CNRS Nantes University UFIP UFIP
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***  3FV1  ***

elNémo ID: 22040500335480429

Job options:

ID        	=	 22040500335480429
JOBID     	=	 3FV1
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 3FV1

HEADER    MEMBRANE PROTEIN                        15-JAN-09   3FV1              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN GLUTAMATE RECEPTOR, GLUR5, LIGAND-     
TITLE    2 BINDING CORE IN COMPLEX WITH DYSIHERBAINE IN SPACE GROUP P1          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE RECEPTOR, IONOTROPIC KAINATE 1;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: LIGAND-BINDING DOMAIN, UNP RESIDUES 445-559, 682-820;      
COMPND   5 SYNONYM: GLUTAMATE RECEPTOR 5, GLUR-5, GLUR5, EXCITATORY AMINO ACID  
COMPND   6 RECEPTOR 3, EAA3;                                                    
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PCOLD-1                                   
KEYWDS    NATURAL COMPOUND, GLUTAMATE RECEPTOR, LIGAND, MEMBRANE PROTEIN        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.UNNO,M.SASAKI,M.IKEDA-SAITO                                         
REVDAT   3   16-AUG-17 3FV1    1       SOURCE REMARK                            
REVDAT   2   26-OCT-11 3FV1    1       JRNL   VERSN                             
REVDAT   1   19-JAN-10 3FV1    0                                                
JRNL        AUTH   M.UNNO,M.SHINOHARA,K.TAKAYAMA,H.TANAKA,K.TERUYA,K.DOH-URA,   
JRNL        AUTH 2 R.SAKAI,M.SASAKI,M.IKEDA-SAITO                               
JRNL        TITL   BINDING AND SELECTIVITY OF THE MARINE TOXIN NEODYSIHERBAINE  
JRNL        TITL 2 A AND ITS SYNTHETIC ANALOGUES TO GLUK1 AND GLUK2 KAINATE     
JRNL        TITL 3 RECEPTORS.                                                   
JRNL        REF    J.MOL.BIOL.                   V. 413   667 2011              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   21893069                                                     
JRNL        DOI    10.1016/J.JMB.2011.08.043                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 75397                          
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) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4011                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5336                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.41                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 273                          
REMARK   3   BIN FREE R VALUE                    : 0.2320                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4056                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 85                                      
REMARK   3   SOLVENT ATOMS            : 462                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.11000                                             
REMARK   3    B22 (A**2) : -0.25000                                             
REMARK   3    B33 (A**2) : 0.23000                                              
REMARK   3    B12 (A**2) : 0.16000                                              
REMARK   3    B13 (A**2) : -0.02000                                             
REMARK   3    B23 (A**2) : -0.04000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.076         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.073         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.042         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.200         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ; 0.009 ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ; 1.270 ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ; 5.563 ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;29.695 ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;12.710 ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ; 9.997 ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ; 0.084 ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ; 0.005 ;  NULL       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ; 0.195 ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ; 0.309 ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ; 0.115 ;  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 ; 0.161 ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ; 0.124 ;  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 ; 0.924 ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ; 1.080 ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ; 1.767 ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ; 2.682 ;  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   415        A   517                          
REMARK   3    RESIDUE RANGE :   A   750        A   790                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.4070   5.1420  18.3830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0436 T22:  -0.0352                                     
REMARK   3      T33:  -0.0037 T12:   0.0174                                     
REMARK   3      T13:   0.0037 T23:   0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5462 L22:   0.9642                                     
REMARK   3      L33:   0.9239 L12:   0.0178                                     
REMARK   3      L13:  -0.0103 L23:   0.0324                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0415 S12:  -0.0494 S13:  -0.0050                       
REMARK   3      S21:  -0.0177 S22:   0.0225 S23:  -0.0061                       
REMARK   3      S31:   0.0395 S32:   0.0668 S33:   0.0189                       
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 :   B   415        B   517                          
REMARK   3    RESIDUE RANGE :   B   750        B   790                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.5170  13.6450 -11.0190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0485 T22:  -0.0323                                     
REMARK   3      T33:  -0.0021 T12:  -0.0193                                     
REMARK   3      T13:   0.0018 T23:   0.0255                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7467 L22:   1.0717                                     
REMARK   3      L33:   0.8613 L12:   0.1759                                     
REMARK   3      L13:  -0.0100 L23:   0.3108                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0766 S12:   0.0921 S13:   0.0193                       
REMARK   3      S21:  -0.0115 S22:   0.0428 S23:   0.0568                       
REMARK   3      S31:  -0.0507 S32:   0.0773 S33:   0.0338                       
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   522        A   746                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.4730  22.0940  21.3050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0328 T22:  -0.0289                                     
REMARK   3      T33:  -0.0137 T12:   0.0302                                     
REMARK   3      T13:  -0.0026 T23:   0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3960 L22:   1.5068                                     
REMARK   3      L33:   0.7541 L12:  -0.2585                                     
REMARK   3      L13:  -0.1332 L23:  -0.1149                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0230 S12:  -0.0598 S13:   0.0383                       
REMARK   3      S21:   0.0465 S22:   0.0077 S23:   0.0525                       
REMARK   3      S31:  -0.0690 S32:  -0.1118 S33:  -0.0307                       
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 :   B   522        B   746                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.4300  -3.0930 -14.2050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0436 T22:  -0.0203                                     
REMARK   3      T33:  -0.0087 T12:  -0.0305                                     
REMARK   3      T13:   0.0141 T23:   0.0200                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0134 L22:   1.5025                                     
REMARK   3      L33:   0.7463 L12:  -0.0665                                     
REMARK   3      L13:   0.0592 L23:  -0.0421                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0156 S12:   0.0285 S13:   0.0160                       
REMARK   3      S21:  -0.0825 S22:   0.0077 S23:   0.0415                       
REMARK   3      S31:   0.0672 S32:  -0.1251 S33:  -0.0233                       
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 :   A   518        A   521                          
REMARK   3    RESIDUE RANGE :   A   747        A   749                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.8520   9.8020  11.2470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0170 T22:  -0.0196                                     
REMARK   3      T33:   0.0236 T12:   0.0194                                     
REMARK   3      T13:  -0.0154 T23:  -0.0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4690 L22:   3.2522                                     
REMARK   3      L33:   1.0308 L12:  -0.9857                                     
REMARK   3      L13:  -1.1219 L23:   0.0815                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0280 S12:  -0.0946 S13:   0.0516                       
REMARK   3      S21:   0.1104 S22:   0.0034 S23:   0.1303                       
REMARK   3      S31:  -0.0241 S32:  -0.0448 S33:   0.0246                       
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   518        B   521                          
REMARK   3    RESIDUE RANGE :   B   747        B   749                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.8730   9.2810  -4.0110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0229 T22:  -0.0199                                     
REMARK   3      T33:   0.0432 T12:  -0.0215                                     
REMARK   3      T13:   0.0178 T23:  -0.0110                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6512 L22:   4.5002                                     
REMARK   3      L33:   1.2674 L12:   0.9883                                     
REMARK   3      L13:   0.8800 L23:   0.8514                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0267 S12:   0.0833 S13:   0.0810                       
REMARK   3      S21:   0.0063 S22:   0.0005 S23:   0.2958                       
REMARK   3      S31:   0.0055 S32:  -0.1377 S33:   0.0263                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A     1                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.9850  15.0130  20.0080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0310 T22:  -0.0348                                     
REMARK   3      T33:   0.0241 T12:   0.0387                                     
REMARK   3      T13:   0.0051 T23:   0.0148                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.5634 L22:   3.5753                                     
REMARK   3      L33:   5.1335 L12:   5.7366                                     
REMARK   3      L13:  -4.4758 L23:  -2.0462                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1995 S12:  -0.1325 S13:   0.0421                       
REMARK   3      S21:  -0.0911 S22:   0.2104 S23:   0.0029                       
REMARK   3      S31:  -0.0439 S32:   0.0121 S33:  -0.0109                       
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     2        B     2                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.0290   3.9860 -12.7640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0531 T22:  -0.0272                                     
REMARK   3      T33:   0.0317 T12:  -0.0337                                     
REMARK   3      T13:   0.0221 T23:   0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.2639 L22:   3.2028                                     
REMARK   3      L33:   5.8994 L12:  -6.3819                                     
REMARK   3      L13:   7.2334 L23:  -2.8474                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0062 S12:   0.2116 S13:  -0.1924                       
REMARK   3      S21:   0.1796 S22:   0.0688 S23:   0.0125                       
REMARK   3      S31:   0.0812 S32:   0.0855 S33:  -0.0625                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3FV1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JAN-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000051076.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-OCT-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL26B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU JUPITER 210                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79411                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04900                            
REMARK 200   FOR THE DATA SET  : 29.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.19300                            
REMARK 200   FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 2ZNT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% PEG3350, 0.3M LISO4, 5MM             
REMARK 280  DYSIHERBAINE, PH5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  303K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ARG A 785    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 787    CG   OD1  ND2                                       
REMARK 470     LYS B 434    CG   CD   CE   NZ                                   
REMARK 470     LYS B 437    CG   CD   CE   NZ                                   
REMARK 470     ARG B 785    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 787    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 697   O   -  C   -  N   ANGL. DEV. = -13.0 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    GLU A 426      113.93   -164.10                                   
REMARK 500    THR A 700      -62.06   -103.90                                   
REMARK 500    GLU B 426      112.27   -163.02                                   
REMARK 500    ARG B 785     -141.02     54.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DYH A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 791                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DYH B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 791                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ZNS   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN DIFFERENT SPACE GROUP                                
REMARK 900 RELATED ID: 2ZNT   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN DIFFERENT SPACE GROUP                                
REMARK 900 RELATED ID: 2ZNU   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN DIFFERENT SPACE GROUP                                
REMARK 900 RELATED ID: 3FUZ   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH DIFFERENT LIGAND                                   
REMARK 900 RELATED ID: 3FV2   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH DIFFERENT LIGAND                                   
REMARK 900 RELATED ID: 3FVG   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH DIFFERENT LIGAND                                   
REMARK 900 RELATED ID: 3FVK   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH DIFFERENT LIGAND                                   
REMARK 900 RELATED ID: 3FVN   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH DIFFERENT LIGAND                                   
REMARK 900 RELATED ID: 3FVO   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH DIFFERENT LIGAND                                   
DBREF  3FV1 A  415   529  UNP    P39086   GRIK1_HUMAN    445    559             
DBREF  3FV1 A  652   790  UNP    P39086   GRIK1_HUMAN    682    820             
DBREF  3FV1 B  415   529  UNP    P39086   GRIK1_HUMAN    445    559             
DBREF  3FV1 B  652   790  UNP    P39086   GRIK1_HUMAN    682    820             
SEQADV 3FV1 GLY A  600  UNP  P39086              LINKER                         
SEQADV 3FV1 THR A  601  UNP  P39086              LINKER                         
SEQADV 3FV1 GLY B  600  UNP  P39086              LINKER                         
SEQADV 3FV1 THR B  601  UNP  P39086              LINKER                         
SEQRES   1 A  256  ALA ASN ARG THR LEU ILE VAL THR THR ILE LEU GLU GLU          
SEQRES   2 A  256  PRO TYR VAL MET TYR ARG LYS SER ASP LYS PRO LEU TYR          
SEQRES   3 A  256  GLY ASN ASP ARG PHE GLU GLY TYR CYS LEU ASP LEU LEU          
SEQRES   4 A  256  LYS GLU LEU SER ASN ILE LEU GLY PHE ILE TYR ASP VAL          
SEQRES   5 A  256  LYS LEU VAL PRO ASP GLY LYS TYR GLY ALA GLN ASN ASP          
SEQRES   6 A  256  LYS GLY GLU TRP ASN GLY MET VAL LYS GLU LEU ILE ASP          
SEQRES   7 A  256  HIS ARG ALA ASP LEU ALA VAL ALA PRO LEU THR ILE THR          
SEQRES   8 A  256  TYR VAL ARG GLU LYS VAL ILE ASP PHE SER LYS PRO PHE          
SEQRES   9 A  256  MET THR LEU GLY ILE SER ILE LEU TYR ARG LYS GLY THR          
SEQRES  10 A  256  PRO ILE ASP SER ALA ASP ASP LEU ALA LYS GLN THR LYS          
SEQRES  11 A  256  ILE GLU TYR GLY ALA VAL ARG ASP GLY SER THR MET THR          
SEQRES  12 A  256  PHE PHE LYS LYS SER LYS ILE SER THR TYR GLU LYS MET          
SEQRES  13 A  256  TRP ALA PHE MET SER SER ARG GLN GLN THR ALA LEU VAL          
SEQRES  14 A  256  ARG ASN SER ASP GLU GLY ILE GLN ARG VAL LEU THR THR          
SEQRES  15 A  256  ASP TYR ALA LEU LEU MET GLU SER THR SER ILE GLU TYR          
SEQRES  16 A  256  VAL THR GLN ARG ASN CYS ASN LEU THR GLN ILE GLY GLY          
SEQRES  17 A  256  LEU ILE ASP SER LYS GLY TYR GLY VAL GLY THR PRO ILE          
SEQRES  18 A  256  GLY SER PRO TYR ARG ASP LYS ILE THR ILE ALA ILE LEU          
SEQRES  19 A  256  GLN LEU GLN GLU GLU GLY LYS LEU HIS MET MET LYS GLU          
SEQRES  20 A  256  LYS TRP TRP ARG GLY ASN GLY CYS PRO                          
SEQRES   1 B  256  ALA ASN ARG THR LEU ILE VAL THR THR ILE LEU GLU GLU          
SEQRES   2 B  256  PRO TYR VAL MET TYR ARG LYS SER ASP LYS PRO LEU TYR          
SEQRES   3 B  256  GLY ASN ASP ARG PHE GLU GLY TYR CYS LEU ASP LEU LEU          
SEQRES   4 B  256  LYS GLU LEU SER ASN ILE LEU GLY PHE ILE TYR ASP VAL          
SEQRES   5 B  256  LYS LEU VAL PRO ASP GLY LYS TYR GLY ALA GLN ASN ASP          
SEQRES   6 B  256  LYS GLY GLU TRP ASN GLY MET VAL LYS GLU LEU ILE ASP          
SEQRES   7 B  256  HIS ARG ALA ASP LEU ALA VAL ALA PRO LEU THR ILE THR          
SEQRES   8 B  256  TYR VAL ARG GLU LYS VAL ILE ASP PHE SER LYS PRO PHE          
SEQRES   9 B  256  MET THR LEU GLY ILE SER ILE LEU TYR ARG LYS GLY THR          
SEQRES  10 B  256  PRO ILE ASP SER ALA ASP ASP LEU ALA LYS GLN THR LYS          
SEQRES  11 B  256  ILE GLU TYR GLY ALA VAL ARG ASP GLY SER THR MET THR          
SEQRES  12 B  256  PHE PHE LYS LYS SER LYS ILE SER THR TYR GLU LYS MET          
SEQRES  13 B  256  TRP ALA PHE MET SER SER ARG GLN GLN THR ALA LEU VAL          
SEQRES  14 B  256  ARG ASN SER ASP GLU GLY ILE GLN ARG VAL LEU THR THR          
SEQRES  15 B  256  ASP TYR ALA LEU LEU MET GLU SER THR SER ILE GLU TYR          
SEQRES  16 B  256  VAL THR GLN ARG ASN CYS ASN LEU THR GLN ILE GLY GLY          
SEQRES  17 B  256  LEU ILE ASP SER LYS GLY TYR GLY VAL GLY THR PRO ILE          
SEQRES  18 B  256  GLY SER PRO TYR ARG ASP LYS ILE THR ILE ALA ILE LEU          
SEQRES  19 B  256  GLN LEU GLN GLU GLU GLY LYS LEU HIS MET MET LYS GLU          
SEQRES  20 B  256  LYS TRP TRP ARG GLY ASN GLY CYS PRO                          
HET    DYH  A   1      21                                                       
HET    SO4  A 791       5                                                       
HET    SO4  A   3       5                                                       
HET    SO4  A   4       5                                                       
HET    SO4  A   5       5                                                       
HET    GOL  B 801       6                                                       
HET    GOL  B 802       6                                                       
HET    GOL  B 803       6                                                       
HET    DYH  B   2      21                                                       
HET    SO4  B 791       5                                                       
HETNAM     DYH (2R,3AR,6S,7R,7AR)-2-[(2S)-2-AMINO-2-CARBOXYETHYL]-6-            
HETNAM   2 DYH  HYDROXY-7-(METHYLAMINO)HEXAHYDRO-2H-FURO[3,2-B]PYRAN-           
HETNAM   3 DYH  2-CARBOXYLIC ACID                                               
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  DYH    2(C12 H20 N2 O7)                                             
FORMUL   4  SO4    5(O4 S 2-)                                                   
FORMUL   8  GOL    3(C3 H8 O3)                                                  
FORMUL  13  HOH   *462(H2 O)                                                    
HELIX    1   1 TYR A  440  ASP A  443  5                                   4    
HELIX    2   2 GLY A  447  GLY A  461  1                                  15    
HELIX    3   3 ASN A  484  ASP A  492  1                                   9    
HELIX    4   4 THR A  505  LYS A  510  1                                   6    
HELIX    5   5 SER A  655  GLN A  662  1                                   8    
HELIX    6   6 GLY A  673  SER A  682  1                                  10    
HELIX    7   7 ILE A  684  ARG A  697  1                                  14    
HELIX    8   8 ARG A  697  LEU A  702  1                                   6    
HELIX    9   9 ASN A  705  THR A  716  1                                  12    
HELIX   10  10 SER A  724  GLN A  732  1                                   9    
HELIX   11  11 TYR A  759  GLU A  773  1                                  15    
HELIX   12  12 GLY A  774  ARG A  785  1                                  12    
HELIX   13  13 TYR B  440  ASP B  443  5                                   4    
HELIX   14  14 GLY B  447  GLY B  461  1                                  15    
HELIX   15  15 ASN B  484  ASP B  492  1                                   9    
HELIX   16  16 THR B  505  LYS B  510  1                                   6    
HELIX   17  17 SER B  655  GLN B  662  1                                   8    
HELIX   18  18 GLY B  673  SER B  682  1                                  10    
HELIX   19  19 ILE B  684  ARG B  697  1                                  14    
HELIX   20  20 ARG B  697  ALA B  701  1                                   5    
HELIX   21  21 ASN B  705  THR B  716  1                                  12    
HELIX   22  22 SER B  724  GLN B  732  1                                   9    
HELIX   23  23 TYR B  759  GLU B  773  1                                  15    
HELIX   24  24 GLY B  774  ARG B  785  1                                  12    
SHEET    1   A 3 TYR A 464  LEU A 468  0                                        
SHEET    2   A 3 LEU A 419  THR A 423  1  N  VAL A 421   O  LYS A 467           
SHEET    3   A 3 LEU A 497  ALA A 498  1  O  LEU A 497   N  THR A 422           
SHEET    1   B 2 MET A 431  TYR A 432  0                                        
SHEET    2   B 2 PHE A 445  GLU A 446 -1  O  GLU A 446   N  MET A 431           
SHEET    1   C 2 ILE A 512  PHE A 514  0                                        
SHEET    2   C 2 GLY A 752  PRO A 754 -1  O  THR A 753   N  ASP A 513           
SHEET    1   D 2 MET A 519  LEU A 521  0                                        
SHEET    2   D 2 LYS A 747  TYR A 749 -1  O  LYS A 747   N  LEU A 521           
SHEET    1   E 4 GLU A 666  GLY A 668  0                                        
SHEET    2   E 4 TYR A 718  GLU A 723  1  O  LEU A 721   N  GLY A 668           
SHEET    3   E 4 ILE A 523  ARG A 528 -1  N  LEU A 526   O  LEU A 720           
SHEET    4   E 4 LEU A 737  ILE A 740 -1  O  THR A 738   N  TYR A 527           
SHEET    1   F 3 TYR B 464  LEU B 468  0                                        
SHEET    2   F 3 LEU B 419  THR B 423  1  N  VAL B 421   O  LYS B 467           
SHEET    3   F 3 LEU B 497  ALA B 498  1  O  LEU B 497   N  THR B 422           
SHEET    1   G 2 MET B 431  TYR B 432  0                                        
SHEET    2   G 2 PHE B 445  GLU B 446 -1  O  GLU B 446   N  MET B 431           
SHEET    1   H 2 ILE B 512  PHE B 514  0                                        
SHEET    2   H 2 GLY B 752  PRO B 754 -1  O  THR B 753   N  ASP B 513           
SHEET    1   I 2 MET B 519  LEU B 521  0                                        
SHEET    2   I 2 LYS B 747  TYR B 749 -1  O  TYR B 749   N  MET B 519           
SHEET    1   J 5 LEU B 702  VAL B 703  0                                        
SHEET    2   J 5 GLU B 666  VAL B 670  1  N  ALA B 669   O  VAL B 703           
SHEET    3   J 5 TYR B 718  GLU B 723  1  O  LEU B 721   N  GLY B 668           
SHEET    4   J 5 ILE B 523  ARG B 528 -1  N  LEU B 526   O  LEU B 720           
SHEET    5   J 5 LEU B 737  ILE B 740 -1  O  ILE B 740   N  ILE B 525           
SSBOND   1 CYS A  735    CYS A  789                          1555   1555  2.04  
SSBOND   2 CYS B  735    CYS B  789                          1555   1555  2.03  
CISPEP   1 GLU A  427    PRO A  428          0        -4.52                     
CISPEP   2 GLY A  786    ASN A  787          0        -4.55                     
CISPEP   3 GLU B  427    PRO B  428          0        -5.53                     
SITE     1 AC1 17 HOH A  26  GLU A 426  TYR A 474  PRO A 501                    
SITE     2 AC1 17 LEU A 502  THR A 503  ARG A 508  VAL A 670                    
SITE     3 AC1 17 GLY A 673  SER A 674  THR A 675  SER A 706                    
SITE     4 AC1 17 MET A 722  GLU A 723  SER A 726  TYR A 749                    
SITE     5 AC1 17 HOH A 794                                                     
SITE     1 AC2  7 HOH A  63  HOH A 128  HOH A 134  ARG A 444                    
SITE     2 AC2  7 LYS A 467  LEU A 468  ARG B 704                               
SITE     1 AC3  2 ARG A 417  TYR A 759                                          
SITE     1 AC4  4 HOH A 166  HOH A 218  LYS A 664  LYS A 782                    
SITE     1 AC5  6 HOH A  62  HOH A 119  ASP A 657  ILE A 684                    
SITE     2 AC5  6 THR A 686  TYR A 687                                          
SITE     1 AC6  7 HOH B 181  HOH B 311  ARG B 671  ASP B 672                    
SITE     2 AC6  7 MET B 676  LYS B 680  TRP B 691                               
SITE     1 AC7  9 HOH B  83  HOH B  84  HOH B 167  LYS B 454                    
SITE     2 AC7  9 TYR B 464  ALA B 660  LYS B 661  THR B 663                    
SITE     3 AC7  9 LYS B 689                                                     
SITE     1 AC8  5 HOH B 171  HOH B 312  ASP B 657  THR B 686                    
SITE     2 AC8  5 TYR B 687                                                     
SITE     1 AC9 17 HOH B   6  HOH B   8  GLU B 426  TYR B 474                    
SITE     2 AC9 17 PRO B 501  LEU B 502  THR B 503  ARG B 508                    
SITE     3 AC9 17 VAL B 670  GLY B 673  SER B 674  THR B 675                    
SITE     4 AC9 17 SER B 706  MET B 722  GLU B 723  SER B 726                    
SITE     5 AC9 17 TYR B 749                                                     
SITE     1 BC1  5 HOH B 344  ARG B 444  VAL B 466  LYS B 467                    
SITE     2 BC1  5 LEU B 468                                                     
CRYST1   47.486   50.740   63.252  80.08  84.18  62.06 P 1           2          
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      0.021059 -0.011167 -0.000568        0.00000                         
SCALE2      0.000000  0.022308 -0.003198        0.00000                         
SCALE3      0.000000  0.000000  0.016054        0.00000                         
ATOM      1  N   ALA A 415      19.457  -8.977  18.960  1.00 27.48           N  
ANISOU    1  N   ALA A 415     2833   3639   3969   1235    191    246       N  
ATOM      2  CA  ALA A 415      18.028  -8.717  18.600  1.00 26.18           C  
ANISOU    2  CA  ALA A 415     2772   3414   3760   1147    208    240       C  
ATOM      3  C   ALA A 415      17.776  -7.242  18.304  1.00 25.46           C  
ANISOU    3  C   ALA A 415     2640   3374   3660   1042    209    220       C  
ATOM      4  O   ALA A 415      18.442  -6.362  18.860  1.00 25.71           O  
ANISOU    4  O   ALA A 415     2581   3481   3707   1023    172    221       O  
ATOM      5  CB  ALA A 415      17.092  -9.192  19.714  1.00 26.16           C  
ANISOU    5  CB  ALA A 415     2855   3362   3723   1147    155    276       C  
ATOM      6  N   ASN A 416      16.808  -6.988  17.428  1.00 24.35           N  
ANISOU    6  N   ASN A 416     2569   3189   3493    976    248    202       N  
ATOM      7  CA  ASN A 416      16.363  -5.630  17.128  1.00 23.62           C  
ANISOU    7  CA  ASN A 416     2460   3128   3387    877    247    187       C  
ATOM      8  C   ASN A 416      16.072  -4.880  18.435  1.00 22.87           C  
ANISOU    8  C   ASN A 416     2345   3066   3280    841    176    207       C  
ATOM      9  O   ASN A 416      15.459  -5.447  19.345  1.00 22.54           O  
ANISOU    9  O   ASN A 416     2359   2990   3217    862    139    232       O  
ATOM     10  CB  ASN A 416      15.114  -5.672  16.229  1.00 23.23           C  
ANISOU   10  CB  ASN A 416     2509   3013   3305    821    281    174       C  
ATOM     11  CG  ASN A 416      15.357  -6.388  14.891  1.00 25.04           C  
ANISOU   11  CG  ASN A 416     2771   3207   3536    851    351    149       C  
ATOM     12  OD1 ASN A 416      16.488  -6.472  14.402  1.00 28.76           O  
ANISOU   12  OD1 ASN A 416     3178   3716   4033    893    390    135       O  
ATOM     13  ND2 ASN A 416      14.279  -6.901  14.291  1.00 25.06           N  
ANISOU   13  ND2 ASN A 416     2874   3138   3509    826    369    142       N  
ATOM     14  N   ARG A 417      16.536  -3.632  18.549  1.00 22.02           N  
ANISOU   14  N   ARG A 417     2163   3021   3182    788    160    196       N  
ATOM     15  CA  ARG A 417      16.287  -2.826  19.759  1.00 20.53           C  
ANISOU   15  CA  ARG A 417     1959   2864   2978    750     93    207       C  
ATOM     16  C   ARG A 417      14.778  -2.692  19.984  1.00 17.83           C  
ANISOU   16  C   ARG A 417     1713   2466   2596    702     85    214       C  
ATOM     17  O   ARG A 417      14.016  -2.511  19.029  1.00 18.28           O  
ANISOU   17  O   ARG A 417     1818   2485   2644    658    124    201       O  
ATOM     18  CB  ARG A 417      16.938  -1.432  19.659  1.00 21.39           C  
ANISOU   18  CB  ARG A 417     1984   3037   3105    687     84    188       C  
ATOM     19  CG  ARG A 417      16.828  -0.572  20.929  1.00 21.84           C  
ANISOU   19  CG  ARG A 417     2023   3129   3147    651     13    193       C  
ATOM     20  CD  ARG A 417      17.426   0.841  20.755  1.00 21.78           C  
ANISOU   20  CD  ARG A 417     1941   3175   3158    578      7    170       C  
ATOM     21  NE  ARG A 417      16.990   1.484  19.518  1.00 21.12           N  
ANISOU   21  NE  ARG A 417     1884   3066   3075    516     65    154       N  
ATOM     22  CZ  ARG A 417      15.925   2.282  19.414  1.00 18.44           C  
ANISOU   22  CZ  ARG A 417     1606   2690   2709    452     63    148       C  
ATOM     23  NH1 ARG A 417      15.184   2.557  20.482  1.00 19.00           N  
ANISOU   23  NH1 ARG A 417     1717   2750   2753    440     13    154       N  
ATOM     24  NH2 ARG A 417      15.610   2.798  18.237  1.00 18.19           N  
ANISOU   24  NH2 ARG A 417     1599   2636   2677    405    112    137       N  
ATOM     25  N   THR A 418      14.348  -2.826  21.240  1.00 15.35           N  
ANISOU   25  N   THR A 418     1426   2148   2258    712     34    236       N  
ATOM     26  CA  THR A 418      12.931  -2.649  21.575  1.00 12.59           C  
ANISOU   26  CA  THR A 418     1156   1754   1874    666     28    242       C  
ATOM     27  C   THR A 418      12.518  -1.206  21.332  1.00 11.66           C  
ANISOU   27  C   THR A 418     1022   1657   1752    584     26    220       C  
ATOM     28  O   THR A 418      13.100  -0.279  21.904  1.00 12.04           O  
ANISOU   28  O   THR A 418     1014   1756   1803    562     -9    211       O  
ATOM     29  CB  THR A 418      12.631  -3.049  23.026  1.00 12.17           C  
ANISOU   29  CB  THR A 418     1134   1699   1791    693    -20    271       C  
ATOM     30  OG1 THR A 418      12.963  -4.432  23.205  1.00 12.09           O  
ANISOU   30  OG1 THR A 418     1150   1659   1784    771    -18    296       O  
ATOM     31  CG2 THR A 418      11.154  -2.861  23.368  1.00 11.79           C  
ANISOU   31  CG2 THR A 418     1160   1609   1710    644    -17    276       C  
ATOM     32  N   LEU A 419      11.505  -1.029  20.491  1.00 10.05           N  
ANISOU   32  N   LEU A 419      870   1409   1541    541     59    210       N  
ATOM     33  CA  LEU A 419      11.060   0.312  20.129  1.00  9.28           C  
ANISOU   33  CA  LEU A 419      765   1321   1441    470     60    191       C  
ATOM     34  C   LEU A 419      10.279   0.958  21.266  1.00  9.46           C  
ANISOU   34  C   LEU A 419      808   1346   1440    442     21    195       C  
ATOM     35  O   LEU A 419       9.479   0.300  21.942  1.00  9.50           O  
ANISOU   35  O   LEU A 419      863   1323   1424    459     13    212       O  
ATOM     36  CB  LEU A 419      10.224   0.303  18.848  1.00  9.11           C  
ANISOU   36  CB  LEU A 419      792   1254   1416    437    100    181       C  
ATOM     37  CG  LEU A 419      10.933  -0.206  17.585  1.00  9.16           C  
ANISOU   37  CG  LEU A 419      788   1256   1438    457    147    171       C  
ATOM     38  CD1 LEU A 419      10.081   0.062  16.353  1.00 10.90           C  
ANISOU   38  CD1 LEU A 419     1059   1437   1645    413    177    159       C  
ATOM     39  CD2 LEU A 419      12.317   0.422  17.424  1.00 11.34           C  
ANISOU   39  CD2 LEU A 419      981   1591   1738    457    154    161       C  
ATOM     40  N   ILE A 420      10.548   2.241  21.493  1.00  8.57           N  
ANISOU   40  N   ILE A 420      659   1266   1330    398      0    178       N  
ATOM     41  CA  ILE A 420       9.811   2.998  22.502  1.00  8.70           C  
ANISOU   41  CA  ILE A 420      699   1284   1323    370    -32    174       C  
ATOM     42  C   ILE A 420       8.619   3.652  21.830  1.00  7.99           C  
ANISOU   42  C   ILE A 420      650   1155   1231    323    -10    164       C  
ATOM     43  O   ILE A 420       8.780   4.407  20.861  1.00  8.28           O  
ANISOU   43  O   ILE A 420      673   1189   1284    287      6    150       O  
ATOM     44  CB  ILE A 420      10.705   4.071  23.157  1.00  8.86           C  
ANISOU   44  CB  ILE A 420      665   1355   1346    346    -71    157       C  
ATOM     45  CG1 ILE A 420      11.920   3.410  23.827  1.00 11.17           C  
ANISOU   45  CG1 ILE A 420      908   1693   1643    395   -101    168       C  
ATOM     46  CG2 ILE A 420       9.875   4.947  24.124  1.00  9.07           C  
ANISOU   46  CG2 ILE A 420      726   1376   1345    314    -98    146       C  
ATOM     47  CD1 ILE A 420      11.594   2.398  24.921  0.50 10.70           C  
ANISOU   47  CD1 ILE A 420      888   1626   1552    448   -125    194       C  
ATOM     48  N   VAL A 421       7.425   3.345  22.335  1.00  7.67           N  
ANISOU   48  N   VAL A 421      659   1085   1171    325    -10    172       N  
ATOM     49  CA  VAL A 421       6.210   3.908  21.778  1.00  7.84           C  
ANISOU   49  CA  VAL A 421      714   1072   1194    288      6    164       C  
ATOM     50  C   VAL A 421       5.634   4.921  22.755  1.00  7.81           C  
ANISOU   50  C   VAL A 421      717   1076   1176    266    -16    152       C  
ATOM     51  O   VAL A 421       5.337   4.582  23.901  1.00  8.43           O  
ANISOU   51  O   VAL A 421      811   1162   1230    285    -28    160       O  
ATOM     52  CB  VAL A 421       5.181   2.802  21.511  1.00  7.57           C  
ANISOU   52  CB  VAL A 421      724    996   1156    302     28    180       C  
ATOM     53  CG1 VAL A 421       3.857   3.398  21.022  1.00  8.89           C  
ANISOU   53  CG1 VAL A 421      916   1134   1329    265     36    171       C  
ATOM     54  CG2 VAL A 421       5.737   1.798  20.473  1.00  8.20           C  
ANISOU   54  CG2 VAL A 421      807   1060   1248    324     52    186       C  
ATOM     55  N   THR A 422       5.509   6.169  22.306  1.00  6.21           N  
ANISOU   55  N   THR A 422      508    869    984    227    -20    132       N  
ATOM     56  CA  THR A 422       4.766   7.166  23.076  1.00  6.64           C  
ANISOU   56  CA  THR A 422      578    919   1027    209    -34    116       C  
ATOM     57  C   THR A 422       3.291   7.098  22.703  1.00  5.97           C  
ANISOU   57  C   THR A 422      525    796    947    203    -15    120       C  
ATOM     58  O   THR A 422       2.930   6.882  21.546  1.00  6.06           O  
ANISOU   58  O   THR A 422      544    783    975    194      0    126       O  
ATOM     59  CB  THR A 422       5.355   8.593  22.914  1.00  6.98           C  
ANISOU   59  CB  THR A 422      602    969   1081    171    -52     92       C  
ATOM     60  OG1 THR A 422       4.669   9.488  23.797  1.00  7.94           O  
ANISOU   60  OG1 THR A 422      746   1083   1188    161    -65     73       O  
ATOM     61  CG2 THR A 422       5.220   9.124  21.476  1.00  7.22           C  
ANISOU   61  CG2 THR A 422      637    972   1135    142    -34     92       C  
ATOM     62  N   THR A 423       2.435   7.217  23.707  1.00  6.12           N  
ANISOU   62  N   THR A 423      562    813    949    211    -15    116       N  
ATOM     63  CA  THR A 423       1.005   7.193  23.473  1.00  6.00           C  
ANISOU   63  CA  THR A 423      565    769    944    206      4    118       C  
ATOM     64  C   THR A 423       0.311   7.966  24.598  1.00  5.80           C  
ANISOU   64  C   THR A 423      551    749    903    208      3    101       C  
ATOM     65  O   THR A 423       0.968   8.544  25.470  1.00  6.14           O  
ANISOU   65  O   THR A 423      595    814    924    209    -14     86       O  
ATOM     66  CB  THR A 423       0.464   5.752  23.329  1.00  6.65           C  
ANISOU   66  CB  THR A 423      661    839   1027    221     25    143       C  
ATOM     67  OG1 THR A 423      -0.853   5.804  22.768  1.00  6.99           O  
ANISOU   67  OG1 THR A 423      710    855   1089    207     38    143       O  
ATOM     68  CG2 THR A 423       0.449   5.011  24.667  1.00  6.78           C  
ANISOU   68  CG2 THR A 423      692    872   1012    244     31    157       C  
ATOM     69  N   ILE A 424      -1.013   7.969  24.572  1.00  5.39           N  
ANISOU   69  N   ILE A 424      506    678    863    208     23    101       N  
ATOM     70  CA  ILE A 424      -1.796   8.764  25.511  1.00  6.37           C  
ANISOU   70  CA  ILE A 424      639    805    977    214     32     81       C  
ATOM     71  C   ILE A 424      -3.095   8.013  25.777  1.00  5.81           C  
ANISOU   71  C   ILE A 424      568    727    911    221     65     95       C  
ATOM     72  O   ILE A 424      -3.626   7.355  24.890  1.00  6.78           O  
ANISOU   72  O   ILE A 424      682    834   1061    213     71    111       O  
ATOM     73  CB  ILE A 424      -2.043  10.179  24.914  1.00  6.38           C  
ANISOU   73  CB  ILE A 424      637    783   1003    201     18     57       C  
ATOM     74  CG1 ILE A 424      -2.515  11.190  25.967  1.00  7.79           C  
ANISOU   74  CG1 ILE A 424      830    963   1168    211     23     28       C  
ATOM     75  CG2 ILE A 424      -2.979  10.120  23.692  1.00  6.77           C  
ANISOU   75  CG2 ILE A 424      676    805   1090    195     22     67       C  
ATOM     76  CD1 ILE A 424      -2.338  12.638  25.518  1.00  8.37           C  
ANISOU   76  CD1 ILE A 424      911   1009   1259    199      2      2       C  
ATOM     77  N   LEU A 425      -3.608   8.104  27.004  1.00  6.50           N  
ANISOU   77  N   LEU A 425      668    830    973    233     86     88       N  
ATOM     78  CA  LEU A 425      -4.886   7.471  27.324  1.00  6.57           C  
ANISOU   78  CA  LEU A 425      671    836    989    235    126    100       C  
ATOM     79  C   LEU A 425      -6.019   8.211  26.613  1.00  6.09           C  
ANISOU   79  C   LEU A 425      583    757    975    232    131     85       C  
ATOM     80  O   LEU A 425      -6.170   9.433  26.753  1.00  7.48           O  
ANISOU   80  O   LEU A 425      757    928   1156    241    124     57       O  
ATOM     81  CB  LEU A 425      -5.151   7.437  28.834  1.00  7.44           C  
ANISOU   81  CB  LEU A 425      804    969   1054    249    155     96       C  
ATOM     82  CG  LEU A 425      -4.236   6.520  29.655  1.00  8.59           C  
ANISOU   82  CG  LEU A 425      981   1133   1148    257    150    119       C  
ATOM     83  CD1 LEU A 425      -4.365   6.864  31.131  1.00 11.23           C  
ANISOU   83  CD1 LEU A 425     1347   1492   1427    271    170    106       C  
ATOM     84  CD2 LEU A 425      -4.555   5.059  29.410  1.00 10.72           C  
ANISOU   84  CD2 LEU A 425     1255   1391   1426    251    172    159       C  
ATOM     85  N   GLU A 426      -6.802   7.461  25.842  1.00  6.63           N  
ANISOU   85  N   GLU A 426      630    813   1076    219    140    104       N  
ATOM     86  CA  GLU A 426      -7.904   8.030  25.069  1.00  6.37           C  
ANISOU   86  CA  GLU A 426      565    766   1091    217    136     94       C  
ATOM     87  C   GLU A 426      -8.811   6.887  24.637  1.00  6.60           C  
ANISOU   87  C   GLU A 426      571    790   1145    197    152    116       C  
ATOM     88  O   GLU A 426      -8.396   6.058  23.846  1.00  6.52           O  
ANISOU   88  O   GLU A 426      572    767   1138    180    135    133       O  
ATOM     89  CB  GLU A 426      -7.354   8.763  23.834  1.00  6.03           C  
ANISOU   89  CB  GLU A 426      525    702   1066    212     92     87       C  
ATOM     90  CG  GLU A 426      -8.411   9.542  23.046  1.00  7.40           C  
ANISOU   90  CG  GLU A 426      670    857   1283    217     77     78       C  
ATOM     91  CD  GLU A 426      -8.801  10.841  23.724  1.00  8.33           C  
ANISOU   91  CD  GLU A 426      786    972   1406    244     85     50       C  
ATOM     92  OE1 GLU A 426      -7.944  11.743  23.851  1.00  9.51           O  
ANISOU   92  OE1 GLU A 426      963   1112   1538    248     68     34       O  
ATOM     93  OE2 GLU A 426      -9.971  10.960  24.137  1.00 13.80           O  
ANISOU   93  OE2 GLU A 426     1448   1673   2124    260    110     43       O  
ATOM     94  N   GLU A 427     -10.044   6.852  25.147  1.00  8.20           N  
ANISOU   94  N   GLU A 427      743   1004   1370    198    186    113       N  
ATOM     95  CA  GLU A 427     -10.982   5.786  24.802  1.00  8.87           C  
ANISOU   95  CA  GLU A 427      801   1086   1484    171    202    133       C  
ATOM     96  C   GLU A 427     -11.486   5.960  23.366  1.00  8.51           C  
ANISOU   96  C   GLU A 427      726   1022   1484    158    160    130       C  
ATOM     97  O   GLU A 427     -11.817   7.081  22.962  1.00  9.06           O  
ANISOU   97  O   GLU A 427      775   1089   1577    178    137    112       O  
ATOM     98  CB  GLU A 427     -12.186   5.864  25.731  1.00  9.60           C  
ANISOU   98  CB  GLU A 427      856   1199   1591    174    254    128       C  
ATOM     99  CG  GLU A 427     -11.876   5.697  27.203  1.00 12.43           C  
ANISOU   99  CG  GLU A 427     1248   1578   1898    185    302    131       C  
ATOM    100  CD  GLU A 427     -13.123   5.697  28.066  1.00 15.89           C  
ANISOU  100  CD  GLU A 427     1649   2039   2349    185    363    127       C  
ATOM    101  OE1 GLU A 427     -14.169   5.196  27.611  1.00 18.95           O  
ANISOU  101  OE1 GLU A 427     1987   2429   2786    160    377    137       O  
ATOM    102  OE2 GLU A 427     -13.052   6.193  29.211  1.00 18.94           O  
ANISOU  102  OE2 GLU A 427     2056   2444   2696    209    400    114       O  
ATOM    103  N   PRO A 428     -11.595   4.861  22.599  1.00  7.58           N  
ANISOU  103  N   PRO A 428      611    890   1378    126    147    148       N  
ATOM    104  CA  PRO A 428     -11.227   3.468  22.862  1.00  7.13           C  
ANISOU  104  CA  PRO A 428      586    824   1300    103    169    170       C  
ATOM    105  C   PRO A 428      -9.904   3.095  22.196  1.00  6.62           C  
ANISOU  105  C   PRO A 428      570    739   1206    106    140    176       C  
ATOM    106  O   PRO A 428      -9.638   1.912  21.943  1.00  7.17           O  
ANISOU  106  O   PRO A 428      667    790   1269     87    144    192       O  
ATOM    107  CB  PRO A 428     -12.370   2.717  22.185  1.00  7.17           C  
ANISOU  107  CB  PRO A 428      558    819   1349     64    164    177       C  
ATOM    108  CG  PRO A 428     -12.595   3.535  20.924  1.00  8.00           C  
ANISOU  108  CG  PRO A 428      641    917   1480     69    110    161       C  
ATOM    109  CD  PRO A 428     -12.288   4.980  21.294  1.00  8.06           C  
ANISOU  109  CD  PRO A 428      644    938   1480    111    105    144       C  
ATOM    110  N   TYR A 429      -9.074   4.104  21.947  1.00  6.11           N  
ANISOU  110  N   TYR A 429      516    679   1128    129    115    162       N  
ATOM    111  CA  TYR A 429      -7.771   3.902  21.317  1.00  6.13           C  
ANISOU  111  CA  TYR A 429      553    669   1106    134     93    165       C  
ATOM    112  C   TYR A 429      -6.742   3.264  22.259  1.00  6.31           C  
ANISOU  112  C   TYR A 429      607    701   1091    149    113    178       C  
ATOM    113  O   TYR A 429      -6.071   2.292  21.890  1.00  7.04           O  
ANISOU  113  O   TYR A 429      725    777   1172    147    112    191       O  
ATOM    114  CB  TYR A 429      -7.236   5.240  20.785  1.00  6.18           C  
ANISOU  114  CB  TYR A 429      559    678   1112    147     64    148       C  
ATOM    115  CG ATYR A 429      -8.060   5.779  19.651  0.50  6.02           C  
ANISOU  115  CG ATYR A 429      521    644   1123    136     34    141       C  
ATOM    116  CG BTYR A 429      -8.281   6.113  20.086  0.50  5.64           C  
ANISOU  116  CG BTYR A 429      462    602   1078    144     41    137       C  
ATOM    117  CD1ATYR A 429      -7.892   5.307  18.353  0.50  5.37           C  
ANISOU  117  CD1ATYR A 429      456    542   1042    118      9    146       C  
ATOM    118  CD1BTYR A 429      -8.466   6.042  18.701  0.50  5.44           C  
ANISOU  118  CD1BTYR A 429      443    559   1066    128      7    139       C  
ATOM    119  CD2ATYR A 429      -9.013   6.760  19.879  0.50  5.72           C  
ANISOU  119  CD2ATYR A 429      451    612   1112    148     29    129       C  
ATOM    120  CD2BTYR A 429      -9.077   7.009  20.809  0.50  5.81           C  
ANISOU  120  CD2BTYR A 429      455    636   1117    161     52    124       C  
ATOM    121  CE1ATYR A 429      -8.667   5.798  17.305  0.50  5.83           C  
ANISOU  121  CE1ATYR A 429      504    589   1123    109    -26    142       C  
ATOM    122  CE1BTYR A 429      -9.412   6.845  18.052  0.50  5.57           C  
ANISOU  122  CE1BTYR A 429      435    569   1113    130    -22    132       C  
ATOM    123  CE2ATYR A 429      -9.799   7.261  18.843  0.50  7.18           C  
ANISOU  123  CE2ATYR A 429      618    784   1326    144     -6    126       C  
ATOM    124  CE2BTYR A 429     -10.039   7.816  20.167  0.50  6.05           C  
ANISOU  124  CE2BTYR A 429      457    658   1183    167     27    115       C  
ATOM    125  CZ ATYR A 429      -9.617   6.781  17.561  0.50  5.82           C  
ANISOU  125  CZ ATYR A 429      467    595   1151    124    -36    134       C  
ATOM    126  CZ BTYR A 429     -10.200   7.723  18.792  0.50  5.58           C  
ANISOU  126  CZ BTYR A 429      401    581   1137    152    -13    122       C  
ATOM    127  OH ATYR A 429     -10.399   7.280  16.548  0.50  7.85           O  
ANISOU  127  OH ATYR A 429      711    841   1430    121    -78    133       O  
ATOM    128  OH BTYR A 429     -11.128   8.509  18.146  0.50  7.51           O  
ANISOU  128  OH BTYR A 429      620    819   1415    162    -45    117       O  
ATOM    129  N   VAL A 430      -6.641   3.812  23.469  1.00  6.88           N  
ANISOU  129  N   VAL A 430      677    796   1142    167    130    173       N  
ATOM    130  CA  VAL A 430      -5.665   3.387  24.466  1.00  7.06           C  
ANISOU  130  CA  VAL A 430      728    832   1123    185    139    185       C  
ATOM    131  C   VAL A 430      -6.339   3.520  25.825  1.00  7.05           C  
ANISOU  131  C   VAL A 430      726    849   1102    191    173    186       C  
ATOM    132  O   VAL A 430      -6.724   4.626  26.225  1.00  7.57           O  
ANISOU  132  O   VAL A 430      776    930   1170    199    176    163       O  
ATOM    133  CB  VAL A 430      -4.385   4.268  24.430  1.00  6.91           C  
ANISOU  133  CB  VAL A 430      713    828   1086    202    110    170       C  
ATOM    134  CG1 VAL A 430      -3.396   3.844  25.518  1.00  8.83           C  
ANISOU  134  CG1 VAL A 430      978   1090   1286    224    111    181       C  
ATOM    135  CG2 VAL A 430      -3.693   4.209  23.042  1.00  8.58           C  
ANISOU  135  CG2 VAL A 430      923   1023   1315    195     85    168       C  
ATOM    136  N   MET A 431      -6.509   2.395  26.517  1.00  7.60           N  
ANISOU  136  N   MET A 431      819    916   1151    187    202    213       N  
ATOM    137  CA  MET A 431      -7.227   2.382  27.804  1.00  8.07           C  
ANISOU  137  CA  MET A 431      885    993   1187    188    245    219       C  
ATOM    138  C   MET A 431      -6.558   1.423  28.763  1.00  8.22           C  
ANISOU  138  C   MET A 431      953   1014   1156    201    257    249       C  
ATOM    139  O   MET A 431      -5.899   0.483  28.338  1.00  7.99           O  
ANISOU  139  O   MET A 431      946    964   1126    203    241    271       O  
ATOM    140  CB  MET A 431      -8.676   1.917  27.618  1.00  9.11           C  
ANISOU  140  CB  MET A 431      988   1116   1357    158    281    227       C  
ATOM    141  CG  MET A 431      -9.445   2.744  26.598  1.00  9.26           C  
ANISOU  141  CG  MET A 431      956   1132   1430    148    262    201       C  
ATOM    142  SD  MET A 431     -11.118   2.151  26.328  1.00 11.01           S  
ANISOU  142  SD  MET A 431     1130   1348   1704    109    296    209       S  
ATOM    143  CE  MET A 431     -10.836   0.616  25.454  1.00 11.41           C  
ANISOU  143  CE  MET A 431     1211   1359   1764     75    280    236       C  
ATOM    144  N   TYR A 432      -6.722   1.660  30.059  1.00  8.50           N  
ANISOU  144  N   TYR A 432     1008   1074   1147    212    284    251       N  
ATOM    145  CA  TYR A 432      -6.283   0.663  31.029  1.00  9.63           C  
ANISOU  145  CA  TYR A 432     1205   1216   1238    222    299    287       C  
ATOM    146  C   TYR A 432      -7.174  -0.569  30.960  1.00 10.21           C  
ANISOU  146  C   TYR A 432     1289   1261   1329    191    342    321       C  
ATOM    147  O   TYR A 432      -8.405  -0.473  31.069  1.00 11.15           O  
ANISOU  147  O   TYR A 432     1381   1383   1472    164    386    317       O  
ATOM    148  CB  TYR A 432      -6.317   1.211  32.457  1.00 10.29           C  
ANISOU  148  CB  TYR A 432     1316   1334   1260    238    321    281       C  
ATOM    149  CG  TYR A 432      -5.221   2.195  32.789  1.00 10.07           C  
ANISOU  149  CG  TYR A 432     1295   1332   1199    266    273    253       C  
ATOM    150  CD1 TYR A 432      -3.870   1.849  32.661  1.00 11.95           C  
ANISOU  150  CD1 TYR A 432     1549   1571   1419    287    222    265       C  
ATOM    151  CD2 TYR A 432      -5.533   3.463  33.274  1.00 11.58           C  
ANISOU  151  CD2 TYR A 432     1476   1546   1378    271    280    213       C  
ATOM    152  CE1 TYR A 432      -2.859   2.760  32.982  1.00 13.18           C  
ANISOU  152  CE1 TYR A 432     1704   1754   1549    305    176    238       C  
ATOM    153  CE2 TYR A 432      -4.530   4.369  33.600  1.00 12.05           C  
ANISOU  153  CE2 TYR A 432     1545   1625   1407    289    234    185       C  
ATOM    154  CZ  TYR A 432      -3.206   4.019  33.455  1.00 12.89           C  
ANISOU  154  CZ  TYR A 432     1663   1737   1499    302    181    198       C  
ATOM    155  OH  TYR A 432      -2.214   4.929  33.779  1.00 15.34           O  
ANISOU  155  OH  TYR A 432     1975   2070   1784    312    133    168       O  
ATOM    156  N   ARG A 433      -6.536  -1.729  30.807  1.00 10.61           N  
ANISOU  156  N   ARG A 433     1379   1282   1369    197    330    355       N  
ATOM    157  CA  ARG A 433      -7.221  -3.012  30.920  1.00 11.35           C  
ANISOU  157  CA  ARG A 433     1503   1340   1471    167    370    392       C  
ATOM    158  C   ARG A 433      -7.692  -3.221  32.357  1.00 12.21           C  
ANISOU  158  C   ARG A 433     1649   1465   1525    163    420    418       C  
ATOM    159  O   ARG A 433      -6.982  -2.900  33.313  1.00 12.13           O  
ANISOU  159  O   ARG A 433     1674   1482   1454    197    408    423       O  
ATOM    160  CB  ARG A 433      -6.267  -4.134  30.498  1.00 11.52           C  
ANISOU  160  CB  ARG A 433     1568   1321   1487    185    341    420       C  
ATOM    161  CG  ARG A 433      -6.778  -5.563  30.714  1.00 14.12           C  
ANISOU  161  CG  ARG A 433     1947   1602   1816    158    379    464       C  
ATOM    162  CD  ARG A 433      -5.812  -6.615  30.148  1.00 17.15           C  
ANISOU  162  CD  ARG A 433     2375   1939   2204    183    348    485       C  
ATOM    163  NE  ARG A 433      -5.984  -6.785  28.708  1.00 21.14           N  
ANISOU  163  NE  ARG A 433     2851   2413   2767    161    331    460       N  
ATOM    164  CZ  ARG A 433      -5.200  -6.263  27.764  1.00 21.84           C  
ANISOU  164  CZ  ARG A 433     2912   2513   2875    187    289    429       C  
ATOM    165  NH1 ARG A 433      -4.135  -5.532  28.079  1.00 22.26           N  
ANISOU  165  NH1 ARG A 433     2952   2605   2901    233    257    419       N  
ATOM    166  NH2 ARG A 433      -5.483  -6.483  26.486  1.00 22.55           N  
ANISOU  166  NH2 ARG A 433     2985   2573   3009    161    279    409       N  
ATOM    167  N   LYS A 434      -8.905  -3.745  32.490  1.00 13.33           N  
ANISOU  167  N   LYS A 434     1784   1594   1688    118    477    434       N  
ATOM    168  CA  LYS A 434      -9.487  -4.067  33.791  1.00 14.96           C  
ANISOU  168  CA  LYS A 434     2028   1812   1845    105    539    463       C  
ATOM    169  C   LYS A 434      -9.169  -5.504  34.168  1.00 15.70           C  
ANISOU  169  C   LYS A 434     2197   1860   1908     98    551    520       C  
ATOM    170  O   LYS A 434      -9.525  -6.437  33.448  1.00 16.68           O  
ANISOU  170  O   LYS A 434     2324   1937   2077     64    558    537       O  
ATOM    171  CB  LYS A 434     -11.003  -3.852  33.768  1.00 15.99           C  
ANISOU  171  CB  LYS A 434     2102   1956   2019     57    601    452       C  
ATOM    172  CG  LYS A 434     -11.402  -2.405  33.561  1.00 18.16           C  
ANISOU  172  CG  LYS A 434     2308   2273   2320     73    595    399       C  
ATOM    173  CD  LYS A 434     -12.906  -2.215  33.673  1.00 22.24           C  
ANISOU  173  CD  LYS A 434     2764   2808   2879     34    660    390       C  
ATOM    174  CE  LYS A 434     -13.283  -0.741  33.694  1.00 24.22           C  
ANISOU  174  CE  LYS A 434     2957   3100   3146     62    660    339       C  
ATOM    175  NZ  LYS A 434     -12.958  -0.059  32.406  1.00 25.59           N  
ANISOU  175  NZ  LYS A 434     3085   3264   3373     77    590    306       N  
ATOM    176  N   SER A 435      -8.486  -5.676  35.296  1.00 15.05           N  
ANISOU  176  N   SER A 435     2182   1789   1747    132    551    548       N  
ATOM    177  CA  SER A 435      -8.132  -7.009  35.786  1.00 15.00           C  
ANISOU  177  CA  SER A 435     2259   1737   1703    135    560    608       C  
ATOM    178  C   SER A 435      -8.191  -7.062  37.298  1.00 15.46           C  
ANISOU  178  C   SER A 435     2384   1819   1672    145    599    641       C  
ATOM    179  O   SER A 435      -7.992  -6.051  37.974  1.00 15.13           O  
ANISOU  179  O   SER A 435     2334   1830   1583    171    593    614       O  
ATOM    180  CB  SER A 435      -6.736  -7.405  35.318  1.00 15.03           C  
ANISOU  180  CB  SER A 435     2291   1718   1703    187    487    616       C  
ATOM    181  OG  SER A 435      -6.401  -8.708  35.756  1.00 15.79           O  
ANISOU  181  OG  SER A 435     2470   1763   1767    197    493    674       O  
ATOM    182  N   ASP A 436      -8.472  -8.255  37.822  1.00 15.54           N  
ANISOU  182  N   ASP A 436     2464   1785   1654    122    640    699       N  
ATOM    183  CA  ASP A 436      -8.453  -8.508  39.263  1.00 16.53           C  
ANISOU  183  CA  ASP A 436     2672   1924   1683    132    677    743       C  
ATOM    184  C   ASP A 436      -7.054  -8.944  39.743  1.00 16.11           C  
ANISOU  184  C   ASP A 436     2696   1860   1566    199    608    777       C  
ATOM    185  O   ASP A 436      -6.810  -9.120  40.940  1.00 17.54           O  
ANISOU  185  O   ASP A 436     2954   2054   1655    219    618    814       O  
ATOM    186  CB AASP A 436      -9.514  -9.551  39.636  0.50 17.31           C  
ANISOU  186  CB AASP A 436     2814   1981   1783     69    762    794       C  
ATOM    187  CB BASP A 436      -9.506  -9.564  39.643  0.50 17.07           C  
ANISOU  187  CB BASP A 436     2785   1950   1751     69    762    795       C  
ATOM    188  CG AASP A 436     -10.943  -9.061  39.394  0.50 18.53           C  
ANISOU  188  CG AASP A 436     2887   2161   1994      4    836    763       C  
ATOM    189  CG BASP A 436      -9.394 -10.860  38.825  0.50 17.65           C  
ANISOU  189  CG BASP A 436     2888   1942   1878     48    748    830       C  
ATOM    190  OD1AASP A 436     -11.163  -7.838  39.235  0.50 18.72           O  
ANISOU  190  OD1AASP A 436     2836   2240   2035     17    830    706       O  
ATOM    191  OD1BASP A 436      -8.347 -11.128  38.201  0.50 16.50           O  
ANISOU  191  OD1BASP A 436     2753   1769   1747     96    675    827       O  
ATOM    192  OD2AASP A 436     -11.861  -9.909  39.380  0.50 20.63           O  
ANISOU  192  OD2AASP A 436     3162   2390   2287    -60    900    796       O  
ATOM    193  OD2BASP A 436     -10.376 -11.632  38.818  0.50 19.18           O  
ANISOU  193  OD2BASP A 436     3094   2096   2098    -19    814    859       O  
ATOM    194  N   LYS A 437      -6.145  -9.101  38.784  1.00 15.46           N  
ANISOU  194  N   LYS A 437     2588   1755   1531    233    538    763       N  
ATOM    195  CA  LYS A 437      -4.764  -9.502  39.032  1.00 14.94           C  
ANISOU  195  CA  LYS A 437     2572   1680   1423    302    465    789       C  
ATOM    196  C   LYS A 437      -3.778  -8.464  38.473  1.00 13.98           C  
ANISOU  196  C   LYS A 437     2381   1605   1324    346    390    733       C  
ATOM    197  O   LYS A 437      -4.149  -7.676  37.600  1.00 12.57           O  
ANISOU  197  O   LYS A 437     2122   1445   1208    321    392    680       O  
ATOM    198  CB  LYS A 437      -4.502 -10.880  38.408  1.00 15.77           C  
ANISOU  198  CB  LYS A 437     2722   1704   1567    308    457    831       C  
ATOM    199  CG  LYS A 437      -5.286 -12.016  39.060  1.00 18.29           C  
ANISOU  199  CG  LYS A 437     3127   1966   1855    267    524    896       C  
ATOM    200  CD  LYS A 437      -4.656 -12.431  40.378  1.00 21.58           C  
ANISOU  200  CD  LYS A 437     3644   2387   2170    314    508    955       C  
ATOM    201  CE  LYS A 437      -5.437 -13.543  41.075  1.00 23.36           C  
ANISOU  201  CE  LYS A 437     3965   2552   2357    270    580   1025       C  
ATOM    202  NZ  LYS A 437      -4.694 -14.043  42.264  1.00 25.61           N  
ANISOU  202  NZ  LYS A 437     4358   2831   2540    325    552   1089       N  
ATOM    203  N   PRO A 438      -2.528  -8.447  38.983  1.00 13.85           N  
ANISOU  203  N   PRO A 438     2394   1610   1257    410    321    746       N  
ATOM    204  CA  PRO A 438      -1.579  -7.437  38.481  1.00 13.66           C  
ANISOU  204  CA  PRO A 438     2299   1633   1257    443    253    694       C  
ATOM    205  C   PRO A 438      -1.266  -7.561  36.998  1.00 13.21           C  
ANISOU  205  C   PRO A 438     2179   1548   1292    444    232    667       C  
ATOM    206  O   PRO A 438      -1.147  -8.676  36.464  1.00 13.76           O  
ANISOU  206  O   PRO A 438     2276   1559   1393    453    236    698       O  
ATOM    207  CB  PRO A 438      -0.312  -7.703  39.304  1.00 14.56           C  
ANISOU  207  CB  PRO A 438     2461   1767   1305    510    184    724       C  
ATOM    208  CG  PRO A 438      -0.787  -8.445  40.517  1.00 15.19           C  
ANISOU  208  CG  PRO A 438     2641   1827   1302    506    222    784       C  
ATOM    209  CD  PRO A 438      -1.920  -9.289  40.033  1.00 15.10           C  
ANISOU  209  CD  PRO A 438     2648   1753   1336    453    300    809       C  
ATOM    210  N   LEU A 439      -1.139  -6.405  36.353  1.00 12.53           N  
ANISOU  210  N   LEU A 439     2014   1501   1244    435    211    608       N  
ATOM    211  CA  LEU A 439      -0.725  -6.304  34.961  1.00 12.66           C  
ANISOU  211  CA  LEU A 439     1969   1503   1337    438    187    577       C  
ATOM    212  C   LEU A 439       0.496  -5.403  34.899  1.00 13.00           C  
ANISOU  212  C   LEU A 439     1965   1598   1376    476    120    544       C  
ATOM    213  O   LEU A 439       0.554  -4.374  35.579  1.00 14.01           O  
ANISOU  213  O   LEU A 439     2081   1776   1467    471    106    518       O  
ATOM    214  CB  LEU A 439      -1.839  -5.712  34.097  1.00 12.20           C  
ANISOU  214  CB  LEU A 439     1858   1441   1337    380    228    538       C  
ATOM    215  CG  LEU A 439      -3.138  -6.511  33.977  1.00 12.55           C  
ANISOU  215  CG  LEU A 439     1928   1438   1402    330    293    562       C  
ATOM    216  CD1 LEU A 439      -4.193  -5.595  33.423  1.00 11.94           C  
ANISOU  216  CD1 LEU A 439     1789   1380   1369    282    323    519       C  
ATOM    217  CD2 LEU A 439      -2.920  -7.738  33.076  1.00 14.18           C  
ANISOU  217  CD2 LEU A 439     2157   1579   1650    334    290    585       C  
ATOM    218  N   TYR A 440       1.467  -5.799  34.087  1.00 13.93           N  
ANISOU  218  N   TYR A 440     2058   1703   1533    511     83    543       N  
ATOM    219  CA  TYR A 440       2.708  -5.038  33.979  1.00 14.25           C  
ANISOU  219  CA  TYR A 440     2045   1792   1576    544     22    515       C  
ATOM    220  C   TYR A 440       3.024  -4.695  32.542  1.00 12.57           C  
ANISOU  220  C   TYR A 440     1766   1574   1435    534     18    478       C  
ATOM    221  O   TYR A 440       2.581  -5.361  31.602  1.00 11.85           O  
ANISOU  221  O   TYR A 440     1680   1434   1388    521     50    483       O  
ATOM    222  CB  TYR A 440       3.882  -5.791  34.618  1.00 16.25           C  
ANISOU  222  CB  TYR A 440     2327   2052   1795    611    -30    554       C  
ATOM    223  CG  TYR A 440       3.657  -6.129  36.076  1.00 19.74           C  
ANISOU  223  CG  TYR A 440     2845   2502   2155    623    -32    595       C  
ATOM    224  CD1 TYR A 440       3.733  -5.140  37.070  1.00 20.73           C  
ANISOU  224  CD1 TYR A 440     2972   2684   2220    615    -57    575       C  
ATOM    225  CD2 TYR A 440       3.331  -7.425  36.458  1.00 22.23           C  
ANISOU  225  CD2 TYR A 440     3238   2762   2446    641     -7    652       C  
ATOM    226  CE1 TYR A 440       3.512  -5.451  38.415  1.00 23.35           C  
ANISOU  226  CE1 TYR A 440     3382   3024   2466    626    -57    612       C  
ATOM    227  CE2 TYR A 440       3.115  -7.751  37.800  1.00 22.81           C  
ANISOU  227  CE2 TYR A 440     3389   2840   2436    651     -6    695       C  
ATOM    228  CZ  TYR A 440       3.199  -6.755  38.769  1.00 24.11           C  
ANISOU  228  CZ  TYR A 440     3555   3068   2538    644    -30    675       C  
ATOM    229  OH  TYR A 440       2.980  -7.080  40.097  1.00 26.30           O  
ANISOU  229  OH  TYR A 440     3918   3351   2723    654    -26    717       O  
ATOM    230  N   GLY A 441       3.803  -3.638  32.384  1.00 11.81           N  
ANISOU  230  N   GLY A 441     1612   1527   1348    538    -22    442       N  
ATOM    231  CA  GLY A 441       4.238  -3.218  31.064  1.00 10.75           C  
ANISOU  231  CA  GLY A 441     1417   1394   1275    529    -26    408       C  
ATOM    232  C   GLY A 441       3.073  -3.046  30.117  1.00  9.72           C  
ANISOU  232  C   GLY A 441     1282   1229   1183    479     22    390       C  
ATOM    233  O   GLY A 441       2.035  -2.473  30.485  1.00  9.42           O  
ANISOU  233  O   GLY A 441     1253   1194   1133    441     47    379       O  
ATOM    234  N   ASN A 442       3.245  -3.522  28.884  1.00  9.10           N  
ANISOU  234  N   ASN A 442     1187   1119   1151    481     33    384       N  
ATOM    235  CA  ASN A 442       2.232  -3.310  27.854  1.00  8.53           C  
ANISOU  235  CA  ASN A 442     1107   1018   1116    434     67    363       C  
ATOM    236  C   ASN A 442       0.885  -3.931  28.176  1.00  8.78           C  
ANISOU  236  C   ASN A 442     1183   1012   1141    403    107    384       C  
ATOM    237  O   ASN A 442      -0.126  -3.493  27.640  1.00  8.55           O  
ANISOU  237  O   ASN A 442     1138    973   1136    359    129    364       O  
ATOM    238  CB  ASN A 442       2.698  -3.853  26.503  1.00  8.65           C  
ANISOU  238  CB  ASN A 442     1111   1004   1173    444     72    355       C  
ATOM    239  CG  ASN A 442       3.976  -3.225  26.036  1.00 10.21           C  
ANISOU  239  CG  ASN A 442     1255   1239   1384    467     44    333       C  
ATOM    240  OD1 ASN A 442       4.395  -2.174  26.538  1.00 10.14           O  
ANISOU  240  OD1 ASN A 442     1212   1279   1363    461     18    317       O  
ATOM    241  ND2 ASN A 442       4.617  -3.861  25.055  1.00 10.57           N  
ANISOU  241  ND2 ASN A 442     1296   1265   1457    491     51    331       N  
ATOM    242  N   ASP A 443       0.881  -4.945  29.044  1.00  9.25           N  
ANISOU  242  N   ASP A 443     1296   1050   1169    425    115    424       N  
ATOM    243  CA  ASP A 443      -0.358  -5.647  29.392  1.00  9.64           C  
ANISOU  243  CA  ASP A 443     1389   1060   1212    391    159    449       C  
ATOM    244  C   ASP A 443      -1.350  -4.772  30.159  1.00  9.27           C  
ANISOU  244  C   ASP A 443     1333   1046   1145    354    183    438       C  
ATOM    245  O   ASP A 443      -2.533  -5.112  30.265  1.00  9.84           O  
ANISOU  245  O   ASP A 443     1420   1095   1225    314    226    449       O  
ATOM    246  CB  ASP A 443      -0.067  -6.917  30.187  1.00 10.99           C  
ANISOU  246  CB  ASP A 443     1629   1197   1350    423    164    500       C  
ATOM    247  CG  ASP A 443       0.734  -7.938  29.395  1.00 13.16           C  
ANISOU  247  CG  ASP A 443     1922   1427   1651    462    151    511       C  
ATOM    248  OD1 ASP A 443       0.699  -7.905  28.145  1.00 15.93           O  
ANISOU  248  OD1 ASP A 443     2246   1760   2048    447    155    482       O  
ATOM    249  OD2 ASP A 443       1.396  -8.773  30.050  1.00 16.79           O  
ANISOU  249  OD2 ASP A 443     2427   1869   2083    511    136    550       O  
ATOM    250  N   ARG A 444      -0.867  -3.649  30.681  1.00  8.56           N  
ANISOU  250  N   ARG A 444     1214   1008   1030    367    156    415       N  
ATOM    251  CA  ARG A 444      -1.738  -2.664  31.341  1.00  8.52           C  
ANISOU  251  CA  ARG A 444     1198   1034   1007    339    179    395       C  
ATOM    252  C   ARG A 444      -2.700  -1.975  30.379  1.00  8.30           C  
ANISOU  252  C   ARG A 444     1123    999   1031    299    198    361       C  
ATOM    253  O   ARG A 444      -3.683  -1.378  30.821  1.00  9.13           O  
ANISOU  253  O   ARG A 444     1217   1118   1133    275    229    348       O  
ATOM    254  CB  ARG A 444      -0.906  -1.605  32.070  1.00  8.98           C  
ANISOU  254  CB  ARG A 444     1243   1143   1026    363    140    372       C  
ATOM    255  CG  ARG A 444      -0.109  -2.140  33.260  1.00  9.28           C  
ANISOU  255  CG  ARG A 444     1329   1197    999    402    115    405       C  
ATOM    256  CD  ARG A 444       0.902  -1.090  33.744  1.00 11.73           C  
ANISOU  256  CD  ARG A 444     1616   1558   1281    421     61    376       C  
ATOM    257  NE  ARG A 444       1.854  -0.776  32.673  1.00 12.40           N  
ANISOU  257  NE  ARG A 444     1647   1649   1416    430     24    353       N  
ATOM    258  CZ  ARG A 444       2.598   0.325  32.604  1.00 12.86           C  
ANISOU  258  CZ  ARG A 444     1664   1745   1479    428    -16    317       C  
ATOM    259  NH1 ARG A 444       2.542   1.254  33.550  1.00 14.83           N  
ANISOU  259  NH1 ARG A 444     1924   2027   1684    419    -30    294       N  
ATOM    260  NH2 ARG A 444       3.408   0.501  31.566  1.00 13.27           N  
ANISOU  260  NH2 ARG A 444     1666   1799   1578    432    -39    302       N  
ATOM    261  N   PHE A 445      -2.414  -2.042  29.077  1.00  8.41           N  
ANISOU  261  N   PHE A 445     1109    993   1092    294    181    347       N  
ATOM    262  CA  PHE A 445      -3.137  -1.253  28.086  1.00  8.44           C  
ANISOU  262  CA  PHE A 445     1069    995   1142    262    184    314       C  
ATOM    263  C   PHE A 445      -3.877  -2.122  27.084  1.00  8.57           C  
ANISOU  263  C   PHE A 445     1089    969   1200    233    202    322       C  
ATOM    264  O   PHE A 445      -3.415  -3.204  26.714  1.00  9.86           O  
ANISOU  264  O   PHE A 445     1282   1098   1366    244    199    342       O  
ATOM    265  CB  PHE A 445      -2.172  -0.330  27.327  1.00  8.14           C  
ANISOU  265  CB  PHE A 445      997    977   1119    275    145    285       C  
ATOM    266  CG  PHE A 445      -1.329   0.528  28.216  1.00  8.82           C  
ANISOU  266  CG  PHE A 445     1079   1104   1170    298    119    272       C  
ATOM    267  CD1 PHE A 445      -1.911   1.559  28.967  1.00  9.11           C  
ANISOU  267  CD1 PHE A 445     1109   1164   1189    287    128    252       C  
ATOM    268  CD2 PHE A 445       0.031   0.309  28.335  1.00  9.48           C  
ANISOU  268  CD2 PHE A 445     1163   1203   1237    330     85    279       C  
ATOM    269  CE1 PHE A 445      -1.137   2.357  29.815  1.00 10.74           C  
ANISOU  269  CE1 PHE A 445     1317   1405   1357    304    100    236       C  
ATOM    270  CE2 PHE A 445       0.811   1.114  29.170  1.00  9.92           C  
ANISOU  270  CE2 PHE A 445     1210   1299   1260    344     54    265       C  
ATOM    271  CZ  PHE A 445       0.228   2.134  29.905  1.00 10.58           C  
ANISOU  271  CZ  PHE A 445     1295   1402   1322    329     60    243       C  
ATOM    272  N   GLU A 446      -5.019  -1.615  26.624  1.00  8.17           N  
ANISOU  272  N   GLU A 446     1005    917   1182    198    216    304       N  
ATOM    273  CA  GLU A 446      -5.744  -2.245  25.527  1.00  8.72           C  
ANISOU  273  CA  GLU A 446     1069    950   1293    164    221    303       C  
ATOM    274  C   GLU A 446      -6.415  -1.168  24.702  1.00  7.56           C  
ANISOU  274  C   GLU A 446      874    817   1182    145    206    271       C  
ATOM    275  O   GLU A 446      -6.516  -0.010  25.129  1.00  7.88           O  
ANISOU  275  O   GLU A 446      888    890   1217    155    202    253       O  
ATOM    276  CB  GLU A 446      -6.779  -3.252  26.032  1.00  9.65           C  
ANISOU  276  CB  GLU A 446     1207   1043   1416    131    261    329       C  
ATOM    277  CG  GLU A 446      -7.952  -2.661  26.794  1.00 11.26           C  
ANISOU  277  CG  GLU A 446     1378   1275   1625    109    296    325       C  
ATOM    278  CD  GLU A 446      -8.964  -3.723  27.248  1.00 13.68           C  
ANISOU  278  CD  GLU A 446     1701   1557   1940     68    342    354       C  
ATOM    279  OE1 GLU A 446      -8.902  -4.884  26.772  1.00 18.52           O  
ANISOU  279  OE1 GLU A 446     2349   2124   2565     49    342    373       O  
ATOM    280  OE2 GLU A 446      -9.823  -3.386  28.068  1.00 18.40           O  
ANISOU  280  OE2 GLU A 446     2278   2180   2534     53    382    356       O  
ATOM    281  N   GLY A 447      -6.901  -1.552  23.526  1.00  6.99           N  
ANISOU  281  N   GLY A 447      794    717   1144    117    194    264       N  
ATOM    282  CA  GLY A 447      -7.638  -0.607  22.687  1.00  6.36           C  
ANISOU  282  CA  GLY A 447      671    647   1098    100    174    239       C  
ATOM    283  C   GLY A 447      -7.235  -0.718  21.237  1.00  6.45           C  
ANISOU  283  C   GLY A 447      692    637   1122     93    141    226       C  
ATOM    284  O   GLY A 447      -6.362  -1.506  20.876  1.00  6.36           O  
ANISOU  284  O   GLY A 447      718    604   1096    105    138    233       O  
ATOM    285  N   TYR A 448      -7.882   0.090  20.408  1.00  5.60           N  
ANISOU  285  N   TYR A 448      553    535   1040     79    116    208       N  
ATOM    286  CA  TYR A 448      -7.612   0.094  18.970  1.00  6.11           C  
ANISOU  286  CA  TYR A 448      632    581   1110     70     83    195       C  
ATOM    287  C   TYR A 448      -6.132   0.246  18.632  1.00  6.48           C  
ANISOU  287  C   TYR A 448      706    628   1128     99     77    192       C  
ATOM    288  O   TYR A 448      -5.599  -0.509  17.805  1.00  6.43           O  
ANISOU  288  O   TYR A 448      734    598   1113     97     73    191       O  
ATOM    289  CB  TYR A 448      -8.427   1.206  18.292  1.00  6.43           C  
ANISOU  289  CB  TYR A 448      635    633   1175     60     53    179       C  
ATOM    290  CG  TYR A 448      -8.177   1.346  16.801  1.00  5.77           C  
ANISOU  290  CG  TYR A 448      572    532   1087     51     16    168       C  
ATOM    291  CD1 TYR A 448      -9.079   0.827  15.870  1.00  6.16           C  
ANISOU  291  CD1 TYR A 448      622    563   1156     17     -9    163       C  
ATOM    292  CD2 TYR A 448      -7.029   1.988  16.323  1.00  6.20           C  
ANISOU  292  CD2 TYR A 448      647    591   1117     72      7    163       C  
ATOM    293  CE1 TYR A 448      -8.838   0.949  14.499  1.00  6.90           C  
ANISOU  293  CE1 TYR A 448      745    641   1235      9    -43    153       C  
ATOM    294  CE2 TYR A 448      -6.786   2.113  14.975  1.00  7.34           C  
ANISOU  294  CE2 TYR A 448      817    720   1250     62    -19    155       C  
ATOM    295  CZ  TYR A 448      -7.692   1.598  14.062  1.00  7.53           C  
ANISOU  295  CZ  TYR A 448      850    726   1286     32    -45    150       C  
ATOM    296  OH  TYR A 448      -7.452   1.736  12.713  1.00  8.75           O  
ANISOU  296  OH  TYR A 448     1038    866   1419     23    -72    142       O  
ATOM    297  N   CYS A 449      -5.467   1.199  19.282  1.00  6.43           N  
ANISOU  297  N   CYS A 449      686    651   1108    124     78    189       N  
ATOM    298  CA  CYS A 449      -4.050   1.449  18.991  1.00  6.61           C  
ANISOU  298  CA  CYS A 449      721    681   1109    147     71    185       C  
ATOM    299  C   CYS A 449      -3.149   0.326  19.487  1.00  6.18           C  
ANISOU  299  C   CYS A 449      692    620   1036    169     89    201       C  
ATOM    300  O   CYS A 449      -2.096   0.079  18.901  1.00  7.19           O  
ANISOU  300  O   CYS A 449      833    745   1155    186     88    198       O  
ATOM    301  CB  CYS A 449      -3.592   2.777  19.563  1.00  6.45           C  
ANISOU  301  CB  CYS A 449      677    690   1082    160     63    175       C  
ATOM    302  SG  CYS A 449      -4.270   4.165  18.617  1.00  9.85           S  
ANISOU  302  SG  CYS A 449     1092   1118   1534    143     36    159       S  
ATOM    303  N   LEU A 450      -3.568  -0.375  20.538  1.00  5.96           N  
ANISOU  303  N   LEU A 450      673    589   1004    173    108    218       N  
ATOM    304  CA  LEU A 450      -2.793  -1.533  20.985  1.00  6.35           C  
ANISOU  304  CA  LEU A 450      754    623   1035    198    122    238       C  
ATOM    305  C   LEU A 450      -2.932  -2.688  19.990  1.00  6.73           C  
ANISOU  305  C   LEU A 450      838    626   1094    186    127    239       C  
ATOM    306  O   LEU A 450      -1.943  -3.346  19.653  1.00  7.30           O  
ANISOU  306  O   LEU A 450      933    683   1157    215    130    241       O  
ATOM    307  CB  LEU A 450      -3.175  -1.952  22.410  1.00  7.07           C  
ANISOU  307  CB  LEU A 450      856    721   1111    204    141    261       C  
ATOM    308  CG  LEU A 450      -2.569  -1.125  23.562  1.00  7.32           C  
ANISOU  308  CG  LEU A 450      872    794   1114    230    135    261       C  
ATOM    309  CD1 LEU A 450      -1.026  -1.200  23.653  1.00  9.98           C  
ANISOU  309  CD1 LEU A 450     1211   1148   1434    270    116    264       C  
ATOM    310  CD2 LEU A 450      -3.016   0.332  23.541  1.00  9.02           C  
ANISOU  310  CD2 LEU A 450     1051   1038   1340    215    125    236       C  
ATOM    311  N   ASP A 451      -4.135  -2.903  19.459  1.00  6.75           N  
ANISOU  311  N   ASP A 451      841    606   1117    145    126    233       N  
ATOM    312  CA  ASP A 451      -4.310  -3.917  18.419  1.00  7.39           C  
ANISOU  312  CA  ASP A 451      960    641   1206    127    125    227       C  
ATOM    313  C   ASP A 451      -3.511  -3.524  17.179  1.00  7.00           C  
ANISOU  313  C   ASP A 451      916    594   1148    139    110    205       C  
ATOM    314  O   ASP A 451      -2.870  -4.364  16.549  1.00  7.62           O  
ANISOU  314  O   ASP A 451     1034    643   1218    154    118    201       O  
ATOM    315  CB  ASP A 451      -5.787  -4.103  18.067  1.00  7.89           C  
ANISOU  315  CB  ASP A 451     1015    688   1296     74    118    222       C  
ATOM    316  CG  ASP A 451      -6.560  -4.845  19.141  1.00  9.28           C  
ANISOU  316  CG  ASP A 451     1195    850   1481     55    145    245       C  
ATOM    317  OD1 ASP A 451      -5.956  -5.265  20.153  1.00  8.55           O  
ANISOU  317  OD1 ASP A 451     1122    757   1368     84    167    268       O  
ATOM    318  OD2 ASP A 451      -7.781  -5.035  18.944  1.00 10.99           O  
ANISOU  318  OD2 ASP A 451     1395   1056   1724      8    143    242       O  
ATOM    319  N   LEU A 452      -3.520  -2.241  16.849  1.00  6.21           N  
ANISOU  319  N   LEU A 452      783    528   1050    134     92    193       N  
ATOM    320  CA  LEU A 452      -2.741  -1.754  15.713  1.00  6.01           C  
ANISOU  320  CA  LEU A 452      765    507   1013    142     83    176       C  
ATOM    321  C   LEU A 452      -1.253  -2.059  15.923  1.00  6.31           C  
ANISOU  321  C   LEU A 452      808    554   1034    185    102    180       C  
ATOM    322  O   LEU A 452      -0.588  -2.542  15.006  1.00  7.01           O  
ANISOU  322  O   LEU A 452      924    627   1113    196    113    170       O  
ATOM    323  CB  LEU A 452      -2.967  -0.258  15.518  1.00  5.64           C  
ANISOU  323  CB  LEU A 452      683    490    969    130     62    168       C  
ATOM    324  CG  LEU A 452      -2.214   0.387  14.351  1.00  6.20           C  
ANISOU  324  CG  LEU A 452      765    567   1025    131     55    156       C  
ATOM    325  CD1 LEU A 452      -2.606  -0.202  12.989  1.00  7.82           C  
ANISOU  325  CD1 LEU A 452     1012    740   1219    109     46    144       C  
ATOM    326  CD2 LEU A 452      -2.432   1.898  14.351  1.00  7.45           C  
ANISOU  326  CD2 LEU A 452      894    748   1188    121     35    153       C  
ATOM    327  N   LEU A 453      -0.739  -1.763  17.116  1.00  6.06           N  
ANISOU  327  N   LEU A 453      750    552   1001    210    106    193       N  
ATOM    328  CA  LEU A 453       0.652  -2.089  17.440  1.00  6.92           C  
ANISOU  328  CA  LEU A 453      854    675   1100    254    118    199       C  
ATOM    329  C   LEU A 453       0.971  -3.582  17.316  1.00  6.88           C  
ANISOU  329  C   LEU A 453      891    630   1092    281    136    208       C  
ATOM    330  O   LEU A 453       2.046  -3.966  16.837  1.00  7.42           O  
ANISOU  330  O   LEU A 453      964    698   1157    315    149    202       O  
ATOM    331  CB  LEU A 453       1.011  -1.601  18.838  1.00  7.96           C  
ANISOU  331  CB  LEU A 453      955    843   1225    273    110    212       C  
ATOM    332  CG  LEU A 453       1.660  -0.219  18.905  1.00 10.06           C  
ANISOU  332  CG  LEU A 453     1178   1153   1490    270     95    200       C  
ATOM    333  CD1 LEU A 453       1.523   0.345  20.315  1.00 12.13           C  
ANISOU  333  CD1 LEU A 453     1422   1443   1743    275     82    207       C  
ATOM    334  CD2 LEU A 453       3.130  -0.269  18.444  1.00 11.62           C  
ANISOU  334  CD2 LEU A 453     1357   1370   1687    298    101    194       C  
ATOM    335  N   LYS A 454       0.045  -4.430  17.756  1.00  6.85           N  
ANISOU  335  N   LYS A 454      919    591   1093    266    140    221       N  
ATOM    336  CA  LYS A 454       0.259  -5.873  17.656  1.00  7.32           C  
ANISOU  336  CA  LYS A 454     1029    601   1151    288    158    230       C  
ATOM    337  C   LYS A 454       0.423  -6.289  16.193  1.00  8.07           C  
ANISOU  337  C   LYS A 454     1157    663   1245    282    165    204       C  
ATOM    338  O   LYS A 454       1.289  -7.100  15.859  1.00  8.41           O  
ANISOU  338  O   LYS A 454     1228    683   1284    323    183    201       O  
ATOM    339  CB  LYS A 454      -0.886  -6.644  18.323  1.00  8.19           C  
ANISOU  339  CB  LYS A 454     1170    674   1268    259    163    250       C  
ATOM    340  CG  LYS A 454      -0.948  -6.474  19.842  1.00  7.79           C  
ANISOU  340  CG  LYS A 454     1104    649   1208    272    164    279       C  
ATOM    341  CD  LYS A 454      -2.090  -7.263  20.454  1.00 10.30           C  
ANISOU  341  CD  LYS A 454     1453    930   1531    237    180    300       C  
ATOM    342  CE  LYS A 454      -2.378  -6.747  21.850  1.00 11.27           C  
ANISOU  342  CE  LYS A 454     1554   1090   1638    239    184    323       C  
ATOM    343  NZ  LYS A 454      -3.339  -7.590  22.615  1.00 13.15           N  
ANISOU  343  NZ  LYS A 454     1826   1295   1876    209    209    351       N  
ATOM    344  N   GLU A 455      -0.410  -5.719  15.326  1.00  8.60           N  
ANISOU  344  N   GLU A 455     1222    730   1314    235    151    185       N  
ATOM    345  CA  GLU A 455      -0.355  -6.005  13.898  1.00  9.36           C  
ANISOU  345  CA  GLU A 455     1356    800   1400    222    154    158       C  
ATOM    346  C   GLU A 455       0.912  -5.444  13.259  1.00  9.63           C  
ANISOU  346  C   GLU A 455     1373    866   1420    255    169    145       C  
ATOM    347  O   GLU A 455       1.616  -6.156  12.532  1.00  9.82           O  
ANISOU  347  O   GLU A 455     1432    866   1433    283    193    130       O  
ATOM    348  CB  GLU A 455      -1.596  -5.447  13.176  1.00  9.80           C  
ANISOU  348  CB  GLU A 455     1411    853   1458    164    126    145       C  
ATOM    349  CG  GLU A 455      -2.928  -6.033  13.645  1.00 12.52           C  
ANISOU  349  CG  GLU A 455     1765   1169   1823    122    114    154       C  
ATOM    350  CD  GLU A 455      -3.229  -7.415  13.086  1.00 14.83           C  
ANISOU  350  CD  GLU A 455     2123   1397   2114    106    120    143       C  
ATOM    351  OE1 GLU A 455      -2.537  -7.865  12.151  1.00 16.19           O  
ANISOU  351  OE1 GLU A 455     2339   1545   2266    125    131    122       O  
ATOM    352  OE2 GLU A 455      -4.178  -8.054  13.592  1.00 18.11           O  
ANISOU  352  OE2 GLU A 455     2548   1785   2549     71    117    154       O  
ATOM    353  N   LEU A 456       1.207  -4.171  13.522  1.00  8.47           N  
ANISOU  353  N   LEU A 456     1174    771   1275    252    159    149       N  
ATOM    354  CA  LEU A 456       2.343  -3.504  12.890  1.00  8.70           C  
ANISOU  354  CA  LEU A 456     1181    833   1293    270    174    138       C  
ATOM    355  C   LEU A 456       3.636  -4.174  13.301  1.00  8.59           C  
ANISOU  355  C   LEU A 456     1154    827   1284    328    201    143       C  
ATOM    356  O   LEU A 456       4.521  -4.384  12.473  1.00  9.61           O  
ANISOU  356  O   LEU A 456     1290    957   1404    352    230    128       O  
ATOM    357  CB  LEU A 456       2.417  -2.035  13.287  1.00  8.71           C  
ANISOU  357  CB  LEU A 456     1128    881   1299    252    157    144       C  
ATOM    358  CG  LEU A 456       1.327  -1.086  12.800  1.00 10.30           C  
ANISOU  358  CG  LEU A 456     1333   1082   1499    203    129    139       C  
ATOM    359  CD1 LEU A 456       1.545   0.262  13.445  1.00 11.59           C  
ANISOU  359  CD1 LEU A 456     1448   1286   1671    197    115    146       C  
ATOM    360  CD2 LEU A 456       1.297  -0.972  11.271  1.00 12.43           C  
ANISOU  360  CD2 LEU A 456     1642   1337   1745    183    133    122       C  
ATOM    361  N   SER A 457       3.736  -4.523  14.578  1.00  8.31           N  
ANISOU  361  N   SER A 457     1101    796   1260    354    192    165       N  
ATOM    362  CA  SER A 457       4.951  -5.151  15.080  1.00  8.47           C  
ANISOU  362  CA  SER A 457     1105    827   1288    417    208    174       C  
ATOM    363  C   SER A 457       5.182  -6.541  14.482  1.00  9.14           C  
ANISOU  363  C   SER A 457     1246    857   1370    452    235    166       C  
ATOM    364  O   SER A 457       6.330  -6.922  14.218  1.00  9.35           O  
ANISOU  364  O   SER A 457     1258    892   1401    505    260    159       O  
ATOM    365  CB  SER A 457       4.959  -5.190  16.607  1.00  8.65           C  
ANISOU  365  CB  SER A 457     1104    867   1315    437    185    202       C  
ATOM    366  OG  SER A 457       3.878  -5.958  17.111  1.00  8.79           O  
ANISOU  366  OG  SER A 457     1169    839   1330    421    180    218       O  
ATOM    367  N   ASN A 458       4.102  -7.297  14.265  1.00  9.09           N  
ANISOU  367  N   ASN A 458     1301    794   1360    424    232    164       N  
