANISOU 2851  C   GLY A 379     4367   4378   4864    223    104    259       C  
ATOM   2852  O   GLY A 379     104.915 113.824   6.583  1.00 38.73           O  
ANISOU 2852  O   GLY A 379     4741   4724   5250    230    118    275       O  
ATOM   2853  N   ILE A 380     104.049 111.745   6.399  1.00 33.73           N  
ANISOU 2853  N   ILE A 380     4091   4151   4576    224     88    267       N  
ATOM   2854  CA  ILE A 380     104.171 111.716   4.953  1.00 34.19           C  
ANISOU 2854  CA  ILE A 380     4140   4225   4624    232     86    294       C  
ATOM   2855  C   ILE A 380     103.277 112.809   4.286  1.00 36.30           C  
ANISOU 2855  C   ILE A 380     4402   4488   4902    260     99    325       C  
ATOM   2856  O   ILE A 380     103.729 113.502   3.406  1.00 36.84           O  
ANISOU 2856  O   ILE A 380     4473   4547   4978    267    107    348       O  
ATOM   2857  CB  ILE A 380     103.853 110.329   4.384  1.00 33.16           C  
ANISOU 2857  CB  ILE A 380     3999   4137   4466    226     67    293       C  
ATOM   2858  CG1 ILE A 380     104.975 109.298   4.697  1.00 31.42           C  
ANISOU 2858  CG1 ILE A 380     3782   3918   4235    200     56    270       C  
ATOM   2859  CG2 ILE A 380     103.635 110.410   2.867  1.00 34.00           C  
ANISOU 2859  CG2 ILE A 380     4095   4265   4559    238     65    324       C  
ATOM   2860  CD1 ILE A 380     104.485 107.844   4.528  1.00 30.34           C  
ANISOU 2860  CD1 ILE A 380     3636   3818   4074    193     40    261       C  
ATOM   2861  N   ARG A 381     102.021 112.936   4.704  1.00 36.96           N  
ANISOU 2861  N   ARG A 381     4478   4580   4987    276    100    327       N  
ATOM   2862  CA  ARG A 381     101.112 113.978   4.181  1.00 37.68           C  
ANISOU 2862  CA  ARG A 381     4562   4665   5090    305    113    357       C  
ATOM   2863  C   ARG A 381     101.602 115.407   4.337  1.00 40.33           C  
ANISOU 2863  C   ARG A 381     4910   4956   5456    313    136    366       C  
ATOM   2864  O   ARG A 381     101.390 116.245   3.453  1.00 44.32           O  
ANISOU 2864  O   ARG A 381     5413   5456   5971    333    147    398       O  
ATOM   2865  CB  ARG A 381      99.763 113.923   4.885  1.00 38.02           C  
ANISOU 2865  CB  ARG A 381     4595   4717   5134    319    114    352       C  
ATOM   2866  CG  ARG A 381      98.685 114.773   4.206  1.00 38.18           C  
ANISOU 2866  CG  ARG A 381     4602   4742   5163    351    123    387       C  
ATOM   2867  CD  ARG A 381      97.333 114.529   4.852  1.00 38.86           C  
ANISOU 2867  CD  ARG A 381     4675   4844   5247    363    122    381       C  
ATOM   2868  NE  ARG A 381      97.208 115.233   6.135  1.00 40.08           N  
ANISOU 2868  NE  ARG A 381     4842   4962   5426    366    141    361       N  
ATOM   2869  CZ  ARG A 381      96.243 115.023   7.029  1.00 39.74           C  
ANISOU 2869  CZ  ARG A 381     4792   4924   5384    371    143    347       C  
ATOM   2870  NH1 ARG A 381      95.321 114.070   6.845  1.00 41.50           N  
ANISOU 2870  NH1 ARG A 381     4996   5187   5586    373    127    348       N  
ATOM   2871  NH2 ARG A 381      96.217 115.743   8.124  1.00 39.85           N  
ANISOU 2871  NH2 ARG A 381     4818   4902   5419    373    162    329       N  
ATOM   2872  N   GLU A 382     102.238 115.689   5.459  1.00 40.11           N  
ANISOU 2872  N   GLU A 382     4898   4897   5445    298    145    338       N  
ATOM   2873  CA  GLU A 382     102.744 117.006   5.746  1.00 43.30           C  
ANISOU 2873  CA  GLU A 382     5317   5257   5880    301    168    340       C  
ATOM   2874  C   GLU A 382     104.085 117.313   5.033  1.00 42.10           C  
ANISOU 2874  C   GLU A 382     5172   5089   5734    288    171    349       C  
ATOM   2875  O   GLU A 382     104.651 118.352   5.274  1.00 40.75           O  
ANISOU 2875  O   GLU A 382     5014   4880   5589    286    190    348       O  
ATOM   2876  CB  GLU A 382     102.882 117.173   7.261  1.00 46.44           C  
ANISOU 2876  CB  GLU A 382     5727   5629   6290    287    175    304       C  
ATOM   2877  CG  GLU A 382     101.533 117.293   7.959  1.00 51.71           C  
ANISOU 2877  CG  GLU A 382     6387   6299   6959    305    181    300       C  
ATOM   2878  CD  GLU A 382     101.546 116.893   9.432  1.00 57.23           C  
ANISOU 2878  CD  GLU A 382     7096   6993   7657    287    179    261       C  
ATOM   2879  OE1 GLU A 382     102.619 116.893  10.096  1.00 61.36           O  
ANISOU 2879  OE1 GLU A 382     7633   7497   8183    263    178    236       O  
ATOM   2880  OE2 GLU A 382     100.445 116.563   9.931  1.00 62.76           O  
ANISOU 2880  OE2 GLU A 382     7788   7708   8350    298    178    256       O  
ATOM   2881  N   GLY A 383     104.557 116.413   4.169  1.00 41.07           N  
ANISOU 2881  N   GLY A 383     5035   4988   5580    279    154    356       N  
ATOM   2882  CA  GLY A 383     105.811 116.577   3.434  1.00 41.40           C  
ANISOU 2882  CA  GLY A 383     5083   5021   5626    266    157    365       C  
ATOM   2883  C   GLY A 383     107.095 116.459   4.239  1.00 40.16           C  
ANISOU 2883  C   GLY A 383     4938   4843   5479    238    157    335       C  
ATOM   2884  O   GLY A 383     108.115 116.946   3.822  1.00 40.72           O  
ANISOU 2884  O   GLY A 383     5016   4895   5562    229    166    341       O  
ATOM   2885  N   LYS A 384     107.067 115.795   5.380  1.00 40.08           N  
ANISOU 2885  N   LYS A 384     4930   4837   5462    223    147    303       N  
ATOM   2886  CA  LYS A 384     108.267 115.610   6.184  1.00 40.09           C  
ANISOU 2886  CA  LYS A 384     4941   4822   5471    196    144    274       C  
ATOM   2887  C   LYS A 384     109.300 114.567   5.691  1.00 39.35           C  
ANISOU 2887  C   LYS A 384     4843   4749   5360    177    128    270       C  
ATOM   2888  O   LYS A 384     110.439 114.561   6.159  1.00 39.06           O  
ANISOU 2888  O   LYS A 384     4811   4697   5331    156    127    253       O  
ATOM   2889  CB  LYS A 384     107.854 115.272   7.592  1.00 42.68           C  
ANISOU 2889  CB  LYS A 384     5273   5149   5796    188    138    243       C  
ATOM   2890  CG  LYS A 384     107.117 116.408   8.244  1.00 45.05           C  
ANISOU 2890  CG  LYS A 384     5580   5419   6116    202    158    241       C  
ATOM   2891  CD  LYS A 384     106.862 116.120   9.709  1.00 47.71           C  
ANISOU 2891  CD  LYS A 384     5923   5753   6450    190    154    207       C  
ATOM   2892  CE  LYS A 384     106.267 117.373  10.346  1.00 50.01           C  
ANISOU 2892  CE  LYS A 384     6224   6011   6766    202    177    203       C  
ATOM   2893  NZ  LYS A 384     105.612 117.013  11.614  1.00 50.40           N  
ANISOU 2893  NZ  LYS A 384     6277   6066   6807    199    175    176       N  
ATOM   2894  N   SER A 385     108.924 113.732   4.738  1.00 36.36           N  
ANISOU 2894  N   SER A 385     4453   4404   4958    184    117    286       N  
ATOM   2895  CA  SER A 385     109.772 112.625   4.340  1.00 39.23           C  
ANISOU 2895  CA  SER A 385     4812   4789   5305    167    102    280       C  
ATOM   2896  C   SER A 385     111.156 113.067   3.849  1.00 38.21           C  
ANISOU 2896  C   SER A 385     4687   4640   5190    154    111    285       C  
ATOM   2897  O   SER A 385     111.242 113.999   3.081  1.00 39.14           O  
ANISOU 2897  O   SER A 385     4807   4744   5320    165    125    308       O  
ATOM   2898  CB  SER A 385     109.076 111.846   3.222  1.00 39.56           C  
ANISOU 2898  CB  SER A 385     4842   4867   5321    179     93    299       C  
ATOM   2899  OG  SER A 385     109.724 110.623   3.044  1.00 44.95           O  
ANISOU 2899  OG  SER A 385     5521   5571   5987    163     79    287       O  
ATOM   2900  N   GLU A 386     112.226 112.399   4.291  1.00 37.99           N  
ANISOU 2900  N   GLU A 386     4660   4613   5161    132    102    265       N  
ATOM   2901  CA  GLU A 386     113.597 112.618   3.752  1.00 38.14           C  
ANISOU 2901  CA  GLU A 386     4680   4620   5191    119    108    270       C  
ATOM   2902  C   GLU A 386     114.190 111.256   3.429  1.00 37.70           C  
ANISOU 2902  C   GLU A 386     4616   4591   5116    106     93    262       C  
ATOM   2903  O   GLU A 386     113.847 110.249   4.076  1.00 34.44           O  
ANISOU 2903  O   GLU A 386     4200   4196   4689    102     79    245       O  
ATOM   2904  CB  GLU A 386     114.474 113.339   4.779  1.00 39.80           C  
ANISOU 2904  CB  GLU A 386     4898   4798   5427    101    115    249       C  
ATOM   2905  CG  GLU A 386     114.045 114.784   5.029  1.00 42.56           C  
ANISOU 2905  CG  GLU A 386     5258   5115   5800    112    134    256       C  
ATOM   2906  CD  GLU A 386     114.764 115.444   6.199  1.00 46.57           C  
ANISOU 2906  CD  GLU A 386     5773   5591   6329     93    139    230       C  
ATOM   2907  OE1 GLU A 386     115.855 114.992   6.603  1.00 50.14           O  
ANISOU 2907  OE1 GLU A 386     6223   6044   6782     71    130    213       O  
ATOM   2908  OE2 GLU A 386     114.238 116.438   6.736  1.00 52.11           O  
ANISOU 2908  OE2 GLU A 386     6484   6268   7048     99    153    226       O  
ATOM   2909  N   ASP A 387     115.074 111.203   2.446  1.00 38.85           N  
ANISOU 2909  N   ASP A 387     4759   4739   5263    102     99    276       N  
ATOM   2910  CA  ASP A 387     115.715 109.918   2.038  1.00 39.45           C  
ANISOU 2910  CA  ASP A 387     4828   4838   5322     91     88    270       C  
ATOM   2911  C   ASP A 387     116.554 109.287   3.124  1.00 36.30           C  
ANISOU 2911  C   ASP A 387     4428   4435   4930     71     77    243       C  
ATOM   2912  O   ASP A 387     117.278 109.970   3.801  1.00 36.83           O  
ANISOU 2912  O   ASP A 387     4498   4478   5017     60     82    234       O  
ATOM   2913  CB  ASP A 387     116.558 110.101   0.789  1.00 42.31           C  
ANISOU 2913  CB  ASP A 387     5189   5202   5687     89     99    289       C  
ATOM   2914  CG  ASP A 387     115.721 110.535  -0.398  1.00 47.34           C  
ANISOU 2914  CG  ASP A 387     5826   5851   6311    109    107    318       C  
ATOM   2915  OD1 ASP A 387     114.481 110.347  -0.374  1.00 51.10           O  
ANISOU 2915  OD1 ASP A 387     6300   6343   6772    123    100    321       O  
ATOM   2916  OD2 ASP A 387     116.300 111.078  -1.349  1.00 53.49           O  
ANISOU 2916  OD2 ASP A 387     6606   6623   7095    111    120    338       O  
ATOM   2917  N   PHE A 388     116.419 107.972   3.283  1.00 34.60           N  
ANISOU 2917  N   PHE A 388     4207   4244   4696     67     63    232       N  
ATOM   2918  CA  PHE A 388     117.181 107.242   4.245  1.00 34.40           C  
ANISOU 2918  CA  PHE A 388     4179   4218   4674     50     53    211       C  
ATOM   2919  C   PHE A 388     118.605 107.115   3.684  1.00 34.77           C  
ANISOU 2919  C   PHE A 388     4220   4260   4731     38     58    215       C  
ATOM   2920  O   PHE A 388     118.777 106.526   2.632  1.00 37.74           O  
ANISOU 2920  O   PHE A 388     4592   4652   5096     41     60    226       O  
ATOM   2921  CB  PHE A 388     116.579 105.841   4.529  1.00 34.39           C  
ANISOU 2921  CB  PHE A 388     4173   4243   4651     51     38    200       C  
ATOM   2922  CG  PHE A 388     117.241 105.141   5.714  1.00 34.51           C  
ANISOU 2922  CG  PHE A 388     4185   4256   4670     36     27    179       C  
ATOM   2923  CD1 PHE A 388     116.739 105.297   6.996  1.00 34.80           C  
ANISOU 2923  CD1 PHE A 388     4227   4288   4708     34     20    164       C  
ATOM   2924  CD2 PHE A 388     118.379 104.379   5.541  1.00 35.38           C  
ANISOU 2924  CD2 PHE A 388     4289   4371   4783     25     23    176       C  
ATOM   2925  CE1 PHE A 388     117.329 104.695   8.085  1.00 34.32           C  
ANISOU 2925  CE1 PHE A 388     4164   4227   4648     21      8    147       C  
ATOM   2926  CE2 PHE A 388     118.987 103.778   6.624  1.00 35.35           C  
ANISOU 2926  CE2 PHE A 388     4281   4367   4782     13     12    160       C  
ATOM   2927  CZ  PHE A 388     118.484 103.947   7.896  1.00 33.75           C  
ANISOU 2927  CZ  PHE A 388     4083   4160   4579     10      4    146       C  
ATOM   2928  N   GLN A 389     119.588 107.622   4.403  1.00 33.28           N  
ANISOU 2928  N   GLN A 389     4031   4051   4562     24     58    204       N  
ATOM   2929  CA  GLN A 389     120.996 107.621   3.954  1.00 35.40           C  
ANISOU 2929  CA  GLN A 389     4293   4314   4845     11     64    208       C  
ATOM   2930  C   GLN A 389     121.642 106.295   4.260  1.00 32.87           C  
ANISOU 2930  C   GLN A 389     3962   4009   4517      2     52    196       C  
ATOM   2931  O   GLN A 389     121.710 105.916   5.416  1.00 32.00           O  
ANISOU 2931  O   GLN A 389     3851   3901   4408     -6     39    179       O  
ATOM   2932  CB  GLN A 389     121.776 108.741   4.679  1.00 38.40           C  
ANISOU 2932  CB  GLN A 389     4675   4666   5251     -2     69    200       C  
ATOM   2933  CG  GLN A 389     121.347 110.154   4.235  1.00 43.91           C  
ANISOU 2933  CG  GLN A 389     5381   5341   5960      6     87    214       C  
ATOM   2934  CD  GLN A 389     121.833 111.311   5.156  1.00 52.70           C  
ANISOU 2934  CD  GLN A 389     6500   6424   7099     -7     92    201       C  
ATOM   2935  OE1 GLN A 389     122.470 111.104   6.209  1.00 57.31           O  
ANISOU 2935  OE1 GLN A 389     7080   7005   7689    -24     81    180       O  
ATOM   2936  NE2 GLN A 389     121.494 112.544   4.765  1.00 55.84           N  
ANISOU 2936  NE2 GLN A 389     6906   6799   7511      1    110    214       N  
ATOM   2937  N   LYS A 390     122.092 105.592   3.225  1.00 32.43           N  
ANISOU 2937  N   LYS A 390     3900   3966   4454      3     56    206       N  
ATOM   2938  CA  LYS A 390     122.882 104.371   3.378  1.00 33.21           C  
ANISOU 2938  CA  LYS A 390     3989   4078   4551     -5     49    198       C  
ATOM   2939  C   LYS A 390     124.369 104.728   3.352  1.00 32.52           C  
ANISOU 2939  C   LYS A 390     3893   3977   4487    -19     55    199       C  
ATOM   2940  O   LYS A 390     124.882 105.085   2.311  1.00 35.41           O  
ANISOU 2940  O   LYS A 390     4257   4339   4858    -18     69    213       O  
ATOM   2941  CB  LYS A 390     122.532 103.399   2.258  1.00 32.85           C  
ANISOU 2941  CB  LYS A 390     3942   4053   4486      4     53    206       C  
ATOM   2942  CG  LYS A 390     121.024 103.134   2.165  1.00 33.72           C  
ANISOU 2942  CG  LYS A 390     4060   4179   4575     16     48    207       C  
ATOM   2943  CD  LYS A 390     120.541 102.187   3.251  1.00 32.98           C  
ANISOU 2943  CD  LYS A 390     3965   4094   4473     14     32    190       C  
ATOM   2944  CE  LYS A 390     120.879 100.756   2.931  1.00 33.69           C  
ANISOU 2944  CE  LYS A 390     4048   4199   4553     12     30    185       C  
ATOM   2945  NZ  LYS A 390     120.033 100.132   1.883  1.00 31.10           N  
ANISOU 2945  NZ  LYS A 390     3722   3890   4204     20     34    190       N  
ATOM   2946  N   LYS A 391     125.050 104.614   4.487  1.00 33.63           N  
ANISOU 2946  N   LYS A 391     4027   4112   4639    -32     43    184       N  
ATOM   2947  CA  LYS A 391     126.437 105.073   4.641  1.00 33.92           C  
ANISOU 2947  CA  LYS A 391     4053   4135   4698    -47     47    183       C  
ATOM   2948  C   LYS A 391     127.375 103.925   4.951  1.00 31.85           C  
ANISOU 2948  C   LYS A 391     3776   3885   4439    -54     37    178       C  
ATOM   2949  O   LYS A 391     126.943 102.810   5.287  1.00 28.11           O  
ANISOU 2949  O   LYS A 391     3303   3428   3951    -48     27    172       O  
ATOM   2950  CB  LYS A 391     126.554 105.999   5.837  1.00 37.45           C  
ANISOU 2950  CB  LYS A 391     4503   4567   5159    -58     39    170       C  
ATOM   2951  CG  LYS A 391     125.627 107.195   5.894  1.00 43.12           C  
ANISOU 2951  CG  LYS A 391     5237   5269   5878    -53     47    171       C  
ATOM   2952  CD  LYS A 391     125.770 107.837   7.286  1.00 47.36           C  
ANISOU 2952  CD  LYS A 391     5776   5793   6425    -66     38    152       C  
ATOM   2953  CE  LYS A 391     124.542 108.626   7.700  1.00 53.47           C  
ANISOU 2953  CE  LYS A 391     6566   6557   7194    -57     41    147       C  
ATOM   2954  NZ  LYS A 391     124.713 110.048   7.288  1.00 56.76           N  
ANISOU 2954  NZ  LYS A 391     6988   6946   7631    -60     59    154       N  
ATOM   2955  N   SER A 392     128.664 104.238   4.863  1.00 28.68           N  
ANISOU 2955  N   SER A 392     3363   3476   4059    -66     42    180       N  
ATOM   2956  CA  SER A 392     129.694 103.405   5.378  1.00 29.06           C  
ANISOU 2956  CA  SER A 392     3395   3532   4116    -75     32    174       C  
ATOM   2957  C   SER A 392     129.566 103.436   6.905  1.00 30.13           C  
ANISOU 2957  C   SER A 392     3530   3669   4250    -83     12    158       C  
ATOM   2958  O   SER A 392     129.376 104.478   7.460  1.00 30.01           O  
ANISOU 2958  O   SER A 392     3521   3640   4240    -91     10    150       O  
ATOM   2959  CB  SER A 392     131.055 103.936   5.000  1.00 27.54           C  
ANISOU 2959  CB  SER A 392     3187   3329   3947    -88     42    180       C  
ATOM   2960  OG  SER A 392     131.197 103.934   3.599  1.00 27.43           O  
ANISOU 2960  OG  SER A 392     3175   3315   3933    -80     62    195       O  
ATOM   2961  N   ILE A 393     129.709 102.296   7.566  1.00 29.46           N  
ANISOU 2961  N   ILE A 393     3436   3598   4157    -82     -2    153       N  
ATOM   2962  CA  ILE A 393     129.440 102.228   8.978  1.00 30.73           C  
ANISOU 2962  CA  ILE A 393     3599   3764   4312    -88    -22    139       C  
ATOM   2963  C   ILE A 393     130.274 101.133   9.648  1.00 28.70           C  
ANISOU 2963  C   ILE A 393     3326   3521   4058    -92    -36    138       C  
ATOM   2964  O   ILE A 393     130.553 100.104   9.054  1.00 27.64           O  
ANISOU 2964  O   ILE A 393     3184   3396   3924    -84    -31    146       O  
ATOM   2965  CB  ILE A 393     127.912 102.092   9.191  1.00 33.76           C  
ANISOU 2965  CB  ILE A 393     4001   4152   4674    -76    -24    135       C  
ATOM   2966  CG1 ILE A 393     127.535 102.244  10.648  1.00 39.10           C  
ANISOU 2966  CG1 ILE A 393     4682   4831   5343    -83    -41    119       C  
ATOM   2967  CG2 ILE A 393     127.399 100.750   8.678  1.00 34.58           C  
ANISOU 2967  CG2 ILE A 393     4105   4270   4762    -63    -23    141       C  
ATOM   2968  CD1 ILE A 393     126.012 102.375  10.900  1.00 42.00           C  
ANISOU 2968  CD1 ILE A 393     5068   5199   5691    -72    -41    114       C  
ATOM   2969  N   LYS A 394     130.693 101.397  10.881  1.00 27.86           N  
ANISOU 2969  N   LYS A 394     3214   3418   3955   -105    -53    127       N  
ATOM   2970  CA  LYS A 394     131.356 100.440  11.710  1.00 29.29           C  
ANISOU 2970  CA  LYS A 394     3379   3614   4136   -108    -69    126       C  
ATOM   2971  C   LYS A 394     130.337 100.008  12.781  1.00 28.64           C  
ANISOU 2971  C   LYS A 394     3309   3541   4031   -104    -84    117       C  
ATOM   2972  O   LYS A 394     129.796 100.830  13.464  1.00 26.72           O  
ANISOU 2972  O   LYS A 394     3078   3293   3781   -110    -89    105       O  
ATOM   2973  CB  LYS A 394     132.560 101.083  12.371  1.00 32.47           C  
ANISOU 2973  CB  LYS A 394     3766   4016   4556   -128    -80    121       C  
ATOM   2974  CG  LYS A 394     133.221 100.182  13.371  1.00 35.96           C  
ANISOU 2974  CG  LYS A 394     4192   4476   4996   -131   -100    121       C  
ATOM   2975  CD  LYS A 394     134.512 100.694  13.936  1.00 41.31           C  
ANISOU 2975  CD  LYS A 394     4848   5156   5690   -150   -112    117       C  
ATOM   2976  CE  LYS A 394     134.492 102.151  14.316  1.00 45.84           C  
ANISOU 2976  CE  LYS A 394     5430   5717   6269   -168   -112    102       C  
ATOM   2977  NZ  LYS A 394     134.283 102.264  15.763  1.00 49.48           N  
ANISOU 2977  NZ  LYS A 394     5894   6190   6715   -179   -134     87       N  
ATOM   2978  N   LEU A 395     130.103  98.719  12.915  1.00 27.66           N  
ANISOU 2978  N   LEU A 395     3183   3430   3897    -93    -89    123       N  
ATOM   2979  CA  LEU A 395     129.230  98.187  13.961  1.00 27.58           C  
ANISOU 2979  CA  LEU A 395     3181   3430   3866    -89   -102    117       C  
ATOM   2980  C   LEU A 395     130.017  97.305  14.899  1.00 27.21           C  
ANISOU 2980  C   LEU A 395     3119   3399   3821    -92   -119    120       C  
ATOM   2981  O   LEU A 395     130.582  96.303  14.481  1.00 29.48           O  
ANISOU 2981  O   LEU A 395     3394   3691   4116    -85   -116    133       O  
ATOM   2982  CB  LEU A 395     128.117  97.366  13.335  1.00 26.89           C  
ANISOU 2982  CB  LEU A 395     3107   3345   3766    -73    -92    121       C  
ATOM   2983  CG  LEU A 395     127.222  98.165  12.413  1.00 27.45           C  
ANISOU 2983  CG  LEU A 395     3192   3404   3832    -67    -76    120       C  
ATOM   2984  CD1 LEU A 395     126.309  97.235  11.670  1.00 28.40           C  
ANISOU 2984  CD1 LEU A 395     3319   3530   3940    -53    -67    125       C  
ATOM   2985  CD2 LEU A 395     126.462  99.268  13.135  1.00 26.73           C  
ANISOU 2985  CD2 LEU A 395     3115   3307   3734    -73    -80    108       C  
ATOM   2986  N   SER A 396     130.015  97.632  16.179  1.00 27.85           N  
ANISOU 2986  N   SER A 396     3202   3488   3893   -102   -137    111       N  
ATOM   2987  CA  SER A 396     130.630  96.729  17.171  1.00 27.78           C  
ANISOU 2987  CA  SER A 396     3179   3497   3881   -104   -155    116       C  
ATOM   2988  C   SER A 396     129.709  95.521  17.492  1.00 26.70           C  
ANISOU 2988  C   SER A 396     3051   3368   3725    -89   -156    122       C  
ATOM   2989  O   SER A 396     128.488  95.549  17.240  1.00 23.65           O  
ANISOU 2989  O   SER A 396     2683   2976   3326    -81   -147    117       O  
ATOM   2990  CB  SER A 396     130.999  97.528  18.407  1.00 28.94           C  
ANISOU 2990  CB  SER A 396     3324   3651   4021   -121   -174    103       C  
ATOM   2991  OG  SER A 396     129.833  97.845  19.142  1.00 31.08           O  
ANISOU 2991  OG  SER A 396     3615   3922   4270   -121   -177     90       O  
ATOM   2992  N   ASP A 397     130.313  94.446  17.981  1.00 26.56           N  
ANISOU 2992  N   ASP A 397     3020   3364   3710    -84   -166    134       N  
ATOM   2993  CA  ASP A 397     129.605  93.238  18.459  1.00 26.82           C  
ANISOU 2993  CA  ASP A 397     3058   3404   3727    -72   -168    141       C  
ATOM   2994  C   ASP A 397     129.975  93.006  19.925  1.00 28.25           C  
ANISOU 2994  C   ASP A 397     3233   3604   3898    -78   -191    143       C  
ATOM   2995  O   ASP A 397     131.024  93.515  20.409  1.00 26.92           O  
ANISOU 2995  O   ASP A 397     3048   3443   3736    -90   -206    142       O  
ATOM   2996  CB  ASP A 397     130.041  92.037  17.620  1.00 27.42           C  
ANISOU 2996  CB  ASP A 397     3123   3478   3818    -58   -156    157       C  
ATOM   2997  CG  ASP A 397     129.065  90.832  17.665  1.00 27.55           C  
ANISOU 2997  CG  ASP A 397     3150   3495   3822    -44   -150    162       C  
ATOM   2998  OD1 ASP A 397     127.989  90.878  18.328  1.00 26.17           O  
ANISOU 2998  OD1 ASP A 397     2992   3324   3628    -44   -154    155       O  
ATOM   2999  OD2 ASP A 397     129.408  89.802  16.986  1.00 27.55           O  
ANISOU 2999  OD2 ASP A 397     3142   3491   3835    -34   -138    174       O  
ATOM   3000  N   GLY A 398     129.103  92.233  20.613  1.00 27.47           N  
ANISOU 3000  N   GLY A 398     3146   3513   3780    -70   -195    145       N  
ATOM   3001  CA  GLY A 398     129.183  91.997  22.029  1.00 26.96           C  
ANISOU 3001  CA  GLY A 398     3079   3466   3698    -75   -215    147       C  
ATOM   3002  C   GLY A 398     128.374  93.046  22.760  1.00 28.14           C  
ANISOU 3002  C   GLY A 398     3247   3617   3827    -86   -221    126       C  
ATOM   3003  O   GLY A 398     128.190  94.171  22.253  1.00 28.29           O  
ANISOU 3003  O   GLY A 398     3274   3624   3852    -94   -213    112       O  
ATOM   3004  N   ALA A 399     127.891  92.702  23.953  1.00 28.80           N  
ANISOU 3004  N   ALA A 399     3338   3716   3889    -87   -233    126       N  
ATOM   3005  CA  ALA A 399     127.132  93.650  24.808  1.00 29.68           C  
ANISOU 3005  CA  ALA A 399     3468   3831   3980    -98   -238    106       C  
ATOM   3006  C   ALA A 399     127.862  94.982  25.081  1.00 28.71           C  
ANISOU 3006  C   ALA A 399     3340   3708   3861   -118   -247     89       C  
ATOM   3007  O   ALA A 399     127.218  96.018  25.185  1.00 25.04           O  
ANISOU 3007  O   ALA A 399     2891   3234   3389   -126   -242     70       O  
ATOM   3008  CB  ALA A 399     126.784  92.989  26.140  1.00 30.01           C  
ANISOU 3008  CB  ALA A 399     3514   3892   3995    -97   -252    110       C  
ATOM   3009  N   ASN A 400     129.188  94.944  25.233  1.00 28.50           N  
ANISOU 3009  N   ASN A 400     3292   3692   3846   -126   -262     97       N  
ATOM   3010  CA  ASN A 400     129.936  96.177  25.501  1.00 30.43           C  
ANISOU 3010  CA  ASN A 400     3530   3936   4095   -147   -271     80       C  
ATOM   3011  C   ASN A 400     130.743  96.654  24.311  1.00 31.45           C  
ANISOU 3011  C   ASN A 400     3646   4050   4254   -150   -260     82       C  
ATOM   3012  O   ASN A 400     131.617  97.458  24.492  1.00 30.68           O  
ANISOU 3012  O   ASN A 400     3537   3954   4166   -167   -269     74       O  
ATOM   3013  CB  ASN A 400     130.884  96.037  26.709  1.00 33.30           C  
ANISOU 3013  CB  ASN A 400     3878   4328   4448   -160   -298     82       C  
ATOM   3014  CG  ASN A 400     130.192  95.520  27.965  1.00 33.88           C  
ANISOU 3014  CG  ASN A 400     3963   4420   4489   -158   -310     82       C  
ATOM   3015  OD1 ASN A 400     130.641  94.548  28.589  1.00 36.30           O  
ANISOU 3015  OD1 ASN A 400     4258   4748   4788   -152   -325    101       O  
ATOM   3016  ND2 ASN A 400     129.151  96.151  28.344  1.00 32.73           N  
ANISOU 3016  ND2 ASN A 400     3842   4269   4327   -162   -303     63       N  
ATOM   3017  N   GLY A 401     130.516  96.106  23.106  1.00 29.66           N  
ANISOU 3017  N   GLY A 401     3535   3853   3881   -222    -56    217       N  
ATOM   3018  CA  GLY A 401     131.180  96.635  21.939  1.00 29.43           C  
ANISOU 3018  CA  GLY A 401     3506   3814   3861   -211    -55    216       C  
ATOM   3019  C   GLY A 401     132.610  96.231  21.762  1.00 29.86           C  
ANISOU 3019  C   GLY A 401     3556   3872   3919   -209    -61    230       C  
ATOM   3020  O   GLY A 401     133.279  96.821  20.936  1.00 28.65           O  
ANISOU 3020  O   GLY A 401     3402   3713   3771   -204    -60    229       O  
ATOM   3021  N   ASP A 402     133.035  95.177  22.466  1.00 29.50           N  
ANISOU 3021  N   ASP A 402     3505   3834   3869   -213    -68    244       N  
ATOM   3022  CA  ASP A 402     134.428  94.727  22.460  1.00 32.62           C  
ANISOU 3022  CA  ASP A 402     3893   4235   4266   -212    -76    257       C  
ATOM   3023  C   ASP A 402     134.622  93.334  21.896  1.00 30.75           C  
ANISOU 3023  C   ASP A 402     3654   3992   4039   -199    -81    269       C  
ATOM   3024  O   ASP A 402     135.698  92.783  22.020  1.00 32.24           O  
ANISOU 3024  O   ASP A 402     3835   4185   4229   -198    -89    281       O  
ATOM   3025  CB  ASP A 402     135.041  94.811  23.893  1.00 34.65           C  
ANISOU 3025  CB  ASP A 402     4146   4508   4510   -227    -82    262       C  
ATOM   3026  CG  ASP A 402     134.220  94.034  24.923  1.00 39.19           C  
ANISOU 3026  CG  ASP A 402     4725   5090   5077   -235    -85    267       C  
ATOM   3027  OD1 ASP A 402     133.129  93.440  24.590  1.00 39.71           O  
ANISOU 3027  OD1 ASP A 402     4795   5146   5146   -230    -81    265       O  
ATOM   3028  OD2 ASP A 402     134.619  94.061  26.090  1.00 43.67           O  
ANISOU 3028  OD2 ASP A 402     5289   5670   5632   -248    -90    272       O  
ATOM   3029  N   GLN A 403     133.623  92.763  21.230  1.00 29.96           N  
ANISOU 3029  N   GLN A 403     3557   3880   3945   -190    -77    267       N  
ATOM   3030  CA  GLN A 403     133.782  91.421  20.665  1.00 29.30           C  
ANISOU 3030  CA  GLN A 403     3472   3789   3871   -179    -82    278       C  
ATOM   3031  C   GLN A 403     133.770  91.400  19.118  1.00 29.21           C  
ANISOU 3031  C   GLN A 403     3460   3765   3873   -164    -77    273       C  
ATOM   3032  O   GLN A 403     132.939  90.735  18.501  1.00 31.30           O  
ANISOU 3032  O   GLN A 403     3728   4021   4144   -155    -74    271       O  
ATOM   3033  CB  GLN A 403     132.741  90.507  21.261  1.00 31.80           C  
ANISOU 3033  CB  GLN A 403     3794   4105   4185   -182    -82    281       C  
ATOM   3034  CG  GLN A 403     132.849  90.344  22.767  1.00 31.84           C  
ANISOU 3034  CG  GLN A 403     3799   4123   4177   -198    -88    288       C  
ATOM   3035  CD  GLN A 403     131.752  89.438  23.296  1.00 33.37           C  
ANISOU 3035  CD  GLN A 403     3999   4315   4367   -203    -87    291       C  
ATOM   3036  OE1 GLN A 403     131.625  88.289  22.890  1.00 32.65           O  
ANISOU 3036  OE1 GLN A 403     3908   4214   4282   -195    -90    299       O  
ATOM   3037  NE2 GLN A 403     130.950  89.964  24.204  1.00 34.12           N  
ANISOU 3037  NE2 GLN A 403     4097   4418   4449   -217    -83    283       N  
ATOM   3038  N   GLY A 404     134.690  92.148  18.510  1.00 25.93           N  
ANISOU 3038  N   GLY A 404     3041   3350   3460   -161    -75    270       N  
ATOM   3039  CA  GLY A 404     134.765  92.300  17.099  1.00 25.18           C  
ANISOU 3039  CA  GLY A 404     2946   3245   3375   -149    -71    265       C  
ATOM   3040  C   GLY A 404     133.638  93.181  16.554  1.00 25.49           C  
ANISOU 3040  C   GLY A 404     2995   3277   3414   -148    -62    252       C  
ATOM   3041  O   GLY A 404     133.090  94.034  17.240  1.00 24.26           O  
ANISOU 3041  O   GLY A 404     2844   3125   3250   -157    -60    244       O  
ATOM   3042  N   GLY A 405     133.300  92.968  15.308  1.00 26.22           N  
ANISOU 3042  N   GLY A 405     3089   3359   3514   -136    -59    248       N  
ATOM   3043  CA  GLY A 405     132.360  93.879  14.616  1.00 26.48           C  
ANISOU 3043  CA  GLY A 405     3130   3385   3547   -132    -52    236       C  
ATOM   3044  C   GLY A 405     132.160  93.450  13.186  1.00 26.56           C  
ANISOU 3044  C   GLY A 405     3140   3385   3566   -119    -49    234       C  
ATOM   3045  O   GLY A 405     132.650  92.408  12.739  1.00 25.25           O  
ANISOU 3045  O   GLY A 405     2969   3218   3407   -112    -52    241       O  
ATOM   3046  N   VAL A 406     131.385  94.270  12.512  1.00 25.98           N  
ANISOU 3046  N   VAL A 406     3075   3305   3492   -114    -45    224       N  
ATOM   3047  CA  VAL A 406     131.095  94.166  11.114  1.00 25.21           C  
ANISOU 3047  CA  VAL A 406     2979   3198   3400   -102    -42    221       C  
ATOM   3048  C   VAL A 406     131.313  95.553  10.534  1.00 24.62           C  
ANISOU 3048  C   VAL A 406     2912   3119   3322   -103    -39    215       C  
ATOM   3049  O   VAL A 406     130.857  96.547  11.110  1.00 24.68           O  
ANISOU 3049  O   VAL A 406     2925   3127   3324   -109    -38    208       O  
ATOM   3050  CB  VAL A 406     129.626  93.756  10.919  1.00 26.27           C  
ANISOU 3050  CB  VAL A 406     3117   3329   3537    -96    -41    213       C  
ATOM   3051  CG1 VAL A 406     129.236  93.750   9.445  1.00 28.00           C  
ANISOU 3051  CG1 VAL A 406     3340   3539   3761    -84    -38    208       C  
ATOM   3052  CG2 VAL A 406     129.376  92.360  11.465  1.00 27.53           C  
ANISOU 3052  CG2 VAL A 406     3271   3491   3699    -97    -43    219       C  
ATOM   3053  N   ALA A 407     132.002  95.631   9.397  1.00 24.68           N  
ANISOU 3053  N   ALA A 407     2920   3123   3334    -98    -37    217       N  
ATOM   3054  CA  ALA A 407     132.144  96.906   8.650  1.00 24.43           C  
ANISOU 3054  CA  ALA A 407     2898   3086   3299    -98    -33    212       C  
ATOM   3055  C   ALA A 407     131.429  96.863   7.286  1.00 23.44           C  
ANISOU 3055  C   ALA A 407     2778   2951   3176    -86    -31    208       C  
ATOM   3056  O   ALA A 407     131.526  95.902   6.561  1.00 23.56           O  
ANISOU 3056  O   ALA A 407     2789   2966   3197    -79    -31    210       O  
ATOM   3057  CB  ALA A 407     133.611  97.258   8.488  1.00 24.75           C  
ANISOU 3057  CB  ALA A 407     2936   3131   3338   -106    -32    217       C  
ATOM   3058  N   ILE A 408     130.713  97.923   6.977  1.00 22.94           N  
ANISOU 3058  N   ILE A 408     2726   2881   3110    -84    -30    200       N  
ATOM   3059  CA  ILE A 408     130.146  98.167   5.693  1.00 24.81           C  
ANISOU 3059  CA  ILE A 408     2970   3109   3347    -73    -29    197       C  
ATOM   3060  C   ILE A 408     130.790  99.391   5.045  1.00 24.33           C  
ANISOU 3060  C   ILE A 408     2920   3043   3282    -77    -27    197       C  
ATOM   3061  O   ILE A 408     130.726 100.481   5.597  1.00 23.82           O  
ANISOU 3061  O   ILE A 408     2862   2974   3213    -83    -27    194       O  
ATOM   3062  CB  ILE A 408     128.652  98.397   5.824  1.00 27.92           C  
ANISOU 3062  CB  ILE A 408     3369   3499   3741    -65    -31    187       C  
ATOM   3063  CG1 ILE A 408     128.034  97.268   6.644  1.00 30.78           C  
ANISOU 3063  CG1 ILE A 408     3720   3867   4106    -65    -33    186       C  
ATOM   3064  CG2 ILE A 408     128.004  98.408   4.466  1.00 28.82           C  
ANISOU 3064  CG2 ILE A 408     3488   3606   3856    -53    -31    184       C  
ATOM   3065  CD1 ILE A 408     126.586  97.443   6.846  1.00 33.51           C  
ANISOU 3065  CD1 ILE A 408     4069   4212   4451    -59    -34    175       C  
ATOM   3066  N   LEU A 409     131.446  99.199   3.900  1.00 24.45           N  
ANISOU 3066  N   LEU A 409     2936   3056   3297    -74    -24    202       N  
ATOM   3067  CA  LEU A 409     132.027 100.322   3.166  1.00 23.53           C  
ANISOU 3067  CA  LEU A 409     2832   2934   3176    -79    -21    203       C  
ATOM   3068  C   LEU A 409     131.211 100.489   1.919  1.00 23.77           C  
ANISOU 3068  C   LEU A 409     2871   2956   3205    -67    -22    200       C  
ATOM   3069  O   LEU A 409     131.054  99.562   1.169  1.00 24.88           O  
ANISOU 3069  O   LEU A 409     3007   3099   3349    -60    -22    201       O  
ATOM   3070  CB  LEU A 409     133.492 100.082   2.859  1.00 24.27           C  
ANISOU 3070  CB  LEU A 409     2918   3034   3268    -88    -17    209       C  
ATOM   3071  CG  LEU A 409     134.399  99.809   4.049  1.00 23.92           C  
ANISOU 3071  CG  LEU A 409     2863   3000   3226    -98    -18    212       C  
ATOM   3072  CD1 LEU A 409     135.833  99.697   3.570  1.00 24.20           C  
ANISOU 3072  CD1 LEU A 409     2893   3043   3261   -106    -14    216       C  
ATOM   3073  CD2 LEU A 409     134.342 100.888   5.108  1.00 24.73           C  
ANISOU 3073  CD2 LEU A 409     2972   3101   3324   -108    -18    209       C  
ATOM   3074  N   ARG A 410     130.692 101.699   1.710  1.00 22.62           N  
ANISOU 3074  N   ARG A 410     2741   2800   3055    -66    -23    197       N  
ATOM   3075  CA  ARG A 410     129.901 102.055   0.553  1.00 24.24           C  
ANISOU 3075  CA  ARG A 410     2957   2997   3258    -55    -26    195       C  
ATOM   3076  C   ARG A 410     130.547 103.190  -0.265  1.00 26.37           C  
ANISOU 3076  C   ARG A 410     3242   3257   3520    -60    -23    199       C  
ATOM   3077  O   ARG A 410     131.113 104.130   0.313  1.00 24.87           O  
ANISOU 3077  O   ARG A 410     3059   3063   3327    -71    -21    200       O  
ATOM   3078  CB  ARG A 410     128.553 102.572   1.039  1.00 23.49           C  
ANISOU 3078  CB  ARG A 410     2867   2894   3163    -46    -31    186       C  
ATOM   3079  CG  ARG A 410     127.720 101.422   1.594  1.00 24.04           C  
ANISOU 3079  CG  ARG A 410     2923   2972   3238    -39    -33    181       C  
ATOM   3080  CD  ARG A 410     126.314 101.861   2.015  1.00 24.65           C  
ANISOU 3080  CD  ARG A 410     3004   3045   3317    -30    -38    171       C  
ATOM   3081  NE  ARG A 410     125.424 100.712   2.188  1.00 26.21           N  
ANISOU 3081  NE  ARG A 410     3189   3250   3519    -23    -39    166       N  
ATOM   3082  CZ  ARG A 410     124.886 100.273   3.333  1.00 26.53           C  
ANISOU 3082  CZ  ARG A 410     3220   3297   3562    -26    -39    160       C  
ATOM   3083  NH1 ARG A 410     125.124 100.863   4.491  1.00 26.95           N  
ANISOU 3083  NH1 ARG A 410     3274   3352   3615    -36    -38    159       N  
ATOM   3084  NH2 ARG A 410     124.093  99.195   3.316  1.00 26.45           N  
ANISOU 3084  NH2 ARG A 410     3201   3293   3556    -20    -40    156       N  
ATOM   3085  N   TYR A 411     130.404 103.136  -1.577  1.00 27.76           N  
ANISOU 3085  N   TYR A 411     3426   3430   3693    -54    -23    201       N  
ATOM   3086  CA  TYR A 411     130.834 104.245  -2.435  1.00 27.91           C  
ANISOU 3086  CA  TYR A 411     3462   3439   3703    -59    -22    206       C  
ATOM   3087  C   TYR A 411     129.624 104.871  -3.100  1.00 32.23           C  
ANISOU 3087  C   TYR A 411     4024   3974   4247    -45    -28    203       C  
ATOM   3088  O   TYR A 411     128.701 104.146  -3.559  1.00 28.95           O  
ANISOU 3088  O   TYR A 411     3603   3562   3834    -31    -33    199       O  
ATOM   3089  CB  TYR A 411     131.787 103.721  -3.478  1.00 28.83           C  
ANISOU 3089  CB  TYR A 411     3575   3562   3816    -64    -16    211       C  
ATOM   3090  CG  TYR A 411     132.402 104.855  -4.234  1.00 28.89           C  
ANISOU 3090  CG  TYR A 411     3601   3561   3814    -73    -13    216       C  
ATOM   3091  CD1 TYR A 411     133.472 105.536  -3.672  1.00 28.37           C  
ANISOU 3091  CD1 TYR A 411     3537   3495   3746    -90     -8    219       C  
ATOM   3092  CD2 TYR A 411     131.862 105.294  -5.481  1.00 27.26           C  
ANISOU 3092  CD2 TYR A 411     3411   3346   3601    -66    -16    219       C  
ATOM   3093  CE1 TYR A 411     133.996 106.633  -4.309  1.00 29.90           C  
ANISOU 3093  CE1 TYR A 411     3750   3680   3931   -100     -4    223       C  
ATOM   3094  CE2 TYR A 411     132.405 106.403  -6.143  1.00 28.16           C  
ANISOU 3094  CE2 TYR A 411     3544   3450   3705    -76    -13    225       C  
ATOM   3095  CZ  TYR A 411     133.487 107.059  -5.543  1.00 28.76           C  
ANISOU 3095  CZ  TYR A 411     3622   3525   3779    -93     -7    227       C  
ATOM   3096  OH  TYR A 411     134.084 108.162  -6.088  1.00 28.93           O  
ANISOU 3096  OH  TYR A 411     3663   3538   3792   -105     -3    232       O  
ATOM   3097  N   GLY A 412     129.630 106.212  -3.185  1.00 35.48           N  
ANISOU 3097  N   GLY A 412     4454   4372   4654    -48    -30    205       N  
ATOM   3098  CA  GLY A 412     128.621 106.919  -4.000  1.00 36.96           C  
ANISOU 3098  CA  GLY A 412     4658   4546   4837    -35    -37    204       C  
ATOM   3099  C   GLY A 412     127.214 106.632  -3.491  1.00 41.24           C  
ANISOU 3099  C   GLY A 412     5193   5089   5386    -19    -45    194       C  
ATOM   3100  O   GLY A 412     126.985 106.614  -2.288  1.00 42.10           O  
ANISOU 3100  O   GLY A 412     5294   5201   5502    -21    -44    188       O  
ATOM   3101  N   ASN A 413     126.266 106.401  -4.384  1.00 43.40           N  
ANISOU 3101  N   ASN A 413     5470   5361   5659     -3    -51    192       N  
ATOM   3102  CA  ASN A 413     124.870 106.282  -3.957  1.00 46.33           C  
ANISOU 3102  CA  ASN A 413     5836   5732   6035     12    -58    181       C  
ATOM   3103  C   ASN A 413     124.570 104.819  -3.931  1.00 44.79           C  
ANISOU 3103  C   ASN A 413     5621   5552   5845     16    -56    177       C  
ATOM   3104  O   ASN A 413     123.883 104.320  -4.790  1.00 42.64           O  
ANISOU 3104  O   ASN A 413     5347   5282   5571     27    -60    175       O  
ATOM   3105  CB  ASN A 413     123.918 107.040  -4.911  1.00 48.65           C  
ANISOU 3105  CB  ASN A 413     6146   6015   6326     28    -68    181       C  
ATOM   3106  N   GLU A 414     125.142 104.124  -2.937  1.00 44.89           N  
ANISOU 3106  N   GLU A 414     5619   5574   5862      5    -50    177       N  
ATOM   3107  CA  GLU A 414     125.177 102.658  -2.929  1.00 41.52           C  
ANISOU 3107  CA  GLU A 414     5175   5161   5441      5    -47    176       C  
ATOM   3108  C   GLU A 414     125.639 102.089  -4.260  1.00 37.56           C  
ANISOU 3108  C   GLU A 414     4674   4662   4934      7    -45    181       C  
ATOM   3109  O   GLU A 414     125.195 101.020  -4.658  1.00 34.84           O  
ANISOU 3109  O   GLU A 414     4319   4326   4593     13    -45    178       O  
ATOM   3110  CB  GLU A 414     123.805 102.051  -2.550  1.00 41.49           C  
ANISOU 3110  CB  GLU A 414     5161   5161   5442     17    -52    165       C  
ATOM   3111  CG  GLU A 414     123.316 102.447  -1.187  1.00 39.50           C  
ANISOU 3111  CG  GLU A 414     4905   4908   5193     15    -53    157       C  
ATOM   3112  CD  GLU A 414     121.974 101.819  -0.868  1.00 40.46           C  
ANISOU 3112  CD  GLU A 414     5017   5037   5321     25    -56    146       C  
ATOM   3113  OE1 GLU A 414     120.968 102.414  -1.317  1.00 38.59           O  
ANISOU 3113  OE1 GLU A 414     4786   4795   5082     39    -63    139       O  
ATOM   3114  OE2 GLU A 414     121.912 100.751  -0.175  1.00 37.77           O  
ANISOU 3114  OE2 GLU A 414     4661   4706   4983     21    -53    143       O  
ATOM   3115  N   ALA A 415     126.596 102.776  -4.905  1.00 37.10           N  
ANISOU 3115  N   ALA A 415     4628   4599   4869     -1    -42    190       N  
ATOM   3116  CA  ALA A 415     127.148 102.322  -6.187  1.00 36.21           C  
ANISOU 3116  CA  ALA A 415     4517   4490   4751     -3    -39    195       C  
ATOM   3117  C   ALA A 415     127.956 101.016  -5.989  1.00 35.38           C  
ANISOU 3117  C   ALA A 415     4394   4398   4652    -10    -32    195       C  
ATOM   3118  O   ALA A 415     127.978 100.185  -6.870  1.00 39.14           O  
ANISOU 3118  O   ALA A 415     4864   4880   5127     -6    -30    195       O  
ATOM   3119  CB  ALA A 415     127.978 103.446  -6.864  1.00 33.56           C  
ANISOU 3119  CB  ALA A 415     4200   4146   4406    -12    -36    203       C  
ATOM   3120  N   MET A 416     128.600 100.859  -4.829  1.00 34.34           N  
ANISOU 3120  N   MET A 416     4252   4269   4525    -19    -28    196       N  
ATOM   3121  CA AMET A 416     129.401  99.656  -4.500  0.50 31.92           C  
ANISOU 3121  CA AMET A 416     3929   3974   4225    -25    -23    198       C  
ATOM   3122  CA BMET A 416     129.408  99.681  -4.494  0.50 34.04           C  
ANISOU 3122  CA BMET A 416     4198   4243   4493    -25    -23    198       C  
ATOM   3123  C   MET A 416     129.392  99.502  -2.969  1.00 31.84           C  
ANISOU 3123  C   MET A 416     3909   3966   4221    -29    -24    196       C  
ATOM   3124  O   MET A 416     129.559 100.483  -2.225  1.00 29.63           O  
ANISOU 3124  O   MET A 416     3637   3682   3939    -36    -25    197       O  
ATOM   3125  CB AMET A 416     130.854  99.736  -5.052  0.50 30.28           C  
ANISOU 3125  CB AMET A 416     3721   3770   4013    -37    -16    204       C  
ATOM   3126  CB BMET A 416     130.847  99.885  -4.980  0.50 35.19           C  
ANISOU 3126  CB BMET A 416     4345   4392   4635    -37    -16    204       C  
ATOM   3127  CG AMET A 416     131.652  98.429  -4.908  0.50 30.39           C  
ANISOU 3127  CG AMET A 416     3717   3795   4035    -40    -12    204       C  
ATOM   3128  CG BMET A 416     131.622  98.599  -5.154  0.50 37.78           C  
ANISOU 3128  CG BMET A 416     4656   4730   4968    -40    -12    204       C  
ATOM   3129  SD AMET A 416     133.316  98.261  -5.647  0.50 28.47           S  
ANISOU 3129  SD AMET A 416     3469   3560   3788    -52     -3    208       S  
ATOM   3130  SD BMET A 416     131.150  97.736  -6.672  0.50 41.37           S  
ANISOU 3130  SD BMET A 416     5109   5188   5421    -29    -11    201       S  
ATOM   3131  CE AMET A 416     133.000  97.861  -7.352  0.50 29.74           C  
ANISOU 3131  CE AMET A 416     3635   3722   3944    -45     -1    206       C  
ATOM   3132  CE BMET A 416     131.646  99.012  -7.853  0.50 38.47           C  
ANISOU 3132  CE BMET A 416     4761   4815   5040    -36     -8    206       C  
ATOM   3133  N   THR A 417     129.224  98.272  -2.506  1.00 28.14           N  
ANISOU 3133  N   THR A 417     3427   3506   3761    -27    -24    194       N  
ATOM   3134  CA  THR A 417     129.107  97.980  -1.091  1.00 26.98           C  
ANISOU 3134  CA  THR A 417     3271   3362   3618    -31    -25    193       C  
ATOM   3135  C   THR A 417     129.939  96.758  -0.701  1.00 26.63           C  
ANISOU 3135  C   THR A 417     3211   3326   3580    -35    -22    197       C  
ATOM   3136  O   THR A 417     129.693  95.654  -1.200  1.00 26.43           O  
ANISOU 3136  O   THR A 417     3179   3304   3560    -29    -22    195       O  
ATOM   3137  CB  THR A 417     127.640  97.740  -0.731  1.00 26.35           C  
ANISOU 3137  CB  THR A 417     3190   3280   3541    -21    -30    185       C  
ATOM   3138  OG1 THR A 417     126.900  98.922  -1.050  1.00 27.43           O  
ANISOU 3138  OG1 THR A 417     3340   3409   3672    -16    -33    181       O  
ATOM   3139  CG2 THR A 417     127.468  97.488   0.749  1.00 26.83           C  
ANISOU 3139  CG2 THR A 417     3243   3345   3605    -27    -30    183       C  
ATOM   3140  N   LEU A 418     130.872  96.961   0.235  1.00 25.68           N  
ANISOU 3140  N   LEU A 418     3087   3210   3461    -46    -21    201       N  
ATOM   3141  CA  LEU A 418     131.748  95.914   0.754  1.00 25.11           C  
ANISOU 3141  CA  LEU A 418     3001   3145   3394    -50    -20    205       C  
ATOM   3142  C   LEU A 418     131.292  95.644   2.199  1.00 24.36           C  
ANISOU 3142  C   LEU A 418     2901   3053   3302    -53    -24    205       C  
ATOM   3143  O   LEU A 418     131.216  96.571   2.996  1.00 23.28           O  
ANISOU 3143  O   LEU A 418     2769   2915   3161    -59    -25    204       O  
ATOM   3144  CB  LEU A 418     133.182  96.413   0.704  1.00 26.05           C  
ANISOU 3144  CB  LEU A 418     3119   3268   3510    -61    -17    210       C  
ATOM   3145  CG  LEU A 418     134.190  95.500   1.388  1.00 28.05           C  
ANISOU 3145  CG  LEU A 418     3357   3530   3770    -65    -17    215       C  
ATOM   3146  CD1 LEU A 418     134.360  94.148   0.700  1.00 29.00           C  
ANISOU 3146  CD1 LEU A 418     3468   3654   3898    -57    -16    215       C  
ATOM   3147  CD2 LEU A 418     135.524  96.227   1.431  1.00 30.13           C  
ANISOU 3147  CD2 LEU A 418     3620   3798   4029    -77    -14    218       C  
ATOM   3148  N   VAL A 419     131.005  94.389   2.518  1.00 22.64           N  
ANISOU 3148  N   VAL A 419     2673   2838   3090    -49    -25    206       N  
ATOM   3149  CA  VAL A 419     130.627  93.984   3.860  1.00 24.12           C  
ANISOU 3149  CA  VAL A 419     2857   3029   3280    -53    -28    207       C  
ATOM   3150  C   VAL A 419     131.711  93.048   4.447  1.00 23.74           C  
ANISOU 3150  C   VAL A 419     2796   2987   3236    -57    -29    215       C  
ATOM   3151  O   VAL A 419     131.922  91.961   3.926  1.00 23.15           O  
ANISOU 3151  O   VAL A 419     2716   2913   3169    -51    -29    216       O  
ATOM   3152  CB  VAL A 419     129.291  93.229   3.806  1.00 23.16           C  
ANISOU 3152  CB  VAL A 419     2734   2906   3161    -45    -29    201       C  
ATOM   3153  CG1 VAL A 419     128.833  92.883   5.178  1.00 23.92           C  
ANISOU 3153  CG1 VAL A 419     2826   3005   3257    -51    -32    201       C  
ATOM   3154  CG2 VAL A 419     128.217  94.081   3.147  1.00 24.63           C  
ANISOU 3154  CG2 VAL A 419     2930   3086   3343    -39    -29    192       C  
ATOM   3155  N   TYR A 420     132.345  93.462   5.544  1.00 25.00           N  
ANISOU 3155  N   TYR A 420     2954   3152   3393    -67    -31    219       N  
ATOM   3156  CA  TYR A 420     133.501  92.731   6.122  1.00 25.27           C  
ANISOU 3156  CA  TYR A 420     2977   3192   3430    -71    -34    227       C  
ATOM   3157  C   TYR A 420     133.101  92.283   7.514  1.00 26.53           C  
ANISOU 3157  C   TYR A 420     3135   3357   3590    -76    -38    230       C  
ATOM   3158  O   TYR A 420     132.685  93.099   8.378  1.00 26.13           O  
ANISOU 3158  O   TYR A 420     3089   3307   3532    -84    -39    228       O  
ATOM   3159  CB  TYR A 420     134.723  93.629   6.097  1.00 25.31           C  
ANISOU 3159  CB  TYR A 420     2982   3202   3432    -80    -32    229       C  
ATOM   3160  CG  TYR A 420     135.986  93.077   6.675  1.00 25.15           C  
ANISOU 3160  CG  TYR A 420     2950   3191   3415    -84    -35    236       C  
ATOM   3161  CD1 TYR A 420     136.409  91.771   6.444  1.00 25.36           C  
ANISOU 3161  CD1 TYR A 420     2967   3219   3450    -76    -37    240       C  
ATOM   3162  CD2 TYR A 420     136.826  93.913   7.425  1.00 25.58           C  
ANISOU 3162  CD2 TYR A 420     3003   3252   3463    -95    -36    238       C  
ATOM   3163  CE1 TYR A 420     137.625  91.306   7.002  1.00 25.41           C  
ANISOU 3163  CE1 TYR A 420     2961   3233   3460    -79    -42    246       C  
ATOM   3164  CE2 TYR A 420     137.997  93.444   7.972  1.00 26.12           C  
ANISOU 3164  CE2 TYR A 420     3060   3330   3534    -99    -40    244       C  
ATOM   3165  CZ  TYR A 420     138.403  92.149   7.763  1.00 25.31           C  
ANISOU 3165  CZ  TYR A 420     2947   3229   3441    -90    -43    248       C  
ATOM   3166  OH  TYR A 420     139.598  91.749   8.372  1.00 25.12           O  
ANISOU 3166  OH  TYR A 420     2911   3214   3419    -93    -48    254       O  
ATOM   3167  N   LYS A 421     133.128  90.967   7.716  1.00 26.53           N  
ANISOU 3167  N   LYS A 421     3128   3357   3597    -72    -41    235       N  
ATOM   3168  CA  LYS A 421     132.615  90.388   8.939  1.00 28.45           C  
ANISOU 3168  CA  LYS A 421     3370   3602   3838    -77    -45    239       C  
ATOM   3169  C   LYS A 421     133.775  89.861   9.846  1.00 27.87           C  
ANISOU 3169  C   LYS A 421     3288   3535   3766    -82    -51    250       C  
ATOM   3170  O   LYS A 421     134.398  88.865   9.526  1.00 27.38           O  
ANISOU 3170  O   LYS A 421     3220   3473   3712    -75    -54    255       O  
ATOM   3171  CB  LYS A 421     131.624  89.277   8.561  1.00 29.55           C  
ANISOU 3171  CB  LYS A 421     3510   3735   3983    -69    -45    237       C  
ATOM   3172  CG  LYS A 421     130.892  88.647   9.750  1.00 30.93           C  
ANISOU 3172  CG  LYS A 421     3685   3912   4156    -75    -48    240       C  
ATOM   3173  CD  LYS A 421     129.934  87.552   9.275  1.00 32.55           C  
ANISOU 3173  CD  LYS A 421     3891   4110   4368    -68    -46    237       C  
ATOM   3174  CE  LYS A 421     129.073  87.000  10.407  1.00 33.71           C  
ANISOU 3174  CE  LYS A 421     4040   4259   4511    -76    -48    238       C  
ATOM   3175  NZ  LYS A 421     129.807  85.914  11.092  1.00 32.60           N  
ANISOU 3175  NZ  LYS A 421     3895   4118   4374    -78    -53    251       N  
ATOM   3176  N   TYR A 422     134.031  90.565  10.951  1.00 27.96           N  
ANISOU 3176  N   TYR A 422     3300   3554   3769    -93    -54    252       N  
ATOM   3177  CA  TYR A 422     135.088  90.226  11.935  1.00 28.64           C  
ANISOU 3177  CA  TYR A 422     3380   3649   3855    -99    -60    262       C  
ATOM   3178  C   TYR A 422     134.383  90.132  13.322  1.00 27.74           C  
ANISOU 3178  C   TYR A 422     3269   3539   3732   -108    -64    264       C  
ATOM   3179  O   TYR A 422     134.795  90.682  14.312  1.00 26.92           O  
ANISOU 3179  O   TYR A 422     3164   3444   3621   -118    -67    267       O  
ATOM   3180  CB  TYR A 422     136.288  91.208  11.880  1.00 30.02           C  
ANISOU 3180  CB  TYR A 422     3551   3831   4026   -105    -60    261       C  
ATOM   3181  CG  TYR A 422     135.870  92.635  11.976  1.00 30.63           C  
ANISOU 3181  CG  TYR A 422     3636   3909   4094   -113    -55    253       C  
ATOM   3182  CD1 TYR A 422     135.431  93.311  10.845  1.00 31.61           C  
ANISOU 3182  CD1 TYR A 422     3767   4025   4219   -108    -48    245       C  
ATOM   3183  CD2 TYR A 422     135.798  93.292  13.211  1.00 30.77           C  
ANISOU 3183  CD2 TYR A 422     3655   3933   4103   -125    -57    253       C  
ATOM   3184  CE1 TYR A 422     134.979  94.632  10.924  1.00 31.27           C  
ANISOU 3184  CE1 TYR A 422     3732   3979   4168   -114    -45    237       C  
ATOM   3185  CE2 TYR A 422     135.351  94.597  13.300  1.00 32.09           C  
ANISOU 3185  CE2 TYR A 422     3831   4099   4263   -131    -52    244       C  
ATOM   3186  CZ  TYR A 422     134.934  95.254  12.135  1.00 33.11           C  
ANISOU 3186  CZ  TYR A 422     3967   4218   4394   -125    -46    236       C  
ATOM   3187  OH  TYR A 422     134.496  96.558  12.143  1.00 35.16           O  
ANISOU 3187  OH  TYR A 422     4236   4475   4648   -130    -42    228       O  
ATOM   3188  N   ALA A 423     133.276  89.390  13.356  1.00 26.76           N  
ANISOU 3188  N   ALA A 423     3148   3409   3610   -105    -63    263       N  
ATOM   3189  CA  ALA A 423     132.385  89.397  14.486  1.00 27.46           C  
ANISOU 3189  CA  ALA A 423     3241   3501   3691   -115    -64    263       C  
ATOM   3190  C   ALA A 423     132.669  88.253  15.479  1.00 26.05           C  
ANISOU 3190  C   ALA A 423     3060   3326   3512   -118    -71    275       C  
ATOM   3191  O   ALA A 423     133.603  87.442  15.303  1.00 25.85           O  
ANISOU 3191  O   ALA A 423     3030   3300   3494   -112    -77    285       O  
ATOM   3192  CB  ALA A 423     130.930  89.310  13.988  1.00 28.59           C  
ANISOU 3192  CB  ALA A 423     3390   3638   3835   -111    -58    253       C  
ATOM   3193  N   ALA A 424     131.876  88.241  16.539  1.00 23.47           N  
ANISOU 3193  N   ALA A 424     2738   3004   3176   -129    -72    275       N  
ATOM   3194  CA  ALA A 424     131.836  87.119  17.470  1.00 25.67           C  
ANISOU 3194  CA  ALA A 424     3017   3284   3453   -134    -78    287       C  
ATOM   3195  C   ALA A 424     131.086  85.921  16.820  1.00 25.88           C  
ANISOU 3195  C   ALA A 424     3047   3299   3489   -126    -76    288       C  
ATOM   3196  O   ALA A 424     130.749  85.984  15.619  1.00 28.57           O  
ANISOU 3196  O   ALA A 424     3386   3631   3837   -116    -70    279       O  
ATOM   3197  CB  ALA A 424     131.196  87.561  18.776  1.00 25.34           C  
ANISOU 3197  CB  ALA A 424     2979   3251   3397   -150    -77    285       C  
ATOM   3198  N   GLN A 425     130.847  84.842  17.567  1.00 25.31           N  
ANISOU 3198  N   GLN A 425     2977   3225   3415   -130    -80    298       N  
ATOM   3199  CA  GLN A 425     130.361  83.596  16.956  1.00 25.49           C  
ANISOU 3199  CA  GLN A 425     3002   3236   3448   -123    -79    300       C  
ATOM   3200  C   GLN A 425     128.940  83.748  16.345  1.00 26.11           C  
ANISOU 3200  C   GLN A 425     3084   3309   3526   -122    -69    285       C  
ATOM   3201  O   GLN A 425     128.663  83.197  15.291  1.00 27.09           O  
ANISOU 3201  O   GLN A 425     3208   3425   3661   -112    -66    280       O  
ATOM   3202  CB  GLN A 425     130.349  82.484  18.010  1.00 27.30           C  
ANISOU 3202  CB  GLN A 425     3236   3464   3674   -130    -86    314       C  
ATOM   3203  CG  GLN A 425     129.870  81.144  17.507  1.00 26.83           C  
ANISOU 3203  CG  GLN A 425     3180   3391   3625   -124    -85    317       C  
ATOM   3204  CD  GLN A 425     130.784  80.556  16.473  1.00 27.50           C  
ANISOU 3204  CD  GLN A 425     3259   3466   3725   -108    -88    321       C  
ATOM   3205  OE1 GLN A 425     131.999  80.832  16.437  1.00 28.16           O  
ANISOU 3205  OE1 GLN A 425     3336   3553   3811   -102    -94    326       O  
ATOM   3206  NE2 GLN A 425     130.213  79.689  15.618  1.00 28.61           N  
ANISOU 3206  NE2 GLN A 425     3402   3594   3876   -100    -84    316       N  
ATOM   3207  N   GLY A 426     128.075  84.500  17.015  1.00 25.85           N  
ANISOU 3207  N   GLY A 426     3055   3285   3483   -134    -65    276       N  
ATOM   3208  CA  GLY A 426     126.725  84.777  16.547  1.00 27.03           C  
ANISOU 3208  CA  GLY A 426     3206   3433   3632   -134    -57    261       C  
ATOM   3209  C   GLY A 426     125.654  83.827  17.089  1.00 28.19           C  
ANISOU 3209  C   GLY A 426     3358   3579   3776   -143    -54    261       C  
ATOM   3210  O   GLY A 426     124.523  83.769  16.560  1.00 27.66           O  
ANISOU 3210  O   GLY A 426     3291   3509   3710   -141    -48    248       O  
ATOM   3211  N   LEU A 427     125.985  83.132  18.176  1.00 28.06           N  
ANISOU 3211  N   LEU A 427     3344   3564   3753   -153    -60    274       N  
ATOM   3212  CA  LEU A 427     125.082  82.153  18.784  1.00 28.74           C  
ANISOU 3212  CA  LEU A 427     3436   3648   3835   -164    -58    277       C  
ATOM   3213  C   LEU A 427     124.879  81.010  17.815  1.00 28.56           C  
ANISOU 3213  C   LEU A 427     3415   3612   3826   -154    -56    278       C  
ATOM   3214  O   LEU A 427     125.737  80.778  16.931  1.00 27.66           O  
ANISOU 3214  O   LEU A 427     3296   3489   3723   -139    -60    282       O  
ATOM   3215  CB  LEU A 427     123.776  82.827  19.287  1.00 29.01           C  
ANISOU 3215  CB  LEU A 427     3471   3693   3858   -176    -50    261       C  
ATOM   3216  CG  LEU A 427     124.016  83.926  20.336  1.00 31.86           C  
ANISOU 3216  CG  LEU A 427     3832   4068   4207   -187    -51    259       C  
ATOM   3217  CD1 LEU A 427     122.681  84.492  20.757  1.00 32.95           C  
ANISOU 3217  CD1 LEU A 427     3969   4214   4335   -198    -42    242       C  
ATOM   3218  CD2 LEU A 427     124.747  83.465  21.592  1.00 32.26           C  
ANISOU 3218  CD2 LEU A 427     3886   4124   4248   -199    -59    277       C  
ATOM   3219  N   SER A 428     123.784  80.269  17.958  1.00 28.82           N  
ANISOU 3219  N   SER A 428     3451   3641   3857   -161    -51    273       N  
ATOM   3220  CA  SER A 428     123.664  78.939  17.297  1.00 33.23           C  
ANISOU 3220  CA  SER A 428     4012   4185   4427   -155    -51    278       C  
ATOM   3221  C   SER A 428     123.716  78.994  15.760  1.00 32.31           C  
ANISOU 3221  C   SER A 428     3890   4061   4324   -138    -47    268       C  
ATOM   3222  O   SER A 428     124.258  78.117  15.140  1.00 31.13           O  
ANISOU 3222  O   SER A 428     3741   3901   4186   -128    -50    275       O  
ATOM   3223  CB  SER A 428     122.309  78.306  17.699  1.00 36.20           C  
ANISOU 3223  CB  SER A 428     4394   4562   4798   -169    -43    271       C  
ATOM   3224  OG  SER A 428     122.085  78.480  19.106  1.00 39.88           O  
ANISOU 3224  OG  SER A 428     4865   5038   5248   -188    -44    277       O  
ATOM   3225  N   HIS A 429     123.188  80.077  15.183  1.00 31.33           N  
ANISOU 3225  N   HIS A 429     3761   3944   4197   -134    -42    252       N  
ATOM   3226  CA  HIS A 429     123.133  80.222  13.752  1.00 33.43           C  
ANISOU 3226  CA  HIS A 429     4023   4205   4474   -118    -39    242       C  
ATOM   3227  C   HIS A 429     124.373  80.831  13.131  1.00 28.91           C  
ANISOU 3227  C   HIS A 429     3446   3632   3907   -106    -43    246       C  
ATOM   3228  O   HIS A 429     124.386  81.037  11.918  1.00 29.14           O  
ANISOU 3228  O   HIS A 429     3472   3657   3943    -94    -40    238       O  
ATOM   3229  CB  HIS A 429     121.904  81.055  13.359  1.00 35.13           C  
ANISOU 3229  CB  HIS A 429     4236   4427   4684   -119    -32    222       C  
ATOM   3230  CG  HIS A 429     120.627  80.435  13.788  1.00 39.57           C  
ANISOU 3230  CG  HIS A 429     4800   4992   5243   -130    -26    214       C  
ATOM   3231  ND1 HIS A 429     120.277  79.161  13.418  1.00 45.76           N  
ANISOU 3231  ND1 HIS A 429     5587   5766   6034   -131    -24    216       N  
ATOM   3232  CD2 HIS A 429     119.641  80.878  14.600  1.00 43.99           C  
ANISOU 3232  CD2 HIS A 429     5361   5562   5792   -143    -22    205       C  
ATOM   3233  CE1 HIS A 429     119.111  78.849  13.957  1.00 45.72           C  
ANISOU 3233  CE1 HIS A 429     5583   5766   6022   -144    -18    208       C  
ATOM   3234  NE2 HIS A 429     118.701  79.874  14.677  1.00 45.95           N  
ANISOU 3234  NE2 HIS A 429     5611   5807   6040   -151    -17    200       N  
ATOM   3235  N   GLY A 430     125.365  81.163  13.943  1.00 26.06           N  
ANISOU 3235  N   GLY A 430     3085   3275   3542   -110    -50    258       N  
ATOM   3236  CA  GLY A 430     126.587  81.723  13.425  1.00 26.10           C  
ANISOU 3236  CA  GLY A 430     3086   3281   3551   -100    -53    262       C  
ATOM   3237  C   GLY A 430     127.403  80.796  12.565  1.00 26.33           C  
ANISOU 3237  C   GLY A 430     3112   3300   3594    -88    -56    268       C  
ATOM   3238  O   GLY A 430     127.419  79.580  12.798  1.00 29.41           O  
ANISOU 3238  O   GLY A 430     3504   3681   3989    -88    -59    277       O  
ATOM   3239  N   HIS A 431     128.146  81.343  11.631  1.00 25.26           N  
ANISOU 3239  N   HIS A 431     2970   3163   3462    -77    -56    265       N  
ATOM   3240  CA  HIS A 431     129.011  80.587  10.734  1.00 26.01           C  
ANISOU 3240  CA  HIS A 431     3061   3251   3571    -65    -58    269       C  
ATOM   3241  C   HIS A 431     130.508  80.662  11.152  1.00 26.16           C  
ANISOU 3241  C   HIS A 431     3075   3273   3592    -63    -65    281       C  
ATOM   3242  O   HIS A 431     130.874  81.534  11.869  1.00 24.49           O  
ANISOU 3242  O   HIS A 431     2863   3071   3371    -70    -68    284       O  
ATOM   3243  CB  HIS A 431     128.773  81.053   9.292  1.00 25.79           C  