ATOM    368  CA  ASN A 458       4.209  -8.574  13.553  1.00  9.68           C  
ANISOU  368  CA  ASN A 458     1442    806   1430    448    257    150       C  
ATOM    369  C   ASN A 458       4.789  -8.395  12.154  1.00 10.25           C  
ANISOU  369  C   ASN A 458     1526    883   1487    452    285    116       C  
ATOM    370  O   ASN A 458       5.643  -9.171  11.715  1.00 11.61           O  
ANISOU  370  O   ASN A 458     1721   1034   1658    505    318    102       O  
ATOM    371  CB  ASN A 458       2.843  -9.258  13.433  1.00  9.80           C  
ANISOU  371  CB  ASN A 458     1519    760   1444    397    244    149       C  
ATOM    372  CG  ASN A 458       2.703 -10.445  14.340  1.00 10.80           C  
ANISOU  372  CG  ASN A 458     1686    836   1581    423    247    174       C  
ATOM    373  OD1 ASN A 458       3.158 -10.424  15.482  1.00 10.67           O  
ANISOU  373  OD1 ASN A 458     1640    843   1572    460    242    204       O  
ATOM    374  ND2 ASN A 458       2.066 -11.498  13.837  1.00 10.94           N  
ANISOU  374  ND2 ASN A 458     1778    781   1598    402    255    162       N  
ATOM    375  N   ILE A 459       4.312  -7.368  11.459  1.00  9.67           N  
ANISOU  375  N   ILE A 459     1439    836   1399    399    273    103       N  
ATOM    376  CA  ILE A 459       4.701  -7.148  10.063  1.00 10.01           C  
ANISOU  376  CA  ILE A 459     1505    881   1417    392    299     73       C  
ATOM    377  C   ILE A 459       6.133  -6.644   9.948  1.00 10.39           C  
ANISOU  377  C   ILE A 459     1498    982   1469    435    333     71       C  
ATOM    378  O   ILE A 459       6.857  -7.041   9.018  1.00 11.08           O  
ANISOU  378  O   ILE A 459     1608   1061   1541    463    376     47       O  
ATOM    379  CB  ILE A 459       3.704  -6.195   9.334  1.00  9.44           C  
ANISOU  379  CB  ILE A 459     1444    819   1325    322    270     65       C  
ATOM    380  CG1 ILE A 459       2.318  -6.841   9.256  1.00 10.09           C  
ANISOU  380  CG1 ILE A 459     1579    849   1407    280    238     61       C  
ATOM    381  CG2 ILE A 459       4.214  -5.827   7.939  1.00  9.70           C  
ANISOU  381  CG2 ILE A 459     1502    862   1323    316    298     39       C  
ATOM    382  CD1 ILE A 459       1.165  -5.849   9.025  1.00  9.90           C  
ANISOU  382  CD1 ILE A 459     1541    842   1378    218    195     64       C  
ATOM    383  N   LEU A 460       6.537  -5.775  10.877  1.00 10.21           N  
ANISOU  383  N   LEU A 460     1401   1013   1466    438    316     92       N  
ATOM    384  CA  LEU A 460       7.866  -5.147  10.842  1.00 10.96           C  
ANISOU  384  CA  LEU A 460     1428   1166   1571    466    342     91       C  
ATOM    385  C   LEU A 460       8.927  -5.921  11.617  1.00 11.30           C  
ANISOU  385  C   LEU A 460     1435   1219   1640    541    355    101       C  
ATOM    386  O   LEU A 460      10.106  -5.688  11.425  1.00 12.94           O  
ANISOU  386  O   LEU A 460     1588   1469   1860    573    384     95       O  
ATOM    387  CB  LEU A 460       7.822  -3.707  11.367  1.00 11.30           C  
ANISOU  387  CB  LEU A 460     1411   1262   1622    425    313    105       C  
ATOM    388  CG  LEU A 460       7.625  -2.544  10.398  1.00 12.26           C  
ANISOU  388  CG  LEU A 460     1535   1402   1723    369    318     95       C  
ATOM    389  CD1 LEU A 460       6.159  -2.448  10.067  1.00 13.00           C  
ANISOU  389  CD1 LEU A 460     1685   1456   1799    322    285     94       C  
ATOM    390  CD2 LEU A 460       8.096  -1.235  11.010  1.00 14.06           C  
ANISOU  390  CD2 LEU A 460     1692   1683   1967    347    301    107       C  
ATOM    391  N   GLY A 461       8.505  -6.815  12.506  1.00 10.83           N  
ANISOU  391  N   GLY A 461     1403   1122   1590    567    333    119       N  
ATOM    392  CA  GLY A 461       9.450  -7.650  13.239  1.00 11.27           C  
ANISOU  392  CA  GLY A 461     1435   1179   1667    645    339    133       C  
ATOM    393  C   GLY A 461      10.093  -6.995  14.450  1.00 11.28           C  
ANISOU  393  C   GLY A 461     1356   1243   1688    663    307    157       C  
ATOM    394  O   GLY A 461      11.308  -7.076  14.631  1.00 13.20           O  
ANISOU  394  O   GLY A 461     1540   1525   1952    718    318    158       O  
ATOM    395  N   PHE A 462       9.291  -6.360  15.300  1.00  9.48           N  
ANISOU  395  N   PHE A 462     1123   1026   1453    618    265    175       N  
ATOM    396  CA  PHE A 462       9.826  -5.765  16.521  1.00  9.29           C  
ANISOU  396  CA  PHE A 462     1034   1057   1439    632    229    195       C  
ATOM    397  C   PHE A 462       8.948  -6.026  17.735  1.00  8.44           C  
ANISOU  397  C   PHE A 462      959    928   1319    624    193    223       C  
ATOM    398  O   PHE A 462       7.759  -6.334  17.581  1.00  8.46           O  
ANISOU  398  O   PHE A 462     1022    883   1310    586    195    224       O  
ATOM    399  CB  PHE A 462      10.092  -4.246  16.346  1.00  8.97           C  
ANISOU  399  CB  PHE A 462      931   1077   1401    581    221    183       C  
ATOM    400  CG  PHE A 462       8.862  -3.405  16.096  1.00  9.13           C  
ANISOU  400  CG  PHE A 462      982   1083   1404    507    209    177       C  
ATOM    401  CD1 PHE A 462       8.480  -3.055  14.800  1.00  9.14           C  
ANISOU  401  CD1 PHE A 462     1011   1068   1395    467    234    157       C  
ATOM    402  CD2 PHE A 462       8.104  -2.932  17.167  1.00  7.81           C  
ANISOU  402  CD2 PHE A 462      816    922   1230    481    171    192       C  
ATOM    403  CE1 PHE A 462       7.359  -2.241  14.568  1.00  9.49           C  
ANISOU  403  CE1 PHE A 462     1078   1101   1427    406    216    153       C  
ATOM    404  CE2 PHE A 462       6.971  -2.111  16.947  1.00  8.23           C  
ANISOU  404  CE2 PHE A 462      889    964   1273    420    160    186       C  
ATOM    405  CZ  PHE A 462       6.601  -1.776  15.639  1.00  8.63           C  
ANISOU  405  CZ  PHE A 462      963    998   1319    385    180    167       C  
ATOM    406  N   ILE A 463       9.541  -5.926  18.925  1.00  8.84           N  
ANISOU  406  N   ILE A 463      971   1017   1372    657    160    244       N  
ATOM    407  CA  ILE A 463       8.754  -5.723  20.147  1.00  9.32           C  
ANISOU  407  CA  ILE A 463     1051   1078   1414    635    126    268       C  
ATOM    408  C   ILE A 463       8.898  -4.259  20.573  1.00  9.06           C  
ANISOU  408  C   ILE A 463      959   1108   1377    593     99    257       C  
ATOM    409  O   ILE A 463       9.751  -3.534  20.055  1.00  8.48           O  
ANISOU  409  O   ILE A 463      827   1077   1319    588    103    238       O  
ATOM    410  CB  ILE A 463       9.144  -6.699  21.293  1.00 10.10           C  
ANISOU  410  CB  ILE A 463     1169   1166   1504    699    103    303       C  
ATOM    411  CG1 ILE A 463      10.612  -6.531  21.691  1.00  9.85           C  
ANISOU  411  CG1 ILE A 463     1064   1192   1487    757     79    306       C  
ATOM    412  CG2 ILE A 463       8.812  -8.152  20.916  1.00 11.13           C  
ANISOU  412  CG2 ILE A 463     1374   1218   1637    733    131    314       C  
ATOM    413  CD1 ILE A 463      10.994  -7.290  22.960  1.00  9.66           C  
ANISOU  413  CD1 ILE A 463     1055   1167   1448    819     42    344       C  
ATOM    414  N   TYR A 464       8.076  -3.839  21.529  1.00  8.61           N  
ANISOU  414  N   TYR A 464      919   1054   1299    563     75    269       N  
ATOM    415  CA  TYR A 464       7.961  -2.427  21.863  1.00  8.60           C  
ANISOU  415  CA  TYR A 464      880   1097   1292    517     54    254       C  
ATOM    416  C   TYR A 464       7.627  -2.228  23.334  1.00  9.06           C  
ANISOU  416  C   TYR A 464      949   1173   1322    518     21    272       C  
ATOM    417  O   TYR A 464       7.198  -3.154  24.022  1.00  9.93           O  
ANISOU  417  O   TYR A 464     1105   1254   1413    543     21    298       O  
ATOM    418  CB  TYR A 464       6.905  -1.751  20.974  1.00  8.71           C  
ANISOU  418  CB  TYR A 464      912   1087   1309    456     74    234       C  
ATOM    419  CG  TYR A 464       5.602  -2.490  20.938  1.00  9.45           C  
ANISOU  419  CG  TYR A 464     1068   1128   1395    440     89    246       C  
ATOM    420  CD1 TYR A 464       5.387  -3.511  20.004  1.00 11.11           C  
ANISOU  420  CD1 TYR A 464     1318   1290   1614    450    116    245       C  
ATOM    421  CD2 TYR A 464       4.587  -2.191  21.852  1.00 10.98           C  
ANISOU  421  CD2 TYR A 464     1279   1319   1573    415     78    255       C  
ATOM    422  CE1 TYR A 464       4.194  -4.220  19.985  1.00 11.43           C  
ANISOU  422  CE1 TYR A 464     1412   1281   1651    428    126    254       C  
ATOM    423  CE2 TYR A 464       3.389  -2.888  21.835  1.00 11.80           C  
ANISOU  423  CE2 TYR A 464     1431   1378   1675    395     95    266       C  
ATOM    424  CZ  TYR A 464       3.207  -3.892  20.893  1.00 12.07           C  
ANISOU  424  CZ  TYR A 464     1500   1364   1721    399    116    265       C  
ATOM    425  OH  TYR A 464       2.039  -4.596  20.879  1.00 14.44           O  
ANISOU  425  OH  TYR A 464     1845   1619   2023    372    130    275       O  
ATOM    426  N   ASP A 465       7.828  -1.003  23.796  1.00  9.11           N  
ANISOU  426  N   ASP A 465      916   1223   1321    489     -4    256       N  
ATOM    427  CA  ASP A 465       7.620  -0.633  25.187  1.00  8.95           C  
ANISOU  427  CA  ASP A 465      906   1226   1268    488    -36    264       C  
ATOM    428  C   ASP A 465       6.702   0.580  25.157  1.00  8.65           C  
ANISOU  428  C   ASP A 465      871   1189   1225    430    -32    241       C  
ATOM    429  O   ASP A 465       7.100   1.644  24.682  1.00  9.02           O  
ANISOU  429  O   ASP A 465      880   1259   1289    400    -39    216       O  
ATOM    430  CB  ASP A 465       8.973  -0.261  25.792  1.00  9.74           C  
ANISOU  430  CB  ASP A 465      951   1384   1367    514    -80    261       C  
ATOM    431  CG  ASP A 465       8.898   0.144  27.256  0.50 10.80           C  
ANISOU  431  CG  ASP A 465     1098   1547   1457    514   -121    267       C  
ATOM    432  OD1 ASP A 465       7.822   0.049  27.887  0.50 12.58           O  
ANISOU  432  OD1 ASP A 465     1379   1749   1652    501   -109    277       O  
ATOM    433  OD2 ASP A 465       9.955   0.566  27.782  0.50 12.31           O  
ANISOU  433  OD2 ASP A 465     1243   1789   1646    527   -165    259       O  
ATOM    434  N   VAL A 466       5.470   0.416  25.643  1.00  7.95           N  
ANISOU  434  N   VAL A 466      830   1074   1118    414    -17    250       N  
ATOM    435  CA  VAL A 466       4.487   1.493  25.599  1.00  8.04           C  
ANISOU  435  CA  VAL A 466      843   1081   1129    368     -9    228       C  
ATOM    436  C   VAL A 466       4.676   2.430  26.789  1.00  8.69           C  
ANISOU  436  C   VAL A 466      920   1201   1181    362    -38    215       C  
ATOM    437  O   VAL A 466       4.627   1.991  27.954  1.00  8.88           O  
ANISOU  437  O   VAL A 466      971   1236   1167    384    -48    233       O  
ATOM    438  CB  VAL A 466       3.050   0.926  25.580  1.00  7.80           C  
ANISOU  438  CB  VAL A 466      856   1011   1097    353     24    241       C  
ATOM    439  CG1 VAL A 466       1.986   2.057  25.672  1.00  8.16           C  
ANISOU  439  CG1 VAL A 466      899   1057   1145    315     31    219       C  
ATOM    440  CG2 VAL A 466       2.841   0.113  24.315  1.00  9.17           C  
ANISOU  440  CG2 VAL A 466     1040   1146   1300    351     47    246       C  
ATOM    441  N   LYS A 467       4.884   3.713  26.489  1.00  8.74           N  
ANISOU  441  N   LYS A 467      897   1223   1201    330    -51    185       N  
ATOM    442  CA  LYS A 467       5.100   4.730  27.520  1.00  9.15           C  
ANISOU  442  CA  LYS A 467      946   1305   1226    318    -80    164       C  
ATOM    443  C   LYS A 467       4.132   5.886  27.345  1.00  8.40           C  
ANISOU  443  C   LYS A 467      862   1191   1138    282    -66    137       C  
ATOM    444  O   LYS A 467       4.150   6.549  26.307  1.00  8.41           O  
ANISOU  444  O   LYS A 467      844   1178   1173    256    -61    123       O  
ATOM    445  CB  LYS A 467       6.519   5.296  27.421  1.00  9.63           C  
ANISOU  445  CB  LYS A 467      958   1403   1297    314   -117    149       C  
ATOM    446  CG  LYS A 467       7.651   4.278  27.581  1.00 12.97           C  
ANISOU  446  CG  LYS A 467     1356   1853   1720    357   -138    172       C  
ATOM    447  CD  LYS A 467       8.939   5.042  27.848  1.00 18.04           C  
ANISOU  447  CD  LYS A 467     1944   2542   2369    345   -183    152       C  
ATOM    448  CE  LYS A 467      10.139   4.155  28.009  1.00 22.48           C  
ANISOU  448  CE  LYS A 467     2466   3139   2937    392   -209    172       C  
ATOM    449  NZ  LYS A 467      11.355   5.024  28.112  1.00 24.01           N  
ANISOU  449  NZ  LYS A 467     2593   3382   3148    369   -251    148       N  
ATOM    450  N   LEU A 468       3.312   6.138  28.356  1.00  8.23           N  
ANISOU  450  N   LEU A 468      873   1170   1085    283    -59    131       N  
ATOM    451  CA  LEU A 468       2.401   7.276  28.315  1.00  7.41           C  
ANISOU  451  CA  LEU A 468      778   1049    989    258    -46    103       C  
ATOM    452  C   LEU A 468       3.185   8.581  28.308  1.00  7.68           C  
ANISOU  452  C   LEU A 468      794   1095   1028    233    -79     70       C  
ATOM    453  O   LEU A 468       4.107   8.768  29.098  1.00  8.56           O  
ANISOU  453  O   LEU A 468      901   1238   1112    236   -114     60       O  
ATOM    454  CB  LEU A 468       1.459   7.238  29.516  1.00  7.95           C  
ANISOU  454  CB  LEU A 468      883   1119   1017    269    -26    102       C  
ATOM    455  CG  LEU A 468       0.465   6.078  29.482  1.00  8.49           C  
ANISOU  455  CG  LEU A 468      969   1170   1088    280     14    133       C  
ATOM    456  CD1 LEU A 468      -0.457   6.152  30.689  1.00  9.26           C  
ANISOU  456  CD1 LEU A 468     1100   1274   1144    287     42    130       C  
ATOM    457  CD2 LEU A 468      -0.348   6.081  28.194  1.00  9.49           C  
ANISOU  457  CD2 LEU A 468     1076   1263   1265    263     37    134       C  
ATOM    458  N   VAL A 469       2.804   9.495  27.416  1.00  7.04           N  
ANISOU  458  N   VAL A 469      707    987    982    208    -71     53       N  
ATOM    459  CA  VAL A 469       3.512  10.769  27.290  1.00  7.94           C  
ANISOU  459  CA  VAL A 469      810   1101   1105    177    -98     23       C  
ATOM    460  C   VAL A 469       3.502  11.499  28.648  1.00  8.81           C  
ANISOU  460  C   VAL A 469      947   1225   1175    176   -118     -7       C  
ATOM    461  O   VAL A 469       2.431  11.689  29.241  1.00  8.89           O  
ANISOU  461  O   VAL A 469      989   1221   1168    189    -95    -17       O  
ATOM    462  CB  VAL A 469       2.918  11.634  26.135  1.00  7.66           C  
ANISOU  462  CB  VAL A 469      777   1024   1109    153    -83     14       C  
ATOM    463  CG1 VAL A 469       1.416  11.910  26.331  1.00  8.15           C  
ANISOU  463  CG1 VAL A 469      867   1058   1173    167    -58      8       C  
ATOM    464  CG2 VAL A 469       3.693  12.932  25.977  1.00  8.38           C  
ANISOU  464  CG2 VAL A 469      864   1109   1212    116   -109    -13       C  
ATOM    465  N   PRO A 470       4.692  11.867  29.154  1.00  9.71           N  
ANISOU  465  N   PRO A 470     1046   1369   1274    160   -159    -23       N  
ATOM    466  CA  PRO A 470       4.742  12.455  30.498  1.00 10.59           C  
ANISOU  466  CA  PRO A 470     1190   1496   1338    159   -184    -54       C  
ATOM    467  C   PRO A 470       3.837  13.648  30.758  1.00 10.62           C  
ANISOU  467  C   PRO A 470     1234   1463   1338    147   -169    -91       C  
ATOM    468  O   PRO A 470       3.204  13.706  31.828  1.00 11.77           O  
ANISOU  468  O   PRO A 470     1420   1613   1439    167   -158   -106       O  
ATOM    469  CB  PRO A 470       6.222  12.809  30.668  1.00 11.33           C  
ANISOU  469  CB  PRO A 470     1250   1624   1432    132   -237    -68       C  
ATOM    470  CG  PRO A 470       6.929  11.784  29.842  1.00 11.06           C  
ANISOU  470  CG  PRO A 470     1165   1610   1428    145   -235    -31       C  
ATOM    471  CD  PRO A 470       6.048  11.635  28.614  1.00 10.61           C  
ANISOU  471  CD  PRO A 470     1111   1510   1410    146   -186    -13       C  
ATOM    472  N   ASP A 471       3.747  14.581  29.807  1.00  9.92           N  
ANISOU  472  N   ASP A 471     1139   1336   1294    119   -165   -104       N  
ATOM    473  CA  ASP A 471       2.931  15.784  30.043  1.00  9.69           C  
ANISOU  473  CA  ASP A 471     1151   1266   1266    114   -153   -140       C  
ATOM    474  C   ASP A 471       1.452  15.613  29.710  1.00  9.56           C  
ANISOU  474  C   ASP A 471     1146   1220   1266    145   -106   -129       C  
ATOM    475  O   ASP A 471       0.671  16.555  29.879  1.00 10.60           O  
ANISOU  475  O   ASP A 471     1308   1316   1404    152    -92   -158       O  
ATOM    476  CB  ASP A 471       3.520  17.023  29.353  1.00  9.76           C  
ANISOU  476  CB  ASP A 471     1158   1240   1309     68   -175   -163       C  
ATOM    477  CG  ASP A 471       3.427  16.979  27.830  1.00  9.32           C  
ANISOU  477  CG  ASP A 471     1077   1158   1305     56   -158   -133       C  
ATOM    478  OD1 ASP A 471       2.823  16.032  27.269  1.00  9.42           O  
ANISOU  478  OD1 ASP A 471     1075   1176   1330     84   -131   -100       O  
ATOM    479  OD2 ASP A 471       3.990  17.927  27.218  1.00  9.72           O  
ANISOU  479  OD2 ASP A 471     1130   1182   1383     15   -173   -145       O  
ATOM    480  N   GLY A 472       1.071  14.421  29.250  1.00  8.72           N  
ANISOU  480  N   GLY A 472     1016   1127   1170    166    -83    -90       N  
ATOM    481  CA  GLY A 472      -0.332  14.121  28.966  1.00  8.45           C  
ANISOU  481  CA  GLY A 472      983   1072   1154    191    -41    -77       C  
ATOM    482  C   GLY A 472      -0.929  14.933  27.829  1.00  8.08           C  
ANISOU  482  C   GLY A 472      932    980   1157    184    -37    -81       C  
ATOM    483  O   GLY A 472      -2.143  15.134  27.785  1.00  9.39           O  
ANISOU  483  O   GLY A 472     1102   1127   1340    207    -10    -85       O  
ATOM    484  N   LYS A 473      -0.084  15.388  26.897  1.00  7.82           N  
ANISOU  484  N   LYS A 473      890    933   1148    153    -62    -77       N  
ATOM    485  CA  LYS A 473      -0.545  16.203  25.770  1.00  7.70           C  
ANISOU  485  CA  LYS A 473      879    871   1174    144    -63    -75       C  
ATOM    486  C   LYS A 473      -0.281  15.535  24.430  1.00  6.61           C  
ANISOU  486  C   LYS A 473      718    734   1061    131    -63    -40       C  
ATOM    487  O   LYS A 473       0.649  14.746  24.278  1.00  6.27           O  
ANISOU  487  O   LYS A 473      654    721   1008    119    -68    -23       O  
ATOM    488  CB  LYS A 473       0.098  17.596  25.777  1.00  7.64           C  
ANISOU  488  CB  LYS A 473      898    832   1172    114    -87   -105       C  
ATOM    489  CG  LYS A 473      -0.262  18.457  26.984  1.00 10.13           C  
ANISOU  489  CG  LYS A 473     1251   1134   1465    127    -87   -148       C  
ATOM    490  CD  LYS A 473       0.696  19.617  27.073  1.00 13.37           C  
ANISOU  490  CD  LYS A 473     1686   1519   1875     85   -118   -178       C  
ATOM    491  CE  LYS A 473       0.526  20.364  28.372  1.00 16.48           C  
ANISOU  491  CE  LYS A 473     2121   1903   2236     94   -122   -227       C  
ATOM    492  NZ  LYS A 473      -0.708  21.181  28.328  1.00 19.26           N  
ANISOU  492  NZ  LYS A 473     2506   2203   2608    129    -99   -245       N  
ATOM    493  N   TYR A 474      -1.110  15.864  23.448  1.00  5.93           N  
ANISOU  493  N   TYR A 474      637    612   1005    137    -59    -29       N  
ATOM    494  CA  TYR A 474      -0.874  15.385  22.088  1.00  5.35           C  
ANISOU  494  CA  TYR A 474      552    534    948    122    -61      2       C  
ATOM    495  C   TYR A 474       0.288  16.159  21.454  1.00  6.24           C  
ANISOU  495  C   TYR A 474      674    632   1064     81    -76      0       C  
ATOM    496  O   TYR A 474       1.243  15.560  20.960  1.00  5.68           O  
ANISOU  496  O   TYR A 474      584    585    988     62    -74     16       O  
ATOM    497  CB  TYR A 474      -2.148  15.506  21.245  1.00  6.08           C  
ANISOU  497  CB  TYR A 474      650    595   1066    140    -59     14       C  
ATOM    498  CG  TYR A 474      -3.155  14.429  21.515  1.00  5.81           C  
ANISOU  498  CG  TYR A 474      593    581   1034    167    -41     25       C  
ATOM    499  CD1 TYR A 474      -3.256  13.335  20.655  1.00  5.93           C  
ANISOU  499  CD1 TYR A 474      595    605   1053    161    -39     51       C  
ATOM    500  CD2 TYR A 474      -4.011  14.495  22.624  1.00  5.87           C  
ANISOU  500  CD2 TYR A 474      595    597   1040    194    -24      7       C  
ATOM    501  CE1 TYR A 474      -4.198  12.314  20.884  1.00  5.33           C  
ANISOU  501  CE1 TYR A 474      500    543    982    177    -22     61       C  
ATOM    502  CE2 TYR A 474      -4.945  13.473  22.864  1.00  5.83           C  
ANISOU  502  CE2 TYR A 474      566    611   1039    211     -2     20       C  
ATOM    503  CZ  TYR A 474      -5.022  12.398  21.988  1.00  6.35           C  
ANISOU  503  CZ  TYR A 474      618    682   1113    200     -3     47       C  
ATOM    504  OH  TYR A 474      -5.935  11.395  22.200  1.00  6.65           O  
ANISOU  504  OH  TYR A 474      635    734   1158    208     17     59       O  
ATOM    505  N   GLY A 475       0.200  17.485  21.479  1.00  6.09           N  
ANISOU  505  N   GLY A 475      685    574   1056     69    -89    -18       N  
ATOM    506  CA  GLY A 475       1.320  18.327  21.041  1.00  6.70           C  
ANISOU  506  CA  GLY A 475      773    634   1137     21   -101    -22       C  
ATOM    507  C   GLY A 475       0.897  19.566  20.271  1.00  7.28           C  
ANISOU  507  C   GLY A 475      890    645   1231      9   -110    -20       C  
ATOM    508  O   GLY A 475       0.193  19.492  19.259  1.00  7.22           O  
ANISOU  508  O   GLY A 475      895    614   1236     23   -108      5       O  
ATOM    509  N   ALA A 476       1.364  20.704  20.757  1.00  8.11           N  
ANISOU  509  N   ALA A 476     1022    720   1339    -17   -122    -46       N  
ATOM    510  CA  ALA A 476       1.182  21.980  20.085  1.00  9.03           C  
ANISOU  510  CA  ALA A 476     1188    768   1474    -36   -132    -43       C  
ATOM    511  C   ALA A 476       2.403  22.840  20.332  1.00 11.34           C  
ANISOU  511  C   ALA A 476     1495   1047   1766    -97   -142    -62       C  
ATOM    512  O   ALA A 476       3.247  22.499  21.151  1.00 10.71           O  
ANISOU  512  O   ALA A 476     1383   1012   1673   -118   -146    -82       O  
ATOM    513  CB  ALA A 476      -0.071  22.674  20.606  1.00  9.87           C  
ANISOU  513  CB  ALA A 476     1328    831   1592     13   -138    -65       C  
ATOM    514  N   GLN A 477       2.474  23.957  19.612  1.00 13.46           N  
ANISOU  514  N   GLN A 477     1812   1251   2050   -127   -148    -53       N  
ATOM    515  CA  GLN A 477       3.537  24.941  19.786  1.00 16.69           C  
ANISOU  515  CA  GLN A 477     2243   1633   2466   -195   -157    -71       C  
ATOM    516  C   GLN A 477       3.137  26.073  20.711  1.00 18.95           C  
ANISOU  516  C   GLN A 477     2580   1862   2757   -187   -174   -114       C  
ATOM    517  O   GLN A 477       1.981  26.508  20.743  1.00 19.47           O  
ANISOU  517  O   GLN A 477     2685   1881   2831   -134   -176   -119       O  
ATOM    518  CB  GLN A 477       3.878  25.574  18.450  1.00 17.52           C  
ANISOU  518  CB  GLN A 477     2383   1690   2583   -239   -148    -35       C  
ATOM    519  CG  GLN A 477       4.552  24.671  17.487  1.00 18.41           C  
ANISOU  519  CG  GLN A 477     2454   1853   2689   -263   -125      2       C  
ATOM    520  CD  GLN A 477       4.794  25.352  16.156  1.00 21.51           C  
ANISOU  520  CD  GLN A 477     2894   2195   3085   -306   -112     40       C  
ATOM    521  OE1 GLN A 477       3.865  25.567  15.369  1.00 23.67           O  
ANISOU  521  OE1 GLN A 477     3213   2424   3355   -272   -117     67       O  
ATOM    522  NE2 GLN A 477       6.043  25.710  15.902  1.00 21.31           N  
ANISOU  522  NE2 GLN A 477     2855   2176   3064   -381    -97     43       N  
ATOM    523  N   ASN A 478       4.112  26.576  21.452  1.00 20.42           N  
ANISOU  523  N   ASN A 478     2767   2052   2940   -241   -188   -148       N  
ATOM    524  CA  ASN A 478       3.878  27.768  22.239  1.00 22.79           C  
ANISOU  524  CA  ASN A 478     3128   2288   3243   -246   -206   -193       C  
ATOM    525  C   ASN A 478       4.293  28.997  21.451  1.00 24.46           C  
ANISOU  525  C   ASN A 478     3398   2418   3478   -306   -210   -182       C  
ATOM    526  O   ASN A 478       4.716  28.896  20.290  1.00 24.56           O  
ANISOU  526  O   ASN A 478     3402   2428   3500   -341   -196   -137       O  
ATOM    527  CB  ASN A 478       4.580  27.693  23.603  1.00 22.90           C  
ANISOU  527  CB  ASN A 478     3123   2345   3234   -270   -226   -243       C  
ATOM    528  CG  ASN A 478       6.100  27.747  23.502  1.00 23.10           C  
ANISOU  528  CG  ASN A 478     3110   2403   3265   -357   -240   -243       C  
ATOM    529  OD1 ASN A 478       6.666  28.057  22.452  1.00 21.45           O  
ANISOU  529  OD1 ASN A 478     2899   2172   3078   -410   -229   -211       O  
ATOM    530  ND2 ASN A 478       6.766  27.442  24.612  1.00 23.46           N  
ANISOU  530  ND2 ASN A 478     3123   2504   3287   -374   -264   -279       N  
ATOM    531  N   ASP A 479       4.134  30.149  22.097  1.00 26.50           N  
ANISOU  531  N   ASP A 479     3722   2605   3742   -315   -226   -224       N  
ATOM    532  CA  ASP A 479       4.595  31.455  21.632  1.00 28.50           C  
ANISOU  532  CA  ASP A 479     4043   2769   4017   -380   -234   -224       C  
ATOM    533  C   ASP A 479       5.975  31.428  20.956  1.00 28.79           C  
ANISOU  533  C   ASP A 479     4046   2831   4063   -478   -228   -198       C  
ATOM    534  O   ASP A 479       6.170  32.054  19.909  1.00 29.84           O  
ANISOU  534  O   ASP A 479     4220   2906   4213   -520   -216   -161       O  
ATOM    535  CB  ASP A 479       4.625  32.402  22.837  1.00 29.64           C  
ANISOU  535  CB  ASP A 479     4242   2863   4157   -392   -256   -291       C  
ATOM    536  CG  ASP A 479       4.757  31.648  24.166  1.00 31.11           C  
ANISOU  536  CG  ASP A 479     4379   3131   4309   -369   -267   -336       C  
ATOM    537  OD1 ASP A 479       3.737  31.095  24.642  1.00 32.15           O  
ANISOU  537  OD1 ASP A 479     4502   3288   4425   -284   -256   -344       O  
ATOM    538  OD2 ASP A 479       5.877  31.590  24.723  1.00 33.12           O  
ANISOU  538  OD2 ASP A 479     4603   3427   4554   -437   -288   -362       O  
ATOM    539  N   LYS A 480       6.914  30.699  21.564  1.00 28.42           N  
ANISOU  539  N   LYS A 480     3923   2871   4004   -513   -235   -216       N  
ATOM    540  CA  LYS A 480       8.300  30.604  21.094  1.00 28.32           C  
ANISOU  540  CA  LYS A 480     3858   2897   4005   -604   -229   -199       C  
ATOM    541  C   LYS A 480       8.520  29.557  19.998  1.00 27.16           C  
ANISOU  541  C   LYS A 480     3651   2811   3857   -594   -195   -143       C  
ATOM    542  O   LYS A 480       9.632  29.422  19.477  1.00 27.54           O  
ANISOU  542  O   LYS A 480     3651   2895   3918   -664   -179   -124       O  
ATOM    543  CB  LYS A 480       9.238  30.304  22.271  1.00 28.81           C  
ANISOU  543  CB  LYS A 480     3861   3029   4057   -641   -259   -246       C  
ATOM    544  CG  LYS A 480       9.360  31.426  23.289  1.00 30.44           C  
ANISOU  544  CG  LYS A 480     4127   3176   4262   -679   -295   -306       C  
ATOM    545  CD  LYS A 480      10.312  31.042  24.412  1.00 32.00           C  
ANISOU  545  CD  LYS A 480     4262   3452   4444   -715   -332   -350       C  
ATOM    546  CE  LYS A 480      10.414  32.139  25.468  1.00 33.48           C  
ANISOU  546  CE  LYS A 480     4517   3581   4623   -755   -373   -417       C  
ATOM    547  NZ  LYS A 480      10.953  33.427  24.931  1.00 35.36           N  
ANISOU  547  NZ  LYS A 480     4809   3730   4896   -851   -374   -421       N  
ATOM    548  N   GLY A 481       7.472  28.808  19.663  1.00 25.57           N  
ANISOU  548  N   GLY A 481     3449   2623   3642   -510   -183   -118       N  
ATOM    549  CA  GLY A 481       7.579  27.732  18.678  1.00 23.72           C  
ANISOU  549  CA  GLY A 481     3166   2445   3401   -493   -153    -71       C  
ATOM    550  C   GLY A 481       8.084  26.406  19.242  1.00 22.18           C  
ANISOU  550  C   GLY A 481     2881   2354   3194   -471   -152    -79       C  
ATOM    551  O   GLY A 481       8.423  25.498  18.479  1.00 22.34           O  
ANISOU  551  O   GLY A 481     2855   2424   3211   -466   -126    -46       O  
ATOM    552  N   GLU A 482       8.153  26.301  20.569  1.00 20.65           N  
ANISOU  552  N   GLU A 482     2668   2188   2990   -456   -181   -123       N  
ATOM    553  CA  GLU A 482       8.550  25.060  21.236  1.00 18.87           C  
ANISOU  553  CA  GLU A 482     2367   2054   2748   -427   -188   -130       C  
ATOM    554  C   GLU A 482       7.353  24.118  21.277  1.00 16.72           C  
ANISOU  554  C   GLU A 482     2097   1797   2457   -338   -176   -116       C  
ATOM    555  O   GLU A 482       6.232  24.549  21.537  1.00 16.26           O  
ANISOU  555  O   GLU A 482     2093   1690   2395   -296   -181   -127       O  
ATOM    556  CB  GLU A 482       9.032  25.335  22.662  1.00 19.45           C  
ANISOU  556  CB  GLU A 482     2429   2151   2810   -444   -228   -181       C  
ATOM    557  CG  GLU A 482      10.237  26.267  22.744  1.00 22.53           C  
ANISOU  557  CG  GLU A 482     2810   2530   3222   -540   -246   -203       C  
ATOM    558  CD  GLU A 482      10.483  26.817  24.146  1.00 26.01           C  
ANISOU  558  CD  GLU A 482     3268   2970   3646   -560   -294   -261       C  
ATOM    559  OE1 GLU A 482       9.510  27.173  24.849  1.00 26.95           O  
ANISOU  559  OE1 GLU A 482     3450   3047   3742   -513   -304   -289       O  
ATOM    560  OE2 GLU A 482      11.666  26.911  24.543  1.00 28.12           O  
ANISOU  560  OE2 GLU A 482     3483   3279   3921   -623   -322   -280       O  
ATOM    561  N   TRP A 483       7.605  22.838  21.023  1.00 14.36           N  
ANISOU  561  N   TRP A 483     1740   1564   2151   -312   -161    -92       N  
ATOM    562  CA  TRP A 483       6.563  21.812  21.031  1.00 12.23           C  
ANISOU  562  CA  TRP A 483     1468   1313   1866   -237   -149    -76       C  
ATOM    563  C   TRP A 483       6.476  21.120  22.377  1.00 11.23           C  
ANISOU  563  C   TRP A 483     1317   1235   1715   -199   -167   -101       C  
ATOM    564  O   TRP A 483       7.423  21.148  23.169  1.00 12.17           O  
ANISOU  564  O   TRP A 483     1405   1391   1827   -227   -191   -123       O  
ATOM    565  CB  TRP A 483       6.847  20.769  19.953  1.00 11.99           C  
ANISOU  565  CB  TRP A 483     1400   1318   1838   -229   -120    -36       C  
ATOM    566  CG  TRP A 483       6.583  21.261  18.570  1.00 11.84           C  
ANISOU  566  CG  TRP A 483     1419   1250   1829   -249    -99     -6       C  
ATOM    567  CD1 TRP A 483       7.465  21.905  17.741  1.00 13.54           C  
ANISOU  567  CD1 TRP A 483     1638   1449   2057   -313    -84      9       C  
ATOM    568  CD2 TRP A 483       5.356  21.144  17.840  1.00 12.34           C  
ANISOU  568  CD2 TRP A 483     1523   1276   1888   -207    -93     17       C  
ATOM    569  NE1 TRP A 483       6.853  22.201  16.542  1.00 14.09           N  
ANISOU  569  NE1 TRP A 483     1758   1472   2124   -311    -68     40       N  
ATOM    570  CE2 TRP A 483       5.560  21.747  16.575  1.00 12.85           C  
ANISOU  570  CE2 TRP A 483     1623   1302   1958   -245    -77     45       C  
ATOM    571  CE3 TRP A 483       4.097  20.601  18.133  1.00 12.46           C  
ANISOU  571  CE3 TRP A 483     1548   1290   1898   -144    -99     16       C  
ATOM    572  CZ2 TRP A 483       4.553  21.812  15.604  1.00 12.55           C  
ANISOU  572  CZ2 TRP A 483     1631   1223   1913   -217    -76     73       C  
ATOM    573  CZ3 TRP A 483       3.090  20.673  17.161  1.00 12.01           C  
ANISOU  573  CZ3 TRP A 483     1527   1195   1843   -119    -97     42       C  
ATOM    574  CH2 TRP A 483       3.328  21.277  15.917  1.00 11.78           C  
ANISOU  574  CH2 TRP A 483     1535   1127   1814   -154    -90     69       C  
ATOM    575  N   ASN A 484       5.320  20.507  22.627  1.00  9.36           N  
ANISOU  575  N   ASN A 484     1093    998   1465   -137   -157    -95       N  
ATOM    576  CA  ASN A 484       5.114  19.672  23.805  1.00  8.32           C  
ANISOU  576  CA  ASN A 484      944    913   1305    -96   -165   -109       C  
ATOM    577  C   ASN A 484       4.462  18.347  23.392  1.00  7.49           C  
ANISOU  577  C   ASN A 484      817    833   1196    -48   -140    -75       C  
ATOM    578  O   ASN A 484       4.389  18.048  22.196  1.00  7.18           O  
ANISOU  578  O   ASN A 484      771    783   1174    -52   -122    -46       O  
ATOM    579  CB  ASN A 484       4.310  20.419  24.882  1.00  8.45           C  
ANISOU  579  CB  ASN A 484     1008    899   1305    -75   -175   -147       C  
ATOM    580  CG  ASN A 484       2.964  20.910  24.379  1.00  7.99           C  
ANISOU  580  CG  ASN A 484      989    783   1262    -42   -156   -142       C  
ATOM    581  OD1 ASN A 484       2.412  20.365  23.430  1.00  9.42           O  
ANISOU  581  OD1 ASN A 484     1159    961   1459    -22   -138   -108       O  
ATOM    582  ND2 ASN A 484       2.416  21.930  25.049  1.00 10.44           N  
ANISOU  582  ND2 ASN A 484     1347   1050   1569    -33   -162   -178       N  
ATOM    583  N   GLY A 485       4.039  17.544  24.368  1.00  7.49           N  
ANISOU  583  N   GLY A 485      810    865   1170     -8   -139    -80       N  
ATOM    584  CA  GLY A 485       3.312  16.298  24.113  1.00  6.45           C  
ANISOU  584  CA  GLY A 485      666    751   1035     35   -116    -51       C  
ATOM    585  C   GLY A 485       4.071  15.260  23.312  1.00  6.38           C  
ANISOU  585  C   GLY A 485      619    773   1034     31   -107    -21       C  
ATOM    586  O   GLY A 485       5.316  15.233  23.305  1.00  6.96           O  
ANISOU  586  O   GLY A 485      661    875   1109      5   -120    -22       O  
ATOM    587  N   MET A 486       3.310  14.393  22.642  1.00  5.77           N  
ANISOU  587  N   MET A 486      541    689    962     57    -85      5       N  
ATOM    588  CA  MET A 486       3.909  13.308  21.860  1.00  5.97           C  
ANISOU  588  CA  MET A 486      539    737    992     61    -71     31       C  
ATOM    589  C   MET A 486       4.763  13.839  20.729  1.00  6.33           C  
ANISOU  589  C   MET A 486      575    774   1055     22    -67     37       C  
ATOM    590  O   MET A 486       5.782  13.237  20.384  1.00  7.05           O  
ANISOU  590  O   MET A 486      632    896   1149     17    -58     47       O  
ATOM    591  CB  MET A 486       2.835  12.375  21.324  1.00  5.33           C  
ANISOU  591  CB  MET A 486      469    642    913     89    -51     52       C  
ATOM    592  CG  MET A 486       2.194  11.504  22.405  1.00  6.19           C  
ANISOU  592  CG  MET A 486      580    768   1004    124    -46     54       C  
ATOM    593  SD  MET A 486       0.902  10.437  21.750  1.00  6.20           S  
ANISOU  593  SD  MET A 486      592    750   1015    145    -24     76       S  
ATOM    594  CE  MET A 486      -0.388  11.651  21.489  1.00  7.04           C  
ANISOU  594  CE  MET A 486      716    818   1140    140    -28     62       C  
ATOM    595  N   VAL A 487       4.367  14.979  20.158  1.00  6.18           N  
ANISOU  595  N   VAL A 487      587    712   1049     -3    -69     32       N  
ATOM    596  CA  VAL A 487       5.131  15.533  19.053  1.00  6.64           C  
ANISOU  596  CA  VAL A 487      645    758   1119    -45    -59     42       C  
ATOM    597  C   VAL A 487       6.549  15.865  19.545  1.00  7.02           C  
ANISOU  597  C   VAL A 487      655    841   1173    -81    -68     28       C  
ATOM    598  O   VAL A 487       7.536  15.494  18.890  1.00  7.08           O  
ANISOU  598  O   VAL A 487      628    875   1188    -99    -50     40       O  
ATOM    599  CB  VAL A 487       4.417  16.756  18.440  1.00  6.46           C  
ANISOU  599  CB  VAL A 487      671    676   1106    -64    -65     42       C  
ATOM    600  CG1 VAL A 487       5.250  17.368  17.319  1.00  7.70           C  
ANISOU  600  CG1 VAL A 487      837    818   1271   -114    -51     57       C  
ATOM    601  CG2 VAL A 487       3.051  16.335  17.893  1.00  6.59           C  
ANISOU  601  CG2 VAL A 487      714    669   1122    -27    -62     58       C  
ATOM    602  N   LYS A 488       6.658  16.510  20.706  1.00  7.45           N  
ANISOU  602  N   LYS A 488      711    897   1222    -89    -96      0       N  
ATOM    603  CA  LYS A 488       7.984  16.816  21.273  1.00  8.51           C  
ANISOU  603  CA  LYS A 488      804   1068   1362   -126   -115    -17       C  
ATOM    604  C   LYS A 488       8.786  15.544  21.563  1.00  8.13           C  
ANISOU  604  C   LYS A 488      698   1083   1308    -98   -115     -6       C  
ATOM    605  O   LYS A 488      10.009  15.513  21.353  1.00  8.89           O  
ANISOU  605  O   LYS A 488      741   1215   1420   -126   -115     -6       O  
ATOM    606  CB  LYS A 488       7.850  17.661  22.538  1.00  9.33           C  
ANISOU  606  CB  LYS A 488      930   1163   1453   -136   -150    -53       C  
ATOM    607  CG  LYS A 488       9.184  17.924  23.243  1.00 11.64           C  
ANISOU  607  CG  LYS A 488     1177   1497   1747   -175   -182    -75       C  
ATOM    608  CD  LYS A 488       9.009  18.700  24.537  1.00 13.89           C  
ANISOU  608  CD  LYS A 488     1494   1772   2011   -184   -220   -115       C  
ATOM    609  CE  LYS A 488      10.327  18.855  25.298  1.00 17.77           C  
ANISOU  609  CE  LYS A 488     1937   2314   2502   -222   -261   -137       C  
ATOM    610  NZ  LYS A 488      11.388  19.511  24.461  1.00 19.61           N  
ANISOU  610  NZ  LYS A 488     2132   2545   2773   -292   -256   -135       N  
ATOM    611  N   GLU A 489       8.118  14.497  22.042  1.00  7.70           N  
ANISOU  611  N   GLU A 489      650   1041   1234    -43   -113      3       N  
ATOM    612  CA  GLU A 489       8.816  13.238  22.318  1.00  7.50           C  
ANISOU  612  CA  GLU A 489      580   1067   1204     -9   -113     17       C  
ATOM    613  C   GLU A 489       9.478  12.697  21.049  1.00  7.89           C  
ANISOU  613  C   GLU A 489      596   1126   1274    -13    -79     38       C  
ATOM    614  O   GLU A 489      10.590  12.158  21.096  1.00  8.40           O  
ANISOU  614  O   GLU A 489      605   1236   1349     -7    -80     42       O  
ATOM    615  CB  GLU A 489       7.897  12.164  22.911  1.00  7.61           C  
ANISOU  615  CB  GLU A 489      617   1080   1193     48   -110     29       C  
ATOM    616  CG  GLU A 489       7.332  12.452  24.289  1.00  7.86           C  
ANISOU  616  CG  GLU A 489      678   1114   1196     61   -136     11       C  
ATOM    617  CD  GLU A 489       8.412  12.699  25.315  1.00  9.28           C  
ANISOU  617  CD  GLU A 489      827   1336   1362     49   -178     -8       C  
ATOM    618  OE1 GLU A 489       9.002  11.708  25.802  1.00 13.49           O  
ANISOU  618  OE1 GLU A 489     1332   1911   1884     83   -191      7       O  
ATOM    619  OE2 GLU A 489       8.692  13.883  25.611  1.00 11.83           O  
ANISOU  619  OE2 GLU A 489     1156   1650   1687      7   -200    -36       O  
ATOM    620  N   LEU A 490       8.790  12.836  19.920  1.00  7.49           N  
ANISOU  620  N   LEU A 490      582   1035   1228    -21    -49     51       N  
ATOM    621  CA  LEU A 490       9.366  12.431  18.632  1.00  7.37           C  
ANISOU  621  CA  LEU A 490      550   1026   1225    -30    -11     68       C  
ATOM    622  C   LEU A 490      10.488  13.360  18.185  1.00  8.59           C  
ANISOU  622  C   LEU A 490      670   1193   1399    -88     -2     62       C  
ATOM    623  O   LEU A 490      11.561  12.895  17.793  1.00  8.90           O  
ANISOU  623  O   LEU A 490      655   1272   1453    -90     20     67       O  
ATOM    624  CB  LEU A 490       8.280  12.378  17.564  1.00  7.21           C  
ANISOU  624  CB  LEU A 490      585    958   1195    -26     12     83       C  
ATOM    625  CG  LEU A 490       7.208  11.318  17.811  1.00  6.37           C  
ANISOU  625  CG  LEU A 490      505    840   1075     24     10     91       C  
ATOM    626  CD1 LEU A 490       6.071  11.526  16.798  1.00  6.30           C  
ANISOU  626  CD1 LEU A 490      548    785   1061     18     20    101       C  
ATOM    627  CD2 LEU A 490       7.755   9.888  17.779  1.00  8.24           C  
ANISOU  627  CD2 LEU A 490      714   1107   1309     64     27    101       C  
ATOM    628  N   ILE A 491      10.245  14.667  18.232  1.00  8.28           N  
ANISOU  628  N   ILE A 491      662   1120   1365   -135    -16     50       N  
ATOM    629  CA  ILE A 491      11.262  15.639  17.824  1.00  9.21           C  
ANISOU  629  CA  ILE A 491      753   1242   1503   -201     -7     45       C  
ATOM    630  C   ILE A 491      12.566  15.408  18.596  1.00 10.35           C  
ANISOU  630  C   ILE A 491      816   1450   1665   -211    -26     31       C  
ATOM    631  O   ILE A 491      13.657  15.446  18.014  1.00 11.27           O  
ANISOU  631  O   ILE A 491      878   1598   1805   -244      1     36       O  
ATOM    632  CB  ILE A 491      10.764  17.108  17.978  1.00  9.36           C  
ANISOU  632  CB  ILE A 491      827   1205   1525   -248    -28     32       C  
ATOM    633  CG1 ILE A 491       9.638  17.404  16.982  1.00  8.37           C  
ANISOU  633  CG1 ILE A 491      773   1019   1387   -240     -9     52       C  
ATOM    634  CG2 ILE A 491      11.907  18.110  17.762  1.00 11.19           C  
ANISOU  634  CG2 ILE A 491     1029   1442   1781   -325    -23     25       C  
ATOM    635  CD1 ILE A 491       8.911  18.714  17.245  1.00  9.34           C  
ANISOU  635  CD1 ILE A 491      957   1079   1511   -264    -34     40       C  
ATOM    636  N   ASP A 492      12.428  15.135  19.889  1.00 10.26           N  
ANISOU  636  N   ASP A 492      796   1460   1643   -180    -70     15       N  
ATOM    637  CA  ASP A 492      13.589  14.973  20.775  1.00 10.69           C  
ANISOU  637  CA  ASP A 492      777   1576   1710   -186   -104     -1       C  
ATOM    638  C   ASP A 492      14.130  13.536  20.788  1.00 11.26           C  
ANISOU  638  C   ASP A 492      793   1700   1784   -124    -94     16       C  
ATOM    639  O   ASP A 492      15.012  13.203  21.588  1.00 11.73           O  
ANISOU  639  O   ASP A 492      791   1814   1852   -112   -129      8       O  
ATOM    640  CB  ASP A 492      13.249  15.396  22.207  1.00 11.13           C  
ANISOU  640  CB  ASP A 492      855   1630   1742   -182   -161    -27       C  
ATOM    641  CG  ASP A 492      13.018  16.886  22.360  1.00 12.30           C  
ANISOU  641  CG  ASP A 492     1047   1731   1894   -246   -178    -52       C  
ATOM    642  OD1 ASP A 492      13.183  17.646  21.389  1.00 14.95           O  
ANISOU  642  OD1 ASP A 492     1393   2035   2251   -298   -149    -46       O  
ATOM    643  OD2 ASP A 492      12.663  17.290  23.493  1.00 14.23           O  
ANISOU  643  OD2 ASP A 492     1321   1969   2115   -242   -220    -78       O  
ATOM    644  N   HIS A 493      13.609  12.677  19.914  1.00 11.09           N  
ANISOU  644  N   HIS A 493      798   1661   1756    -84    -50     39       N  
ATOM    645  CA  HIS A 493      14.049  11.279  19.865  1.00 11.18           C  
ANISOU  645  CA  HIS A 493      769   1708   1770    -21    -37     54       C  
ATOM    646  C   HIS A 493      13.976  10.593  21.240  1.00 11.15           C  
ANISOU  646  C   HIS A 493      759   1731   1747     31    -86     52       C  
ATOM    647  O   HIS A 493      14.874   9.830  21.618  1.00 12.15           O  
ANISOU  647  O   HIS A 493      824   1906   1885     68   -100     57       O  
ATOM    648  CB  HIS A 493      15.462  11.178  19.266  1.00 11.46           C  
ANISOU  648  CB  HIS A 493      719   1794   1841    -37    -10     55       C  
ATOM    649  CG  HIS A 493      15.506  11.420  17.791  1.00 12.96           C  
ANISOU  649  CG  HIS A 493      924   1961   2039    -69     55     65       C  
ATOM    650  ND1 HIS A 493      15.868  10.440  16.892  1.00 16.11           N  
ANISOU  650  ND1 HIS A 493     1303   2374   2443    -31    107     78       N  
ATOM    651  CD2 HIS A 493      15.225  12.520  17.056  1.00 13.32           C  
ANISOU  651  CD2 HIS A 493     1009   1968   2083   -134     76     65       C  
ATOM    652  CE1 HIS A 493      15.825  10.933  15.667  1.00 15.31           C  
ANISOU  652  CE1 HIS A 493     1230   2249   2340    -73    158     85       C  
ATOM    653  NE2 HIS A 493      15.441  12.194  15.738  1.00 14.09           N  
ANISOU  653  NE2 HIS A 493     1111   2062   2182   -136    140     80       N  
ATOM    654  N   ARG A 494      12.907  10.893  21.980  1.00 11.24           N  
ANISOU  654  N   ARG A 494      833   1709   1729     34   -112     45       N  
ATOM    655  CA  ARG A 494      12.608  10.197  23.227  1.00 11.29           C  
ANISOU  655  CA  ARG A 494      853   1730   1706     84   -149     48       C  
ATOM    656  C   ARG A 494      11.813   8.927  22.942  1.00 11.24           C  
ANISOU  656  C   ARG A 494      885   1700   1685    141   -120     73       C  
ATOM    657  O   ARG A 494      11.794   8.004  23.757  1.00 13.30           O  
ANISOU  657  O   ARG A 494     1150   1977   1927    191   -139     86       O  
ATOM    658  CB  ARG A 494      11.815  11.092  24.190  1.00 11.69           C  
ANISOU  658  CB  ARG A 494      955   1758   1728     61   -182     27       C  
ATOM    659  CG  ARG A 494      12.476  12.416  24.522  1.00 14.39           C  
ANISOU  659  CG  ARG A 494     1275   2111   2081     -2   -214     -3       C  
ATOM    660  CD  ARG A 494      13.644  12.213  25.447  1.00 16.98           C  
ANISOU  660  CD  ARG A 494     1542   2502   2408      3   -265    -12       C  
ATOM    661  NE  ARG A 494      14.229  13.478  25.897  1.00 19.43           N  
ANISOU  661  NE  ARG A 494     1835   2821   2726    -63   -304    -46       N  
ATOM    662  CZ  ARG A 494      15.340  13.564  26.622  1.00 21.06           C  
ANISOU  662  CZ  ARG A 494     1980   3084   2937    -77   -357    -61       C  
ATOM    663  NH1 ARG A 494      15.986  12.464  26.982  1.00 22.63           N  
ANISOU  663  NH1 ARG A 494     2128   3336   3135    -22   -378    -41       N  
ATOM    664  NH2 ARG A 494      15.801  14.751  26.997  1.00 24.35           N  
ANISOU  664  NH2 ARG A 494     2388   3502   3361   -146   -393    -95       N  
ATOM    665  N   ALA A 495      11.142   8.896  21.789  1.00 10.14           N  
ANISOU  665  N   ALA A 495      780   1520   1554    131    -75     81       N  
ATOM    666  CA  ALA A 495      10.358   7.747  21.368  1.00  9.36           C  
ANISOU  666  CA  ALA A 495      720   1393   1445    175    -47    101       C  
ATOM    667  C   ALA A 495      10.646   7.446  19.916  1.00  9.41           C  
ANISOU  667  C   ALA A 495      719   1388   1470    170     -1    108       C  
ATOM    668  O   ALA A 495      10.955   8.350  19.147  1.00  9.65           O  
ANISOU  668  O   ALA A 495      738   1415   1513    123     15    100       O  
ATOM    669  CB  ALA A 495       8.879   8.024  21.543  1.00  9.25           C  
ANISOU  669  CB  ALA A 495      769   1334   1411    167    -46    100       C  
ATOM    670  N   ASP A 496      10.509   6.173  19.553  1.00  9.01           N  
ANISOU  670  N   ASP A 496      682   1326   1415    216     23    123       N  
ATOM    671  CA  ASP A 496      10.656   5.737  18.167  1.00  9.07           C  
ANISOU  671  CA  ASP A 496      697   1317   1431    218     70    127       C  
ATOM    672  C   ASP A 496       9.389   5.948  17.363  1.00  8.40           C  
ANISOU  672  C   ASP A 496      678   1181   1331    194     85    128       C  
ATOM    673  O   ASP A 496       9.445   6.302  16.185  1.00  9.23           O  
ANISOU  673  O   ASP A 496      796   1273   1437    167    114    126       O  
ATOM    674  CB  ASP A 496      11.039   4.268  18.128  1.00  8.95           C  
ANISOU  674  CB  ASP A 496      677   1306   1418    281     86    138       C  
ATOM    675  CG  ASP A 496      12.405   4.024  18.723  1.00 10.43           C  
ANISOU  675  CG  ASP A 496      790   1547   1625    312     72    138       C  
ATOM    676  OD1 ASP A 496      13.400   4.420  18.068  1.00 12.89           O  
ANISOU  676  OD1 ASP A 496     1048   1891   1960    294     96    130       O  
ATOM    677  OD2 ASP A 496      12.482   3.457  19.831  1.00  9.20           O  
ANISOU  677  OD2 ASP A 496      629   1405   1463    352     37    148       O  
ATOM    678  N   LEU A 497       8.246   5.711  18.004  1.00  7.75           N  
ANISOU  678  N   LEU A 497      635   1073   1235    204     65    133       N  
ATOM    679  CA  LEU A 497       6.937   5.791  17.348  1.00  7.59           C  
ANISOU  679  CA  LEU A 497      670   1008   1206    187     72    135       C  
ATOM    680  C   LEU A 497       5.958   6.446  18.290  1.00  6.92           C  
ANISOU  680  C   LEU A 497      601    912   1115    176     43    131       C  
ATOM    681  O   LEU A 497       6.048   6.259  19.497  1.00  7.45           O  
ANISOU  681  O   LEU A 497      656    998   1175    195     24    132       O  
ATOM    682  CB  LEU A 497       6.366   4.391  17.052  1.00  8.52           C  
ANISOU  682  CB  LEU A 497      823   1100   1316    221     88    145       C  
ATOM    683  CG  LEU A 497       7.166   3.347  16.275  0.50  7.32           C  
ANISOU  683  CG  LEU A 497      668    949   1166    250    120    147       C  
ATOM    684  CD1 LEU A 497       6.355   2.058  16.229  0.50  7.04           C  
ANISOU  684  CD1 LEU A 497      678    876   1122    277    127    155       C  
ATOM    685  CD2 LEU A 497       7.485   3.814  14.874  0.50  7.95           C  
ANISOU  685  CD2 LEU A 497      755   1023   1242    222    149    139       C  
ATOM    686  N   ALA A 498       5.012   7.198  17.736  1.00  6.29           N  
ANISOU  686  N   ALA A 498      551    802   1036    148     40    127       N  
ATOM    687  CA  ALA A 498       3.818   7.604  18.476  1.00  6.21           C  
ANISOU  687  CA  ALA A 498      561    776   1024    146     22    124       C  
ATOM    688  C   ALA A 498       2.631   6.872  17.863  1.00  6.30           C  
ANISOU  688  C   ALA A 498      603    755   1034    152     30    133       C  
ATOM    689  O   ALA A 498       2.321   7.082  16.685  1.00  6.95           O  
ANISOU  689  O   ALA A 498      706    817   1119    135     34    134       O  
ATOM    690  CB  ALA A 498       3.613   9.115  18.412  1.00  6.33           C  
ANISOU  690  CB  ALA A 498      581    779   1045    114      6    111       C  
ATOM    691  N   VAL A 499       2.011   5.980  18.635  1.00  6.22           N  
ANISOU  691  N   VAL A 499      599    743   1020    174     32    140       N  
ATOM    692  CA  VAL A 499       0.848   5.216  18.155  1.00  6.57           C  
ANISOU  692  CA  VAL A 499      669    759   1069    174     38    148       C  
ATOM    693  C   VAL A 499      -0.329   5.605  19.039  1.00  6.91           C  
ANISOU  693  C   VAL A 499      710    799   1118    172     31    145       C  
ATOM    694  O   VAL A 499      -0.433   5.191  20.203  1.00  7.72           O  
ANISOU  694  O   VAL A 499      809    915   1211    188     36    150       O  
ATOM    695  CB  VAL A 499       1.079   3.681  18.143  1.00  7.10           C  
ANISOU  695  CB  VAL A 499      749    818   1130    196     55    160       C  
ATOM    696  CG1 VAL A 499      -0.120   2.991  17.494  1.00  6.39           C  
ANISOU  696  CG1 VAL A 499      687    695   1047    182     58    164       C  
ATOM    697  CG2 VAL A 499       2.356   3.358  17.381  1.00  8.01           C  
ANISOU  697  CG2 VAL A 499      860    942   1241    207     68    159       C  
ATOM    698  N   ALA A 500      -1.181   6.441  18.460  1.00  6.50           N  
ANISOU  698  N   ALA A 500      661    730   1079    155     19    139       N  
ATOM    699  CA  ALA A 500      -2.219   7.171  19.172  1.00  6.72           C  
ANISOU  699  CA  ALA A 500      680    757   1118    156     12    131       C  
ATOM    700  C   ALA A 500      -3.115   7.749  18.088  1.00  6.09           C  
ANISOU  700  C   ALA A 500      606    652   1056    142     -5    129       C  
ATOM    701  O   ALA A 500      -2.757   7.714  16.909  1.00  6.20           O  
ANISOU  701  O   ALA A 500      636    654   1066    129    -13    133       O  
ATOM    702  CB  ALA A 500      -1.591   8.300  19.975  1.00  7.48           C  
ANISOU  702  CB  ALA A 500      769    868   1206    158      5    116       C  
ATOM    703  N   PRO A 501      -4.289   8.276  18.470  1.00  6.14           N  
ANISOU  703  N   PRO A 501      599    653   1081    147    -11    123       N  
ATOM    704  CA  PRO A 501      -5.087   9.029  17.499  1.00  6.01           C  
ANISOU  704  CA  PRO A 501      585    615   1084    142    -36    122       C  
ATOM    705  C   PRO A 501      -4.457  10.414  17.282  1.00  5.89           C  
ANISOU  705  C   PRO A 501      584    588   1065    140    -50    114       C  
ATOM    706  O   PRO A 501      -4.953  11.428  17.781  1.00  5.62           O  
ANISOU  706  O   PRO A 501      545    545   1046    152    -57    102       O  
ATOM    707  CB  PRO A 501      -6.473   9.083  18.163  1.00  6.28           C  
ANISOU  707  CB  PRO A 501      590    652   1144    155    -32    117       C  
ATOM    708  CG  PRO A 501      -6.171   9.059  19.622  1.00  6.63           C  
ANISOU  708  CG  PRO A 501      627    718   1175    168     -4    108       C  
ATOM    709  CD  PRO A 501      -4.982   8.139  19.766  1.00  6.94           C  
ANISOU  709  CD  PRO A 501      682    768   1186    162      8    118       C  
ATOM    710  N   LEU A 502      -3.333  10.405  16.558  1.00  6.16           N  
ANISOU  710  N   LEU A 502      638    621   1081    123    -50    120       N  
ATOM    711  CA  LEU A 502      -2.498  11.588  16.364  1.00  5.77           C  
ANISOU  711  CA  LEU A 502      604    562   1027    110    -56    115       C  
ATOM    712  C   LEU A 502      -2.782  12.167  14.983  1.00  6.02           C  
ANISOU  712  C   LEU A 502      666    564   1059     96    -77    127       C  
ATOM    713  O   LEU A 502      -2.485  11.555  13.956  1.00  6.67           O  
ANISOU  713  O   LEU A 502      765    644   1124     83    -75    139       O  
ATOM    714  CB  LEU A 502      -1.021  11.197  16.496  1.00  6.42           C  
ANISOU  714  CB  LEU A 502      681    667   1090     97    -37    115       C  
ATOM    715  CG  LEU A 502       0.018  12.324  16.474  1.00  6.96           C  
ANISOU  715  CG  LEU A 502      755    732   1156     74    -39    109       C  
ATOM    716  CD1 LEU A 502      -0.041  13.196  17.732  1.00  8.16           C  
ANISOU  716  CD1 LEU A 502      899    885   1315     80    -48     88       C  
ATOM    717  CD2 LEU A 502       1.429  11.740  16.284  1.00  7.06           C  
ANISOU  717  CD2 LEU A 502      753    774   1157     62    -20    112       C  
ATOM    718  N   THR A 503      -3.387  13.341  14.968  1.00  5.01           N  
ANISOU  718  N   THR A 503      548    409    945    103    -98    125       N  
ATOM    719  CA  THR A 503      -3.893  13.940  13.750  1.00  5.23           C  
ANISOU  719  CA  THR A 503      609    405    974     99   -126    140       C  
ATOM    720  C   THR A 503      -2.785  14.456  12.858  1.00  5.44           C  
ANISOU  720  C   THR A 503      672    418    976     67   -120    152       C  
ATOM    721  O   THR A 503      -1.892  15.193  13.309  1.00  5.63           O  
ANISOU  721  O   THR A 503      701    439   1001     51   -107    145       O  
ATOM    722  CB  THR A 503      -4.871  15.049  14.128  1.00  5.33           C  
ANISOU  722  CB  THR A 503      620    390   1014    124   -150    133       C  
ATOM    723  OG1 THR A 503      -5.877  14.471  14.971  1.00  6.12           O  
ANISOU  723  OG1 THR A 503      678    510   1136    151   -145    122       O  
ATOM    724  CG2 THR A 503      -5.513  15.715  12.897  1.00  5.88           C  
ANISOU  724  CG2 THR A 503      725    425   1086    128   -188    154       C  
ATOM    725  N   ILE A 504      -2.849  14.055  11.592  1.00  6.00           N  
ANISOU  725  N   ILE A 504      772    481   1025     55   -128    170       N  
ATOM    726  CA  ILE A 504      -1.907  14.489  10.572  1.00  6.05           C  
ANISOU  726  CA  ILE A 504      821    475   1003     23   -117    186       C  
ATOM    727  C   ILE A 504      -2.256  15.904  10.129  1.00  6.79           C  
ANISOU  727  C   ILE A 504      955    523   1100     20   -144    200       C  
ATOM    728  O   ILE A 504      -3.328  16.147   9.571  1.00  7.80           O  
ANISOU  728  O   ILE A 504     1103    628   1231     39   -183    212       O  
ATOM    729  CB  ILE A 504      -1.951  13.550   9.359  1.00  6.14           C  
ANISOU  729  CB  ILE A 504      859    492    981     15   -116    198       C  
ATOM    730  CG1 ILE A 504      -1.570  12.123   9.759  1.00  6.27           C  
ANISOU  730  CG1 ILE A 504      843    544    996     21    -87    184       C  
ATOM    731  CG2 ILE A 504      -1.037  14.085   8.252  1.00  7.95           C  
ANISOU  731  CG2 ILE A 504     1138    708   1175    -18    -98    216       C  
ATOM    732  CD1 ILE A 504      -1.975  11.095   8.725  1.00  7.71           C  
ANISOU  732  CD1 ILE A 504     1053    724   1151     19    -94    188       C  
ATOM    733  N   THR A 505      -1.346  16.839  10.397  1.00  6.61           N  
ANISOU  733  N   THR A 505      945    487   1080     -5   -127    199       N  
ATOM    734  CA  THR A 505      -1.548  18.238  10.049  1.00  7.67           C  
ANISOU  734  CA  THR A 505     1126    569   1218    -12   -149    213       C  
ATOM    735  C   THR A 505      -0.308  18.786   9.351  1.00  7.93           C  
ANISOU  735  C   THR A 505     1196    590   1226    -63   -120    230       C  
ATOM    736  O   THR A 505       0.801  18.264   9.537  1.00  8.40           O  
ANISOU  736  O   THR A 505     1226    686   1279    -91    -81    221       O  
ATOM    737  CB  THR A 505      -1.838  19.129  11.277  1.00  8.22           C  
ANISOU  737  CB  THR A 505     1180    618   1324      6   -159    190       C  
ATOM    738  OG1 THR A 505      -0.660  19.227  12.089  1.00  8.62           O  
ANISOU  738  OG1 THR A 505     1207    690   1377    -24   -128    171       O  
ATOM    739  CG2 THR A 505      -3.000  18.574  12.118  1.00  8.28           C  
ANISOU  739  CG2 THR A 505     1143    645   1357     55   -175    171       C  
ATOM    740  N   TYR A 506      -0.510  19.837   8.561  1.00  8.81           N  
ANISOU  740  N   TYR A 506     1371    650   1328    -75   -139    255       N  
ATOM    741  CA  TYR A 506       0.571  20.551   7.896  1.00  9.68           C  
ANISOU  741  CA  TYR A 506     1524    738   1415   -130   -110    276       C  
ATOM    742  C   TYR A 506       1.666  20.983   8.872  1.00 10.00           C  
ANISOU  742  C   TYR A 506     1529    791   1481   -166    -79    253       C  
ATOM    743  O   TYR A 506       2.846  20.714   8.646  1.00 10.01           O  
ANISOU  743  O   TYR A 506     1512    822   1470   -209    -36    254       O  
ATOM    744  CB  TYR A 506      -0.012  21.748   7.119  1.00 10.95           C  
ANISOU  744  CB  TYR A 506     1764    830   1567   -129   -143    308       C  
ATOM    745  CG  TYR A 506       0.974  22.831   6.731  1.00 11.70           C  
ANISOU  745  CG  TYR A 506     1909    884   1651   -188   -116    328       C  
ATOM    746  CD1 TYR A 506       1.739  22.731   5.565  1.00 12.90           C  
ANISOU  746  CD1 TYR A 506     2104   1041   1758   -235    -81    359       C  
ATOM    747  CD2 TYR A 506       1.121  23.971   7.513  1.00 13.91           C  
ANISOU  747  CD2 TYR A 506     2201   1119   1965   -201   -124    316       C  
ATOM    748  CE1 TYR A 506       2.629  23.745   5.199  1.00 13.67           C  
ANISOU  748  CE1 TYR A 506     2248   1100   1847   -296    -51    380       C  
ATOM    749  CE2 TYR A 506       2.006  24.974   7.163  1.00 13.85           C  
ANISOU  749  CE2 TYR A 506     2242   1069   1952   -262    -99    335       C  
ATOM    750  CZ  TYR A 506       2.764  24.853   6.010  1.00 14.96           C  
ANISOU  750  CZ  TYR A 506     2419   1217   2050   -312    -61    369       C  
ATOM    751  OH  TYR A 506       3.648  25.855   5.665  1.00 16.79           O  
ANISOU  751  OH  TYR A 506     2697   1406   2277   -381    -31    390       O  
ATOM    752  N   VAL A 507       1.272  21.622   9.972  1.00 10.02           N  
ANISOU  752  N   VAL A 507     1518    772   1518   -146   -101    229       N  
ATOM    753  CA  VAL A 507       2.268  22.138  10.928  1.00 10.31           C  
ANISOU  753  CA  VAL A 507     1527    814   1575   -184    -82    204       C  
ATOM    754  C   VAL A 507       3.094  21.020  11.571  1.00  9.60           C  
ANISOU  754  C   VAL A 507     1363    798   1485   -190    -55    181       C  
ATOM    755  O   VAL A 507       4.299  21.157  11.769  1.00 10.22           O  
ANISOU  755  O   VAL A 507     1415    899   1568   -237    -29    174       O  
ATOM    756  CB  VAL A 507       1.651  23.113  11.980  1.00 10.46           C  
ANISOU  756  CB  VAL A 507     1559    790   1625   -161   -112    178       C  
ATOM    757  CG1 VAL A 507       0.568  22.453  12.846  1.00 10.64           C  
ANISOU  757  CG1 VAL A 507     1543    838   1663    -95   -132    154       C  
ATOM    758  CG2 VAL A 507       2.726  23.766  12.827  0.50 10.44           C  
ANISOU  758  CG2 VAL A 507     1543    786   1638   -210    -99    152       C  
ATOM    759  N   ARG A 508       2.455  19.891  11.868  1.00  8.41           N  
ANISOU  759  N   ARG A 508     1178    686   1333   -142    -61    173       N  
ATOM    760  CA  ARG A 508       3.180  18.767  12.441  1.00  7.82           C  
ANISOU  760  CA  ARG A 508     1039    674   1257   -139    -38    156       C  
ATOM    761  C   ARG A 508       4.038  18.030  11.426  1.00  8.11           C  
ANISOU  761  C   ARG A 508     1070    742   1271   -163     -1    175       C  
ATOM    762  O   ARG A 508       5.122  17.569  11.760  1.00  8.10           O  
ANISOU  762  O   ARG A 508     1020    784   1274   -180     25    164       O  
ATOM    763  CB  ARG A 508       2.225  17.777  13.101  1.00  7.30           C  
ANISOU  763  CB  ARG A 508      945    632   1195    -85    -53    144       C  
ATOM    764  CG  ARG A 508       1.592  18.317  14.354  1.00  6.62           C  
ANISOU  764  CG  ARG A 508      851    534   1130    -60    -76    119       C  
ATOM    765  CD  ARG A 508       0.476  17.380  14.784  1.00  6.99           C  
ANISOU  765  CD  ARG A 508      876    600   1181    -10    -85    114       C  
ATOM    766  NE  ARG A 508       0.024  17.673  16.143  1.00  6.40           N  
ANISOU  766  NE  ARG A 508      785    527   1121     14    -93     86       N  
ATOM    767  CZ  ARG A 508      -0.972  17.031  16.755  1.00  5.41           C  
ANISOU  767  CZ  ARG A 508      639    417   1001     55    -96     79       C  
ATOM    768  NH1 ARG A 508      -1.639  16.053  16.136  1.00  5.02           N  
ANISOU  768  NH1 ARG A 508      579    379    949     71    -95     96       N  
ATOM    769  NH2 ARG A 508      -1.285  17.343  18.004  1.00  6.46           N  
ANISOU  769  NH2 ARG A 508      761    553   1139     74    -96     53       N  
ATOM    770  N   GLU A 509       3.528  17.875  10.205  1.00  8.25           N  
ANISOU  770  N   GLU A 509     1133    738   1262   -159     -1    200       N  
ATOM    771  CA  GLU A 509       4.261  17.145   9.183  1.00  7.75           C  
ANISOU  771  CA  GLU A 509     1073    702   1171   -177     39    214       C  
ATOM    772  C   GLU A 509       5.606  17.818   8.857  1.00  8.25           C  
ANISOU  772  C   GLU A 509     1132    770   1233   -236     80    222       C  
ATOM    773  O   GLU A 509       6.533  17.163   8.398  1.00  8.10           O  
ANISOU  773  O   GLU A 509     1086    789   1201   -250    125    223       O  
ATOM    774  CB  GLU A 509       3.385  16.972   7.936  1.00  7.97           C  
ANISOU  774  CB  GLU A 509     1164    702   1164   -164     25    238       C  
ATOM    775  CG  GLU A 509       3.980  16.088   6.838  1.00  9.52           C  
ANISOU  775  CG  GLU A 509     1374    923   1320   -175     67    248       C  
ATOM    776  CD  GLU A 509       4.084  14.633   7.253  1.00  9.78           C  
ANISOU  776  CD  GLU A 509     1357   1001   1357   -141     81    226       C  
ATOM    777  OE1 GLU A 509       3.170  13.860   6.906  1.00 10.81           O  
ANISOU  777  OE1 GLU A 509     1508   1126   1473   -112     58    225       O  
ATOM    778  OE2 GLU A 509       5.061  14.246   7.928  1.00  9.08           O  
ANISOU  778  OE2 GLU A 509     1211    951   1289   -144    111    211       O  
ATOM    779  N   LYS A 510       5.706  19.122   9.109  1.00  8.86           N  
ANISOU  779  N   LYS A 510     1233    807   1326   -270     67    225       N  
ATOM    780  CA  LYS A 510       6.980  19.831   8.933  1.00  9.75           C  
ANISOU  780  CA  LYS A 510     1336    924   1446   -336    104    230       C  
ATOM    781  C   LYS A 510       8.043  19.448   9.959  1.00 10.01           C  
ANISOU  781  C   LYS A 510     1281   1013   1508   -348    118    201       C  
ATOM    782  O   LYS A 510       9.238  19.615   9.699  1.00 11.21           O  
ANISOU  782  O   LYS A 510     1401   1192   1668   -398    159    204       O  
ATOM    783  CB  LYS A 510       6.758  21.340   8.941  1.00 10.36           C  
ANISOU  783  CB  LYS A 510     1471    932   1533   -372     82    241       C  
ATOM    784  CG  LYS A 510       6.062  21.827   7.681  1.00 11.90           C  
ANISOU  784  CG  LYS A 510     1756   1073   1693   -373     76    280       C  
ATOM    785  CD  LYS A 510       6.185  23.334   7.511  1.00 16.38           C  
ANISOU  785  CD  LYS A 510     2385   1569   2268   -422     69    298       C  
ATOM    786  CE  LYS A 510       5.216  24.104   8.385  1.00 18.73           C  
ANISOU  786  CE  LYS A 510     2706   1815   2595   -386     14    281       C  
ATOM    787  NZ  LYS A 510       5.321  25.577   8.068  1.00 19.89           N  
ANISOU  787  NZ  LYS A 510     2930   1881   2747   -432      8    303       N  
ATOM    788  N   VAL A 511       7.616  18.926  11.113  1.00  9.33           N  
ANISOU  788  N   VAL A 511     1156    949   1439   -303     86    175       N  
ATOM    789  CA  VAL A 511       8.547  18.647  12.218  1.00  9.68           C  
ANISOU  789  CA  VAL A 511     1124   1044   1509   -310     86    148       C  
ATOM    790  C   VAL A 511       8.728  17.164  12.595  1.00  8.65           C  
ANISOU  790  C   VAL A 511      937    974   1377   -259     94    138       C  
ATOM    791  O   VAL A 511       9.701  16.811  13.274  1.00  9.60           O  
ANISOU  791  O   VAL A 511      990   1144   1515   -264     99    123       O  
ATOM    792  CB  VAL A 511       8.242  19.517  13.481  1.00  9.44           C  
ANISOU  792  CB  VAL A 511     1096    990   1500   -314     41    121       C  
ATOM    793  CG1 VAL A 511       8.420  21.010  13.158  1.00 11.16           C  
ANISOU  793  CG1 VAL A 511     1364   1150   1728   -375     39    128       C  
ATOM    794  CG2 VAL A 511       6.846  19.213  14.050  1.00  9.70           C  
ANISOU  794  CG2 VAL A 511     1155   1003   1527   -251      7    113       C  
ATOM    795  N   ILE A 512       7.793  16.305  12.173  1.00  8.12           N  
ANISOU  795  N   ILE A 512      898    899   1289   -211     92    148       N  
ATOM    796  CA  ILE A 512       7.910  14.840  12.365  1.00  8.04           C  
ANISOU  796  CA  ILE A 512      848    933   1274   -164    104    142       C  
ATOM    797  C   ILE A 512       7.578  14.150  11.044  1.00  8.41           C  
ANISOU  797  C   ILE A 512      935    970   1292   -151    132    160       C  
ATOM    798  O   ILE A 512       7.067  14.801  10.130  1.00  8.03           O  
ANISOU  798  O   ILE A 512      946    881   1224   -173    131    178       O  
ATOM    799  CB  ILE A 512       6.991  14.273  13.503  1.00  7.08           C  
ANISOU  799  CB  ILE A 512      719    814   1158   -114     67    128       C  
ATOM    800  CG1 ILE A 512       5.500  14.528  13.199  1.00  7.26           C  
ANISOU  800  CG1 ILE A 512      799    789   1171    -95     42    136       C  
ATOM    801  CG2 ILE A 512       7.412  14.839  14.864  1.00  7.82           C  
ANISOU  801  CG2 ILE A 512      777    925   1271   -123     40    106       C  
ATOM    802  CD1 ILE A 512       4.543  13.778  14.165  1.00  6.96           C  
ANISOU  802  CD1 ILE A 512      750    758   1137    -47     18    125       C  
ATOM    803  N   ASP A 513       7.868  12.856  10.934  1.00  8.65           N  
ANISOU  803  N   ASP A 513      938   1032   1315   -116    154    157       N  
ATOM    804  CA  ASP A 513       7.471  12.084   9.755  1.00  9.33           C  
ANISOU  804  CA  ASP A 513     1069   1106   1369   -101    177    167       C  
ATOM    805  C   ASP A 513       6.256  11.228  10.082  1.00  8.56           C  
ANISOU  805  C   ASP A 513      992    993   1267    -56    144    163       C  
ATOM    806  O   ASP A 513       6.377  10.235  10.806  1.00  9.52           O  
ANISOU  806  O   ASP A 513     1079   1139   1401    -21    144    152       O  
ATOM    807  CB  ASP A 513       8.599  11.148   9.290  1.00  9.50           C  
ANISOU  807  CB  ASP A 513     1056   1168   1386    -90    230    163       C  
ATOM    808  CG  ASP A 513       9.609  11.822   8.360  1.00 12.59           C  
ANISOU  808  CG  ASP A 513     1447   1569   1767   -138    280    173       C  
ATOM    809  OD1 ASP A 513       9.380  12.949   7.876  1.00 14.40           O  
ANISOU  809  OD1 ASP A 513     1719   1766   1985   -182    275    188       O  
ATOM    810  OD2 ASP A 513      10.672  11.217   8.105  1.00 12.45           O  
ANISOU  810  OD2 ASP A 513     1385   1591   1753   -131    329    167       O  
ATOM    811  N   PHE A 514       5.095  11.580   9.542  1.00  7.84           N  
ANISOU  811  N   PHE A 514      955    862   1160    -59    116    172       N  
ATOM    812  CA  PHE A 514       3.908  10.754   9.745  1.00  7.11           C  
ANISOU  812  CA  PHE A 514      877    757   1066    -25     87    168       C  
ATOM    813  C   PHE A 514       3.814   9.594   8.764  1.00  6.91           C  
ANISOU  813  C   PHE A 514      883    731   1013    -11    107    168       C  
ATOM    814  O   PHE A 514       4.153   9.741   7.581  1.00  7.17           O  
ANISOU  814  O   PHE A 514      955    755   1013    -32    130    176       O  
ATOM    815  CB  PHE A 514       2.646  11.561   9.509  1.00  7.62           C  
ANISOU  815  CB  PHE A 514      982    784   1131    -29     44    177       C  
ATOM    816  CG  PHE A 514       2.171  12.351  10.672  1.00  6.40           C  
ANISOU  816  CG  PHE A 514      803    622   1007    -23     14    170       C  
ATOM    817  CD1 PHE A 514       1.500  11.720  11.738  1.00  6.04           C  
ANISOU  817  CD1 PHE A 514      727    588    981      9     -1    158       C  
ATOM    818  CD2 PHE A 514       2.265  13.745  10.651  1.00  7.25           C  
ANISOU  818  CD2 PHE A 514      929    705   1122    -47      3    176       C  
ATOM    819  CE1 PHE A 514       0.982  12.476  12.794  1.00  7.66           C  
ANISOU  819  CE1 PHE A 514      916    785   1209     17    -23    148       C  
ATOM    820  CE2 PHE A 514       1.748  14.492  11.705  1.00  8.04           C  
ANISOU  820  CE2 PHE A 514     1014    792   1248    -37    -23    165       C  
ATOM    821  CZ  PHE A 514       1.117  13.853  12.763  1.00  7.43           C  
ANISOU  821  CZ  PHE A 514      905    732   1187     -3    -35    150       C  
ATOM    822  N   SER A 515       3.301   8.454   9.232  1.00  6.93           N  
ANISOU  822  N   SER A 515      875    736   1022     20     98    159       N  
ATOM    823  CA  SER A 515       2.840   7.408   8.322  1.00  7.22           C  
ANISOU  823  CA  SER A 515      954    757   1032     29    103    155       C  
ATOM    824  C   SER A 515       1.632   7.909   7.543  1.00  7.40           C  
ANISOU  824  C   SER A 515     1025    749   1038     13     61    164       C  
ATOM    825  O   SER A 515       1.015   8.940   7.899  1.00  7.35           O  
ANISOU  825  O   SER A 515     1013    730   1048      5     27    173       O  
ATOM    826  CB  SER A 515       2.445   6.126   9.078  1.00  7.23           C  
ANISOU  826  CB  SER A 515      937    760   1049     61     98    145       C  
ATOM    827  OG  SER A 515       1.189   6.302   9.734  1.00  6.46           O  
ANISOU  827  OG  SER A 515      833    648    972     62     56    147       O  
ATOM    828  N   LYS A 516       1.259   7.177   6.507  1.00  6.82           N  
ANISOU  828  N   LYS A 516     1001    660    931     11     60    160       N  
ATOM    829  CA  LYS A 516      -0.057   7.390   5.913  1.00  7.10           C  
ANISOU  829  CA  LYS A 516     1074    670    955      1      7    166       C  
ATOM    830  C   LYS A 516      -1.169   7.088   6.923  1.00  6.75           C  
ANISOU  830  C   LYS A 516      990    622    952     16    -31    161       C  
ATOM    831  O   LYS A 516      -0.953   6.394   7.915  1.00  6.30           O  
ANISOU  831  O   LYS A 516      895    579    921     34    -12    152       O  
ATOM    832  CB  LYS A 516      -0.205   6.595   4.630  1.00  7.68           C  
ANISOU  832  CB  LYS A 516     1210    729    980     -7      9    159       C  
ATOM    833  CG  LYS A 516       0.602   7.258   3.520  1.00  8.90           C  
ANISOU  833  CG  LYS A 516     1413    882   1086    -28     38    170       C  
ATOM    834  CD  LYS A 516       0.327   6.694   2.170  1.00  8.63           C  
ANISOU  834  CD  LYS A 516     1455    832    993    -39     33    163       C  
ATOM    835  CE  LYS A 516       1.051   7.467   1.088  1.00  8.72           C  
ANISOU  835  CE  LYS A 516     1521    843    951    -62     64    180       C  
ATOM    836  NZ  LYS A 516       2.534   7.519   1.315  1.00  8.29           N  
ANISOU  836  NZ  LYS A 516     1433    815    902    -62    142    177       N  
ATOM    837  N   PRO A 517      -2.347   7.682   6.720  1.00  7.34           N  
ANISOU  837  N   PRO A 517     1073    681   1035     12    -82    169       N  
ATOM    838  CA  PRO A 517      -3.386   7.559   7.746  1.00  7.35           C  
ANISOU  838  CA  PRO A 517     1027    684   1080     25   -109    165       C  
ATOM    839  C   PRO A 517      -3.981   6.168   7.916  1.00  7.21           C  
ANISOU  839  C   PRO A 517     1003    666   1072     26   -112    152       C  
ATOM    840  O   PRO A 517      -4.118   5.429   6.937  1.00  8.19           O  
ANISOU  840  O   PRO A 517     1169    776   1166     13   -120    146       O  
ATOM    841  CB  PRO A 517      -4.461   8.544   7.264  1.00  8.51           C  
ANISOU  841  CB  PRO A 517     1186    815   1234     23   -164    177       C  
ATOM    842  CG  PRO A 517      -4.219   8.704   5.801  1.00  9.02           C  
ANISOU  842  CG  PRO A 517     1317    865   1247      5   -176    186       C  
ATOM    843  CD  PRO A 517      -2.746   8.563   5.602  1.00  8.44           C  
ANISOU  843  CD  PRO A 517     1261    800   1144     -4   -117    185       C  
ATOM    844  N   PHE A 518      -4.341   5.853   9.152  1.00  6.65           N  
ANISOU  844  N   PHE A 518      777    661   1087    163   -135    105       N  
ATOM    845  CA  PHE A 518      -5.060   4.614   9.461  1.00  6.66           C  
ANISOU  845  CA  PHE A 518      785    662   1082    154    -91    112       C  
ATOM    846  C   PHE A 518      -6.550   4.804   9.774  1.00  6.77           C  
ANISOU  846  C   PHE A 518      771    680   1120    143    -86     74       C  
ATOM    847  O   PHE A 518      -7.275   3.815   9.883  1.00  6.97           O  
ANISOU  847  O   PHE A 518      786    686   1177    126    -36     70       O  
ATOM    848  CB  PHE A 518      -4.381   3.799  10.579  1.00  7.67           C  
ANISOU  848  CB  PHE A 518      926    808   1182    181    -52    154       C  
ATOM    849  CG  PHE A 518      -4.231   4.540  11.895  1.00  6.01           C  
ANISOU  849  CG  PHE A 518      715    640    928    215    -84    143       C  
ATOM    850  CD1 PHE A 518      -3.019   5.127  12.233  1.00  6.54           C  
ANISOU  850  CD1 PHE A 518      769    731    985    233   -146    143       C  
ATOM    851  CD2 PHE A 518      -5.276   4.622  12.809  1.00  6.41           C  
ANISOU  851  CD2 PHE A 518      782    698    954    229    -48    128       C  
ATOM    852  CE1 PHE A 518      -2.854   5.784  13.451  1.00  7.13           C  
ANISOU  852  CE1 PHE A 518      856    845   1007    264   -196    113       C  
ATOM    853  CE2 PHE A 518      -5.121   5.292  14.019  1.00  6.60           C  
ANISOU  853  CE2 PHE A 518      838    755    914    269    -73    112       C  
ATOM    854  CZ  PHE A 518      -3.904   5.883  14.341  1.00  6.73           C  
ANISOU  854  CZ  PHE A 518      851    805    901    286   -160     97       C  
ATOM    855  N   MET A 519      -6.994   6.054   9.918  1.00  6.88           N  
ANISOU  855  N   MET A 519      766    709   1140    152   -123     48       N  
ATOM    856  CA  MET A 519      -8.389   6.348  10.238  1.00  7.16           C  
ANISOU  856  CA  MET A 519      760    741   1218    149   -109     20       C  
ATOM    857  C   MET A 519      -8.631   7.792   9.855  1.00  7.62           C  
ANISOU  857  C   MET A 519      806    804   1284    166   -157      1       C  
ATOM    858  O   MET A 519      -7.716   8.615   9.967  1.00  8.03           O  
ANISOU  858  O   MET A 519      884    859   1307    177   -173      5       O  
ATOM    859  CB  MET A 519      -8.658   6.135  11.735  1.00  7.19           C  
ANISOU  859  CB  MET A 519      778    748   1205    169    -38     31       C  
ATOM    860  CG  MET A 519     -10.133   6.191  12.129  1.00  8.44           C  
ANISOU  860  CG  MET A 519      888    879   1438    167     19     13       C  
ATOM    861  SD  MET A 519     -10.462   5.881  13.874  1.00 10.69           S  
ANISOU  861  SD  MET A 519     1228   1145   1690    211    146     40       S  
ATOM    862  CE  MET A 519      -9.848   4.208  14.029  1.00 11.27           C  
ANISOU  862  CE  MET A 519     1339   1203   1739    214    211     86       C  
ATOM    863  N   THR A 520      -9.845   8.102   9.407  1.00  8.44           N  
ANISOU  863  N   THR A 520      861    902   1444    169   -177    -21       N  
ATOM    864  CA  THR A 520     -10.225   9.461   9.050  1.00  9.66           C  
ANISOU  864  CA  THR A 520     1002   1056   1611    200   -208    -27       C  
ATOM    865  C   THR A 520     -11.162  10.056  10.092  1.00  9.20           C  
ANISOU  865  C   THR A 520      906    989   1599    212   -156    -37       C  
ATOM    866  O   THR A 520     -11.841   9.339  10.835  1.00  9.64           O  
ANISOU  866  O   THR A 520      931   1033   1697    199    -98    -40       O  
ATOM    867  CB  THR A 520     -10.946   9.503   7.692  1.00 11.08           C  
ANISOU  867  CB  THR A 520     1157   1238   1813    219   -284    -39       C  
ATOM    868  OG1 THR A 520     -12.137   8.720   7.775  1.00 15.21           O  
ANISOU  868  OG1 THR A 520     1600   1762   2419    197   -294    -70       O  
ATOM    869  CG2 THR A 520     -10.052   8.977   6.587  1.00 12.59           C  
ANISOU  869  CG2 THR A 520     1417   1425   1941    220   -320    -29       C  
ATOM    870  N   LEU A 521     -11.204  11.383  10.126  1.00  7.95           N  
ANISOU  870  N   LEU A 521      756    821   1442    242   -154    -37       N  
ATOM    871  CA  LEU A 521     -12.020  12.108  11.098  1.00  8.37           C  
ANISOU  871  CA  LEU A 521      792    854   1536    260    -88    -45       C  
ATOM    872  C   LEU A 521     -12.177  13.540  10.648  1.00  8.63           C  
ANISOU  872  C   LEU A 521      824    867   1588    298    -94    -40       C  
ATOM    873  O   LEU A 521     -11.488  13.998   9.738  1.00  8.53           O  
ANISOU  873  O   LEU A 521      841    853   1548    312   -136    -29       O  
ATOM    874  CB  LEU A 521     -11.380  12.060  12.499  1.00  8.55           C  
ANISOU  874  CB  LEU A 521      884    873   1492    252    -28    -58       C  
ATOM    875  CG  LEU A 521     -10.079  12.784  12.921  1.00  9.41           C  
ANISOU  875  CG  LEU A 521     1061    985   1528    247    -50    -83       C  
ATOM    876  CD1 LEU A 521      -8.881  12.288  12.095  1.00 11.13           C  
ANISOU  876  CD1 LEU A 521     1282   1222   1723    225   -115    -72       C  
ATOM    877  CD2 LEU A 521     -10.155  14.297  12.960  1.00 12.44           C  
ANISOU  877  CD2 LEU A 521     1456   1333   1936    262    -29   -108       C  
ATOM    878  N   GLY A 522     -13.083  14.247  11.307  1.00  6.35           N  
ANISOU  878  N   GLY A 522      868    686    860    254    -91      9       N  
ATOM    879  CA  GLY A 522     -13.167  15.691  11.182  1.00  6.98           C  
ANISOU  879  CA  GLY A 522      955    796    900    279    -79     50       C  
ATOM    880  C   GLY A 522     -13.623  16.254  12.507  1.00  6.85           C  
ANISOU  880  C   GLY A 522      895    781    926    264    -90     86       C  
ATOM    881  O   GLY A 522     -14.247  15.554  13.302  1.00  7.40           O  
ANISOU  881  O   GLY A 522      932    845   1035    238   -116     81       O  
ATOM    882  N   ILE A 523     -13.293  17.517  12.753  1.00  6.50           N  
ANISOU  882  N   ILE A 523      854    740    876    282    -65    123       N  
ATOM    883  CA  ILE A 523     -13.762  18.203  13.957  1.00  6.59           C  
ANISOU  883  CA  ILE A 523      834    755    916    275    -73    147       C  
ATOM    884  C   ILE A 523     -15.275  18.412  13.880  1.00  6.41           C  
ANISOU  884  C   ILE A 523      793    767    876    281   -112    148       C  
ATOM    885  O   ILE A 523     -15.813  18.786  12.833  1.00  7.32           O  
ANISOU  885  O   ILE A 523      926    907    949    304   -131    148       O  
ATOM    886  CB  ILE A 523     -13.067  19.566  14.117  1.00  6.05           C  
ANISOU  886  CB  ILE A 523      776    672    851    292    -40    176       C  
ATOM    887  CG1 ILE A 523     -11.568  19.375  14.393  1.00  6.85           C  
ANISOU  887  CG1 ILE A 523      875    737    989    281     -6    177       C  
ATOM    888  CG2 ILE A 523     -13.729  20.426  15.220  1.00  7.57           C  
ANISOU  888  CG2 ILE A 523      948    869   1061    294    -48    189       C  
ATOM    889  CD1 ILE A 523     -10.796  20.683  14.211  1.00  7.70           C  
ANISOU  889  CD1 ILE A 523      991    823   1110    293     30    203       C  
ATOM    890  N   SER A 524     -15.960  18.175  14.990  1.00  6.42           N  
ANISOU  890  N   SER A 524      757    773    911    263   -122    153       N  
ATOM    891  CA  SER A 524     -17.364  18.570  15.097  1.00  6.78           C  
ANISOU  891  CA  SER A 524      770    849    956    273   -147    161       C  
ATOM    892  C   SER A 524     -17.622  19.053  16.520  1.00  6.46           C  
ANISOU  892  C   SER A 524      705    808    942    271   -123    179       C  
ATOM    893  O   SER A 524     -16.673  19.364  17.241  1.00  6.77           O  
ANISOU  893  O   SER A 524      762    826    984    269    -97    184       O  
ATOM    894  CB  SER A 524     -18.292  17.429  14.656  1.00  7.98           C  
ANISOU  894  CB  SER A 524      894   1016   1123    249   -190    137       C  
ATOM    895  OG  SER A 524     -19.643  17.844  14.570  1.00  8.44           O  
ANISOU  895  OG  SER A 524      910   1108   1189    261   -220    145       O  
ATOM    896  N   ILE A 525     -18.894  19.162  16.909  1.00  7.09           N  
ANISOU  896  N   ILE A 525      743    914   1038    276   -132    187       N  
ATOM    897  CA  ILE A 525     -19.272  19.701  18.226  1.00  7.40           C  
ANISOU  897  CA  ILE A 525      764    959   1090    283    -99    201       C  
ATOM    898  C   ILE A 525     -20.006  18.645  19.038  1.00  7.51           C  
ANISOU  898  C   ILE A 525      734    985   1135    253    -93    210       C  
ATOM    899  O   ILE A 525     -20.913  18.006  18.527  1.00  7.80           O  
ANISOU  899  O   ILE A 525      730   1034   1199    239   -119    208       O  
ATOM    900  CB  ILE A 525     -20.188  20.943  18.059  1.00  8.14           C  
ANISOU  900  CB  ILE A 525      839   1068   1184    326    -96    211       C  
ATOM    901  CG1 ILE A 525     -19.482  22.013  17.222  1.00  8.65           C  
ANISOU  901  CG1 ILE A 525      948   1113   1227    356    -96    215       C  
ATOM    902  CG2 ILE A 525     -20.651  21.488  19.431  1.00  9.31           C  
ANISOU  902  CG2 ILE A 525      971   1222   1343    339    -53    216       C  
ATOM    903  CD1 ILE A 525     -20.422  23.045  16.623  1.00  9.96           C  
ANISOU  903  CD1 ILE A 525     1098   1291   1397    402   -108    234       C  
ATOM    904  N   LEU A 526     -19.601  18.481  20.297  1.00  7.15           N  
ANISOU  904  N   LEU A 526      699    934   1083    244    -60    221       N  
ATOM    905  CA  LEU A 526     -20.301  17.629  21.262  1.00  7.16           C  
ANISOU  905  CA  LEU A 526      665    948   1107    222    -36    245       C  
ATOM    906  C   LEU A 526     -21.055  18.509  22.244  1.00  7.99           C  
ANISOU  906  C   LEU A 526      756   1081   1199    251      8    255       C  
ATOM    907  O   LEU A 526     -20.471  19.400  22.865  1.00  8.46           O  
ANISOU  907  O   LEU A 526      855   1140   1220    275     27    244       O  
ATOM    908  CB  LEU A 526     -19.301  16.768  22.048  1.00  6.71           C  
ANISOU  908  CB  LEU A 526      636    872   1040    198    -27    260       C  
ATOM    909  CG  LEU A 526     -19.894  15.763  23.046  1.00  7.28           C  
ANISOU  909  CG  LEU A 526      681    951   1134    174      3    299       C  
ATOM    910  CD1 LEU A 526     -20.430  14.580  22.278  1.00 10.64           C  
ANISOU  910  CD1 LEU A 526     1066   1352   1624    137    -19    301       C  
ATOM    911  CD2 LEU A 526     -18.865  15.338  24.107  1.00  7.87           C  
ANISOU  911  CD2 LEU A 526      797   1018   1177    171     14    324       C  
ATOM    912  N   TYR A 527     -22.349  18.260  22.398  1.00  8.21           N  
ANISOU  912  N   TYR A 527      723   1132   1265    248     27    273       N  
ATOM    913  CA  TYR A 527     -23.111  18.937  23.440  1.00  9.21           C  
ANISOU  913  CA  TYR A 527      832   1286   1383    278     85    285       C  
ATOM    914  C   TYR A 527     -24.218  18.028  23.977  1.00 10.65           C  
ANISOU  914  C   TYR A 527      947   1487   1612    254    122    322       C  
ATOM    915  O   TYR A 527     -24.334  16.869  23.578  1.00 10.49           O  
ANISOU  915  O   TYR A 527      897   1451   1638    209     98    337       O  
ATOM    916  CB  TYR A 527     -23.624  20.325  22.966  1.00 10.09           C  
ANISOU  916  CB  TYR A 527      933   1403   1497    328     84    265       C  
ATOM    917  CG  TYR A 527     -24.174  21.181  24.101  1.00 10.79           C  
ANISOU  917  CG  TYR A 527     1021   1511   1568    368    152    263       C  
ATOM    918  CD1 TYR A 527     -23.375  21.502  25.200  1.00 12.21           C  
ANISOU  918  CD1 TYR A 527     1265   1689   1684    376    184    248       C  
ATOM    919  CD2 TYR A 527     -25.494  21.634  24.095  1.00 13.09           C  
ANISOU  919  CD2 TYR A 527     1245   1824   1906    400    184    274       C  
ATOM    920  CE1 TYR A 527     -23.878  22.249  26.273  1.00 12.35           C  
ANISOU  920  CE1 TYR A 527     1293   1727   1673    416    250    235       C  
ATOM    921  CE2 TYR A 527     -26.002  22.396  25.162  1.00 13.43           C  
ANISOU  921  CE2 TYR A 527     1289   1883   1932    443    258    267       C  
ATOM    922  CZ  TYR A 527     -25.183  22.700  26.241  1.00 13.63           C  
ANISOU  922  CZ  TYR A 527     1391   1907   1882    451    293    244       C  
ATOM    923  OH  TYR A 527     -25.662  23.446  27.298  1.00 15.03           O  
ANISOU  923  OH  TYR A 527     1580   2100   2029    496    368    226       O  
ATOM    924  N   ARG A 528     -24.991  18.535  24.931  1.00 11.61           N  
ANISOU  924  N   ARG A 528     1047   1638   1727    282    189    337       N  
ATOM    925  CA  ARG A 528     -26.205  17.848  25.348  1.00 13.78           C  
ANISOU  925  CA  ARG A 528     1242   1932   2063    264    237    378       C  
ATOM    926  C   ARG A 528     -27.314  18.121  24.336  1.00 14.69           C  
ANISOU  926  C   ARG A 528     1270   2054   2257    272    204    370       C  
ATOM    927  O   ARG A 528     -27.183  18.939  23.425  1.00 14.39           O  
ANISOU  927  O   ARG A 528     1244   2012   2213    300    152    338       O  
ATOM    928  CB  ARG A 528     -26.643  18.300  26.740  1.00 14.76           C  
ANISOU  928  CB  ARG A 528     1373   2090   2146    298    333    398       C  
ATOM    929  CG  ARG A 528     -25.619  18.058  27.827  1.00 16.12           C  
ANISOU  929  CG  ARG A 528     1633   2266   2226    296    358    408       C  
ATOM    930  CD  ARG A 528     -26.187  18.348  29.215  1.00 17.92           C  
ANISOU  930  CD  ARG A 528     1869   2536   2402    329    459    431       C  
ATOM    931  NE  ARG A 528     -26.964  19.593  29.316  1.00 21.63           N  
ANISOU  931  NE  ARG A 528     2318   3026   2876    386    504    397       N  
ATOM    932  CZ  ARG A 528     -26.449  20.797  29.559  1.00 22.47           C  
ANISOU  932  CZ  ARG A 528     2490   3130   2919    432    501    340       C  
ATOM    933  NH1 ARG A 528     -25.140  20.959  29.703  1.00 21.19           N  
ANISOU  933  NH1 ARG A 528     2415   2952   2686    424    449    309       N  
ATOM    934  NH2 ARG A 528     -27.253  21.853  29.650  1.00 24.28           N  
ANISOU  934  NH2 ARG A 528     2691   3367   3166    486    549    313       N  
ATOM    935  N   LYS A 529     -28.420  17.424  24.517  1.00 16.19           N  
ANISOU  935  N   LYS A 529     1369   2255   2526    246    234    404       N  
ATOM    936  CA  LYS A 529     -29.556  17.581  23.625  1.00 17.42           C  
ANISOU  936  CA  LYS A 529     1427   2423   2769    249    194    399       C  
ATOM    937  C   LYS A 529     -30.443  18.769  23.990  1.00 18.57           C  
ANISOU  937  C   LYS A 529     1527   2600   2929    314    248    403       C  
ATOM    938  O   LYS A 529     -30.322  19.330  25.087  1.00 18.96           O  
ANISOU  938  O   LYS A 529     1616   2662   2926    351    333    409       O  
ATOM    939  CB  LYS A 529     -30.352  16.291  23.630  1.00 18.22           C  
ANISOU  939  CB  LYS A 529     1438   2516   2970    186    198    431       C  
ATOM    940  CG  LYS A 529     -29.572  15.161  23.024  1.00 17.57           C  
ANISOU  940  CG  LYS A 529     1394   2392   2891    126    132    416       C  
ATOM    941  CD  LYS A 529     -30.125  13.861  23.442  1.00 18.40           C  
ANISOU  941  CD  LYS A 529     1433   2473   3084     63    163    456       C  
ATOM    942  CE  LYS A 529     -29.519  12.751  22.610  1.00 16.55           C  
ANISOU  942  CE  LYS A 529     1223   2187   2877      6     85    427       C  
ATOM    943  NZ  LYS A 529     -30.370  11.560  22.764  1.00 16.97           N  
ANISOU  943  NZ  LYS A 529     1184   2208   3054    -61    100    458       N  
ATOM    944  N   GLY A 600     -31.320  19.158  23.067  1.00 19.55           N  
ANISOU  944  N   GLY A 600     1570   2735   3123    332    196    396       N  
ATOM    945  CA  GLY A 600     -32.377  20.121  23.379  1.00 20.81           C  
ANISOU  945  CA  GLY A 600     1657   2921   3328    394    249    408       C  
ATOM    946  C   GLY A 600     -32.207  21.588  23.015  1.00 21.24           C  
ANISOU  946  C   GLY A 600     1753   2972   3346    471    234    383       C  
ATOM    947  O   GLY A 600     -33.124  22.384  23.249  1.00 22.84           O  
ANISOU  947  O   GLY A 600     1890   3190   3599    528    280    393       O  
ATOM    948  N   THR A 601     -31.053  21.966  22.459  1.00 20.65           N  
ANISOU  948  N   THR A 601     1781   2872   3194    475    178    354       N  
ATOM    949  CA  THR A 601     -30.855  23.356  22.017  1.00 20.67           C  
ANISOU  949  CA  THR A 601     1823   2859   3173    543    162    338       C  
ATOM    950  C   THR A 601     -31.145  23.506  20.523  1.00 20.47           C  
ANISOU  950  C   THR A 601     1763   2837   3178    553     55    343       C  
ATOM    951  O   THR A 601     -31.186  22.503  19.799  1.00 20.13           O  
ANISOU  951  O   THR A 601     1694   2805   3149    499    -16    343       O  
ATOM    952  CB  THR A 601     -29.422  23.898  22.312  1.00 20.32           C  
ANISOU  952  CB  THR A 601     1908   2779   3034    549    173    307       C  
ATOM    953  OG1 THR A 601     -28.500  23.395  21.343  1.00 20.07           O  
ANISOU  953  OG1 THR A 601     1927   2732   2966    508     92    299       O  
ATOM    954  CG2 THR A 601     -28.972  23.537  23.715  1.00 21.05           C  
ANISOU  954  CG2 THR A 601     2047   2875   3076    529    254    299       C  
ATOM    955  N   PRO A 652     -31.363  24.752  20.059  1.00 20.92           N  
ANISOU  955  N   PRO A 652     1823   2883   3243    623     43    349       N  
ATOM    956  CA  PRO A 652     -31.516  24.991  18.632  1.00 21.15           C  
ANISOU  956  CA  PRO A 652     1839   2919   3277    642    -61    362       C  
ATOM    957  C   PRO A 652     -30.185  25.193  17.914  1.00 20.06           C  
ANISOU  957  C   PRO A 652     1818   2753   3052    631   -103    349       C  
ATOM    958  O   PRO A 652     -30.183  25.522  16.727  1.00 20.68           O  
ANISOU  958  O   PRO A 652     1908   2837   3114    655   -179    364       O  
ATOM    959  CB  PRO A 652     -32.338  26.283  18.593  1.00 22.00           C  
ANISOU  959  CB  PRO A 652     1899   3022   3439    730    -41    386       C  
ATOM    960  CG  PRO A 652     -31.883  27.038  19.790  1.00 21.93           C  
ANISOU  960  CG  PRO A 652     1949   2976   3407    760     67    365       C  
ATOM    961  CD  PRO A 652     -31.536  25.997  20.838  1.00 21.33           C  
ANISOU  961  CD  PRO A 652     1890   2914   3302    694    124    344       C  
ATOM    962  N   ILE A 653     -29.072  25.007  18.625  1.00 18.71           N  
ANISOU  962  N   ILE A 653     1730   2554   2824    599    -54    324       N  
ATOM    963  CA  ILE A 653     -27.756  25.167  18.018  1.00 17.53           C  
ANISOU  963  CA  ILE A 653     1681   2375   2605    586    -82    313       C  
ATOM    964  C   ILE A 653     -27.537  24.026  17.036  1.00 17.40           C  
ANISOU  964  C   ILE A 653     1665   2380   2565    535   -159    307       C  
ATOM    965  O   ILE A 653     -27.636  22.852  17.399  1.00 17.09           O  
ANISOU  965  O   ILE A 653     1598   2354   2541    479   -159    294       O  
ATOM    966  CB  ILE A 653     -26.624  25.214  19.067  1.00 16.54           C  
ANISOU  966  CB  ILE A 653     1632   2218   2436    563    -19    286       C  
ATOM    967  CG1 ILE A 653     -26.872  26.368  20.050  1.00 17.12           C  
ANISOU  967  CG1 ILE A 653     1711   2267   2526    615     54    277       C  
ATOM    968  CG2 ILE A 653     -25.268  25.367  18.370  1.00 15.67           C  
ANISOU  968  CG2 ILE A 653     1607   2075   2270    547    -47    279       C  
ATOM    969  CD1 ILE A 653     -25.934  26.410  21.234  1.00 17.93           C  
ANISOU  969  CD1 ILE A 653     1881   2348   2583    594    110    243       C  
ATOM    970  N   ASP A 654     -27.255  24.384  15.793  1.00 16.90           N  
ANISOU  970  N   ASP A 654     1637   2318   2465    556   -220    318       N  
ATOM    971  CA  ASP A 654     -27.203  23.406  14.715  1.00 17.22           C  
ANISOU  971  CA  ASP A 654     1680   2385   2477    520   -299    305       C  
ATOM    972  C   ASP A 654     -25.895  23.430  13.948  1.00 15.65           C  
ANISOU  972  C   ASP A 654     1581   2166   2199    512   -310    297       C  
ATOM    973  O   ASP A 654     -25.701  22.629  13.035  1.00 15.68           O  
ANISOU  973  O   ASP A 654     1604   2188   2165    486   -367    277       O  
ATOM    974  CB  ASP A 654     -28.366  23.657  13.744  1.00 18.59           C  
ANISOU  974  CB  ASP A 654     1788   2600   2674    557   -380    326       C  
ATOM    975  CG  ASP A 654     -28.592  22.500  12.786  1.00 21.33           C  
ANISOU  975  CG  ASP A 654     2120   2981   3003    512   -471    296       C  
ATOM    976  OD1 ASP A 654     -28.585  21.339  13.247  1.00 23.70           O  
ANISOU  976  OD1 ASP A 654     2395   3276   3334    448   -464    263       O  
ATOM    977  OD2 ASP A 654     -28.782  22.758  11.574  1.00 24.93           O  
ANISOU  977  OD2 ASP A 654     2592   3467   3412    543   -551    305       O  
ATOM    978  N   SER A 655     -24.994  24.341  14.319  1.00 14.48           N  
ANISOU  978  N   SER A 655     1494   1977   2030    535   -252    309       N  
ATOM    979  CA  SER A 655     -23.739  24.532  13.586  1.00 12.92           C  
ANISOU  979  CA  SER A 655     1381   1756   1771    533   -249    312       C  
ATOM    980  C   SER A 655     -22.746  25.335  14.407  1.00 11.72           C  
ANISOU  980  C   SER A 655     1276   1551   1625    537   -178    312       C  
ATOM    981  O   SER A 655     -23.120  25.942  15.407  1.00 11.39           O  
ANISOU  981  O   SER A 655     1210   1491   1625    554   -137    310       O  
ATOM    982  CB  SER A 655     -24.000  25.293  12.276  1.00 13.65           C  
ANISOU  982  CB  SER A 655     1496   1864   1825    586   -294    351       C  
ATOM    983  OG  SER A 655     -24.445  26.618  12.549  1.00 15.72           O  
ANISOU  983  OG  SER A 655     1744   2102   2125    644   -267    390       O  
ATOM    984  N   ALA A 656     -21.496  25.358  13.957  1.00 11.48           N  
ANISOU  984  N   ALA A 656     1310   1495   1558    523   -162    312       N  
ATOM    985  CA  ALA A 656     -20.469  26.206  14.564  1.00 10.52           C  
ANISOU  985  CA  ALA A 656     1230   1318   1450    524   -106    313       C  
ATOM    986  C   ALA A 656     -20.884  27.684  14.452  1.00 11.10           C  
ANISOU  986  C   ALA A 656     1306   1359   1552    581    -88    348       C  
ATOM    987  O   ALA A 656     -20.731  28.437  15.411  1.00 11.00           O  
ANISOU  987  O   ALA A 656     1296   1305   1579    588    -46    333       O  
ATOM    988  CB  ALA A 656     -19.100  25.967  13.913  1.00  9.80           C  
ANISOU  988  CB  ALA A 656     1193   1206   1325    500    -93    315       C  
ATOM    989  N   ASP A 657     -21.450  28.087  13.312  1.00 11.96           N  
ANISOU  989  N   ASP A 657     1416   1486   1641    624   -123    392       N  
ATOM    990  CA  ASP A 657     -21.968  29.449  13.179  1.00 12.77           C  
ANISOU  990  CA  ASP A 657     1516   1556   1780    687   -109    435       C  
ATOM    991  C   ASP A 657     -22.954  29.774  14.308  1.00 12.08           C  
ANISOU  991  C   ASP A 657     1371   1464   1754    707    -90    413       C  
ATOM    992  O   ASP A 657     -22.862  30.825  14.953  1.00 11.88           O  
ANISOU  992  O   ASP A 657     1356   1381   1776    734    -43    410       O  
ATOM    993  CB  ASP A 657     -22.673  29.653  11.825  1.00 13.38           C  
ANISOU  993  CB  ASP A 657     1592   1671   1822    736   -165    492       C  
ATOM    994  CG  ASP A 657     -21.708  29.886  10.668  1.00 17.76           C  
ANISOU  994  CG  ASP A 657     2219   2214   2314    742   -159    535       C  
ATOM    995  OD1 ASP A 657     -20.476  29.911  10.864  1.00 19.09           O  
ANISOU  995  OD1 ASP A 657     2431   2340   2482    707   -108    523       O  
ATOM    996  OD2 ASP A 657     -22.198  30.069   9.533  1.00 21.31           O  
ANISOU  996  OD2 ASP A 657     2682   2700   2716    786   -206    585       O  
ATOM    997  N   ASP A 658     -23.915  28.880  14.542  1.00 11.54           N  
ANISOU  997  N   ASP A 658     1240   1454   1692    695   -122    395       N  
ATOM    998  CA  ASP A 658     -24.886  29.102  15.617  1.00 12.21           C  
ANISOU  998  CA  ASP A 658     1264   1541   1833    715    -92    377       C  
ATOM    999  C   ASP A 658     -24.193  29.185  16.966  1.00 11.41           C  
ANISOU  999  C   ASP A 658     1191   1405   1739    686    -27    329       C  
ATOM   1000  O   ASP A 658     -24.509  30.053  17.781  1.00 12.40           O  
ANISOU 1000  O   ASP A 658     1312   1497   1904    722     22    315       O  
ATOM   1001  CB  ASP A 658     -25.922  27.981  15.684  1.00 12.48           C  
ANISOU 1001  CB  ASP A 658     1220   1641   1880    693   -130    367       C  
ATOM   1002  CG  ASP A 658     -26.855  27.953  14.492  1.00 15.32           C  
ANISOU 1002  CG  ASP A 658     1534   2044   2244    727   -207    406       C  
ATOM   1003  OD1 ASP A 658     -26.913  28.940  13.728  1.00 17.18           O  
ANISOU 1003  OD1 ASP A 658     1791   2262   2476    784   -225    450       O  
ATOM   1004  OD2 ASP A 658     -27.565  26.931  14.351  1.00 17.59           O  
ANISOU 1004  OD2 ASP A 658     1760   2382   2543    696   -254    393       O  
ATOM   1005  N   LEU A 659     -23.262  28.258  17.204  1.00 10.37           N  
ANISOU 1005  N   LEU A 659     1091   1281   1568    625    -29    302       N  
ATOM   1006  CA  LEU A 659     -22.536  28.204  18.466  1.00 10.07           C  
ANISOU 1006  CA  LEU A 659     1083   1220   1524    594     17    259       C  
ATOM   1007  C   LEU A 659     -21.723  29.466  18.751  1.00 10.07           C  
ANISOU 1007  C   LEU A 659     1136   1151   1541    613     51    245       C  
ATOM   1008  O   LEU A 659     -21.751  29.974  19.874  1.00 10.16           O  
ANISOU 1008  O   LEU A 659     1156   1139   1564    622     92    206       O  
ATOM   1009  CB  LEU A 659     -21.631  26.978  18.498  1.00  9.56           C  
ANISOU 1009  CB  LEU A 659     1039   1173   1420    531     -1    244       C  
ATOM   1010  CG  LEU A 659     -20.833  26.734  19.782  1.00  8.64           C  
ANISOU 1010  CG  LEU A 659      950   1044   1288    498     30    206       C  
ATOM   1011  CD1 LEU A 659     -21.763  26.451  20.978  1.00  9.99           C  
ANISOU 1011  CD1 LEU A 659     1086   1248   1463    505     64    191       C  
ATOM   1012  CD2 LEU A 659     -19.852  25.594  19.557  1.00  9.06           C  
ANISOU 1012  CD2 LEU A 659     1022   1107   1314    446      5    203       C  
ATOM   1013  N   ALA A 660     -21.039  29.986  17.733  1.00 10.51           N  
ANISOU 1013  N   ALA A 660     1226   1170   1596    619     38    276       N  
ATOM   1014  CA  ALA A 660     -20.222  31.192  17.910  1.00 10.49           C  
ANISOU 1014  CA  ALA A 660     1268   1089   1627    629     70    268       C  
ATOM   1015  C   ALA A 660     -21.100  32.420  18.120  1.00 11.36           C  
ANISOU 1015  C   ALA A 660     1366   1158   1791    694     97    275       C  
ATOM   1016  O   ALA A 660     -20.707  33.356  18.813  1.00 11.27           O  
ANISOU 1016  O   ALA A 660     1383   1081   1818    701    133    239       O  
ATOM   1017  CB  ALA A 660     -19.296  31.402  16.715  1.00 10.55           C  
ANISOU 1017  CB  ALA A 660     1312   1068   1628    620     61    312       C  
ATOM   1018  N   LYS A 661     -22.293  32.416  17.524  1.00 11.31           N  
ANISOU 1018  N   LYS A 661     1315   1188   1794    741     77    317       N  
ATOM   1019  CA  LYS A 661     -23.172  33.586  17.567  1.00 12.98           C  
ANISOU 1019  CA  LYS A 661     1506   1358   2066    813    101    335       C  
ATOM   1020  C   LYS A 661     -23.846  33.755  18.928  1.00 13.22           C  
ANISOU 1020  C   LYS A 661     1510   1389   2123    832    148    277       C  
ATOM   1021  O   LYS A 661     -23.914  34.864  19.474  1.00 14.53           O  
ANISOU 1021  O   LYS A 661     1695   1487   2340    871    193    251       O  
ATOM   1022  CB  LYS A 661     -24.233  33.472  16.476  1.00 13.58           C  
ANISOU 1022  CB  LYS A 661     1533   1480   2145    861     54    402       C  
ATOM   1023  CG  LYS A 661     -24.959  34.770  16.202  1.00 15.45           C  
ANISOU 1023  CG  LYS A 661     1755   1664   2450    944     70    444       C  
ATOM   1024  CD  LYS A 661     -26.125  34.572  15.256  1.00 17.57           C  
ANISOU 1024  CD  LYS A 661     1962   1993   2722    993     11    507       C  
ATOM   1025  CE  LYS A 661     -25.639  34.158  13.879  1.00 17.92           C  
ANISOU 1025  CE  LYS A 661     2041   2071   2697    977    -51    562       C  
ATOM   1026  NZ  LYS A 661     -26.793  34.080  12.944  1.00 20.87           N  
ANISOU 1026  NZ  LYS A 661     2357   2503   3069   1032   -122    621       N  
ATOM   1027  N   GLN A 662     -24.358  32.648  19.459  1.00 13.21           N  
ANISOU 1027  N   GLN A 662     1467   1463   2090    804    143    257       N  
ATOM   1028  CA  GLN A 662     -25.103  32.681  20.709  1.00 13.67           C  
ANISOU 1028  CA  GLN A 662     1496   1536   2161    825    197    212       C  
ATOM   1029  C   GLN A 662     -24.172  32.911  21.890  1.00 13.48           C  
ANISOU 1029  C   GLN A 662     1537   1477   2107    795    236    141       C  
ATOM   1030  O   GLN A 662     -22.954  32.726  21.792  1.00 12.96           O  
ANISOU 1030  O   GLN A 662     1523   1391   2011    744    211    127       O  
ATOM   1031  CB  GLN A 662     -25.954  31.415  20.879  1.00 13.50           C  
ANISOU 1031  CB  GLN A 662     1406   1601   2123    803    185    225       C  
ATOM   1032  CG  GLN A 662     -25.180  30.102  20.936  1.00 13.38           C  
ANISOU 1032  CG  GLN A 662     1411   1626   2046    724    154    217       C  
ATOM   1033  CD  GLN A 662     -24.549  29.841  22.293  1.00 12.46           C  
ANISOU 1033  CD  GLN A 662     1338   1510   1887    692    198    164       C  
ATOM   1034  OE1 GLN A 662     -25.241  29.850  23.323  1.00 12.44           O  
ANISOU 1034  OE1 GLN A 662     1313   1529   1883    713    253    141       O  
ATOM   1035  NE2 GLN A 662     -23.241  29.628  22.308  1.00 12.68           N  
ANISOU 1035  NE2 GLN A 662     1426   1516   1875    645    175    145       N  
ATOM   1036  N   THR A 663     -24.758  33.337  23.003  1.00 14.09           N  
ANISOU 1036  N   THR A 663     1610   1551   2193    830    296     94       N  
ATOM   1037  CA  THR A 663     -23.984  33.721  24.174  1.00 14.75           C  
ANISOU 1037  CA  THR A 663     1761   1602   2243    813    328     15       C  
ATOM   1038  C   THR A 663     -24.436  33.002  25.442  1.00 15.72           C  
ANISOU 1038  C   THR A 663     1876   1791   2306    806    373    -22       C  
ATOM   1039  O   THR A 663     -24.047  33.392  26.547  1.00 17.40           O  
ANISOU 1039  O   THR A 663     2145   1988   2480    808    407    -93       O  
ATOM   1040  CB  THR A 663     -24.044  35.262  24.406  1.00 15.32           C  
ANISOU 1040  CB  THR A 663     1866   1580   2376    870    368    -27       C  
ATOM   1041  OG1 THR A 663     -25.410  35.703  24.458  1.00 15.41           O  
ANISOU 1041  OG1 THR A 663     1820   1596   2439    946    416    -11       O  
ATOM   1042  CG2 THR A 663     -23.301  36.025  23.301  1.00 16.10           C  
ANISOU 1042  CG2 THR A 663     1990   1599   2530    866    331     10       C  
ATOM   1043  N   LYS A 664     -25.256  31.963  25.293  1.00 15.70           N  
ANISOU 1043  N   LYS A 664     1807   1862   2296    798    374     27       N  
ATOM   1044  CA  LYS A 664     -25.781  31.242  26.466  1.00 16.83           C  
ANISOU 1044  CA  LYS A 664     1937   2069   2389    793    430      9       C  
ATOM   1045  C   LYS A 664     -24.843  30.116  26.889  1.00 16.41           C  
ANISOU 1045  C   LYS A 664     1923   2055   2258    721    397      8       C  
ATOM   1046  O   LYS A 664     -24.615  29.901  28.078  1.00 17.93           O  
ANISOU 1046  O   LYS A 664     2159   2274   2381    714    434    -29       O  
ATOM   1047  CB  LYS A 664     -27.183  30.695  26.193  1.00 17.30           C  
ANISOU 1047  CB  LYS A 664     1895   2181   2498    818    456     64       C  
ATOM   1048  CG  LYS A 664     -28.202  31.770  25.776  1.00 20.63           C  
ANISOU 1048  CG  LYS A 664     2263   2568   3006    897    485     74       C  
ATOM   1049  CD  LYS A 664     -29.575  31.183  25.433  1.00 23.77           C  
ANISOU 1049  CD  LYS A 664     2543   3023   3467    917    497    132       C  
ATOM   1050  CE  LYS A 664     -30.466  32.236  24.786  1.00 26.43           C  
ANISOU 1050  CE  LYS A 664     2821   3323   3899    997    502    154       C  
ATOM   1051  NZ  LYS A 664     -31.799  31.705  24.374  1.00 27.87           N  
ANISOU 1051  NZ  LYS A 664     2874   3559   4156   1016    498    211       N  
ATOM   1052  N   ILE A 665     -24.298  29.413  25.904  1.00 15.37           N  
ANISOU 1052  N   ILE A 665     1779   1926   2135    674    329     50       N  
ATOM   1053  CA AILE A 665     -23.432  28.247  26.099  0.50 14.76           C  
ANISOU 1053  CA AILE A 665     1726   1879   2003    609    292     61       C  
ATOM   1054  CA BILE A 665     -23.396  28.321  26.227  0.50 15.06           C  
ANISOU 1054  CA BILE A 665     1770   1916   2037    611    297     54       C  
ATOM   1055  C   ILE A 665     -21.988  28.610  25.746  1.00 14.45           C  
ANISOU 1055  C   ILE A 665     1747   1790   1952    579    240     36       C  
ATOM   1056  O   ILE A 665     -21.766  29.206  24.686  1.00 14.91           O  
ANISOU 1056  O   ILE A 665     1802   1805   2058    588    211     51       O  
ATOM   1057  CB AILE A 665     -23.932  27.094  25.187  0.50 14.14           C  
ANISOU 1057  CB AILE A 665     1581   1837   1955    579    258    122       C  
ATOM   1058  CB BILE A 665     -23.912  26.923  25.782  0.50 14.87           C  
ANISOU 1058  CB BILE A 665     1685   1943   2023    575    279    113       C  
ATOM   1059  CG1AILE A 665     -25.359  26.706  25.587  0.50 14.84           C  
ANISOU 1059  CG1AILE A 665     1595   1971   2072    602    311    148       C  
ATOM   1060  CG1BILE A 665     -23.657  26.662  24.298  0.50 13.95           C  
ANISOU 1060  CG1BILE A 665     1545   1809   1946    554    210    146       C  
ATOM   1061  CG2AILE A 665     -23.002  25.878  25.232  0.50 13.08           C  
ANISOU 1061  CG2AILE A 665     1470   1719   1780    516    219    135       C  
ATOM   1062  CG2BILE A 665     -25.389  26.734  26.162  0.50 15.61           C  
ANISOU 1062  CG2BILE A 665     1705   2077   2149    607    339    137       C  
ATOM   1063  CD1AILE A 665     -26.110  25.915  24.555  0.50 15.35           C  
ANISOU 1063  CD1AILE A 665     1579   2060   2193    583    271    197       C  
ATOM   1064  CD1BILE A 665     -23.660  25.182  23.952  0.50 12.72           C  
ANISOU 1064  CD1BILE A 665     1358   1688   1787    502    178    181       C  
ATOM   1065  N   GLU A 666     -21.030  28.249  26.596  1.00 13.71           N  
ANISOU 1065  N   GLU A 666     1704   1706   1800    545    227      5       N  
ATOM   1066  CA  GLU A 666     -19.630  28.454  26.248  1.00 13.56           C  
ANISOU 1066  CA  GLU A 666     1724   1644   1784    509    175    -13       C  
ATOM   1067  C   GLU A 666     -19.105  27.216  25.543  1.00 11.84           C  
ANISOU 1067  C   GLU A 666     1485   1448   1565    463    132     35       C  
ATOM   1068  O   GLU A 666     -19.824  26.240  25.366  1.00 11.79           O  
ANISOU 1068  O   GLU A 666     1438   1484   1556    455    138     76       O  
ATOM   1069  CB  GLU A 666     -18.793  28.823  27.465  1.00 14.57           C  
ANISOU 1069  CB  GLU A 666     1913   1764   1860    499    169    -78       C  
ATOM   1070  CG  GLU A 666     -18.921  27.895  28.629  1.00 18.35           C  
ANISOU 1070  CG  GLU A 666     2407   2309   2256    489    183    -77       C  
ATOM   1071  CD  GLU A 666     -17.936  28.217  29.734  1.00 23.66           C  
ANISOU 1071  CD  GLU A 666     3144   2981   2866    477    155   -141       C  
ATOM   1072  OE1 GLU A 666     -17.859  29.395  30.154  1.00 27.23           O  
ANISOU 1072  OE1 GLU A 666     3634   3393   3321    501    165   -211       O  
ATOM   1073  OE2 GLU A 666     -17.244  27.285  30.188  1.00 24.52           O  
ANISOU 1073  OE2 GLU A 666     3265   3125   2925    444    118   -122       O  
ATOM   1074  N   TYR A 667     -17.860  27.273  25.098  1.00 10.10           N  
ANISOU 1074  N   TYR A 667     1288   1194   1357    431     91     29       N  
ATOM   1075  CA  TYR A 667     -17.298  26.166  24.332  1.00  8.81           C  
ANISOU 1075  CA  TYR A 667     1106   1043   1199    394     56     69       C  
ATOM   1076  C   TYR A 667     -15.789  26.239  24.351  1.00  8.86           C  
ANISOU 1076  C   TYR A 667     1138   1016   1212    362     22     50       C  
ATOM   1077  O   TYR A 667     -15.201  27.283  24.662  1.00  9.07           O  
ANISOU 1077  O   TYR A 667     1191   1000   1255    364     18     10       O  
ATOM   1078  CB  TYR A 667     -17.808  26.185  22.878  1.00  8.74           C  
ANISOU 1078  CB  TYR A 667     1066   1025   1229    406     51    108       C  
ATOM   1079  CG  TYR A 667     -17.579  27.504  22.179  1.00  8.15           C  
ANISOU 1079  CG  TYR A 667     1008    895   1193    431     56    104       C  
ATOM   1080  CD1 TYR A 667     -18.585  28.470  22.125  1.00  8.47           C  
ANISOU 1080  CD1 TYR A 667     1038    922   1258    480     83    103       C  
ATOM   1081  CD2 TYR A 667     -16.350  27.797  21.581  1.00  8.32           C  
ANISOU 1081  CD2 TYR A 667     1051    874   1238    409     41    106       C  
ATOM   1082  CE1 TYR A 667     -18.369  29.692  21.494  1.00  9.50           C  
ANISOU 1082  CE1 TYR A 667     1186    991   1433    505     91    108       C  
ATOM   1083  CE2 TYR A 667     -16.132  29.010  20.942  1.00  9.18           C  
ANISOU 1083  CE2 TYR A 667     1175    924   1390    430     54    113       C  
ATOM   1084  CZ  TYR A 667     -17.138  29.952  20.912  1.00  8.15           C  
ANISOU 1084  CZ  TYR A 667     1040    776   1281    478     78    115       C  
ATOM   1085  OH  TYR A 667     -16.939  31.166  20.286  1.00  9.93           O  
ANISOU 1085  OH  TYR A 667     1282    934   1558    501     93    131       O  
ATOM   1086  N   GLY A 668     -15.165  25.121  23.994  1.00  7.56           N  
ANISOU 1086  N   GLY A 668      960    866   1045    330     -4     78       N  
ATOM   1087  CA  GLY A 668     -13.717  25.037  24.014  1.00  7.40           C  
ANISOU 1087  CA  GLY A 668      950    819   1041    300    -36     67       C  
ATOM   1088  C   GLY A 668     -13.252  23.739  23.415  1.00  6.44           C  
ANISOU 1088  C   GLY A 668      808    711    927    277    -52    103       C  
ATOM   1089  O   GLY A 668     -13.994  23.069  22.704  1.00  7.22           O  
ANISOU 1089  O   GLY A 668      889    828   1026    282    -42    131       O  
ATOM   1090  N   ALA A 669     -12.009  23.397  23.708  1.00  6.72           N  
ANISOU 1090  N   ALA A 669      844    735    975    253    -81     98       N  
ATOM   1091  CA  ALA A 669     -11.371  22.201  23.164  1.00  6.11           C  
ANISOU 1091  CA  ALA A 669      747    659    917    236    -93    128       C  
ATOM   1092  C   ALA A 669     -10.369  21.684  24.180  1.00  6.48           C  
ANISOU 1092  C   ALA A 669      791    713    958    219   -132    124       C  
ATOM   1093  O   ALA A 669     -10.054  22.371  25.158  1.00  7.31           O  
ANISOU 1093  O   ALA A 669      912    821   1043    218   -155     93       O  
ATOM   1094  CB  ALA A 669     -10.669  22.524  21.839  1.00  6.69           C  
ANISOU 1094  CB  ALA A 669      810    694   1039    232    -79    135       C  
ATOM   1095  N   VAL A 670      -9.856  20.475  23.953  1.00  5.91           N  
ANISOU 1095  N   VAL A 670      700    642    904    209   -143    154       N  
ATOM   1096  CA  VAL A 670      -8.743  19.989  24.747  1.00  6.81           C  
ANISOU 1096  CA  VAL A 670      803    757   1027    199   -186    159       C  
ATOM   1097  C   VAL A 670      -7.493  20.829  24.450  1.00  7.04           C  
ANISOU 1097  C   VAL A 670      812    749   1113    186   -204    134       C  
ATOM   1098  O   VAL A 670      -7.185  21.115  23.294  1.00  8.01           O  
ANISOU 1098  O   VAL A 670      919    840   1285    184   -172    137       O  
ATOM   1099  CB  VAL A 670      -8.479  18.498  24.476  1.00  6.46           C  
ANISOU 1099  CB  VAL A 670      739    710   1006    197   -188    200       C  
ATOM   1100  CG1 VAL A 670      -7.187  18.039  25.138  1.00  7.31           C  
ANISOU 1100  CG1 VAL A 670      825    812   1139    193   -236    213       C  
ATOM   1101  CG2 VAL A 670      -9.660  17.654  24.979  1.00  7.35           C  
ANISOU 1101  CG2 VAL A 670      867    852   1074    202   -173    229       C  
ATOM   1102  N   ARG A 671      -6.771  21.216  25.492  1.00  7.84           N  
ANISOU 1102  N   ARG A 671      912    857   1209    178   -255    111       N  
ATOM   1103  CA  ARG A 671      -5.593  22.055  25.329  1.00  8.69           C  
ANISOU 1103  CA  ARG A 671      990    926   1385    158   -278     83       C  
ATOM   1104  C   ARG A 671      -4.473  21.293  24.623  1.00  8.38           C  
ANISOU 1104  C   ARG A 671      898    863   1422    151   -278    115       C  
ATOM   1105  O   ARG A 671      -4.230  20.121  24.911  1.00  8.86           O  
ANISOU 1105  O   ARG A 671      946    943   1478    160   -298    147       O  
ATOM   1106  CB  ARG A 671      -5.122  22.549  26.698  1.00  9.54           C  
ANISOU 1106  CB  ARG A 671     1108   1052   1463    148   -349     42       C  
ATOM   1107  CG  ARG A 671      -4.058  23.649  26.657  1.00 13.25           C  
ANISOU 1107  CG  ARG A 671     1546   1475   2012    120   -380     -2       C  
ATOM   1108  CD  ARG A 671      -3.556  24.015  28.063  1.00 16.12           C  
ANISOU 1108  CD  ARG A 671     1922   1863   2339    109   -469    -53       C  
ATOM   1109  NE  ARG A 671      -4.644  24.401  28.967  1.00 19.34           N  
ANISOU 1109  NE  ARG A 671     2400   2308   2639    129   -467    -88       N  
ATOM   1110  CZ  ARG A 671      -5.131  25.635  29.087  1.00 21.27           C  
ANISOU 1110  CZ  ARG A 671     2678   2524   2878    127   -449   -148       C  
ATOM   1111  NH1 ARG A 671      -4.625  26.637  28.376  1.00 22.77           N  
ANISOU 1111  NH1 ARG A 671     2840   2644   3168    103   -435   -175       N  
ATOM   1112  NH2 ARG A 671      -6.127  25.870  29.937  1.00 21.82           N  
ANISOU 1112  NH2 ARG A 671     2811   2633   2848    153   -439   -179       N  
ATOM   1113  N   ASP A 672      -3.826  21.975  23.681  1.00  8.45           N  
ANISOU 1113  N   ASP A 672      877    827   1505    139   -245    110       N  
ATOM   1114  CA  ASP A 672      -2.581  21.513  23.057  1.00  9.25           C  
ANISOU 1114  CA  ASP A 672      920    901   1695    132   -236    132       C  
ATOM   1115  C   ASP A 672      -2.721  20.273  22.187  1.00  8.32           C  
ANISOU 1115  C   ASP A 672      799    787   1576    153   -191    169       C  
ATOM   1116  O   ASP A 672      -1.812  19.447  22.095  1.00  8.39           O  
ANISOU 1116  O   ASP A 672      763    786   1639    158   -198    190       O  
ATOM   1117  CB  ASP A 672      -1.463  21.386  24.097  1.00 10.33           C  
ANISOU 1117  CB  ASP A 672     1010   1042   1872    117   -316    121       C  
ATOM   1118  CG  ASP A 672      -1.030  22.744  24.637  1.00 12.49           C  
ANISOU 1118  CG  ASP A 672     1273   1293   2179     87   -356     72       C  
ATOM   1119  OD1 ASP A 672      -1.297  23.771  23.969  1.00 16.30           O  
ANISOU 1119  OD1 ASP A 672     1768   1737   2687     76   -306     57       O  
ATOM   1120  OD2 ASP A 672      -0.477  22.797  25.750  1.00 15.40           O  
ANISOU 1120  OD2 ASP A 672     1626   1680   2544     75   -441     46       O  
ATOM   1121  N   GLY A 673      -3.884  20.165  21.549  1.00  7.88           N  
ANISOU 1121  N   GLY A 673      789    743   1463    167   -148    174       N  
ATOM   1122  CA  GLY A 673      -4.112  19.209  20.480  1.00  8.24           C  
ANISOU 1122  CA  GLY A 673      840    784   1506    184   -100    193       C  
ATOM   1123  C   GLY A 673      -4.405  19.900  19.160  1.00  7.62           C  
ANISOU 1123  C   GLY A 673      782    691   1422    191    -38    193       C  
ATOM   1124  O   GLY A 673      -4.392  21.146  19.051  1.00  8.07           O  
ANISOU 1124  O   GLY A 673      844    732   1489    183    -26    187       O  
ATOM   1125  N   SER A 674      -4.673  19.083  18.146  1.00  7.06           N  
ANISOU 1125  N   SER A 674      727    622   1334    208      1    200       N  
ATOM   1126  CA  SER A 674      -4.913  19.579  16.798  1.00  7.01           C  
ANISOU 1126  CA  SER A 674      748    611   1306    222     58    205       C  
ATOM   1127  C   SER A 674      -6.209  20.367  16.674  1.00  6.72           C  
ANISOU 1127  C   SER A 674      752    594   1206    228     51    202       C  
ATOM   1128  O   SER A 674      -6.316  21.249  15.830  1.00  6.80           O  
ANISOU 1128  O   SER A 674      782    596   1205    239     88    216       O  
ATOM   1129  CB  SER A 674      -4.874  18.435  15.779  1.00  6.36           C  
ANISOU 1129  CB  SER A 674      679    529   1208    241     94    201       C  
ATOM   1130  OG  SER A 674      -5.838  17.435  16.075  1.00  6.26           O  
ANISOU 1130  OG  SER A 674      686    536   1158    242     58    187       O  
ATOM   1131  N   THR A 675      -7.206  20.046  17.496  1.00  5.83           N  
ANISOU 1131  N   THR A 675      651    508   1056    225      9    192       N  
ATOM   1132  CA  THR A 675      -8.454  20.819  17.460  1.00  6.07           C  
ANISOU 1132  CA  THR A 675      709    558   1040    235      4    190       C  
ATOM   1133  C   THR A 675      -8.219  22.248  17.929  1.00  6.33           C  
ANISOU 1133  C   THR A 675      741    568   1096    231      5    188       C  
ATOM   1134  O   THR A 675      -8.595  23.193  17.242  1.00  6.57           O  
ANISOU 1134  O   THR A 675      790    587   1119    245     31    200       O  
ATOM   1135  CB  THR A 675      -9.552  20.115  18.255  1.00  6.22           C  
ANISOU 1135  CB  THR A 675      730    609   1024    232    -30    183       C  
ATOM   1136  OG1 THR A 675      -9.824  18.868  17.614  1.00  6.31           O  
ANISOU 1136  OG1 THR A 675      744    629   1026    233    -29    182       O  
ATOM   1137  CG2 THR A 675     -10.840  20.947  18.280  1.00  6.01           C  
ANISOU 1137  CG2 THR A 675      719    603    962    246    -32    182       C  
ATOM   1138  N   MET A 676      -7.553  22.405  19.072  1.00  6.79           N  
ANISOU 1138  N   MET A 676      778    616   1186    211    -25    172       N  
ATOM   1139  CA  MET A 676      -7.152  23.728  19.532  1.00  7.32           C  
ANISOU 1139  CA  MET A 676      842    651   1289    201    -29    157       C  
ATOM   1140  C   MET A 676      -6.375  24.462  18.432  1.00  7.32           C  
ANISOU 1140  C   MET A 676      832    606   1342    199     20    179       C  
ATOM   1141  O   MET A 676      -6.654  25.608  18.120  1.00  7.33           O  
ANISOU 1141  O   MET A 676      850    578   1357    205     43    186       O  
ATOM   1142  CB  MET A 676      -6.281  23.618  20.792  1.00  7.75           C  
ANISOU 1142  CB  MET A 676      870    702   1372    177    -79    132       C  
ATOM   1143  CG  MET A 676      -5.958  24.970  21.401  1.00  9.12           C  
ANISOU 1143  CG  MET A 676     1045    840   1582    161    -96     98       C  
ATOM   1144  SD  MET A 676      -4.525  25.008  22.457  1.00 10.43           S  
ANISOU 1144  SD  MET A 676     1166    990   1806    127   -160     67       S  
ATOM   1145  CE  MET A 676      -3.216  24.871  21.232  1.00 12.24           C  
ANISOU 1145  CE  MET A 676     1337   1177   2137    113   -113    106       C  
ATOM   1146  N   THR A 677      -5.398  23.777  17.834  1.00  7.20           N  
ANISOU 1146  N   THR A 677      789    583   1362    193     44    197       N  
ATOM   1147  CA  THR A 677      -4.530  24.407  16.844  1.00  8.18           C  
ANISOU 1147  CA  THR A 677      898    667   1542    190    103    225       C  
ATOM   1148  C   THR A 677      -5.283  24.794  15.574  1.00  8.08           C  
ANISOU 1148  C   THR A 677      932    661   1478    220    155    258       C  
ATOM   1149  O   THR A 677      -4.978  25.824  14.954  1.00  9.01           O  
ANISOU 1149  O   THR A 677     1054    740   1630    222    202    288       O  
ATOM   1150  CB  THR A 677      -3.323  23.514  16.548  1.00  8.21           C  
ANISOU 1150  CB  THR A 677      857    666   1597    184    124    235       C  
ATOM   1151  OG1 THR A 677      -2.570  23.348  17.755  1.00 10.07           O  
ANISOU 1151  OG1 THR A 677     1044    893   1888    157     65    211       O  
ATOM   1152  CG2 THR A 677      -2.436  24.121  15.473  1.00  8.94           C  
ANISOU 1152  CG2 THR A 677      931    720   1747    183    202    271       C  
ATOM   1153  N   PHE A 678      -6.265  23.981  15.193  1.00  7.49           N  
ANISOU 1153  N   PHE A 678      889    632   1324    244    143    254       N  
ATOM   1154  CA  PHE A 678      -7.121  24.302  14.058  1.00  7.56           C  
ANISOU 1154  CA  PHE A 678      943    658   1270    276    171    281       C  
ATOM   1155  C   PHE A 678      -7.762  25.670  14.258  1.00  7.67           C  
ANISOU 1155  C   PHE A 678      973    649   1292    285    168    296       C  
ATOM   1156  O   PHE A 678      -7.762  26.514  13.350  1.00  8.62           O  
ANISOU 1156  O   PHE A 678     1116    749   1411    304    212    339       O  
ATOM   1157  CB  PHE A 678      -8.226  23.256  13.896  1.00  7.38           C  
ANISOU 1157  CB  PHE A 678      942    688   1174    291    135    262       C  
ATOM   1158  CG  PHE A 678      -9.272  23.644  12.883  1.00  7.74           C  
ANISOU 1158  CG  PHE A 678     1029    761   1152    325    139    284       C  
ATOM   1159  CD1 PHE A 678      -9.129  23.284  11.547  1.00  8.93           C  
ANISOU 1159  CD1 PHE A 678     1213    930   1250    347    172    300       C  
ATOM   1160  CD2 PHE A 678     -10.397  24.373  13.263  1.00  7.40           C  
ANISOU 1160  CD2 PHE A 678      992    726   1095    338    108    288       C  
ATOM   1161  CE1 PHE A 678     -10.083  23.648  10.601  1.00  9.33           C  
ANISOU 1161  CE1 PHE A 678     1304   1012   1229    382    163    322       C  
ATOM   1162  CE2 PHE A 678     -11.350  24.746  12.332  1.00  8.19           C  
ANISOU 1162  CE2 PHE A 678     1121    851   1138    374    103    314       C  
ATOM   1163  CZ  PHE A 678     -11.190  24.392  10.987  1.00  7.65           C  
ANISOU 1163  CZ  PHE A 678     1089    807   1011    395    125    333       C  
ATOM   1164  N   PHE A 679      -8.299  25.898  15.450  1.00  8.40           N  
ANISOU 1164  N   PHE A 679     1056    742   1393    275    122    263       N  
ATOM   1165  CA  PHE A 679      -8.917  27.191  15.720  1.00  8.46           C  
ANISOU 1165  CA  PHE A 679     1078    720   1416    288    122    267       C  
ATOM   1166  C   PHE A 679      -7.886  28.303  15.776  1.00  9.32           C  
ANISOU 1166  C   PHE A 679     1173    757   1611    267    154    277       C  
ATOM   1167  O   PHE A 679      -8.103  29.360  15.189  1.00  9.88           O  
ANISOU 1167  O   PHE A 679     1263    789   1702    285    188    313       O  
ATOM   1168  CB  PHE A 679      -9.805  27.104  16.957  1.00  8.13           C  
ANISOU 1168  CB  PHE A 679     1034    702   1354    288     76    224       C  
ATOM   1169  CG  PHE A 679     -11.087  26.395  16.671  1.00  6.42           C  
ANISOU 1169  CG  PHE A 679      828    542   1071    314     58    230       C  
ATOM   1170  CD1 PHE A 679     -12.147  27.060  16.042  1.00  7.54           C  
ANISOU 1170  CD1 PHE A 679      986    689   1189    352     65    256       C  
ATOM   1171  CD2 PHE A 679     -11.215  25.040  16.936  1.00  6.33           C  
ANISOU 1171  CD2 PHE A 679      804    574   1028    300     33    214       C  
ATOM   1172  CE1 PHE A 679     -13.313  26.387  15.717  1.00  7.59           C  
ANISOU 1172  CE1 PHE A 679      990    748   1144    372     40    260       C  
ATOM   1173  CE2 PHE A 679     -12.380  24.366  16.619  1.00  8.29           C  
ANISOU 1173  CE2 PHE A 679     1053    867   1229    316     14    218       C  
ATOM   1174  CZ  PHE A 679     -13.439  25.043  16.004  1.00  8.36           C  
ANISOU 1174  CZ  PHE A 679     1072    886   1217    351     15    238       C  
ATOM   1175  N   LYS A 680      -6.754  28.038  16.427  1.00  9.78           N  
ANISOU 1175  N   LYS A 680     1193    796   1726    228    141    251       N  
ATOM   1176  CA  LYS A 680      -5.685  29.024  16.549  1.00 10.92           C  
ANISOU 1176  CA  LYS A 680     1309    869   1971    197    163    253       C  
ATOM   1177  C   LYS A 680      -5.185  29.533  15.183  1.00 11.69           C  
ANISOU 1177  C   LYS A 680     1411    931   2100    207    242    321       C  
ATOM   1178  O   LYS A 680      -4.825  30.716  15.032  1.00 12.77           O  
ANISOU 1178  O   LYS A 680     1543    997   2313    194    276    343       O  
ATOM   1179  CB  LYS A 680      -4.534  28.419  17.363  1.00 11.39           C  
ANISOU 1179  CB  LYS A 680     1317    929   2083    157    126    217       C  
ATOM   1180  CG  LYS A 680      -3.406  29.378  17.699  1.00 13.95           C  
ANISOU 1180  CG  LYS A 680     1597   1180   2525    115    128    205       C  
ATOM   1181  CD  LYS A 680      -2.499  28.779  18.772  1.00 18.21           C  
ANISOU 1181  CD  LYS A 680     2084   1732   3102     81     61    159       C  
ATOM   1182  CE  LYS A 680      -1.607  29.846  19.401  1.00 21.61           C  
ANISOU 1182  CE  LYS A 680     2472   2091   3646     33     34    123       C  
ATOM   1183  NZ  LYS A 680      -0.692  29.289  20.455  1.00 24.03           N  
ANISOU 1183  NZ  LYS A 680     2726   2418   3988      2    -47     77       N  
ATOM   1184  N   LYS A 681      -5.182  28.644  14.193  1.00 11.85           N  
ANISOU 1184  N   LYS A 681     1445    997   2060    230    275    354       N  
ATOM   1185  CA  LYS A 681      -4.579  28.927  12.887  1.00 13.19           C  
ANISOU 1185  CA  LYS A 681     1622   1146   2242    242    360    420       C  
ATOM   1186  C   LYS A 681      -5.589  29.322  11.813  1.00 13.00           C  
ANISOU 1186  C   LYS A 681     1662   1144   2134    291    388    473       C  
ATOM   1187  O   LYS A 681      -5.189  29.734  10.719  1.00 14.69           O  
ANISOU 1187  O   LYS A 681     1895   1340   2345    308    463    538       O  
ATOM   1188  CB  LYS A 681      -3.788  27.711  12.390  1.00 13.79           C  
ANISOU 1188  CB  LYS A 681     1677   1258   2303    241    388    420       C  
ATOM   1189  CG  LYS A 681      -2.595  27.325  13.257  1.00 17.52           C  
ANISOU 1189  CG  LYS A 681     2076   1707   2872    199    368    386       C  
ATOM   1190  CD  LYS A 681      -1.352  28.111  12.889  1.00 22.59           C  
ANISOU 1190  CD  LYS A 681     2670   2285   3630    171    437    426       C  
ATOM   1191  CE  LYS A 681      -0.101  27.436  13.438  1.00 25.10           C  
ANISOU 1191  CE  LYS A 681     2906   2595   4037    140    424    400       C  
ATOM   1192  NZ  LYS A 681       1.145  28.082  12.930  1.00 27.73           N  
ANISOU 1192  NZ  LYS A 681     3178   2868   4492    114    505    445       N  
ATOM   1193  N   SER A 682      -6.881  29.178  12.108  1.00 12.34           N  
ANISOU 1193  N   SER A 682     1608   1101   1981    317    331    449       N  
ATOM   1194  CA  SER A 682      -7.920  29.412  11.100  1.00 12.16           C  
ANISOU 1194  CA  SER A 682     1638   1111   1873    368    339    496       C  
ATOM   1195  C   SER A 682      -7.970  30.855  10.625  1.00 13.49           C  
ANISOU 1195  C   SER A 682     1827   1217   2083    387    385    562       C  
ATOM   1196  O   SER A 682      -7.771  31.786  11.406  1.00 13.85           O  
ANISOU 1196  O   SER A 682     1850   1193   2220    365    383    550       O  
ATOM   1197  CB  SER A 682      -9.305  29.020  11.618  1.00 11.50           C  
ANISOU 1197  CB  SER A 682     1562   1077   1729    388    266    457       C  
ATOM   1198  OG  SER A 682     -10.261  29.127  10.568  1.00 10.64           O  
ANISOU 1198  OG  SER A 682     1496   1008   1538    437    262    501       O  
ATOM   1199  N   LYS A 683      -8.262  31.020   9.338  1.00 13.92           N  
ANISOU 1199  N   LYS A 683     1929   1295   2066    431    423    632       N  
ATOM   1200  CA  LYS A 683      -8.513  32.334   8.756  1.00 15.52           C  
ANISOU 1200  CA  LYS A 683     2160   1444   2291    463    464    713       C  
ATOM   1201  C   LYS A 683      -9.984  32.479   8.351  1.00 15.38           C  
ANISOU 1201  C   LYS A 683     2182   1476   2187    522    412    735       C  
ATOM   1202  O   LYS A 683     -10.361  33.442   7.670  1.00 16.52           O  
ANISOU 1202  O   LYS A 683     2359   1591   2326    565    438    815       O  
ATOM   1203  CB  LYS A 683      -7.604  32.563   7.546  1.00 16.79           C  
ANISOU 1203  CB  LYS A 683     2347   1591   2440    473    560    797       C  
ATOM   1204  CG  LYS A 683      -6.131  32.690   7.882  1.00 19.07           C  
ANISOU 1204  CG  LYS A 683     2584   1816   2846    416    623    792       C  
ATOM   1205  CD  LYS A 683      -5.285  32.797   6.618  1.00 23.84           C  
ANISOU 1205  CD  LYS A 683     3212   2417   3429    431    732    879       C  
ATOM   1206  CE  LYS A 683      -3.815  32.514   6.924  1.00 26.28           C  
ANISOU 1206  CE  LYS A 683     3453   2686   3845    375    789    860       C  
ATOM   1207  NZ  LYS A 683      -2.974  32.367   5.695  1.00 29.29           N  
ANISOU 1207  NZ  LYS A 683     3853   3080   4195    393    905    937       N  
ATOM   1208  N   ILE A 684     -10.806  31.522   8.776  1.00 14.03           N  
ANISOU 1208  N   ILE A 684     1999   1374   1956    525    338    670       N  
ATOM   1209  CA  ILE A 684     -12.245  31.555   8.554  1.00 14.01           C  
ANISOU 1209  CA  ILE A 684     2013   1421   1890    573    276    679       C  
ATOM   1210  C   ILE A 684     -12.876  32.346   9.695  1.00 13.11           C  
ANISOU 1210  C   ILE A 684     1866   1256   1858    574    250    650       C  
ATOM   1211  O   ILE A 684     -12.662  32.025  10.863  1.00 12.07           O  
ANISOU 1211  O   ILE A 684     1699   1112   1775    533    232    578       O  
ATOM   1212  CB  ILE A 684     -12.834  30.124   8.495  1.00 13.97           C  
ANISOU 1212  CB  ILE A 684     2002   1507   1799    569    213    619       C  
ATOM   1213  CG1 ILE A 684     -12.301  29.384   7.258  1.00 15.32           C  
ANISOU 1213  CG1 ILE A 684     2216   1727   1878    579    240    640       C  
ATOM   1214  CG2 ILE A 684     -14.370  30.149   8.528  1.00 15.01           C  
ANISOU 1214  CG2 ILE A 684     2124   1684   1894    609    140    616       C  
ATOM   1215  CD1 ILE A 684     -12.594  27.910   7.248  0.50 13.21           C  
ANISOU 1215  CD1 ILE A 684     1943   1528   1549    562    189    569       C  
ATOM   1216  N   SER A 685     -13.658  33.371   9.352  1.00 13.06           N  
ANISOU 1216  N   SER A 685     1876   1223   1862    626    248    708       N  
ATOM   1217  CA  SER A 685     -14.151  34.338  10.352  1.00 12.85           C  
ANISOU 1217  CA  SER A 685     1826   1130   1927    634    243    685       C  
ATOM   1218  C   SER A 685     -14.790  33.719  11.588  1.00 12.32           C  
ANISOU 1218  C   SER A 685     1719   1097   1866    615    192    594       C  
ATOM   1219  O   SER A 685     -14.385  34.038  12.711  1.00 12.30           O  
ANISOU 1219  O   SER A 685     1698   1043   1933    582    203    536       O  
ATOM   1220  CB  SER A 685     -15.092  35.363   9.721  1.00 14.28           C  
ANISOU 1220  CB  SER A 685     2027   1288   2112    707    240    764       C  
ATOM   1221  OG ASER A 685     -16.293  34.760   9.280  0.50 14.32           O  
ANISOU 1221  OG ASER A 685     2025   1383   2032    750    175    770       O  
ATOM   1222  OG BSER A 685     -14.455  36.015   8.640  0.50 14.55           O  
ANISOU 1222  OG BSER A 685     2103   1282   2143    725    297    861       O  
ATOM   1223  N   THR A 686     -15.768  32.832  11.396  1.00 11.77           N  
ANISOU 1223  N   THR A 686     1636   1114   1723    635    138    580       N  
ATOM   1224  CA  THR A 686     -16.443  32.175  12.527  1.00 12.23           C  
ANISOU 1224  CA  THR A 686     1653   1209   1785    618    100    505       C  
ATOM   1225  C   THR A 686     -15.413  31.512  13.433  1.00 11.08           C  
ANISOU 1225  C   THR A 686     1498   1055   1658    553    111    440       C  
ATOM   1226  O   THR A 686     -15.467  31.658  14.649  1.00 11.59           O  
ANISOU 1226  O   THR A 686     1544   1099   1762    535    109    385       O  
ATOM   1227  CB  THR A 686     -17.494  31.130  12.054  1.00 12.06           C  
ANISOU 1227  CB  THR A 686     1611   1282   1690    634     41    502       C  
ATOM   1228  OG1 THR A 686     -18.557  31.820  11.389  1.00 15.72           O  
ANISOU 1228  OG1 THR A 686     2071   1755   2146    699     18    557       O  
ATOM   1229  CG2 THR A 686     -18.091  30.336  13.227  1.00 13.11           C  
ANISOU 1229  CG2 THR A 686     1699   1450   1833    608     15    433       C  
ATOM   1230  N   TYR A 687     -14.463  30.804  12.833  1.00 10.81           N  
ANISOU 1230  N   TYR A 687     1478   1038   1593    522    123    449       N  
ATOM   1231  CA  TYR A 687     -13.479  30.077  13.628  1.00  9.51           C  
ANISOU 1231  CA  TYR A 687     1297    869   1448    466    125    395       C  
ATOM   1232  C   TYR A 687     -12.444  30.994  14.282  1.00  9.56           C  
ANISOU 1232  C   TYR A 687     1300    794   1539    438    159    381       C  
ATOM   1233  O   TYR A 687     -11.969  30.694  15.386  1.00  9.10           O  
ANISOU 1233  O   TYR A 687     1222    729   1508    400    143    323       O  
ATOM   1234  CB  TYR A 687     -12.815  28.969  12.804  1.00  9.63           C  
ANISOU 1234  CB  TYR A 687     1321    926   1412    448    130    403       C  
ATOM   1235  CG  TYR A 687     -13.784  28.053  12.080  1.00  9.56           C  
ANISOU 1235  CG  TYR A 687     1319    992   1322    472     89    406       C  
ATOM   1236  CD1 TYR A 687     -15.046  27.768  12.613  1.00  9.72           C  
ANISOU 1236  CD1 TYR A 687     1313   1049   1331    484     42    381       C  
ATOM   1237  CD2 TYR A 687     -13.433  27.461  10.864  1.00  9.64           C  
ANISOU 1237  CD2 TYR A 687     1360   1034   1270    480    100    428       C  
ATOM   1238  CE1 TYR A 687     -15.936  26.946  11.952  1.00 10.48           C  
ANISOU 1238  CE1 TYR A 687     1406   1208   1369    498     -3    379       C  
ATOM   1239  CE2 TYR A 687     -14.322  26.618  10.195  1.00 10.07           C  
ANISOU 1239  CE2 TYR A 687     1421   1154   1250    497     51    418       C  
ATOM   1240  CZ  TYR A 687     -15.571  26.370  10.748  1.00 10.34           C  
ANISOU 1240  CZ  TYR A 687     1422   1220   1288    503     -5    393       C  
ATOM   1241  OH  TYR A 687     -16.458  25.551  10.102  1.00 11.46           O  
ANISOU 1241  OH  TYR A 687     1561   1421   1371    513    -60    379       O  
ATOM   1242  N   GLU A 688     -12.096  32.097  13.616  1.00 10.28           N  
ANISOU 1242  N   GLU A 688     1410    822   1673    454    202    435       N  
ATOM   1243  CA  GLU A 688     -11.266  33.135  14.234  1.00 10.76           C  
ANISOU 1243  CA  GLU A 688     1463    791   1834    425    230    419       C  
ATOM   1244  C   GLU A 688     -11.939  33.689  15.494  1.00 10.66           C  
ANISOU 1244  C   GLU A 688     1444    752   1854    431    203    355       C  
ATOM   1245  O   GLU A 688     -11.279  33.889  16.514  1.00 10.77           O  
ANISOU 1245  O   GLU A 688     1445    729   1919    391    192    294       O  
ATOM   1246  CB  GLU A 688     -11.005  34.298  13.266  1.00 12.14           C  
ANISOU 1246  CB  GLU A 688     1661    893   2057    448    286    500       C  
ATOM   1247  CG  GLU A 688     -10.032  34.003  12.151  1.00 14.24           C  
ANISOU 1247  CG  GLU A 688     1936   1164   2310    436    337    562       C  
ATOM   1248  CD  GLU A 688      -9.902  35.158  11.168  1.00 17.25           C  
ANISOU 1248  CD  GLU A 688     2347   1479   2730    465    399    658       C  
ATOM   1249  OE1 GLU A 688     -10.867  35.942  11.022  1.00 20.78           O  
ANISOU 1249  OE1 GLU A 688     2815   1903   3178    515    391    692       O  
ATOM   1250  OE2 GLU A 688      -8.834  35.270  10.526  1.00 20.73           O  
ANISOU 1250  OE2 GLU A 688     2786   1888   3203    442    462    707       O  
ATOM   1251  N   LYS A 689     -13.248  33.947  15.413  1.00 10.03           N  
ANISOU 1251  N   LYS A 689     1372    695   1744    485    191    369       N  
ATOM   1252  CA  LYS A 689     -13.996  34.422  16.567  1.00  9.61           C  
ANISOU 1252  CA  LYS A 689     1313    625   1714    501    177    309       C  
ATOM   1253  C   LYS A 689     -13.974  33.363  17.665  1.00  9.36           C  
ANISOU 1253  C   LYS A 689     1264    657   1637    467    142    237       C  
ATOM   1254  O   LYS A 689     -13.748  33.676  18.836  1.00  8.97           O  
ANISOU 1254  O   LYS A 689     1216    580   1611    448    135    169       O  
ATOM   1255  CB  LYS A 689     -15.440  34.746  16.173  1.00  9.71           C  
ANISOU 1255  CB  LYS A 689     1323    660   1706    569    173    346       C  
ATOM   1256  CG  LYS A 689     -16.344  35.086  17.357  1.00  9.52           C  
ANISOU 1256  CG  LYS A 689     1288    633   1698    594    169    283       C  
ATOM   1257  CD  LYS A 689     -17.737  35.468  16.887  1.00  9.01           C  
ANISOU 1257  CD  LYS A 689     1207    585   1632    666    169    328       C  
ATOM   1258  CE  LYS A 689     -18.627  35.825  18.061  1.00  9.92           C  
ANISOU 1258  CE  LYS A 689     1307    695   1769    696    180    265       C  
ATOM   1259  NZ  LYS A 689     -20.020  36.142  17.617  1.00 11.60           N  
ANISOU 1259  NZ  LYS A 689     1488    927   1992    770    179    312       N  
ATOM   1260  N   MET A 690     -14.202  32.117  17.275  1.00  8.94           N  
ANISOU 1260  N   MET A 690     1198    684   1515    461    119    254       N  
ATOM   1261  CA  MET A 690     -14.221  31.014  18.238  1.00  9.41           C  
ANISOU 1261  CA  MET A 690     1241    802   1531    432     90    203       C  
ATOM   1262  C   MET A 690     -12.877  30.872  18.936  1.00  9.31           C  
ANISOU 1262  C   MET A 690     1229    763   1547    380     81    162       C  
ATOM   1263  O   MET A 690     -12.823  30.666  20.144  1.00  9.79           O  
ANISOU 1263  O   MET A 690     1288    837   1594    363     60    106       O  
ATOM   1264  CB  MET A 690     -14.634  29.710  17.561  1.00  9.58           C  
ANISOU 1264  CB  MET A 690     1249    900   1492    431     69    230       C  
ATOM   1265  CG  MET A 690     -16.119  29.686  17.212  1.00  9.88           C  
ANISOU 1265  CG  MET A 690     1272    978   1504    477     58    253       C  
ATOM   1266  SD  MET A 690     -16.633  28.231  16.269  1.00 10.45           S  
ANISOU 1266  SD  MET A 690     1328   1129   1515    472     23    277       S  
ATOM   1267  CE  MET A 690     -16.539  26.950  17.529  1.00 10.61           C  
ANISOU 1267  CE  MET A 690     1325   1186   1520    427      8    228       C  
ATOM   1268  N   TRP A 691     -11.792  31.007  18.181  1.00  9.39           N  
ANISOU 1268  N   TRP A 691     1237    736   1594    356     98    192       N  
ATOM   1269  CA  TRP A 691     -10.462  30.999  18.793  1.00  9.54           C  
ANISOU 1269  CA  TRP A 691     1242    722   1660    306     86    156       C  
ATOM   1270  C   TRP A 691     -10.280  32.155  19.772  1.00 10.00           C  
ANISOU 1270  C   TRP A 691     1309    714   1775    296     79    100       C  
ATOM   1271  O   TRP A 691      -9.789  31.949  20.883  1.00  9.64           O  
ANISOU 1271  O   TRP A 691     1257    676   1728    266     41     39       O  
ATOM   1272  CB  TRP A 691      -9.330  31.004  17.766  1.00  9.66           C  
ANISOU 1272  CB  TRP A 691     1244    705   1720    285    118    204       C  
ATOM   1273  CG  TRP A 691      -8.003  31.077  18.469  1.00  9.54           C  
ANISOU 1273  CG  TRP A 691     1199    653   1773    233    100    165       C  
ATOM   1274  CD1 TRP A 691      -7.073  32.072  18.373  1.00 12.07           C  
ANISOU 1274  CD1 TRP A 691     1503    891   2191    204    121    166       C  
ATOM   1275  CD2 TRP A 691      -7.491  30.135  19.428  1.00 10.02           C  
ANISOU 1275  CD2 TRP A 691     1238    757   1814    205     49    120       C  
ATOM   1276  NE1 TRP A 691      -5.999  31.797  19.197  1.00 12.06           N  
ANISOU 1276  NE1 TRP A 691     1465    883   2236    157     81    119       N  
ATOM   1277  CE2 TRP A 691      -6.231  30.616  19.853  1.00 11.14           C  
ANISOU 1277  CE2 TRP A 691     1346    844   2042    160     34     93       C  
ATOM   1278  CE3 TRP A 691      -7.971  28.930  19.958  1.00  9.16           C  
ANISOU 1278  CE3 TRP A 691     1131    723   1628    212     15    105       C  
ATOM   1279  CZ2 TRP A 691      -5.442  29.933  20.786  1.00 11.87           C  
ANISOU 1279  CZ2 TRP A 691     1409    963   2139    129    -23     52       C  
ATOM   1280  CZ3 TRP A 691      -7.193  28.253  20.892  1.00  9.08           C  
ANISOU 1280  CZ3 TRP A 691     1097    733   1619    183    -32     72       C  
ATOM   1281  CH2 TRP A 691      -5.938  28.755  21.290  1.00 10.21           C  
ANISOU 1281  CH2 TRP A 691     1208    828   1842    144    -55     46       C  
ATOM   1282  N   ALA A 692     -10.664  33.365  19.367  1.00  9.95           N  
ANISOU 1282  N   ALA A 692     1319    641   1819    322    112    118       N  
ATOM   1283  CA  ALA A 692     -10.551  34.506  20.256  1.00 10.75           C  
ANISOU 1283  CA  ALA A 692     1433    668   1982    315    108     55       C  
ATOM   1284  C   ALA A 692     -11.313  34.245  21.550  1.00 10.93           C  
ANISOU 1284  C   ALA A 692     1472    739   1941    331     78    -18       C  
ATOM   1285  O   ALA A 692     -10.828  34.583  22.627  1.00 11.79           O  
ANISOU 1285  O   ALA A 692     1591    823   2065    304     49    -96       O  
ATOM   1286  CB  ALA A 692     -11.050  35.776  19.576  1.00 10.87           C  
ANISOU 1286  CB  ALA A 692     1467    602   2061    353    154     95       C  
ATOM   1287  N   PHE A 693     -12.496  33.641  21.441  1.00 10.57           N  
ANISOU 1287  N   PHE A 693     1428    763   1824    373     86      7       N  
ATOM   1288  CA  PHE A 693     -13.284  33.305  22.624  1.00 11.32           C  
ANISOU 1288  CA  PHE A 693     1534    912   1856    391     73    -49       C  
ATOM   1289  C   PHE A 693     -12.595  32.266  23.513  1.00 11.55           C  
ANISOU 1289  C   PHE A 693     1560    999   1830    349     29    -85       C  
ATOM   1290  O   PHE A 693     -12.420  32.489  24.709  1.00 11.24           O  
ANISOU 1290  O   PHE A 693     1542    961   1768    340      8   -156       O  
ATOM   1291  CB  PHE A 693     -14.685  32.825  22.234  1.00 10.92           C  
ANISOU 1291  CB  PHE A 693     1470    922   1757    439     93     -6       C  
ATOM   1292  CG  PHE A 693     -15.543  32.460  23.416  1.00 12.98           C  
ANISOU 1292  CG  PHE A 693     1736   1238   1958    459     97    -52       C  
ATOM   1293  CD1 PHE A 693     -16.251  33.439  24.106  1.00 16.30           C  
ANISOU 1293  CD1 PHE A 693     2175   1625   2392    501    128   -100       C  
ATOM   1294  CD2 PHE A 693     -15.620  31.132  23.846  1.00 15.36           C  
ANISOU 1294  CD2 PHE A 693     2024   1621   2190    439     77    -44       C  
ATOM   1295  CE1 PHE A 693     -17.043  33.096  25.213  1.00 17.72           C  
ANISOU 1295  CE1 PHE A 693     2361   1861   2509    523    145   -141       C  
ATOM   1296  CE2 PHE A 693     -16.408  30.783  24.938  1.00 17.30           C  
ANISOU 1296  CE2 PHE A 693     2275   1919   2378    457     93    -75       C  
ATOM   1297  CZ  PHE A 693     -17.124  31.764  25.615  1.00 17.46           C  
ANISOU 1297  CZ  PHE A 693     2315   1915   2405    500    130   -123       C  
ATOM   1298  N   MET A 694     -12.201  31.145  22.920  1.00 11.57           N  
ANISOU 1298  N   MET A 694     1537   1048   1810    328     15    -36       N  
ATOM   1299  CA  MET A 694     -11.482  30.096  23.660  1.00 12.88           C  
ANISOU 1299  CA  MET A 694     1696   1263   1935    293    -27    -55       C  
ATOM   1300  C   MET A 694     -10.219  30.609  24.326  1.00 14.09           C  
ANISOU 1300  C   MET A 694     1850   1371   2131    253    -65   -108       C  
ATOM   1301  O   MET A 694      -9.897  30.201  25.451  1.00 15.47           O  
ANISOU 1301  O   MET A 694     2035   1582   2259    238   -109   -152       O  
ATOM   1302  CB  MET A 694     -11.053  28.981  22.722  1.00 12.71           C  
ANISOU 1302  CB  MET A 694     1646   1272   1911    277    -29      5       C  
ATOM   1303  CG  MET A 694     -12.154  28.162  22.163  1.00 13.00           C  
ANISOU 1303  CG  MET A 694     1677   1362   1901    303    -12     48       C  
ATOM   1304  SD  MET A 694     -11.402  26.839  21.191  1.00 12.85           S  
ANISOU 1304  SD  MET A 694     1633   1367   1882    279    -20     94       S  
ATOM   1305  CE  MET A 694     -12.744  26.616  20.029  1.00 14.46           C  
ANISOU 1305  CE  MET A 694     1837   1600   2059    315      3    138       C  
ATOM   1306  N   SER A 695      -9.484  31.450  23.606  1.00 15.50           N  
ANISOU 1306  N   SER A 695     2015   1474   2400    234    -52    -99       N  
ATOM   1307  CA  SER A 695      -8.231  32.023  24.091  1.00 17.39           C  
ANISOU 1307  CA  SER A 695     2241   1659   2708    188    -90   -148       C  
ATOM   1308  C   SER A 695      -8.429  33.030  25.223  1.00 18.67           C  
ANISOU 1308  C   SER A 695     2439   1783   2870    190   -114   -239       C  
ATOM   1309  O   SER A 695      -7.587  33.144  26.112  1.00 19.37           O  
ANISOU 1309  O   SER A 695     2526   1865   2970    154   -173   -304       O  
ATOM   1310  CB  SER A 695      -7.483  32.690  22.928  1.00 17.36           C  
ANISOU 1310  CB  SER A 695     2209   1576   2812    167    -53   -102       C  
ATOM   1311  OG  SER A 695      -6.215  33.171  23.347  1.00 21.32           O  
ANISOU 1311  OG  SER A 695     2681   2022   3399    115    -91   -145       O  
ATOM   1312  N   SER A 696      -9.528  33.779  25.171  1.00 19.40           N  
ANISOU 1312  N   SER A 696     2564   1851   2956    234    -69   -249       N  
ATOM   1313  CA  SER A 696      -9.833  34.812  26.162  1.00 22.02           C  
ANISOU 1313  CA  SER A 696     2937   2138   3292    246    -77   -342       C  
ATOM   1314  C   SER A 696     -10.167  34.196  27.501  1.00 23.88           C  
ANISOU 1314  C   SER A 696     3205   2457   3411    257   -113   -402       C  
ATOM   1315  O   SER A 696      -9.861  34.768  28.559  1.00 25.53           O  
ANISOU 1315  O   SER A 696     3449   2646   3606    245   -151   -498       O  
ATOM   1316  CB  SER A 696     -11.051  35.611  25.722  1.00 21.52           C  
ANISOU 1316  CB  SER A 696     2895   2036   3246    303    -11   -324       C  
ATOM   1317  OG  SER A 696     -12.231  34.872  26.010  1.00 20.80           O  
ANISOU 1317  OG  SER A 696     2813   2033   3056    349     11   -305       O  
ATOM   1318  N   ARG A 697     -10.898  33.069  27.447  1.00 25.37           N  
ANISOU 1318  N   ARG A 697     3388   2736   3514    283    -95   -346       N  
ATOM   1319  CA  ARG A 697     -11.199  32.322  28.654  1.00 27.24           C  
ANISOU 1319  CA  ARG A 697     3654   3059   3636    293   -119   -379       C  
ATOM   1320  C   ARG A 697     -10.457  31.041  28.624  1.00 27.53           C  
ANISOU 1320  C   ARG A 697     3662   3156   3644    261   -164   -330       C  
ATOM   1321  O   ARG A 697     -10.912  29.990  29.049  1.00 27.70           O  
ANISOU 1321  O   ARG A 697     3688   3255   3581    275   -162   -297       O  
ATOM   1322  CB  ARG A 697     -12.678  32.030  28.845  1.00 27.41           C  
ANISOU 1322  CB  ARG A 697     3691   3135   3588    348    -58   -356       C  
ATOM   1323  CG  ARG A 697     -13.526  31.786  27.622  1.00 27.74           C  
ANISOU 1323  CG  ARG A 697     3695   3177   3668    373     -7   -272       C  
ATOM   1324  CD  ARG A 697     -14.991  31.869  28.053  1.00 31.01           C  
ANISOU 1324  CD  ARG A 697     4120   3629   4034    429     51   -276       C  
ATOM   1325  NE  ARG A 697     -15.142  32.223  29.470  1.00 33.20           N  
ANISOU 1325  NE  ARG A 697     4449   3927   4240    446     55   -359       N  
ATOM   1326  CZ  ARG A 697     -14.907  33.427  29.998  1.00 35.62           C  
ANISOU 1326  CZ  ARG A 697     4795   4168   4570    455     53   -448       C  
ATOM   1327  NH1 ARG A 697     -15.068  33.611  31.303  1.00 37.35           N  
ANISOU 1327  NH1 ARG A 697     5069   4420   4703    473     55   -528       N  
ATOM   1328  NH2 ARG A 697     -14.498  34.444  29.237  1.00 36.80           N  
ANISOU 1328  NH2 ARG A 697     4936   4219   4827    446     51   -458       N  
ATOM   1329  N   GLN A 698      -9.261  30.870  28.258  1.00 27.96           N  
ANISOU 1329  N   GLN A 698     3681   3184   3758    218   -208   -318       N  
ATOM   1330  CA  GLN A 698      -8.388  29.687  28.003  1.00 27.87           C  
ANISOU 1330  CA  GLN A 698     3628   3211   3749    190   -246   -264       C  
ATOM   1331  C   GLN A 698      -8.297  28.952  29.318  1.00 28.01           C  
ANISOU 1331  C   GLN A 698     3674   3304   3665    193   -299   -290       C  
ATOM   1332  O   GLN A 698      -8.449  27.705  29.408  1.00 26.63           O  
ANISOU 1332  O   GLN A 698     3489   3192   3436    200   -302   -232       O  
ATOM   1333  CB  GLN A 698      -7.008  30.163  27.562  1.00 28.52           C  
ANISOU 1333  CB  GLN A 698     3667   3227   3941    143   -282   -276       C  
ATOM   1334  CG  GLN A 698      -6.390  31.195  28.527  1.00 30.53           C  
ANISOU 1334  CG  GLN A 698     3940   3439   4220    117   -341   -375       C  
ATOM   1335  CD  GLN A 698      -5.563  30.532  29.630  1.00 32.19           C  
ANISOU 1335  CD  GLN A 698     4147   3707   4376     96   -435   -408       C  
ATOM   1336  OE1 GLN A 698      -5.227  29.336  29.540  1.00 31.57           O  
ANISOU 1336  OE1 GLN A 698     4040   3685   4272     96   -453   -347       O  
ATOM   1337  NE2 GLN A 698      -5.247  31.297  30.679  1.00 34.50           N  
ANISOU 1337  NE2 GLN A 698     4472   3985   4650     82   -498   -507       N  
ATOM   1338  N   GLN A 699      -7.893  29.709  30.375  1.00 29.37           N  
ANISOU 1338  N   GLN A 699     3880   3466   3813    183   -352   -378       N  
ATOM   1339  CA  GLN A 699      -7.687  29.280  31.768  1.00 30.34           C  
ANISOU 1339  CA  GLN A 699     4044   3659   3826    187   -416   -420       C  
ATOM   1340  C   GLN A 699      -8.820  28.354  32.016  1.00 29.67           C  
ANISOU 1340  C   GLN A 699     3984   3648   3641    228   -361   -362       C  
ATOM   1341  O   GLN A 699      -8.683  27.287  32.635  1.00 30.10           O  
ANISOU 1341  O   GLN A 699     4045   3772   3618    233   -391   -322       O  
ATOM   1342  CB  GLN A 699      -7.811  30.505  32.692  1.00 31.71           C  
ANISOU 1342  CB  GLN A 699     4275   3805   3967    193   -438   -535       C  
ATOM   1343  CG  GLN A 699      -7.388  31.883  32.058  1.00 32.95           C  
ANISOU 1343  CG  GLN A 699     4413   3847   4259    165   -433   -592       C  
ATOM   1344  CD  GLN A 699      -8.521  32.543  31.225  1.00 32.17           C  
ANISOU 1344  CD  GLN A 699     4322   3698   4205    201   -330   -568       C  
ATOM   1345  OE1 GLN A 699      -9.695  32.268  31.432  1.00 32.36           O  
ANISOU 1345  OE1 GLN A 699     4377   3770   4149    249   -271   -549       O  
ATOM   1346  NE2 GLN A 699      -8.153  33.445  30.303  1.00 31.80           N  
ANISOU 1346  NE2 GLN A 699     4243   3550   4289    179   -310   -567       N  
ATOM   1347  N   THR A 700      -9.957  28.778  31.451  1.00 28.91           N  
ANISOU 1347  N   THR A 700     3894   3531   3560    257   -277   -350       N  
ATOM   1348  CA  THR A 700     -11.196  28.116  31.698  1.00 27.71           C  
ANISOU 1348  CA  THR A 700     3758   3440   3329    296   -215   -305       C  
ATOM   1349  C   THR A 700     -11.625  27.244  30.513  1.00 25.17           C  
ANISOU 1349  C   THR A 700     3385   3121   3059    294   -173   -212       C  
ATOM   1350  O   THR A 700     -11.714  26.039  30.649  1.00 25.74           O  
ANISOU 1350  O   THR A 700     3445   3243   3092    292   -175   -152       O  
ATOM   1351  CB  THR A 700     -12.284  29.119  32.196  1.00 28.67           C  
ANISOU 1351  CB  THR A 700     3926   3553   3414    339   -154   -366       C  
ATOM   1352  OG1 THR A 700     -13.531  28.882  31.514  1.00 29.36           O  
ANISOU 1352  OG1 THR A 700     3986   3649   3519    370    -73   -307       O  
ATOM   1353  CG2 THR A 700     -11.852  30.564  31.959  1.00 29.49           C  
ANISOU 1353  CG2 THR A 700     4040   3567   3599    329   -168   -447       C  
ATOM   1354  N   ALA A 701     -11.882  27.832  29.265  1.00 22.54           N  
ANISOU 1354  N   ALA A 701     3020   2728   2816    296   -136   -195       N  
ATOM   1355  CA  ALA A 701     -12.443  27.105  28.108  1.00 19.00           C  
ANISOU 1355  CA  ALA A 701     2531   2286   2403    300    -99   -119       C  
ATOM   1356  C   ALA A 701     -11.663  25.891  27.578  1.00 17.15           C  
ANISOU 1356  C   ALA A 701     2263   2066   2189    270   -130    -63       C  
ATOM   1357  O   ALA A 701     -12.251  24.985  26.977  1.00 16.23           O  
ANISOU 1357  O   ALA A 701     2123   1973   2072    275   -105     -9       O  
ATOM   1358  CB  ALA A 701     -12.733  28.071  26.974  1.00 18.96           C  
ANISOU 1358  CB  ALA A 701     2511   2219   2475    311    -66   -115       C  
ATOM   1359  N   LEU A 702     -10.349  25.887  27.758  1.00 15.17           N  
ANISOU 1359  N   LEU A 702     2003   1795   1965    241   -184    -80       N  
ATOM   1360  CA  LEU A 702      -9.530  24.778  27.263  1.00 14.15           C  
ANISOU 1360  CA  LEU A 702     1838   1673   1867    219   -209    -31       C  
ATOM   1361  C   LEU A 702      -9.304  23.775  28.371  1.00 14.44           C  
ANISOU 1361  C   LEU A 702     1886   1765   1836    219   -249    -15       C  
ATOM   1362  O   LEU A 702      -8.797  24.129  29.440  1.00 16.88           O  
ANISOU 1362  O   LEU A 702     2220   2090   2104    215   -298    -57       O  
ATOM   1363  CB  LEU A 702      -8.187  25.269  26.716  1.00 13.70           C  
ANISOU 1363  CB  LEU A 702     1749   1562   1896    190   -238    -45       C  
ATOM   1364  CG  LEU A 702      -8.241  26.326  25.607  1.00 12.84           C  
ANISOU 1364  CG  LEU A 702     1630   1390   1859    189   -196    -49       C  
ATOM   1365  CD1 LEU A 702      -6.842  26.716  25.159  1.00 13.60           C  
ANISOU 1365  CD1 LEU A 702     1688   1434   2047    155   -217    -54       C  
ATOM   1366  CD2 LEU A 702      -9.087  25.857  24.424  1.00 11.99           C  
ANISOU 1366  CD2 LEU A 702     1516   1291   1750    209   -141      5       C  
ATOM   1367  N   VAL A 703      -9.673  22.526  28.111  1.00 11.94           N  
ANISOU 1367  N   VAL A 703     1554   1475   1508    223   -230     45       N  
ATOM   1368  CA  VAL A 703      -9.665  21.479  29.140  1.00 11.48           C  
ANISOU 1368  CA  VAL A 703     1510   1466   1384    228   -255     80       C  
ATOM   1369  C   VAL A 703      -8.452  20.553  28.996  1.00 11.51           C  
ANISOU 1369  C   VAL A 703     1480   1459   1433    213   -304    115       C  
ATOM   1370  O   VAL A 703      -7.817  20.501  27.935  1.00 11.17           O  
ANISOU 1370  O   VAL A 703     1398   1374   1473    200   -300    121       O  
ATOM   1371  CB  VAL A 703     -10.981  20.672  29.118  1.00 10.60           C  
ANISOU 1371  CB  VAL A 703     1403   1385   1240    243   -197    128       C  
ATOM   1372  CG1 VAL A 703     -12.173  21.577  29.464  1.00 11.72           C  
ANISOU 1372  CG1 VAL A 703     1572   1544   1337    265   -148     95       C  
ATOM   1373  CG2 VAL A 703     -11.178  20.019  27.764  1.00 10.50           C  
ANISOU 1373  CG2 VAL A 703     1350   1340   1299    232   -170    162       C  
ATOM   1374  N   ARG A 704      -8.129  19.823  30.059  1.00 11.85           N  
ANISOU 1374  N   ARG A 704     1539   1543   1421    220   -346    143       N  
ATOM   1375  CA  ARG A 704      -6.919  18.994  30.086  1.00 12.34           C  
ANISOU 1375  CA  ARG A 704     1565   1595   1528    214   -402    178       C  
ATOM   1376  C   ARG A 704      -6.976  17.799  29.130  1.00 11.69           C  
ANISOU 1376  C   ARG A 704     1447   1483   1511    213   -365    236       C  
ATOM   1377  O   ARG A 704      -5.967  17.424  28.508  1.00 11.74           O  
ANISOU 1377  O   ARG A 704     1409   1455   1598    206   -384    247       O  
ATOM   1378  CB  ARG A 704      -6.658  18.500  31.516  1.00 13.83           C  
ANISOU 1378  CB  ARG A 704     1786   1840   1629    230   -459    203       C  
ATOM   1379  CG  ARG A 704      -5.440  17.623  31.666  1.00 17.82           C  
ANISOU 1379  CG  ARG A 704     2251   2338   2180    231   -525    248       C  
ATOM   1380  CD  ARG A 704      -5.191  17.287  33.127  1.00 22.95           C  
ANISOU 1380  CD  ARG A 704     2941   3051   2727    252   -593    274       C  
ATOM   1381  NE  ARG A 704      -4.847  18.475  33.909  1.00 28.48           N  
ANISOU 1381  NE  ARG A 704     3673   3781   3368    247   -655    193       N  
ATOM   1382  CZ  ARG A 704      -3.619  18.982  34.019  1.00 30.81           C  
ANISOU 1382  CZ  ARG A 704     3930   4065   3713    231   -744    150       C  
ATOM   1383  NH1 ARG A 704      -2.591  18.407  33.396  1.00 32.06           N  
ANISOU 1383  NH1 ARG A 704     4013   4185   3984    223   -774    185       N  
ATOM   1384  NH2 ARG A 704      -3.418  20.069  34.754  1.00 32.73           N  
ANISOU 1384  NH2 ARG A 704     4207   4330   3900    222   -801     66       N  
ATOM   1385  N   ASN A 705      -8.143  17.175  29.065  1.00 10.41           N  
ANISOU 1385  N   ASN A 705     1302   1333   1319    220   -311    271       N  
ATOM   1386  CA  ASN A 705      -8.328  15.929  28.331  1.00  9.97           C  
ANISOU 1386  CA  ASN A 705     1222   1249   1319    217   -281    320       C  
ATOM   1387  C   ASN A 705      -9.800  15.742  28.012  1.00 10.04           C  
ANISOU 1387  C   ASN A 705     1241   1264   1309    214   -219    330       C  
ATOM   1388  O   ASN A 705     -10.634  16.536  28.469  1.00  9.81           O  
ANISOU 1388  O   ASN A 705     1238   1268   1223    221   -197    307       O  
ATOM   1389  CB  ASN A 705      -7.754  14.728  29.120  1.00 10.83           C  
ANISOU 1389  CB  ASN A 705     1327   1365   1424    228   -317    385       C  
ATOM   1390  CG  ASN A 705      -8.301  14.620  30.541  1.00 11.33           C  
ANISOU 1390  CG  ASN A 705     1436   1485   1383    242   -326    419       C  
ATOM   1391  OD1 ASN A 705      -9.456  14.910  30.799  1.00 11.27           O  
ANISOU 1391  OD1 ASN A 705     1456   1504   1323    243   -277    415       O  
ATOM   1392  ND2 ASN A 705      -7.460  14.172  31.462  1.00 13.74           N  
ANISOU 1392  ND2 ASN A 705     1749   1812   1661    258   -387    457       N  
ATOM   1393  N   SER A 706     -10.117  14.708  27.237  1.00  9.54           N  
ANISOU 1393  N   SER A 706     1156   1169   1301    206   -192    360       N  
ATOM   1394  CA  SER A 706     -11.488  14.439  26.828  1.00 10.17           C  
ANISOU 1394  CA  SER A 706     1232   1251   1382    197   -144    367       C  
ATOM   1395  C   SER A 706     -12.446  14.280  28.001  1.00 10.92           C  
ANISOU 1395  C   SER A 706     1347   1389   1414    203   -117    404       C  
ATOM   1396  O   SER A 706     -13.558  14.795  27.951  1.00 10.91           O  
ANISOU 1396  O   SER A 706     1344   1408   1393    203    -79    390       O  
ATOM   1397  CB  SER A 706     -11.554  13.191  25.957  1.00 10.34           C  
ANISOU 1397  CB  SER A 706     1228   1225   1476    183   -132    388       C  
ATOM   1398  OG  SER A 706     -10.688  13.327  24.848  1.00 12.50           O  
ANISOU 1398  OG  SER A 706     1489   1464   1798    184   -143    352       O  
ATOM   1399  N   ASP A 707     -12.025  13.570  29.047  1.00 11.80           N  
ANISOU 1399  N   ASP A 707     1475   1514   1494    211   -134    458       N  
ATOM   1400  CA  ASP A 707     -12.911  13.333  30.188  1.00 12.45           C  
ANISOU 1400  CA  ASP A 707     1582   1641   1509    219    -98    506       C  
ATOM   1401  C   ASP A 707     -13.293  14.606  30.919  1.00 12.24           C  
ANISOU 1401  C   ASP A 707     1590   1669   1392    238    -86    463       C  
ATOM   1402  O   ASP A 707     -14.457  14.774  31.292  1.00 12.24           O  
ANISOU 1402  O   ASP A 707     1595   1698   1359    243    -27    474       O  
ATOM   1403  CB  ASP A 707     -12.319  12.312  31.148  1.00 13.52           C  
ANISOU 1403  CB  ASP A 707     1735   1781   1620    229   -120    583       C  
ATOM   1404  CG  ASP A 707     -12.496  10.893  30.661  1.00 15.44           C  
ANISOU 1404  CG  ASP A 707     1948   1967   1953    211    -99    643       C  
ATOM   1405  OD1 ASP A 707     -13.499  10.611  29.964  1.00 18.75           O  
ANISOU 1405  OD1 ASP A 707     2337   2360   2427    188    -53    636       O  
ATOM   1406  OD2 ASP A 707     -11.643  10.057  30.992  1.00 18.40           O  
ANISOU 1406  OD2 ASP A 707     2325   2319   2349    222   -133    694       O  
ATOM   1407  N   GLU A 708     -12.337  15.522  31.091  1.00 11.58           N  
ANISOU 1407  N   GLU A 708     1527   1593   1279    248   -140    409       N  
ATOM   1408  CA  GLU A 708     -12.679  16.814  31.676  1.00 11.81           C  
ANISOU 1408  CA  GLU A 708     1592   1661   1235    265   -130    350       C  
ATOM   1409  C   GLU A 708     -13.676  17.531  30.764  1.00 11.04           C  
ANISOU 1409  C   GLU A 708     1470   1545   1181    262    -79    311       C  
ATOM   1410  O   GLU A 708     -14.638  18.129  31.242  1.00 11.86           O  
ANISOU 1410  O   GLU A 708     1589   1679   1237    280    -31    295       O  
ATOM   1411  CB  GLU A 708     -11.455  17.702  31.926  1.00 12.23           C  
ANISOU 1411  CB  GLU A 708     1664   1713   1271    267   -203    290       C  
ATOM   1412  CG  GLU A 708     -11.831  18.980  32.691  1.00 14.78           C  
ANISOU 1412  CG  GLU A 708     2033   2070   1513    286   -194    223       C  
ATOM   1413  CD  GLU A 708     -10.735  20.028  32.770  1.00 17.92           C  
ANISOU 1413  CD  GLU A 708     2441   2451   1917    279   -264    147       C  
ATOM   1414  OE1 GLU A 708      -9.565  19.712  32.509  1.00 18.58           O  
ANISOU 1414  OE1 GLU A 708     2496   2511   2051    263   -328    154       O  
ATOM   1415  OE2 GLU A 708     -11.065  21.188  33.113  1.00 23.31           O  
ANISOU 1415  OE2 GLU A 708     3156   3138   2562    291   -253     77       O  
ATOM   1416  N   GLY A 709     -13.439  17.467  29.453  1.00 10.44           N  
ANISOU 1416  N   GLY A 709     1355   1421   1192    245    -90    298       N  
ATOM   1417  CA  GLY A 709     -14.328  18.116  28.487  1.00  9.25           C  
ANISOU 1417  CA  GLY A 709     1181   1254   1080    246    -54    269       C  
ATOM   1418  C   GLY A 709     -15.734  17.544  28.549  1.00  9.55           C  
ANISOU 1418  C   GLY A 709     1194   1311   1123    246      3    307       C  
ATOM   1419  O   GLY A 709     -16.726  18.283  28.620  1.00  9.85           O  
ANISOU 1419  O   GLY A 709     1226   1368   1148    263     43    287       O  
ATOM   1420  N   ILE A 710     -15.822  16.218  28.538  1.00  9.61           N  
ANISOU 1420  N   ILE A 710     1183   1309   1160    226      7    362       N  
ATOM   1421  CA  ILE A 710     -17.120  15.541  28.579  1.00 10.25           C  
ANISOU 1421  CA  ILE A 710     1228   1398   1267    216     60    404       C  
ATOM   1422  C   ILE A 710     -17.858  15.841  29.886  1.00 11.12           C  
ANISOU 1422  C   ILE A 710     1360   1562   1303    238    115    427       C  
ATOM   1423  O   ILE A 710     -19.062  16.102  29.868  1.00 11.61           O  
ANISOU 1423  O   ILE A 710     1391   1641   1379    244    169    429       O  
ATOM   1424  CB  ILE A 710     -16.989  14.018  28.332  1.00 10.81           C  
ANISOU 1424  CB  ILE A 710     1276   1433   1397    186     53    458       C  
ATOM   1425  CG1 ILE A 710     -16.469  13.754  26.916  1.00 11.29           C  
ANISOU 1425  CG1 ILE A 710     1316   1444   1529    168     12    424       C  
ATOM   1426  CG2 ILE A 710     -18.337  13.309  28.518  1.00 10.93           C  
ANISOU 1426  CG2 ILE A 710     1250   1453   1450    168    110    506       C  
ATOM   1427  CD1 ILE A 710     -15.805  12.377  26.758  1.00 13.44           C  
ANISOU 1427  CD1 ILE A 710     1583   1669   1854    148     -7    461       C  
ATOM   1428  N   GLN A 711     -17.148  15.796  31.014  1.00 11.75           N  
ANISOU 1428  N   GLN A 711     1493   1670   1302    253    102    444       N  
ATOM   1429  CA  GLN A 711     -17.754  16.178  32.298  1.00 12.74           C  
ANISOU 1429  CA  GLN A 711     1655   1854   1333    282    157    457       C  
ATOM   1430  C   GLN A 711     -18.270  17.615  32.277  1.00 12.69           C  
ANISOU 1430  C   GLN A 711     1657   1864   1299    310    182    383       C  
ATOM   1431  O   GLN A 711     -19.332  17.908  32.820  1.00 12.64           O  
ANISOU 1431  O   GLN A 711     1647   1893   1264    332    255    390       O  
ATOM   1432  CB  GLN A 711     -16.765  16.009  33.454  1.00 14.31           C  
ANISOU 1432  CB  GLN A 711     1919   2087   1433    298    120    476       C  
ATOM   1433  CG  GLN A 711     -16.515  14.568  33.858  1.00 17.77           C  
ANISOU 1433  CG  GLN A 711     2355   2518   1878    284    119    572       C  
ATOM   1434  CD  GLN A 711     -17.739  13.922  34.461  1.00 22.62           C  
ANISOU 1434  CD  GLN A 711     2958   3157   2481    285    213    648       C  
ATOM   1435  OE1 GLN A 711     -18.289  12.976  33.900  1.00 26.25           O  
ANISOU 1435  OE1 GLN A 711     3362   3575   3035    254    242    699       O  
ATOM   1436  NE2 GLN A 711     -18.199  14.454  35.589  1.00 24.10           N  
ANISOU 1436  NE2 GLN A 711     3193   3410   2554    319    265    650       N  
ATOM   1437  N   ARG A 712     -17.520  18.510  31.638  1.00 11.54           N  
ANISOU 1437  N   ARG A 712     1521   1689   1174    312    126    315       N  
ATOM   1438  CA  ARG A 712     -17.950  19.904  31.534  1.00 11.87           C  
ANISOU 1438  CA  ARG A 712     1572   1731   1207    339    147    246       C  
ATOM   1439  C   ARG A 712     -19.230  20.033  30.705  1.00 11.26           C  
ANISOU 1439  C   ARG A 712     1433   1643   1204    344    197    255       C  
ATOM   1440  O   ARG A 712     -20.136  20.795  31.058  1.00 11.77           O  
ANISOU 1440  O   ARG A 712     1493   1727   1252    377    254    233       O  
ATOM   1441  CB  ARG A 712     -16.828  20.756  30.960  1.00 11.58           C  
ANISOU 1441  CB  ARG A 712     1552   1653   1193    333     79    184       C  
ATOM   1442  CG  ARG A 712     -16.974  22.217  31.254  1.00 14.23           C  
ANISOU 1442  CG  ARG A 712     1920   1984   1504    363     92    109       C  
ATOM   1443  CD  ARG A 712     -15.669  22.891  31.021  1.00 16.15           C  
ANISOU 1443  CD  ARG A 712     2185   2188   1762    349     22     57       C  
ATOM   1444  NE  ARG A 712     -15.798  24.339  31.082  1.00 18.20           N  
ANISOU 1444  NE  ARG A 712     2469   2421   2025    372     33    -17       N  
ATOM   1445  CZ  ARG A 712     -14.762  25.162  31.024  1.00 20.37           C  