ANISOU 3243  CB  HIS A 431     3031   3222   3547    -55    -51    255       C  
ATOM   3244  CG  HIS A 431     127.423  80.684   8.767  1.00 26.90           C  
ANISOU 3244  CG  HIS A 431     3174   3358   3688    -55    -45    244       C  
ATOM   3245  ND1 HIS A 431     127.006  81.005   7.510  1.00 27.92           N  
ANISOU 3245  ND1 HIS A 431     3301   3486   3819    -47    -39    232       N  
ATOM   3246  CD2 HIS A 431     126.396  80.019   9.340  1.00 26.62           C  
ANISOU 3246  CD2 HIS A 431     3144   3321   3651    -63    -43    243       C  
ATOM   3247  CE1 HIS A 431     125.792  80.549   7.324  1.00 28.84           C  
ANISOU 3247  CE1 HIS A 431     3421   3600   3936    -49    -35    224       C  
ATOM   3248  NE2 HIS A 431     125.397  79.959   8.422  1.00 27.56           N  
ANISOU 3248  NE2 HIS A 431     3263   3438   3772    -59    -37    230       N  
ATOM   3249  N   TYR A 432     131.330  79.726  10.695  1.00 26.12           N  
ANISOU 3249  N   TYR A 432     3065   3260   3598    -53    -69    286       N  
ATOM   3250  CA  TYR A 432     132.772  79.627  11.004  1.00 26.86           C  
ANISOU 3250  CA  TYR A 432     3152   3357   3697    -48    -77    297       C  
ATOM   3251  C   TYR A 432     133.455  80.386   9.904  1.00 26.49           C  
ANISOU 3251  C   TYR A 432     3097   3314   3652    -41    -73    288       C  
ATOM   3252  O   TYR A 432     133.978  79.853   8.990  1.00 26.98           O  
ANISOU 3252  O   TYR A 432     3154   3371   3725    -31    -72    285       O  
ATOM   3253  CB  TYR A 432     133.172  78.158  11.089  1.00 27.57           C  
ANISOU 3253  CB  TYR A 432     3242   3436   3799    -41    -83    306       C  
ATOM   3254  CG  TYR A 432     132.487  77.494  12.239  1.00 28.87           C  
ANISOU 3254  CG  TYR A 432     3415   3596   3958    -51    -87    316       C  
ATOM   3255  CD1 TYR A 432     132.992  77.597  13.511  1.00 31.00           C  
ANISOU 3255  CD1 TYR A 432     3687   3872   4220    -59    -96    329       C  
ATOM   3256  CD2 TYR A 432     131.291  76.843  12.075  1.00 30.46           C  
ANISOU 3256  CD2 TYR A 432     3624   3789   4160    -54    -81    311       C  
ATOM   3257  CE1 TYR A 432     132.356  77.036  14.584  1.00 30.20           C  
ANISOU 3257  CE1 TYR A 432     3595   3768   4112    -69    -99    338       C  
ATOM   3258  CE2 TYR A 432     130.650  76.276  13.140  1.00 29.50           C  
ANISOU 3258  CE2 TYR A 432     3512   3664   4033    -66    -84    320       C  
ATOM   3259  CZ  TYR A 432     131.188  76.383  14.396  1.00 31.22           C  
ANISOU 3259  CZ  TYR A 432     3732   3889   4242    -73    -93    334       C  
ATOM   3260  OH  TYR A 432     130.571  75.846  15.457  1.00 30.38           O  
ANISOU 3260  OH  TYR A 432     3635   3780   4128    -86    -96    342       O  
ATOM   3261  N   ASP A 433     133.420  81.688  10.039  1.00 26.95           N  
ANISOU 3261  N   ASP A 433     3156   3382   3700    -48    -70    283       N  
ATOM   3262  CA  ASP A 433     133.725  82.600   8.921  1.00 27.96           C  
ANISOU 3262  CA  ASP A 433     3281   3514   3828    -43    -64    273       C  
ATOM   3263  C   ASP A 433     134.442  83.905   9.344  1.00 26.87           C  
ANISOU 3263  C   ASP A 433     3141   3387   3681    -50    -65    274       C  
ATOM   3264  O   ASP A 433     134.130  84.966   8.850  1.00 27.20           O  
ANISOU 3264  O   ASP A 433     3187   3432   3717    -53    -59    266       O  
ATOM   3265  CB  ASP A 433     132.415  82.903   8.184  1.00 29.15           C  
ANISOU 3265  CB  ASP A 433     3439   3661   3976    -43    -56    262       C  
ATOM   3266  CG  ASP A 433     131.441  83.709   9.032  1.00 32.52           C  
ANISOU 3266  CG  ASP A 433     3872   4092   4391    -53    -55    259       C  
ATOM   3267  OD1 ASP A 433     131.664  83.921  10.253  1.00 34.67           O  
ANISOU 3267  OD1 ASP A 433     4146   4371   4657    -62    -60    267       O  
ATOM   3268  OD2 ASP A 433     130.445  84.229   8.512  1.00 37.78           O  
ANISOU 3268  OD2 ASP A 433     4544   4758   5054    -53    -50    249       O  
ATOM   3269  N   LYS A 434     135.387  83.816  10.262  1.00 26.21           N  
ANISOU 3269  N   LYS A 434     3053   3309   3596    -54    -73    284       N  
ATOM   3270  CA  LYS A 434     136.118  84.998  10.755  1.00 26.13           C  
ANISOU 3270  CA  LYS A 434     3041   3311   3577    -62    -74    284       C  
ATOM   3271  C   LYS A 434     136.791  85.699   9.587  1.00 24.93           C  
ANISOU 3271  C   LYS A 434     2884   3161   3427    -58    -68    276       C  
ATOM   3272  O   LYS A 434     137.401  85.038   8.778  1.00 23.91           O  
ANISOU 3272  O   LYS A 434     2748   3029   3308    -49    -68    275       O  
ATOM   3273  CB  LYS A 434     137.191  84.624  11.805  1.00 26.51           C  
ANISOU 3273  CB  LYS A 434     3081   3365   3624    -65    -84    296       C  
ATOM   3274  CG  LYS A 434     136.675  83.896  13.036  1.00 26.54           C  
ANISOU 3274  CG  LYS A 434     3091   3368   3625    -70    -91    306       C  
ATOM   3275  CD  LYS A 434     135.566  84.630  13.788  1.00 26.37           C  
ANISOU 3275  CD  LYS A 434     3079   3350   3591    -83    -87    303       C  
ATOM   3276  CE  LYS A 434     134.187  84.191  13.313  1.00 26.29           C  
ANISOU 3276  CE  LYS A 434     3076   3329   3582    -80    -81    296       C  
ATOM   3277  NZ  LYS A 434     133.180  84.627  14.288  1.00 26.57           N  
ANISOU 3277  NZ  LYS A 434     3120   3370   3607    -93    -80    295       N  
ATOM   3278  N   LEU A 435     136.587  87.011   9.483  1.00 24.63           N  
ANISOU 3278  N   LEU A 435     2851   3127   3380    -65    -63    270       N  
ATOM   3279  CA  LEU A 435     137.194  87.865   8.460  1.00 26.06           C  
ANISOU 3279  CA  LEU A 435     3030   3310   3560    -65    -57    263       C  
ATOM   3280  C   LEU A 435     136.707  87.609   7.023  1.00 26.40           C  
ANISOU 3280  C   LEU A 435     3076   3346   3609    -55    -50    255       C  
ATOM   3281  O   LEU A 435     137.338  88.073   6.108  1.00 28.95           O  
ANISOU 3281  O   LEU A 435     3397   3671   3933    -54    -46    251       O  
ATOM   3282  CB  LEU A 435     138.751  87.787   8.513  1.00 26.38           C  
ANISOU 3282  CB  LEU A 435     3059   3360   3605    -65    -61    267       C  
ATOM   3283  CG  LEU A 435     139.407  87.880   9.877  1.00 25.57           C  
ANISOU 3283  CG  LEU A 435     2951   3266   3497    -72    -69    275       C  
ATOM   3284  CD1 LEU A 435     140.923  87.949   9.769  1.00 27.08           C  
ANISOU 3284  CD1 LEU A 435     3129   3467   3691    -72    -71    276       C  
ATOM   3285  CD2 LEU A 435     138.911  89.067  10.665  1.00 24.91           C  
ANISOU 3285  CD2 LEU A 435     2876   3187   3401    -85    -67    273       C  
ATOM   3286  N   SER A 436     135.570  86.915   6.830  1.00 25.20           N  
ANISOU 3286  N   SER A 436     2929   3186   3461    -50    -49    253       N  
ATOM   3287  CA  SER A 436     134.989  86.788   5.513  1.00 24.92           C  
ANISOU 3287  CA  SER A 436     2896   3144   3428    -42    -43    245       C  
ATOM   3288  C   SER A 436     134.416  88.121   5.003  1.00 25.04           C  
ANISOU 3288  C   SER A 436     2921   3160   3434    -46    -38    237       C  
ATOM   3289  O   SER A 436     134.147  89.044   5.783  1.00 23.89           O  
ANISOU 3289  O   SER A 436     2780   3017   3280    -54    -39    238       O  
ATOM   3290  CB  SER A 436     133.896  85.723   5.472  1.00 25.89           C  
ANISOU 3290  CB  SER A 436     3022   3260   3557    -37    -43    243       C  
ATOM   3291  OG  SER A 436     132.864  86.064   6.357  1.00 25.92           O  
ANISOU 3291  OG  SER A 436     3033   3263   3553    -44    -45    243       O  
ATOM   3292  N   PHE A 437     134.297  88.233   3.676  1.00 25.26           N  
ANISOU 3292  N   PHE A 437     2950   3184   3463    -40    -33    231       N  
ATOM   3293  CA  PHE A 437     133.609  89.401   3.103  1.00 26.24           C  
ANISOU 3293  CA  PHE A 437     3084   3306   3578    -42    -29    224       C  
ATOM   3294  C   PHE A 437     132.670  88.989   1.999  1.00 25.70           C  
ANISOU 3294  C   PHE A 437     3019   3232   3512    -33    -26    217       C  
ATOM   3295  O   PHE A 437     132.766  87.887   1.440  1.00 25.91           O  
ANISOU 3295  O   PHE A 437     3040   3258   3547    -26    -25    216       O  
ATOM   3296  CB  PHE A 437     134.607  90.465   2.598  1.00 26.14           C  
ANISOU 3296  CB  PHE A 437     3073   3298   3561    -47    -26    224       C  
ATOM   3297  CG  PHE A 437     135.233  90.111   1.274  1.00 27.98           C  
ANISOU 3297  CG  PHE A 437     3302   3531   3797    -42    -21    221       C  
ATOM   3298  CD1 PHE A 437     136.319  89.219   1.207  1.00 29.41           C  
ANISOU 3298  CD1 PHE A 437     3471   3717   3987    -40    -22    223       C  
ATOM   3299  CD2 PHE A 437     134.737  90.665   0.087  1.00 28.74           C  
ANISOU 3299  CD2 PHE A 437     3406   3624   3888    -39    -17    215       C  
ATOM   3300  CE1 PHE A 437     136.879  88.861  -0.023  1.00 29.98           C  
ANISOU 3300  CE1 PHE A 437     3538   3791   4063    -35    -16    219       C  
ATOM   3301  CE2 PHE A 437     135.293  90.328  -1.145  1.00 30.34           C  
ANISOU 3301  CE2 PHE A 437     3606   3829   4093    -35    -12    212       C  
ATOM   3302  CZ  PHE A 437     136.367  89.410  -1.201  1.00 31.43           C  
ANISOU 3302  CZ  PHE A 437     3730   3971   4240    -34    -11    213       C  
ATOM   3303  N   SER A 438     131.787  89.926   1.667  1.00 25.12           N  
ANISOU 3303  N   SER A 438     2956   3157   3431    -33    -24    212       N  
ATOM   3304  CA  SER A 438     130.963  89.834   0.498  1.00 25.04           C  
ANISOU 3304  CA  SER A 438     2951   3143   3421    -25    -22    204       C  
ATOM   3305  C   SER A 438     130.895  91.206  -0.181  1.00 24.91           C  
ANISOU 3305  C   SER A 438     2944   3125   3395    -26    -20    202       C  
ATOM   3306  O   SER A 438     131.251  92.205   0.429  1.00 25.37           O  
ANISOU 3306  O   SER A 438     3007   3184   3448    -33    -21    204       O  
ATOM   3307  CB  SER A 438     129.589  89.238   0.856  1.00 25.06           C  
ANISOU 3307  CB  SER A 438     2953   3142   3425    -21    -24    199       C  
ATOM   3308  OG  SER A 438     128.845  90.032   1.748  1.00 24.37           O  
ANISOU 3308  OG  SER A 438     2872   3055   3332    -25    -26    198       O  
ATOM   3309  N   LEU A 439     130.560  91.220  -1.471  1.00 24.03           N  
ANISOU 3309  N   LEU A 439     2836   3012   3282    -20    -18    197       N  
ATOM   3310  CA  LEU A 439     130.588  92.421  -2.303  1.00 25.01           C  
ANISOU 3310  CA  LEU A 439     2972   3134   3397    -20    -16    195       C  
ATOM   3311  C   LEU A 439     129.350  92.508  -3.189  1.00 25.05           C  
ANISOU 3311  C   LEU A 439     2983   3136   3398    -11    -17    188       C  
ATOM   3312  O   LEU A 439     128.975  91.518  -3.795  1.00 23.47           O  
ANISOU 3312  O   LEU A 439     2777   2936   3203     -5    -16    184       O  
ATOM   3313  CB  LEU A 439     131.819  92.413  -3.199  1.00 26.53           C  
ANISOU 3313  CB  LEU A 439     3162   3331   3589    -24    -11    198       C  
ATOM   3314  CG  LEU A 439     132.036  93.638  -4.116  1.00 27.57           C  
ANISOU 3314  CG  LEU A 439     3306   3460   3710    -27     -9    198       C  
ATOM   3315  CD1 LEU A 439     132.337  94.880  -3.310  1.00 28.27           C  
ANISOU 3315  CD1 LEU A 439     3403   3546   3793    -36    -10    202       C  
ATOM   3316  CD2 LEU A 439     133.222  93.370  -4.975  1.00 27.41           C  
ANISOU 3316  CD2 LEU A 439     3280   3445   3689    -31     -3    199       C  
ATOM   3317  N   TYR A 440     128.783  93.723  -3.287  1.00 23.98           N  
ANISOU 3317  N   TYR A 440     2860   2996   3256    -10    -20    187       N  
ATOM   3318  CA  TYR A 440     127.512  94.018  -3.937  1.00 23.88           C  
ANISOU 3318  CA  TYR A 440     2855   2981   3239     -1    -23    180       C  
ATOM   3319  C   TYR A 440     127.703  95.301  -4.776  1.00 24.43           C  
ANISOU 3319  C   TYR A 440     2938   3045   3298     -1    -24    182       C  
ATOM   3320  O   TYR A 440     128.519  96.172  -4.416  1.00 24.24           O  
ANISOU 3320  O   TYR A 440     2920   3019   3271    -10    -22    188       O  
ATOM   3321  CB  TYR A 440     126.360  94.246  -2.897  1.00 23.95           C  
ANISOU 3321  CB  TYR A 440     2863   2987   3248      2    -28    175       C  
ATOM   3322  CG  TYR A 440     126.299  93.160  -1.826  1.00 24.13           C  
ANISOU 3322  CG  TYR A 440     2875   3014   3280     -2    -27    175       C  
ATOM   3323  CD1 TYR A 440     127.177  93.170  -0.758  1.00 24.19           C  
ANISOU 3323  CD1 TYR A 440     2878   3023   3289    -11    -26    182       C  
ATOM   3324  CD2 TYR A 440     125.438  92.076  -1.951  1.00 24.17           C  
ANISOU 3324  CD2 TYR A 440     2872   3021   3289      4    -27    169       C  
ATOM   3325  CE1 TYR A 440     127.175  92.171   0.199  1.00 25.46           C  
ANISOU 3325  CE1 TYR A 440     3030   3188   3457    -15    -26    183       C  
ATOM   3326  CE2 TYR A 440     125.431  91.049  -1.012  1.00 25.23           C  
ANISOU 3326  CE2 TYR A 440     2998   3158   3431      0    -26    170       C  
ATOM   3327  CZ  TYR A 440     126.284  91.103   0.084  1.00 26.08           C  
ANISOU 3327  CZ  TYR A 440     3103   3267   3540     -9    -26    178       C  
ATOM   3328  OH  TYR A 440     126.329  90.093   1.048  1.00 26.20           O  
ANISOU 3328  OH  TYR A 440     3111   3284   3561    -14    -26    181       O  
ATOM   3329  N   GLU A 441     126.992  95.386  -5.892  1.00 24.06           N  
ANISOU 3329  N   GLU A 441     2898   2997   3248      7    -26    178       N  
ATOM   3330  CA  GLU A 441     126.906  96.587  -6.706  1.00 26.20           C  
ANISOU 3330  CA  GLU A 441     3184   3262   3508      9    -28    181       C  
ATOM   3331  C   GLU A 441     125.434  96.862  -7.011  1.00 26.85           C  
ANISOU 3331  C   GLU A 441     3272   3342   3588     22    -35    173       C  
ATOM   3332  O   GLU A 441     124.791  96.092  -7.688  1.00 28.03           O  
ANISOU 3332  O   GLU A 441     3417   3496   3739     29    -36    168       O  
ATOM   3333  CB  GLU A 441     127.710  96.451  -8.008  1.00 26.89           C  
ANISOU 3333  CB  GLU A 441     3275   3353   3590      6    -23    184       C  
ATOM   3334  CG  GLU A 441     127.578  97.659  -8.963  1.00 27.75           C  
ANISOU 3334  CG  GLU A 441     3401   3455   3686      7    -26    187       C  
ATOM   3335  CD  GLU A 441     128.730  97.843  -9.993  1.00 28.44           C  
ANISOU 3335  CD  GLU A 441     3494   3545   3766     -2    -20    193       C  
ATOM   3336  OE1 GLU A 441     128.844  98.988 -10.478  1.00 28.62           O  
ANISOU 3336  OE1 GLU A 441     3534   3561   3779     -5    -21    198       O  
ATOM   3337  OE2 GLU A 441     129.476  96.887 -10.336  1.00 26.58           O  
ANISOU 3337  OE2 GLU A 441     3248   3318   3534     -6    -13    192       O  
ATOM   3338  N   LYS A 442     124.902  97.958  -6.494  1.00 29.26           N  
ANISOU 3338  N   LYS A 442     3588   3640   3891     24    -40    173       N  
ATOM   3339  CA  LYS A 442     123.493  98.405  -6.775  1.00 31.02           C  
ANISOU 3339  CA  LYS A 442     3816   3859   4112     37    -48    165       C  
ATOM   3340  C   LYS A 442     122.464  97.264  -6.675  1.00 29.37           C  
ANISOU 3340  C   LYS A 442     3593   3658   3908     45    -49    155       C  
ATOM   3341  O   LYS A 442     121.700  97.061  -7.584  1.00 30.97           O  
ANISOU 3341  O   LYS A 442     3796   3863   4108     55    -53    150       O  
ATOM   3342  CB  LYS A 442     123.361  99.035  -8.177  1.00 32.13           C  
ANISOU 3342  CB  LYS A 442     3970   3995   4242     44    -52    168       C  
ATOM   3343  CG  LYS A 442     124.262 100.233  -8.380  1.00 38.80           C  
ANISOU 3343  CG  LYS A 442     4832   4832   5080     36    -51    178       C  
ATOM   3344  CD  LYS A 442     123.587 101.351  -9.165  1.00 43.53           C  
ANISOU 3344  CD  LYS A 442     5449   5421   5670     45    -59    179       C  
ATOM   3345  CE  LYS A 442     124.358 102.651  -9.103  1.00 49.78           C  
ANISOU 3345  CE  LYS A 442     6257   6201   6456     37    -59    188       C  
ATOM   3346  NZ  LYS A 442     124.811 103.075 -10.451  1.00 53.88           N  
ANISOU 3346  NZ  LYS A 442     6792   6718   6964     35    -59    196       N  
ATOM   3347  N   GLY A 443     122.550  96.449  -5.651  1.00 28.13           N  
ANISOU 3347  N   GLY A 443     3424   3506   3760     40    -46    153       N  
ATOM   3348  CA  GLY A 443     121.559  95.374  -5.444  1.00 26.88           C  
ANISOU 3348  CA  GLY A 443     3253   3354   3607     45    -46    143       C  
ATOM   3349  C   GLY A 443     121.959  94.049  -6.046  1.00 27.36           C  
ANISOU 3349  C   GLY A 443     3304   3420   3671     43    -41    144       C  
ATOM   3350  O   GLY A 443     121.227  93.082  -5.927  1.00 27.77           O  
ANISOU 3350  O   GLY A 443     3346   3477   3728     46    -40    136       O  
ATOM   3351  N   THR A 444     123.123  93.978  -6.684  1.00 27.25           N  
ANISOU 3351  N   THR A 444     3292   3406   3655     38    -37    152       N  
ATOM   3352  CA  THR A 444     123.578  92.729  -7.284  1.00 26.11           C  
ANISOU 3352  CA  THR A 444     3138   3267   3515     37    -31    151       C  
ATOM   3353  C   THR A 444     124.747  92.204  -6.478  1.00 26.52           C  
ANISOU 3353  C   THR A 444     3183   3320   3574     27    -26    158       C  
ATOM   3354  O   THR A 444     125.736  92.900  -6.222  1.00 23.90           O  
ANISOU 3354  O   THR A 444     2856   2985   3239     19    -25    166       O  
ATOM   3355  CB  THR A 444     124.031  92.968  -8.733  1.00 26.08           C  
ANISOU 3355  CB  THR A 444     3141   3264   3503     39    -30    153       C  
ATOM   3356  OG1 THR A 444     122.943  93.530  -9.466  1.00 27.96           O  
ANISOU 3356  OG1 THR A 444     3387   3501   3734     49    -37    148       O  
ATOM   3357  CG2 THR A 444     124.382  91.687  -9.421  1.00 25.26           C  
ANISOU 3357  CG2 THR A 444     3027   3166   3404     38    -25    150       C  
ATOM   3358  N   GLU A 445     124.645  90.936  -6.130  1.00 26.20           N  
ANISOU 3358  N   GLU A 445     3131   3281   3541     26    -24    155       N  
ATOM   3359  CA  GLU A 445     125.668  90.218  -5.433  1.00 27.04           C  
ANISOU 3359  CA  GLU A 445     3229   3388   3655     19    -20    161       C  
ATOM   3360  C   GLU A 445     126.769  89.796  -6.451  1.00 26.87           C  
ANISOU 3360  C   GLU A 445     3205   3369   3635     18    -15    164       C  
ATOM   3361  O   GLU A 445     126.471  89.199  -7.514  1.00 25.78           O  
ANISOU 3361  O   GLU A 445     3065   3233   3497     23    -13    157       O  
ATOM   3362  CB  GLU A 445     124.917  89.044  -4.769  1.00 29.80           C  
ANISOU 3362  CB  GLU A 445     3570   3740   4014     20    -20    156       C  
ATOM   3363  CG  GLU A 445     125.683  88.191  -3.826  1.00 31.96           C  
ANISOU 3363  CG  GLU A 445     3836   4012   4296     14    -18    162       C  
ATOM   3364  CD  GLU A 445     124.827  87.016  -3.362  1.00 32.67           C  
ANISOU 3364  CD  GLU A 445     3919   4102   4393     15    -18    157       C  
ATOM   3365  OE1 GLU A 445     124.589  86.196  -4.252  1.00 33.81           O  
ANISOU 3365  OE1 GLU A 445     4059   4246   4540     19    -15    151       O  
ATOM   3366  OE2 GLU A 445     124.413  86.904  -2.142  1.00 30.82           O  
ANISOU 3366  OE2 GLU A 445     3683   3866   4160     10    -20    159       O  
ATOM   3367  N   ILE A 446     128.020  90.173  -6.141  1.00 25.10           N  
ANISOU 3367  N   ILE A 446     2980   3145   3410     10    -13    171       N  
ATOM   3368  CA AILE A 446     129.155  89.944  -6.992  0.50 25.10           C  
ANISOU 3368  CA AILE A 446     2978   3149   3411      8     -8    173       C  
ATOM   3369  CA BILE A 446     129.178  89.939  -6.985  0.50 25.36           C  
ANISOU 3369  CA BILE A 446     3010   3182   3444      7     -8    173       C  
ATOM   3370  C   ILE A 446     130.050  88.841  -6.399  1.00 25.79           C  
ANISOU 3370  C   ILE A 446     3052   3238   3510      5     -5    176       C  
ATOM   3371  O   ILE A 446     130.497  87.926  -7.137  1.00 25.59           O  
ANISOU 3371  O   ILE A 446     3019   3215   3490      8     -1    172       O  
ATOM   3372  CB AILE A 446     129.914  91.274  -7.191  0.50 25.43           C  
ANISOU 3372  CB AILE A 446     3029   3191   3443      1     -7    179       C  
ATOM   3373  CB BILE A 446     130.009  91.230  -7.109  0.50 26.02           C  
ANISOU 3373  CB BILE A 446     3103   3265   3518      0     -7    179       C  
ATOM   3374  CG1AILE A 446     128.930  92.397  -7.670  0.50 25.37           C  
ANISOU 3374  CG1AILE A 446     3036   3178   3424      5    -11    177       C  
ATOM   3375  CG1BILE A 446     129.158  92.320  -7.772  0.50 26.45           C  
ANISOU 3375  CG1BILE A 446     3172   3317   3562      4    -10    178       C  
ATOM   3376  CG2AILE A 446     131.041  91.073  -8.175  0.50 25.36           C  
ANISOU 3376  CG2AILE A 446     3017   3187   3433     -3     -1    179       C  
ATOM   3377  CG2BILE A 446     131.274  90.993  -7.911  0.50 26.10           C  
ANISOU 3377  CG2BILE A 446     3108   3280   3528     -5      0    180       C  
ATOM   3378  CD1AILE A 446     128.057  92.019  -8.881  0.50 25.01           C  
ANISOU 3378  CD1AILE A 446     2993   3135   3376     13    -12    170       C  
ATOM   3379  CD1BILE A 446     129.643  93.697  -7.484  0.50 26.60           C  
ANISOU 3379  CD1BILE A 446     3202   3331   3572     -4    -11    184       C  
ATOM   3380  N   LEU A 447     130.517  89.060  -5.163  1.00 26.94           N  
ANISOU 3380  N   LEU A 447     3195   3382   3657     -1     -8    182       N  
ATOM   3381  CA  LEU A 447     131.090  88.001  -4.310  1.00 27.74           C  
ANISOU 3381  CA  LEU A 447     3285   3484   3770     -2     -8    186       C  
ATOM   3382  C   LEU A 447     130.137  87.681  -3.133  1.00 27.37           C  
ANISOU 3382  C   LEU A 447     3239   3435   3727     -2    -13    187       C  
ATOM   3383  O   LEU A 447     129.868  88.536  -2.285  1.00 26.69           O  
ANISOU 3383  O   LEU A 447     3159   3348   3635     -6    -16    190       O  
ATOM   3384  CB  LEU A 447     132.473  88.357  -3.808  1.00 29.00           C  
ANISOU 3384  CB  LEU A 447     3440   3647   3930     -9     -7    192       C  
ATOM   3385  CG  LEU A 447     133.455  88.244  -4.963  1.00 33.88           C  
ANISOU 3385  CG  LEU A 447     4054   4270   4548     -9     -2    190       C  
ATOM   3386  CD1 LEU A 447     134.504  89.332  -4.832  1.00 40.28           C  
ANISOU 3386  CD1 LEU A 447     4867   5085   5352    -19      0    194       C  
ATOM   3387  CD2 LEU A 447     134.078  86.855  -5.025  1.00 35.00           C  
ANISOU 3387  CD2 LEU A 447     4182   4413   4703     -5      0    188       C  
ATOM   3388  N   GLN A 448     129.632  86.450  -3.093  1.00 25.17           N  
ANISOU 3388  N   GLN A 448     2954   3153   3456      3    -13    183       N  
ATOM   3389  CA  GLN A 448     128.653  86.035  -2.082  1.00 23.93           C  
ANISOU 3389  CA  GLN A 448     2798   2994   3301      2    -16    183       C  
ATOM   3390  C   GLN A 448     129.089  85.360  -0.783  1.00 24.55           C  
ANISOU 3390  C   GLN A 448     2871   3071   3386     -3    -19    191       C  
ATOM   3391  O   GLN A 448     130.199  84.826  -0.654  1.00 24.17           O  
ANISOU 3391  O   GLN A 448     2817   3023   3345     -3    -19    197       O  
ATOM   3392  CB  GLN A 448     127.634  85.081  -2.743  1.00 22.65           C  
ANISOU 3392  CB  GLN A 448     2633   2829   3143      8    -14    174       C  
ATOM   3393  CG  GLN A 448     128.137  83.642  -2.889  1.00 23.24           C  
ANISOU 3393  CG  GLN A 448     2700   2900   3230     11    -12    175       C  
ATOM   3394  CD  GLN A 448     127.050  82.613  -3.198  1.00 23.48           C  
ANISOU 3394  CD  GLN A 448     2729   2928   3266     14    -10    166       C  
ATOM   3395  OE1 GLN A 448     126.007  82.561  -2.536  1.00 22.32           O  
ANISOU 3395  OE1 GLN A 448     2585   2780   3117     12    -12    164       O  
ATOM   3396  NE2 GLN A 448     127.307  81.764  -4.196  1.00 24.84           N  
ANISOU 3396  NE2 GLN A 448     2896   3099   3444     19     -6    161       N  
ATOM   3397  N   ASP A 449     128.142  85.403   0.159  1.00 23.57           N  
ANISOU 3397  N   ASP A 449     2749   2945   3259     -6    -21    191       N  
ATOM   3398  CA  ASP A 449     128.164  84.737   1.453  1.00 25.04           C  
ANISOU 3398  CA  ASP A 449     2933   3130   3449    -12    -24    198       C  
ATOM   3399  C   ASP A 449     126.998  83.821   1.130  1.00 25.39           C  
ANISOU 3399  C   ASP A 449     2978   3172   3498     -9    -22    190       C  
ATOM   3400  O   ASP A 449     125.952  84.277   0.666  1.00 24.17           O  
ANISOU 3400  O   ASP A 449     2827   3019   3338     -6    -21    181       O  
ATOM   3401  CB  ASP A 449     127.834  85.647   2.618  1.00 26.92           C  
ANISOU 3401  CB  ASP A 449     3176   3372   3679    -20    -27    200       C  
ATOM   3402  CG  ASP A 449     128.095  84.971   3.951  1.00 29.58           C  
ANISOU 3402  CG  ASP A 449     3511   3709   4019    -27    -31    209       C  
ATOM   3403  OD1 ASP A 449     128.019  83.723   4.007  1.00 28.50           O  
ANISOU 3403  OD1 ASP A 449     3370   3567   3890    -25    -31    211       O  
ATOM   3404  OD2 ASP A 449     128.393  85.685   4.930  1.00 30.64           O  
ANISOU 3404  OD2 ASP A 449     3646   3847   4147    -34    -34    214       O  
ATOM   3405  N   TYR A 450     127.169  82.529   1.344  1.00 22.85           N  
ANISOU 3405  N   TYR A 450     2652   2845   3185     -8    -22    193       N  
ATOM   3406  CA  TYR A 450     126.194  81.565   0.873  1.00 23.16           C  
ANISOU 3406  CA  TYR A 450     2690   2880   3229     -5    -19    185       C  
ATOM   3407  C   TYR A 450     124.827  81.705   1.512  1.00 23.81           C  
ANISOU 3407  C   TYR A 450     2777   2964   3306    -11    -19    179       C  
ATOM   3408  O   TYR A 450     123.809  81.397   0.855  1.00 23.59           O  
ANISOU 3408  O   TYR A 450     2749   2937   3279     -8    -16    168       O  
ATOM   3409  CB  TYR A 450     126.690  80.119   0.998  1.00 24.03           C  
ANISOU 3409  CB  TYR A 450     2796   2982   3352     -4    -20    190       C  
ATOM   3410  CG  TYR A 450     125.814  79.124   0.310  1.00 23.01           C  
ANISOU 3410  CG  TYR A 450     2666   2848   3228     -1    -15    180       C  
ATOM   3411  CD1 TYR A 450     124.736  78.575   0.965  1.00 24.39           C  
ANISOU 3411  CD1 TYR A 450     2844   3020   3402     -7    -15    177       C  
ATOM   3412  CD2 TYR A 450     126.017  78.783  -1.020  1.00 24.06           C  
ANISOU 3412  CD2 TYR A 450     2795   2980   3366      7    -12    172       C  
ATOM   3413  CE1 TYR A 450     123.858  77.694   0.333  1.00 25.18           C  
ANISOU 3413  CE1 TYR A 450     2943   3117   3508     -6    -10    167       C  
ATOM   3414  CE2 TYR A 450     125.172  77.878  -1.685  1.00 23.81           C  
ANISOU 3414  CE2 TYR A 450     2763   2945   3340      9     -7    161       C  
ATOM   3415  CZ  TYR A 450     124.075  77.357  -1.012  1.00 25.36           C  
ANISOU 3415  CZ  TYR A 450     2962   3138   3535      3     -7    159       C  
ATOM   3416  OH  TYR A 450     123.177  76.474  -1.593  1.00 24.45           O  
ANISOU 3416  OH  TYR A 450     2846   3020   3425      3     -2    148       O  
ATOM   3417  N   GLY A 451     124.761  82.080   2.799  1.00 25.06           N  
ANISOU 3417  N   GLY A 451     2938   3125   3460    -19    -22    185       N  
ATOM   3418  CA  GLY A 451     123.473  82.092   3.530  1.00 23.72           C  
ANISOU 3418  CA  GLY A 451     2771   2958   3285    -26    -21    179       C  
ATOM   3419  C   GLY A 451     123.214  80.676   4.067  1.00 25.33           C  
ANISOU 3419  C   GLY A 451     2973   3156   3495    -31    -21    183       C  
ATOM   3420  O   GLY A 451     124.164  79.887   4.280  1.00 22.88           O  
ANISOU 3420  O   GLY A 451     2662   2839   3192    -31    -23    193       O  
ATOM   3421  N   LEU A 452     121.940  80.342   4.323  1.00 24.98           N  
ANISOU 3421  N   LEU A 452     2931   3114   3449    -36    -18    174       N  
ATOM   3422  CA  LEU A 452     121.591  79.006   4.880  1.00 24.58           C  
ANISOU 3422  CA  LEU A 452     2881   3056   3403    -44    -16    177       C  
ATOM   3423  C   LEU A 452     121.310  77.962   3.816  1.00 25.79           C  
ANISOU 3423  C   LEU A 452     3031   3202   3565    -38    -12    170       C  
ATOM   3424  O   LEU A 452     121.171  78.286   2.634  1.00 27.96           O  
ANISOU 3424  O   LEU A 452     3304   3480   3841    -29    -10    160       O  
ATOM   3425  CB  LEU A 452     120.412  79.106   5.883  1.00 24.96           C  
ANISOU 3425  CB  LEU A 452     2931   3110   3443    -56    -14    172       C  
ATOM   3426  CG  LEU A 452     119.256  80.019   5.456  1.00 25.24           C  
ANISOU 3426  CG  LEU A 452     2964   3155   3471    -54    -11    155       C  
ATOM   3427  CD1 LEU A 452     118.701  79.683   4.079  1.00 24.62           C  
ANISOU 3427  CD1 LEU A 452     2882   3075   3398    -44     -8    143       C  
ATOM   3428  CD2 LEU A 452     118.116  79.999   6.463  1.00 26.17           C  
ANISOU 3428  CD2 LEU A 452     3083   3279   3582    -67     -9    149       C  
ATOM   3429  N   ALA A 453     121.188  76.702   4.243  1.00 25.79           N  
ANISOU 3429  N   ALA A 453     3034   3194   3572    -44    -11    174       N  
ATOM   3430  CA  ALA A 453     120.685  75.643   3.400  1.00 25.01           C  
ANISOU 3430  CA  ALA A 453     2933   3089   3482    -41     -6    165       C  
ATOM   3431  C   ALA A 453     119.383  75.227   4.065  1.00 25.26           C  
ANISOU 3431  C   ALA A 453     2967   3122   3508    -54     -2    158       C  
ATOM   3432  O   ALA A 453     119.349  74.414   4.991  1.00 24.29           O  
ANISOU 3432  O   ALA A 453     2849   2992   3386    -64     -2    167       O  
ATOM   3433  CB  ALA A 453     121.655  74.481   3.255  1.00 25.82           C  
ANISOU 3433  CB  ALA A 453     3036   3178   3597    -37     -8    175       C  
ATOM   3434  N   ARG A 454     118.306  75.807   3.541  1.00 24.70           N  
ANISOU 3434  N   ARG A 454     2892   3061   3431    -53      1    142       N  
ATOM   3435  CA  ARG A 454     116.959  75.722   4.102  1.00 25.26           C  
ANISOU 3435  CA  ARG A 454     2964   3139   3496    -64      6    132       C  
ATOM   3436  C   ARG A 454     116.077  76.500   3.174  1.00 25.55           C  
ANISOU 3436  C   ARG A 454     2994   3186   3527    -57      7    114       C  
ATOM   3437  O   ARG A 454     116.488  77.554   2.682  1.00 25.51           O  
ANISOU 3437  O   ARG A 454     2988   3186   3520    -47      4    114       O  
ATOM   3438  CB  ARG A 454     116.893  76.370   5.509  1.00 25.92           C  
ANISOU 3438  CB  ARG A 454     3051   3228   3570    -75      3    139       C  
ATOM   3439  CG  ARG A 454     115.518  76.343   6.171  1.00 25.96           C  
ANISOU 3439  CG  ARG A 454     3055   3242   3567    -88      8    127       C  
ATOM   3440  CD  ARG A 454     115.546  76.892   7.566  1.00 27.43           C  
ANISOU 3440  CD  ARG A 454     3244   3434   3744   -100      6    135       C  
ATOM   3441  NE  ARG A 454     114.204  77.089   8.135  1.00 27.09           N  
ANISOU 3441  NE  ARG A 454     3199   3403   3693   -112     11    120       N  
ATOM   3442  CZ  ARG A 454     113.863  78.076   8.967  1.00 26.76           C  
ANISOU 3442  CZ  ARG A 454     3156   3372   3641   -117     11    117       C  
ATOM   3443  NH1 ARG A 454     114.734  79.024   9.333  1.00 27.13           N  
ANISOU 3443  NH1 ARG A 454     3204   3420   3684   -113      5    126       N  
ATOM   3444  NH2 ARG A 454     112.625  78.171   9.372  1.00 25.57           N  
ANISOU 3444  NH2 ARG A 454     3000   3231   3483   -127     16    102       N  
ATOM   3445  N   PHE A 455     114.866  75.989   2.916  1.00 25.77           N  
ANISOU 3445  N   PHE A 455     3018   3217   3554    -62     13     99       N  
ATOM   3446  CA  PHE A 455     113.898  76.640   2.075  1.00 24.77           C  
ANISOU 3446  CA  PHE A 455     2885   3101   3423    -55     14     81       C  
ATOM   3447  C   PHE A 455     112.763  76.962   3.020  1.00 25.81           C  
ANISOU 3447  C   PHE A 455     3016   3244   3548    -66     16     72       C  
ATOM   3448  O   PHE A 455     111.856  76.126   3.287  1.00 24.44           O  
ANISOU 3448  O   PHE A 455     2840   3071   3374    -78     22     63       O  
ATOM   3449  CB  PHE A 455     113.547  75.739   0.865  1.00 26.99           C  
ANISOU 3449  CB  PHE A 455     3163   3380   3712    -50     18     70       C  
ATOM   3450  CG  PHE A 455     114.709  75.542  -0.076  1.00 28.46           C  
ANISOU 3450  CG  PHE A 455     3350   3557   3905    -39     15     78       C  
ATOM   3451  CD1 PHE A 455     114.944  76.429  -1.112  1.00 28.12           C  
ANISOU 3451  CD1 PHE A 455     3305   3521   3859    -26     12     74       C  
ATOM   3452  CD2 PHE A 455     115.656  74.520   0.168  1.00 29.13           C  
ANISOU 3452  CD2 PHE A 455     3439   3629   4000    -42     16     91       C  
ATOM   3453  CE1 PHE A 455     116.047  76.268  -1.958  1.00 30.43           C  
ANISOU 3453  CE1 PHE A 455     3598   3807   4157    -17     11     81       C  
ATOM   3454  CE2 PHE A 455     116.774  74.394  -0.666  1.00 31.45           C  
ANISOU 3454  CE2 PHE A 455     3733   3916   4300    -31     14     97       C  
ATOM   3455  CZ  PHE A 455     116.956  75.258  -1.736  1.00 30.59           C  
ANISOU 3455  CZ  PHE A 455     3621   3814   4188    -19     13     91       C  
ATOM   3456  N   VAL A 456     112.837  78.168   3.600  1.00 25.52           N  
ANISOU 3456  N   VAL A 456     2979   3214   3503    -65     12     74       N  
ATOM   3457  CA  VAL A 456     112.074  78.502   4.819  1.00 25.14           C  
ANISOU 3457  CA  VAL A 456     2931   3175   3447    -78     14     70       C  
ATOM   3458  C   VAL A 456     110.546  78.277   4.602  1.00 25.44           C  
ANISOU 3458  C   VAL A 456     2960   3223   3482    -82     19     48       C  
ATOM   3459  O   VAL A 456     109.933  78.888   3.736  1.00 26.00           O  
ANISOU 3459  O   VAL A 456     3024   3301   3551    -71     17     34       O  
ATOM   3460  CB  VAL A 456     112.424  79.924   5.333  1.00 24.08           C  
ANISOU 3460  CB  VAL A 456     2798   3047   3307    -73      9     73       C  
ATOM   3461  CG1 VAL A 456     111.542  80.339   6.499  1.00 25.13           C  
ANISOU 3461  CG1 VAL A 456     2928   3189   3430    -86     11     65       C  
ATOM   3462  CG2 VAL A 456     113.878  79.993   5.765  1.00 23.66           C  
ANISOU 3462  CG2 VAL A 456     2751   2983   3254    -73      5     94       C  
ATOM   3463  N   ASN A 457     109.954  77.359   5.369  1.00 24.90           N  
ANISOU 3463  N   ASN A 457     2892   3155   3413    -99     25     45       N  
ATOM   3464  CA  ASN A 457     108.517  77.072   5.313  1.00 24.67           C  
ANISOU 3464  CA  ASN A 457     2855   3137   3380   -107     32     24       C  
ATOM   3465  C   ASN A 457     108.028  76.398   4.033  1.00 25.21           C  
ANISOU 3465  C   ASN A 457     2918   3205   3455   -100     34     12       C  
ATOM   3466  O   ASN A 457     106.794  76.377   3.756  1.00 24.60           O  
ANISOU 3466  O   ASN A 457     2832   3140   3375   -103     38     -9       O  
ATOM   3467  CB  ASN A 457     107.617  78.307   5.589  1.00 24.09           C  
ANISOU 3467  CB  ASN A 457     2774   3080   3299   -104     30      8       C  
ATOM   3468  CG  ASN A 457     107.899  78.991   6.888  1.00 23.93           C  
ANISOU 3468  CG  ASN A 457     2757   3063   3271   -112     29     16       C  
ATOM   3469  OD1 ASN A 457     108.297  78.367   7.902  1.00 25.22           O  
ANISOU 3469  OD1 ASN A 457     2928   3222   3433   -128     32     29       O  
ATOM   3470  ND2 ASN A 457     107.658  80.295   6.896  1.00 23.23           N  
ANISOU 3470  ND2 ASN A 457     2664   2983   3179   -103     24      8       N  
ATOM   3471  N   ILE A 458     108.946  75.806   3.270  1.00 25.82           N  
ANISOU 3471  N   ILE A 458     3001   3270   3541    -93     32     23       N  
ATOM   3472  CA  ILE A 458     108.560  75.004   2.103  1.00 25.47           C  
ANISOU 3472  CA  ILE A 458     2951   3223   3502    -88     36     11       C  
ATOM   3473  C   ILE A 458     108.610  73.551   2.559  1.00 26.70           C  
ANISOU 3473  C   ILE A 458     3113   3368   3664   -104     42     17       C  
ATOM   3474  O   ILE A 458     109.716  72.958   2.692  1.00 25.93           O  
ANISOU 3474  O   ILE A 458     3025   3255   3574   -104     41     35       O  
ATOM   3475  CB  ILE A 458     109.440  75.231   0.873  1.00 26.85           C  
ANISOU 3475  CB  ILE A 458     3127   3392   3682    -71     31     17       C  
ATOM   3476  CG1 ILE A 458     109.442  76.734   0.513  1.00 26.89           C  
ANISOU 3476  CG1 ILE A 458     3129   3407   3680    -56     23     14       C  
ATOM   3477  CG2 ILE A 458     108.923  74.383  -0.277  1.00 26.14           C  
ANISOU 3477  CG2 ILE A 458     3032   3302   3597    -68     35      3       C  
ATOM   3478  CD1 ILE A 458     110.146  77.109  -0.745  1.00 26.98           C  
ANISOU 3478  CD1 ILE A 458     3141   3416   3695    -39     19     17       C  
ATOM   3479  N   GLU A 459     107.416  72.983   2.759  1.00 25.63           N  
ANISOU 3479  N   GLU A 459     2973   3240   3526   -118     50      1       N  
ATOM   3480  CA  GLU A 459     107.271  71.622   3.300  1.00 27.48           C  
ANISOU 3480  CA  GLU A 459     3213   3463   3764   -136     57      5       C  
ATOM   3481  C   GLU A 459     108.039  70.498   2.593  1.00 27.65           C  
ANISOU 3481  C   GLU A 459     3241   3467   3798   -132     58     13       C  
ATOM   3482  O   GLU A 459     108.505  69.581   3.238  1.00 27.82           O  
ANISOU 3482  O   GLU A 459     3273   3474   3824   -143     60     27       O  
ATOM   3483  CB  GLU A 459     105.790  71.215   3.296  1.00 28.35           C  
ANISOU 3483  CB  GLU A 459     3316   3587   3871   -149     65    -18       C  
ATOM   3484  CG  GLU A 459     105.492  70.002   4.197  1.00 32.36           C  
ANISOU 3484  CG  GLU A 459     3832   4086   4379   -173     74    -14       C  
ATOM   3485  CD  GLU A 459     104.013  69.566   4.168  1.00 33.40           C  
ANISOU 3485  CD  GLU A 459     3955   4231   4506   -189     83    -38       C  
ATOM   3486  OE1 GLU A 459     103.311  69.969   3.235  1.00 34.20           O  
ANISOU 3486  OE1 GLU A 459     4044   4346   4607   -178     83    -58       O  
ATOM   3487  OE2 GLU A 459     103.549  68.906   5.125  1.00 35.14           O  
ANISOU 3487  OE2 GLU A 459     4179   4449   4722   -211     91    -38       O  
ATOM   3488  N   GLN A 460     108.105  70.584   1.269  1.00 27.85           N  
ANISOU 3488  N   GLN A 460     3261   3494   3828   -118     57      4       N  
ATOM   3489  CA  GLN A 460     108.722  69.590   0.429  1.00 28.99           C  
ANISOU 3489  CA  GLN A 460     3408   3624   3983   -113     58      7       C  
ATOM   3490  C   GLN A 460     110.242  69.559   0.632  1.00 30.23           C  
ANISOU 3490  C   GLN A 460     3574   3765   4147   -104     52     30       C  
ATOM   3491  O   GLN A 460     110.858  68.641   0.200  1.00 29.93           O  
ANISOU 3491  O   GLN A 460     3540   3713   4120   -102     54     35       O  
ATOM   3492  CB  GLN A 460     108.412  69.918  -1.022  1.00 30.76           C  
ANISOU 3492  CB  GLN A 460     3622   3857   4208    -98     57     -9       C  
ATOM   3493  CG  GLN A 460     106.923  69.722  -1.425  1.00 32.33           C  
ANISOU 3493  CG  GLN A 460     3811   4070   4402   -106     63    -34       C  
ATOM   3494  CD  GLN A 460     105.948  70.805  -0.891  1.00 32.67           C  
ANISOU 3494  CD  GLN A 460     3847   4133   4433   -107     61    -45       C  
ATOM   3495  OE1 GLN A 460     106.313  71.936  -0.482  1.00 31.35           O  
ANISOU 3495  OE1 GLN A 460     3680   3971   4261    -99     54    -37       O  
ATOM   3496  NE2 GLN A 460     104.723  70.432  -0.832  1.00 35.74           N  
ANISOU 3496  NE2 GLN A 460     4228   4532   4818   -119     67    -64       N  
ATOM   3497  N   LYS A 461     110.835  70.619   1.209  1.00 29.65           N  
ANISOU 3497  N   LYS A 461     3502   3696   4068    -99     46     42       N  
ATOM   3498  CA  LYS A 461     112.237  70.653   1.515  1.00 30.36           C  
ANISOU 3498  CA  LYS A 461     3599   3774   4163    -92     40     63       C  
ATOM   3499  C   LYS A 461     112.429  70.439   3.014  1.00 29.17           C  
ANISOU 3499  C   LYS A 461     3457   3618   4009   -106     39     78       C  
ATOM   3500  O   LYS A 461     112.629  71.403   3.775  1.00 28.75           O  
ANISOU 3500  O   LYS A 461     3404   3572   3947   -107     35     85       O  
ATOM   3501  CB  LYS A 461     112.872  72.003   1.056  1.00 31.37           C  
ANISOU 3501  CB  LYS A 461     3723   3910   4286    -76     33     66       C  
ATOM   3502  CG  LYS A 461     112.961  72.173  -0.448  1.00 32.47           C  
ANISOU 3502  CG  LYS A 461     3857   4053   4429    -61     33     56       C  
ATOM   3503  CD  LYS A 461     113.826  71.049  -1.028  1.00 32.18           C  
ANISOU 3503  CD  LYS A 461     3823   4000   4405    -58     34     62       C  
ATOM   3504  CE  LYS A 461     114.966  71.510  -1.839  1.00 30.77           C  
ANISOU 3504  CE  LYS A 461     3643   3820   4230    -43     30     68       C  
ATOM   3505  NZ  LYS A 461     115.467  70.357  -2.637  1.00 31.09           N  
ANISOU 3505  NZ  LYS A 461     3683   3848   4283    -39     34     66       N  
ATOM   3506  N   GLY A 462     112.428  69.156   3.403  1.00 27.99           N  
ANISOU 3506  N   GLY A 462     3314   3454   3866   -118     43     84       N  
ATOM   3507  CA  GLY A 462     112.627  68.712   4.776  1.00 27.22           C  
ANISOU 3507  CA  GLY A 462     3228   3349   3766   -133     42    100       C  
ATOM   3508  C   GLY A 462     111.746  69.460   5.792  1.00 25.90           C  
ANISOU 3508  C   GLY A 462     3059   3198   3585   -146     44     95       C  
ATOM   3509  O   GLY A 462     112.201  69.964   6.796  1.00 24.62           O  
ANISOU 3509  O   GLY A 462     2901   3037   3416   -150     40    108       O  
ATOM   3510  N   GLY A 463     110.493  69.603   5.467  1.00 26.46           N  
ANISOU 3510  N   GLY A 463     3122   3281   3650   -152     51     74       N  
ATOM   3511  CA  GLY A 463     109.523  70.234   6.388  1.00 26.41           C  
ANISOU 3511  CA  GLY A 463     3113   3291   3631   -165     54     66       C  
ATOM   3512  C   GLY A 463     109.735  71.751   6.572  1.00 25.52           C  
ANISOU 3512  C   GLY A 463     2994   3192   3510   -155     47     66       C  
ATOM   3513  O   GLY A 463     109.204  72.368   7.533  1.00 26.34           O  
ANISOU 3513  O   GLY A 463     3096   3307   3603   -165     49     62       O  
ATOM   3514  N   GLY A 464     110.531  72.345   5.697  1.00 24.46           N  
ANISOU 3514  N   GLY A 464     2857   3055   3380   -135     41     69       N  
ATOM   3515  CA  GLY A 464     110.761  73.802   5.739  1.00 24.34           C  
ANISOU 3515  CA  GLY A 464     2837   3051   3358   -124     35     69       C  
ATOM   3516  C   GLY A 464     111.802  74.199   6.746  1.00 24.61           C  
ANISOU 3516  C   GLY A 464     2879   3081   3390   -126     30     89       C  
ATOM   3517  O   GLY A 464     111.951  75.389   7.024  1.00 22.24           O  
ANISOU 3517  O   GLY A 464     2577   2790   3084   -121     25     89       O  
ATOM   3518  N   ASN A 465     112.512  73.182   7.283  1.00 24.60           N  
ANISOU 3518  N   ASN A 465     2887   3066   3394   -134     29    106       N  
ATOM   3519  CA  ASN A 465     113.431  73.307   8.392  1.00 25.59           C  
ANISOU 3519  CA  ASN A 465     3020   3186   3516   -139     24    126       C  
ATOM   3520  C   ASN A 465     114.903  73.177   7.939  1.00 25.45           C  
ANISOU 3520  C   ASN A 465     3006   3156   3508   -125     17    142       C  
ATOM   3521  O   ASN A 465     115.164  72.781   6.815  1.00 26.31           O  
ANISOU 3521  O   ASN A 465     3111   3258   3626   -113     17    138       O  
ATOM   3522  CB  ASN A 465     113.124  72.196   9.434  1.00 27.12           C  
ANISOU 3522  CB  ASN A 465     3224   3374   3708   -159     28    134       C  
ATOM   3523  CG  ASN A 465     111.673  72.244   9.967  1.00 27.57           C  
ANISOU 3523  CG  ASN A 465     3278   3444   3755   -177     36    117       C  
ATOM   3524  OD1 ASN A 465     111.004  71.180  10.186  1.00 28.43           O  
ANISOU 3524  OD1 ASN A 465     3390   3548   3864   -192     43    114       O  
ATOM   3525  ND2 ASN A 465     111.178  73.434  10.170  1.00 24.44           N  
ANISOU 3525  ND2 ASN A 465     2873   3064   3349   -175     36    106       N  
ATOM   3526  N   TYR A 466     115.850  73.482   8.819  1.00 25.57           N  
ANISOU 3526  N   TYR A 466     3026   3170   3520   -126     10    160       N  
ATOM   3527  CA  TYR A 466     117.280  73.376   8.484  1.00 26.77           C  
ANISOU 3527  CA  TYR A 466     3180   3311   3681   -113      3    175       C  
ATOM   3528  C   TYR A 466     117.571  72.000   7.911  1.00 27.94           C  
ANISOU 3528  C   TYR A 466     3331   3443   3843   -110      4    179       C  
ATOM   3529  O   TYR A 466     117.078  70.962   8.435  1.00 27.62           O  
ANISOU 3529  O   TYR A 466     3298   3395   3803   -123      8    181       O  
ATOM   3530  CB  TYR A 466     118.185  73.713   9.707  1.00 27.36           C  
ANISOU 3530  CB  TYR A 466     3259   3386   3749   -118     -4    194       C  
ATOM   3531  CG  TYR A 466     118.221  75.205   9.880  1.00 28.26           C  
ANISOU 3531  CG  TYR A 466     3369   3515   3855   -115     -6    189       C  
ATOM   3532  CD1 TYR A 466     118.892  75.991   8.970  1.00 28.96           C  
ANISOU 3532  CD1 TYR A 466     3451   3605   3947    -99     -9    187       C  
ATOM   3533  CD2 TYR A 466     117.481  75.839  10.882  1.00 29.61           C  
ANISOU 3533  CD2 TYR A 466     3540   3698   4012   -128     -4    185       C  
ATOM   3534  CE1 TYR A 466     118.887  77.395   9.061  1.00 30.51           C  
ANISOU 3534  CE1 TYR A 466     3645   3813   4135    -96    -10    182       C  
ATOM   3535  CE2 TYR A 466     117.436  77.238  10.962  1.00 30.83           C  
ANISOU 3535  CE2 TYR A 466     3690   3865   4160   -125     -5    178       C  
ATOM   3536  CZ  TYR A 466     118.162  78.011  10.049  1.00 31.47           C  
ANISOU 3536  CZ  TYR A 466     3767   3945   4245   -108     -9    177       C  
ATOM   3537  OH  TYR A 466     118.111  79.391  10.074  1.00 31.47           O  
ANISOU 3537  OH  TYR A 466     3764   3956   4239   -104    -10    171       O  
ATOM   3538  N   LEU A 467     118.295  71.997   6.798  1.00 27.73           N  
ANISOU 3538  N   LEU A 467     3299   3411   3825    -94      3    177       N  
ATOM   3539  CA  LEU A 467     118.720  70.754   6.141  1.00 28.61           C  
ANISOU 3539  CA  LEU A 467     3413   3507   3951    -88      3    180       C  
ATOM   3540  C   LEU A 467     120.075  70.344   6.659  1.00 27.67           C  
ANISOU 3540  C   LEU A 467     3299   3376   3839    -83     -5    200       C  
ATOM   3541  O   LEU A 467     120.856  71.173   7.216  1.00 28.35           O  
ANISOU 3541  O   LEU A 467     3384   3469   3920    -81    -11    210       O  
ATOM   3542  CB  LEU A 467     118.735  70.985   4.633  1.00 29.48           C  
ANISOU 3542  CB  LEU A 467     3515   3620   4068    -74      6    165       C  
ATOM   3543  CG  LEU A 467     117.361  71.453   4.101  1.00 30.37           C  
ANISOU 3543  CG  LEU A 467     3623   3745   4173    -77     13    145       C  
ATOM   3544  CD1 LEU A 467     117.404  72.090   2.733  1.00 30.32           C  
ANISOU 3544  CD1 LEU A 467     3608   3745   4167    -63     14    133       C  
ATOM   3545  CD2 LEU A 467     116.320  70.336   4.136  1.00 30.88           C  
ANISOU 3545  CD2 LEU A 467     3690   3804   4240    -89     20    136       C  
ATOM   3546  N   LYS A 468     120.395  69.095   6.418  1.00 27.44           N  
ANISOU 3546  N   LYS A 468     3274   3331   3822    -81     -5    204       N  
ATOM   3547  CA  LYS A 468     121.673  68.499   6.820  1.00 28.62           C  
ANISOU 3547  CA  LYS A 468     3427   3467   3981    -75    -13    222       C  
ATOM   3548  C   LYS A 468     122.873  69.301   6.262  1.00 26.50           C  
ANISOU 3548  C   LYS A 468     3149   3203   3715    -59    -18    225       C  
ATOM   3549  O   LYS A 468     123.863  69.474   6.922  1.00 26.81           O  
ANISOU 3549  O   LYS A 468     3189   3242   3755    -56    -26    240       O  
ATOM   3550  CB  LYS A 468     121.730  67.056   6.323  1.00 31.20           C  
ANISOU 3550  CB  LYS A 468     3758   3774   4323    -72    -11    222       C  
ATOM   3551  CG  LYS A 468     123.093  66.392   6.529  1.00 36.00           C  
ANISOU 3551  CG  LYS A 468     4368   4367   4944    -61    -20    238       C  
ATOM   3552  CD  LYS A 468     123.091  64.906   6.127  1.00 40.40           C  
ANISOU 3552  CD  LYS A 468     4931   4902   5517    -59    -18    237       C  
ATOM   3553  CE  LYS A 468     124.436  64.255   6.483  1.00 44.65           C  
ANISOU 3553  CE  LYS A 468     5472   5426   6068    -48    -28    255       C  
ATOM   3554  NZ  LYS A 468     124.599  63.031   5.659  1.00 49.27           N  
ANISOU 3554  NZ  LYS A 468     6058   5991   6672    -39    -26    249       N  
ATOM   3555  N   GLU A 469     122.730  69.833   5.069  1.00 26.60           N  
ANISOU 3555  N   GLU A 469     3154   3224   3730    -50    -13    210       N  
ATOM   3556  CA  GLU A 469     123.797  70.560   4.379  1.00 26.26           C  
ANISOU 3556  CA  GLU A 469     3102   3186   3689    -36    -17    210       C  
ATOM   3557  C   GLU A 469     123.963  71.966   4.937  1.00 25.97           C  
ANISOU 3557  C   GLU A 469     3064   3164   3638    -38    -20    214       C  
ATOM   3558  O   GLU A 469     124.887  72.693   4.570  1.00 27.90           O  
ANISOU 3558  O   GLU A 469     3303   3414   3883    -30    -23    216       O  
ATOM   3559  CB  GLU A 469     123.523  70.559   2.882  1.00 26.71           C  
ANISOU 3559  CB  GLU A 469     3153   3245   3751    -27    -10    193       C  
ATOM   3560  CG  GLU A 469     123.553  69.187   2.220  1.00 27.80           C  
ANISOU 3560  CG  GLU A 469     3291   3368   3904    -23     -7    188       C  
ATOM   3561  CD  GLU A 469     122.253  68.384   2.386  1.00 29.57           C  
ANISOU 3561  CD  GLU A 469     3522   3587   4128    -34      0    180       C  
ATOM   3562  OE1 GLU A 469     121.226  68.962   2.839  1.00 29.26           O  
ANISOU 3562  OE1 GLU A 469     3484   3558   4076    -45      2    176       O  
ATOM   3563  OE2 GLU A 469     122.239  67.166   2.054  1.00 31.19           O  
ANISOU 3563  OE2 GLU A 469     3730   3777   4346    -34      2    178       O  
ATOM   3564  N   ASN A 470     123.098  72.385   5.849  1.00 26.03           N  
ANISOU 3564  N   ASN A 470     3077   3179   3635    -51    -19    214       N  
ATOM   3565  CA  ASN A 470     123.324  73.672   6.513  1.00 25.99           C  
ANISOU 3565  CA  ASN A 470     3070   3186   3617    -54    -23    219       C  
ATOM   3566  C   ASN A 470     124.516  73.557   7.435  1.00 27.76           C  
ANISOU 3566  C   ASN A 470     3297   3408   3843    -54    -31    237       C  
ATOM   3567  O   ASN A 470     125.346  74.440   7.482  1.00 26.97           O  
ANISOU 3567  O   ASN A 470     3192   3315   3739    -49    -35    241       O  
ATOM   3568  CB  ASN A 470     122.119  74.154   7.283  1.00 26.18           C  
ANISOU 3568  CB  ASN A 470     3098   3220   3628    -68    -19    213       C  
ATOM   3569  CG  ASN A 470     122.253  75.622   7.701  1.00 26.03           C  
ANISOU 3569  CG  ASN A 470     3077   3215   3598    -69    -22    213       C  
ATOM   3570  OD1 ASN A 470     122.129  76.502   6.875  1.00 25.91           O  
ANISOU 3570  OD1 ASN A 470     3057   3207   3581    -61    -20    202       O  
ATOM   3571  ND2 ASN A 470     122.573  75.878   8.963  1.00 26.51           N  
ANISOU 3571  ND2 ASN A 470     3141   3279   3651    -78    -26    225       N  
ATOM   3572  N   THR A 471     124.631  72.419   8.122  1.00 28.20           N  
ANISOU 3572  N   THR A 471     3359   3452   3904    -59    -35    248       N  
ATOM   3573  CA  THR A 471     125.824  72.127   8.903  1.00 28.49           C  
ANISOU 3573  CA  THR A 471     3397   3484   3944    -57    -44    266       C  
ATOM   3574  C   THR A 471     127.009  71.739   8.017  1.00 27.67           C  
ANISOU 3574  C   THR A 471     3287   3373   3855    -40    -48    268       C  
ATOM   3575  O   THR A 471     128.112  72.235   8.234  1.00 26.91           O  
ANISOU 3575  O   THR A 471     3186   3281   3759    -34    -54    276       O  
ATOM   3576  CB  THR A 471     125.519  71.066  10.003  1.00 29.31           C  
ANISOU 3576  CB  THR A 471     3512   3577   4048    -68    -48    279       C  
ATOM   3577  OG1 THR A 471     124.607  71.666  10.935  1.00 29.50           O  
ANISOU 3577  OG1 THR A 471     3541   3612   4055    -84    -45    278       O  
ATOM   3578  CG2 THR A 471     126.804  70.594  10.779  1.00 28.65           C  
ANISOU 3578  CG2 THR A 471     3430   3486   3968    -64    -60    299       C  
ATOM   3579  N   THR A 472     126.822  70.800   7.107  1.00 27.82           N  
ANISOU 3579  N   THR A 472     3304   3379   3886    -33    -43    260       N  
ATOM   3580  CA  THR A 472     127.935  70.282   6.305  1.00 27.13           C  
ANISOU 3580  CA  THR A 472     3210   3284   3813    -18    -46    260       C  
ATOM   3581  C   THR A 472     128.538  71.198   5.241  1.00 27.80           C  
ANISOU 3581  C   THR A 472     3284   3379   3898     -8    -43    250       C  
ATOM   3582  O   THR A 472     129.670  71.038   4.900  1.00 28.23           O  
ANISOU 3582  O   THR A 472     3332   3432   3962      3    -47    253       O  
ATOM   3583  CB  THR A 472     127.675  68.858   5.774  1.00 27.48           C  
ANISOU 3583  CB  THR A 472     3258   3310   3873    -14    -43    257       C  
ATOM   3584  OG1 THR A 472     126.598  68.869   4.859  1.00 25.65           O  
ANISOU 3584  OG1 THR A 472     3025   3080   3639    -17    -33    239       O  
ATOM   3585  CG2 THR A 472     127.334  67.954   6.898  1.00 27.13           C  
ANISOU 3585  CG2 THR A 472     3225   3254   3828    -24    -47    270       C  
ATOM   3586  N   TRP A 473     127.760  72.147   4.752  1.00 25.10           N  
ANISOU 3586  N   TRP A 473     2940   3049   3546    -12    -37    239       N  
ATOM   3587  CA  TRP A 473     128.221  73.110   3.785  1.00 24.87           C  
ANISOU 3587  CA  TRP A 473     2904   3030   3514     -4    -34    230       C  
ATOM   3588  C   TRP A 473     128.141  74.571   4.293  1.00 25.99           C  
ANISOU 3588  C   TRP A 473     3047   3188   3642    -10    -35    231       C  
ATOM   3589  O   TRP A 473     129.149  75.196   4.476  1.00 26.56           O  
ANISOU 3589  O   TRP A 473     3114   3265   3712     -8    -39    238       O  
ATOM   3590  CB  TRP A 473     127.530  72.976   2.414  1.00 24.43           C  
ANISOU 3590  CB  TRP A 473     2845   2974   3462      0    -25    213       C  
ATOM   3591  CG  TRP A 473     127.874  74.125   1.498  1.00 24.36           C  
ANISOU 3591  CG  TRP A 473     2830   2977   3447      6    -23    205       C  
ATOM   3592  CD1 TRP A 473     127.081  75.164   1.168  1.00 24.54           C  
ANISOU 3592  CD1 TRP A 473     2856   3011   3458      2    -19    196       C  
ATOM   3593  CD2 TRP A 473     129.138  74.392   0.910  1.00 23.54           C  
ANISOU 3593  CD2 TRP A 473     2719   2877   3348     14    -24    206       C  
ATOM   3594  NE1 TRP A 473     127.741  76.035   0.392  1.00 24.58           N  
ANISOU 3594  NE1 TRP A 473     2856   3024   3460      8    -18    193       N  
ATOM   3595  CE2 TRP A 473     129.013  75.578   0.196  1.00 25.17           C  
ANISOU 3595  CE2 TRP A 473     2924   3095   3544     15    -20    198       C  
ATOM   3596  CE3 TRP A 473     130.358  73.719   0.890  1.00 24.78           C  
ANISOU 3596  CE3 TRP A 473     2870   3027   3516     22    -28    212       C  
ATOM   3597  CZ2 TRP A 473     130.066  76.119  -0.526  1.00 25.40           C  
ANISOU 3597  CZ2 TRP A 473     2947   3130   3574     21    -19    197       C  
ATOM   3598  CZ3 TRP A 473     131.386  74.255   0.179  1.00 25.08           C  
ANISOU 3598  CZ3 TRP A 473     2900   3072   3556     29    -27    209       C  
ATOM   3599  CH2 TRP A 473     131.239  75.445  -0.517  1.00 24.88           C  
ANISOU 3599  CH2 TRP A 473     2875   3060   3520     27    -22    201       C  
ATOM   3600  N   ALA A 474     126.937  75.114   4.401  1.00 26.53           N  
ANISOU 3600  N   ALA A 474     3119   3262   3700    -18    -31    224       N  
ATOM   3601  CA  ALA A 474     126.709  76.504   4.730  1.00 26.40           C  
ANISOU 3601  CA  ALA A 474     3103   3257   3670    -23    -31    222       C  
ATOM   3602  C   ALA A 474     127.491  77.141   5.855  1.00 26.83           C  
ANISOU 3602  C   ALA A 474     3159   3318   3718    -28    -38    235       C  
ATOM   3603  O   ALA A 474     127.994  78.211   5.692  1.00 27.38           O  
ANISOU 3603  O   ALA A 474     3226   3396   3783    -27    -38    234       O  
ATOM   3604  CB  ALA A 474     125.232  76.815   4.843  1.00 25.87           C  
ANISOU 3604  CB  ALA A 474     3040   3195   3594    -31    -26    212       C  
ATOM   3605  N   LYS A 475     127.566  76.474   6.980  1.00 26.55           N  
ANISOU 3605  N   LYS A 475     3127   3278   3683    -35    -42    246       N  
ATOM   3606  CA  LYS A 475     128.273  76.993   8.116  1.00 28.94           C  
ANISOU 3606  CA  LYS A 475     3430   3586   3979    -41    -49    259       C  
ATOM   3607  C   LYS A 475     129.813  76.871   8.055  1.00 27.16           C  
ANISOU 3607  C   LYS A 475     3198   3360   3760    -32    -56    268       C  
ATOM   3608  O   LYS A 475     130.472  77.533   8.770  1.00 26.44           O  
ANISOU 3608  O   LYS A 475     3106   3277   3664    -36    -61    275       O  
ATOM   3609  CB  LYS A 475     127.798  76.281   9.392  1.00 30.54           C  
ANISOU 3609  CB  LYS A 475     3641   3786   4178    -52    -53    269       C  
ATOM   3610  CG  LYS A 475     126.400  76.581   9.844  1.00 33.73           C  
ANISOU 3610  CG  LYS A 475     4050   4194   4571    -64    -47    261       C  
ATOM   3611  CD  LYS A 475     126.025  75.789  11.068  1.00 35.14           C  
ANISOU 3611  CD  LYS A 475     4237   4369   4746    -76    -50    272       C  
ATOM   3612  CE  LYS A 475     125.250  76.623  12.045  1.00 36.29           C  
ANISOU 3612  CE  LYS A 475     4386   4527   4877    -91    -49    269       C  
ATOM   3613  NZ  LYS A 475     124.559  75.798  13.044  1.00 36.59           N  
ANISOU 3613  NZ  LYS A 475     4433   4562   4910   -105    -48    275       N  
ATOM   3614  N   GLN A 476     130.344  76.009   7.206  1.00 27.48           N  
ANISOU 3614  N   GLN A 476     3235   3392   3815    -21    -56    267       N  
ATOM   3615  CA  GLN A 476     131.788  75.713   7.167  1.00 26.57           C  
ANISOU 3615  CA  GLN A 476     3111   3275   3708    -12    -62    274       C  
ATOM   3616  C   GLN A 476     132.605  76.834   6.516  1.00 25.69           C  
ANISOU 3616  C   GLN A 476     2992   3174   3593     -8    -60    269       C  
ATOM   3617  O   GLN A 476     132.112  77.586   5.677  1.00 25.56           O  
ANISOU 3617  O   GLN A 476     2976   3164   3573     -8    -53    257       O  
ATOM   3618  CB  GLN A 476     132.009  74.398   6.417  1.00 27.32           C  
ANISOU 3618  CB  GLN A 476     3204   3357   3820     -1    -62    272       C  
ATOM   3619  CG  GLN A 476     131.330  73.208   7.083  1.00 28.22           C  
ANISOU 3619  CG  GLN A 476     3327   3457   3938     -6    -64    279       C  
ATOM   3620  CD  GLN A 476     131.725  73.013   8.541  1.00 30.44           C  
ANISOU 3620  CD  GLN A 476     3613   3738   4215    -12    -74    297       C  
ATOM   3621  OE1 GLN A 476     132.911  73.100   8.923  1.00 30.24           O  
ANISOU 3621  OE1 GLN A 476     3582   3716   4192     -7    -83    306       O  
ATOM   3622  NE2 GLN A 476     130.734  72.778   9.376  1.00 32.58           N  
ANISOU 3622  NE2 GLN A 476     3894   4006   4478    -25    -74    301       N  
ATOM   3623  N   THR A 477     133.859  76.951   6.924  1.00 25.46           N  
ANISOU 3623  N   THR A 477     2957   3151   3568     -5    -67    277       N  
ATOM   3624  CA  THR A 477     134.743  77.973   6.430  1.00 24.85           C  
ANISOU 3624  CA  THR A 477     2872   3084   3487     -3    -66    273       C  
ATOM   3625  C   THR A 477     134.970  77.954   4.904  1.00 25.67           C  
ANISOU 3625  C   THR A 477     2969   3186   3598      6    -58    260       C  
ATOM   3626  O   THR A 477     135.005  79.036   4.265  1.00 24.37           O  
ANISOU 3626  O   THR A 477     2803   3030   3425      3    -52    253       O  
ATOM   3627  CB  THR A 477     136.084  77.894   7.161  1.00 24.57           C  
ANISOU 3627  CB  THR A 477     2829   3053   3454     -1    -75    284       C  
ATOM   3628  OG1 THR A 477     135.810  77.837   8.545  1.00 24.07           O  
ANISOU 3628  OG1 THR A 477     2772   2991   3384    -10    -82    295       O  
ATOM   3629  CG2 THR A 477     136.940  79.170   6.869  1.00 24.39           C  
ANISOU 3629  CG2 THR A 477     2799   3044   3424     -3    -73    279       C  
ATOM   3630  N   ILE A 478     135.135  76.745   4.336  1.00 25.20           N  
ANISOU 3630  N   ILE A 478     2906   3116   3552     15    -58    258       N  
ATOM   3631  CA  ILE A 478     135.350  76.570   2.905  1.00 25.76           C  
ANISOU 3631  CA  ILE A 478     2970   3186   3630     24    -50    245       C  
ATOM   3632  C   ILE A 478     134.242  77.152   2.032  1.00 25.04           C  
ANISOU 3632  C   ILE A 478     2885   3097   3530     20    -41    234       C  
ATOM   3633  O   ILE A 478     134.465  77.458   0.866  1.00 24.95           O  
ANISOU 3633  O   ILE A 478     2870   3090   3520     24    -35    224       O  
ATOM   3634  CB  ILE A 478     135.651  75.101   2.494  1.00 27.31           C  
ANISOU 3634  CB  ILE A 478     3163   3371   3844     35    -52    244       C  
ATOM   3635  CG1 ILE A 478     136.204  74.997   1.044  1.00 28.43           C  
ANISOU 3635  CG1 ILE A 478     3294   3514   3993     43    -44    230       C  
ATOM   3636  CG2 ILE A 478     134.435  74.235   2.631  1.00 28.20           C  
ANISOU 3636  CG2 ILE A 478     3285   3471   3960     33    -50    243       C  
ATOM   3637  CD1 ILE A 478     137.498  75.749   0.808  1.00 30.30           C  
ANISOU 3637  CD1 ILE A 478     3521   3764   4229     45    -45    229       C  
ATOM   3638  N   ALA A 479     133.058  77.319   2.599  1.00 23.98           N  
ANISOU 3638  N   ALA A 479     2762   2962   3389     13    -41    235       N  
ATOM   3639  CA  ALA A 479     131.980  77.953   1.913  1.00 23.97           C  
ANISOU 3639  CA  ALA A 479     2765   2964   3379     10    -34    224       C  
ATOM   3640  C   ALA A 479     132.013  79.481   1.883  1.00 24.49           C  
ANISOU 3640  C   ALA A 479     2833   3040   3431      4    -33    223       C  
ATOM   3641  O   ALA A 479     131.115  80.053   1.298  1.00 25.06           O  
ANISOU 3641  O   ALA A 479     2910   3115   3497      3    -28    214       O  
ATOM   3642  CB  ALA A 479     130.665  77.483   2.507  1.00 23.79           C  
ANISOU 3642  CB  ALA A 479     2750   2934   3353      4    -34    224       C  
ATOM   3643  N   HIS A 480     133.037  80.115   2.467  1.00 24.99           N  
ANISOU 3643  N   HIS A 480     2893   3110   3491      2    -37    230       N  
ATOM   3644  CA  HIS A 480     133.153  81.575   2.641  1.00 24.37           C  
ANISOU 3644  CA  HIS A 480     2818   3042   3401     -5    -36    230       C  
ATOM   3645  C   HIS A 480     134.430  82.137   1.993  1.00 23.84           C  
ANISOU 3645  C   HIS A 480     2744   2981   3334     -3    -34    229       C  
ATOM   3646  O   HIS A 480     135.429  81.412   1.802  1.00 21.27           O  
ANISOU 3646  O   HIS A 480     2408   2654   3018      2    -36    231       O  
ATOM   3647  CB  HIS A 480     133.245  81.870   4.133  1.00 26.08           C  
ANISOU 3647  CB  HIS A 480     3037   3261   3612    -14    -43    241       C  
ATOM   3648  CG  HIS A 480     131.988  81.600   4.837  1.00 26.36           C  
ANISOU 3648  CG  HIS A 480     3079   3292   3643    -19    -43    241       C  
ATOM   3649  ND1 HIS A 480     131.640  80.327   5.278  1.00 27.62           N  
ANISOU 3649  ND1 HIS A 480     3240   3443   3810    -17    -46    246       N  
ATOM   3650  CD2 HIS A 480     130.907  82.394   5.027  1.00 25.85           C  
ANISOU 3650  CD2 HIS A 480     3023   3231   3569    -24    -41    236       C  
ATOM   3651  CE1 HIS A 480     130.401  80.370   5.748  1.00 27.43           C  
ANISOU 3651  CE1 HIS A 480     3223   3419   3780    -24    -44    243       C  
ATOM   3652  NE2 HIS A 480     129.951  81.615   5.627  1.00 27.61           N  
ANISOU 3652  NE2 HIS A 480     3249   3448   3793    -28    -41    237       N  
ATOM   3653  N   ASN A 481     134.395  83.437   1.711  1.00 22.72           N  
ANISOU 3653  N   ASN A 481     2606   2845   3181     -9    -31    226       N  
ATOM   3654  CA  ASN A 481     135.525  84.134   1.172  1.00 24.14           C  
ANISOU 3654  CA  ASN A 481     2781   3031   3358    -10    -29    225       C  
ATOM   3655  C   ASN A 481     136.469  84.516   2.305  1.00 25.02           C  
ANISOU 3655  C   ASN A 481     2888   3149   3468    -16    -35    234       C  
ATOM   3656  O   ASN A 481     136.525  85.692   2.710  1.00 26.62           O  
ANISOU 3656  O   ASN A 481     3096   3357   3660    -25    -34    235       O  
ATOM   3657  CB  ASN A 481     135.061  85.372   0.388  1.00 24.13           C  
ANISOU 3657  CB  ASN A 481     2789   3033   3347    -14    -23    218       C  
ATOM   3658  CG  ASN A 481     133.981  85.051  -0.635  1.00 24.66           C  
ANISOU 3658  CG  ASN A 481     2860   3095   3413     -7    -19    210       C  
ATOM   3659  OD1 ASN A 481     134.121  84.132  -1.437  1.00 26.11           O  
ANISOU 3659  OD1 ASN A 481     3038   3276   3605     -1    -16    205       O  
ATOM   3660  ND2 ASN A 481     132.915  85.853  -0.658  1.00 24.77           N  
ANISOU 3660  ND2 ASN A 481     2885   3108   3419    -10    -19    207       N  
ATOM   3661  N   THR A 482     137.187  83.529   2.850  1.00 25.61           N  
ANISOU 3661  N   THR A 482     2954   3224   3553    -12    -40    240       N  
ATOM   3662  CA  THR A 482     138.176  83.758   3.925  1.00 26.31           C  
ANISOU 3662  CA  THR A 482     3037   3319   3640    -17    -47    248       C  
ATOM   3663  C   THR A 482     139.194  82.577   3.984  1.00 27.64           C  
ANISOU 3663  C   THR A 482     3193   3487   3823     -8    -52    252       C  
ATOM   3664  O   THR A 482     139.035  81.581   3.252  1.00 27.77           O  
ANISOU 3664  O   THR A 482     3206   3495   3849      2    -50    247       O  
ATOM   3665  CB  THR A 482     137.515  84.004   5.281  1.00 27.39           C  
ANISOU 3665  CB  THR A 482     3181   3455   3769    -25    -53    256       C  
ATOM   3666  OG1 THR A 482     138.451  84.626   6.171  1.00 27.87           O  
ANISOU 3666  OG1 THR A 482     3237   3527   3825    -32    -57    262       O  
ATOM   3667  CG2 THR A 482     136.995  82.725   5.918  1.00 28.18           C  
ANISOU 3667  CG2 THR A 482     3283   3548   3878    -20    -58    262       C  
ATOM   3668  N   LEU A 483     140.227  82.706   4.816  1.00 26.23           N  
ANISOU 3668  N   LEU A 483     3006   3316   3643    -10    -59    258       N  
ATOM   3669  CA  LEU A 483     141.291  81.722   4.872  1.00 27.78           C  
ANISOU 3669  CA  LEU A 483     3189   3513   3853     -1    -65    261       C  
ATOM   3670  C   LEU A 483     140.839  80.371   5.471  1.00 27.09           C  
ANISOU 3670  C   LEU A 483     3104   3413   3775      7    -73    269       C  
ATOM   3671  O   LEU A 483     140.209  80.355   6.485  1.00 27.32           O  
ANISOU 3671  O   LEU A 483     3142   3440   3798      1    -78    278       O  
ATOM   3672  CB  LEU A 483     142.464  82.289   5.692  1.00 29.01           C  
ANISOU 3672  CB  LEU A 483     3337   3682   4005     -6    -71    266       C  
ATOM   3673  CG  LEU A 483     143.740  81.450   5.613  1.00 31.08           C  
ANISOU 3673  CG  LEU A 483     3582   3947   4280      4    -77    267       C  
ATOM   3674  CD1 LEU A 483     144.426  81.605   4.286  1.00 31.69           C  
ANISOU 3674  CD1 LEU A 483     3649   4029   4362      8    -68    254       C  
ATOM   3675  CD2 LEU A 483     144.706  81.871   6.696  1.00 34.53           C  
ANISOU 3675  CD2 LEU A 483     4011   4396   4712     -1    -86    274       C  
ATOM   3676  N   VAL A 484     141.165  79.264   4.813  1.00 28.08           N  
ANISOU 3676  N   VAL A 484     3223   3532   3916     19    -73    265       N  
ATOM   3677  CA  VAL A 484     141.020  77.925   5.349  1.00 28.60           C  
ANISOU 3677  CA  VAL A 484     3289   3585   3992     28    -81    273       C  
ATOM   3678  C   VAL A 484     142.422  77.277   5.437  1.00 28.51           C  
ANISOU 3678  C   VAL A 484     3262   3576   3993     39    -89    275       C  
ATOM   3679  O   VAL A 484     143.170  77.276   4.471  1.00 30.19           O  
ANISOU 3679  O   VAL A 484     3463   3793   4213     45    -84    265       O  
ATOM   3680  CB  VAL A 484     140.128  77.034   4.465  1.00 30.28           C  
ANISOU 3680  CB  VAL A 484     3507   3784   4214     34    -75    266       C  
ATOM   3681  CG1 VAL A 484     139.601  75.848   5.218  1.00 29.89           C  
ANISOU 3681  CG1 VAL A 484     3465   3721   4172     38    -82    276       C  
ATOM   3682  CG2 VAL A 484     138.942  77.812   3.914  1.00 34.06           C  
ANISOU 3682  CG2 VAL A 484     3997   4263   4681     26    -65    259       C  
ATOM   3683  N   GLN A 485     142.732  76.696   6.591  1.00 28.42           N  
ANISOU 3683  N   GLN A 485     3251   3562   3985     41   -101    289       N  
ATOM   3684  CA  GLN A 485     144.033  76.105   6.886  1.00 28.61           C  
ANISOU 3684  CA  GLN A 485     3260   3589   4020     52   -112    293       C  
ATOM   3685  C   GLN A 485     143.801  74.607   7.020  1.00 27.85           C  
ANISOU 3685  C   GLN A 485     3168   3475   3940     64   -119    299       C  
ATOM   3686  O   GLN A 485     142.916  74.173   7.798  1.00 27.31           O  
ANISOU 3686  O   GLN A 485     3114   3396   3868     60   -123    309       O  
ATOM   3687  CB  GLN A 485     144.602  76.685   8.183  1.00 29.14           C  
ANISOU 3687  CB  GLN A 485     3326   3669   4078     45   -122    304       C  
ATOM   3688  CG  GLN A 485     145.992  76.158   8.536  1.00 30.25           C  
ANISOU 3688  CG  GLN A 485     3451   3815   4229     56   -134    308       C  
ATOM   3689  CD  GLN A 485     146.524  76.777   9.802  1.00 30.62           C  
ANISOU 3689  CD  GLN A 485     3495   3875   4264     48   -145    319       C  
ATOM   3690  OE1 GLN A 485     146.951  77.936   9.813  1.00 30.29           O  
ANISOU 3690  OE1 GLN A 485     3449   3850   4212     38   -140    314       O  
ATOM   3691  NE2 GLN A 485     146.495  76.017  10.893  1.00 31.04           N  
ANISOU 3691  NE2 GLN A 485     3553   3921   4318     52   -159    334       N  
ATOM   3692  N   ASN A 486     144.561  73.844   6.249  1.00 27.29           N  
ANISOU 3692  N   ASN A 486     3084   3399   3885     79   -119    291       N  
ATOM   3693  CA  ASN A 486     144.567  72.379   6.295  1.00 27.35           C  
ANISOU 3693  CA  ASN A 486     3092   3388   3910     93   -126    295       C  
ATOM   3694  C   ASN A 486     143.174  71.773   6.244  1.00 27.96           C  
ANISOU 3694  C   ASN A 486     3188   3449   3987     89   -121    297       C  
ATOM   3695  O   ASN A 486     142.824  70.901   7.020  1.00 28.23           O  
ANISOU 3695  O   ASN A 486     3231   3469   4025     92   -130    310       O  
ATOM   3696  CB  ASN A 486     145.371  71.853   7.500  1.00 28.25           C  
ANISOU 3696  CB  ASN A 486     3204   3503   4029    100   -144    311       C  
ATOM   3697  CG  ASN A 486     146.807  72.377   7.513  1.00 29.75           C  
ANISOU 3697  CG  ASN A 486     3373   3710   4220    105   -149    306       C  
ATOM   3698  OD1 ASN A 486     147.366  72.627   6.475  1.00 30.97           O  
ANISOU 3698  OD1 ASN A 486     3515   3872   4381    109   -140    291       O  
ATOM   3699  ND2 ASN A 486     147.390  72.553   8.699  1.00 30.41           N  
ANISOU 3699  ND2 ASN A 486     3455   3802   4298    104   -163    320       N  
ATOM   3700  N   GLU A 487     142.369  72.272   5.317  1.00 28.65           N  
ANISOU 3700  N   GLU A 487     3280   3538   4069     83   -107    285       N  
ATOM   3701  CA  GLU A 487     141.032  71.728   5.055  1.00 29.68           C  
ANISOU 3701  CA  GLU A 487     3424   3654   4199     79   -101    284       C  
ATOM   3702  C   GLU A 487     140.196  71.589   6.287  1.00 29.65           C  
ANISOU 3702  C   GLU A 487     3435   3644   4186     69   -107    299       C  
ATOM   3703  O   GLU A 487     139.469  70.630   6.405  1.00 28.29           O  
ANISOU 3703  O   GLU A 487     3273   3455   4020     70   -108    302       O  
ATOM   3704  CB  GLU A 487     141.140  70.393   4.341  1.00 30.24           C  
ANISOU 3704  CB  GLU A 487     3492   3708   4290     93   -100    277       C  
ATOM   3705  CG  GLU A 487     141.850  70.616   3.040  1.00 31.70           C  
ANISOU 3705  CG  GLU A 487     3662   3901   4481    100    -92    260       C  
ATOM   3706  CD  GLU A 487     141.907  69.424   2.108  1.00 33.80           C  
ANISOU 3706  CD  GLU A 487     3924   4153   4767    114    -88    249       C  
ATOM   3707  OE1 GLU A 487     141.071  68.470   2.200  1.00 35.32           O  
ANISOU 3707  OE1 GLU A 487     4127   4327   4966    115    -88    252       O  
ATOM   3708  OE2 GLU A 487     142.780  69.538   1.231  1.00 34.09           O  
ANISOU 3708  OE2 GLU A 487     3945   4198   4810    121    -84    236       O  
ATOM   3709  N   THR A 488     140.337  72.560   7.203  1.00 28.88           N  
ANISOU 3709  N   THR A 488     3340   3560   4074     59   -112    307       N  
ATOM   3710  CA  THR A 488     139.709  72.543   8.504  1.00 28.18           C  
ANISOU 3710  CA  THR A 488     3264   3469   3975     48   -119    322       C  
ATOM   3711  C   THR A 488     139.025  73.890   8.715  1.00 27.35           C  
ANISOU 3711  C   THR A 488     3164   3377   3850     33   -112    319       C  
ATOM   3712  O   THR A 488     139.606  74.944   8.400  1.00 25.74           O  
ANISOU 3712  O   THR A 488     2952   3188   3640     30   -108    312       O  
ATOM   3713  CB  THR A 488     140.811  72.300   9.577  1.00 31.48           C  
ANISOU 3713  CB  THR A 488     3676   3890   4394     53   -134    337       C  
ATOM   3714  OG1 THR A 488     141.476  71.055   9.312  1.00 31.77           O  
ANISOU 3714  OG1 THR A 488     3707   3913   4450     70   -142    339       O  
ATOM   3715  CG2 THR A 488     140.296  72.323  11.007  1.00 31.16           C  
ANISOU 3715  CG2 THR A 488     3649   3850   4341     41   -143    353       C  
ATOM   3716  N   SER A 489     137.809  73.868   9.289  1.00 26.26           N  
ANISOU 3716  N   SER A 489     3040   3234   3703     21   -109    323       N  
ATOM   3717  CA  SER A 489     137.082  75.086   9.588  1.00 26.37           C  
ANISOU 3717  CA  SER A 489     3060   3260   3700      7   -103    320       C  
ATOM   3718  C   SER A 489     137.697  75.808  10.777  1.00 27.69           C  
ANISOU 3718  C   SER A 489     3225   3440   3855     -1   -112    330       C  
ATOM   3719  O   SER A 489     138.349  75.227  11.635  1.00 27.61           O  
ANISOU 3719  O   SER A 489     3214   3429   3848      2   -124    343       O  
ATOM   3720  CB  SER A 489     135.592  74.848   9.861  1.00 27.01           C  
ANISOU 3720  CB  SER A 489     3154   3334   3774     -3    -98    319       C  
ATOM   3721  OG  SER A 489     134.903  74.563   8.652  1.00 26.65           O  
ANISOU 3721  OG  SER A 489     3108   3281   3735      2    -88    305       O  
ATOM   3722  N   HIS A 490     137.443  77.106  10.828  1.00 26.65           N  
ANISOU 3722  N   HIS A 490     3094   3321   3710    -11   -106    324       N  
ATOM   3723  CA  HIS A 490     137.789  77.869  12.002  1.00 26.69           C  
ANISOU 3723  CA  HIS A 490     3100   3339   3702    -21   -113    333       C  
ATOM   3724  C   HIS A 490     137.268  77.219  13.256  1.00 27.04           C  
ANISOU 3724  C   HIS A 490     3154   3379   3741    -29   -120    346       C  
ATOM   3725  O   HIS A 490     136.088  76.772  13.275  1.00 26.85           O  
ANISOU 3725  O   HIS A 490     3141   3346   3716    -34   -115    345       O  
ATOM   3726  CB  HIS A 490     137.202  79.264  11.898  1.00 25.82           C  
ANISOU 3726  CB  HIS A 490     2993   3239   3579    -32   -104    323       C  
ATOM   3727  CG  HIS A 490     137.778  80.039  10.769  1.00 26.13           C  
ANISOU 3727  CG  HIS A 490     3024   3284   3621    -27    -97    311       C  
ATOM   3728  ND1 HIS A 490     137.292  81.259  10.389  1.00 26.41           N  
ANISOU 3728  ND1 HIS A 490     3062   3325   3646    -35    -88    302       N  
ATOM   3729  CD2 HIS A 490     138.780  79.748   9.917  1.00 25.19           C  
ANISOU 3729  CD2 HIS A 490     2893   3165   3513    -16    -97    308       C  
ATOM   3730  CE1 HIS A 490     138.014  81.721   9.382  1.00 26.15           C  
ANISOU 3730  CE1 HIS A 490     3022   3297   3618    -29    -84    294       C  
ATOM   3731  NE2 HIS A 490     138.897  80.803   9.055  1.00 25.30           N  
ANISOU 3731  NE2 HIS A 490     2905   3186   3523    -19    -88    296       N  
ATOM   3732  N   PHE A 491     138.118  77.188  14.303  1.00 26.07           N  
ANISOU 3732  N   PHE A 491     3028   3263   3614    -31   -132    359       N  
ATOM   3733  CA  PHE A 491     137.744  76.574  15.605  1.00 27.19           C  
ANISOU 3733  CA  PHE A 491     3181   3402   3749    -39   -141    374       C  
ATOM   3734  C   PHE A 491     137.342  75.087  15.469  1.00 26.80           C  
ANISOU 3734  C   PHE A 491     3139   3334   3712    -31   -144    381       C  
ATOM   3735  O   PHE A 491     136.599  74.549  16.322  1.00 27.05           O  
ANISOU 3735  O   PHE A 491     3182   3359   3736    -41   -147    391       O  
ATOM   3736  CB  PHE A 491     136.583  77.341  16.296  1.00 26.13           C  
ANISOU 3736  CB  PHE A 491     3056   3275   3597    -57   -134    372       C  
ATOM   3737  CG  PHE A 491     136.749  78.845  16.319  1.00 25.82           C  
ANISOU 3737  CG  PHE A 491     3012   3251   3547    -65   -129    362       C  
ATOM   3738  CD1 PHE A 491     137.765  79.442  17.048  1.00 26.18           C  
ANISOU 3738  CD1 PHE A 491     3051   3311   3585    -68   -137    368       C  
ATOM   3739  CD2 PHE A 491     135.886  79.675  15.550  1.00 25.39           C  
ANISOU 3739  CD2 PHE A 491     2960   3199   3490    -68   -116    347       C  
ATOM   3740  CE1 PHE A 491     137.906  80.847  17.071  1.00 26.44           C  
ANISOU 3740  CE1 PHE A 491     3079   3357   3608    -77   -132    359       C  
ATOM   3741  CE2 PHE A 491     136.029  81.057  15.553  1.00 25.02           C  
ANISOU 3741  CE2 PHE A 491     2909   3163   3432    -75   -112    339       C  
ATOM   3742  CZ  PHE A 491     137.047  81.642  16.320  1.00 25.50           C  
ANISOU 3742  CZ  PHE A 491     2964   3237   3486    -80   -119    345       C  
ATOM   3743  N   GLU A 492     137.794  74.463  14.391  1.00 28.17           N  
ANISOU 3743  N   GLU A 492     3305   3497   3902    -16   -142    375       N  
ATOM   3744  CA  GLU A 492     137.391  73.077  13.988  1.00 30.32           C  
ANISOU 3744  CA  GLU A 492     3583   3748   4188     -7   -143    378       C  
ATOM   3745  C   GLU A 492     135.887  72.919  13.850  1.00 30.89           C  
ANISOU 3745  C   GLU A 492     3668   3814   4256    -18   -132    372       C  
ATOM   3746  O   GLU A 492     135.349  71.853  14.057  1.00 28.12           O  
ANISOU 3746  O   GLU A 492     3328   3448   3910    -19   -134    378       O  
ATOM   3747  CB  GLU A 492     137.976  72.037  14.942  1.00 32.70           C  
ANISOU 3747  CB  GLU A 492     3889   4042   4495     -3   -158    396       C  
ATOM   3748  CG  GLU A 492     139.513  72.066  15.004  1.00 36.82           C  
ANISOU 3748  CG  GLU A 492     4396   4570   5024     11   -170    401       C  
ATOM   3749  CD  GLU A 492     140.118  71.053  16.002  1.00 41.22           C  
ANISOU 3749  CD  GLU A 492     4958   5119   5585     17   -188    421       C  
ATOM   3750  OE1 GLU A 492     139.488  70.676  17.019  1.00 46.13           O  
ANISOU 3750  OE1 GLU A 492     5595   5736   6197      5   -193    435       O  
ATOM   3751  OE2 GLU A 492     141.266  70.678  15.799  1.00 45.34           O  
ANISOU 3751  OE2 GLU A 492     5467   5639   6119     32   -197    423       O  
ATOM   3752  N   GLY A 493     135.197  74.012  13.481  1.00 30.36           N  
ANISOU 3752  N   GLY A 493     3600   3757   4178    -27   -121    359       N  
ATOM   3753  CA  GLY A 493     133.769  73.966  13.391  1.00 31.28           C  
ANISOU 3753  CA  GLY A 493     3726   3869   4288    -37   -111    352       C  
ATOM   3754  C   GLY A 493     133.045  73.537  14.659  1.00 31.90           C  
ANISOU 3754  C   GLY A 493     3819   3946   4357    -51   -115    364       C  
ATOM   3755  O   GLY A 493     131.955  73.019  14.556  1.00 30.69           O  
ANISOU 3755  O   GLY A 493     3674   3784   4203    -58   -109    360       O  
ATOM   3756  N   LYS A 494     133.625  73.796  15.841  1.00 32.99           N  
ANISOU 3756  N   LYS A 494     3958   4092   4485    -58   -125    377       N  
ATOM   3757  CA  LYS A 494     133.007  73.456  17.122  1.00 32.76           C  
ANISOU 3757  CA  LYS A 494     3941   4063   4443    -73   -129    390       C  
ATOM   3758  C   LYS A 494     132.441  74.659  17.871  1.00 31.68           C  
ANISOU 3758  C   LYS A 494     3806   3944   4287    -90   -125    385       C  
ATOM   3759  O   LYS A 494     133.176  75.605  18.219  1.00 30.25           O  
ANISOU 3759  O   LYS A 494     3618   3777   4100    -91   -129    386       O  
ATOM   3760  CB  LYS A 494     134.033  72.815  18.024  1.00 34.97           C  
ANISOU 3760  CB  LYS A 494     4223   4340   4725    -70   -145    409       C  
ATOM   3761  CG  LYS A 494     134.677  71.519  17.508  1.00 36.71           C  
ANISOU 3761  CG  LYS A 494     4442   4542   4964    -52   -152    417       C  
ATOM   3762  CD  LYS A 494     135.412  70.876  18.674  1.00 39.51           C  
ANISOU 3762  CD  LYS A 494     4802   4893   5315    -52   -169    438       C  
ATOM   3763  CE  LYS A 494     136.734  70.273  18.310  1.00 45.86           C  
ANISOU 3763  CE  LYS A 494     5597   5691   6138    -32   -181    444       C  
ATOM   3764  NZ  LYS A 494     136.557  68.970  17.661  1.00 48.18           N  
ANISOU 3764  NZ  LYS A 494     5896   5961   6449    -20   -181    445       N  
ATOM   3765  N   TYR A 495     131.136  74.609  18.145  1.00 29.88           N  
ANISOU 3765  N   TYR A 495     3587   3715   4050   -104   -116    380       N  
ATOM   3766  CA  TYR A 495     130.446  75.694  18.799  1.00 29.88           C  
ANISOU 3766  CA  TYR A 495     3589   3731   4034   -119   -111    373       C  
ATOM   3767  C   TYR A 495     131.058  76.027  20.183  1.00 32.54           C  
ANISOU 3767  C   TYR A 495     3928   4080   4356   -130   -121    387       C  
ATOM   3768  O   TYR A 495     131.253  77.217  20.539  1.00 32.32           O  
ANISOU 3768  O   TYR A 495     3895   4068   4318   -136   -120    381       O  
ATOM   3769  CB  TYR A 495     128.931  75.399  18.916  1.00 30.08           C  
ANISOU 3769  CB  TYR A 495     3623   3754   4053   -132   -101    365       C  
ATOM   3770  CG  TYR A 495     128.221  76.574  19.488  1.00 29.68           C  
ANISOU 3770  CG  TYR A 495     3572   3720   3986   -147    -94    355       C  
ATOM   3771  CD1 TYR A 495     127.939  77.687  18.684  1.00 29.92           C  
ANISOU 3771  CD1 TYR A 495     3594   3757   4017   -142    -86    337       C  
ATOM   3772  CD2 TYR A 495     127.978  76.679  20.874  1.00 29.94           C  
ANISOU 3772  CD2 TYR A 495     3611   3761   4002   -164    -97    363       C  
ATOM   3773  CE1 TYR A 495     127.343  78.833  19.212  1.00 28.94           C  
ANISOU 3773  CE1 TYR A 495     3469   3647   3879   -153    -81    327       C  
ATOM   3774  CE2 TYR A 495     127.413  77.832  21.415  1.00 29.47           C  
ANISOU 3774  CE2 TYR A 495     3551   3719   3929   -177    -92    352       C  
ATOM   3775  CZ  TYR A 495     127.076  78.910  20.560  1.00 29.96           C  
ANISOU 3775  CZ  TYR A 495     3604   3785   3993   -170    -83    333       C  
ATOM   3776  OH  TYR A 495     126.511  80.083  21.066  1.00 31.46           O  
ANISOU 3776  OH  TYR A 495     3793   3990   4171   -181    -78    321       O  
ATOM   3777  N   GLU A 496     131.388  74.982  20.943  1.00 31.45           N  
ANISOU 3777  N   GLU A 496     3797   3934   4218   -132   -131    405       N  
ATOM   3778  CA  GLU A 496     131.910  75.149  22.256  1.00 34.09           C  
ANISOU 3778  CA  GLU A 496     4135   4279   4538   -142   -142    420       C  
ATOM   3779  C   GLU A 496     133.262  75.869  22.280  1.00 33.05           C  
ANISOU 3779  C   GLU A 496     3991   4159   4408   -133   -150    422       C  
ATOM   3780  O   GLU A 496     133.564  76.477  23.294  1.00 33.39           O  
ANISOU 3780  O   GLU A 496     4034   4216   4436   -144   -156    428       O  
ATOM   3781  CB  GLU A 496     131.925  73.813  23.058  1.00 37.44           C  
ANISOU 3781  CB  GLU A 496     4573   4692   4962   -146   -152    440       C  
ATOM   3782  CG  GLU A 496     132.864  72.750  22.544  1.00 40.98           C  
ANISOU 3782  CG  GLU A 496     5019   5123   5429   -127   -162    451       C  
ATOM   3783  CD  GLU A 496     132.324  71.880  21.388  1.00 44.77           C  
ANISOU 3783  CD  GLU A 496     5502   5583   5926   -117   -154    443       C  
ATOM   3784  OE1 GLU A 496     131.223  72.134  20.782  1.00 39.35           O  
ANISOU 3784  OE1 GLU A 496     4816   4897   5240   -123   -140    427       O  
ATOM   3785  OE2 GLU A 496     133.070  70.906  21.080  1.00 51.22           O  
ANISOU 3785  OE2 GLU A 496     6319   6385   6759   -102   -164    453       O  
ATOM   3786  N   VAL A 497     134.026  75.847  21.180  1.00 31.83           N  
ANISOU 3786  N   VAL A 497     3827   3999   4270   -114   -151    417       N  
ATOM   3787  CA  VAL A 497     135.274  76.616  21.047  1.00 31.24           C  
ANISOU 3787  CA  VAL A 497     3738   3935   4197   -106   -157    416       C  
ATOM   3788  C   VAL A 497     134.977  78.019  20.467  1.00 31.69           C  
ANISOU 3788  C   VAL A 497     3788   4003   4249   -110   -145    397       C  
ATOM   3789  O   VAL A 497     135.341  79.030  21.063  1.00 31.63           O  
ANISOU 3789  O   VAL A 497     3777   4012   4230   -118   -146    395       O  
ATOM   3790  CB  VAL A 497     136.295  75.870  20.169  1.00 31.07           C  
ANISOU 3790  CB  VAL A 497     3707   3902   4194    -85   -163    419       C  
ATOM   3791  CG1 VAL A 497     137.576  76.661  20.033  1.00 30.39           C  
ANISOU 3791  CG1 VAL A 497     3607   3830   4110    -78   -168    416       C  
ATOM   3792  CG2 VAL A 497     136.633  74.497  20.803  1.00 31.72           C  
ANISOU 3792  CG2 VAL A 497     3798   3972   4282    -80   -177    438       C  
ATOM   3793  N   GLY A 498     134.304  78.057  19.320  1.00 30.63           N  
ANISOU 3793  N   GLY A 498     3654   3861   4124   -104   -133    383       N  
ATOM   3794  CA  GLY A 498     134.059  79.307  18.599  1.00 30.45           C  
ANISOU 3794  CA  GLY A 498     3625   3845   4098   -104   -123    366       C  
ATOM   3795  C   GLY A 498     133.274  80.336  19.410  1.00 29.87           C  
ANISOU 3795  C   GLY A 498     3557   3785   4008   -121   -117    360       C  
ATOM   3796  O   GLY A 498     133.576  81.536  19.359  1.00 26.89           O  
ANISOU 3796  O   GLY A 498     3174   3419   3625   -124   -114    351       O  
ATOM   3797  N   SER A 499     132.269  79.851  20.163  1.00 28.01           N  
ANISOU 3797  N   SER A 499     3331   3548   3764   -133   -116    363       N  
ATOM   3798  CA  SER A 499     131.471  80.705  21.071  1.00 28.31           C  
ANISOU 3798  CA  SER A 499     3374   3599   3785   -151   -111    357       C  
ATOM   3799  C   SER A 499     132.276  81.450  22.145  1.00 27.91           C  
ANISOU 3799  C   SER A 499     3320   3564   3722   -160   -118    364       C  
ATOM   3800  O   SER A 499     131.783  82.419  22.686  1.00 27.99           O  
ANISOU 3800  O   SER A 499     3330   3584   3719   -172   -113    355       O  
ATOM   3801  CB  SER A 499     130.393  79.868  21.808  1.00 30.25           C  
ANISOU 3801  CB  SER A 499     3630   3840   4023   -164   -109    362       C  
ATOM   3802  OG  SER A 499     131.023  78.874  22.649  1.00 28.40           O  
ANISOU 3802  OG  SER A 499     3401   3603   3788   -166   -121    382       O  
ATOM   3803  N   GLN A 500     133.492  81.018  22.445  1.00 27.28           N  
ANISOU 3803  N   GLN A 500     3236   3485   3646   -154   -130    378       N  
ATOM   3804  CA  GLN A 500     134.386  81.745  23.377  1.00 29.49           C  
ANISOU 3804  CA  GLN A 500     3510   3780   3913   -162   -138    383       C  
ATOM   3805  C   GLN A 500     135.270  82.816  22.693  1.00 30.07           C  
ANISOU 3805  C   GLN A 500     3573   3861   3992   -154   -136    373       C  
ATOM   3806  O   GLN A 500     136.080  83.442  23.353  1.00 29.85           O  
ANISOU 3806  O   GLN A 500     3539   3846   3956   -160   -142    376       O  
ATOM   3807  CB  GLN A 500     135.298  80.728  24.130  1.00 31.91           C  
ANISOU 3807  CB  GLN A 500     3818   4086   4220   -159   -154    404       C  
ATOM   3808  CG  GLN A 500     134.520  79.577  24.828  1.00 34.32           C  
ANISOU 3808  CG  GLN A 500     4136   4383   4520   -167   -157    417       C  
ATOM   3809  CD  GLN A 500     133.360  80.145  25.664  1.00 38.11           C  
ANISOU 3809  CD  GLN A 500     4624   4873   4982   -188   -149    410       C  
ATOM   3810  OE1 GLN A 500     133.607  80.916  26.597  1.00 39.44           O  
ANISOU 3810  OE1 GLN A 500     4792   5058   5136   -200   -151    410       O  
ATOM   3811  NE2 GLN A 500     132.082  79.855  25.271  1.00 40.02           N  
ANISOU 3811  NE2 GLN A 500     4874   5107   5227   -192   -137    401       N  
ATOM   3812  N   HIS A 501     135.180  82.983  21.380  1.00 30.65           N  
ANISOU 3812  N   HIS A 501     3643   3926   4078   -142   -128    362       N  
ATOM   3813  CA  HIS A 501     136.183  83.771  20.653  1.00 31.62           C  
ANISOU 3813  CA  HIS A 501     3755   4053   4207   -134   -127    356       C  
ATOM   3814  C   HIS A 501     135.537  84.738  19.676  1.00 30.53           C  
ANISOU 3814  C   HIS A 501     3617   3912   4070   -133   -114    338       C  
ATOM   3815  O   HIS A 501     134.416  84.519  19.201  1.00 33.54           O  
ANISOU 3815  O   HIS A 501     4005   4285   4454   -132   -107    331       O  
ATOM   3816  CB  HIS A 501     137.170  82.876  19.920  1.00 31.82           C  
ANISOU 3816  CB  HIS A 501     3772   4070   4247   -117   -134    363       C  
ATOM   3817  CG  HIS A 501     138.058  82.087  20.819  1.00 31.53           C  
ANISOU 3817  CG  HIS A 501     3732   4037   4209   -116   -149    380       C  
ATOM   3818  ND1 HIS A 501     139.023  82.669  21.614  1.00 33.50           N  
ANISOU 3818  ND1 HIS A 501     3976   4303   4451   -122   -157    384       N  
ATOM   3819  CD2 HIS A 501     138.149  80.748  21.032  1.00 33.47           C  
ANISOU 3819  CD2 HIS A 501     3982   4272   4462   -109   -157    393       C  
ATOM   3820  CE1 HIS A 501     139.659  81.722  22.299  1.00 33.52           C  
ANISOU 3820  CE1 HIS A 501     3978   4305   4455   -118   -171    400       C  
ATOM   3821  NE2 HIS A 501     139.151  80.546  21.958  1.00 33.91           N  
ANISOU 3821  NE2 HIS A 501     4033   4337   4513   -110   -171    406       N  
ATOM   3822  N   HIS A 502     136.256  85.798  19.375  1.00 28.17           N  
ANISOU 3822  N   HIS A 502     3312   3621   3771   -133   -112    332       N  
ATOM   3823  CA  HIS A 502     135.846  86.786  18.386  1.00 28.24           C  
ANISOU 3823  CA  HIS A 502     3322   3627   3781   -131   -101    316       C  
ATOM   3824  C   HIS A 502     137.056  87.358  17.670  1.00 27.61           C  
ANISOU 3824  C   HIS A 502     3233   3551   3707   -125   -101    314       C  
ATOM   3825  O   HIS A 502     138.127  87.386  18.223  1.00 27.67           O  
ANISOU 3825  O   HIS A 502     3233   3568   3712   -128   -109    320       O  
ATOM   3826  CB  HIS A 502     135.072  87.920  19.094  1.00 28.40           C  
ANISOU 3826  CB  HIS A 502     3348   3655   3788   -145    -96    307       C  
ATOM   3827  CG  HIS A 502     135.850  88.583  20.188  1.00 29.38           C  
ANISOU 3827  CG  HIS A 502     3469   3793   3901   -157   -101    311       C  
ATOM   3828  ND1 HIS A 502     136.716  89.636  19.954  1.00 31.51           N  
ANISOU 3828  ND1 HIS A 502     3733   4070   4170   -159   -100    305       N  
ATOM   3829  CD2 HIS A 502     135.922  88.326  21.519  1.00 29.57           C  
ANISOU 3829  CD2 HIS A 502     3494   3827   3914   -168   -108    320       C  
ATOM   3830  CE1 HIS A 502     137.288  90.001  21.094  1.00 30.67           C  
ANISOU 3830  CE1 HIS A 502     3624   3977   4053   -171   -106    310       C  
ATOM   3831  NE2 HIS A 502     136.830  89.212  22.053  1.00 30.89           N  
ANISOU 3831  NE2 HIS A 502     3656   4008   4075   -176   -111    319       N  
ATOM   3832  N   SER A 503     136.883  87.877  16.457  1.00 29.57           N  
ANISOU 3832  N   SER A 503     3482   3793   3961   -119    -93    303       N  
ATOM   3833  CA  SER A 503     137.970  88.639  15.820  1.00 27.84           C  
ANISOU 3833  CA  SER A 503     3256   3579   3745   -117    -91    299       C  
ATOM   3834  C   SER A 503     138.094  90.009  16.483  1.00 29.01           C  
ANISOU 3834  C   SER A 503     3405   3736   3880   -131    -89    293       C  
ATOM   3835  O   SER A 503     137.232  90.393  17.288  1.00 27.36           O  
ANISOU 3835  O   SER A 503     3204   3530   3662   -140    -87    291       O  
ATOM   3836  CB  SER A 503     137.732  88.707  14.341  1.00 28.12           C  
ANISOU 3836  CB  SER A 503     3292   3604   3789   -107    -83    290       C  
ATOM   3837  OG  SER A 503     137.705  87.408  13.759  1.00 27.78           O  
ANISOU 3837  OG  SER A 503     3246   3553   3757    -94    -85    294       O  
ATOM   3838  N   GLU A 504     139.188  90.717  16.192  1.00 31.30           N  
ANISOU 3838  N   GLU A 504     3689   4034   4170   -133    -88    290       N  
ATOM   3839  CA  GLU A 504     139.524  91.974  16.839  1.00 34.14           C  
ANISOU 3839  CA  GLU A 504     4049   4403   4519   -147    -86    285       C  
ATOM   3840  C   GLU A 504     139.695  93.102  15.804  1.00 30.83           C  
ANISOU 3840  C   GLU A 504     3633   3980   4101   -147    -77    274       C  
ATOM   3841  O   GLU A 504     140.539  93.025  14.910  1.00 28.08           O  
ANISOU 3841  O   GLU A 504     3278   3632   3759   -142    -75    274       O  
ATOM   3842  CB  GLU A 504     140.862  91.865  17.582  1.00 41.37           C  
ANISOU 3842  CB  GLU A 504     4953   5333   5432   -152    -95    292       C  
ATOM   3843  CG  GLU A 504     140.938  90.785  18.647  1.00 49.88           C  
ANISOU 3843  CG  GLU A 504     6028   6416   6508   -151   -106    305       C  
ATOM   3844  CD  GLU A 504     140.409  91.211  20.011  1.00 56.91           C  
ANISOU 3844  CD  GLU A 504     6924   7315   7384   -166   -109    307       C  
ATOM   3845  OE1 GLU A 504     139.800  92.324  20.152  1.00 61.06           O  
ANISOU 3845  OE1 GLU A 504     7457   7841   7903   -176   -101    296       O  
ATOM   3846  OE2 GLU A 504     140.607  90.392  20.948  1.00 63.23           O  
ANISOU 3846  OE2 GLU A 504     7722   8122   8182   -167   -119    318       O  
ATOM   3847  N   LEU A 505     138.977  94.199  15.995  1.00 28.98           N  
ANISOU 3847  N   LEU A 505     3409   3744   3859   -156    -71    266       N  
ATOM   3848  CA  LEU A 505     139.226  95.368  15.164  1.00 28.38           C  
ANISOU 3848  CA  LEU A 505     3336   3664   3782   -159    -63    257       C  
ATOM   3849  C   LEU A 505     140.671  95.853  15.357  1.00 28.38           C  
ANISOU 3849  C   LEU A 505     3328   3676   3780   -167    -64    258       C  
ATOM   3850  O   LEU A 505     141.116  95.969  16.475  1.00 28.89           O  
ANISOU 3850  O   LEU A 505     3387   3752   3838   -177    -70    261       O  
ATOM   3851  CB  LEU A 505     138.278  96.493  15.517  1.00 29.51           C  
ANISOU 3851  CB  LEU A 505     3491   3803   3918   -166    -58    248       C  
ATOM   3852  CG  LEU A 505     138.434  97.777  14.667  1.00 29.75           C  
ANISOU 3852  CG  LEU A 505     3528   3826   3947   -169    -50    239       C  
ATOM   3853  CD1 LEU A 505     138.068  97.511  13.221  1.00 29.81           C  
ANISOU 3853  CD1 LEU A 505     3541   3823   3963   -156    -46    237       C  
ATOM   3854  CD2 LEU A 505     137.502  98.835  15.211  1.00 31.27           C  
ANISOU 3854  CD2 LEU A 505     3733   4016   4134   -177    -47    230       C  
ATOM   3855  N   TYR A 506     141.404  96.061  14.262  1.00 27.91           N  
ANISOU 3855  N   TYR A 506     3264   3614   3725   -164    -60    255       N  
ATOM   3856  CA  TYR A 506     142.699  96.711  14.301  1.00 27.36           C  
ANISOU 3856  CA  TYR A 506     3187   3555   3653   -173    -59    253       C  
ATOM   3857  C   TYR A 506     142.469  98.230  14.059  1.00 27.99           C  
ANISOU 3857  C   TYR A 506     3278   3629   3725   -184    -50    244       C  
ATOM   3858  O   TYR A 506     142.808  99.070  14.919  1.00 30.11           O  
ANISOU 3858  O   TYR A 506     3548   3907   3986   -198    -50    240       O  
ATOM   3859  CB  TYR A 506     143.667  96.046  13.340  1.00 26.97           C  
ANISOU 3859  CB  TYR A 506     3127   3509   3612   -165    -59    255       C  
ATOM   3860  CG  TYR A 506     145.062  96.623  13.366  1.00 28.82           C  
ANISOU 3860  CG  TYR A 506     3351   3756   3844   -175    -58    252       C  
ATOM   3861  CD1 TYR A 506     145.819  96.652  14.556  1.00 29.88           C  
ANISOU 3861  CD1 TYR A 506     3475   3906   3973   -184    -65    255       C  
ATOM   3862  CD2 TYR A 506     145.641  97.177  12.194  1.00 30.06           C  
ANISOU 3862  CD2 TYR A 506     3508   3910   4002   -177    -49    245       C  
ATOM   3863  CE1 TYR A 506     147.091  97.198  14.586  1.00 31.08           C  
ANISOU 3863  CE1 TYR A 506     3617   4071   4122   -194    -64    251       C  
ATOM   3864  CE2 TYR A 506     146.914  97.761  12.228  1.00 30.39           C  
ANISOU 3864  CE2 TYR A 506     3540   3966   4041   -189    -47    241       C  
ATOM   3865  CZ  TYR A 506     147.636  97.769  13.416  1.00 31.76           C  
ANISOU 3865  CZ  TYR A 506     3703   4155   4210   -197    -54    244       C  
ATOM   3866  OH  TYR A 506     148.907  98.321  13.455  1.00 32.81           O  
ANISOU 3866  OH  TYR A 506     3824   4301   4339   -209    -52    238       O  
ATOM   3867  N   PHE A 507     141.910  98.599  12.909  1.00 27.54           N  
ANISOU 3867  N   PHE A 507     3233   3560   3672   -179    -43    239       N  
ATOM   3868  CA  PHE A 507     141.362  99.966  12.732  1.00 26.39           C  
ANISOU 3868  CA  PHE A 507     3102   3405   3520   -186    -36    231       C  
ATOM   3869  C   PHE A 507     140.269 100.031  11.673  1.00 25.93           C  
ANISOU 3869  C   PHE A 507     3055   3330   3465   -175    -32    228       C  
ATOM   3870  O   PHE A 507     140.117  99.130  10.862  1.00 25.70           O  
ANISOU 3870  O   PHE A 507     3023   3298   3443   -163    -32    231       O  
ATOM   3871  CB  PHE A 507     142.497 101.012  12.430  1.00 26.44           C  
ANISOU 3871  CB  PHE A 507     3108   3416   3522   -200    -30    227       C  
ATOM   3872  CG  PHE A 507     143.151 100.811  11.121  1.00 27.23           C  
ANISOU 3872  CG  PHE A 507     3205   3514   3627   -195    -26    227       C  
ATOM   3873  CD1 PHE A 507     144.222  99.969  10.979  1.00 28.12           C  
ANISOU 3873  CD1 PHE A 507     3302   3639   3745   -193    -29    231       C  
ATOM   3874  CD2 PHE A 507     142.654 101.446   9.980  1.00 29.49           C  
ANISOU 3874  CD2 PHE A 507     3506   3786   3913   -193    -19    223       C  
ATOM   3875  CE1 PHE A 507     144.801  99.755   9.727  1.00 27.43           C  
ANISOU 3875  CE1 PHE A 507     3210   3550   3661   -189    -23    229       C  
ATOM   3876  CE2 PHE A 507     143.226 101.258   8.750  1.00 27.60           C  
ANISOU 3876  CE2 PHE A 507     3264   3545   3676   -189    -14    223       C  
ATOM   3877  CZ  PHE A 507     144.289 100.385   8.616  1.00 27.51           C  
ANISOU 3877  CZ  PHE A 507     3235   3547   3669   -188    -16    226       C  
ATOM   3878  N   PHE A 508     139.522 101.137  11.706  1.00 26.74           N  
ANISOU 3878  N   PHE A 508     3173   3424   3564   -179    -28    221       N  
ATOM   3879  CA  PHE A 508     138.477 101.482  10.744  1.00 25.69           C  
ANISOU 3879  CA  PHE A 508     3053   3275   3432   -170    -24    217       C  
ATOM   3880  C   PHE A 508     138.651 102.954  10.439  1.00 26.25           C  
ANISOU 3880  C   PHE A 508     3137   3339   3498   -179    -19    211       C  
ATOM   3881  O   PHE A 508     138.636 103.775  11.349  1.00 25.05           O  
ANISOU 3881  O   PHE A 508     2988   3188   3341   -190    -18    207       O  
ATOM   3882  CB  PHE A 508     137.112 101.256  11.365  1.00 25.65           C  
ANISOU 3882  CB  PHE A 508     3052   3266   3428   -163    -28    214       C  
ATOM   3883  CG  PHE A 508     135.948 101.664  10.514  1.00 26.41           C  
ANISOU 3883  CG  PHE A 508     3161   3347   3525   -153    -25    209       C  
ATOM   3884  CD1 PHE A 508     135.483 102.981  10.521  1.00 27.25           C  
ANISOU 3884  CD1 PHE A 508     3281   3445   3628   -157    -22    202       C  
ATOM   3885  CD2 PHE A 508     135.227 100.704   9.785  1.00 27.04           C  
ANISOU 3885  CD2 PHE A 508     3239   3423   3611   -139    -27    211       C  
ATOM   3886  CE1 PHE A 508     134.372 103.355   9.759  1.00 27.71           C  
ANISOU 3886  CE1 PHE A 508     3351   3489   3688   -146    -22    197       C  
ATOM   3887  CE2 PHE A 508     134.121 101.067   9.028  1.00 28.03           C  
ANISOU 3887  CE2 PHE A 508     3376   3537   3738   -129    -25    205       C  
ATOM   3888  CZ  PHE A 508     133.694 102.402   8.997  1.00 27.43           C  
ANISOU 3888  CZ  PHE A 508     3313   3452   3658   -132    -23    199       C  
ATOM   3889  N   ASP A 509     138.757 103.304   9.171  1.00 26.58           N  
ANISOU 3889  N   ASP A 509     3187   3371   3541   -176    -14    211       N  
ATOM   3890  CA  ASP A 509     138.789 104.737   8.814  1.00 28.59           C  
ANISOU 3890  CA  ASP A 509     3457   3615   3790   -184     -9    206       C  
ATOM   3891  C   ASP A 509     138.089 104.895   7.466  1.00 27.76           C  
ANISOU 3891  C   ASP A 509     3365   3496   3687   -173     -7    207       C  
ATOM   3892  O   ASP A 509     138.650 104.540   6.428  1.00 27.16           O  
ANISOU 3892  O   ASP A 509     3287   3421   3612   -171     -4    210       O  
ATOM   3893  CB  ASP A 509     140.263 105.206   8.803  1.00 30.22           C  
ANISOU 3893  CB  ASP A 509     3659   3830   3993   -200     -4    207       C  
ATOM   3894  CG  ASP A 509     140.417 106.667   8.547  1.00 32.00           C  
ANISOU 3894  CG  ASP A 509     3900   4045   4213   -212      1    203       C  
ATOM   3895  OD1 ASP A 509     139.436 107.367   8.241  1.00 32.16           O  
ANISOU 3895  OD1 ASP A 509     3937   4049   4233   -206      2    199       O  
ATOM   3896  OD2 ASP A 509     141.572 107.134   8.600  1.00 38.62           O  
ANISOU 3896  OD2 ASP A 509     4736   4891   5048   -227      6    202       O  
ATOM   3897  N   ALA A 510     136.852 105.420   7.508  1.00 27.15           N  
ANISOU 3897  N   ALA A 510     3300   3406   3610   -165     -9    202       N  
ATOM   3898  CA  ALA A 510     136.067 105.698   6.336  1.00 26.57           C  
ANISOU 3898  CA  ALA A 510     3240   3319   3537   -154     -8    201       C  
ATOM   3899  C   ALA A 510     135.795 107.185   6.139  1.00 28.84           C  
ANISOU 3899  C   ALA A 510     3547   3591   3820   -158     -6    197       C  
ATOM   3900  O   ALA A 510     134.873 107.514   5.404  1.00 28.76           O  
ANISOU 3900  O   ALA A 510     3549   3568   3810   -147     -8    196       O  
ATOM   3901  CB  ALA A 510     134.712 104.978   6.414  1.00 26.20           C  
ANISOU 3901  CB  ALA A 510     3191   3270   3495   -138    -13    199       C  
ATOM   3902  N   SER A 511     136.567 108.081   6.742  1.00 28.43           N  
ANISOU 3902  N   SER A 511     3498   3540   3764   -174     -3    195       N  
ATOM   3903  CA  SER A 511     136.258 109.533   6.642  1.00 28.95           C  
ANISOU 3903  CA  SER A 511     3584   3589   3827   -179     -1    190       C  
ATOM   3904  C   SER A 511     136.487 110.093   5.217  1.00 28.66           C  
ANISOU 3904  C   SER A 511     3563   3539   3786   -178      3    195       C  
ATOM   3905  O   SER A 511     135.816 111.045   4.801  1.00 30.41           O  
ANISOU 3905  O   SER A 511     3804   3743   4007   -174      1    193       O  
ATOM   3906  CB  SER A 511     137.135 110.352   7.652  1.00 28.63           C  
ANISOU 3906  CB  SER A 511     3542   3552   3782   -199      3    186       C  
ATOM   3907  OG  SER A 511     138.536 110.090   7.386  1.00 28.78           O  
ANISOU 3907  OG  SER A 511     3553   3584   3799   -212      8    192       O  
ATOM   3908  N   ASN A 512     137.454 109.535   4.491  1.00 27.26           N  
ANISOU 3908  N   ASN A 512     3380   3372   3608   -183      7    201       N  
ATOM   3909  CA  ASN A 512     137.703 109.906   3.108  1.00 27.02           C  
ANISOU 3909  CA  ASN A 512     3362   3331   3572   -184     10    206       C  
ATOM   3910  C   ASN A 512     136.831 109.004   2.203  1.00 25.96           C  
ANISOU 3910  C   ASN A 512     3227   3196   3442   -165      6    209       C  
ATOM   3911  O   ASN A 512     137.123 107.812   2.080  1.00 25.84           O  
ANISOU 3911  O   ASN A 512     3195   3195   3430   -160      6    211       O  
ATOM   3912  CB  ASN A 512     139.200 109.765   2.743  1.00 27.48           C  
ANISOU 3912  CB  ASN A 512     3413   3401   3626   -200     18    210       C  
ATOM   3913  CG  ASN A 512     139.465 110.116   1.303  1.00 28.99           C  
ANISOU 3913  CG  ASN A 512     3618   3585   3812   -202     22    215       C  
ATOM   3914  OD1 ASN A 512     138.530 110.458   0.583  1.00 28.97           O  
ANISOU 3914  OD1 ASN A 512     3631   3567   3808   -191     19    216       O  
ATOM   3915  ND2 ASN A 512     140.730 110.041   0.861  1.00 30.51           N  
ANISOU 3915  ND2 ASN A 512     3805   3788   4000   -217     30    216       N  
ATOM   3916  N   PRO A 513     135.789 109.571   1.551  1.00 26.42           N  
ANISOU 3916  N   PRO A 513     3302   3238   3498   -153      2    209       N  
ATOM   3917  CA  PRO A 513     134.891 108.718   0.726  1.00 26.67           C  
ANISOU 3917  CA  PRO A 513     3331   3269   3532   -134     -3    210       C  
ATOM   3918  C   PRO A 513     135.597 108.068  -0.471  1.00 26.95           C  
ANISOU 3918  C   PRO A 513     3363   3311   3565   -136      1    216       C  
ATOM   3919  O   PRO A 513     135.144 107.034  -0.928  1.00 25.15           O  
ANISOU 3919  O   PRO A 513     3126   3090   3341   -124     -1    216       O  
ATOM   3920  CB  PRO A 513     133.778 109.666   0.267  1.00 26.62           C  
ANISOU 3920  CB  PRO A 513     3346   3244   3525   -124     -8    208       C  
ATOM   3921  CG  PRO A 513     134.307 111.043   0.456  1.00 27.29           C  
ANISOU 3921  CG  PRO A 513     3447   3316   3605   -138     -5    209       C  
ATOM   3922  CD  PRO A 513     135.433 111.013   1.449  1.00 26.22           C  
ANISOU 3922  CD  PRO A 513     3299   3193   3470   -156      1    207       C  
ATOM   3923  N   GLU A 514     136.767 108.579  -0.872  1.00 26.29           N  
ANISOU 3923  N   GLU A 514     3285   3230   3476   -152      9    219       N  
ATOM   3924  CA  GLU A 514     137.538 107.963  -1.947  1.00 28.07           C  
ANISOU 3924  CA  GLU A 514     3505   3464   3697   -156     14    224       C  
ATOM   3925  C   GLU A 514     138.415 106.791  -1.520  1.00 28.95           C  
ANISOU 3925  C   GLU A 514     3592   3595   3814   -160     17    222       C  
ATOM   3926  O   GLU A 514     138.814 105.997  -2.377  1.00 29.68           O  
ANISOU 3926  O   GLU A 514     3676   3696   3906   -157     20    224       O  
ATOM   3927  CB  GLU A 514     138.415 109.023  -2.652  1.00 28.71           C  
ANISOU 3927  CB  GLU A 514     3602   3539   3768   -173     21    227       C  
ATOM   3928  CG  GLU A 514     137.591 110.171  -3.203  1.00 30.45           C  
ANISOU 3928  CG  GLU A 514     3849   3738   3983   -169     18    230       C  
ATOM   3929  CD  GLU A 514     136.873 109.823  -4.492  1.00 32.91           C  
ANISOU 3929  CD  GLU A 514     4169   4044   4290   -155     14    234       C  
ATOM   3930  OE1 GLU A 514     137.473 109.944  -5.607  1.00 36.53           O  
ANISOU 3930  OE1 GLU A 514     4636   4504   4741   -163     20    239       O  
ATOM   3931  OE2 GLU A 514     135.710 109.423  -4.378  1.00 33.92           O  
ANISOU 3931  OE2 GLU A 514     4295   4169   4424   -137      6    231       O  
ATOM   3932  N   VAL A 515     138.773 106.729  -0.230  1.00 27.84           N  
ANISOU 3932  N   VAL A 515     3439   3461   3677   -166     16    220       N  
ATOM   3933  CA  VAL A 515     139.732 105.755   0.257  1.00 27.24           C  
ANISOU 3933  CA  VAL A 515     3340   3403   3606   -171     18    219       C  
ATOM   3934  C   VAL A 515     139.277 105.387   1.647  1.00 27.00           C  
ANISOU 3934  C   VAL A 515     3300   3377   3582   -166     12    217       C  
ATOM   3935  O   VAL A 515     139.565 106.072   2.611  1.00 27.28           O  
ANISOU 3935  O   VAL A 515     3337   3414   3616   -177     12    215       O  
ATOM   3936  CB  VAL A 515     141.209 106.297   0.310  1.00 28.02           C  
ANISOU 3936  CB  VAL A 515     3437   3511   3700   -191     26    219       C  
ATOM   3937  CG1 VAL A 515     142.167 105.204   0.668  1.00 27.30           C  
ANISOU 3937  CG1 VAL A 515     3321   3439   3614   -193     26    218       C  
ATOM   3938  CG2 VAL A 515     141.636 106.953  -0.990  1.00 28.19           C  
ANISOU 3938  CG2 VAL A 515     3472   3526   3713   -200     33    221       C  
ATOM   3939  N   GLN A 516     138.556 104.284   1.748  1.00 25.79           N  
ANISOU 3939  N   GLN A 516     3136   3227   3434   -151      7    217       N  
ATOM   3940  CA  GLN A 516     138.018 103.834   3.017  1.00 24.72           C  
ANISOU 3940  CA  GLN A 516     2992   3096   3304   -147      1    215       C  
ATOM   3941  C   GLN A 516     138.672 102.496   3.324  1.00 24.69           C  
ANISOU 3941  C   GLN A 516     2967   3107   3306   -145     -1    218       C  
ATOM   3942  O   GLN A 516     138.705 101.641   2.463  1.00 25.24           O  
ANISOU 3942  O   GLN A 516     3031   3178   3379   -136      0    219       O  
ATOM   3943  CB  GLN A 516     136.515 103.695   2.866  1.00 25.56           C  
ANISOU 3943  CB  GLN A 516     3107   3193   3414   -132     -4    213       C  
ATOM   3944  CG  GLN A 516     135.779 104.939   2.506  1.00 24.83           C  
ANISOU 3944  CG  GLN A 516     3035   3085   3317   -130     -4    210       C  
ATOM   3945  CD  GLN A 516     134.274 104.733   2.340  1.00 25.93           C  
ANISOU 3945  CD  GLN A 516     3179   3216   3459   -114    -10    207       C  
ATOM   3946  OE1 GLN A 516     133.499 105.077   3.200  1.00 27.70           O  
ANISOU 3946  OE1 GLN A 516     3405   3436   3684   -111    -14    202       O  
ATOM   3947  NE2 GLN A 516     133.857 104.219   1.210  1.00 28.02           N  
ANISOU 3947  NE2 GLN A 516     3446   3478   3724   -103    -11    208       N  
ATOM   3948  N   VAL A 517     139.155 102.303   4.559  1.00 25.76           N  
ANISOU 3948  N   VAL A 517     3091   3252   3443   -152     -3    218       N  
ATOM   3949  CA  VAL A 517     140.005 101.153   4.935  1.00 26.00           C  
ANISOU 3949  CA  VAL A 517     3103   3298   3480   -151     -5    221       C  
ATOM   3950  C   VAL A 517     139.568 100.610   6.308  1.00 26.05           C  
ANISOU 3950  C   VAL A 517     3101   3309   3489   -149    -12    222       C  
ATOM   3951  O   VAL A 517     139.248 101.355   7.228  1.00 27.88           O  
ANISOU 3951  O   VAL A 517     3338   3539   3716   -156    -13    220       O  
ATOM   3952  CB  VAL A 517     141.510 101.543   5.022  1.00 26.74           C  
ANISOU 3952  CB  VAL A 517     3188   3402   3570   -166     -1    221       C  
ATOM   3953  CG1 VAL A 517     142.385 100.312   5.124  1.00 27.97           C  
ANISOU 3953  CG1 VAL A 517     3324   3572   3733   -163     -4    223       C  
ATOM   3954  CG2 VAL A 517     141.956 102.344   3.822  1.00 27.19           C  
ANISOU 3954  CG2 VAL A 517     3256   3453   3621   -173      7    219       C  
ATOM   3955  N   VAL A 518     139.535  99.298   6.427  1.00 25.22           N  
ANISOU 3955  N   VAL A 518     2983   3209   3390   -140    -16    226       N  
ATOM   3956  CA  VAL A 518     139.234  98.640   7.663  1.00 24.77           C  
ANISOU 3956  CA  VAL A 518     2918   3157   3335   -139    -23    228       C  
ATOM   3957  C   VAL A 518     140.124  97.440   7.780  1.00 23.96           C  
ANISOU 3957  C   VAL A 518     2799   3065   3238   -135    -27    234       C  
ATOM   3958  O   VAL A 518     140.454  96.793   6.769  1.00 23.54           O  
ANISOU 3958  O   VAL A 518     2741   3012   3192   -127    -24    234       O  
ATOM   3959  CB  VAL A 518     137.748  98.214   7.724  1.00 25.33           C  
ANISOU 3959  CB  VAL A 518     2996   3220   3408   -128    -26    227       C  
ATOM   3960  CG1 VAL A 518     137.360  97.377   6.540  1.00 26.66           C  
ANISOU 3960  CG1 VAL A 518     3163   3383   3582   -115    -24    227       C  
ATOM   3961  CG2 VAL A 518     137.460  97.493   9.045  1.00 25.38           C  
ANISOU 3961  CG2 VAL A 518     2995   3233   3416   -129    -32    230       C  
ATOM   3962  N   SER A 519     140.534  97.134   8.998  1.00 25.13           N  
ANISOU 3962  N   SER A 519     2938   3223   3386   -140    -32    237       N  
ATOM   3963  CA  SER A 519     141.568  96.070   9.225  1.00 24.83           C  
ANISOU 3963  CA  SER A 519     2883   3196   3354   -137    -37    243       C  
ATOM   3964  C   SER A 519     141.203  95.364  10.505  1.00 24.17           C  
ANISOU 3964  C   SER A 519     2795   3116   3271   -136    -46    249       C  
ATOM   3965  O   SER A 519     140.798  96.026  11.478  1.00 25.48           O  
ANISOU 3965  O   SER A 519     2967   3285   3430   -145    -47    248       O  
ATOM   3966  CB  SER A 519     142.983  96.686   9.281  1.00 25.93           C  
ANISOU 3966  CB  SER A 519     3015   3347   3491   -149    -35    241       C  
ATOM   3967  OG  SER A 519     144.005  95.694   9.382  1.00 26.67           O  
ANISOU 3967  OG  SER A 519     3092   3452   3591   -144    -40    245       O  
ATOM   3968  N   ALA A 520     141.275  94.027  10.480  1.00 23.59           N  
ANISOU 3968  N   ALA A 520     2714   3044   3206   -125    -51    254       N  
ATOM   3969  CA  ALA A 520     141.048  93.195  11.638  1.00 23.84           C  
ANISOU 3969  CA  ALA A 520     2740   3079   3237   -124    -60    262       C  
ATOM   3970  C   ALA A 520     141.949  91.945  11.713  1.00 24.90           C  
ANISOU 3970  C   ALA A 520     2860   3218   3380   -116    -67    269       C  
ATOM   3971  O   ALA A 520     142.522  91.506  10.728  1.00 24.61           O  
ANISOU 3971  O   ALA A 520     2818   3181   3352   -108    -65    267       O  
ATOM   3972  CB  ALA A 520     139.577  92.784  11.743  1.00 23.97           C  
ANISOU 3972  CB  ALA A 520     2767   3085   3254   -119    -60    262       C  
ATOM   3973  N   LYS A 521     142.045  91.387  12.926  1.00 26.06           N  
ANISOU 3973  N   LYS A 521     3003   3372   3526   -118    -76    277       N  
ATOM   3974  CA  LYS A 521     142.885  90.219  13.189  1.00 27.93           C  
ANISOU 3974  CA  LYS A 521     3227   3613   3770   -110    -85    286       C  
ATOM   3975  C   LYS A 521     142.125  89.064  13.835  1.00 28.14           C  
ANISOU 3975  C   LYS A 521     3258   3634   3800   -103    -93    295       C  
ATOM   3976  O   LYS A 521     141.152  89.281  14.586  1.00 26.99           O  
ANISOU 3976  O   LYS A 521     3122   3486   3646   -110    -93    296       O  
ATOM   3977  CB  LYS A 521     144.017  90.636  14.117  1.00 27.64           C  
ANISOU 3977  CB  LYS A 521     3181   3592   3728   -119    -92    288       C  
ATOM   3978  CG  LYS A 521     144.942  91.683  13.487  1.00 27.85           C  
ANISOU 3978  CG  LYS A 521     3203   3627   3753   -126    -85    279       C  
ATOM   3979  CD  LYS A 521     146.141  91.984  14.369  1.00 28.22           C  
ANISOU 3979  CD  LYS A 521     3237   3691   3794   -135    -92    281       C  
ATOM   3980  CE  LYS A 521     146.944  93.128  13.731  1.00 28.92           C  
ANISOU 3980  CE  LYS A 521     3323   3787   3880   -145    -83    271       C  
ATOM   3981  NZ  LYS A 521     148.066  93.504  14.628  1.00 31.02           N  
ANISOU 3981  NZ  LYS A 521     3576   4071   4140   -155    -89    271       N  
ATOM   3982  N   GLU A 522     142.646  87.864  13.627  1.00 27.80           N  
ANISOU 3982  N   GLU A 522     3206   3588   3768    -91    -99    301       N  
ATOM   3983  CA  GLU A 522     142.062  86.665  14.187  1.00 28.88           C  
ANISOU 3983  CA  GLU A 522     3347   3718   3909    -85   -106    310       C  
ATOM   3984  C   GLU A 522     143.188  85.702  14.521  1.00 31.11           C  
ANISOU 3984  C   GLU A 522     3617   4005   4200    -76   -118    319       C  
ATOM   3985  O   GLU A 522     143.874  85.215  13.631  1.00 30.83           O  
ANISOU 3985  O   GLU A 522     3571   3967   4175    -65   -117    316       O  
ATOM   3986  CB  GLU A 522     141.098  86.030  13.194  1.00 29.58           C  
ANISOU 3986  CB  GLU A 522     3442   3791   4006    -76   -100    306       C  
ATOM   3987  CG  GLU A 522     140.521  84.672  13.614  1.00 30.31           C  
ANISOU 3987  CG  GLU A 522     3538   3874   4104    -69   -106    316       C  
ATOM   3988  CD  GLU A 522     139.832  84.719  14.943  1.00 31.85           C  
ANISOU 3988  CD  GLU A 522     3742   4071   4288    -80   -111    323       C  
ATOM   3989  OE1 GLU A 522     138.909  85.584  15.077  1.00 31.17           O  
ANISOU 3989  OE1 GLU A 522     3665   3986   4193    -89   -104    317       O  
ATOM   3990  OE2 GLU A 522     140.220  83.931  15.866  1.00 30.14           O  
ANISOU 3990  OE2 GLU A 522     3523   3857   4072    -79   -122    336       O  
ATOM   3991  N   GLN A 523     143.338  85.380  15.799  1.00 33.05           N  
ANISOU 3991  N   GLN A 523     3862   4256   4439    -81   -129    330       N  
ATOM   3992  CA  GLN A 523     144.413  84.501  16.180  1.00 35.29           C  
ANISOU 3992  CA  GLN A 523     4134   4545   4731    -72   -142    340       C  
ATOM   3993  C   GLN A 523     143.969  83.202  16.870  1.00 32.37           C  
ANISOU 3993  C   GLN A 523     3770   4165   4364    -66   -152    354       C  
ATOM   3994  O   GLN A 523     144.803  82.408  17.208  1.00 30.17           O  
ANISOU 3994  O   GLN A 523     3482   3888   4092    -57   -164    362       O  
ATOM   3995  CB  GLN A 523     145.497  85.280  16.945  1.00 38.82           C  
ANISOU 3995  CB  GLN A 523     4571   5011   5169    -81   -148    340       C  
ATOM   3996  CG  GLN A 523     145.105  85.786  18.315  1.00 43.23           C  
ANISOU 3996  CG  GLN A 523     5136   5578   5711    -96   -152    347       C  
ATOM   3997  CD  GLN A 523     146.311  86.371  19.076  1.00 47.77           C  
ANISOU 3997  CD  GLN A 523     5699   6172   6278   -103   -160    348       C  
ATOM   3998  OE1 GLN A 523     147.045  87.209  18.548  1.00 51.33           O  
ANISOU 3998  OE1 GLN A 523     6141   6632   6729   -107   -154    337       O  
ATOM   3999  NE2 GLN A 523     146.552  85.878  20.275  1.00 48.71           N  
ANISOU 3999  NE2 GLN A 523     5818   6299   6392   -106   -174    360       N  
ATOM   4000  N   ASN A 524     142.664  82.968  17.006  1.00 29.33           N  
ANISOU 4000  N   ASN A 524     3399   3769   3975    -70   -147    355       N  
ATOM   4001  CA  ASN A 524     142.166  81.774  17.699  1.00 29.84           C  
ANISOU 4001  CA  ASN A 524     3473   3825   4042    -67   -156    368       C  
ATOM   4002  C   ASN A 524     141.490  80.762  16.804  1.00 29.92           C  
ANISOU 4002  C   ASN A 524     3488   3816   4066    -55   -152    367       C  
ATOM   4003  O   ASN A 524     141.422  79.580  17.180  1.00 31.67           O  
ANISOU 4003  O   ASN A 524     3713   4028   4293    -49   -160    378       O  
ATOM   4004  CB  ASN A 524     141.254  82.164  18.855  1.00 30.80           C  
ANISOU 4004  CB  ASN A 524     3605   3950   4146    -83   -156    373       C  
ATOM   4005  CG  ASN A 524     141.975  82.977  19.917  1.00 30.56           C  
ANISOU 4005  CG  ASN A 524     3570   3938   4103    -95   -163    377       C  
ATOM   4006  OD1 ASN A 524     141.700  84.166  20.100  1.00 33.44           O  
ANISOU 4006  OD1 ASN A 524     3937   4313   4457   -107   -156    368       O  
ATOM   4007  ND2 ASN A 524     142.903  82.357  20.594  1.00 28.67           N  
ANISOU 4007  ND2 ASN A 524     3324   3704   3864    -90   -177    389       N  
ATOM   4008  N   ALA A 525     141.036  81.209  15.622  1.00 28.51           N  
ANISOU 4008  N   ALA A 525     3309   3632   3891    -53   -139    353       N  
ATOM   4009  CA  ALA A 525     140.478  80.355  14.582  1.00 28.01           C  
ANISOU 4009  CA  ALA A 525     3249   3554   3841    -42   -133    348       C  
ATOM   4010  C   ALA A 525     141.371  79.155  14.309  1.00 27.94           C  
ANISOU 4010  C   ALA A 525     3231   3537   3847    -26   -142    354       C  
ATOM   4011  O   ALA A 525     140.886  78.039  14.224  1.00 26.29           O  
ANISOU 4011  O   ALA A 525     3028   3314   3647    -19   -144    359       O  
ATOM   4012  CB  ALA A 525     140.219  81.150  13.310  1.00 27.09           C  
ANISOU 4012  CB  ALA A 525     3130   3436   3725    -41   -119    332       C  
ATOM   4013  N   TYR A 526     142.675  79.406  14.224  1.00 28.95           N  
ANISOU 4013  N   TYR A 526     3345   3676   3979    -20   -147    354       N  
ATOM   4014  CA  TYR A 526     143.679  78.349  14.057  1.00 30.45           C  
ANISOU 4014  CA  TYR A 526     3524   3861   4185     -4   -157    358       C  
ATOM   4015  C   TYR A 526     144.780  78.638  15.062  1.00 30.00           C  
ANISOU 4015  C   TYR A 526     3458   3820   4122     -6   -170    367       C  
ATOM   4016  O   TYR A 526     145.612  79.508  14.796  1.00 28.05           O  
ANISOU 4016  O   TYR A 526     3198   3586   3872     -9   -167    359       O  
ATOM   4017  CB  TYR A 526     144.238  78.375  12.623  1.00 29.71           C  
ANISOU 4017  CB  TYR A 526     3419   3767   4104      6   -148    344       C  
ATOM   4018  CG  TYR A 526     143.201  78.072  11.558  1.00 29.24           C  
ANISOU 4018  CG  TYR A 526     3368   3694   4050      9   -136    335       C  
ATOM   4019  CD1 TYR A 526     142.561  76.818  11.503  1.00 28.32           C  
ANISOU 4019  CD1 TYR A 526     3258   3559   3943     17   -139    340       C  
ATOM   4020  CD2 TYR A 526     142.868  79.030  10.594  1.00 28.94           C  
ANISOU 4020  CD2 TYR A 526     3330   3660   4007      4   -122    321       C  
ATOM   4021  CE1 TYR A 526     141.597  76.576  10.565  1.00 27.95           C  
ANISOU 4021  CE1 TYR A 526     3219   3501   3900     18   -128    331       C  
ATOM   4022  CE2 TYR A 526     141.958  78.768   9.599  1.00 28.83           C  
ANISOU 4022  CE2 TYR A 526     3322   3634   3997      7   -112    312       C  
ATOM   4023  CZ  TYR A 526     141.311  77.553   9.592  1.00 27.86           C  
ANISOU 4023  CZ  TYR A 526     3206   3496   3884     14   -115    317       C  
ATOM   4024  OH  TYR A 526     140.434  77.337   8.567  1.00 25.90           O  
ANISOU 4024  OH  TYR A 526     2963   3238   3640     16   -104    307       O  
ATOM   4025  N   PRO A 527     144.759  77.965  16.242  1.00 31.03           N  
ANISOU 4025  N   PRO A 527     3593   3947   4248     -7   -183    383       N  
ATOM   4026  CA  PRO A 527     145.816  78.251  17.259  1.00 31.86           C  
ANISOU 4026  CA  PRO A 527     3689   4068   4346     -9   -197    392       C  
ATOM   4027  C   PRO A 527     147.215  78.062  16.656  1.00 32.34           C  
ANISOU 4027  C   PRO A 527     3730   4137   4422      5   -202    386       C  