ANISOU 1445  CZ  ARG A 712     2765   2654   2319    360    -20    -74       C  
ATOM   1446  NH1 ARG A 712     -13.535  24.661  30.918  1.00 19.97           N  
ANISOU 1446  NH1 ARG A 712     2708   2595   2285    327    -87    -63       N  
ATOM   1447  NH2 ARG A 712     -14.949  26.475  31.070  1.00 21.47           N  
ANISOU 1447  NH2 ARG A 712     2926   2757   2475    380     -4   -142       N  
ATOM   1448  N   VAL A 713     -19.305  19.260  29.626  1.00  9.92           N  
ANISOU 1448  N   VAL A 713     1212   1443   1114    313    174    286       N  
ATOM   1449  CA  VAL A 713     -20.499  19.218  28.772  1.00 10.47           C  
ANISOU 1449  CA  VAL A 713     1216   1506   1258    311    202    298       C  
ATOM   1450  C   VAL A 713     -21.714  18.709  29.555  1.00 11.84           C  
ANISOU 1450  C   VAL A 713     1354   1716   1427    316    279    346       C  
ATOM   1451  O   VAL A 713     -22.814  19.261  29.440  1.00 12.41           O  
ANISOU 1451  O   VAL A 713     1383   1801   1530    340    325    338       O  
ATOM   1452  CB  VAL A 713     -20.280  18.339  27.510  1.00 10.05           C  
ANISOU 1452  CB  VAL A 713     1124   1416   1280    273    154    315       C  
ATOM   1453  CG1 VAL A 713     -21.571  18.190  26.726  1.00  9.41           C  
ANISOU 1453  CG1 VAL A 713      971   1335   1270    269    171    327       C  
ATOM   1454  CG2 VAL A 713     -19.213  18.934  26.605  1.00  9.49           C  
ANISOU 1454  CG2 VAL A 713     1078   1310   1218    273     96    273       C  
ATOM   1455  N   LEU A 714     -21.504  17.676  30.364  1.00 12.07           N  
ANISOU 1455  N   LEU A 714     1401   1761   1425    298    297    400       N  
ATOM   1456  CA  LEU A 714     -22.605  17.048  31.096  1.00 13.13           C  
ANISOU 1456  CA  LEU A 714     1499   1926   1564    297    380    461       C  
ATOM   1457  C   LEU A 714     -23.122  17.906  32.238  1.00 14.15           C  
ANISOU 1457  C   LEU A 714     1662   2106   1607    346    456    446       C  
ATOM   1458  O   LEU A 714     -24.318  17.872  32.538  1.00 15.59           O  
ANISOU 1458  O   LEU A 714     1795   2313   1816    358    538    476       O  
ATOM   1459  CB  LEU A 714     -22.215  15.650  31.603  1.00 13.33           C  
ANISOU 1459  CB  LEU A 714     1536   1945   1584    264    382    537       C  
ATOM   1460  CG  LEU A 714     -22.070  14.594  30.498  1.00 12.85           C  
ANISOU 1460  CG  LEU A 714     1425   1827   1630    215    332    557       C  
ATOM   1461  CD1 LEU A 714     -21.354  13.335  30.994  1.00 13.93           C  
ANISOU 1461  CD1 LEU A 714     1588   1942   1761    191    320    624       C  
ATOM   1462  CD2 LEU A 714     -23.434  14.260  29.869  1.00 14.00           C  
ANISOU 1462  CD2 LEU A 714     1478   1961   1880    191    368    573       C  
ATOM   1463  N   THR A 715     -22.226  18.666  32.871  1.00 14.28           N  
ANISOU 1463  N   THR A 715     1761   2138   1526    373    429    397       N  
ATOM   1464  CA  THR A 715     -22.546  19.362  34.131  1.00 15.38           C  
ANISOU 1464  CA  THR A 715     1955   2330   1558    421    498    375       C  
ATOM   1465  C   THR A 715     -22.677  20.888  34.049  1.00 15.44           C  
ANISOU 1465  C   THR A 715     1984   2330   1551    464    503    282       C  
ATOM   1466  O   THR A 715     -23.147  21.526  35.000  1.00 15.81           O  
ANISOU 1466  O   THR A 715     2069   2415   1522    509    573    253       O  
ATOM   1467  CB  THR A 715     -21.534  19.005  35.250  1.00 16.00           C  
ANISOU 1467  CB  THR A 715     2123   2443   1512    425    470    389       C  
ATOM   1468  OG1 THR A 715     -20.241  19.523  34.923  1.00 16.12           O  
ANISOU 1468  OG1 THR A 715     2181   2430   1515    417    368    326       O  
ATOM   1469  CG2 THR A 715     -21.449  17.495  35.454  1.00 16.70           C  
ANISOU 1469  CG2 THR A 715     2196   2535   1615    391    476    493       C  
ATOM   1470  N   THR A 716     -22.242  21.478  32.936  1.00 14.53           N  
ANISOU 1470  N   THR A 716     1850   2163   1507    453    434    236       N  
ATOM   1471  CA  THR A 716     -22.329  22.927  32.751  1.00 14.45           C  
ANISOU 1471  CA  THR A 716     1857   2129   1503    492    436    155       C  
ATOM   1472  C   THR A 716     -22.762  23.239  31.319  1.00 13.69           C  
ANISOU 1472  C   THR A 716     1689   1987   1525    486    411    156       C  
ATOM   1473  O   THR A 716     -22.805  22.344  30.465  1.00 13.14           O  
ANISOU 1473  O   THR A 716     1569   1906   1519    448    377    204       O  
ATOM   1474  CB  THR A 716     -20.973  23.637  33.018  1.00 14.74           C  
ANISOU 1474  CB  THR A 716     1973   2144   1484    490    363     85       C  
ATOM   1475  OG1 THR A 716     -20.073  23.356  31.940  1.00 13.20           O  
ANISOU 1475  OG1 THR A 716     1757   1903   1355    449    280     94       O  
ATOM   1476  CG2 THR A 716     -20.336  23.177  34.335  1.00 15.43           C  
ANISOU 1476  CG2 THR A 716     2134   2282   1448    490    357     89       C  
ATOM   1477  N   ASP A 717     -23.054  24.511  31.053  1.00 14.00           N  
ANISOU 1477  N   ASP A 717     1730   1998   1590    527    423    101       N  
ATOM   1478  CA  ASP A 717     -23.469  24.927  29.718  1.00 13.20           C  
ANISOU 1478  CA  ASP A 717     1569   1858   1589    531    396    106       C  
ATOM   1479  C   ASP A 717     -22.236  25.185  28.862  1.00 12.36           C  
ANISOU 1479  C   ASP A 717     1494   1702   1500    503    311     85       C  
ATOM   1480  O   ASP A 717     -21.803  26.324  28.663  1.00 12.82           O  
ANISOU 1480  O   ASP A 717     1585   1717   1569    525    295     35       O  
ATOM   1481  CB  ASP A 717     -24.403  26.140  29.795  1.00 14.18           C  
ANISOU 1481  CB  ASP A 717     1674   1968   1744    594    454     71       C  
ATOM   1482  CG  ASP A 717     -25.784  25.779  30.326  1.00 16.00           C  
ANISOU 1482  CG  ASP A 717     1842   2247   1992    621    544    108       C  
ATOM   1483  OD1 ASP A 717     -26.078  24.577  30.504  1.00 16.47           O  
ANISOU 1483  OD1 ASP A 717     1865   2343   2050    585    558    167       O  
ATOM   1484  OD2 ASP A 717     -26.590  26.707  30.564  1.00 18.30           O  
ANISOU 1484  OD2 ASP A 717     2115   2533   2307    679    605     80       O  
ATOM   1485  N   TYR A 718     -21.668  24.085  28.377  1.00 11.17           N  
ANISOU 1485  N   TYR A 718     1332   1555   1358    455    262    125       N  
ATOM   1486  CA  TYR A 718     -20.404  24.086  27.651  1.00 10.35           C  
ANISOU 1486  CA  TYR A 718     1254   1412   1266    425    192    113       C  
ATOM   1487  C   TYR A 718     -20.447  23.021  26.576  1.00  9.69           C  
ANISOU 1487  C   TYR A 718     1125   1326   1231    390    157    160       C  
ATOM   1488  O   TYR A 718     -20.801  21.880  26.857  1.00 10.90           O  
ANISOU 1488  O   TYR A 718     1253   1506   1382    366    169    199       O  
ATOM   1489  CB  TYR A 718     -19.290  23.766  28.638  1.00 10.77           C  
ANISOU 1489  CB  TYR A 718     1366   1477   1251    405    168     96       C  
ATOM   1490  CG  TYR A 718     -17.897  23.574  28.057  1.00  8.78           C  
ANISOU 1490  CG  TYR A 718     1130   1190   1016    370     99     91       C  
ATOM   1491  CD1 TYR A 718     -17.020  24.651  27.935  1.00  9.92           C  
ANISOU 1491  CD1 TYR A 718     1306   1292   1170    373     70     39       C  
ATOM   1492  CD2 TYR A 718     -17.434  22.307  27.685  1.00  9.45           C  
ANISOU 1492  CD2 TYR A 718     1196   1279   1115    335     69    136       C  
ATOM   1493  CE1 TYR A 718     -15.725  24.478  27.432  1.00  9.66           C  
ANISOU 1493  CE1 TYR A 718     1278   1228   1165    341     16     38       C  
ATOM   1494  CE2 TYR A 718     -16.151  22.126  27.182  1.00  8.77           C  
ANISOU 1494  CE2 TYR A 718     1120   1163   1051    310     17    131       C  
ATOM   1495  CZ  TYR A 718     -15.298  23.212  27.056  1.00  9.37           C  
ANISOU 1495  CZ  TYR A 718     1219   1202   1138    312     -8     84       C  
ATOM   1496  OH  TYR A 718     -14.027  23.004  26.572  1.00 10.87           O  
ANISOU 1496  OH  TYR A 718     1408   1363   1361    287    -52     85       O  
ATOM   1497  N   ALA A 719     -20.050  23.394  25.361  1.00  8.26           N  
ANISOU 1497  N   ALA A 719      939   1110   1091    386    117    154       N  
ATOM   1498  CA  ALA A 719     -19.900  22.463  24.235  1.00  7.64           C  
ANISOU 1498  CA  ALA A 719      832   1024   1046    355     78    183       C  
ATOM   1499  C   ALA A 719     -18.427  22.227  23.920  1.00  7.33           C  
ANISOU 1499  C   ALA A 719      830    956    998    329     38    173       C  
ATOM   1500  O   ALA A 719     -17.597  23.150  23.998  1.00  7.51           O  
ANISOU 1500  O   ALA A 719      887    951   1015    337     30    145       O  
ATOM   1501  CB  ALA A 719     -20.610  23.005  22.996  1.00  7.95           C  
ANISOU 1501  CB  ALA A 719      838   1054   1128    378     64    188       C  
ATOM   1502  N   LEU A 720     -18.109  20.984  23.572  1.00  6.61           N  
ANISOU 1502  N   LEU A 720      726    867    918    296     17    196       N  
ATOM   1503  CA  LEU A 720     -16.731  20.596  23.307  1.00  6.45           C  
ANISOU 1503  CA  LEU A 720      731    821    899    274    -14    192       C  
ATOM   1504  C   LEU A 720     -16.502  20.389  21.829  1.00  6.48           C  
ANISOU 1504  C   LEU A 720      726    803    932    268    -35    193       C  
ATOM   1505  O   LEU A 720     -17.231  19.633  21.183  1.00  7.03           O  
ANISOU 1505  O   LEU A 720      769    883   1019    259    -43    205       O  
ATOM   1506  CB  LEU A 720     -16.394  19.305  24.056  1.00  7.00           C  
ANISOU 1506  CB  LEU A 720      800    901    960    249    -19    218       C  
ATOM   1507  CG  LEU A 720     -14.935  18.831  23.960  1.00  6.83           C  
ANISOU 1507  CG  LEU A 720      795    853    948    232    -51    217       C  
ATOM   1508  CD1 LEU A 720     -13.930  19.756  24.665  1.00  7.27           C  
ANISOU 1508  CD1 LEU A 720      880    903    980    240    -66    191       C  
ATOM   1509  CD2 LEU A 720     -14.787  17.406  24.493  1.00  7.99           C  
ANISOU 1509  CD2 LEU A 720      934   1002   1100    212    -56    255       C  
ATOM   1510  N   LEU A 721     -15.498  21.077  21.294  1.00  6.12           N  
ANISOU 1510  N   LEU A 721      703    729    892    273    -43    180       N  
ATOM   1511  CA  LEU A 721     -15.055  20.815  19.932  1.00  6.53           C  
ANISOU 1511  CA  LEU A 721      758    764    959    269    -53    184       C  
ATOM   1512  C   LEU A 721     -14.212  19.552  19.989  1.00  6.59           C  
ANISOU 1512  C   LEU A 721      763    761    978    243    -65    187       C  
ATOM   1513  O   LEU A 721     -13.247  19.470  20.766  1.00  6.97           O  
ANISOU 1513  O   LEU A 721      818    797   1032    233    -69    187       O  
ATOM   1514  CB  LEU A 721     -14.281  22.018  19.375  1.00  6.79           C  
ANISOU 1514  CB  LEU A 721      814    766   1001    284    -43    178       C  
ATOM   1515  CG  LEU A 721     -15.134  23.186  18.829  1.00  7.46           C  
ANISOU 1515  CG  LEU A 721      902    849   1083    317    -32    185       C  
ATOM   1516  CD1 LEU A 721     -15.799  22.827  17.487  1.00  9.01           C  
ANISOU 1516  CD1 LEU A 721     1093   1065   1265    331    -46    202       C  
ATOM   1517  CD2 LEU A 721     -16.173  23.697  19.834  1.00 10.60           C  
ANISOU 1517  CD2 LEU A 721     1287   1263   1477    335    -22    176       C  
ATOM   1518  N   MET A 722     -14.602  18.564  19.185  1.00  6.19           N  
ANISOU 1518  N   MET A 722      703    713    936    233    -74    189       N  
ATOM   1519  CA  MET A 722     -14.149  17.179  19.377  1.00  7.01           C  
ANISOU 1519  CA  MET A 722      800    803   1062    210    -82    193       C  
ATOM   1520  C   MET A 722     -14.122  16.487  18.032  1.00  7.05           C  
ANISOU 1520  C   MET A 722      810    795   1075    207    -89    175       C  
ATOM   1521  O   MET A 722     -14.969  16.736  17.182  1.00  7.85           O  
ANISOU 1521  O   MET A 722      911    914   1159    215   -101    163       O  
ATOM   1522  CB  MET A 722     -15.124  16.452  20.330  1.00  7.15           C  
ANISOU 1522  CB  MET A 722      793    837   1086    195    -81    213       C  
ATOM   1523  CG  MET A 722     -14.719  14.989  20.667  1.00  8.77           C  
ANISOU 1523  CG  MET A 722      991   1016   1324    171    -86    229       C  
ATOM   1524  SD  MET A 722     -15.843  14.191  21.837  1.00 12.85           S  
ANISOU 1524  SD  MET A 722     1480   1548   1853    152    -71    269       S  
ATOM   1525  CE  MET A 722     -14.765  13.893  23.250  1.00 11.83           C  
ANISOU 1525  CE  MET A 722     1373   1416   1705    157    -69    308       C  
ATOM   1526  N   GLU A 723     -13.167  15.581  17.855  1.00  5.89           N  
ANISOU 1526  N   GLU A 723      668    618    953    198    -86    170       N  
ATOM   1527  CA  GLU A 723     -13.092  14.796  16.635  1.00  5.98           C  
ANISOU 1527  CA  GLU A 723      691    612    968    197    -89    141       C  
ATOM   1528  C   GLU A 723     -14.244  13.791  16.514  1.00  5.93           C  
ANISOU 1528  C   GLU A 723      667    606    980    174   -114    127       C  
ATOM   1529  O   GLU A 723     -14.680  13.191  17.504  1.00  6.09           O  
ANISOU 1529  O   GLU A 723      662    619   1032    153   -116    150       O  
ATOM   1530  CB  GLU A 723     -11.722  14.134  16.552  1.00  5.58           C  
ANISOU 1530  CB  GLU A 723      646    524    951    199    -70    138       C  
ATOM   1531  CG  GLU A 723     -10.629  15.197  16.454  1.00  6.06           C  
ANISOU 1531  CG  GLU A 723      714    583   1005    217    -45    148       C  
ATOM   1532  CD  GLU A 723      -9.219  14.634  16.570  1.00  5.52           C  
ANISOU 1532  CD  GLU A 723      632    479    985    221    -27    153       C  
ATOM   1533  OE1 GLU A 723      -9.016  13.560  17.215  1.00  6.70           O  
ANISOU 1533  OE1 GLU A 723      765    606   1174    212    -40    162       O  
ATOM   1534  OE2 GLU A 723      -8.309  15.302  16.029  1.00  6.24           O  
ANISOU 1534  OE2 GLU A 723      726    564   1082    235      3    154       O  
ATOM   1535  N   SER A 724     -14.721  13.632  15.283  1.00  6.37           N  
ANISOU 1535  N   SER A 724      738    670   1014    177   -132     91       N  
ATOM   1536  CA  SER A 724     -15.922  12.852  14.979  1.00  6.90           C  
ANISOU 1536  CA  SER A 724      782    740   1100    153   -169     66       C  
ATOM   1537  C   SER A 724     -15.833  11.397  15.410  1.00  7.70           C  
ANISOU 1537  C   SER A 724      867    790   1268    120   -169     59       C  
ATOM   1538  O   SER A 724     -16.827  10.797  15.816  1.00  8.34           O  
ANISOU 1538  O   SER A 724      910    865   1393     89   -187     65       O  
ATOM   1539  CB  SER A 724     -16.220  12.958  13.479  1.00  7.87           C  
ANISOU 1539  CB  SER A 724      934    883   1174    167   -198     19       C  
ATOM   1540  OG  SER A 724     -15.119  12.456  12.740  1.00  8.32           O  
ANISOU 1540  OG  SER A 724     1033    911   1217    179   -175    -12       O  
ATOM   1541  N   THR A 725     -14.639  10.820  15.325  1.00  7.16           N  
ANISOU 1541  N   THR A 725      822    681   1218    128   -145     52       N  
ATOM   1542  CA  THR A 725     -14.388   9.457  15.786  1.00  8.09           C  
ANISOU 1542  CA  THR A 725      928    739   1408    105   -140     54       C  
ATOM   1543  C   THR A 725     -14.740   9.312  17.267  1.00  7.70           C  
ANISOU 1543  C   THR A 725      844    688   1393     88   -131    120       C  
ATOM   1544  O   THR A 725     -15.411   8.360  17.683  1.00  7.55           O  
ANISOU 1544  O   THR A 725      799    637   1432     56   -136    133       O  
ATOM   1545  CB  THR A 725     -12.895   9.159  15.606  1.00  8.62           C  
ANISOU 1545  CB  THR A 725     1018    769   1487    131   -109     50       C  
ATOM   1546  OG1 THR A 725     -12.168  10.325  15.993  1.00 10.31           O  
ANISOU 1546  OG1 THR A 725     1236   1019   1664    156    -90     84       O  
ATOM   1547  CG2 THR A 725     -12.584   8.852  14.166  1.00  9.71           C  
ANISOU 1547  CG2 THR A 725     1194    893   1603    146   -105    -19       C  
ATOM   1548  N   SER A 726     -14.298  10.288  18.054  1.00  7.16           N  
ANISOU 1548  N   SER A 726      778    656   1287    108   -116    160       N  
ATOM   1549  CA  SER A 726     -14.512  10.284  19.489  1.00  7.41           C  
ANISOU 1549  CA  SER A 726      791    699   1326    101   -105    220       C  
ATOM   1550  C   SER A 726     -15.960  10.618  19.838  1.00  7.32           C  
ANISOU 1550  C   SER A 726      751    725   1307     84   -105    233       C  
ATOM   1551  O   SER A 726     -16.520  10.063  20.792  1.00  7.97           O  
ANISOU 1551  O   SER A 726      810    801   1418     66    -90    278       O  
ATOM   1552  CB  SER A 726     -13.521  11.251  20.156  1.00  7.65           C  
ANISOU 1552  CB  SER A 726      837    755   1314    129    -97    242       C  
ATOM   1553  OG  SER A 726     -12.193  10.834  19.877  1.00  8.94           O  
ANISOU 1553  OG  SER A 726     1012    882   1504    142    -96    236       O  
ATOM   1554  N   ILE A 727     -16.574  11.505  19.056  1.00  7.21           N  
ANISOU 1554  N   ILE A 727      735    747   1259     94   -120    199       N  
ATOM   1555  CA  ILE A 727     -17.998  11.814  19.239  1.00  8.32           C  
ANISOU 1555  CA  ILE A 727      835    920   1405     83   -123    208       C  
ATOM   1556  C   ILE A 727     -18.834  10.569  18.973  1.00  9.12           C  
ANISOU 1556  C   ILE A 727      899    988   1579     41   -138    199       C  
ATOM   1557  O   ILE A 727     -19.731  10.250  19.756  1.00  9.80           O  
ANISOU 1557  O   ILE A 727      941   1078   1704     18   -119    237       O  
ATOM   1558  CB  ILE A 727     -18.472  12.955  18.324  1.00  8.06           C  
ANISOU 1558  CB  ILE A 727      805    929   1330    108   -144    177       C  
ATOM   1559  CG1 ILE A 727     -17.719  14.243  18.676  1.00  8.21           C  
ANISOU 1559  CG1 ILE A 727      857    969   1294    144   -123    189       C  
ATOM   1560  CG2 ILE A 727     -19.984  13.148  18.454  1.00  9.30           C  
ANISOU 1560  CG2 ILE A 727      906   1116   1510     98   -152    186       C  
ATOM   1561  CD1 ILE A 727     -18.029  15.431  17.759  1.00  8.17           C  
ANISOU 1561  CD1 ILE A 727      861    992   1250    175   -138    171       C  
ATOM   1562  N   GLU A 728     -18.517   9.844  17.897  1.00  9.53           N  
ANISOU 1562  N   GLU A 728      967   1003   1652     29   -168    148       N  
ATOM   1563  CA  GLU A 728     -19.255   8.620  17.575  1.00 10.82           C  
ANISOU 1563  CA  GLU A 728     1097   1121   1895    -17   -191    125       C  
ATOM   1564  C   GLU A 728     -19.174   7.629  18.732  1.00 10.52           C  
ANISOU 1564  C   GLU A 728     1040   1034   1925    -43   -153    184       C  
ATOM   1565  O   GLU A 728     -20.182   7.017  19.105  1.00 11.95           O  
ANISOU 1565  O   GLU A 728     1169   1197   2176    -83   -148    207       O  
ATOM   1566  CB  GLU A 728     -18.720   7.970  16.294  1.00 11.43           C  
ANISOU 1566  CB  GLU A 728     1211   1159   1974    -19   -224     50       C  
ATOM   1567  CG  GLU A 728     -19.458   6.699  15.875  1.00 15.95           C  
ANISOU 1567  CG  GLU A 728     1752   1674   2634    -70   -256      8       C  
ATOM   1568  CD  GLU A 728     -18.894   6.099  14.603  1.00 19.22           C  
ANISOU 1568  CD  GLU A 728     2215   2051   3038    -66   -286    -79       C  
ATOM   1569  OE1 GLU A 728     -18.540   6.877  13.689  1.00 23.38           O  
ANISOU 1569  OE1 GLU A 728     2784   2625   3474    -29   -302   -118       O  
ATOM   1570  OE2 GLU A 728     -18.830   4.852  14.509  1.00 21.44           O  
ANISOU 1570  OE2 GLU A 728     2493   2253   3399    -98   -290   -109       O  
ATOM   1571  N   TYR A 729     -17.982   7.491  19.312  1.00  9.58           N  
ANISOU 1571  N   TYR A 729      958    894   1789    -20   -127    217       N  
ATOM   1572  CA  TYR A 729     -17.799   6.581  20.439  1.00  9.86           C  
ANISOU 1572  CA  TYR A 729      983    886   1877    -35    -94    286       C  
ATOM   1573  C   TYR A 729     -18.648   6.972  21.648  1.00 10.45           C  
ANISOU 1573  C   TYR A 729     1027   1006   1938    -41    -58    356       C  
ATOM   1574  O   TYR A 729     -19.420   6.153  22.171  1.00 11.23           O  
ANISOU 1574  O   TYR A 729     1088   1073   2107    -77    -34    400       O  
ATOM   1575  CB  TYR A 729     -16.319   6.507  20.823  1.00  9.70           C  
ANISOU 1575  CB  TYR A 729     1004    847   1833      0    -84    309       C  
ATOM   1576  CG  TYR A 729     -16.035   5.647  22.039  1.00 10.13           C  
ANISOU 1576  CG  TYR A 729     1056    865   1927     -4    -57    393       C  
ATOM   1577  CD1 TYR A 729     -16.001   4.260  21.950  1.00 11.27           C  
ANISOU 1577  CD1 TYR A 729     1191    922   2170    -29    -51    406       C  
ATOM   1578  CD2 TYR A 729     -15.757   6.240  23.272  1.00 10.72           C  
ANISOU 1578  CD2 TYR A 729     1143    990   1939     20    -38    459       C  
ATOM   1579  CE1 TYR A 729     -15.726   3.473  23.092  1.00 11.59           C  
ANISOU 1579  CE1 TYR A 729     1231    926   2246    -28    -25    499       C  
ATOM   1580  CE2 TYR A 729     -15.483   5.481  24.397  1.00 12.81           C  
ANISOU 1580  CE2 TYR A 729     1413   1231   2224     23    -17    544       C  
ATOM   1581  CZ  TYR A 729     -15.474   4.112  24.309  1.00 11.38           C  
ANISOU 1581  CZ  TYR A 729     1219    963   2141      0     -9    571       C  
ATOM   1582  OH  TYR A 729     -15.175   3.367  25.443  1.00 17.44           O  
ANISOU 1582  OH  TYR A 729     1995   1705   2927      9     13    670       O  
ATOM   1583  N   VAL A 730     -18.529   8.227  22.079  1.00 10.31           N  
ANISOU 1583  N   VAL A 730     1026   1057   1836     -6    -48    365       N  
ATOM   1584  CA  VAL A 730     -19.219   8.657  23.312  1.00 11.34           C  
ANISOU 1584  CA  VAL A 730     1138   1233   1937     -1     -4    427       C  
ATOM   1585  C   VAL A 730     -20.737   8.724  23.153  1.00 11.48           C  
ANISOU 1585  C   VAL A 730     1092   1269   1999    -28      8    425       C  
ATOM   1586  O   VAL A 730     -21.473   8.360  24.073  1.00 11.85           O  
ANISOU 1586  O   VAL A 730     1106   1321   2074    -45     57    487       O  
ATOM   1587  CB  VAL A 730     -18.655   9.981  23.909  1.00 11.64           C  
ANISOU 1587  CB  VAL A 730     1215   1332   1875     44      3    428       C  
ATOM   1588  CG1 VAL A 730     -17.174   9.854  24.259  1.00 13.31           C  
ANISOU 1588  CG1 VAL A 730     1475   1527   2056     66    -12    440       C  
ATOM   1589  CG2 VAL A 730     -18.871  11.150  22.977  1.00 12.09           C  
ANISOU 1589  CG2 VAL A 730     1272   1423   1899     64    -22    366       C  
ATOM   1590  N   THR A 731     -21.209   9.163  21.990  1.00 10.55           N  
ANISOU 1590  N   THR A 731      955   1164   1891    -31    -34    360       N  
ATOM   1591  CA  THR A 731     -22.654   9.340  21.803  1.00 11.47           C  
ANISOU 1591  CA  THR A 731     1000   1305   2053    -51    -33    357       C  
ATOM   1592  C   THR A 731     -23.385   8.016  21.655  1.00 13.36           C  
ANISOU 1592  C   THR A 731     1182   1487   2407   -111    -37    366       C  
ATOM   1593  O   THR A 731     -24.604   7.982  21.708  1.00 14.14           O  
ANISOU 1593  O   THR A 731     1205   1599   2567   -137    -28    378       O  
ATOM   1594  CB  THR A 731     -22.997  10.250  20.614  1.00 10.95           C  
ANISOU 1594  CB  THR A 731      927   1276   1959    -31    -88    292       C  
ATOM   1595  OG1 THR A 731     -22.459   9.700  19.406  1.00 11.05           O  
ANISOU 1595  OG1 THR A 731      967   1250   1980    -44   -145    231       O  
ATOM   1596  CG2 THR A 731     -22.499  11.663  20.843  1.00 10.82           C  
ANISOU 1596  CG2 THR A 731      953   1309   1848     25    -74    292       C  
ATOM   1597  N   GLN A 732     -22.658   6.917  21.472  1.00 13.91           N  
ANISOU 1597  N   GLN A 732     1280   1487   2520   -134    -49    361       N  
ATOM   1598  CA  GLN A 732     -23.327   5.616  21.455  1.00 15.98           C  
ANISOU 1598  CA  GLN A 732     1488   1677   2905   -195    -46    374       C  
ATOM   1599  C   GLN A 732     -23.284   4.949  22.826  1.00 16.65           C  
ANISOU 1599  C   GLN A 732     1569   1734   3023   -207     29    477       C  
ATOM   1600  O   GLN A 732     -23.820   3.834  23.006  1.00 18.27           O  
ANISOU 1600  O   GLN A 732     1728   1870   3342   -259     48    510       O  
ATOM   1601  CB  GLN A 732     -22.776   4.712  20.347  1.00 16.65           C  
ANISOU 1601  CB  GLN A 732     1599   1689   3037   -219   -103    299       C  
ATOM   1602  CG  GLN A 732     -23.241   5.125  18.942  1.00 19.42           C  
ANISOU 1602  CG  GLN A 732     1939   2066   3374   -223   -180    200       C  
ATOM   1603  CD  GLN A 732     -24.764   5.274  18.816  1.00 23.04           C  
ANISOU 1603  CD  GLN A 732     2304   2553   3898   -259   -201    196       C  
ATOM   1604  OE1 GLN A 732     -25.535   4.386  19.196  1.00 27.28           O  
ANISOU 1604  OE1 GLN A 732     2775   3040   4552   -316   -184    225       O  
ATOM   1605  NE2 GLN A 732     -25.199   6.405  18.266  1.00 24.35           N  
ANISOU 1605  NE2 GLN A 732     2458   2796   3997   -227   -237    165       N  
ATOM   1606  N   ARG A 733     -22.692   5.663  23.788  1.00 15.89           N  
ANISOU 1606  N   ARG A 733     1520   1691   2827   -158     70    529       N  
ATOM   1607  CA AARG A 733     -22.552   5.170  25.154  0.50 16.87           C  
ANISOU 1607  CA AARG A 733     1656   1806   2947   -155    139    633       C  
ATOM   1608  CA BARG A 733     -22.541   5.169  25.155  0.50 16.83           C  
ANISOU 1608  CA BARG A 733     1651   1801   2941   -155    139    633       C  
ATOM   1609  C   ARG A 733     -23.265   6.026  26.195  1.00 16.73           C  
ANISOU 1609  C   ARG A 733     1622   1869   2864   -131    204    688       C  
ATOM   1610  O   ARG A 733     -23.719   5.516  27.221  1.00 19.22           O  
ANISOU 1610  O   ARG A 733     1920   2180   3201   -143    275    778       O  
ATOM   1611  CB AARG A 733     -21.078   5.002  25.505  0.50 16.08           C  
ANISOU 1611  CB AARG A 733     1634   1690   2786   -118    126    652       C  
ATOM   1612  CB BARG A 733     -21.060   5.037  25.507  0.50 16.01           C  
ANISOU 1612  CB BARG A 733     1626   1683   2773   -117    125    651       C  
ATOM   1613  CG AARG A 733     -20.529   3.691  24.992  0.50 16.96           C  
ANISOU 1613  CG AARG A 733     1751   1699   2994   -146    102    645       C  
ATOM   1614  CG BARG A 733     -20.346   3.957  24.702  0.50 16.38           C  
ANISOU 1614  CG BARG A 733     1687   1637   2901   -137     84    617       C  
ATOM   1615  CD AARG A 733     -19.096   3.791  24.532  0.50 16.46           C  
ANISOU 1615  CD AARG A 733     1747   1621   2885   -107     58    603       C  
ATOM   1616  CD BARG A 733     -18.838   4.010  24.885  0.50 16.35           C  
ANISOU 1616  CD BARG A 733     1748   1627   2837    -91     64    622       C  
ATOM   1617  NE AARG A 733     -18.729   2.571  23.821  0.50 17.02           N  
ANISOU 1617  NE AARG A 733     1816   1589   3060   -133     36    574       N  
ATOM   1618  NE BARG A 733     -18.412   3.706  26.253  0.50 17.52           N  
ANISOU 1618  NE BARG A 733     1922   1782   2951    -69    103    728       N  
ATOM   1619  CZ AARG A 733     -18.847   2.388  22.507  0.50 16.72           C  
ANISOU 1619  CZ AARG A 733     1771   1517   3066   -153     -7    475       C  
ATOM   1620  CZ BARG A 733     -18.069   2.498  26.697  0.50 18.75           C  
ANISOU 1620  CZ BARG A 733     2083   1863   3178    -79    120    799       C  
ATOM   1621  NH1AARG A 733     -19.308   3.355  21.713  0.50 12.91           N  
ANISOU 1621  NH1AARG A 733     1279   1098   2528   -149    -40    402       N  
ATOM   1622  NH1BARG A 733     -18.100   1.440  25.894  0.50 20.17           N  
ANISOU 1622  NH1BARG A 733     2243   1943   3479   -113    106    767       N  
ATOM   1623  NH2AARG A 733     -18.486   1.226  21.983  0.50 16.57           N  
ANISOU 1623  NH2AARG A 733     1757   1398   3142   -173    -20    447       N  
ATOM   1624  NH2BARG A 733     -17.692   2.344  27.959  0.50 19.21           N  
ANISOU 1624  NH2BARG A 733     2172   1943   3185    -51    150    901       N  
ATOM   1625  N   ASN A 734     -23.366   7.323  25.934  1.00 15.61           N  
ANISOU 1625  N   ASN A 734     1489   1797   2645    -94    187    636       N  
ATOM   1626  CA  ASN A 734     -24.123   8.213  26.794  1.00 15.24           C  
ANISOU 1626  CA  ASN A 734     1425   1823   2543    -66    250    669       C  
ATOM   1627  C   ASN A 734     -25.201   8.886  25.958  1.00 14.83           C  
ANISOU 1627  C   ASN A 734     1302   1799   2535    -72    229    614       C  
ATOM   1628  O   ASN A 734     -24.910   9.760  25.141  1.00 14.36           O  
ANISOU 1628  O   ASN A 734     1262   1761   2432    -44    173    544       O  
ATOM   1629  CB  ASN A 734     -23.196   9.242  27.460  1.00 14.55           C  
ANISOU 1629  CB  ASN A 734     1419   1792   2319     -6    254    663       C  
ATOM   1630  CG  ASN A 734     -23.913  10.093  28.502  1.00 16.44           C  
ANISOU 1630  CG  ASN A 734     1653   2101   2491     28    329    695       C  
ATOM   1631  OD1 ASN A 734     -25.096  10.411  28.368  1.00 16.78           O  
ANISOU 1631  OD1 ASN A 734     1628   2166   2583     22    364    692       O  
ATOM   1632  ND2 ASN A 734     -23.188  10.471  29.548  1.00 17.37           N  
ANISOU 1632  ND2 ASN A 734     1845   2257   2499     67    352    721       N  
ATOM   1633  N   CYS A 735     -26.450   8.477  26.160  1.00 15.35           N  
ANISOU 1633  N   CYS A 735     1280   1860   2692   -106    274    651       N  
ATOM   1634  CA  CYS A 735     -27.538   8.969  25.314  1.00 15.76           C  
ANISOU 1634  CA  CYS A 735     1247   1933   2807   -116    242    602       C  
ATOM   1635  C   CYS A 735     -27.976  10.400  25.633  1.00 15.50           C  
ANISOU 1635  C   CYS A 735     1210   1978   2702    -55    274    592       C  
ATOM   1636  O   CYS A 735     -28.891  10.921  25.006  1.00 15.87           O  
ANISOU 1636  O   CYS A 735     1183   2048   2798    -51    250    560       O  
ATOM   1637  CB  CYS A 735     -28.724   8.008  25.338  1.00 17.14           C  
ANISOU 1637  CB  CYS A 735     1314   2072   3128   -179    270    640       C  
ATOM   1638  SG  CYS A 735     -28.265   6.299  24.951  1.00 19.51           S  
ANISOU 1638  SG  CYS A 735     1618   2261   3533   -253    234    647       S  
ATOM   1639  N   ASN A 736     -27.325  11.031  26.607  1.00 14.30           N  
ANISOU 1639  N   ASN A 736     1134   1861   2437     -7    325    615       N  
ATOM   1640  CA  ASN A 736     -27.553  12.448  26.881  1.00 14.71           C  
ANISOU 1640  CA  ASN A 736     1200   1975   2416     55    351    590       C  
ATOM   1641  C   ASN A 736     -26.719  13.354  25.980  1.00 13.33           C  
ANISOU 1641  C   ASN A 736     1083   1802   2180     87    270    516       C  
ATOM   1642  O   ASN A 736     -26.934  14.568  25.934  1.00 13.51           O  
ANISOU 1642  O   ASN A 736     1111   1860   2162    136    276    486       O  
ATOM   1643  CB  ASN A 736     -27.279  12.773  28.352  1.00 15.36           C  
ANISOU 1643  CB  ASN A 736     1342   2096   2399     93    440    637       C  
ATOM   1644  CG  ASN A 736     -28.229  12.057  29.282  1.00 18.56           C  
ANISOU 1644  CG  ASN A 736     1689   2510   2854     71    541    720       C  
ATOM   1645  OD1 ASN A 736     -29.440  12.019  29.044  1.00 20.96           O  
ANISOU 1645  OD1 ASN A 736     1889   2819   3256     55    573    732       O  
ATOM   1646  ND2 ASN A 736     -27.684  11.462  30.340  1.00 21.89           N  
ANISOU 1646  ND2 ASN A 736     2171   2932   3213     70    593    785       N  
ATOM   1647  N   LEU A 737     -25.769  12.760  25.261  1.00 12.60           N  
ANISOU 1647  N   LEU A 737     1033   1667   2088     62    201    489       N  
ATOM   1648  CA  LEU A 737     -24.844  13.510  24.412  1.00 11.80           C  
ANISOU 1648  CA  LEU A 737      990   1563   1929     90    135    429       C  
ATOM   1649  C   LEU A 737     -25.202  13.400  22.940  1.00 11.44           C  
ANISOU 1649  C   LEU A 737      906   1502   1939     72     59    381       C  
ATOM   1650  O   LEU A 737     -25.766  12.405  22.498  1.00 11.21           O  
ANISOU 1650  O   LEU A 737      823   1445   1992     25     36    382       O  
ATOM   1651  CB  LEU A 737     -23.401  13.028  24.631  1.00 11.70           C  
ANISOU 1651  CB  LEU A 737     1057   1521   1869     84    117    432       C  
ATOM   1652  CG  LEU A 737     -22.790  13.239  26.023  1.00 12.45           C  
ANISOU 1652  CG  LEU A 737     1208   1638   1885    109    167    471       C  
ATOM   1653  CD1 LEU A 737     -21.484  12.463  26.124  1.00 13.01           C  
ANISOU 1653  CD1 LEU A 737     1333   1671   1939     96    137    483       C  
ATOM   1654  CD2 LEU A 737     -22.577  14.721  26.341  1.00 14.83           C  
ANISOU 1654  CD2 LEU A 737     1548   1979   2106    161    177    436       C  
ATOM   1655  N   THR A 738     -24.877  14.441  22.180  1.00 10.61           N  
ANISOU 1655  N   THR A 738      832   1414   1786    110     19    338       N  
ATOM   1656  CA  THR A 738     -25.128  14.433  20.750  1.00 11.07           C  
ANISOU 1656  CA  THR A 738      870   1467   1870    103    -57    294       C  
ATOM   1657  C   THR A 738     -24.084  15.249  19.998  1.00 10.29           C  
ANISOU 1657  C   THR A 738      845   1367   1696    138    -92    260       C  
ATOM   1658  O   THR A 738     -23.458  16.160  20.557  1.00  9.64           O  
ANISOU 1658  O   THR A 738      810   1294   1558    174    -59    266       O  
ATOM   1659  CB  THR A 738     -26.540  14.977  20.440  1.00 11.20           C  
ANISOU 1659  CB  THR A 738      801   1519   1936    117    -68    296       C  
ATOM   1660  OG1 THR A 738     -26.837  14.798  19.047  1.00 13.77           O  
ANISOU 1660  OG1 THR A 738     1105   1844   2282    106   -156    254       O  
ATOM   1661  CG2 THR A 738     -26.670  16.461  20.793  1.00 12.37           C  
ANISOU 1661  CG2 THR A 738      963   1701   2036    182    -34    302       C  
ATOM   1662  N   GLN A 739     -23.895  14.907  18.725  1.00 10.41           N  
ANISOU 1662  N   GLN A 739      873   1371   1713    126   -157    221       N  
ATOM   1663  CA  GLN A 739     -23.153  15.768  17.804  1.00 10.35           C  
ANISOU 1663  CA  GLN A 739      923   1369   1639    164   -186    195       C  
ATOM   1664  C   GLN A 739     -24.016  16.954  17.362  1.00 10.88           C  
ANISOU 1664  C   GLN A 739      962   1475   1698    208   -204    200       C  
ATOM   1665  O   GLN A 739     -25.221  16.792  17.127  1.00 12.95           O  
ANISOU 1665  O   GLN A 739     1151   1760   2011    200   -233    202       O  
ATOM   1666  CB  GLN A 739     -22.713  14.959  16.586  1.00 10.22           C  
ANISOU 1666  CB  GLN A 739      935   1333   1616    142   -242    152       C  
ATOM   1667  CG  GLN A 739     -21.788  15.728  15.639  1.00 11.05           C  
ANISOU 1667  CG  GLN A 739     1108   1442   1647    179   -256    134       C  
ATOM   1668  CD  GLN A 739     -21.237  14.861  14.536  1.00 13.24           C  
ANISOU 1668  CD  GLN A 739     1424   1701   1906    162   -295     88       C  
ATOM   1669  OE1 GLN A 739     -20.614  13.836  14.802  1.00 17.21           O  
ANISOU 1669  OE1 GLN A 739     1941   2163   2436    132   -280     75       O  
ATOM   1670  NE2 GLN A 739     -21.447  15.271  13.289  1.00 12.06           N  
ANISOU 1670  NE2 GLN A 739     1297   1580   1707    187   -342     64       N  
ATOM   1671  N   ILE A 740     -23.401  18.130  17.248  1.00 10.66           N  
ANISOU 1671  N   ILE A 740      984   1450   1617    252   -189    205       N  
ATOM   1672  CA  ILE A 740     -24.067  19.325  16.710  1.00 11.74           C  
ANISOU 1672  CA  ILE A 740     1104   1612   1746    303   -207    216       C  
ATOM   1673  C   ILE A 740     -23.403  19.683  15.391  1.00 11.24           C  
ANISOU 1673  C   ILE A 740     1099   1547   1626    323   -249    203       C  
ATOM   1674  O   ILE A 740     -22.197  19.902  15.336  1.00 10.72           O  
ANISOU 1674  O   ILE A 740     1097   1455   1520    326   -224    200       O  
ATOM   1675  CB  ILE A 740     -23.978  20.519  17.687  1.00 12.23           C  
ANISOU 1675  CB  ILE A 740     1178   1668   1800    343   -145    235       C  
ATOM   1676  CG1 ILE A 740     -24.777  20.216  18.962  1.00 14.67           C  
ANISOU 1676  CG1 ILE A 740     1431   1990   2152    331    -94    250       C  
ATOM   1677  CG2 ILE A 740     -24.436  21.823  17.027  1.00 14.12           C  
ANISOU 1677  CG2 ILE A 740     1415   1917   2034    401   -161    249       C  
ATOM   1678  CD1 ILE A 740     -24.914  21.394  19.898  1.00 17.81           C  
ANISOU 1678  CD1 ILE A 740     1838   2388   2542    377    -34    257       C  
ATOM   1679  N   GLY A 741     -24.200  19.737  14.326  1.00 11.52           N  
ANISOU 1679  N   GLY A 741     1107   1613   1657    339   -314    199       N  
ATOM   1680  CA  GLY A 741     -23.677  20.070  13.011  1.00 11.53           C  
ANISOU 1680  CA  GLY A 741     1169   1623   1590    364   -353    194       C  
ATOM   1681  C   GLY A 741     -22.905  18.935  12.386  1.00 11.83           C  
ANISOU 1681  C   GLY A 741     1251   1648   1595    326   -374    152       C  
ATOM   1682  O   GLY A 741     -22.884  17.814  12.898  1.00 11.84           O  
ANISOU 1682  O   GLY A 741     1230   1630   1639    277   -369    127       O  
ATOM   1683  N   GLY A 742     -22.278  19.229  11.255  1.00 11.75           N  
ANISOU 1683  N   GLY A 742     1307   1646   1511    352   -391    148       N  
ATOM   1684  CA  GLY A 742     -21.497  18.244  10.524  1.00 11.38           C  
ANISOU 1684  CA  GLY A 742     1312   1589   1424    327   -402    103       C  
ATOM   1685  C   GLY A 742     -20.025  18.345  10.871  1.00 11.26           C  
ANISOU 1685  C   GLY A 742     1350   1532   1395    326   -328    111       C  
ATOM   1686  O   GLY A 742     -19.660  18.863  11.932  1.00 10.27           O  
ANISOU 1686  O   GLY A 742     1213   1383   1308    325   -277    140       O  
ATOM   1687  N   LEU A 743     -19.189  17.833   9.975  1.00 11.48           N  
ANISOU 1687  N   LEU A 743     1436   1554   1371    326   -324     82       N  
ATOM   1688  CA  LEU A 743     -17.742  17.906  10.141  1.00 11.75           C  
ANISOU 1688  CA  LEU A 743     1514   1552   1400    327   -254     90       C  
ATOM   1689  C   LEU A 743     -17.214  19.209   9.547  1.00 11.24           C  
ANISOU 1689  C   LEU A 743     1492   1494   1283    373   -219    137       C  
ATOM   1690  O   LEU A 743     -17.594  19.593   8.431  1.00 13.00           O  
ANISOU 1690  O   LEU A 743     1749   1754   1436    407   -248    146       O  
ATOM   1691  CB  LEU A 743     -17.067  16.681   9.505  1.00 12.15           C  
ANISOU 1691  CB  LEU A 743     1600   1585   1431    309   -252     36       C  
ATOM   1692  CG  LEU A 743     -16.920  15.431  10.386  1.00 14.28           C  
ANISOU 1692  CG  LEU A 743     1835   1813   1777    262   -248      6       C  
ATOM   1693  CD1 LEU A 743     -18.224  14.998  11.038  1.00 14.94           C  
ANISOU 1693  CD1 LEU A 743     1854   1904   1917    230   -296      2       C  
ATOM   1694  CD2 LEU A 743     -16.338  14.300   9.582  1.00 15.11           C  
ANISOU 1694  CD2 LEU A 743     1980   1896   1865    254   -247    -53       C  
ATOM   1695  N   ILE A 744     -16.347  19.880  10.303  1.00 10.42           N  
ANISOU 1695  N   ILE A 744     1388   1354   1216    373   -159    168       N  
ATOM   1696  CA AILE A 744     -15.857  21.172   9.813  0.50 10.62           C  
ANISOU 1696  CA AILE A 744     1448   1373   1213    411   -120    218       C  
ATOM   1697  CA BILE A 744     -15.766  21.187   9.994  0.50 10.52           C  
ANISOU 1697  CA BILE A 744     1432   1355   1212    407   -115    218       C  
ATOM   1698  C   ILE A 744     -14.536  21.071   9.066  1.00 10.46           C  
ANISOU 1698  C   ILE A 744     1477   1336   1162    417    -63    222       C  
ATOM   1699  O   ILE A 744     -14.148  22.019   8.377  1.00 11.15           O  
ANISOU 1699  O   ILE A 744     1600   1421   1216    449    -27    268       O  
ATOM   1700  CB AILE A 744     -15.833  22.291  10.879  0.50 10.22           C  
ANISOU 1700  CB AILE A 744     1370   1291   1221    414    -93    252       C  
ATOM   1701  CB BILE A 744     -15.400  21.886  11.341  0.50  9.91           C  
ANISOU 1701  CB BILE A 744     1323   1238   1206    393    -80    237       C  
ATOM   1702  CG1AILE A 744     -14.740  22.041  11.918  0.50 10.34           C  
ANISOU 1702  CG1AILE A 744     1372   1265   1293    380    -52    238       C  
ATOM   1703  CG1BILE A 744     -16.678  22.355  12.059  0.50 10.27           C  
ANISOU 1703  CG1BILE A 744     1326   1298   1278    402   -113    244       C  
ATOM   1704  CG2AILE A 744     -17.222  22.467  11.507  0.50 10.57           C  
ANISOU 1704  CG2AILE A 744     1367   1358   1292    419   -137    252       C  
ATOM   1705  CG2BILE A 744     -14.411  23.017  11.148  0.50 10.88           C  
ANISOU 1705  CG2BILE A 744     1473   1324   1338    410    -24    276       C  
ATOM   1706  CD1AILE A 744     -14.527  23.214  12.858  0.50 10.89           C  
ANISOU 1706  CD1AILE A 744     1428   1300   1411    384    -26    260       C  
ATOM   1707  CD1BILE A 744     -16.520  22.642  13.548  0.50 10.64           C  
ANISOU 1707  CD1BILE A 744     1343   1317   1382    383    -90    239       C  
ATOM   1708  N   ASP A 745     -13.900  19.906   9.115  1.00  9.37           N  
ANISOU 1708  N   ASP A 745     1340   1185   1035    391    -52    178       N  
ATOM   1709  CA  ASP A 745     -12.733  19.626   8.291  1.00  9.37           C  
ANISOU 1709  CA  ASP A 745     1383   1174   1005    402      5    173       C  
ATOM   1710  C   ASP A 745     -12.643  18.127   8.032  1.00  9.17           C  
ANISOU 1710  C   ASP A 745     1365   1148    972    384    -12    107       C  
ATOM   1711  O   ASP A 745     -13.538  17.366   8.426  1.00  8.99           O  
ANISOU 1711  O   ASP A 745     1314   1132    968    360    -73     70       O  
ATOM   1712  CB  ASP A 745     -11.441  20.215   8.905  1.00  8.57           C  
ANISOU 1712  CB  ASP A 745     1263   1024    969    393     75    206       C  
ATOM   1713  CG  ASP A 745     -11.020  19.536  10.212  1.00  8.55           C  
ANISOU 1713  CG  ASP A 745     1209    988   1050    354     67    182       C  
ATOM   1714  OD1 ASP A 745     -11.738  18.645  10.723  1.00  8.01           O  
ANISOU 1714  OD1 ASP A 745     1120    928    994    334     18    149       O  
ATOM   1715  OD2 ASP A 745      -9.926  19.889  10.717  1.00  9.18           O  
ANISOU 1715  OD2 ASP A 745     1268   1033   1187    344    110    201       O  
ATOM   1716  N   SER A 746     -11.582  17.705   7.355  1.00  9.57           N  
ANISOU 1716  N   SER A 746     1450   1186   1002    396     46     92       N  
ATOM   1717  CA  SER A 746     -11.409  16.300   7.025  1.00 10.34           C  
ANISOU 1717  CA  SER A 746     1561   1272   1096    386     38     23       C  
ATOM   1718  C   SER A 746      -9.926  15.991   7.038  1.00  9.80           C  
ANISOU 1718  C   SER A 746     1491   1163   1071    391    122     25       C  
ATOM   1719  O   SER A 746      -9.149  16.640   6.357  1.00 11.07           O  
ANISOU 1719  O   SER A 746     1680   1329   1197    420    191     57       O  
ATOM   1720  CB  SER A 746     -12.002  16.006   5.643  1.00 11.63           C  
ANISOU 1720  CB  SER A 746     1789   1482   1146    412      8    -19       C  
ATOM   1721  OG  SER A 746     -11.815  14.644   5.285  1.00 15.43           O  
ANISOU 1721  OG  SER A 746     2291   1945   1628    403      3    -99       O  
ATOM   1722  N   LYS A 747      -9.536  15.005   7.838  1.00  8.94           N  
ANISOU 1722  N   LYS A 747      992    859   1544    347   -160      9       N  
ATOM   1723  CA  LYS A 747      -8.122  14.671   8.004  1.00  8.34           C  
ANISOU 1723  CA  LYS A 747      948    770   1451    305   -148     -1       C  
ATOM   1724  C   LYS A 747      -8.015  13.239   8.482  1.00  7.57           C  
ANISOU 1724  C   LYS A 747      836    719   1321    264   -181    -10       C  
ATOM   1725  O   LYS A 747      -9.003  12.503   8.515  1.00  7.20           O  
ANISOU 1725  O   LYS A 747      759    701   1275    263   -204    -11       O  
ATOM   1726  CB  LYS A 747      -7.443  15.621   8.991  1.00  9.36           C  
ANISOU 1726  CB  LYS A 747     1079    863   1613    278   -102    -42       C  
ATOM   1727  CG  LYS A 747      -8.216  15.839  10.245  1.00 10.55           C  
ANISOU 1727  CG  LYS A 747     1217   1032   1760    268    -87    -80       C  
ATOM   1728  CD  LYS A 747      -7.994  17.233  10.784  1.00 13.00           C  
ANISOU 1728  CD  LYS A 747     1545   1286   2110    266    -32   -121       C  
ATOM   1729  CE  LYS A 747      -8.637  17.359  12.145  1.00 11.52           C  
ANISOU 1729  CE  LYS A 747     1374   1108   1895    259     -8   -165       C  
ATOM   1730  NZ  LYS A 747      -8.508  18.715  12.695  1.00 10.24           N  
ANISOU 1730  NZ  LYS A 747     1240    882   1767    255     50   -219       N  
ATOM   1731  N   GLY A 748      -6.809  12.841   8.849  1.00  7.50           N  
ANISOU 1731  N   GLY A 748      841    708   1302    232   -178    -17       N  
ATOM   1732  CA  GLY A 748      -6.591  11.464   9.262  1.00  6.82           C  
ANISOU 1732  CA  GLY A 748      750    658   1183    207   -194    -11       C  
ATOM   1733  C   GLY A 748      -5.657  11.381  10.441  1.00  5.96           C  
ANISOU 1733  C   GLY A 748      641    563   1059    188   -198    -34       C  
ATOM   1734  O   GLY A 748      -4.927  12.342  10.737  1.00  6.60           O  
ANISOU 1734  O   GLY A 748      718    622   1169    180   -203    -65       O  
ATOM   1735  N   TYR A 749      -5.687  10.232  11.118  1.00  5.68           N  
ANISOU 1735  N   TYR A 749      613    563    982    185   -199    -22       N  
ATOM   1736  CA  TYR A 749      -4.690   9.893  12.139  1.00  5.96           C  
ANISOU 1736  CA  TYR A 749      660    625    981    188   -224    -31       C  
ATOM   1737  C   TYR A 749      -3.571   9.078  11.515  1.00  5.97           C  
ANISOU 1737  C   TYR A 749      646    621   1003    183   -234      8       C  
ATOM   1738  O   TYR A 749      -3.829   8.207  10.697  1.00  6.15           O  
ANISOU 1738  O   TYR A 749      677    631   1029    179   -203     46       O  
ATOM   1739  CB  TYR A 749      -5.297   9.021  13.234  1.00  6.30           C  
ANISOU 1739  CB  TYR A 749      737    698    957    213   -195    -20       C  
ATOM   1740  CG  TYR A 749      -6.424   9.628  14.028  1.00  6.53           C  
ANISOU 1740  CG  TYR A 749      793    722    967    229   -155    -47       C  
ATOM   1741  CD1 TYR A 749      -6.377  10.947  14.497  1.00  7.07           C  
ANISOU 1741  CD1 TYR A 749      876    779   1031    230   -173   -101       C  
ATOM   1742  CD2 TYR A 749      -7.524   8.851  14.352  1.00  6.26           C  
ANISOU 1742  CD2 TYR A 749      767    678    933    243    -79    -21       C  
ATOM   1743  CE1 TYR A 749      -7.423  11.484  15.249  1.00  6.71           C  
ANISOU 1743  CE1 TYR A 749      865    716    969    251   -114   -121       C  
ATOM   1744  CE2 TYR A 749      -8.560   9.360  15.116  1.00  7.07           C  
ANISOU 1744  CE2 TYR A 749      893    760   1035    264    -15    -36       C  
ATOM   1745  CZ  TYR A 749      -8.517  10.668  15.553  1.00  7.47           C  
ANISOU 1745  CZ  TYR A 749      969    803   1068    271    -32    -83       C  
ATOM   1746  OH  TYR A 749      -9.557  11.140  16.316  1.00  7.90           O  
ANISOU 1746  OH  TYR A 749     1055    824   1122    298     53    -92       O  
ATOM   1747  N   GLY A 750      -2.335   9.381  11.892  1.00  4.55           N  
ANISOU 1747  N   GLY A 750      537    376    815     66    -64    155       N  
ATOM   1748  CA  GLY A 750      -1.194   8.555  11.457  1.00  4.72           C  
ANISOU 1748  CA  GLY A 750      570    411    813     60    -31    154       C  
ATOM   1749  C   GLY A 750      -0.268   8.208  12.603  1.00  4.99           C  
ANISOU 1749  C   GLY A 750      568    472    856     74     -4    148       C  
ATOM   1750  O   GLY A 750      -0.335   8.792  13.684  1.00  5.92           O  
ANISOU 1750  O   GLY A 750      660    600    991     81    -10    143       O  
ATOM   1751  N   VAL A 751       0.588   7.226  12.369  1.00  4.66           N  
ANISOU 1751  N   VAL A 751      527    442    800     81     25    146       N  
ATOM   1752  CA  VAL A 751       1.662   6.925  13.304  1.00  4.96           C  
ANISOU 1752  CA  VAL A 751      530    509    845     97     46    143       C  
ATOM   1753  C   VAL A 751       2.770   7.965  13.128  1.00  5.50           C  
ANISOU 1753  C   VAL A 751      583    593    912     78     57    142       C  
ATOM   1754  O   VAL A 751       3.193   8.241  12.004  1.00  6.44           O  
ANISOU 1754  O   VAL A 751      726    706   1016     58     72    146       O  
ATOM   1755  CB  VAL A 751       2.203   5.509  13.078  1.00  5.51           C  
ANISOU 1755  CB  VAL A 751      605    583    905    119     72    142       C  
ATOM   1756  CG1 VAL A 751       3.441   5.252  13.934  1.00  6.90           C  
ANISOU 1756  CG1 VAL A 751      741    793   1089    141     90    141       C  
ATOM   1757  CG2 VAL A 751       1.116   4.487  13.372  1.00  6.42           C  
ANISOU 1757  CG2 VAL A 751      736    679   1025    130     62    144       C  
ATOM   1758  N   GLY A 752       3.203   8.573  14.229  1.00  5.62           N  
ANISOU 1758  N   GLY A 752      566    629    942     78     49    136       N  
ATOM   1759  CA  GLY A 752       4.270   9.573  14.172  1.00  6.31           C  
ANISOU 1759  CA  GLY A 752      634    730   1032     52     56    133       C  
ATOM   1760  C   GLY A 752       5.628   8.942  14.376  1.00  6.71           C  
ANISOU 1760  C   GLY A 752      644    820   1086     63     80    130       C  
ATOM   1761  O   GLY A 752       5.769   8.000  15.151  1.00  6.71           O  
ANISOU 1761  O   GLY A 752      623    838   1089     96     79    129       O  
ATOM   1762  N   THR A 753       6.624   9.443  13.648  1.00  6.55           N  
ANISOU 1762  N   THR A 753      611    811   1065     35    104    132       N  
ATOM   1763  CA  THR A 753       8.010   9.038  13.856  1.00  7.42           C  
ANISOU 1763  CA  THR A 753      668    965   1188     43    128    128       C  
ATOM   1764  C   THR A 753       8.878  10.292  13.767  1.00  7.97           C  
ANISOU 1764  C   THR A 753      711   1048   1270     -6    132    124       C  
ATOM   1765  O   THR A 753       8.447  11.291  13.212  1.00  7.74           O  
ANISOU 1765  O   THR A 753      719    987   1234    -44    129    129       O  
ATOM   1766  CB  THR A 753       8.476   8.010  12.786  1.00  7.75           C  
ANISOU 1766  CB  THR A 753      717   1012   1217     63    172    131       C  
ATOM   1767  OG1 THR A 753       8.672   8.667  11.525  1.00  8.77           O  
ANISOU 1767  OG1 THR A 753      874   1128   1331     24    201    137       O  
ATOM   1768  CG2 THR A 753       7.461   6.885  12.625  1.00 10.32           C  
ANISOU 1768  CG2 THR A 753     1085   1308   1527     98    167    134       C  
ATOM   1769  N   PRO A 754      10.084  10.263  14.347  1.00  8.25           N  
ANISOU 1769  N   PRO A 754      681   1130   1325     -8    137    117       N  
ATOM   1770  CA  PRO A 754      10.976  11.417  14.151  1.00  9.07           C  
ANISOU 1770  CA  PRO A 754      756   1247   1445    -65    146    113       C  
ATOM   1771  C   PRO A 754      11.336  11.578  12.680  1.00 10.24           C  
ANISOU 1771  C   PRO A 754      924   1385   1581    -94    198    125       C  
ATOM   1772  O   PRO A 754      11.407  10.575  11.966  1.00 10.42           O  
ANISOU 1772  O   PRO A 754      955   1414   1591    -61    233    130       O  
ATOM   1773  CB  PRO A 754      12.218  11.040  14.966  1.00  9.79           C  
ANISOU 1773  CB  PRO A 754      763   1397   1561    -52    140    103       C  
ATOM   1774  CG  PRO A 754      11.741  10.002  15.957  1.00  8.88           C  
ANISOU 1774  CG  PRO A 754      647   1289   1438     11    110    102       C  
ATOM   1775  CD  PRO A 754      10.700   9.225  15.199  1.00  7.98           C  
ANISOU 1775  CD  PRO A 754      596   1135   1301     40    129    113       C  
ATOM   1776  N   ILE A 755      11.575  12.818  12.237  1.00 10.53           N  
ANISOU 1776  N   ILE A 755      975   1405   1622   -156    206    130       N  
ATOM   1777  CA  ILE A 755      12.025  13.063  10.864  1.00 11.87           C  
ANISOU 1777  CA  ILE A 755     1166   1569   1776   -191    262    145       C  
ATOM   1778  C   ILE A 755      13.245  12.207  10.574  1.00 12.18           C  
ANISOU 1778  C   ILE A 755     1137   1664   1827   -174    312    140       C  
ATOM   1779  O   ILE A 755      14.173  12.138  11.394  1.00 11.96           O  
ANISOU 1779  O   ILE A 755     1028   1683   1834   -172    304    128       O  
ATOM   1780  CB  ILE A 755      12.358  14.561  10.607  1.00 12.47           C  
ANISOU 1780  CB  ILE A 755     1256   1622   1859   -267    266    153       C  
ATOM   1781  CG1 ILE A 755      11.071  15.359  10.402  1.00 13.76           C  
ANISOU 1781  CG1 ILE A 755     1508   1719   2003   -277    230    164       C  
ATOM   1782  CG2 ILE A 755      13.252  14.732   9.354  1.00 14.12           C  
ANISOU 1782  CG2 ILE A 755     1463   1845   2058   -310    336    168       C  
ATOM   1783  CD1 ILE A 755      11.274  16.845  10.153  0.50 12.78           C  
ANISOU 1783  CD1 ILE A 755     1415   1557   1884   -347    230    174       C  
ATOM   1784  N   GLY A 756      13.234  11.542   9.420  1.00 12.55           N  
ANISOU 1784  N   GLY A 756     1217   1706   1845   -157    363    148       N  
ATOM   1785  CA  GLY A 756      14.330  10.664   9.026  1.00 13.97           C  
ANISOU 1785  CA  GLY A 756     1339   1934   2035   -131    420    142       C  
ATOM   1786  C   GLY A 756      14.229   9.245   9.559  1.00 14.11           C  
ANISOU 1786  C   GLY A 756     1335   1967   2058    -52    408    130       C  
ATOM   1787  O   GLY A 756      15.088   8.413   9.281  1.00 15.33           O  
ANISOU 1787  O   GLY A 756     1443   2158   2222    -16    453    123       O  
ATOM   1788  N   SER A 757      13.165   8.951  10.303  1.00 13.36           N  
ANISOU 1788  N   SER A 757     1277   1843   1957    -22    351    129       N  
ATOM   1789  CA  SER A 757      13.001   7.620  10.861  1.00 13.97           C  
ANISOU 1789  CA  SER A 757     1343   1926   2038     48    338    122       C  
ATOM   1790  C   SER A 757      13.083   6.530   9.796  1.00 14.60           C  
ANISOU 1790  C   SER A 757     1456   1997   2095     85    392    119       C  
ATOM   1791  O   SER A 757      12.397   6.621   8.771  1.00 14.54           O  
ANISOU 1791  O   SER A 757     1523   1953   2050     66    408    123       O  
ATOM   1792  CB  SER A 757      11.649   7.487  11.538  1.00 13.33           C  
ANISOU 1792  CB  SER A 757     1315   1805   1945     64    282    125       C  
ATOM   1793  OG  SER A 757      11.436   6.128  11.890  1.00 14.94           O  
ANISOU 1793  OG  SER A 757     1523   2006   2147    126    279    122       O  
ATOM   1794  N   PRO A 758      13.883   5.479  10.055  1.00 15.74           N  
ANISOU 1794  N   PRO A 758     1549   2172   2258    142    414    111       N  
ATOM   1795  CA  PRO A 758      13.954   4.320   9.167  1.00 16.48           C  
ANISOU 1795  CA  PRO A 758     1679   2252   2332    188    463    102       C  
ATOM   1796  C   PRO A 758      12.745   3.394   9.281  1.00 16.11           C  
ANISOU 1796  C   PRO A 758     1707   2152   2261    222    432    101       C  
ATOM   1797  O   PRO A 758      12.695   2.373   8.588  1.00 18.08           O  
ANISOU 1797  O   PRO A 758     1999   2380   2492    259    466     91       O  
ATOM   1798  CB  PRO A 758      15.209   3.590   9.660  1.00 17.02           C  
ANISOU 1798  CB  PRO A 758     1659   2370   2439    244    486     95       C  
ATOM   1799  CG  PRO A 758      15.255   3.901  11.117  1.00 17.54           C  
ANISOU 1799  CG  PRO A 758     1671   2458   2536    248    419    102       C  
ATOM   1800  CD  PRO A 758      14.795   5.334  11.209  1.00 16.53           C  
ANISOU 1800  CD  PRO A 758     1557   2321   2401    170    390    108       C  
ATOM   1801  N   TYR A 759      11.799   3.733  10.158  1.00 14.48           N  
ANISOU 1801  N   TYR A 759     1518   1926   2058    209    370    110       N  
ATOM   1802  CA  TYR A 759      10.581   2.941  10.319  1.00 13.28           C  
ANISOU 1802  CA  TYR A 759     1431   1726   1889    231    340    111       C  
ATOM   1803  C   TYR A 759       9.343   3.504   9.633  1.00 12.35           C  
ANISOU 1803  C   TYR A 759     1385   1567   1740    186    320    114       C  
ATOM   1804  O   TYR A 759       8.393   2.757   9.396  1.00 12.49           O  
ANISOU 1804  O   TYR A 759     1459   1546   1741    198    307    111       O  
ATOM   1805  CB  TYR A 759      10.268   2.728  11.809  1.00 13.34           C  
ANISOU 1805  CB  TYR A 759     1411   1739   1919    254    289    119       C  
ATOM   1806  CG  TYR A 759      11.327   1.927  12.524  1.00 14.34           C  
ANISOU 1806  CG  TYR A 759     1479   1899   2072    311    297    119       C  
ATOM   1807  CD1 TYR A 759      11.321   0.537  12.474  1.00 16.03           C  
ANISOU 1807  CD1 TYR A 759     1719   2088   2283    369    312    118       C  
ATOM   1808  CD2 TYR A 759      12.338   2.559  13.244  1.00 16.14           C  
ANISOU 1808  CD2 TYR A 759     1626   2179   2326    308    285    121       C  
ATOM   1809  CE1 TYR A 759      12.291  -0.209  13.125  1.00 16.30           C  
ANISOU 1809  CE1 TYR A 759     1702   2150   2343    430    315    121       C  
ATOM   1810  CE2 TYR A 759      13.336   1.815  13.893  1.00 15.78           C  
ANISOU 1810  CE2 TYR A 759     1521   2168   2306    366    284    122       C  
ATOM   1811  CZ  TYR A 759      13.295   0.434  13.823  1.00 15.69           C  
ANISOU 1811  CZ  TYR A 759     1538   2130   2292    430    300    124       C  
ATOM   1812  OH  TYR A 759      14.257  -0.312  14.469  1.00 18.09           O  
ANISOU 1812  OH  TYR A 759     1786   2464   2622    495    295    129       O  
ATOM   1813  N   ARG A 760       9.331   4.807   9.326  1.00 11.77           N  
ANISOU 1813  N   ARG A 760     1310   1501   1662    134    315    121       N  
ATOM   1814  CA  ARG A 760       8.098   5.450   8.839  1.00 10.34           C  
ANISOU 1814  CA  ARG A 760     1192   1281   1457     98    283    128       C  
ATOM   1815  C   ARG A 760       7.561   4.783   7.569  1.00  9.85           C  
ANISOU 1815  C   ARG A 760     1202   1186   1353    100    302    123       C  
ATOM   1816  O   ARG A 760       6.376   4.466   7.490  1.00  9.51           O  
ANISOU 1816  O   ARG A 760     1205   1109   1299    100    265    122       O  
ATOM   1817  CB  ARG A 760       8.301   6.960   8.601  1.00 10.58           C  
ANISOU 1817  CB  ARG A 760     1217   1317   1487     45    280    139       C  
ATOM   1818  CG  ARG A 760       7.018   7.727   8.232  1.00  9.49           C  
ANISOU 1818  CG  ARG A 760     1137   1137   1330     17    239    149       C  
ATOM   1819  CD  ARG A 760       6.687   7.687   6.730  1.00 13.12           C  
ANISOU 1819  CD  ARG A 760     1670   1572   1743     -1    257    154       C  
ATOM   1820  NE  ARG A 760       7.693   8.418   5.959  1.00 12.74           N  
ANISOU 1820  NE  ARG A 760     1622   1539   1679    -36    305    162       N  
ATOM   1821  CZ  ARG A 760       7.646   9.727   5.712  1.00 15.87           C  
ANISOU 1821  CZ  ARG A 760     2036   1922   2071    -80    295    179       C  
ATOM   1822  NH1 ARG A 760       6.640  10.459   6.173  1.00 14.02           N  
ANISOU 1822  NH1 ARG A 760     1820   1659   1848    -88    237    188       N  
ATOM   1823  NH2 ARG A 760       8.613  10.316   5.025  1.00 14.30           N  
ANISOU 1823  NH2 ARG A 760     1837   1738   1858   -117    345    189       N  
ATOM   1824  N   ASP A 761       8.427   4.584   6.580  1.00 10.39           N  
ANISOU 1824  N   ASP A 761     1282   1267   1399     99    358    116       N  
ATOM   1825  CA  ASP A 761       7.984   3.993   5.315  1.00 10.69           C  
ANISOU 1825  CA  ASP A 761     1399   1275   1389     99    377    107       C  
ATOM   1826  C   ASP A 761       7.506   2.545   5.503  1.00 10.25           C  
ANISOU 1826  C   ASP A 761     1368   1193   1333    142    369     91       C  
ATOM   1827  O   ASP A 761       6.518   2.117   4.904  1.00  9.69           O  
ANISOU 1827  O   ASP A 761     1365   1085   1233    134    345     84       O  
ATOM   1828  CB  ASP A 761       9.084   4.060   4.250  1.00 11.72           C  
ANISOU 1828  CB  ASP A 761     1536   1426   1490     92    450    101       C  
ATOM   1829  CG  ASP A 761       9.415   5.490   3.821  1.00 13.56           C  
ANISOU 1829  CG  ASP A 761     1767   1673   1713     36    462    121       C  
ATOM   1830  OD1 ASP A 761       8.518   6.355   3.833  1.00 16.97           O  
ANISOU 1830  OD1 ASP A 761     2231   2081   2137      3    411    137       O  
ATOM   1831  OD2 ASP A 761      10.582   5.742   3.458  1.00 17.40           O  
ANISOU 1831  OD2 ASP A 761     2217   2193   2200     26    524    121       O  
ATOM   1832  N   LYS A 762       8.179   1.801   6.374  1.00 10.05           N  
ANISOU 1832  N   LYS A 762     1290   1185   1343    187    383     85       N  
ATOM   1833  CA  LYS A 762       7.730   0.430   6.659  1.00 10.46           C  
ANISOU 1833  CA  LYS A 762     1371   1205   1400    228    374     74       C  
ATOM   1834  C   LYS A 762       6.373   0.414   7.365  1.00  9.63           C  
ANISOU 1834  C   LYS A 762     1283   1072   1305    212    311     84       C  
ATOM   1835  O   LYS A 762       5.513  -0.437   7.075  1.00  9.57           O  
ANISOU 1835  O   LYS A 762     1330   1024   1284    213    295     74       O  
ATOM   1836  CB  LYS A 762       8.789  -0.314   7.474  1.00 10.99           C  
ANISOU 1836  CB  LYS A 762     1378   1295   1501    285    400     72       C  
ATOM   1837  CG  LYS A 762      10.027  -0.581   6.656  1.00 14.50           C  
ANISOU 1837  CG  LYS A 762     1809   1763   1937    310    470     57       C  
ATOM   1838  CD  LYS A 762      11.071  -1.399   7.379  1.00 19.55           C  
ANISOU 1838  CD  LYS A 762     2389   2426   2615    377    494     54       C  
ATOM   1839  CE  LYS A 762      12.300  -1.513   6.487  1.00 23.09           C  
ANISOU 1839  CE  LYS A 762     2814   2904   3057    399    570     38       C  
ATOM   1840  NZ  LYS A 762      13.156  -2.673   6.845  1.00 26.05           N  
ANISOU 1840  NZ  LYS A 762     3154   3282   3460    480    600     27       N  
ATOM   1841  N   ILE A 763       6.159   1.385   8.257  1.00  8.86           N  
ANISOU 1841  N   ILE A 763     1139    995   1232    193    277    100       N  
ATOM   1842  CA  ILE A 763       4.882   1.532   8.937  1.00  8.74           C  
ANISOU 1842  CA  ILE A 763     1132    959   1229    177    224    109       C  
ATOM   1843  C   ILE A 763       3.773   1.908   7.943  1.00  7.80           C  
ANISOU 1843  C   ILE A 763     1070    811   1081    138    197    107       C  
ATOM   1844  O   ILE A 763       2.690   1.329   7.966  1.00  8.20           O  
ANISOU 1844  O   ILE A 763     1150    832   1132    133    167    104       O  
ATOM   1845  CB  ILE A 763       4.977   2.549  10.108  1.00  8.91           C  
ANISOU 1845  CB  ILE A 763     1095   1011   1280    169    199    122       C  
ATOM   1846  CG1AILE A 763       5.799   1.935  11.250  0.50  9.59           C  
ANISOU 1846  CG1AILE A 763     1132   1121   1390    210    208    125       C  
ATOM   1847  CG1BILE A 763       5.893   2.020  11.228  0.50  9.54           C  
ANISOU 1847  CG1BILE A 763     1123   1118   1385    209    210    124       C  
ATOM   1848  CG2 ILE A 763       3.588   2.929  10.610  1.00  8.38           C  
ANISOU 1848  CG2 ILE A 763     1039    924   1221    148    151    129       C  
ATOM   1849  CD1AILE A 763       6.428   2.949  12.182  0.50 11.02           C  
ANISOU 1849  CD1AILE A 763     1253   1342   1593    203    195    131       C  
ATOM   1850  CD1BILE A 763       5.257   1.026  12.175  0.50 10.39           C  
ANISOU 1850  CD1BILE A 763     1239   1206   1504    236    190    130       C  
ATOM   1851  N   THR A 764       4.068   2.846   7.043  1.00  7.98           N  
ANISOU 1851  N   THR A 764     1109    843   1080    111    207    110       N  
ATOM   1852  CA  THR A 764       3.129   3.185   5.985  1.00  8.03           C  
ANISOU 1852  CA  THR A 764     1176    823   1052     80    179    111       C  
ATOM   1853  C   THR A 764       2.730   1.967   5.166  1.00  8.27           C  
ANISOU 1853  C   THR A 764     1267    823   1052     86    184     92       C  
ATOM   1854  O   THR A 764       1.541   1.747   4.907  1.00  8.34           O  
ANISOU 1854  O   THR A 764     1310    806   1054     69    138     89       O  
ATOM   1855  CB  THR A 764       3.706   4.288   5.100  1.00  8.17           C  
ANISOU 1855  CB  THR A 764     1212    853   1041     52    199    120       C  
ATOM   1856  OG1 THR A 764       3.529   5.521   5.791  1.00  7.04           O  
ANISOU 1856  OG1 THR A 764     1031    720    925     35    171    138       O  
ATOM   1857  CG2 THR A 764       2.990   4.356   3.739  1.00  8.67           C  
ANISOU 1857  CG2 THR A 764     1355    889   1051     27    180    120       C  
ATOM   1858  N   ILE A 765       3.726   1.164   4.791  1.00  8.44           N  
ANISOU 1858  N   ILE A 765     1300    847   1058    112    238     76       N  
ATOM   1859  CA  ILE A 765       3.484  -0.015   3.964  1.00  8.98           C  
ANISOU 1859  CA  ILE A 765     1436    882   1093    121    250     52       C  
ATOM   1860  C   ILE A 765       2.601  -1.017   4.723  1.00  8.60           C  
ANISOU 1860  C   ILE A 765     1390    804   1075    131    216     47       C  
ATOM   1861  O   ILE A 765       1.652  -1.560   4.154  1.00  9.00           O  
ANISOU 1861  O   ILE A 765     1495    820   1106    110    184     34       O  
ATOM   1862  CB  ILE A 765       4.817  -0.626   3.468  1.00  9.52           C  
ANISOU 1862  CB  ILE A 765     1512    961   1144    155    324     35       C  
ATOM   1863  CG1 ILE A 765       5.445   0.292   2.414  1.00  9.37           C  
ANISOU 1863  CG1 ILE A 765     1514    965   1083    131    360     39       C  
ATOM   1864  CG2 ILE A 765       4.613  -2.054   2.912  1.00 10.60           C  
ANISOU 1864  CG2 ILE A 765     1717   1054   1257    176    338      5       C  
ATOM   1865  CD1 ILE A 765       6.914   0.047   2.205  1.00  9.51           C  
ANISOU 1865  CD1 ILE A 765     1502   1011   1099    164    439     29       C  
ATOM   1866  N   ALA A 766       2.896  -1.212   6.011  1.00  8.28           N  
ANISOU 1866  N   ALA A 766     1289    776   1080    158    219     59       N  
ATOM   1867  CA  ALA A 766       2.107  -2.098   6.859  1.00  8.79           C  
ANISOU 1867  CA  ALA A 766     1353    814   1173    164    193     61       C  
ATOM   1868  C   ALA A 766       0.662  -1.598   7.042  1.00  8.57           C  
ANISOU 1868  C   ALA A 766     1323    778   1157    123    135     70       C  
ATOM   1869  O   ALA A 766      -0.280  -2.397   7.011  1.00  9.18           O  
ANISOU 1869  O   ALA A 766     1429    821   1238    107    110     62       O  
ATOM   1870  CB  ALA A 766       2.796  -2.288   8.202  1.00  9.36           C  
ANISOU 1870  CB  ALA A 766     1366    907   1283    203    209     75       C  
ATOM   1871  N   ILE A 767       0.485  -0.283   7.188  1.00  8.23           N  
ANISOU 1871  N   ILE A 767     1245    763   1120    105    113     85       N  
ATOM   1872  CA  ILE A 767      -0.854   0.289   7.317  1.00  7.89           C  
ANISOU 1872  CA  ILE A 767     1192    715   1090     74     59     93       C  
ATOM   1873  C   ILE A 767      -1.667   0.046   6.054  1.00  7.36           C  
ANISOU 1873  C   ILE A 767     1185    621    990     44     28     80       C  
ATOM   1874  O   ILE A 767      -2.829  -0.347   6.134  1.00  8.71           O  
ANISOU 1874  O   ILE A 767     1359    774   1176     23    -12     76       O  
ATOM   1875  CB  ILE A 767      -0.805   1.782   7.655  1.00  7.99           C  
ANISOU 1875  CB  ILE A 767     1165    757   1115     67     45    110       C  
ATOM   1876  CG1 ILE A 767      -0.445   1.953   9.130  1.00  8.52           C  
ANISOU 1876  CG1 ILE A 767     1173    847   1219     90     57    120       C  
ATOM   1877  CG2 ILE A 767      -2.151   2.455   7.367  1.00  8.43           C  
ANISOU 1877  CG2 ILE A 767     1223    803   1176     41    -11    116       C  
ATOM   1878  CD1 ILE A 767      -0.025   3.352   9.481  1.00  9.24           C  
ANISOU 1878  CD1 ILE A 767     1229    963   1317     86     54    131       C  
ATOM   1879  N   LEU A 768      -1.044   0.252   4.893  1.00  7.80           N  
ANISOU 1879  N   LEU A 768     1288    676    998     40     46     71       N  
ATOM   1880  CA  LEU A 768      -1.719  -0.020   3.623  1.00  8.37           C  
ANISOU 1880  CA  LEU A 768     1429    724   1027     13     14     56       C  
ATOM   1881  C   LEU A 768      -2.106  -1.483   3.501  1.00  8.82           C  
ANISOU 1881  C   LEU A 768     1525    745   1082      9     13     32       C  
ATOM   1882  O   LEU A 768      -3.191  -1.789   3.008  1.00 10.01           O  
ANISOU 1882  O   LEU A 768     1705    875   1225    -23    -37     21       O  
ATOM   1883  CB  LEU A 768      -0.853   0.409   2.436  1.00  8.55           C  
ANISOU 1883  CB  LEU A 768     1504    754    991     11     46     52       C  
ATOM   1884  CG  LEU A 768      -0.642   1.921   2.304  1.00  8.72           C  
ANISOU 1884  CG  LEU A 768     1507    801   1007      1     39     78       C  
ATOM   1885  CD1 LEU A 768       0.363   2.186   1.214  1.00  9.02           C  
ANISOU 1885  CD1 LEU A 768     1596    846    987     -1     87     75       C  
ATOM   1886  CD2 LEU A 768      -1.956   2.664   1.999  1.00  9.60           C  
ANISOU 1886  CD2 LEU A 768     1626    904   1117    -25    -37     91       C  
ATOM   1887  N   GLN A 769      -1.220  -2.377   3.944  1.00  9.10           N  
ANISOU 1887  N   GLN A 769     1561    771   1127     42     66     22       N  
ATOM   1888  CA  GLN A 769      -1.522  -3.812   3.962  1.00 10.28           C  
ANISOU 1888  CA  GLN A 769     1750    875   1280     43     70      1       C  
ATOM   1889  C   GLN A 769      -2.761  -4.092   4.819  1.00  9.79           C  
ANISOU 1889  C   GLN A 769     1654    801   1264     16     25     11       C  
ATOM   1890  O   GLN A 769      -3.704  -4.751   4.367  1.00  9.96           O  
ANISOU 1890  O   GLN A 769     1714    790   1281    -19    -11     -6       O  
ATOM   1891  CB  GLN A 769      -0.314  -4.605   4.471  1.00 11.21           C  
ANISOU 1891  CB  GLN A 769     1864    986   1408     94    134     -4       C  
ATOM   1892  CG  GLN A 769      -0.470  -6.115   4.330  1.00 14.45           C  
ANISOU 1892  CG  GLN A 769     2335   1340   1816    100    145    -29       C  
ATOM   1893  CD  GLN A 769       0.639  -6.903   5.016  1.00 14.96           C  
ANISOU 1893  CD  GLN A 769     2388   1394   1901    160    201    -27       C  
ATOM   1894  OE1 GLN A 769       1.742  -6.401   5.220  1.00 18.07           O  
ANISOU 1894  OE1 GLN A 769     2741   1826   2297    198    239    -17       O  
ATOM   1895  NE2 GLN A 769       0.339  -8.145   5.384  1.00 20.31           N  
ANISOU 1895  NE2 GLN A 769     3102   2019   2595    166    203    -35       N  
ATOM   1896  N   LEU A 770      -2.762  -3.570   6.042  1.00  8.92           N  
ANISOU 1896  N   LEU A 770     1473    718   1197     30     28     37       N  
ATOM   1897  CA  LEU A 770      -3.890  -3.765   6.957  1.00  9.12           C  
ANISOU 1897  CA  LEU A 770     1460    739   1267      7     -3     49       C  
ATOM   1898  C   LEU A 770      -5.201  -3.161   6.435  1.00 10.14           C  
ANISOU 1898  C   LEU A 770     1578    874   1400    -37    -65     48       C  
ATOM   1899  O   LEU A 770      -6.279  -3.739   6.617  1.00 10.53           O  
ANISOU 1899  O   LEU A 770     1622    905   1475    -70    -95     44       O  
ATOM   1900  CB  LEU A 770      -3.564  -3.200   8.336  1.00  9.00           C  
ANISOU 1900  CB  LEU A 770     1376    756   1286     34     16     75       C  
ATOM   1901  CG  LEU A 770      -2.388  -3.899   9.031  1.00  8.59           C  
ANISOU 1901  CG  LEU A 770     1326    700   1238     80     67     80       C  
ATOM   1902  CD1 LEU A 770      -1.889  -3.102  10.227  1.00 10.00           C  
ANISOU 1902  CD1 LEU A 770     1441    920   1439    106     78    102       C  
ATOM   1903  CD2 LEU A 770      -2.745  -5.332   9.446  1.00  9.54           C  
ANISOU 1903  CD2 LEU A 770     1479    774   1373     77     76     77       C  
ATOM   1904  N   GLN A 771      -5.097  -2.015   5.768  1.00 10.31           N  
ANISOU 1904  N   GLN A 771     1598    921   1398    -37    -85     52       N  
ATOM   1905  CA  GLN A 771      -6.244  -1.362   5.144  1.00 11.73           C  
ANISOU 1905  CA  GLN A 771     1773   1107   1577    -69   -149     53       C  
ATOM   1906  C   GLN A 771      -6.811  -2.281   4.068  1.00 11.55           C  
ANISOU 1906  C   GLN A 771     1814   1050   1523   -104   -183     27       C  
ATOM   1907  O   GLN A 771      -7.995  -2.626   4.082  1.00 12.24           O  
ANISOU 1907  O   GLN A 771     1885   1129   1636   -140   -230     21       O  
ATOM   1908  CB  GLN A 771      -5.770  -0.006   4.584  1.00 11.66           C  
ANISOU 1908  CB  GLN A 771     1767   1123   1539    -56   -156     67       C  
ATOM   1909  CG  GLN A 771      -6.575   0.706   3.464  1.00 16.53           C  
ANISOU 1909  CG  GLN A 771     2412   1741   2127    -80   -221     68       C  
ATOM   1910  CD  GLN A 771      -5.825   1.947   2.894  1.00 17.60           C  
ANISOU 1910  CD  GLN A 771     2569   1892   2226    -66   -211     85       C  
ATOM   1911  OE1 GLN A 771      -5.262   2.751   3.655  1.00 20.69           O  
ANISOU 1911  OE1 GLN A 771     2918   2302   2641    -44   -181    103       O  
ATOM   1912  NE2 GLN A 771      -5.817   2.102   1.553  1.00 15.58           N  
ANISOU 1912  NE2 GLN A 771     2384   1626   1908    -81   -235     81       N  
ATOM   1913  N   GLU A 772      -5.941  -2.711   3.153  1.00 11.70           N  
ANISOU 1913  N   GLU A 772     1907   1052   1488    -95   -154      8       N  
ATOM   1914  CA  GLU A 772      -6.366  -3.528   2.025  1.00 12.59           C  
ANISOU 1914  CA  GLU A 772     2095   1131   1558   -128   -185    -23       C  
ATOM   1915  C   GLU A 772      -6.954  -4.881   2.452  1.00 13.06           C  
ANISOU 1915  C   GLU A 772     2164   1150   1650   -153   -188    -41       C  
ATOM   1916  O   GLU A 772      -7.892  -5.380   1.823  1.00 14.54           O  
ANISOU 1916  O   GLU A 772     2381   1315   1828   -198   -242    -62       O  
ATOM   1917  CB  GLU A 772      -5.213  -3.700   1.032  1.00 12.75           C  
ANISOU 1917  CB  GLU A 772     2194   1141   1511   -107   -139    -41       C  
ATOM   1918  CG  GLU A 772      -4.813  -2.376   0.400  1.00 12.90           C  
ANISOU 1918  CG  GLU A 772     2217   1193   1491    -98   -143    -22       C  
ATOM   1919  CD  GLU A 772      -3.638  -2.473  -0.542  1.00 13.88           C  
ANISOU 1919  CD  GLU A 772     2411   1313   1548    -80    -87    -38       C  
ATOM   1920  OE1 GLU A 772      -3.148  -3.597  -0.817  1.00 13.96           O  
ANISOU 1920  OE1 GLU A 772     2474   1293   1537    -69    -47    -68       O  
ATOM   1921  OE2 GLU A 772      -3.213  -1.393  -1.006  1.00 13.73           O  
ANISOU 1921  OE2 GLU A 772     2398   1321   1499    -75    -80    -18       O  
ATOM   1922  N   GLU A 773      -6.418  -5.446   3.534  1.00 13.15           N  
ANISOU 1922  N   GLU A 773     2149   1152   1697   -126   -135    -31       N  
ATOM   1923  CA  GLU A 773      -6.870  -6.747   4.041  1.00 13.95           C  
ANISOU 1923  CA  GLU A 773     2264   1208   1829   -147   -129    -42       C  
ATOM   1924  C   GLU A 773      -8.161  -6.632   4.855  1.00 13.98           C  
ANISOU 1924  C   GLU A 773     2197   1224   1891   -186   -168    -25       C  
ATOM   1925  O   GLU A 773      -8.715  -7.646   5.285  1.00 14.74           O  
ANISOU 1925  O   GLU A 773     2300   1284   2017   -217   -168    -31       O  
ATOM   1926  CB  GLU A 773      -5.774  -7.380   4.895  1.00 13.84           C  
ANISOU 1926  CB  GLU A 773     2253   1177   1827    -98    -59    -34       C  
ATOM   1927  CG  GLU A 773      -4.572  -7.864   4.092  1.00 16.53           C  
ANISOU 1927  CG  GLU A 773     2667   1495   2118    -60    -13    -58       C  
ATOM   1928  CD  GLU A 773      -3.458  -8.426   4.965  1.00 19.08           C  
ANISOU 1928  CD  GLU A 773     2982   1808   2460     -2     51    -47       C  
ATOM   1929  OE1 GLU A 773      -3.536  -8.310   6.210  1.00 22.37           O  
ANISOU 1929  OE1 GLU A 773     3338   2241   2920     10     58    -16       O  
ATOM   1930  OE2 GLU A 773      -2.497  -8.976   4.392  1.00 22.72           O  
ANISOU 1930  OE2 GLU A 773     3498   2247   2889     34     93    -68       O  
ATOM   1931  N   GLY A 774      -8.630  -5.404   5.072  1.00 13.42           N  
ANISOU 1931  N   GLY A 774     2059   1201   1838   -184   -198     -4       N  
ATOM   1932  CA  GLY A 774      -9.861  -5.167   5.818  1.00 13.93           C  
ANISOU 1932  CA  GLY A 774     2047   1286   1960   -215   -231     11       C  
ATOM   1933  C   GLY A 774      -9.678  -5.166   7.325  1.00 13.39           C  
ANISOU 1933  C   GLY A 774     1921   1230   1935   -191   -181     38       C  
ATOM   1934  O   GLY A 774     -10.656  -5.066   8.073  1.00 13.61           O  
ANISOU 1934  O   GLY A 774     1887   1274   2012   -214   -193     50       O  
ATOM   1935  N   LYS A 775      -8.433  -5.286   7.777  1.00 12.66           N  
ANISOU 1935  N   LYS A 775     1851   1135   1826   -144   -126     46       N  
ATOM   1936  CA  LYS A 775      -8.143  -5.399   9.205  1.00 12.76           C  
ANISOU 1936  CA  LYS A 775     1823   1157   1869   -118    -81     70       C  
ATOM   1937  C   LYS A 775      -8.409  -4.108   9.973  1.00 11.89           C  
ANISOU 1937  C   LYS A 775     1637   1099   1782   -101    -87     91       C  
ATOM   1938  O   LYS A 775      -8.871  -4.156  11.112  1.00 11.99           O  
ANISOU 1938  O   LYS A 775     1604   1123   1829   -104    -69    109       O  
ATOM   1939  CB  LYS A 775      -6.702  -5.884   9.436  1.00 13.15           C  
ANISOU 1939  CB  LYS A 775     1912   1191   1892    -68    -29     73       C  
ATOM   1940  CG  LYS A 775      -6.354  -6.156  10.893  1.00 17.01           C  
ANISOU 1940  CG  LYS A 775     2372   1685   2405    -40     11     99       C  
ATOM   1941  CD  LYS A 775      -6.962  -7.465  11.372  1.00 22.93           C  
ANISOU 1941  CD  LYS A 775     3149   2387   3177    -70     22    104       C  
ATOM   1942  CE  LYS A 775      -7.190  -7.461  12.869  1.00 25.39           C  
ANISOU 1942  CE  LYS A 775     3418   2715   3515    -62     47    136       C  
ATOM   1943  NZ  LYS A 775      -7.745  -8.755  13.329  1.00 28.50           N  
ANISOU 1943  NZ  LYS A 775     3845   3057   3928    -95     64    145       N  
ATOM   1944  N   LEU A 776      -8.152  -2.958   9.356  1.00 11.39           N  
ANISOU 1944  N   LEU A 776     1565   1063   1699    -86   -109     89       N  
ATOM   1945  CA  LEU A 776      -8.411  -1.682  10.023  1.00 10.80           C  
ANISOU 1945  CA  LEU A 776     1427   1030   1647    -68   -115    106       C  
ATOM   1946  C   LEU A 776      -9.906  -1.494  10.237  1.00 11.33           C  
ANISOU 1946  C   LEU A 776     1440   1108   1757   -100   -152    108       C  
ATOM   1947  O   LEU A 776     -10.324  -1.031  11.293  1.00 10.47           O  
ANISOU 1947  O   LEU A 776     1274   1023   1680    -90   -137    121       O  
ATOM   1948  CB  LEU A 776      -7.813  -0.513   9.231  1.00 10.66           C  
ANISOU 1948  CB  LEU A 776     1421   1030   1599    -49   -132    105       C  
ATOM   1949  CG  LEU A 776      -6.290  -0.492   9.073  1.00 11.06           C  
ANISOU 1949  CG  LEU A 776     1508   1081   1615    -17    -90    104       C  
ATOM   1950  CD1 LEU A 776      -5.875   0.777   8.322  1.00 12.08           C  
ANISOU 1950  CD1 LEU A 776     1645   1228   1718     -9   -106    107       C  
ATOM   1951  CD2 LEU A 776      -5.563  -0.603  10.421  1.00 12.23           C  
ANISOU 1951  CD2 LEU A 776     1625   1243   1779     14    -45    117       C  
ATOM   1952  N   HIS A 777     -10.700  -1.870   9.236  1.00 12.08           N  
ANISOU 1952  N   HIS A 777     1551   1187   1850   -139   -199     93       N  
ATOM   1953  CA  HIS A 777     -12.153  -1.820   9.346  1.00 13.37           C  
ANISOU 1953  CA  HIS A 777     1656   1363   2060   -174   -239     92       C  
ATOM   1954  C   HIS A 777     -12.631  -2.715  10.495  1.00 13.16           C  
ANISOU 1954  C   HIS A 777     1598   1329   2072   -196   -199    101       C  
ATOM   1955  O   HIS A 777     -13.445  -2.300  11.326  1.00 12.83           O  
ANISOU 1955  O   HIS A 777     1485   1315   2074   -198   -192    111       O  
ATOM   1956  CB  HIS A 777     -12.800  -2.230   8.020  1.00 14.54           C  
ANISOU 1956  CB  HIS A 777     1837   1494   2194   -216   -302     72       C  
ATOM   1957  CG  HIS A 777     -14.295  -2.185   8.040  1.00 18.27           C  
ANISOU 1957  CG  HIS A 777     2240   1983   2718   -254   -350     70       C  
ATOM   1958  ND1 HIS A 777     -15.068  -3.294   8.302  1.00 22.38           N  
ANISOU 1958  ND1 HIS A 777     2745   2487   3273   -307   -350     62       N  
ATOM   1959  CD2 HIS A 777     -15.161  -1.161   7.848  1.00 21.88           C  
ANISOU 1959  CD2 HIS A 777     2636   2475   3203   -246   -401     75       C  
ATOM   1960  CE1 HIS A 777     -16.346  -2.961   8.255  1.00 23.36           C  
ANISOU 1960  CE1 HIS A 777     2793   2639   3445   -334   -397     61       C  
ATOM   1961  NE2 HIS A 777     -16.430  -1.671   7.987  1.00 23.57           N  
ANISOU 1961  NE2 HIS A 777     2789   2698   3470   -292   -430     69       N  
ATOM   1962  N   MET A 778     -12.093  -3.931  10.561  1.00 12.83           N  
ANISOU 1962  N   MET A 778     1613   1247   2014   -209   -167     96       N  
ATOM   1963  CA  MET A 778     -12.448  -4.880  11.621  1.00 13.79           C  
ANISOU 1963  CA  MET A 778     1722   1353   2166   -232   -126    109       C  
ATOM   1964  C   MET A 778     -12.088  -4.340  12.999  1.00 12.39           C  
ANISOU 1964  C   MET A 778     1505   1205   1997   -192    -76    133       C  
ATOM   1965  O   MET A 778     -12.850  -4.488  13.954  1.00 12.58           O  
ANISOU 1965  O   MET A 778     1482   1241   2056   -210    -52    147       O  
ATOM   1966  CB  MET A 778     -11.730  -6.209  11.412  1.00 14.75           C  
ANISOU 1966  CB  MET A 778     1925   1417   2261   -240   -100    102       C  
ATOM   1967  CG  MET A 778     -12.295  -7.076  10.309  1.00 18.61           C  
ANISOU 1967  CG  MET A 778     2459   1866   2747   -295   -141     76       C  
ATOM   1968  SD  MET A 778     -11.418  -8.654  10.207  1.00 26.85           S  
ANISOU 1968  SD  MET A 778     3606   2834   3763   -295   -101     67       S  
ATOM   1969  CE  MET A 778     -11.402  -9.136  11.931  1.00 22.50           C  
ANISOU 1969  CE  MET A 778     3028   2277   3243   -285    -38    106       C  
ATOM   1970  N   MET A 779     -10.917  -3.716  13.097  1.00 10.70           N  
ANISOU 1970  N   MET A 779     1312   1003   1750   -139    -60    137       N  
ATOM   1971  CA  MET A 779     -10.474  -3.157  14.362  1.00 10.42           C  
ANISOU 1971  CA  MET A 779     1248    997   1716   -101    -20    156       C  
ATOM   1972  C   MET A 779     -11.373  -2.015  14.828  1.00 10.26           C  
ANISOU 1972  C   MET A 779     1154   1019   1727    -98    -32    159       C  
ATOM   1973  O   MET A 779     -11.668  -1.907  16.015  1.00  9.88           O  
ANISOU 1973  O   MET A 779     1071    990   1694    -91      3    172       O  
ATOM   1974  CB  MET A 779      -9.015  -2.714  14.264  1.00 10.53           C  
ANISOU 1974  CB  MET A 779     1294   1017   1691    -52     -8    156       C  
ATOM   1975  CG  MET A 779      -8.062  -3.891  14.216  1.00 11.60           C  
ANISOU 1975  CG  MET A 779     1491   1115   1802    -40     19    158       C  
ATOM   1976  SD  MET A 779      -6.418  -3.343  13.725  1.00 18.31           S  
ANISOU 1976  SD  MET A 779     2367   1977   2612     12     27    152       S  
ATOM   1977  CE  MET A 779      -6.282  -1.967  14.810  1.00 10.64           C  
ANISOU 1977  CE  MET A 779     1337   1057   1650     38     33    165       C  
ATOM   1978  N   LYS A 780     -11.803  -1.162  13.895  1.00 10.47           N  
ANISOU 1978  N   LYS A 780     1160   1058   1760   -100    -80    146       N  
ATOM   1979  CA  LYS A 780     -12.724  -0.076  14.231  1.00 11.01           C  
ANISOU 1979  CA  LYS A 780     1159   1162   1863    -91    -95    146       C  
ATOM   1980  C   LYS A 780     -14.044  -0.660  14.738  1.00 11.31           C  
ANISOU 1980  C   LYS A 780     1142   1208   1949   -131    -87    149       C  
ATOM   1981  O   LYS A 780     -14.572  -0.222  15.766  1.00 11.38           O  
ANISOU 1981  O   LYS A 780     1097   1244   1984   -119    -55    156       O  
ATOM   1982  CB  LYS A 780     -12.976   0.840  13.033  1.00 11.31           C  
ANISOU 1982  CB  LYS A 780     1194   1206   1898    -85   -156    136       C  
ATOM   1983  CG  LYS A 780     -13.955   1.989  13.320  1.00 14.67           C  
ANISOU 1983  CG  LYS A 780     1547   1662   2364    -67   -177    136       C  