ATOM   4028  O   PRO A 527     147.419  77.123  15.939  1.00 33.14           O  
ANISOU 4028  O   PRO A 527     3827   4225   4540     21   -203    384       O  
ATOM   4029  CB  PRO A 527     145.505  77.257  18.385  1.00 31.61           C  
ANISOU 4029  CB  PRO A 527     3669   4029   4313     -9   -211    411       C  
ATOM   4030  CG  PRO A 527     143.989  77.098  18.295  1.00 31.82           C  
ANISOU 4030  CG  PRO A 527     3714   4042   4335    -18   -200    411       C  
ATOM   4031  CD  PRO A 527     143.724  77.053  16.792  1.00 31.78           C  
ANISOU 4031  CD  PRO A 527     3705   4027   4343     -9   -187    395       C  
ATOM   4032  N   GLY A 528     148.096  79.041  16.824  1.00 33.44           N  
ANISOU 4032  N   GLY A 528     3857   4296   4554     -1   -202    380       N  
ATOM   4033  CA  GLY A 528     149.442  78.978  16.212  1.00 35.85           C  
ANISOU 4033  CA  GLY A 528     4141   4610   4871     11   -206    372       C  
ATOM   4034  C   GLY A 528     149.567  79.713  14.885  1.00 35.62           C  
ANISOU 4034  C   GLY A 528     4105   4584   4845      9   -189    353       C  
ATOM   4035  O   GLY A 528     150.641  79.786  14.328  1.00 36.00           O  
ANISOU 4035  O   GLY A 528     4135   4641   4901     17   -189    343       O  
ATOM   4036  N   THR A 529     148.451  80.257  14.388  1.00 34.63           N  
ANISOU 4036  N   THR A 529     3994   4452   4714      0   -174    347       N  
ATOM   4037  CA  THR A 529     148.404  81.000  13.144  1.00 32.77           C  
ANISOU 4037  CA  THR A 529     3755   4218   4479     -4   -158    330       C  
ATOM   4038  C   THR A 529     147.747  82.357  13.486  1.00 33.46           C  
ANISOU 4038  C   THR A 529     3853   4311   4547    -23   -149    328       C  
ATOM   4039  O   THR A 529     146.760  82.395  14.218  1.00 31.86           O  
ANISOU 4039  O   THR A 529     3666   4104   4337    -31   -151    335       O  
ATOM   4040  CB  THR A 529     147.589  80.208  12.047  1.00 32.68           C  
ANISOU 4040  CB  THR A 529     3751   4186   4479      7   -150    325       C  
ATOM   4041  OG1 THR A 529     148.317  79.033  11.573  1.00 31.81           O  
ANISOU 4041  OG1 THR A 529     3629   4071   4388     25   -156    325       O  
ATOM   4042  CG2 THR A 529     147.274  81.052  10.850  1.00 31.44           C  
ANISOU 4042  CG2 THR A 529     3595   4030   4319      1   -133    310       C  
ATOM   4043  N   GLU A 530     148.278  83.449  12.930  1.00 34.11           N  
ANISOU 4043  N   GLU A 530     3929   4406   4626    -32   -140    316       N  
ATOM   4044  CA  GLU A 530     147.653  84.787  13.019  1.00 37.75           C  
ANISOU 4044  CA  GLU A 530     4402   4872   5072    -49   -130    311       C  
ATOM   4045  C   GLU A 530     147.168  85.203  11.615  1.00 33.84           C  
ANISOU 4045  C   GLU A 530     3911   4368   4579    -49   -115    298       C  
ATOM   4046  O   GLU A 530     147.901  85.097  10.640  1.00 33.27           O  
ANISOU 4046  O   GLU A 530     3828   4298   4515    -42   -110    290       O  
ATOM   4047  CB  GLU A 530     148.606  85.860  13.586  1.00 43.28           C  
ANISOU 4047  CB  GLU A 530     5093   5591   5762    -62   -131    308       C  
ATOM   4048  CG  GLU A 530     147.868  87.189  13.883  1.00 52.89           C  
ANISOU 4048  CG  GLU A 530     6323   6810   6963    -80   -123    304       C  
ATOM   4049  CD  GLU A 530     148.749  88.453  13.850  1.00 59.84           C  
ANISOU 4049  CD  GLU A 530     7196   7706   7835    -93   -117    295       C  
ATOM   4050  OE1 GLU A 530     149.967  88.408  14.140  1.00 68.33           O  
ANISOU 4050  OE1 GLU A 530     8255   8795   8911    -93   -124    294       O  
ATOM   4051  OE2 GLU A 530     148.207  89.515  13.521  1.00 66.52           O  
ANISOU 4051  OE2 GLU A 530     8053   8550   8673   -104   -106    288       O  
ATOM   4052  N   MET A 531     145.923  85.633  11.520  1.00 29.73           N  
ANISOU 4052  N   MET A 531     3407   3839   4052    -55   -107    297       N  
ATOM   4053  CA  MET A 531     145.380  86.142  10.262  1.00 29.61           C  
ANISOU 4053  CA  MET A 531     3398   3816   4036    -56    -94    287       C  
ATOM   4054  C   MET A 531     145.155  87.644  10.451  1.00 27.75           C  
ANISOU 4054  C   MET A 531     3171   3587   3786    -72    -87    282       C  
ATOM   4055  O   MET A 531     144.493  88.048  11.420  1.00 27.48           O  
ANISOU 4055  O   MET A 531     3146   3553   3743    -80    -90    287       O  
ATOM   4056  CB  MET A 531     144.045  85.472   9.944  1.00 30.71           C  
ANISOU 4056  CB  MET A 531     3550   3940   4179    -49    -91    288       C  
ATOM   4057  CG  MET A 531     144.123  83.995   9.571  1.00 33.65           C  
ANISOU 4057  CG  MET A 531     3916   4302   4566    -33    -96    291       C  
ATOM   4058  SD  MET A 531     142.546  83.128   9.859  1.00 40.57           S  
ANISOU 4058  SD  MET A 531     4809   5161   5444    -30    -97    297       S  
ATOM   4059  CE  MET A 531     141.421  84.091   8.882  1.00 44.91           C  
ANISOU 4059  CE  MET A 531     5371   5707   5987    -36    -83    286       C  
ATOM   4060  N   HIS A 532     145.694  88.458   9.557  1.00 26.55           N  
ANISOU 4060  N   HIS A 532     3016   3440   3632    -76    -78    272       N  
ATOM   4061  CA  HIS A 532     145.518  89.909   9.601  1.00 26.16           C  
ANISOU 4061  CA  HIS A 532     2975   3393   3570    -91    -70    267       C  
ATOM   4062  C   HIS A 532     144.993  90.373   8.243  1.00 26.25           C  
ANISOU 4062  C   HIS A 532     2996   3397   3582    -91    -59    258       C  
ATOM   4063  O   HIS A 532     145.743  90.460   7.257  1.00 26.71           O  
ANISOU 4063  O   HIS A 532     3047   3459   3644    -89    -53    252       O  
ATOM   4064  CB  HIS A 532     146.845  90.617   9.978  1.00 26.65           C  
ANISOU 4064  CB  HIS A 532     3025   3473   3628   -102    -72    264       C  
ATOM   4065  CG  HIS A 532     146.719  92.103  10.080  1.00 25.97           C  
ANISOU 4065  CG  HIS A 532     2949   3390   3529   -118    -64    259       C  
ATOM   4066  ND1 HIS A 532     147.805  92.951  10.048  1.00 26.65           N  
ANISOU 4066  ND1 HIS A 532     3028   3488   3611   -130    -61    253       N  
ATOM   4067  CD2 HIS A 532     145.628  92.900  10.173  1.00 24.88           C  
ANISOU 4067  CD2 HIS A 532     2828   3242   3383   -125    -59    258       C  
ATOM   4068  CE1 HIS A 532     147.388  94.204  10.136  1.00 26.45           C  
ANISOU 4068  CE1 HIS A 532     3015   3461   3575   -143    -54    250       C  
ATOM   4069  NE2 HIS A 532     146.072  94.199  10.204  1.00 25.16           N  
ANISOU 4069  NE2 HIS A 532     2866   3283   3409   -139    -53    252       N  
ATOM   4070  N   ARG A 533     143.700  90.720   8.190  1.00 26.12           N  
ANISOU 4070  N   ARG A 533     2994   3369   3560    -92    -55    258       N  
ATOM   4071  CA  ARG A 533     143.088  91.088   6.933  1.00 26.43           C  
ANISOU 4071  CA  ARG A 533     3043   3399   3598    -89    -46    251       C  
ATOM   4072  C   ARG A 533     142.672  92.564   6.876  1.00 26.00           C  
ANISOU 4072  C   ARG A 533     3002   3343   3532   -101    -39    247       C  
ATOM   4073  O   ARG A 533     141.860  93.023   7.684  1.00 26.55           O  
ANISOU 4073  O   ARG A 533     3081   3410   3596   -106    -42    249       O  
ATOM   4074  CB  ARG A 533     141.888  90.187   6.602  1.00 26.46           C  
ANISOU 4074  CB  ARG A 533     3054   3392   3609    -78    -46    252       C  
ATOM   4075  CG  ARG A 533     141.493  90.256   5.132  1.00 27.23           C  
ANISOU 4075  CG  ARG A 533     3156   3482   3708    -72    -38    245       C  
ATOM   4076  CD  ARG A 533     140.253  89.398   4.814  1.00 27.04           C  
ANISOU 4076  CD  ARG A 533     3139   3446   3689    -62    -38    245       C  
ATOM   4077  NE  ARG A 533     140.297  88.898   3.452  1.00 26.92           N  
ANISOU 4077  NE  ARG A 533     3120   3427   3679    -54    -33    239       N  
ATOM   4078  CZ  ARG A 533     139.511  87.950   2.929  1.00 27.42           C  
ANISOU 4078  CZ  ARG A 533     3185   3482   3749    -44    -32    237       C  
ATOM   4079  NH1 ARG A 533     138.560  87.351   3.642  1.00 27.22           N  
ANISOU 4079  NH1 ARG A 533     3164   3450   3726    -40    -37    241       N  
ATOM   4080  NH2 ARG A 533     139.651  87.645   1.642  1.00 28.55           N  
ANISOU 4080  NH2 ARG A 533     3327   3625   3897    -38    -26    230       N  
ATOM   4081  N   THR A 534     143.163  93.251   5.860  1.00 25.86           N  
ANISOU 4081  N   THR A 534     2986   3327   3512   -106    -31    241       N  
ATOM   4082  CA  THR A 534     142.896  94.663   5.616  1.00 26.87           C  
ANISOU 4082  CA  THR A 534     3127   3451   3630   -117    -25    237       C  
ATOM   4083  C   THR A 534     142.186  94.756   4.258  1.00 27.55           C  
ANISOU 4083  C   THR A 534     3224   3527   3715   -110    -18    232       C  
ATOM   4084  O   THR A 534     142.651  94.207   3.253  1.00 28.65           O  
ANISOU 4084  O   THR A 534     3357   3669   3861   -105    -14    230       O  
ATOM   4085  CB  THR A 534     144.198  95.504   5.611  1.00 26.49           C  
ANISOU 4085  CB  THR A 534     3074   3415   3577   -130    -21    234       C  
ATOM   4086  OG1 THR A 534     144.898  95.272   6.845  1.00 25.91           O  
ANISOU 4086  OG1 THR A 534     2988   3352   3504   -135    -28    237       O  
ATOM   4087  CG2 THR A 534     143.876  97.003   5.464  1.00 27.21           C  
ANISOU 4087  CG2 THR A 534     3182   3500   3658   -143    -15    230       C  
ATOM   4088  N   MET A 535     141.043  95.435   4.267  1.00 26.97           N  
ANISOU 4088  N   MET A 535     3167   3444   3637   -111    -17    231       N  
ATOM   4089  CA  MET A 535     140.214  95.636   3.106  1.00 27.88           C  
ANISOU 4089  CA  MET A 535     3293   3549   3751   -105    -13    228       C  
ATOM   4090  C   MET A 535     140.017  97.115   2.864  1.00 26.12           C  
ANISOU 4090  C   MET A 535     3085   3320   3517   -114     -8    225       C  
ATOM   4091  O   MET A 535     139.868  97.839   3.790  1.00 25.76           O  
ANISOU 4091  O   MET A 535     3045   3275   3468   -121    -10    226       O  
ATOM   4092  CB  MET A 535     138.871  94.949   3.299  1.00 29.39           C  
ANISOU 4092  CB  MET A 535     3488   3732   3946    -93    -17    228       C  
ATOM   4093  CG  MET A 535     139.082  93.451   3.602  1.00 32.07           C  
ANISOU 4093  CG  MET A 535     3814   4076   4295    -85    -21    232       C  
ATOM   4094  SD  MET A 535     137.762  92.486   2.922  1.00 36.36           S  
ANISOU 4094  SD  MET A 535     4361   4609   4844    -70    -22    229       S  
ATOM   4095  CE  MET A 535     138.053  92.487   1.174  1.00 36.14           C  
ANISOU 4095  CE  MET A 535     4335   4581   4818    -66    -14    224       C  
ATOM   4096  N   ALA A 536     140.070  97.537   1.606  1.00 26.19           N  
ANISOU 4096  N   ALA A 536     3102   3325   3523   -114     -2    223       N  
ATOM   4097  CA  ALA A 536     139.888  98.932   1.269  1.00 26.81           C  
ANISOU 4097  CA  ALA A 536     3198   3396   3592   -123      2    221       C  
ATOM   4098  C   ALA A 536     138.992  99.055   0.049  1.00 27.18           C  
ANISOU 4098  C   ALA A 536     3258   3433   3636   -114      4    220       C  
ATOM   4099  O   ALA A 536     138.963  98.195  -0.808  1.00 27.64           O  
ANISOU 4099  O   ALA A 536     3311   3493   3699   -106      5    219       O  
ATOM   4100  CB  ALA A 536     141.227  99.608   1.049  1.00 27.19           C  
ANISOU 4100  CB  ALA A 536     3244   3451   3635   -138      8    221       C  
ATOM   4101  N   LEU A 537     138.228 100.131   0.022  1.00 27.41           N  
ANISOU 4101  N   LEU A 537     3304   3451   3659   -115      3    219       N  
ATOM   4102  CA  LEU A 537     137.415 100.506  -1.108  1.00 26.18           C  
ANISOU 4102  CA  LEU A 537     3163   3285   3499   -108      4    218       C  
ATOM   4103  C   LEU A 537     137.997 101.824  -1.597  1.00 26.39           C  
ANISOU 4103  C   LEU A 537     3204   3307   3516   -121      9    219       C  
ATOM   4104  O   LEU A 537     137.927 102.843  -0.892  1.00 23.77           O  
ANISOU 4104  O   LEU A 537     2881   2969   3180   -129      8    219       O  
ATOM   4105  CB  LEU A 537     135.976 100.670  -0.660  1.00 26.31           C  
ANISOU 4105  CB  LEU A 537     3187   3293   3517    -98     -2    216       C  
ATOM   4106  CG  LEU A 537     134.904 100.902  -1.724  1.00 25.99           C  
ANISOU 4106  CG  LEU A 537     3160   3243   3473    -87     -4    215       C  
ATOM   4107  CD1 LEU A 537     134.854  99.710  -2.662  1.00 27.00           C  
ANISOU 4107  CD1 LEU A 537     3279   3375   3604    -78     -3    214       C  
ATOM   4108  CD2 LEU A 537     133.536 101.062  -1.073  1.00 25.57           C  
ANISOU 4108  CD2 LEU A 537     3111   3182   3422    -77    -10    211       C  
ATOM   4109  N   ILE A 538     138.595 101.782  -2.793  1.00 27.40           N  
ANISOU 4109  N   ILE A 538     3334   3437   3640   -125     15    220       N  
ATOM   4110  CA  ILE A 538     139.481 102.864  -3.289  1.00 28.97           C  
ANISOU 4110  CA  ILE A 538     3544   3635   3829   -141     22    222       C  
ATOM   4111  C   ILE A 538     139.043 103.306  -4.680  1.00 27.60           C  
ANISOU 4111  C   ILE A 538     3388   3453   3648   -138     24    223       C  
ATOM   4112  O   ILE A 538     138.912 102.494  -5.605  1.00 28.24           O  
ANISOU 4112  O   ILE A 538     3463   3537   3728   -131     25    222       O  
ATOM   4113  CB  ILE A 538     140.947 102.388  -3.349  1.00 30.32           C  
ANISOU 4113  CB  ILE A 538     3698   3821   4002   -152     28    220       C  
ATOM   4114  CG1 ILE A 538     141.393 101.974  -1.959  1.00 30.26           C  
ANISOU 4114  CG1 ILE A 538     3674   3822   4001   -154     25    219       C  
ATOM   4115  CG2 ILE A 538     141.862 103.461  -3.965  1.00 31.02           C  
ANISOU 4115  CG2 ILE A 538     3798   3909   4079   -170     37    221       C  
ATOM   4116  CD1 ILE A 538     142.759 101.334  -1.928  1.00 31.80           C  
ANISOU 4116  CD1 ILE A 538     3849   4033   4199   -162     29    217       C  
ATOM   4117  N   LYS A 539     138.769 104.587  -4.782  1.00 27.02           N  
ANISOU 4117  N   LYS A 539     3334   3366   3566   -144     24    226       N  
ATOM   4118  CA  LYS A 539     138.592 105.281  -6.039  1.00 28.30           C  
ANISOU 4118  CA  LYS A 539     3516   3519   3718   -147     26    229       C  
ATOM   4119  C   LYS A 539     139.829 106.107  -6.332  1.00 27.67           C  
ANISOU 4119  C   LYS A 539     3443   3441   3629   -168     35    231       C  
ATOM   4120  O   LYS A 539     140.202 106.987  -5.557  1.00 27.60           O  
ANISOU 4120  O   LYS A 539     3440   3428   3619   -179     37    231       O  
ATOM   4121  CB  LYS A 539     137.389 106.202  -5.980  1.00 30.01           C  
ANISOU 4121  CB  LYS A 539     3754   3718   3932   -138     19    231       C  
ATOM   4122  CG  LYS A 539     137.073 106.935  -7.276  1.00 33.01           C  
ANISOU 4122  CG  LYS A 539     4156   4087   4300   -138     19    236       C  
ATOM   4123  CD  LYS A 539     136.952 105.989  -8.494  1.00 36.07           C  
ANISOU 4123  CD  LYS A 539     4538   4483   4685   -130     20    236       C  
ATOM   4124  CE  LYS A 539     136.781 106.776  -9.775  1.00 40.28           C  
ANISOU 4124  CE  LYS A 539     5094   5006   5204   -133     21    242       C  
ATOM   4125  NZ  LYS A 539     135.380 107.287  -9.798  1.00 46.48           N  
ANISOU 4125  NZ  LYS A 539     5895   5776   5990   -117     10    244       N  
ATOM   4126  N   THR A 540     140.476 105.829  -7.439  1.00 28.61           N  
ANISOU 4126  N   THR A 540     3561   3568   3741   -174     42    232       N  
ATOM   4127  CA  THR A 540     141.699 106.566  -7.817  1.00 28.50           C  
ANISOU 4127  CA  THR A 540     3552   3557   3718   -197     52    233       C  
ATOM   4128  C   THR A 540     141.733 106.713  -9.348  1.00 30.13           C  
ANISOU 4128  C   THR A 540     3772   3762   3912   -200     57    236       C  
ATOM   4129  O   THR A 540     141.018 106.003 -10.095  1.00 27.97           O  
ANISOU 4129  O   THR A 540     3498   3490   3640   -186     54    236       O  
ATOM   4130  CB  THR A 540     142.942 105.892  -7.206  1.00 28.95           C  
ANISOU 4130  CB  THR A 540     3585   3634   3782   -206     58    227       C  
ATOM   4131  OG1 THR A 540     144.102 106.758  -7.276  1.00 29.25           O  
ANISOU 4131  OG1 THR A 540     3627   3676   3811   -229     68    226       O  
ATOM   4132  CG2 THR A 540     143.198 104.553  -7.843  1.00 28.47           C  
ANISOU 4132  CG2 THR A 540     3504   3587   3725   -198     60    223       C  
ATOM   4133  N   ASP A 541     142.570 107.635  -9.785  1.00 29.88           N  
ANISOU 4133  N   ASP A 541     3754   3730   3870   -221     66    238       N  
ATOM   4134  CA  ASP A 541     142.746 107.977 -11.175  1.00 32.86           C  
ANISOU 4134  CA  ASP A 541     4147   4106   4234   -229     72    242       C  
ATOM   4135  C   ASP A 541     143.183 106.751 -11.979  1.00 32.23           C  
ANISOU 4135  C   ASP A 541     4047   4044   4155   -226     77    236       C  
ATOM   4136  O   ASP A 541     144.021 105.994 -11.516  1.00 32.55           O  
ANISOU 4136  O   ASP A 541     4064   4101   4204   -229     81    229       O  
ATOM   4137  CB  ASP A 541     143.799 109.123 -11.312  1.00 35.20           C  
ANISOU 4137  CB  ASP A 541     4457   4400   4519   -256     82    244       C  
ATOM   4138  CG  ASP A 541     143.759 109.821 -12.690  1.00 37.78           C  
ANISOU 4138  CG  ASP A 541     4808   4718   4828   -266     86    251       C  
ATOM   4139  OD1 ASP A 541     142.965 109.397 -13.544  1.00 37.98           O  
ANISOU 4139  OD1 ASP A 541     4840   4741   4850   -252     81    254       O  
ATOM   4140  OD2 ASP A 541     144.499 110.825 -12.913  1.00 40.45           O  
ANISOU 4140  OD2 ASP A 541     5162   5052   5154   -289     94    254       O  
ATOM   4141  N   GLY A 542     142.577 106.540 -13.150  1.00 30.01           N  
ANISOU 4141  N   GLY A 542     3777   3761   3866   -219     75    239       N  
ATOM   4142  CA  GLY A 542     142.925 105.398 -13.985  1.00 32.12           C  
ANISOU 4142  CA  GLY A 542     4026   4044   4133   -216     81    233       C  
ATOM   4143  C   GLY A 542     141.907 104.250 -13.971  1.00 32.52           C  
ANISOU 4143  C   GLY A 542     4065   4096   4195   -191     72    230       C  
ATOM   4144  O   GLY A 542     142.051 103.325 -14.745  1.00 34.06           O  
ANISOU 4144  O   GLY A 542     4248   4303   4390   -187     76    224       O  
ATOM   4145  N   PHE A 543     140.901 104.329 -13.097  1.00 32.24           N  
ANISOU 4145  N   PHE A 543     4033   4049   4168   -176     61    232       N  
ATOM   4146  CA  PHE A 543     139.837 103.304 -12.923  1.00 31.98           C  
ANISOU 4146  CA  PHE A 543     3989   4017   4146   -154     52    229       C  
ATOM   4147  C   PHE A 543     138.490 104.010 -13.018  1.00 31.72           C  
ANISOU 4147  C   PHE A 543     3977   3966   4109   -141     42    235       C  
ATOM   4148  O   PHE A 543     138.324 105.089 -12.548  1.00 30.20           O  
ANISOU 4148  O   PHE A 543     3801   3761   3913   -146     39    240       O  
ATOM   4149  CB  PHE A 543     139.951 102.587 -11.591  1.00 31.24           C  
ANISOU 4149  CB  PHE A 543     3874   3928   4069   -147     49    224       C  
ATOM   4150  CG  PHE A 543     141.271 101.852 -11.415  1.00 30.93           C  
ANISOU 4150  CG  PHE A 543     3812   3906   4036   -156     58    218       C  
ATOM   4151  CD1 PHE A 543     142.353 102.509 -10.895  1.00 29.94           C  
ANISOU 4151  CD1 PHE A 543     3685   3785   3908   -174     64    218       C  
ATOM   4152  CD2 PHE A 543     141.404 100.510 -11.799  1.00 30.41           C  
ANISOU 4152  CD2 PHE A 543     3726   3851   3977   -147     60    212       C  
ATOM   4153  CE1 PHE A 543     143.575 101.867 -10.756  1.00 31.79           C  
ANISOU 4153  CE1 PHE A 543     3898   4035   4147   -182     71    212       C  
ATOM   4154  CE2 PHE A 543     142.610  99.851 -11.681  1.00 31.23           C  
ANISOU 4154  CE2 PHE A 543     3809   3970   4086   -155     67    205       C  
ATOM   4155  CZ  PHE A 543     143.714 100.541 -11.157  1.00 32.60           C  
ANISOU 4155  CZ  PHE A 543     3980   4149   4258   -172     72    205       C  
ATOM   4156  N   GLU A 544     137.571 103.424 -13.737  1.00 30.83           N  
ANISOU 4156  N   GLU A 544     3866   3853   3995   -127     37    233       N  
ATOM   4157  CA  GLU A 544     136.234 103.997 -13.958  1.00 32.25           C  
ANISOU 4157  CA  GLU A 544     4064   4019   4171   -113     26    238       C  
ATOM   4158  C   GLU A 544     135.428 103.975 -12.611  1.00 30.78           C  
ANISOU 4158  C   GLU A 544     3872   3826   3998   -100     17    236       C  
ATOM   4159  O   GLU A 544     134.601 104.830 -12.312  1.00 29.30           O  
ANISOU 4159  O   GLU A 544     3700   3624   3809    -94      9    239       O  
ATOM   4160  CB  GLU A 544     135.574 103.044 -15.003  1.00 34.36           C  
ANISOU 4160  CB  GLU A 544     4326   4293   4436   -100     24    234       C  
ATOM   4161  CG  GLU A 544     134.146 103.345 -15.409  1.00 37.78           C  
ANISOU 4161  CG  GLU A 544     4773   4716   4865    -84     12    236       C  
ATOM   4162  CD  GLU A 544     133.517 102.206 -16.219  1.00 40.22           C  
ANISOU 4162  CD  GLU A 544     5072   5035   5176    -71     10    230       C  
ATOM   4163  OE1 GLU A 544     134.227 101.277 -16.661  1.00 41.29           O  
ANISOU 4163  OE1 GLU A 544     5192   5185   5313    -77     19    225       O  
ATOM   4164  OE2 GLU A 544     132.300 102.229 -16.405  1.00 41.63           O  
ANISOU 4164  OE2 GLU A 544     5257   5208   5354    -56      0    229       O  
ATOM   4165  N   LYS A 545     135.703 102.955 -11.802  1.00 28.65           N  
ANISOU 4165  N   LYS A 545     3579   3565   3741    -98     19    230       N  
ATOM   4166  CA  LYS A 545     134.998 102.720 -10.577  1.00 28.24           C  
ANISOU 4166  CA  LYS A 545     3519   3510   3701    -87     12    227       C  
ATOM   4167  C   LYS A 545     135.931 102.446  -9.399  1.00 27.24           C  
ANISOU 4167  C   LYS A 545     3376   3390   3583    -96     17    225       C  
ATOM   4168  O   LYS A 545     137.078 102.102  -9.575  1.00 27.56           O  
ANISOU 4168  O   LYS A 545     3406   3441   3623   -107     24    224       O  
ATOM   4169  CB  LYS A 545     134.015 101.546 -10.790  1.00 28.25           C  
ANISOU 4169  CB  LYS A 545     3508   3515   3709    -70      7    221       C  
ATOM   4170  CG  LYS A 545     132.733 101.995 -11.512  1.00 29.54           C  
ANISOU 4170  CG  LYS A 545     3688   3670   3866    -57     -1    222       C  
ATOM   4171  CD  LYS A 545     131.813 100.844 -11.843  1.00 30.36           C  
ANISOU 4171  CD  LYS A 545     3780   3779   3975    -41     -5    216       C  
ATOM   4172  CE  LYS A 545     130.609 101.322 -12.656  1.00 30.22           C  
ANISOU 4172  CE  LYS A 545     3778   3755   3950    -29    -14    216       C  
ATOM   4173  NZ  LYS A 545     129.714 100.175 -12.916  1.00 30.97           N  
ANISOU 4173  NZ  LYS A 545     3860   3857   4051    -15    -17    208       N  
ATOM   4174  N   PRO A 546     135.406 102.562  -8.180  1.00 27.12           N  
ANISOU 4174  N   PRO A 546     3359   3371   3577    -91     11    224       N  
ATOM   4175  CA  PRO A 546     136.123 102.105  -7.001  1.00 26.55           C  
ANISOU 4175  CA  PRO A 546     3268   3306   3513    -97     13    222       C  
ATOM   4176  C   PRO A 546     136.392 100.617  -7.119  1.00 25.81           C  
ANISOU 4176  C   PRO A 546     3154   3225   3428    -91     15    218       C  
ATOM   4177  O   PRO A 546     135.599  99.941  -7.763  1.00 25.28           O  
ANISOU 4177  O   PRO A 546     3085   3158   3362    -79     12    215       O  
ATOM   4178  CB  PRO A 546     135.136 102.395  -5.867  1.00 27.21           C  
ANISOU 4178  CB  PRO A 546     3354   3382   3602    -89      5    220       C  
ATOM   4179  CG  PRO A 546     133.791 102.378  -6.536  1.00 26.45           C  
ANISOU 4179  CG  PRO A 546     3268   3278   3504    -74     -1    219       C  
ATOM   4180  CD  PRO A 546     134.048 103.063  -7.827  1.00 26.73           C  
ANISOU 4180  CD  PRO A 546     3320   3309   3528    -79      2    223       C  
ATOM   4181  N   PHE A 547     137.528 100.163  -6.557  1.00 25.07           N  
ANISOU 4181  N   PHE A 547     3044   3142   3338   -100     19    217       N  
ATOM   4182  CA  PHE A 547     137.908  98.764  -6.491  1.00 24.57           C  
ANISOU 4182  CA  PHE A 547     2960   3089   3285    -94     20    214       C  
ATOM   4183  C   PHE A 547     138.070  98.394  -5.037  1.00 25.80           C  
ANISOU 4183  C   PHE A 547     3103   3248   3450    -94     16    214       C  
ATOM   4184  O   PHE A 547     138.231  99.291  -4.184  1.00 25.73           O  
ANISOU 4184  O   PHE A 547     3100   3236   3438   -103     15    216       O  
ATOM   4185  CB  PHE A 547     139.157  98.434  -7.347  1.00 25.12           C  
ANISOU 4185  CB  PHE A 547     3022   3171   3354   -103     29    211       C  
ATOM   4186  CG  PHE A 547     140.415  99.158  -6.957  1.00 25.11           C  
ANISOU 4186  CG  PHE A 547     3018   3175   3349   -120     35    213       C  
ATOM   4187  CD1 PHE A 547     141.135  98.796  -5.811  1.00 25.50           C  
ANISOU 4187  CD1 PHE A 547     3051   3232   3406   -124     33    212       C  
ATOM   4188  CD2 PHE A 547     140.915 100.198  -7.760  1.00 25.42           C  
ANISOU 4188  CD2 PHE A 547     3071   3212   3374   -134     41    214       C  
ATOM   4189  CE1 PHE A 547     142.314  99.492  -5.465  1.00 26.01           C  
ANISOU 4189  CE1 PHE A 547     3114   3304   3467   -140     38    212       C  
ATOM   4190  CE2 PHE A 547     142.100 100.884  -7.419  1.00 25.13           C  
ANISOU 4190  CE2 PHE A 547     3033   3182   3334   -152     47    214       C  
ATOM   4191  CZ  PHE A 547     142.789 100.524  -6.278  1.00 25.62           C  
ANISOU 4191  CZ  PHE A 547     3078   3253   3405   -154     46    213       C  
ATOM   4192  N   VAL A 548     138.010  97.082  -4.770  1.00 24.29           N  
ANISOU 4192  N   VAL A 548     2896   3063   3270    -85     14    212       N  
ATOM   4193  CA  VAL A 548     138.282  96.527  -3.489  1.00 25.98           C  
ANISOU 4193  CA  VAL A 548     3097   3282   3492    -85     10    213       C  
ATOM   4194  C   VAL A 548     139.709  96.014  -3.499  1.00 26.28           C  
ANISOU 4194  C   VAL A 548     3119   3331   3535    -91     14    212       C  
ATOM   4195  O   VAL A 548     140.085  95.233  -4.380  1.00 26.21           O  
ANISOU 4195  O   VAL A 548     3102   3327   3529    -87     18    209       O  
ATOM   4196  CB  VAL A 548     137.305  95.368  -3.154  1.00 26.43           C  
ANISOU 4196  CB  VAL A 548     3147   3336   3559    -71      5    212       C  
ATOM   4197  CG1 VAL A 548     137.735  94.636  -1.911  1.00 27.36           C  
ANISOU 4197  CG1 VAL A 548     3251   3460   3685    -71      0    215       C  
ATOM   4198  CG2 VAL A 548     135.880  95.899  -2.954  1.00 26.27           C  
ANISOU 4198  CG2 VAL A 548     3141   3306   3535    -65      0    212       C  
ATOM   4199  N   LEU A 549     140.473  96.425  -2.488  1.00 26.90           N  
ANISOU 4199  N   LEU A 549     3193   3415   3614   -101     13    215       N  
ATOM   4200  CA  LEU A 549     141.799  95.873  -2.212  1.00 27.64           C  
ANISOU 4200  CA  LEU A 549     3269   3522   3713   -106     15    214       C  
ATOM   4201  C   LEU A 549     141.675  94.998  -0.957  1.00 27.35           C  
ANISOU 4201  C   LEU A 549     3219   3486   3685    -99      7    217       C  
ATOM   4202  O   LEU A 549     141.117  95.421   0.067  1.00 26.43           O  
ANISOU 4202  O   LEU A 549     3109   3367   3567   -101      2    220       O  
ATOM   4203  CB  LEU A 549     142.841  96.984  -2.049  1.00 27.97           C  
ANISOU 4203  CB  LEU A 549     3312   3569   3746   -123     20    213       C  
ATOM   4204  CG  LEU A 549     144.239  96.587  -1.623  1.00 29.37           C  
ANISOU 4204  CG  LEU A 549     3470   3761   3928   -129     21    211       C  
ATOM   4205  CD1 LEU A 549     144.981  95.790  -2.668  1.00 28.85           C  
ANISOU 4205  CD1 LEU A 549     3392   3704   3867   -126     27    206       C  
ATOM   4206  CD2 LEU A 549     145.053  97.842  -1.332  1.00 32.85           C  
ANISOU 4206  CD2 LEU A 549     3915   4206   4360   -148     26    211       C  
ATOM   4207  N   ASP A 550     142.202  93.776  -1.064  1.00 28.07           N  
ANISOU 4207  N   ASP A 550     3295   3584   3787    -91      6    215       N  
ATOM   4208  CA  ASP A 550     142.172  92.772  -0.020  1.00 28.74           C  
ANISOU 4208  CA  ASP A 550     3368   3671   3881    -84     -2    219       C  
ATOM   4209  C   ASP A 550     143.597  92.274   0.278  1.00 28.29           C  
ANISOU 4209  C   ASP A 550     3292   3626   3830    -86     -3    218       C  
ATOM   4210  O   ASP A 550     144.243  91.668  -0.587  1.00 27.69           O  
ANISOU 4210  O   ASP A 550     3206   3555   3760    -82      1    213       O  
ATOM   4211  CB  ASP A 550     141.335  91.598  -0.494  1.00 32.14           C  
ANISOU 4211  CB  ASP A 550     3798   4095   4321    -69     -4    218       C  
ATOM   4212  CG  ASP A 550     141.366  90.432   0.480  1.00 35.99           C  
ANISOU 4212  CG  ASP A 550     4274   4583   4819    -61    -12    222       C  
ATOM   4213  OD1 ASP A 550     141.313  90.709   1.682  1.00 40.28           O  
ANISOU 4213  OD1 ASP A 550     4817   5127   5359    -66    -18    228       O  
ATOM   4214  OD2 ASP A 550     141.428  89.237   0.082  1.00 39.41           O  
ANISOU 4214  OD2 ASP A 550     4698   5014   5262    -51    -13    221       O  
ATOM   4215  N   ILE A 551     144.073  92.518   1.498  1.00 27.97           N  
ANISOU 4215  N   ILE A 551     3247   3591   3789    -92     -9    223       N  
ATOM   4216  CA  ILE A 551     145.402  92.068   1.929  1.00 27.66           C  
ANISOU 4216  CA  ILE A 551     3189   3565   3756    -93    -12    222       C  
ATOM   4217  C   ILE A 551     145.147  91.112   3.079  1.00 27.97           C  
ANISOU 4217  C   ILE A 551     3221   3603   3803    -85    -23    230       C  
ATOM   4218  O   ILE A 551     144.622  91.525   4.118  1.00 27.02           O  
ANISOU 4218  O   ILE A 551     3108   3480   3677    -89    -28    235       O  
ATOM   4219  CB  ILE A 551     146.280  93.252   2.394  1.00 28.00           C  
ANISOU 4219  CB  ILE A 551     3230   3618   3789   -110     -9    221       C  
ATOM   4220  CG1 ILE A 551     146.528  94.215   1.213  1.00 28.14           C  
ANISOU 4220  CG1 ILE A 551     3258   3636   3799   -120      2    215       C  
ATOM   4221  CG2 ILE A 551     147.598  92.724   2.999  1.00 28.06           C  
ANISOU 4221  CG2 ILE A 551     3217   3640   3804   -110    -14    221       C  
ATOM   4222  CD1 ILE A 551     146.962  95.621   1.610  1.00 29.23           C  
ANISOU 4222  CD1 ILE A 551     3403   3778   3926   -138      6    214       C  
ATOM   4223  N   LEU A 552     145.523  89.854   2.899  1.00 27.64           N  
ANISOU 4223  N   LEU A 552     3166   3562   3773    -72    -26    229       N  
ATOM   4224  CA  LEU A 552     145.371  88.844   3.911  1.00 28.08           C  
ANISOU 4224  CA  LEU A 552     3217   3616   3837    -64    -37    237       C  
ATOM   4225  C   LEU A 552     146.718  88.349   4.317  1.00 27.86           C  
ANISOU 4225  C   LEU A 552     3170   3601   3817    -61    -43    237       C  
ATOM   4226  O   LEU A 552     147.278  87.520   3.655  1.00 27.00           O  
ANISOU 4226  O   LEU A 552     3049   3493   3718    -52    -42    233       O  
ATOM   4227  CB  LEU A 552     144.493  87.682   3.392  1.00 31.07           C  
ANISOU 4227  CB  LEU A 552     3598   3982   4225    -50    -38    237       C  
ATOM   4228  CG  LEU A 552     143.607  87.029   4.465  1.00 32.24           C  
ANISOU 4228  CG  LEU A 552     3751   4122   4375    -45    -47    246       C  
ATOM   4229  CD1 LEU A 552     142.647  86.018   3.876  1.00 34.53           C  
ANISOU 4229  CD1 LEU A 552     4047   4400   4673    -34    -46    245       C  
ATOM   4230  CD2 LEU A 552     144.410  86.384   5.565  1.00 33.38           C  
ANISOU 4230  CD2 LEU A 552     3885   4273   4526    -42    -58    254       C  
ATOM   4231  N   ARG A 553     147.242  88.858   5.437  1.00 29.18           N  
ANISOU 4231  N   ARG A 553     3333   3776   3977    -70    -49    242       N  
ATOM   4232  CA  ARG A 553     148.556  88.501   5.930  1.00 28.85           C  
ANISOU 4232  CA  ARG A 553     3272   3748   3941    -68    -56    242       C  
ATOM   4233  C   ARG A 553     148.436  87.332   6.921  1.00 30.62           C  
ANISOU 4233  C   ARG A 553     3492   3969   4174    -57    -69    252       C  
ATOM   4234  O   ARG A 553     147.607  87.352   7.809  1.00 31.77           O  
ANISOU 4234  O   ARG A 553     3648   4109   4314    -59    -75    261       O  
ATOM   4235  CB  ARG A 553     149.198  89.731   6.583  1.00 28.85           C  
ANISOU 4235  CB  ARG A 553     3271   3761   3930    -85    -55    241       C  
ATOM   4236  CG  ARG A 553     150.617  89.487   7.113  1.00 29.50           C  
ANISOU 4236  CG  ARG A 553     3333   3860   4016    -85    -62    240       C  
ATOM   4237  CD  ARG A 553     151.238  90.810   7.554  1.00 30.73           C  
ANISOU 4237  CD  ARG A 553     3488   4030   4160   -104    -58    236       C  
ATOM   4238  NE  ARG A 553     150.562  91.314   8.758  1.00 31.95           N  
ANISOU 4238  NE  ARG A 553     3654   4181   4304   -112    -64    245       N  
ATOM   4239  CZ  ARG A 553     150.829  90.916  10.013  1.00 32.53           C  
ANISOU 4239  CZ  ARG A 553     3720   4262   4377   -111    -76    253       C  
ATOM   4240  NH1 ARG A 553     151.784  90.052  10.279  1.00 33.66           N  
ANISOU 4240  NH1 ARG A 553     3845   4414   4529   -101    -86    254       N  
ATOM   4241  NH2 ARG A 553     150.195  91.422  11.042  1.00 32.27           N  
ANISOU 4241  NH2 ARG A 553     3699   4228   4335   -119    -80    259       N  
ATOM   4242  N   VAL A 554     149.265  86.323   6.764  1.00 30.36           N  
ANISOU 4242  N   VAL A 554     3443   3940   4154    -44    -75    251       N  
ATOM   4243  CA  VAL A 554     149.189  85.096   7.577  1.00 30.83           C  
ANISOU 4243  CA  VAL A 554     3498   3993   4223    -31    -88    262       C  
ATOM   4244  C   VAL A 554     150.592  84.838   8.144  1.00 31.98           C  
ANISOU 4244  C   VAL A 554     3623   4153   4373    -28    -98    262       C  
ATOM   4245  O   VAL A 554     151.571  84.801   7.409  1.00 33.07           O  
ANISOU 4245  O   VAL A 554     3746   4301   4518    -25    -94    252       O  
ATOM   4246  CB  VAL A 554     148.786  83.877   6.719  1.00 31.50           C  
ANISOU 4246  CB  VAL A 554     3582   4064   4322    -15    -87    259       C  
ATOM   4247  CG1 VAL A 554     148.475  82.641   7.548  1.00 30.90           C  
ANISOU 4247  CG1 VAL A 554     3507   3977   4254     -3   -100    271       C  
ATOM   4248  CG2 VAL A 554     147.593  84.193   5.836  1.00 30.58           C  
ANISOU 4248  CG2 VAL A 554     3483   3936   4201    -18    -75    255       C  
ATOM   4249  N   GLY A 555     150.664  84.671   9.457  1.00 33.18           N  
ANISOU 4249  N   GLY A 555     3775   4309   4522    -29   -111    274       N  
ATOM   4250  CA  GLY A 555     151.876  84.281  10.168  1.00 33.41           C  
ANISOU 4250  CA  GLY A 555     3786   4351   4555    -24   -123    277       C  
ATOM   4251  C   GLY A 555     151.557  82.990  10.886  1.00 34.51           C  
ANISOU 4251  C   GLY A 555     3929   4480   4705     -9   -138    290       C  
ATOM   4252  O   GLY A 555     150.487  82.875  11.465  1.00 34.39           O  
ANISOU 4252  O   GLY A 555     3930   4454   4683    -12   -140    300       O  
ATOM   4253  N   SER A 556     152.464  82.024  10.850  1.00 34.11           N  
ANISOU 4253  N   SER A 556     3861   4431   4667      7   -148    290       N  
ATOM   4254  CA  SER A 556     152.248  80.754  11.479  1.00 35.82           C  
ANISOU 4254  CA  SER A 556     4080   4636   4894     21   -162    303       C  
ATOM   4255  C   SER A 556     153.569  80.146  11.951  1.00 38.16           C  
ANISOU 4255  C   SER A 556     4356   4943   5200     34   -177    305       C  
ATOM   4256  O   SER A 556     154.604  80.569  11.519  1.00 36.37           O  
ANISOU 4256  O   SER A 556     4111   4732   4975     33   -174    293       O  
ATOM   4257  CB  SER A 556     151.596  79.820  10.458  1.00 35.69           C  
ANISOU 4257  CB  SER A 556     4069   4599   4891     34   -155    299       C  
ATOM   4258  OG  SER A 556     151.129  78.642  11.100  1.00 36.65           O  
ANISOU 4258  OG  SER A 556     4198   4705   5020     46   -168    313       O  
ATOM   4259  N   ASN A 557     153.493  79.092  12.753  1.00 41.60           N  
ANISOU 4259  N   ASN A 557     4794   5369   5642     46   -193    319       N  
ATOM   4260  CA  ASN A 557     154.699  78.388  13.256  1.00 46.45           C  
ANISOU 4260  CA  ASN A 557     5389   5992   6267     61   -210    323       C  
ATOM   4261  C   ASN A 557     154.988  77.022  12.605  1.00 44.72           C  
ANISOU 4261  C   ASN A 557     5163   5758   6070     85   -215    321       C  
ATOM   4262  O   ASN A 557     155.982  76.407  12.909  1.00 50.27           O  
ANISOU 4262  O   ASN A 557     5849   6466   6784    100   -230    322       O  
ATOM   4263  CB  ASN A 557     154.665  78.276  14.808  1.00 49.76           C  
ANISOU 4263  CB  ASN A 557     5815   6415   6675     58   -228    342       C  
ATOM   4264  CG  ASN A 557     153.343  77.707  15.368  1.00 53.17           C  
ANISOU 4264  CG  ASN A 557     6272   6827   7103     56   -231    358       C  
ATOM   4265  OD1 ASN A 557     152.583  77.004  14.700  1.00 50.45           O  
ANISOU 4265  OD1 ASN A 557     5937   6462   6768     63   -224    357       O  
ATOM   4266  ND2 ASN A 557     153.100  77.984  16.638  1.00 57.95           N  
ANISOU 4266  ND2 ASN A 557     6886   7438   7693     45   -240    372       N  
ATOM   4267  N   ALA A 558     154.122  76.574  11.709  1.00 41.80           N  
ANISOU 4267  N   ALA A 558     4804   5369   5708     89   -204    316       N  
ATOM   4268  CA  ALA A 558     154.332  75.400  10.876  1.00 40.01           C  
ANISOU 4268  CA  ALA A 558     4570   5129   5503    109   -205    310       C  
ATOM   4269  C   ALA A 558     153.988  75.731   9.422  1.00 40.15           C  
ANISOU 4269  C   ALA A 558     4587   5144   5523    105   -184    292       C  
ATOM   4270  O   ALA A 558     153.236  76.717   9.117  1.00 39.03           O  
ANISOU 4270  O   ALA A 558     4458   5005   5367     88   -170    288       O  
ATOM   4271  CB  ALA A 558     153.449  74.233  11.349  1.00 39.30           C  
ANISOU 4271  CB  ALA A 558     4498   5014   5419    119   -214    326       C  
ATOM   4272  N   ALA A 559     154.491  74.874   8.539  1.00 38.14           N  
ANISOU 4272  N   ALA A 559     4321   4884   5288    122   -183    281       N  
ATOM   4273  CA  ALA A 559     154.128  74.875   7.149  1.00 38.30           C  
ANISOU 4273  CA  ALA A 559     4340   4897   5313    122   -166    264       C  
ATOM   4274  C   ALA A 559     152.728  74.223   6.968  1.00 39.48           C  
ANISOU 4274  C   ALA A 559     4512   5023   5464    123   -162    272       C  
ATOM   4275  O   ALA A 559     152.503  73.075   7.351  1.00 38.94           O  
ANISOU 4275  O   ALA A 559     4450   4937   5409    137   -172    281       O  
ATOM   4276  CB  ALA A 559     155.169  74.148   6.348  1.00 36.81           C  
ANISOU 4276  CB  ALA A 559     4130   4712   5145    140   -166    249       C  
ATOM   4277  N   ASN A 560     151.796  74.972   6.391  1.00 37.30           N  
ANISOU 4277  N   ASN A 560     4250   4746   5177    108   -146    267       N  
ATOM   4278  CA  ASN A 560     150.423  74.499   6.185  1.00 36.86           C  
ANISOU 4278  CA  ASN A 560     4214   4670   5120    107   -141    272       C  
ATOM   4279  C   ASN A 560     149.943  74.611   4.762  1.00 35.62           C  
ANISOU 4279  C   ASN A 560     4059   4510   4966    105   -124    255       C  
ATOM   4280  O   ASN A 560     150.610  75.179   3.871  1.00 36.49           O  
ANISOU 4280  O   ASN A 560     4157   4634   5075    102   -114    240       O  
ATOM   4281  CB  ASN A 560     149.436  75.303   7.048  1.00 36.92           C  
ANISOU 4281  CB  ASN A 560     4241   4678   5108     90   -141    284       C  
ATOM   4282  CG  ASN A 560     149.798  75.327   8.529  1.00 36.05           C  
ANISOU 4282  CG  ASN A 560     4131   4573   4992     88   -157    301       C  
ATOM   4283  OD1 ASN A 560     149.668  74.338   9.234  1.00 36.62           O  
ANISOU 4283  OD1 ASN A 560     4209   4633   5072     97   -170    313       O  
ATOM   4284  ND2 ASN A 560     150.167  76.515   9.019  1.00 35.62           N  
ANISOU 4284  ND2 ASN A 560     4074   4537   4923     74   -156    301       N  
ATOM   4285  N   GLN A 561     148.764  74.053   4.538  1.00 34.03           N  
ANISOU 4285  N   GLN A 561     3874   4290   4766    106   -120    258       N  
ATOM   4286  CA  GLN A 561     148.043  74.314   3.303  1.00 33.82           C  
ANISOU 4286  CA  GLN A 561     3853   4260   4736    101   -103    245       C  
ATOM   4287  C   GLN A 561     146.998  75.445   3.516  1.00 32.50           C  
ANISOU 4287  C   GLN A 561     3702   4097   4549     82    -96    250       C  
ATOM   4288  O   GLN A 561     146.067  75.292   4.307  1.00 32.36           O  
ANISOU 4288  O   GLN A 561     3701   4070   4526     78   -101    262       O  
ATOM   4289  CB  GLN A 561     147.385  73.038   2.813  1.00 34.10           C  
ANISOU 4289  CB  GLN A 561     3895   4276   4787    112   -102    243       C  
ATOM   4290  CG  GLN A 561     146.659  73.210   1.489  1.00 34.46           C  
ANISOU 4290  CG  GLN A 561     3944   4318   4830    108    -86    228       C  
ATOM   4291  CD  GLN A 561     145.956  71.947   1.060  1.00 36.41           C  
ANISOU 4291  CD  GLN A 561     4197   4545   5090    118    -85    226       C  
ATOM   4292  OE1 GLN A 561     146.567  71.100   0.439  1.00 38.44           O  
ANISOU 4292  OE1 GLN A 561     4444   4798   5365    132    -85    216       O  
ATOM   4293  NE2 GLN A 561     144.649  71.830   1.343  1.00 36.60           N  
ANISOU 4293  NE2 GLN A 561     4240   4557   5108    111    -83    233       N  
ATOM   4294  N   TYR A 562     147.152  76.555   2.801  1.00 31.44           N  
ANISOU 4294  N   TYR A 562     3566   3977   4404     72    -85    239       N  
ATOM   4295  CA  TYR A 562     146.177  77.670   2.834  1.00 30.04           C  
ANISOU 4295  CA  TYR A 562     3404   3801   4208     56    -77    241       C  
ATOM   4296  C   TYR A 562     145.308  77.745   1.597  1.00 28.98           C  
ANISOU 4296  C   TYR A 562     3278   3662   4072     54    -64    230       C  
ATOM   4297  O   TYR A 562     145.816  77.673   0.482  1.00 31.14           O  
ANISOU 4297  O   TYR A 562     3542   3940   4351     58    -56    217       O  
ATOM   4298  CB  TYR A 562     146.902  79.010   2.977  1.00 29.71           C  
ANISOU 4298  CB  TYR A 562     3357   3778   4153     43    -75    239       C  
ATOM   4299  CG  TYR A 562     147.750  79.111   4.219  1.00 28.81           C  
ANISOU 4299  CG  TYR A 562     3235   3673   4038     43    -87    249       C  
ATOM   4300  CD1 TYR A 562     147.230  78.833   5.475  1.00 27.59           C  
ANISOU 4300  CD1 TYR A 562     3091   3513   3881     42    -98    264       C  
ATOM   4301  CD2 TYR A 562     149.097  79.486   4.128  1.00 28.89           C  
ANISOU 4301  CD2 TYR A 562     3227   3699   4050     43    -88    243       C  
ATOM   4302  CE1 TYR A 562     148.028  78.921   6.594  1.00 28.13           C  
ANISOU 4302  CE1 TYR A 562     3151   3589   3947     41   -110    274       C  
ATOM   4303  CE2 TYR A 562     149.880  79.601   5.247  1.00 28.65           C  
ANISOU 4303  CE2 TYR A 562     3189   3679   4019     42   -100    251       C  
ATOM   4304  CZ  TYR A 562     149.354  79.308   6.470  1.00 29.10           C  
ANISOU 4304  CZ  TYR A 562     3256   3729   4072     42   -112    267       C  
ATOM   4305  OH  TYR A 562     150.172  79.391   7.579  1.00 30.33           O  
ANISOU 4305  OH  TYR A 562     3402   3895   4225     41   -124    275       O  
ATOM   4306  N   ASP A 563     143.992  77.822   1.795  1.00 28.53           N  
ANISOU 4306  N   ASP A 563     3238   3595   4008     49    -63    235       N  
ATOM   4307  CA  ASP A 563     143.015  77.932   0.708  1.00 27.95           C  
ANISOU 4307  CA  ASP A 563     3173   3516   3931     47    -51    226       C  
ATOM   4308  C   ASP A 563     142.332  79.291   0.860  1.00 27.71           C  
ANISOU 4308  C   ASP A 563     3154   3492   3881     33    -47    228       C  
ATOM   4309  O   ASP A 563     141.940  79.652   1.963  1.00 27.26           O  
ANISOU 4309  O   ASP A 563     3106   3435   3818     26    -53    238       O  
ATOM   4310  CB  ASP A 563     141.946  76.845   0.776  1.00 28.75           C  
ANISOU 4310  CB  ASP A 563     3284   3601   4041     53    -53    228       C  
ATOM   4311  CG  ASP A 563     142.432  75.483   0.261  1.00 30.72           C  
ANISOU 4311  CG  ASP A 563     3523   3841   4309     68    -54    223       C  
ATOM   4312  OD1 ASP A 563     143.335  75.421  -0.575  1.00 31.43           O  
ANISOU 4312  OD1 ASP A 563     3599   3938   4405     73    -50    212       O  
ATOM   4313  OD2 ASP A 563     141.915  74.453   0.716  1.00 32.80           O  
ANISOU 4313  OD2 ASP A 563     3791   4090   4581     74    -60    229       O  
ATOM   4314  N   LEU A 564     142.155  80.021  -0.245  1.00 28.37           N  
ANISOU 4314  N   LEU A 564     3240   3581   3958     28    -36    218       N  
ATOM   4315  CA  LEU A 564     141.453  81.323  -0.237  1.00 27.27           C  
ANISOU 4315  CA  LEU A 564     3114   3446   3802     16    -32    219       C  
ATOM   4316  C   LEU A 564     140.365  81.349  -1.313  1.00 27.62           C  
ANISOU 4316  C   LEU A 564     3168   3484   3843     17    -24    210       C  
ATOM   4317  O   LEU A 564     140.653  81.553  -2.502  1.00 27.92           O  
ANISOU 4317  O   LEU A 564     3203   3527   3880     17    -16    200       O  
ATOM   4318  CB  LEU A 564     142.438  82.505  -0.376  1.00 27.80           C  
ANISOU 4318  CB  LEU A 564     3177   3527   3861      7    -28    216       C  
ATOM   4319  CG  LEU A 564     141.774  83.918  -0.222  1.00 28.91           C  
ANISOU 4319  CG  LEU A 564     3331   3670   3984     -6    -25    218       C  
ATOM   4320  CD1 LEU A 564     141.028  84.009   1.080  1.00 28.34           C  
ANISOU 4320  CD1 LEU A 564     3267   3593   3907     -9    -33    229       C  
ATOM   4321  CD2 LEU A 564     142.722  85.130  -0.352  1.00 28.53           C  
ANISOU 4321  CD2 LEU A 564     3279   3634   3926    -17    -21    216       C  
ATOM   4322  N   PRO A 565     139.089  81.093  -0.930  1.00 26.51           N  
ANISOU 4322  N   PRO A 565     3038   3334   3700     17    -26    214       N  
ATOM   4323  CA  PRO A 565     138.002  81.066  -1.938  1.00 25.79           C  
ANISOU 4323  CA  PRO A 565     2954   3238   3605     18    -19    205       C  
ATOM   4324  C   PRO A 565     137.460  82.441  -2.313  1.00 25.34           C  
ANISOU 4324  C   PRO A 565     2909   3187   3533     10    -14    203       C  
ATOM   4325  O   PRO A 565     137.497  83.390  -1.453  1.00 24.99           O  
ANISOU 4325  O   PRO A 565     2869   3146   3480      2    -18    210       O  
ATOM   4326  CB  PRO A 565     136.893  80.261  -1.245  1.00 25.71           C  
ANISOU 4326  CB  PRO A 565     2952   3218   3600     21    -23    210       C  
ATOM   4327  CG  PRO A 565     137.585  79.610  -0.071  1.00 26.26           C  
ANISOU 4327  CG  PRO A 565     3015   3284   3678     23    -32    220       C  
ATOM   4328  CD  PRO A 565     138.614  80.582   0.353  1.00 26.13           C  
ANISOU 4328  CD  PRO A 565     2994   3279   3655     17    -34    224       C  
ATOM   4329  N   PHE A 566     137.004  82.542  -3.570  1.00 23.65           N  
ANISOU 4329  N   PHE A 566     2698   2972   3315     12     -7    194       N  
ATOM   4330  CA  PHE A 566     136.228  83.680  -4.069  1.00 24.55           C  
ANISOU 4330  CA  PHE A 566     2824   3089   3416      6     -4    191       C  
ATOM   4331  C   PHE A 566     134.996  83.124  -4.780  1.00 25.17           C  
ANISOU 4331  C   PHE A 566     2907   3161   3495     12     -1    184       C  
ATOM   4332  O   PHE A 566     135.080  82.628  -5.870  1.00 26.29           O  
ANISOU 4332  O   PHE A 566     3046   3304   3640     16      4    176       O  
ATOM   4333  CB  PHE A 566     137.051  84.541  -5.037  1.00 24.71           C  
ANISOU 4333  CB  PHE A 566     2843   3117   3428      1      2    187       C  
ATOM   4334  CG  PHE A 566     138.238  85.228  -4.396  1.00 24.34           C  
ANISOU 4334  CG  PHE A 566     2791   3077   3378     -6      1    193       C  
ATOM   4335  CD1 PHE A 566     139.419  84.574  -4.289  1.00 26.27           C  
ANISOU 4335  CD1 PHE A 566     3022   3327   3633     -4      1    192       C  
ATOM   4336  CD2 PHE A 566     138.157  86.523  -3.951  1.00 24.54           C  
ANISOU 4336  CD2 PHE A 566     2826   3105   3392    -15      0    197       C  
ATOM   4337  CE1 PHE A 566     140.535  85.180  -3.709  1.00 27.41           C  
ANISOU 4337  CE1 PHE A 566     3159   3479   3775    -11     -1    196       C  
ATOM   4338  CE2 PHE A 566     139.245  87.147  -3.352  1.00 27.23           C  
ANISOU 4338  CE2 PHE A 566     3162   3453   3730    -23     -1    202       C  
ATOM   4339  CZ  PHE A 566     140.440  86.477  -3.233  1.00 27.79           C  
ANISOU 4339  CZ  PHE A 566     3218   3531   3811    -21     -1    201       C  
ATOM   4340  N   TYR A 567     133.839  83.184  -4.123  1.00 25.77           N  
ANISOU 4340  N   TYR A 567     2991   3232   3568     11     -5    187       N  
ATOM   4341  CA  TYR A 567     132.591  82.683  -4.680  1.00 24.68           C  
ANISOU 4341  CA  TYR A 567     2858   3090   3431     16     -3    179       C  
ATOM   4342  C   TYR A 567     131.925  83.790  -5.470  1.00 24.90           C  
ANISOU 4342  C   TYR A 567     2895   3121   3445     14     -1    175       C  
ATOM   4343  O   TYR A 567     131.166  84.605  -4.922  1.00 24.63           O  
ANISOU 4343  O   TYR A 567     2870   3087   3403     11     -4    177       O  
ATOM   4344  CB  TYR A 567     131.676  82.118  -3.561  1.00 24.57           C  
ANISOU 4344  CB  TYR A 567     2847   3070   3421     15     -8    183       C  
ATOM   4345  CG  TYR A 567     132.236  80.803  -3.009  1.00 24.36           C  
ANISOU 4345  CG  TYR A 567     2812   3037   3408     19    -11    187       C  
ATOM   4346  CD1 TYR A 567     132.187  79.649  -3.766  1.00 24.37           C  
ANISOU 4346  CD1 TYR A 567     2808   3033   3420     25     -7    180       C  
ATOM   4347  CD2 TYR A 567     132.882  80.749  -1.747  1.00 24.28           C  
ANISOU 4347  CD2 TYR A 567     2799   3026   3401     15    -17    198       C  
ATOM   4348  CE1 TYR A 567     132.734  78.443  -3.301  1.00 25.38           C  
ANISOU 4348  CE1 TYR A 567     2928   3153   3561     30    -10    184       C  
ATOM   4349  CE2 TYR A 567     133.440  79.558  -1.280  1.00 24.46           C  
ANISOU 4349  CE2 TYR A 567     2815   3042   3436     20    -20    203       C  
ATOM   4350  CZ  TYR A 567     133.364  78.409  -2.072  1.00 24.91           C  
ANISOU 4350  CZ  TYR A 567     2868   3093   3504     27    -17    195       C  
ATOM   4351  OH  TYR A 567     133.896  77.225  -1.673  1.00 27.75           O  
ANISOU 4351  OH  TYR A 567     3221   3444   3877     33    -20    199       O  
ATOM   4352  N   PHE A 568     132.209  83.794  -6.766  1.00 25.19           N  
ANISOU 4352  N   PHE A 568     2931   3162   3480     16      4    168       N  
ATOM   4353  CA  PHE A 568     131.819  84.873  -7.685  1.00 25.43           C  
ANISOU 4353  CA  PHE A 568     2970   3196   3496     15      6    164       C  
ATOM   4354  C   PHE A 568     130.481  84.526  -8.311  1.00 26.71           C  
ANISOU 4354  C   PHE A 568     3137   3356   3656     20      6    156       C  
ATOM   4355  O   PHE A 568     130.090  83.354  -8.366  1.00 26.20           O  
ANISOU 4355  O   PHE A 568     3066   3288   3601     25      7    151       O  
ATOM   4356  CB  PHE A 568     132.895  85.125  -8.716  1.00 25.36           C  
ANISOU 4356  CB  PHE A 568     2958   3193   3483     12     12    162       C  
ATOM   4357  CG  PHE A 568     133.144  83.974  -9.622  1.00 25.10           C  
ANISOU 4357  CG  PHE A 568     2916   3162   3460     17     17    153       C  
ATOM   4358  CD1 PHE A 568     132.398  83.840 -10.786  1.00 24.21           C  
ANISOU 4358  CD1 PHE A 568     2807   3051   3341     21     20    144       C  
ATOM   4359  CD2 PHE A 568     134.113  83.045  -9.331  1.00 25.58           C  
ANISOU 4359  CD2 PHE A 568     2964   3222   3533     19     19    152       C  
ATOM   4360  CE1 PHE A 568     132.577  82.773 -11.633  1.00 25.55           C  
ANISOU 4360  CE1 PHE A 568     2968   3222   3518     25     25    134       C  
ATOM   4361  CE2 PHE A 568     134.310  81.955 -10.200  1.00 26.19           C  
ANISOU 4361  CE2 PHE A 568     3032   3299   3618     25     24    142       C  
ATOM   4362  CZ  PHE A 568     133.536  81.820 -11.325  1.00 25.78           C  
ANISOU 4362  CZ  PHE A 568     2984   3250   3561     27     27    133       C  
ATOM   4363  N   LYS A 569     129.745  85.557  -8.690  1.00 25.95           N  
ANISOU 4363  N   LYS A 569     3050   3261   3547     20      4    155       N  
ATOM   4364  CA  LYS A 569     128.504  85.412  -9.421  1.00 26.71           C  
ANISOU 4364  CA  LYS A 569     3150   3357   3639     26      4    147       C  
ATOM   4365  C   LYS A 569     128.667  85.897 -10.865  1.00 28.23           C  
ANISOU 4365  C   LYS A 569     3348   3556   3822     26      7    143       C  
ATOM   4366  O   LYS A 569     129.062  87.039 -11.093  1.00 29.84           O  
ANISOU 4366  O   LYS A 569     3560   3761   4015     22      6    148       O  
ATOM   4367  CB  LYS A 569     127.411  86.238  -8.761  1.00 26.87           C  
ANISOU 4367  CB  LYS A 569     3179   3375   3653     26     -2    148       C  
ATOM   4368  CG  LYS A 569     127.242  85.994  -7.255  1.00 27.60           C  
ANISOU 4368  CG  LYS A 569     3270   3465   3753     23     -5    153       C  
ATOM   4369  CD  LYS A 569     126.818  84.616  -6.820  1.00 28.17           C  
ANISOU 4369  CD  LYS A 569     3333   3533   3836     25     -5    150       C  
ATOM   4370  CE  LYS A 569     125.528  84.142  -7.472  1.00 29.75           C  
ANISOU 4370  CE  LYS A 569     3533   3734   4036     30     -4    139       C  
ATOM   4371  NZ  LYS A 569     124.421  85.068  -7.138  1.00 30.49           N  
ANISOU 4371  NZ  LYS A 569     3634   3829   4121     31     -9    136       N  
ATOM   4372  N   GLY A 570     128.291  85.058 -11.823  1.00 27.64           N  
ANISOU 4372  N   GLY A 570     3269   3484   3749     31     10    133       N  
ATOM   4373  CA  GLY A 570     128.283  85.414 -13.226  1.00 27.54           C  
ANISOU 4373  CA  GLY A 570     3261   3477   3726     31     13    128       C  
ATOM   4374  C   GLY A 570     128.971  84.394 -14.132  1.00 27.53           C  
ANISOU 4374  C   GLY A 570     3249   3480   3729     31     20    120       C  
ATOM   4375  O   GLY A 570     129.402  83.327 -13.690  1.00 26.68           O  
ANISOU 4375  O   GLY A 570     3131   3370   3636     32     23    118       O  
ATOM   4376  N   GLN A 571     128.996  84.765 -15.416  1.00 27.29           N  
ANISOU 4376  N   GLN A 571     3224   3457   3688     31     23    116       N  
ATOM   4377  CA  GLN A 571     129.571  84.041 -16.536  1.00 26.19           C  
ANISOU 4377  CA  GLN A 571     3077   3325   3549     30     31    106       C  
ATOM   4378  C   GLN A 571     131.059  84.362 -16.722  1.00 25.93           C  
ANISOU 4378  C   GLN A 571     3041   3296   3515     22     37    110       C  
ATOM   4379  O   GLN A 571     131.432  85.512 -16.995  1.00 24.16           O  
ANISOU 4379  O   GLN A 571     2827   3075   3279     16     37    117       O  
ATOM   4380  CB  GLN A 571     128.775  84.424 -17.772  1.00 27.42           C  
ANISOU 4380  CB  GLN A 571     3241   3487   3690     31     30    101       C  
ATOM   4381  CG  GLN A 571     129.282  83.945 -19.126  1.00 28.37           C  
ANISOU 4381  CG  GLN A 571     3357   3617   3806     29     38     91       C  
ATOM   4382  CD  GLN A 571     129.311  82.435 -19.206  1.00 28.70           C  
ANISOU 4382  CD  GLN A 571     3383   3657   3863     32     43     79       C  
ATOM   4383  OE1 GLN A 571     128.280  81.811 -19.072  1.00 27.14           O  
ANISOU 4383  OE1 GLN A 571     3184   3456   3670     38     40     73       O  
ATOM   4384  NE2 GLN A 571     130.495  81.853 -19.422  1.00 29.12           N  
ANISOU 4384  NE2 GLN A 571     3426   3713   3924     29     51     75       N  
ATOM   4385  N   VAL A 572     131.908  83.339 -16.615  1.00 24.64           N  
ANISOU 4385  N   VAL A 572     2863   3132   3365     22     42    105       N  
ATOM   4386  CA  VAL A 572     133.334  83.468 -16.879  1.00 25.39           C  
ANISOU 4386  CA  VAL A 572     2952   3234   3461     16     49    105       C  
ATOM   4387  C   VAL A 572     133.602  84.008 -18.277  1.00 26.54           C  
ANISOU 4387  C   VAL A 572     3103   3390   3591     10     55    100       C  
ATOM   4388  O   VAL A 572     133.026  83.516 -19.286  1.00 28.30           O  
ANISOU 4388  O   VAL A 572     3326   3618   3810     12     58     90       O  
ATOM   4389  CB  VAL A 572     134.050  82.122 -16.654  1.00 25.78           C  
ANISOU 4389  CB  VAL A 572     2985   3282   3530     20     53     98       C  
ATOM   4390  CG1 VAL A 572     135.515  82.182 -17.026  1.00 26.34           C  
ANISOU 4390  CG1 VAL A 572     3047   3361   3601     14     60     95       C  
ATOM   4391  CG2 VAL A 572     133.955  81.751 -15.208  1.00 25.76           C  
ANISOU 4391  CG2 VAL A 572     2979   3269   3540     24     47    106       C  
ATOM   4392  N   MET A 573     134.421  85.057 -18.348  1.00 25.95           N  
ANISOU 4392  N   MET A 573     3035   3319   3506      0     57    107       N  
ATOM   4393  CA  MET A 573     134.800  85.682 -19.594  1.00 27.15           C  
ANISOU 4393  CA  MET A 573     3193   3481   3641     -8     63    105       C  
ATOM   4394  C   MET A 573     136.251  85.405 -20.093  1.00 28.36           C  
ANISOU 4394  C   MET A 573     3335   3645   3797    -16     74     98       C  
ATOM   4395  O   MET A 573     136.468  85.288 -21.275  1.00 31.33           O  
ANISOU 4395  O   MET A 573     3710   4031   4164    -21     81     89       O  
ATOM   4396  CB  MET A 573     134.671  87.203 -19.439  1.00 27.85           C  
ANISOU 4396  CB  MET A 573     3300   3568   3714    -15     59    117       C  
ATOM   4397  CG  MET A 573     133.239  87.715 -19.439  1.00 28.88           C  
ANISOU 4397  CG  MET A 573     3445   3692   3836     -8     49    122       C  
ATOM   4398  SD  MET A 573     132.428  87.580 -21.060  1.00 32.55           S  
ANISOU 4398  SD  MET A 573     3917   4165   4286     -6     50    113       S  
ATOM   4399  CE  MET A 573     131.141  86.432 -20.708  1.00 29.96           C  
ANISOU 4399  CE  MET A 573     3580   3832   3970      8     45    105       C  
ATOM   4400  N   GLN A 574     137.212  85.375 -19.181  1.00 28.28           N  
ANISOU 4400  N   GLN A 574     3315   3633   3796    -19     74    101       N  
ATOM   4401  CA  GLN A 574     138.627  85.487 -19.504  1.00 31.65           C  
ANISOU 4401  CA  GLN A 574     3732   4070   4223    -28     83     97       C  
ATOM   4402  C   GLN A 574     139.492  85.120 -18.296  1.00 31.23           C  
ANISOU 4402  C   GLN A 574     3665   4014   4186    -26     81    100       C  
ATOM   4403  O   GLN A 574     139.138  85.461 -17.157  1.00 27.73           O  
ANISOU 4403  O   GLN A 574     3227   3562   3747    -23     73    111       O  
ATOM   4404  CB  GLN A 574     138.942  86.945 -19.867  1.00 36.88           C  
ANISOU 4404  CB  GLN A 574     4411   4738   4866    -42     85    106       C  
ATOM   4405  CG  GLN A 574     140.354  87.176 -20.338  1.00 44.44           C  
ANISOU 4405  CG  GLN A 574     5359   5707   5818    -55     96    100       C  
ATOM   4406  CD  GLN A 574     140.678  86.448 -21.647  1.00 53.13           C  
ANISOU 4406  CD  GLN A 574     6451   6820   6916    -57    106     85       C  
ATOM   4407  OE1 GLN A 574     140.043  86.669 -22.719  1.00 59.90           O  
ANISOU 4407  OE1 GLN A 574     7320   7681   7758    -60    108     83       O  
ATOM   4408  NE2 GLN A 574     141.680  85.559 -21.578  1.00 59.30           N  
ANISOU 4408  NE2 GLN A 574     7211   7608   7712    -56    112     74       N  
ATOM   4409  N   THR A 575     140.608  84.434 -18.534  1.00 29.64           N  
ANISOU 4409  N   THR A 575     3447   3821   3995    -27     89     90       N  
ATOM   4410  CA  THR A 575     141.628  84.300 -17.536  1.00 30.41           C  
ANISOU 4410  CA  THR A 575     3531   3919   4104    -27     87     92       C  
ATOM   4411  C   THR A 575     142.955  84.634 -18.212  1.00 30.75           C  
ANISOU 4411  C   THR A 575     3565   3976   4141    -39     98     84       C  
ATOM   4412  O   THR A 575     143.022  84.574 -19.435  1.00 30.63           O  
ANISOU 4412  O   THR A 575     3551   3971   4118    -44    106     75       O  
ATOM   4413  CB  THR A 575     141.727  82.872 -16.994  1.00 30.53           C  
ANISOU 4413  CB  THR A 575     3530   3928   4143    -13     84     86       C  
ATOM   4414  OG1 THR A 575     142.198  82.014 -18.020  1.00 30.49           O  
ANISOU 4414  OG1 THR A 575     3512   3931   4143    -11     93     70       O  
ATOM   4415  CG2 THR A 575     140.409  82.350 -16.482  1.00 31.18           C  
ANISOU 4415  CG2 THR A 575     3620   3997   4231     -2     76     91       C  
ATOM   4416  N   ASN A 576     143.998  84.939 -17.432  1.00 29.87           N  
ANISOU 4416  N   ASN A 576     3445   3870   4036    -43     97     88       N  
ATOM   4417  CA  ASN A 576     145.362  85.090 -17.985  1.00 30.05           C  
ANISOU 4417  CA  ASN A 576     3454   3908   4055    -54    108     77       C  
ATOM   4418  C   ASN A 576     146.241  83.868 -17.672  1.00 29.62           C  
ANISOU 4418  C   ASN A 576     3374   3857   4022    -44    108     66       C  
ATOM   4419  O   ASN A 576     147.458  83.944 -17.748  1.00 29.44           O  
ANISOU 4419  O   ASN A 576     3337   3847   4002    -50    114     58       O  
ATOM   4420  CB  ASN A 576     146.001  86.401 -17.491  1.00 31.19           C  
ANISOU 4420  CB  ASN A 576     3605   4056   4187    -69    108     87       C  
ATOM   4421  CG  ASN A 576     146.491  86.358 -16.029  1.00 32.40           C  
ANISOU 4421  CG  ASN A 576     3751   4207   4355    -65    100     94       C  
ATOM   4422  OD1 ASN A 576     146.163  85.459 -15.214  1.00 32.90           O  
ANISOU 4422  OD1 ASN A 576     3806   4260   4434    -50     91     96       O  
ATOM   4423  ND2 ASN A 576     147.284  87.337 -15.688  1.00 31.77           N  
ANISOU 4423  ND2 ASN A 576     3672   4134   4267    -78    102     98       N  
ATOM   4424  N   PHE A 577     145.620  82.746 -17.314  1.00 29.11           N  
ANISOU 4424  N   PHE A 577     3305   3781   3974    -27    102     65       N  
ATOM   4425  CA  PHE A 577     146.338  81.515 -17.009  1.00 30.60           C  
ANISOU 4425  CA  PHE A 577     3472   3970   4185    -15    101     55       C  
ATOM   4426  C   PHE A 577     145.605  80.341 -17.672  1.00 31.49           C  
ANISOU 4426  C   PHE A 577     3582   4076   4307     -3    102     44       C  
ATOM   4427  O   PHE A 577     144.367  80.407 -17.884  1.00 29.42           O  
ANISOU 4427  O   PHE A 577     3336   3805   4038     -2    100     50       O  
ATOM   4428  CB  PHE A 577     146.462  81.293 -15.480  1.00 31.03           C  
ANISOU 4428  CB  PHE A 577     3522   4014   4253     -6     88     67       C  
ATOM   4429  CG  PHE A 577     145.119  81.265 -14.733  1.00 29.37           C  
ANISOU 4429  CG  PHE A 577     3328   3788   4043      0     78     80       C  
ATOM   4430  CD1 PHE A 577     144.426  80.095 -14.571  1.00 30.20           C  
ANISOU 4430  CD1 PHE A 577     3432   3881   4163     14     74     78       C  
ATOM   4431  CD2 PHE A 577     144.576  82.440 -14.207  1.00 28.87           C  
ANISOU 4431  CD2 PHE A 577     3282   3721   3965     -8     74     94       C  
ATOM   4432  CE1 PHE A 577     143.186  80.070 -13.902  1.00 31.22           C  
ANISOU 4432  CE1 PHE A 577     3575   3996   4291     19     65     90       C  
ATOM   4433  CE2 PHE A 577     143.354  82.437 -13.553  1.00 29.78           C  
ANISOU 4433  CE2 PHE A 577     3411   3823   4080     -3     65    105       C  
ATOM   4434  CZ  PHE A 577     142.654  81.267 -13.374  1.00 28.89           C  
ANISOU 4434  CZ  PHE A 577     3296   3699   3981     10     61    103       C  
ATOM   4435  N   ASP A 578     146.359  79.275 -17.965  1.00 31.94           N  
ANISOU 4435  N   ASP A 578     3619   4136   4380      5    106     29       N  
ATOM   4436  CA  ASP A 578     145.820  78.042 -18.504  1.00 33.01           C  
ANISOU 4436  CA  ASP A 578     3749   4264   4528     17    108     18       C  
ATOM   4437  C   ASP A 578     145.323  77.193 -17.360  1.00 33.95           C  
ANISOU 4437  C   ASP A 578     3868   4364   4666     32     96     27       C  
ATOM   4438  O   ASP A 578     145.850  77.251 -16.228  1.00 34.12           O  
ANISOU 4438  O   ASP A 578     3885   4383   4696     36     87     36       O  
ATOM   4439  CB  ASP A 578     146.889  77.225 -19.290  1.00 36.58           C  
ANISOU 4439  CB  ASP A 578     4180   4727   4992     20    117     -3       C  
ATOM   4440  CG  ASP A 578     147.416  77.965 -20.535  1.00 40.66           C  
ANISOU 4440  CG  ASP A 578     4695   5264   5490      3    131    -15       C  
ATOM   4441  OD1 ASP A 578     146.652  78.690 -21.213  1.00 41.44           O  
ANISOU 4441  OD1 ASP A 578     4812   5365   5569     -7    135    -10       O  
ATOM   4442  OD2 ASP A 578     148.624  77.847 -20.814  1.00 49.37           O  
ANISOU 4442  OD2 ASP A 578     5780   6380   6598      0    138    -27       O  
ATOM   4443  N   PHE A 579     144.331  76.359 -17.661  1.00 33.53           N  
ANISOU 4443  N   PHE A 579     3820   4300   4619     40     95     23       N  
ATOM   4444  CA  PHE A 579     143.814  75.417 -16.689  1.00 34.39           C  
ANISOU 4444  CA  PHE A 579     3930   4392   4746     53     85     30       C  
ATOM   4445  C   PHE A 579     143.276  74.180 -17.390  1.00 33.81           C  
ANISOU 4445  C   PHE A 579     3852   4310   4684     62     89     16       C  
ATOM   4446  O   PHE A 579     142.885  74.229 -18.519  1.00 32.66           O  
ANISOU 4446  O   PHE A 579     3709   4171   4528     57     97      5       O  
ATOM   4447  CB  PHE A 579     142.729  76.074 -15.776  1.00 32.72           C  
ANISOU 4447  CB  PHE A 579     3737   4171   4525     50     75     49       C  
ATOM   4448  CG  PHE A 579     141.584  76.672 -16.519  1.00 32.71           C  
ANISOU 4448  CG  PHE A 579     3753   4171   4506     43     79     49       C  
ATOM   4449  CD1 PHE A 579     141.659  77.972 -17.003  1.00 32.76           C  
ANISOU 4449  CD1 PHE A 579     3768   4189   4491     30     83     53       C  
ATOM   4450  CD2 PHE A 579     140.401  75.965 -16.682  1.00 34.00           C  
ANISOU 4450  CD2 PHE A 579     3922   4323   4673     49     77     47       C  
ATOM   4451  CE1 PHE A 579     140.601  78.548 -17.697  1.00 31.63           C  
ANISOU 4451  CE1 PHE A 579     3639   4047   4330     24     85     54       C  
ATOM   4452  CE2 PHE A 579     139.305  76.524 -17.349  1.00 32.39           C  
ANISOU 4452  CE2 PHE A 579     3732   4122   4452     43     79     47       C  
ATOM   4453  CZ  PHE A 579     139.423  77.820 -17.877  1.00 33.00           C  
ANISOU 4453  CZ  PHE A 579     3819   4212   4509     31     83     50       C  
ATOM   4454  N   THR A 580     143.285  73.068 -16.688  1.00 36.00           N  
ANISOU 4454  N   THR A 580     4124   4573   4983     75     82     16       N  
ATOM   4455  CA  THR A 580     142.844  71.798 -17.240  1.00 39.00           C  
ANISOU 4455  CA  THR A 580     4499   4942   5377     85     85      3       C  
ATOM   4456  C   THR A 580     141.363  71.630 -16.999  1.00 39.96           C  
ANISOU 4456  C   THR A 580     4638   5052   5495     84     81     10       C  
ATOM   4457  O   THR A 580     140.861  72.111 -16.019  1.00 46.06           O  
ANISOU 4457  O   THR A 580     5422   5818   6263     83     72     27       O  
ATOM   4458  CB  THR A 580     143.377  70.614 -16.426  1.00 42.57           C  
ANISOU 4458  CB  THR A 580     4940   5379   5855    100     78      3       C  
ATOM   4459  OG1 THR A 580     142.740  70.658 -15.127  1.00 50.42           O  
ANISOU 4459  OG1 THR A 580     5947   6360   6852    102     66     23       O  
ATOM   4460  CG2 THR A 580     144.857  70.619 -16.287  1.00 41.14           C  
ANISOU 4460  CG2 THR A 580     4741   5208   5683    104     78     -3       C  
ATOM   4461  N   THR A 581     140.700  70.881 -17.841  1.00 39.30           N  
ANISOU 4461  N   THR A 581     4555   4964   5414     87     87     -3       N  
ATOM   4462  CA  THR A 581     139.324  70.558 -17.690  1.00 46.05           C  
ANISOU 4462  CA  THR A 581     5423   5807   6267     87     84      1       C  
ATOM   4463  C   THR A 581     139.203  69.043 -17.607  1.00 41.92           C  
ANISOU 4463  C   THR A 581     4894   5267   5767     98     83     -8       C  
ATOM   4464  O   THR A 581     139.388  68.354 -18.567  1.00 40.95           O  
ANISOU 4464  O   THR A 581     4762   5146   5651    101     92    -27       O  
ATOM   4465  CB  THR A 581     138.499  71.203 -18.820  1.00 52.37           C  
ANISOU 4465  CB  THR A 581     6232   6620   7047     77     91     -6       C  
ATOM   4466  OG1 THR A 581     138.132  72.529 -18.378  1.00 61.63           O  
ANISOU 4466  OG1 THR A 581     7418   7799   8200     68     86     10       O  
ATOM   4467  CG2 THR A 581     137.215  70.437 -19.141  1.00 53.13           C  
ANISOU 4467  CG2 THR A 581     6335   6706   7145     79     92    -13       C  
ATOM   4468  N   PRO A 582     138.898  68.519 -16.426  1.00 43.02           N  
ANISOU 4468  N   PRO A 582     5037   5389   5918    104     74      4       N  
ATOM   4469  CA  PRO A 582     138.892  67.046 -16.343  1.00 40.50           C  
ANISOU 4469  CA  PRO A 582     4713   5052   5622    115     73     -4       C  
ATOM   4470  C   PRO A 582     137.707  66.395 -17.077  1.00 40.01           C  
ANISOU 4470  C   PRO A 582     4658   4984   5560    113     79    -16       C  
ATOM   4471  O   PRO A 582     136.699  67.027 -17.329  1.00 35.67           O  
ANISOU 4471  O   PRO A 582     4120   4441   4993    104     81    -13       O  
ATOM   4472  CB  PRO A 582     138.905  66.775 -14.840  1.00 39.64           C  
ANISOU 4472  CB  PRO A 582     4609   4927   5524    121     61     15       C  
ATOM   4473  CG  PRO A 582     138.422  68.010 -14.193  1.00 42.75           C  
ANISOU 4473  CG  PRO A 582     5016   5329   5899    111     56     32       C  
ATOM   4474  CD  PRO A 582     138.518  69.166 -15.156  1.00 42.51           C  
ANISOU 4474  CD  PRO A 582     4985   5320   5848    101     63     26       C  
ATOM   4475  N   LYS A 583     137.898  65.162 -17.485  1.00 42.36           N  
ANISOU 4475  N   LYS A 583     4948   5271   5877    121     83    -31       N  
ATOM   4476  CA  LYS A 583     136.884  64.379 -18.175  1.00 48.46           C  
ANISOU 4476  CA  LYS A 583     5725   6036   6652    119     89    -45       C  
ATOM   4477  C   LYS A 583     135.752  63.928 -17.226  1.00 44.39           C  
ANISOU 4477  C   LYS A 583     5223   5503   6140    118     82    -32       C  
ATOM   4478  O   LYS A 583     134.646  63.747 -17.667  1.00 49.08           O  
ANISOU 4478  O   LYS A 583     5824   6096   6727    112     86    -39       O  
ATOM   4479  CB  LYS A 583     137.536  63.161 -18.876  1.00 56.82           C  
ANISOU 4479  CB  LYS A 583     6770   7087   7731    129     96    -65       C  
ATOM   4480  CG  LYS A 583     138.392  63.520 -20.101  1.00 66.36           C  
ANISOU 4480  CG  LYS A 583     7964   8317   8933    127    107    -83       C  
ATOM   4481  CD  LYS A 583     139.117  62.312 -20.726  1.00 75.31           C  
ANISOU 4481  CD  LYS A 583     9083   9443  10089    137    113   -105       C  
ATOM   4482  CE  LYS A 583     139.928  62.709 -21.968  1.00 80.75           C  
ANISOU 4482  CE  LYS A 583     9757  10154  10769    133    125   -124       C  
ATOM   4483  NZ  LYS A 583     140.538  61.541 -22.674  1.00 85.07           N  
ANISOU 4483  NZ  LYS A 583    10290  10696  11338    143    133   -149       N  
ATOM   4484  N   SER A 584     136.026  63.811 -15.937  1.00 39.92           N  
ANISOU 4484  N   SER A 584     4661   4924   5583    123     72    -14       N  
ATOM   4485  CA  SER A 584     135.010  63.527 -14.951  1.00 41.20           C  
ANISOU 4485  CA  SER A 584     4837   5071   5746    120     65     -1       C  
ATOM   4486  C   SER A 584     135.162  64.502 -13.797  1.00 39.90           C  
ANISOU 4486  C   SER A 584     4679   4910   5571    116     55     21       C  
ATOM   4487  O   SER A 584     136.267  64.927 -13.551  1.00 38.89           O  
ANISOU 4487  O   SER A 584     4542   4789   5444    121     52     27       O  
ATOM   4488  CB  SER A 584     135.158  62.098 -14.428  1.00 43.25           C  
ANISOU 4488  CB  SER A 584     5097   5306   6030    129     62     -1       C  
ATOM   4489  OG  SER A 584     136.157  62.094 -13.417  1.00 47.44           O  
ANISOU 4489  OG  SER A 584     5624   5829   6570    137     52     14       O  
ATOM   4490  N   LEU A 585     134.068  64.864 -13.109  1.00 37.93           N  
ANISOU 4490  N   LEU A 585     4443   4659   5311    108     51     33       N  
ATOM   4491  CA  LEU A 585     134.167  65.716 -11.898  1.00 39.41           C  
ANISOU 4491  CA  LEU A 585     4636   4848   5489    105     42     54       C  
ATOM   4492  C   LEU A 585     134.261  64.891 -10.598  1.00 39.30           C  
ANISOU 4492  C   LEU A 585     4628   4814   5490    109     33     69       C  
ATOM   4493  O   LEU A 585     133.403  63.984 -10.317  1.00 36.51           O  
ANISOU 4493  O   LEU A 585     4284   4446   5145    108     33     68       O  
ATOM   4494  CB  LEU A 585     133.014  66.720 -11.801  1.00 41.34           C  
ANISOU 4494  CB  LEU A 585     4892   5103   5713     94     42     59       C  
ATOM   4495  CG  LEU A 585     132.836  67.650 -13.024  1.00 42.05           C  
ANISOU 4495  CG  LEU A 585     4979   5213   5785     89     50     48       C  
ATOM   4496  CD1 LEU A 585     131.766  68.685 -12.769  1.00 43.60           C  
ANISOU 4496  CD1 LEU A 585     5187   5418   5963     80     48     55       C  
ATOM   4497  CD2 LEU A 585     134.114  68.331 -13.500  1.00 41.18           C  
ANISOU 4497  CD2 LEU A 585     4859   5115   5671     91     52     46       C  
ATOM   4498  N   GLU A 586     135.305  65.193  -9.824  1.00 36.43           N  
ANISOU 4498  N   GLU A 586     4260   4452   5130    114     25     81       N  
ATOM   4499  CA  GLU A 586     135.542  64.568  -8.530  1.00 37.70           C  
ANISOU 4499  CA  GLU A 586     4426   4596   5302    119     14     97       C  
ATOM   4500  C   GLU A 586     135.415  65.629  -7.433  1.00 34.60           C  
ANISOU 4500  C   GLU A 586     4040   4211   4894    111      6    116       C  
ATOM   4501  O   GLU A 586     135.708  66.786  -7.672  1.00 33.41           O  
ANISOU 4501  O   GLU A 586     3886   4078   4729    107      8    116       O  
ATOM   4502  CB  GLU A 586     136.967  63.985  -8.466  1.00 42.66           C  
ANISOU 4502  CB  GLU A 586     5041   5219   5949    133      9     96       C  
ATOM   4503  CG  GLU A 586     137.367  63.075  -9.620  1.00 48.55           C  
ANISOU 4503  CG  GLU A 586     5776   5959   6710    142     17     75       C  
ATOM   4504  CD  GLU A 586     136.572  61.787  -9.650  1.00 53.69           C  
ANISOU 4504  CD  GLU A 586     6436   6589   7376    144     19     71       C  
ATOM   4505  OE1 GLU A 586     136.038  61.378  -8.600  1.00 57.28           O  
ANISOU 4505  OE1 GLU A 586     6903   7029   7833    141     11     86       O  
ATOM   4506  OE2 GLU A 586     136.461  61.184 -10.739  1.00 63.76           O  
ANISOU 4506  OE2 GLU A 586     7705   7862   8658    146     28     51       O  
ATOM   4507  N   PRO A 587     135.047  65.222  -6.208  1.00 35.70           N  
ANISOU 4507  N   PRO A 587     4190   4338   5037    109     -2    132       N  
ATOM   4508  CA  PRO A 587     135.032  66.148  -5.061  1.00 33.92           C  
ANISOU 4508  CA  PRO A 587     3971   4120   4798    102    -10    150       C  
ATOM   4509  C   PRO A 587     136.423  66.674  -4.742  1.00 32.45           C  
ANISOU 4509  C   PRO A 587     3774   3943   4614    108    -17    156       C  
ATOM   4510  O   PRO A 587     137.407  65.952  -4.894  1.00 28.96           O  
ANISOU 4510  O   PRO A 587     3322   3494   4187    120    -20    153       O  
ATOM   4511  CB  PRO A 587     134.528  65.301  -3.894  1.00 34.42           C  
ANISOU 4511  CB  PRO A 587     4045   4164   4867    100    -18    164       C  
ATOM   4512  CG  PRO A 587     133.934  64.090  -4.528  1.00 36.94           C  
ANISOU 4512  CG  PRO A 587     4368   4468   5200    102    -12    152       C  
ATOM   4513  CD  PRO A 587     134.614  63.858  -5.828  1.00 35.64           C  
ANISOU 4513  CD  PRO A 587     4190   4307   5045    112     -5    134       C  
ATOM   4514  N   LEU A 588     136.483  67.931  -4.334  1.00 29.19           N  
ANISOU 4514  N   LEU A 588     3362   3545   4183    101    -19    164       N  
ATOM   4515  CA  LEU A 588     137.750  68.563  -4.008  1.00 31.43           C  
ANISOU 4515  CA  LEU A 588     3636   3839   4466    104    -24    169       C  
ATOM   4516  C   LEU A 588     138.424  67.937  -2.770  1.00 32.10           C  
ANISOU 4516  C   LEU A 588     3720   3914   4562    111    -37    185       C  
ATOM   4517  O   LEU A 588     139.633  67.835  -2.720  1.00 32.85           O  
ANISOU 4517  O   LEU A 588     3803   4012   4666    120    -42    185       O  
ATOM   4518  CB  LEU A 588     137.553  70.088  -3.834  1.00 30.42           C  
ANISOU 4518  CB  LEU A 588     3512   3730   4318     93    -22    174       C  
ATOM   4519  CG  LEU A 588     138.796  70.897  -3.516  1.00 31.11           C  
ANISOU 4519  CG  LEU A 588     3590   3831   4402     94    -27    179       C  
ATOM   4520  CD1 LEU A 588     139.787  70.777  -4.657  1.00 31.97           C  
ANISOU 4520  CD1 LEU A 588     3683   3947   4518    101    -20    164       C  
ATOM   4521  CD2 LEU A 588     138.454  72.365  -3.232  1.00 30.39           C  
ANISOU 4521  CD2 LEU A 588     3504   3753   4289     81    -25    184       C  
ATOM   4522  N   GLY A 589     137.630  67.550  -1.769  1.00 32.90           N  
ANISOU 4522  N   GLY A 589     3836   4004   4662    106    -43    198       N  
ATOM   4523  CA  GLY A 589     138.139  66.886  -0.581  1.00 31.81           C  
ANISOU 4523  CA  GLY A 589     3700   3854   4533    111    -56    214       C  
ATOM   4524  C   GLY A 589     137.080  66.026   0.058  1.00 32.59           C  
ANISOU 4524  C   GLY A 589     3815   3935   4634    106    -58    222       C  
ATOM   4525  O   GLY A 589     135.981  65.858  -0.489  1.00 31.69           O  
ANISOU 4525  O   GLY A 589     3707   3817   4517     99    -49    213       O  
ATOM   4526  N   SER A 590     137.404  65.494   1.233  1.00 32.37           N  
ANISOU 4526  N   SER A 590     3791   3896   4610    108    -71    239       N  
ATOM   4527  CA  SER A 590     136.542  64.508   1.903  1.00 34.66           C  
ANISOU 4527  CA  SER A 590     4097   4166   4905    104    -74    249       C  
ATOM   4528  C   SER A 590     135.716  65.034   3.105  1.00 35.08           C  
ANISOU 4528  C   SER A 590     4165   4224   4941     88    -77    264       C  
ATOM   4529  O   SER A 590     134.802  64.355   3.519  1.00 36.01           O  
ANISOU 4529  O   SER A 590     4296   4328   5059     81    -77    269       O  
ATOM   4530  CB  SER A 590     137.407  63.314   2.357  1.00 34.23           C  
ANISOU 4530  CB  SER A 590     4043   4094   4871    118    -85    258       C  
ATOM   4531  OG  SER A 590     138.338  63.816   3.282  1.00 35.41           O  
ANISOU 4531  OG  SER A 590     4186   4252   5015    121    -98    272       O  
ATOM   4532  N   ASP A 591     136.057  66.203   3.660  1.00 34.77           N  
ANISOU 4532  N   ASP A 591     4122   4203   4887     82    -81    271       N  
ATOM   4533  CA  ASP A 591     135.491  66.680   4.936  1.00 36.69           C  
ANISOU 4533  CA  ASP A 591     4376   4450   5114     68    -86    286       C  
ATOM   4534  C   ASP A 591     135.325  68.223   5.047  1.00 32.39           C  
ANISOU 4534  C   ASP A 591     3829   3928   4550     58    -82    284       C  
ATOM   4535  O   ASP A 591     135.915  68.960   4.270  1.00 30.04           O  
ANISOU 4535  O   ASP A 591     3520   3642   4251     63    -78    274       O  
ATOM   4536  CB  ASP A 591     136.427  66.276   6.064  1.00 41.76           C  
ANISOU 4536  CB  ASP A 591     5020   5087   5761     74   -102    304       C  
ATOM   4537  CG  ASP A 591     136.303  64.830   6.413  1.00 48.01           C  
ANISOU 4537  CG  ASP A 591     5820   5854   6566     79   -108    313       C  
ATOM   4538  OD1 ASP A 591     135.298  64.549   7.088  1.00 53.50           O  
ANISOU 4538  OD1 ASP A 591     6531   6542   7253     66   -107    321       O  
ATOM   4539  OD2 ASP A 591     137.200  64.004   6.055  1.00 49.96           O  
ANISOU 4539  OD2 ASP A 591     6061   6091   6832     96   -113    312       O  
ATOM   4540  N   ASN A 592     134.565  68.652   6.061  1.00 29.19           N  
ANISOU 4540  N   ASN A 592     3434   3526   4129     44    -84    293       N  
ATOM   4541  CA  ASN A 592     134.508  70.039   6.494  1.00 30.32           C  
ANISOU 4541  CA  ASN A 592     3577   3689   4255     34    -83    295       C  
ATOM   4542  C   ASN A 592     134.037  70.996   5.358  1.00 28.70           C  
ANISOU 4542  C   ASN A 592     3366   3495   4043     32    -71    277       C  
ATOM   4543  O   ASN A 592     134.501  72.138   5.250  1.00 29.31           O  
ANISOU 4543  O   ASN A 592     3438   3587   4112     31    -71    275       O  
ATOM   4544  CB  ASN A 592     135.896  70.457   7.049  1.00 30.64           C  
ANISOU 4544  CB  ASN A 592     3608   3738   4296     40    -94    304       C  
ATOM   4545  CG  ASN A 592     136.385  69.513   8.129  1.00 32.42           C  
ANISOU 4545  CG  ASN A 592     3838   3952   4528     43   -107    322       C  
ATOM   4546  OD1 ASN A 592     135.584  69.037   8.915  1.00 32.58           O  
ANISOU 4546  OD1 ASN A 592     3871   3964   4543     34   -109    331       O  
ATOM   4547  ND2 ASN A 592     137.691  69.197   8.139  1.00 30.63           N  
ANISOU 4547  ND2 ASN A 592     3600   3725   4312     57   -116    326       N  
ATOM   4548  N   GLY A 593     133.173  70.456   4.503  1.00 27.56           N  
ANISOU 4548  N   GLY A 593     3225   3343   3904     33    -63    266       N  
ATOM   4549  CA  GLY A 593     132.607  71.131   3.343  1.00 28.03           C  
ANISOU 4549  CA  GLY A 593     3281   3410   3958     32    -52    249       C  
ATOM   4550  C   GLY A 593     133.224  70.842   1.995  1.00 27.57           C  
ANISOU 4550  C   GLY A 593     3213   3351   3911     44    -47    236       C  
ATOM   4551  O   GLY A 593     132.554  70.991   0.974  1.00 26.10           O  
ANISOU 4551  O   GLY A 593     3027   3168   3723     44    -38    223       O  
ATOM   4552  N   TYR A 594     134.495  70.411   1.970  1.00 26.68           N  
ANISOU 4552  N   TYR A 594     3092   3236   3811     55    -53    240       N  
ATOM   4553  CA  TYR A 594     135.162  70.126   0.704  1.00 27.06           C  
ANISOU 4553  CA  TYR A 594     3128   3284   3870     66    -47    227       C  
ATOM   4554  C   TYR A 594     134.465  68.974  -0.057  1.00 27.10           C  
ANISOU 4554  C   TYR A 594     3136   3274   3886     69    -41    216       C  
ATOM   4555  O   TYR A 594     134.595  68.846  -1.290  1.00 27.40           O  
ANISOU 4555  O   TYR A 594     3167   3315   3930     75    -33    201       O  
ATOM   4556  CB  TYR A 594     136.653  69.735   0.936  1.00 27.18           C  
ANISOU 4556  CB  TYR A 594     3132   3297   3897     77    -55    232       C  
ATOM   4557  CG  TYR A 594     137.567  70.850   1.337  1.00 27.10           C  
ANISOU 4557  CG  TYR A 594     3115   3304   3878     75    -60    238       C  
ATOM   4558  CD1 TYR A 594     137.548  71.374   2.643  1.00 28.92           C  
ANISOU 4558  CD1 TYR A 594     3352   3539   4098     67    -68    253       C  
ATOM   4559  CD2 TYR A 594     138.402  71.442   0.420  1.00 27.36           C  
ANISOU 4559  CD2 TYR A 594     3136   3350   3911     79    -54    227       C  
ATOM   4560  CE1 TYR A 594     138.365  72.439   3.002  1.00 28.33           C  
ANISOU 4560  CE1 TYR A 594     3270   3480   4014     64    -71    257       C  
ATOM   4561  CE2 TYR A 594     139.233  72.511   0.782  1.00 28.36           C  
ANISOU 4561  CE2 TYR A 594     3255   3491   4028     75    -57    231       C  
ATOM   4562  CZ  TYR A 594     139.227  72.982   2.077  1.00 28.65           C  
ANISOU 4562  CZ  TYR A 594     3298   3532   4056     68    -66    246       C  
ATOM   4563  OH  TYR A 594     140.086  74.018   2.454  1.00 29.78           O  
ANISOU 4563  OH  TYR A 594     3434   3690   4190     64    -69    249       O  
ATOM   4564  N   GLN A 595     133.769  68.114   0.674  1.00 27.25           N  
ANISOU 4564  N   GLN A 595     3166   3279   3909     66    -44    224       N  
ATOM   4565  CA  GLN A 595     132.958  67.047   0.029  1.00 29.02           C  
ANISOU 4565  CA  GLN A 595     3395   3490   4143     67    -38    214       C  
ATOM   4566  C   GLN A 595     131.756  67.549  -0.784  1.00 28.80           C  
ANISOU 4566  C   GLN A 595     3369   3469   4103     58    -27    200       C  
ATOM   4567  O   GLN A 595     131.186  66.795  -1.585  1.00 29.01           O  
ANISOU 4567  O   GLN A 595     3396   3488   4138     60    -20    187       O  
ATOM   4568  CB  GLN A 595     132.535  65.986   1.055  1.00 28.89           C  
ANISOU 4568  CB  GLN A 595     3389   3454   4132     63    -44    226       C  
ATOM   4569  CG  GLN A 595     131.373  66.346   1.968  1.00 30.40           C  
ANISOU 4569  CG  GLN A 595     3594   3648   4309     47    -44    234       C  
ATOM   4570  CD  GLN A 595     131.779  67.148   3.207  1.00 31.63           C  
ANISOU 4570  CD  GLN A 595     3752   3814   4453     41    -53    250       C  
ATOM   4571  OE1 GLN A 595     132.811  67.870   3.241  1.00 30.48           O  
ANISOU 4571  OE1 GLN A 595     3597   3679   4305     47    -57    254       O  
ATOM   4572  NE2 GLN A 595     130.961  67.040   4.232  1.00 31.76           N  
ANISOU 4572  NE2 GLN A 595     3780   3827   4461     29    -55    260       N  
ATOM   4573  N   HIS A 596     131.391  68.821  -0.607  1.00 27.32           N  
ANISOU 4573  N   HIS A 596     3183   3298   3899     51    -26    201       N  
ATOM   4574  CA  HIS A 596     130.341  69.446  -1.417  1.00 26.37           C  
ANISOU 4574  CA  HIS A 596     3065   3188   3768     45    -17    187       C  
ATOM   4575  C   HIS A 596     130.821  70.237  -2.662  1.00 26.67           C  
ANISOU 4575  C   HIS A 596     3092   3238   3801     50    -11    175       C  
ATOM   4576  O   HIS A 596     129.980  70.806  -3.363  1.00 25.87           O  
ANISOU 4576  O   HIS A 596     2994   3146   3691     46     -5    165       O  
ATOM   4577  CB  HIS A 596     129.490  70.352  -0.494  1.00 26.70           C  
ANISOU 4577  CB  HIS A 596     3114   3237   3793     33    -19    194       C  
ATOM   4578  CG  HIS A 596     128.773  69.597   0.600  1.00 25.58           C  
ANISOU 4578  CG  HIS A 596     2983   3085   3653     25    -22    203       C  
ATOM   4579  ND1 HIS A 596     127.931  68.538   0.338  1.00 26.03           N  
ANISOU 4579  ND1 HIS A 596     3044   3130   3717     22    -17    196       N  
ATOM   4580  CD2 HIS A 596     128.812  69.716   1.940  1.00 26.69           C  
ANISOU 4580  CD2 HIS A 596     3129   3224   3788     17    -29    218       C  
ATOM   4581  CE1 HIS A 596     127.463  68.050   1.467  1.00 27.40           C  
ANISOU 4581  CE1 HIS A 596     3227   3295   3889     13    -21    207       C  
ATOM   4582  NE2 HIS A 596     127.963  68.765   2.463  1.00 27.49           N  
ANISOU 4582  NE2 HIS A 596     3239   3313   3892     10    -28    221       N  
ATOM   4583  N   LEU A 597     132.138  70.296  -2.909  1.00 25.41           N  
ANISOU 4583  N   LEU A 597     2924   3082   3649     59    -14    177       N  
ATOM   4584  CA  LEU A 597     132.724  71.015  -4.077  1.00 25.87           C  
ANISOU 4584  CA  LEU A 597     2974   3153   3703     62     -8    166       C  
ATOM   4585  C   LEU A 597     133.235  70.061  -5.140  1.00 27.47           C  
ANISOU 4585  C   LEU A 597     3168   3349   3920     72     -3    153       C  
ATOM   4586  O   LEU A 597     134.049  69.180  -4.832  1.00 27.30           O  
ANISOU 4586  O   LEU A 597     3141   3318   3914     80     -7    157       O  
ATOM   4587  CB  LEU A 597     133.887  71.904  -3.649  1.00 26.10           C  
ANISOU 4587  CB  LEU A 597     2997   3192   3728     63    -13    175       C  
ATOM   4588  CG  LEU A 597     133.566  73.086  -2.732  1.00 26.49           C  
ANISOU 4588  CG  LEU A 597     3054   3250   3762     54    -17    185       C  
ATOM   4589  CD1 LEU A 597     134.839  73.809  -2.359  1.00 26.98           C  
ANISOU 4589  CD1 LEU A 597     3109   3321   3822     55    -21    192       C  
ATOM   4590  CD2 LEU A 597     132.625  74.035  -3.425  1.00 26.43           C  
ANISOU 4590  CD2 LEU A 597     3051   3251   3739     48    -10    177       C  
ATOM   4591  N   TRP A 598     132.741  70.218  -6.382  1.00 27.31           N  
ANISOU 4591  N   TRP A 598     3146   3335   3895     71      6    138       N  
ATOM   4592  CA  TRP A 598     133.319  69.520  -7.528  1.00 27.27           C  
ANISOU 4592  CA  TRP A 598     3131   3329   3901     79     12    124       C  
ATOM   4593  C   TRP A 598     134.551  70.319  -7.995  1.00 27.47           C  
ANISOU 4593  C   TRP A 598     3147   3368   3924     82     13    122       C  
ATOM   4594  O   TRP A 598     134.485  71.550  -8.110  1.00 25.36           O  
ANISOU 4594  O   TRP A 598     2881   3114   3640     76     14    125       O  
ATOM   4595  CB  TRP A 598     132.326  69.482  -8.687  1.00 27.40           C  
ANISOU 4595  CB  TRP A 598     3149   3349   3911     76     21    108       C  
ATOM   4596  CG  TRP A 598     131.055  68.725  -8.515  1.00 28.60           C  
ANISOU 4596  CG  TRP A 598     3309   3491   4066     72     23    105       C  
ATOM   4597  CD1 TRP A 598     129.739  69.214  -8.610  1.00 28.42           C  
ANISOU 4597  CD1 TRP A 598     3295   3474   4031     64     25    102       C  
ATOM   4598  CD2 TRP A 598     130.953  67.334  -8.269  1.00 28.23           C  
ANISOU 4598  CD2 TRP A 598     3263   3426   4037     76     22    103       C  
ATOM   4599  NE1 TRP A 598     128.854  68.151  -8.475  1.00 31.72           N  
ANISOU 4599  NE1 TRP A 598     3717   3879   4456     62     27     97       N  
ATOM   4600  CE2 TRP A 598     129.573  67.005  -8.235  1.00 30.55           C  
ANISOU 4600  CE2 TRP A 598     3565   3715   4326     68     25     99       C  
ATOM   4601  CE3 TRP A 598     131.886  66.349  -8.070  1.00 29.64           C  
ANISOU 4601  CE3 TRP A 598     3436   3591   4233     85     20    105       C  
ATOM   4602  CZ2 TRP A 598     129.131  65.741  -7.981  1.00 33.41           C  
ANISOU 4602  CZ2 TRP A 598     3932   4061   4702     68     26     96       C  
ATOM   4603  CZ3 TRP A 598     131.447  65.073  -7.859  1.00 33.54           C  
ANISOU 4603  CZ3 TRP A 598     3935   4067   4741     86     20    103       C  
ATOM   4604  CH2 TRP A 598     130.098  64.775  -7.784  1.00 33.79           C  
ANISOU 4604  CH2 TRP A 598     3976   4094   4769     77     23     99       C  
ATOM   4605  N   SER A 599     135.652  69.619  -8.235  1.00 28.90           N  
ANISOU 4605  N   SER A 599     3316   3545   4119     91     13    118       N  
ATOM   4606  CA ASER A 599     136.819  70.194  -8.849  0.50 29.19           C  
ANISOU 4606  CA ASER A 599     3342   3596   4155     93     16    112       C  
ATOM   4607  CA BSER A 599     136.832  70.185  -8.879  0.50 29.75           C  
ANISOU 4607  CA BSER A 599     3412   3666   4225     93     17    112       C  
ATOM   4608  C   SER A 599     136.545  70.310 -10.360  1.00 30.81           C  
ANISOU 4608  C   SER A 599     3543   3809   4353     92     28     94       C  
ATOM   4609  O   SER A 599     136.454  69.283 -11.073  1.00 31.31           O  
ANISOU 4609  O   SER A 599     3602   3866   4429     97     33     81       O  
ATOM   4610  CB ASER A 599     138.017  69.289  -8.558  0.50 29.91           C  
ANISOU 4610  CB ASER A 599     3421   3679   4265    105     12    112       C  
ATOM   4611  CB BSER A 599     138.048  69.267  -8.710  0.50 31.10           C  
ANISOU 4611  CB BSER A 599     3570   3830   4416    105     13    110       C  
ATOM   4612  OG ASER A 599     139.167  69.758  -9.217  0.50 29.24           O  
ANISOU 4612  OG ASER A 599     3322   3608   4179    107     16    104       O  
ATOM   4613  OG BSER A 599     138.658  69.474  -7.470  0.50 31.46           O  
ANISOU 4613  OG BSER A 599     3615   3874   4463    106      2    126       O  
ATOM   4614  N   GLU A 600     136.362  71.548 -10.836  1.00 31.54           N  
ANISOU 4614  N   GLU A 600     3640   3917   4427     83     31     94       N  
ATOM   4615  CA  GLU A 600     135.976  71.800 -12.216  1.00 33.54           C  
ANISOU 4615  CA  GLU A 600     3892   4180   4671     80     41     79       C  
ATOM   4616  C   GLU A 600     137.165  72.235 -13.107  1.00 33.42           C  
ANISOU 4616  C   GLU A 600     3866   4179   4653     80     47     70       C  
ATOM   4617  O   GLU A 600     137.017  72.301 -14.287  1.00 36.17           O  
ANISOU 4617  O   GLU A 600     4212   4535   4994     77     55     57       O  
ATOM   4618  CB  GLU A 600     134.874  72.872 -12.308  1.00 36.11           C  
ANISOU 4618  CB  GLU A 600     4231   4513   4977     71     41     84       C  
ATOM   4619  CG  GLU A 600     133.482  72.384 -12.574  1.00 42.03           C  
ANISOU 4619  CG  GLU A 600     4989   5257   5725     70     42     78       C  
ATOM   4620  CD  GLU A 600     132.497  73.478 -13.083  1.00 44.68           C  
ANISOU 4620  CD  GLU A 600     5334   5603   6040     63     44     77       C  
ATOM   4621  OE1 GLU A 600     132.531  74.640 -12.644  1.00 38.91           O  
ANISOU 4621  OE1 GLU A 600     4609   4878   5297     59     40     87       O  
ATOM   4622  OE2 GLU A 600     131.655  73.145 -13.941  1.00 50.89           O  
ANISOU 4622  OE2 GLU A 600     6122   6391   6823     63     48     65       O  
ATOM   4623  N   GLY A 601     138.342  72.491 -12.559  1.00 33.44           N  
ANISOU 4623  N   GLY A 601     3861   4186   4661     82     44     76       N  
ATOM   4624  CA  GLY A 601     139.489  72.829 -13.388  1.00 31.83           C  
ANISOU 4624  CA  GLY A 601     3645   3996   4455     80     51     67       C  
ATOM   4625  C   GLY A 601     140.592  73.314 -12.517  1.00 32.68           C  
ANISOU 4625  C   GLY A 601     3746   4108   4564     80     45     77       C  
ATOM   4626  O   GLY A 601     140.310  73.892 -11.475  1.00 34.95           O  
ANISOU 4626  O   GLY A 601     4042   4392   4846     77     37     92       O  
ATOM   4627  N   LEU A 602     141.828  73.029 -12.917  1.00 33.24           N  
ANISOU 4627  N   LEU A 602     3801   4186   4644     85     48     67       N  
ATOM   4628  CA  LEU A 602     143.005  73.267 -12.119  1.00 35.51           C  
ANISOU 4628  CA  LEU A 602     4078   4478   4937     87     42     74       C  
ATOM   4629  C   LEU A 602     143.993  74.051 -12.978  1.00 34.37           C  
ANISOU 4629  C   LEU A 602     3924   4353   4783     79     52     63       C  
ATOM   4630  O   LEU A 602     144.340  73.614 -14.062  1.00 35.81           O  
ANISOU 4630  O   LEU A 602     4097   4542   4969     81     61     47       O  
ATOM   4631  CB  LEU A 602     143.621  71.920 -11.677  1.00 38.46           C  
ANISOU 4631  CB  LEU A 602     4439   4840   5335    102     37     70       C  
ATOM   4632  CG  LEU A 602     145.036  72.007 -11.069  1.00 42.75           C  
ANISOU 4632  CG  LEU A 602     4967   5390   5887    107     31     72       C  
ATOM   4633  CD1 LEU A 602     144.962  72.758  -9.750  1.00 42.26           C  
ANISOU 4633  CD1 LEU A 602     4912   5327   5816    102     21     93       C  
ATOM   4634  CD2 LEU A 602     145.702  70.637 -10.887  1.00 44.57           C  
ANISOU 4634  CD2 LEU A 602     5182   5609   6142    124     26     66       C  
ATOM   4635  N   GLY A 603     144.422  75.201 -12.499  1.00 34.32           N  
ANISOU 4635  N   GLY A 603     3920   4357   4764     69     50     73       N  
ATOM   4636  CA  GLY A 603     145.388  76.039 -13.213  1.00 37.17           C  
ANISOU 4636  CA  GLY A 603     4272   4736   5114     60     58     65       C  
ATOM   4637  C   GLY A 603     146.636  76.332 -12.409  1.00 36.65           C  
ANISOU 4637  C   GLY A 603     4194   4679   5053     60     53     69       C  
ATOM   4638  O   GLY A 603     146.682  76.161 -11.192  1.00 34.47           O  
ANISOU 4638  O   GLY A 603     3918   4394   4785     65     42     82       O  
ATOM   4639  N   GLN A 604     147.635  76.805 -13.113  1.00 41.06           N  
ANISOU 4639  N   GLN A 604     4741   5254   5607     52     62     58       N  
ATOM   4640  CA  GLN A 604     148.898  77.214 -12.520  1.00 46.15           C  
ANISOU 4640  CA  GLN A 604     5371   5910   6253     50     59     59       C  
ATOM   4641  C   GLN A 604     149.159  78.640 -13.062  1.00 43.41           C  
ANISOU 4641  C   GLN A 604     5031   5579   5884     30     69     59       C  
ATOM   4642  O   GLN A 604     148.902  78.925 -14.251  1.00 45.25           O  
ANISOU 4642  O   GLN A 604     5269   5819   6106     22     80     49       O  
ATOM   4643  CB  GLN A 604     149.946  76.167 -12.903  1.00 52.90           C  
ANISOU 4643  CB  GLN A 604     6203   6770   7128     62     62     42       C  
ATOM   4644  CG  GLN A 604     151.383  76.622 -13.084  1.00 61.61           C  
ANISOU 4644  CG  GLN A 604     7287   7893   8230     55     67     32       C  
ATOM   4645  CD  GLN A 604     152.301  75.437 -13.406  1.00 71.74           C  
ANISOU 4645  CD  GLN A 604     8545   9178   9535     71     68     14       C  
ATOM   4646  OE1 GLN A 604     151.840  74.311 -13.673  1.00 77.71           O  
ANISOU 4646  OE1 GLN A 604     9301   9921  10306     84     66      8       O  
ATOM   4647  NE2 GLN A 604     153.607  75.689 -13.403  1.00 78.75           N  
ANISOU 4647  NE2 GLN A 604     9413  10083  10425     68     70      5       N  
ATOM   4648  N   PRO A 605     149.598  79.557 -12.207  1.00 40.54           N  
ANISOU 4648  N   PRO A 605     4669   5221   5513     22     64     70       N  
ATOM   4649  CA  PRO A 605     149.873  80.913 -12.698  1.00 43.52           C  
ANISOU 4649  CA  PRO A 605     5054   5612   5869      2     73     70       C  
ATOM   4650  C   PRO A 605     150.935  80.952 -13.790  1.00 45.70           C  
ANISOU 4650  C   PRO A 605     5314   5906   6142     -5     86     51       C  
ATOM   4651  O   PRO A 605     151.869  80.165 -13.735  1.00 42.13           O  
ANISOU 4651  O   PRO A 605     4841   5460   5707      4     85     40       O  
ATOM   4652  CB  PRO A 605     150.391  81.643 -11.470  1.00 41.70           C  
ANISOU 4652  CB  PRO A 605     4823   5385   5636     -3     65     82       C  
ATOM   4653  CG  PRO A 605     149.801  80.916 -10.328  1.00 42.01           C  
ANISOU 4653  CG  PRO A 605     4866   5409   5689     11     51     94       C  
ATOM   4654  CD  PRO A 605     149.603  79.490 -10.741  1.00 43.07           C  
ANISOU 4654  CD  PRO A 605     4991   5534   5841     28     50     85       C  
ATOM   4655  N   LYS A 606     150.748  81.845 -14.769  1.00 49.92           N  
ANISOU 4655  N   LYS A 606     5861   6449   6658    -21     97     48       N  
ATOM   4656  CA  LYS A 606     151.769  82.154 -15.786  1.00 53.43           C  
ANISOU 4656  CA  LYS A 606     6292   6912   7094    -33    111     32       C  
ATOM   4657  C   LYS A 606     152.729  83.263 -15.348  1.00 51.35           C  
ANISOU 4657  C   LYS A 606     6027   6664   6822    -50    113     36       C  
ATOM   4658  O   LYS A 606     153.773  83.424 -15.966  1.00 54.27           O  
ANISOU 4658  O   LYS A 606     6381   7050   7187    -59    123     21       O  
ATOM   4659  CB  LYS A 606     151.135  82.558 -17.122  1.00 58.51           C  
ANISOU 4659  CB  LYS A 606     6951   7559   7721    -44    122     27       C  
ATOM   4660  CG  LYS A 606     150.259  81.482 -17.765  1.00 66.42           C  
ANISOU 4660  CG  LYS A 606     7954   8551   8731    -31    122     20       C  
ATOM   4661  CD  LYS A 606     150.537  81.240 -19.257  1.00 70.87           C  
ANISOU 4661  CD  LYS A 606     8512   9128   9288    -38    137      2       C  
ATOM   4662  CE  LYS A 606     150.281  82.455 -20.146  1.00 73.25           C  
ANISOU 4662  CE  LYS A 606     8832   9438   9562    -58    146      5       C  
ATOM   4663  NZ  LYS A 606     148.961  82.378 -20.837  1.00 76.02           N  
ANISOU 4663  NZ  LYS A 606     9201   9780   9904    -56    145      8       N  
ATOM   4664  N   GLY A 607     152.375  84.036 -14.319  1.00 49.87           N  
ANISOU 4664  N   GLY A 607     5852   6468   6627    -54    104     53       N  
ATOM   4665  CA  GLY A 607     153.213  85.147 -13.840  1.00 46.28           C  
ANISOU 4665  CA  GLY A 607     5396   6025   6162    -70    106     56       C  
ATOM   4666  C   GLY A 607     152.898  85.574 -12.424  1.00 44.18           C  
ANISOU 4666  C   GLY A 607     5139   5750   5898    -68     93     74       C  
ATOM   4667  O   GLY A 607     152.285  84.829 -11.657  1.00 43.92           O  
ANISOU 4667  O   GLY A 607     5107   5703   5878    -51     81     82       O  
ATOM   4668  N   ASP A 608     153.277  86.806 -12.100  1.00 41.13           N  
ANISOU 4668  N   ASP A 608     4759   5370   5497    -85     96     80       N  
ATOM   4669  CA  ASP A 608     153.164  87.344 -10.750  1.00 41.03           C  
ANISOU 4669  CA  ASP A 608     4753   5352   5485    -86     85     94       C  
ATOM   4670  C   ASP A 608     151.742  87.753 -10.345  1.00 37.81           C  
ANISOU 4670  C   ASP A 608     4371   4926   5070    -84     78    110       C  
ATOM   4671  O   ASP A 608     151.466  87.895  -9.158  1.00 34.63           O  
ANISOU 4671  O   ASP A 608     3972   4516   4670    -80     67    121       O  
ATOM   4672  CB  ASP A 608     154.071  88.568 -10.597  1.00 44.86           C  
ANISOU 4672  CB  ASP A 608     5238   5851   5957   -108     91     93       C  
ATOM   4673  CG  ASP A 608     155.572  88.212 -10.624  1.00 49.63           C  
ANISOU 4673  CG  ASP A 608     5813   6475   6569   -110     95     78       C  
ATOM   4674  OD1 ASP A 608     155.982  87.146 -10.108  1.00 51.34           O  
ANISOU 4674  OD1 ASP A 608     6009   6693   6803    -93     87     74       O  
ATOM   4675  OD2 ASP A 608     156.332  89.022 -11.181  1.00 57.27           O  
ANISOU 4675  OD2 ASP A 608     6778   7457   7524   -129    107     70       O  
ATOM   4676  N   ASN A 609     150.883  88.000 -11.324  1.00 35.14           N  
ANISOU 4676  N   ASN A 609     4049   4581   4721    -87     84    110       N  
ATOM   4677  CA  ASN A 609     149.493  88.392 -11.122  1.00 35.98           C  
ANISOU 4677  CA  ASN A 609     4180   4671   4821    -84     78    122       C  
ATOM   4678  C   ASN A 609     148.638  87.434 -11.954  1.00 35.72           C  
ANISOU 4678  C   ASN A 609     4148   4630   4793    -71     79    117       C  
ATOM   4679  O   ASN A 609     148.880  87.274 -13.143  1.00 38.79           O  
ANISOU 4679  O   ASN A 609     4535   5027   5177    -75     89    106       O  
ATOM   4680  CB  ASN A 609     149.241  89.826 -11.622  1.00 35.85           C  
ANISOU 4680  CB  ASN A 609     4184   4655   4783   -102     85    127       C  
ATOM   4681  CG  ASN A 609     149.825  90.931 -10.717  1.00 38.07           C  
ANISOU 4681  CG  ASN A 609     4469   4939   5057   -116     84    134       C  
ATOM   4682  OD1 ASN A 609     149.665  92.091 -11.050  1.00 41.60           O  
ANISOU 4682  OD1 ASN A 609     4934   5386   5488   -131     89    138       O  
ATOM   4683  ND2 ASN A 609     150.491  90.603  -9.589  1.00 38.07           N  
ANISOU 4683  ND2 ASN A 609     4453   4945   5069   -112     76    135       N  
ATOM   4684  N   SER A 610     147.666  86.779 -11.326  1.00 33.23           N  
ANISOU 4684  N   SER A 610     3838   4301   4487    -57     70    124       N  
ATOM   4685  CA  SER A 610     146.713  85.933 -12.012  1.00 30.91           C  
ANISOU 4685  CA  SER A 610     3548   3999   4197    -46     70    120       C  
ATOM   4686  C   SER A 610     145.353  86.682 -12.031  1.00 31.20           C  
ANISOU 4686  C   SER A 610     3609   4024   4221    -48     67    130       C  
ATOM   4687  O   SER A 610     145.029  87.359 -11.058  1.00 29.37           O  
ANISOU 4687  O   SER A 610     3387   3787   3986    -51     60    141       O  
ATOM   4688  CB  SER A 610     146.613  84.619 -11.285  1.00 31.30           C  
ANISOU 4688  CB  SER A 610     3585   4040   4266    -28     61    120       C  
ATOM   4689  OG  SER A 610     147.858  83.914 -11.378  1.00 30.93           O  
ANISOU 4689  OG  SER A 610     3515   4004   4232    -25     64    109       O  
ATOM   4690  N   GLN A 611     144.601  86.546 -13.141  1.00 30.63           N  
ANISOU 4690  N   GLN A 611     3546   3950   4143    -46     72    125       N  
ATOM   4691  CA  GLN A 611     143.384  87.269 -13.406  1.00 31.00           C  
ANISOU 4691  CA  GLN A 611     3615   3989   4176    -48     69    132       C  
ATOM   4692  C   GLN A 611     142.276  86.356 -13.897  1.00 28.80           C  
ANISOU 4692  C   GLN A 611     3337   3702   3902    -36     67    128       C  
ATOM   4693  O   GLN A 611     142.502  85.462 -14.727  1.00 28.88           O  
ANISOU 4693  O   GLN A 611     3337   3717   3918    -31     73    117       O  
ATOM   4694  CB  GLN A 611     143.527  88.430 -14.416  1.00 32.44           C  
ANISOU 4694  CB  GLN A 611     3811   4178   4339    -63     77    132       C  
ATOM   4695  CG  GLN A 611     144.498  89.514 -14.005  1.00 37.51           C  
ANISOU 4695  CG  GLN A 611     4453   4825   4972    -79     80    137       C  
ATOM   4696  CD  GLN A 611     144.349  90.792 -14.844  1.00 38.28           C  
ANISOU 4696  CD  GLN A 611     4571   4925   5049    -93     86    140       C  
ATOM   4697  OE1 GLN A 611     144.254  90.728 -16.040  1.00 40.44           O  
ANISOU 4697  OE1 GLN A 611     4849   5204   5314    -96     93    134       O  
ATOM   4698  NE2 GLN A 611     144.313  91.926 -14.197  1.00 37.96           N  
ANISOU 4698  NE2 GLN A 611     4544   4880   5001   -102     83    150       N  
ATOM   4699  N   LEU A 612     141.076  86.639 -13.381  1.00 26.29           N  
ANISOU 4699  N   LEU A 612     3035   3374   3582    -31     60    137       N  
ATOM   4700  CA  LEU A 612     139.810  86.001 -13.772  1.00 25.52           C  
ANISOU 4700  CA  LEU A 612     2942   3268   3486    -21     57    134       C  
ATOM   4701  C   LEU A 612     138.775  87.099 -13.957  1.00 24.98           C  
ANISOU 4701  C   LEU A 612     2894   3195   3402    -25     54    141       C  
ATOM   4702  O   LEU A 612     138.615  87.922 -13.071  1.00 25.55           O  
ANISOU 4702  O   LEU A 612     2975   3263   3471    -28     48    151       O  
ATOM   4703  CB  LEU A 612     139.332  85.086 -12.661  1.00 26.00           C  
ANISOU 4703  CB  LEU A 612     2997   3320   3563    -10     49    137       C  
ATOM   4704  CG  LEU A 612     137.901  84.526 -12.823  1.00 27.32           C  
ANISOU 4704  CG  LEU A 612     3171   3478   3732     -1     45    136       C  
ATOM   4705  CD1 LEU A 612     137.721  83.638 -14.014  1.00 27.76           C  
ANISOU 4705  CD1 LEU A 612     3221   3537   3790      3     51    123       C  
ATOM   4706  CD2 LEU A 612     137.509  83.747 -11.594  1.00 28.29           C  
ANISOU 4706  CD2 LEU A 612     3290   3592   3869      7     37    140       C  
ATOM   4707  N   SER A 613     138.090  87.145 -15.098  1.00 24.09           N  
ANISOU 4707  N   SER A 613     2789   3083   3279    -24     57    136       N  
ATOM   4708  CA  SER A 613     137.070  88.127 -15.332  1.00 24.13           C  
ANISOU 4708  CA  SER A 613     2814   3084   3270    -25     52    142       C  
ATOM   4709  C   SER A 613     135.746  87.400 -15.578  1.00 24.60           C  
ANISOU 4709  C   SER A 613     2875   3138   3333    -14     48    138       C  
ATOM   4710  O   SER A 613     135.730  86.320 -16.130  1.00 24.03           O  
ANISOU 4710  O   SER A 613     2792   3069   3268     -9     52    128       O  
ATOM   4711  CB  SER A 613     137.377  89.033 -16.541  1.00 24.72           C  
ANISOU 4711  CB  SER A 613     2900   3165   3326    -36     58    142       C  
ATOM   4712  OG  SER A 613     138.465  89.907 -16.222  1.00 26.82           O  
ANISOU 4712  OG  SER A 613     3168   3436   3588    -48     62    147       O  
ATOM   4713  N   TRP A 614     134.654  88.069 -15.260  1.00 24.21           N  
ANISOU 4713  N   TRP A 614     2839   3082   3277    -11     41    144       N  
ATOM   4714  CA  TRP A 614     133.324  87.526 -15.496  1.00 25.36           C  
ANISOU 4714  CA  TRP A 614     2987   3223   3424     -1     36    139       C  
ATOM   4715  C   TRP A 614     132.307  88.622 -15.758  1.00 24.08           C  
ANISOU 4715  C   TRP A 614     2843   3058   3248      0     30    144       C  
ATOM   4716  O   TRP A 614     132.570  89.795 -15.538  1.00 24.51           O  
ANISOU 4716  O   TRP A 614     2909   3111   3294     -6     28    152       O  
ATOM   4717  CB  TRP A 614     132.879  86.653 -14.315  1.00 25.22           C  
ANISOU 4717  CB  TRP A 614     2961   3199   3423      7     31    139       C  
ATOM   4718  CG  TRP A 614     132.723  87.340 -12.997  1.00 25.54           C  
ANISOU 4718  CG  TRP A 614     3007   3233   3465      5     25    149       C  
ATOM   4719  CD1 TRP A 614     131.571  87.862 -12.497  1.00 24.43           C  
ANISOU 4719  CD1 TRP A 614     2875   3086   3319      9     18    152       C  
ATOM   4720  CD2 TRP A 614     133.730  87.490 -11.934  1.00 25.43           C  
ANISOU 4720  CD2 TRP A 614     2986   3218   3456      0     25    156       C  
ATOM   4721  NE1 TRP A 614     131.798  88.357 -11.205  1.00 26.36           N  
ANISOU 4721  NE1 TRP A 614     3121   3326   3567      6     14    160       N  
ATOM   4722  CE2 TRP A 614     133.110  88.181 -10.862  1.00 25.65           C  
ANISOU 4722  CE2 TRP A 614     3023   3240   3484      0     18    163       C  
ATOM   4723  CE3 TRP A 614     135.080  87.164 -11.825  1.00 27.12           C  
ANISOU 4723  CE3 TRP A 614     3190   3438   3678     -5     29    156       C  
ATOM   4724  CZ2 TRP A 614     133.780  88.496  -9.667  1.00 26.82           C  
ANISOU 4724  CZ2 TRP A 614     3168   3386   3635     -6     16    170       C  
ATOM   4725  CZ3 TRP A 614     135.774  87.529 -10.661  1.00 27.50           C  
ANISOU 4725  CZ3 TRP A 614     3235   3485   3730    -10     27    163       C  
ATOM   4726  CH2 TRP A 614     135.128  88.160  -9.591  1.00 27.14           C  
ANISOU 4726  CH2 TRP A 614     3197   3432   3681    -10     20    171       C  
ATOM   4727  N   LEU A 615     131.146  88.210 -16.266  1.00 24.35           N  
ANISOU 4727  N   LEU A 615     2880   3093   3281      9     27    138       N  
ATOM   4728  CA  LEU A 615     130.034  89.109 -16.588  1.00 24.40           C  
ANISOU 4728  CA  LEU A 615     2901   3096   3275     13     19    140       C  
ATOM   4729  C   LEU A 615     128.802  88.762 -15.733  1.00 24.80           C  
ANISOU 4729  C   LEU A 615     2950   3141   3333     22     12    138       C  
ATOM   4730  O   LEU A 615     128.304  87.606 -15.742  1.00 25.34           O  
ANISOU 4730  O   LEU A 615     3007   3210   3411     28     13    130       O  
ATOM   4731  CB  LEU A 615     129.750  89.028 -18.073  1.00 25.14           C  
ANISOU 4731  CB  LEU A 615     2999   3197   3356     13     22    134       C  
ATOM   4732  CG  LEU A 615     128.445  89.620 -18.617  1.00 26.97           C  
ANISOU 4732  CG  LEU A 615     3243   3428   3576     21     13    134       C  
ATOM   4733  CD1 LEU A 615     128.520  91.127 -18.553  1.00 27.05           C  
ANISOU 4733  CD1 LEU A 615     3272   3433   3574     17      8    145       C  
ATOM   4734  CD2 LEU A 615     128.215  89.114 -20.038  1.00 27.99           C  
ANISOU 4734  CD2 LEU A 615     3372   3567   3697     22     16    125       C  
ATOM   4735  N   GLU A 616     128.298  89.756 -15.013  1.00 23.50           N  
ANISOU 4735  N   GLU A 616     2795   2969   3164     23      5    145       N  
ATOM   4736  CA  GLU A 616     127.123  89.598 -14.159  1.00 24.44           C  
ANISOU 4736  CA  GLU A 616     2913   3084   3290     31     -2    143       C  
ATOM   4737  C   GLU A 616     126.180  90.770 -14.282  1.00 24.98           C  
ANISOU 4737  C   GLU A 616     2996   3149   3347     36    -10    145       C  
ATOM   4738  O   GLU A 616     126.564  91.940 -14.063  1.00 25.60           O  
ANISOU 4738  O   GLU A 616     3085   3222   3418     31    -12    154       O  
ATOM   4739  CB  GLU A 616     127.530  89.435 -12.664  1.00 25.38           C  
ANISOU 4739  CB  GLU A 616     3026   3198   3420     27     -2    148       C  
ATOM   4740  CG  GLU A 616     126.400  89.344 -11.633  1.00 27.75           C  
ANISOU 4740  CG  GLU A 616     3325   3494   3726     32     -8    146       C  
ATOM   4741  CD  GLU A 616     125.496  88.101 -11.818  1.00 31.50           C  
ANISOU 4741  CD  GLU A 616     3789   3970   4208     39     -7    135       C  
ATOM   4742  OE1 GLU A 616     125.785  87.233 -12.632  1.00 33.58           O  
ANISOU 4742  OE1 GLU A 616     4046   4238   4474     39     -3    130       O  
ATOM   4743  OE2 GLU A 616     124.484  87.961 -11.133  1.00 37.97           O  
ANISOU 4743  OE2 GLU A 616     4607   4788   5030     42    -12    132       O  
ATOM   4744  N   ASN A 617     124.926  90.463 -14.563  1.00 25.04           N  
ANISOU 4744  N   ASN A 617     3002   3158   3354     45    -15    137       N  
ATOM   4745  CA  ASN A 617     123.880  91.508 -14.680  1.00 25.80           C  
ANISOU 4745  CA  ASN A 617     3111   3251   3441     52    -24    138       C  
ATOM   4746  C   ASN A 617     124.375  92.720 -15.509  1.00 25.25           C  
ANISOU 4746  C   ASN A 617     3058   3180   3357     49    -26    146       C  
ATOM   4747  O   ASN A 617     124.180  93.855 -15.127  1.00 24.07           O  
ANISOU 4747  O   ASN A 617     2921   3024   3203     50    -32    153       O  
ATOM   4748  CB  ASN A 617     123.381  91.956 -13.278  1.00 25.93           C  
ANISOU 4748  CB  ASN A 617     3127   3261   3464     54    -29    140       C  
ATOM   4749  CG  ASN A 617     122.094  92.812 -13.347  1.00 29.51           C  
ANISOU 4749  CG  ASN A 617     3590   3713   3912     64    -39    136       C  
ATOM   4750  OD1 ASN A 617     121.370  92.740 -14.293  1.00 31.08           O  
ANISOU 4750  OD1 ASN A 617     3790   3916   4104     72    -43    131       O  
ATOM   4751  ND2 ASN A 617     121.855  93.636 -12.371  1.00 30.02           N  
ANISOU 4751  ND2 ASN A 617     3659   3769   3977     65    -43    140       N  
ATOM   4752  N   GLY A 618     124.978  92.465 -16.660  1.00 24.87           N  
ANISOU 4752  N   GLY A 618     3011   3138   3301     45    -21    146       N  
ATOM   4753  CA  GLY A 618     125.353  93.541 -17.553  1.00 25.01           C  
ANISOU 4753  CA  GLY A 618     3045   3154   3303     41    -22    154       C  
ATOM   4754  C   GLY A 618     126.686  94.241 -17.284  1.00 25.04           C  
ANISOU 4754  C   GLY A 618     3055   3154   3304     28    -16    164       C  
ATOM   4755  O   GLY A 618     126.958  95.204 -17.942  1.00 26.37           O  
ANISOU 4755  O   GLY A 618     3239   3320   3459     24    -18    171       O  
ATOM   4756  N   ARG A 619     127.457  93.825 -16.280  1.00 25.08           N  
ANISOU 4756  N   ARG A 619     3050   3159   3322     22    -11    165       N  
ATOM   4757  CA  ARG A 619     128.718  94.500 -15.911  1.00 25.42           C  
ANISOU 4757  CA  ARG A 619     3096   3198   3362      9     -5    173       C  
ATOM   4758  C   ARG A 619     129.837  93.486 -15.850  1.00 25.40           C  
ANISOU 4758  C   ARG A 619     3078   3203   3369      2      5    170       C  
ATOM   4759  O   ARG A 619     129.582  92.332 -15.488  1.00 25.10           O  
ANISOU 4759  O   ARG A 619     3025   3168   3343      7      6    163       O  
ATOM   4760  CB  ARG A 619     128.579  95.156 -14.548  1.00 25.38           C  
ANISOU 4760  CB  ARG A 619     3095   3185   3365      9    -10    178       C  
ATOM   4761  CG  ARG A 619     127.555  96.271 -14.515  1.00 27.09           C  
ANISOU 4761  CG  ARG A 619     3327   3392   3573     17    -19    181       C  
ATOM   4762  CD  ARG A 619     127.450  96.856 -13.129  1.00 28.35           C  
ANISOU 4762  CD  ARG A 619     3488   3544   3740     16    -23    184       C  
ATOM   4763  NE  ARG A 619     126.329  97.773 -12.959  1.00 28.26           N  
ANISOU 4763  NE  ARG A 619     3489   3524   3725     26    -33    184       N  
ATOM   4764  CZ  ARG A 619     125.173  97.494 -12.365  1.00 28.89           C  
ANISOU 4764  CZ  ARG A 619     3562   3603   3811     37    -39    177       C  
ATOM   4765  NH1 ARG A 619     124.890  96.309 -11.822  1.00 29.65           N  
ANISOU 4765  NH1 ARG A 619     3642   3706   3919     39    -36    170       N  
ATOM   4766  NH2 ARG A 619     124.295  98.443 -12.268  1.00 30.34           N  
ANISOU 4766  NH2 ARG A 619     3758   3778   3990     45    -48    177       N  
ATOM   4767  N   PHE A 620     131.063  93.927 -16.169  1.00 25.66           N  
ANISOU 4767  N   PHE A 620     3113   3239   3396    -11     12    174       N  
ATOM   4768  CA  PHE A 620     132.246  93.099 -16.038  1.00 26.10           C  
ANISOU 4768  CA  PHE A 620     3153   3302   3460    -18     21    171       C  
ATOM   4769  C   PHE A 620     132.933  93.300 -14.722  1.00 26.38           C  
ANISOU 4769  C   PHE A 620     3184   3335   3506    -23     21    176       C  
ATOM   4770  O   PHE A 620     132.926  94.409 -14.142  1.00 25.78           O  
ANISOU 4770  O   PHE A 620     3120   3252   3425    -27     18    183       O  
ATOM   4771  CB  PHE A 620     133.238  93.309 -17.215  1.00 26.41           C  
ANISOU 4771  CB  PHE A 620     3196   3350   3488    -29     30    170       C  
ATOM   4772  CG  PHE A 620     132.625  93.084 -18.546  1.00 26.91           C  
ANISOU 4772  CG  PHE A 620     3265   3419   3542    -25     30    165       C  
ATOM   4773  CD1 PHE A 620     132.483  91.781 -19.039  1.00 27.31           C  
ANISOU 4773  CD1 PHE A 620     3300   3477   3600    -19     33    154       C  
ATOM   4774  CD2 PHE A 620     132.202  94.143 -19.348  1.00 27.72           C  
ANISOU 4774  CD2 PHE A 620     3388   3519   3626    -27     26    171       C  
ATOM   4775  CE1 PHE A 620     131.936  91.550 -20.281  1.00 26.19           C  
ANISOU 4775  CE1 PHE A 620     3163   3342   3447    -16     34    149       C  
ATOM   4776  CE2 PHE A 620     131.637  93.895 -20.604  1.00 26.84           C  
ANISOU 4776  CE2 PHE A 620     3281   3414   3505    -23     25    167       C  
ATOM   4777  CZ  PHE A 620     131.536  92.590 -21.072  1.00 26.96           C  
ANISOU 4777  CZ  PHE A 620     3279   3438   3526    -19     29    155       C  
ATOM   4778  N   TYR A 621     133.583  92.221 -14.269  1.00 25.59           N  
ANISOU 4778  N   TYR A 621     3065   3239   3418    -23     25    171       N  
ATOM   4779  CA  TYR A 621     134.346  92.229 -13.049  1.00 25.57           C  
ANISOU 4779  CA  TYR A 621     3055   3236   3426    -28     26    175       C  
ATOM   4780  C   TYR A 621     135.635  91.497 -13.305  1.00 25.65           C  
ANISOU 4780  C   TYR A 621     3050   3255   3441    -33     34    171       C  
ATOM   4781  O   TYR A 621     135.640  90.560 -14.069  1.00 25.13           O  
ANISOU 4781  O   TYR A 621     2974   3194   3379    -29     38    163       O  
ATOM   4782  CB  TYR A 621     133.555  91.563 -11.892  1.00 25.87           C  
ANISOU 4782  CB  TYR A 621     3085   3268   3475    -18     19    175       C  
ATOM   4783  CG  TYR A 621     132.277  92.295 -11.587  1.00 25.20           C  
ANISOU 4783  CG  TYR A 621     3014   3175   3385    -13     11    177       C  
ATOM   4784  CD1 TYR A 621     132.273  93.391 -10.724  1.00 25.30           C  
ANISOU 4784  CD1 TYR A 621     3036   3182   3394    -17      8    184       C  
ATOM   4785  CD2 TYR A 621     131.073  91.937 -12.218  1.00 25.51           C  
ANISOU 4785  CD2 TYR A 621     3057   3214   3423     -3      8    172       C  
ATOM   4786  CE1 TYR A 621     131.085  94.113 -10.489  1.00 24.54           C  
ANISOU 4786  CE1 TYR A 621     2952   3078   3294    -11      0    185       C  
ATOM   4787  CE2 TYR A 621     129.874  92.623 -11.965  1.00 24.87           C  
ANISOU 4787  CE2 TYR A 621     2985   3126   3337      4      0    173       C  
ATOM   4788  CZ  TYR A 621     129.893  93.726 -11.131  1.00 24.37           C  
ANISOU 4788  CZ  TYR A 621     2932   3056   3270      0     -4    179       C  
ATOM   4789  OH  TYR A 621     128.732  94.429 -10.894  1.00 22.83           O  
ANISOU 4789  OH  TYR A 621     2747   2854   3071      7    -11    179       O  
ATOM   4790  N   THR A 622     136.720  91.959 -12.690  1.00 25.78           N  
ANISOU 4790  N   THR A 622     3063   3274   3459    -43     37    175       N  
ATOM   4791  CA  THR A 622     138.015  91.277 -12.749  1.00 26.88           C  
ANISOU 4791  CA  THR A 622     3184   3422   3605    -48     43    170       C  
ATOM   4792  C   THR A 622     138.576  91.146 -11.346  1.00 27.27           C  
ANISOU 4792  C   THR A 622     3224   3471   3666    -49     40    175       C  
ATOM   4793  O   THR A 622     138.632  92.123 -10.591  1.00 27.45           O  
ANISOU 4793  O   THR A 622     3256   3490   3684    -55     37    182       O  
ATOM   4794  CB  THR A 622     139.019  92.046 -13.637  1.00 27.35           C  
ANISOU 4794  CB  THR A 622     3248   3490   3652    -62     52    169       C  
ATOM   4795  OG1 THR A 622     138.462  92.234 -14.917  1.00 26.63           O  
ANISOU 4795  OG1 THR A 622     3169   3400   3550    -62     55    167       O  
ATOM   4796  CG2 THR A 622     140.379  91.294 -13.795  1.00 27.96           C  
ANISOU 4796  CG2 THR A 622     3306   3580   3738    -66     60    162       C  
ATOM   4797  N   LEU A 623     138.951  89.913 -11.006  1.00 27.76           N  
ANISOU 4797  N   LEU A 623     3269   3537   3743    -42     40    170       N  
ATOM   4798  CA  LEU A 623     139.746  89.585  -9.848  1.00 27.65           C  
ANISOU 4798  CA  LEU A 623     3242   3524   3739    -43     37    173       C  
ATOM   4799  C   LEU A 623     141.179  89.443 -10.293  1.00 28.71           C  
ANISOU 4799  C   LEU A 623     3364   3670   3876    -50     44    167       C  
ATOM   4800  O   LEU A 623     141.468  88.591 -11.146  1.00 28.24           O  
ANISOU 4800  O   LEU A 623     3294   3616   3821    -45     49    159       O  
ATOM   4801  CB  LEU A 623     139.270  88.256  -9.227  1.00 28.28           C  
ANISOU 4801  CB  LEU A 623     3312   3599   3835    -30     31    172       C  
ATOM   4802  CG  LEU A 623     140.073  87.680  -8.052  1.00 28.77           C  
ANISOU 4802  CG  LEU A 623     3360   3663   3909    -28     27    175       C  
ATOM   4803  CD1 LEU A 623     140.024  88.622  -6.865  1.00 29.58           C  
ANISOU 4803  CD1 LEU A 623     3469   3763   4006    -35     21    185       C  
ATOM   4804  CD2 LEU A 623     139.638  86.280  -7.640  1.00 28.90           C  
ANISOU 4804  CD2 LEU A 623     3367   3673   3940    -16     22    174       C  
ATOM   4805  N   THR A 624     142.089  90.216  -9.669  1.00 28.74           N  
ANISOU 4805  N   THR A 624     3365   3679   3875    -60     45    171       N  
ATOM   4806  CA  THR A 624     143.545  90.074  -9.904  1.00 28.90           C  
ANISOU 4806  CA  THR A 624     3370   3712   3899    -68     52    165       C  
ATOM   4807  C   THR A 624     144.149  89.731  -8.528  1.00 30.54           C  
ANISOU 4807  C   THR A 624     3565   3921   4118    -65     45    169       C  
ATOM   4808  O   THR A 624     143.828  90.391  -7.536  1.00 31.76           O  
ANISOU 4808  O   THR A 624     3727   4071   4269    -69     39    178       O  
ATOM   4809  CB  THR A 624     144.129  91.384 -10.450  1.00 29.33           C  
ANISOU 4809  CB  THR A 624     3435   3772   3937    -85     59    166       C  
ATOM   4810  OG1 THR A 624     143.410  91.789 -11.634  1.00 27.96           O  
ANISOU 4810  OG1 THR A 624     3277   3595   3751    -87     63    165       O  
ATOM   4811  CG2 THR A 624     145.641  91.274 -10.757  1.00 29.18           C  
ANISOU 4811  CG2 THR A 624     3399   3769   3920    -94     67    158       C  
ATOM   4812  N   THR A 625     144.989  88.700  -8.466  1.00 30.68           N  