ATOM   1984  CD  LYS A 780     -13.230   3.280  13.612  1.00 18.57           C  
ANISOU 1984  CD  LYS A 780     2048   2168   2841    -18   -168    139       C  
ATOM   1985  CE  LYS A 780     -14.194   4.442  13.864  1.00 18.88           C  
ANISOU 1985  CE  LYS A 780     2023   2229   2920      8   -189    137       C  
ATOM   1986  NZ  LYS A 780     -14.818   5.016  12.636  1.00 20.40           N  
ANISOU 1986  NZ  LYS A 780     2210   2418   3123      8   -259    135       N  
ATOM   1987  N   GLU A 781     -14.569  -1.656  14.025  1.00 11.59           N  
ANISOU 1987  N   GLU A 781     1192   1218   1995   -181   -112    142       N  
ATOM   1988  CA  GLU A 781     -15.828  -2.302  14.435  1.00 13.03           C  
ANISOU 1988  CA  GLU A 781     1319   1406   2227   -231   -103    145       C  
ATOM   1989  C   GLU A 781     -15.713  -2.920  15.826  1.00 12.59           C  
ANISOU 1989  C   GLU A 781     1263   1347   2174   -234    -30    165       C  
ATOM   1990  O   GLU A 781     -16.643  -2.838  16.631  1.00 13.39           O  
ANISOU 1990  O   GLU A 781     1299   1474   2314   -251     -1    172       O  
ATOM   1991  CB  GLU A 781     -16.274  -3.351  13.415  1.00 14.34           C  
ANISOU 1991  CB  GLU A 781     1513   1536   2398   -291   -145    131       C  
ATOM   1992  CG  GLU A 781     -16.713  -2.763  12.089  1.00 18.90           C  
ANISOU 1992  CG  GLU A 781     2080   2124   2976   -296   -224    112       C  
ATOM   1993  CD  GLU A 781     -17.689  -3.651  11.331  1.00 25.43           C  
ANISOU 1993  CD  GLU A 781     2898   2935   3831   -367   -272     96       C  
ATOM   1994  OE1 GLU A 781     -17.668  -4.891  11.511  1.00 28.86           O  
ANISOU 1994  OE1 GLU A 781     3369   3330   4265   -413   -246     95       O  
ATOM   1995  OE2 GLU A 781     -18.486  -3.098  10.543  1.00 29.64           O  
ANISOU 1995  OE2 GLU A 781     3387   3490   4383   -377   -340     86       O  
ATOM   1996  N   LYS A 782     -14.551  -3.504  16.122  1.00 11.92           N  
ANISOU 1996  N   LYS A 782     1251   1233   2046   -215      1    174       N  
ATOM   1997  CA  LYS A 782     -14.310  -4.139  17.415  1.00 12.04           C  
ANISOU 1997  CA  LYS A 782     1281   1240   2052   -213     65    198       C  
ATOM   1998  C   LYS A 782     -14.406  -3.152  18.582  1.00 11.61           C  
ANISOU 1998  C   LYS A 782     1179   1232   2000   -175    101    207       C  
ATOM   1999  O   LYS A 782     -14.980  -3.463  19.628  1.00 12.15           O  
ANISOU 1999  O   LYS A 782     1222   1311   2082   -192    150    223       O  
ATOM   2000  CB  LYS A 782     -12.935  -4.816  17.430  1.00 11.70           C  
ANISOU 2000  CB  LYS A 782     1323   1160   1962   -186     81    206       C  
ATOM   2001  CG  LYS A 782     -12.568  -5.467  18.769  1.00 12.55           C  
ANISOU 2001  CG  LYS A 782     1458   1258   2053   -175    140    235       C  
ATOM   2002  CD  LYS A 782     -11.180  -6.086  18.722  1.00 12.19           C  
ANISOU 2002  CD  LYS A 782     1489   1177   1964   -138    147    242       C  
ATOM   2003  CE  LYS A 782     -10.712  -6.498  20.110  1.00 12.75           C  
ANISOU 2003  CE  LYS A 782     1585   1247   2011   -113    196    274       C  
ATOM   2004  NZ  LYS A 782      -9.340  -7.085  20.070  1.00 14.50           N  
ANISOU 2004  NZ  LYS A 782     1874   1440   2197    -68    198    282       N  
ATOM   2005  N   TRP A 783     -13.825  -1.969  18.401  1.00 10.83           N  
ANISOU 2005  N   TRP A 783     1075   1157   1883   -126     80    196       N  
ATOM   2006  CA  TRP A 783     -13.667  -1.027  19.500  1.00 11.04           C  
ANISOU 2006  CA  TRP A 783     1075   1219   1900    -84    113    200       C  
ATOM   2007  C   TRP A 783     -14.759   0.034  19.557  1.00 11.76           C  
ANISOU 2007  C   TRP A 783     1089   1346   2033    -78    103    187       C  
ATOM   2008  O   TRP A 783     -14.934   0.680  20.593  1.00 13.23           O  
ANISOU 2008  O   TRP A 783     1247   1560   2218    -51    141    188       O  
ATOM   2009  CB  TRP A 783     -12.267  -0.388  19.453  1.00  9.76           C  
ANISOU 2009  CB  TRP A 783      958   1058   1694    -35    102    197       C  
ATOM   2010  CG  TRP A 783     -11.231  -1.394  19.786  1.00  8.95           C  
ANISOU 2010  CG  TRP A 783      917    928   1554    -30    125    213       C  
ATOM   2011  CD1 TRP A 783     -10.409  -2.053  18.910  1.00  8.86           C  
ANISOU 2011  CD1 TRP A 783      957    884   1524    -30    105    210       C  
ATOM   2012  CD2 TRP A 783     -10.939  -1.912  21.087  1.00  8.28           C  
ANISOU 2012  CD2 TRP A 783      853    846   1447    -20    172    234       C  
ATOM   2013  NE1 TRP A 783      -9.611  -2.944  19.598  1.00  8.94           N  
ANISOU 2013  NE1 TRP A 783     1015    876   1507    -16    135    229       N  
ATOM   2014  CE2 TRP A 783      -9.924  -2.880  20.934  1.00  8.71           C  
ANISOU 2014  CE2 TRP A 783      970    868   1473    -11    173    246       C  
ATOM   2015  CE3 TRP A 783     -11.443  -1.660  22.371  1.00  9.09           C  
ANISOU 2015  CE3 TRP A 783      932    976   1547    -15    215    245       C  
ATOM   2016  CZ2 TRP A 783      -9.394  -3.586  22.021  1.00  9.91           C  
ANISOU 2016  CZ2 TRP A 783     1160   1011   1596      5    209    272       C  
ATOM   2017  CZ3 TRP A 783     -10.925  -2.375  23.451  1.00  9.17           C  
ANISOU 2017  CZ3 TRP A 783      985    979   1521     -5    253    270       C  
ATOM   2018  CH2 TRP A 783      -9.906  -3.317  23.265  1.00  9.86           C  
ANISOU 2018  CH2 TRP A 783     1133   1031   1581      6    246    285       C  
ATOM   2019  N   TRP A 784     -15.509   0.193  18.469  1.00 12.51           N  
ANISOU 2019  N   TRP A 784     1150   1440   2163    -99     52    175       N  
ATOM   2020  CA  TRP A 784     -16.650   1.136  18.467  1.00 14.13           C  
ANISOU 2020  CA  TRP A 784     1272   1679   2416    -88     38    164       C  
ATOM   2021  C   TRP A 784     -18.034   0.475  18.702  1.00 17.32           C  
ANISOU 2021  C   TRP A 784     1607   2099   2876   -138     55    167       C  
ATOM   2022  O   TRP A 784     -18.993   1.166  19.049  1.00 19.31           O  
ANISOU 2022  O   TRP A 784     1780   2385   3171   -124     64    160       O  
ATOM   2023  CB  TRP A 784     -16.650   2.003  17.191  1.00 12.88           C  
ANISOU 2023  CB  TRP A 784     1112   1519   2264    -69    -35    150       C  
ATOM   2024  CG  TRP A 784     -15.820   3.283  17.288  1.00 11.31           C  
ANISOU 2024  CG  TRP A 784      938   1323   2036    -12    -41    145       C  
ATOM   2025  CD1 TRP A 784     -16.298   4.570  17.363  1.00  9.90           C  
ANISOU 2025  CD1 TRP A 784      717   1164   1882     29    -57    136       C  
ATOM   2026  CD2 TRP A 784     -14.386   3.392  17.323  1.00  8.13           C  
ANISOU 2026  CD2 TRP A 784      606    903   1579      9    -32    148       C  
ATOM   2027  NE1 TRP A 784     -15.248   5.466  17.440  1.00  8.47           N  
ANISOU 2027  NE1 TRP A 784      583    973   1664     67    -58    132       N  
ATOM   2028  CE2 TRP A 784     -14.068   4.770  17.408  1.00  7.26           C  
ANISOU 2028  CE2 TRP A 784      494    802   1464     54    -44    140       C  
ATOM   2029  CE3 TRP A 784     -13.335   2.461  17.268  1.00  8.23           C  
ANISOU 2029  CE3 TRP A 784      682    894   1552     -4    -17    156       C  
ATOM   2030  CZ2 TRP A 784     -12.749   5.230  17.474  1.00  7.29           C  
ANISOU 2030  CZ2 TRP A 784      551    795   1424     77    -39    139       C  
ATOM   2031  CZ3 TRP A 784     -12.027   2.925  17.323  1.00  7.78           C  
ANISOU 2031  CZ3 TRP A 784      672    831   1453     26    -13    156       C  
ATOM   2032  CH2 TRP A 784     -11.751   4.291  17.421  1.00  8.25           C  
ANISOU 2032  CH2 TRP A 784      722    902   1509     61    -24    147       C  
ATOM   2033  N   ARG A 785     -18.122  -0.841  18.520  1.00 20.41           N  
ANISOU 2033  N   ARG A 785     2025   2463   3268   -195     62    176       N  
ATOM   2034  CA  ARG A 785     -19.381  -1.595  18.683  1.00 23.12           C  
ANISOU 2034  CA  ARG A 785     2305   2815   3665   -256     78    180       C  
ATOM   2035  C   ARG A 785     -20.013  -1.478  20.075  1.00 24.88           C  
ANISOU 2035  C   ARG A 785     2474   3072   3909   -254    157    192       C  
ATOM   2036  O   ARG A 785     -19.298  -1.373  21.080  1.00 25.19           O  
ANISOU 2036  O   ARG A 785     2556   3112   3904   -222    211    204       O  
ATOM   2037  CB  ARG A 785     -19.170  -3.079  18.350  1.00 23.82           C  
ANISOU 2037  CB  ARG A 785     2453   2855   3741   -318     79    189       C  
ATOM   2038  N   GLY A 786     -21.352  -1.493  20.108  1.00 26.77           N  
ANISOU 2038  N   GLY A 786     2617   3342   4213   -289    163    187       N  
ATOM   2039  CA  GLY A 786     -22.147  -1.543  21.350  1.00 28.35           C  
ANISOU 2039  CA  GLY A 786     2754   3576   4440   -301    246    198       C  
ATOM   2040  C   GLY A 786     -22.201  -0.253  22.164  1.00 28.74           C  
ANISOU 2040  C   GLY A 786     2767   3667   4485   -229    283    188       C  
ATOM   2041  O   GLY A 786     -21.230   0.508  22.172  1.00 28.65           O  
ANISOU 2041  O   GLY A 786     2812   3647   4427   -169    265    181       O  
ATOM   2042  N   ASN A 787     -23.318   0.019  22.848  1.00 29.29           N  
ANISOU 2042  N   ASN A 787     2743   3782   4604   -233    336    185       N  
ATOM   2043  CA  ASN A 787     -24.547  -0.784  22.806  1.00 29.86           C  
ANISOU 2043  CA  ASN A 787     2731   3872   4743   -307    356    191       C  
ATOM   2044  C   ASN A 787     -25.731  -0.010  22.205  1.00 29.80           C  
ANISOU 2044  C   ASN A 787     2597   3909   4816   -292    313    169       C  
ATOM   2045  O   ASN A 787     -26.695  -0.611  21.716  1.00 30.95           O  
ANISOU 2045  O   ASN A 787     2667   4068   5025   -356    291    168       O  
ATOM   2046  CB  ASN A 787     -24.901  -1.304  24.202  1.00 30.96           C  
ANISOU 2046  CB  ASN A 787     2861   4029   4874   -335    468    212       C  
ATOM   2047  N   GLY A 788     -25.668   1.320  22.263  1.00 28.33           N  
ANISOU 2047  N   GLY A 788     2388   3746   4631   -209    299    151       N  
ATOM   2048  CA  GLY A 788     -26.520   2.138  21.413  1.00 26.15           C  
ANISOU 2048  CA  GLY A 788     2016   3498   4421   -179    230    131       C  
ATOM   2049  C   GLY A 788     -27.474   3.154  22.015  1.00 25.24           C  
ANISOU 2049  C   GLY A 788     1792   3436   4363   -121    271    115       C  
ATOM   2050  O   GLY A 788     -27.974   3.008  23.135  1.00 25.69           O  
ANISOU 2050  O   GLY A 788     1805   3524   4433   -128    368    118       O  
ATOM   2051  N   CYS A 789     -27.724   4.191  21.227  1.00 23.72           N  
ANISOU 2051  N   CYS A 789     1561   3251   4202    -61    195     99       N  
ATOM   2052  CA  CYS A 789     -28.661   5.247  21.570  1.00 23.11           C  
ANISOU 2052  CA  CYS A 789     1376   3218   4187      7    215     80       C  
ATOM   2053  C   CYS A 789     -29.532   5.520  20.352  1.00 23.42           C  
ANISOU 2053  C   CYS A 789     1324   3275   4298     11    111     74       C  
ATOM   2054  O   CYS A 789     -29.102   5.278  19.221  1.00 23.18           O  
ANISOU 2054  O   CYS A 789     1347   3213   4246    -13     16     80       O  
ATOM   2055  CB  CYS A 789     -27.900   6.521  21.943  1.00 22.22           C  
ANISOU 2055  CB  CYS A 789     1330   3085   4027    102    224     67       C  
ATOM   2056  SG  CYS A 789     -26.895   6.408  23.442  1.00 19.33           S  
ANISOU 2056  SG  CYS A 789     1068   2705   3573    110    337     69       S  
ATOM   2057  N   PRO A 790     -30.750   6.038  20.569  1.00 24.14           N  
ANISOU 2057  N   PRO A 790     1278   3419   4474     45    126     61       N  
ATOM   2058  CA  PRO A 790     -31.589   6.425  19.435  1.00 25.15           C  
ANISOU 2058  CA  PRO A 790     1314   3568   4673     62     18     55       C  
ATOM   2059  C   PRO A 790     -31.021   7.611  18.655  1.00 24.75           C  
ANISOU 2059  C   PRO A 790     1328   3481   4593    149    -69     51       C  
ATOM   2060  O   PRO A 790     -31.503   7.927  17.563  1.00 25.91           O  
ANISOU 2060  O   PRO A 790     1431   3634   4779    165   -176     52       O  
ATOM   2061  CB  PRO A 790     -32.907   6.835  20.097  1.00 26.10           C  
ANISOU 2061  CB  PRO A 790     1275   3754   4888     97     77     41       C  
ATOM   2062  CG  PRO A 790     -32.874   6.245  21.467  1.00 26.15           C  
ANISOU 2062  CG  PRO A 790     1285   3777   4874     59    217     44       C  
ATOM   2063  CD  PRO A 790     -31.433   6.268  21.855  1.00 24.72           C  
ANISOU 2063  CD  PRO A 790     1271   3538   4583     69    244     51       C  
ATOM   2064  OXT PRO A 790     -30.099   8.289  19.107  1.00 24.19           O  
ANISOU 2064  OXT PRO A 790     1354   3376   4461    203    -35     48       O  
TER    2065      PRO A 790                                                      
ATOM   2066  N   ALA B 415      19.391  27.975 -11.745  1.00 25.63           N  
ANISOU 2066  N   ALA B 415     2739   3552   3449  -1291     74    129       N  
ATOM   2067  CA  ALA B 415      17.991  27.704 -11.294  1.00 24.42           C  
ANISOU 2067  CA  ALA B 415     2663   3331   3283  -1192     31    164       C  
ATOM   2068  C   ALA B 415      17.768  26.213 -11.074  1.00 23.99           C  
ANISOU 2068  C   ALA B 415     2560   3331   3226  -1086     22    143       C  
ATOM   2069  O   ALA B 415      18.429  25.389 -11.702  1.00 24.34           O  
ANISOU 2069  O   ALA B 415     2531   3451   3265  -1088     60    120       O  
ATOM   2070  CB  ALA B 415      16.990  28.230 -12.315  1.00 24.68           C  
ANISOU 2070  CB  ALA B 415     2798   3298   3283  -1213     50    236       C  
ATOM   2071  N   ASN B 416      16.822  25.881 -10.197  1.00 23.32           N  
ANISOU 2071  N   ASN B 416     2516   3202   3144   -997    -22    150       N  
ATOM   2072  CA  ASN B 416      16.446  24.487  -9.948  1.00 22.67           C  
ANISOU 2072  CA  ASN B 416     2403   3152   3057   -896    -31    138       C  
ATOM   2073  C   ASN B 416      16.102  23.771 -11.261  1.00 22.20           C  
ANISOU 2073  C   ASN B 416     2345   3118   2971   -890     15    163       C  
ATOM   2074  O   ASN B 416      15.482  24.369 -12.147  1.00 22.23           O  
ANISOU 2074  O   ASN B 416     2414   3082   2951   -931     34    209       O  
ATOM   2075  CB  ASN B 416      15.259  24.415  -8.974  1.00 22.53           C  
ANISOU 2075  CB  ASN B 416     2451   3068   3040   -817    -73    154       C  
ATOM   2076  CG  ASN B 416      15.454  25.270  -7.715  1.00 23.59           C  
ANISOU 2076  CG  ASN B 416     2605   3167   3191   -829   -115    130       C  
ATOM   2077  OD1 ASN B 416      16.580  25.519  -7.278  1.00 26.35           O  
ANISOU 2077  OD1 ASN B 416     2898   3559   3555   -870   -129     89       O  
ATOM   2078  ND2 ASN B 416      14.339  25.707  -7.118  1.00 24.01           N  
ANISOU 2078  ND2 ASN B 416     2736   3145   3243   -793   -137    150       N  
ATOM   2079  N   ARG B 417      16.522  22.509 -11.394  1.00 20.96           N  
ANISOU 2079  N   ARG B 417     2120   3027   2818   -840     30    131       N  
ATOM   2080  CA  ARG B 417      16.220  21.714 -12.593  1.00 19.50           C  
ANISOU 2080  CA  ARG B 417     1934   2869   2606   -830     74    144       C  
ATOM   2081  C   ARG B 417      14.711  21.626 -12.803  1.00 16.90           C  
ANISOU 2081  C   ARG B 417     1692   2475   2256   -786     59    192       C  
ATOM   2082  O   ARG B 417      13.947  21.465 -11.849  1.00 17.28           O  
ANISOU 2082  O   ARG B 417     1769   2478   2319   -721     20    197       O  
ATOM   2083  CB  ARG B 417      16.793  20.292 -12.492  1.00 19.92           C  
ANISOU 2083  CB  ARG B 417     1905   2987   2676   -765     85     97       C  
ATOM   2084  CG  ARG B 417      16.760  19.510 -13.820  1.00 21.04           C  
ANISOU 2084  CG  ARG B 417     2034   3170   2791   -771    141     94       C  
ATOM   2085  CD  ARG B 417      17.366  18.098 -13.705  1.00 21.53           C  
ANISOU 2085  CD  ARG B 417     2014   3288   2878   -701    152     41       C  
ATOM   2086  NE  ARG B 417      16.951  17.417 -12.484  1.00 21.75           N  
ANISOU 2086  NE  ARG B 417     2048   3285   2931   -606     98     37       N  
ATOM   2087  CZ  ARG B 417      15.887  16.616 -12.384  1.00 18.40           C  
ANISOU 2087  CZ  ARG B 417     1672   2820   2499   -538     88     56       C  
ATOM   2088  NH1 ARG B 417      15.120  16.373 -13.440  1.00 18.44           N  
ANISOU 2088  NH1 ARG B 417     1719   2814   2473   -550    121     77       N  
ATOM   2089  NH2 ARG B 417      15.597  16.065 -11.219  1.00 19.08           N  
ANISOU 2089  NH2 ARG B 417     1766   2878   2604   -462     44     54       N  
ATOM   2090  N   THR B 418      14.288  21.767 -14.054  1.00 14.54           N  
ANISOU 2090  N   THR B 418     1432   2173   1921   -825     90    225       N  
ATOM   2091  CA  THR B 418      12.878  21.600 -14.395  1.00 12.06           C  
ANISOU 2091  CA  THR B 418     1187   1807   1589   -783     73    266       C  
ATOM   2092  C   THR B 418      12.464  20.163 -14.140  1.00 11.67           C  
ANISOU 2092  C   THR B 418     1108   1777   1548   -696     71    241       C  
ATOM   2093  O   THR B 418      13.090  19.221 -14.631  1.00 12.14           O  
ANISOU 2093  O   THR B 418     1114   1898   1602   -688    105    207       O  
ATOM   2094  CB  THR B 418      12.620  22.012 -15.848  1.00 11.95           C  
ANISOU 2094  CB  THR B 418     1221   1795   1526   -846    100    306       C  
ATOM   2095  OG1 THR B 418      12.942  23.404 -15.986  1.00 12.05           O  
ANISOU 2095  OG1 THR B 418     1274   1773   1533   -926     99    337       O  
ATOM   2096  CG2 THR B 418      11.164  21.798 -16.249  1.00 10.85           C  
ANISOU 2096  CG2 THR B 418     1144   1608   1371   -800     73    344       C  
ATOM   2097  N   LEU B 419      11.423  19.997 -13.343  1.00  9.93           N  
ANISOU 2097  N   LEU B 419      923   1504   1346   -632     36    253       N  
ATOM   2098  CA  LEU B 419      10.995  18.651 -12.979  1.00  9.22           C  
ANISOU 2098  CA  LEU B 419      813   1423   1269   -553     35    232       C  
ATOM   2099  C   LEU B 419      10.212  17.997 -14.108  1.00  9.57           C  
ANISOU 2099  C   LEU B 419      877   1471   1287   -546     54    245       C  
ATOM   2100  O   LEU B 419       9.414  18.643 -14.788  1.00 10.17           O  
ANISOU 2100  O   LEU B 419     1006   1516   1344   -573     44    283       O  
ATOM   2101  CB  LEU B 419      10.170  18.648 -11.695  1.00  8.90           C  
ANISOU 2101  CB  LEU B 419      802   1326   1253   -493      0    237       C  
ATOM   2102  CG  LEU B 419      10.882  19.164 -10.434  1.00  8.24           C  
ANISOU 2102  CG  LEU B 419      704   1239   1188   -492    -25    218       C  
ATOM   2103  CD1 LEU B 419      10.035  18.834  -9.205  1.00  9.49           C  
ANISOU 2103  CD1 LEU B 419      893   1352   1359   -425    -49    218       C  
ATOM   2104  CD2 LEU B 419      12.293  18.599 -10.290  1.00  9.89           C  
ANISOU 2104  CD2 LEU B 419      838   1516   1404   -494    -17    177       C  
ATOM   2105  N   ILE B 420      10.467  16.714 -14.322  1.00  9.09           N  
ANISOU 2105  N   ILE B 420      777   1449   1229   -508     77    211       N  
ATOM   2106  CA  ILE B 420       9.744  15.963 -15.342  1.00  9.04           C  
ANISOU 2106  CA  ILE B 420      787   1448   1199   -500     94    213       C  
ATOM   2107  C   ILE B 420       8.559  15.321 -14.661  1.00  8.35           C  
ANISOU 2107  C   ILE B 420      725   1312   1137   -433     71    218       C  
ATOM   2108  O   ILE B 420       8.717  14.584 -13.683  1.00  8.35           O  
ANISOU 2108  O   ILE B 420      702   1305   1166   -378     67    196       O  
ATOM   2109  CB  ILE B 420      10.639  14.889 -16.028  1.00  9.37           C  
ANISOU 2109  CB  ILE B 420      774   1554   1231   -498    139    166       C  
ATOM   2110  CG1AILE B 420      11.861  15.563 -16.671  0.50 10.66           C  
ANISOU 2110  CG1AILE B 420      907   1772   1373   -572    172    155       C  
ATOM   2111  CG1BILE B 420      11.896  15.527 -16.634  0.50 10.96           C  
ANISOU 2111  CG1BILE B 420      942   1811   1413   -569    172    153       C  
ATOM   2112  CG2 ILE B 420       9.833  14.094 -17.069  1.00  8.85           C  
ANISOU 2112  CG2 ILE B 420      734   1492   1138   -491    155    162       C  
ATOM   2113  CD1AILE B 420      12.847  14.618 -17.354  0.50 10.85           C  
ANISOU 2113  CD1AILE B 420      868   1864   1392   -574    224    101       C  
ATOM   2114  CD1BILE B 420      11.620  16.566 -17.706  0.50 12.37           C  
ANISOU 2114  CD1BILE B 420     1173   1986   1540   -649    181    194       C  
ATOM   2115  N   VAL B 421       7.369  15.624 -15.177  1.00  7.94           N  
ANISOU 2115  N   VAL B 421      718   1225   1073   -439     54    249       N  
ATOM   2116  CA  VAL B 421       6.148  15.074 -14.629  1.00  7.87           C  
ANISOU 2116  CA  VAL B 421      728   1172   1092   -385     37    252       C  
ATOM   2117  C   VAL B 421       5.559  14.053 -15.591  1.00  8.34           C  
ANISOU 2117  C   VAL B 421      786   1246   1136   -377     51    237       C  
ATOM   2118  O   VAL B 421       5.235  14.400 -16.729  1.00  8.94           O  
ANISOU 2118  O   VAL B 421      883   1335   1177   -416     45    253       O  
ATOM   2119  CB  VAL B 421       5.113  16.193 -14.355  1.00  7.56           C  
ANISOU 2119  CB  VAL B 421      732   1077   1065   -389      2    291       C  
ATOM   2120  CG1 VAL B 421       3.760  15.571 -13.911  1.00  7.94           C  
ANISOU 2120  CG1 VAL B 421      789   1084   1144   -338     -8    288       C  
ATOM   2121  CG2 VAL B 421       5.644  17.166 -13.288  1.00  8.72           C  
ANISOU 2121  CG2 VAL B 421      884   1202   1229   -394    -11    298       C  
ATOM   2122  N   THR B 422       5.454  12.799 -15.143  1.00  7.69           N  
ANISOU 2122  N   THR B 422      683   1160   1077   -329     68    206       N  
ATOM   2123  CA  THR B 422       4.706  11.797 -15.897  1.00  7.78           C  
ANISOU 2123  CA  THR B 422      699   1173   1084   -319     78    187       C  
ATOM   2124  C   THR B 422       3.233  11.886 -15.549  1.00  7.12           C  
ANISOU 2124  C   THR B 422      640   1039   1027   -298     52    206       C  
ATOM   2125  O   THR B 422       2.855  12.091 -14.384  1.00  6.84           O  
ANISOU 2125  O   THR B 422      610    963   1025   -267     44    217       O  
ATOM   2126  CB  THR B 422       5.290  10.359 -15.735  1.00  8.11           C  
ANISOU 2126  CB  THR B 422      711   1230   1142   -282    111    142       C  
ATOM   2127  OG1 THR B 422       4.620   9.455 -16.625  1.00  8.59           O  
ANISOU 2127  OG1 THR B 422      778   1293   1194   -284    123    119       O  
ATOM   2128  CG2 THR B 422       5.183   9.832 -14.316  1.00  6.84           C  
ANISOU 2128  CG2 THR B 422      549   1028   1023   -226    109    141       C  
ATOM   2129  N   THR B 423       2.393  11.752 -16.571  1.00  6.96           N  
ANISOU 2129  N   THR B 423      632   1023    991   -317     40    208       N  
ATOM   2130  CA  THR B 423       0.957  11.772 -16.361  1.00  7.01           C  
ANISOU 2130  CA  THR B 423      648    987   1028   -299     14    218       C  
ATOM   2131  C   THR B 423       0.263  10.999 -17.469  1.00  6.79           C  
ANISOU 2131  C   THR B 423      619    975    985   -312      9    197       C  
ATOM   2132  O   THR B 423       0.915  10.376 -18.315  1.00  6.97           O  
ANISOU 2132  O   THR B 423      639   1039    971   -333     31    170       O  
ATOM   2133  CB  THR B 423       0.395  13.224 -16.206  1.00  7.20           C  
ANISOU 2133  CB  THR B 423      693    982   1059   -308    -26    261       C  
ATOM   2134  OG1 THR B 423      -0.921  13.176 -15.625  1.00  7.68           O  
ANISOU 2134  OG1 THR B 423      750    999   1170   -277    -41    262       O  
ATOM   2135  CG2 THR B 423       0.375  13.973 -17.535  1.00  8.04           C  
ANISOU 2135  CG2 THR B 423      823   1113   1118   -354    -57    288       C  
ATOM   2136  N   ILE B 424      -1.060  11.035 -17.449  1.00  6.46           N  
ANISOU 2136  N   ILE B 424      577    904    973   -302    -19    202       N  
ATOM   2137  CA  ILE B 424      -1.856  10.236 -18.364  1.00  6.94           C  
ANISOU 2137  CA  ILE B 424      633    977   1028   -313    -29    175       C  
ATOM   2138  C   ILE B 424      -3.138  11.001 -18.627  1.00  7.33           C  
ANISOU 2138  C   ILE B 424      682   1006   1097   -314    -84    200       C  
ATOM   2139  O   ILE B 424      -3.663  11.658 -17.728  1.00  7.18           O  
ANISOU 2139  O   ILE B 424      657    948   1124   -289    -95    220       O  
ATOM   2140  CB  ILE B 424      -2.137   8.832 -17.762  1.00  7.59           C  
ANISOU 2140  CB  ILE B 424      695   1036   1152   -287     10    133       C  
ATOM   2141  CG1 ILE B 424      -2.658   7.836 -18.806  1.00  8.39           C  
ANISOU 2141  CG1 ILE B 424      792   1155   1240   -308      8     93       C  
ATOM   2142  CG2 ILE B 424      -3.052   8.921 -16.541  1.00  7.44           C  
ANISOU 2142  CG2 ILE B 424      665    965   1195   -255     13    142       C  
ATOM   2143  CD1 ILE B 424      -2.477   6.376 -18.353  1.00  8.61           C  
ANISOU 2143  CD1 ILE B 424      812   1162   1298   -288     59     49       C  
ATOM   2144  N   LEU B 425      -3.634  10.913 -19.860  1.00  7.31           N  
ANISOU 2144  N   LEU B 425      687   1031   1060   -341   -121    195       N  
ATOM   2145  CA  LEU B 425      -4.907  11.528 -20.207  1.00  8.34           C  
ANISOU 2145  CA  LEU B 425      811   1144   1212   -337   -184    215       C  
ATOM   2146  C   LEU B 425      -6.032  10.796 -19.473  1.00  8.24           C  
ANISOU 2146  C   LEU B 425      755   1098   1276   -308   -174    182       C  
ATOM   2147  O   LEU B 425      -6.164   9.575 -19.588  1.00  9.32           O  
ANISOU 2147  O   LEU B 425      877   1243   1421   -315   -144    137       O  
ATOM   2148  CB  LEU B 425      -5.149  11.484 -21.721  1.00  8.92           C  
ANISOU 2148  CB  LEU B 425      906   1260   1223   -374   -232    214       C  
ATOM   2149  CG  LEU B 425      -4.220  12.368 -22.557  1.00 10.35           C  
ANISOU 2149  CG  LEU B 425     1138   1473   1323   -410   -246    255       C  
ATOM   2150  CD1 LEU B 425      -4.341  12.028 -24.029  1.00 13.06           C  
ANISOU 2150  CD1 LEU B 425     1508   1865   1589   -451   -277    244       C  
ATOM   2151  CD2 LEU B 425      -4.533  13.836 -22.324  1.00 11.51           C  
ANISOU 2151  CD2 LEU B 425     1305   1585   1484   -398   -296    315       C  
ATOM   2152  N   GLU B 426      -6.811  11.540 -18.694  1.00  7.46           N  
ANISOU 2152  N   GLU B 426      638    961   1235   -279   -192    200       N  
ATOM   2153  CA  GLU B 426      -7.914  10.975 -17.905  1.00  7.67           C  
ANISOU 2153  CA  GLU B 426      621    955   1339   -256   -174    170       C  
ATOM   2154  C   GLU B 426      -8.834  12.126 -17.487  1.00  8.06           C  
ANISOU 2154  C   GLU B 426      649    972   1440   -227   -214    194       C  
ATOM   2155  O   GLU B 426      -8.427  12.978 -16.702  1.00  8.90           O  
ANISOU 2155  O   GLU B 426      773   1052   1555   -208   -202    220       O  
ATOM   2156  CB  GLU B 426      -7.348  10.276 -16.664  1.00  7.03           C  
ANISOU 2156  CB  GLU B 426      542    850   1278   -241    -98    153       C  
ATOM   2157  CG  GLU B 426      -8.404   9.577 -15.826  1.00  7.69           C  
ANISOU 2157  CG  GLU B 426      589    900   1432   -227    -64    122       C  
ATOM   2158  CD  GLU B 426      -8.844   8.259 -16.411  1.00  8.82           C  
ANISOU 2158  CD  GLU B 426      714   1053   1583   -251    -51     78       C  
ATOM   2159  OE1 GLU B 426      -7.996   7.360 -16.607  1.00 10.14           O  
ANISOU 2159  OE1 GLU B 426      905   1231   1715   -262    -18     61       O  
ATOM   2160  OE2 GLU B 426     -10.054   8.118 -16.661  1.00 15.11           O  
ANISOU 2160  OE2 GLU B 426     1468   1846   2427   -257    -74     55       O  
ATOM   2161  N   GLU B 427     -10.056  12.164 -18.020  1.00  9.77           N  
ANISOU 2161  N   GLU B 427      827   1190   1696   -223   -265    181       N  
ATOM   2162  CA  GLU B 427     -10.999  13.245 -17.684  1.00 10.49           C  
ANISOU 2162  CA  GLU B 427      890   1249   1848   -188   -308    198       C  
ATOM   2163  C   GLU B 427     -11.518  13.090 -16.250  1.00  9.83           C  
ANISOU 2163  C   GLU B 427      770   1125   1839   -161   -245    172       C  
ATOM   2164  O   GLU B 427     -11.841  11.973 -15.842  1.00 10.80           O  
ANISOU 2164  O   GLU B 427      866   1249   1989   -172   -193    132       O  
ATOM   2165  CB  GLU B 427     -12.208  13.203 -18.620  1.00 11.65           C  
ANISOU 2165  CB  GLU B 427      992   1412   2023   -187   -383    184       C  
ATOM   2166  CG  GLU B 427     -11.897  13.349 -20.085  1.00 14.76           C  
ANISOU 2166  CG  GLU B 427     1424   1846   2337   -215   -454    208       C  
ATOM   2167  CD  GLU B 427     -13.153  13.378 -20.949  1.00 19.15           C  
ANISOU 2167  CD  GLU B 427     1935   2418   2923   -209   -541    195       C  
ATOM   2168  OE1 GLU B 427     -13.065  12.979 -22.130  1.00 22.91           O  
ANISOU 2168  OE1 GLU B 427     2434   2938   3334   -243   -587    192       O  
ATOM   2169  OE2 GLU B 427     -14.228  13.779 -20.444  1.00 22.39           O  
ANISOU 2169  OE2 GLU B 427     2286   2801   3422   -172   -564    183       O  
ATOM   2170  N   PRO B 428     -11.623  14.201 -15.484  1.00  9.40           N  
ANISOU 2170  N   PRO B 428      719   1034   1818   -128   -246    193       N  
ATOM   2171  CA  PRO B 428     -11.223  15.598 -15.729  1.00  9.36           C  
ANISOU 2171  CA  PRO B 428      752   1011   1792   -113   -297    241       C  
ATOM   2172  C   PRO B 428      -9.886  15.953 -15.078  1.00  8.90           C  
ANISOU 2172  C   PRO B 428      752    945   1686   -122   -253    264       C  
ATOM   2173  O   PRO B 428      -9.639  17.117 -14.781  1.00  9.25           O  
ANISOU 2173  O   PRO B 428      823    958   1734   -107   -271    293       O  
ATOM   2174  CB  PRO B 428     -12.333  16.377 -15.021  1.00  9.76           C  
ANISOU 2174  CB  PRO B 428      759   1018   1933    -67   -307    230       C  
ATOM   2175  CG  PRO B 428     -12.558  15.538 -13.767  1.00  9.72           C  
ANISOU 2175  CG  PRO B 428      726   1003   1966    -65   -215    185       C  
ATOM   2176  CD  PRO B 428     -12.290  14.082 -14.170  1.00  9.78           C  
ANISOU 2176  CD  PRO B 428      731   1048   1938   -104   -185    162       C  
ATOM   2177  N   TYR B 429      -9.047  14.944 -14.856  1.00  8.01           N  
ANISOU 2177  N   TYR B 429      654    857   1532   -146   -198    248       N  
ATOM   2178  CA  TYR B 429      -7.745  15.151 -14.212  1.00  7.75           C  
ANISOU 2178  CA  TYR B 429      665    823   1457   -154   -160    264       C  
ATOM   2179  C   TYR B 429      -6.721  15.775 -15.165  1.00  8.61           C  
ANISOU 2179  C   TYR B 429      817    956   1497   -184   -196    301       C  
ATOM   2180  O   TYR B 429      -6.041  16.740 -14.810  1.00  8.88           O  
ANISOU 2180  O   TYR B 429      884    973   1518   -186   -199    328       O  
ATOM   2181  CB  TYR B 429      -7.207  13.815 -13.674  1.00  7.93           C  
ANISOU 2181  CB  TYR B 429      687    863   1464   -163    -96    234       C  
ATOM   2182  CG ATYR B 429      -8.244  12.972 -12.918  0.50  8.29           C  
ANISOU 2182  CG ATYR B 429      695    886   1568   -148    -53    197       C  
ATOM   2183  CG BTYR B 429      -8.011  13.280 -12.542  0.50  6.45           C  
ANISOU 2183  CG BTYR B 429      474    645   1332   -141    -46    204       C  
ATOM   2184  CD1ATYR B 429      -8.384  13.054 -11.524  0.50  9.53           C  
ANISOU 2184  CD1ATYR B 429      857   1011   1754   -126     -3    188       C  
ATOM   2185  CD1BTYR B 429      -7.792  13.712 -11.239  0.50  5.76           C  
ANISOU 2185  CD1BTYR B 429      404    528   1257   -122     -9    205       C  
ATOM   2186  CD2ATYR B 429      -9.074  12.082 -13.603  0.50  8.91           C  
ANISOU 2186  CD2ATYR B 429      738    979   1668   -160    -61    170       C  
ATOM   2187  CD2BTYR B 429      -9.005  12.339 -12.771  0.50  5.77           C  
ANISOU 2187  CD2BTYR B 429      348    561   1284   -146    -35    172       C  
ATOM   2188  CE1ATYR B 429      -9.335  12.271 -10.843  0.50  9.22           C  
ANISOU 2188  CE1ATYR B 429      787    952   1764   -121     45    155       C  
ATOM   2189  CE1BTYR B 429      -8.548  13.214 -10.195  0.50  5.56           C  
ANISOU 2189  CE1BTYR B 429      362    477   1275   -107     44    178       C  
ATOM   2190  CE2ATYR B 429     -10.014  11.299 -12.935  0.50  9.56           C  
ANISOU 2190  CE2ATYR B 429      785   1041   1806   -156    -17    135       C  
ATOM   2191  CE2BTYR B 429      -9.770  11.830 -11.734  0.50  6.77           C  
ANISOU 2191  CE2BTYR B 429      452    660   1462   -135     20    144       C  
ATOM   2192  CZ ATYR B 429     -10.144  11.395 -11.561  0.50  9.26           C  
ANISOU 2192  CZ ATYR B 429      753    970   1796   -137     39    129       C  
ATOM   2193  CZ BTYR B 429      -9.541  12.271 -10.453  0.50  5.51           C  
ANISOU 2193  CZ BTYR B 429      314    471   1307   -115     61    149       C  
ATOM   2194  OH ATYR B 429     -11.086  10.611 -10.924  0.50 10.90           O  
ANISOU 2194  OH ATYR B 429      929   1158   2055   -141     91     95       O  
ATOM   2195  OH BTYR B 429     -10.308  11.766  -9.443  0.50  7.32           O  
ANISOU 2195  OH BTYR B 429      528    676   1579   -110    122    122       O  
ATOM   2196  N   VAL B 430      -6.601  15.195 -16.362  1.00  8.95           N  
ANISOU 2196  N   VAL B 430      863   1041   1497   -212   -218    301       N  
ATOM   2197  CA  VAL B 430      -5.649  15.637 -17.385  1.00  9.48           C  
ANISOU 2197  CA  VAL B 430      972   1139   1491   -250   -242    332       C  
ATOM   2198  C   VAL B 430      -6.354  15.475 -18.734  1.00 10.22           C  
ANISOU 2198  C   VAL B 430     1065   1258   1559   -266   -300    337       C  
ATOM   2199  O   VAL B 430      -6.747  14.367 -19.111  1.00 10.18           O  
ANISOU 2199  O   VAL B 430     1034   1280   1554   -273   -291    300       O  
ATOM   2200  CB  VAL B 430      -4.344  14.781 -17.372  1.00  9.39           C  
ANISOU 2200  CB  VAL B 430      971   1167   1430   -275   -187    313       C  
ATOM   2201  CG1 VAL B 430      -3.366  15.241 -18.467  1.00 10.86           C  
ANISOU 2201  CG1 VAL B 430     1196   1391   1541   -321   -201    340       C  
ATOM   2202  CG2 VAL B 430      -3.688  14.801 -15.974  1.00 10.63           C  
ANISOU 2202  CG2 VAL B 430     1125   1302   1612   -255   -138    304       C  
ATOM   2203  N   MET B 431      -6.534  16.591 -19.445  1.00 11.17           N  
ANISOU 2203  N   MET B 431     1217   1368   1658   -272   -363    384       N  
ATOM   2204  CA  MET B 431      -7.276  16.598 -20.703  1.00 12.48           C  
ANISOU 2204  CA  MET B 431     1389   1555   1796   -283   -434    396       C  
ATOM   2205  C   MET B 431      -6.602  17.541 -21.679  1.00 13.24           C  
ANISOU 2205  C   MET B 431     1554   1661   1814   -320   -473    453       C  
ATOM   2206  O   MET B 431      -5.895  18.458 -21.265  1.00 12.52           O  
ANISOU 2206  O   MET B 431     1497   1543   1718   -326   -459    486       O  
ATOM   2207  CB  MET B 431      -8.710  17.095 -20.484  1.00 13.13           C  
ANISOU 2207  CB  MET B 431     1433   1598   1958   -236   -493    398       C  
ATOM   2208  CG  MET B 431      -9.489  16.315 -19.430  1.00 13.90           C  
ANISOU 2208  CG  MET B 431     1462   1680   2141   -203   -449    344       C  
ATOM   2209  SD  MET B 431     -11.185  16.884 -19.207  1.00 14.39           S  
ANISOU 2209  SD  MET B 431     1462   1702   2305   -149   -512    336       S  
ATOM   2210  CE  MET B 431     -10.970  18.415 -18.304  1.00 15.44           C  
ANISOU 2210  CE  MET B 431     1623   1769   2476   -112   -512    375       C  
ATOM   2211  N   TYR B 432      -6.811  17.302 -22.970  1.00 14.19           N  
ANISOU 2211  N   TYR B 432     1699   1821   1870   -349   -520    462       N  
ATOM   2212  CA  TYR B 432      -6.392  18.267 -23.977  1.00 16.08           C  
ANISOU 2212  CA  TYR B 432     2012   2065   2031   -384   -567    524       C  
ATOM   2213  C   TYR B 432      -7.328  19.463 -23.937  1.00 17.54           C  
ANISOU 2213  C   TYR B 432     2209   2191   2264   -343   -651    573       C  
ATOM   2214  O   TYR B 432      -8.549  19.311 -24.071  1.00 17.97           O  
ANISOU 2214  O   TYR B 432     2222   2237   2368   -303   -712    559       O  
ATOM   2215  CB  TYR B 432      -6.395  17.656 -25.377  1.00 16.73           C  
ANISOU 2215  CB  TYR B 432     2124   2209   2022   -427   -596    518       C  
ATOM   2216  CG  TYR B 432      -5.255  16.702 -25.652  1.00 16.93           C  
ANISOU 2216  CG  TYR B 432     2157   2292   1984   -475   -514    478       C  
ATOM   2217  CD1 TYR B 432      -3.925  17.094 -25.486  1.00 19.13           C  
ANISOU 2217  CD1 TYR B 432     2467   2578   2222   -511   -452    496       C  
ATOM   2218  CD2 TYR B 432      -5.507  15.419 -26.120  1.00 17.92           C  
ANISOU 2218  CD2 TYR B 432     2254   2463   2092   -486   -499    419       C  
ATOM   2219  CE1 TYR B 432      -2.876  16.214 -25.757  1.00 18.61           C  
ANISOU 2219  CE1 TYR B 432     2399   2567   2106   -550   -376    453       C  
ATOM   2220  CE2 TYR B 432      -4.469  14.541 -26.402  1.00 17.22           C  
ANISOU 2220  CE2 TYR B 432     2170   2422   1949   -524   -424    378       C  
ATOM   2221  CZ  TYR B 432      -3.161  14.940 -26.217  1.00 17.99           C  
ANISOU 2221  CZ  TYR B 432     2293   2529   2012   -552   -363    395       C  
ATOM   2222  OH  TYR B 432      -2.136  14.066 -26.493  1.00 19.47           O  
ANISOU 2222  OH  TYR B 432     2476   2766   2156   -584   -287    348       O  
ATOM   2223  N   ARG B 433      -6.748  20.643 -23.739  1.00 18.69           N  
ANISOU 2223  N   ARG B 433     2407   2294   2401   -351   -654    625       N  
ATOM   2224  CA  ARG B 433      -7.477  21.910 -23.784  1.00 21.13           C  
ANISOU 2224  CA  ARG B 433     2744   2536   2748   -314   -734    679       C  
ATOM   2225  C   ARG B 433      -8.069  22.107 -25.182  1.00 22.78           C  
ANISOU 2225  C   ARG B 433     2998   2764   2894   -324   -831    722       C  
ATOM   2226  O   ARG B 433      -7.417  21.803 -26.186  1.00 22.89           O  
ANISOU 2226  O   ARG B 433     3065   2831   2802   -385   -824    738       O  
ATOM   2227  CB  ARG B 433      -6.519  23.054 -23.404  1.00 21.28           C  
ANISOU 2227  CB  ARG B 433     2823   2507   2754   -338   -707    726       C  
ATOM   2228  CG  ARG B 433      -7.039  24.482 -23.560  1.00 25.06           C  
ANISOU 2228  CG  ARG B 433     3354   2907   3261   -309   -787    792       C  
ATOM   2229  CD  ARG B 433      -5.964  25.511 -23.173  1.00 28.34           C  
ANISOU 2229  CD  ARG B 433     3832   3277   3660   -347   -747    830       C  
ATOM   2230  NE  ARG B 433      -5.962  25.778 -21.734  1.00 30.17           N  
ANISOU 2230  NE  ARG B 433     4018   3461   3984   -308   -701    792       N  
ATOM   2231  CZ  ARG B 433      -5.095  25.278 -20.856  1.00 30.48           C  
ANISOU 2231  CZ  ARG B 433     4027   3527   4028   -330   -614    746       C  
ATOM   2232  NH1 ARG B 433      -4.110  24.477 -21.246  1.00 30.36           N  
ANISOU 2232  NH1 ARG B 433     4012   3584   3940   -388   -559    729       N  
ATOM   2233  NH2 ARG B 433      -5.211  25.592 -19.570  1.00 30.29           N  
ANISOU 2233  NH2 ARG B 433     3971   3456   4081   -292   -584    714       N  
ATOM   2234  N   LYS B 434      -9.315  22.580 -25.230  1.00 24.27           N  
ANISOU 2234  N   LYS B 434     3161   2912   3147   -264   -920    737       N  
ATOM   2235  CA  LYS B 434      -9.988  22.911 -26.486  1.00 26.63           C  
ANISOU 2235  CA  LYS B 434     3504   3219   3394   -262  -1032    784       C  
ATOM   2236  C   LYS B 434      -9.385  24.182 -27.076  1.00 28.02           C  
ANISOU 2236  C   LYS B 434     3792   3352   3503   -291  -1069    874       C  
ATOM   2237  O   LYS B 434      -9.146  25.161 -26.359  1.00 27.87           O  
ANISOU 2237  O   LYS B 434     3793   3261   3536   -271  -1055    903       O  
ATOM   2238  CB  LYS B 434     -11.490  23.089 -26.260  1.00 26.98           C  
ANISOU 2238  CB  LYS B 434     3477   3229   3544   -181  -1119    769       C  
ATOM   2239  N   SER B 435      -9.122  24.153 -28.379  1.00 29.81           N  
ANISOU 2239  N   SER B 435     4096   3621   3610   -343  -1113    917       N  
ATOM   2240  CA  SER B 435      -8.467  25.269 -29.052  1.00 31.85           C  
ANISOU 2240  CA  SER B 435     4474   3843   3786   -387  -1139   1007       C  
ATOM   2241  C   SER B 435      -8.843  25.344 -30.526  1.00 33.68           C  
ANISOU 2241  C   SER B 435     4782   4107   3907   -411  -1238   1061       C  
ATOM   2242  O   SER B 435      -9.197  24.335 -31.138  1.00 34.29           O  
ANISOU 2242  O   SER B 435     4830   4259   3940   -423  -1255   1017       O  
ATOM   2243  CB  SER B 435      -6.949  25.147 -28.907  1.00 31.23           C  
ANISOU 2243  CB  SER B 435     4433   3794   3640   -468  -1020   1001       C  
ATOM   2244  OG  SER B 435      -6.292  26.301 -29.396  1.00 32.84           O  
ANISOU 2244  OG  SER B 435     4747   3953   3779   -516  -1032   1086       O  
ATOM   2245  N   ASP B 436      -8.771  26.550 -31.083  1.00 35.46           N  
ANISOU 2245  N   ASP B 436     5114   4273   4087   -420  -1304   1155       N  
ATOM   2246  CA  ASP B 436      -8.962  26.759 -32.517  1.00 37.43           C  
ANISOU 2246  CA  ASP B 436     5463   4548   4209   -454  -1396   1222       C  
ATOM   2247  C   ASP B 436      -7.645  26.560 -33.264  1.00 37.48           C  
ANISOU 2247  C   ASP B 436     5559   4613   4067   -567  -1309   1241       C  
ATOM   2248  O   ASP B 436      -7.640  26.300 -34.471  1.00 38.61           O  
ANISOU 2248  O   ASP B 436     5775   4812   4082   -614  -1351   1268       O  
ATOM   2249  CB  ASP B 436      -9.501  28.168 -32.789  1.00 39.05           C  
ANISOU 2249  CB  ASP B 436     5752   4654   4432   -410  -1511   1323       C  
ATOM   2250  CG  ASP B 436     -10.841  28.431 -32.116  1.00 40.34           C  
ANISOU 2250  CG  ASP B 436     5822   4758   4746   -293  -1601   1302       C  
ATOM   2251  OD1 ASP B 436     -11.708  27.527 -32.123  1.00 41.85           O  
ANISOU 2251  OD1 ASP B 436     5917   5004   4981   -252  -1638   1237       O  
ATOM   2252  OD2 ASP B 436     -11.027  29.551 -31.587  1.00 42.24           O  
ANISOU 2252  OD2 ASP B 436     6087   4897   5066   -244  -1632   1349       O  
ATOM   2253  N   LYS B 437      -6.537  26.693 -32.536  1.00 36.31           N  
ANISOU 2253  N   LYS B 437     5405   4454   3938   -609  -1189   1224       N  
ATOM   2254  CA  LYS B 437      -5.191  26.578 -33.097  1.00 35.90           C  
ANISOU 2254  CA  LYS B 437     5423   4454   3765   -717  -1091   1235       C  
ATOM   2255  C   LYS B 437      -4.374  25.503 -32.364  1.00 34.22           C  
ANISOU 2255  C   LYS B 437     5114   4304   3583   -740   -959   1136       C  
ATOM   2256  O   LYS B 437      -4.707  25.139 -31.224  1.00 33.22           O  
ANISOU 2256  O   LYS B 437     4885   4158   3580   -677   -936   1077       O  
ATOM   2257  CB  LYS B 437      -4.478  27.932 -33.028  1.00 36.57           C  
ANISOU 2257  CB  LYS B 437     5604   4460   3832   -759  -1074   1319       C  
ATOM   2258  N   PRO B 438      -3.310  24.978 -33.015  1.00 33.66           N  
ANISOU 2258  N   PRO B 438     5077   4310   3403   -829   -872   1117       N  
ATOM   2259  CA  PRO B 438      -2.447  23.985 -32.362  1.00 31.98           C  
ANISOU 2259  CA  PRO B 438     4777   4154   3220   -848   -749   1026       C  
ATOM   2260  C   PRO B 438      -1.825  24.508 -31.064  1.00 30.35           C  
ANISOU 2260  C   PRO B 438     4524   3892   3115   -834   -685   1017       C  
ATOM   2261  O   PRO B 438      -1.416  25.672 -30.993  1.00 30.80           O  
ANISOU 2261  O   PRO B 438     4648   3889   3167   -863   -688   1083       O  
ATOM   2262  CB  PRO B 438      -1.353  23.729 -33.406  1.00 32.58           C  
ANISOU 2262  CB  PRO B 438     4920   4305   3154   -952   -675   1029       C  
ATOM   2263  CG  PRO B 438      -1.979  24.097 -34.711  1.00 34.36           C  
ANISOU 2263  CG  PRO B 438     5253   4538   3266   -974   -771   1097       C  
ATOM   2264  CD  PRO B 438      -2.865  25.262 -34.394  1.00 34.88           C  
ANISOU 2264  CD  PRO B 438     5353   4501   3397   -913   -881   1176       C  
ATOM   2265  N   LEU B 439      -1.777  23.649 -30.048  1.00 28.27           N  
ANISOU 2265  N   LEU B 439     4153   3647   2941   -791   -631    936       N  
ATOM   2266  CA  LEU B 439      -1.146  23.984 -28.772  1.00 26.58           C  
ANISOU 2266  CA  LEU B 439     3891   3393   2817   -778   -568    915       C  
ATOM   2267  C   LEU B 439       0.081  23.106 -28.542  1.00 25.42           C  
ANISOU 2267  C   LEU B 439     3693   3317   2649   -823   -454    848       C  
ATOM   2268  O   LEU B 439       0.159  21.982 -29.060  1.00 25.40           O  
ANISOU 2268  O   LEU B 439     3662   3386   2601   -834   -425    796       O  
ATOM   2269  CB  LEU B 439      -2.138  23.831 -27.615  1.00 25.84           C  
ANISOU 2269  CB  LEU B 439     3717   3250   2852   -683   -605    881       C  
ATOM   2270  CG  LEU B 439      -3.396  24.710 -27.581  1.00 26.12           C  
ANISOU 2270  CG  LEU B 439     3777   3207   2942   -619   -714    933       C  
ATOM   2271  CD1 LEU B 439      -4.297  24.313 -26.417  1.00 24.88           C  
ANISOU 2271  CD1 LEU B 439     3523   3020   2909   -532   -725    879       C  
ATOM   2272  CD2 LEU B 439      -3.058  26.198 -27.520  1.00 27.72           C  
ANISOU 2272  CD2 LEU B 439     4059   3328   3144   -641   -736   1010       C  
ATOM   2273  N   TYR B 440       1.024  23.617 -27.751  1.00 24.23           N  
ANISOU 2273  N   TYR B 440     3528   3144   2536   -847   -393    845       N  
ATOM   2274  CA  TYR B 440       2.300  22.939 -27.508  1.00 23.29           C  
ANISOU 2274  CA  TYR B 440     3358   3088   2403   -890   -289    786       C  
ATOM   2275  C   TYR B 440       2.729  22.988 -26.039  1.00 21.28           C  
ANISOU 2275  C   TYR B 440     3032   2804   2251   -854   -251    748       C  
ATOM   2276  O   TYR B 440       2.309  23.870 -25.285  1.00 21.42           O  
ANISOU 2276  O   TYR B 440     3060   2746   2333   -821   -291    779       O  
ATOM   2277  CB  TYR B 440       3.402  23.540 -28.395  1.00 24.35           C  
ANISOU 2277  CB  TYR B 440     3560   3251   2439   -993   -238    824       C  
ATOM   2278  CG  TYR B 440       3.076  23.540 -29.876  1.00 26.85           C  
ANISOU 2278  CG  TYR B 440     3962   3601   2637  -1039   -270    865       C  
ATOM   2279  CD1 TYR B 440       3.205  22.376 -30.638  1.00 28.25           C  
ANISOU 2279  CD1 TYR B 440     4122   3864   2749  -1056   -235    811       C  
ATOM   2280  CD2 TYR B 440       2.624  24.697 -30.509  1.00 28.99           C  
ANISOU 2280  CD2 TYR B 440     4338   3815   2860  -1064   -340    958       C  
ATOM   2281  CE1 TYR B 440       2.899  22.366 -31.999  1.00 29.88           C  
ANISOU 2281  CE1 TYR B 440     4413   4105   2836  -1101   -266    846       C  
ATOM   2282  CE2 TYR B 440       2.319  24.701 -31.873  1.00 29.99           C  
ANISOU 2282  CE2 TYR B 440     4554   3974   2867  -1107   -377   1001       C  
ATOM   2283  CZ  TYR B 440       2.457  23.529 -32.607  1.00 30.33           C  
ANISOU 2283  CZ  TYR B 440     4576   4109   2839  -1127   -339    942       C  
ATOM   2284  OH  TYR B 440       2.153  23.518 -33.951  1.00 32.51           O  
ANISOU 2284  OH  TYR B 440     4944   4420   2987  -1171   -377    980       O  
ATOM   2285  N   GLY B 441       3.573  22.037 -25.645  1.00 19.74           N  
ANISOU 2285  N   GLY B 441     2767   2667   2067   -859   -176    680       N  
ATOM   2286  CA  GLY B 441       4.096  21.969 -24.276  1.00 16.93           C  
ANISOU 2286  CA  GLY B 441     2344   2294   1796   -827   -141    640       C  
ATOM   2287  C   GLY B 441       2.999  21.779 -23.242  1.00 15.18           C  
ANISOU 2287  C   GLY B 441     2086   2020   1662   -738   -188    627       C  
ATOM   2288  O   GLY B 441       1.983  21.128 -23.515  1.00 14.44           O  
ANISOU 2288  O   GLY B 441     1983   1929   1574   -694   -225    616       O  
ATOM   2289  N   ASN B 442       3.194  22.361 -22.059  1.00 14.10           N  
ANISOU 2289  N   ASN B 442     1929   1835   1592   -716   -185    624       N  
ATOM   2290  CA  ASN B 442       2.211  22.218 -20.969  1.00 12.90           C  
ANISOU 2290  CA  ASN B 442     1744   1635   1524   -636   -217    606       C  
ATOM   2291  C   ASN B 442       0.854  22.821 -21.309  1.00 13.30           C  
ANISOU 2291  C   ASN B 442     1833   1627   1592   -599   -294    649       C  
ATOM   2292  O   ASN B 442      -0.170  22.391 -20.764  1.00 12.48           O  
ANISOU 2292  O   ASN B 442     1693   1502   1546   -534   -320    627       O  
ATOM   2293  CB  ASN B 442       2.723  22.822 -19.658  1.00 12.48           C  
ANISOU 2293  CB  ASN B 442     1672   1541   1528   -625   -199    593       C  
ATOM   2294  CG  ASN B 442       3.976  22.145 -19.147  1.00 12.43           C  
ANISOU 2294  CG  ASN B 442     1613   1591   1519   -645   -135    543       C  
ATOM   2295  OD1 ASN B 442       4.355  21.065 -19.612  1.00 12.06           O  
ANISOU 2295  OD1 ASN B 442     1533   1608   1442   -650   -100    510       O  
ATOM   2296  ND2 ASN B 442       4.626  22.772 -18.177  1.00 14.28           N  
ANISOU 2296  ND2 ASN B 442     1838   1801   1787   -653   -122    535       N  
ATOM   2297  N   ASP B 443       0.860  23.797 -22.215  1.00 14.30           N  
ANISOU 2297  N   ASP B 443     2033   1730   1670   -643   -330    712       N  
ATOM   2298  CA AASP B 443      -0.368  24.473 -22.635  0.50 14.61           C  
ANISOU 2298  CA AASP B 443     2115   1712   1724   -607   -414    761       C  
ATOM   2299  CA BASP B 443      -0.360  24.478 -22.640  0.50 14.68           C  
ANISOU 2299  CA BASP B 443     2125   1721   1733   -608   -414    761       C  
ATOM   2300  C   ASP B 443      -1.354  23.556 -23.351  1.00 14.66           C  
ANISOU 2300  C   ASP B 443     2101   1755   1713   -574   -455    746       C  
ATOM   2301  O   ASP B 443      -2.526  23.902 -23.509  1.00 14.90           O  
ANISOU 2301  O   ASP B 443     2141   1744   1778   -527   -529    771       O  
ATOM   2302  CB AASP B 443      -0.044  25.685 -23.505  0.50 15.77           C  
ANISOU 2302  CB AASP B 443     2355   1822   1813   -665   -445    837       C  
ATOM   2303  CB BASP B 443      -0.012  25.672 -23.529  0.50 15.93           C  
ANISOU 2303  CB BASP B 443     2377   1846   1831   -668   -443    837       C  
ATOM   2304  CG AASP B 443       0.653  26.789 -22.733  0.50 16.53           C  
ANISOU 2304  CG AASP B 443     2477   1859   1945   -691   -422    855       C  
ATOM   2305  CG BASP B 443      -1.127  26.694 -23.596  0.50 17.35           C  
ANISOU 2305  CG BASP B 443     2603   1938   2051   -620   -532    892       C  
ATOM   2306  OD1AASP B 443       0.607  26.778 -21.482  0.50 15.95           O  
ANISOU 2306  OD1AASP B 443     2353   1758   1950   -647   -403    813       O  
ATOM   2307  OD1BASP B 443      -1.685  27.043 -22.532  0.50 19.13           O  
ANISOU 2307  OD1BASP B 443     2795   2104   2370   -559   -547    873       O  
ATOM   2308  OD2AASP B 443       1.242  27.675 -23.382  0.50 19.06           O  
ANISOU 2308  OD2AASP B 443     2872   2157   2213   -758   -422    910       O  
ATOM   2309  OD2BASP B 443      -1.438  27.151 -24.714  0.50 19.08           O  
ANISOU 2309  OD2BASP B 443     2894   2147   2208   -644   -588    954       O  
ATOM   2310  N   ARG B 444      -0.893  22.385 -23.779  1.00 13.94           N  
ANISOU 2310  N   ARG B 444     1980   1742   1575   -599   -408    702       N  
ATOM   2311  CA  ARG B 444      -1.795  21.411 -24.392  1.00 14.30           C  
ANISOU 2311  CA  ARG B 444     2001   1824   1607   -572   -441    677       C  
ATOM   2312  C   ARG B 444      -2.829  20.906 -23.391  1.00 13.74           C  
ANISOU 2312  C   ARG B 444     1860   1723   1636   -496   -456    635       C  
ATOM   2313  O   ARG B 444      -3.902  20.462 -23.788  1.00 14.33           O  
ANISOU 2313  O   ARG B 444     1916   1803   1724   -464   -507    625       O  
ATOM   2314  CB  ARG B 444      -1.015  20.198 -24.906  1.00 14.80           C  
ANISOU 2314  CB  ARG B 444     2043   1970   1611   -611   -376    626       C  
ATOM   2315  CG  ARG B 444      -0.173  20.459 -26.133  1.00 16.79           C  
ANISOU 2315  CG  ARG B 444     2360   2267   1752   -691   -357    656       C  
ATOM   2316  CD  ARG B 444       0.742  19.279 -26.430  1.00 19.44           C  
ANISOU 2316  CD  ARG B 444     2661   2680   2045   -723   -276    593       C  
ATOM   2317  NE  ARG B 444       1.717  19.077 -25.358  1.00 21.17           N  
ANISOU 2317  NE  ARG B 444     2826   2901   2317   -717   -205    555       N  
ATOM   2318  CZ  ARG B 444       2.532  18.029 -25.261  1.00 23.77           C  
ANISOU 2318  CZ  ARG B 444     3106   3285   2642   -724   -135    493       C  
ATOM   2319  NH1 ARG B 444       2.504  17.066 -26.177  1.00 25.48           N  
ANISOU 2319  NH1 ARG B 444     3323   3557   2803   -741   -117    456       N  
ATOM   2320  NH2 ARG B 444       3.381  17.946 -24.246  1.00 24.15           N  
ANISOU 2320  NH2 ARG B 444     3105   3330   2740   -712    -85    465       N  
ATOM   2321  N   PHE B 445      -2.494  20.966 -22.101  1.00 12.96           N  
ANISOU 2321  N   PHE B 445     1724   1597   1603   -470   -411    609       N  
ATOM   2322  CA  PHE B 445      -3.255  20.257 -21.063  1.00 12.41           C  
ANISOU 2322  CA  PHE B 445     1587   1512   1616   -409   -398    560       C  
ATOM   2323  C   PHE B 445      -4.013  21.166 -20.104  1.00 12.60           C  
ANISOU 2323  C   PHE B 445     1603   1463   1723   -357   -428    573       C  
ATOM   2324  O   PHE B 445      -3.589  22.279 -19.819  1.00 13.70           O  
ANISOU 2324  O   PHE B 445     1781   1557   1867   -368   -434    607       O  
ATOM   2325  CB  PHE B 445      -2.321  19.349 -20.250  1.00 11.85           C  
ANISOU 2325  CB  PHE B 445     1476   1474   1552   -414   -317    509       C  
ATOM   2326  CG  PHE B 445      -1.483  18.437 -21.097  1.00 12.82           C  
ANISOU 2326  CG  PHE B 445     1600   1667   1603   -459   -278    486       C  
ATOM   2327  CD1 PHE B 445      -2.072  17.404 -21.832  1.00 14.09           C  
ANISOU 2327  CD1 PHE B 445     1744   1864   1744   -456   -289    457       C  
ATOM   2328  CD2 PHE B 445      -0.107  18.627 -21.194  1.00 12.74           C  
ANISOU 2328  CD2 PHE B 445     1605   1686   1548   -506   -230    489       C  
ATOM   2329  CE1 PHE B 445      -1.294  16.563 -22.641  1.00 15.95           C  
ANISOU 2329  CE1 PHE B 445     1985   2163   1914   -496   -249    429       C  
ATOM   2330  CE2 PHE B 445       0.680  17.791 -21.998  1.00 13.29           C  
ANISOU 2330  CE2 PHE B 445     1671   1822   1556   -546   -188    461       C  
ATOM   2331  CZ  PHE B 445       0.084  16.756 -22.720  1.00 14.58           C  
ANISOU 2331  CZ  PHE B 445     1824   2019   1698   -539   -196    430       C  
ATOM   2332  N   GLU B 446      -5.124  20.655 -19.580  1.00 12.09           N  
ANISOU 2332  N   GLU B 446     1485   1383   1726   -304   -439    539       N  
ATOM   2333  CA  GLU B 446      -5.849  21.300 -18.493  1.00 11.72           C  
ANISOU 2333  CA  GLU B 446     1415   1272   1765   -251   -447    532       C  
ATOM   2334  C   GLU B 446      -6.476  20.211 -17.628  1.00 10.45           C  
ANISOU 2334  C   GLU B 446     1187   1123   1661   -215   -404    472       C  
ATOM   2335  O   GLU B 446      -6.547  19.052 -18.034  1.00  9.85           O  
ANISOU 2335  O   GLU B 446     1085   1095   1563   -228   -387    443       O  
ATOM   2336  CB  GLU B 446      -6.949  22.221 -19.031  1.00 12.79           C  
ANISOU 2336  CB  GLU B 446     1564   1361   1935   -217   -532    569       C  
ATOM   2337  CG  GLU B 446      -8.112  21.492 -19.739  1.00 15.66           C  
ANISOU 2337  CG  GLU B 446     1884   1753   2314   -194   -582    551       C  
ATOM   2338  CD  GLU B 446      -9.234  22.421 -20.183  1.00 19.77           C  
ANISOU 2338  CD  GLU B 446     2406   2225   2880   -150   -675    585       C  
ATOM   2339  OE1 GLU B 446      -9.143  23.644 -19.950  1.00 22.16           O  
ANISOU 2339  OE1 GLU B 446     2750   2465   3204   -133   -701    625       O  
ATOM   2340  OE2 GLU B 446     -10.222  21.911 -20.753  1.00 23.77           O  
ANISOU 2340  OE2 GLU B 446     2872   2755   3405   -129   -726    570       O  
ATOM   2341  N   GLY B 447      -6.966  20.592 -16.456  1.00  9.87           N  
ANISOU 2341  N   GLY B 447     1090   1003   1659   -174   -386    453       N  
ATOM   2342  CA  GLY B 447      -7.642  19.625 -15.595  1.00  9.01           C  
ANISOU 2342  CA  GLY B 447      923    899   1602   -144   -341    400       C  
ATOM   2343  C   GLY B 447      -7.260  19.775 -14.147  1.00  8.77           C  
ANISOU 2343  C   GLY B 447      893    841   1599   -129   -281    377       C  
ATOM   2344  O   GLY B 447      -6.389  20.570 -13.801  1.00  7.86           O  
ANISOU 2344  O   GLY B 447      819    707   1461   -143   -274    397       O  
ATOM   2345  N   TYR B 448      -7.901  18.973 -13.304  1.00  7.86           N  
ANISOU 2345  N   TYR B 448      735    724   1528   -105   -235    334       N  
ATOM   2346  CA  TYR B 448      -7.655  18.964 -11.869  1.00  8.72           C  
ANISOU 2346  CA  TYR B 448      848    811   1656    -90   -175    308       C  
ATOM   2347  C   TYR B 448      -6.177  18.810 -11.560  1.00  8.44           C  
ANISOU 2347  C   TYR B 448      851    799   1557   -121   -146    317       C  
ATOM   2348  O   TYR B 448      -5.639  19.550 -10.734  1.00  8.92           O  
ANISOU 2348  O   TYR B 448      939    834   1615   -119   -132    319       O  
ATOM   2349  CB  TYR B 448      -8.473  17.857 -11.199  1.00  7.93           C  
ANISOU 2349  CB  TYR B 448      702    716   1594    -73   -124    265       C  
ATOM   2350  CG  TYR B 448      -8.212  17.696  -9.707  1.00  7.23           C  
ANISOU 2350  CG  TYR B 448      627    609   1510    -62    -57    240       C  
ATOM   2351  CD1 TYR B 448      -9.086  18.242  -8.762  1.00  7.15           C  
ANISOU 2351  CD1 TYR B 448      601    559   1558    -31    -32    215       C  
ATOM   2352  CD2 TYR B 448      -7.088  17.000  -9.241  1.00  7.21           C  
ANISOU 2352  CD2 TYR B 448      655    632   1453    -82    -21    240       C  
ATOM   2353  CE1 TYR B 448      -8.854  18.089  -7.399  1.00  7.09           C  
ANISOU 2353  CE1 TYR B 448      615    537   1542    -25     30    192       C  
ATOM   2354  CE2 TYR B 448      -6.843  16.850  -7.899  1.00  8.73           C  
ANISOU 2354  CE2 TYR B 448      867    809   1640    -71     31    222       C  
ATOM   2355  CZ  TYR B 448      -7.730  17.391  -6.970  1.00  8.55           C  
ANISOU 2355  CZ  TYR B 448      836    748   1664    -46     58    199       C  
ATOM   2356  OH  TYR B 448      -7.481  17.224  -5.626  1.00 10.24           O  
ANISOU 2356  OH  TYR B 448     1080    950   1861    -40    111    180       O  
ATOM   2357  N   CYS B 449      -5.513  17.868 -12.232  1.00  7.89           N  
ANISOU 2357  N   CYS B 449      782    778   1439   -149   -138    318       N  
ATOM   2358  CA  CYS B 449      -4.100  17.603 -11.943  1.00  8.69           C  
ANISOU 2358  CA  CYS B 449      906    907   1489   -173   -109    320       C  
ATOM   2359  C   CYS B 449      -3.180  18.704 -12.432  1.00  7.84           C  
ANISOU 2359  C   CYS B 449      833    799   1345   -205   -139    354       C  
ATOM   2360  O   CYS B 449      -2.123  18.928 -11.841  1.00  8.15           O  
ANISOU 2360  O   CYS B 449      890    846   1362   -220   -119    352       O  
ATOM   2361  CB  CYS B 449      -3.652  16.249 -12.485  1.00  8.92           C  
ANISOU 2361  CB  CYS B 449      921    985   1485   -189    -87    304       C  
ATOM   2362  SG  CYS B 449      -4.257  14.881 -11.474  1.00 12.10           S  
ANISOU 2362  SG  CYS B 449     1299   1377   1920   -159    -33    265       S  
ATOM   2363  N   LEU B 450      -3.574  19.410 -13.491  1.00  7.31           N  
ANISOU 2363  N   LEU B 450      781    724   1274   -217   -188    385       N  
ATOM   2364  CA  LEU B 450      -2.788  20.558 -13.944  1.00  8.30           C  
ANISOU 2364  CA  LEU B 450      948    837   1367   -253   -214    423       C  
ATOM   2365  C   LEU B 450      -2.920  21.685 -12.928  1.00  8.28           C  
ANISOU 2365  C   LEU B 450      965    775   1406   -234   -217    424       C  
ATOM   2366  O   LEU B 450      -1.929  22.318 -12.572  1.00  8.36           O  
ANISOU 2366  O   LEU B 450     1002    779   1396   -262   -207    431       O  
ATOM   2367  CB  LEU B 450      -3.193  20.996 -15.350  1.00  8.77           C  
ANISOU 2367  CB  LEU B 450     1030    900   1404   -272   -268    462       C  
ATOM   2368  CG  LEU B 450      -2.614  20.204 -16.528  1.00  9.90           C  
ANISOU 2368  CG  LEU B 450     1175   1107   1478   -314   -263    467       C  
ATOM   2369  CD1 LEU B 450      -1.078  20.344 -16.657  1.00 12.14           C  
ANISOU 2369  CD1 LEU B 450     1479   1425   1708   -366   -229    473       C  
ATOM   2370  CD2 LEU B 450      -3.042  18.728 -16.465  1.00 12.03           C  
ANISOU 2370  CD2 LEU B 450     1399   1413   1759   -293   -236    422       C  
ATOM   2371  N   ASP B 451      -4.128  21.905 -12.418  1.00  8.31           N  
ANISOU 2371  N   ASP B 451      952    736   1471   -186   -226    410       N  
ATOM   2372  CA  ASP B 451      -4.332  22.902 -11.362  1.00  8.19           C  
ANISOU 2372  CA  ASP B 451      953    660   1498   -163   -221    400       C  
ATOM   2373  C   ASP B 451      -3.546  22.529 -10.100  1.00  8.06           C  
ANISOU 2373  C   ASP B 451      938    658   1467   -167   -168    366       C  
ATOM   2374  O   ASP B 451      -2.901  23.376  -9.488  1.00  9.04           O  
ANISOU 2374  O   ASP B 451     1093    755   1586   -182   -165    365       O  
ATOM   2375  CB  ASP B 451      -5.825  23.061 -11.041  1.00  8.86           C  
ANISOU 2375  CB  ASP B 451     1006    704   1657   -108   -231    381       C  
ATOM   2376  CG  ASP B 451      -6.588  23.836 -12.106  1.00  9.77           C  
ANISOU 2376  CG  ASP B 451     1128    787   1798    -93   -300    417       C  
ATOM   2377  OD1 ASP B 451      -6.004  24.227 -13.143  1.00  9.96           O  
ANISOU 2377  OD1 ASP B 451     1190    820   1776   -130   -339    463       O  
ATOM   2378  OD2 ASP B 451      -7.799  24.064 -11.894  1.00 12.28           O  
ANISOU 2378  OD2 ASP B 451     1412   1069   2184    -44   -316    400       O  
ATOM   2379  N   LEU B 452      -3.594  21.255  -9.722  1.00  7.62           N  
ANISOU 2379  N   LEU B 452      853    642   1402   -156   -129    339       N  
ATOM   2380  CA  LEU B 452      -2.804  20.755  -8.598  1.00  7.50           C  
ANISOU 2380  CA  LEU B 452      843    644   1362   -158    -87    313       C  
ATOM   2381  C   LEU B 452      -1.313  21.056  -8.793  1.00  7.77           C  
ANISOU 2381  C   LEU B 452      897    707   1347   -202    -96    327       C  
ATOM   2382  O   LEU B 452      -0.642  21.528  -7.867  1.00  8.35           O  
ANISOU 2382  O   LEU B 452      991    771   1411   -209    -87    313       O  
ATOM   2383  CB  LEU B 452      -3.036  19.253  -8.393  1.00  7.39           C  
ANISOU 2383  CB  LEU B 452      800    665   1341   -143    -51    292       C  
ATOM   2384  CG  LEU B 452      -2.259  18.595  -7.242  1.00  7.81           C  
ANISOU 2384  CG  LEU B 452      866    736   1366   -139    -14    271       C  
ATOM   2385  CD1 LEU B 452      -2.615  19.211  -5.888  1.00  9.94           C  
ANISOU 2385  CD1 LEU B 452     1159    965   1652   -118      7    250       C  
ATOM   2386  CD2 LEU B 452      -2.465  17.090  -7.209  1.00  7.75           C  
ANISOU 2386  CD2 LEU B 452      839    754   1353   -126     18    258       C  
ATOM   2387  N   LEU B 453      -0.796  20.790  -9.993  1.00  7.37           N  
ANISOU 2387  N   LEU B 453      841    696   1265   -234   -111    350       N  
ATOM   2388  CA  LEU B 453       0.609  21.091 -10.311  1.00  8.16           C  
ANISOU 2388  CA  LEU B 453      950    827   1322   -282   -113    360       C  
ATOM   2389  C   LEU B 453       0.946  22.580 -10.202  1.00  7.96           C  
ANISOU 2389  C   LEU B 453      962    759   1303   -311   -137    378       C  
ATOM   2390  O   LEU B 453       2.005  22.942  -9.697  1.00  7.49           O  
ANISOU 2390  O   LEU B 453      909    710   1227   -340   -129    368       O  
ATOM   2391  CB  LEU B 453       0.964  20.596 -11.716  1.00  9.13           C  
ANISOU 2391  CB  LEU B 453     1063    997   1408   -314   -119    379       C  
ATOM   2392  CG  LEU B 453       1.591  19.216 -11.848  1.00 11.11           C  
ANISOU 2392  CG  LEU B 453     1280   1308   1634   -312    -88    354       C  
ATOM   2393  CD1 LEU B 453       1.541  18.748 -13.296  1.00 14.64           C  
ANISOU 2393  CD1 LEU B 453     1722   1792   2050   -337    -94    367       C  
ATOM   2394  CD2 LEU B 453       3.031  19.234 -11.330  1.00 12.38           C  
ANISOU 2394  CD2 LEU B 453     1430   1500   1772   -335    -72    339       C  
ATOM   2395  N   LYS B 454       0.052  23.446 -10.664  1.00  8.39           N  
ANISOU 2395  N   LYS B 454     1040    761   1385   -302   -167    404       N  
ATOM   2396  CA  LYS B 454       0.272  24.890 -10.537  1.00  8.53           C  
ANISOU 2396  CA  LYS B 454     1101    722   1417   -326   -190    422       C  
ATOM   2397  C   LYS B 454       0.395  25.298  -9.073  1.00  8.62           C  
ANISOU 2397  C   LYS B 454     1121    701   1452   -308   -172    384       C  
ATOM   2398  O   LYS B 454       1.267  26.104  -8.724  1.00  8.90           O  
ANISOU 2398  O   LYS B 454     1182    722   1478   -346   -175    381       O  
ATOM   2399  CB  LYS B 454      -0.855  25.665 -11.222  1.00  9.90           C  
ANISOU 2399  CB  LYS B 454     1299    838   1626   -304   -232    455       C  
ATOM   2400  CG  LYS B 454      -0.903  25.424 -12.713  1.00  9.96           C  
ANISOU 2400  CG  LYS B 454     1312    875   1597   -329   -259    498       C  
ATOM   2401  CD  LYS B 454      -1.997  26.248 -13.393  1.00 12.82           C  
ANISOU 2401  CD  LYS B 454     1702   1178   1992   -304   -314    536       C  
ATOM   2402  CE  LYS B 454      -2.301  25.696 -14.769  1.00 12.73           C  
ANISOU 2402  CE  LYS B 454     1688   1207   1941   -316   -344    568       C  
ATOM   2403  NZ  LYS B 454      -3.295  26.542 -15.512  1.00 14.25           N  
ANISOU 2403  NZ  LYS B 454     1912   1342   2159   -291   -411    612       N  
ATOM   2404  N   GLU B 455      -0.446  24.699  -8.222  1.00  9.14           N  
ANISOU 2404  N   GLU B 455     1167    762   1545   -255   -150    352       N  
ATOM   2405  CA  GLU B 455      -0.424  24.991  -6.791  1.00  9.69           C  
ANISOU 2405  CA  GLU B 455     1250    805   1627   -236   -128    313       C  
ATOM   2406  C   GLU B 455       0.813  24.427  -6.113  1.00  9.09           C  
ANISOU 2406  C   GLU B 455     1168    780   1505   -260   -111    292       C  
ATOM   2407  O   GLU B 455       1.511  25.149  -5.391  1.00  9.97           O  
ANISOU 2407  O   GLU B 455     1303    877   1608   -283   -115    274       O  
ATOM   2408  CB  GLU B 455      -1.679  24.451  -6.097  1.00  9.99           C  
ANISOU 2408  CB  GLU B 455     1269    825   1700   -179   -101    285       C  
ATOM   2409  CG  GLU B 455      -2.974  25.073  -6.585  1.00 12.08           C  
ANISOU 2409  CG  GLU B 455     1530   1036   2025   -146   -122    295       C  
ATOM   2410  CD  GLU B 455      -3.244  26.466  -6.024  1.00 13.56           C  
ANISOU 2410  CD  GLU B 455     1753   1148   2252   -135   -132    282       C  
ATOM   2411  OE1 GLU B 455      -2.522  26.928  -5.105  1.00 14.81           O  
ANISOU 2411  OE1 GLU B 455     1942   1295   2391   -154   -118    257       O  
ATOM   2412  OE2 GLU B 455      -4.197  27.101  -6.516  1.00 16.65           O  
ANISOU 2412  OE2 GLU B 455     2142   1489   2696   -105   -159    295       O  
ATOM   2413  N   LEU B 456       1.098  23.147  -6.354  1.00  8.81           N  
ANISOU 2413  N   LEU B 456     1099    804   1443   -254    -95    291       N  
ATOM   2414  CA  LEU B 456       2.237  22.497  -5.729  1.00  8.71           C  
ANISOU 2414  CA  LEU B 456     1076    842   1393   -265    -85    272       C  
ATOM   2415  C   LEU B 456       3.539  23.182  -6.101  1.00  8.38           C  
ANISOU 2415  C   LEU B 456     1034    821   1330   -322   -104    279       C  
ATOM   2416  O   LEU B 456       4.391  23.417  -5.241  1.00  9.31           O  
ANISOU 2416  O   LEU B 456     1155    950   1431   -336   -109    255       O  
ATOM   2417  CB  LEU B 456       2.322  21.021  -6.117  1.00  8.50           C  
ANISOU 2417  CB  LEU B 456     1013    867   1348   -247    -67    273       C  
ATOM   2418  CG  LEU B 456       1.200  20.121  -5.607  1.00 10.13           C  
ANISOU 2418  CG  LEU B 456     1218   1060   1572   -198    -40    261       C  
ATOM   2419  CD1 LEU B 456       1.370  18.748  -6.212  1.00 10.77           C  
ANISOU 2419  CD1 LEU B 456     1268   1185   1638   -190    -26    265       C  
ATOM   2420  CD2 LEU B 456       1.184  20.042  -4.075  1.00 11.41           C  
ANISOU 2420  CD2 LEU B 456     1405   1207   1723   -174    -21    234       C  
ATOM   2421  N   SER B 457       3.691  23.485  -7.391  1.00  8.30           N  
ANISOU 2421  N   SER B 457     1019    818   1317   -357   -115    311       N  
ATOM   2422  CA  SER B 457       4.914  24.123  -7.885  1.00  8.21           C  
ANISOU 2422  CA  SER B 457     1005    828   1285   -422   -125    319       C  
ATOM   2423  C   SER B 457       5.128  25.519  -7.297  1.00  8.42           C  
ANISOU 2423  C   SER B 457     1071    800   1329   -453   -141    313       C  
ATOM   2424  O   SER B 457       6.271  25.919  -7.040  1.00  8.55           O  
ANISOU 2424  O   SER B 457     1080    838   1332   -500   -145    298       O  
ATOM   2425  CB  SER B 457       4.940  24.141  -9.412  1.00  8.71           C  
ANISOU 2425  CB  SER B 457     1067    909   1334   -457   -126    357       C  
ATOM   2426  OG  SER B 457       3.864  24.901  -9.949  1.00  8.98           O  
ANISOU 2426  OG  SER B 457     1140    882   1390   -449   -147    390       O  
ATOM   2427  N   ASN B 458       4.044  26.269  -7.084  1.00  8.55           N  
ANISOU 2427  N   ASN B 458     1127    744   1379   -426   -151    321       N  
ATOM   2428  CA  ASN B 458       4.138  27.555  -6.387  1.00  9.44           C  
ANISOU 2428  CA  ASN B 458     1281    793   1513   -446   -164    306       C  
ATOM   2429  C   ASN B 458       4.690  27.389  -4.976  1.00 10.04           C  
ANISOU 2429  C   ASN B 458     1353    887   1575   -438   -157    255       C  
ATOM   2430  O   ASN B 458       5.528  28.180  -4.530  1.00 11.09           O  
ANISOU 2430  O   ASN B 458     1501   1008   1703   -484   -168    236       O  
ATOM   2431  CB  ASN B 458       2.776  28.229  -6.309  1.00  9.68           C  
ANISOU 2431  CB  ASN B 458     1346    743   1589   -402   -172    314       C  
ATOM   2432  CG  ASN B 458       2.651  29.415  -7.238  1.00 10.50           C  
ANISOU 2432  CG  ASN B 458     1491    784   1713   -436   -199    356       C  
ATOM   2433  OD1 ASN B 458       3.102  29.379  -8.383  1.00 12.37           O  
ANISOU 2433  OD1 ASN B 458     1728   1047   1926   -478   -208    397       O  
ATOM   2434  ND2 ASN B 458       2.030  30.477  -6.746  1.00  9.85           N  
ANISOU 2434  ND2 ASN B 458     1450    616   1675   -417   -211    346       N  
ATOM   2435  N   ILE B 459       4.202  26.369  -4.273  1.00  9.94           N  
ANISOU 2435  N   ILE B 459     1323    900   1553   -383   -139    235       N  
ATOM   2436  CA  ILE B 459       4.583  26.171  -2.883  1.00 10.50           C  
ANISOU 2436  CA  ILE B 459     1402    984   1602   -369   -135    191       C  
ATOM   2437  C   ILE B 459       6.019  25.669  -2.760  1.00 10.53           C  
ANISOU 2437  C   ILE B 459     1371   1060   1570   -402   -149    180       C  
ATOM   2438  O   ILE B 459       6.715  26.034  -1.811  1.00 11.48           O  
ANISOU 2438  O   ILE B 459     1502   1187   1673   -419   -165    146       O  
ATOM   2439  CB  ILE B 459       3.612  25.207  -2.161  1.00  9.82           C  
ANISOU 2439  CB  ILE B 459     1318    902   1513   -305   -108    178       C  
ATOM   2440  CG1 ILE B 459       2.218  25.840  -2.068  1.00 10.17           C  
ANISOU 2440  CG1 ILE B 459     1389    875   1602   -272    -92    175       C  
ATOM   2441  CG2 ILE B 459       4.157  24.836  -0.767  1.00  9.85           C  
ANISOU 2441  CG2 ILE B 459     1336    931   1476   -294   -107    140       C  
ATOM   2442  CD1 ILE B 459       1.103  24.853  -1.737  1.00 10.56           C  
ANISOU 2442  CD1 ILE B 459     1426    928   1659   -217    -57    169       C  
ATOM   2443  N   LEU B 460       6.446  24.819  -3.698  1.00 10.54           N  
ANISOU 2443  N   LEU B 460     1328   1115   1561   -408   -144    203       N  
ATOM   2444  CA  LEU B 460       7.766  24.178  -3.644  1.00 11.12           C  
ANISOU 2444  CA  LEU B 460     1354   1261   1609   -427   -155    188       C  
ATOM   2445  C   LEU B 460       8.843  24.917  -4.425  1.00 10.96           C  
ANISOU 2445  C   LEU B 460     1311   1262   1593   -501   -164    193       C  
ATOM   2446  O   LEU B 460      10.024  24.654  -4.227  1.00 12.80           O  
ANISOU 2446  O   LEU B 460     1499   1551   1813   -525   -176    170       O  
ATOM   2447  CB  LEU B 460       7.722  22.720  -4.134  1.00 11.19           C  
ANISOU 2447  CB  LEU B 460     1324   1321   1608   -388   -138    200       C  
ATOM   2448  CG  LEU B 460       7.498  21.576  -3.147  1.00 13.41           C  
ANISOU 2448  CG  LEU B 460     1607   1618   1871   -326   -135    185       C  
ATOM   2449  CD1 LEU B 460       6.031  21.416  -2.931  1.00 13.78           C  
ANISOU 2449  CD1 LEU B 460     1690   1614   1930   -285   -110    195       C  
ATOM   2450  CD2 LEU B 460       8.084  20.290  -3.704  1.00 15.42           C  
ANISOU 2450  CD2 LEU B 460     1812   1931   2117   -307   -128    189       C  
ATOM   2451  N   GLY B 461       8.441  25.810  -5.325  1.00 10.30           N  
ANISOU 2451  N   GLY B 461     1255   1133   1526   -538   -159    223       N  
ATOM   2452  CA  GLY B 461       9.411  26.644  -6.040  1.00 10.57           C  
ANISOU 2452  CA  GLY B 461     1279   1176   1561   -620   -161    231       C  
ATOM   2453  C   GLY B 461      10.043  26.010  -7.270  1.00 10.57           C  
ANISOU 2453  C   GLY B 461     1232   1240   1545   -650   -140    251       C  
ATOM   2454  O   GLY B 461      11.240  26.149  -7.495  1.00 12.22           O  
ANISOU 2454  O   GLY B 461     1399   1495   1748   -707   -135    235       O  
ATOM   2455  N   PHE B 462       9.242  25.337  -8.090  1.00  9.59           N  
ANISOU 2455  N   PHE B 462     1111   1118   1414   -616   -125    280       N  
ATOM   2456  CA  PHE B 462       9.758  24.714  -9.312  1.00  9.45           C  
ANISOU 2456  CA  PHE B 462     1056   1159   1374   -644   -101    294       C  
ATOM   2457  C   PHE B 462       8.868  24.962 -10.525  1.00  9.57           C  
ANISOU 2457  C   PHE B 462     1112   1143   1380   -654    -96    343       C  
ATOM   2458  O   PHE B 462       7.690  25.276 -10.384  1.00  8.61           O  
ANISOU 2458  O   PHE B 462     1035    960   1275   -615   -113    363       O  
ATOM   2459  CB  PHE B 462      10.016  23.203  -9.111  1.00  9.56           C  
ANISOU 2459  CB  PHE B 462     1014   1239   1381   -590    -89    267       C  
ATOM   2460  CG  PHE B 462       8.769  22.365  -8.875  1.00  8.84           C  
ANISOU 2460  CG  PHE B 462      942   1123   1294   -514    -90    275       C  
ATOM   2461  CD1 PHE B 462       8.368  22.031  -7.578  1.00  8.84           C  
ANISOU 2461  CD1 PHE B 462      952   1102   1304   -458   -102    254       C  
ATOM   2462  CD2 PHE B 462       8.018  21.877  -9.945  1.00  8.91           C  
ANISOU 2462  CD2 PHE B 462      959   1133   1295   -503    -76    301       C  
ATOM   2463  CE1 PHE B 462       7.233  21.226  -7.353  1.00  9.62           C  
ANISOU 2463  CE1 PHE B 462     1066   1180   1410   -397    -94    260       C  
ATOM   2464  CE2 PHE B 462       6.881  21.075  -9.729  1.00  7.18           C  
ANISOU 2464  CE2 PHE B 462      749    893   1085   -440    -75    303       C  
ATOM   2465  CZ  PHE B 462       6.493  20.745  -8.422  1.00  8.85           C  
ANISOU 2465  CZ  PHE B 462      968   1083   1313   -388    -80    282       C  
ATOM   2466  N   ILE B 463       9.461  24.849 -11.713  1.00  9.03           N  
ANISOU 2466  N   ILE B 463     1029   1119   1284   -707    -72    359       N  
ATOM   2467  CA  ILE B 463       8.690  24.668 -12.939  1.00  9.30           C  
ANISOU 2467  CA  ILE B 463     1093   1146   1293   -707    -68    400       C  
ATOM   2468  C   ILE B 463       8.843  23.218 -13.395  1.00  9.61           C  
ANISOU 2468  C   ILE B 463     1081   1257   1313   -676    -43    377       C  
ATOM   2469  O   ILE B 463       9.673  22.477 -12.853  1.00  9.01           O  
ANISOU 2469  O   ILE B 463      947   1232   1243   -661    -27    335       O  
ATOM   2470  CB  ILE B 463       9.076  25.659 -14.062  1.00 10.30           C  
ANISOU 2470  CB  ILE B 463     1262   1261   1391   -793    -60    442       C  
ATOM   2471  CG1 ILE B 463      10.553  25.500 -14.447  1.00  9.26           C  
ANISOU 2471  CG1 ILE B 463     1079   1203   1237   -863    -17    417       C  
ATOM   2472  CG2 ILE B 463       8.723  27.105 -13.646  1.00 10.72           C  
ANISOU 2472  CG2 ILE B 463     1379   1224   1470   -815    -90    469       C  
ATOM   2473  CD1 ILE B 463      10.933  26.178 -15.769  1.00  9.80           C  
ANISOU 2473  CD1 ILE B 463     1186   1276   1261   -953      8    458       C  
ATOM   2474  N   TYR B 464       8.047  22.826 -14.386  1.00  9.54           N  
ANISOU 2474  N   TYR B 464     1094   1248   1281   -664    -43    403       N  
ATOM   2475  CA  TYR B 464       7.911  21.408 -14.730  1.00  9.82           C  
ANISOU 2475  CA  TYR B 464     1091   1335   1305   -624    -23    378       C  
ATOM   2476  C   TYR B 464       7.554  21.185 -16.192  1.00 10.22           C  
ANISOU 2476  C   TYR B 464     1166   1408   1311   -652    -15    403       C  
ATOM   2477  O   TYR B 464       7.034  22.076 -16.870  1.00 11.04           O  
ANISOU 2477  O   TYR B 464     1326   1474   1394   -683    -37    450       O  
ATOM   2478  CB  TYR B 464       6.849  20.734 -13.832  1.00  9.13           C  
ANISOU 2478  CB  TYR B 464     1002   1215   1253   -542    -42    365       C  
ATOM   2479  CG  TYR B 464       5.553  21.505 -13.812  1.00 10.04           C  
ANISOU 2479  CG  TYR B 464     1169   1260   1387   -522    -78    400       C  
ATOM   2480  CD1 TYR B 464       5.362  22.543 -12.901  1.00 10.43           C  
ANISOU 2480  CD1 TYR B 464     1244   1251   1467   -518    -99    407       C  
ATOM   2481  CD2 TYR B 464       4.545  21.243 -14.747  1.00 11.40           C  
ANISOU 2481  CD2 TYR B 464     1360   1424   1547   -510    -93    424       C  
ATOM   2482  CE1 TYR B 464       4.196  23.290 -12.900  1.00 10.41           C  
ANISOU 2482  CE1 TYR B 464     1284   1181   1490   -496   -130    434       C  
ATOM   2483  CE2 TYR B 464       3.366  21.987 -14.754  1.00 12.82           C  
ANISOU 2483  CE2 TYR B 464     1578   1540   1752   -488   -132    454       C  
ATOM   2484  CZ  TYR B 464       3.201  23.005 -13.823  1.00 12.72           C  
ANISOU 2484  CZ  TYR B 464     1589   1468   1777   -478   -148    459       C  
ATOM   2485  OH  TYR B 464       2.050  23.757 -13.822  1.00 15.64           O  
ANISOU 2485  OH  TYR B 464     1992   1771   2179   -449   -185    484       O  
ATOM   2486  N   ASP B 465       7.835  19.970 -16.653  1.00  9.90           N  
ANISOU 2486  N   ASP B 465     1084   1425   1252   -637     15    371       N  
ATOM   2487  CA AASP B 465       7.551  19.566 -18.010  0.50 10.40           C  
ANISOU 2487  CA AASP B 465     1167   1519   1265   -662     27    382       C  
ATOM   2488  CA BASP B 465       7.538  19.551 -18.020  0.50 10.59           C  
ANISOU 2488  CA BASP B 465     1191   1543   1289   -661     27    382       C  
ATOM   2489  C   ASP B 465       6.596  18.374 -17.959  1.00  9.91           C  
ANISOU 2489  C   ASP B 465     1091   1455   1218   -595     18    361       C  
ATOM   2490  O   ASP B 465       6.958  17.314 -17.435  1.00 10.01           O  
ANISOU 2490  O   ASP B 465     1056   1493   1253   -556     42    317       O  
ATOM   2491  CB AASP B 465       8.876  19.166 -18.659  0.50 11.20           C  
ANISOU 2491  CB AASP B 465     1229   1695   1333   -712     83    351       C  
ATOM   2492  CB BASP B 465       8.807  19.080 -18.732  0.50 11.56           C  
ANISOU 2492  CB BASP B 465     1275   1742   1376   -710     83    350       C  
ATOM   2493  CG AASP B 465       8.811  19.107 -20.165  0.50 12.86           C  
ANISOU 2493  CG AASP B 465     1474   1940   1474   -765    103    367       C  
ATOM   2494  CG BASP B 465       9.690  20.211 -19.181  0.50 14.19           C  
ANISOU 2494  CG BASP B 465     1626   2085   1680   -796    103    374       C  
ATOM   2495  OD1AASP B 465       7.736  19.344 -20.751  0.50 14.66           O  
ANISOU 2495  OD1AASP B 465     1758   2136   1678   -760     66    406       O  
ATOM   2496  OD1BASP B 465       9.170  21.312 -19.459  0.50 16.42           O  
ANISOU 2496  OD1BASP B 465     1975   2317   1947   -828     72    428       O  
ATOM   2497  OD2AASP B 465       9.868  18.828 -20.768  0.50 15.23           O  
ANISOU 2497  OD2AASP B 465     1742   2303   1743   -812    157    338       O  
ATOM   2498  OD2BASP B 465      10.917  19.986 -19.262  0.50 16.82           O  
ANISOU 2498  OD2BASP B 465     1907   2476   2009   -831    150    337       O  
ATOM   2499  N   VAL B 466       5.389  18.557 -18.492  1.00  9.73           N  
ANISOU 2499  N   VAL B 466     1111   1400   1186   -584    -18    392       N  
ATOM   2500  CA  VAL B 466       4.372  17.499 -18.461  1.00  9.41           C  
ANISOU 2500  CA  VAL B 466     1057   1354   1165   -529    -30    371       C  
ATOM   2501  C   VAL B 466       4.570  16.535 -19.632  1.00  9.96           C  
ANISOU 2501  C   VAL B 466     1119   1480   1185   -550     -3    346       C  
ATOM   2502  O   VAL B 466       4.548  16.943 -20.803  1.00 11.18           O  
ANISOU 2502  O   VAL B 466     1312   1655   1282   -600    -10    371       O  
ATOM   2503  CB  VAL B 466       2.941  18.084 -18.475  1.00  9.26           C  
ANISOU 2503  CB  VAL B 466     1073   1277   1167   -504    -85    407       C  
ATOM   2504  CG1 VAL B 466       1.866  16.957 -18.482  1.00  9.85           C  
ANISOU 2504  CG1 VAL B 466     1126   1349   1266   -455    -93    380       C  
ATOM   2505  CG2 VAL B 466       2.734  18.999 -17.259  1.00 10.17           C  
ANISOU 2505  CG2 VAL B 466     1196   1334   1335   -479   -103    422       C  
ATOM   2506  N   LYS B 467       4.757  15.258 -19.312  1.00  9.12           N  
ANISOU 2506  N   LYS B 467      970   1396   1099   -513     27    297       N  
ATOM   2507  CA  LYS B 467       5.047  14.251 -20.331  1.00  9.52           C  
ANISOU 2507  CA  LYS B 467     1009   1498   1109   -529     60    260       C  
ATOM   2508  C   LYS B 467       4.099  13.073 -20.187  1.00  8.68           C  
ANISOU 2508  C   LYS B 467      891   1375   1033   -479     53    230       C  
ATOM   2509  O   LYS B 467       4.105  12.405 -19.160  1.00  9.45           O  
ANISOU 2509  O   LYS B 467      959   1451   1182   -429     65    206       O  
ATOM   2510  CB  LYS B 467       6.487  13.751 -20.201  1.00 10.12           C  
ANISOU 2510  CB  LYS B 467     1038   1622   1184   -537    116    217       C  
ATOM   2511  CG  LYS B 467       7.556  14.835 -20.322  1.00 13.57           C  
ANISOU 2511  CG  LYS B 467     1475   2083   1598   -595    133    237       C  
ATOM   2512  CD  LYS B 467       7.518  15.526 -21.676  1.00 19.63           C  
ANISOU 2512  CD  LYS B 467     2293   2874   2290   -668    136    269       C  
ATOM   2513  CE ALYS B 467       8.692  16.473 -21.845  0.50 20.66           C  
ANISOU 2513  CE ALYS B 467     2419   3032   2397   -735    167    282       C  
ATOM   2514  CE BLYS B 467       8.590  16.607 -21.776  0.50 20.57           C  
ANISOU 2514  CE BLYS B 467     2415   3013   2389   -735    160    290       C  
ATOM   2515  NZ ALYS B 467       8.580  17.278 -23.094  0.50 22.63           N  
ANISOU 2515  NZ ALYS B 467     2735   3293   2569   -811    167    327       N  
ATOM   2516  NZ BLYS B 467       9.983  16.080 -21.635  0.50 21.91           N  
ANISOU 2516  NZ BLYS B 467     2514   3240   2570   -746    221    235       N  
ATOM   2517  N   LEU B 468       3.303  12.815 -21.218  1.00  9.04           N  
ANISOU 2517  N   LEU B 468      962   1431   1043   -496     34    230       N  
ATOM   2518  CA  LEU B 468       2.379  11.684 -21.191  1.00  8.64           C  
ANISOU 2518  CA  LEU B 468      898   1364   1019   -459     28    196       C  
ATOM   2519  C   LEU B 468       3.146  10.370 -21.176  1.00  8.94           C  
ANISOU 2519  C   LEU B 468      903   1429   1064   -443     83    136       C  
ATOM   2520  O   LEU B 468       4.100  10.183 -21.942  1.00  9.84           O  
ANISOU 2520  O   LEU B 468     1012   1593   1132   -475    120    112       O  
ATOM   2521  CB  LEU B 468       1.440  11.727 -22.393  1.00  9.06           C  
ANISOU 2521  CB  LEU B 468      984   1430   1027   -488    -12    205       C  
ATOM   2522  CG  LEU B 468       0.414  12.869 -22.402  1.00 10.44           C  
ANISOU 2522  CG  LEU B 468     1188   1569   1211   -488    -79    262       C  
ATOM   2523  CD1 LEU B 468      -0.401  12.819 -23.688  1.00 11.57           C  