ANISOU 4812  N   THR A 625     3562   3945   4148    -59     45    163       N  
ATOM   4813  CA  THR A 625     145.611  88.292  -7.226  1.00 32.39           C  
ANISOU 4813  CA  THR A 625     3766   4164   4375    -55     37    167       C  
ATOM   4814  C   THR A 625     147.135  87.991  -7.411  1.00 32.41           C  
ANISOU 4814  C   THR A 625     3748   4182   4385    -59     42    159       C  
ATOM   4815  O   THR A 625     147.538  87.510  -8.443  1.00 30.93           O  
ANISOU 4815  O   THR A 625     3552   4000   4200    -57     49    148       O  
ATOM   4816  CB  THR A 625     144.807  87.122  -6.595  1.00 34.09           C  
ANISOU 4816  CB  THR A 625     3980   4370   4605    -39     28    171       C  
ATOM   4817  OG1 THR A 625     145.196  86.925  -5.226  1.00 35.82           O  
ANISOU 4817  OG1 THR A 625     4191   4589   4831    -37     19    178       O  
ATOM   4818  CG2 THR A 625     145.021  85.848  -7.347  1.00 35.46           C  
ANISOU 4818  CG2 THR A 625     4139   4543   4790    -28     31    161       C  
ATOM   4819  N   ALA A 626     147.963  88.367  -6.434  1.00 33.27           N  
ANISOU 4819  N   ALA A 626     3849   4298   4495    -64     37    162       N  
ATOM   4820  CA  ALA A 626     149.420  88.116  -6.478  1.00 35.36           C  
ANISOU 4820  CA  ALA A 626     4091   4578   4765    -67     40    154       C  
ATOM   4821  C   ALA A 626     149.672  86.624  -6.295  1.00 37.57           C  
ANISOU 4821  C   ALA A 626     4354   4857   5064    -49     34    150       C  
ATOM   4822  O   ALA A 626     149.280  86.036  -5.287  1.00 42.50           O  
ANISOU 4822  O   ALA A 626     4978   5473   5698    -39     23    158       O  
ATOM   4823  CB  ALA A 626     150.131  88.913  -5.406  1.00 33.99           C  
ANISOU 4823  CB  ALA A 626     3915   4413   4588    -78     36    159       C  
ATOM   4824  N   THR A 627     150.218  85.979  -7.313  1.00 37.98           N  
ANISOU 4824  N   THR A 627     4393   4915   5123    -45     42    137       N  
ATOM   4825  CA  THR A 627     150.494  84.540  -7.239  1.00 37.63           C  
ANISOU 4825  CA  THR A 627     4332   4869   5098    -27     36    131       C  
ATOM   4826  C   THR A 627     151.993  84.284  -7.259  1.00 39.49           C  
ANISOU 4826  C   THR A 627     4543   5120   5341    -27     38    120       C  
ATOM   4827  O   THR A 627     152.733  85.073  -7.851  1.00 38.42           O  
ANISOU 4827  O   THR A 627     4403   4999   5196    -41     48    112       O  
ATOM   4828  CB  THR A 627     149.775  83.784  -8.397  1.00 37.33           C  
ANISOU 4828  CB  THR A 627     4297   4822   5063    -19     43    123       C  
ATOM   4829  OG1 THR A 627     149.831  84.539  -9.618  1.00 35.17           O  
ANISOU 4829  OG1 THR A 627     4030   4557   4775    -32     56    115       O  
ATOM   4830  CG2 THR A 627     148.263  83.566  -8.025  1.00 38.74           C  
ANISOU 4830  CG2 THR A 627     4495   4983   5241    -12     36    134       C  
ATOM   4831  N   ASN A 628     152.412  83.237  -6.534  1.00 42.85           N  
ANISOU 4831  N   ASN A 628     4952   5543   5784    -11     27    121       N  
ATOM   4832  CA  ASN A 628     153.732  82.581  -6.650  1.00 45.27           C  
ANISOU 4832  CA  ASN A 628     5233   5863   6105     -4     27    108       C  
ATOM   4833  C   ASN A 628     153.541  81.466  -7.679  1.00 47.44           C  
ANISOU 4833  C   ASN A 628     5502   6133   6392      9     32     96       C  
ATOM   4834  O   ASN A 628     152.426  80.922  -7.809  1.00 46.08           O  
ANISOU 4834  O   ASN A 628     5343   5944   6223     17     30    101       O  
ATOM   4835  CB  ASN A 628     154.123  81.916  -5.320  1.00 47.53           C  
ANISOU 4835  CB  ASN A 628     5509   6147   6405      9     11    117       C  
ATOM   4836  CG  ASN A 628     154.013  82.849  -4.102  1.00 52.50           C  
ANISOU 4836  CG  ASN A 628     6147   6777   7022     -1      3    132       C  
ATOM   4837  OD1 ASN A 628     154.144  84.064  -4.200  1.00 55.54           O  
ANISOU 4837  OD1 ASN A 628     6540   7171   7392    -19     10    132       O  
ATOM   4838  ND2 ASN A 628     153.772  82.264  -2.940  1.00 56.00           N  
ANISOU 4838  ND2 ASN A 628     6592   7212   7475     10    -12    144       N  
ATOM   4839  N   ASN A 629     154.596  81.065  -8.374  1.00 49.57           N  
ANISOU 4839  N   ASN A 629     5750   6415   6669     11     39     79       N  
ATOM   4840  CA  ASN A 629     154.473  79.980  -9.397  1.00 51.67           C  
ANISOU 4840  CA  ASN A 629     6008   6676   6947     24     45     65       C  
ATOM   4841  C   ASN A 629     154.096  78.570  -8.881  1.00 46.29           C  
ANISOU 4841  C   ASN A 629     5322   5977   6287     47     33     69       C  
ATOM   4842  O   ASN A 629     153.634  77.748  -9.640  1.00 44.95           O  
ANISOU 4842  O   ASN A 629     5153   5799   6126     55     37     60       O  
ATOM   4843  CB  ASN A 629     155.700  79.915 -10.323  1.00 57.68           C  
ANISOU 4843  CB  ASN A 629     6746   7457   7711     20     56     43       C  
ATOM   4844  CG  ASN A 629     156.983  79.833  -9.561  1.00 65.39           C  
ANISOU 4844  CG  ASN A 629     7700   8447   8698     24     49     40       C  
ATOM   4845  OD1 ASN A 629     157.329  78.777  -9.039  1.00 73.41           O  
ANISOU 4845  OD1 ASN A 629     8702   9458   9734     43     38     38       O  
ATOM   4846  ND2 ASN A 629     157.687  80.968  -9.441  1.00 71.64           N  
ANISOU 4846  ND2 ASN A 629     8488   9256   9475      5     54     39       N  
ATOM   4847  N   ASP A 630     154.267  78.297  -7.594  1.00 43.18           N  
ANISOU 4847  N   ASP A 630     4926   5578   5902     55     18     81       N  
ATOM   4848  CA  ASP A 630     153.753  77.045  -6.999  1.00 41.08           C  
ANISOU 4848  CA  ASP A 630     4662   5292   5654     75      5     89       C  
ATOM   4849  C   ASP A 630     152.260  77.096  -6.572  1.00 38.01           C  
ANISOU 4849  C   ASP A 630     4299   4885   5258     73      1    105       C  
ATOM   4850  O   ASP A 630     151.778  76.160  -5.966  1.00 34.90           O  
ANISOU 4850  O   ASP A 630     3910   4475   4877     87     -9    113       O  
ATOM   4851  CB  ASP A 630     154.625  76.670  -5.792  1.00 43.46           C  
ANISOU 4851  CB  ASP A 630     4949   5596   5967     86    -10     96       C  
ATOM   4852  CG  ASP A 630     155.977  76.097  -6.199  1.00 48.73           C  
ANISOU 4852  CG  ASP A 630     5588   6277   6650     96     -9     78       C  
ATOM   4853  OD1 ASP A 630     156.071  75.487  -7.290  1.00 53.16           O  
ANISOU 4853  OD1 ASP A 630     6141   6838   7220    102      0     61       O  
ATOM   4854  OD2 ASP A 630     156.945  76.240  -5.419  1.00 53.02           O  
ANISOU 4854  OD2 ASP A 630     6116   6832   7197     99    -18     79       O  
ATOM   4855  N   ASP A 631     151.550  78.195  -6.832  1.00 35.56           N  
ANISOU 4855  N   ASP A 631     4007   4578   4928     57      9    110       N  
ATOM   4856  CA  ASP A 631     150.134  78.311  -6.405  1.00 34.50           C  
ANISOU 4856  CA  ASP A 631     3895   4427   4786     55      5    124       C  
ATOM   4857  C   ASP A 631     149.277  77.450  -7.275  1.00 34.24           C  
ANISOU 4857  C   ASP A 631     3868   4381   4760     63     10    117       C  
ATOM   4858  O   ASP A 631     149.570  77.264  -8.434  1.00 39.50           O  
ANISOU 4858  O   ASP A 631     4527   5054   5428     63     21    101       O  
ATOM   4859  CB  ASP A 631     149.636  79.748  -6.500  1.00 34.19           C  
ANISOU 4859  CB  ASP A 631     3872   4393   4724     36     11    130       C  
ATOM   4860  CG  ASP A 631     150.074  80.601  -5.336  1.00 35.29           C  
ANISOU 4860  CG  ASP A 631     4012   4540   4857     28      4    141       C  
ATOM   4861  OD1 ASP A 631     150.546  80.066  -4.329  1.00 37.52           O  
ANISOU 4861  OD1 ASP A 631     4285   4821   5149     37     -8    148       O  
ATOM   4862  OD2 ASP A 631     150.027  81.826  -5.431  1.00 35.66           O  
ANISOU 4862  OD2 ASP A 631     4067   4594   4886     12      9    143       O  
ATOM   4863  N   GLU A 632     148.212  76.909  -6.720  1.00 33.80           N  
ANISOU 4863  N   GLU A 632     3826   4309   4708     69      3    127       N  
ATOM   4864  CA  GLU A 632     147.211  76.241  -7.516  1.00 33.92           C  
ANISOU 4864  CA  GLU A 632     3850   4312   4727     74      9    121       C  
ATOM   4865  C   GLU A 632     145.912  77.111  -7.584  1.00 33.56           C  
ANISOU 4865  C   GLU A 632     3826   4263   4662     62     12    129       C  
ATOM   4866  O   GLU A 632     145.516  77.752  -6.604  1.00 32.55           O  
ANISOU 4866  O   GLU A 632     3709   4133   4526     56      5    143       O  
ATOM   4867  CB  GLU A 632     146.930  74.878  -6.967  1.00 34.54           C  
ANISOU 4867  CB  GLU A 632     3927   4374   4824     89     -1    125       C  
ATOM   4868  CG  GLU A 632     148.089  73.886  -7.060  1.00 36.17           C  
ANISOU 4868  CG  GLU A 632     4112   4581   5051    104     -4    116       C  
ATOM   4869  CD  GLU A 632     147.716  72.521  -6.451  1.00 38.56           C  
ANISOU 4869  CD  GLU A 632     4417   4862   5372    119    -14    121       C  
ATOM   4870  OE1 GLU A 632     146.645  72.358  -5.801  1.00 40.44           O  
ANISOU 4870  OE1 GLU A 632     4672   5087   5607    118    -19    134       O  
ATOM   4871  OE2 GLU A 632     148.505  71.589  -6.579  1.00 42.33           O  
ANISOU 4871  OE2 GLU A 632     4879   5336   5867    133    -17    113       O  
ATOM   4872  N   LEU A 633     145.331  77.189  -8.779  1.00 32.85           N  
ANISOU 4872  N   LEU A 633     3741   4174   4566     58     22    119       N  
ATOM   4873  CA  LEU A 633     144.108  77.960  -8.997  1.00 32.76           C  
ANISOU 4873  CA  LEU A 633     3749   4159   4538     49     25    124       C  
ATOM   4874  C   LEU A 633     142.992  76.960  -9.313  1.00 31.57           C  
ANISOU 4874  C   LEU A 633     3605   3995   4395     58     25    121       C  
ATOM   4875  O   LEU A 633     143.023  76.325 -10.351  1.00 32.75           O  
ANISOU 4875  O   LEU A 633     3748   4144   4550     62     32    107       O  
ATOM   4876  CB  LEU A 633     144.290  78.980 -10.108  1.00 33.05           C  
ANISOU 4876  CB  LEU A 633     3788   4209   4558     37     36    116       C  
ATOM   4877  CG  LEU A 633     145.410  80.002  -9.883  1.00 34.27           C  
ANISOU 4877  CG  LEU A 633     3937   4379   4705     27     38    118       C  
ATOM   4878  CD1 LEU A 633     145.645  80.886 -11.111  1.00 36.89           C  
ANISOU 4878  CD1 LEU A 633     4272   4723   5021     15     50    109       C  
ATOM   4879  CD2 LEU A 633     145.180  80.891  -8.680  1.00 34.46           C  
ANISOU 4879  CD2 LEU A 633     3972   4401   4721     20     30    134       C  
ATOM   4880  N   HIS A 634     142.050  76.786  -8.388  1.00 28.50           N  
ANISOU 4880  N   HIS A 634     3227   3594   4007     59     17    133       N  
ATOM   4881  CA  HIS A 634     141.014  75.785  -8.526  1.00 28.75           C  
ANISOU 4881  CA  HIS A 634     3265   3611   4046     66     17    130       C  
ATOM   4882  C   HIS A 634     139.671  76.399  -8.899  1.00 29.42           C  
ANISOU 4882  C   HIS A 634     3365   3695   4116     59     20    131       C  
ATOM   4883  O   HIS A 634     139.086  77.141  -8.110  1.00 31.03           O  
ANISOU 4883  O   HIS A 634     3581   3899   4311     53     15    142       O  
ATOM   4884  CB  HIS A 634     140.866  75.019  -7.201  1.00 30.40           C  
ANISOU 4884  CB  HIS A 634     3475   3807   4267     73      6    143       C  
ATOM   4885  CG  HIS A 634     142.036  74.127  -6.860  1.00 31.07           C  
ANISOU 4885  CG  HIS A 634     3545   3889   4370     83      0    141       C  
ATOM   4886  ND1 HIS A 634     142.022  72.773  -7.090  1.00 32.16           N  
ANISOU 4886  ND1 HIS A 634     3678   4015   4526     95      0    135       N  
ATOM   4887  CD2 HIS A 634     143.235  74.395  -6.293  1.00 33.05           C  
ANISOU 4887  CD2 HIS A 634     3785   4149   4624     85     -5    146       C  
ATOM   4888  CE1 HIS A 634     143.150  72.234  -6.662  1.00 33.00           C  
ANISOU 4888  CE1 HIS A 634     3771   4121   4647    104     -7    136       C  
ATOM   4889  NE2 HIS A 634     143.900  73.197  -6.161  1.00 33.94           N  
ANISOU 4889  NE2 HIS A 634     3886   4253   4757     98    -10    142       N  
ATOM   4890  N   PHE A 635     139.163  76.095 -10.087  1.00 27.76           N  
ANISOU 4890  N   PHE A 635     3157   3486   3905     60     28    118       N  
ATOM   4891  CA  PHE A 635     137.751  76.314 -10.352  1.00 28.48           C  
ANISOU 4891  CA  PHE A 635     3262   3574   3986     56     29    118       C  
ATOM   4892  C   PHE A 635     136.930  75.239  -9.650  1.00 27.90           C  
ANISOU 4892  C   PHE A 635     3192   3485   3925     62     24    122       C  
ATOM   4893  O   PHE A 635     137.192  74.034  -9.831  1.00 28.01           O  
ANISOU 4893  O   PHE A 635     3197   3490   3954     71     25    115       O  
ATOM   4894  CB  PHE A 635     137.435  76.308 -11.839  1.00 28.31           C  
ANISOU 4894  CB  PHE A 635     3240   3559   3958     55     39    104       C  
ATOM   4895  CG  PHE A 635     137.843  77.567 -12.556  1.00 29.99           C  
ANISOU 4895  CG  PHE A 635     3455   3785   4153     46     44    103       C  
ATOM   4896  CD1 PHE A 635     137.087  78.714 -12.436  1.00 30.14           C  
ANISOU 4896  CD1 PHE A 635     3489   3807   4156     39     42    110       C  
ATOM   4897  CD2 PHE A 635     138.957  77.585 -13.391  1.00 30.02           C  
ANISOU 4897  CD2 PHE A 635     3448   3799   4157     45     51     93       C  
ATOM   4898  CE1 PHE A 635     137.481  79.894 -13.098  1.00 30.77           C  
ANISOU 4898  CE1 PHE A 635     3573   3899   4220     30     46    110       C  
ATOM   4899  CE2 PHE A 635     139.326  78.729 -14.069  1.00 30.27           C  
ANISOU 4899  CE2 PHE A 635     3484   3844   4173     35     57     92       C  
ATOM   4900  CZ  PHE A 635     138.583  79.881 -13.930  1.00 30.26           C  
ANISOU 4900  CZ  PHE A 635     3499   3844   4155     27     54    101       C  
ATOM   4901  N   VAL A 636     135.941  75.658  -8.858  1.00 27.86           N  
ANISOU 4901  N   VAL A 636     3198   3475   3912     58     19    131       N  
ATOM   4902  CA  VAL A 636     135.063  74.712  -8.125  1.00 26.77           C  
ANISOU 4902  CA  VAL A 636     3065   3324   3783     61     14    135       C  
ATOM   4903  C   VAL A 636     133.604  75.004  -8.435  1.00 27.97           C  
ANISOU 4903  C   VAL A 636     3227   3475   3923     57     17    131       C  
ATOM   4904  O   VAL A 636     133.259  76.087  -8.961  1.00 27.29           O  
ANISOU 4904  O   VAL A 636     3147   3399   3823     52     19    129       O  
ATOM   4905  CB  VAL A 636     135.324  74.689  -6.589  1.00 27.33           C  
ANISOU 4905  CB  VAL A 636     3138   3389   3858     60      5    151       C  
ATOM   4906  CG1 VAL A 636     136.764  74.243  -6.278  1.00 26.75           C  
ANISOU 4906  CG1 VAL A 636     3053   3315   3797     66      1    154       C  
ATOM   4907  CG2 VAL A 636     135.084  76.046  -5.926  1.00 27.38           C  
ANISOU 4907  CG2 VAL A 636     3153   3403   3848     51      2    160       C  
ATOM   4908  N   ARG A 637     132.758  74.020  -8.142  1.00 27.61           N  
ANISOU 4908  N   ARG A 637     3185   3419   3887     58     16    130       N  
ATOM   4909  CA  ARG A 637     131.312  74.153  -8.286  1.00 28.78           C  
ANISOU 4909  CA  ARG A 637     3343   3567   4027     54     17    126       C  
ATOM   4910  C   ARG A 637     130.595  73.432  -7.131  1.00 27.02           C  
ANISOU 4910  C   ARG A 637     3125   3331   3809     52     12    133       C  
ATOM   4911  O   ARG A 637     130.882  72.271  -6.829  1.00 26.47           O  
ANISOU 4911  O   ARG A 637     3052   3250   3755     56     11    134       O  
ATOM   4912  CB  ARG A 637     130.982  73.572  -9.651  1.00 30.47           C  
ANISOU 4912  CB  ARG A 637     3553   3782   4242     58     25    109       C  
ATOM   4913  CG  ARG A 637     129.545  73.242  -9.975  1.00 31.77           C  
ANISOU 4913  CG  ARG A 637     3723   3944   4403     55     27    101       C  
ATOM   4914  CD  ARG A 637     128.852  74.274 -10.810  1.00 29.95           C  
ANISOU 4914  CD  ARG A 637     3498   3727   4157     52     29     95       C  
ATOM   4915  NE  ARG A 637     129.655  74.820 -11.904  1.00 28.88           N  
ANISOU 4915  NE  ARG A 637     3357   3601   4014     54     34     89       N  
ATOM   4916  CZ  ARG A 637     129.509  76.056 -12.385  1.00 27.88           C  
ANISOU 4916  CZ  ARG A 637     3237   3486   3872     51     33     91       C  
ATOM   4917  NH1 ARG A 637     128.536  76.849 -11.901  1.00 25.56           N  
ANISOU 4917  NH1 ARG A 637     2951   3193   3566     48     29     96       N  
ATOM   4918  NH2 ARG A 637     130.318  76.490 -13.360  1.00 26.67           N  
ANISOU 4918  NH2 ARG A 637     3079   3341   3712     50     38     86       N  
ATOM   4919  N   ILE A 638     129.686  74.132  -6.470  1.00 25.42           N  
ANISOU 4919  N   ILE A 638     2930   3131   3596     46      9    138       N  
ATOM   4920  CA  ILE A 638     128.989  73.595  -5.334  1.00 26.31           C  
ANISOU 4920  CA  ILE A 638     3049   3235   3712     42      5    145       C  
ATOM   4921  C   ILE A 638     127.996  72.563  -5.884  1.00 26.66           C  
ANISOU 4921  C   ILE A 638     3095   3273   3763     42     10    134       C  
ATOM   4922  O   ILE A 638     127.405  72.788  -6.952  1.00 25.57           O  
ANISOU 4922  O   ILE A 638     2956   3142   3619     42     15    121       O  
ATOM   4923  CB  ILE A 638     128.272  74.700  -4.561  1.00 28.26           C  
ANISOU 4923  CB  ILE A 638     3303   3489   3945     34      2    151       C  
ATOM   4924  CG1 ILE A 638     129.243  75.706  -3.987  1.00 28.83           C  
ANISOU 4924  CG1 ILE A 638     3375   3568   4011     33     -3    162       C  
ATOM   4925  CG2 ILE A 638     127.431  74.118  -3.439  1.00 29.89           C  
ANISOU 4925  CG2 ILE A 638     3516   3688   4154     28     -1    157       C  
ATOM   4926  CD1 ILE A 638     128.566  77.036  -3.656  1.00 28.93           C  
ANISOU 4926  CD1 ILE A 638     3394   3589   4008     27     -4    164       C  
ATOM   4927  N   GLY A 639     127.858  71.422  -5.200  1.00 27.01           N  
ANISOU 4927  N   GLY A 639     3141   3304   3819     41      9    138       N  
ATOM   4928  CA  GLY A 639     126.860  70.424  -5.565  1.00 26.75           C  
ANISOU 4928  CA  GLY A 639     3110   3263   3791     39     13    127       C  
ATOM   4929  C   GLY A 639     127.195  68.963  -5.396  1.00 27.68           C  
ANISOU 4929  C   GLY A 639     3227   3363   3926     42     14    128       C  
ATOM   4930  O   GLY A 639     126.296  68.124  -5.602  1.00 26.64           O  
ANISOU 4930  O   GLY A 639     3098   3224   3799     38     18    119       O  
ATOM   4931  N   ALA A 640     128.447  68.624  -5.042  1.00 26.93           N  
ANISOU 4931  N   ALA A 640     3129   3262   3843     49      9    137       N  
ATOM   4932  CA  ALA A 640     128.790  67.262  -4.693  1.00 27.53           C  
ANISOU 4932  CA  ALA A 640     3205   3320   3936     53      7    140       C  
ATOM   4933  C   ALA A 640     128.091  66.821  -3.392  1.00 28.16           C  
ANISOU 4933  C   ALA A 640     3296   3389   4015     44      3    152       C  
ATOM   4934  O   ALA A 640     127.781  67.655  -2.526  1.00 27.94           O  
ANISOU 4934  O   ALA A 640     3273   3368   3974     36     -1    162       O  
ATOM   4935  CB  ALA A 640     130.300  67.082  -4.581  1.00 28.52           C  
ANISOU 4935  CB  ALA A 640     3323   3441   4072     63      2    147       C  
ATOM   4936  N   ASN A 641     127.913  65.500  -3.238  1.00 28.08           N  
ANISOU 4936  N   ASN A 641     3290   3360   4018     44      3    152       N  
ATOM   4937  CA  ASN A 641     127.309  64.893  -2.071  1.00 28.61           C  
ANISOU 4937  CA  ASN A 641     3369   3416   4087     35     -1    163       C  
ATOM   4938  C   ASN A 641     126.033  65.703  -1.637  1.00 28.66           C  
ANISOU 4938  C   ASN A 641     3381   3434   4074     21      2    162       C  
ATOM   4939  O   ASN A 641     125.915  66.159  -0.485  1.00 28.01           O  
ANISOU 4939  O   ASN A 641     3305   3355   3983     13     -3    175       O  
ATOM   4940  CB  ASN A 641     128.343  64.778  -0.934  1.00 31.49           C  
ANISOU 4940  CB  ASN A 641     3736   3773   4456     39    -12    183       C  
ATOM   4941  CG  ASN A 641     129.396  63.688  -1.196  1.00 34.99           C  
ANISOU 4941  CG  ASN A 641     4175   4199   4920     52    -15    184       C  
ATOM   4942  OD1 ASN A 641     129.063  62.492  -1.237  1.00 37.53           O  
ANISOU 4942  OD1 ASN A 641     4503   4503   5254     52    -13    182       O  
ATOM   4943  ND2 ASN A 641     130.654  64.088  -1.390  1.00 34.88           N  
ANISOU 4943  ND2 ASN A 641     4151   4191   4910     63    -20    187       N  
ATOM   4944  N   ASP A 642     125.134  65.897  -2.601  1.00 28.83           N  
ANISOU 4944  N   ASP A 642     3400   3464   4091     18     10    145       N  
ATOM   4945  CA  ASP A 642     123.877  66.663  -2.421  1.00 29.99           C  
ANISOU 4945  CA  ASP A 642     3549   3624   4221      7     14    139       C  
ATOM   4946  C   ASP A 642     122.710  65.855  -2.984  1.00 30.48           C  
ANISOU 4946  C   ASP A 642     3613   3681   4286      1     22    124       C  
ATOM   4947  O   ASP A 642     122.086  66.234  -3.966  1.00 30.68           O  
ANISOU 4947  O   ASP A 642     3633   3718   4305      2     27    108       O  
ATOM   4948  CB  ASP A 642     123.971  68.041  -3.109  1.00 29.12           C  
ANISOU 4948  CB  ASP A 642     3433   3534   4099     12     14    133       C  
ATOM   4949  CG  ASP A 642     122.740  68.912  -2.865  1.00 30.92           C  
ANISOU 4949  CG  ASP A 642     3664   3775   4312      3     16    128       C  
ATOM   4950  OD1 ASP A 642     121.982  68.714  -1.856  1.00 32.46           O  
ANISOU 4950  OD1 ASP A 642     3864   3966   4502     -8     15    133       O  
ATOM   4951  OD2 ASP A 642     122.488  69.796  -3.689  1.00 29.07           O  
ANISOU 4951  OD2 ASP A 642     3424   3553   4067      7     18    119       O  
ATOM   4952  N   PRO A 643     122.403  64.719  -2.363  1.00 31.77           N  
ANISOU 4952  N   PRO A 643     3784   3828   4458     -6     22    128       N  
ATOM   4953  CA  PRO A 643     121.433  63.773  -2.961  1.00 32.28           C  
ANISOU 4953  CA  PRO A 643     3851   3887   4529    -12     31    113       C  
ATOM   4954  C   PRO A 643     120.003  64.323  -3.203  1.00 33.05           C  
ANISOU 4954  C   PRO A 643     3947   4000   4612    -22     37     99       C  
ATOM   4955  O   PRO A 643     119.282  63.744  -3.984  1.00 31.28           O  
ANISOU 4955  O   PRO A 643     3720   3775   4390    -25     44     82       O  
ATOM   4956  CB  PRO A 643     121.398  62.592  -1.945  1.00 32.76           C  
ANISOU 4956  CB  PRO A 643     3923   3926   4599    -20     29    124       C  
ATOM   4957  CG  PRO A 643     121.964  63.157  -0.670  1.00 33.40           C  
ANISOU 4957  CG  PRO A 643     4008   4008   4673    -22     20    145       C  
ATOM   4958  CD  PRO A 643     122.954  64.227  -1.088  1.00 32.26           C  
ANISOU 4958  CD  PRO A 643     3855   3877   4525     -9     15    148       C  
ATOM   4959  N   GLU A 644     119.620  65.429  -2.574  1.00 33.53           N  
ANISOU 4959  N   GLU A 644     4008   4076   4658    -27     33    104       N  
ATOM   4960  CA  GLU A 644     118.248  65.970  -2.684  1.00 36.93           C  
ANISOU 4960  CA  GLU A 644     4435   4520   5074    -36     38     90       C  
ATOM   4961  C   GLU A 644     118.163  67.340  -3.357  1.00 34.25           C  
ANISOU 4961  C   GLU A 644     4089   4201   4724    -28     36     84       C  
ATOM   4962  O   GLU A 644     117.113  68.003  -3.289  1.00 35.08           O  
ANISOU 4962  O   GLU A 644     4192   4320   4817    -34     37     75       O  
ATOM   4963  CB  GLU A 644     117.629  66.063  -1.283  1.00 41.08           C  
ANISOU 4963  CB  GLU A 644     4970   5047   5593    -50     36    100       C  
ATOM   4964  CG  GLU A 644     117.710  64.757  -0.507  1.00 45.34           C  
ANISOU 4964  CG  GLU A 644     5519   5566   6142    -60     37    109       C  
ATOM   4965  CD  GLU A 644     117.082  64.850   0.875  1.00 53.45           C  
ANISOU 4965  CD  GLU A 644     6554   6594   7160    -76     36    119       C  
ATOM   4966  OE1 GLU A 644     117.441  65.740   1.706  1.00 55.56           O  
ANISOU 4966  OE1 GLU A 644     6823   6869   7418    -76     30    131       O  
ATOM   4967  OE2 GLU A 644     116.206  64.011   1.132  1.00 61.18           O  
ANISOU 4967  OE2 GLU A 644     7538   7567   8140    -90     42    113       O  
ATOM   4968  N   PHE A 645     119.257  67.736  -4.006  1.00 31.42           N  
ANISOU 4968  N   PHE A 645     3726   3843   4368    -15     33     87       N  
ATOM   4969  CA  PHE A 645     119.398  68.993  -4.679  1.00 29.79           C  
ANISOU 4969  CA  PHE A 645     3515   3653   4152     -8     31     83       C  
ATOM   4970  C   PHE A 645     119.053  70.120  -3.674  1.00 29.20           C  
ANISOU 4970  C   PHE A 645     3443   3588   4064    -13     26     92       C  
ATOM   4971  O   PHE A 645     118.175  70.971  -3.910  1.00 29.54           O  
ANISOU 4971  O   PHE A 645     3484   3645   4096    -14     26     82       O  
ATOM   4972  CB  PHE A 645     118.529  69.056  -5.938  1.00 30.07           C  
ANISOU 4972  CB  PHE A 645     3544   3698   4182     -5     36     63       C  
ATOM   4973  CG  PHE A 645     118.994  68.192  -7.069  1.00 29.77           C  
ANISOU 4973  CG  PHE A 645     3501   3654   4155      1     41     54       C  
ATOM   4974  CD1 PHE A 645     120.110  68.554  -7.841  1.00 29.96           C  
ANISOU 4974  CD1 PHE A 645     3522   3681   4181     12     40     56       C  
ATOM   4975  CD2 PHE A 645     118.286  67.031  -7.419  1.00 29.79           C  
ANISOU 4975  CD2 PHE A 645     3504   3650   4165     -5     47     41       C  
ATOM   4976  CE1 PHE A 645     120.529  67.730  -8.905  1.00 31.11           C  
ANISOU 4976  CE1 PHE A 645     3663   3821   4337     17     45     45       C  
ATOM   4977  CE2 PHE A 645     118.718  66.214  -8.460  1.00 29.20           C  
ANISOU 4977  CE2 PHE A 645     3425   3568   4100      1     52     31       C  
ATOM   4978  CZ  PHE A 645     119.816  66.572  -9.207  1.00 30.69           C  
ANISOU 4978  CZ  PHE A 645     3609   3760   4292     12     51     33       C  
ATOM   4979  N   ASN A 646     119.698  70.090  -2.531  1.00 26.89           N  
ANISOU 4979  N   ASN A 646     3156   3289   3774    -16     22    108       N  
ATOM   4980  CA  ASN A 646     119.492  71.102  -1.508  1.00 27.26           C  
ANISOU 4980  CA  ASN A 646     3205   3343   3808    -21     17    116       C  
ATOM   4981  C   ASN A 646     120.419  72.290  -1.665  1.00 28.03           C  
ANISOU 4981  C   ASN A 646     3301   3449   3901    -13     12    124       C  
ATOM   4982  O   ASN A 646     120.194  73.317  -0.984  1.00 29.28           O  
ANISOU 4982  O   ASN A 646     3461   3616   4048    -16      9    128       O  
ATOM   4983  CB  ASN A 646     119.647  70.527  -0.100  1.00 26.72           C  
ANISOU 4983  CB  ASN A 646     3144   3265   3742    -32     15    131       C  
ATOM   4984  CG  ASN A 646     118.517  69.597   0.306  1.00 27.21           C  
ANISOU 4984  CG  ASN A 646     3211   3323   3806    -44     20    124       C  
ATOM   4985  OD1 ASN A 646     117.369  69.712  -0.137  1.00 27.83           O  
ANISOU 4985  OD1 ASN A 646     3286   3410   3879    -48     25    109       O  
ATOM   4986  ND2 ASN A 646     118.831  68.690   1.201  1.00 28.37           N  
ANISOU 4986  ND2 ASN A 646     3364   3455   3959    -51     18    137       N  
ATOM   4987  N   LEU A 647     121.412  72.179  -2.549  1.00 26.61           N  
ANISOU 4987  N   LEU A 647     3116   3266   3727     -3     12    124       N  
ATOM   4988  CA  LEU A 647     122.442  73.217  -2.725  1.00 26.88           C  
ANISOU 4988  CA  LEU A 647     3149   3307   3758      4      8    131       C  
ATOM   4989  C   LEU A 647     122.408  73.780  -4.151  1.00 28.02           C  
ANISOU 4989  C   LEU A 647     3288   3459   3897     12     11    119       C  
ATOM   4990  O   LEU A 647     122.061  73.069  -5.147  1.00 27.94           O  
ANISOU 4990  O   LEU A 647     3275   3448   3892     15     16    107       O  
ATOM   4991  CB  LEU A 647     123.850  72.653  -2.446  1.00 27.86           C  
ANISOU 4991  CB  LEU A 647     3272   3421   3893      9      5    143       C  
ATOM   4992  CG  LEU A 647     124.112  72.167  -1.007  1.00 28.36           C  
ANISOU 4992  CG  LEU A 647     3340   3475   3960      2      0    158       C  
ATOM   4993  CD1 LEU A 647     125.489  71.552  -0.907  1.00 29.06           C  
ANISOU 4993  CD1 LEU A 647     3426   3554   4060      9     -4    168       C  
ATOM   4994  CD2 LEU A 647     123.960  73.222   0.085  1.00 28.45           C  
ANISOU 4994  CD2 LEU A 647     3356   3496   3959     -5     -5    167       C  
ATOM   4995  N   ARG A 648     122.772  75.052  -4.241  1.00 27.14           N  
ANISOU 4995  N   ARG A 648     3178   3358   3777     15      8    123       N  
ATOM   4996  CA  ARG A 648     122.867  75.745  -5.486  1.00 27.33           C  
ANISOU 4996  CA  ARG A 648     3199   3390   3794     22      9    115       C  
ATOM   4997  C   ARG A 648     124.173  75.373  -6.215  1.00 27.84           C  
ANISOU 4997  C   ARG A 648     3259   3451   3867     28     11    117       C  
ATOM   4998  O   ARG A 648     125.214  75.235  -5.595  1.00 31.69           O  
ANISOU 4998  O   ARG A 648     3746   3934   4361     28      9    128       O  
ATOM   4999  CB  ARG A 648     122.812  77.248  -5.232  1.00 25.73           C  
ANISOU 4999  CB  ARG A 648     3001   3196   3579     22      5    119       C  
ATOM   5000  CG  ARG A 648     121.482  77.778  -4.718  1.00 25.40           C  
ANISOU 5000  CG  ARG A 648     2963   3161   3529     17      4    114       C  
ATOM   5001  CD  ARG A 648     121.445  79.306  -4.811  1.00 24.73           C  
ANISOU 5001  CD  ARG A 648     2881   3084   3432     20      0    116       C  
ATOM   5002  NE  ARG A 648     122.521  79.960  -4.051  1.00 25.16           N  
ANISOU 5002  NE  ARG A 648     2938   3136   3485     18     -3    129       N  
ATOM   5003  CZ  ARG A 648     122.518  80.235  -2.735  1.00 25.92           C  
ANISOU 5003  CZ  ARG A 648     3037   3232   3580     11     -6    137       C  
ATOM   5004  NH1 ARG A 648     121.521  79.807  -1.921  1.00 25.58           N  
ANISOU 5004  NH1 ARG A 648     2995   3189   3537      5     -6    134       N  
ATOM   5005  NH2 ARG A 648     123.558  80.901  -2.193  1.00 25.88           N  
ANISOU 5005  NH2 ARG A 648     3034   3227   3573      9     -9    149       N  
ATOM   5006  N   ARG A 649     124.130  75.295  -7.538  1.00 27.63           N  
ANISOU 5006  N   ARG A 649     3229   3429   3839     33     15    105       N  
ATOM   5007  CA  ARG A 649     125.326  75.048  -8.331  1.00 25.80           C  
ANISOU 5007  CA  ARG A 649     2993   3197   3614     38     18    105       C  
ATOM   5008  C   ARG A 649     126.140  76.299  -8.686  1.00 25.42           C  
ANISOU 5008  C   ARG A 649     2945   3158   3555     40     17    110       C  
ATOM   5009  O   ARG A 649     126.493  76.484  -9.829  1.00 24.13           O  
ANISOU 5009  O   ARG A 649     2780   3001   3389     43     20    103       O  
ATOM   5010  CB  ARG A 649     124.960  74.267  -9.546  1.00 27.31           C  
ANISOU 5010  CB  ARG A 649     3179   3389   3808     41     24     90       C  
ATOM   5011  CG  ARG A 649     125.065  72.777  -9.363  1.00 28.85           C  
ANISOU 5011  CG  ARG A 649     3371   3571   4020     42     27     87       C  
ATOM   5012  CD  ARG A 649     124.098  72.245  -8.368  1.00 29.91           C  
ANISOU 5012  CD  ARG A 649     3510   3698   4157     36     25     89       C  
ATOM   5013  NE  ARG A 649     124.141  70.771  -8.282  1.00 29.60           N  
ANISOU 5013  NE  ARG A 649     3469   3645   4133     35     29     85       N  
ATOM   5014  CZ  ARG A 649     123.626  70.084  -7.269  1.00 32.03           C  
ANISOU 5014  CZ  ARG A 649     3782   3943   4447     29     27     90       C  
ATOM   5015  NH1 ARG A 649     123.107  70.706  -6.198  1.00 33.64           N  
ANISOU 5015  NH1 ARG A 649     3991   4150   4642     23     23     99       N  
ATOM   5016  NH2 ARG A 649     123.666  68.766  -7.281  1.00 33.17           N  
ANISOU 5016  NH2 ARG A 649     3926   4073   4605     29     30     87       N  
ATOM   5017  N   ASP A 650     126.477  77.106  -7.673  1.00 24.77           N  
ANISOU 5017  N   ASP A 650     2867   3076   3469     37     12    122       N  
ATOM   5018  CA  ASP A 650     127.271  78.316  -7.825  1.00 24.63           C  
ANISOU 5018  CA  ASP A 650     2851   3065   3442     36     10    128       C  
ATOM   5019  C   ASP A 650     128.738  77.892  -7.946  1.00 25.98           C  
ANISOU 5019  C   ASP A 650     3015   3235   3622     39     12    132       C  
ATOM   5020  O   ASP A 650     129.123  76.823  -7.448  1.00 25.14           O  
ANISOU 5020  O   ASP A 650     2903   3120   3529     40     11    134       O  
ATOM   5021  CB  ASP A 650     127.097  79.224  -6.606  1.00 24.05           C  
ANISOU 5021  CB  ASP A 650     2783   2992   3361     31      4    139       C  
ATOM   5022  CG  ASP A 650     125.647  79.768  -6.449  1.00 25.53           C  
ANISOU 5022  CG  ASP A 650     2977   3183   3540     30      3    134       C  
ATOM   5023  OD1 ASP A 650     124.957  79.954  -7.449  1.00 26.20           O  
ANISOU 5023  OD1 ASP A 650     3063   3273   3619     33      4    124       O  
ATOM   5024  OD2 ASP A 650     125.184  80.029  -5.312  1.00 26.92           O  
ANISOU 5024  OD2 ASP A 650     3157   3358   3714     25     -1    139       O  
ATOM   5025  N   ALA A 651     129.539  78.736  -8.601  1.00 26.44           N  
ANISOU 5025  N   ALA A 651     3073   3301   3673     38     13    133       N  
ATOM   5026  CA  ALA A 651     130.973  78.489  -8.784  1.00 26.01           C  
ANISOU 5026  CA  ALA A 651     3010   3247   3626     40     15    135       C  
ATOM   5027  C   ALA A 651     131.853  79.256  -7.815  1.00 25.00           C  
ANISOU 5027  C   ALA A 651     2881   3121   3495     36     11    147       C  
ATOM   5028  O   ALA A 651     131.400  80.182  -7.139  1.00 25.25           O  
ANISOU 5028  O   ALA A 651     2921   3154   3518     31      7    153       O  
ATOM   5029  CB  ALA A 651     131.348  78.882 -10.181  1.00 27.13           C  
ANISOU 5029  CB  ALA A 651     3150   3398   3761     40     22    126       C  
ATOM   5030  N   GLY A 652     133.130  78.908  -7.819  1.00 25.29           N  
ANISOU 5030  N   GLY A 652     2909   3159   3540     38     12    148       N  
ATOM   5031  CA  GLY A 652     134.175  79.702  -7.145  1.00 26.02           C  
ANISOU 5031  CA  GLY A 652     3000   3256   3629     33      9    158       C  
ATOM   5032  C   GLY A 652     135.536  79.446  -7.744  1.00 25.76           C  
ANISOU 5032  C   GLY A 652     2956   3229   3604     35     13    153       C  
ATOM   5033  O   GLY A 652     135.732  78.531  -8.554  1.00 25.19           O  
ANISOU 5033  O   GLY A 652     2876   3156   3540     41     17    144       O  
ATOM   5034  N   LEU A 653     136.468  80.281  -7.333  1.00 26.33           N  
ANISOU 5034  N   LEU A 653     3026   3309   3671     30     12    160       N  
ATOM   5035  CA  LEU A 653     137.873  80.131  -7.653  1.00 26.65           C  
ANISOU 5035  CA  LEU A 653     3053   3355   3717     31     14    157       C  
ATOM   5036  C   LEU A 653     138.553  80.063  -6.321  1.00 25.38           C  
ANISOU 5036  C   LEU A 653     2888   3193   3563     31      6    167       C  
ATOM   5037  O   LEU A 653     138.393  80.972  -5.513  1.00 24.76           O  
ANISOU 5037  O   LEU A 653     2817   3117   3475     24      2    176       O  
ATOM   5038  CB  LEU A 653     138.423  81.329  -8.449  1.00 27.77           C  
ANISOU 5038  CB  LEU A 653     3198   3509   3845     23     21    154       C  
ATOM   5039  CG  LEU A 653     139.894  81.221  -8.895  1.00 28.62           C  
ANISOU 5039  CG  LEU A 653     3292   3626   3958     22     25    148       C  
ATOM   5040  CD1 LEU A 653     140.101  80.225  -9.999  1.00 28.92           C  
ANISOU 5040  CD1 LEU A 653     3319   3665   4004     29     32    134       C  
ATOM   5041  CD2 LEU A 653     140.400  82.552  -9.402  1.00 30.73           C  
ANISOU 5041  CD2 LEU A 653     3563   3904   4209     10     30    148       C  
ATOM   5042  N   ILE A 654     139.332  79.019  -6.092  1.00 25.02           N  
ANISOU 5042  N   ILE A 654     2830   3144   3532     39      4    166       N  
ATOM   5043  CA  ILE A 654     140.111  78.916  -4.860  1.00 25.83           C  
ANISOU 5043  CA  ILE A 654     2927   3247   3640     40     -5    177       C  
ATOM   5044  C   ILE A 654     141.624  79.028  -5.149  1.00 27.26           C  
ANISOU 5044  C   ILE A 654     3092   3439   3825     40     -3    172       C  
ATOM   5045  O   ILE A 654     142.156  78.250  -5.946  1.00 27.59           O  
ANISOU 5045  O   ILE A 654     3124   3482   3879     48      1    161       O  
ATOM   5046  CB  ILE A 654     139.747  77.624  -4.083  1.00 26.35           C  
ANISOU 5046  CB  ILE A 654     2992   3299   3720     48    -12    182       C  
ATOM   5047  CG1 ILE A 654     138.220  77.583  -3.823  1.00 25.74           C  
ANISOU 5047  CG1 ILE A 654     2929   3213   3637     45    -13    185       C  
ATOM   5048  CG2 ILE A 654     140.529  77.508  -2.774  1.00 26.43           C  
ANISOU 5048  CG2 ILE A 654     2996   3309   3735     49    -22    194       C  
ATOM   5049  CD1 ILE A 654     137.737  76.293  -3.249  1.00 27.11           C  
ANISOU 5049  CD1 ILE A 654     3104   3372   3823     52    -18    189       C  
ATOM   5050  N   ILE A 655     142.303  79.946  -4.442  1.00 26.09           N  
ANISOU 5050  N   ILE A 655     2943   3299   3670     33     -6    179       N  
ATOM   5051  CA  ILE A 655     143.758  80.002  -4.459  1.00 27.59           C  
ANISOU 5051  CA  ILE A 655     3117   3501   3865     33     -6    175       C  
ATOM   5052  C   ILE A 655     144.271  79.048  -3.360  1.00 28.24           C  
ANISOU 5052  C   ILE A 655     3190   3577   3961     43    -17    183       C  
ATOM   5053  O   ILE A 655     143.936  79.209  -2.186  1.00 27.07           O  
ANISOU 5053  O   ILE A 655     3049   3426   3811     40    -26    196       O  
ATOM   5054  CB  ILE A 655     144.330  81.413  -4.199  1.00 29.18           C  
ANISOU 5054  CB  ILE A 655     3320   3715   4052     20     -4    179       C  
ATOM   5055  CG1 ILE A 655     143.648  82.433  -5.102  1.00 32.58           C  
ANISOU 5055  CG1 ILE A 655     3764   4147   4467     10      5    175       C  
ATOM   5056  CG2 ILE A 655     145.822  81.440  -4.527  1.00 29.25           C  
ANISOU 5056  CG2 ILE A 655     3310   3737   4065     19     -1    171       C  
ATOM   5057  CD1 ILE A 655     143.944  83.833  -4.658  1.00 36.24           C  
ANISOU 5057  CD1 ILE A 655     4235   4620   4917     -4      5    180       C  
ATOM   5058  N   ARG A 656     145.100  78.083  -3.755  1.00 27.47           N  
ANISOU 5058  N   ARG A 656     3077   3480   3879     54    -18    175       N  
ATOM   5059  CA  ARG A 656     145.626  77.103  -2.839  1.00 29.03           C  
ANISOU 5059  CA  ARG A 656     3267   3672   4093     65    -29    182       C  
ATOM   5060  C   ARG A 656     147.142  77.257  -2.795  1.00 30.30           C  
ANISOU 5060  C   ARG A 656     3408   3846   4258     67    -31    177       C  
ATOM   5061  O   ARG A 656     147.783  77.145  -3.806  1.00 30.64           O  
ANISOU 5061  O   ARG A 656     3439   3897   4305     69    -23    163       O  
ATOM   5062  CB  ARG A 656     145.274  75.685  -3.280  1.00 29.44           C  
ANISOU 5062  CB  ARG A 656     3316   3709   4161     79    -30    176       C  
ATOM   5063  CG  ARG A 656     145.997  74.613  -2.463  1.00 30.80           C  
ANISOU 5063  CG  ARG A 656     3478   3874   4351     92    -42    182       C  
ATOM   5064  CD  ARG A 656     145.393  73.243  -2.622  1.00 31.14           C  
ANISOU 5064  CD  ARG A 656     3525   3898   4410    104    -44    181       C  
ATOM   5065  NE  ARG A 656     144.108  73.147  -1.942  1.00 32.43           N  
ANISOU 5065  NE  ARG A 656     3707   4049   4566     99    -47    193       N  
ATOM   5066  CZ  ARG A 656     143.333  72.061  -1.897  1.00 34.80           C  
ANISOU 5066  CZ  ARG A 656     4015   4331   4877    106    -49    195       C  
ATOM   5067  NH1 ARG A 656     143.697  70.925  -2.486  1.00 33.88           N  
ANISOU 5067  NH1 ARG A 656     3890   4205   4778    119    -49    185       N  
ATOM   5068  NH2 ARG A 656     142.198  72.098  -1.197  1.00 35.56           N  
ANISOU 5068  NH2 ARG A 656     4128   4419   4966     99    -52    205       N  
ATOM   5069  N   ARG A 657     147.676  77.468  -1.601  1.00 32.77           N  
ANISOU 5069  N   ARG A 657     3718   4164   4571     66    -42    188       N  
ATOM   5070  CA  ARG A 657     149.094  77.698  -1.367  1.00 34.55           C  
ANISOU 5070  CA  ARG A 657     3924   4404   4799     67    -45    185       C  
ATOM   5071  C   ARG A 657     149.590  76.608  -0.390  1.00 36.74           C  
ANISOU 5071  C   ARG A 657     4193   4675   5093     82    -61    193       C  
ATOM   5072  O   ARG A 657     149.305  76.643   0.811  1.00 41.45           O  
ANISOU 5072  O   ARG A 657     4798   5267   5685     81    -71    208       O  
ATOM   5073  CB  ARG A 657     149.248  79.112  -0.849  1.00 35.08           C  
ANISOU 5073  CB  ARG A 657     3996   4484   4848     50    -44    190       C  
ATOM   5074  CG  ARG A 657     150.623  79.696  -0.892  1.00 37.31           C  
ANISOU 5074  CG  ARG A 657     4262   4786   5129     45    -43    183       C  
ATOM   5075  CD  ARG A 657     150.590  81.224  -0.735  1.00 37.20           C  
ANISOU 5075  CD  ARG A 657     4257   4784   5096     26    -37    185       C  
ATOM   5076  NE  ARG A 657     150.271  81.912  -1.959  1.00 35.26           N  
ANISOU 5076  NE  ARG A 657     4018   4540   4839     16    -22    176       N  
ATOM   5077  CZ  ARG A 657     150.179  83.234  -2.111  1.00 35.69           C  
ANISOU 5077  CZ  ARG A 657     4081   4601   4876     -1    -15    176       C  
ATOM   5078  NH1 ARG A 657     150.396  84.071  -1.084  1.00 33.28           N  
ANISOU 5078  NH1 ARG A 657     3779   4303   4563    -11    -20    184       N  
ATOM   5079  NH2 ARG A 657     149.859  83.731  -3.324  1.00 35.97           N  
ANISOU 5079  NH2 ARG A 657     4124   4638   4904     -8     -2    167       N  
ATOM   5080  N   LYS A 658     150.271  75.603  -0.906  1.00 36.04           N  
ANISOU 5080  N   LYS A 658     4089   4583   5021     97    -62    183       N  
ATOM   5081  CA  LYS A 658     150.715  74.452  -0.071  1.00 38.08           C  
ANISOU 5081  CA  LYS A 658     4341   4832   5297    114    -77    191       C  
ATOM   5082  C   LYS A 658     152.061  74.702   0.575  1.00 36.67           C  
ANISOU 5082  C   LYS A 658     4143   4669   5121    117    -86    192       C  
ATOM   5083  O   LYS A 658     152.785  75.594   0.155  1.00 35.33           O  
ANISOU 5083  O   LYS A 658     3962   4518   4943    107    -79    182       O  
ATOM   5084  CB  LYS A 658     150.843  73.182  -0.914  1.00 39.88           C  
ANISOU 5084  CB  LYS A 658     4559   5047   5545    130    -75    179       C  
ATOM   5085  CG  LYS A 658     149.519  72.610  -1.358  1.00 43.47           C  
ANISOU 5085  CG  LYS A 658     5032   5484   6002    131    -69    180       C  
ATOM   5086  CD  LYS A 658     149.712  71.685  -2.550  1.00 48.47           C  
ANISOU 5086  CD  LYS A 658     5654   6110   6650    143    -61    162       C  
ATOM   5087  CE  LYS A 658     148.797  70.492  -2.480  1.00 52.95           C  
ANISOU 5087  CE  LYS A 658     6234   6654   7230    152    -65    166       C  
ATOM   5088  NZ  LYS A 658     148.502  69.959  -3.843  1.00 57.29           N  
ANISOU 5088  NZ  LYS A 658     6781   7199   7787    156    -52    148       N  
ATOM   5089  N   ASN A 659     152.351  73.898   1.603  1.00 39.23           N  
ANISOU 5089  N   ASN A 659     4465   4985   5456    129   -103    204       N  
ATOM   5090  CA  ASN A 659     153.652  73.841   2.288  1.00 41.40           C  
ANISOU 5090  CA  ASN A 659     4721   5274   5737    137   -115    205       C  
ATOM   5091  C   ASN A 659     154.226  75.227   2.611  1.00 39.29           C  
ANISOU 5091  C   ASN A 659     4447   5029   5451    120   -112    204       C  
ATOM   5092  O   ASN A 659     155.358  75.525   2.302  1.00 35.54           O  
ANISOU 5092  O   ASN A 659     3952   4572   4980    120   -110    192       O  
ATOM   5093  CB  ASN A 659     154.641  73.006   1.450  1.00 45.30           C  
ANISOU 5093  CB  ASN A 659     5191   5769   6250    154   -114    187       C  
ATOM   5094  CG  ASN A 659     155.925  72.676   2.213  1.00 51.56           C  
ANISOU 5094  CG  ASN A 659     5964   6572   7054    167   -130    189       C  
ATOM   5095  OD1 ASN A 659     155.889  72.316   3.409  1.00 57.40           O  
ANISOU 5095  OD1 ASN A 659     6710   7306   7796    173   -147    207       O  
ATOM   5096  ND2 ASN A 659     157.075  72.817   1.535  1.00 53.29           N  
ANISOU 5096  ND2 ASN A 659     6159   6809   7280    170   -125    170       N  
ATOM   5097  N   THR A 660     153.401  76.061   3.245  1.00 36.54           N  
ANISOU 5097  N   THR A 660     4118   4681   5086    104   -111    216       N  
ATOM   5098  CA  THR A 660     153.712  77.461   3.408  1.00 37.29           C  
ANISOU 5098  CA  THR A 660     4211   4794   5163     85   -105    215       C  
ATOM   5099  C   THR A 660     153.456  77.816   4.855  1.00 36.89           C  
ANISOU 5099  C   THR A 660     4171   4744   5102     79   -118    233       C  
ATOM   5100  O   THR A 660     152.415  77.435   5.416  1.00 35.66           O  
ANISOU 5100  O   THR A 660     4033   4573   4944     79   -123    246       O  
ATOM   5101  CB  THR A 660     152.834  78.361   2.468  1.00 36.35           C  
ANISOU 5101  CB  THR A 660     4108   4675   5031     69    -88    208       C  
ATOM   5102  OG1 THR A 660     153.121  78.067   1.103  1.00 35.62           O  
ANISOU 5102  OG1 THR A 660     4006   4583   4946     74    -76    191       O  
ATOM   5103  CG2 THR A 660     153.077  79.820   2.693  1.00 36.89           C  
ANISOU 5103  CG2 THR A 660     4178   4759   5080     50    -82    208       C  
ATOM   5104  N   LYS A 661     154.361  78.610   5.415  1.00 35.30           N  
ANISOU 5104  N   LYS A 661     3958   4563   4893     70   -122    232       N  
ATOM   5105  CA  LYS A 661     154.248  79.085   6.795  1.00 37.81           C  
ANISOU 5105  CA  LYS A 661     4283   4885   5198     62   -133    248       C  
ATOM   5106  C   LYS A 661     153.704  80.527   6.867  1.00 34.91           C  
ANISOU 5106  C   LYS A 661     3929   4525   4811     39   -122    248       C  
ATOM   5107  O   LYS A 661     152.553  80.715   7.194  1.00 33.71           O  
ANISOU 5107  O   LYS A 661     3797   4362   4650     33   -121    257       O  
ATOM   5108  CB  LYS A 661     155.617  78.935   7.485  1.00 41.46           C  
ANISOU 5108  CB  LYS A 661     4724   5364   5666     69   -146    248       C  
ATOM   5109  CG  LYS A 661     155.596  79.246   8.964  1.00 46.05           C  
ANISOU 5109  CG  LYS A 661     5310   5951   6236     62   -161    264       C  
ATOM   5110  CD  LYS A 661     156.744  78.528   9.694  1.00 51.71           C  
ANISOU 5110  CD  LYS A 661     6008   6677   6964     77   -179    268       C  
ATOM   5111  CE  LYS A 661     158.075  79.157   9.377  1.00 55.73           C  
ANISOU 5111  CE  LYS A 661     6492   7210   7473     74   -176    253       C  
ATOM   5112  NZ  LYS A 661     159.157  78.671  10.297  1.00 61.44           N  
ANISOU 5112  NZ  LYS A 661     7197   7946   8203     86   -196    258       N  
ATOM   5113  N   ASN A 662     154.525  81.519   6.521  1.00 33.64           N  
ANISOU 5113  N   ASN A 662     3757   4383   4642     27   -114    237       N  
ATOM   5114  CA  ASN A 662     154.141  82.943   6.446  1.00 34.88           C  
ANISOU 5114  CA  ASN A 662     3926   4546   4780      6   -103    235       C  
ATOM   5115  C   ASN A 662     153.881  83.299   5.011  1.00 34.26           C  
ANISOU 5115  C   ASN A 662     3851   4465   4701      1    -86    222       C  
ATOM   5116  O   ASN A 662     154.631  82.919   4.163  1.00 34.76           O  
ANISOU 5116  O   ASN A 662     3899   4534   4774      8    -81    209       O  
ATOM   5117  CB  ASN A 662     155.216  83.883   7.010  1.00 34.08           C  
ANISOU 5117  CB  ASN A 662     3811   4466   4670     -7   -105    231       C  
ATOM   5118  CG  ASN A 662     155.581  83.540   8.459  1.00 36.98           C  
ANISOU 5118  CG  ASN A 662     4174   4840   5037     -3   -123    244       C  
ATOM   5119  OD1 ASN A 662     154.740  83.203   9.268  1.00 36.15           O  
ANISOU 5119  OD1 ASN A 662     4082   4723   4929      0   -131    258       O  
ATOM   5120  ND2 ASN A 662     156.857  83.597   8.770  1.00 39.35           N  
ANISOU 5120  ND2 ASN A 662     4453   5159   5340     -1   -130    239       N  
ATOM   5121  N   THR A 663     152.747  83.934   4.734  1.00 33.37           N  
ANISOU 5121  N   THR A 663     3760   4343   4578     -9    -77    224       N  
ATOM   5122  CA  THR A 663     152.426  84.386   3.384  1.00 33.72           C  
ANISOU 5122  CA  THR A 663     3810   4384   4618    -15    -61    213       C  
ATOM   5123  C   THR A 663     151.426  85.531   3.470  1.00 33.49           C  
ANISOU 5123  C   THR A 663     3802   4350   4572    -30    -54    217       C  
ATOM   5124  O   THR A 663     150.777  85.687   4.474  1.00 33.03           O  
ANISOU 5124  O   THR A 663     3755   4287   4509    -33    -61    229       O  
ATOM   5125  CB  THR A 663     151.886  83.248   2.497  1.00 36.28           C  
ANISOU 5125  CB  THR A 663     4135   4694   4956      1    -58    209       C  
ATOM   5126  OG1 THR A 663     151.871  83.671   1.128  1.00 36.84           O  
ANISOU 5126  OG1 THR A 663     4207   4767   5022     -5    -43    196       O  
ATOM   5127  CG2 THR A 663     150.498  82.834   2.893  1.00 36.64           C  
ANISOU 5127  CG2 THR A 663     4200   4722   5001      5    -62    220       C  
ATOM   5128  N   THR A 664     151.321  86.313   2.401  1.00 33.76           N  
ANISOU 5128  N   THR A 664     3842   4385   4598    -40    -40    208       N  
ATOM   5129  CA  THR A 664     150.413  87.428   2.315  1.00 33.03           C  
ANISOU 5129  CA  THR A 664     3771   4288   4492    -53    -33    211       C  
ATOM   5130  C   THR A 664     149.693  87.333   0.978  1.00 33.69           C  
ANISOU 5130  C   THR A 664     3864   4362   4575    -51    -23    205       C  
ATOM   5131  O   THR A 664     150.322  87.415  -0.048  1.00 34.15           O  
ANISOU 5131  O   THR A 664     3914   4427   4634    -53    -14    194       O  
ATOM   5132  CB  THR A 664     151.170  88.764   2.415  1.00 33.57           C  
ANISOU 5132  CB  THR A 664     3838   4370   4548    -72    -27    207       C  
ATOM   5133  OG1 THR A 664     151.860  88.825   3.658  1.00 31.92           O  
ANISOU 5133  OG1 THR A 664     3618   4171   4338    -75    -38    212       O  
ATOM   5134  CG2 THR A 664     150.219  89.975   2.383  1.00 33.36           C  
ANISOU 5134  CG2 THR A 664     3833   4335   4506    -85    -21    210       C  
ATOM   5135  N   PHE A 665     148.361  87.186   1.002  1.00 30.97           N  
ANISOU 5135  N   PHE A 665     3536   4002   4228    -47    -24    211       N  
ATOM   5136  CA  PHE A 665     147.599  87.199  -0.195  1.00 30.02           C  
ANISOU 5136  CA  PHE A 665     3426   3874   4106    -45    -14    205       C  
ATOM   5137  C   PHE A 665     147.230  88.648  -0.475  1.00 30.44           C  
ANISOU 5137  C   PHE A 665     3495   3927   4143    -61     -7    205       C  
ATOM   5138  O   PHE A 665     146.851  89.361   0.436  1.00 32.43           O  
ANISOU 5138  O   PHE A 665     3756   4177   4387    -68    -11    212       O  
ATOM   5139  CB  PHE A 665     146.335  86.410   0.002  1.00 30.62           C  
ANISOU 5139  CB  PHE A 665     3512   3934   4187    -34    -19    211       C  
ATOM   5140  CG  PHE A 665     146.553  84.930   0.197  1.00 30.81           C  
ANISOU 5140  CG  PHE A 665     3524   3954   4228    -19    -26    211       C  
ATOM   5141  CD1 PHE A 665     146.624  84.064  -0.906  1.00 32.01           C  
ANISOU 5141  CD1 PHE A 665     3669   4103   4390     -9    -21    202       C  
ATOM   5142  CD2 PHE A 665     146.663  84.398   1.465  1.00 31.88           C  
ANISOU 5142  CD2 PHE A 665     3655   4088   4368    -14    -38    221       C  
ATOM   5143  CE1 PHE A 665     146.773  82.688  -0.738  1.00 32.10           C  
ANISOU 5143  CE1 PHE A 665     3671   4109   4418      6    -28    203       C  
ATOM   5144  CE2 PHE A 665     146.833  83.016   1.646  1.00 33.16           C  
ANISOU 5144  CE2 PHE A 665     3808   4244   4546      1    -46    223       C  
ATOM   5145  CZ  PHE A 665     146.880  82.165   0.540  1.00 32.70           C  
ANISOU 5145  CZ  PHE A 665     3745   4182   4500     11    -40    214       C  
ATOM   5146  N   VAL A 666     147.354  89.082  -1.715  1.00 30.40           N  
ANISOU 5146  N   VAL A 666     3494   3925   4133    -66      4    196       N  
ATOM   5147  CA  VAL A 666     146.920  90.436  -2.132  1.00 29.86           C  
ANISOU 5147  CA  VAL A 666     3442   3854   4049    -79     11    197       C  
ATOM   5148  C   VAL A 666     146.018  90.317  -3.364  1.00 29.28           C  
ANISOU 5148  C   VAL A 666     3380   3771   3972    -75     17    193       C  
ATOM   5149  O   VAL A 666     146.412  89.734  -4.376  1.00 30.08           O  
ANISOU 5149  O   VAL A 666     3473   3877   4078    -71     23    185       O  
ATOM   5150  CB  VAL A 666     148.120  91.347  -2.506  1.00 29.26           C  
ANISOU 5150  CB  VAL A 666     3362   3792   3966    -95     19    191       C  
ATOM   5151  CG1 VAL A 666     147.665  92.757  -2.836  1.00 28.99           C  
ANISOU 5151  CG1 VAL A 666     3348   3753   3916   -109     26    192       C  
ATOM   5152  CG2 VAL A 666     149.130  91.376  -1.381  1.00 30.16           C  
ANISOU 5152  CG2 VAL A 666     3460   3917   4082    -99     13    192       C  
ATOM   5153  N   SER A 667     144.839  90.928  -3.303  1.00 27.84           N  
ANISOU 5153  N   SER A 667     3217   3578   3782    -76     16    198       N  
ATOM   5154  CA  SER A 667     143.908  90.845  -4.378  1.00 29.09           C  
ANISOU 5154  CA  SER A 667     3387   3729   3937    -71     21    195       C  
ATOM   5155  C   SER A 667     143.166  92.140  -4.618  1.00 29.07           C  
ANISOU 5155  C   SER A 667     3405   3720   3920    -80     23    198       C  
ATOM   5156  O   SER A 667     142.908  92.910  -3.680  1.00 28.93           O  
ANISOU 5156  O   SER A 667     3395   3699   3898    -85     19    204       O  
ATOM   5157  CB  SER A 667     142.869  89.771  -4.095  1.00 30.64           C  
ANISOU 5157  CB  SER A 667     3584   3916   4143    -57     14    197       C  
ATOM   5158  OG  SER A 667     143.483  88.547  -3.767  1.00 32.07           O  
ANISOU 5158  OG  SER A 667     3747   4100   4338    -48     11    195       O  
ATOM   5159  N   ILE A 668     142.816  92.356  -5.881  1.00 28.13           N  
ANISOU 5159  N   ILE A 668     3294   3598   3794    -80     30    194       N  
ATOM   5160  CA  ILE A 668     141.962  93.466  -6.268  1.00 29.33           C  
ANISOU 5160  CA  ILE A 668     3467   3742   3933    -85     31    197       C  
ATOM   5161  C   ILE A 668     140.744  92.950  -7.007  1.00 29.15           C  
ANISOU 5161  C   ILE A 668     3452   3711   3911    -73     29    195       C  
ATOM   5162  O   ILE A 668     140.830  92.035  -7.771  1.00 27.96           O  
ANISOU 5162  O   ILE A 668     3293   3564   3766    -67     32    189       O  
ATOM   5163  CB  ILE A 668     142.725  94.526  -7.098  1.00 31.48           C  
ANISOU 5163  CB  ILE A 668     3748   4020   4194   -100     40    195       C  
ATOM   5164  CG1 ILE A 668     143.716  95.272  -6.172  1.00 33.28           C  
ANISOU 5164  CG1 ILE A 668     3971   4254   4419   -113     40    197       C  
ATOM   5165  CG2 ILE A 668     141.757  95.499  -7.726  1.00 31.63           C  
ANISOU 5165  CG2 ILE A 668     3789   4028   4200   -102     40    198       C  
ATOM   5166  CD1 ILE A 668     144.335  96.522  -6.768  1.00 36.30           C  
ANISOU 5166  CD1 ILE A 668     4365   4638   4788   -131     48    197       C  
ATOM   5167  N   LEU A 669     139.601  93.547  -6.712  1.00 28.43           N  
ANISOU 5167  N   LEU A 669     3377   3611   3816    -70     25    199       N  
ATOM   5168  CA  LEU A 669     138.381  93.268  -7.410  1.00 30.51           C  
ANISOU 5168  CA  LEU A 669     3648   3867   4077    -60     23    197       C  
ATOM   5169  C   LEU A 669     137.867  94.565  -8.057  1.00 27.83           C  
ANISOU 5169  C   LEU A 669     3329   3522   3723    -65     24    199       C  
ATOM   5170  O   LEU A 669     137.510  95.527  -7.328  1.00 23.23           O  
ANISOU 5170  O   LEU A 669     2757   2933   3136    -69     20    204       O  
ATOM   5171  CB  LEU A 669     137.318  92.767  -6.447  1.00 34.87           C  
ANISOU 5171  CB  LEU A 669     4199   4412   4636    -51     15    199       C  
ATOM   5172  CG  LEU A 669     136.056  92.576  -7.288  1.00 45.15           C  
ANISOU 5172  CG  LEU A 669     5510   5708   5935    -41     14    195       C  
ATOM   5173  CD1 LEU A 669     136.187  91.333  -8.156  1.00 48.97           C  
ANISOU 5173  CD1 LEU A 669     5982   6197   6426    -34     17    188       C  
ATOM   5174  CD2 LEU A 669     134.942  92.373  -6.371  1.00 50.28           C  
ANISOU 5174  CD2 LEU A 669     6162   6352   6590    -34      7    196       C  
ATOM   5175  N   GLU A 670     137.866  94.591  -9.394  1.00 27.78           N  
ANISOU 5175  N   GLU A 670     3328   3517   3709    -66     29    196       N  
ATOM   5176  CA  GLU A 670     137.416  95.782 -10.142  1.00 28.95           C  
ANISOU 5176  CA  GLU A 670     3497   3660   3844    -71     29    199       C  
ATOM   5177  C   GLU A 670     136.021  95.545 -10.721  1.00 27.44           C  
ANISOU 5177  C   GLU A 670     3314   3463   3651    -58     24    197       C  
ATOM   5178  O   GLU A 670     135.690  94.447 -11.143  1.00 27.88           O  
ANISOU 5178  O   GLU A 670     3360   3522   3713    -49     24    191       O  
ATOM   5179  CB  GLU A 670     138.282  96.086 -11.357  1.00 29.58           C  
ANISOU 5179  CB  GLU A 670     3580   3747   3913    -81     38    197       C  
ATOM   5180  CG  GLU A 670     139.740  96.371 -11.147  1.00 33.87           C  
ANISOU 5180  CG  GLU A 670     4115   4298   4455    -96     46    197       C  
ATOM   5181  CD  GLU A 670     140.503  96.206 -12.484  1.00 34.18           C  
ANISOU 5181  CD  GLU A 670     4152   4348   4488   -104     55    192       C  
ATOM   5182  OE1 GLU A 670     141.006  95.085 -12.748  1.00 34.40           O  
ANISOU 5182  OE1 GLU A 670     4162   4386   4524   -100     59    184       O  
ATOM   5183  OE2 GLU A 670     140.550  97.193 -13.268  1.00 34.86           O  
ANISOU 5183  OE2 GLU A 670     4255   4432   4559   -114     59    195       O  
ATOM   5184  N   SER A 671     135.281  96.613 -10.877  1.00 26.75           N  
ANISOU 5184  N   SER A 671     3245   3366   3553    -57     20    201       N  
ATOM   5185  CA  SER A 671     134.070  96.625 -11.696  1.00 26.65           C  
ANISOU 5185  CA  SER A 671     3243   3349   3535    -46     15    199       C  
ATOM   5186  C   SER A 671     134.303  97.588 -12.879  1.00 28.23           C  
ANISOU 5186  C   SER A 671     3460   3548   3720    -54     18    203       C  
ATOM   5187  O   SER A 671     134.735  98.752 -12.681  1.00 28.86           O  
ANISOU 5187  O   SER A 671     3553   3621   3791    -64     19    209       O  
ATOM   5188  CB  SER A 671     132.896  97.109 -10.865  1.00 26.26           C  
ANISOU 5188  CB  SER A 671     3200   3289   3488    -38      6    201       C  
ATOM   5189  OG  SER A 671     131.680  97.127 -11.641  1.00 26.31           O  
ANISOU 5189  OG  SER A 671     3216   3293   3490    -26      0    198       O  
ATOM   5190  N   HIS A 672     133.997  97.137 -14.089  1.00 27.99           N  
ANISOU 5190  N   HIS A 672     3430   3521   3682    -50     20    199       N  
ATOM   5191  CA  HIS A 672     134.182  97.970 -15.281  1.00 29.23           C  
ANISOU 5191  CA  HIS A 672     3606   3679   3824    -57     22    204       C  
ATOM   5192  C   HIS A 672     133.306  97.582 -16.435  1.00 28.43           C  
ANISOU 5192  C   HIS A 672     3509   3580   3715    -48     19    200       C  
ATOM   5193  O   HIS A 672     133.024  96.397 -16.668  1.00 27.92           O  
ANISOU 5193  O   HIS A 672     3429   3522   3658    -40     20    192       O  
ATOM   5194  CB  HIS A 672     135.664  97.951 -15.732  1.00 29.99           C  
ANISOU 5194  CB  HIS A 672     3695   3784   3915    -74     34    203       C  
ATOM   5195  CG  HIS A 672     136.213  96.573 -15.838  1.00 30.75           C  
ANISOU 5195  CG  HIS A 672     3769   3893   4022    -72     40    194       C  
ATOM   5196  ND1 HIS A 672     136.128  95.819 -16.990  1.00 32.33           N  
ANISOU 5196  ND1 HIS A 672     3965   4102   4219    -69     44    187       N  
ATOM   5197  CD2 HIS A 672     136.779  95.767 -14.907  1.00 33.20           C  
ANISOU 5197  CD2 HIS A 672     4060   4207   4347    -71     42    190       C  
ATOM   5198  CE1 HIS A 672     136.679  94.629 -16.784  1.00 31.89           C  
ANISOU 5198  CE1 HIS A 672     3887   4054   4176    -67     49    179       C  
ATOM   5199  NE2 HIS A 672     137.079  94.567 -15.529  1.00 32.99           N  
ANISOU 5199  NE2 HIS A 672     4017   4191   4327    -67     47    181       N  
ATOM   5200  N   GLY A 673     132.899  98.594 -17.192  1.00 27.33           N  
ANISOU 5200  N   GLY A 673     3365   3332   3688   -172     17    -68       N  
ATOM   5201  CA  GLY A 673     132.204  98.369 -18.381  1.00 30.34           C  
ANISOU 5201  CA  GLY A 673     3748   3704   4075   -178     16    -56       C  
ATOM   5202  C   GLY A 673     130.795  97.825 -18.276  1.00 30.71           C  
ANISOU 5202  C   GLY A 673     3765   3794   4110   -159     34    -85       C  
ATOM   5203  O   GLY A 673     130.220  97.716 -17.202  1.00 32.06           O  
ANISOU 5203  O   GLY A 673     3891   4047   4242   -155     45   -121       O  
ATOM   5204  N   HIS A 674     130.263  97.495 -19.439  1.00 32.75           N  
ANISOU 5204  N   HIS A 674     4029   4036   4377   -165     37    -67       N  