ANISOU 2523  CD1 LEU B 468     1363   1733   1301   -515   -125    267       C  
ATOM   2524  CD2 LEU B 468      -0.506  12.818 -21.196  1.00 11.85           C  
ANISOU 2524  CD2 LEU B 468     1339   1690   1472   -433    -98    263       C  
ATOM   2525  N   VAL B 469       2.720   9.456 -20.304  1.00  7.76           N  
ANISOU 2525  N   VAL B 469      733   1243    973   -392     91    112       N  
ATOM   2526  CA  VAL B 469       3.408   8.168 -20.172  1.00  8.55           C  
ANISOU 2526  CA  VAL B 469      805   1353   1090   -365    138     58       C  
ATOM   2527  C   VAL B 469       3.359   7.415 -21.511  1.00  9.24           C  
ANISOU 2527  C   VAL B 469      901   1478   1131   -395    157     14       C  
ATOM   2528  O   VAL B 469       2.280   7.203 -22.072  1.00  9.25           O  
ANISOU 2528  O   VAL B 469      923   1469   1122   -408    128     11       O  
ATOM   2529  CB  VAL B 469       2.843   7.334 -18.983  1.00  8.02           C  
ANISOU 2529  CB  VAL B 469      728   1230   1091   -309    140     48       C  
ATOM   2530  CG1 VAL B 469       1.349   7.083 -19.131  1.00  9.06           C  
ANISOU 2530  CG1 VAL B 469      874   1327   1240   -310    113     50       C  
ATOM   2531  CG2 VAL B 469       3.583   6.035 -18.849  1.00  9.36           C  
ANISOU 2531  CG2 VAL B 469      877   1400   1280   -277    183     -2       C  
ATOM   2532  N   PRO B 470       4.531   7.066 -22.063  1.00  9.73           N  
ANISOU 2532  N   PRO B 470      947   1587   1164   -410    203    -23       N  
ATOM   2533  CA  PRO B 470       4.528   6.477 -23.406  1.00 10.65           C  
ANISOU 2533  CA  PRO B 470     1078   1744   1224   -446    226    -68       C  
ATOM   2534  C   PRO B 470       3.613   5.275 -23.616  1.00 10.88           C  
ANISOU 2534  C   PRO B 470     1115   1745   1275   -427    222   -111       C  
ATOM   2535  O   PRO B 470       2.967   5.188 -24.659  1.00 12.38           O  
ANISOU 2535  O   PRO B 470     1333   1955   1414   -465    204   -124       O  
ATOM   2536  CB  PRO B 470       6.004   6.133 -23.641  1.00 11.54           C  
ANISOU 2536  CB  PRO B 470     1156   1903   1325   -449    288   -112       C  
ATOM   2537  CG  PRO B 470       6.721   7.164 -22.847  1.00 10.84           C  
ANISOU 2537  CG  PRO B 470     1047   1817   1254   -448    282    -68       C  
ATOM   2538  CD  PRO B 470       5.910   7.289 -21.581  1.00 10.12           C  
ANISOU 2538  CD  PRO B 470      960   1660   1224   -401    237    -30       C  
ATOM   2539  N   ASP B 471       3.543   4.356 -22.657  1.00  9.57           N  
ANISOU 2539  N   ASP B 471      928   1529   1179   -372    237   -132       N  
ATOM   2540  CA  ASP B 471       2.703   3.167 -22.868  1.00  9.66           C  
ANISOU 2540  CA  ASP B 471      949   1507   1215   -361    240   -177       C  
ATOM   2541  C   ASP B 471       1.235   3.370 -22.517  1.00  9.73           C  
ANISOU 2541  C   ASP B 471      971   1475   1252   -363    190   -146       C  
ATOM   2542  O   ASP B 471       0.438   2.451 -22.673  1.00 10.48           O  
ANISOU 2542  O   ASP B 471     1070   1540   1371   -362    190   -182       O  
ATOM   2543  CB  ASP B 471       3.277   1.911 -22.191  1.00  9.74           C  
ANISOU 2543  CB  ASP B 471      938   1478   1283   -307    284   -221       C  
ATOM   2544  CG  ASP B 471       3.238   1.967 -20.664  1.00  9.53           C  
ANISOU 2544  CG  ASP B 471      902   1397   1322   -255    273   -181       C  
ATOM   2545  OD1 ASP B 471       2.673   2.919 -20.076  1.00  8.77           O  
ANISOU 2545  OD1 ASP B 471      812   1289   1231   -261    237   -125       O  
ATOM   2546  OD2 ASP B 471       3.782   1.015 -20.056  1.00 10.29           O  
ANISOU 2546  OD2 ASP B 471      989   1459   1463   -207    302   -207       O  
ATOM   2547  N   GLY B 472       0.882   4.566 -22.042  1.00  9.27           N  
ANISOU 2547  N   GLY B 472      916   1412   1196   -367    151    -84       N  
ATOM   2548  CA  GLY B 472      -0.521   4.888 -21.740  1.00  8.85           C  
ANISOU 2548  CA  GLY B 472      866   1322   1173   -367    103    -57       C  
ATOM   2549  C   GLY B 472      -1.113   4.087 -20.584  1.00  8.62           C  
ANISOU 2549  C   GLY B 472      823   1231   1221   -327    120    -66       C  
ATOM   2550  O   GLY B 472      -2.332   3.894 -20.528  1.00  9.94           O  
ANISOU 2550  O   GLY B 472      986   1371   1419   -333     97    -70       O  
ATOM   2551  N   LYS B 473      -0.256   3.623 -19.669  1.00  7.89           N  
ANISOU 2551  N   LYS B 473      725   1116   1158   -288    159    -70       N  
ATOM   2552  CA  LYS B 473      -0.697   2.800 -18.526  1.00  7.59           C  
ANISOU 2552  CA  LYS B 473      687   1014   1184   -251    180    -74       C  
ATOM   2553  C   LYS B 473      -0.381   3.456 -17.192  1.00  6.49           C  
ANISOU 2553  C   LYS B 473      548    851   1068   -217    179    -28       C  
ATOM   2554  O   LYS B 473       0.589   4.217 -17.060  1.00  7.36           O  
ANISOU 2554  O   LYS B 473      652    991   1152   -212    174     -6       O  
ATOM   2555  CB  LYS B 473      -0.038   1.411 -18.549  1.00  8.05           C  
ANISOU 2555  CB  LYS B 473      749   1051   1259   -227    225   -123       C  
ATOM   2556  CG  LYS B 473      -0.400   0.569 -19.761  1.00  9.74           C  
ANISOU 2556  CG  LYS B 473      968   1278   1456   -259    233   -181       C  
ATOM   2557  CD  LYS B 473       0.421  -0.696 -19.805  1.00 11.93           C  
ANISOU 2557  CD  LYS B 473     1249   1532   1750   -230    280   -232       C  
ATOM   2558  CE  LYS B 473       0.063  -1.531 -21.019  1.00 15.70           C  
ANISOU 2558  CE  LYS B 473     1736   2021   2209   -265    291   -298       C  
ATOM   2559  NZ  LYS B 473      -1.281  -2.117 -20.889  1.00 19.50           N  
ANISOU 2559  NZ  LYS B 473     2227   2453   2730   -285    280   -311       N  
ATOM   2560  N   TYR B 474      -1.183   3.112 -16.186  1.00  6.30           N  
ANISOU 2560  N   TYR B 474      530    772   1090   -198    187    -17       N  
ATOM   2561  CA  TYR B 474      -0.930   3.589 -14.832  1.00  5.66           C  
ANISOU 2561  CA  TYR B 474      459    666   1027   -166    191     22       C  
ATOM   2562  C   TYR B 474       0.224   2.802 -14.223  1.00  6.22           C  
ANISOU 2562  C   TYR B 474      538    722   1102   -125    217     13       C  
ATOM   2563  O   TYR B 474       1.194   3.398 -13.741  1.00  5.81           O  
ANISOU 2563  O   TYR B 474      482    691   1035   -106    208     34       O  
ATOM   2564  CB  TYR B 474      -2.198   3.458 -13.990  1.00  6.16           C  
ANISOU 2564  CB  TYR B 474      529    678   1133   -164    199     33       C  
ATOM   2565  CG  TYR B 474      -3.201   4.550 -14.266  1.00  5.46           C  
ANISOU 2565  CG  TYR B 474      423    602   1048   -189    165     51       C  
ATOM   2566  CD1 TYR B 474      -3.288   5.653 -13.417  1.00  5.20           C  
ANISOU 2566  CD1 TYR B 474      393    563   1021   -176    152     87       C  
ATOM   2567  CD2 TYR B 474      -4.083   4.471 -15.348  1.00  5.35           C  
ANISOU 2567  CD2 TYR B 474      390    605   1037   -222    142     28       C  
ATOM   2568  CE1 TYR B 474      -4.209   6.680 -13.652  1.00  6.12           C  
ANISOU 2568  CE1 TYR B 474      493    684   1149   -191    119    102       C  
ATOM   2569  CE2 TYR B 474      -5.006   5.493 -15.591  1.00  5.50           C  
ANISOU 2569  CE2 TYR B 474      391    634   1066   -236    101     46       C  
ATOM   2570  CZ  TYR B 474      -5.058   6.582 -14.738  1.00  6.02           C  
ANISOU 2570  CZ  TYR B 474      458    687   1142   -218     91     83       C  
ATOM   2571  OH  TYR B 474      -5.982   7.575 -14.969  1.00  7.66           O  
ANISOU 2571  OH  TYR B 474      647    897   1367   -224     50     99       O  
ATOM   2572  N   GLY B 475       0.119   1.476 -14.241  1.00  6.12           N  
ANISOU 2572  N   GLY B 475      538    672   1115   -111    246    -18       N  
ATOM   2573  CA  GLY B 475       1.247   0.599 -13.889  1.00  6.62           C  
ANISOU 2573  CA  GLY B 475      609    720   1186    -66    266    -33       C  
ATOM   2574  C   GLY B 475       0.848  -0.628 -13.100  1.00  7.04           C  
ANISOU 2574  C   GLY B 475      698    698   1280    -38    293    -36       C  
ATOM   2575  O   GLY B 475       0.139  -0.546 -12.090  1.00  7.27           O  
ANISOU 2575  O   GLY B 475      753    686   1325    -35    298     -4       O  
ATOM   2576  N   ALA B 476       1.324  -1.769 -13.571  1.00  7.86           N  
ANISOU 2576  N   ALA B 476      807    781   1399    -19    315    -76       N  
ATOM   2577  CA  ALA B 476       1.164  -3.028 -12.867  1.00  8.69           C  
ANISOU 2577  CA  ALA B 476      953    806   1543     12    341    -79       C  
ATOM   2578  C   ALA B 476       2.424  -3.844 -13.077  1.00 10.90           C  
ANISOU 2578  C   ALA B 476     1228   1080   1833     64    349   -109       C  
ATOM   2579  O   ALA B 476       3.200  -3.572 -13.988  1.00 10.00           O  
ANISOU 2579  O   ALA B 476     1074   1026   1699     61    345   -142       O  
ATOM   2580  CB  ALA B 476      -0.066  -3.769 -13.388  1.00  9.95           C  
ANISOU 2580  CB  ALA B 476     1127    926   1729    -32    366   -110       C  
ATOM   2581  N   GLN B 477       2.638  -4.832 -12.216  1.00 12.99           N  
ANISOU 2581  N   GLN B 477     1534   1271   2129    112    360    -96       N  
ATOM   2582  CA  GLN B 477       3.816  -5.676 -12.340  1.00 16.28           C  
ANISOU 2582  CA  GLN B 477     1947   1672   2568    172    363   -125       C  
ATOM   2583  C   GLN B 477       3.433  -7.045 -12.876  1.00 18.02           C  
ANISOU 2583  C   GLN B 477     2196   1824   2826    172    399   -172       C  
ATOM   2584  O   GLN B 477       2.406  -7.612 -12.493  1.00 18.75           O  
ANISOU 2584  O   GLN B 477     2336   1848   2939    147    419   -160       O  
ATOM   2585  CB  GLN B 477       4.571  -5.765 -11.005  1.00 16.44           C  
ANISOU 2585  CB  GLN B 477     1992   1660   2594    240    337    -76       C  
ATOM   2586  CG  GLN B 477       3.851  -6.487  -9.893  1.00 18.99           C  
ANISOU 2586  CG  GLN B 477     2391   1890   2934    252    349    -32       C  
ATOM   2587  CD  GLN B 477       4.695  -6.677  -8.649  1.00 20.73           C  
ANISOU 2587  CD  GLN B 477     2645   2079   3153    324    316     15       C  
ATOM   2588  OE1 GLN B 477       5.925  -6.751  -8.708  1.00 21.10           O  
ANISOU 2588  OE1 GLN B 477     2657   2152   3208    382    287      1       O  
ATOM   2589  NE2 GLN B 477       4.030  -6.778  -7.511  1.00 23.28           N  
ANISOU 2589  NE2 GLN B 477     3035   2346   3463    320    320     70       N  
ATOM   2590  N   ASN B 478       4.253  -7.565 -13.787  1.00 20.18           N  
ANISOU 2590  N   ASN B 478     2441   2116   3112    195    411   -232       N  
ATOM   2591  CA  ASN B 478       4.055  -8.917 -14.309  1.00 23.11           C  
ANISOU 2591  CA  ASN B 478     2842   2417   3523    202    445   -287       C  
ATOM   2592  C   ASN B 478       4.604  -9.997 -13.368  1.00 24.72           C  
ANISOU 2592  C   ASN B 478     3092   2525   3775    281    446   -268       C  
ATOM   2593  O   ASN B 478       5.015  -9.702 -12.239  1.00 24.92           O  
ANISOU 2593  O   ASN B 478     3134   2539   3797    325    416   -207       O  
ATOM   2594  CB  ASN B 478       4.602  -9.051 -15.747  1.00 23.41           C  
ANISOU 2594  CB  ASN B 478     2833   2513   3550    188    466   -368       C  
ATOM   2595  CG  ASN B 478       6.132  -8.908 -15.837  1.00 23.75           C  
ANISOU 2595  CG  ASN B 478     2825   2602   3596    252    459   -388       C  
ATOM   2596  OD1 ASN B 478       6.864  -9.095 -14.860  1.00 22.99           O  
ANISOU 2596  OD1 ASN B 478     2733   2475   3528    323    437   -353       O  
ATOM   2597  ND2 ASN B 478       6.611  -8.584 -17.033  1.00 26.54           N  
ANISOU 2597  ND2 ASN B 478     3129   3034   3921    225    477   -446       N  
ATOM   2598  N   ASP B 479       4.613 -11.243 -13.844  1.00 27.60           N  
ANISOU 2598  N   ASP B 479     3484   2820   4183    298    476   -321       N  
ATOM   2599  CA  ASP B 479       5.048 -12.409 -13.061  1.00 29.78           C  
ANISOU 2599  CA  ASP B 479     3816   2988   4511    373    477   -306       C  
ATOM   2600  C   ASP B 479       6.495 -12.281 -12.588  1.00 30.44           C  
ANISOU 2600  C   ASP B 479     3865   3096   4605    466    441   -292       C  
ATOM   2601  O   ASP B 479       6.857 -12.767 -11.508  1.00 31.23           O  
ANISOU 2601  O   ASP B 479     4012   3126   4729    533    415   -242       O  
ATOM   2602  CB  ASP B 479       4.909 -13.696 -13.887  1.00 31.17           C  
ANISOU 2602  CB  ASP B 479     4017   3091   4734    374    518   -381       C  
ATOM   2603  CG  ASP B 479       4.173 -13.484 -15.210  1.00 32.63           C  
ANISOU 2603  CG  ASP B 479     4172   3332   4895    286    546   -449       C  
ATOM   2604  OD1 ASP B 479       3.199 -12.694 -15.252  1.00 34.56           O  
ANISOU 2604  OD1 ASP B 479     4409   3620   5101    212    540   -423       O  
ATOM   2605  OD2 ASP B 479       4.574 -14.122 -16.211  1.00 35.49           O  
ANISOU 2605  OD2 ASP B 479     4517   3691   5275    294    573   -532       O  
ATOM   2606  N   LYS B 480       7.312 -11.627 -13.412  1.00 30.51           N  
ANISOU 2606  N   LYS B 480     3792   3205   4596    468    438   -338       N  
ATOM   2607  CA  LYS B 480       8.730 -11.415 -13.133  1.00 30.63           C  
ANISOU 2607  CA  LYS B 480     3751   3262   4626    548    406   -341       C  
ATOM   2608  C   LYS B 480       8.951 -10.250 -12.168  1.00 29.34           C  
ANISOU 2608  C   LYS B 480     3572   3155   4422    549    357   -267       C  
ATOM   2609  O   LYS B 480      10.073 -10.014 -11.716  1.00 29.96           O  
ANISOU 2609  O   LYS B 480     3607   3266   4512    613    320   -258       O  
ATOM   2610  CB  LYS B 480       9.483 -11.162 -14.442  1.00 31.23           C  
ANISOU 2610  CB  LYS B 480     3743   3426   4696    537    434   -425       C  
ATOM   2611  CG  LYS B 480       9.290 -12.256 -15.491  1.00 33.35           C  
ANISOU 2611  CG  LYS B 480     4027   3649   4997    530    486   -510       C  
ATOM   2612  CD  LYS B 480       9.386 -11.687 -16.899  1.00 35.75           C  
ANISOU 2612  CD  LYS B 480     4273   4055   5257    465    523   -581       C  
ATOM   2613  CE  LYS B 480       8.882 -12.678 -17.937  1.00 37.23           C  
ANISOU 2613  CE  LYS B 480     4489   4197   5459    436    573   -663       C  
ATOM   2614  NZ  LYS B 480       8.867 -12.069 -19.301  1.00 37.81           N  
ANISOU 2614  NZ  LYS B 480     4519   4374   5472    362    605   -724       N  
ATOM   2615  N   GLY B 481       7.878  -9.523 -11.854  1.00 27.41           N  
ANISOU 2615  N   GLY B 481     3359   2922   4134    478    357   -219       N  
ATOM   2616  CA  GLY B 481       7.970  -8.363 -10.975  1.00 25.38           C  
ANISOU 2616  CA  GLY B 481     3092   2716   3836    470    316   -156       C  
ATOM   2617  C   GLY B 481       8.370  -7.096 -11.715  1.00 23.53           C  
ANISOU 2617  C   GLY B 481     2779   2599   3563    424    311   -177       C  
ATOM   2618  O   GLY B 481       8.774  -6.110 -11.090  1.00 23.97           O  
ANISOU 2618  O   GLY B 481     2811   2705   3591    426    275   -138       O  
ATOM   2619  N   GLU B 482       8.266  -7.135 -13.043  1.00 22.00           N  
ANISOU 2619  N   GLU B 482     2550   2445   3364    381    349   -240       N  
ATOM   2620  CA  GLU B 482       8.563  -5.985 -13.899  1.00 19.63           C  
ANISOU 2620  CA  GLU B 482     2187   2251   3021    327    352   -261       C  
ATOM   2621  C   GLU B 482       7.345  -5.084 -14.025  1.00 17.02           C  
ANISOU 2621  C   GLU B 482     1880   1941   2646    246    350   -226       C  
ATOM   2622  O   GLU B 482       6.258  -5.538 -14.375  1.00 15.94           O  
ANISOU 2622  O   GLU B 482     1782   1763   2511    208    371   -236       O  
ATOM   2623  CB  GLU B 482       8.996  -6.441 -15.292  1.00 20.82           C  
ANISOU 2623  CB  GLU B 482     2298   2437   3176    314    395   -344       C  
ATOM   2624  CG  GLU B 482      10.191  -7.395 -15.289  1.00 23.63           C  
ANISOU 2624  CG  GLU B 482     2621   2770   3586    399    405   -393       C  
ATOM   2625  CD  GLU B 482      10.335  -8.195 -16.572  1.00 27.66           C  
ANISOU 2625  CD  GLU B 482     3117   3283   4110    390    458   -482       C  
ATOM   2626  OE1 GLU B 482       9.472  -8.081 -17.471  1.00 28.96           O  
ANISOU 2626  OE1 GLU B 482     3302   3465   4236    316    485   -506       O  
ATOM   2627  OE2 GLU B 482      11.326  -8.951 -16.685  1.00 30.65           O  
ANISOU 2627  OE2 GLU B 482     3461   3647   4538    460    472   -533       O  
ATOM   2628  N   TRP B 483       7.547  -3.804 -13.745  1.00 14.39           N  
ANISOU 2628  N   TRP B 483     1521   1670   2278    222    323   -189       N  
ATOM   2629  CA  TRP B 483       6.475  -2.811 -13.830  1.00 12.52           C  
ANISOU 2629  CA  TRP B 483     1300   1454   2003    153    314   -154       C  
ATOM   2630  C   TRP B 483       6.384  -2.160 -15.206  1.00 11.47           C  
ANISOU 2630  C   TRP B 483     1134   1393   1831     90    329   -188       C  
ATOM   2631  O   TRP B 483       7.322  -2.215 -16.005  1.00 12.67           O  
ANISOU 2631  O   TRP B 483     1244   1595   1974     92    347   -232       O  
ATOM   2632  CB  TRP B 483       6.692  -1.728 -12.776  1.00 12.61           C  
ANISOU 2632  CB  TRP B 483     1308   1486   1996    159    277    -96       C  
ATOM   2633  CG  TRP B 483       6.450  -2.218 -11.395  1.00 11.85           C  
ANISOU 2633  CG  TRP B 483     1263   1320   1921    205    261    -53       C  
ATOM   2634  CD1 TRP B 483       7.345  -2.874 -10.585  1.00 14.43           C  
ANISOU 2634  CD1 TRP B 483     1596   1615   2271    277    243    -45       C  
ATOM   2635  CD2 TRP B 483       5.235  -2.110 -10.647  1.00 12.94           C  
ANISOU 2635  CD2 TRP B 483     1454   1408   2053    182    263    -11       C  
ATOM   2636  NE1 TRP B 483       6.753  -3.167  -9.376  1.00 14.23           N  
ANISOU 2636  NE1 TRP B 483     1636   1524   2247    297    232      4       N  
ATOM   2637  CE2 TRP B 483       5.462  -2.707  -9.389  1.00 13.13           C  
ANISOU 2637  CE2 TRP B 483     1525   1374   2091    237    250     23       C  
ATOM   2638  CE3 TRP B 483       3.971  -1.565 -10.920  1.00 12.91           C  
ANISOU 2638  CE3 TRP B 483     1462   1406   2037    122    275     -1       C  
ATOM   2639  CZ2 TRP B 483       4.466  -2.777  -8.406  1.00 13.53           C  
ANISOU 2639  CZ2 TRP B 483     1636   1368   2135    226    259     66       C  
ATOM   2640  CZ3 TRP B 483       2.994  -1.633  -9.946  1.00 13.35           C  
ANISOU 2640  CZ3 TRP B 483     1567   1408   2098    115    282     36       C  
ATOM   2641  CH2 TRP B 483       3.245  -2.240  -8.705  1.00 13.08           C  
ANISOU 2641  CH2 TRP B 483     1582   1317   2071    163    279     69       C  
ATOM   2642  N   ASN B 484       5.231  -1.544 -15.467  1.00  9.64           N  
ANISOU 2642  N   ASN B 484      923   1166   1574     33    320   -165       N  
ATOM   2643  CA  ASN B 484       5.048  -0.707 -16.644  1.00  8.47           C  
ANISOU 2643  CA  ASN B 484      755   1085   1378    -30    319   -179       C  
ATOM   2644  C   ASN B 484       4.390   0.610 -16.237  1.00  7.55           C  
ANISOU 2644  C   ASN B 484      646    984   1239    -63    285   -121       C  
ATOM   2645  O   ASN B 484       4.304   0.910 -15.045  1.00  7.53           O  
ANISOU 2645  O   ASN B 484      656    951   1254    -37    268    -79       O  
ATOM   2646  CB  ASN B 484       4.248  -1.449 -17.733  1.00  8.82           C  
ANISOU 2646  CB  ASN B 484      816   1119   1415    -65    340   -226       C  
ATOM   2647  CG  ASN B 484       2.900  -1.956 -17.237  1.00  8.23           C  
ANISOU 2647  CG  ASN B 484      778    977   1372    -73    335   -211       C  
ATOM   2648  OD1 ASN B 484       2.337  -1.444 -16.264  1.00  9.01           O  
ANISOU 2648  OD1 ASN B 484      890   1050   1484    -69    315   -160       O  
ATOM   2649  ND2 ASN B 484       2.374  -2.964 -17.915  1.00 10.91           N  
ANISOU 2649  ND2 ASN B 484     1133   1287   1724    -89    356   -261       N  
ATOM   2650  N   GLY B 485       3.970   1.406 -17.216  1.00  6.86           N  
ANISOU 2650  N   GLY B 485      554    943   1109   -120    275   -120       N  
ATOM   2651  CA  GLY B 485       3.222   2.635 -16.949  1.00  7.38           C  
ANISOU 2651  CA  GLY B 485      630   1015   1159   -150    240    -69       C  
ATOM   2652  C   GLY B 485       3.972   3.689 -16.159  1.00  6.78           C  
ANISOU 2652  C   GLY B 485      541    958   1077   -139    222    -29       C  
ATOM   2653  O   GLY B 485       5.219   3.735 -16.158  1.00  6.94           O  
ANISOU 2653  O   GLY B 485      534   1012   1090   -124    233    -43       O  
ATOM   2654  N   MET B 486       3.206   4.555 -15.503  1.00  5.76           N  
ANISOU 2654  N   MET B 486      428    809    953   -147    195     15       N  
ATOM   2655  CA  MET B 486       3.797   5.644 -14.713  1.00  5.98           C  
ANISOU 2655  CA  MET B 486      450    848    974   -142    175     51       C  
ATOM   2656  C   MET B 486       4.670   5.125 -13.587  1.00  6.40           C  
ANISOU 2656  C   MET B 486      497    884   1051    -90    180     50       C  
ATOM   2657  O   MET B 486       5.692   5.749 -13.237  1.00  6.50           O  
ANISOU 2657  O   MET B 486      489    927   1055    -85    169     57       O  
ATOM   2658  CB  MET B 486       2.736   6.600 -14.170  1.00  5.81           C  
ANISOU 2658  CB  MET B 486      449    799    959   -155    149     90       C  
ATOM   2659  CG  MET B 486       2.090   7.442 -15.266  1.00  5.72           C  
ANISOU 2659  CG  MET B 486      442    812    921   -203    127    102       C  
ATOM   2660  SD  MET B 486       0.848   8.552 -14.601  1.00  7.01           S  
ANISOU 2660  SD  MET B 486      622    937   1106   -206     94    143       S  
ATOM   2661  CE  MET B 486      -0.468   7.374 -14.332  1.00  6.47           C  
ANISOU 2661  CE  MET B 486      556    823   1081   -188    112    120       C  
ATOM   2662  N   VAL B 487       4.296   3.974 -13.029  1.00  6.21           N  
ANISOU 2662  N   VAL B 487      493    809   1057    -52    196     40       N  
ATOM   2663  CA  VAL B 487       5.075   3.422 -11.927  1.00  7.18           C  
ANISOU 2663  CA  VAL B 487      620    909   1199      3    193     45       C  
ATOM   2664  C   VAL B 487       6.481   3.084 -12.413  1.00  7.34           C  
ANISOU 2664  C   VAL B 487      596    972   1219     24    199     11       C  
ATOM   2665  O   VAL B 487       7.465   3.461 -11.763  1.00  7.99           O  
ANISOU 2665  O   VAL B 487      657   1076   1302     48    178     19       O  
ATOM   2666  CB  VAL B 487       4.387   2.211 -11.272  1.00  7.11           C  
ANISOU 2666  CB  VAL B 487      652    829   1219     37    211     46       C  
ATOM   2667  CG1 VAL B 487       5.277   1.627 -10.170  1.00  8.57           C  
ANISOU 2667  CG1 VAL B 487      850    989   1417     99    199     57       C  
ATOM   2668  CG2 VAL B 487       3.030   2.646 -10.694  1.00  7.88           C  
ANISOU 2668  CG2 VAL B 487      783    891   1320     13    211     77       C  
ATOM   2669  N   LYS B 488       6.579   2.458 -13.587  1.00  7.79           N  
ANISOU 2669  N   LYS B 488      637   1048   1275     10    226    -32       N  
ATOM   2670  CA  LYS B 488       7.892   2.162 -14.167  1.00  8.92           C  
ANISOU 2670  CA  LYS B 488      731   1238   1420     25    242    -74       C  
ATOM   2671  C   LYS B 488       8.688   3.442 -14.444  1.00  8.52           C  
ANISOU 2671  C   LYS B 488      642   1256   1341    -14    232    -65       C  
ATOM   2672  O   LYS B 488       9.896   3.485 -14.207  1.00  9.02           O  
ANISOU 2672  O   LYS B 488      658   1352   1416     10    229    -82       O  
ATOM   2673  CB  LYS B 488       7.767   1.324 -15.444  1.00  9.54           C  
ANISOU 2673  CB  LYS B 488      803   1325   1495      9    280   -128       C  
ATOM   2674  CG  LYS B 488       9.093   1.117 -16.167  1.00 12.25           C  
ANISOU 2674  CG  LYS B 488     1091   1725   1838     17    308   -179       C  
ATOM   2675  CD  LYS B 488       8.913   0.368 -17.477  1.00 13.73           C  
ANISOU 2675  CD  LYS B 488     1280   1925   2011     -7    350   -237       C  
ATOM   2676  CE  LYS B 488      10.194   0.333 -18.302  1.00 17.14           C  
ANISOU 2676  CE  LYS B 488     1654   2425   2435    -11    387   -293       C  
ATOM   2677  NZ  LYS B 488      11.247  -0.512 -17.656  1.00 20.08           N  
ANISOU 2677  NZ  LYS B 488     1984   2779   2867     69    392   -323       N  
ATOM   2678  N   GLU B 489       8.025   4.493 -14.923  1.00  7.67           N  
ANISOU 2678  N   GLU B 489      551   1166   1197    -74    223    -39       N  
ATOM   2679  CA  GLU B 489       8.747   5.748 -15.189  1.00  7.98           C  
ANISOU 2679  CA  GLU B 489      563   1262   1208   -118    216    -26       C  
ATOM   2680  C   GLU B 489       9.427   6.290 -13.932  1.00  7.97           C  
ANISOU 2680  C   GLU B 489      546   1258   1226    -91    185     -3       C  
ATOM   2681  O   GLU B 489      10.521   6.854 -13.999  1.00  8.64           O  
ANISOU 2681  O   GLU B 489      585   1390   1306   -107    185    -14       O  
ATOM   2682  CB  GLU B 489       7.828   6.829 -15.755  1.00  7.95           C  
ANISOU 2682  CB  GLU B 489      592   1261   1167   -179    202      9       C  
ATOM   2683  CG  GLU B 489       7.226   6.542 -17.134  1.00  7.52           C  
ANISOU 2683  CG  GLU B 489      554   1223   1079   -219    221    -11       C  
ATOM   2684  CD  GLU B 489       8.287   6.286 -18.175  1.00  8.19           C  
ANISOU 2684  CD  GLU B 489      605   1370   1138   -243    262    -56       C  
ATOM   2685  OE1 GLU B 489       8.902   7.271 -18.642  1.00 11.71           O  
ANISOU 2685  OE1 GLU B 489     1038   1862   1550   -293    268    -45       O  
ATOM   2686  OE2 GLU B 489       8.536   5.103 -18.507  1.00 10.70           O  
ANISOU 2686  OE2 GLU B 489      907   1687   1472   -214    292   -106       O  
ATOM   2687  N   LEU B 490       8.763   6.135 -12.792  1.00  8.30           N  
ANISOU 2687  N   LEU B 490      625   1244   1285    -55    160     27       N  
ATOM   2688  CA  LEU B 490       9.343   6.564 -11.523  1.00  8.00           C  
ANISOU 2688  CA  LEU B 490      582   1201   1257    -27    126     47       C  
ATOM   2689  C   LEU B 490      10.465   5.644 -11.067  1.00  8.36           C  
ANISOU 2689  C   LEU B 490      590   1255   1331     34    120     19       C  
ATOM   2690  O   LEU B 490      11.539   6.108 -10.672  1.00  8.79           O  
ANISOU 2690  O   LEU B 490      600   1348   1390     40     98     11       O  
ATOM   2691  CB  LEU B 490       8.253   6.617 -10.456  1.00  7.80           C  
ANISOU 2691  CB  LEU B 490      616   1115   1233     -8    108     84       C  
ATOM   2692  CG  LEU B 490       7.160   7.668 -10.678  1.00  6.33           C  
ANISOU 2692  CG  LEU B 490      460    915   1029    -58    105    113       C  
ATOM   2693  CD1 LEU B 490       6.085   7.480  -9.614  1.00  6.00           C  
ANISOU 2693  CD1 LEU B 490      469    814    998    -33    100    138       C  
ATOM   2694  CD2 LEU B 490       7.726   9.094 -10.645  1.00  8.58           C  
ANISOU 2694  CD2 LEU B 490      730   1235   1296    -99     84    127       C  
ATOM   2695  N   ILE B 491      10.227   4.340 -11.129  1.00  8.19           N  
ANISOU 2695  N   ILE B 491      583   1197   1332     80    137      1       N  
ATOM   2696  CA  ILE B 491      11.238   3.363 -10.699  1.00  9.32           C  
ANISOU 2696  CA  ILE B 491      695   1337   1510    150    127    -24       C  
ATOM   2697  C   ILE B 491      12.531   3.575 -11.477  1.00 10.06           C  
ANISOU 2697  C   ILE B 491      705   1503   1613    139    141    -70       C  
ATOM   2698  O   ILE B 491      13.636   3.562 -10.896  1.00 11.18           O  
ANISOU 2698  O   ILE B 491      797   1671   1778    178    112    -83       O  
ATOM   2699  CB  ILE B 491      10.727   1.897 -10.862  1.00  9.32           C  
ANISOU 2699  CB  ILE B 491      728   1277   1536    195    151    -40       C  
ATOM   2700  CG1 ILE B 491       9.585   1.617  -9.888  1.00  9.19           C  
ANISOU 2700  CG1 ILE B 491      790   1187   1515    208    140      6       C  
ATOM   2701  CG2 ILE B 491      11.863   0.883 -10.607  1.00 10.16           C  
ANISOU 2701  CG2 ILE B 491      797   1380   1685    272    141    -72       C  
ATOM   2702  CD1 ILE B 491       8.892   0.294 -10.139  1.00 10.05           C  
ANISOU 2702  CD1 ILE B 491      938   1231   1648    232    170     -8       C  
ATOM   2703  N   ASP B 492      12.391   3.821 -12.775  1.00 10.22           N  
ANISOU 2703  N   ASP B 492      710   1561   1613     82    184    -96       N  
ATOM   2704  CA  ASP B 492      13.548   4.013 -13.654  1.00 11.25           C  
ANISOU 2704  CA  ASP B 492      764   1763   1746     59    213   -144       C  
ATOM   2705  C   ASP B 492      14.063   5.452 -13.694  1.00 11.23           C  
ANISOU 2705  C   ASP B 492      732   1817   1719     -6    204   -128       C  
ATOM   2706  O   ASP B 492      14.906   5.795 -14.533  1.00 12.15           O  
ANISOU 2706  O   ASP B 492      791   1998   1829    -47    238   -164       O  
ATOM   2707  CB  ASP B 492      13.204   3.584 -15.084  1.00 11.69           C  
ANISOU 2707  CB  ASP B 492      824   1835   1781     22    270   -182       C  
ATOM   2708  CG  ASP B 492      12.982   2.100 -15.221  1.00 13.16           C  
ANISOU 2708  CG  ASP B 492     1025   1975   2000     82    289   -217       C  
ATOM   2709  OD1 ASP B 492      13.175   1.345 -14.249  1.00 15.67           O  
ANISOU 2709  OD1 ASP B 492     1348   2246   2361    157    261   -211       O  
ATOM   2710  OD2 ASP B 492      12.590   1.694 -16.332  1.00 14.89           O  
ANISOU 2710  OD2 ASP B 492     1257   2202   2200     51    331   -250       O  
ATOM   2711  N   HIS B 493      13.551   6.307 -12.813  1.00 11.16           N  
ANISOU 2711  N   HIS B 493      763   1782   1694    -20    162    -78       N  
ATOM   2712  CA  HIS B 493      13.984   7.705 -12.775  1.00 11.41           C  
ANISOU 2712  CA  HIS B 493      775   1854   1705    -83    150    -61       C  
ATOM   2713  C   HIS B 493      13.912   8.378 -14.152  1.00 11.31           C  
ANISOU 2713  C   HIS B 493      761   1882   1655   -166    195    -68       C  
ATOM   2714  O   HIS B 493      14.821   9.098 -14.558  1.00 12.16           O  
ANISOU 2714  O   HIS B 493      819   2045   1755   -216    212    -84       O  
ATOM   2715  CB  HIS B 493      15.395   7.807 -12.192  1.00 12.14           C  
ANISOU 2715  CB  HIS B 493      790   1992   1831    -60    128    -90       C  
ATOM   2716  CG  HIS B 493      15.457   7.567 -10.716  1.00 13.58           C  
ANISOU 2716  CG  HIS B 493      989   2138   2034      6     68    -69       C  
ATOM   2717  ND1 HIS B 493      15.792   8.560  -9.819  1.00 16.14           N  
ANISOU 2717  ND1 HIS B 493     1309   2472   2350    -14     23    -49       N  
ATOM   2718  CD2 HIS B 493      15.219   6.457  -9.979  1.00 14.33           C  
ANISOU 2718  CD2 HIS B 493     1111   2185   2150     87     44    -63       C  
ATOM   2719  CE1 HIS B 493      15.757   8.069  -8.592  1.00 14.78           C  
ANISOU 2719  CE1 HIS B 493     1163   2265   2189     53    -27    -33       C  
ATOM   2720  NE2 HIS B 493      15.417   6.795  -8.661  1.00 13.88           N  
ANISOU 2720  NE2 HIS B 493     1068   2113   2091    115    -15    -38       N  
ATOM   2721  N   ARG B 494      12.819   8.121 -14.859  1.00 10.89           N  
ANISOU 2721  N   ARG B 494      762   1801   1575   -182    213    -55       N  
ATOM   2722  CA  ARG B 494      12.518   8.822 -16.105  1.00 11.05           C  
ANISOU 2722  CA  ARG B 494      802   1850   1546   -261    243    -47       C  
ATOM   2723  C   ARG B 494      11.739  10.095 -15.813  1.00 10.98           C  
ANISOU 2723  C   ARG B 494      845   1812   1513   -304    209     11       C  
ATOM   2724  O   ARG B 494      11.734  11.018 -16.630  1.00 13.23           O  
ANISOU 2724  O   ARG B 494     1147   2121   1760   -373    221     29       O  
ATOM   2725  CB  ARG B 494      11.721   7.933 -17.069  1.00 11.15           C  
ANISOU 2725  CB  ARG B 494      846   1850   1539   -258    271    -66       C  
ATOM   2726  CG  ARG B 494      12.350   6.601 -17.388  1.00 13.30           C  
ANISOU 2726  CG  ARG B 494     1077   2139   1839   -211    307   -128       C  
ATOM   2727  CD  ARG B 494      13.623   6.789 -18.160  1.00 16.61           C  
ANISOU 2727  CD  ARG B 494     1431   2632   2248   -247    354   -173       C  
ATOM   2728  NE  ARG B 494      14.133   5.528 -18.690  1.00 18.18           N  
ANISOU 2728  NE  ARG B 494     1591   2846   2469   -206    398   -241       N  
ATOM   2729  CZ  ARG B 494      15.258   5.436 -19.391  1.00 20.28           C  
ANISOU 2729  CZ  ARG B 494     1791   3178   2736   -226    450   -296       C  
ATOM   2730  NH1 ARG B 494      15.966   6.528 -19.642  1.00 22.15           N  
ANISOU 2730  NH1 ARG B 494     1996   3471   2950   -293    466   -288       N  
ATOM   2731  NH2 ARG B 494      15.669   4.259 -19.844  1.00 23.24           N  
ANISOU 2731  NH2 ARG B 494     2132   3560   3137   -182    491   -363       N  
ATOM   2732  N   ALA B 495      11.068  10.134 -14.657  1.00  9.98           N  
ANISOU 2732  N   ALA B 495      751   1631   1410   -261    168     41       N  
ATOM   2733  CA  ALA B 495      10.287  11.286 -14.245  1.00  9.47           C  
ANISOU 2733  CA  ALA B 495      735   1531   1333   -290    136     89       C  
ATOM   2734  C   ALA B 495      10.593  11.575 -12.783  1.00  9.17           C  
ANISOU 2734  C   ALA B 495      693   1471   1322   -255    101     99       C  
ATOM   2735  O   ALA B 495      10.938  10.659 -12.017  1.00  9.63           O  
ANISOU 2735  O   ALA B 495      732   1522   1405   -195     93     80       O  
ATOM   2736  CB  ALA B 495       8.807  11.002 -14.412  1.00  9.70           C  
ANISOU 2736  CB  ALA B 495      818   1511   1357   -277    128    111       C  
ATOM   2737  N   ASP B 496      10.443  12.843 -12.399  1.00  8.25           N  
ANISOU 2737  N   ASP B 496      600   1339   1196   -292     78    128       N  
ATOM   2738  CA  ASP B 496      10.588  13.266 -11.004  1.00  8.41           C  
ANISOU 2738  CA  ASP B 496      629   1335   1233   -267     42    137       C  
ATOM   2739  C   ASP B 496       9.320  13.041 -10.195  1.00  8.08           C  
ANISOU 2739  C   ASP B 496      642   1231   1197   -225     27    161       C  
ATOM   2740  O   ASP B 496       9.376  12.672  -9.018  1.00  9.07           O  
ANISOU 2740  O   ASP B 496      778   1337   1333   -179      7    159       O  
ATOM   2741  CB  ASP B 496      10.994  14.733 -10.944  1.00  9.08           C  
ANISOU 2741  CB  ASP B 496      717   1426   1308   -328     27    152       C  
ATOM   2742  CG  ASP B 496      12.352  14.965 -11.553  1.00  9.94           C  
ANISOU 2742  CG  ASP B 496      764   1598   1415   -374     46    125       C  
ATOM   2743  OD1 ASP B 496      13.355  14.565 -10.907  1.00 12.39           O  
ANISOU 2743  OD1 ASP B 496     1021   1940   1746   -346     34     94       O  
ATOM   2744  OD2 ASP B 496      12.426  15.518 -12.676  1.00  9.53           O  
ANISOU 2744  OD2 ASP B 496      716   1566   1340   -437     73    134       O  
ATOM   2745  N   LEU B 497       8.181  13.272 -10.833  1.00  7.58           N  
ANISOU 2745  N   LEU B 497      615   1139   1127   -243     35    182       N  
ATOM   2746  CA  LEU B 497       6.877  13.167 -10.178  1.00  7.23           C  
ANISOU 2746  CA  LEU B 497      615   1038   1094   -213     28    200       C  
ATOM   2747  C   LEU B 497       5.910  12.509 -11.122  1.00  7.17           C  
ANISOU 2747  C   LEU B 497      617   1020   1087   -212     46    201       C  
ATOM   2748  O   LEU B 497       6.012  12.697 -12.330  1.00  7.52           O  
ANISOU 2748  O   LEU B 497      651   1093   1112   -250     54    201       O  
ATOM   2749  CB  LEU B 497       6.283  14.549  -9.864  1.00  7.92           C  
ANISOU 2749  CB  LEU B 497      737   1092   1181   -240      7    226       C  
ATOM   2750  CG  LEU B 497       7.065  15.614  -9.106  0.50  6.49           C  
ANISOU 2750  CG  LEU B 497      556    913    997   -262    -14    227       C  
ATOM   2751  CD1 LEU B 497       6.213  16.873  -9.025  0.50  5.85           C  
ANISOU 2751  CD1 LEU B 497      516    785    921   -285    -29    251       C  
ATOM   2752  CD2 LEU B 497       7.443  15.140  -7.723  0.50  7.55           C  
ANISOU 2752  CD2 LEU B 497      692   1042   1135   -217    -26    212       C  
ATOM   2753  N   ALA B 498       4.947  11.779 -10.572  1.00  6.42           N  
ANISOU 2753  N   ALA B 498      543    885   1011   -174     53    201       N  
ATOM   2754  CA  ALA B 498       3.763  11.349 -11.316  1.00  6.88           C  
ANISOU 2754  CA  ALA B 498      612    925   1077   -178     62    202       C  
ATOM   2755  C   ALA B 498       2.592  12.094 -10.712  1.00  6.89           C  
ANISOU 2755  C   ALA B 498      640    881   1097   -175     50    223       C  
ATOM   2756  O   ALA B 498       2.276  11.885  -9.544  1.00  7.47           O  
ANISOU 2756  O   ALA B 498      730    923   1185   -145     57    223       O  
ATOM   2757  CB  ALA B 498       3.541   9.837 -11.192  1.00  6.85           C  
ANISOU 2757  CB  ALA B 498      605    908   1088   -142     87    180       C  
ATOM   2758  N   VAL B 499       1.987  12.989 -11.485  1.00  6.78           N  
ANISOU 2758  N   VAL B 499      632    864   1080   -205     30    241       N  
ATOM   2759  CA  VAL B 499       0.842  13.765 -11.015  1.00  7.14           C  
ANISOU 2759  CA  VAL B 499      696    865   1153   -198     16    256       C  
ATOM   2760  C   VAL B 499      -0.339  13.368 -11.886  1.00  7.18           C  
ANISOU 2760  C   VAL B 499      692    862   1173   -200     11    254       C  
ATOM   2761  O   VAL B 499      -0.448  13.755 -13.059  1.00  7.94           O  
ANISOU 2761  O   VAL B 499      788    977   1251   -229    -13    266       O  
ATOM   2762  CB  VAL B 499       1.095  15.298 -11.023  1.00  7.48           C  
ANISOU 2762  CB  VAL B 499      756    898   1189   -223    -12    280       C  
ATOM   2763  CG1 VAL B 499      -0.090  16.018 -10.375  1.00  7.60           C  
ANISOU 2763  CG1 VAL B 499      786    860   1241   -203    -22    288       C  
ATOM   2764  CG2 VAL B 499       2.375  15.634 -10.256  1.00  7.57           C  
ANISOU 2764  CG2 VAL B 499      769    925   1184   -229     -9    275       C  
ATOM   2765  N   ALA B 500      -1.203  12.552 -11.287  1.00  7.05           N  
ANISOU 2765  N   ALA B 500      671    819   1188   -173     33    238       N  
ATOM   2766  CA  ALA B 500      -2.263  11.840 -11.982  1.00  7.16           C  
ANISOU 2766  CA  ALA B 500      669    830   1223   -175     35    224       C  
ATOM   2767  C   ALA B 500      -3.144  11.257 -10.894  1.00  6.65           C  
ANISOU 2767  C   ALA B 500      604    725   1199   -149     68    209       C  
ATOM   2768  O   ALA B 500      -2.761  11.283  -9.729  1.00  7.08           O  
ANISOU 2768  O   ALA B 500      677    762   1250   -130     89    212       O  
ATOM   2769  CB  ALA B 500      -1.655  10.708 -12.820  1.00  7.91           C  
ANISOU 2769  CB  ALA B 500      755    958   1292   -187     49    203       C  
ATOM   2770  N   PRO B 501      -4.338  10.743 -11.249  1.00  6.62           N  
ANISOU 2770  N   PRO B 501      579    708   1230   -152     72    193       N  
ATOM   2771  CA  PRO B 501      -5.109   9.982 -10.253  1.00  6.41           C  
ANISOU 2771  CA  PRO B 501      551    646   1239   -136    117    176       C  
ATOM   2772  C   PRO B 501      -4.466   8.602 -10.046  1.00  6.47           C  
ANISOU 2772  C   PRO B 501      575    652   1230   -131    153    163       C  
ATOM   2773  O   PRO B 501      -4.954   7.592 -10.554  1.00  6.61           O  
ANISOU 2773  O   PRO B 501      581    666   1265   -143    168    140       O  
ATOM   2774  CB  PRO B 501      -6.500   9.890 -10.895  1.00  6.89           C  
ANISOU 2774  CB  PRO B 501      573    700   1344   -148    106    158       C  
ATOM   2775  CG  PRO B 501      -6.245   9.981 -12.348  1.00  6.75           C  
ANISOU 2775  CG  PRO B 501      545    719   1299   -169     59    161       C  
ATOM   2776  CD  PRO B 501      -5.067  10.890 -12.523  1.00  6.60           C  
ANISOU 2776  CD  PRO B 501      552    722   1234   -172     35    190       C  
ATOM   2777  N   LEU B 502      -3.341   8.611  -9.334  1.00  6.30           N  
ANISOU 2777  N   LEU B 502      581    634   1177   -114    160    176       N  
ATOM   2778  CA  LEU B 502      -2.512   7.422  -9.139  1.00  5.88           C  
ANISOU 2778  CA  LEU B 502      546    580   1108    -99    182    168       C  
ATOM   2779  C   LEU B 502      -2.791   6.830  -7.765  1.00  6.61           C  
ANISOU 2779  C   LEU B 502      673    628   1209    -78    221    173       C  
ATOM   2780  O   LEU B 502      -2.479   7.428  -6.737  1.00  7.45           O  
ANISOU 2780  O   LEU B 502      804    727   1298    -63    221    190       O  
ATOM   2781  CB  LEU B 502      -1.034   7.794  -9.278  1.00  6.41           C  
ANISOU 2781  CB  LEU B 502      615    684   1138    -92    158    177       C  
ATOM   2782  CG  LEU B 502      -0.052   6.622  -9.279  1.00  6.30           C  
ANISOU 2782  CG  LEU B 502      607    675   1113    -70    172    164       C  
ATOM   2783  CD1 LEU B 502      -0.146   5.786 -10.546  1.00  8.19           C  
ANISOU 2783  CD1 LEU B 502      826    927   1357    -85    179    136       C  
ATOM   2784  CD2 LEU B 502       1.374   7.181  -9.101  1.00  7.83           C  
ANISOU 2784  CD2 LEU B 502      793    904   1277    -59    147    172       C  
ATOM   2785  N   THR B 503      -3.426   5.669  -7.766  1.00  5.75           N  
ANISOU 2785  N   THR B 503      571    490   1125    -82    256    158       N  
ATOM   2786  CA  THR B 503      -3.914   5.052  -6.543  1.00  5.96           C  
ANISOU 2786  CA  THR B 503      637    469   1160    -73    302    166       C  
ATOM   2787  C   THR B 503      -2.785   4.536  -5.654  1.00  5.98           C  
ANISOU 2787  C   THR B 503      688    460   1126    -39    303    186       C  
ATOM   2788  O   THR B 503      -1.881   3.807  -6.116  1.00  6.27           O  
ANISOU 2788  O   THR B 503      725    504   1154    -21    289    181       O  
ATOM   2789  CB  THR B 503      -4.898   3.938  -6.920  1.00  5.84           C  
ANISOU 2789  CB  THR B 503      614    422   1184    -95    339    143       C  
ATOM   2790  OG1 THR B 503      -5.912   4.527  -7.749  1.00  6.60           O  
ANISOU 2790  OG1 THR B 503      657    537   1313   -123    324    123       O  
ATOM   2791  CG2 THR B 503      -5.505   3.242  -5.694  1.00  7.00           C  
ANISOU 2791  CG2 THR B 503      805    515   1340    -97    397    152       C  
ATOM   2792  N   ILE B 504      -2.858   4.920  -4.375  1.00  6.25           N  
ANISOU 2792  N   ILE B 504      761    475   1140    -27    318    206       N  
ATOM   2793  CA  ILE B 504      -1.896   4.510  -3.350  1.00  6.63           C  
ANISOU 2793  CA  ILE B 504      863    510   1147      7    312    229       C  
ATOM   2794  C   ILE B 504      -2.225   3.095  -2.915  1.00  7.16           C  
ANISOU 2794  C   ILE B 504      977    523   1222     13    354    237       C  
ATOM   2795  O   ILE B 504      -3.296   2.852  -2.341  1.00  8.17           O  
ANISOU 2795  O   ILE B 504     1129    613   1361    -10    405    238       O  
ATOM   2796  CB  ILE B 504      -1.957   5.471  -2.127  1.00  6.26           C  
ANISOU 2796  CB  ILE B 504      849    462   1067     10    313    245       C  
ATOM   2797  CG1 ILE B 504      -1.555   6.890  -2.547  1.00  6.53           C  
ANISOU 2797  CG1 ILE B 504      843    542   1097      3    269    237       C  
ATOM   2798  CG2 ILE B 504      -1.074   4.950  -0.985  1.00  8.92           C  
ANISOU 2798  CG2 ILE B 504     1250    784   1355     45    303    271       C  
ATOM   2799  CD1 ILE B 504      -1.966   7.937  -1.529  1.00  7.01           C  
ANISOU 2799  CD1 ILE B 504      928    595   1139     -2    279    239       C  
ATOM   2800  N   THR B 505      -1.328   2.158  -3.226  1.00  7.49           N  
ANISOU 2800  N   THR B 505     1028    556   1260     42    336    239       N  
ATOM   2801  CA  THR B 505      -1.526   0.756  -2.869  1.00  8.09           C  
ANISOU 2801  CA  THR B 505     1156    571   1346     52    371    249       C  
ATOM   2802  C   THR B 505      -0.288   0.200  -2.189  1.00  8.20           C  
ANISOU 2802  C   THR B 505     1217    572   1328    106    339    276       C  
ATOM   2803  O   THR B 505       0.819   0.707  -2.390  1.00  8.35           O  
ANISOU 2803  O   THR B 505     1205    638   1331    135    287    273       O  
ATOM   2804  CB  THR B 505      -1.856  -0.123  -4.097  1.00  8.58           C  
ANISOU 2804  CB  THR B 505     1185    620   1455     34    387    216       C  
ATOM   2805  OG1 THR B 505      -0.712  -0.186  -4.955  1.00  8.04           O  
ANISOU 2805  OG1 THR B 505     1080    590   1386     62    344    199       O  
ATOM   2806  CG2 THR B 505      -3.037   0.468  -4.890  1.00  8.31           C  
ANISOU 2806  CG2 THR B 505     1095    608   1454    -17    403    187       C  
ATOM   2807  N   TYR B 506      -0.489  -0.859  -1.410  1.00  9.13           N  
ANISOU 2807  N   TYR B 506     1407    623   1438    119    368    301       N  
ATOM   2808  CA  TYR B 506       0.592  -1.549  -0.719  1.00  9.82           C  
ANISOU 2808  CA  TYR B 506     1549    685   1497    178    333    332       C  
ATOM   2809  C   TYR B 506       1.696  -1.976  -1.691  1.00 10.25           C  
ANISOU 2809  C   TYR B 506     1553    762   1581    218    290    307       C  
ATOM   2810  O   TYR B 506       2.880  -1.694  -1.475  1.00  9.91           O  
ANISOU 2810  O   TYR B 506     1494    754   1518    264    234    314       O  
ATOM   2811  CB  TYR B 506       0.001  -2.754   0.030  1.00 11.10           C  
ANISOU 2811  CB  TYR B 506     1802    760   1656    176    380    364       C  
ATOM   2812  CG  TYR B 506       0.973  -3.841   0.429  1.00 12.21           C  
ANISOU 2812  CG  TYR B 506     2000    851   1788    239    347    393       C  
ATOM   2813  CD1 TYR B 506       1.757  -3.721   1.580  1.00 13.58           C  
ANISOU 2813  CD1 TYR B 506     2232   1023   1903    286    301    437       C  
ATOM   2814  CD2 TYR B 506       1.085  -5.008  -0.325  1.00 14.80           C  
ANISOU 2814  CD2 TYR B 506     2326   1130   2166    255    359    375       C  
ATOM   2815  CE1 TYR B 506       2.633  -4.729   1.963  1.00 14.80           C  
ANISOU 2815  CE1 TYR B 506     2441   1129   2053    352    261    467       C  
ATOM   2816  CE2 TYR B 506       1.966  -6.016   0.047  1.00 14.55           C  
ANISOU 2816  CE2 TYR B 506     2348   1045   2134    321    326    402       C  
ATOM   2817  CZ  TYR B 506       2.739  -5.868   1.188  1.00 15.58           C  
ANISOU 2817  CZ  TYR B 506     2535   1176   2210    372    274    450       C  
ATOM   2818  OH  TYR B 506       3.609  -6.876   1.560  1.00 17.34           O  
ANISOU 2818  OH  TYR B 506     2810   1342   2435    445    232    479       O  
ATOM   2819  N   VAL B 507       1.302  -2.635  -2.778  1.00 10.46           N  
ANISOU 2819  N   VAL B 507     1548    773   1655    199    318    273       N  
ATOM   2820  CA AVAL B 507       2.272  -3.152  -3.739  0.50 10.62           C  
ANISOU 2820  CA AVAL B 507     1523    809   1704    235    291    241       C  
ATOM   2821  CA BVAL B 507       2.287  -3.148  -3.737  0.50 10.96           C  
ANISOU 2821  CA BVAL B 507     1565    853   1747    235    290    241       C  
ATOM   2822  C   VAL B 507       3.082  -2.020  -4.399  1.00 10.21           C  
ANISOU 2822  C   VAL B 507     1391    848   1642    235    249    217       C  
ATOM   2823  O   VAL B 507       4.283  -2.154  -4.635  1.00 10.64           O  
ANISOU 2823  O   VAL B 507     1413    929   1700    280    212    204       O  
ATOM   2824  CB AVAL B 507       1.598  -4.133  -4.754  0.50 11.00           C  
ANISOU 2824  CB AVAL B 507     1563    817   1801    207    335    203       C  
ATOM   2825  CB BVAL B 507       1.651  -4.104  -4.775  0.50 11.33           C  
ANISOU 2825  CB BVAL B 507     1602    862   1842    209    333    202       C  
ATOM   2826  CG1AVAL B 507       0.634  -3.417  -5.713  0.50  9.09           C  
ANISOU 2826  CG1AVAL B 507     1264    619   1571    140    356    169       C  
ATOM   2827  CG1BVAL B 507       2.574  -4.343  -5.946  0.50 12.77           C  
ANISOU 2827  CG1BVAL B 507     1723   1081   2048    233    311    156       C  
ATOM   2828  CG2AVAL B 507       2.631  -4.982  -5.485  0.50 11.83           C  
ANISOU 2828  CG2AVAL B 507     1645    915   1934    256    316    171       C  
ATOM   2829  CG2BVAL B 507       1.318  -5.433  -4.114  0.50 11.96           C  
ANISOU 2829  CG2BVAL B 507     1765    842   1936    225    364    226       C  
ATOM   2830  N   ARG B 508       2.433  -0.889  -4.671  1.00  8.97           N  
ANISOU 2830  N   ARG B 508     1201    735   1474    184    256    211       N  
ATOM   2831  CA  ARG B 508       3.148   0.241  -5.268  1.00  7.97           C  
ANISOU 2831  CA  ARG B 508     1008    686   1334    176    220    194       C  
ATOM   2832  C   ARG B 508       4.014   0.977  -4.255  1.00  7.90           C  
ANISOU 2832  C   ARG B 508     1008    703   1289    205    176    220       C  
ATOM   2833  O   ARG B 508       5.118   1.417  -4.572  1.00  8.22           O  
ANISOU 2833  O   ARG B 508     1001    797   1326    221    139    206       O  
ATOM   2834  CB  ARG B 508       2.189   1.224  -5.916  1.00  7.52           C  
ANISOU 2834  CB  ARG B 508      919    660   1279    117    235    182       C  
ATOM   2835  CG  ARG B 508       1.545   0.666  -7.173  1.00  7.03           C  
ANISOU 2835  CG  ARG B 508      830    593   1247     86    261    147       C  
ATOM   2836  CD  ARG B 508       0.444   1.598  -7.629  1.00  7.86           C  
ANISOU 2836  CD  ARG B 508      911    719   1356     33    268    143       C  
ATOM   2837  NE  ARG B 508      -0.007   1.290  -8.979  1.00  7.68           N  
ANISOU 2837  NE  ARG B 508      854    712   1352      1    276    107       N  
ATOM   2838  CZ  ARG B 508      -1.001   1.922  -9.587  1.00  5.97           C  
ANISOU 2838  CZ  ARG B 508      613    512   1143    -41    274     98       C  
ATOM   2839  NH1 ARG B 508      -1.650   2.899  -8.965  1.00  5.27           N  
ANISOU 2839  NH1 ARG B 508      525    424   1052    -53    270    121       N  
ATOM   2840  NH2 ARG B 508      -1.320   1.609 -10.833  1.00  6.65           N  
ANISOU 2840  NH2 ARG B 508      672    617   1238    -69    274     65       N  
ATOM   2841  N   GLU B 509       3.513   1.112  -3.031  1.00  7.83           N  
ANISOU 2841  N   GLU B 509     1062    662   1252    206    182    255       N  
ATOM   2842  CA  GLU B 509       4.263   1.851  -2.022  1.00  8.04           C  
ANISOU 2842  CA  GLU B 509     1103    715   1238    228    138    277       C  
ATOM   2843  C   GLU B 509       5.595   1.168  -1.711  1.00  8.60           C  
ANISOU 2843  C   GLU B 509     1174    788   1306    292     89    282       C  
ATOM   2844  O   GLU B 509       6.543   1.808  -1.264  1.00  8.43           O  
ANISOU 2844  O   GLU B 509     1132    810   1262    312     38    284       O  
ATOM   2845  CB  GLU B 509       3.405   2.046  -0.768  1.00  8.26           C  
ANISOU 2845  CB  GLU B 509     1205    704   1228    215    161    309       C  
ATOM   2846  CG  GLU B 509       4.038   2.918   0.300  1.00  9.98           C  
ANISOU 2846  CG  GLU B 509     1446    950   1395    228    117    326       C  
ATOM   2847  CD  GLU B 509       4.102   4.381  -0.097  1.00  9.52           C  
ANISOU 2847  CD  GLU B 509     1332    948   1337    191    101    304       C  
ATOM   2848  OE1 GLU B 509       3.163   5.123   0.258  1.00 11.80           O  
ANISOU 2848  OE1 GLU B 509     1640   1229   1615    156    131    305       O  
ATOM   2849  OE2 GLU B 509       5.075   4.788  -0.775  1.00  9.27           O  
ANISOU 2849  OE2 GLU B 509     1238    967   1319    196     63    284       O  
ATOM   2850  N   LYS B 510       5.674  -0.130  -1.978  1.00  9.00           N  
ANISOU 2850  N   LYS B 510     1242    791   1385    326    103    280       N  
ATOM   2851  CA  LYS B 510       6.935  -0.844  -1.779  1.00 10.28           C  
ANISOU 2851  CA  LYS B 510     1396    951   1558    397     55    281       C  
ATOM   2852  C   LYS B 510       8.017  -0.450  -2.795  1.00 10.54           C  
ANISOU 2852  C   LYS B 510     1330   1056   1620    405     29    236       C  
ATOM   2853  O   LYS B 510       9.208  -0.626  -2.531  1.00 12.13           O  
ANISOU 2853  O   LYS B 510     1501   1279   1827    460    -22    231       O  
ATOM   2854  CB  LYS B 510       6.711  -2.357  -1.806  1.00 11.03           C  
ANISOU 2854  CB  LYS B 510     1542    965   1682    433     79    290       C  
ATOM   2855  CG  LYS B 510       6.066  -2.872  -0.532  1.00 12.70           C  
ANISOU 2855  CG  LYS B 510     1864   1105   1857    441     90    344       C  
ATOM   2856  CD  LYS B 510       6.205  -4.380  -0.386  1.00 17.15           C  
ANISOU 2856  CD  LYS B 510     2486   1582   2447    493     95    361       C  
ATOM   2857  CE  LYS B 510       5.200  -5.133  -1.223  1.00 19.27           C  
ANISOU 2857  CE  LYS B 510     2763   1800   2760    451    166    338       C  
ATOM   2858  NZ  LYS B 510       5.343  -6.611  -0.949  1.00 20.43           N  
ANISOU 2858  NZ  LYS B 510     2981   1849   2932    502    170    359       N  
ATOM   2859  N   VAL B 511       7.604   0.088  -3.942  1.00 10.07           N  
ANISOU 2859  N   VAL B 511     1218   1033   1576    350     63    203       N  
ATOM   2860  CA  VAL B 511       8.555   0.364  -5.041  1.00 10.14           C  
ANISOU 2860  CA  VAL B 511     1137   1107   1608    348     54    157       C  
ATOM   2861  C   VAL B 511       8.715   1.837  -5.437  1.00  9.46           C  
ANISOU 2861  C   VAL B 511     1001   1093   1502    293     45    147       C  
ATOM   2862  O   VAL B 511       9.658   2.186  -6.162  1.00 10.13           O  
ANISOU 2862  O   VAL B 511     1014   1237   1599    288     36    115       O  
ATOM   2863  CB  VAL B 511       8.258  -0.488  -6.311  1.00 10.37           C  
ANISOU 2863  CB  VAL B 511     1145   1121   1674    339    101    117       C  
ATOM   2864  CG1 VAL B 511       8.460  -1.971  -6.029  1.00 12.08           C  
ANISOU 2864  CG1 VAL B 511     1399   1268   1922    403    103    117       C  
ATOM   2865  CG2 VAL B 511       6.858  -0.211  -6.862  1.00 10.29           C  
ANISOU 2865  CG2 VAL B 511     1157   1096   1657    272    145    118       C  
ATOM   2866  N   ILE B 512       7.796   2.686  -4.986  1.00  8.09           N  
ANISOU 2866  N   ILE B 512      863    911   1299    250     53    173       N  
ATOM   2867  CA  ILE B 512       7.912   4.134  -5.183  1.00  8.23           C  
ANISOU 2867  CA  ILE B 512      847    983   1298    200     40    171       C  
ATOM   2868  C   ILE B 512       7.560   4.824  -3.872  1.00  8.34           C  
ANISOU 2868  C   ILE B 512      912    978   1277    198     19    203       C  
ATOM   2869  O   ILE B 512       7.046   4.175  -2.952  1.00  8.00           O  
ANISOU 2869  O   ILE B 512      935    884   1222    225     25    229       O  
ATOM   2870  CB  ILE B 512       7.009   4.668  -6.346  1.00  7.36           C  
ANISOU 2870  CB  ILE B 512      719    884   1193    139     76    158       C  
ATOM   2871  CG1 ILE B 512       5.520   4.415  -6.059  1.00  7.71           C  
ANISOU 2871  CG1 ILE B 512      819    872   1239    123    109    177       C  
ATOM   2872  CG2 ILE B 512       7.434   4.066  -7.705  1.00  8.24           C  
ANISOU 2872  CG2 ILE B 512      782   1022   1326    135     98    120       C  
ATOM   2873  CD1 ILE B 512       4.558   5.254  -6.936  1.00  8.03           C  
ANISOU 2873  CD1 ILE B 512      843    926   1281     66    126    172       C  
ATOM   2874  N   ASP B 513       7.839   6.119  -3.778  1.00  7.86           N  
ANISOU 2874  N   ASP B 513      829    959   1200    163     -3    202       N  
ATOM   2875  CA  ASP B 513       7.435   6.907  -2.613  1.00  8.90           C  
ANISOU 2875  CA  ASP B 513     1010   1074   1296    153    -18    224       C  
ATOM   2876  C   ASP B 513       6.234   7.776  -2.945  1.00  8.76           C  
ANISOU 2876  C   ASP B 513     1005   1042   1281    102     16    227       C  
ATOM   2877  O   ASP B 513       6.346   8.746  -3.696  1.00  9.72           O  
ANISOU 2877  O   ASP B 513     1088   1196   1410     62     12    216       O  
ATOM   2878  CB  ASP B 513       8.583   7.816  -2.151  1.00  9.19           C  
ANISOU 2878  CB  ASP B 513     1016   1159   1315    150    -70    215       C  
ATOM   2879  CG  ASP B 513       9.590   7.117  -1.227  1.00 10.70           C  
ANISOU 2879  CG  ASP B 513     1216   1356   1494    209   -120    220       C  
ATOM   2880  OD1 ASP B 513       9.356   5.994  -0.731  1.00 12.93           O  
ANISOU 2880  OD1 ASP B 513     1546   1595   1772    256   -116    239       O  
ATOM   2881  OD2 ASP B 513      10.646   7.717  -0.966  1.00 12.17           O  
ANISOU 2881  OD2 ASP B 513     1361   1589   1674    208   -168    205       O  
ATOM   2882  N   PHE B 514       5.085   7.442  -2.383  1.00  8.17           N  
ANISOU 2882  N   PHE B 514      985    918   1202    104     49    243       N  
ATOM   2883  CA  PHE B 514       3.893   8.254  -2.579  1.00  7.49           C  
ANISOU 2883  CA  PHE B 514      907    816   1124     64     79    243       C  
ATOM   2884  C   PHE B 514       3.803   9.411  -1.598  1.00  7.24           C  
ANISOU 2884  C   PHE B 514      902    783   1064     51     65    248       C  
ATOM   2885  O   PHE B 514       4.135   9.269  -0.414  1.00  7.64           O  
ANISOU 2885  O   PHE B 514      998    824   1079     74     50    258       O  
ATOM   2886  CB  PHE B 514       2.638   7.424  -2.315  1.00  7.68           C  
ANISOU 2886  CB  PHE B 514      970    788   1161     67    128    252       C  
ATOM   2887  CG  PHE B 514       2.137   6.628  -3.480  1.00  6.47           C  
ANISOU 2887  CG  PHE B 514      787    627   1044     57    154    239       C  
ATOM   2888  CD1 PHE B 514       1.464   7.250  -4.535  1.00  5.98           C  
ANISOU 2888  CD1 PHE B 514      687    580   1007     20    161    226       C  
ATOM   2889  CD2 PHE B 514       2.237   5.244  -3.465  1.00  6.43           C  
ANISOU 2889  CD2 PHE B 514      802    593   1048     84    170    241       C  
ATOM   2890  CE1 PHE B 514       0.937   6.492  -5.582  1.00  7.80           C  
ANISOU 2890  CE1 PHE B 514      894    805   1266      8    181    211       C  
ATOM   2891  CE2 PHE B 514       1.720   4.488  -4.514  1.00  8.32           C  
ANISOU 2891  CE2 PHE B 514     1019    822   1322     71    196    223       C  
ATOM   2892  CZ  PHE B 514       1.075   5.118  -5.552  1.00  8.48           C  
ANISOU 2892  CZ  PHE B 514      998    864   1361     32    201    206       C  
ATOM   2893  N   SER B 515       3.303  10.545  -2.076  1.00  6.92           N  
ANISOU 2893  N   SER B 515      842    748   1038     15     68    240       N  
ATOM   2894  CA  SER B 515       2.829  11.585  -1.171  1.00  6.93           C  
ANISOU 2894  CA  SER B 515      878    732   1024      2     70    239       C  
ATOM   2895  C   SER B 515       1.619  11.084  -0.388  1.00  7.68           C  
ANISOU 2895  C   SER B 515     1020    781   1117     12    120    243       C  
ATOM   2896  O   SER B 515       1.020  10.059  -0.733  1.00  7.97           O  
ANISOU 2896  O   SER B 515     1056    798   1174     19    152    248       O  
ATOM   2897  CB  SER B 515       2.426  12.852  -1.930  1.00  7.82           C  
ANISOU 2897  CB  SER B 515      962    847   1163    -33     65    231       C  
ATOM   2898  OG  SER B 515       1.176  12.656  -2.590  1.00  7.60           O  
ANISOU 2898  OG  SER B 515      922    795   1172    -41     99    231       O  
ATOM   2899  N   LYS B 516       1.240  11.821   0.642  1.00  7.17           N  
ANISOU 2899  N   LYS B 516      995    699   1029      7    130    238       N  
ATOM   2900  CA  LYS B 516      -0.072  11.621   1.250  1.00  7.65           C  
ANISOU 2900  CA  LYS B 516     1090    720   1097      5    189    234       C  
ATOM   2901  C   LYS B 516      -1.177  11.936   0.227  1.00  7.26           C  
ANISOU 2901  C   LYS B 516      991    658   1108    -13    214    223       C  
ATOM   2902  O   LYS B 516      -0.937  12.620  -0.768  1.00  7.42           O  
ANISOU 2902  O   LYS B 516      968    698   1155    -27    181    220       O  
ATOM   2903  CB  LYS B 516      -0.198  12.407   2.549  1.00  8.09           C  
ANISOU 2903  CB  LYS B 516     1198    763   1111      3    199    223       C  
ATOM   2904  CG  LYS B 516       0.601  11.719   3.644  1.00  8.73           C  
ANISOU 2904  CG  LYS B 516     1340    850   1126     25    181    239       C  
ATOM   2905  CD  LYS B 516       0.386  12.321   5.006  1.00  9.36           C  
ANISOU 2905  CD  LYS B 516     1486    918   1152     21    198    227       C  
ATOM   2906  CE  LYS B 516       1.037  11.501   6.090  1.00  9.54           C  
ANISOU 2906  CE  LYS B 516     1580    943   1102     43    180    250       C  
ATOM   2907  NZ  LYS B 516       2.520  11.449   5.941  1.00  7.76           N  
ANISOU 2907  NZ  LYS B 516     1335    757    858     63     98    259       N  
ATOM   2908  N   PRO B 517      -2.361  11.331   0.418  1.00  7.99           N  
ANISOU 2908  N   PRO B 517     1091    720   1224    -16    270    218       N  
ATOM   2909  CA  PRO B 517      -3.394  11.455  -0.606  1.00  7.70           C  
ANISOU 2909  CA  PRO B 517      999    676   1249    -30    285    206       C  
ATOM   2910  C   PRO B 517      -3.995  12.848  -0.750  1.00  7.74           C  
ANISOU 2910  C   PRO B 517      980    674   1286    -38    276    189       C  
ATOM   2911  O   PRO B 517      -4.163  13.573   0.240  1.00  8.99           O  
ANISOU 2911  O   PRO B 517     1169    817   1428    -35    294    176       O  
ATOM   2912  CB  PRO B 517      -4.468  10.464  -0.132  1.00  8.72           C  
ANISOU 2912  CB  PRO B 517     1145    775   1395    -35    351    201       C  
ATOM   2913  CG  PRO B 517      -4.247  10.308   1.303  1.00  9.51           C  
ANISOU 2913  CG  PRO B 517     1315    859   1439    -26    380    207       C  
ATOM   2914  CD  PRO B 517      -2.773  10.431   1.512  1.00  8.95           C  
ANISOU 2914  CD  PRO B 517     1270    815   1316     -9    321    225       C  
ATOM   2915  N   PHE B 518      -4.350  13.175  -1.983  1.00  7.27           N  
ANISOU 2915  N   PHE B 518      854    602   1308   -134    164    -56       N  
ATOM   2916  CA  PHE B 518      -5.060  14.420  -2.270  1.00  7.75           C  
ANISOU 2916  CA  PHE B 518      894    658   1393   -109    144    -32       C  
ATOM   2917  C   PHE B 518      -6.551  14.224  -2.574  1.00  8.15           C  
ANISOU 2917  C   PHE B 518      878    723   1495    -96    152    -48       C  
ATOM   2918  O   PHE B 518      -7.289  15.205  -2.693  1.00  8.61           O  
ANISOU 2918  O   PHE B 518      902    756   1613    -61    118    -45       O  
ATOM   2919  CB  PHE B 518      -4.373  15.209  -3.397  1.00  7.99           C  
ANISOU 2919  CB  PHE B 518      933    701   1401   -132     92      6       C  
ATOM   2920  CG  PHE B 518      -4.245  14.460  -4.703  1.00  6.89           C  
ANISOU 2920  CG  PHE B 518      786    610   1222   -180     91      7       C  
ATOM   2921  CD1 PHE B 518      -3.050  13.837  -5.046  1.00  7.40           C  
ANISOU 2921  CD1 PHE B 518      854    693   1266   -219    133    -15       C  
ATOM   2922  CD2 PHE B 518      -5.303  14.417  -5.607  1.00  7.21           C  
ANISOU 2922  CD2 PHE B 518      821    660   1259   -188     40     21       C  
ATOM   2923  CE1 PHE B 518      -2.916  13.181  -6.261  1.00  6.87           C  
ANISOU 2923  CE1 PHE B 518      800    660   1149   -270    156    -27       C  
ATOM   2924  CE2 PHE B 518      -5.175  13.752  -6.830  1.00  6.74           C  
ANISOU 2924  CE2 PHE B 518      797    627   1136   -242     32     23       C  
ATOM   2925  CZ  PHE B 518      -3.981  13.123  -7.152  1.00  6.66           C  
ANISOU 2925  CZ  PHE B 518      807    644   1081   -285    106     -4       C  
ATOM   2926  N   MET B 519      -6.985  12.973  -2.708  1.00  8.20           N  
ANISOU 2926  N   MET B 519      856    759   1501   -121    181    -70       N  
ATOM   2927  CA  MET B 519      -8.377  12.656  -3.011  1.00  9.03           C  
ANISOU 2927  CA  MET B 519      876    871   1685   -118    181    -91       C  
ATOM   2928  C   MET B 519      -8.625  11.206  -2.624  1.00  8.71           C  
ANISOU 2928  C   MET B 519      836    847   1626   -159    241   -119       C  
ATOM   2929  O   MET B 519      -7.724  10.376  -2.751  1.00  9.08           O  
ANISOU 2929  O   MET B 519      941    909   1599   -184    232   -113       O  
ATOM   2930  CB  MET B 519      -8.665  12.861  -4.504  1.00  9.34           C  
ANISOU 2930  CB  MET B 519      893    922   1734   -126     68    -59       C  
ATOM   2931  CG  MET B 519     -10.144  12.799  -4.892  1.00 10.06           C  
ANISOU 2931  CG  MET B 519      880    990   1953   -111     12    -79       C  
ATOM   2932  SD  MET B 519     -10.482  13.117  -6.635  1.00 12.34           S  
ANISOU 2932  SD  MET B 519     1204   1248   2235   -129   -180    -33       S  
ATOM   2933  CE  MET B 519      -9.963  14.822  -6.783  1.00 13.14           C  
ANISOU 2933  CE  MET B 519     1376   1302   2313   -102   -252      6       C  
ATOM   2934  N   THR B 520      -9.840  10.910  -2.161  1.00  9.56           N  
ANISOU 2934  N   THR B 520      872    942   1818   -168    304   -157       N  
ATOM   2935  CA  THR B 520     -10.257   9.559  -1.779  1.00 10.54           C  
ANISOU 2935  CA  THR B 520     1002   1072   1929   -225    366   -182       C  
ATOM   2936  C   THR B 520     -11.186   8.963  -2.832  1.00 10.40           C  
ANISOU 2936  C   THR B 520      880   1076   1994   -240    300   -183       C  
ATOM   2937  O   THR B 520     -11.842   9.696  -3.571  1.00 12.00           O  
ANISOU 2937  O   THR B 520      993   1269   2299   -205    221   -179       O  
ATOM   2938  CB  THR B 520     -11.011   9.560  -0.426  1.00 12.09           C  
ANISOU 2938  CB  THR B 520     1206   1228   2161   -256    519   -234       C  
ATOM   2939  OG1 THR B 520     -12.197  10.351  -0.546  1.00 17.40           O  
ANISOU 2939  OG1 THR B 520     1729   1887   2997   -224    553   -276       O  
ATOM   2940  CG2 THR B 520     -10.124  10.105   0.682  1.00 13.73           C  
ANISOU 2940  CG2 THR B 520     1561   1390   2267   -251    565   -232       C  
ATOM   2941  N   LEU B 521     -11.218   7.634  -2.902  1.00  9.39           N  
ANISOU 2941  N   LEU B 521      781    963   1824   -292    307   -186       N  
ATOM   2942  CA  LEU B 521     -12.071   6.929  -3.863  1.00  9.98           C  
ANISOU 2942  CA  LEU B 521      776   1046   1969   -316    230   -186       C  
ATOM   2943  C   LEU B 521     -12.226   5.490  -3.423  1.00  9.87           C  
ANISOU 2943  C   LEU B 521      803   1032   1914   -385    281   -201       C  
ATOM   2944  O   LEU B 521     -11.528   5.025  -2.524  1.00  9.48           O  
ANISOU 2944  O   LEU B 521      867    970   1766   -412    345   -206       O  
ATOM   2945  CB  LEU B 521     -11.465   6.989  -5.282  1.00  9.68           C  
ANISOU 2945  CB  LEU B 521      788   1027   1864   -297     91   -145       C  
ATOM   2946  CG  LEU B 521     -10.149   6.294  -5.705  1.00 11.08           C  
ANISOU 2946  CG  LEU B 521     1085   1229   1894   -308     77   -133       C  
ATOM   2947  CD1 LEU B 521      -8.963   6.839  -4.900  1.00 12.54           C  
ANISOU 2947  CD1 LEU B 521     1330   1414   2021   -283    140   -135       C  
ATOM   2948  CD2 LEU B 521     -10.181   4.778  -5.683  1.00 13.23           C  
ANISOU 2948  CD2 LEU B 521     1391   1504   2131   -352     78   -151       C  
ATOM   2949  N   GLY B 522     -13.152   4.789  -4.062  1.00  7.11           N  
ANISOU 2949  N   GLY B 522      699    862   1140   -136    132    -54       N  
ATOM   2950  CA  GLY B 522     -13.248   3.349  -3.941  1.00  7.24           C  
ANISOU 2950  CA  GLY B 522      732    913   1106   -159    132    -20       C  
ATOM   2951  C   GLY B 522     -13.710   2.772  -5.257  1.00  6.68           C  
ANISOU 2951  C   GLY B 522      631    849   1057   -171    155     26       C  
ATOM   2952  O   GLY B 522     -14.342   3.460  -6.060  1.00  7.24           O  
ANISOU 2952  O   GLY B 522      674    916   1160   -159    177     33       O  
ATOM   2953  N   ILE B 523     -13.358   1.520  -5.498  1.00  6.51           N  
ANISOU 2953  N   ILE B 523      621    833   1020   -193    143     56       N  
ATOM   2954  CA  ILE B 523     -13.837   0.832  -6.693  1.00  6.38           C  
ANISOU 2954  CA  ILE B 523      589    824   1012   -208    160     92       C  
ATOM   2955  C   ILE B 523     -15.345   0.610  -6.612  1.00  6.68           C  
ANISOU 2955  C   ILE B 523      613    904   1020   -215    190    104       C  
ATOM   2956  O   ILE B 523     -15.875   0.256  -5.561  1.00  7.45           O  
ANISOU 2956  O   ILE B 523      726   1031   1075   -222    204    100       O  
ATOM   2957  CB  ILE B 523     -13.153  -0.531  -6.849  1.00  4.93           C  
ANISOU 2957  CB  ILE B 523      426    630    819   -229    142    114       C  
ATOM   2958  CG1 ILE B 523     -11.645  -0.350  -7.105  1.00  6.26           C  
ANISOU 2958  CG1 ILE B 523      590    755   1035   -219    118    106       C  
ATOM   2959  CG2 ILE B 523     -13.811  -1.346  -7.977  1.00  6.63           C  
ANISOU 2959  CG2 ILE B 523      634    853   1031   -248    158    142       C  
ATOM   2960  CD1 ILE B 523     -10.878  -1.648  -6.945  1.00  7.64           C  
ANISOU 2960  CD1 ILE B 523      783    914   1205   -229     95    122       C  
ATOM   2961  N   SER B 524     -16.025   0.829  -7.733  1.00  6.34           N  
ANISOU 2961  N   SER B 524      542    867   1001   -215    200    121       N  
ATOM   2962  CA  SER B 524     -17.424   0.458  -7.874  1.00  6.72           C  
ANISOU 2962  CA  SER B 524      564    953   1037   -227    219    137       C  
ATOM   2963  C   SER B 524     -17.685  -0.011  -9.310  1.00  6.30           C  
ANISOU 2963  C   SER B 524      500    897    998   -242    203    163       C  
ATOM   2964  O   SER B 524     -16.740  -0.309 -10.045  1.00  6.94           O  
ANISOU 2964  O   SER B 524      605    949   1083   -246    188    168       O  
ATOM   2965  CB  SER B 524     -18.343   1.607  -7.417  1.00  6.73           C  
ANISOU 2965  CB  SER B 524      532    973   1053   -197    245    118       C  
ATOM   2966  OG  SER B 524     -19.698   1.198  -7.353  1.00  8.57           O  
ANISOU 2966  OG  SER B 524      728   1247   1282   -210    268    133       O  
ATOM   2967  N   ILE B 525     -18.957  -0.136  -9.692  1.00  6.94           N  
ANISOU 2967  N   ILE B 525      545   1008   1083   -251    206    176       N  
ATOM   2968  CA  ILE B 525     -19.335  -0.651 -11.009  1.00  7.56           C  
ANISOU 2968  CA  ILE B 525      619   1089   1165   -269    180    197       C  
ATOM   2969  C   ILE B 525     -20.042   0.423 -11.825  1.00  7.39           C  
ANISOU 2969  C   ILE B 525      562   1074   1171   -241    167    206       C  
ATOM   2970  O   ILE B 525     -20.960   1.065 -11.324  1.00  7.40           O  
ANISOU 2970  O   ILE B 525      518   1097   1195   -223    182    202       O  
ATOM   2971  CB  ILE B 525     -20.276  -1.867 -10.846  1.00  7.59           C  
ANISOU 2971  CB  ILE B 525      607   1117   1158   -313    177    208       C  
ATOM   2972  CG1 ILE B 525     -19.575  -2.963 -10.038  1.00  8.73           C  
ANISOU 2972  CG1 ILE B 525      793   1247   1277   -339    187    208       C  
ATOM   2973  CG2 ILE B 525     -20.750  -2.379 -12.209  1.00  8.84           C  
ANISOU 2973  CG2 ILE B 525      763   1277   1319   -334    138    221       C  
ATOM   2974  CD1 ILE B 525     -20.530  -4.027  -9.503  1.00  9.84           C  
ANISOU 2974  CD1 ILE B 525      918   1408   1414   -383    198    225       C  
ATOM   2975  N   LEU B 526     -19.602   0.604 -13.074  1.00  7.51           N  
ANISOU 2975  N   LEU B 526      601   1071   1181   -235    143    219       N  
ATOM   2976  CA  LEU B 526     -20.280   1.448 -14.056  1.00  6.99           C  
ANISOU 2976  CA  LEU B 526      514   1011   1132   -211    119    240       C  
ATOM   2977  C   LEU B 526     -21.038   0.572 -15.047  1.00  8.11           C  
ANISOU 2977  C   LEU B 526      655   1175   1252   -240     76    254       C  
ATOM   2978  O   LEU B 526     -20.459  -0.334 -15.655  1.00  7.32           O  
ANISOU 2978  O   LEU B 526      602   1063   1115   -266     65    251       O  
ATOM   2979  CB  LEU B 526     -19.258   2.296 -14.817  1.00  7.00           C  
ANISOU 2979  CB  LEU B 526      552    975   1134   -186    122    252       C  
ATOM   2980  CG  LEU B 526     -19.876   3.277 -15.816  1.00  7.53           C  
ANISOU 2980  CG  LEU B 526      607   1041   1214   -156     95    283       C  
ATOM   2981  CD1 LEU B 526     -20.435   4.459 -15.049  1.00  9.88           C  
ANISOU 2981  CD1 LEU B 526      857   1332   1565   -119    108    277       C  
ATOM   2982  CD2 LEU B 526     -18.862   3.713 -16.854  1.00  8.56           C  
ANISOU 2982  CD2 LEU B 526      789   1138   1325   -146    101    307       C  
ATOM   2983  N   TYR B 527     -22.330   0.837 -15.218  1.00  8.30           N  
ANISOU 2983  N   TYR B 527      623   1228   1301   -236     49    266       N  
ATOM   2984  CA  TYR B 527     -23.112   0.124 -16.233  1.00  9.41           C  
ANISOU 2984  CA  TYR B 527      759   1390   1427   -264     -8    277       C  
ATOM   2985  C   TYR B 527     -24.210   1.029 -16.794  1.00 10.31           C  
ANISOU 2985  C   TYR B 527      819   1524   1576   -233    -51    301       C  
ATOM   2986  O   TYR B 527     -24.329   2.192 -16.409  1.00  9.88           O  
ANISOU 2986  O   TYR B 527      734   1462   1559   -188    -30    308       O  
ATOM   2987  CB  TYR B 527     -23.656  -1.251 -15.721  1.00 10.18           C  
ANISOU 2987  CB  TYR B 527      837   1505   1527   -319    -10    263       C  
ATOM   2988  CG  TYR B 527     -24.143  -2.136 -16.872  1.00 11.59           C  
ANISOU 2988  CG  TYR B 527     1032   1689   1681   -356    -76    264       C  
ATOM   2989  CD1 TYR B 527     -23.319  -2.391 -17.967  1.00 13.82           C  
ANISOU 2989  CD1 TYR B 527     1394   1951   1907   -355    -98    259       C  
ATOM   2990  CD2 TYR B 527     -25.440  -2.649 -16.902  1.00 15.63           C  
ANISOU 2990  CD2 TYR B 527     1478   2229   2230   -390   -116    267       C  
ATOM   2991  CE1 TYR B 527     -23.757  -3.157 -19.062  1.00 15.88           C  
ANISOU 2991  CE1 TYR B 527     1683   2217   2134   -386   -163    252       C  
ATOM   2992  CE2 TYR B 527     -25.887  -3.427 -17.992  1.00 15.77           C  
ANISOU 2992  CE2 TYR B 527     1515   2250   2227   -427   -189    261       C  
ATOM   2993  CZ  TYR B 527     -25.030  -3.677 -19.067  1.00 17.01           C  
ANISOU 2993  CZ  TYR B 527     1765   2385   2314   -423   -215    250       C  
ATOM   2994  OH  TYR B 527     -25.451  -4.423 -20.157  1.00 18.00           O  
ANISOU 2994  OH  TYR B 527     1922   2512   2406   -457   -290    236       O  
ATOM   2995  N   ARG B 528     -24.976   0.502 -17.747  1.00 11.58           N  
ANISOU 2995  N   ARG B 528      971   1705   1724   -256   -118    311       N  
ATOM   2996  CA  ARG B 528     -26.180   1.182 -18.219  1.00 13.70           C  
ANISOU 2996  CA  ARG B 528     1173   1998   2036   -231   -173    335       C  
ATOM   2997  C   ARG B 528     -27.333   0.941 -17.237  1.00 14.67           C  
ANISOU 2997  C   ARG B 528     1193   2150   2230   -245   -157    326       C  
ATOM   2998  O   ARG B 528     -27.241   0.130 -16.315  1.00 14.72           O  
ANISOU 2998  O   ARG B 528     1191   2161   2240   -283   -108    305       O  
ATOM   2999  CB  ARG B 528     -26.572   0.697 -19.616  1.00 14.58           C  
ANISOU 2999  CB  ARG B 528     1315   2120   2103   -251   -263    347       C  
ATOM   3000  CG  ARG B 528     -25.570   1.059 -20.709  1.00 15.65           C  
ANISOU 3000  CG  ARG B 528     1553   2233   2162   -230   -274    363       C  
ATOM   3001  CD  ARG B 528     -26.109   0.771 -22.104  1.00 19.46           C  
ANISOU 3001  CD  ARG B 528     2069   2733   2591   -241   -371    378       C  
ATOM   3002  NE  ARG B 528     -26.801  -0.518 -22.217  1.00 23.33           N  
ANISOU 3002  NE  ARG B 528     2539   3244   3081   -300   -423    347       N  
ATOM   3003  CZ  ARG B 528     -26.210  -1.696 -22.408  1.00 24.54           C  
ANISOU 3003  CZ  ARG B 528     2758   3383   3182   -345   -413    312       C  
ATOM   3004  NH1 ARG B 528     -26.948  -2.796 -22.504  1.00 26.11           N  
ANISOU 3004  NH1 ARG B 528     2933   3593   3394   -401   -467    285       N  
ATOM   3005  NH2 ARG B 528     -24.892  -1.787 -22.504  1.00 24.66           N  
ANISOU 3005  NH2 ARG B 528     2859   3369   3141   -336   -350    302       N  
ATOM   3006  N   LYS B 529     -28.422   1.656 -17.449  1.00 16.92           N  
ANISOU 3006  N   LYS B 529     1398   2455   2575   -214   -195    345       N  
ATOM   3007  CA  LYS B 529     -29.576   1.536 -16.565  1.00 18.17           C  
ANISOU 3007  CA  LYS B 529     1446   2645   2813   -221   -170    339       C  
ATOM   3008  C   LYS B 529     -30.520   0.387 -16.938  1.00 19.62           C  
ANISOU 3008  C   LYS B 529     1577   2857   3019   -284   -228    339       C  
ATOM   3009  O   LYS B 529     -30.376  -0.236 -17.998  1.00 19.81           O  
ANISOU 3009  O   LYS B 529     1653   2877   2996   -316   -304    341       O  
ATOM   3010  CB  LYS B 529     -30.321   2.861 -16.552  1.00 18.80           C  
ANISOU 3010  CB  LYS B 529     1451   2728   2963   -152   -178    358       C  
ATOM   3011  CG  LYS B 529     -29.534   3.962 -15.904  1.00 20.04           C  
ANISOU 3011  CG  LYS B 529     1645   2852   3119    -97   -109    349       C  
ATOM   3012  CD  LYS B 529     -30.039   5.300 -16.332  1.00 21.58           C  
ANISOU 3012  CD  LYS B 529     1798   3031   3369    -25   -140    374       C  
ATOM   3013  CE  LYS B 529     -29.552   6.374 -15.389  1.00 20.93           C  
ANISOU 3013  CE  LYS B 529     1726   2915   3313     28    -61    353       C  
ATOM   3014  NZ  LYS B 529     -30.373   7.586 -15.582  1.00 22.31           N  
ANISOU 3014  NZ  LYS B 529     1831   3074   3570    100    -83    372       N  
ATOM   3015  N   GLY B 600     -31.472   0.092 -16.055  1.00 21.01           N  
ANISOU 3015  N   GLY B 600     1653   3060   3269   -304   -189    335       N  
ATOM   3016  CA  GLY B 600     -32.556  -0.840 -16.380  1.00 22.86           C  
ANISOU 3016  CA  GLY B 600     1811   3321   3555   -364   -247    339       C  
ATOM   3017  C   GLY B 600     -32.247  -2.301 -16.138  1.00 23.36           C  
ANISOU 3017  C   GLY B 600     1917   3374   3586   -445   -233    323       C  
ATOM   3018  O   GLY B 600     -32.956  -3.196 -16.632  1.00 25.17           O  
ANISOU 3018  O   GLY B 600     2106   3611   3846   -505   -299    322       O  
ATOM   3019  N   THR B 601     -31.210  -2.521 -15.340  1.00 23.23           N  
ANISOU 3019  N   THR B 601     1977   3336   3515   -447   -152    311       N  
ATOM   3020  CA  THR B 601     -30.657  -3.828 -15.037  1.00 22.79           C  
ANISOU 3020  CA  THR B 601     1982   3257   3419   -512   -131    299       C  
ATOM   3021  C   THR B 601     -31.061  -4.303 -13.630  1.00 22.60           C  
ANISOU 3021  C   THR B 601     1906   3246   3435   -543    -38    306       C  
ATOM   3022  O   THR B 601     -31.191  -3.479 -12.715  1.00 22.65           O  
ANISOU 3022  O   THR B 601     1875   3271   3459   -498     37    309       O  
ATOM   3023  CB  THR B 601     -29.107  -3.756 -15.144  1.00 22.37           C  
ANISOU 3023  CB  THR B 601     2055   3167   3276   -487   -109    286       C  
ATOM   3024  OG1 THR B 601     -28.519  -4.857 -14.454  1.00 21.95           O  
ANISOU 3024  OG1 THR B 601     2052   3090   3197   -534    -64    278       O  
ATOM   3025  CG2 THR B 601     -28.549  -2.420 -14.563  1.00 21.10           C  
ANISOU 3025  CG2 THR B 601     1904   3007   3107   -414    -50    287       C  
ATOM   3026  N   PRO B 652     -31.253  -5.627 -13.442  1.00 22.71           N  
ANISOU 3026  N   PRO B 652     1923   3247   3459   -619    -38    309       N  
ATOM   3027  CA  PRO B 652     -31.489  -6.119 -12.081  1.00 22.29           C  
ANISOU 3027  CA  PRO B 652     1841   3202   3427   -650     59    324       C  
ATOM   3028  C   PRO B 652     -30.214  -6.255 -11.238  1.00 20.87           C  
ANISOU 3028  C   PRO B 652     1766   2996   3166   -634    124    320       C  
ATOM   3029  O   PRO B 652     -30.298  -6.538 -10.044  1.00 21.03           O  
ANISOU 3029  O   PRO B 652     1781   3026   3184   -649    207    335       O  
ATOM   3030  CB  PRO B 652     -32.121  -7.498 -12.312  1.00 23.19           C  
ANISOU 3030  CB  PRO B 652     1926   3299   3585   -742     24    333       C  
ATOM   3031  CG  PRO B 652     -31.547  -7.954 -13.605  1.00 23.86           C  
ANISOU 3031  CG  PRO B 652     2089   3349   3627   -756    -77    309       C  
ATOM   3032  CD  PRO B 652     -31.289  -6.722 -14.435  1.00 23.19           C  
ANISOU 3032  CD  PRO B 652     2018   3281   3513   -681   -124    298       C  
ATOM   3033  N   ILE B 653     -29.048  -6.042 -11.851  1.00 19.35           N  
ANISOU 3033  N   ILE B 653     1668   2774   2909   -602     87    302       N  
ATOM   3034  CA  ILE B 653     -27.770  -6.187 -11.149  1.00 18.11           C  
ANISOU 3034  CA  ILE B 653     1605   2590   2687   -585    133    296       C  
ATOM   3035  C   ILE B 653     -27.607  -5.052 -10.143  1.00 17.45           C  
ANISOU 3035  C   ILE B 653     1509   2530   2590   -527    202    293       C  
ATOM   3036  O   ILE B 653     -27.703  -3.879 -10.505  1.00 17.13           O  
ANISOU 3036  O   ILE B 653     1443   2502   2563   -472    190    282       O  
ATOM   3037  CB  ILE B 653     -26.573  -6.239 -12.130  1.00 17.48           C  
ANISOU 3037  CB  ILE B 653     1616   2471   2554   -566     80    277       C  
ATOM   3038  CG1 ILE B 653     -26.720  -7.428 -13.088  1.00 18.50           C  
ANISOU 3038  CG1 ILE B 653     1769   2572   2687   -622     16    270       C  
ATOM   3039  CG2 ILE B 653     -25.252  -6.315 -11.373  1.00 16.95           C  
ANISOU 3039  CG2 ILE B 653     1628   2377   2435   -544    123    272       C  
ATOM   3040  CD1 ILE B 653     -25.843  -7.326 -14.335  1.00 19.70           C  
ANISOU 3040  CD1 ILE B 653     1997   2699   2791   -598    -38    247       C  
ATOM   3041  N   ASP B 654     -27.381  -5.411  -8.882  1.00 16.58           N  
ANISOU 3041  N   ASP B 654     1423   2422   2453   -538    271    303       N  
ATOM   3042  CA  ASP B 654     -27.324  -4.426  -7.800  1.00 16.50           C  
ANISOU 3042  CA  ASP B 654     1408   2438   2425   -488    340    293       C  
ATOM   3043  C   ASP B 654     -26.022  -4.466  -7.002  1.00 14.79           C  
ANISOU 3043  C   ASP B 654     1287   2198   2136   -470    362    284       C  
ATOM   3044  O   ASP B 654     -25.834  -3.695  -6.055  1.00 14.72           O  
ANISOU 3044  O   ASP B 654     1291   2204   2098   -430    412    268       O  
ATOM   3045  CB  ASP B 654     -28.509  -4.642  -6.851  1.00 17.76           C  
ANISOU 3045  CB  ASP B 654     1494   2637   2618   -513    416    312       C  
ATOM   3046  CG  ASP B 654     -28.779  -3.437  -5.972  1.00 20.63           C  
ANISOU 3046  CG  ASP B 654     1831   3033   2976   -452    486    292       C  
ATOM   3047  OD1 ASP B 654     -28.835  -2.308  -6.511  1.00 23.47           O  
ANISOU 3047  OD1 ASP B 654     2161   3393   3363   -397    460    268       O  
ATOM   3048  OD2 ASP B 654     -28.947  -3.625  -4.746  1.00 24.82           O  
ANISOU 3048  OD2 ASP B 654     2373   3584   3472   -459    568    299       O  
ATOM   3049  N   SER B 655     -25.128  -5.377  -7.372  1.00 13.15           N  
ANISOU 3049  N   SER B 655     1146   1950   1900   -497    321    290       N  
ATOM   3050  CA  SER B 655     -23.886  -5.563  -6.625  1.00 11.88           C  
ANISOU 3050  CA  SER B 655     1069   1764   1681   -483    331    287       C  
ATOM   3051  C   SER B 655     -22.858  -6.361  -7.411  1.00 10.98           C  
ANISOU 3051  C   SER B 655     1014   1601   1557   -498    275    286       C  
ATOM   3052  O   SER B 655     -23.188  -6.979  -8.408  1.00 10.50           O  
ANISOU 3052  O   SER B 655      940   1525   1525   -529    237    289       O  
ATOM   3053  CB  SER B 655     -24.164  -6.329  -5.332  1.00 12.55           C  
ANISOU 3053  CB  SER B 655     1173   1862   1735   -516    387    316       C  
ATOM   3054  OG  SER B 655     -24.593  -7.646  -5.636  1.00 14.50           O  
ANISOU 3054  OG  SER B 655     1415   2089   2007   -580    374    347       O  
ATOM   3055  N   ALA B 656     -21.623  -6.371  -6.919  1.00 10.63           N  
ANISOU 3055  N   ALA B 656     1034   1531   1475   -475    271    279       N  
ATOM   3056  CA  ALA B 656     -20.576  -7.222  -7.483  1.00 10.08           C  
ANISOU 3056  CA  ALA B 656     1018   1412   1400   -484    230    280       C  
ATOM   3057  C   ALA B 656     -20.967  -8.705  -7.389  1.00 10.60           C  
ANISOU 3057  C   ALA B 656     1099   1453   1474   -542    227    309       C  
ATOM   3058  O   ALA B 656     -20.736  -9.461  -8.332  1.00 10.11           O  
ANISOU 3058  O   ALA B 656     1055   1355   1431   -562    191    303       O  
ATOM   3059  CB  ALA B 656     -19.248  -6.969  -6.787  1.00 10.07           C  
ANISOU 3059  CB  ALA B 656     1069   1391   1368   -449    225    271       C  
ATOM   3060  N   ASP B 657     -21.582  -9.109  -6.275  1.00 11.06           N  
ANISOU 3060  N   ASP B 657     1153   1531   1518   -569    269    340       N  
ATOM   3061  CA  ASP B 657     -22.085 -10.477  -6.147  1.00 12.09           C  
ANISOU 3061  CA  ASP B 657     1292   1634   1666   -630    273    376       C  