ATOM   5205  CA  HIS A 674     128.820  97.192 -19.571  1.00 37.01           C  
ANISOU 5205  CA  HIS A 674     4540   4620   4904   -151     44    -94       C  
ATOM   5206  C   HIS A 674     128.660  96.327 -20.840  1.00 34.02           C  
ANISOU 5206  C   HIS A 674     4176   4216   4536   -172     57    -54       C  
ATOM   5207  O   HIS A 674     129.457  96.421 -21.795  1.00 31.48           O  
ANISOU 5207  O   HIS A 674     3866   3873   4220   -185     52    -38       O  
ATOM   5208  CB  HIS A 674     127.897  98.479 -19.560  1.00 39.61           C  
ANISOU 5208  CB  HIS A 674     4848   4945   5257    -84    -18   -183       C  
ATOM   5209  CG  HIS A 674     126.439  98.196 -19.244  1.00 53.95           C  
ANISOU 5209  CG  HIS A 674     6584   6887   7026    -58     -2   -260       C  
ATOM   5210  ND1 HIS A 674     125.919  98.187 -17.958  1.00 59.80           N  
ANISOU 5210  ND1 HIS A 674     7223   7813   7686    -53     16   -349       N  
ATOM   5211  CD2 HIS A 674     125.388  97.909 -20.066  1.00 58.67           C  
ANISOU 5211  CD2 HIS A 674     7168   7501   7624    -53      0   -267       C  
ATOM   5212  CE1 HIS A 674     124.628  97.889 -18.003  1.00 61.70           C  
ANISOU 5212  CE1 HIS A 674     7377   8204   7862    -56     31   -408       C  
ATOM   5213  NE2 HIS A 674     124.283  97.710 -19.269  1.00 61.13           N  
ANISOU 5213  NE2 HIS A 674     7367   8009   7850    -49     21   -356       N  
ATOM   5214  N   TYR A 675     127.625  95.473 -20.792  1.00 30.08           N  
ANISOU 5214  N   TYR A 675     3656   3755   4017   -190     65    -45       N  
ATOM   5215  CA  TYR A 675     127.185  94.686 -21.943  1.00 27.41           C  
ANISOU 5215  CA  TYR A 675     3327   3391   3697   -195     59    -28       C  
ATOM   5216  C   TYR A 675     125.674  94.737 -21.969  1.00 27.49           C  
ANISOU 5216  C   TYR A 675     3306   3460   3677   -201     68    -39       C  
ATOM   5217  O   TYR A 675     125.047  94.626 -20.937  1.00 26.55           O  
ANISOU 5217  O   TYR A 675     3140   3447   3499   -238     72    -44       O  
ATOM   5218  CB  TYR A 675     127.648  93.228 -21.919  1.00 25.98           C  
ANISOU 5218  CB  TYR A 675     3162   3167   3542   -217      6     -1       C  
ATOM   5219  CG  TYR A 675     127.248  92.532 -23.177  1.00 25.80           C  
ANISOU 5219  CG  TYR A 675     3139   3117   3548   -195    -19    -21       C  
ATOM   5220  CD1 TYR A 675     127.930  92.802 -24.374  1.00 26.58           C  
ANISOU 5220  CD1 TYR A 675     3209   3241   3648   -152      1    -83       C  
ATOM   5221  CD2 TYR A 675     126.104  91.709 -23.240  1.00 25.41           C  
ANISOU 5221  CD2 TYR A 675     3100   3056   3499   -237    -61     23       C  
ATOM   5222  CE1 TYR A 675     127.532  92.239 -25.567  1.00 25.94           C  
ANISOU 5222  CE1 TYR A 675     3104   3175   3576   -129    -16   -123       C  
ATOM   5223  CE2 TYR A 675     125.691  91.146 -24.427  1.00 24.87           C  
ANISOU 5223  CE2 TYR A 675     3030   2958   3463   -206    -87     -6       C  
ATOM   5224  CZ  TYR A 675     126.422  91.403 -25.601  1.00 25.82           C  
ANISOU 5224  CZ  TYR A 675     3115   3103   3590   -140    -61    -91       C  
ATOM   5225  OH  TYR A 675     126.052  90.845 -26.824  1.00 25.14           O  
ANISOU 5225  OH  TYR A 675     3005   3026   3520   -106    -85   -144       O  
ATOM   5226  N   SER A 676     125.111  94.944 -23.153  1.00 27.69           N  
ANISOU 5226  N   SER A 676     3340   3456   3726   -177     68    -50       N  
ATOM   5227  CA  SER A 676     123.668  94.907 -23.346  1.00 29.25           C  
ANISOU 5227  CA  SER A 676     3502   3713   3900   -174     71    -72       C  
ATOM   5228  C   SER A 676     123.350  93.937 -24.472  1.00 27.20           C  
ANISOU 5228  C   SER A 676     3265   3411   3658   -194     68    -31       C  
ATOM   5229  O   SER A 676     123.864  94.110 -25.550  1.00 25.01           O  
ANISOU 5229  O   SER A 676     3009   3082   3410   -175     66    -33       O  
ATOM   5230  CB  SER A 676     123.142  96.290 -23.756  1.00 30.12           C  
ANISOU 5230  CB  SER A 676     3606   3797   4042   -104     32   -146       C  
ATOM   5231  OG  SER A 676     121.832  96.127 -24.261  1.00 30.67           O  
ANISOU 5231  OG  SER A 676     3640   3912   4100    -90     30   -178       O  
ATOM   5232  N   PRO A 677     122.471  92.944 -24.236  1.00 27.69           N  
ANISOU 5232  N   PRO A 677     3310   3522   3688   -251     53      8       N  
ATOM   5233  CA  PRO A 677     122.046  92.119 -25.399  1.00 27.31           C  
ANISOU 5233  CA  PRO A 677     3285   3417   3673   -252     28     29       C  
ATOM   5234  C   PRO A 677     120.996  92.805 -26.338  1.00 27.02           C  
ANISOU 5234  C   PRO A 677     3229   3404   3634   -215     61     -8       C  
ATOM   5235  O   PRO A 677     120.466  92.157 -27.240  1.00 27.32           O  
ANISOU 5235  O   PRO A 677     3277   3417   3686   -221     49      8       O  
ATOM   5236  CB  PRO A 677     121.421  90.863 -24.711  1.00 28.40           C  
ANISOU 5236  CB  PRO A 677     3426   3587   3778   -362    -45    114       C  
ATOM   5237  CG  PRO A 677     120.858  91.406 -23.391  1.00 29.24           C  
ANISOU 5237  CG  PRO A 677     3459   3874   3775   -432     -6    120       C  
ATOM   5238  CD  PRO A 677     121.808  92.525 -22.965  1.00 27.64           C  
ANISOU 5238  CD  PRO A 677     3252   3656   3594   -346     41     45       C  
ATOM   5239  N   VAL A 678     120.613  94.056 -26.060  1.00 26.53           N  
ANISOU 5239  N   VAL A 678     3137   3380   3562   -169     72    -69       N  
ATOM   5240  CA  VAL A 678     119.699  94.820 -26.911  1.00 26.11           C  
ANISOU 5240  CA  VAL A 678     3077   3311   3533   -122     49   -116       C  
ATOM   5241  C   VAL A 678     120.533  95.572 -27.972  1.00 26.93           C  
ANISOU 5241  C   VAL A 678     3241   3305   3687   -121      9    -84       C  
ATOM   5242  O   VAL A 678     120.286  95.491 -29.173  1.00 26.86           O  
ANISOU 5242  O   VAL A 678     3251   3270   3686   -143     -2    -52       O  
ATOM   5243  CB  VAL A 678     118.856  95.797 -26.063  1.00 27.57           C  
ANISOU 5243  CB  VAL A 678     3187   3587   3702    -53     13   -240       C  
ATOM   5244  CG1 VAL A 678     117.927  96.637 -26.961  1.00 28.21           C  
ANISOU 5244  CG1 VAL A 678     3269   3609   3841     20    -66   -311       C  
ATOM   5245  CG2 VAL A 678     118.012  95.047 -25.020  1.00 28.05           C  
ANISOU 5245  CG2 VAL A 678     3142   3866   3649   -107     61   -267       C  
ATOM   5246  N   SER A 679     121.546  96.293 -27.519  1.00 27.10           N  
ANISOU 5246  N   SER A 679     3284   3290   3721   -124    -22    -79       N  
ATOM   5247  CA  SER A 679     122.414  97.010 -28.427  1.00 27.32           C  
ANISOU 5247  CA  SER A 679     3357   3267   3758   -184    -79    -15       C  
ATOM   5248  C   SER A 679     123.540  96.098 -28.974  1.00 26.53           C  
ANISOU 5248  C   SER A 679     3233   3247   3601   -241    -10     19       C  
ATOM   5249  O   SER A 679     124.153  96.442 -29.981  1.00 27.44           O  
ANISOU 5249  O   SER A 679     3341   3417   3669   -326    -36     68       O  
ATOM   5250  CB  SER A 679     122.979  98.234 -27.725  1.00 26.91           C  
ANISOU 5250  CB  SER A 679     3338   3146   3743   -176   -176    -22       C  
ATOM   5251  OG  SER A 679     123.987  97.816 -26.823  1.00 27.34           O  
ANISOU 5251  OG  SER A 679     3375   3246   3767   -178   -106    -25       O  
ATOM   5252  N   GLU A 680     123.813  94.987 -28.288  1.00 26.86           N  
ANISOU 5252  N   GLU A 680     3251   3312   3640   -203     46    -16       N  
ATOM   5253  CA  GLU A 680     124.982  94.140 -28.516  1.00 27.32           C  
ANISOU 5253  CA  GLU A 680     3275   3431   3677   -205     63    -47       C  
ATOM   5254  C   GLU A 680     126.353  94.866 -28.457  1.00 28.82           C  
ANISOU 5254  C   GLU A 680     3445   3683   3821   -253     58    -38       C  
ATOM   5255  O   GLU A 680     127.314  94.414 -29.090  1.00 28.67           O  
ANISOU 5255  O   GLU A 680     3356   3791   3748   -267     67    -92       O  
ATOM   5256  CB  GLU A 680     124.802  93.346 -29.812  1.00 28.46           C  
ANISOU 5256  CB  GLU A 680     3374   3640   3801   -201     64    -90       C  
ATOM   5257  CG  GLU A 680     123.542  92.479 -29.769  1.00 29.13           C  
ANISOU 5257  CG  GLU A 680     3484   3652   3934   -165     51    -88       C  
ATOM   5258  CD  GLU A 680     123.390  91.548 -30.974  1.00 30.87           C  
ANISOU 5258  CD  GLU A 680     3659   3916   4153   -138     28   -153       C  
ATOM   5259  OE1 GLU A 680     123.755  91.953 -32.106  1.00 32.05           O  
ANISOU 5259  OE1 GLU A 680     3751   4191   4237   -171     50   -181       O  
ATOM   5260  OE2 GLU A 680     122.890  90.407 -30.783  1.00 30.39           O  
ANISOU 5260  OE2 GLU A 680     3619   3779   4151   -101    -33   -172       O  
ATOM   5261  N   PHE A 681     126.447  95.929 -27.653  1.00 29.35           N  
ANISOU 5261  N   PHE A 681     3559   3687   3907   -269     31      6       N  
ATOM   5262  CA  PHE A 681     127.711  96.653 -27.374  1.00 31.69           C  
ANISOU 5262  CA  PHE A 681     3852   4023   4167   -328      9     36       C  
ATOM   5263  C   PHE A 681     128.358  96.197 -26.071  1.00 30.11           C  
ANISOU 5263  C   PHE A 681     3652   3797   3994   -267     39     -7       C  
ATOM   5264  O   PHE A 681     127.730  96.203 -25.016  1.00 29.46           O  
ANISOU 5264  O   PHE A 681     3598   3642   3955   -217     41    -17       O  
ATOM   5265  CB  PHE A 681     127.478  98.187 -27.312  1.00 35.74           C  
ANISOU 5265  CB  PHE A 681     4432   4442   4707   -386   -101    112       C  
ATOM   5266  CG  PHE A 681     127.590  98.878 -28.645  1.00 43.94           C  
ANISOU 5266  CG  PHE A 681     5475   5535   5684   -536   -187    214       C  
ATOM   5267  CD1 PHE A 681     128.848  99.221 -29.172  1.00 51.23           C  
ANISOU 5267  CD1 PHE A 681     6354   6617   6492   -695   -210    289       C  
ATOM   5268  CD2 PHE A 681     126.452  99.208 -29.390  1.00 48.28           C  
ANISOU 5268  CD2 PHE A 681     6062   6011   6271   -548   -260    245       C  
ATOM   5269  CE1 PHE A 681     128.956  99.874 -30.422  1.00 55.59           C  
ANISOU 5269  CE1 PHE A 681     6898   7278   6945   -901   -310    420       C  
ATOM   5270  CE2 PHE A 681     126.550  99.854 -30.626  1.00 49.90           C  
ANISOU 5270  CE2 PHE A 681     6278   6271   6409   -727   -369    371       C  
ATOM   5271  CZ  PHE A 681     127.801 100.190 -31.144  1.00 55.53           C  
ANISOU 5271  CZ  PHE A 681     6946   7167   6986   -923   -398    472       C  
ATOM   5272  N   SER A 682     129.616  95.791 -26.155  1.00 28.54           N  
ANISOU 5272  N   SER A 682     3399   3693   3751   -280     56    -44       N  
ATOM   5273  CA  SER A 682     130.456  95.494 -25.018  1.00 29.40           C  
ANISOU 5273  CA  SER A 682     3511   3777   3882   -240     61    -75       C  
ATOM   5274  C   SER A 682     131.442  96.702 -24.848  1.00 31.01           C  
ANISOU 5274  C   SER A 682     3718   4026   4037   -321     43    -20       C  
ATOM   5275  O   SER A 682     132.196  96.978 -25.762  1.00 33.32           O  
ANISOU 5275  O   SER A 682     3949   4474   4239   -411     38    -10       O  
ATOM   5276  CB  SER A 682     131.223  94.212 -25.368  1.00 30.49           C  
ANISOU 5276  CB  SER A 682     3574   3992   4019   -180     48   -189       C  
ATOM   5277  OG  SER A 682     132.128  93.858 -24.370  1.00 31.29           O  
ANISOU 5277  OG  SER A 682     3676   4061   4151   -140     23   -226       O  
ATOM   5278  N   VAL A 683     131.410  97.408 -23.713  1.00 32.64           N  
ANISOU 5278  N   VAL A 683     3984   4130   4288   -306     21     11       N  
ATOM   5279  CA  VAL A 683     132.272  98.595 -23.406  1.00 32.58           C  
ANISOU 5279  CA  VAL A 683     4001   4117   4259   -380    -34     71       C  
ATOM   5280  C   VAL A 683     133.166  98.304 -22.184  1.00 30.75           C  
ANISOU 5280  C   VAL A 683     3763   3880   4040   -333     -1     32       C  
ATOM   5281  O   VAL A 683     132.686  97.637 -21.257  1.00 27.48           O  
ANISOU 5281  O   VAL A 683     3359   3410   3672   -254     29    -10       O  
ATOM   5282  CB  VAL A 683     131.410  99.861 -23.108  1.00 34.57           C  
ANISOU 5282  CB  VAL A 683     4332   4221   4580   -376   -146    108       C  
ATOM   5283  CG1 VAL A 683     132.286 101.101 -22.988  1.00 34.39           C  
ANISOU 5283  CG1 VAL A 683     4355   4158   4552   -475   -269    190       C  
ATOM   5284  CG2 VAL A 683     130.417 100.100 -24.254  1.00 35.61           C  
ANISOU 5284  CG2 VAL A 683     4481   4329   4720   -412   -204    144       C  
ATOM   5285  N   ASN A 684     134.436  98.774 -22.247  1.00 28.81           N  
ANISOU 5285  N   ASN A 684     3492   3719   3735   -411    -17     62       N  
ATOM   5286  CA AASN A 684     135.427  98.701 -21.197  0.50 28.86           C  
ANISOU 5286  CA AASN A 684     3493   3726   3746   -384      1     36       C  
ATOM   5287  CA BASN A 684     135.454  98.702 -21.147  0.50 30.04           C  
ANISOU 5287  CA BASN A 684     3643   3873   3897   -382      1     35       C  
ATOM   5288  C   ASN A 684     135.438  97.332 -20.523  1.00 28.86           C  
ANISOU 5288  C   ASN A 684     3471   3703   3792   -276     46    -52       C  
ATOM   5289  O   ASN A 684     135.208  97.190 -19.337  1.00 27.79           O  
ANISOU 5289  O   ASN A 684     3376   3481   3704   -234     45    -50       O  
ATOM   5290  CB AASN A 684     135.224  99.900 -20.249  0.50 28.67           C  
ANISOU 5290  CB AASN A 684     3550   3568   3778   -385    -69     83       C  
ATOM   5291  CB BASN A 684     135.294  99.827 -20.054  0.50 31.24           C  
ANISOU 5291  CB BASN A 684     3873   3889   4107   -373    -61     75       C  
ATOM   5292  CG AASN A 684     135.490 101.247 -20.948  0.50 28.50           C  
ANISOU 5292  CG AASN A 684     3570   3529   3730   -522   -198    193       C  
ATOM   5293  CG BASN A 684     136.578 100.042 -19.175  0.50 32.31           C  
ANISOU 5293  CG BASN A 684     4003   4049   4225   -389    -56     77       C  
ATOM   5294  OD1AASN A 684     134.808 102.259 -20.705  0.50 28.98           O  
ANISOU 5294  OD1AASN A 684     3707   3434   3871   -507   -330    214       O  
ATOM   5295  OD1BASN A 684     137.676  99.609 -19.546  0.50 33.86           O  
ANISOU 5295  OD1BASN A 684     4133   4382   4351   -433    -21     62       O  
ATOM   5296  ND2AASN A 684     136.433 101.241 -21.845  0.50 28.03           N  
ANISOU 5296  ND2AASN A 684     3451   3645   3555   -662   -194    253       N  
ATOM   5297  ND2BASN A 684     136.432 100.721 -18.013  0.50 30.18           N  
ANISOU 5297  ND2BASN A 684     3783   3674   4011   -343    -98     67       N  
ATOM   5298  N   ALA A 685     135.674  96.319 -21.351  1.00 30.39           N  
ANISOU 5298  N   ALA A 685     3594   3988   3966   -245     52   -132       N  
ATOM   5299  CA  ALA A 685     135.604  94.919 -20.933  1.00 30.67           C  
ANISOU 5299  CA  ALA A 685     3624   3956   4073   -150     13   -213       C  
ATOM   5300  C   ALA A 685     136.896  94.381 -20.377  1.00 30.69           C  
ANISOU 5300  C   ALA A 685     3584   3984   4092    -99    -32   -300       C  
ATOM   5301  O   ALA A 685     136.871  93.337 -19.762  1.00 31.30           O  
ANISOU 5301  O   ALA A 685     3692   3946   4256    -37   -122   -336       O  
ATOM   5302  CB  ALA A 685     135.075  94.012 -22.055  1.00 31.35           C  
ANISOU 5302  CB  ALA A 685     3663   4078   4170   -104    -16   -291       C  
ATOM   5303  N   ASN A 686     137.995  95.115 -20.509  1.00 32.38           N  
ANISOU 5303  N   ASN A 686     3737   4339   4226   -143      3   -318       N  
ATOM   5304  CA  ASN A 686     139.279  94.694 -19.892  1.00 34.28           C  
ANISOU 5304  CA  ASN A 686     3928   4618   4480    -88    -39   -415       C  
ATOM   5305  C   ASN A 686     139.559  95.347 -18.514  1.00 31.54           C  
ANISOU 5305  C   ASN A 686     3669   4157   4157   -125    -23   -309       C  
ATOM   5306  O   ASN A 686     139.047  96.417 -18.194  1.00 31.72           O  
ANISOU 5306  O   ASN A 686     3758   4133   4160   -199     22   -188       O  
ATOM   5307  CB  ASN A 686     140.468  94.967 -20.859  1.00 37.21           C  
ANISOU 5307  CB  ASN A 686     4134   5291   4714   -120    -14   -533       C  
ATOM   5308  CG  ASN A 686     140.506  94.030 -22.076  1.00 41.65           C  
ANISOU 5308  CG  ASN A 686     4550   6031   5244    -36    -55   -732       C  
ATOM   5309  OD1 ASN A 686     140.881  94.464 -23.149  1.00 46.56           O  
ANISOU 5309  OD1 ASN A 686     5033   6953   5706   -125     -5   -776       O  
ATOM   5310  ND2 ASN A 686     140.175  92.746 -21.912  1.00 42.42           N  
ANISOU 5310  ND2 ASN A 686     4667   5966   5483    120   -173   -858       N  
ATOM   5311  N   SER A 687     140.387  94.690 -17.717  1.00 30.88           N  
ANISOU 5311  N   SER A 687     3578   4028   4127    -62    -88   -377       N  
ATOM   5312  CA  SER A 687     140.911  95.237 -16.471  1.00 30.04           C  
ANISOU 5312  CA  SER A 687     3527   3858   4028    -95    -74   -304       C  
ATOM   5313  C   SER A 687     141.713  96.518 -16.812  1.00 30.56           C  
ANISOU 5313  C   SER A 687     3546   4079   3986   -180     -3   -271       C  
ATOM   5314  O   SER A 687     142.239  96.626 -17.913  1.00 30.65           O  
ANISOU 5314  O   SER A 687     3449   4292   3905   -213     13   -337       O  
ATOM   5315  CB  SER A 687     141.803  94.205 -15.795  1.00 30.37           C  
ANISOU 5315  CB  SER A 687     3554   3838   4146    -12   -188   -401       C  
ATOM   5316  OG  SER A 687     142.609  94.759 -14.727  1.00 31.13           O  
ANISOU 5316  OG  SER A 687     3676   3920   4230    -44   -168   -355       O  
ATOM   5317  N   SER A 688     141.771  97.446 -15.862  1.00 29.17           N  
ANISOU 5317  N   SER A 688     3542   3729   3814   -136     78    188       N  
ATOM   5318  CA  SER A 688     142.697  98.580 -15.891  1.00 30.07           C  
ANISOU 5318  CA  SER A 688     3664   3843   3916   -156     85    192       C  
ATOM   5319  C   SER A 688     143.922  98.338 -14.996  1.00 31.46           C  
ANISOU 5319  C   SER A 688     3821   4030   4103   -164     90    187       C  
ATOM   5320  O   SER A 688     144.727  99.242 -14.828  1.00 32.63           O  
ANISOU 5320  O   SER A 688     3974   4180   4243   -182     95    189       O  
ATOM   5321  CB  SER A 688     141.967  99.873 -15.473  1.00 29.61           C  
ANISOU 5321  CB  SER A 688     3632   3769   3851   -158     78    203       C  
ATOM   5322  OG  SER A 688     140.996 100.197 -16.465  1.00 30.14           O  
ANISOU 5322  OG  SER A 688     3718   3829   3906   -153     74    208       O  
ATOM   5323  N   ILE A 689     144.101  97.141 -14.440  1.00 32.89           N  
ANISOU 5323  N   ILE A 689     3978   4217   4300   -153     87    180       N  
ATOM   5324  CA  ILE A 689     145.322  96.879 -13.653  1.00 35.71           C  
ANISOU 5324  CA  ILE A 689     4316   4586   4668   -159     91    176       C  
ATOM   5325  C   ILE A 689     146.464  96.529 -14.578  1.00 36.06           C  
ANISOU 5325  C   ILE A 689     4346   4647   4708   -170    103    165       C  
ATOM   5326  O   ILE A 689     146.365  95.615 -15.346  1.00 36.26           O  
ANISOU 5326  O   ILE A 689     4363   4678   4737   -163    106    158       O  
ATOM   5327  CB  ILE A 689     145.203  95.714 -12.621  1.00 38.40           C  
ANISOU 5327  CB  ILE A 689     4636   4927   5028   -143     83    173       C  
ATOM   5328  CG1 ILE A 689     144.110  96.004 -11.578  1.00 39.39           C  
ANISOU 5328  CG1 ILE A 689     4771   5037   5156   -133     71    182       C  
ATOM   5329  CG2 ILE A 689     146.540  95.481 -11.906  1.00 39.03           C  
ANISOU 5329  CG2 ILE A 689     4695   5020   5116   -150     86    168       C  
ATOM   5330  CD1 ILE A 689     144.463  97.109 -10.601  1.00 41.48           C  
ANISOU 5330  CD1 ILE A 689     5044   5299   5417   -144     70    188       C  
ATOM   5331  N   SER A 690     147.579  97.231 -14.445  1.00 36.42           N  
ANISOU 5331  N   SER A 690     4389   4701   4747   -189    111    163       N  
ATOM   5332  CA  SER A 690     148.788  96.827 -15.110  1.00 36.65           C  
ANISOU 5332  CA  SER A 690     4401   4749   4776   -199    122    151       C  
ATOM   5333  C   SER A 690     149.539  95.837 -14.208  1.00 38.91           C  
ANISOU 5333  C   SER A 690     4658   5044   5081   -190    119    144       C  
ATOM   5334  O   SER A 690     150.044  94.858 -14.673  1.00 37.89           O  
ANISOU 5334  O   SER A 690     4510   4927   4960   -185    123    133       O  
ATOM   5335  CB  SER A 690     149.640  98.044 -15.404  1.00 37.54           C  
ANISOU 5335  CB  SER A 690     4525   4867   4873   -225    132    152       C  
ATOM   5336  OG  SER A 690     150.813  97.557 -15.956  1.00 41.54           O  
ANISOU 5336  OG  SER A 690     5011   5393   5381   -234    143    139       O  
ATOM   5337  N   LYS A 691     149.633  96.123 -12.914  1.00 39.09           N  
ANISOU 5337  N   LYS A 691     4679   5064   5112   -189    112    150       N  
ATOM   5338  CA  LYS A 691     150.269  95.217 -11.984  1.00 40.44           C  
ANISOU 5338  CA  LYS A 691     4824   5243   5300   -179    107    145       C  
ATOM   5339  C   LYS A 691     149.948  95.603 -10.505  1.00 36.87           C  
ANISOU 5339  C   LYS A 691     4376   4781   4853   -176     96    155       C  
ATOM   5340  O   LYS A 691     149.693  96.750 -10.180  1.00 36.12           O  
ANISOU 5340  O   LYS A 691     4298   4678   4747   -187     95    162       O  
ATOM   5341  CB  LYS A 691     151.779  95.229 -12.272  1.00 46.01           C  
ANISOU 5341  CB  LYS A 691     5510   5968   6004   -194    117    133       C  
ATOM   5342  CG  LYS A 691     152.683  94.493 -11.303  1.00 51.26           C  
ANISOU 5342  CG  LYS A 691     6147   6643   6685   -187    112    127       C  
ATOM   5343  CD  LYS A 691     154.164  94.750 -11.599  1.00 54.93           C  
ANISOU 5343  CD  LYS A 691     6595   7130   7147   -204    123    114       C  
ATOM   5344  CE  LYS A 691     154.545  96.218 -11.683  1.00 56.97           C  
ANISOU 5344  CE  LYS A 691     6870   7390   7388   -229    131    118       C  
ATOM   5345  NZ  LYS A 691     155.325  96.671 -10.508  1.00 58.58           N  
ANISOU 5345  NZ  LYS A 691     7063   7600   7594   -237    128    118       N  
ATOM   5346  N   ILE A 692     149.943  94.600  -9.642  1.00 35.54           N  
ANISOU 5346  N   ILE A 692     4190   4613   4700   -160     87    154       N  
ATOM   5347  CA  ILE A 692     149.969  94.799  -8.206  1.00 38.08           C  
ANISOU 5347  CA  ILE A 692     4509   4932   5028   -158     77    161       C  
ATOM   5348  C   ILE A 692     151.220  94.102  -7.702  1.00 38.00           C  
ANISOU 5348  C   ILE A 692     4471   4938   5029   -157     76    153       C  
ATOM   5349  O   ILE A 692     151.538  92.989  -8.125  1.00 34.00           O  
ANISOU 5349  O   ILE A 692     3947   4437   4533   -145     77    145       O  
ATOM   5350  CB  ILE A 692     148.703  94.337  -7.444  1.00 40.22           C  
ANISOU 5350  CB  ILE A 692     4787   5188   5306   -141     65    170       C  
ATOM   5351  CG1 ILE A 692     148.428  92.845  -7.592  1.00 44.29           C  
ANISOU 5351  CG1 ILE A 692     5289   5702   5836   -122     61    166       C  
ATOM   5352  CG2 ILE A 692     147.496  95.113  -7.937  1.00 42.46           C  
ANISOU 5352  CG2 ILE A 692     5098   5458   5579   -143     65    176       C  
ATOM   5353  CD1 ILE A 692     146.989  92.441  -7.229  1.00 45.19           C  
ANISOU 5353  CD1 ILE A 692     5415   5801   5955   -107     52    174       C  
ATOM   5354  N   GLU A 693     151.920  94.771  -6.801  1.00 36.54           N  
ANISOU 5354  N   GLU A 693     4282   4760   4842   -168     75    155       N  
ATOM   5355  CA  GLU A 693     153.168  94.237  -6.287  1.00 39.30           C  
ANISOU 5355  CA  GLU A 693     4605   5126   5201   -168     73    147       C  
ATOM   5356  C   GLU A 693     153.285  94.510  -4.798  1.00 37.28           C  
ANISOU 5356  C   GLU A 693     4346   4870   4948   -168     63    154       C  
ATOM   5357  O   GLU A 693     153.004  95.610  -4.313  1.00 34.41           O  
ANISOU 5357  O   GLU A 693     3999   4502   4575   -181     63    161       O  
ATOM   5358  CB  GLU A 693     154.349  94.861  -7.035  1.00 42.15           C  
ANISOU 5358  CB  GLU A 693     4959   5504   5553   -188     87    136       C  
ATOM   5359  CG  GLU A 693     155.647  94.090  -6.849  1.00 47.56           C  
ANISOU 5359  CG  GLU A 693     5613   6208   6250   -184     87    124       C  
ATOM   5360  CD  GLU A 693     156.797  94.622  -7.714  1.00 51.38           C  
ANISOU 5360  CD  GLU A 693     6088   6711   6725   -205    102    111       C  
ATOM   5361  OE1 GLU A 693     156.545  95.247  -8.763  1.00 53.93           O  
ANISOU 5361  OE1 GLU A 693     6427   7030   7035   -217    113    110       O  
ATOM   5362  OE2 GLU A 693     157.964  94.407  -7.350  1.00 55.20           O  
ANISOU 5362  OE2 GLU A 693     6547   7211   7214   -208    102    101       O  
ATOM   5363  N   LEU A 694     153.731  93.478  -4.101  1.00 35.83           N  
ANISOU 5363  N   LEU A 694     4141   4693   4779   -155     54    153       N  
ATOM   5364  CA  LEU A 694     154.092  93.544  -2.712  1.00 37.11           C  
ANISOU 5364  CA  LEU A 694     4295   4860   4945   -154     44    158       C  
ATOM   5365  C   LEU A 694     155.509  94.126  -2.588  1.00 36.95           C  
ANISOU 5365  C   LEU A 694     4260   4860   4921   -171     49    149       C  
ATOM   5366  O   LEU A 694     156.469  93.474  -2.958  1.00 37.35           O  
ANISOU 5366  O   LEU A 694     4287   4924   4978   -167     52    138       O  
ATOM   5367  CB  LEU A 694     153.968  92.113  -2.161  1.00 40.15           C  
ANISOU 5367  CB  LEU A 694     4665   5243   5347   -132     32    161       C  
ATOM   5368  CG  LEU A 694     153.655  91.848  -0.704  1.00 41.93           C  
ANISOU 5368  CG  LEU A 694     4890   5464   5576   -124     17    171       C  
ATOM   5369  CD1 LEU A 694     152.670  92.801  -0.028  1.00 41.27           C  
ANISOU 5369  CD1 LEU A 694     4829   5368   5482   -132     15    182       C  
ATOM   5370  CD2 LEU A 694     153.182  90.408  -0.656  1.00 42.39           C  
ANISOU 5370  CD2 LEU A 694     4941   5513   5650   -102      9    174       C  
ATOM   5371  N   MET A 695     155.620  95.373  -2.140  1.00 36.50           N  
ANISOU 5371  N   MET A 695     4213   4803   4850   -190     52    152       N  
ATOM   5372  CA  MET A 695     156.901  96.098  -2.082  1.00 38.86           C  
ANISOU 5372  CA  MET A 695     4501   5122   5144   -209     60    142       C  
ATOM   5373  C   MET A 695     157.618  95.858  -0.778  1.00 38.93           C  
ANISOU 5373  C   MET A 695     4490   5143   5159   -207     49    143       C  
ATOM   5374  O   MET A 695     158.809  96.043  -0.701  1.00 38.51           O  
ANISOU 5374  O   MET A 695     4419   5109   5105   -217     52    133       O  
ATOM   5375  CB  MET A 695     156.724  97.625  -2.257  1.00 39.77           C  
ANISOU 5375  CB  MET A 695     4638   5231   5241   -233     69    145       C  
ATOM   5376  CG  MET A 695     156.160  98.068  -3.598  1.00 40.23           C  
ANISOU 5376  CG  MET A 695     4716   5279   5290   -239     81    144       C  
ATOM   5377  SD  MET A 695     157.008  97.352  -5.016  1.00 45.54           S  
ANISOU 5377  SD  MET A 695     5372   5967   5966   -239     92    130       S  
ATOM   5378  CE  MET A 695     158.541  98.292  -4.987  1.00 45.07           C  
ANISOU 5378  CE  MET A 695     5299   5929   5896   -267    104    118       C  
ATOM   5379  N   LEU A 696     156.862  95.474   0.251  1.00 37.67           N  
ANISOU 5379  N   LEU A 696     4335   4973   5004   -194     35    154       N  
ATOM   5380  CA  LEU A 696     157.402  95.202   1.545  1.00 36.46           C  
ANISOU 5380  CA  LEU A 696     4166   4830   4855   -190     23    157       C  
ATOM   5381  C   LEU A 696     156.424  94.273   2.204  1.00 36.99           C  
ANISOU 5381  C   LEU A 696     4238   4883   4932   -170     10    168       C  
ATOM   5382  O   LEU A 696     155.191  94.554   2.200  1.00 33.98           O  
ANISOU 5382  O   LEU A 696     3880   4484   4546   -168     10    177       O  
ATOM   5383  CB  LEU A 696     157.504  96.494   2.343  1.00 37.50           C  
ANISOU 5383  CB  LEU A 696     4308   4965   4975   -211     24    159       C  
ATOM   5384  CG  LEU A 696     158.285  96.545   3.646  1.00 40.28           C  
ANISOU 5384  CG  LEU A 696     4644   5333   5328   -214     14    159       C  
ATOM   5385  CD1 LEU A 696     159.771  96.225   3.445  1.00 41.81           C  
ANISOU 5385  CD1 LEU A 696     4810   5551   5527   -218     16    146       C  
ATOM   5386  CD2 LEU A 696     158.154  97.954   4.226  1.00 40.37           C  
ANISOU 5386  CD2 LEU A 696     4672   5343   5325   -236     19    161       C  
ATOM   5387  N   ASP A 697     156.957  93.198   2.785  1.00 36.09           N  
ANISOU 5387  N   ASP A 697     4104   4778   4831   -154     -2    169       N  
ATOM   5388  CA  ASP A 697     156.155  92.131   3.381  1.00 37.91           C  
ANISOU 5388  CA  ASP A 697     4337   4996   5071   -134    -15    180       C  
ATOM   5389  C   ASP A 697     156.795  91.591   4.664  1.00 39.10           C  
ANISOU 5389  C   ASP A 697     4471   5158   5228   -127    -30    184       C  
ATOM   5390  O   ASP A 697     157.373  90.508   4.650  1.00 38.82           O  
ANISOU 5390  O   ASP A 697     4416   5127   5205   -111    -38    182       O  
ATOM   5391  CB  ASP A 697     156.002  90.988   2.387  1.00 38.98           C  
ANISOU 5391  CB  ASP A 697     4466   5125   5219   -117    -13    175       C  
ATOM   5392  CG  ASP A 697     155.013  89.908   2.867  1.00 42.45           C  
ANISOU 5392  CG  ASP A 697     4912   5548   5668    -97    -25    187       C  
ATOM   5393  OD1 ASP A 697     154.193  90.159   3.795  1.00 41.80           O  
ANISOU 5393  OD1 ASP A 697     4845   5457   5581    -98    -31    198       O  
ATOM   5394  OD2 ASP A 697     155.041  88.799   2.281  1.00 46.10           O  
ANISOU 5394  OD2 ASP A 697     5365   6006   6143    -81    -26    183       O  
ATOM   5395  N   THR A 698     156.729  92.365   5.742  1.00 36.68           N  
ANISOU 5395  N   THR A 698     4171   4855   4912   -139    -35    190       N  
ATOM   5396  CA  THR A 698     157.297  91.959   7.012  1.00 38.09           C  
ANISOU 5396  CA  THR A 698     4335   5045   5094   -134    -50    195       C  
ATOM   5397  C   THR A 698     156.188  91.924   8.056  1.00 39.09           C  
ANISOU 5397  C   THR A 698     4478   5158   5215   -131    -59    210       C  
ATOM   5398  O   THR A 698     155.057  92.382   7.788  1.00 39.74           O  
ANISOU 5398  O   THR A 698     4582   5225   5292   -135    -53    214       O  
ATOM   5399  CB  THR A 698     158.389  92.942   7.461  1.00 38.54           C  
ANISOU 5399  CB  THR A 698     4380   5123   5141   -153    -48    188       C  
ATOM   5400  OG1 THR A 698     157.796  94.219   7.724  1.00 38.34           O  
ANISOU 5400  OG1 THR A 698     4374   5091   5100   -172    -40    190       O  
ATOM   5401  CG2 THR A 698     159.498  93.071   6.387  1.00 36.66           C  
ANISOU 5401  CG2 THR A 698     4124   4899   4905   -159    -36    172       C  
ATOM   5402  N   LYS A 699     156.514  91.426   9.240  1.00 39.37           N  
ANISOU 5402  N   LYS A 699     4504   5202   5253   -125    -74    217       N  
ATOM   5403  CA  LYS A 699     155.601  91.479  10.387  1.00 44.36           C  
ANISOU 5403  CA  LYS A 699     5151   5826   5879   -126    -83    230       C  
ATOM   5404  C   LYS A 699     155.209  92.909  10.748  1.00 41.11           C  
ANISOU 5404  C   LYS A 699     4754   5414   5451   -148    -75    229       C  
ATOM   5405  O   LYS A 699     154.067  93.145  11.108  1.00 41.45           O  
ANISOU 5405  O   LYS A 699     4816   5443   5488   -149    -75    236       O  
ATOM   5406  CB  LYS A 699     156.177  90.816  11.645  1.00 48.49           C  
ANISOU 5406  CB  LYS A 699     5659   6360   6404   -119   -101    238       C  
ATOM   5407  CG  LYS A 699     156.195  89.304  11.600  1.00 59.08           C  
ANISOU 5407  CG  LYS A 699     6992   7695   7761    -95   -113    245       C  
ATOM   5408  CD  LYS A 699     157.009  88.721  12.771  1.00 66.65           C  
ANISOU 5408  CD  LYS A 699     7934   8668   8722    -89   -131    252       C  
ATOM   5409  CE  LYS A 699     156.231  88.710  14.088  1.00 71.01           C  
ANISOU 5409  CE  LYS A 699     8501   9216   9265    -92   -142    267       C  
ATOM   5410  NZ  LYS A 699     155.372  87.492  14.260  1.00 74.32           N  
ANISOU 5410  NZ  LYS A 699     8929   9616   9692    -75   -150    280       N  
ATOM   5411  N   GLU A 700     156.149  93.845  10.656  1.00 39.67           N  
ANISOU 5411  N   GLU A 700     4563   5247   5262   -164    -69    219       N  
ATOM   5412  CA  GLU A 700     155.917  95.214  11.114  1.00 41.27           C  
ANISOU 5412  CA  GLU A 700     4780   5452   5451   -185    -62    217       C  
ATOM   5413  C   GLU A 700     155.160  96.069  10.070  1.00 37.47           C  
ANISOU 5413  C   GLU A 700     4319   4954   4964   -194    -47    213       C  
ATOM   5414  O   GLU A 700     154.367  96.964  10.443  1.00 36.25           O  
ANISOU 5414  O   GLU A 700     4183   4790   4800   -204    -43    215       O  
ATOM   5415  CB  GLU A 700     157.248  95.882  11.490  1.00 45.23           C  
ANISOU 5415  CB  GLU A 700     5264   5976   5946   -201    -61    208       C  
ATOM   5416  CG  GLU A 700     158.052  95.143  12.570  1.00 53.75           C  
ANISOU 5416  CG  GLU A 700     6322   7072   7029   -193    -78    212       C  
ATOM   5417  CD  GLU A 700     158.819  93.848  12.144  1.00 58.99           C  
ANISOU 5417  CD  GLU A 700     6963   7743   7708   -173    -86    210       C  
ATOM   5418  OE1 GLU A 700     158.904  93.448  10.939  1.00 57.54           O  
ANISOU 5418  OE1 GLU A 700     6777   7554   7533   -165    -78    204       O  
ATOM   5419  OE2 GLU A 700     159.342  93.190  13.081  1.00 66.20           O  
ANISOU 5419  OE2 GLU A 700     7862   8668   8624   -164   -102    216       O  
ATOM   5420  N   TYR A 701     155.462  95.837   8.786  1.00 33.56           N  
ANISOU 5420  N   TYR A 701     3820   4457   4474   -190    -38    206       N  
ATOM   5421  CA  TYR A 701     154.951  96.685   7.679  1.00 34.62           C  
ANISOU 5421  CA  TYR A 701     3972   4579   4603   -199    -23    201       C  
ATOM   5422  C   TYR A 701     154.605  95.866   6.436  1.00 32.90           C  
ANISOU 5422  C   TYR A 701     3755   4352   4394   -184    -18    200       C  
ATOM   5423  O   TYR A 701     155.332  94.940   6.060  1.00 32.26           O  
ANISOU 5423  O   TYR A 701     3655   4279   4323   -173    -21    196       O  
ATOM   5424  CB  TYR A 701     155.986  97.769   7.267  1.00 35.44           C  
ANISOU 5424  CB  TYR A 701     4072   4697   4699   -220    -11    190       C  
ATOM   5425  CG  TYR A 701     156.311  98.738   8.385  1.00 36.40           C  
ANISOU 5425  CG  TYR A 701     4194   4826   4810   -238    -13    189       C  
ATOM   5426  CD1 TYR A 701     155.422  99.747   8.692  1.00 36.55           C  
ANISOU 5426  CD1 TYR A 701     4236   4833   4820   -249     -9    192       C  
ATOM   5427  CD2 TYR A 701     157.477  98.607   9.182  1.00 37.98           C  
ANISOU 5427  CD2 TYR A 701     4371   5048   5010   -243    -20    185       C  
ATOM   5428  CE1 TYR A 701     155.649 100.610   9.747  1.00 38.11           C  
ANISOU 5428  CE1 TYR A 701     4435   5037   5008   -264    -11    191       C  
ATOM   5429  CE2 TYR A 701     157.734  99.510  10.238  1.00 38.63           C  
ANISOU 5429  CE2 TYR A 701     4455   5140   5082   -260    -22    184       C  
ATOM   5430  CZ  TYR A 701     156.804 100.506  10.507  1.00 38.19           C  
ANISOU 5430  CZ  TYR A 701     4423   5069   5017   -271    -17    187       C  
ATOM   5431  OH  TYR A 701     156.951 101.451  11.488  1.00 39.43           O  
ANISOU 5431  OH  TYR A 701     4584   5233   5165   -288    -18    184       O  
ATOM   5432  N   THR A 702     153.504  96.254   5.799  1.00 30.70           N  
ANISOU 5432  N   THR A 702     3499   4056   4112   -184    -11    202       N  
ATOM   5433  CA  THR A 702     153.080  95.735   4.504  1.00 29.20           C  
ANISOU 5433  CA  THR A 702     3312   3855   3926   -174     -5    200       C  
ATOM   5434  C   THR A 702     152.933  96.910   3.556  1.00 29.56           C  
ANISOU 5434  C   THR A 702     3374   3895   3961   -190      9    195       C  
ATOM   5435  O   THR A 702     152.383  97.953   3.943  1.00 29.47           O  
ANISOU 5435  O   THR A 702     3381   3875   3940   -201     11    198       O  
ATOM   5436  CB  THR A 702     151.714  95.033   4.570  1.00 28.27           C  
ANISOU 5436  CB  THR A 702     3208   3720   3814   -158    -10    208       C  
ATOM   5437  OG1 THR A 702     151.696  94.043   5.604  1.00 28.57           O  
ANISOU 5437  OG1 THR A 702     3235   3761   3860   -146    -24    215       O  
ATOM   5438  CG2 THR A 702     151.419  94.344   3.244  1.00 28.59           C  
ANISOU 5438  CG2 THR A 702     3248   3753   3860   -147     -4    205       C  
ATOM   5439  N   ALA A 703     153.402  96.757   2.317  1.00 29.31           N  
ANISOU 5439  N   ALA A 703     3339   3867   3931   -190     19    187       N  
ATOM   5440  CA  ALA A 703     153.255  97.832   1.314  1.00 29.26           C  
ANISOU 5440  CA  ALA A 703     3349   3854   3913   -205     32    183       C  
ATOM   5441  C   ALA A 703     152.933  97.229  -0.007  1.00 29.03           C  
ANISOU 5441  C   ALA A 703     3323   3819   3888   -196     38    181       C  
ATOM   5442  O   ALA A 703     153.581  96.276  -0.429  1.00 28.05           O  
ANISOU 5442  O   ALA A 703     3179   3705   3772   -187     38    175       O  
ATOM   5443  CB  ALA A 703     154.529  98.720   1.194  1.00 30.72           C  
ANISOU 5443  CB  ALA A 703     3527   4055   4091   -227     41    175       C  
ATOM   5444  N   VAL A 704     151.910  97.795  -0.653  1.00 28.57           N  
ANISOU 5444  N   VAL A 704     3287   3744   3822   -197     42    184       N  
ATOM   5445  CA  VAL A 704     151.384  97.299  -1.920  1.00 28.86           C  
ANISOU 5445  CA  VAL A 704     3331   3775   3861   -188     47    183       C  
ATOM   5446  C   VAL A 704     151.308  98.436  -2.915  1.00 28.27           C  
ANISOU 5446  C   VAL A 704     3276   3695   3772   -204     59    181       C  
ATOM   5447  O   VAL A 704     150.735  99.492  -2.614  1.00 27.50           O  
ANISOU 5447  O   VAL A 704     3197   3586   3665   -213     59    186       O  
ATOM   5448  CB  VAL A 704     149.962  96.682  -1.732  1.00 28.82           C  
ANISOU 5448  CB  VAL A 704     3336   3753   3861   -170     39    190       C  
ATOM   5449  CG1 VAL A 704     149.313  96.351  -3.079  1.00 28.80           C  
ANISOU 5449  CG1 VAL A 704     3343   3742   3857   -162     45    188       C  
ATOM   5450  CG2 VAL A 704     150.076  95.432  -0.895  1.00 30.02           C  
ANISOU 5450  CG2 VAL A 704     3470   3909   4026   -154     28    192       C  
ATOM   5451  N   LEU A 705     151.917  98.199  -4.069  1.00 29.73           N  
ANISOU 5451  N   LEU A 705     3453   3887   3955   -208     68    173       N  
ATOM   5452  CA  LEU A 705     151.999  99.129  -5.182  1.00 32.80           C  
ANISOU 5452  CA  LEU A 705     3858   4274   4330   -224     80    171       C  
ATOM   5453  C   LEU A 705     150.932  98.648  -6.183  1.00 32.12           C  
ANISOU 5453  C   LEU A 705     3784   4175   4243   -210     80    174       C  
ATOM   5454  O   LEU A 705     150.842  97.465  -6.474  1.00 30.63           O  
ANISOU 5454  O   LEU A 705     3583   3991   4066   -195     78    170       O  
ATOM   5455  CB  LEU A 705     153.385  99.076  -5.840  1.00 34.79           C  
ANISOU 5455  CB  LEU A 705     4093   4545   4579   -237     91    160       C  
ATOM   5456  CG  LEU A 705     153.723 100.148  -6.904  1.00 38.79           C  
ANISOU 5456  CG  LEU A 705     4616   5053   5071   -259    105    157       C  
ATOM   5457  CD1 LEU A 705     153.797 101.560  -6.315  1.00 38.75           C  
ANISOU 5457  CD1 LEU A 705     4629   5042   5055   -278    107    162       C  
ATOM   5458  CD2 LEU A 705     155.074  99.829  -7.567  1.00 39.90           C  
ANISOU 5458  CD2 LEU A 705     4735   5215   5210   -270    116    143       C  
ATOM   5459  N   ILE A 706     150.163  99.588  -6.693  1.00 31.27           N  
ANISOU 5459  N   ILE A 706     3703   4054   4124   -216     83    180       N  
ATOM   5460  CA  ILE A 706     149.123  99.349  -7.688  1.00 34.44           C  
ANISOU 5460  CA  ILE A 706     4119   4444   4523   -206     83    182       C  
ATOM   5461  C   ILE A 706     149.401 100.263  -8.879  1.00 34.00           C  
ANISOU 5461  C   ILE A 706     4079   4389   4451   -223     95    181       C  
ATOM   5462  O   ILE A 706     149.334 101.499  -8.726  1.00 33.35           O  
ANISOU 5462  O   ILE A 706     4015   4297   4358   -238     97    186       O  
ATOM   5463  CB  ILE A 706     147.735  99.706  -7.091  1.00 36.16           C  
ANISOU 5463  CB  ILE A 706     4355   4643   4741   -196     74    192       C  
ATOM   5464  CG1 ILE A 706     147.496  98.879  -5.842  1.00 36.69           C  
ANISOU 5464  CG1 ILE A 706     4407   4711   4821   -182     63    193       C  
ATOM   5465  CG2 ILE A 706     146.612  99.492  -8.110  1.00 37.83           C  
ANISOU 5465  CG2 ILE A 706     4581   4844   4948   -184     73    194       C  
ATOM   5466  CD1 ILE A 706     146.472  99.451  -4.952  1.00 39.34           C  
ANISOU 5466  CD1 ILE A 706     4758   5033   5156   -177     55    201       C  
ATOM   5467  N   ASP A 707     149.741  99.671 -10.026  1.00 35.20           N  
ANISOU 5467  N   ASP A 707     4224   4549   4601   -223    102    174       N  
ATOM   5468  CA  ASP A 707     149.909 100.405 -11.286  1.00 39.07           C  
ANISOU 5468  CA  ASP A 707     4730   5039   5075   -239    113    174       C  
ATOM   5469  C   ASP A 707     148.686 100.205 -12.128  1.00 35.51           C  
ANISOU 5469  C   ASP A 707     4296   4576   4620   -226    110    179       C  
ATOM   5470  O   ASP A 707     148.336  99.056 -12.431  1.00 33.66           O  
ANISOU 5470  O   ASP A 707     4050   4345   4396   -210    107    174       O  
ATOM   5471  CB  ASP A 707     151.080  99.885 -12.143  1.00 44.73           C  
ANISOU 5471  CB  ASP A 707     5428   5776   5790   -249    125    162       C  
ATOM   5472  CG  ASP A 707     152.385 100.020 -11.489  1.00 53.31           C  
ANISOU 5472  CG  ASP A 707     6496   6879   6881   -262    129    154       C  
ATOM   5473  OD1 ASP A 707     152.431 100.225 -10.246  1.00 62.13           O  
ANISOU 5473  OD1 ASP A 707     7608   7992   8004   -260    122    158       O  
ATOM   5474  OD2 ASP A 707     153.396  99.911 -12.210  1.00 62.52           O  
ANISOU 5474  OD2 ASP A 707     7651   8062   8044   -275    141    144       O  
ATOM   5475  N   ALA A 708     148.063 101.300 -12.531  1.00 34.45           N  
ANISOU 5475  N   ALA A 708     4189   4427   4472   -234    110    187       N  
ATOM   5476  CA  ALA A 708     146.979 101.244 -13.505  1.00 38.56           C  
ANISOU 5476  CA  ALA A 708     4727   4938   4986   -224    107    192       C  
ATOM   5477  C   ALA A 708     147.577 101.266 -14.917  1.00 43.08           C  
ANISOU 5477  C   ALA A 708     5302   5522   5545   -238    119    187       C  
ATOM   5478  O   ALA A 708     148.685 101.722 -15.083  1.00 42.62           O  
ANISOU 5478  O   ALA A 708     5240   5474   5480   -258    129    182       O  
ATOM   5479  CB  ALA A 708     146.042 102.396 -13.310  1.00 37.53           C  
ANISOU 5479  CB  ALA A 708     4624   4788   4846   -225    101    203       C  
ATOM   5480  N   LYS A 709     146.844 100.759 -15.910  1.00 46.86           N  
ANISOU 5480  N   LYS A 709     5787   5999   6020   -227    118    186       N  
ATOM   5481  CA  LYS A 709     147.301 100.742 -17.334  1.00 49.66           C  
ANISOU 5481  CA  LYS A 709     6145   6364   6361   -240    129    181       C  
ATOM   5482  C   LYS A 709     147.479 102.138 -17.896  1.00 53.00           C  
ANISOU 5482  C   LYS A 709     6595   6780   6763   -261    135    190       C  
ATOM   5483  O   LYS A 709     148.364 102.357 -18.687  1.00 51.20           O  
ANISOU 5483  O   LYS A 709     6366   6565   6524   -280    147    185       O  
ATOM   5484  CB  LYS A 709     146.343  99.974 -18.252  1.00 47.48           C  
ANISOU 5484  CB  LYS A 709     5871   6086   6083   -224    126    180       C  
ATOM   5485  CG  LYS A 709     146.489  98.481 -18.098  1.00 50.28           C  
ANISOU 5485  CG  LYS A 709     6197   6452   6456   -209    125    169       C  
ATOM   5486  CD  LYS A 709     145.667  97.698 -19.104  1.00 50.81           C  
ANISOU 5486  CD  LYS A 709     6265   6519   6520   -196    124    165       C  
ATOM   5487  CE  LYS A 709     145.862  96.199 -18.897  1.00 51.06           C  
ANISOU 5487  CE  LYS A 709     6269   6560   6571   -181    123    153       C  
ATOM   5488  NZ  LYS A 709     144.614  95.463 -19.258  1.00 51.61           N  
ANISOU 5488  NZ  LYS A 709     6342   6623   6645   -162    116    153       N  
ATOM   5489  N   SER A 710     146.635 103.070 -17.465  1.00 60.40           N  
ANISOU 5489  N   SER A 710     7555   7697   7696   -258    126    202       N  
ATOM   5490  CA  SER A 710     146.721 104.449 -17.929  1.00 70.07           C  
ANISOU 5490  CA  SER A 710     8809   8913   8903   -277    130    211       C  
ATOM   5491  C   SER A 710     148.172 104.918 -17.909  1.00 74.74           C  
ANISOU 5491  C   SER A 710     9394   9517   9488   -304    144    205       C  
ATOM   5492  O   SER A 710     148.498 105.987 -18.425  1.00 78.95           O  
ANISOU 5492  O   SER A 710     9948  10044  10004   -324    151    211       O  
ATOM   5493  CB  SER A 710     145.859 105.364 -17.058  1.00 73.41           C  
ANISOU 5493  CB  SER A 710     9252   9313   9328   -270    119    222       C  
ATOM   5494  OG  SER A 710     144.525 105.412 -17.534  1.00 68.95           O  
ANISOU 5494  OG  SER A 710     8705   8735   8760   -253    108    230       O  
ATOM   5495  N   ASN A 711     149.035 104.105 -17.305  1.00 82.26           N  
ANISOU 5495  N   ASN A 711    10315  10486  10454   -303    148    194       N  
ATOM   5496  CA  ASN A 711     150.460 104.407 -17.210  1.00 87.17           C  
ANISOU 5496  CA  ASN A 711    10925  11123  11072   -327    161    186       C  
ATOM   5497  C   ASN A 711     150.824 105.362 -16.075  1.00 86.48           C  
ANISOU 5497  C   ASN A 711    10843  11029  10987   -338    159    190       C  
ATOM   5498  O   ASN A 711     151.183 104.931 -14.979  1.00 92.31           O  
ANISOU 5498  O   ASN A 711    11560  11773  11740   -331    155    185       O  
ATOM   5499  CB  ASN A 711     150.990 104.946 -18.542  1.00 91.35           C  
ANISOU 5499  CB  ASN A 711    11468  11659  11580   -350    174    185       C  
ATOM   5500  CG  ASN A 711     152.367 104.410 -18.882  1.00 93.67           C  
ANISOU 5500  CG  ASN A 711    11736  11980  11875   -365    188    169       C  
ATOM   5501  OD1 ASN A 711     153.010 103.754 -18.062  1.00 96.37           O  
ANISOU 5501  OD1 ASN A 711    12050  12334  12233   -360    188    159       O  
ATOM   5502  ND2 ASN A 711     152.827 104.688 -20.096  1.00 95.12           N  
ANISOU 5502  ND2 ASN A 711    11929  12173  12041   -385    201    166       N  
ATOM   5503  N   THR A 712     150.732 106.660 -16.346  1.00 79.17           N  
ANISOU 5503  N   THR A 712     9946  10089  10045   -355    162    199       N  
ATOM   5504  CA  THR A 712     151.068 107.682 -15.355  1.00 75.57           C  
ANISOU 5504  CA  THR A 712     9499   9625   9590   -368    162    203       C  
ATOM   5505  C   THR A 712     150.300 107.506 -14.023  1.00 70.61           C  
ANISOU 5505  C   THR A 712     8865   8985   8978   -347    147    206       C  
ATOM   5506  O   THR A 712     150.359 108.383 -13.174  1.00 67.12           O  
ANISOU 5506  O   THR A 712     8434   8534   8537   -355    145    210       O  
ATOM   5507  CB  THR A 712     150.835 109.140 -15.893  1.00 76.81           C  
ANISOU 5507  CB  THR A 712     9693   9763   9727   -387    165    214       C  
ATOM   5508  OG1 THR A 712     149.522 109.262 -16.446  1.00 75.96           O  
ANISOU 5508  OG1 THR A 712     9609   9637   9616   -370    155    226       O  
ATOM   5509  CG2 THR A 712     151.899 109.541 -16.946  1.00 74.19           C  
ANISOU 5509  CG2 THR A 712     9366   9444   9379   -416    182    210       C  
ATOM   5510  N   GLU A 713     149.614 106.375 -13.815  1.00 63.30           N  
ANISOU 5510  N   GLU A 713     7924   8061   8065   -321    138    204       N  
ATOM   5511  CA  GLU A 713     148.773 106.207 -12.627  1.00 59.62           C  
ANISOU 5511  CA  GLU A 713     7456   7584   7613   -302    125    208       C  
ATOM   5512  C   GLU A 713     149.272 105.102 -11.683  1.00 54.21           C  
ANISOU 5512  C   GLU A 713     6738   6914   6945   -292    122    200       C  
ATOM   5513  O   GLU A 713     149.035 103.924 -11.914  1.00 47.43           O  
ANISOU 5513  O   GLU A 713     5863   6063   6096   -275    119    195       O  
ATOM   5514  CB  GLU A 713     147.318 105.974 -13.047  1.00 60.04           C  
ANISOU 5514  CB  GLU A 713     7524   7622   7667   -280    114    216       C  
ATOM   5515  CG  GLU A 713     146.716 107.049 -13.942  1.00 60.66           C  
ANISOU 5515  CG  GLU A 713     7636   7683   7728   -287    115    225       C  
ATOM   5516  CD  GLU A 713     147.161 108.484 -13.616  1.00 69.75           C  
ANISOU 5516  CD  GLU A 713     8808   8824   8871   -309    119    231       C  
ATOM   5517  OE1 GLU A 713     147.027 108.973 -12.465  1.00 72.44           O  
ANISOU 5517  OE1 GLU A 713     9150   9156   9219   -308    114    232       O  
ATOM   5518  OE2 GLU A 713     147.674 109.177 -14.524  1.00 75.29           O  
ANISOU 5518  OE2 GLU A 713     9526   9525   9556   -329    128    233       O  
ATOM   5519  N   GLN A 714     149.930 105.527 -10.597  1.00 52.73           N  
ANISOU 5519  N   GLN A 714     6542   6731   6762   -301    122    197       N  
ATOM   5520  CA  GLN A 714     150.571 104.609  -9.617  1.00 49.61           C  
ANISOU 5520  CA  GLN A 714     6117   6351   6382   -294    119    190       C  
ATOM   5521  C   GLN A 714     150.286 105.029  -8.161  1.00 43.04           C  
ANISOU 5521  C   GLN A 714     5285   5511   5557   -291    110    194       C  
ATOM   5522  O   GLN A 714     150.472 106.199  -7.796  1.00 43.28           O  
ANISOU 5522  O   GLN A 714     5330   5534   5579   -308    113    196       O  
ATOM   5523  CB  GLN A 714     152.071 104.587  -9.853  1.00 50.34           C  
ANISOU 5523  CB  GLN A 714     6190   6464   6471   -314    131    179       C  
ATOM   5524  CG  GLN A 714     152.603 103.204 -10.068  1.00 53.56           C  
ANISOU 5524  CG  GLN A 714     6569   6891   6891   -302    131    170       C  
ATOM   5525  CD  GLN A 714     154.102 103.176 -10.317  1.00 56.38           C  
ANISOU 5525  CD  GLN A 714     6907   7271   7245   -321    143    157       C  
ATOM   5526  OE1 GLN A 714     154.741 104.225 -10.457  1.00 58.70           O  
ANISOU 5526  OE1 GLN A 714     7211   7567   7527   -346    152    156       O  
ATOM   5527  NE2 GLN A 714     154.678 101.972 -10.345  1.00 54.88           N  
ANISOU 5527  NE2 GLN A 714     6687   7097   7066   -310    143    147       N  
ATOM   5528  N   THR A 715     149.813 104.078  -7.362  1.00 37.59           N  
ANISOU 5528  N   THR A 715     4580   4823   4881   -271     99    194       N  
ATOM   5529  CA  THR A 715     149.507 104.295  -5.966  1.00 35.55           C  
ANISOU 5529  CA  THR A 715     4320   4560   4629   -267     91    197       C  
ATOM   5530  C   THR A 715     150.173 103.281  -5.069  1.00 33.96           C  
ANISOU 5530  C   THR A 715     4089   4375   4440   -260     86    191       C  
ATOM   5531  O   THR A 715     150.484 102.176  -5.494  1.00 34.51           O  
ANISOU 5531  O   THR A 715     4141   4455   4517   -250     86    187       O  
ATOM   5532  CB  THR A 715     147.987 104.283  -5.694  1.00 36.94           C  
ANISOU 5532  CB  THR A 715     4512   4717   4808   -249     80    204       C  
ATOM   5533  OG1 THR A 715     147.372 103.133  -6.277  1.00 38.37           O  
ANISOU 5533  OG1 THR A 715     4685   4898   4995   -229     76    204       O  
ATOM   5534  CG2 THR A 715     147.334 105.551  -6.271  1.00 37.69           C  
ANISOU 5534  CG2 THR A 715     4638   4793   4891   -256     82    210       C  
ATOM   5535  N   LEU A 716     150.349 103.663  -3.807  1.00 33.12           N  
ANISOU 5535  N   LEU A 716     3979   4269   4336   -264     81    192       N  
ATOM   5536  CA  LEU A 716     151.064 102.850  -2.810  1.00 33.34           C  
ANISOU 5536  CA  LEU A 716     3980   4313   4375   -260     75    188       C  
ATOM   5537  C   LEU A 716     150.309 102.896  -1.461  1.00 33.01           C  
ANISOU 5537  C   LEU A 716     3941   4263   4337   -251     64    194       C  
ATOM   5538  O   LEU A 716     150.080 103.969  -0.903  1.00 31.99           O  
ANISOU 5538  O   LEU A 716     3827   4126   4203   -262     64    196       O  
ATOM   5539  CB  LEU A 716     152.496 103.382  -2.642  1.00 33.05           C  
ANISOU 5539  CB  LEU A 716     3931   4293   4333   -281     84    180       C  
ATOM   5540  CG  LEU A 716     153.354 102.616  -1.629  1.00 33.99           C  
ANISOU 5540  CG  LEU A 716     4021   4430   4462   -278     77    176       C  
ATOM   5541  CD1 LEU A 716     153.739 101.231  -2.161  1.00 34.33           C  
ANISOU 5541  CD1 LEU A 716     4043   4485   4516   -262     76    171       C  
ATOM   5542  CD2 LEU A 716     154.614 103.383  -1.296  1.00 34.05           C  
ANISOU 5542  CD2 LEU A 716     4021   4454   4464   -301     84    168       C  
ATOM   5543  N   LEU A 717     149.934 101.731  -0.954  1.00 31.94           N  
ANISOU 5543  N   LEU A 717     3791   4130   4213   -232     55    196       N  
ATOM   5544  CA  LEU A 717     149.364 101.603   0.396  1.00 32.33           C  
ANISOU 5544  CA  LEU A 717     3840   4176   4268   -225     44    200       C  
ATOM   5545  C   LEU A 717     150.395 100.981   1.301  1.00 32.01           C  
ANISOU 5545  C   LEU A 717     3775   4155   4234   -226     39    197       C  
ATOM   5546  O   LEU A 717     150.981  99.945   0.963  1.00 31.35           O  
ANISOU 5546  O   LEU A 717     3672   4082   4159   -217     39    194       O  
ATOM   5547  CB  LEU A 717     148.104 100.702   0.373  1.00 33.29           C  
ANISOU 5547  CB  LEU A 717     3965   4287   4397   -203     36    205       C  
ATOM   5548  CG  LEU A 717     147.377 100.494   1.704  1.00 35.04           C  
ANISOU 5548  CG  LEU A 717     4186   4504   4622   -196     26    210       C  
ATOM   5549  CD1 LEU A 717     146.822 101.779   2.276  1.00 36.47           C  
ANISOU 5549  CD1 LEU A 717     4386   4675   4795   -206     26    211       C  
ATOM   5550  CD2 LEU A 717     146.266  99.466   1.586  1.00 36.20           C  
ANISOU 5550  CD2 LEU A 717     4334   4643   4777   -176     19    214       C  
ATOM   5551  N   ILE A 718     150.612 101.621   2.443  1.00 31.44           N  
ANISOU 5551  N   ILE A 718     3702   4086   4159   -236     36    198       N  
ATOM   5552  CA  ILE A 718     151.546 101.156   3.421  1.00 32.95           C  
ANISOU 5552  CA  ILE A 718     3872   4295   4354   -238     30    196       C  
ATOM   5553  C   ILE A 718     150.757 100.960   4.698  1.00 31.74           C  
ANISOU 5553  C   ILE A 718     3720   4136   4203   -230     19    202       C  
ATOM   5554  O   ILE A 718     150.046 101.854   5.100  1.00 31.69           O  
ANISOU 5554  O   ILE A 718     3731   4118   4190   -236     19    204       O  
ATOM   5555  CB  ILE A 718     152.700 102.147   3.704  1.00 33.87           C  
ANISOU 5555  CB  ILE A 718     3982   4423   4462   -261     37    189       C  
ATOM   5556  CG1 ILE A 718     153.402 102.584   2.428  1.00 35.25           C  
ANISOU 5556  CG1 ILE A 718     4160   4602   4632   -273     50    182       C  
ATOM   5557  CG2 ILE A 718     153.691 101.480   4.640  1.00 35.28           C  
ANISOU 5557  CG2 ILE A 718     4135   4622   4647   -260     29    187       C  
ATOM   5558  CD1 ILE A 718     154.328 103.788   2.635  1.00 36.13           C  
ANISOU 5558  CD1 ILE A 718     4273   4721   4734   -299     58    176       C  
ATOM   5559  N   LEU A 719     150.888  99.795   5.315  1.00 31.46           N  
ANISOU 5559  N   LEU A 719     3668   4109   4177   -216      9    205       N  
ATOM   5560  CA  LEU A 719     150.248  99.491   6.595  1.00 32.48           C  
ANISOU 5560  CA  LEU A 719     3797   4236   4307   -210     -2    212       C  
ATOM   5561  C   LEU A 719     151.291  99.297   7.649  1.00 31.40           C  
ANISOU 5561  C   LEU A 719     3641   4118   4171   -216     -9    211       C  
ATOM   5562  O   LEU A 719     152.282  98.630   7.393  1.00 29.73           O  
ANISOU 5562  O   LEU A 719     3411   3920   3966   -212    -10    208       O  
ATOM   5563  CB  LEU A 719     149.437  98.187   6.514  1.00 34.89           C  
ANISOU 5563  CB  LEU A 719     4101   4534   4623   -189     -9    218       C  
ATOM   5564  CG  LEU A 719     148.360  98.121   5.430  1.00 37.01           C  
ANISOU 5564  CG  LEU A 719     4385   4786   4892   -180     -4    219       C  
ATOM   5565  CD1 LEU A 719     147.762  96.725   5.382  1.00 37.85           C  
ANISOU 5565  CD1 LEU A 719     4485   4887   5009   -160    -11    223       C  
ATOM   5566  CD2 LEU A 719     147.248  99.156   5.667  1.00 38.03           C  
ANISOU 5566  CD2 LEU A 719     4536   4901   5013   -185     -2    220       C  
ATOM   5567  N   ALA A 720     151.078  99.898   8.822  1.00 32.04           N  
ANISOU 5567  N   ALA A 720     3728   4201   4246   -225    -13    213       N  
ATOM   5568  CA  ALA A 720     151.827  99.565  10.023  1.00 33.55           C  
ANISOU 5568  CA  ALA A 720     3901   4408   4437   -227    -23    214       C  
ATOM   5569  C   ALA A 720     150.998  98.502  10.769  1.00 33.94           C  
ANISOU 5569  C   ALA A 720     3950   4453   4492   -211    -35    224       C  
ATOM   5570  O   ALA A 720     149.868  98.758  11.086  1.00 32.28           O  
ANISOU 5570  O   ALA A 720     3755   4230   4278   -210    -35    227       O  
ATOM   5571  CB  ALA A 720     152.008 100.810  10.882  1.00 33.96           C  
ANISOU 5571  CB  ALA A 720     3960   4466   4479   -247    -20    211       C  
ATOM   5572  N   ASN A 721     151.572  97.333  11.035  1.00 34.05           N  
ANISOU 5572  N   ASN A 721     3946   4477   4514   -199    -44    228       N  
ATOM   5573  CA  ASN A 721     150.818  96.170  11.533  1.00 35.40           C  
ANISOU 5573  CA  ASN A 721     4117   4642   4692   -182    -55    238       C  
ATOM   5574  C   ASN A 721     150.815  95.962  13.046  1.00 36.91           C  
ANISOU 5574  C   ASN A 721     4304   4842   4879   -185    -67    245       C  
ATOM   5575  O   ASN A 721     150.009  95.147  13.572  1.00 35.49           O  
ANISOU 5575  O   ASN A 721     4128   4655   4702   -174    -75    253       O  
ATOM   5576  CB  ASN A 721     151.379  94.899  10.881  1.00 35.28           C  
ANISOU 5576  CB  ASN A 721     4086   4629   4689   -166    -58    239       C  
ATOM   5577  CG  ASN A 721     151.197  94.881   9.368  1.00 34.74           C  
ANISOU 5577  CG  ASN A 721     4023   4551   4626   -161    -47    233       C  
ATOM   5578  OD1 ASN A 721     150.142  95.270   8.858  1.00 33.80           O  
ANISOU 5578  OD1 ASN A 721     3922   4417   4504   -161    -41    233       O  
ATOM   5579  ND2 ASN A 721     152.216  94.435   8.642  1.00 34.13           N  
ANISOU 5579  ND2 ASN A 721     3929   4483   4556   -157    -45    227       N  
ATOM   5580  N   GLU A 722     151.725  96.644  13.749  1.00 36.93           N  
ANISOU 5580  N   GLU A 722     4297   4860   4874   -199    -68    241       N  
ATOM   5581  CA  GLU A 722     151.941  96.381  15.188  1.00 41.14           C  
ANISOU 5581  CA  GLU A 722     4823   5406   5402   -202    -81    247       C  
ATOM   5582  C   GLU A 722     151.692  97.590  16.074  1.00 39.60           C  
ANISOU 5582  C   GLU A 722     4638   5215   5194   -221    -78    244       C  
ATOM   5583  O   GLU A 722     152.084  97.604  17.222  1.00 43.82           O  
ANISOU 5583  O   GLU A 722     5164   5763   5721   -227    -87    247       O  
ATOM   5584  CB  GLU A 722     153.343  95.795  15.416  1.00 42.94           C  
ANISOU 5584  CB  GLU A 722     5027   5653   5635   -198    -90    247       C  
ATOM   5585  CG  GLU A 722     153.498  94.439  14.755  1.00 47.15           C  
ANISOU 5585  CG  GLU A 722     5550   6182   6182   -177    -95    251       C  
ATOM   5586  CD  GLU A 722     154.876  93.801  14.940  1.00 54.09           C  
ANISOU 5586  CD  GLU A 722     6405   7080   7068   -171   -104    250       C  
ATOM   5587  OE1 GLU A 722     155.861  94.489  15.287  1.00 61.86           O  
ANISOU 5587  OE1 GLU A 722     7377   8081   8045   -184   -104    243       O  
ATOM   5588  OE2 GLU A 722     154.988  92.585  14.704  1.00 60.69           O  
ANISOU 5588  OE2 GLU A 722     7233   7912   7916   -152   -112    255       O  
ATOM   5589  N   ASN A 723     151.040  98.604  15.539  1.00 38.27           N  
ANISOU 5589  N   ASN A 723     4487   5034   5022   -229    -66    238       N  
ATOM   5590  CA  ASN A 723     150.743  99.795  16.294  1.00 38.98           C  
ANISOU 5590  CA  ASN A 723     4587   5125   5100   -247    -62    233       C  
ATOM   5591  C   ASN A 723     149.705 100.602  15.537  1.00 38.97           C  
ANISOU 5591  C   ASN A 723     4607   5103   5097   -249    -51    228       C  
ATOM   5592  O   ASN A 723     150.014 101.171  14.505  1.00 37.48           O  
ANISOU 5592  O   ASN A 723     4422   4910   4910   -253    -41    222       O  
ATOM   5593  CB  ASN A 723     152.006 100.674  16.518  1.00 40.87           C  
ANISOU 5593  CB  ASN A 723     4816   5381   5333   -265    -59    224       C  
ATOM   5594  CG  ASN A 723     151.794 101.727  17.615  1.00 43.46           C  
ANISOU 5594  CG  ASN A 723     5151   5714   5649   -283    -58    220       C  
ATOM   5595  OD1 ASN A 723     150.712 102.300  17.766  1.00 41.72           O  
ANISOU 5595  OD1 ASN A 723     4948   5479   5424   -286    -54    218       O  
ATOM   5596  ND2 ASN A 723     152.821 101.947  18.421  1.00 46.65           N  
ANISOU 5596  ND2 ASN A 723     5540   6138   6046   -295    -63    216       N  