ATOM   3062  C   ASP B 657     -23.029 -10.828  -7.299  1.00 11.86           C  
ANISOU 3062  C   ASP B 657     1211   1603   1694   -671    245    367       C  
ATOM   3063  O   ASP B 657     -22.908 -11.892  -7.919  1.00 11.94           O  
ANISOU 3063  O   ASP B 657     1247   1564   1727   -708    210    368       O  
ATOM   3064  CB  ASP B 657     -22.832 -10.667  -4.818  1.00 12.82           C  
ANISOU 3064  CB  ASP B 657     1376   1759   1737   -656    338    416       C  
ATOM   3065  CG  ASP B 657     -21.909 -10.860  -3.627  1.00 16.21           C  
ANISOU 3065  CG  ASP B 657     1881   2177   2101   -635    351    438       C  
ATOM   3066  OD1 ASP B 657     -20.672 -10.878  -3.780  1.00 18.84           O  
ANISOU 3066  OD1 ASP B 657     2265   2475   2418   -601    306    423       O  
ATOM   3067  OD2 ASP B 657     -22.445 -11.015  -2.505  1.00 21.82           O  
ANISOU 3067  OD2 ASP B 657     2600   2915   2776   -653    409    474       O  
ATOM   3068  N   ASP B 658     -23.966  -9.926  -7.594  1.00 11.52           N  
ANISOU 3068  N   ASP B 658     1094   1608   1674   -662    256    354       N  
ATOM   3069  CA  ASP B 658     -24.925 -10.150  -8.683  1.00 12.23           C  
ANISOU 3069  CA  ASP B 658     1127   1702   1818   -698    217    345       C  
ATOM   3070  C   ASP B 658     -24.196 -10.237 -10.012  1.00 11.52           C  
ANISOU 3070  C   ASP B 658     1079   1577   1721   -682    150    312       C  
ATOM   3071  O   ASP B 658     -24.482 -11.097 -10.842  1.00 12.28           O  
ANISOU 3071  O   ASP B 658     1182   1643   1842   -724    105    303       O  
ATOM   3072  CB  ASP B 658     -25.932  -8.999  -8.782  1.00 13.09           C  
ANISOU 3072  CB  ASP B 658     1148   1868   1957   -674    232    338       C  
ATOM   3073  CG  ASP B 658     -26.935  -8.974  -7.647  1.00 14.85           C  
ANISOU 3073  CG  ASP B 658     1311   2131   2202   -696    306    368       C  
ATOM   3074  OD1 ASP B 658     -27.025  -9.960  -6.874  1.00 16.57           O  
ANISOU 3074  OD1 ASP B 658     1550   2332   2413   -743    343    401       O  
ATOM   3075  OD2 ASP B 658     -27.667  -7.957  -7.567  1.00 16.42           O  
ANISOU 3075  OD2 ASP B 658     1438   2375   2425   -664    331    359       O  
ATOM   3076  N   LEU B 659     -23.259  -9.318 -10.208  1.00 10.41           N  
ANISOU 3076  N   LEU B 659      969   1440   1547   -621    147    291       N  
ATOM   3077  CA  LEU B 659     -22.526  -9.242 -11.454  1.00  9.53           C  
ANISOU 3077  CA  LEU B 659      898   1302   1421   -599    100    262       C  
ATOM   3078  C   LEU B 659     -21.709 -10.511 -11.711  1.00  9.84           C  
ANISOU 3078  C   LEU B 659     1006   1281   1452   -622     82    255       C  
ATOM   3079  O   LEU B 659     -21.686 -11.027 -12.827  1.00 10.02           O  
ANISOU 3079  O   LEU B 659     1054   1278   1477   -637     40    231       O  
ATOM   3080  CB  LEU B 659     -21.632  -8.002 -11.425  1.00  9.22           C  
ANISOU 3080  CB  LEU B 659      872   1274   1356   -534    114    249       C  
ATOM   3081  CG  LEU B 659     -20.777  -7.705 -12.660  1.00  8.19           C  
ANISOU 3081  CG  LEU B 659      782   1121   1207   -504     84    226       C  
ATOM   3082  CD1 LEU B 659     -21.663  -7.428 -13.889  1.00  9.80           C  
ANISOU 3082  CD1 LEU B 659      960   1346   1417   -513     40    218       C  
ATOM   3083  CD2 LEU B 659     -19.821  -6.544 -12.405  1.00  9.69           C  
ANISOU 3083  CD2 LEU B 659      982   1314   1386   -449    107    220       C  
ATOM   3084  N   ALA B 660     -21.043 -11.005 -10.669  1.00 10.00           N  
ANISOU 3084  N   ALA B 660     1061   1277   1462   -620    111    275       N  
ATOM   3085  CA  ALA B 660     -20.217 -12.211 -10.791  1.00 10.25           C  
ANISOU 3085  CA  ALA B 660     1156   1244   1496   -633     95    272       C  
ATOM   3086  C   ALA B 660     -21.041 -13.460 -11.040  1.00 10.95           C  
ANISOU 3086  C   ALA B 660     1244   1298   1617   -701     75    280       C  
ATOM   3087  O   ALA B 660     -20.578 -14.399 -11.676  1.00 11.09           O  
ANISOU 3087  O   ALA B 660     1311   1258   1645   -713     47    260       O  
ATOM   3088  CB  ALA B 660     -19.375 -12.400  -9.542  1.00 10.44           C  
ANISOU 3088  CB  ALA B 660     1214   1251   1502   -613    122    299       C  
ATOM   3089  N   LYS B 661     -22.254 -13.477 -10.502  1.00 10.93           N  
ANISOU 3089  N   LYS B 661     1186   1328   1639   -744     93    308       N  
ATOM   3090  CA  LYS B 661     -23.106 -14.652 -10.585  1.00 11.92           C  
ANISOU 3090  CA  LYS B 661     1300   1419   1809   -818     78    322       C  
ATOM   3091  C   LYS B 661     -23.737 -14.825 -11.963  1.00 12.48           C  
ANISOU 3091  C   LYS B 661     1351   1484   1905   -846     17    282       C  
ATOM   3092  O   LYS B 661     -23.818 -15.936 -12.494  1.00 12.81           O  
ANISOU 3092  O   LYS B 661     1426   1468   1973   -892    -20    266       O  
ATOM   3093  CB  LYS B 661     -24.200 -14.557  -9.529  1.00 12.73           C  
ANISOU 3093  CB  LYS B 661     1338   1563   1935   -856    127    369       C  
ATOM   3094  CG  LYS B 661     -24.937 -15.854  -9.317  1.00 14.76           C  
ANISOU 3094  CG  LYS B 661     1588   1775   2245   -938    127    399       C  
ATOM   3095  CD  LYS B 661     -26.156 -15.659  -8.434  1.00 16.40           C  
ANISOU 3095  CD  LYS B 661     1715   2032   2484   -978    185    443       C  
ATOM   3096  CE  LYS B 661     -25.795 -15.118  -7.060  1.00 18.07           C  
ANISOU 3096  CE  LYS B 661     1945   2280   2639   -940    259    481       C  
ATOM   3097  NZ  LYS B 661     -27.019 -15.072  -6.195  1.00 18.66           N  
ANISOU 3097  NZ  LYS B 661     1946   2400   2743   -984    331    526       N  
ATOM   3098  N   GLN B 662     -24.203 -13.716 -12.526  1.00 12.77           N  
ANISOU 3098  N   GLN B 662     1339   1580   1934   -819      1    265       N  
ATOM   3099  CA  GLN B 662     -24.918 -13.752 -13.790  1.00 13.87           C  
ANISOU 3099  CA  GLN B 662     1456   1725   2089   -844    -66    232       C  
ATOM   3100  C   GLN B 662     -23.963 -14.036 -14.956  1.00 13.83           C  
ANISOU 3100  C   GLN B 662     1536   1679   2041   -818   -107    184       C  
ATOM   3101  O   GLN B 662     -22.745 -13.891 -14.832  1.00 13.46           O  
ANISOU 3101  O   GLN B 662     1547   1612   1957   -768    -77    178       O  
ATOM   3102  CB  GLN B 662     -25.730 -12.457 -13.988  1.00 13.78           C  
ANISOU 3102  CB  GLN B 662     1365   1787   2085   -817    -72    237       C  
ATOM   3103  CG  GLN B 662     -24.899 -11.175 -14.027  1.00 13.45           C  
ANISOU 3103  CG  GLN B 662     1342   1774   1993   -737    -48    231       C  
ATOM   3104  CD  GLN B 662     -24.261 -10.928 -15.381  1.00 14.20           C  
ANISOU 3104  CD  GLN B 662     1495   1856   2043   -705    -97    195       C  
ATOM   3105  OE1 GLN B 662     -24.955 -10.891 -16.407  1.00 15.15           O  
ANISOU 3105  OE1 GLN B 662     1600   1990   2165   -722   -160    178       O  
ATOM   3106  NE2 GLN B 662     -22.942 -10.783 -15.394  1.00 12.76           N  
ANISOU 3106  NE2 GLN B 662     1380   1649   1819   -661    -68    185       N  
ATOM   3107  N   THR B 663     -24.538 -14.448 -16.078  1.00 15.35           N  
ANISOU 3107  N   THR B 663     1734   1860   2238   -852   -175    149       N  
ATOM   3108  CA  THR B 663     -23.778 -14.863 -17.248  1.00 16.49           C  
ANISOU 3108  CA  THR B 663     1966   1963   2335   -835   -213     97       C  
ATOM   3109  C   THR B 663     -24.226 -14.127 -18.518  1.00 17.92           C  
ANISOU 3109  C   THR B 663     2145   2188   2477   -819   -274     69       C  
ATOM   3110  O   THR B 663     -23.875 -14.531 -19.635  1.00 19.54           O  
ANISOU 3110  O   THR B 663     2424   2366   2636   -816   -316     21       O  
ATOM   3111  CB  THR B 663     -23.907 -16.386 -17.461  1.00 17.13           C  
ANISOU 3111  CB  THR B 663     2091   1967   2449   -898   -246     70       C  
ATOM   3112  OG1 THR B 663     -25.292 -16.761 -17.398  1.00 17.17           O  
ANISOU 3112  OG1 THR B 663     2026   1982   2517   -972   -290     80       O  
ATOM   3113  CG2 THR B 663     -23.151 -17.145 -16.390  1.00 17.70           C  
ANISOU 3113  CG2 THR B 663     2194   1984   2546   -898   -188     98       C  
ATOM   3114  N   LYS B 664     -24.986 -13.048 -18.340  1.00 18.20           N  
ANISOU 3114  N   LYS B 664     2101   2289   2527   -804   -279     99       N  
ATOM   3115  CA  LYS B 664     -25.536 -12.293 -19.472  1.00 19.30           C  
ANISOU 3115  CA  LYS B 664     2229   2470   2634   -788   -346     85       C  
ATOM   3116  C   LYS B 664     -24.593 -11.182 -19.937  1.00 18.85           C  
ANISOU 3116  C   LYS B 664     2218   2435   2508   -710   -317     88       C  
ATOM   3117  O   LYS B 664     -24.382 -10.993 -21.140  1.00 20.13           O  
ANISOU 3117  O   LYS B 664     2440   2601   2607   -691   -360     62       O  
ATOM   3118  CB  LYS B 664     -26.929 -11.731 -19.137  1.00 19.57           C  
ANISOU 3118  CB  LYS B 664     2146   2557   2734   -810   -375    116       C  
ATOM   3119  CG  LYS B 664     -27.962 -12.787 -18.723  1.00 21.56           C  
ANISOU 3119  CG  LYS B 664     2336   2788   3066   -894   -402    118       C  
ATOM   3120  CD  LYS B 664     -29.338 -12.174 -18.431  1.00 24.09           C  
ANISOU 3120  CD  LYS B 664     2526   3165   3462   -912   -425    149       C  
ATOM   3121  CE  LYS B 664     -30.230 -13.164 -17.687  1.00 26.31           C  
ANISOU 3121  CE  LYS B 664     2734   3425   3836   -995   -415    166       C  
ATOM   3122  NZ  LYS B 664     -31.649 -12.721 -17.542  1.00 28.46           N  
ANISOU 3122  NZ  LYS B 664     2867   3749   4197  -1021   -442    190       N  
ATOM   3123  N   ILE B 665     -24.022 -10.445 -18.989  1.00 17.60           N  
ANISOU 3123  N   ILE B 665     2036   2290   2360   -668   -243    119       N  
ATOM   3124  CA  ILE B 665     -23.133  -9.338 -19.343  1.00 16.93           C  
ANISOU 3124  CA  ILE B 665     1985   2221   2227   -601   -212    127       C  
ATOM   3125  C   ILE B 665     -21.667  -9.615 -18.965  1.00 15.87           C  
ANISOU 3125  C   ILE B 665     1912   2045   2072   -573   -146    118       C  
ATOM   3126  O   ILE B 665     -21.388 -10.247 -17.946  1.00 15.69           O  
ANISOU 3126  O   ILE B 665     1881   1997   2084   -589   -110    125       O  
ATOM   3127  CB  ILE B 665     -23.660  -7.971 -18.812  1.00 17.69           C  
ANISOU 3127  CB  ILE B 665     2003   2366   2353   -566   -195    165       C  
ATOM   3128  CG1 ILE B 665     -23.425  -7.802 -17.316  1.00 18.38           C  
ANISOU 3128  CG1 ILE B 665     2049   2453   2480   -559   -125    186       C  
ATOM   3129  CG2 ILE B 665     -25.159  -7.783 -19.152  1.00 18.16           C  
ANISOU 3129  CG2 ILE B 665     1987   2463   2449   -592   -264    174       C  
ATOM   3130  CD1 ILE B 665     -23.471  -6.343 -16.878  1.00 20.23           C  
ANISOU 3130  CD1 ILE B 665     2238   2721   2728   -506    -95    209       C  
ATOM   3131  N   GLU B 666     -20.751  -9.179 -19.825  1.00 14.35           N  
ANISOU 3131  N   GLU B 666     1780   1847   1826   -531   -131    105       N  
ATOM   3132  CA  GLU B 666     -19.301  -9.282 -19.589  1.00 13.22           C  
ANISOU 3132  CA  GLU B 666     1682   1668   1673   -497    -68     98       C  
ATOM   3133  C   GLU B 666     -18.921  -8.140 -18.634  1.00 12.00           C  
ANISOU 3133  C   GLU B 666     1478   1535   1548   -460    -23    133       C  
ATOM   3134  O   GLU B 666     -19.690  -7.199 -18.442  1.00 12.28           O  
ANISOU 3134  O   GLU B 666     1460   1609   1596   -452    -36    156       O  
ATOM   3135  CB  GLU B 666     -18.533  -9.185 -20.934  1.00 14.05           C  
ANISOU 3135  CB  GLU B 666     1864   1762   1711   -468    -61     73       C  
ATOM   3136  CG  GLU B 666     -16.979  -9.369 -20.881  1.00 14.98           C  
ANISOU 3136  CG  GLU B 666     2024   1841   1826   -431      9     61       C  
ATOM   3137  CD  GLU B 666     -16.272  -9.341 -22.252  1.00 19.22           C  
ANISOU 3137  CD  GLU B 666     2639   2369   2295   -404     31     35       C  
ATOM   3138  OE1 GLU B 666     -16.700  -8.594 -23.160  1.00 21.58           O  
ANISOU 3138  OE1 GLU B 666     2958   2703   2539   -394      8     47       O  
ATOM   3139  OE2 GLU B 666     -15.265 -10.061 -22.421  1.00 19.39           O  
ANISOU 3139  OE2 GLU B 666     2703   2348   2315   -388     75      6       O  
ATOM   3140  N   TYR B 667     -17.765  -8.243 -17.996  1.00  9.60           N  
ANISOU 3140  N   TYR B 667     1188   1202   1259   -438     26    132       N  
ATOM   3141  CA  TYR B 667     -17.285  -7.151 -17.152  1.00  8.62           C  
ANISOU 3141  CA  TYR B 667     1025   1092   1159   -404     62    156       C  
ATOM   3142  C   TYR B 667     -15.774  -7.201 -17.064  1.00  8.13           C  
ANISOU 3142  C   TYR B 667      992    994   1104   -373    105    148       C  
ATOM   3143  O   TYR B 667     -15.145  -8.217 -17.398  1.00  8.39           O  
ANISOU 3143  O   TYR B 667     1067    990   1132   -377    113    126       O  
ATOM   3144  CB  TYR B 667     -17.913  -7.200 -15.747  1.00  8.36           C  
ANISOU 3144  CB  TYR B 667      941   1074   1162   -422     65    173       C  
ATOM   3145  CG  TYR B 667     -17.685  -8.513 -15.031  1.00  6.72           C  
ANISOU 3145  CG  TYR B 667      752    832    968   -452     68    170       C  
ATOM   3146  CD1 TYR B 667     -18.632  -9.542 -15.095  1.00  7.42           C  
ANISOU 3146  CD1 TYR B 667      840    914   1064   -502     39    167       C  
ATOM   3147  CD2 TYR B 667     -16.511  -8.735 -14.322  1.00  7.79           C  
ANISOU 3147  CD2 TYR B 667      907    937   1116   -430     95    171       C  
ATOM   3148  CE1 TYR B 667     -18.411 -10.766 -14.448  1.00  7.91           C  
ANISOU 3148  CE1 TYR B 667      925    935   1145   -530     43    171       C  
ATOM   3149  CE2 TYR B 667     -16.281  -9.938 -13.678  1.00  7.28           C  
ANISOU 3149  CE2 TYR B 667      865    835   1066   -452     92    175       C  
ATOM   3150  CZ  TYR B 667     -17.233 -10.948 -13.745  1.00  6.79           C  
ANISOU 3150  CZ  TYR B 667      807    762   1009   -501     70    176       C  
ATOM   3151  OH  TYR B 667     -17.006 -12.142 -13.107  1.00  9.01           O  
ANISOU 3151  OH  TYR B 667     1115    998   1309   -524     69    187       O  
ATOM   3152  N   GLY B 668     -15.178  -6.106 -16.627  1.00  7.76           N  
ANISOU 3152  N   GLY B 668      918    953   1076   -341    132    163       N  
ATOM   3153  CA  GLY B 668     -13.728  -6.044 -16.566  1.00  8.42           C  
ANISOU 3153  CA  GLY B 668     1014   1004   1180   -313    170    157       C  
ATOM   3154  C   GLY B 668     -13.240  -4.735 -16.015  1.00  7.89           C  
ANISOU 3154  C   GLY B 668      910    945   1144   -287    189    172       C  
ATOM   3155  O   GLY B 668     -13.964  -4.042 -15.303  1.00  8.37           O  
ANISOU 3155  O   GLY B 668      937   1030   1212   -289    174    183       O  
ATOM   3156  N   ALA B 669     -11.996  -4.411 -16.343  1.00  7.95           N  
ANISOU 3156  N   ALA B 669      921    926   1173   -263    224    170       N  
ATOM   3157  CA  ALA B 669     -11.319  -3.247 -15.788  1.00  7.29           C  
ANISOU 3157  CA  ALA B 669      800    835   1133   -243    239    180       C  
ATOM   3158  C   ALA B 669     -10.334  -2.739 -16.818  1.00  7.01           C  
ANISOU 3158  C   ALA B 669      774    780   1110   -224    285    187       C  
ATOM   3159  O   ALA B 669     -10.031  -3.437 -17.792  1.00  7.17           O  
ANISOU 3159  O   ALA B 669      832    791   1102   -222    310    179       O  
ATOM   3160  CB  ALA B 669     -10.595  -3.623 -14.492  1.00  7.88           C  
ANISOU 3160  CB  ALA B 669      854    891   1249   -240    227    170       C  
ATOM   3161  N   VAL B 670      -9.812  -1.532 -16.605  1.00  7.02           N  
ANISOU 3161  N   VAL B 670      743    771   1154   -211    301    201       N  
ATOM   3162  CA  VAL B 670      -8.714  -1.032 -17.440  1.00  7.35           C  
ANISOU 3162  CA  VAL B 670      783    787   1223   -197    355    214       C  
ATOM   3163  C   VAL B 670      -7.466  -1.888 -17.182  1.00  7.45           C  
ANISOU 3163  C   VAL B 670      779    769   1281   -189    378    195       C  
ATOM   3164  O   VAL B 670      -7.108  -2.174 -16.035  1.00  7.99           O  
ANISOU 3164  O   VAL B 670      816    827   1391   -190    345    181       O  
ATOM   3165  CB  VAL B 670      -8.437   0.459 -17.174  1.00  6.99           C  
ANISOU 3165  CB  VAL B 670      700    726   1228   -191    364    233       C  
ATOM   3166  CG1 VAL B 670      -7.154   0.923 -17.844  1.00  7.89           C  
ANISOU 3166  CG1 VAL B 670      799    808   1391   -184    425    250       C  
ATOM   3167  CG2 VAL B 670      -9.602   1.294 -17.683  1.00  7.18           C  
ANISOU 3167  CG2 VAL B 670      744    773   1211   -190    348    258       C  
ATOM   3168  N   ARG B 671      -6.796  -2.300 -18.253  1.00  7.49           N  
ANISOU 3168  N   ARG B 671      807    761   1277   -179    434    194       N  
ATOM   3169  CA AARG B 671      -5.623  -3.147 -18.080  0.50  7.92           C  
ANISOU 3169  CA AARG B 671      840    785   1385   -164    460    175       C  
ATOM   3170  CA BARG B 671      -5.603  -3.128 -18.135  0.50  8.22           C  
ANISOU 3170  CA BARG B 671      878    823   1422   -164    463    175       C  
ATOM   3171  C   ARG B 671      -4.497  -2.381 -17.389  1.00  7.85           C  
ANISOU 3171  C   ARG B 671      759    749   1474   -158    468    182       C  
ATOM   3172  O   ARG B 671      -4.235  -1.214 -17.685  1.00  8.57           O  
ANISOU 3172  O   ARG B 671      827    835   1593   -161    496    205       O  
ATOM   3173  CB AARG B 671      -5.145  -3.741 -19.406  0.50  8.83           C  
ANISOU 3173  CB AARG B 671      996    891   1468   -149    530    167       C  
ATOM   3174  CB BARG B 671      -5.116  -3.514 -19.531  0.50  9.34           C  
ANISOU 3174  CB BARG B 671     1059    957   1532   -149    538    172       C  
ATOM   3175  CG AARG B 671      -3.940  -4.675 -19.243  0.50  8.75           C  
ANISOU 3175  CG AARG B 671      957    844   1524   -126    562    143       C  
ATOM   3176  CG BARG B 671      -4.142  -4.682 -19.557  0.50 10.37           C  
ANISOU 3176  CG BARG B 671     1181   1056   1704   -128    570    143       C  
ATOM   3177  CD AARG B 671      -3.390  -5.199 -20.567  0.50 10.70           C  
ANISOU 3177  CD AARG B 671     1244   1081   1742   -105    648    129       C  
ATOM   3178  CD BARG B 671      -3.788  -5.098 -20.990  0.50 12.96           C  
ANISOU 3178  CD BARG B 671     1561   1380   1984   -111    653    132       C  
ATOM   3179  NE AARG B 671      -4.421  -5.846 -21.380  0.50 11.38           N  
ANISOU 3179  NE AARG B 671     1418   1187   1718   -114    636    110       N  
ATOM   3180  NE BARG B 671      -4.962  -5.259 -21.857  0.50 14.09           N  
ANISOU 3180  NE BARG B 671     1789   1554   2012   -125    637    128       N  
ATOM   3181  CZ AARG B 671      -4.603  -7.158 -21.481  0.50 12.23           C  
ANISOU 3181  CZ AARG B 671     1567   1276   1802   -108    622     72       C  
ATOM   3182  CZ BARG B 671      -5.548  -6.419 -22.153  0.50 14.62           C  
ANISOU 3182  CZ BARG B 671     1914   1619   2021   -128    611     91       C  
ATOM   3183  NH1AARG B 671      -3.819  -8.001 -20.824  0.50 11.92           N  
ANISOU 3183  NH1AARG B 671     1492   1198   1839    -89    620     52       N  
ATOM   3184  NH1BARG B 671      -5.079  -7.564 -21.660  0.50 15.92           N  
ANISOU 3184  NH1BARG B 671     2069   1747   2231   -116    603     59       N  
ATOM   3185  NH2AARG B 671      -5.578  -7.625 -22.256  0.50 13.05           N  
ANISOU 3185  NH2AARG B 671     1751   1398   1809   -123    603     53       N  
ATOM   3186  NH2BARG B 671      -6.607  -6.430 -22.961  0.50 13.01           N  
ANISOU 3186  NH2BARG B 671     1781   1446   1718   -144    586     88       N  
ATOM   3187  N   ASP B 672      -3.878  -3.058 -16.425  1.00  7.86           N  
ANISOU 3187  N   ASP B 672      726    731   1529   -150    433    165       N  
ATOM   3188  CA  ASP B 672      -2.643  -2.586 -15.774  1.00  8.11           C  
ANISOU 3188  CA  ASP B 672      684    733   1665   -143    430    165       C  
ATOM   3189  C   ASP B 672      -2.787  -1.328 -14.932  1.00  7.85           C  
ANISOU 3189  C   ASP B 672      618    702   1662   -159    386    171       C  
ATOM   3190  O   ASP B 672      -1.862  -0.527 -14.827  1.00  8.45           O  
ANISOU 3190  O   ASP B 672      637    753   1822   -161    400    176       O  
ATOM   3191  CB  ASP B 672      -1.497  -2.490 -16.789  1.00  9.24           C  
ANISOU 3191  CB  ASP B 672      794    851   1864   -128    517    172       C  
ATOM   3192  CG  ASP B 672      -1.056  -3.861 -17.285  1.00  9.81           C  
ANISOU 3192  CG  ASP B 672      885    909   1934   -102    552    152       C  
ATOM   3193  OD1 ASP B 672      -1.391  -4.887 -16.639  1.00 13.18           O  
ANISOU 3193  OD1 ASP B 672     1334   1333   2342    -96    497    135       O  
ATOM   3194  OD2 ASP B 672      -0.392  -3.922 -18.331  1.00 14.11           O  
ANISOU 3194  OD2 ASP B 672     1425   1442   2493    -86    640    154       O  
ATOM   3195  N   GLY B 673      -3.950  -1.210 -14.302  1.00  7.60           N  
ANISOU 3195  N   GLY B 673      622    699   1568   -171    335    167       N  
ATOM   3196  CA  GLY B 673      -4.164  -0.233 -13.256  1.00  7.51           C  
ANISOU 3196  CA  GLY B 673      590    689   1576   -181    284    160       C  
ATOM   3197  C   GLY B 673      -4.462  -0.922 -11.938  1.00  7.24           C  
ANISOU 3197  C   GLY B 673      567    668   1517   -181    215    142       C  
ATOM   3198  O   GLY B 673      -4.442  -2.167 -11.824  1.00  8.51           O  
ANISOU 3198  O   GLY B 673      748    830   1656   -175    204    141       O  
ATOM   3199  N   SER B 674      -4.732  -0.097 -10.934  1.00  6.61           N  
ANISOU 3199  N   SER B 674      481    593   1438   -188    170    128       N  
ATOM   3200  CA  SER B 674      -4.964  -0.596  -9.584  1.00  6.69           C  
ANISOU 3200  CA  SER B 674      509    618   1415   -188    107    113       C  
ATOM   3201  C   SER B 674      -6.284  -1.361  -9.441  1.00  6.55           C  
ANISOU 3201  C   SER B 674      543    637   1307   -195    108    122       C  
ATOM   3202  O   SER B 674      -6.391  -2.226  -8.580  1.00  7.05           O  
ANISOU 3202  O   SER B 674      630    710   1340   -196     72    122       O  
ATOM   3203  CB  SER B 674      -4.873   0.548  -8.565  1.00  6.71           C  
ANISOU 3203  CB  SER B 674      498    615   1436   -192     63     88       C  
ATOM   3204  OG  SER B 674      -5.875   1.521  -8.825  1.00  7.10           O  
ANISOU 3204  OG  SER B 674      562    679   1455   -196     88     86       O  
ATOM   3205  N   THR B 675      -7.281  -1.051 -10.267  1.00  6.50           N  
ANISOU 3205  N   THR B 675      554    652   1264   -201    145    132       N  
ATOM   3206  CA  THR B 675      -8.528  -1.806 -10.204  1.00  6.43           C  
ANISOU 3206  CA  THR B 675      581    676   1185   -213    145    140       C  
ATOM   3207  C   THR B 675      -8.292  -3.239 -10.675  1.00  6.59           C  
ANISOU 3207  C   THR B 675      622    685   1196   -216    152    149       C  
ATOM   3208  O   THR B 675      -8.703  -4.191 -10.002  1.00  7.45           O  
ANISOU 3208  O   THR B 675      756    801   1273   -226    128    155       O  
ATOM   3209  CB  THR B 675      -9.646  -1.088 -10.982  1.00  5.76           C  
ANISOU 3209  CB  THR B 675      501    616   1073   -217    172    148       C  
ATOM   3210  OG1 THR B 675      -9.885   0.176 -10.367  1.00  6.36           O  
ANISOU 3210  OG1 THR B 675      560    695   1162   -209    163    136       O  
ATOM   3211  CG2 THR B 675     -10.953  -1.888 -10.950  1.00  5.92           C  
ANISOU 3211  CG2 THR B 675      545    670   1035   -233    168    157       C  
ATOM   3212  N   MET B 676      -7.587  -3.393 -11.799  1.00  6.91           N  
ANISOU 3212  N   MET B 676      655    702   1268   -207    187    151       N  
ATOM   3213  CA  MET B 676      -7.224  -4.736 -12.262  1.00  6.89           C  
ANISOU 3213  CA  MET B 676      674    678   1265   -203    197    151       C  
ATOM   3214  C   MET B 676      -6.439  -5.470 -11.172  1.00  7.24           C  
ANISOU 3214  C   MET B 676      709    698   1343   -193    155    150       C  
ATOM   3215  O   MET B 676      -6.706  -6.625 -10.859  1.00  7.96           O  
ANISOU 3215  O   MET B 676      830    780   1413   -199    137    156       O  
ATOM   3216  CB  MET B 676      -6.406  -4.658 -13.552  1.00  7.95           C  
ANISOU 3216  CB  MET B 676      800    791   1431   -188    251    148       C  
ATOM   3217  CG  MET B 676      -6.079  -6.029 -14.104  1.00  9.01           C  
ANISOU 3217  CG  MET B 676      962    899   1563   -179    268    138       C  
ATOM   3218  SD  MET B 676      -4.629  -6.061 -15.165  1.00  9.20           S  
ANISOU 3218  SD  MET B 676      959    888   1649   -148    338    129       S  
ATOM   3219  CE  MET B 676      -3.307  -5.987 -13.959  1.00 11.58           C  
ANISOU 3219  CE  MET B 676     1190   1158   2052   -129    301    131       C  
ATOM   3220  N   THR B 677      -5.459  -4.788 -10.589  1.00  7.31           N  
ANISOU 3220  N   THR B 677      676    694   1409   -180    135    145       N  
ATOM   3221  CA  THR B 677      -4.615  -5.432  -9.588  1.00  7.84           C  
ANISOU 3221  CA  THR B 677      730    736   1511   -166     84    147       C  
ATOM   3222  C   THR B 677      -5.393  -5.795  -8.318  1.00  7.51           C  
ANISOU 3222  C   THR B 677      730    718   1407   -179     33    157       C  
ATOM   3223  O   THR B 677      -5.122  -6.830  -7.695  1.00  7.85           O  
ANISOU 3223  O   THR B 677      792    742   1448   -172     -4    171       O  
ATOM   3224  CB  THR B 677      -3.417  -4.542  -9.274  1.00  7.83           C  
ANISOU 3224  CB  THR B 677      670    716   1590   -153     64    136       C  
ATOM   3225  OG1 THR B 677      -2.664  -4.360 -10.480  1.00  9.03           O  
ANISOU 3225  OG1 THR B 677      783    845   1803   -141    126    134       O  
ATOM   3226  CG2 THR B 677      -2.524  -5.159  -8.213  1.00  8.66           C  
ANISOU 3226  CG2 THR B 677      758    798   1734   -136     -5    139       C  
ATOM   3227  N   PHE B 678      -6.372  -4.972  -7.948  1.00  7.57           N  
ANISOU 3227  N   PHE B 678      751    762   1362   -196     34    152       N  
ATOM   3228  CA  PHE B 678      -7.233  -5.310  -6.812  1.00  7.41           C  
ANISOU 3228  CA  PHE B 678      772    770   1273   -210      6    163       C  
ATOM   3229  C   PHE B 678      -7.851  -6.691  -7.011  1.00  7.41           C  
ANISOU 3229  C   PHE B 678      810    765   1242   -225     17    187       C  
ATOM   3230  O   PHE B 678      -7.861  -7.522  -6.095  1.00  7.89           O  
ANISOU 3230  O   PHE B 678      902    818   1276   -228    -16    208       O  
ATOM   3231  CB  PHE B 678      -8.342  -4.274  -6.651  1.00  7.43           C  
ANISOU 3231  CB  PHE B 678      779    814   1231   -223     27    151       C  
ATOM   3232  CG  PHE B 678      -9.388  -4.660  -5.643  1.00  7.26           C  
ANISOU 3232  CG  PHE B 678      796    826   1137   -239     21    164       C  
ATOM   3233  CD1 PHE B 678      -9.254  -4.295  -4.313  1.00  8.26           C  
ANISOU 3233  CD1 PHE B 678      943    967   1227   -233    -14    155       C  
ATOM   3234  CD2 PHE B 678     -10.519  -5.374  -6.034  1.00  7.00           C  
ANISOU 3234  CD2 PHE B 678      779    810   1069   -262     53    184       C  
ATOM   3235  CE1 PHE B 678     -10.219  -4.645  -3.384  1.00  9.06           C  
ANISOU 3235  CE1 PHE B 678     1086   1103   1255   -247     -5    170       C  
ATOM   3236  CE2 PHE B 678     -11.476  -5.750  -5.102  1.00  8.01           C  
ANISOU 3236  CE2 PHE B 678      936    968   1138   -281     59    201       C  
ATOM   3237  CZ  PHE B 678     -11.333  -5.382  -3.789  1.00  7.62           C  
ANISOU 3237  CZ  PHE B 678      912    937   1048   -272     37    196       C  
ATOM   3238  N   PHE B 679      -8.363  -6.935  -8.212  1.00  7.64           N  
ANISOU 3238  N   PHE B 679      839    792   1271   -235     59    185       N  
ATOM   3239  CA  PHE B 679      -8.985  -8.226  -8.476  1.00  8.27           C  
ANISOU 3239  CA  PHE B 679      954    859   1328   -255     66    201       C  
ATOM   3240  C   PHE B 679      -7.956  -9.339  -8.532  1.00  9.04           C  
ANISOU 3240  C   PHE B 679     1061    903   1470   -236     48    207       C  
ATOM   3241  O   PHE B 679      -8.182 -10.413  -7.972  1.00  9.49           O  
ANISOU 3241  O   PHE B 679     1152    939   1513   -246     27    230       O  
ATOM   3242  CB  PHE B 679      -9.881  -8.156  -9.721  1.00  8.26           C  
ANISOU 3242  CB  PHE B 679      956    873   1309   -273    103    191       C  
ATOM   3243  CG  PHE B 679     -11.163  -7.437  -9.451  1.00  7.17           C  
ANISOU 3243  CG  PHE B 679      811    785   1130   -295    111    195       C  
ATOM   3244  CD1 PHE B 679     -12.216  -8.093  -8.805  1.00  7.02           C  
ANISOU 3244  CD1 PHE B 679      810    782   1075   -326    106    214       C  
ATOM   3245  CD2 PHE B 679     -11.290  -6.083  -9.739  1.00  6.77           C  
ANISOU 3245  CD2 PHE B 679      732    760   1082   -283    125    182       C  
ATOM   3246  CE1 PHE B 679     -13.388  -7.416  -8.495  1.00  7.74           C  
ANISOU 3246  CE1 PHE B 679      883    920   1136   -342    121    218       C  
ATOM   3247  CE2 PHE B 679     -12.458  -5.398  -9.438  1.00  7.86           C  
ANISOU 3247  CE2 PHE B 679      858    939   1191   -294    133    184       C  
ATOM   3248  CZ  PHE B 679     -13.518  -6.065  -8.806  1.00  8.29           C  
ANISOU 3248  CZ  PHE B 679      923   1015   1212   -323    133    200       C  
ATOM   3249  N   LYS B 680      -6.818  -9.056  -9.160  1.00  8.89           N  
ANISOU 3249  N   LYS B 680     1008    858   1510   -206     60    189       N  
ATOM   3250  CA  LYS B 680      -5.762 -10.055  -9.323  1.00 10.05           C  
ANISOU 3250  CA  LYS B 680     1152    951   1715   -178     52    190       C  
ATOM   3251  C   LYS B 680      -5.256 -10.553  -7.971  1.00 10.35           C  
ANISOU 3251  C   LYS B 680     1197    971   1764   -165    -12    215       C  
ATOM   3252  O   LYS B 680      -4.910 -11.730  -7.830  1.00 11.60           O  
ANISOU 3252  O   LYS B 680     1376   1083   1947   -152    -31    231       O  
ATOM   3253  CB  LYS B 680      -4.615  -9.464 -10.150  1.00 10.31           C  
ANISOU 3253  CB  LYS B 680     1134    968   1817   -148     85    167       C  
ATOM   3254  CG  LYS B 680      -3.515 -10.464 -10.487  1.00 11.55           C  
ANISOU 3254  CG  LYS B 680     1277   1068   2045   -112     92    162       C  
ATOM   3255  CD  LYS B 680      -2.647  -9.939 -11.632  1.00 14.98           C  
ANISOU 3255  CD  LYS B 680     1666   1492   2534    -88    156    139       C  
ATOM   3256  CE  LYS B 680      -1.603 -10.966 -12.068  1.00 16.83           C  
ANISOU 3256  CE  LYS B 680     1882   1669   2842    -47    179    127       C  
ATOM   3257  NZ  LYS B 680      -0.735 -10.432 -13.160  1.00 20.39           N  
ANISOU 3257  NZ  LYS B 680     2287   2114   3347    -24    256    107       N  
ATOM   3258  N   LYS B 681      -5.230  -9.661  -6.983  1.00 11.08           N  
ANISOU 3258  N   LYS B 681     1279   1097   1835   -168    -49    219       N  
ATOM   3259  CA  LYS B 681      -4.660  -9.963  -5.666  1.00 11.95           C  
ANISOU 3259  CA  LYS B 681     1400   1196   1946   -154   -121    242       C  
ATOM   3260  C   LYS B 681      -5.692 -10.394  -4.620  1.00 12.12           C  
ANISOU 3260  C   LYS B 681     1484   1242   1878   -181   -141    275       C  
ATOM   3261  O   LYS B 681      -5.323 -10.861  -3.540  1.00 13.48           O  
ANISOU 3261  O   LYS B 681     1685   1404   2034   -170   -200    303       O  
ATOM   3262  CB  LYS B 681      -3.860  -8.757  -5.145  1.00 12.87           C  
ANISOU 3262  CB  LYS B 681     1470   1328   2091   -139   -158    221       C  
ATOM   3263  CG  LYS B 681      -2.625  -8.428  -5.977  1.00 16.71           C  
ANISOU 3263  CG  LYS B 681     1884   1782   2682   -112   -144    199       C  
ATOM   3264  CD  LYS B 681      -1.416  -9.259  -5.573  1.00 22.62           C  
ANISOU 3264  CD  LYS B 681     2606   2483   3505    -76   -200    214       C  
ATOM   3265  CE  LYS B 681      -0.190  -8.911  -6.413  1.00 26.35           C  
ANISOU 3265  CE  LYS B 681     2993   2926   4092    -50   -172    193       C  
ATOM   3266  NZ  LYS B 681       0.200  -7.478  -6.280  1.00 28.79           N  
ANISOU 3266  NZ  LYS B 681     3250   3256   4432    -61   -182    169       N  
ATOM   3267  N   SER B 682      -6.975 -10.256  -4.934  1.00 11.13           N  
ANISOU 3267  N   SER B 682     1380   1151   1698   -215    -93    274       N  
ATOM   3268  CA  SER B 682      -8.022 -10.467  -3.934  1.00 11.06           C  
ANISOU 3268  CA  SER B 682     1420   1175   1608   -244    -95    303       C  
ATOM   3269  C   SER B 682      -8.073 -11.895  -3.416  1.00 12.19           C  
ANISOU 3269  C   SER B 682     1612   1278   1740   -252   -118    351       C  
ATOM   3270  O   SER B 682      -7.868 -12.842  -4.172  1.00 13.01           O  
ANISOU 3270  O   SER B 682     1718   1333   1893   -250   -109    356       O  
ATOM   3271  CB  SER B 682      -9.404 -10.066  -4.472  1.00 10.58           C  
ANISOU 3271  CB  SER B 682     1356   1155   1510   -279    -37    293       C  
ATOM   3272  OG  SER B 682     -10.359 -10.130  -3.417  1.00 11.00           O  
ANISOU 3272  OG  SER B 682     1445   1245   1491   -304    -29    320       O  
ATOM   3273  N   LYS B 683      -8.346 -12.023  -2.121  1.00 12.64           N  
ANISOU 3273  N   LYS B 683     1715   1356   1730   -260   -146    387       N  
ATOM   3274  CA  LYS B 683      -8.606 -13.319  -1.494  1.00 14.41           C  
ANISOU 3274  CA  LYS B 683     1999   1548   1930   -276   -161    446       C  
ATOM   3275  C   LYS B 683     -10.071 -13.445  -1.080  1.00 14.19           C  
ANISOU 3275  C   LYS B 683     2003   1559   1829   -325   -108    473       C  
ATOM   3276  O   LYS B 683     -10.432 -14.360  -0.335  1.00 15.22           O  
ANISOU 3276  O   LYS B 683     2188   1673   1922   -346   -112    531       O  
ATOM   3277  CB  LYS B 683      -7.677 -13.538  -0.298  1.00 15.74           C  
ANISOU 3277  CB  LYS B 683     2203   1702   2077   -245   -239    479       C  
ATOM   3278  CG  LYS B 683      -6.225 -13.747  -0.694  1.00 18.04           C  
ANISOU 3278  CG  LYS B 683     2453   1939   2461   -196   -295    464       C  
ATOM   3279  CD  LYS B 683      -5.294 -13.585   0.493  1.00 22.94           C  
ANISOU 3279  CD  LYS B 683     3094   2562   3061   -163   -386    484       C  
ATOM   3280  CE  LYS B 683      -3.830 -13.513   0.045  1.00 25.68           C  
ANISOU 3280  CE  LYS B 683     3374   2866   3519   -115   -440    459       C  
ATOM   3281  NZ  LYS B 683      -3.260 -14.864  -0.258  1.00 28.05           N  
ANISOU 3281  NZ  LYS B 683     3678   3088   3892    -88   -461    495       N  
ATOM   3282  N   ILE B 684     -10.906 -12.518  -1.548  1.00 12.77           N  
ANISOU 3282  N   ILE B 684     1787   1430   1635   -343    -57    437       N  
ATOM   3283  CA  ILE B 684     -12.355 -12.562  -1.316  1.00 12.78           C  
ANISOU 3283  CA  ILE B 684     1797   1471   1587   -389      2    456       C  
ATOM   3284  C   ILE B 684     -12.969 -13.368  -2.453  1.00 12.39           C  
ANISOU 3284  C   ILE B 684     1728   1388   1592   -423     30    457       C  
ATOM   3285  O   ILE B 684     -12.722 -13.059  -3.619  1.00 11.68           O  
ANISOU 3285  O   ILE B 684     1599   1287   1553   -411     32    414       O  
ATOM   3286  CB  ILE B 684     -12.954 -11.144  -1.256  1.00 12.78           C  
ANISOU 3286  CB  ILE B 684     1761   1538   1555   -385     37    414       C  
ATOM   3287  CG1 ILE B 684     -12.433 -10.410  -0.016  1.00 14.54           C  
ANISOU 3287  CG1 ILE B 684     2017   1792   1714   -356      7    408       C  
ATOM   3288  CG2 ILE B 684     -14.490 -11.197  -1.275  0.50 11.24           C  
ANISOU 3288  CG2 ILE B 684     1552   1382   1336   -430    104    429       C  
ATOM   3289  CD1 ILE B 684     -12.823  -8.948   0.058  0.50 13.53           C  
ANISOU 3289  CD1 ILE B 684     1859   1717   1565   -343     34    357       C  
ATOM   3290  N   SER B 685     -13.762 -14.386  -2.112  1.00 12.80           N  
ANISOU 3290  N   SER B 685     1811   1422   1631   -468     51    506       N  
ATOM   3291  CA ASER B 685     -14.264 -15.353  -3.095  0.50 12.55           C  
ANISOU 3291  CA ASER B 685     1771   1343   1656   -505     63    508       C  
ATOM   3292  CA BSER B 685     -14.246 -15.357  -3.100  0.50 12.75           C  
ANISOU 3292  CA BSER B 685     1796   1367   1681   -504     62    507       C  
ATOM   3293  C   SER B 685     -14.906 -14.728  -4.328  1.00 12.04           C  
ANISOU 3293  C   SER B 685     1650   1306   1620   -518     88    455       C  
ATOM   3294  O   SER B 685     -14.542 -15.064  -5.457  1.00 11.30           O  
ANISOU 3294  O   SER B 685     1548   1172   1574   -511     73    422       O  
ATOM   3295  CB ASER B 685     -15.242 -16.325  -2.441  0.50 13.60           C  
ANISOU 3295  CB ASER B 685     1935   1462   1771   -562     91    570       C  
ATOM   3296  CB BSER B 685     -15.180 -16.388  -2.460  0.50 13.86           C  
ANISOU 3296  CB BSER B 685     1971   1490   1807   -561     88    571       C  
ATOM   3297  OG ASER B 685     -14.614 -17.000  -1.371  0.50 13.89           O  
ANISOU 3297  OG ASER B 685     2035   1464   1777   -550     63    627       O  
ATOM   3298  OG BSER B 685     -16.404 -15.799  -2.066  0.50 14.91           O  
ANISOU 3298  OG BSER B 685     2075   1690   1900   -596    144    579       O  
ATOM   3299  N   THR B 686     -15.861 -13.813  -4.121  1.00 11.40           N  
ANISOU 3299  N   THR B 686     1532   1293   1507   -532    125    447       N  
ATOM   3300  CA  THR B 686     -16.538 -13.162  -5.261  1.00 11.83           C  
ANISOU 3300  CA  THR B 686     1532   1376   1588   -541    140    404       C  
ATOM   3301  C   THR B 686     -15.521 -12.485  -6.183  1.00 10.72           C  
ANISOU 3301  C   THR B 686     1379   1226   1470   -493    115    356       C  
ATOM   3302  O   THR B 686     -15.596 -12.604  -7.403  1.00 10.78           O  
ANISOU 3302  O   THR B 686     1373   1216   1508   -497    109    326       O  
ATOM   3303  CB  THR B 686     -17.628 -12.155  -4.807  1.00 12.38           C  
ANISOU 3303  CB  THR B 686     1558   1519   1627   -551    183    402       C  
ATOM   3304  OG1 THR B 686     -18.691 -12.867  -4.163  1.00 14.97           O  
ANISOU 3304  OG1 THR B 686     1886   1856   1947   -604    218    448       O  
ATOM   3305  CG2 THR B 686     -18.204 -11.353  -5.986  1.00 12.97           C  
ANISOU 3305  CG2 THR B 686     1575   1621   1731   -548    185    361       C  
ATOM   3306  N   TYR B 687     -14.545 -11.808  -5.589  1.00  9.56           N  
ANISOU 3306  N   TYR B 687     1239   1086   1307   -448    101    348       N  
ATOM   3307  CA  TYR B 687     -13.554 -11.069  -6.369  1.00  8.73           C  
ANISOU 3307  CA  TYR B 687     1114    973   1231   -406     86    308       C  
ATOM   3308  C   TYR B 687     -12.524 -11.988  -7.048  1.00  8.65           C  
ANISOU 3308  C   TYR B 687     1123    897   1266   -389     64    301       C  
ATOM   3309  O   TYR B 687     -12.073 -11.682  -8.161  1.00  8.73           O  
ANISOU 3309  O   TYR B 687     1116    896   1305   -370     71    267       O  
ATOM   3310  CB  TYR B 687     -12.912  -9.954  -5.526  1.00  9.23           C  
ANISOU 3310  CB  TYR B 687     1169   1064   1274   -370     75    297       C  
ATOM   3311  CG  TYR B 687     -13.907  -9.033  -4.826  1.00  9.07           C  
ANISOU 3311  CG  TYR B 687     1134   1103   1208   -379    103    296       C  
ATOM   3312  CD1 TYR B 687     -15.169  -8.764  -5.380  1.00  9.89           C  
ANISOU 3312  CD1 TYR B 687     1206   1240   1313   -405    139    291       C  
ATOM   3313  CD2 TYR B 687     -13.573  -8.416  -3.624  1.00 10.04           C  
ANISOU 3313  CD2 TYR B 687     1276   1250   1290   -359     92    295       C  
ATOM   3314  CE1 TYR B 687     -16.074  -7.931  -4.740  1.00  9.53           C  
ANISOU 3314  CE1 TYR B 687     1139   1246   1236   -406    172    288       C  
ATOM   3315  CE2 TYR B 687     -14.473  -7.574  -2.968  1.00  9.80           C  
ANISOU 3315  CE2 TYR B 687     1237   1271   1216   -362    127    286       C  
ATOM   3316  CZ  TYR B 687     -15.721  -7.333  -3.532  1.00  9.37           C  
ANISOU 3316  CZ  TYR B 687     1143   1246   1172   -383    171    283       C  
ATOM   3317  OH  TYR B 687     -16.615  -6.511  -2.875  1.00 12.12           O  
ANISOU 3317  OH  TYR B 687     1476   1643   1487   -380    212    272       O  
ATOM   3318  N   GLU B 688     -12.165 -13.099  -6.398  1.00  9.50           N  
ANISOU 3318  N   GLU B 688     1270    960   1380   -393     42    334       N  
ATOM   3319  CA AGLU B 688     -11.348 -14.147  -7.027  0.50  9.55           C  
ANISOU 3319  CA AGLU B 688     1297    895   1437   -378     25    328       C  
ATOM   3320  CA BGLU B 688     -11.346 -14.133  -7.040  0.50  9.51           C  
ANISOU 3320  CA BGLU B 688     1291    891   1432   -377     25    328       C  
ATOM   3321  C   GLU B 688     -12.026 -14.694  -8.287  1.00  9.54           C  
ANISOU 3321  C   GLU B 688     1299    873   1452   -407     45    302       C  
ATOM   3322  O   GLU B 688     -11.370 -14.913  -9.310  1.00  9.87           O  
ANISOU 3322  O   GLU B 688     1343    880   1528   -383     50    266       O  
ATOM   3323  CB AGLU B 688     -11.062 -15.313  -6.059  0.50 10.51           C  
ANISOU 3323  CB AGLU B 688     1463    966   1563   -381     -4    378       C  
ATOM   3324  CB BGLU B 688     -11.039 -15.285  -6.080  0.50 10.50           C  
ANISOU 3324  CB BGLU B 688     1462    966   1563   -380     -4    376       C  
ATOM   3325  CG AGLU B 688     -10.142 -14.976  -4.894  0.50 12.42           C  
ANISOU 3325  CG AGLU B 688     1713   1215   1791   -344    -43    402       C  
ATOM   3326  CG BGLU B 688     -10.147 -14.916  -4.921  0.50 12.30           C  
ANISOU 3326  CG BGLU B 688     1696   1203   1776   -343    -42    400       C  
ATOM   3327  CD AGLU B 688      -9.700 -16.206  -4.100  0.50 14.13           C  
ANISOU 3327  CD AGLU B 688     1979   1371   2019   -338    -82    455       C  
ATOM   3328  CD BGLU B 688      -9.837 -16.107  -4.045  0.50 13.95           C  
ANISOU 3328  CD BGLU B 688     1956   1357   1987   -342    -78    456       C  
ATOM   3329  OE1AGLU B 688      -9.490 -17.282  -4.704  0.50 15.34           O  
ANISOU 3329  OE1AGLU B 688     2149   1453   2225   -337    -85    457       O  
ATOM   3330  OE1BGLU B 688     -10.730 -16.965  -3.874  0.50 14.25           O  
ANISOU 3330  OE1BGLU B 688     2029   1375   2011   -387    -62    492       O  
ATOM   3331  OE2AGLU B 688      -9.546 -16.092  -2.864  0.50 15.86           O  
ANISOU 3331  OE2AGLU B 688     2226   1609   2192   -331   -113    496       O  
ATOM   3332  OE2BGLU B 688      -8.701 -16.188  -3.528  0.50 16.74           O  
ANISOU 3332  OE2BGLU B 688     2313   1684   2363   -298   -127    468       O  
ATOM   3333  N   LYS B 689     -13.332 -14.934  -8.202  1.00  9.34           N  
ANISOU 3333  N   LYS B 689     1275    869   1405   -460     57    318       N  
ATOM   3334  CA  LYS B 689     -14.083 -15.423  -9.348  1.00  9.08           C  
ANISOU 3334  CA  LYS B 689     1245    820   1386   -495     62    290       C  
ATOM   3335  C   LYS B 689     -14.067 -14.370 -10.450  1.00  9.30           C  
ANISOU 3335  C   LYS B 689     1242    889   1402   -474     74    245       C  
ATOM   3336  O   LYS B 689     -13.817 -14.686 -11.608  1.00  9.46           O  
ANISOU 3336  O   LYS B 689     1280    881   1435   -467     73    208       O  
ATOM   3337  CB  LYS B 689     -15.516 -15.755  -8.938  1.00  9.70           C  
ANISOU 3337  CB  LYS B 689     1313    920   1453   -559     70    320       C  
ATOM   3338  CG  LYS B 689     -16.389 -16.158 -10.127  1.00  9.17           C  
ANISOU 3338  CG  LYS B 689     1240    842   1402   -601     62    288       C  
ATOM   3339  CD  LYS B 689     -17.774 -16.519  -9.668  1.00  8.52           C  
ANISOU 3339  CD  LYS B 689     1133    777   1326   -667     69    321       C  
ATOM   3340  CE  LYS B 689     -18.644 -16.922 -10.847  1.00  9.05           C  
ANISOU 3340  CE  LYS B 689     1189    832   1416   -712     44    285       C  
ATOM   3341  NZ  LYS B 689     -20.062 -17.235 -10.431  1.00  9.65           N  
ANISOU 3341  NZ  LYS B 689     1223    927   1515   -783     51    317       N  
ATOM   3342  N   MET B 690     -14.326 -13.126 -10.074  1.00  8.47           N  
ANISOU 3342  N   MET B 690     1100    847   1272   -462     86    250       N  
ATOM   3343  CA  MET B 690     -14.294 -12.031 -11.029  1.00  7.91           C  
ANISOU 3343  CA  MET B 690     1003    812   1192   -440     97    219       C  
ATOM   3344  C   MET B 690     -12.945 -11.906 -11.717  1.00  7.80           C  
ANISOU 3344  C   MET B 690     1000    766   1198   -394    104    192       C  
ATOM   3345  O   MET B 690     -12.896 -11.698 -12.936  1.00  7.76           O  
ANISOU 3345  O   MET B 690     1002    761   1187   -386    115    163       O  
ATOM   3346  CB  MET B 690     -14.691 -10.718 -10.357  1.00  7.54           C  
ANISOU 3346  CB  MET B 690      916    825   1125   -429    109    229       C  
ATOM   3347  CG  MET B 690     -16.167 -10.715  -9.977  1.00  8.38           C  
ANISOU 3347  CG  MET B 690      998    970   1217   -472    115    248       C  
ATOM   3348  SD  MET B 690     -16.704  -9.254  -9.063  1.00  9.34           S  
ANISOU 3348  SD  MET B 690     1076   1156   1317   -454    138    255       S  
ATOM   3349  CE  MET B 690     -16.614  -7.986 -10.330  1.00  8.77           C  
ANISOU 3349  CE  MET B 690      976   1104   1253   -422    136    225       C  
ATOM   3350  N   TRP B 691     -11.854 -12.027 -10.958  1.00  7.53           N  
ANISOU 3350  N   TRP B 691      967    705   1188   -363     98    204       N  
ATOM   3351  CA  TRP B 691     -10.525 -12.036 -11.574  1.00  7.77           C  
ANISOU 3351  CA  TRP B 691      997    700   1254   -319    110    181       C  
ATOM   3352  C   TRP B 691     -10.350 -13.203 -12.540  1.00  7.87           C  
ANISOU 3352  C   TRP B 691     1049    659   1283   -321    118    156       C  
ATOM   3353  O   TRP B 691      -9.845 -13.006 -13.647  1.00  7.84           O  
ANISOU 3353  O   TRP B 691     1049    647   1282   -298    147    124       O  
ATOM   3354  CB  TRP B 691      -9.402 -12.046 -10.545  1.00  7.86           C  
ANISOU 3354  CB  TRP B 691      995    690   1301   -287     90    198       C  
ATOM   3355  CG  TRP B 691      -8.080 -12.107 -11.235  1.00  8.26           C  
ANISOU 3355  CG  TRP B 691     1032    703   1405   -243    108    175       C  
ATOM   3356  CD1 TRP B 691      -7.155 -13.093 -11.133  1.00  9.19           C  
ANISOU 3356  CD1 TRP B 691     1158    761   1573   -215     98    175       C  
ATOM   3357  CD2 TRP B 691      -7.578 -11.178 -12.202  1.00  8.95           C  
ANISOU 3357  CD2 TRP B 691     1091    807   1503   -222    147    150       C  
ATOM   3358  NE1 TRP B 691      -6.079 -12.824 -11.953  1.00 10.32           N  
ANISOU 3358  NE1 TRP B 691     1272    886   1763   -176    134    148       N  
ATOM   3359  CE2 TRP B 691      -6.317 -11.654 -12.618  1.00 10.09           C  
ANISOU 3359  CE2 TRP B 691     1222    903   1707   -183    167    134       C  
ATOM   3360  CE3 TRP B 691      -8.067  -9.985 -12.747  1.00  7.36           C  
ANISOU 3360  CE3 TRP B 691      873    652   1271   -231    170    144       C  
ATOM   3361  CZ2 TRP B 691      -5.532 -10.973 -13.554  1.00 10.56           C  
ANISOU 3361  CZ2 TRP B 691     1254    965   1793   -157    217    114       C  
ATOM   3362  CZ3 TRP B 691      -7.295  -9.315 -13.684  1.00  8.50           C  
ANISOU 3362  CZ3 TRP B 691      997    795   1438   -206    213    128       C  
ATOM   3363  CH2 TRP B 691      -6.039  -9.810 -14.073  1.00  8.69           C  
ANISOU 3363  CH2 TRP B 691     1008    775   1518   -172    241    114       C  
ATOM   3364  N   ALA B 692     -10.774 -14.404 -12.146  1.00  8.36           N  
ANISOU 3364  N   ALA B 692     1143    680   1352   -348     97    169       N  
ATOM   3365  CA  ALA B 692     -10.659 -15.552 -13.048  1.00  8.66           C  
ANISOU 3365  CA  ALA B 692     1224    657   1408   -351    101    138       C  
ATOM   3366  C   ALA B 692     -11.442 -15.299 -14.341  1.00  8.80           C  
ANISOU 3366  C   ALA B 692     1257    701   1386   -374    112    100       C  
ATOM   3367  O   ALA B 692     -10.984 -15.650 -15.433  1.00  8.96           O  
ANISOU 3367  O   ALA B 692     1308    691   1404   -354    133     57       O  
ATOM   3368  CB  ALA B 692     -11.136 -16.822 -12.362  1.00  9.22           C  
ANISOU 3368  CB  ALA B 692     1328    676   1498   -385     73    165       C  
ATOM   3369  N   PHE B 693     -12.605 -14.671 -14.207  1.00  8.47           N  
ANISOU 3369  N   PHE B 693     1193    716   1308   -412     99    116       N  
ATOM   3370  CA  PHE B 693     -13.426 -14.311 -15.362  1.00  8.96           C  
ANISOU 3370  CA  PHE B 693     1264    811   1331   -433     94     87       C  
ATOM   3371  C   PHE B 693     -12.700 -13.322 -16.276  1.00  9.07           C  
ANISOU 3371  C   PHE B 693     1275    851   1322   -389    127     66       C  
ATOM   3372  O   PHE B 693     -12.552 -13.561 -17.476  1.00  9.17           O  
ANISOU 3372  O   PHE B 693     1328    849   1306   -381    138     28       O  
ATOM   3373  CB  PHE B 693     -14.769 -13.715 -14.914  1.00  8.90           C  
ANISOU 3373  CB  PHE B 693     1215    861   1304   -475     73    114       C  
ATOM   3374  CG  PHE B 693     -15.639 -13.282 -16.062  1.00  9.72           C  
ANISOU 3374  CG  PHE B 693     1320   1001   1372   -493     55     91       C  
ATOM   3375  CD1 PHE B 693     -16.561 -14.165 -16.617  1.00 11.38           C  
ANISOU 3375  CD1 PHE B 693     1553   1192   1580   -542     17     70       C  
ATOM   3376  CD2 PHE B 693     -15.510 -12.000 -16.611  1.00 11.80           C  
ANISOU 3376  CD2 PHE B 693     1566   1312   1606   -461     69     90       C  
ATOM   3377  CE1 PHE B 693     -17.366 -13.772 -17.690  1.00 13.36           C  
ANISOU 3377  CE1 PHE B 693     1806   1478   1794   -558    -15     48       C  
ATOM   3378  CE2 PHE B 693     -16.301 -11.610 -17.685  1.00 12.96           C  
ANISOU 3378  CE2 PHE B 693     1719   1491   1715   -474     43     75       C  
ATOM   3379  CZ  PHE B 693     -17.228 -12.491 -18.217  1.00 13.14           C  
ANISOU 3379  CZ  PHE B 693     1763   1501   1730   -521     -3     53       C  
ATOM   3380  N   MET B 694     -12.250 -12.215 -15.703  1.00  8.61           N  
ANISOU 3380  N   MET B 694     1173    827   1272   -363    144     91       N  
ATOM   3381  CA  MET B 694     -11.524 -11.215 -16.492  1.00  9.45           C  
ANISOU 3381  CA  MET B 694     1272    953   1367   -325    181     80       C  
ATOM   3382  C   MET B 694     -10.304 -11.804 -17.171  1.00 10.38           C  
ANISOU 3382  C   MET B 694     1417   1022   1504   -289    220     51       C  
ATOM   3383  O   MET B 694     -10.041 -11.500 -18.338  1.00 10.84           O  
ANISOU 3383  O   MET B 694     1501   1087   1530   -273    254     29       O  
ATOM   3384  CB  MET B 694     -11.072 -10.063 -15.613  1.00  9.32           C  
ANISOU 3384  CB  MET B 694     1202    963   1375   -304    189    108       C  
ATOM   3385  CG  MET B 694     -12.175  -9.237 -15.033  1.00  9.69           C  
ANISOU 3385  CG  MET B 694     1218   1060   1402   -327    166    131       C  
ATOM   3386  SD  MET B 694     -11.463  -7.920 -14.008  1.00 10.07           S  
ANISOU 3386  SD  MET B 694     1218   1127   1482   -298    176    150       S  
ATOM   3387  CE  MET B 694     -12.883  -7.560 -12.977  1.00 11.76           C  
ANISOU 3387  CE  MET B 694     1409   1387   1674   -328    150    170       C  
ATOM   3388  N   SER B 695      -9.559 -12.629 -16.437  1.00 10.81           N  
ANISOU 3388  N   SER B 695     1467   1028   1611   -274    217     53       N  
ATOM   3389  CA ASER B 695      -8.331 -13.224 -16.955  0.50 12.08           C  
ANISOU 3389  CA ASER B 695     1642   1137   1809   -231    257     26       C  
ATOM   3390  CA BSER B 695      -8.338 -13.248 -16.951  0.50 12.03           C  
ANISOU 3390  CA BSER B 695     1637   1130   1803   -232    256     25       C  
ATOM   3391  C   SER B 695      -8.627 -14.147 -18.137  1.00 12.94           C  
ANISOU 3391  C   SER B 695     1819   1215   1882   -238    270    -22       C  
ATOM   3392  O   SER B 695      -7.917 -14.123 -19.144  1.00 14.25           O  
ANISOU 3392  O   SER B 695     2007   1370   2037   -205    324    -54       O  
ATOM   3393  CB ASER B 695      -7.581 -13.968 -15.842  0.50 12.31           C  
ANISOU 3393  CB ASER B 695     1651   1118   1908   -212    236     43       C  
ATOM   3394  CB BSER B 695      -7.656 -14.064 -15.857  0.50 12.29           C  
ANISOU 3394  CB BSER B 695     1654   1113   1904   -215    234     42       C  
ATOM   3395  OG ASER B 695      -6.261 -14.310 -16.240  0.50 13.80           O  
ANISOU 3395  OG ASER B 695     1830   1262   2152   -161    278     21       O  
ATOM   3396  OG BSER B 695      -7.197 -13.220 -14.832  0.50 12.68           O  
ANISOU 3396  OG BSER B 695     1647   1188   1982   -202    219     77       O  
ATOM   3397  N   SER B 696      -9.682 -14.945 -18.022  1.00 12.76           N  
ANISOU 3397  N   SER B 696     1830   1179   1839   -283    223    -28       N  
ATOM   3398  CA  SER B 696     -10.039 -15.893 -19.079  1.00 14.12           C  
ANISOU 3398  CA  SER B 696     2072   1314   1979   -297    221    -80       C  
ATOM   3399  C   SER B 696     -10.563 -15.229 -20.360  1.00 14.04           C  
ANISOU 3399  C   SER B 696     2096   1353   1886   -305    231   -107       C  
ATOM   3400  O   SER B 696     -10.619 -15.874 -21.412  1.00 15.15           O  
ANISOU 3400  O   SER B 696     2304   1467   1986   -304    239   -160       O  
ATOM   3401  CB  SER B 696     -11.058 -16.914 -18.562  1.00 14.40           C  
ANISOU 3401  CB  SER B 696     2128   1316   2028   -351    163    -76       C  
ATOM   3402  OG  SER B 696     -12.269 -16.279 -18.233  1.00 16.32           O  
ANISOU 3402  OG  SER B 696     2341   1619   2241   -399    124    -45       O  
ATOM   3403  N   ARG B 697     -10.949 -13.956 -20.248  1.00 13.01           N  
ANISOU 3403  N   ARG B 697     1924   1290   1730   -311    227    -70       N  
ATOM   3404  CA AARG B 697     -11.516 -13.179 -21.351  0.50 12.98           C  
ANISOU 3404  CA AARG B 697     1948   1336   1648   -317    225    -78       C  
ATOM   3405  CA BARG B 697     -11.486 -13.198 -21.381  0.50 13.01           C  
ANISOU 3405  CA BARG B 697     1953   1339   1651   -316    227    -80       C  
ATOM   3406  C   ARG B 697     -10.689 -11.906 -21.564  1.00 12.15           C  
ANISOU 3406  C   ARG B 697     1812   1265   1539   -277    283    -51       C  
ATOM   3407  O   ARG B 697     -11.209 -10.918 -22.064  1.00 10.88           O  
ANISOU 3407  O   ARG B 697     1650   1153   1330   -282    276    -31       O  
ATOM   3408  CB AARG B 697     -12.969 -12.765 -21.035  0.50 13.10           C  
ANISOU 3408  CB AARG B 697     1935   1398   1644   -366    158    -51       C  
ATOM   3409  CB BARG B 697     -12.968 -12.856 -21.161  0.50 13.21           C  
ANISOU 3409  CB BARG B 697     1957   1409   1652   -366    158    -57       C  
ATOM   3410  CG AARG B 697     -14.045 -13.827 -21.242  0.50 14.29           C  
ANISOU 3410  CG AARG B 697     2120   1528   1783   -418     95    -80       C  
ATOM   3411  CG BARG B 697     -13.854 -14.029 -20.785  0.50 14.26           C  
ANISOU 3411  CG BARG B 697     2103   1509   1807   -416    101    -73       C  
ATOM   3412  CD AARG B 697     -14.310 -14.626 -19.979  0.50 14.16           C  
ANISOU 3412  CD AARG B 697     2070   1476   1836   -448     73    -60       C  
ATOM   3413  CD BARG B 697     -15.307 -13.682 -20.973  0.50 14.34           C  
ANISOU 3413  CD BARG B 697     2094   1566   1788   -463     38    -62       C  
ATOM   3414  NE AARG B 697     -15.569 -15.366 -20.048  0.50 16.28           N  
ANISOU 3414  NE AARG B 697     2346   1735   2105   -510     10    -72       N  
ATOM   3415  NE BARG B 697     -16.168 -14.839 -20.756  0.50 16.02           N  
ANISOU 3415  NE BARG B 697     2316   1742   2027   -519    -15    -79       N  
ATOM   3416  CZ AARG B 697     -15.834 -16.456 -19.343  0.50 16.83           C  
ANISOU 3416  CZ AARG B 697     2416   1752   2226   -546    -10    -68       C  
ATOM   3417  CZ BARG B 697     -17.405 -14.954 -21.225  0.50 16.07           C  
ANISOU 3417  CZ BARG B 697     2321   1771   2014   -568    -80    -90       C  
ATOM   3418  NH1AARG B 697     -14.927 -16.951 -18.506  0.50 14.99           N  
ANISOU 3418  NH1AARG B 697     2182   1471   2041   -521     23    -51       N  
ATOM   3419  NH1BARG B 697     -17.933 -13.986 -21.953  0.50 15.06           N  
ANISOU 3419  NH1BARG B 697     2186   1703   1834   -561   -105    -84       N  
ATOM   3420  NH2AARG B 697     -17.012 -17.053 -19.473  0.50 18.92           N  
ANISOU 3420  NH2AARG B 697     2681   2009   2499   -609    -66    -78       N  
ATOM   3421  NH2BARG B 697     -18.113 -16.049 -20.966  0.50 17.38           N  
ANISOU 3421  NH2BARG B 697     2490   1895   2219   -624   -123   -105       N  
ATOM   3422  N   GLN B 698      -9.412 -11.937 -21.170  1.00 11.74           N  
ANISOU 3422  N   GLN B 698     1731   1183   1547   -238    337    -48       N  
ATOM   3423  CA  GLN B 698      -8.562 -10.733 -21.091  1.00 10.82           C  
ANISOU 3423  CA  GLN B 698     1565   1089   1456   -207    387    -16       C  
ATOM   3424  C   GLN B 698      -8.608  -9.830 -22.319  1.00 10.42           C  
ANISOU 3424  C   GLN B 698     1548   1075   1335   -198    427    -11       C  
ATOM   3425  O   GLN B 698      -8.637  -8.597 -22.195  1.00  8.64           O  
ANISOU 3425  O   GLN B 698     1286    884   1114   -196    434     30       O  
ATOM   3426  CB  GLN B 698      -7.114 -11.102 -20.731  1.00 12.76           C  
ANISOU 3426  CB  GLN B 698     1777   1289   1781   -166    439    -23       C  
ATOM   3427  CG  GLN B 698      -6.437 -12.061 -21.699  1.00 15.49           C  
ANISOU 3427  CG  GLN B 698     2177   1593   2117   -136    496    -73       C  
ATOM   3428  CD  GLN B 698      -5.670 -11.343 -22.804  1.00 20.71           C  
ANISOU 3428  CD  GLN B 698     2849   2270   2748   -105    586    -77       C  
ATOM   3429  OE1 GLN B 698      -5.194 -10.216 -22.621  1.00 23.33           O  
ANISOU 3429  OE1 GLN B 698     3126   2628   3110    -98    615    -37       O  
ATOM   3430  NE2 GLN B 698      -5.544 -11.995 -23.960  1.00 21.78           N  
ANISOU 3430  NE2 GLN B 698     3061   2390   2823    -89    633   -125       N  
ATOM   3431  N   GLN B 699      -8.644 -10.447 -23.494  1.00  9.90           N  
ANISOU 3431  N   GLN B 699     1560   1000   1201   -192    451    -52       N  
ATOM   3432  CA  GLN B 699      -8.584  -9.714 -24.762  1.00 10.02           C  
ANISOU 3432  CA  GLN B 699     1626   1048   1134   -179    496    -46       C  
ATOM   3433  C   GLN B 699      -9.685  -8.658 -24.878  1.00  9.99           C  
ANISOU 3433  C   GLN B 699     1617   1098   1081   -204    440     -4       C  
ATOM   3434  O   GLN B 699      -9.485  -7.605 -25.491  1.00  9.76           O  
ANISOU 3434  O   GLN B 699     1596   1096   1017   -190    477     31       O  
ATOM   3435  CB  GLN B 699      -8.639 -10.682 -25.950  1.00 10.69           C  
ANISOU 3435  CB  GLN B 699     1811   1117   1135   -173    514   -107       C  
ATOM   3436  CG  GLN B 699      -9.877 -11.594 -25.991  1.00 11.08           C  
ANISOU 3436  CG  GLN B 699     1905   1159   1144   -215    419   -143       C  
ATOM   3437  CD  GLN B 699      -9.761 -12.851 -25.137  1.00 10.59           C  
ANISOU 3437  CD  GLN B 699     1826   1038   1160   -224    395   -175       C  
ATOM   3438  OE1 GLN B 699      -8.728 -13.113 -24.518  1.00 11.75           O  
ANISOU 3438  OE1 GLN B 699     1929   1147   1387   -193    443   -172       O  
ATOM   3439  NE2 GLN B 699     -10.826 -13.641 -25.117  1.00 10.10           N  
ANISOU 3439  NE2 GLN B 699     1795    964   1078   -267    315   -202       N  
ATOM   3440  N   THR B 700     -10.844  -8.947 -24.287  1.00  9.86           N  
ANISOU 3440  N   THR B 700     1585   1093   1069   -240    352     -4       N  
ATOM   3441  CA  THR B 700     -11.983  -8.031 -24.301  1.00 10.22           C  
ANISOU 3441  CA  THR B 700     1612   1186   1085   -261    292     33       C  
ATOM   3442  C   THR B 700     -12.378  -7.557 -22.906  1.00 10.44           C  
ANISOU 3442  C   THR B 700     1553   1223   1191   -275    258     66       C  
ATOM   3443  O   THR B 700     -12.868  -6.437 -22.757  1.00 12.40           O  
ANISOU 3443  O   THR B 700     1767   1503   1441   -273    241    105       O  
ATOM   3444  CB  THR B 700     -13.211  -8.657 -24.984  1.00 10.34           C  
ANISOU 3444  CB  THR B 700     1681   1217   1030   -294    215      5       C  
ATOM   3445  OG1 THR B 700     -13.459  -9.952 -24.425  1.00 10.73           O  
ANISOU 3445  OG1 THR B 700     1730   1231   1117   -322    182    -34       O  
ATOM   3446  CG2 THR B 700     -12.968  -8.816 -26.478  1.00 10.49           C  
ANISOU 3446  CG2 THR B 700     1799   1241    944   -279    240    -23       C  
ATOM   3447  N   ALA B 701     -12.171  -8.382 -21.888  1.00  9.99           N  
ANISOU 3447  N   ALA B 701     1466   1135   1194   -285    250     52       N  
ATOM   3448  CA  ALA B 701     -12.566  -7.979 -20.538  1.00  9.58           C  
ANISOU 3448  CA  ALA B 701     1344   1095   1202   -298    221     80       C  
ATOM   3449  C   ALA B 701     -11.669  -6.862 -20.009  1.00  9.66           C  
ANISOU 3449  C   ALA B 701     1306   1107   1258   -268    264    109       C  
ATOM   3450  O   ALA B 701     -12.123  -5.964 -19.283  1.00  9.72           O  
ANISOU 3450  O   ALA B 701     1267   1138   1289   -271    244    136       O  
ATOM   3451  CB  ALA B 701     -12.559  -9.163 -19.602  1.00  9.92           C  
ANISOU 3451  CB  ALA B 701     1378   1104   1286   -317    202     65       C  
ATOM   3452  N   LEU B 702     -10.389  -6.926 -20.338  1.00  9.37           N  
ANISOU 3452  N   LEU B 702     1277   1042   1242   -240    323    101       N  
ATOM   3453  CA  LEU B 702      -9.479  -5.865 -19.937  1.00  9.84           C  
ANISOU 3453  CA  LEU B 702     1287   1097   1355   -218    361    126       C  
ATOM   3454  C   LEU B 702      -9.403  -4.863 -21.070  1.00 10.41           C  
ANISOU 3454  C   LEU B 702     1383   1187   1386   -205    400    149       C  
ATOM   3455  O   LEU B 702      -9.147  -5.224 -22.215  1.00 12.43           O  
ANISOU 3455  O   LEU B 702     1694   1440   1587   -196    438    135       O  
ATOM   3456  CB  LEU B 702      -8.109  -6.426 -19.538  1.00  9.70           C  
ANISOU 3456  CB  LEU B 702     1245   1037   1403   -195    401    111       C  
ATOM   3457  CG  LEU B 702      -8.160  -7.436 -18.380  1.00  9.16           C  
ANISOU 3457  CG  LEU B 702     1161    947   1373   -204    356     99       C  
ATOM   3458  CD1 LEU B 702      -6.753  -7.890 -18.009  1.00 12.24           C  
ANISOU 3458  CD1 LEU B 702     1519   1293   1837   -174    387     89       C  
ATOM   3459  CD2 LEU B 702      -8.888  -6.878 -17.146  1.00  9.93           C  
ANISOU 3459  CD2 LEU B 702     1221   1069   1484   -224    303    121       C  
ATOM   3460  N   VAL B 703      -9.671  -3.604 -20.756  1.00  9.27           N  
ANISOU 3460  N   VAL B 703     1202   1059   1261   -205    390    183       N  
ATOM   3461  CA  VAL B 703      -9.746  -2.550 -21.771  1.00  9.21           C  
ANISOU 3461  CA  VAL B 703     1220   1066   1215   -195    418    217       C  
ATOM   3462  C   VAL B 703      -8.522  -1.638 -21.689  1.00  9.26           C  
ANISOU 3462  C   VAL B 703     1187   1045   1287   -179    482    241       C  
ATOM   3463  O   VAL B 703      -7.883  -1.542 -20.636  1.00  9.17           O  
ANISOU 3463  O   VAL B 703     1116   1012   1356   -178    480    233       O  
ATOM   3464  CB  VAL B 703     -11.086  -1.752 -21.714  1.00  8.39           C  
ANISOU 3464  CB  VAL B 703     1110    994   1084   -204    357    243       C  
ATOM   3465  CG1 VAL B 703     -12.258  -2.670 -22.072  1.00  9.04           C  
ANISOU 3465  CG1 VAL B 703     1230   1102   1102   -224    298    221       C  
ATOM   3466  CG2 VAL B 703     -11.298  -1.132 -20.338  1.00  9.96           C  
ANISOU 3466  CG2 VAL B 703     1240   1189   1354   -207    328    248       C  
ATOM   3467  N   ARG B 704      -8.187  -0.985 -22.798  1.00  9.23           N  
ANISOU 3467  N   ARG B 704     1217   1042   1249   -169    537    272       N  
ATOM   3468  CA  ARG B 704      -6.934  -0.237 -22.883  1.00  9.63           C  
ANISOU 3468  CA  ARG B 704     1230   1062   1366   -159    612    297       C  
ATOM   3469  C   ARG B 704      -6.889   0.945 -21.920  1.00 10.21           C  
ANISOU 3469  C   ARG B 704     1237   1118   1524   -166    585    320       C  
ATOM   3470  O   ARG B 704      -5.830   1.278 -21.352  1.00 10.66           O  
ANISOU 3470  O   ARG B 704     1233   1143   1673   -166    615    319       O  
ATOM   3471  CB  ARG B 704      -6.726   0.250 -24.314  1.00 10.17           C  
ANISOU 3471  CB  ARG B 704     1359   1137   1368   -151    680    334       C  
ATOM   3472  CG  ARG B 704      -5.321   0.709 -24.568  1.00 11.94           C  
ANISOU 3472  CG  ARG B 704     1548   1329   1660   -144    779    356       C  
ATOM   3473  CD  ARG B 704      -5.222   1.266 -25.960  1.00 13.65           C  
ANISOU 3473  CD  ARG B 704     1833   1555   1799   -137    851    404       C  
ATOM   3474  NE  ARG B 704      -5.715   0.330 -26.973  1.00 13.90           N  
ANISOU 3474  NE  ARG B 704     1962   1619   1702   -127    854    379       N  
ATOM   3475  CZ  ARG B 704      -4.972  -0.595 -27.579  1.00 15.22           C  
ANISOU 3475  CZ  ARG B 704     2161   1782   1839   -113    929    344       C  
ATOM   3476  NH1 ARG B 704      -3.680  -0.739 -27.281  1.00 16.42           N  
ANISOU 3476  NH1 ARG B 704     2247   1902   2089   -104   1010    334       N  
ATOM   3477  NH2 ARG B 704      -5.515  -1.384 -28.501  1.00 14.78           N  
ANISOU 3477  NH2 ARG B 704     2204   1753   1659   -105    922    315       N  
ATOM   3478  N   ASN B 705      -8.028   1.597 -21.769  1.00  9.77           N  
ANISOU 3478  N   ASN B 705     1190   1081   1440   -170    528    338       N  
ATOM   3479  CA  ASN B 705      -8.125   2.854 -21.029  1.00 10.54           C  
ANISOU 3479  CA  ASN B 705     1239   1158   1606   -171    507    358       C  
ATOM   3480  C   ASN B 705      -9.588   3.186 -20.727  1.00 10.93           C  
ANISOU 3480  C   ASN B 705     1297   1235   1621   -169    435    362       C  
ATOM   3481  O   ASN B 705     -10.503   2.481 -21.190  1.00 10.61           O  
ANISOU 3481  O   ASN B 705     1295   1230   1505   -171    401    354       O  
ATOM   3482  CB  ASN B 705      -7.424   3.983 -21.812  1.00 11.36           C  
ANISOU 3482  CB  ASN B 705     1347   1232   1739   -168    571    410       C  
ATOM   3483  CG  ASN B 705      -7.933   4.104 -23.236  1.00 11.56           C  
ANISOU 3483  CG  ASN B 705     1449   1279   1665   -160    594    452       C  
ATOM   3484  OD1 ASN B 705      -9.138   4.086 -23.475  1.00 11.31           O  
ANISOU 3484  OD1 ASN B 705     1452   1277   1567   -155    535    458       O  
ATOM   3485  ND2 ASN B 705      -7.018   4.211 -24.189  1.00 14.45           N  
ANISOU 3485  ND2 ASN B 705     1841   1630   2018   -158    680    481       N  
ATOM   3486  N   SER B 706      -9.821   4.250 -19.962  1.00 11.45           N  
ANISOU 3486  N   SER B 706     1322   1282   1745   -165    411    369       N  
ATOM   3487  CA  SER B 706     -11.191   4.619 -19.579  1.00 11.93           C  
ANISOU 3487  CA  SER B 706     1378   1367   1789   -158    351    369       C  
ATOM   3488  C   SER B 706     -12.104   4.890 -20.778  1.00 12.39           C  
ANISOU 3488  C   SER B 706     1482   1447   1778   -146    335    411       C  
ATOM   3489  O   SER B 706     -13.252   4.462 -20.790  1.00 11.92           O  
ANISOU 3489  O   SER B 706     1428   1424   1678   -146    283    402       O  
ATOM   3490  CB  SER B 706     -11.184   5.818 -18.627  1.00 13.03           C  
ANISOU 3490  CB  SER B 706     1471   1472   2006   -149    339    367       C  
ATOM   3491  OG  SER B 706     -10.284   5.582 -17.562  1.00 14.06           O  
ANISOU 3491  OG  SER B 706     1566   1584   2193   -160    344    328       O  
ATOM   3492  N   ASP B 707     -11.596   5.600 -21.788  1.00 12.91           N  
ANISOU 3492  N   ASP B 707     1582   1491   1834   -139    377    460       N  
ATOM   3493  CA  ASP B 707     -12.387   5.871 -22.999  1.00 13.56           C  
ANISOU 3493  CA  ASP B 707     1720   1594   1839   -126    356    506       C  
ATOM   3494  C   ASP B 707     -12.923   4.586 -23.642  1.00 12.96           C  
ANISOU 3494  C   ASP B 707     1691   1565   1667   -135    327    482       C  
ATOM   3495  O   ASP B 707     -14.107   4.479 -23.959  1.00 12.59           O  
ANISOU 3495  O   ASP B 707     1658   1551   1574   -130    261    489       O  
ATOM   3496  CB  ASP B 707     -11.574   6.672 -24.023  1.00 14.76           C  
ANISOU 3496  CB  ASP B 707     1914   1714   1982   -121    421    567       C  
ATOM   3497  CG  ASP B 707     -11.424   8.139 -23.648  1.00 18.86           C  
ANISOU 3497  CG  ASP B 707     2398   2180   2588   -111    429    606       C  
ATOM   3498  OD1 ASP B 707     -12.310   8.682 -22.957  1.00 21.95           O  
ANISOU 3498  OD1 ASP B 707     2754   2567   3019    -96    372    597       O  
ATOM   3499  OD2 ASP B 707     -10.417   8.751 -24.069  1.00 22.25           O  
ANISOU 3499  OD2 ASP B 707     2836   2568   3051   -118    497    644       O  
ATOM   3500  N   GLU B 708     -12.045   3.603 -23.819  1.00 11.41           N  
ANISOU 3500  N   GLU B 708     1516   1369   1449   -148    374    451       N  
ATOM   3501  CA  GLU B 708     -12.464   2.342 -24.421  1.00 10.74           C  
ANISOU 3501  CA  GLU B 708     1482   1319   1279   -158    350    420       C  
ATOM   3502  C   GLU B 708     -13.435   1.595 -23.499  1.00  9.85           C  
ANISOU 3502  C   GLU B 708     1329   1229   1183   -173    279    377       C  
ATOM   3503  O   GLU B 708     -14.405   1.008 -23.973  1.00 10.20           O  
ANISOU 3503  O   GLU B 708     1402   1305   1169   -182    222    366       O  
ATOM   3504  CB  GLU B 708     -11.249   1.476 -24.777  1.00 10.67           C  
ANISOU 3504  CB  GLU B 708     1503   1297   1256   -163    424    392       C  
ATOM   3505  CG  GLU B 708     -10.397   2.080 -25.899  1.00 13.47           C  
ANISOU 3505  CG  GLU B 708     1907   1637   1573   -150    505    437       C  
ATOM   3506  CD  GLU B 708      -9.473   1.078 -26.571  1.00 14.25           C  
ANISOU 3506  CD  GLU B 708     2053   1734   1627   -148    577    406       C  
ATOM   3507  OE1 GLU B 708      -9.849  -0.107 -26.695  1.00 16.33           O  
ANISOU 3507  OE1 GLU B 708     2350   2015   1840   -154    545    355       O  
ATOM   3508  OE2 GLU B 708      -8.377   1.502 -27.004  1.00 16.15           O  
ANISOU 3508  OE2 GLU B 708     2297   1952   1889   -141    671    432       O  
ATOM   3509  N   GLY B 709     -13.170   1.630 -22.194  1.00  8.94           N  
ANISOU 3509  N   GLY B 709     1150   1098   1149   -178    283    354       N  
ATOM   3510  CA  GLY B 709     -14.068   1.010 -21.223  1.00  8.74           C  
ANISOU 3510  CA  GLY B 709     1085   1093   1142   -193    230    322       C  
ATOM   3511  C   GLY B 709     -15.463   1.612 -21.252  1.00  8.90           C  
ANISOU 3511  C   GLY B 709     1083   1140   1157   -186    169    343       C  
ATOM   3512  O   GLY B 709     -16.464   0.894 -21.312  1.00  9.06           O  
ANISOU 3512  O   GLY B 709     1102   1191   1151   -203    118    327       O  
ATOM   3513  N   ILE B 710     -15.537   2.939 -21.222  1.00  9.68           N  
ANISOU 3513  N   ILE B 710     1162   1224   1292   -162    174    378       N  
ATOM   3514  CA  ILE B 710     -16.833   3.626 -21.235  1.00 10.85           C  
ANISOU 3514  CA  ILE B 710     1281   1392   1451   -146    119    400       C  
ATOM   3515  C   ILE B 710     -17.576   3.340 -22.536  1.00 11.34           C  
ANISOU 3515  C   ILE B 710     1390   1482   1435   -146     69    424       C  
ATOM   3516  O   ILE B 710     -18.772   3.043 -22.529  1.00 11.90           O  
ANISOU 3516  O   ILE B 710     1434   1586   1501   -152      5    418       O  
ATOM   3517  CB  ILE B 710     -16.673   5.134 -21.003  1.00 11.30           C  
ANISOU 3517  CB  ILE B 710     1314   1413   1567   -115    136    433       C  
ATOM   3518  CG1 ILE B 710     -16.158   5.392 -19.584  1.00 12.17           C  
ANISOU 3518  CG1 ILE B 710     1375   1499   1750   -116    166    397       C  
ATOM   3519  CG2 ILE B 710     -18.007   5.880 -21.252  1.00 12.58           C  
ANISOU 3519  CG2 ILE B 710     1450   1590   1740    -88     78    464       C  
ATOM   3520  CD1 ILE B 710     -15.574   6.788 -19.410  1.00 14.18           C  
ANISOU 3520  CD1 ILE B 710     1618   1702   2067    -94    195    420       C  
ATOM   3521  N   GLN B 711     -16.868   3.395 -23.661  1.00 11.52           N  
ANISOU 3521  N   GLN B 711     1484   1496   1396   -142     97    449       N  
ATOM   3522  CA  GLN B 711     -17.515   3.068 -24.925  1.00 13.10           C  
ANISOU 3522  CA  GLN B 711     1746   1727   1505   -143     44    467       C  
ATOM   3523  C   GLN B 711     -18.034   1.630 -24.960  1.00 12.98           C  
ANISOU 3523  C   GLN B 711     1740   1740   1450   -176      0    414       C  
ATOM   3524  O   GLN B 711     -19.093   1.366 -25.522  1.00 13.20           O  
ANISOU 3524  O   GLN B 711     1777   1799   1438   -183    -79    417       O  
ATOM   3525  CB  GLN B 711     -16.597   3.340 -26.110  1.00 14.20           C  
ANISOU 3525  CB  GLN B 711     1971   1852   1571   -133     95    502       C  
ATOM   3526  CG  GLN B 711     -17.385   3.567 -27.381  1.00 17.79           C  
ANISOU 3526  CG  GLN B 711     2492   2335   1934   -120     30    542       C  
ATOM   3527  CD  GLN B 711     -16.580   4.274 -28.435  1.00 21.76           C  
ANISOU 3527  CD  GLN B 711     3075   2820   2374   -102     88    600       C  
ATOM   3528  OE1 GLN B 711     -16.877   5.416 -28.796  1.00 21.49           O  
ANISOU 3528  OE1 GLN B 711     3047   2773   2345    -76     70    667       O  
ATOM   3529  NE2 GLN B 711     -15.551   3.604 -28.939  1.00 24.06           N  
ANISOU 3529  NE2 GLN B 711     3427   3107   2607   -113    163    578       N  
ATOM   3530  N   ARG B 712     -17.300   0.705 -24.342  1.00 11.85           N  
ANISOU 3530  N   ARG B 712     1592   1584   1326   -198     46    368       N  
ATOM   3531  CA  ARG B 712     -17.748  -0.682 -24.273  1.00 12.82           C  
ANISOU 3531  CA  ARG B 712     1724   1722   1425   -232      9    319       C  
ATOM   3532  C   ARG B 712     -19.055  -0.788 -23.474  1.00 12.16           C  
ANISOU 3532  C   ARG B 712     1562   1662   1395   -248    -55    312       C  
ATOM   3533  O   ARG B 712     -19.971  -1.506 -23.875  1.00 13.04           O  
ANISOU 3533  O   ARG B 712     1679   1796   1480   -274   -123    295       O  
ATOM   3534  CB  ARG B 712     -16.651  -1.564 -23.663  1.00 12.79           C  
ANISOU 3534  CB  ARG B 712     1725   1690   1446   -245     73    279       C  
ATOM   3535  CG  ARG B 712     -16.819  -3.069 -23.891  1.00 15.76           C  
ANISOU 3535  CG  ARG B 712     2137   2065   1785   -277     48    229       C  
ATOM   3536  CD  ARG B 712     -16.528  -3.503 -25.326  1.00 18.78           C  
ANISOU 3536  CD  ARG B 712     2617   2449   2068   -274     50    215       C  
ATOM   3537  NE  ARG B 712     -15.125  -3.288 -25.695  1.00 19.89           N  
ANISOU 3537  NE  ARG B 712     2798   2565   2194   -248    143    220       N  
ATOM   3538  CZ  ARG B 712     -14.110  -4.064 -25.311  1.00 19.75           C  
ANISOU 3538  CZ  ARG B 712     2782   2515   2207   -248    203    186       C  
ATOM   3539  NH1 ARG B 712     -14.334  -5.118 -24.540  1.00 19.07           N  
ANISOU 3539  NH1 ARG B 712     2671   2414   2161   -272    177    147       N  
ATOM   3540  NH2 ARG B 712     -12.860  -3.776 -25.694  1.00 16.46           N  
ANISOU 3540  NH2 ARG B 712     2389   2077   1787   -223    291    195       N  
ATOM   3541  N   VAL B 713     -19.145  -0.047 -22.369  1.00 11.26           N  
ANISOU 3541  N   VAL B 713     1379   1542   1359   -234    -34    324       N  
ATOM   3542  CA  VAL B 713     -20.361  -0.017 -21.539  1.00 11.35           C  
ANISOU 3542  CA  VAL B 713     1310   1577   1427   -243    -75    321       C  
ATOM   3543  C   VAL B 713     -21.554   0.509 -22.325  1.00 12.97           C  
ANISOU 3543  C   VAL B 713     1497   1810   1620   -230   -152    350       C  
ATOM   3544  O   VAL B 713     -22.657  -0.036 -22.239  1.00 13.66           O  
ANISOU 3544  O   VAL B 713     1540   1924   1725   -255   -209    339       O  
ATOM   3545  CB  VAL B 713     -20.156   0.842 -20.255  1.00 10.44           C  
ANISOU 3545  CB  VAL B 713     1133   1447   1385   -221    -29    325       C  
ATOM   3546  CG1 VAL B 713     -21.463   1.014 -19.511  1.00  9.83           C  
ANISOU 3546  CG1 VAL B 713      975   1397   1362   -222    -60    324       C  
ATOM   3547  CG2 VAL B 713     -19.126   0.189 -19.327  1.00  9.83           C  
ANISOU 3547  CG2 VAL B 713     1064   1348   1323   -237     27    294       C  
ATOM   3548  N   LEU B 714     -21.318   1.560 -23.104  1.00 13.62           N  
ANISOU 3548  N   LEU B 714     1613   1883   1678   -194   -154    392       N  
ATOM   3549  CA  LEU B 714     -22.386   2.191 -23.877  1.00 15.00           C  
ANISOU 3549  CA  LEU B 714     1776   2081   1844   -172   -233    430       C  
ATOM   3550  C   LEU B 714     -22.861   1.354 -25.058  1.00 16.43           C  
ANISOU 3550  C   LEU B 714     2014   2289   1940   -197   -310    422       C  
ATOM   3551  O   LEU B 714     -24.046   1.394 -25.396  1.00 17.78           O  
ANISOU 3551  O   LEU B 714     2146   2488   2121   -198   -398    434       O  
ATOM   3552  CB  LEU B 714     -21.961   3.586 -24.351  1.00 15.18           C  
ANISOU 3552  CB  LEU B 714     1825   2077   1864   -124   -213    487       C  
ATOM   3553  CG  LEU B 714     -21.844   4.657 -23.262  1.00 15.38           C  
ANISOU 3553  CG  LEU B 714     1785   2073   1985    -94   -165    496       C  
ATOM   3554  CD1 LEU B 714     -21.100   5.875 -23.782  1.00 14.85           C  
ANISOU 3554  CD1 LEU B 714     1763   1966   1915    -58   -131    548       C  
ATOM   3555  CD2 LEU B 714     -23.234   5.049 -22.729  1.00 15.92           C  
ANISOU 3555  CD2 LEU B 714     1760   2163   2127    -74   -220    500       C  
ATOM   3556  N   THR B 715     -21.958   0.590 -25.667  1.00 16.56           N  
ANISOU 3556  N   THR B 715     2120   2295   1878   -216   -278    398       N  
ATOM   3557  CA  THR B 715     -22.236  -0.046 -26.963  1.00 18.01           C  
ANISOU 3557  CA  THR B 715     2385   2499   1959   -232   -345    388       C  
ATOM   3558  C   THR B 715     -22.417  -1.565 -26.931  1.00 17.85           C  
ANISOU 3558  C   THR B 715     2380   2483   1920   -284   -371    323       C  
ATOM   3559  O   THR B 715     -22.923  -2.144 -27.900  1.00 18.94           O  
ANISOU 3559  O   THR B 715     2573   2639   1985   -303   -449    304       O  
ATOM   3560  CB  THR B 715     -21.150   0.294 -28.019  1.00 18.52           C  
ANISOU 3560  CB  THR B 715     2563   2550   1925   -209   -293    412       C  
ATOM   3561  OG1 THR B 715     -19.886  -0.229 -27.590  1.00 19.35           O  
ANISOU 3561  OG1 THR B 715     2692   2625   2036   -218   -190    379       O  
ATOM   3562  CG2 THR B 715     -21.047   1.813 -28.252  1.00 19.57           C  
ANISOU 3562  CG2 THR B 715     2693   2672   2070   -162   -278    487       C  
ATOM   3563  N   THR B 716     -21.991  -2.205 -25.837  1.00 16.35           N  
ANISOU 3563  N   THR B 716     2148   2272   1792   -306   -311    289       N  
ATOM   3564  CA  THR B 716     -22.070  -3.665 -25.683  1.00 16.14           C  
ANISOU 3564  CA  THR B 716     2136   2236   1762   -355   -325    231       C  
ATOM   3565  C   THR B 716     -22.548  -3.999 -24.273  1.00 15.37           C  
ANISOU 3565  C   THR B 716     1938   2135   1767   -381   -311    222       C  
ATOM   3566  O   THR B 716     -22.621  -3.115 -23.418  1.00 14.45           O  
ANISOU 3566  O   THR B 716     1753   2023   1713   -356   -276    252       O  
ATOM   3567  CB  THR B 716     -20.701  -4.362 -25.914  1.00 16.04           C  
ANISOU 3567  CB  THR B 716     2207   2188   1700   -355   -247    197       C  
ATOM   3568  OG1 THR B 716     -19.840  -4.114 -24.796  1.00 16.18           O  
ANISOU 3568  OG1 THR B 716     2182   2182   1785   -340   -160    204       O  
ATOM   3569  CG2 THR B 716     -20.017  -3.858 -27.181  1.00 17.49           C  
ANISOU 3569  CG2 THR B 716     2489   2374   1782   -322   -225    214       C  
ATOM   3570  N   ASP B 717     -22.847  -5.274 -24.026  1.00 15.34           N  
ANISOU 3570  N   ASP B 717     1931   2119   1778   -431   -333    180       N  
ATOM   3571  CA  ASP B 717     -23.283  -5.711 -22.700  1.00 14.95           C  
ANISOU 3571  CA  ASP B 717     1797   2065   1817   -460   -312    177       C  
ATOM   3572  C   ASP B 717     -22.077  -5.976 -21.820  1.00 13.52           C  
ANISOU 3572  C   ASP B 717     1635   1850   1651   -450   -220    168       C  
ATOM   3573  O   ASP B 717     -21.641  -7.126 -21.631  1.00 14.22           O  
ANISOU 3573  O   ASP B 717     1759   1906   1738   -480   -204    136       O  
ATOM   3574  CB  ASP B 717     -24.202  -6.927 -22.789  1.00 16.08           C  
ANISOU 3574  CB  ASP B 717     1923   2205   1981   -523   -378    145       C  
ATOM   3575  CG  ASP B 717     -25.571  -6.586 -23.334  1.00 18.72           C  
ANISOU 3575  CG  ASP B 717     2201   2579   2333   -536   -475    159       C  
ATOM   3576  OD1 ASP B 717     -25.907  -5.386 -23.461  1.00 21.09           O  
ANISOU 3576  OD1 ASP B 717     2463   2909   2643   -493   -488    198       O  
ATOM   3577  OD2 ASP B 717     -26.317  -7.532 -23.634  1.00 22.22           O  
ANISOU 3577  OD2 ASP B 717     2635   3018   2790   -591   -544    130       O  
ATOM   3578  N   TYR B 718     -21.552  -4.881 -21.283  1.00 12.00           N  
ANISOU 3578  N   TYR B 718     1419   1661   1480   -407   -166    197       N  
ATOM   3579  CA  TYR B 718     -20.312  -4.876 -20.526  1.00 10.25           C  
ANISOU 3579  CA  TYR B 718     1213   1410   1273   -389    -89    193       C  
ATOM   3580  C   TYR B 718     -20.406  -3.865 -19.391  1.00  9.96           C  
ANISOU 3580  C   TYR B 718     1108   1385   1293   -365    -55    218       C  
ATOM   3581  O   TYR B 718     -20.796  -2.719 -19.618  1.00 10.59           O  
ANISOU 3581  O   TYR B 718     1161   1483   1381   -334    -66    244       O  
ATOM   3582  CB  TYR B 718     -19.156  -4.511 -21.471  1.00 11.01           C  
ANISOU 3582  CB  TYR B 718     1383   1488   1314   -357    -54    194       C  
ATOM   3583  CG  TYR B 718     -17.793  -4.381 -20.823  1.00  9.57           C  
ANISOU 3583  CG  TYR B 718     1207   1274   1156   -335     21    192       C  
ATOM   3584  CD1 TYR B 718     -16.972  -5.491 -20.654  1.00 10.07           C  
ANISOU 3584  CD1 TYR B 718     1305   1304   1219   -347     50    161       C  
ATOM   3585  CD2 TYR B 718     -17.310  -3.131 -20.409  1.00 10.12           C  
ANISOU 3585  CD2 TYR B 718     1247   1343   1256   -300     58    220       C  
ATOM   3586  CE1 TYR B 718     -15.702  -5.372 -20.075  1.00  8.86           C  
ANISOU 3586  CE1 TYR B 718     1149   1122   1097   -324    110    160       C  
ATOM   3587  CE2 TYR B 718     -16.046  -3.001 -19.830  1.00  8.64           C  
ANISOU 3587  CE2 TYR B 718     1059   1126   1099   -284    116    216       C  
ATOM   3588  CZ  TYR B 718     -15.243  -4.118 -19.670  1.00  7.56           C  
ANISOU 3588  CZ  TYR B 718      950    961    963   -295    140    188       C  
ATOM   3589  OH  TYR B 718     -14.009  -3.981 -19.086  1.00  8.96           O  
ANISOU 3589  OH  TYR B 718     1115   1109   1179   -277    188    185       O  
ATOM   3590  N   ALA B 719     -20.010  -4.288 -18.189  1.00  8.26           N  
ANISOU 3590  N   ALA B 719      873   1155   1112   -375    -15    209       N  
ATOM   3591  CA  ALA B 719     -19.874  -3.412 -17.025  1.00  7.62           C  
ANISOU 3591  CA  ALA B 719      745   1078   1071   -350     24    222       C  
ATOM   3592  C   ALA B 719     -18.405  -3.181 -16.703  1.00  7.37           C  
ANISOU 3592  C   ALA B 719      747   1015   1039   -326     71    216       C  
ATOM   3593  O   ALA B 719     -17.601  -4.118 -16.737  1.00  6.80           O  
ANISOU 3593  O   ALA B 719      713    915    954   -339     84    200       O  
ATOM   3594  CB  ALA B 719     -20.581  -4.012 -15.816  1.00  7.90           C  
ANISOU 3594  CB  ALA B 719      735   1128   1140   -380     32    219       C  
ATOM   3595  N   LEU B 720     -18.068  -1.937 -16.383  1.00  7.00           N  
ANISOU 3595  N   LEU B 720      680    966   1015   -292     94    228       N  
ATOM   3596  CA  LEU B 720     -16.699  -1.555 -16.085  1.00  6.16           C  
ANISOU 3596  CA  LEU B 720      592    827    922   -271    132    223       C  
ATOM   3597  C   LEU B 720     -16.486  -1.354 -14.591  1.00  6.85           C  
ANISOU 3597  C   LEU B 720      650    912   1041   -267    149    212       C  
ATOM   3598  O   LEU B 720     -17.210  -0.593 -13.955  1.00  6.67           O  
ANISOU 3598  O   LEU B 720      591    908   1037   -255    148    214       O  
ATOM   3599  CB  LEU B 720     -16.353  -0.270 -16.844  1.00  6.23           C  
ANISOU 3599  CB  LEU B 720      606    826    936   -239    143    244       C  
ATOM   3600  CG  LEU B 720     -14.916   0.225 -16.686  1.00  6.15           C  
ANISOU 3600  CG  LEU B 720      605    778    953   -223    184    243       C  