ATOM   5597  N   LYS A 724     148.507 100.652  16.096  1.00 38.65           N  
ANISOU 5597  N   LYS A 724     4579   5053   5054   -246    -53    231       N  
ATOM   5598  CA  LYS A 724     147.353 101.349  15.548  1.00 41.70           C  
ANISOU 5598  CA  LYS A 724     4985   5420   5439   -246    -45    227       C  
ATOM   5599  C   LYS A 724     147.222 102.808  15.965  1.00 42.15           C  
ANISOU 5599  C   LYS A 724     5054   5474   5487   -263    -38    218       C  
ATOM   5600  O   LYS A 724     146.320 103.520  15.492  1.00 40.28           O  
ANISOU 5600  O   LYS A 724     4834   5221   5249   -263    -31    214       O  
ATOM   5601  CB  LYS A 724     146.070 100.648  16.016  1.00 43.27           C  
ANISOU 5601  CB  LYS A 724     5191   5610   5639   -234    -50    233       C  
ATOM   5602  CG  LYS A 724     145.703 100.939  17.471  1.00 45.15           C  
ANISOU 5602  CG  LYS A 724     5431   5856   5869   -244    -55    233       C  
ATOM   5603  CD  LYS A 724     144.471 100.201  17.958  1.00 47.17           C  
ANISOU 5603  CD  LYS A 724     5692   6105   6125   -235    -60    238       C  
ATOM   5604  CE  LYS A 724     144.729  98.726  18.185  1.00 49.48           C  
ANISOU 5604  CE  LYS A 724     5973   6404   6423   -223    -70    250       C  
ATOM   5605  NZ  LYS A 724     143.460  97.961  17.972  1.00 52.40           N  
ANISOU 5605  NZ  LYS A 724     6351   6761   6798   -210    -71    254       N  
ATOM   5606  N   ASN A 725     148.068 103.260  16.871  1.00 40.99           N  
ANISOU 5606  N   ASN A 725     4898   5343   5333   -278    -40    215       N  
ATOM   5607  CA  ASN A 725     147.951 104.632  17.317  1.00 43.13           C  
ANISOU 5607  CA  ASN A 725     5179   5611   5595   -295    -33    206       C  
ATOM   5608  C   ASN A 725     148.002 105.649  16.159  1.00 40.40           C  
ANISOU 5608  C   ASN A 725     4847   5251   5250   -301    -21    199       C  
ATOM   5609  O   ASN A 725     148.936 105.661  15.403  1.00 40.10           O  
ANISOU 5609  O   ASN A 725     4803   5219   5215   -304    -17    198       O  
ATOM   5610  CB  ASN A 725     148.994 104.956  18.366  1.00 46.00           C  
ANISOU 5610  CB  ASN A 725     5530   5996   5952   -312    -37    202       C  
ATOM   5611  CG  ASN A 725     148.604 106.177  19.173  1.00 50.66           C  
ANISOU 5611  CG  ASN A 725     6132   6584   6533   -328    -33    193       C  
ATOM   5612  OD1 ASN A 725     148.611 107.301  18.680  1.00 51.18           O  
ANISOU 5612  OD1 ASN A 725     6210   6639   6597   -338    -23    185       O  
ATOM   5613  ND2 ASN A 725     148.200 105.952  20.398  1.00 57.10           N  
ANISOU 5613  ND2 ASN A 725     6944   7408   7342   -330    -40    195       N  
ATOM   5614  N   VAL A 726     146.977 106.488  16.051  1.00 40.55           N  
ANISOU 5614  N   VAL A 726     4886   5253   5269   -302    -16    195       N  
ATOM   5615  CA  VAL A 726     146.840 107.483  14.982  1.00 42.12           C  
ANISOU 5615  CA  VAL A 726     5101   5434   5467   -307     -6    190       C  
ATOM   5616  C   VAL A 726     147.904 108.566  15.012  1.00 43.04           C  
ANISOU 5616  C   VAL A 726     5218   5557   5578   -328      2    182       C  
ATOM   5617  O   VAL A 726     148.065 109.228  14.009  1.00 43.10           O  
ANISOU 5617  O   VAL A 726     5237   5553   5586   -332     10    180       O  
ATOM   5618  CB  VAL A 726     145.441 108.204  14.928  1.00 42.97           C  
ANISOU 5618  CB  VAL A 726     5230   5521   5575   -302     -3    186       C  
ATOM   5619  CG1 VAL A 726     144.310 107.190  14.663  1.00 44.63           C  
ANISOU 5619  CG1 VAL A 726     5441   5723   5791   -281     -8    192       C  
ATOM   5620  CG2 VAL A 726     145.156 109.038  16.188  1.00 42.12           C  
ANISOU 5620  CG2 VAL A 726     5127   5416   5461   -315     -3    178       C  
ATOM   5621  N   ASN A 727     148.577 108.759  16.149  1.00 45.22           N  
ANISOU 5621  N   ASN A 727     5483   5850   5848   -342     -1    178       N  
ATOM   5622  CA  ASN A 727     149.673 109.750  16.289  1.00 47.87           C  
ANISOU 5622  CA  ASN A 727     5817   6195   6178   -364      5    170       C  
ATOM   5623  C   ASN A 727     151.081 109.188  16.293  1.00 46.55           C  
ANISOU 5623  C   ASN A 727     5627   6051   6010   -369      3    170       C  
ATOM   5624  O   ASN A 727     152.026 109.926  16.464  1.00 48.36           O  
ANISOU 5624  O   ASN A 727     5851   6289   6234   -388      8    163       O  
ATOM   5625  CB  ASN A 727     149.449 110.586  17.556  1.00 48.39           C  
ANISOU 5625  CB  ASN A 727     5887   6264   6236   -378      5    162       C  
ATOM   5626  CG  ASN A 727     148.172 111.390  17.470  1.00 50.11           C  
ANISOU 5626  CG  ASN A 727     6127   6458   6455   -375      9    158       C  
ATOM   5627  OD1 ASN A 727     147.914 112.066  16.477  1.00 55.09           O  
ANISOU 5627  OD1 ASN A 727     6774   7069   7088   -375     17    156       O  
ATOM   5628  ND2 ASN A 727     147.338 111.269  18.462  1.00 51.80           N  
ANISOU 5628  ND2 ASN A 727     6342   6673   6667   -371      4    157       N  
ATOM   5629  N   LYS A 728     151.231 107.896  16.063  1.00 46.31           N  
ANISOU 5629  N   LYS A 728     5582   6029   5986   -353     -5    179       N  
ATOM   5630  CA  LYS A 728     152.556 107.299  16.008  1.00 47.03           C  
ANISOU 5630  CA  LYS A 728     5650   6141   6078   -356     -8    178       C  
ATOM   5631  C   LYS A 728     153.219 107.522  14.630  1.00 47.13           C  
ANISOU 5631  C   LYS A 728     5663   6150   6093   -359      3    175       C  
ATOM   5632  O   LYS A 728     152.631 107.226  13.565  1.00 41.71           O  
ANISOU 5632  O   LYS A 728     4987   5447   5412   -346      6    179       O  
ATOM   5633  CB  LYS A 728     152.454 105.823  16.303  1.00 48.28           C  
ANISOU 5633  CB  LYS A 728     5793   6308   6242   -336    -20    188       C  
ATOM   5634  CG  LYS A 728     153.756 105.054  16.205  1.00 50.20           C  
ANISOU 5634  CG  LYS A 728     6012   6572   6489   -334    -25    189       C  
ATOM   5635  CD  LYS A 728     154.711 105.414  17.329  1.00 52.61           C  
ANISOU 5635  CD  LYS A 728     6303   6901   6787   -350    -30    183       C  
ATOM   5636  CE  LYS A 728     156.110 104.916  16.986  1.00 55.97           C  
ANISOU 5636  CE  LYS A 728     6704   7346   7215   -351    -32    180       C  
ATOM   5637  NZ  LYS A 728     156.691 104.208  18.133  1.00 57.90           N  
ANISOU 5637  NZ  LYS A 728     6929   7613   7459   -347    -47    184       N  
ATOM   5638  N   GLU A 729     154.455 108.012  14.675  1.00 46.36           N  
ANISOU 5638  N   GLU A 729     5555   6069   5992   -377      7    167       N  
ATOM   5639  CA  GLU A 729     155.244 108.271  13.492  1.00 46.47           C  
ANISOU 5639  CA  GLU A 729     5567   6083   6006   -384     18    163       C  
ATOM   5640  C   GLU A 729     155.896 106.972  13.045  1.00 43.03           C  
ANISOU 5640  C   GLU A 729     5109   5662   5579   -369     12    166       C  
ATOM   5641  O   GLU A 729     156.391 106.206  13.860  1.00 44.11           O  
ANISOU 5641  O   GLU A 729     5225   5817   5717   -363      1    168       O  
ATOM   5642  CB  GLU A 729     156.328 109.343  13.747  1.00 50.81           C  
ANISOU 5642  CB  GLU A 729     6113   6645   6548   -411     26    151       C  
ATOM   5643  CG  GLU A 729     156.497 110.301  12.559  1.00 57.41           C  
ANISOU 5643  CG  GLU A 729     6966   7468   7381   -425     41    146       C  
ATOM   5644  CD  GLU A 729     157.873 110.993  12.439  1.00 63.75           C  
ANISOU 5644  CD  GLU A 729     7757   8287   8177   -451     51    134       C  
ATOM   5645  OE1 GLU A 729     158.757 110.862  13.346  1.00 59.96           O  
ANISOU 5645  OE1 GLU A 729     7256   7831   7695   -459     45    129       O  
ATOM   5646  OE2 GLU A 729     158.065 111.670  11.391  1.00 65.67           O  
ANISOU 5646  OE2 GLU A 729     8015   8520   8418   -462     63    131       O  
ATOM   5647  N   HIS A 730     155.912 106.748  11.742  1.00 40.30           N  
ANISOU 5647  N   HIS A 730     4768   5308   5238   -363     19    167       N  
ATOM   5648  CA  HIS A 730     156.642 105.625  11.146  1.00 40.48           C  
ANISOU 5648  CA  HIS A 730     4769   5344   5268   -351     16    167       C  
ATOM   5649  C   HIS A 730     157.606 106.153  10.099  1.00 39.15           C  
ANISOU 5649  C   HIS A 730     4597   5181   5097   -366     29    158       C  
ATOM   5650  O   HIS A 730     157.236 107.040   9.359  1.00 36.50           O  
ANISOU 5650  O   HIS A 730     4282   4829   4755   -377     41    156       O  
ATOM   5651  CB  HIS A 730     155.654 104.643  10.496  1.00 40.51           C  
ANISOU 5651  CB  HIS A 730     4779   5332   5280   -327     12    176       C  
ATOM   5652  CG  HIS A 730     154.605 104.153  11.443  1.00 40.62           C  
ANISOU 5652  CG  HIS A 730     4798   5338   5296   -313      1    185       C  
ATOM   5653  ND1 HIS A 730     154.855 103.173  12.378  1.00 40.61           N  
ANISOU 5653  ND1 HIS A 730     4779   5350   5299   -302    -13    190       N  
ATOM   5654  CD2 HIS A 730     153.330 104.562  11.652  1.00 39.82           C  
ANISOU 5654  CD2 HIS A 730     4719   5218   5193   -310      1    189       C  
ATOM   5655  CE1 HIS A 730     153.768 102.979  13.106  1.00 42.27           C  
ANISOU 5655  CE1 HIS A 730     5001   5552   5510   -294    -20    197       C  
ATOM   5656  NE2 HIS A 730     152.827 103.810  12.683  1.00 41.21           N  
ANISOU 5656  NE2 HIS A 730     4889   5397   5371   -298    -12    196       N  
ATOM   5657  N   ILE A 731     158.823 105.606  10.076  1.00 42.58           N  
ANISOU 5657  N   ILE A 731     5006   5639   5534   -368     28    151       N  
ATOM   5658  CA  ILE A 731     159.858 105.882   9.067  1.00 47.03           C  
ANISOU 5658  CA  ILE A 731     5560   6213   6096   -381     40    141       C  
ATOM   5659  C   ILE A 731     160.259 104.511   8.509  1.00 45.67           C  
ANISOU 5659  C   ILE A 731     5367   6051   5935   -361     34    142       C  
ATOM   5660  O   ILE A 731     160.715 103.660   9.263  1.00 46.69           O  
ANISOU 5660  O   ILE A 731     5474   6196   6070   -350     22    143       O  
ATOM   5661  CB  ILE A 731     161.178 106.466   9.656  1.00 52.00           C  
ANISOU 5661  CB  ILE A 731     6171   6866   6719   -404     43    129       C  
ATOM   5662  CG1 ILE A 731     160.953 107.483  10.786  1.00 56.06           C  
ANISOU 5662  CG1 ILE A 731     6697   7379   7224   -420     41    128       C  
ATOM   5663  CG2 ILE A 731     162.062 107.050   8.551  1.00 54.03           C  
ANISOU 5663  CG2 ILE A 731     6427   7130   6971   -423     59    118       C  
ATOM   5664  CD1 ILE A 731     160.224 108.732  10.394  1.00 58.13           C  
ANISOU 5664  CD1 ILE A 731     6990   7617   7478   -435     53    129       C  
ATOM   5665  N   ILE A 732     160.094 104.287   7.211  1.00 43.04           N  
ANISOU 5665  N   ILE A 732     5041   5709   5605   -356     43    141       N  
ATOM   5666  CA  ILE A 732     160.610 103.073   6.585  1.00 43.23           C  
ANISOU 5666  CA  ILE A 732     5043   5744   5640   -339     40    139       C  
ATOM   5667  C   ILE A 732     161.297 103.398   5.267  1.00 42.28           C  
ANISOU 5667  C   ILE A 732     4921   5629   5516   -353     56    128       C  
ATOM   5668  O   ILE A 732     161.179 104.520   4.737  1.00 40.12           O  
ANISOU 5668  O   ILE A 732     4667   5345   5231   -373     69    126       O  
ATOM   5669  CB  ILE A 732     159.507 102.019   6.359  1.00 46.04           C  
ANISOU 5669  CB  ILE A 732     5406   6083   6005   -313     32    150       C  
ATOM   5670  CG1 ILE A 732     158.470 102.527   5.341  1.00 48.69           C  
ANISOU 5670  CG1 ILE A 732     5770   6394   6336   -314     42    154       C  
ATOM   5671  CG2 ILE A 732     158.847 101.683   7.686  1.00 46.15           C  
ANISOU 5671  CG2 ILE A 732     5422   6093   6021   -302     17    160       C  
ATOM   5672  CD1 ILE A 732     157.384 101.533   5.020  1.00 50.31           C  
ANISOU 5672  CD1 ILE A 732     5982   6584   6550   -289     35    163       C  
ATOM   5673  N   GLU A 733     161.998 102.396   4.745  1.00 41.02           N  
ANISOU 5673  N   GLU A 733     4737   5482   5365   -341     55    122       N  
ATOM   5674  CA  GLU A 733     162.671 102.492   3.455  1.00 42.63           C  
ANISOU 5674  CA  GLU A 733     4936   5694   5566   -351     69    111       C  
ATOM   5675  C   GLU A 733     162.104 101.418   2.520  1.00 40.62           C  
ANISOU 5675  C   GLU A 733     4682   5430   5322   -328     68    115       C  
ATOM   5676  O   GLU A 733     162.006 100.271   2.897  1.00 40.17           O  
ANISOU 5676  O   GLU A 733     4610   5375   5277   -306     56    118       O  
ATOM   5677  CB  GLU A 733     164.203 102.371   3.634  1.00 42.97           C  
ANISOU 5677  CB  GLU A 733     4948   5768   5612   -361     71     96       C  
ATOM   5678  CG  GLU A 733     164.996 102.282   2.351  1.00 47.04           C  
ANISOU 5678  CG  GLU A 733     5452   6294   6126   -370     86     83       C  
ATOM   5679  CD  GLU A 733     166.499 102.027   2.582  1.00 48.65           C  
ANISOU 5679  CD  GLU A 733     5621   6531   6334   -377     86     66       C  
ATOM   5680  OE1 GLU A 733     167.200 102.922   3.094  1.00 50.81           O  
ANISOU 5680  OE1 GLU A 733     5890   6818   6599   -400     90     59       O  
ATOM   5681  OE2 GLU A 733     166.968 100.927   2.258  1.00 50.33           O  
ANISOU 5681  OE2 GLU A 733     5810   6755   6558   -359     81     60       O  
ATOM   5682  N   ILE A 734     161.751 101.822   1.305  1.00 40.83           N  
ANISOU 5682  N   ILE A 734     4726   5445   5342   -336     82    114       N  
ATOM   5683  CA  ILE A 734     161.387 100.925   0.219  1.00 44.84           C  
ANISOU 5683  CA  ILE A 734     5234   5947   5857   -320     84    114       C  
ATOM   5684  C   ILE A 734     162.212 101.303  -0.991  1.00 44.39           C  
ANISOU 5684  C   ILE A 734     5172   5901   5793   -338    101    101       C  
ATOM   5685  O   ILE A 734     162.225 102.479  -1.407  1.00 43.23           O  
ANISOU 5685  O   ILE A 734     5044   5748   5632   -361    113    100       O  
ATOM   5686  CB  ILE A 734     159.882 101.058  -0.140  1.00 47.32           C  
ANISOU 5686  CB  ILE A 734     5578   6233   6169   -310     83    127       C  
ATOM   5687  CG1 ILE A 734     159.014 100.633   1.049  1.00 46.03           C  
ANISOU 5687  CG1 ILE A 734     5418   6058   6012   -292     67    139       C  
ATOM   5688  CG2 ILE A 734     159.537 100.248  -1.402  1.00 48.67           C  
ANISOU 5688  CG2 ILE A 734     5749   6398   6344   -297     87    126       C  
ATOM   5689  CD1 ILE A 734     157.554 101.057   0.905  1.00 46.33           C  
ANISOU 5689  CD1 ILE A 734     5487   6071   6045   -288     66    151       C  
ATOM   5690  N   LYS A 735     162.921 100.319  -1.537  1.00 48.82           N  
ANISOU 5690  N   LYS A 735     5708   6478   6364   -328    102     91       N  
ATOM   5691  CA  LYS A 735     163.832 100.485  -2.717  1.00 50.34           C  
ANISOU 5691  CA  LYS A 735     5890   6685   6550   -344    118     76       C  
ATOM   5692  C   LYS A 735     164.714 101.705  -2.604  1.00 49.17           C  
ANISOU 5692  C   LYS A 735     5744   6551   6389   -375    130     67       C  
ATOM   5693  O   LYS A 735     164.913 102.443  -3.568  1.00 51.08           O  
ANISOU 5693  O   LYS A 735     5998   6792   6618   -397    146     62       O  
ATOM   5694  CB  LYS A 735     163.055 100.509  -4.043  1.00 55.50           C  
ANISOU 5694  CB  LYS A 735     6566   7323   7198   -343    128     79       C  
ATOM   5695  CG  LYS A 735     162.288  99.209  -4.337  1.00 60.89           C  
ANISOU 5695  CG  LYS A 735     7245   7995   7895   -313    119     84       C  
ATOM   5696  CD  LYS A 735     163.162  98.139  -4.979  1.00 66.83           C  
ANISOU 5696  CD  LYS A 735     7968   8767   8658   -304    122     69       C  
ATOM   5697  CE  LYS A 735     162.320  97.020  -5.595  1.00 72.77           C  
ANISOU 5697  CE  LYS A 735     8723   9505   9420   -279    118     73       C  
ATOM   5698  NZ  LYS A 735     161.489  96.252  -4.609  1.00 75.68           N  
ANISOU 5698  NZ  LYS A 735     9093   9860   9802   -253    100     86       N  
ATOM   5699  N   GLY A 736     165.245 101.909  -1.406  1.00 47.72           N  
ANISOU 5699  N   GLY A 736     5546   6378   6207   -379    122     66       N  
ATOM   5700  CA  GLY A 736     166.169 102.987  -1.147  1.00 48.96           C  
ANISOU 5700  CA  GLY A 736     5699   6550   6352   -409    131     56       C  
ATOM   5701  C   GLY A 736     165.535 104.309  -0.806  1.00 47.24           C  
ANISOU 5701  C   GLY A 736     5514   6314   6122   -428    135     66       C  
ATOM   5702  O   GLY A 736     166.236 105.246  -0.493  1.00 44.91           O  
ANISOU 5702  O   GLY A 736     5217   6028   5817   -453    143     59       O  
ATOM   5703  N   LYS A 737     164.209 104.390  -0.857  1.00 47.80           N  
ANISOU 5703  N   LYS A 737     5612   6358   6192   -416    130     81       N  
ATOM   5704  CA  LYS A 737     163.507 105.654  -0.600  1.00 47.07           C  
ANISOU 5704  CA  LYS A 737     5552   6245   6088   -432    134     91       C  
ATOM   5705  C   LYS A 737     162.765 105.652   0.759  1.00 46.12           C  
ANISOU 5705  C   LYS A 737     5437   6114   5972   -419    118    101       C  
ATOM   5706  O   LYS A 737     162.066 104.677   1.132  1.00 42.57           O  
ANISOU 5706  O   LYS A 737     4983   5658   5533   -392    105    109       O  
ATOM   5707  CB  LYS A 737     162.573 105.949  -1.761  1.00 51.18           C  
ANISOU 5707  CB  LYS A 737     6101   6742   6601   -431    142     99       C  
ATOM   5708  CG  LYS A 737     161.984 107.339  -1.708  1.00 58.58           C  
ANISOU 5708  CG  LYS A 737     7072   7659   7525   -450    147    106       C  
ATOM   5709  CD  LYS A 737     161.675 107.869  -3.099  1.00 64.13           C  
ANISOU 5709  CD  LYS A 737     7800   8350   8218   -461    161    109       C  
ATOM   5710  CE  LYS A 737     161.061 109.266  -3.027  1.00 67.59           C  
ANISOU 5710  CE  LYS A 737     8273   8764   8644   -478    165    117       C  
ATOM   5711  NZ  LYS A 737     159.677 109.215  -2.475  1.00 65.22           N  
ANISOU 5711  NZ  LYS A 737     7991   8440   8349   -457    152    131       N  
ATOM   5712  N   GLU A 738     162.937 106.748   1.494  1.00 45.13           N  
ANISOU 5712  N   GLU A 738     5322   5988   5839   -439    121    100       N  
ATOM   5713  CA  GLU A 738     162.332 106.937   2.795  1.00 45.30           C  
ANISOU 5713  CA  GLU A 738     5349   6001   5862   -432    108    108       C  
ATOM   5714  C   GLU A 738     160.843 107.303   2.687  1.00 43.64           C  
ANISOU 5714  C   GLU A 738     5172   5761   5650   -423    105    122       C  
ATOM   5715  O   GLU A 738     160.485 108.112   1.860  1.00 42.35           O  
ANISOU 5715  O   GLU A 738     5033   5582   5478   -435    116    124       O  
ATOM   5716  CB  GLU A 738     163.061 108.025   3.562  1.00 48.27           C  
ANISOU 5716  CB  GLU A 738     5724   6388   6229   -459    113    101       C  
ATOM   5717  CG  GLU A 738     162.702 108.037   5.038  1.00 52.87           C  
ANISOU 5717  CG  GLU A 738     6304   6970   6814   -452     99    106       C  
ATOM   5718  CD  GLU A 738     163.492 109.050   5.846  1.00 55.93           C  
ANISOU 5718  CD  GLU A 738     6687   7370   7193   -478    103     97       C  
ATOM   5719  OE1 GLU A 738     164.456 108.623   6.537  1.00 56.81           O  
ANISOU 5719  OE1 GLU A 738     6770   7509   7308   -480     97     88       O  
ATOM   5720  OE2 GLU A 738     163.117 110.255   5.793  1.00 56.83           O  
ANISOU 5720  OE2 GLU A 738     6827   7467   7297   -497    112     98       O  
ATOM   5721  N   TYR A 739     159.990 106.679   3.504  1.00 40.86           N  
ANISOU 5721  N   TYR A 739     4819   5400   5306   -401     91    131       N  
ATOM   5722  CA  TYR A 739     158.562 107.072   3.605  1.00 40.76           C  
ANISOU 5722  CA  TYR A 739     4836   5361   5292   -392     87    143       C  
ATOM   5723  C   TYR A 739     158.227 107.287   5.066  1.00 39.91           C  
ANISOU 5723  C   TYR A 739     4727   5252   5184   -391     76    146       C  
ATOM   5724  O   TYR A 739     158.502 106.431   5.916  1.00 40.17           O  
ANISOU 5724  O   TYR A 739     4739   5300   5225   -379     65    147       O  
ATOM   5725  CB  TYR A 739     157.615 106.011   3.044  1.00 40.32           C  
ANISOU 5725  CB  TYR A 739     4782   5293   5244   -365     81    151       C  
ATOM   5726  CG  TYR A 739     157.728 105.822   1.570  1.00 40.61           C  
ANISOU 5726  CG  TYR A 739     4823   5327   5279   -366     91    149       C  
ATOM   5727  CD1 TYR A 739     158.729 104.996   1.040  1.00 42.01           C  
ANISOU 5727  CD1 TYR A 739     4975   5524   5461   -364     94    140       C  
ATOM   5728  CD2 TYR A 739     156.848 106.469   0.681  1.00 39.69           C  
ANISOU 5728  CD2 TYR A 739     4736   5189   5156   -368     97    155       C  
ATOM   5729  CE1 TYR A 739     158.866 104.826  -0.325  1.00 40.83           C  
ANISOU 5729  CE1 TYR A 739     4829   5375   5309   -365    104    137       C  
ATOM   5730  CE2 TYR A 739     156.970 106.294  -0.686  1.00 39.15           C  
ANISOU 5730  CE2 TYR A 739     4672   5120   5084   -370    107    153       C  
ATOM   5731  CZ  TYR A 739     157.997 105.474  -1.179  1.00 41.55           C  
ANISOU 5731  CZ  TYR A 739     4950   5445   5393   -369    111    143       C  
ATOM   5732  OH  TYR A 739     158.164 105.287  -2.534  1.00 42.64           O  
ANISOU 5732  OH  TYR A 739     5090   5583   5526   -372    121    140       O  
ATOM   5733  N   ARG A 740     157.581 108.413   5.322  1.00 40.81           N  
ANISOU 5733  N   ARG A 740     4866   5348   5290   -402     80    149       N  
ATOM   5734  CA  ARG A 740     157.332 108.941   6.655  1.00 43.39           C  
ANISOU 5734  CA  ARG A 740     5196   5674   5615   -407     73    149       C  
ATOM   5735  C   ARG A 740     155.852 109.291   6.747  1.00 40.26           C  
ANISOU 5735  C   ARG A 740     4827   5252   5219   -396     70    158       C  
ATOM   5736  O   ARG A 740     155.340 109.937   5.877  1.00 39.76           O  
ANISOU 5736  O   ARG A 740     4786   5170   5152   -400     77    160       O  
ATOM   5737  CB  ARG A 740     158.190 110.192   6.849  1.00 50.16           C  
ANISOU 5737  CB  ARG A 740     6057   6538   6463   -437     84    140       C  
ATOM   5738  CG  ARG A 740     158.204 110.797   8.237  1.00 58.09           C  
ANISOU 5738  CG  ARG A 740     7061   7547   7464   -447     79    137       C  
ATOM   5739  CD  ARG A 740     158.970 112.112   8.235  1.00 63.89           C  
ANISOU 5739  CD  ARG A 740     7803   8283   8188   -478     91    127       C  
ATOM   5740  NE  ARG A 740     160.356 111.949   7.781  1.00 72.62           N  
ANISOU 5740  NE  ARG A 740     8888   9413   9293   -493     98    117       N  
ATOM   5741  CZ  ARG A 740     161.429 111.779   8.566  1.00 78.51           C  
ANISOU 5741  CZ  ARG A 740     9607  10186  10038   -502     95    108       C  
ATOM   5742  NH1 ARG A 740     161.321 111.728   9.891  1.00 83.53           N  
ANISOU 5742  NH1 ARG A 740    10235  10830  10674   -500     85    108       N  
ATOM   5743  NH2 ARG A 740     162.635 111.647   8.016  1.00 79.31           N  
ANISOU 5743  NH2 ARG A 740     9689  10308  10137   -515    103     98       N  
ATOM   5744  N   TRP A 741     155.156 108.842   7.786  1.00 38.70           N  
ANISOU 5744  N   TRP A 741     4626   5053   5026   -383     58    163       N  
ATOM   5745  CA  TRP A 741     153.717 109.164   7.965  1.00 36.75           C  
ANISOU 5745  CA  TRP A 741     4401   4781   4779   -372     54    170       C  
ATOM   5746  C   TRP A 741     153.354 108.913   9.411  1.00 36.54           C  
ANISOU 5746  C   TRP A 741     4367   4761   4754   -367     43    171       C  
ATOM   5747  O   TRP A 741     154.160 108.317  10.172  1.00 37.09           O  
ANISOU 5747  O   TRP A 741     4414   4853   4826   -368     37    169       O  
ATOM   5748  CB  TRP A 741     152.814 108.336   7.007  1.00 36.36           C  
ANISOU 5748  CB  TRP A 741     4359   4720   4737   -350     52    177       C  
ATOM   5749  CG  TRP A 741     152.635 106.881   7.443  1.00 34.26           C  
ANISOU 5749  CG  TRP A 741     4074   4464   4480   -328     40    182       C  
ATOM   5750  CD1 TRP A 741     151.574 106.348   8.096  1.00 33.70           C  
ANISOU 5750  CD1 TRP A 741     4006   4385   4413   -312     30    188       C  
ATOM   5751  CD2 TRP A 741     153.595 105.805   7.292  1.00 33.13           C  
ANISOU 5751  CD2 TRP A 741     3905   4341   4343   -322     37    181       C  
ATOM   5752  NE1 TRP A 741     151.800 105.007   8.361  1.00 32.59           N  
ANISOU 5752  NE1 TRP A 741     3845   4257   4281   -296     21    192       N  
ATOM   5753  CE2 TRP A 741     153.021 104.645   7.869  1.00 31.70           C  
ANISOU 5753  CE2 TRP A 741     3714   4161   4170   -301     25    187       C  
ATOM   5754  CE3 TRP A 741     154.853 105.718   6.713  1.00 33.42           C  
ANISOU 5754  CE3 TRP A 741     3925   4393   4378   -332     44    174       C  
ATOM   5755  CZ2 TRP A 741     153.672 103.409   7.907  1.00 31.95           C  
ANISOU 5755  CZ2 TRP A 741     3722   4209   4210   -289     18    188       C  
ATOM   5756  CZ3 TRP A 741     155.512 104.500   6.736  1.00 35.29           C  
ANISOU 5756  CZ3 TRP A 741     4137   4647   4624   -320     37    173       C  
ATOM   5757  CH2 TRP A 741     154.909 103.340   7.335  1.00 34.79           C  
ANISOU 5757  CH2 TRP A 741     4065   4583   4569   -298     24    180       C  
ATOM   5758  N   THR A 742     152.168 109.378   9.819  1.00 36.03           N  
ANISOU 5758  N   THR A 742     4322   4679   4690   -362     40    174       N  
ATOM   5759  CA  THR A 742     151.646 109.014  11.140  1.00 39.80           C  
ANISOU 5759  CA  THR A 742     4793   5161   5168   -354     30    176       C  
ATOM   5760  C   THR A 742     150.360 108.172  11.062  1.00 38.93           C  
ANISOU 5760  C   THR A 742     4689   5039   5065   -331     22    184       C  
ATOM   5761  O   THR A 742     149.514 108.380  10.199  1.00 37.03           O  
ANISOU 5761  O   THR A 742     4465   4779   4825   -323     26    187       O  
ATOM   5762  CB  THR A 742     151.299 110.234  12.023  1.00 42.50           C  
ANISOU 5762  CB  THR A 742     5150   5496   5504   -369     32    170       C  
ATOM   5763  OG1 THR A 742     150.333 111.013  11.338  1.00 46.96           O  
ANISOU 5763  OG1 THR A 742     5740   6035   6068   -367     37    171       O  
ATOM   5764  CG2 THR A 742     152.545 111.076  12.328  1.00 44.02           C  
ANISOU 5764  CG2 THR A 742     5336   5702   5689   -395     39    161       C  
ATOM   5765  N   GLY A 743     150.213 107.257  12.000  1.00 38.59           N  
ANISOU 5765  N   GLY A 743     4631   5007   5025   -321     11    188       N  
ATOM   5766  CA  GLY A 743     149.047 106.393  12.044  1.00 38.78           C  
ANISOU 5766  CA  GLY A 743     4659   5022   5055   -300      4    195       C  
ATOM   5767  C   GLY A 743     149.224 105.082  11.320  1.00 39.09           C  
ANISOU 5767  C   GLY A 743     4685   5065   5102   -283      1    201       C  
ATOM   5768  O   GLY A 743     150.294 104.788  10.756  1.00 36.39           O  
ANISOU 5768  O   GLY A 743     4330   4734   4761   -287      3    199       O  
ATOM   5769  N   PRO A 744     148.171 104.251  11.340  1.00 37.98           N  
ANISOU 5769  N   PRO A 744     4548   4916   4967   -265     -6    207       N  
ATOM   5770  CA  PRO A 744     148.414 102.880  10.914  1.00 36.73           C  
ANISOU 5770  CA  PRO A 744     4374   4763   4816   -250    -11    212       C  
ATOM   5771  C   PRO A 744     148.516 102.630   9.400  1.00 33.39           C  
ANISOU 5771  C   PRO A 744     3955   4334   4399   -243     -4    212       C  
ATOM   5772  O   PRO A 744     148.917 101.559   8.994  1.00 32.27           O  
ANISOU 5772  O   PRO A 744     3799   4199   4264   -232     -7    214       O  
ATOM   5773  CB  PRO A 744     147.271 102.110  11.594  1.00 37.63           C  
ANISOU 5773  CB  PRO A 744     4491   4872   4934   -236    -19    219       C  
ATOM   5774  CG  PRO A 744     146.154 103.096  11.663  1.00 38.81           C  
ANISOU 5774  CG  PRO A 744     4661   5005   5078   -239    -15    216       C  
ATOM   5775  CD  PRO A 744     146.830 104.424  11.917  1.00 39.29           C  
ANISOU 5775  CD  PRO A 744     4727   5069   5131   -259     -9    208       C  
ATOM   5776  N   TYR A 745     148.134 103.581   8.566  1.00 33.67           N  
ANISOU 5776  N   TYR A 745     4008   4355   4429   -249      5    209       N  
ATOM   5777  CA  TYR A 745     148.287 103.418   7.133  1.00 33.81           C  
ANISOU 5777  CA  TYR A 745     4030   4368   4450   -245     12    208       C  
ATOM   5778  C   TYR A 745     148.512 104.742   6.440  1.00 35.74           C  
ANISOU 5778  C   TYR A 745     4290   4604   4685   -261     23    204       C  
ATOM   5779  O   TYR A 745     148.234 105.805   6.990  1.00 33.85           O  
ANISOU 5779  O   TYR A 745     4063   4357   4440   -272     24    202       O  
ATOM   5780  CB  TYR A 745     147.103 102.699   6.511  1.00 34.41           C  
ANISOU 5780  CB  TYR A 745     4113   4430   4531   -225      9    213       C  
ATOM   5781  CG  TYR A 745     145.932 103.583   6.288  1.00 33.54           C  
ANISOU 5781  CG  TYR A 745     4026   4301   4416   -225     12    213       C  
ATOM   5782  CD1 TYR A 745     145.073 103.860   7.319  1.00 35.81           C  
ANISOU 5782  CD1 TYR A 745     4320   4583   4702   -223      6    213       C  
ATOM   5783  CD2 TYR A 745     145.718 104.214   5.069  1.00 35.10           C  
ANISOU 5783  CD2 TYR A 745     4240   4488   4611   -227     19    212       C  
ATOM   5784  CE1 TYR A 745     143.995 104.723   7.140  1.00 36.19           C  
ANISOU 5784  CE1 TYR A 745     4389   4614   4747   -222      8    212       C  
ATOM   5785  CE2 TYR A 745     144.629 105.068   4.875  1.00 36.12           C  
ANISOU 5785  CE2 TYR A 745     4390   4598   4735   -225     20    212       C  
ATOM   5786  CZ  TYR A 745     143.782 105.301   5.943  1.00 36.33           C  
ANISOU 5786  CZ  TYR A 745     4422   4620   4763   -222     14    211       C  
ATOM   5787  OH  TYR A 745     142.716 106.122   5.859  1.00 41.70           O  
ANISOU 5787  OH  TYR A 745     5121   5283   5440   -219     14    210       O  
ATOM   5788  N   GLN A 746     149.018 104.631   5.227  1.00 35.30           N  
ANISOU 5788  N   GLN A 746     4234   4550   4630   -262     30    202       N  
ATOM   5789  CA  GLN A 746     149.177 105.757   4.341  1.00 38.66           C  
ANISOU 5789  CA  GLN A 746     4677   4966   5047   -276     40    200       C  
ATOM   5790  C   GLN A 746     148.873 105.258   2.949  1.00 35.75           C  
ANISOU 5790  C   GLN A 746     4313   4591   4680   -265     44    202       C  
ATOM   5791  O   GLN A 746     149.287 104.158   2.604  1.00 34.39           O  
ANISOU 5791  O   GLN A 746     4123   4429   4514   -256     42    201       O  
ATOM   5792  CB  GLN A 746     150.614 106.299   4.359  1.00 42.72           C  
ANISOU 5792  CB  GLN A 746     5181   5495   5556   -297     48    193       C  
ATOM   5793  CG  GLN A 746     150.635 107.781   3.965  1.00 50.63           C  
ANISOU 5793  CG  GLN A 746     6205   6484   6547   -316     57    191       C  
ATOM   5794  CD  GLN A 746     152.021 108.272   3.596  1.00 56.59           C  
ANISOU 5794  CD  GLN A 746     6952   7253   7296   -338     67    184       C  
ATOM   5795  OE1 GLN A 746     152.894 107.485   3.219  1.00 65.42           O  
ANISOU 5795  OE1 GLN A 746     8051   8389   8419   -337     69    181       O  
ATOM   5796  NE2 GLN A 746     152.235 109.575   3.699  1.00 58.40           N  
ANISOU 5796  NE2 GLN A 746     7197   7474   7517   -358     75    181       N  
ATOM   5797  N   PHE A 747     148.170 106.075   2.182  1.00 34.28           N  
ANISOU 5797  N   PHE A 747     4150   4386   4488   -267     48    203       N  
ATOM   5798  CA  PHE A 747     147.876 105.818   0.779  1.00 36.55           C  
ANISOU 5798  CA  PHE A 747     4446   4668   4774   -260     53    205       C  
ATOM   5799  C   PHE A 747     148.405 107.019   0.011  1.00 37.76           C  
ANISOU 5799  C   PHE A 747     4616   4816   4917   -280     64    204       C  
ATOM   5800  O   PHE A 747     147.941 108.122   0.236  1.00 36.06           O  
ANISOU 5800  O   PHE A 747     4421   4586   4696   -288     64    205       O  
ATOM   5801  CB  PHE A 747     146.349 105.710   0.544  1.00 35.66           C  
ANISOU 5801  CB  PHE A 747     4349   4536   4663   -243     47    210       C  
ATOM   5802  CG  PHE A 747     145.979 105.336  -0.865  1.00 35.53           C  
ANISOU 5802  CG  PHE A 747     4340   4515   4645   -234     50    212       C  
ATOM   5803  CD1 PHE A 747     146.265 104.066  -1.356  1.00 36.03           C  
ANISOU 5803  CD1 PHE A 747     4385   4590   4716   -223     50    211       C  
ATOM   5804  CD2 PHE A 747     145.348 106.247  -1.707  1.00 38.50           C  
ANISOU 5804  CD2 PHE A 747     4741   4875   5014   -236     53    215       C  
ATOM   5805  CE1 PHE A 747     145.959 103.719  -2.647  1.00 35.51           C  
ANISOU 5805  CE1 PHE A 747     4324   4519   4647   -217     53    211       C  
ATOM   5806  CE2 PHE A 747     144.990 105.898  -3.015  1.00 35.93           C  
ANISOU 5806  CE2 PHE A 747     4421   4544   4685   -229     55    217       C  
ATOM   5807  CZ  PHE A 747     145.296 104.638  -3.480  1.00 36.30           C  
ANISOU 5807  CZ  PHE A 747     4449   4604   4738   -219     56    215       C  
ATOM   5808  N   ILE A 748     149.347 106.799  -0.890  1.00 40.60           N  
ANISOU 5808  N   ILE A 748     4967   5186   5272   -289     72    200       N  
ATOM   5809  CA  ILE A 748     150.001 107.883  -1.602  1.00 44.11           C  
ANISOU 5809  CA  ILE A 748     5426   5628   5706   -311     83    199       C  
ATOM   5810  C   ILE A 748     150.124 107.652  -3.105  1.00 41.87           C  
ANISOU 5810  C   ILE A 748     5148   5344   5417   -311     91    199       C  
ATOM   5811  O   ILE A 748     150.428 106.555  -3.570  1.00 38.93           O  
ANISOU 5811  O   ILE A 748     4758   4985   5050   -302     91    196       O  
ATOM   5812  CB  ILE A 748     151.392 108.247  -1.005  1.00 50.31           C  
ANISOU 5812  CB  ILE A 748     6196   6431   6489   -332     89    191       C  
ATOM   5813  CG1 ILE A 748     152.349 107.071  -1.052  1.00 54.26           C  
ANISOU 5813  CG1 ILE A 748     6666   6955   6996   -328     89    185       C  
ATOM   5814  CG2 ILE A 748     151.213 108.810   0.403  1.00 53.44           C  
ANISOU 5814  CG2 ILE A 748     6594   6825   6887   -336     83    191       C  
ATOM   5815  CD1 ILE A 748     153.517 107.164  -0.080  1.00 57.82           C  
ANISOU 5815  CD1 ILE A 748     7096   7425   7448   -342     90    178       C  
ATOM   5816  N   LYS A 749     149.880 108.730  -3.842  1.00 41.22           N  
ANISOU 5816  N   LYS A 749     5091   5247   5323   -323     97    203       N  
ATOM   5817  CA  LYS A 749     150.095 108.772  -5.290  1.00 45.15           C  
ANISOU 5817  CA  LYS A 749     5598   5744   5812   -329    105    204       C  
ATOM   5818  C   LYS A 749     151.594 108.929  -5.537  1.00 43.20           C  
ANISOU 5818  C   LYS A 749     5338   5517   5560   -352    117    195       C  
ATOM   5819  O   LYS A 749     152.204 109.844  -5.019  1.00 44.08           O  
ANISOU 5819  O   LYS A 749     5454   5629   5667   -372    122    193       O  
ATOM   5820  CB  LYS A 749     149.294 109.933  -5.943  1.00 47.29           C  
ANISOU 5820  CB  LYS A 749     5905   5992   6073   -334    106    212       C  
ATOM   5821  CG  LYS A 749     148.536 109.468  -7.157  1.00 51.03           C  
ANISOU 5821  CG  LYS A 749     6388   6459   6543   -320    105    216       C  
ATOM   5822  CD  LYS A 749     147.665 110.510  -7.829  1.00 54.66           C  
ANISOU 5822  CD  LYS A 749     6881   6894   6992   -321    103    225       C  
ATOM   5823  CE  LYS A 749     147.463 110.227  -9.320  1.00 56.37           C  
ANISOU 5823  CE  LYS A 749     7107   7110   7200   -318    107    229       C  
ATOM   5824  NZ  LYS A 749     147.621 108.812  -9.790  1.00 59.41           N  
ANISOU 5824  NZ  LYS A 749     7468   7514   7592   -306    107    223       N  
ATOM   5825  N   ILE A 750     152.173 107.992  -6.275  1.00 43.88           N  
ANISOU 5825  N   ILE A 750     5405   5619   5647   -350    122    190       N  
ATOM   5826  CA  ILE A 750     153.590 108.016  -6.648  1.00 46.60           C  
ANISOU 5826  CA  ILE A 750     5734   5983   5987   -370    134    181       C  
ATOM   5827  C   ILE A 750     153.767 108.758  -7.984  1.00 50.34           C  
ANISOU 5827  C   ILE A 750     6230   6453   6446   -389    146    182       C  
ATOM   5828  O   ILE A 750     153.231 108.322  -9.016  1.00 50.11           O  
ANISOU 5828  O   ILE A 750     6208   6419   6413   -379    147    186       O  
ATOM   5829  CB  ILE A 750     154.137 106.585  -6.807  1.00 46.30           C  
ANISOU 5829  CB  ILE A 750     5665   5967   5960   -358    133    172       C  
ATOM   5830  CG1 ILE A 750     154.000 105.804  -5.481  1.00 46.19           C  
ANISOU 5830  CG1 ILE A 750     5631   5959   5961   -340    121    172       C  
ATOM   5831  CG2 ILE A 750     155.605 106.588  -7.297  1.00 46.26           C  
ANISOU 5831  CG2 ILE A 750     5643   5985   5950   -379    146    161       C  
ATOM   5832  CD1 ILE A 750     154.745 106.398  -4.283  1.00 45.41           C  
ANISOU 5832  CD1 ILE A 750     5523   5868   5863   -354    120    168       C  
ATOM   5833  N   ASN A 751     154.567 109.827  -7.947  1.00 53.28           N  
ANISOU 5833  N   ASN A 751     6610   6826   6807   -416    156    180       N  
ATOM   5834  CA AASN A 751     154.752 110.795  -9.053  1.00 56.92           C  
ANISOU 5834  CA AASN A 751     7097   7278   7251   -438    168    183       C  
ATOM   5835  C   ASN A 751     156.126 110.730  -9.758  1.00 63.09           C  
ANISOU 5835  C   ASN A 751     7865   8084   8025   -462    184    172       C  
ATOM   5836  O   ASN A 751     156.921 109.806  -9.530  1.00 65.98           O  
ANISOU 5836  O   ASN A 751     8198   8473   8399   -458    185    161       O  
ATOM   5837  CB AASN A 751     154.561 112.216  -8.503  1.00 55.57           C  
ANISOU 5837  CB AASN A 751     6953   7089   7073   -454    168    189       C  
ATOM   5838  CG AASN A 751     153.145 112.465  -7.989  1.00 53.93           C  
ANISOU 5838  CG AASN A 751     6764   6855   6871   -432    155    199       C  
ATOM   5839  OD1AASN A 751     152.935 112.990  -6.877  1.00 52.13           O  
ANISOU 5839  OD1AASN A 751     6539   6620   6648   -432    149    200       O  
ATOM   5840  ND2AASN A 751     152.164 112.094  -8.794  1.00 51.05           N  
ANISOU 5840  ND2AASN A 751     6412   6480   6506   -414    149    207       N  
TER    5841      ASN A 751                                                      
ATOM   5842  N   ALA B  25     117.478 116.732 -61.424  1.00 60.90           N  
ANISOU 5842  N   ALA B  25     8033   7557   7549   -193   -131    187       N  
ATOM   5843  CA  ALA B  25     116.072 116.784 -60.879  1.00 61.16           C  
ANISOU 5843  CA  ALA B  25     8049   7590   7600   -173   -143    197       C  
ATOM   5844  C   ALA B  25     115.853 116.096 -59.507  1.00 56.30           C  
ANISOU 5844  C   ALA B  25     7418   6967   7006   -166   -136    176       C  
ATOM   5845  O   ALA B  25     114.969 116.526 -58.751  1.00 57.10           O  
ANISOU 5845  O   ALA B  25     7510   7058   7129   -148   -137    184       O  
ATOM   5846  CB  ALA B  25     115.072 116.236 -61.903  1.00 62.34           C  
ANISOU 5846  CB  ALA B  25     8189   7764   7734   -175   -165    208       C  
ATOM   5847  N   GLN B  26     116.612 115.038 -59.188  1.00 50.62           N  
ANISOU 5847  N   GLN B  26     6695   6255   6283   -180   -128    151       N  
ATOM   5848  CA  GLN B  26     116.479 114.369 -57.871  1.00 43.97           C  
ANISOU 5848  CA  GLN B  26     5839   5406   5460   -174   -120    132       C  
ATOM   5849  C   GLN B  26     116.855 115.286 -56.715  1.00 41.32           C  
ANISOU 5849  C   GLN B  26     5511   5047   5143   -165   -105    131       C  
ATOM   5850  O   GLN B  26     117.958 115.774 -56.630  1.00 42.30           O  
ANISOU 5850  O   GLN B  26     5648   5160   5263   -174    -93    127       O  
ATOM   5851  CB  GLN B  26     117.313 113.092 -57.776  1.00 41.50           C  
ANISOU 5851  CB  GLN B  26     5523   5105   5140   -190   -113    108       C  
ATOM   5852  CG  GLN B  26     116.929 112.173 -56.612  1.00 40.98           C  
ANISOU 5852  CG  GLN B  26     5440   5039   5092   -184   -110     92       C  
ATOM   5853  CD  GLN B  26     117.732 110.858 -56.613  1.00 40.58           C  
ANISOU 5853  CD  GLN B  26     5385   4999   5035   -198   -103     70       C  
ATOM   5854  OE1 GLN B  26     117.831 110.205 -57.632  1.00 40.43           O  
ANISOU 5854  OE1 GLN B  26     5368   4995   5000   -210   -108     67       O  
ATOM   5855  NE2 GLN B  26     118.282 110.473 -55.474  1.00 40.51           N  
ANISOU 5855  NE2 GLN B  26     5371   4983   5040   -198    -90     57       N  
ATOM   5856  N   GLU B  27     115.924 115.474 -55.803  1.00 40.69           N  
ANISOU 5856  N   GLU B  27     5420   4958   5083   -148   -106    134       N  
ATOM   5857  CA  GLU B  27     116.168 116.153 -54.537  1.00 42.12           C  
ANISOU 5857  CA  GLU B  27     5605   5116   5281   -140    -91    129       C  
ATOM   5858  C   GLU B  27     116.999 115.340 -53.555  1.00 38.67           C  
ANISOU 5858  C   GLU B  27     5165   4680   4847   -150    -80    104       C  
ATOM   5859  O   GLU B  27     116.980 114.092 -53.543  1.00 37.27           O  
ANISOU 5859  O   GLU B  27     4975   4519   4666   -156    -84     92       O  
ATOM   5860  CB  GLU B  27     114.836 116.461 -53.879  1.00 46.56           C  
ANISOU 5860  CB  GLU B  27     6157   5671   5863   -119    -93    138       C  
ATOM   5861  CG  GLU B  27     114.003 117.418 -54.713  1.00 52.85           C  
ANISOU 5861  CG  GLU B  27     6955   6463   6661   -106   -103    165       C  
ATOM   5862  CD  GLU B  27     112.821 117.983 -53.957  1.00 59.33           C  
ANISOU 5862  CD  GLU B  27     7767   7271   7506    -83   -100    176       C  
ATOM   5863  OE1 GLU B  27     112.042 117.184 -53.377  1.00 59.78           O  
ANISOU 5863  OE1 GLU B  27     7805   7336   7573    -76   -104    169       O  
ATOM   5864  OE2 GLU B  27     112.684 119.233 -53.951  1.00 68.71           O  
ANISOU 5864  OE2 GLU B  27     8966   8438   8703    -72    -93    192       O  
ATOM   5865  N   HIS B  28     117.712 116.061 -52.717  1.00 37.99           N  
ANISOU 5865  N   HIS B  28     5090   4576   4767   -152    -66     99       N  
ATOM   5866  CA  HIS B  28     118.549 115.473 -51.659  1.00 38.46           C  
ANISOU 5866  CA  HIS B  28     5147   4636   4831   -161    -56     78       C  
ATOM   5867  C   HIS B  28     118.334 116.306 -50.405  1.00 38.54           C  
ANISOU 5867  C   HIS B  28     5162   4625   4855   -151    -45     76       C  
ATOM   5868  O   HIS B  28     118.510 117.505 -50.482  1.00 40.38           O  
ANISOU 5868  O   HIS B  28     5411   4841   5091   -150    -39     84       O  
ATOM   5869  CB  HIS B  28     120.024 115.475 -52.043  1.00 37.92           C  
ANISOU 5869  CB  HIS B  28     5088   4569   4749   -180    -49     72       C  
ATOM   5870  CG  HIS B  28     120.353 114.544 -53.158  1.00 38.06           C  
ANISOU 5870  CG  HIS B  28     5101   4606   4752   -191    -55     70       C  
ATOM   5871  ND1 HIS B  28     120.324 114.928 -54.480  1.00 38.44           N  
ANISOU 5871  ND1 HIS B  28     5159   4660   4787   -194    -62     83       N  
ATOM   5872  CD2 HIS B  28     120.709 113.238 -53.160  1.00 39.62           C  
ANISOU 5872  CD2 HIS B  28     5287   4819   4947   -199    -55     56       C  
ATOM   5873  CE1 HIS B  28     120.632 113.901 -55.249  1.00 38.31           C  
ANISOU 5873  CE1 HIS B  28     5138   4662   4758   -205    -65     76       C  
ATOM   5874  NE2 HIS B  28     120.887 112.864 -54.475  1.00 38.12           N  
ANISOU 5874  NE2 HIS B  28     5100   4642   4740   -207    -61     60       N  
ATOM   5875  N   PRO B  29     117.964 115.701 -49.266  1.00 36.48           N  
ANISOU 5875  N   PRO B  29     4890   4365   4604   -146    -41     64       N  
ATOM   5876  CA  PRO B  29     117.733 114.254 -49.135  1.00 34.23           C  
ANISOU 5876  CA  PRO B  29     4587   4100   4320   -147    -47     55       C  
ATOM   5877  C   PRO B  29     116.388 113.864 -49.724  1.00 33.71           C  
ANISOU 5877  C   PRO B  29     4508   4042   4258   -134    -59     66       C  
ATOM   5878  O   PRO B  29     115.534 114.735 -49.976  1.00 33.47           O  
ANISOU 5878  O   PRO B  29     4481   4003   4235   -121    -62     81       O  
ATOM   5879  CB  PRO B  29     117.735 114.041 -47.615  1.00 33.83           C  
ANISOU 5879  CB  PRO B  29     4532   4042   4279   -144    -38     42       C  
ATOM   5880  CG  PRO B  29     117.128 115.300 -47.117  1.00 34.61           C  
ANISOU 5880  CG  PRO B  29     4642   4121   4388   -132    -30     50       C  
ATOM   5881  CD  PRO B  29     117.696 116.392 -47.998  1.00 35.12           C  
ANISOU 5881  CD  PRO B  29     4724   4175   4445   -138    -30     60       C  
ATOM   5882  N   SER B  30     116.223 112.582 -49.998  1.00 32.27           N  
ANISOU 5882  N   SER B  30     4311   3878   4072   -139    -67     59       N  
ATOM   5883  CA  SER B  30     114.917 112.044 -50.452  1.00 32.96           C  
ANISOU 5883  CA  SER B  30     4383   3977   4164   -129    -79     66       C  
ATOM   5884  C   SER B  30     114.655 110.561 -50.129  1.00 32.91           C  
ANISOU 5884  C   SER B  30     4358   3984   4161   -132    -81     54       C  
ATOM   5885  O   SER B  30     113.488 110.167 -50.159  1.00 34.33           O  
ANISOU 5885  O   SER B  30     4524   4171   4350   -123    -90     59       O  
ATOM   5886  CB  SER B  30     114.675 112.246 -51.972  1.00 33.27           C  
ANISOU 5886  CB  SER B  30     4426   4026   4190   -133    -93     80       C  
ATOM   5887  OG  SER B  30     115.377 111.314 -52.810  1.00 31.37           O  
ANISOU 5887  OG  SER B  30     4185   3801   3933   -150    -97     71       O  
ATOM   5888  N   LEU B  31     115.685 109.756 -49.876  1.00 30.12           N  
ANISOU 5888  N   LEU B  31     4006   3637   3803   -145    -75     39       N  
ATOM   5889  CA  LEU B  31     115.472 108.315 -49.632  1.00 31.32           C  
ANISOU 5889  CA  LEU B  31     4142   3801   3959   -149    -75     27       C  
ATOM   5890  C   LEU B  31     114.616 108.011 -48.372  1.00 31.60           C  
ANISOU 5890  C   LEU B  31     4163   3831   4011   -136    -71     25       C  
ATOM   5891  O   LEU B  31     113.605 107.291 -48.441  1.00 30.96           O  
ANISOU 5891  O   LEU B  31     4068   3759   3938   -130    -78     26       O  
ATOM   5892  CB  LEU B  31     116.826 107.576 -49.557  1.00 31.17           C  
ANISOU 5892  CB  LEU B  31     4125   3786   3933   -163    -67     14       C  
ATOM   5893  CG  LEU B  31     117.452 107.195 -50.908  1.00 31.69           C  
ANISOU 5893  CG  LEU B  31     4197   3861   3983   -177    -70     12       C  
ATOM   5894  CD1 LEU B  31     117.812 108.396 -51.802  1.00 32.53           C  
ANISOU 5894  CD1 LEU B  31     4320   3964   4077   -181    -73     23       C  
ATOM   5895  CD2 LEU B  31     118.688 106.312 -50.722  1.00 31.03           C  
ANISOU 5895  CD2 LEU B  31     4112   3781   3898   -189    -59     -1       C  
ATOM   5896  N   ILE B  32     115.048 108.557 -47.228  1.00 31.44           N  
ANISOU 5896  N   ILE B  32     4149   3799   3997   -132    -60     22       N  
ATOM   5897  CA  ILE B  32     114.542 108.191 -45.934  1.00 32.28           C  
ANISOU 5897  CA  ILE B  32     4247   3903   4116   -123    -53     17       C  
ATOM   5898  C   ILE B  32     113.969 109.471 -45.306  1.00 34.69           C  
ANISOU 5898  C   ILE B  32     4560   4191   4429   -110    -47     24       C  
ATOM   5899  O   ILE B  32     112.768 109.632 -45.215  1.00 34.33           O  
ANISOU 5899  O   ILE B  32     4506   4144   4395    -96    -50     32       O  
ATOM   5900  CB  ILE B  32     115.651 107.535 -45.066  1.00 31.78           C  
ANISOU 5900  CB  ILE B  32     4183   3841   4051   -133    -43      4       C  
ATOM   5901  CG1 ILE B  32     116.350 106.389 -45.811  1.00 32.32           C  
ANISOU 5901  CG1 ILE B  32     4246   3923   4113   -146    -46     -2       C  
ATOM   5902  CG2 ILE B  32     115.083 107.078 -43.740  1.00 30.88           C  
ANISOU 5902  CG2 ILE B  32     4058   3725   3948   -124    -36      0       C  
ATOM   5903  CD1 ILE B  32     115.447 105.194 -46.148  1.00 33.71           C  
ANISOU 5903  CD1 ILE B  32     4405   4108   4295   -144    -52     -4       C  
ATOM   5904  N   LEU B  33     114.829 110.412 -44.934  1.00 36.10           N  
ANISOU 5904  N   LEU B  33     4755   4358   4602   -114    -39     22       N  
ATOM   5905  CA  LEU B  33     114.396 111.779 -44.608  1.00 36.09           C  
ANISOU 5905  CA  LEU B  33     4767   4339   4607   -104    -33     30       C  
ATOM   5906  C   LEU B  33     114.132 112.504 -45.914  1.00 36.62           C  
ANISOU 5906  C   LEU B  33     4840   4405   4671   -101    -42     44       C  
ATOM   5907  O   LEU B  33     114.995 112.506 -46.777  1.00 38.08           O  
ANISOU 5907  O   LEU B  33     5032   4594   4842   -114    -47     44       O  
ATOM   5908  CB  LEU B  33     115.509 112.485 -43.806  1.00 37.49           C  
ANISOU 5908  CB  LEU B  33     4961   4504   4778   -113    -21     21       C  
ATOM   5909  CG  LEU B  33     115.223 113.905 -43.326  1.00 38.72           C  
ANISOU 5909  CG  LEU B  33     5134   4639   4940   -105    -11     25       C  
ATOM   5910  CD1 LEU B  33     113.963 113.950 -42.475  1.00 39.06           C  
ANISOU 5910  CD1 LEU B  33     5168   4674   4997    -87     -4     26       C  
ATOM   5911  CD2 LEU B  33     116.401 114.467 -42.548  1.00 37.52           C  
ANISOU 5911  CD2 LEU B  33     4999   4479   4780   -119     -1     13       C  
ATOM   5912  N   THR B  34     112.943 113.100 -46.072  1.00 37.31           N  
ANISOU 5912  N   THR B  34     4923   4484   4769    -84    -44     58       N  
ATOM   5913  CA  THR B  34     112.566 113.841 -47.287  1.00 37.32           C  
ANISOU 5913  CA  THR B  34     4928   4485   4768    -79    -54     76       C  
ATOM   5914  C   THR B  34     112.500 115.358 -46.965  1.00 39.71           C  
ANISOU 5914  C   THR B  34     5248   4763   5078    -69    -42     84       C  
ATOM   5915  O   THR B  34     112.443 115.765 -45.796  1.00 39.75           O  
ANISOU 5915  O   THR B  34     5259   4753   5092    -64    -28     76       O  
ATOM   5916  CB  THR B  34     111.190 113.439 -47.861  1.00 35.46           C  
ANISOU 5916  CB  THR B  34     4673   4260   4541    -67    -67     89       C  
ATOM   5917  OG1 THR B  34     110.162 114.035 -47.075  1.00 35.62           O  
ANISOU 5917  OG1 THR B  34     4688   4266   4580    -47    -59     97       O  
ATOM   5918  CG2 THR B  34     110.977 111.944 -47.886  1.00 36.33           C  
ANISOU 5918  CG2 THR B  34     4765   4390   4649    -74    -75     79       C  
ATOM   5919  N   LYS B  35     112.494 116.185 -47.999  1.00 40.19           N  
ANISOU 5919  N   LYS B  35     5317   4819   5135    -68    -48    100       N  
ATOM   5920  CA  LYS B  35     112.493 117.661 -47.793  1.00 43.08           C  
ANISOU 5920  CA  LYS B  35     5701   5159   5509    -59    -36    109       C  
ATOM   5921  C   LYS B  35     111.195 118.178 -47.206  1.00 40.66           C  
ANISOU 5921  C   LYS B  35     5386   4839   5223    -35    -29    120       C  
ATOM   5922  O   LYS B  35     111.186 119.100 -46.376  1.00 41.16           O  
ANISOU 5922  O   LYS B  35     5462   4879   5297    -28    -11    117       O  
ATOM   5923  CB  LYS B  35     112.785 118.398 -49.107  1.00 48.28           C  
ANISOU 5923  CB  LYS B  35     6370   5816   6158    -62    -44    127       C  
ATOM   5924  CG  LYS B  35     114.276 118.486 -49.340  1.00 52.22           C  
ANISOU 5924  CG  LYS B  35     6886   6316   6640    -84    -41    116       C  
ATOM   5925  CD  LYS B  35     114.679 118.781 -50.768  1.00 54.27           C  
ANISOU 5925  CD  LYS B  35     7153   6583   6886    -92    -51    130       C  
ATOM   5926  CE  LYS B  35     115.218 120.174 -50.892  1.00 55.68           C  
ANISOU 5926  CE  LYS B  35     7354   6737   7066    -93    -40    139       C  
ATOM   5927  NZ  LYS B  35     116.483 120.299 -50.125  1.00 58.05           N  
ANISOU 5927  NZ  LYS B  35     7667   7028   7360   -110    -27    119       N  
ATOM   5928  N   ALA B  36     110.089 117.596 -47.648  1.00 38.68           N  
ANISOU 5928  N   ALA B  36     5114   4603   4980    -24    -42    132       N  
ATOM   5929  CA  ALA B  36     108.793 117.878 -47.041  1.00 39.32           C  
ANISOU 5929  CA  ALA B  36     5183   4675   5084     -1    -35    141       C  
ATOM   5930  C   ALA B  36     108.774 117.378 -45.590  1.00 37.44           C  
ANISOU 5930  C   ALA B  36     4942   4432   4853     -1    -20    121       C  
ATOM   5931  O   ALA B  36     108.260 118.041 -44.731  1.00 37.02           O  
ANISOU 5931  O   ALA B  36     4893   4360   4815     13     -3    121       O  
ATOM   5932  CB  ALA B  36     107.658 117.260 -47.855  1.00 39.93           C  
ANISOU 5932  CB  ALA B  36     5234   4771   5166      7    -54    158       C  
ATOM   5933  N   GLY B  37     109.381 116.223 -45.313  1.00 36.99           N  
ANISOU 5933  N   GLY B  37     4880   4392   4783    -17    -24    103       N  
ATOM   5934  CA  GLY B  37     109.503 115.769 -43.930  1.00 35.69           C  
ANISOU 5934  CA  GLY B  37     4714   4223   4621    -18    -10     85       C  
ATOM   5935  C   GLY B  37     110.263 116.759 -43.034  1.00 35.05           C  
ANISOU 5935  C   GLY B  37     4657   4120   4538    -22      9     74       C  
ATOM   5936  O   GLY B  37     109.866 117.000 -41.920  1.00 31.96           O  
ANISOU 5936  O   GLY B  37     4269   3717   4157    -14     26     66       O  
ATOM   5937  N   VAL B  38     111.375 117.304 -43.519  1.00 36.65           N  
ANISOU 5937  N   VAL B  38     4879   4319   4729    -37      8     71       N  
ATOM   5938  CA  VAL B  38     112.152 118.285 -42.731  1.00 37.81           C  
ANISOU 5938  CA  VAL B  38     5051   4445   4873    -44     25     60       C  
ATOM   5939  C   VAL B  38     111.270 119.478 -42.343  1.00 39.13           C  
ANISOU 5939  C   VAL B  38     5225   4585   5057    -24     42     69       C  
ATOM   5940  O   VAL B  38     111.200 119.849 -41.157  1.00 38.09           O  
ANISOU 5940  O   VAL B  38     5104   4438   4930    -22     60     57       O  
ATOM   5941  CB  VAL B  38     113.460 118.691 -43.446  1.00 38.49           C  
ANISOU 5941  CB  VAL B  38     5153   4530   4943    -63     20     59       C  
ATOM   5942  CG1 VAL B  38     114.194 119.813 -42.694  1.00 38.89           C  
ANISOU 5942  CG1 VAL B  38     5228   4557   4992    -72     38     48       C  
ATOM   5943  CG2 VAL B  38     114.390 117.468 -43.527  1.00 38.93           C  
ANISOU 5943  CG2 VAL B  38     5199   4609   4983    -82     10     47       C  
ATOM   5944  N   GLU B  39     110.536 120.014 -43.305  1.00 42.77           N  
ANISOU 5944  N   GLU B  39     5681   5041   5529     -9     36     91       N  
ATOM   5945  CA  GLU B  39     109.639 121.173 -43.051  1.00 45.90           C  
ANISOU 5945  CA  GLU B  39     6083   5410   5945     12     52    103       C  
ATOM   5946  C   GLU B  39     108.628 120.862 -41.978  1.00 42.59           C  
ANISOU 5946  C   GLU B  39     5652   4988   5542     28     65     98       C  
ATOM   5947  O   GLU B  39     108.414 121.673 -41.083  1.00 40.13           O  
ANISOU 5947  O   GLU B  39     5354   4651   5240     36     87     92       O  
ATOM   5948  CB  GLU B  39     108.854 121.610 -44.303  1.00 49.16           C  
ANISOU 5948  CB  GLU B  39     6486   5823   6368     28     40    132       C  
ATOM   5949  CG  GLU B  39     109.696 122.045 -45.477  1.00 59.26           C  
ANISOU 5949  CG  GLU B  39     7777   7105   7634     16     28    142       C  
ATOM   5950  CD  GLU B  39     110.784 123.053 -45.125  1.00 68.24           C  
ANISOU 5950  CD  GLU B  39     8945   8219   8766      3     44    131       C  
ATOM   5951  OE1 GLU B  39     110.506 124.043 -44.406  1.00 75.44           O  
ANISOU 5951  OE1 GLU B  39     9871   9102   9692     13     66    130       O  
ATOM   5952  OE2 GLU B  39     111.939 122.852 -45.575  1.00 80.61           O  
ANISOU 5952  OE2 GLU B  39    10521   9795  10313    -19     36    123       O  
ATOM   5953  N   LYS B  40     107.982 119.698 -42.076  1.00 40.14           N  
ANISOU 5953  N   LYS B  40     5317   4701   5234     32     52    101       N  
ATOM   5954  CA  LYS B  40     106.969 119.352 -41.086  1.00 41.13           C  
ANISOU 5954  CA  LYS B  40     5429   4825   5375     47     64     97       C  
ATOM   5955  C   LYS B  40     107.563 119.104 -39.703  1.00 37.72           C  
ANISOU 5955  C   LYS B  40     5009   4388   4933     36     80     72       C  
ATOM   5956  O   LYS B  40     106.931 119.449 -38.690  1.00 37.62           O  
ANISOU 5956  O   LYS B  40     4999   4360   4933     48    101     67       O  
ATOM   5957  CB  LYS B  40     106.176 118.143 -41.501  1.00 45.40           C  
ANISOU 5957  CB  LYS B  40     5939   5391   5919     52     46    105       C  
ATOM   5958  CG  LYS B  40     105.300 118.387 -42.696  1.00 52.15           C  
ANISOU 5958  CG  LYS B  40     6778   6251   6786     66     31    132       C  
ATOM   5959  CD  LYS B  40     104.828 117.073 -43.308  1.00 58.93           C  
ANISOU 5959  CD  LYS B  40     7609   7140   7641     61      8    137       C  
ATOM   5960  CE  LYS B  40     104.464 117.259 -44.778  1.00 62.87           C  
ANISOU 5960  CE  LYS B  40     8097   7649   8139     64    -14    161       C  
ATOM   5961  NZ  LYS B  40     103.936 115.992 -45.359  1.00 63.79           N  
ANISOU 5961  NZ  LYS B  40     8189   7795   8253     58    -36    163       N  
ATOM   5962  N   ILE B  41     108.744 118.478 -39.657  1.00 33.49           N  
ANISOU 5962  N   ILE B  41     4480   3867   4377     12     71     57       N  
ATOM   5963  CA  ILE B  41     109.391 118.235 -38.386  1.00 33.30           C  
ANISOU 5963  CA  ILE B  41     4468   3842   4342     -1     84     35       C  
ATOM   5964  C   ILE B  41     109.600 119.596 -37.705  1.00 34.09           C  
ANISOU 5964  C   ILE B  41     4595   3912   4444      1    107     27       C  
ATOM   5965  O   ILE B  41     109.252 119.768 -36.557  1.00 34.65           O  
ANISOU 5965  O   ILE B  41     4673   3972   4519      5    126     16       O  
ATOM   5966  CB  ILE B  41     110.717 117.480 -38.547  1.00 33.07           C  
ANISOU 5966  CB  ILE B  41     4442   3831   4291    -26     70     23       C  
ATOM   5967  CG1 ILE B  41     110.426 115.990 -38.859  1.00 33.24           C  
ANISOU 5967  CG1 ILE B  41     4438   3881   4312    -27     54     26       C  
ATOM   5968  CG2 ILE B  41     111.573 117.629 -37.290  1.00 32.67           C  
ANISOU 5968  CG2 ILE B  41     4411   3776   4228    -41     83      3       C  
ATOM   5969  CD1 ILE B  41     111.595 115.166 -39.325  1.00 32.36           C  
ANISOU 5969  CD1 ILE B  41     4325   3788   4183    -48     39     19       C  
ATOM   5970  N   ARG B  42     110.200 120.524 -38.435  1.00 35.09           N  
ANISOU 5970  N   ARG B  42     4738   4025   4568     -5    105     33       N  
ATOM   5971  CA  ARG B  42     110.526 121.848 -37.922  1.00 38.48           C  
ANISOU 5971  CA  ARG B  42     5195   4424   4999     -7    126     25       C  
ATOM   5972  C   ARG B  42     109.333 122.623 -37.385  1.00 37.19           C  
ANISOU 5972  C   ARG B  42     5035   4237   4859     17    149     31       C  
ATOM   5973  O   ARG B  42     109.457 123.280 -36.403  1.00 37.84           O  
ANISOU 5973  O   ARG B  42     5138   4299   4941     14    171     16       O  
ATOM   5974  CB  ARG B  42     111.209 122.683 -38.996  1.00 38.61           C  
ANISOU 5974  CB  ARG B  42     5225   4431   5013    -14    119     36       C  
ATOM   5975  CG  ARG B  42     112.666 122.358 -39.168  1.00 39.35           C  
ANISOU 5975  CG  ARG B  42     5328   4539   5084    -43    108     24       C  
ATOM   5976  CD  ARG B  42     113.232 123.218 -40.300  1.00 40.63           C  
ANISOU 5976  CD  ARG B  42     5502   4690   5244    -48    102     36       C  
ATOM   5977  NE  ARG B  42     114.559 122.796 -40.708  1.00 43.03           N  
ANISOU 5977  NE  ARG B  42     5810   5011   5529    -73     89     29       N  
ATOM   5978  CZ  ARG B  42     115.196 123.229 -41.799  1.00 45.17           C  
ANISOU 5978  CZ  ARG B  42     6088   5281   5795    -81     80     40       C  
ATOM   5979  NH1 ARG B  42     114.630 124.122 -42.597  1.00 48.44           N  
ANISOU 5979  NH1 ARG B  42     6507   5678   6221    -66     83     59       N  
ATOM   5980  NH2 ARG B  42     116.415 122.790 -42.091  1.00 45.26           N  
ANISOU 5980  NH2 ARG B  42     6101   5308   5789   -104     70     32       N  
ATOM   5981  N   ALA B  43     108.190 122.501 -38.045  1.00 38.97           N  
ANISOU 5981  N   ALA B  43     5238   4464   5103     40    143     53       N  
ATOM   5982  CA  ALA B  43     106.941 123.140 -37.638  1.00 39.57           C  
ANISOU 5982  CA  ALA B  43     5311   4520   5205     67    164     62       C  
ATOM   5983  C   ALA B  43     106.397 122.561 -36.336  1.00 41.86           C  
ANISOU 5983  C   ALA B  43     5595   4812   5497     72    180     47       C  
ATOM   5984  O   ALA B  43     105.668 123.225 -35.628  1.00 44.16           O  
ANISOU 5984  O   ALA B  43     5893   5081   5805     88    206     46       O  
ATOM   5985  CB  ALA B  43     105.902 122.968 -38.751  1.00 38.89           C  
ANISOU 5985  CB  ALA B  43     5198   4443   5137     88    149     92       C  
ATOM   5986  N   GLU B  44     106.695 121.291 -36.057  1.00 43.25           N  
ANISOU 5986  N   GLU B  44     5758   5017   5659     58    165     37       N  
ATOM   5987  CA  GLU B  44     106.177 120.606 -34.891  1.00 40.69           C  
ANISOU 5987  CA  GLU B  44     5425   4699   5335     62    178     26       C  
ATOM   5988  C   GLU B  44     107.133 120.540 -33.703  1.00 40.51           C  
ANISOU 5988  C   GLU B  44     5426   4676   5291     40    189     -1       C  
ATOM   5989  O   GLU B  44     106.673 120.262 -32.574  1.00 39.11           O  
ANISOU 5989  O   GLU B  44     524