ATOM   3601  CD1 LEU B 720     -13.906  -0.735 -17.330  1.00  7.30           C  
ANISOU 3601  CD1 LEU B 720      793    904   1077   -231    207    233       C  
ATOM   3602  CD2 LEU B 720     -14.771   1.619 -17.283  1.00  7.66           C  
ANISOU 3602  CD2 LEU B 720      794    954   1161   -196    196    271       C  
ATOM   3603  N   LEU B 721     -15.511  -2.062 -14.025  1.00  6.43           N  
ANISOU 3603  N   LEU B 721      616    836    992   -274    161    199       N  
ATOM   3604  CA  LEU B 721     -15.076  -1.793 -12.658  1.00  6.52           C  
ANISOU 3604  CA  LEU B 721      612    841   1023   -266    170    189       C  
ATOM   3605  C   LEU B 721     -14.214  -0.531 -12.708  1.00  6.57           C  
ANISOU 3605  C   LEU B 721      609    824   1062   -237    183    186       C  
ATOM   3606  O   LEU B 721     -13.244  -0.456 -13.465  1.00  7.22           O  
ANISOU 3606  O   LEU B 721      705    880   1159   -230    197    190       O  
ATOM   3607  CB  LEU B 721     -14.334  -3.006 -12.067  1.00  6.06           C  
ANISOU 3607  CB  LEU B 721      579    764    961   -282    167    182       C  
ATOM   3608  CG  LEU B 721     -15.208  -4.162 -11.543  1.00  7.11           C  
ANISOU 3608  CG  LEU B 721      718    913   1071   -314    156    189       C  
ATOM   3609  CD1 LEU B 721     -15.926  -3.762 -10.244  1.00  7.76           C  
ANISOU 3609  CD1 LEU B 721      779   1025   1146   -316    164    191       C  
ATOM   3610  CD2 LEU B 721     -16.210  -4.666 -12.585  1.00  8.67           C  
ANISOU 3610  CD2 LEU B 721      916   1124   1254   -338    144    194       C  
ATOM   3611  N   MET B 722     -14.636   0.478 -11.945  1.00  7.35           N  
ANISOU 3611  N   MET B 722      684    932   1178   -222    184    178       N  
ATOM   3612  CA  MET B 722     -14.153   1.839 -12.123  1.00  8.11           C  
ANISOU 3612  CA  MET B 722      768   1002   1313   -197    193    176       C  
ATOM   3613  C   MET B 722     -14.114   2.519 -10.763  1.00  7.82           C  
ANISOU 3613  C   MET B 722      718    961   1292   -185    190    148       C  
ATOM   3614  O   MET B 722     -14.926   2.235  -9.891  1.00  8.51           O  
ANISOU 3614  O   MET B 722      802   1080   1353   -188    190    136       O  
ATOM   3615  CB  MET B 722     -15.140   2.591 -13.045  1.00  8.72           C  
ANISOU 3615  CB  MET B 722      832   1090   1390   -183    192    199       C  
ATOM   3616  CG  MET B 722     -14.669   3.981 -13.503  1.00 11.06           C  
ANISOU 3616  CG  MET B 722     1124   1350   1729   -158    202    211       C  
ATOM   3617  SD  MET B 722     -15.874   4.832 -14.544  1.00 13.89           S  
ANISOU 3617  SD  MET B 722     1471   1718   2087   -135    190    247       S  
ATOM   3618  CE  MET B 722     -14.846   5.200 -15.963  1.00 13.07           C  
ANISOU 3618  CE  MET B 722     1404   1579   1983   -134    209    286       C  
ATOM   3619  N   GLU B 723     -13.186   3.451 -10.586  1.00  6.44           N  
ANISOU 3619  N   GLU B 723      539    748   1160   -172    189    135       N  
ATOM   3620  CA  GLU B 723     -13.142   4.225  -9.353  1.00  6.59           C  
ANISOU 3620  CA  GLU B 723      553    758   1192   -159    180     98       C  
ATOM   3621  C   GLU B 723     -14.281   5.232  -9.226  1.00  6.46           C  
ANISOU 3621  C   GLU B 723      520    750   1184   -135    193     90       C  
ATOM   3622  O   GLU B 723     -14.708   5.847 -10.210  1.00  6.84           O  
ANISOU 3622  O   GLU B 723      554    787   1256   -121    200    116       O  
ATOM   3623  CB  GLU B 723     -11.775   4.892  -9.248  1.00  5.87           C  
ANISOU 3623  CB  GLU B 723      458    617   1157   -158    168     83       C  
ATOM   3624  CG  GLU B 723     -10.671   3.814  -9.192  1.00  5.79           C  
ANISOU 3624  CG  GLU B 723      453    601   1146   -176    154     88       C  
ATOM   3625  CD  GLU B 723      -9.250   4.362  -9.338  1.00  5.30           C  
ANISOU 3625  CD  GLU B 723      369    489   1156   -180    146     82       C  
ATOM   3626  OE1 GLU B 723      -9.056   5.420  -9.985  1.00  6.70           O  
ANISOU 3626  OE1 GLU B 723      530    633   1384   -175    165     92       O  
ATOM   3627  OE2 GLU B 723      -8.318   3.705  -8.812  1.00  7.09           O  
ANISOU 3627  OE2 GLU B 723      591    707   1394   -187    120     71       O  
ATOM   3628  N   SER B 724     -14.769   5.379  -7.996  1.00  6.47           N  
ANISOU 3628  N   SER B 724      526    771   1163   -125    195     54       N  
ATOM   3629  CA  SER B 724     -15.950   6.183  -7.709  1.00  6.68           C  
ANISOU 3629  CA  SER B 724      532    810   1195    -97    216     40       C  
ATOM   3630  C   SER B 724     -15.877   7.648  -8.154  1.00  7.42           C  
ANISOU 3630  C   SER B 724      613    854   1353    -67    216     33       C  
ATOM   3631  O   SER B 724     -16.887   8.221  -8.566  1.00  8.12           O  
ANISOU 3631  O   SER B 724      676    947   1463    -41    229     46       O  
ATOM   3632  CB  SER B 724     -16.272   6.091  -6.219  1.00  7.07           C  
ANISOU 3632  CB  SER B 724      599    885   1201    -91    228     -4       C  
ATOM   3633  OG  SER B 724     -15.172   6.562  -5.456  1.00  9.06           O  
ANISOU 3633  OG  SER B 724      880   1102   1459    -90    202    -44       O  
ATOM   3634  N   THR B 725     -14.690   8.245  -8.048  1.00  7.50           N  
ANISOU 3634  N   THR B 725      637    812   1402    -72    199     16       N  
ATOM   3635  CA  THR B 725     -14.418   9.603  -8.531  1.00  8.89           C  
ANISOU 3635  CA  THR B 725      803    925   1649    -52    198     17       C  
ATOM   3636  C   THR B 725     -14.767   9.739 -10.014  1.00  8.32           C  
ANISOU 3636  C   THR B 725      718    848   1597    -47    207     80       C  
ATOM   3637  O   THR B 725     -15.409  10.703 -10.445  1.00  8.64           O  
ANISOU 3637  O   THR B 725      745    862   1675    -17    213     94       O  
ATOM   3638  CB  THR B 725     -12.915   9.895  -8.368  1.00  9.72           C  
ANISOU 3638  CB  THR B 725      918    979   1798    -74    177      1       C  
ATOM   3639  OG1 THR B 725     -12.189   8.726  -8.759  1.00 11.38           O  
ANISOU 3639  OG1 THR B 725     1130   1212   1981   -104    172     29       O  
ATOM   3640  CG2 THR B 725     -12.591  10.215  -6.937  1.00 12.03           C  
ANISOU 3640  CG2 THR B 725     1228   1260   2083    -71    154    -68       C  
ATOM   3641  N   SER B 726     -14.320   8.766 -10.795  1.00  7.85           N  
ANISOU 3641  N   SER B 726      665    809   1508    -74    207    117       N  
ATOM   3642  CA  SER B 726     -14.531   8.755 -12.230  1.00  7.65           C  
ANISOU 3642  CA  SER B 726      642    784   1481    -73    213    175       C  
ATOM   3643  C   SER B 726     -15.980   8.401 -12.568  1.00  7.74           C  
ANISOU 3643  C   SER B 726      639    844   1456    -59    206    193       C  
ATOM   3644  O   SER B 726     -16.528   8.945 -13.529  1.00  7.70           O  
ANISOU 3644  O   SER B 726      631    831   1463    -40    199    233       O  
ATOM   3645  CB  SER B 726     -13.559   7.782 -12.879  1.00  8.16           C  
ANISOU 3645  CB  SER B 726      725    855   1522   -104    220    196       C  
ATOM   3646  OG  SER B 726     -12.235   8.196 -12.571  1.00  9.47           O  
ANISOU 3646  OG  SER B 726      889    973   1738   -116    226    181       O  
ATOM   3647  N   ILE B 727     -16.595   7.519 -11.778  1.00  7.77           N  
ANISOU 3647  N   ILE B 727      634    898   1421    -69    205    167       N  
ATOM   3648  CA  ILE B 727     -18.020   7.212 -11.975  1.00  8.11           C  
ANISOU 3648  CA  ILE B 727      649    987   1447    -59    199    181       C  
ATOM   3649  C   ILE B 727     -18.860   8.471 -11.748  1.00  8.85           C  
ANISOU 3649  C   ILE B 727      710   1062   1590    -13    204    173       C  
ATOM   3650  O   ILE B 727     -19.763   8.773 -12.531  1.00  9.27           O  
ANISOU 3650  O   ILE B 727      738   1124   1660      7    187    206       O  
ATOM   3651  CB  ILE B 727     -18.507   6.081 -11.048  1.00  7.85           C  
ANISOU 3651  CB  ILE B 727      607   1004   1371    -82    208    157       C  
ATOM   3652  CG1 ILE B 727     -17.778   4.781 -11.395  1.00  7.98           C  
ANISOU 3652  CG1 ILE B 727      655   1032   1346   -123    199    169       C  
ATOM   3653  CG2 ILE B 727     -20.020   5.900 -11.161  1.00  8.53           C  
ANISOU 3653  CG2 ILE B 727      647   1134   1460    -73    207    169       C  
ATOM   3654  CD1 ILE B 727     -18.096   3.614 -10.455  1.00  8.19           C  
ANISOU 3654  CD1 ILE B 727      683   1095   1332   -150    207    154       C  
ATOM   3655  N   GLU B 728     -18.563   9.192 -10.666  1.00  8.83           N  
ANISOU 3655  N   GLU B 728      710   1031   1613      4    221    126       N  
ATOM   3656  CA  GLU B 728     -19.280  10.430 -10.325  1.00 10.67           C  
ANISOU 3656  CA  GLU B 728      917   1236   1900     53    232    106       C  
ATOM   3657  C   GLU B 728     -19.201  11.426 -11.488  1.00 10.74           C  
ANISOU 3657  C   GLU B 728      926   1192   1961     77    213    153       C  
ATOM   3658  O   GLU B 728     -20.209  12.042 -11.859  1.00 11.94           O  
ANISOU 3658  O   GLU B 728     1045   1340   2150    117    206    173       O  
ATOM   3659  CB  GLU B 728     -18.703  11.034  -9.032  1.00 11.19           C  
ANISOU 3659  CB  GLU B 728     1005   1269   1978     63    249     40       C  
ATOM   3660  CG  GLU B 728     -19.368  12.339  -8.573  1.00 15.29           C  
ANISOU 3660  CG  GLU B 728     1505   1749   2555    117    266      5       C  
ATOM   3661  CD  GLU B 728     -18.633  13.010  -7.419  1.00 19.52           C  
ANISOU 3661  CD  GLU B 728     2076   2241   3100    123    272    -67       C  
ATOM   3662  OE1 GLU B 728     -17.772  12.364  -6.790  1.00 24.53           O  
ANISOU 3662  OE1 GLU B 728     2743   2890   3687     87    262    -92       O  
ATOM   3663  OE2 GLU B 728     -18.914  14.189  -7.141  1.00 21.67           O  
ANISOU 3663  OE2 GLU B 728     2345   2460   3429    165    281   -101       O  
ATOM   3664  N   TYR B 729     -18.008  11.556 -12.072  1.00 10.17           N  
ANISOU 3664  N   TYR B 729      889   1079   1895     53    207    176       N  
ATOM   3665  CA  TYR B 729     -17.799  12.457 -13.201  1.00 10.65           C  
ANISOU 3665  CA  TYR B 729      961   1087   1998     69    197    230       C  
ATOM   3666  C   TYR B 729     -18.637  12.060 -14.414  1.00 11.05           C  
ANISOU 3666  C   TYR B 729     1005   1176   2016     76    172    292       C  
ATOM   3667  O   TYR B 729     -19.369  12.888 -14.971  1.00 11.69           O  
ANISOU 3667  O   TYR B 729     1072   1234   2134    115    154    328       O  
ATOM   3668  CB  TYR B 729     -16.315  12.514 -13.585  1.00 10.70           C  
ANISOU 3668  CB  TYR B 729     1001   1050   2014     34    207    246       C  
ATOM   3669  CG  TYR B 729     -16.044  13.457 -14.730  1.00 11.36           C  
ANISOU 3669  CG  TYR B 729     1102   1076   2138     46    208    310       C  
ATOM   3670  CD1 TYR B 729     -16.037  14.831 -14.520  1.00 11.98           C  
ANISOU 3670  CD1 TYR B 729     1176   1078   2297     74    209    307       C  
ATOM   3671  CD2 TYR B 729     -15.813  12.983 -16.029  1.00 12.14           C  
ANISOU 3671  CD2 TYR B 729     1228   1193   2191     29    209    374       C  
ATOM   3672  CE1 TYR B 729     -15.796  15.718 -15.558  1.00 12.67           C  
ANISOU 3672  CE1 TYR B 729     1284   1106   2424     84    212    375       C  
ATOM   3673  CE2 TYR B 729     -15.578  13.876 -17.085  1.00 12.99           C  
ANISOU 3673  CE2 TYR B 729     1361   1249   2326     40    215    442       C  
ATOM   3674  CZ  TYR B 729     -15.564  15.236 -16.825  1.00 12.42           C  
ANISOU 3674  CZ  TYR B 729     1282   1098   2339     66    217    445       C  
ATOM   3675  OH  TYR B 729     -15.329  16.170 -17.818  1.00 16.86           O  
ANISOU 3675  OH  TYR B 729     1872   1600   2935     76    224    520       O  
ATOM   3676  N   VAL B 730     -18.555  10.792 -14.807  1.00 10.98           N  
ANISOU 3676  N   VAL B 730     1009   1223   1941     40    165    303       N  
ATOM   3677  CA  VAL B 730     -19.205  10.366 -16.049  1.00 11.55           C  
ANISOU 3677  CA  VAL B 730     1088   1328   1973     39    133    357       C  
ATOM   3678  C   VAL B 730     -20.724  10.292 -15.935  1.00 11.38           C  
ANISOU 3678  C   VAL B 730     1013   1348   1962     65    104    357       C  
ATOM   3679  O   VAL B 730     -21.428  10.620 -16.889  1.00 12.29           O  
ANISOU 3679  O   VAL B 730     1122   1468   2080     88     64    404       O  
ATOM   3680  CB  VAL B 730     -18.613   9.048 -16.622  1.00 11.70           C  
ANISOU 3680  CB  VAL B 730     1143   1383   1919     -7    133    364       C  
ATOM   3681  CG1 VAL B 730     -17.127   9.204 -16.901  1.00 13.77           C  
ANISOU 3681  CG1 VAL B 730     1447   1602   2182    -26    167    373       C  
ATOM   3682  CG2 VAL B 730     -18.849   7.886 -15.702  1.00 12.34           C  
ANISOU 3682  CG2 VAL B 730     1204   1511   1972    -34    138    318       C  
ATOM   3683  N   THR B 731     -21.223   9.893 -14.768  1.00 10.52           N  
ANISOU 3683  N   THR B 731      866   1271   1862     63    123    306       N  
ATOM   3684  CA  THR B 731     -22.666   9.721 -14.598  1.00 10.79           C  
ANISOU 3684  CA  THR B 731      835   1349   1915     83    106    304       C  
ATOM   3685  C   THR B 731     -23.403  11.046 -14.439  1.00 12.28           C  
ANISOU 3685  C   THR B 731      982   1503   2182    146    105    307       C  
ATOM   3686  O   THR B 731     -24.622  11.092 -14.515  1.00 13.22           O  
ANISOU 3686  O   THR B 731     1038   1651   2333    172     85    316       O  
ATOM   3687  CB  THR B 731     -23.013   8.816 -13.403  1.00 10.04           C  
ANISOU 3687  CB  THR B 731      711   1301   1801     57    140    256       C  
ATOM   3688  OG1 THR B 731     -22.472   9.364 -12.191  1.00 10.24           O  
ANISOU 3688  OG1 THR B 731      749   1298   1843     71    186    205       O  
ATOM   3689  CG2 THR B 731     -22.535   7.386 -13.636  1.00 10.34           C  
ANISOU 3689  CG2 THR B 731      783   1373   1772     -2    132    259       C  
ATOM   3690  N   GLN B 732     -22.676  12.131 -14.215  1.00 12.78           N  
ANISOU 3690  N   GLN B 732     1074   1498   2284    170    125    298       N  
ATOM   3691  CA  GLN B 732     -23.325  13.435 -14.182  1.00 15.05           C  
ANISOU 3691  CA  GLN B 732     1329   1738   2652    234    120    304       C  
ATOM   3692  C   GLN B 732     -23.300  14.108 -15.555  1.00 15.64           C  
ANISOU 3692  C   GLN B 732     1427   1773   2743    256     73    381       C  
ATOM   3693  O   GLN B 732     -23.858  15.200 -15.735  1.00 17.02           O  
ANISOU 3693  O   GLN B 732     1578   1900   2988    312     58    402       O  
ATOM   3694  CB  GLN B 732     -22.767  14.320 -13.059  1.00 15.69           C  
ANISOU 3694  CB  GLN B 732     1424   1761   2778    255    165    243       C  
ATOM   3695  CG  GLN B 732     -23.226  13.886 -11.642  1.00 19.30           C  
ANISOU 3695  CG  GLN B 732     1850   2262   3223    256    211    168       C  
ATOM   3696  CD  GLN B 732     -24.743  13.585 -11.519  1.00 23.20           C  
ANISOU 3696  CD  GLN B 732     2265   2813   3738    285    215    171       C  
ATOM   3697  OE1 GLN B 732     -25.136  12.511 -11.045  1.00 26.90           O  
ANISOU 3697  OE1 GLN B 732     2710   3350   4161    252    234    154       O  
ATOM   3698  NE2 GLN B 732     -25.584  14.526 -11.936  1.00 25.88           N  
ANISOU 3698  NE2 GLN B 732     2558   3121   4154    347    197    193       N  
ATOM   3699  N   ARG B 733     -22.688  13.429 -16.526  1.00 15.19           N  
ANISOU 3699  N   ARG B 733     1420   1735   2617    213     52    424       N  
ATOM   3700  CA  ARG B 733     -22.557  13.946 -17.891  1.00 16.40           C  
ANISOU 3700  CA  ARG B 733     1614   1858   2760    226     12    503       C  
ATOM   3701  C   ARG B 733     -23.190  13.076 -18.973  1.00 16.36           C  
ANISOU 3701  C   ARG B 733     1614   1916   2687    210    -46    548       C  
ATOM   3702  O   ARG B 733     -23.516  13.567 -20.062  1.00 18.70           O  
ANISOU 3702  O   ARG B 733     1932   2197   2975    236    -95    616       O  
ATOM   3703  CB  ARG B 733     -21.086  14.143 -18.209  1.00 15.80           C  
ANISOU 3703  CB  ARG B 733     1608   1734   2663    193     48    520       C  
ATOM   3704  CG  ARG B 733     -20.485  15.290 -17.435  1.00 17.89           C  
ANISOU 3704  CG  ARG B 733     1872   1916   3008    213     85    492       C  
ATOM   3705  CD  ARG B 733     -18.983  15.256 -17.493  1.00 20.14           C  
ANISOU 3705  CD  ARG B 733     2206   2165   3281    167    124    491       C  
ATOM   3706  NE  ARG B 733     -18.454  15.480 -18.839  1.00 26.18           N  
ANISOU 3706  NE  ARG B 733     3025   2907   4017    156    122    574       N  
ATOM   3707  CZ  ARG B 733     -18.156  16.671 -19.354  1.00 28.33           C  
ANISOU 3707  CZ  ARG B 733     3322   3099   4344    177    127    629       C  
ATOM   3708  NH1 ARG B 733     -17.671  16.749 -20.586  1.00 30.11           N  
ANISOU 3708  NH1 ARG B 733     3603   3312   4526    163    134    708       N  
ATOM   3709  NH2 ARG B 733     -18.335  17.785 -18.648  1.00 30.46           N  
ANISOU 3709  NH2 ARG B 733     3567   3297   4710    211    130    604       N  
ATOM   3710  N   ASN B 734     -23.332  11.787 -18.689  1.00 14.91           N  
ANISOU 3710  N   ASN B 734     1417   1797   2451    167    -44    511       N  
ATOM   3711  CA  ASN B 734     -24.029  10.875 -19.567  1.00 14.45           C  
ANISOU 3711  CA  ASN B 734     1358   1798   2336    147   -105    537       C  
ATOM   3712  C   ASN B 734     -25.112  10.179 -18.753  1.00 14.17           C  
ANISOU 3712  C   ASN B 734     1237   1817   2329    139   -112    493       C  
ATOM   3713  O   ASN B 734     -24.826   9.329 -17.913  1.00 12.87           O  
ANISOU 3713  O   ASN B 734     1067   1678   2146    101    -70    444       O  
ATOM   3714  CB  ASN B 734     -23.046   9.867 -20.176  1.00 13.98           C  
ANISOU 3714  CB  ASN B 734     1373   1757   2181     92    -94    538       C  
ATOM   3715  CG  ASN B 734     -23.672   9.022 -21.271  1.00 15.35           C  
ANISOU 3715  CG  ASN B 734     1566   1981   2286     72   -164    564       C  
ATOM   3716  OD1 ASN B 734     -24.856   8.697 -21.223  1.00 14.66           O  
ANISOU 3716  OD1 ASN B 734     1416   1933   2221     77   -217    558       O  
ATOM   3717  ND2 ASN B 734     -22.871   8.658 -22.270  1.00 16.61           N  
ANISOU 3717  ND2 ASN B 734     1811   2138   2361     49   -164    590       N  
ATOM   3718  N   CYS B 735     -26.364  10.545 -19.007  1.00 14.33           N  
ANISOU 3718  N   CYS B 735     1191   1854   2401    178   -165    516       N  
ATOM   3719  CA  CYS B 735     -27.472  10.079 -18.173  1.00 15.04           C  
ANISOU 3719  CA  CYS B 735     1183   1989   2541    177   -160    478       C  
ATOM   3720  C   CYS B 735     -27.928   8.666 -18.511  1.00 14.49           C  
ANISOU 3720  C   CYS B 735     1099   1983   2423    119   -200    472       C  
ATOM   3721  O   CYS B 735     -28.870   8.151 -17.903  1.00 15.28           O  
ANISOU 3721  O   CYS B 735     1115   2124   2567    107   -195    447       O  
ATOM   3722  CB  CYS B 735     -28.649  11.055 -18.225  1.00 15.85           C  
ANISOU 3722  CB  CYS B 735     1201   2081   2739    246   -195    501       C  
ATOM   3723  SG  CYS B 735     -28.214  12.783 -17.838  1.00 18.88           S  
ANISOU 3723  SG  CYS B 735     1602   2376   3197    321   -153    506       S  
ATOM   3724  N   ASN B 736     -27.252   8.031 -19.467  1.00 13.82           N  
ANISOU 3724  N   ASN B 736     1098   1903   2251     80   -233    491       N  
ATOM   3725  CA  ASN B 736     -27.491   6.616 -19.741  1.00 14.39           C  
ANISOU 3725  CA  ASN B 736     1174   2023   2272     18   -265    473       C  
ATOM   3726  C   ASN B 736     -26.654   5.698 -18.865  1.00 13.16           C  
ANISOU 3726  C   ASN B 736     1048   1869   2083    -31   -192    426       C  
ATOM   3727  O   ASN B 736     -26.862   4.487 -18.854  1.00 13.82           O  
ANISOU 3727  O   ASN B 736     1129   1984   2138    -84   -206    406       O  
ATOM   3728  CB  ASN B 736     -27.286   6.293 -21.229  1.00 15.24           C  
ANISOU 3728  CB  ASN B 736     1359   2137   2296      2   -341    510       C  
ATOM   3729  CG  ASN B 736     -28.476   6.708 -22.082  1.00 18.32           C  
ANISOU 3729  CG  ASN B 736     1701   2546   2713     34   -444    552       C  
ATOM   3730  OD1 ASN B 736     -29.614   6.745 -21.611  1.00 20.67           O  
ANISOU 3730  OD1 ASN B 736     1892   2869   3094     46   -468    545       O  
ATOM   3731  ND2 ASN B 736     -28.218   7.027 -23.346  1.00 22.03           N  
ANISOU 3731  ND2 ASN B 736     2251   3007   3114     48   -504    600       N  
ATOM   3732  N   LEU B 737     -25.719   6.293 -18.128  1.00 12.41           N  
ANISOU 3732  N   LEU B 737      983   1737   1997    -14   -121    410       N  
ATOM   3733  CA  LEU B 737     -24.789   5.558 -17.267  1.00 11.59           C  
ANISOU 3733  CA  LEU B 737      913   1629   1862    -52    -59    369       C  
ATOM   3734  C   LEU B 737     -25.170   5.679 -15.798  1.00 11.26           C  
ANISOU 3734  C   LEU B 737      812   1596   1869    -43     -2    332       C  
ATOM   3735  O   LEU B 737     -25.740   6.680 -15.380  1.00 11.29           O  
ANISOU 3735  O   LEU B 737      766   1589   1934      4     12    330       O  
ATOM   3736  CB  LEU B 737     -23.360   6.076 -17.477  1.00 11.26           C  
ANISOU 3736  CB  LEU B 737      948   1539   1791    -43    -25    375       C  
ATOM   3737  CG  LEU B 737     -22.730   5.816 -18.852  1.00 12.94           C  
ANISOU 3737  CG  LEU B 737     1237   1744   1937    -57    -55    408       C  
ATOM   3738  CD1 LEU B 737     -21.423   6.583 -18.993  1.00 12.83           C  
ANISOU 3738  CD1 LEU B 737     1277   1677   1919    -43    -10    421       C  
ATOM   3739  CD2 LEU B 737     -22.522   4.326 -19.104  1.00 14.27           C  
ANISOU 3739  CD2 LEU B 737     1437   1940   2045   -110    -65    386       C  
ATOM   3740  N   THR B 738     -24.813   4.669 -15.014  1.00 10.30           N  
ANISOU 3740  N   THR B 738      704   1491   1719    -87     35    302       N  
ATOM   3741  CA  THR B 738     -25.133   4.646 -13.592  1.00 10.54           C  
ANISOU 3741  CA  THR B 738      693   1535   1776    -84     94    268       C  
ATOM   3742  C   THR B 738     -24.122   3.802 -12.830  1.00  9.55           C  
ANISOU 3742  C   THR B 738      623   1405   1600   -123    132    243       C  
ATOM   3743  O   THR B 738     -23.495   2.890 -13.396  1.00  9.14           O  
ANISOU 3743  O   THR B 738      620   1349   1504   -161    110    251       O  
ATOM   3744  CB  THR B 738     -26.558   4.099 -13.336  1.00 10.81           C  
ANISOU 3744  CB  THR B 738      642   1618   1848   -100     89    271       C  
ATOM   3745  OG1 THR B 738     -26.892   4.258 -11.948  1.00 12.89           O  
ANISOU 3745  OG1 THR B 738      869   1896   2134    -88    162    241       O  
ATOM   3746  CG2 THR B 738     -26.668   2.630 -13.728  1.00 11.91           C  
ANISOU 3746  CG2 THR B 738      793   1781   1951   -166     59    278       C  
ATOM   3747  N   GLN B 739     -23.955   4.119 -11.552  1.00  9.80           N  
ANISOU 3747  N   GLN B 739      652   1435   1638   -109    186    212       N  
ATOM   3748  CA  GLN B 739     -23.190   3.271 -10.649  1.00  9.82           C  
ANISOU 3748  CA  GLN B 739      699   1439   1594   -143    216    191       C  
ATOM   3749  C   GLN B 739     -24.069   2.097 -10.224  1.00 10.15           C  
ANISOU 3749  C   GLN B 739      707   1523   1627   -186    230    199       C  
ATOM   3750  O   GLN B 739     -25.278   2.266 -10.009  1.00 12.25           O  
ANISOU 3750  O   GLN B 739      902   1820   1931   -177    247    202       O  
ATOM   3751  CB  GLN B 739     -22.753   4.068  -9.422  1.00 10.03           C  
ANISOU 3751  CB  GLN B 739      741   1451   1620   -112    261    154       C  
ATOM   3752  CG  GLN B 739     -21.849   3.309  -8.453  1.00 10.63           C  
ANISOU 3752  CG  GLN B 739      871   1526   1643   -141    280    135       C  
ATOM   3753  CD  GLN B 739     -21.351   4.193  -7.328  1.00 13.12           C  
ANISOU 3753  CD  GLN B 739     1211   1822   1951   -109    309     92       C  
ATOM   3754  OE1 GLN B 739     -20.832   5.285  -7.571  1.00 17.22           O  
ANISOU 3754  OE1 GLN B 739     1739   2301   2501    -76    297     77       O  
ATOM   3755  NE2 GLN B 739     -21.525   3.740  -6.094  1.00 12.10           N  
ANISOU 3755  NE2 GLN B 739     1097   1722   1780   -119    347     73       N  
ATOM   3756  N   ILE B 740     -23.458   0.919 -10.108  1.00  9.86           N  
ANISOU 3756  N   ILE B 740      715   1483   1547   -231    226    203       N  
ATOM   3757  CA  ILE B 740     -24.124  -0.276  -9.584  1.00 11.21           C  
ANISOU 3757  CA  ILE B 740      867   1683   1710   -280    244    213       C  
ATOM   3758  C   ILE B 740     -23.490  -0.644  -8.244  1.00 10.50           C  
ANISOU 3758  C   ILE B 740      822   1591   1576   -288    290    200       C  
ATOM   3759  O   ILE B 740     -22.280  -0.863  -8.154  1.00 10.12           O  
ANISOU 3759  O   ILE B 740      838   1514   1495   -289    276    193       O  
ATOM   3760  CB  ILE B 740     -24.014  -1.477 -10.571  1.00 11.39           C  
ANISOU 3760  CB  ILE B 740      912   1696   1721   -329    195    232       C  
ATOM   3761  CG1 ILE B 740     -24.638  -1.135 -11.943  1.00 14.01           C  
ANISOU 3761  CG1 ILE B 740     1210   2032   2080   -321    138    244       C  
ATOM   3762  CG2 ILE B 740     -24.613  -2.746  -9.968  1.00 12.69           C  
ANISOU 3762  CG2 ILE B 740     1062   1877   1884   -385    215    245       C  
ATOM   3763  CD1 ILE B 740     -26.113  -0.803 -11.937  1.00 17.05           C  
ANISOU 3763  CD1 ILE B 740     1502   2454   2522   -317    135    254       C  
ATOM   3764  N   GLY B 741     -24.322  -0.707  -7.203  1.00 11.46           N  
ANISOU 3764  N   GLY B 741      910   1746   1697   -292    345    199       N  
ATOM   3765  CA  GLY B 741     -23.831  -1.022  -5.871  1.00 11.73           C  
ANISOU 3765  CA  GLY B 741      994   1785   1676   -298    389    191       C  
ATOM   3766  C   GLY B 741     -23.047   0.096  -5.223  1.00 11.65           C  
ANISOU 3766  C   GLY B 741     1023   1760   1643   -248    400    152       C  
ATOM   3767  O   GLY B 741     -23.034   1.243  -5.704  1.00 12.03           O  
ANISOU 3767  O   GLY B 741     1049   1792   1728   -206    387    132       O  
ATOM   3768  N   GLY B 742     -22.420  -0.233  -4.102  1.00 11.49           N  
ANISOU 3768  N   GLY B 742     1063   1741   1562   -254    419    143       N  
ATOM   3769  CA  GLY B 742     -21.611   0.730  -3.374  1.00 11.00           C  
ANISOU 3769  CA  GLY B 742     1046   1662   1473   -214    419    100       C  
ATOM   3770  C   GLY B 742     -20.136   0.610  -3.699  1.00 10.44           C  
ANISOU 3770  C   GLY B 742     1027   1546   1393   -217    359     96       C  
ATOM   3771  O   GLY B 742     -19.755   0.070  -4.743  1.00  9.86           O  
ANISOU 3771  O   GLY B 742      948   1452   1347   -237    321    121       O  
ATOM   3772  N   LEU B 743     -19.312   1.140  -2.805  1.00 11.11           N  
ANISOU 3772  N   LEU B 743     1161   1618   1443   -195    350     61       N  
ATOM   3773  CA  LEU B 743     -17.860   1.072  -2.966  1.00 11.60           C  
ANISOU 3773  CA  LEU B 743     1262   1637   1507   -197    292     55       C  
ATOM   3774  C   LEU B 743     -17.332  -0.228  -2.359  1.00 11.01           C  
ANISOU 3774  C   LEU B 743     1236   1568   1381   -228    274     83       C  
ATOM   3775  O   LEU B 743     -17.756  -0.639  -1.263  1.00 13.01           O  
ANISOU 3775  O   LEU B 743     1521   1852   1570   -236    304     88       O  
ATOM   3776  CB  LEU B 743     -17.189   2.305  -2.341  1.00 12.17           C  
ANISOU 3776  CB  LEU B 743     1358   1686   1580   -162    276      1       C  
ATOM   3777  CG  LEU B 743     -16.996   3.527  -3.259  1.00 15.29           C  
ANISOU 3777  CG  LEU B 743     1717   2042   2050   -136    263    -18       C  
ATOM   3778  CD1 LEU B 743     -18.284   3.964  -3.964  1.00 16.41           C  
ANISOU 3778  CD1 LEU B 743     1803   2202   2231   -121    301     -5       C  
ATOM   3779  CD2 LEU B 743     -16.402   4.681  -2.456  1.00 15.89           C  
ANISOU 3779  CD2 LEU B 743     1821   2090   2127   -107    248    -76       C  
ATOM   3780  N   ILE B 744     -16.421  -0.870  -3.087  1.00 10.24           N  
ANISOU 3780  N   ILE B 744     1144   1437   1310   -242    230    104       N  
ATOM   3781  CA AILE B 744     -15.932  -2.162  -2.600  0.50 10.02           C  
ANISOU 3781  CA AILE B 744     1159   1404   1245   -268    210    135       C  
ATOM   3782  CA BILE B 744     -15.834  -2.179  -2.790  0.50 10.31           C  
ANISOU 3782  CA BILE B 744     1191   1435   1291   -268    205    136       C  
ATOM   3783  C   ILE B 744     -14.612  -2.070  -1.854  1.00 10.25           C  
ANISOU 3783  C   ILE B 744     1232   1409   1255   -253    158    118       C  
ATOM   3784  O   ILE B 744     -14.208  -3.030  -1.198  1.00 11.01           O  
ANISOU 3784  O   ILE B 744     1370   1501   1311   -265    135    144       O  
ATOM   3785  CB AILE B 744     -15.911  -3.277  -3.671  0.50  9.68           C  
ANISOU 3785  CB AILE B 744     1102   1341   1236   -296    199    172       C  
ATOM   3786  CB BILE B 744     -15.439  -2.851  -4.148  0.50 10.03           C  
ANISOU 3786  CB BILE B 744     1136   1368   1308   -283    184    158       C  
ATOM   3787  CG1AILE B 744     -14.855  -2.994  -4.738  0.50  9.31           C  
ANISOU 3787  CG1AILE B 744     1041   1252   1243   -282    164    160       C  
ATOM   3788  CG1BILE B 744     -16.700  -3.267  -4.930  0.50 10.51           C  
ANISOU 3788  CG1BILE B 744     1161   1450   1383   -308    215    180       C  
ATOM   3789  CG2AILE B 744     -17.305  -3.467  -4.273  0.50  9.17           C  
ANISOU 3789  CG2AILE B 744      995   1303   1185   -318    238    189       C  
ATOM   3790  CG2BILE B 744     -14.503  -4.029  -3.948  0.50 10.95           C  
ANISOU 3790  CG2BILE B 744     1290   1455   1417   -296    148    182       C  
ATOM   3791  CD1AILE B 744     -14.608  -4.171  -5.659  0.50  8.70           C  
ANISOU 3791  CD1AILE B 744      967   1149   1188   -303    152    186       C  
ATOM   3792  CD1BILE B 744     -16.458  -3.633  -6.396  0.50 11.81           C  
ANISOU 3792  CD1BILE B 744     1310   1588   1591   -316    195    189       C  
ATOM   3793  N   ASP B 745     -13.986  -0.898  -1.875  1.00  9.21           N  
ANISOU 3793  N   ASP B 745     1090   1258   1153   -226    135     75       N  
ATOM   3794  CA  ASP B 745     -12.802  -0.628  -1.063  1.00  9.39           C  
ANISOU 3794  CA  ASP B 745     1146   1259   1163   -213     78     50       C  
ATOM   3795  C   ASP B 745     -12.701   0.873  -0.825  1.00  9.05           C  
ANISOU 3795  C   ASP B 745     1094   1207   1139   -188     75     -7       C  
ATOM   3796  O   ASP B 745     -13.592   1.625  -1.233  1.00  9.03           O  
ANISOU 3796  O   ASP B 745     1062   1215   1155   -177    121    -21       O  
ATOM   3797  CB  ASP B 745     -11.525  -1.216  -1.709  1.00  8.84           C  
ANISOU 3797  CB  ASP B 745     1062   1146   1150   -217     28     68       C  
ATOM   3798  CG  ASP B 745     -11.113  -0.512  -2.997  1.00  8.51           C  
ANISOU 3798  CG  ASP B 745      967   1073   1195   -210     35     58       C  
ATOM   3799  OD1 ASP B 745     -11.838   0.392  -3.488  1.00  8.35           O  
ANISOU 3799  OD1 ASP B 745      921   1059   1191   -203     71     43       O  
ATOM   3800  OD2 ASP B 745     -10.027  -0.868  -3.521  1.00  9.51           O  
ANISOU 3800  OD2 ASP B 745     1076   1164   1374   -210      5     67       O  
ATOM   3801  N   SER B 746     -11.648   1.300  -0.132  1.00  8.99           N  
ANISOU 3801  N   SER B 746     1110   1175   1129   -178     15    -41       N  
ATOM   3802  CA  SER B 746     -11.461   2.713   0.178  1.00  9.81           C  
ANISOU 3802  CA  SER B 746     1212   1260   1256   -158      2   -102       C  
ATOM   3803  C   SER B 746      -9.984   3.006   0.183  1.00  9.38           C  
ANISOU 3803  C   SER B 746     1147   1158   1260   -160    -74   -122       C  
ATOM   3804  O   SER B 746      -9.222   2.325   0.851  1.00 10.18           O  
ANISOU 3804  O   SER B 746     1277   1260   1332   -165   -133   -114       O  
ATOM   3805  CB  SER B 746     -12.059   3.055   1.545  1.00 10.84           C  
ANISOU 3805  CB  SER B 746     1403   1424   1290   -144     15   -143       C  
ATOM   3806  OG  SER B 746     -11.859   4.417   1.869  1.00 14.80           O  
ANISOU 3806  OG  SER B 746     1909   1899   1815   -123     -1   -211       O  
ATOM   3807  N   LYS B 747      -9.583   4.016  -0.582  1.00  9.39           N  
ANISOU 3807  N   LYS B 747     1173    872   1523   -461    381   -208       N  
ATOM   3808  CA  LYS B 747      -8.167   4.342  -0.740  1.00  9.22           C  
ANISOU 3808  CA  LYS B 747     1205    840   1457   -402    296   -197       C  
ATOM   3809  C   LYS B 747      -8.025   5.754  -1.269  1.00  8.75           C  
ANISOU 3809  C   LYS B 747     1059    820   1444   -339    297   -181       C  
ATOM   3810  O   LYS B 747      -8.998   6.499  -1.343  1.00  8.61           O  
ANISOU 3810  O   LYS B 747      958    822   1493   -331    349   -182       O  
ATOM   3811  CB  LYS B 747      -7.472   3.330  -1.656  1.00  9.72           C  
ANISOU 3811  CB  LYS B 747     1270    917   1506   -389    198   -204       C  
ATOM   3812  CG  LYS B 747      -8.118   3.199  -3.001  1.00 10.03           C  
ANISOU 3812  CG  LYS B 747     1207   1021   1584   -383    176   -199       C  
ATOM   3813  CD  LYS B 747      -7.947   1.795  -3.574  1.00 12.28           C  
ANISOU 3813  CD  LYS B 747     1527   1297   1841   -404    112   -217       C  
ATOM   3814  CE  LYS B 747      -8.752   1.643  -4.847  1.00 12.60           C  
ANISOU 3814  CE  LYS B 747     1499   1381   1906   -412     77   -208       C  
ATOM   3815  NZ  LYS B 747      -8.544   0.313  -5.446  0.50  5.98           N  
ANISOU 3815  NZ  LYS B 747      711    529   1031   -430     13   -231       N  
ATOM   3816  N   GLY B 748      -6.804   6.130  -1.627  1.00  8.21           N  
ANISOU 3816  N   GLY B 748     1008    753   1358   -296    236   -174       N  
ATOM   3817  CA  GLY B 748      -6.548   7.509  -2.012  1.00  7.27           C  
ANISOU 3817  CA  GLY B 748      841    656   1266   -252    235   -154       C  
ATOM   3818  C   GLY B 748      -5.640   7.586  -3.219  1.00  5.95           C  
ANISOU 3818  C   GLY B 748      645    524   1093   -236    186   -151       C  
ATOM   3819  O   GLY B 748      -4.965   6.610  -3.561  1.00  6.40           O  
ANISOU 3819  O   GLY B 748      718    578   1137   -245    162   -179       O  
ATOM   3820  N   TYR B 749      -5.673   8.743  -3.876  1.00  5.83           N  
ANISOU 3820  N   TYR B 749      597    532   1087   -220    179   -125       N  
ATOM   3821  CA  TYR B 749      -4.701   9.087  -4.917  1.00  5.72           C  
ANISOU 3821  CA  TYR B 749      587    538   1047   -228    168   -122       C  
ATOM   3822  C   TYR B 749      -3.580   9.907  -4.308  1.00  6.00           C  
ANISOU 3822  C   TYR B 749      633    541   1104   -212    175   -121       C  
ATOM   3823  O   TYR B 749      -3.838  10.784  -3.482  1.00  6.79           O  
ANISOU 3823  O   TYR B 749      747    613   1218   -189    170    -99       O  
ATOM   3824  CB  TYR B 749      -5.327   9.971  -5.998  1.00  6.13           C  
ANISOU 3824  CB  TYR B 749      640    608   1080   -241    135    -85       C  
ATOM   3825  CG  TYR B 749      -6.464   9.373  -6.794  1.00  6.26           C  
ANISOU 3825  CG  TYR B 749      650    636   1093   -259     85    -79       C  
ATOM   3826  CD1 TYR B 749      -6.431   8.044  -7.251  1.00  6.18           C  
ANISOU 3826  CD1 TYR B 749      656    641   1052   -285     88   -108       C  
ATOM   3827  CD2 TYR B 749      -7.560  10.158  -7.135  1.00  6.84           C  
ANISOU 3827  CD2 TYR B 749      699    687   1211   -249     12    -49       C  
ATOM   3828  CE1 TYR B 749      -7.485   7.512  -8.003  1.00  6.43           C  
ANISOU 3828  CE1 TYR B 749      690    670   1085   -307     20    -98       C  
ATOM   3829  CE2 TYR B 749      -8.605   9.646  -7.894  1.00  7.17           C  
ANISOU 3829  CE2 TYR B 749      729    718   1279   -266    -69    -44       C  
ATOM   3830  CZ  TYR B 749      -8.568   8.336  -8.324  1.00  7.27           C  
ANISOU 3830  CZ  TYR B 749      767    749   1248   -299    -65    -64       C  
ATOM   3831  OH  TYR B 749      -9.609   7.872  -9.090  1.00  8.20           O  
ANISOU 3831  OH  TYR B 749      880    840   1395   -320   -168    -55       O  
ATOM   3832  N   GLY B 750      -2.348   9.614  -4.722  1.00  4.74           N  
ANISOU 3832  N   GLY B 750      504    373    925    -50    209    213       N  
ATOM   3833  CA  GLY B 750      -1.194  10.396  -4.261  1.00  5.36           C  
ANISOU 3833  CA  GLY B 750      597    473    967    -43    176    223       C  
ATOM   3834  C   GLY B 750      -0.299  10.770  -5.418  1.00  6.08           C  
ANISOU 3834  C   GLY B 750      654    605   1052    -57    136    225       C  
ATOM   3835  O   GLY B 750      -0.392  10.189  -6.501  1.00  6.90           O  
ANISOU 3835  O   GLY B 750      731    723   1168    -67    136    218       O  
ATOM   3836  N   VAL B 751       0.568  11.756  -5.194  1.00  5.59           N  
ANISOU 3836  N   VAL B 751      593    563    968    -64    105    230       N  
ATOM   3837  CA  VAL B 751       1.618  12.082  -6.150  1.00  5.87           C  
ANISOU 3837  CA  VAL B 751      599    641    991    -83     75    231       C  
ATOM   3838  C   VAL B 751       2.723  11.036  -5.985  1.00  6.08           C  
ANISOU 3838  C   VAL B 751      619    691   1000    -60     74    224       C  
ATOM   3839  O   VAL B 751       3.146  10.750  -4.862  1.00  6.90           O  
ANISOU 3839  O   VAL B 751      748    785   1087    -33     71    227       O  
ATOM   3840  CB  VAL B 751       2.159  13.489  -5.911  1.00  5.60           C  
ANISOU 3840  CB  VAL B 751      569    614    945   -104     47    236       C  
ATOM   3841  CG1 VAL B 751       3.403  13.752  -6.771  1.00  7.63           C  
ANISOU 3841  CG1 VAL B 751      794    918   1186   -130     24    236       C  
ATOM   3842  CG2 VAL B 751       1.078  14.513  -6.232  1.00  6.27           C  
ANISOU 3842  CG2 VAL B 751      659    670   1055   -121     44    244       C  
ATOM   3843  N   GLY B 752       3.149  10.423  -7.083  1.00  5.72           N  
ANISOU 3843  N   GLY B 752      542    674    958    -67     76    214       N  
ATOM   3844  CA  GLY B 752       4.221   9.424  -7.013  1.00  6.53           C  
ANISOU 3844  CA  GLY B 752      631    797   1054    -38     75    202       C  
ATOM   3845  C   GLY B 752       5.582  10.042  -7.233  1.00  6.88           C  
ANISOU 3845  C   GLY B 752      640    890   1084    -52     48    194       C  
ATOM   3846  O   GLY B 752       5.729  10.950  -8.036  1.00  6.97           O  
ANISOU 3846  O   GLY B 752      632    927   1091    -94     42    195       O  
ATOM   3847  N   THR B 753       6.574   9.555  -6.497  1.00  7.01           N  
ANISOU 3847  N   THR B 753      649    919   1095    -17     32    187       N  
ATOM   3848  CA  THR B 753       7.967   9.945  -6.706  1.00  7.59           C  
ANISOU 3848  CA  THR B 753      675   1045   1164    -26      8    171       C  
ATOM   3849  C   THR B 753       8.830   8.699  -6.614  1.00  8.34           C  
ANISOU 3849  C   THR B 753      744   1153   1271     25      4    153       C  
ATOM   3850  O   THR B 753       8.432   7.711  -6.012  1.00  7.79           O  
ANISOU 3850  O   THR B 753      710   1043   1206     70      9    161       O  
ATOM   3851  CB  THR B 753       8.462  10.969  -5.651  1.00  7.97           C  
ANISOU 3851  CB  THR B 753      734   1100   1196    -34    -28    178       C  
ATOM   3852  OG1 THR B 753       8.613  10.326  -4.372  1.00  9.60           O  
ANISOU 3852  OG1 THR B 753      972   1285   1391     17    -48    184       O  
ATOM   3853  CG2 THR B 753       7.514  12.163  -5.533  1.00  8.67           C  
ANISOU 3853  CG2 THR B 753      858   1160   1278    -73    -24    195       C  
ATOM   3854  N   PRO B 754      10.033   8.729  -7.207  1.00  8.26           N  
ANISOU 3854  N   PRO B 754      672   1197   1271     18     -2    126       N  
ATOM   3855  CA  PRO B 754      10.912   7.562  -7.025  1.00  9.48           C  
ANISOU 3855  CA  PRO B 754      796   1361   1446     78    -12    105       C  
ATOM   3856  C   PRO B 754      11.298   7.385  -5.552  1.00 10.10           C  
ANISOU 3856  C   PRO B 754      900   1421   1517    128    -59    121       C  
ATOM   3857  O   PRO B 754      11.337   8.378  -4.813  1.00 10.43           O  
ANISOU 3857  O   PRO B 754      958   1469   1536    105    -87    134       O  
ATOM   3858  CB  PRO B 754      12.148   7.923  -7.865  1.00  9.80           C  
ANISOU 3858  CB  PRO B 754      754   1470   1498     52     -8     69       C  
ATOM   3859  CG  PRO B 754      11.669   8.994  -8.822  1.00  9.48           C  
ANISOU 3859  CG  PRO B 754      716   1447   1438    -26     18     76       C  
ATOM   3860  CD  PRO B 754      10.647   9.769  -8.058  1.00  8.59           C  
ANISOU 3860  CD  PRO B 754      668   1290   1307    -42      2    113       C  
ATOM   3861  N   ILE B 755      11.563   6.147  -5.124  1.00 10.92           N  
ANISOU 3861  N   ILE B 755     1014   1500   1635    195    -70    120       N  
ATOM   3862  CA  ILE B 755      12.024   5.906  -3.746  1.00 12.78           C  
ANISOU 3862  CA  ILE B 755     1278   1720   1856    247   -123    138       C  
ATOM   3863  C   ILE B 755      13.225   6.791  -3.451  1.00 13.30           C  
ANISOU 3863  C   ILE B 755     1284   1849   1920    235   -172    119       C  
ATOM   3864  O   ILE B 755      14.149   6.880  -4.257  1.00 13.29           O  
ANISOU 3864  O   ILE B 755     1200   1900   1948    225   -168     83       O  
ATOM   3865  CB  ILE B 755      12.382   4.410  -3.478  1.00 13.78           C  
ANISOU 3865  CB  ILE B 755     1417   1813   2007    328   -136    139       C  
ATOM   3866  CG1 ILE B 755      11.105   3.593  -3.245  1.00 15.34           C  
ANISOU 3866  CG1 ILE B 755     1700   1933   2194    338    -98    170       C  
ATOM   3867  CG2 ILE B 755      13.321   4.263  -2.250  1.00 15.08           C  
ANISOU 3867  CG2 ILE B 755     1584   1985   2159    386   -210    151       C  
ATOM   3868  CD1 ILE B 755      11.328   2.090  -3.133  1.00 17.65           C  
ANISOU 3868  CD1 ILE B 755     2013   2177   2515    409   -101    172       C  
ATOM   3869  N   GLY B 756      13.199   7.443  -2.293  1.00 13.41           N  
ANISOU 3869  N   GLY B 756     1339   1858   1900    232   -214    139       N  
ATOM   3870  CA  GLY B 756      14.289   8.316  -1.885  1.00 13.78           C  
ANISOU 3870  CA  GLY B 756     1333   1960   1942    216   -266    118       C  
ATOM   3871  C   GLY B 756      14.210   9.735  -2.408  1.00 14.01           C  
ANISOU 3871  C   GLY B 756     1338   2018   1966    131   -247    106       C  
ATOM   3872  O   GLY B 756      15.088  10.544  -2.121  1.00 15.40           O  
ANISOU 3872  O   GLY B 756     1470   2239   2142    105   -285     85       O  
ATOM   3873  N   SER B 757      13.151  10.046  -3.158  1.00 12.97           N  
ANISOU 3873  N   SER B 757     1238   1859   1832     89   -191    119       N  
ATOM   3874  CA  SER B 757      12.996  11.366  -3.751  1.00 13.81           C  
ANISOU 3874  CA  SER B 757     1331   1982   1935     11   -173    114       C  
ATOM   3875  C   SER B 757      13.063  12.462  -2.696  1.00 14.58           C  
ANISOU 3875  C   SER B 757     1459   2075   2006    -14   -212    118       C  
ATOM   3876  O   SER B 757      12.400  12.356  -1.663  1.00 14.66           O  
ANISOU 3876  O   SER B 757     1539   2045   1988     13   -224    138       O  
ATOM   3877  CB  SER B 757      11.654  11.480  -4.458  1.00 13.42           C  
ANISOU 3877  CB  SER B 757     1327   1891   1882    -16   -122    136       C  
ATOM   3878  OG  SER B 757      11.394  12.844  -4.754  1.00 14.71           O  
ANISOU 3878  OG  SER B 757     1497   2055   2037    -81   -116    140       O  
ATOM   3879  N   PRO B 758      13.843  13.527  -2.960  1.00 15.41           N  
ANISOU 3879  N   PRO B 758     1517   2220   2118    -70   -226     97       N  
ATOM   3880  CA  PRO B 758      13.896  14.663  -2.053  1.00 16.12           C  
ANISOU 3880  CA  PRO B 758     1637   2302   2185   -104   -260     94       C  
ATOM   3881  C   PRO B 758      12.683  15.584  -2.163  1.00 15.64           C  
ANISOU 3881  C   PRO B 758     1642   2189   2112   -145   -227    115       C  
ATOM   3882  O   PRO B 758      12.633  16.607  -1.469  1.00 17.63           O  
ANISOU 3882  O   PRO B 758     1925   2426   2348   -175   -248    109       O  
ATOM   3883  CB  PRO B 758      15.151  15.407  -2.514  1.00 16.46           C  
ANISOU 3883  CB  PRO B 758     1600   2404   2251   -158   -276     61       C  
ATOM   3884  CG  PRO B 758      15.205  15.145  -3.979  1.00 17.05           C  
ANISOU 3884  CG  PRO B 758     1628   2499   2351   -183   -223     59       C  
ATOM   3885  CD  PRO B 758      14.735  13.715  -4.125  1.00 16.05           C  
ANISOU 3885  CD  PRO B 758     1515   2355   2228   -111   -205     71       C  
ATOM   3886  N   TYR B 759      11.732  15.240  -3.034  1.00 14.39           N  
ANISOU 3886  N   TYR B 759     1502   2003   1964   -144   -180    136       N  
ATOM   3887  CA  TYR B 759      10.521  16.046  -3.203  1.00 12.91           C  
ANISOU 3887  CA  TYR B 759     1368   1765   1774   -173   -153    155       C  
ATOM   3888  C   TYR B 759       9.287  15.479  -2.505  1.00 11.79           C  
ANISOU 3888  C   TYR B 759     1290   1571   1619   -129   -135    173       C  
ATOM   3889  O   TYR B 759       8.350  16.217  -2.243  1.00 11.93           O  
ANISOU 3889  O   TYR B 759     1351   1546   1634   -144   -122    181       O  
ATOM   3890  CB  TYR B 759      10.204  16.271  -4.694  1.00 12.99           C  
ANISOU 3890  CB  TYR B 759     1356   1778   1802   -213   -117    166       C  
ATOM   3891  CG  TYR B 759      11.282  17.050  -5.420  1.00 13.66           C  
ANISOU 3891  CG  TYR B 759     1390   1907   1894   -274   -122    152       C  
ATOM   3892  CD1 TYR B 759      11.335  18.437  -5.335  1.00 14.66           C  
ANISOU 3892  CD1 TYR B 759     1535   2014   2020   -331   -133    155       C  
ATOM   3893  CD2 TYR B 759      12.257  16.393  -6.163  1.00 15.27           C  
ANISOU 3893  CD2 TYR B 759     1527   2168   2108   -276   -111    133       C  
ATOM   3894  CE1 TYR B 759      12.328  19.161  -5.995  1.00 14.40           C  
ANISOU 3894  CE1 TYR B 759     1459   2018   1993   -396   -131    143       C  
ATOM   3895  CE2 TYR B 759      13.267  17.105  -6.815  1.00 15.36           C  
ANISOU 3895  CE2 TYR B 759     1488   2223   2127   -340   -107    117       C  
ATOM   3896  CZ  TYR B 759      13.288  18.488  -6.719  1.00 15.45           C  
ANISOU 3896  CZ  TYR B 759     1523   2213   2135   -403   -116    124       C  
ATOM   3897  OH  TYR B 759      14.266  19.216  -7.359  1.00 17.54           O  
ANISOU 3897  OH  TYR B 759     1742   2517   2406   -475   -105    110       O  
ATOM   3898  N   ARG B 760       9.282  14.176  -2.206  1.00 11.33           N  
ANISOU 3898  N   ARG B 760     1235   1514   1556    -75   -133    178       N  
ATOM   3899  CA  ARG B 760       8.061  13.534  -1.702  1.00  9.93           C  
ANISOU 3899  CA  ARG B 760     1116   1287   1371    -42   -103    196       C  
ATOM   3900  C   ARG B 760       7.523  14.201  -0.433  1.00  9.79           C  
ANISOU 3900  C   ARG B 760     1160   1236   1323    -42   -109    197       C  
ATOM   3901  O   ARG B 760       6.336  14.518  -0.347  1.00  9.31           O  
ANISOU 3901  O   ARG B 760     1136   1134   1268    -50    -74    204       O  
ATOM   3902  CB  ARG B 760       8.262  12.032  -1.456  1.00  9.97           C  
ANISOU 3902  CB  ARG B 760     1125   1291   1372     14   -102    203       C  
ATOM   3903  CG  ARG B 760       6.945  11.297  -1.090  1.00  9.86           C  
ANISOU 3903  CG  ARG B 760     1169   1223   1355     37    -60    222       C  
ATOM   3904  CD  ARG B 760       6.613  11.316   0.424  1.00 12.18           C  
ANISOU 3904  CD  ARG B 760     1535   1488   1606     57    -67    233       C  
ATOM   3905  NE  ARG B 760       7.626  10.586   1.190  1.00 13.64           N  
ANISOU 3905  NE  ARG B 760     1730   1690   1763    100   -111    238       N  
ATOM   3906  CZ  ARG B 760       7.608   9.274   1.411  1.00 15.51           C  
ANISOU 3906  CZ  ARG B 760     1992   1904   1996    146   -106    256       C  
ATOM   3907  NH1 ARG B 760       6.621   8.528   0.936  1.00 13.74           N  
ANISOU 3907  NH1 ARG B 760     1784   1641   1795    147    -52    267       N  
ATOM   3908  NH2 ARG B 760       8.592   8.704   2.091  1.00 13.45           N  
ANISOU 3908  NH2 ARG B 760     1739   1658   1713    190   -158    262       N  
ATOM   3909  N   ASP B 761       8.409  14.406   0.539  1.00 10.35           N  
ANISOU 3909  N   ASP B 761     1240   1329   1363    -33   -154    186       N  
ATOM   3910  CA  ASP B 761       7.999  14.980   1.825  1.00 10.71           C  
ANISOU 3910  CA  ASP B 761     1352   1348   1370    -34   -160    181       C  
ATOM   3911  C   ASP B 761       7.509  16.422   1.660  1.00 10.05           C  
ANISOU 3911  C   ASP B 761     1276   1242   1300    -82   -148    167       C  
ATOM   3912  O   ASP B 761       6.532  16.829   2.286  1.00  9.86           O  
ANISOU 3912  O   ASP B 761     1305   1177   1265    -83   -120    164       O  
ATOM   3913  CB  ASP B 761       9.131  14.923   2.858  1.00 11.58           C  
ANISOU 3913  CB  ASP B 761     1469   1491   1439    -17   -222    169       C  
ATOM   3914  CG  ASP B 761       9.466  13.501   3.301  1.00 13.70           C  
ANISOU 3914  CG  ASP B 761     1752   1766   1687     43   -240    188       C  
ATOM   3915  OD1 ASP B 761       8.557  12.650   3.285  1.00 16.06           O  
ANISOU 3915  OD1 ASP B 761     2089   2028   1986     68   -195    211       O  
ATOM   3916  OD2 ASP B 761      10.635  13.256   3.670  1.00 16.98           O  
ANISOU 3916  OD2 ASP B 761     2141   2222   2090     64   -301    179       O  
ATOM   3917  N   LYS B 762       8.172  17.185   0.792  1.00  9.85           N  
ANISOU 3917  N   LYS B 762     1200   1241   1302   -124   -165    157       N  
ATOM   3918  CA  LYS B 762       7.711  18.546   0.502  1.00 10.52           C  
ANISOU 3918  CA  LYS B 762     1296   1295   1407   -170   -154    150       C  
ATOM   3919  C   LYS B 762       6.341  18.548  -0.199  1.00  9.29           C  
ANISOU 3919  C   LYS B 762     1153   1095   1281   -165   -107    168       C  
ATOM   3920  O   LYS B 762       5.501  19.401   0.078  1.00  9.55           O  
ANISOU 3920  O   LYS B 762     1221   1084   1325   -174    -91    162       O  
ATOM   3921  CB  LYS B 762       8.738  19.289  -0.350  1.00 11.60           C  
ANISOU 3921  CB  LYS B 762     1380   1464   1564   -221   -178    142       C  
ATOM   3922  CG  LYS B 762      10.058  19.568   0.334  1.00 15.38           C  
ANISOU 3922  CG  LYS B 762     1837   1985   2023   -238   -228    114       C  
ATOM   3923  CD  LYS B 762      11.119  19.913  -0.705  1.00 20.85           C  
ANISOU 3923  CD  LYS B 762     2458   2721   2742   -286   -238    108       C  
ATOM   3924  CE  LYS B 762      12.517  19.876  -0.113  1.00 24.32           C  
ANISOU 3924  CE  LYS B 762     2853   3217   3172   -294   -289     77       C  
ATOM   3925  NZ  LYS B 762      13.559  19.865  -1.179  1.00 26.71           N  
ANISOU 3925  NZ  LYS B 762     3073   3572   3504   -332   -286     68       N  
ATOM   3926  N   ILE B 763       6.123  17.588  -1.098  1.00  8.38           N  
ANISOU 3926  N   ILE B 763     1007    993   1183   -148    -88    187       N  
ATOM   3927  CA  ILE B 763       4.844  17.456  -1.791  1.00  8.26           C  
ANISOU 3927  CA  ILE B 763      997    944   1197   -143    -51    202       C  
ATOM   3928  C   ILE B 763       3.735  17.081  -0.801  1.00  7.47           C  
ANISOU 3928  C   ILE B 763      943    805   1090   -110    -18    198       C  
ATOM   3929  O   ILE B 763       2.660  17.672  -0.820  1.00  8.12           O  
ANISOU 3929  O   ILE B 763     1040    847   1197   -113      5    196       O  
ATOM   3930  CB  ILE B 763       4.927  16.457  -2.966  1.00  8.15           C  
ANISOU 3930  CB  ILE B 763      942    957   1198   -136    -39    215       C  
ATOM   3931  CG1AILE B 763       5.769  17.066  -4.092  0.50  9.00           C  
ANISOU 3931  CG1AILE B 763     1009   1098   1314   -180    -57    217       C  
ATOM   3932  CG1BILE B 763       5.824  17.001  -4.093  0.50  9.08           C  
ANISOU 3932  CG1BILE B 763     1017   1111   1323   -179    -58    217       C  
ATOM   3933  CG2 ILE B 763       3.531  16.109  -3.471  1.00  8.79           C  
ANISOU 3933  CG2 ILE B 763     1029   1004   1305   -125     -6    226       C  
ATOM   3934  CD1AILE B 763       6.370  16.053  -5.024  0.50  9.76           C  
ANISOU 3934  CD1AILE B 763     1060   1237   1410   -176    -51    218       C  
ATOM   3935  CD1BILE B 763       5.168  18.024  -5.015  0.50 10.13           C  
ANISOU 3935  CD1BILE B 763     1154   1218   1477   -215    -55    232       C  
ATOM   3936  N   THR B 764       4.016  16.127   0.085  1.00  7.75           N  
ANISOU 3936  N   THR B 764     1002    850   1092    -79    -16    198       N  
ATOM   3937  CA  THR B 764       3.074  15.802   1.152  1.00  7.76           C  
ANISOU 3937  CA  THR B 764     1056    816   1075    -56     20    195       C  
ATOM   3938  C   THR B 764       2.709  17.028   1.974  1.00  7.93           C  
ANISOU 3938  C   THR B 764     1115    811   1086    -72     24    173       C  
ATOM   3939  O   THR B 764       1.532  17.267   2.225  1.00  8.27           O  
ANISOU 3939  O   THR B 764     1178    817   1149    -67     67    164       O  
ATOM   3940  CB  THR B 764       3.640  14.714   2.055  1.00  7.42           C  
ANISOU 3940  CB  THR B 764     1046    787    985    -25     11    204       C  
ATOM   3941  OG1 THR B 764       3.522  13.465   1.373  1.00  7.66           O  
ANISOU 3941  OG1 THR B 764     1054    822   1035     -4     27    222       O  
ATOM   3942  CG2 THR B 764       2.907  14.658   3.414  1.00  8.47           C  
ANISOU 3942  CG2 THR B 764     1251    889   1078    -13     44    199       C  
ATOM   3943  N   ILE B 765       3.714  17.813   2.375  1.00  8.53           N  
ANISOU 3943  N   ILE B 765     1197    906   1138    -91    -20    158       N  
ATOM   3944  CA  ILE B 765       3.442  19.004   3.185  1.00  8.73           C  
ANISOU 3944  CA  ILE B 765     1262    903   1153   -107    -18    129       C  
ATOM   3945  C   ILE B 765       2.571  19.996   2.410  1.00  8.72           C  
ANISOU 3945  C   ILE B 765     1243    860   1209   -124      2    125       C  
ATOM   3946  O   ILE B 765       1.614  20.541   2.967  1.00  9.29           O  
ANISOU 3946  O   ILE B 765     1346    890   1292   -117     36    105       O  
ATOM   3947  CB  ILE B 765       4.757  19.634   3.716  1.00  9.45           C  
ANISOU 3947  CB  ILE B 765     1358   1023   1208   -131    -74    110       C  
ATOM   3948  CG1 ILE B 765       5.365  18.723   4.791  1.00  9.87           C  
ANISOU 3948  CG1 ILE B 765     1446   1107   1199   -103    -97    111       C  
ATOM   3949  CG2 ILE B 765       4.530  21.058   4.258  1.00  9.45           C  
ANISOU 3949  CG2 ILE B 765     1392    987   1211   -159    -75     76       C  
ATOM   3950  CD1 ILE B 765       6.854  18.937   5.014  1.00 10.41           C  
ANISOU 3950  CD1 ILE B 765     1491   1223   1242   -118   -166     99       C  
ATOM   3951  N   ALA B 766       2.892  20.205   1.128  1.00  8.31           N  
ANISOU 3951  N   ALA B 766     1143    820   1193   -144    -19    144       N  
ATOM   3952  CA  ALA B 766       2.074  21.079   0.275  1.00  8.46           C  
ANISOU 3952  CA  ALA B 766     1150    800   1266   -156    -10    150       C  
ATOM   3953  C   ALA B 766       0.639  20.574   0.099  1.00  8.63           C  
ANISOU 3953  C   ALA B 766     1166    793   1321   -125     34    154       C  
ATOM   3954  O   ALA B 766      -0.303  21.360   0.110  1.00  8.91           O  
ANISOU 3954  O   ALA B 766     1208    783   1395   -119     50    142       O  
ATOM   3955  CB  ALA B 766       2.743  21.282  -1.076  1.00  8.62           C  
ANISOU 3955  CB  ALA B 766     1129    843   1304   -187    -40    175       C  
ATOM   3956  N   ILE B 767       0.462  19.264  -0.045  1.00  8.24           N  
ANISOU 3956  N   ILE B 767     1101    768   1262   -106     54    168       N  
ATOM   3957  CA  ILE B 767      -0.886  18.702  -0.162  1.00  8.52           C  
ANISOU 3957  CA  ILE B 767     1127    781   1331    -83     98    167       C  
ATOM   3958  C   ILE B 767      -1.692  18.961   1.109  1.00  8.72           C  
ANISOU 3958  C   ILE B 767     1191    771   1350    -68    143    138       C  
ATOM   3959  O   ILE B 767      -2.854  19.373   1.045  1.00  9.24           O  
ANISOU 3959  O   ILE B 767     1245    803   1463    -57    173    123       O  
ATOM   3960  CB  ILE B 767      -0.839  17.209  -0.503  1.00  8.41           C  
ANISOU 3960  CB  ILE B 767     1095    794   1306    -71    113    184       C  
ATOM   3961  CG1 ILE B 767      -0.425  17.044  -1.967  1.00  9.62           C  
ANISOU 3961  CG1 ILE B 767     1203    974   1478    -86     82    205       C  
ATOM   3962  CG2 ILE B 767      -2.199  16.552  -0.265  1.00  8.82           C  
ANISOU 3962  CG2 ILE B 767     1146    820   1386    -54    168    176       C  
ATOM   3963  CD1 ILE B 767      -0.042  15.630  -2.343  1.00 10.41           C  
ANISOU 3963  CD1 ILE B 767     1288   1104   1564    -77     89    217       C  
ATOM   3964  N   LEU B 768      -1.067  18.750   2.267  1.00  8.52           N  
ANISOU 3964  N   LEU B 768     1213    759   1266    -66    146    127       N  
ATOM   3965  CA  LEU B 768      -1.744  19.040   3.534  1.00  8.55           C  
ANISOU 3965  CA  LEU B 768     1264    734   1249    -58    193     96       C  
ATOM   3966  C   LEU B 768      -2.123  20.509   3.646  1.00  9.40           C  
ANISOU 3966  C   LEU B 768     1377    803   1391    -64    190     64       C  
ATOM   3967  O   LEU B 768      -3.230  20.817   4.101  1.00 10.08           O  
ANISOU 3967  O   LEU B 768     1469    855   1505    -50    241     36       O  
ATOM   3968  CB  LEU B 768      -0.885  18.606   4.731  1.00  9.15           C  
ANISOU 3968  CB  LEU B 768     1400    834   1244    -57    184     93       C  
ATOM   3969  CG  LEU B 768      -0.619  17.102   4.846  1.00  8.53           C  
ANISOU 3969  CG  LEU B 768     1331    780   1129    -42    191    123       C  
ATOM   3970  CD1 LEU B 768       0.369  16.876   5.948  1.00  9.11           C  
ANISOU 3970  CD1 LEU B 768     1462    877   1122    -39    161    124       C  
ATOM   3971  CD2 LEU B 768      -1.903  16.318   5.123  1.00 10.27           C  
ANISOU 3971  CD2 LEU B 768     1562    975   1364    -32    266    123       C  
ATOM   3972  N   GLN B 769      -1.223  21.393   3.217  1.00  9.21           N  
ANISOU 3972  N   GLN B 769     1348    782   1369    -85    135     68       N  
ATOM   3973  CA  GLN B 769      -1.519  22.832   3.165  1.00 10.35           C  
ANISOU 3973  CA  GLN B 769     1500    880   1554    -93    126     43       C  
ATOM   3974  C   GLN B 769      -2.758  23.099   2.304  1.00 10.05           C  
ANISOU 3974  C   GLN B 769     1420    805   1595    -73    145     48       C  
ATOM   3975  O   GLN B 769      -3.691  23.791   2.737  1.00 10.48           O  
ANISOU 3975  O   GLN B 769     1481    813   1687    -54    177     14       O  
ATOM   3976  CB  GLN B 769      -0.319  23.612   2.628  1.00 11.05           C  
ANISOU 3976  CB  GLN B 769     1585    978   1637   -129     65     55       C  
ATOM   3977  CG  GLN B 769      -0.486  25.137   2.712  1.00 13.89           C  
ANISOU 3977  CG  GLN B 769     1967   1279   2032   -142     53     28       C  
ATOM   3978  CD  GLN B 769       0.637  25.912   2.040  1.00 15.91           C  
ANISOU 3978  CD  GLN B 769     2218   1538   2290   -186     -2     44       C  
ATOM   3979  OE1 GLN B 769       1.745  25.412   1.887  1.00 16.90           O  
ANISOU 3979  OE1 GLN B 769     2329   1717   2376   -210    -31     60       O  
ATOM   3980  NE2 GLN B 769       0.352  27.150   1.644  1.00 19.96           N  
ANISOU 3980  NE2 GLN B 769     2742   1991   2851   -197    -15     40       N  
ATOM   3981  N   LEU B 770      -2.770  22.545   1.096  1.00  9.14           N  
ANISOU 3981  N   LEU B 770     1259    711   1503    -74    122     86       N  
ATOM   3982  CA  LEU B 770      -3.886  22.743   0.173  1.00  9.79           C  
ANISOU 3982  CA  LEU B 770     1298    765   1656    -55    125     95       C  
ATOM   3983  C   LEU B 770      -5.194  22.178   0.709  1.00 10.41           C  
ANISOU 3983  C   LEU B 770     1360    831   1765    -25    187     69       C  
ATOM   3984  O   LEU B 770      -6.253  22.782   0.522  1.00 11.14           O  
ANISOU 3984  O   LEU B 770     1427    884   1923     -2    198     50       O  
ATOM   3985  CB  LEU B 770      -3.574  22.159  -1.204  1.00  9.13           C  
ANISOU 3985  CB  LEU B 770     1176    715   1578    -68     88    139       C  
ATOM   3986  CG  LEU B 770      -2.404  22.853  -1.905  1.00  9.68           C  
ANISOU 3986  CG  LEU B 770     1255    794   1628   -103     34    164       C  
ATOM   3987  CD1 LEU B 770      -1.947  22.041  -3.107  1.00 11.39           C  
ANISOU 3987  CD1 LEU B 770     1439   1057   1831   -119     11    200       C  
ATOM   3988  CD2 LEU B 770      -2.725  24.307  -2.296  1.00 10.48           C  
ANISOU 3988  CD2 LEU B 770     1369    838   1775   -106      5    166       C  
ATOM   3989  N   GLN B 771      -5.117  21.030   1.381  1.00 10.57           N  
ANISOU 3989  N   GLN B 771     1395    882   1740    -27    227     66       N  
ATOM   3990  CA  GLN B 771      -6.300  20.442   1.981  1.00 12.43           C  
ANISOU 3990  CA  GLN B 771     1619   1106   1996     -9    296     40       C  
ATOM   3991  C   GLN B 771      -6.849  21.355   3.066  1.00 12.41           C  
ANISOU 3991  C   GLN B 771     1646   1065   2003      3    339     -9       C  
ATOM   3992  O   GLN B 771      -8.034  21.694   3.067  1.00 12.63           O  
ANISOU 3992  O   GLN B 771     1638   1063   2096     24    376    -39       O  
ATOM   3993  CB  GLN B 771      -5.985  19.068   2.563  1.00 12.28           C  
ANISOU 3993  CB  GLN B 771     1628   1121   1918    -18    330     53       C  
ATOM   3994  CG  GLN B 771      -7.121  18.475   3.429  1.00 17.39           C  
ANISOU 3994  CG  GLN B 771     2279   1754   2573    -11    416     24       C  
ATOM   3995  CD  GLN B 771      -8.447  18.307   2.686  1.00 22.69           C  
ANISOU 3995  CD  GLN B 771     2878   2411   3331      0    442     12       C  
ATOM   3996  OE1 GLN B 771      -8.475  18.001   1.491  1.00 25.40           O  
ANISOU 3996  OE1 GLN B 771     3173   2767   3710     -1    400     37       O  
ATOM   3997  NE2 GLN B 771      -9.553  18.490   3.404  1.00 24.72           N  
ANISOU 3997  NE2 GLN B 771     3125   2646   3622      8    513    -31       N  
ATOM   3998  N   GLU B 772      -5.965  21.760   3.976  1.00 12.76           N  
ANISOU 3998  N   GLU B 772     1752   1113   1982    -11    332    -22       N  
ATOM   3999  CA  GLU B 772      -6.358  22.567   5.132  1.00 13.81           C  
ANISOU 3999  CA  GLU B 772     1927   1214   2108     -4    376    -75       C  
ATOM   4000  C   GLU B 772      -6.918  23.929   4.723  1.00 14.50           C  
ANISOU 4000  C   GLU B 772     1989   1247   2274     14    360   -102       C  
ATOM   4001  O   GLU B 772      -7.839  24.439   5.362  1.00 16.23           O  
ANISOU 4001  O   GLU B 772     2208   1431   2528     35    415   -153       O  
ATOM   4002  CB  GLU B 772      -5.185  22.722   6.098  1.00 13.63           C  
ANISOU 4002  CB  GLU B 772     1976   1209   1993    -27    357    -83       C  
ATOM   4003  CG  GLU B 772      -4.781  21.387   6.726  1.00 13.99           C  
ANISOU 4003  CG  GLU B 772     2057   1299   1960    -35    377    -60       C  
ATOM   4004  CD  GLU B 772      -3.602  21.482   7.672  1.00 15.39           C  
ANISOU 4004  CD  GLU B 772     2304   1500   2044    -53    345    -65       C  
ATOM   4005  OE1 GLU B 772      -3.133  22.613   7.963  1.00 15.93           O  
ANISOU 4005  OE1 GLU B 772     2395   1551   2106    -64    315    -95       O  
ATOM   4006  OE2 GLU B 772      -3.158  20.399   8.126  1.00 14.14           O  
ANISOU 4006  OE2 GLU B 772     2177   1375   1819    -54    347    -39       O  
ATOM   4007  N   GLU B 773      -6.375  24.492   3.644  1.00 14.51           N  
ANISOU 4007  N   GLU B 773     1970   1239   2304      8    288    -68       N  
ATOM   4008  CA  GLU B 773      -6.817  25.790   3.109  1.00 15.35           C  
ANISOU 4008  CA  GLU B 773     2060   1287   2486     26    259    -80       C  
ATOM   4009  C   GLU B 773      -8.108  25.682   2.300  1.00 14.93           C  
ANISOU 4009  C   GLU B 773     1936   1214   2521     62    268    -76       C  
ATOM   4010  O   GLU B 773      -8.665  26.704   1.890  1.00 15.81           O  
ANISOU 4010  O   GLU B 773     2031   1271   2705     89    245    -87       O  
ATOM   4011  CB  GLU B 773      -5.720  26.403   2.236  1.00 15.22           C  
ANISOU 4011  CB  GLU B 773     2056   1267   2459     -3    181    -38       C  
ATOM   4012  CG  GLU B 773      -4.520  26.944   3.005  1.00 16.97           C  
ANISOU 4012  CG  GLU B 773     2339   1492   2618    -38    163    -55       C  
ATOM   4013  CD  GLU B 773      -3.387  27.425   2.100  1.00 19.30           C  
ANISOU 4013  CD  GLU B 773     2638   1792   2902    -76     93    -13       C  
ATOM   4014  OE1 GLU B 773      -3.472  27.263   0.859  1.00 21.60           O  
ANISOU 4014  OE1 GLU B 773     2892   2090   3225    -77     61     33       O  
ATOM   4015  OE2 GLU B 773      -2.387  27.952   2.636  1.00 21.94           O  
ANISOU 4015  OE2 GLU B 773     3013   2128   3195   -110     73    -29       O  
ATOM   4016  N   GLY B 774      -8.574  24.461   2.056  1.00 14.12           N  
ANISOU 4016  N   GLY B 774     1795   1154   2417     64    295    -62       N  
ATOM   4017  CA  GLY B 774      -9.823  24.237   1.318  1.00 14.02           C  
ANISOU 4017  CA  GLY B 774     1708   1131   2488     94    301    -64       C  
ATOM   4018  C   GLY B 774      -9.662  24.233  -0.195  1.00 13.89           C  
ANISOU 4018  C   GLY B 774     1656   1124   2498     92    223    -10       C  
ATOM   4019  O   GLY B 774     -10.650  24.115  -0.925  1.00 13.98           O  
ANISOU 4019  O   GLY B 774     1605   1128   2578    117    211     -9       O  
ATOM   4020  N   LYS B 775      -8.423  24.341  -0.667  1.00 12.85           N  
ANISOU 4020  N   LYS B 775     1562   1010   2311     60    171     32       N  
ATOM   4021  CA ALYS B 775      -8.132  24.448  -2.097  0.50 13.00           C  
ANISOU 4021  CA ALYS B 775     1562   1038   2341     50     99     83       C  
ATOM   4022  CA BLYS B 775      -8.180  24.461  -2.104  0.50 12.90           C  
ANISOU 4022  CA BLYS B 775     1548   1023   2331     52    100     83       C  
ATOM   4023  C   LYS B 775      -8.424  23.155  -2.859  1.00 12.58           C  
ANISOU 4023  C   LYS B 775     1463   1035   2283     44    100    106       C  
ATOM   4024  O   LYS B 775      -8.910  23.179  -3.989  1.00 12.30           O  
ANISOU 4024  O   LYS B 775     1390   1000   2285     53     55    130       O  
ATOM   4025  CB ALYS B 775      -6.674  24.880  -2.310  0.50 13.04           C  
ANISOU 4025  CB ALYS B 775     1618   1053   2285     10     57    115       C  
ATOM   4026  CB BLYS B 775      -6.790  25.042  -2.394  0.50 12.89           C  
ANISOU 4026  CB BLYS B 775     1596   1024   2276     14     53    115       C  
ATOM   4027  CG ALYS B 775      -6.333  25.259  -3.739  0.50 13.94           C  
ANISOU 4027  CG ALYS B 775     1725   1165   2405     -7    -11    167       C  
ATOM   4028  CG BLYS B 775      -6.599  26.454  -1.842  0.50 13.93           C  
ANISOU 4028  CG BLYS B 775     1772   1095   2427     17     43     94       C  
ATOM   4029  CD ALYS B 775      -7.187  26.420  -4.212  0.50 16.20           C  
ANISOU 4029  CD ALYS B 775     2006   1385   2765     26    -47    170       C  
ATOM   4030  CD BLYS B 775      -5.333  27.105  -2.367  0.50 15.55           C  
ANISOU 4030  CD BLYS B 775     2017   1298   2594    -28     -9    129       C  
ATOM   4031  CE ALYS B 775      -7.057  26.629  -5.703  0.50 17.67           C  
ANISOU 4031  CE ALYS B 775     2187   1573   2952     12   -114    228       C  
ATOM   4032  CE BLYS B 775      -4.929  28.321  -1.532  0.50 17.79           C  
ANISOU 4032  CE BLYS B 775     2353   1526   2880    -37     -8     97       C  
ATOM   4033  NZ ALYS B 775      -8.025  27.642  -6.189  0.50 19.20           N  
ANISOU 4033  NZ ALYS B 775     2372   1700   3222     54   -158    236       N  
ATOM   4034  NZ BLYS B 775      -6.056  29.011  -0.843  0.50 19.83           N  
ANISOU 4034  NZ BLYS B 775     2611   1721   3203     11     23     49       N  
ATOM   4035  N   LEU B 776      -8.121  22.015  -2.237  1.00 12.28           N  
ANISOU 4035  N   LEU B 776     1433   1037   2195     28    147     97       N  
ATOM   4036  CA  LEU B 776      -8.402  20.734  -2.880  1.00 12.05           C  
ANISOU 4036  CA  LEU B 776     1366   1049   2165     20    154    112       C  
ATOM   4037  C   LEU B 776      -9.903  20.550  -3.097  1.00 12.76           C  
ANISOU 4037  C   LEU B 776     1392   1124   2332     46    175     86       C  
ATOM   4038  O   LEU B 776     -10.315  20.073  -4.148  1.00 12.53           O  
ANISOU 4038  O   LEU B 776     1319   1113   2328     45    142    103       O  
ATOM   4039  CB  LEU B 776      -7.808  19.560  -2.092  1.00 11.81           C  
ANISOU 4039  CB  LEU B 776     1365   1053   2071      1    201    109       C  
ATOM   4040  CG  LEU B 776      -6.289  19.539  -1.916  1.00 12.09           C  
ANISOU 4040  CG  LEU B 776     1449   1113   2033    -22    175    132       C  
ATOM   4041  CD1 LEU B 776      -5.878  18.273  -1.201  1.00 13.35           C  
ANISOU 4041  CD1 LEU B 776     1632   1301   2141    -29    215    131       C  
ATOM   4042  CD2 LEU B 776      -5.567  19.651  -3.269  1.00 13.04           C  
ANISOU 4042  CD2 LEU B 776     1554   1256   2144    -41    112    170       C  
ATOM   4043  N   HIS B 777     -10.705  20.962  -2.112  1.00 13.32           N  
ANISOU 4043  N   HIS B 777     1455   1163   2442     70    228     42       N  
ATOM   4044  CA  HIS B 777     -12.157  20.867  -2.202  1.00 15.22           C  
ANISOU 4044  CA  HIS B 777     1625   1391   2768     96    255      7       C  
ATOM   4045  C   HIS B 777     -12.661  21.748  -3.340  1.00 15.00           C  
ANISOU 4045  C   HIS B 777     1555   1339   2806    125    176     23       C  
ATOM   4046  O   HIS B 777     -13.512  21.330  -4.133  1.00 15.17           O  
ANISOU 4046  O   HIS B 777     1511   1374   2879    135    153     22       O  
ATOM   4047  CB  HIS B 777     -12.809  21.269  -0.875  1.00 16.25           C  
ANISOU 4047  CB  HIS B 777     1760   1492   2924    115    333    -49       C  
ATOM   4048  CG  HIS B 777     -14.303  21.193  -0.896  1.00 20.24           C  
ANISOU 4048  CG  HIS B 777     2181   1986   3524    141    370    -93       C  
ATOM   4049  ND1 HIS B 777     -14.986  19.997  -0.878  1.00 24.66           N  
ANISOU 4049  ND1 HIS B 777     2695   2576   4100    122    421   -108       N  
ATOM   4050  CD2 HIS B 777     -15.243  22.164  -0.964  1.00 24.33           C  
ANISOU 4050  CD2 HIS B 777     2648   2465   4133    187    360   -128       C  
ATOM   4051  CE1 HIS B 777     -16.286  20.234  -0.914  1.00 25.61           C  
ANISOU 4051  CE1 HIS B 777     2733   2682   4316    150    444   -153       C  
ATOM   4052  NE2 HIS B 777     -16.469  21.541  -0.968  1.00 25.45           N  
ANISOU 4052  NE2 HIS B 777     2706   2620   4345    194    406   -167       N  
ATOM   4053  N   MET B 778     -12.105  22.955  -3.428  1.00 14.89           N  
ANISOU 4053  N   MET B 778     1583   1287   2787    136    130     39       N  
ATOM   4054  CA  MET B 778     -12.454  23.906  -4.483  1.00 15.59           C  
ANISOU 4054  CA  MET B 778     1651   1342   2929    164     49     65       C  
ATOM   4055  C   MET B 778     -12.094  23.370  -5.861  1.00 14.47           C  
ANISOU 4055  C   MET B 778     1502   1241   2756    139    -18    118       C  
ATOM   4056  O   MET B 778     -12.835  23.546  -6.818  1.00 14.66           O  
ANISOU 4056  O   MET B 778     1482   1259   2830    162    -75    131       O  
ATOM   4057  CB  MET B 778     -11.738  25.235  -4.264  1.00 16.73           C  
ANISOU 4057  CB  MET B 778     1860   1436   3062    167     19     77       C  
ATOM   4058  CG  MET B 778     -12.326  26.096  -3.169  1.00 20.39           C  
ANISOU 4058  CG  MET B 778     2325   1844   3579    204     65     21       C  
ATOM   4059  SD  MET B 778     -11.519  27.707  -3.027  1.00 28.37           S  
ANISOU 4059  SD  MET B 778     3414   2782   4584    206     22     34       S  
ATOM   4060  CE  MET B 778     -11.306  28.150  -4.753  1.00 24.47           C  
ANISOU 4060  CE  MET B 778     2923   2277   4098    203    -89    112       C  
ATOM   4061  N   MET B 779     -10.940  22.719  -5.960  1.00 13.19           N  
ANISOU 4061  N   MET B 779     1383   1119   2509     94    -12    145       N  
ATOM   4062  CA  MET B 779     -10.497  22.199  -7.245  1.00 12.71           C  
ANISOU 4062  CA  MET B 779     1321   1099   2410     67    -66    189       C  
ATOM   4063  C   MET B 779     -11.394  21.061  -7.707  1.00 12.09           C  
ANISOU 4063  C   MET B 779     1179   1056   2360     69    -56    173       C  
ATOM   4064  O   MET B 779     -11.689  20.945  -8.901  1.00 11.48           O  
ANISOU 4064  O   MET B 779     1077    995   2289     67   -116    197       O  
ATOM   4065  CB  MET B 779      -9.049  21.737  -7.159  1.00 12.68           C  
ANISOU 4065  CB  MET B 779     1368   1131   2318     22    -53    212       C  
ATOM   4066  CG  MET B 779      -8.072  22.883  -7.102  1.00 14.03           C  
ANISOU 4066  CG  MET B 779     1597   1275   2460      7    -82    236       C  
ATOM   4067  SD  MET B 779      -6.461  22.312  -6.547  1.00 18.82           S  
ANISOU 4067  SD  MET B 779     2247   1924   2978    -38    -51    241       S  
ATOM   4068  CE  MET B 779      -6.261  20.919  -7.626  1.00 13.66           C  
ANISOU 4068  CE  MET B 779     1565   1335   2290    -60    -59    261       C  
ATOM   4069  N   LYS B 780     -11.830  20.232  -6.757  1.00 12.33           N  
ANISOU 4069  N   LYS B 780     1186   1096   2403     69     20    132       N  
ATOM   4070  CA  LYS B 780     -12.743  19.147  -7.087  1.00 12.75           C  
ANISOU 4070  CA  LYS B 780     1176   1177   2491     65     38    109       C  
ATOM   4071  C   LYS B 780     -14.062  19.714  -7.591  1.00 13.35           C  
ANISOU 4071  C   LYS B 780     1181   1232   2658    103     -3     91       C  
ATOM   4072  O   LYS B 780     -14.565  19.280  -8.628  1.00 13.44           O  
ANISOU 4072  O   LYS B 780     1149   1269   2690    100    -52     98       O  
ATOM   4073  CB  LYS B 780     -12.950  18.185  -5.914  1.00 13.20           C  
ANISOU 4073  CB  LYS B 780     1232   1242   2543     52    134     72       C  
ATOM   4074  CG  LYS B 780     -13.983  17.102  -6.215  1.00 16.15           C  
ANISOU 4074  CG  LYS B 780     1538   1637   2963     41    159     44       C  
ATOM   4075  CD  LYS B 780     -13.576  15.765  -5.680  1.00 18.68           C  
ANISOU 4075  CD  LYS B 780     1885   1977   3234      6    225     40       C  
ATOM   4076  CE  LYS B 780     -14.363  14.673  -6.374  1.00 18.94           C  
ANISOU 4076  CE  LYS B 780     1860   2033   3304    -15    228     22       C  
ATOM   4077  NZ  LYS B 780     -14.889  13.698  -5.391  1.00 21.97           N  
ANISOU 4077  NZ  LYS B 780     2237   2411   3701    -37    324    -11       N  
ATOM   4078  N   GLU B 781     -14.594  20.706  -6.884  1.00 13.48           N  
ANISOU 4078  N   GLU B 781     1187   1203   2732    142     13     65       N  
ATOM   4079  CA  GLU B 781     -15.832  21.353  -7.325  1.00 15.01           C  
ANISOU 4079  CA  GLU B 781     1309   1372   3024    190    -32     46       C  
ATOM   4080  C   GLU B 781     -15.701  21.986  -8.713  1.00 14.64           C  
ANISOU 4080  C   GLU B 781     1271   1319   2973    202   -146     98       C  
ATOM   4081  O   GLU B 781     -16.646  21.949  -9.502  1.00 15.40           O  
ANISOU 4081  O   GLU B 781     1302   1423   3128    226   -203     93       O  
ATOM   4082  CB  GLU B 781     -16.302  22.394  -6.308  1.00 16.12           C  
ANISOU 4082  CB  GLU B 781     1443   1457   3224    234      6      6       C  
ATOM   4083  CG  GLU B 781     -16.769  21.797  -4.995  1.00 20.39           C  
ANISOU 4083  CG  GLU B 781     1961   2004   3781    226    121    -53       C  
ATOM   4084  CD  GLU B 781     -17.905  22.577  -4.365  1.00 26.64           C  
ANISOU 4084  CD  GLU B 781     2693   2755   4675    278    153   -112       C  
ATOM   4085  OE1 GLU B 781     -17.769  23.808  -4.175  1.00 30.19           O  
ANISOU 4085  OE1 GLU B 781     3171   3152   5148    316    126   -112       O  
ATOM   4086  OE2 GLU B 781     -18.944  21.952  -4.059  1.00 30.35           O  
ANISOU 4086  OE2 GLU B 781     3083   3243   5207    280    210   -162       O  
ATOM   4087  N   LYS B 782     -14.529  22.552  -9.008  1.00 13.15           N  
ANISOU 4087  N   LYS B 782     1164   1120   2713    182   -180    148       N  
ATOM   4088  CA  LYS B 782     -14.292  23.198 -10.293  1.00 12.97           C  
ANISOU 4088  CA  LYS B 782     1168   1089   2671    185   -281    204       C  
ATOM   4089  C   LYS B 782     -14.395  22.206 -11.451  1.00 12.72           C  
ANISOU 4089  C   LYS B 782     1112   1116   2606    156   -323    222       C  
ATOM   4090  O   LYS B 782     -14.986  22.506 -12.486  1.00 13.36           O  
ANISOU 4090  O   LYS B 782     1169   1197   2710    175   -407    245       O  
ATOM   4091  CB  LYS B 782     -12.918  23.878 -10.303  1.00 12.36           C  
ANISOU 4091  CB  LYS B 782     1184    994   2518    154   -291    249       C  
ATOM   4092  CG  LYS B 782     -12.529  24.507 -11.639  1.00 12.61           C  
ANISOU 4092  CG  LYS B 782     1259   1019   2513    142   -384    315       C  
ATOM   4093  CD  LYS B 782     -11.149  25.166 -11.566  1.00 12.24           C  
ANISOU 4093  CD  LYS B 782     1299    955   2395    102   -380    353       C  
ATOM   4094  CE  LYS B 782     -10.663  25.539 -12.960  1.00 12.61           C  
ANISOU 4094  CE  LYS B 782     1395   1010   2388     73   -458    420       C  
ATOM   4095  NZ  LYS B 782      -9.322  26.157 -12.916  1.00 15.41           N  
ANISOU 4095  NZ  LYS B 782     1826   1351   2677     25   -447    454       N  
ATOM   4096  N   TRP B 783     -13.817  21.022 -11.267  1.00 12.17           N  
ANISOU 4096  N   TRP B 783     1051   1095   2478    110   -267    211       N  
ATOM   4097  CA  TRP B 783     -13.668  20.077 -12.369  1.00 12.39           C  
ANISOU 4097  CA  TRP B 783     1071   1177   2458     74   -300    227       C  
ATOM   4098  C   TRP B 783     -14.783  19.040 -12.458  1.00 13.21           C  
ANISOU 4098  C   TRP B 783     1093   1310   2617     76   -284    181       C  
ATOM   4099  O   TRP B 783     -14.988  18.449 -13.520  1.00 14.40           O  
ANISOU 4099  O   TRP B 783     1226   1499   2748     56   -333    188       O  
ATOM   4100  CB  TRP B 783     -12.271  19.432 -12.340  1.00 11.18           C  
ANISOU 4100  CB  TRP B 783      980   1057   2210     24   -261    246       C  
ATOM   4101  CG  TRP B 783     -11.223  20.431 -12.690  1.00 10.47           C  
ANISOU 4101  CG  TRP B 783      961    951   2065     11   -297    296       C  
ATOM   4102  CD1 TRP B 783     -10.384  21.075 -11.827  1.00 10.55           C  
ANISOU 4102  CD1 TRP B 783     1019    933   2056      7   -262    302       C  
ATOM   4103  CD2 TRP B 783     -10.952  20.968 -13.995  1.00 10.43           C  
ANISOU 4103  CD2 TRP B 783      990    953   2019     -4   -377    346       C  
ATOM   4104  NE1 TRP B 783      -9.584  21.961 -12.517  1.00 10.94           N  
ANISOU 4104  NE1 TRP B 783     1126    971   2061    -13   -311    352       N  
ATOM   4105  CE2 TRP B 783      -9.912  21.915 -13.848  1.00 11.00           C  
ANISOU 4105  CE2 TRP B 783     1130    999   2052    -21   -379    382       C  
ATOM   4106  CE3 TRP B 783     -11.473  20.727 -15.276  1.00 11.48           C  
ANISOU 4106  CE3 TRP B 783     1107   1114   2141     -9   -446    364       C  
ATOM   4107  CZ2 TRP B 783      -9.388  22.628 -14.936  1.00 11.83           C  
ANISOU 4107  CZ2 TRP B 783     1288   1101   2105    -45   -441    439       C  
ATOM   4108  CZ3 TRP B 783     -10.959  21.442 -16.354  1.00 11.74           C  
ANISOU 4108  CZ3 TRP B 783     1199   1146   2116    -29   -513    422       C  
ATOM   4109  CH2 TRP B 783      -9.923  22.371 -16.175  1.00 11.63           C  
ANISOU 4109  CH2 TRP B 783     1254   1103   2063    -49   -506    460       C  
ATOM   4110  N   TRP B 784     -15.501  18.832 -11.360  1.00 13.79           N  
ANISOU 4110  N   TRP B 784     1119   1366   2756     95   -214    131       N  
ATOM   4111  CA  TRP B 784     -16.644  17.908 -11.350  1.00 15.39           C  
ANISOU 4111  CA  TRP B 784     1236   1591   3022     92   -190     81       C  
ATOM   4112  C   TRP B 784     -17.973  18.641 -11.584  1.00 18.59           C  
ANISOU 4112  C   TRP B 784     1557   1974   3531    144   -243     57       C  
ATOM   4113  O   TRP B 784     -18.984  18.011 -11.881  1.00 20.21           O  
ANISOU 4113  O   TRP B 784     1680   2204   3796    142   -251     18       O  
ATOM   4114  CB  TRP B 784     -16.672  17.076 -10.055  1.00 13.97           C  
ANISOU 4114  CB  TRP B 784     1050   1409   2848     71    -73     39       C  
ATOM   4115  CG  TRP B 784     -15.860  15.779 -10.122  1.00 11.90           C  
ANISOU 4115  CG  TRP B 784      829   1180   2511     19    -31     47       C  
ATOM   4116  CD1 TRP B 784     -16.357  14.500 -10.184  1.00 10.73           C  
ANISOU 4116  CD1 TRP B 784      643   1056   2379    -14      9     14       C  
ATOM   4117  CD2 TRP B 784     -14.429  15.652 -10.144  1.00  9.12           C  
ANISOU 4117  CD2 TRP B 784      562    838   2065     -4    -27     86       C  
ATOM   4118  NE1 TRP B 784     -15.321  13.588 -10.240  1.00  8.78           N  
ANISOU 4118  NE1 TRP B 784      456    827   2054    -50     36     32       N  
ATOM   4119  CE2 TRP B 784     -14.130  14.265 -10.212  1.00  8.75           C  
ANISOU 4119  CE2 TRP B 784      523    817   1983    -43     15     75       C  
ATOM   4120  CE3 TRP B 784     -13.367  16.569 -10.096  1.00  9.57           C  
ANISOU 4120  CE3 TRP B 784      686    883   2069      3    -52    126       C  
ATOM   4121  CZ2 TRP B 784     -12.820  13.777 -10.248  1.00  9.14           C  
ANISOU 4121  CZ2 TRP B 784      639    883   1950    -66     28    101       C  
ATOM   4122  CZ3 TRP B 784     -12.061  16.080 -10.134  1.00  9.37           C  
ANISOU 4122  CZ3 TRP B 784      721    878   1960    -27    -37    151       C  
ATOM   4123  CH2 TRP B 784     -11.800  14.701 -10.207  1.00  9.11           C  
ANISOU 4123  CH2 TRP B 784      690    874   1898    -57      2    138       C  
ATOM   4124  N   ARG B 785     -17.949  19.966 -11.469  1.00 21.31           N  
ANISOU 4124  N   ARG B 785     1923   2272   3900    190   -283     78       N  
ATOM   4125  CA  ARG B 785     -19.135  20.789 -11.699  1.00 24.31           C  
ANISOU 4125  CA  ARG B 785     2229   2624   4385    251   -344     60       C  
ATOM   4126  C   ARG B 785     -20.270  20.285 -10.809  1.00 25.93           C  
ANISOU 4126  C   ARG B 785     2335   2833   4685    264   -264    -17       C  
ATOM   4127  O   ARG B 785     -20.023  19.906  -9.656  1.00 26.82           O  
ANISOU 4127  O   ARG B 785     2465   2941   4785    242   -155    -47       O  
ATOM   4128  CB  ARG B 785     -19.526  20.775 -13.184  1.00 24.70           C  
ANISOU 4128  CB  ARG B 785     2254   2700   4431    257   -465     90       C  
ATOM   4129  N   GLY B 786     -21.497  20.274 -11.338  1.00 27.74           N  
ANISOU 4129  N   GLY B 786     2461   3073   5006    295   -318    -49       N  
ATOM   4130  CA  GLY B 786     -22.663  19.813 -10.583  1.00 28.86           C  
ANISOU 4130  CA  GLY B 786     2493   3222   5249    303   -243   -127       C  
ATOM   4131  C   GLY B 786     -23.521  18.799 -11.323  1.00 29.37           C  
ANISOU 4131  C   GLY B 786     2465   3340   5355    276   -274   -160       C  
ATOM   4132  O   GLY B 786     -23.162  18.330 -12.411  1.00 29.61           O  
ANISOU 4132  O   GLY B 786     2523   3404   5323    246   -349   -123       O  
ATOM   4133  N   ASN B 787     -24.665  18.479 -10.722  1.00 30.05           N  
ANISOU 4133  N   ASN B 787     2440   3433   5546    283   -212   -233       N  
ATOM   4134  CA  ASN B 787     -25.599  17.484 -11.240  1.00 29.87           C  
ANISOU 4134  CA  ASN B 787     2313   3458   5579    250   -224   -280       C  
ATOM   4135  C   ASN B 787     -26.169  17.796 -12.630  1.00 29.85           C  
ANISOU 4135  C   ASN B 787     2253   3477   5610    284   -380   -264       C  
ATOM   4136  O   ASN B 787     -26.762  18.857 -12.856  1.00 31.09           O  
ANISOU 4136  O   ASN B 787     2361   3609   5844    359   -458   -264       O  
ATOM   4137  CB  ASN B 787     -26.743  17.261 -10.242  1.00 31.15           C  
ANISOU 4137  CB  ASN B 787     2359   3618   5857    254   -121   -365       C  
ATOM   4138  N   GLY B 788     -25.982  16.854 -13.550  1.00 28.18           N  
ANISOU 4138  N   GLY B 788     2053   3312   5341    229   -426   -252       N  
ATOM   4139  CA  GLY B 788     -26.524  16.949 -14.895  1.00 27.20           C  
ANISOU 4139  CA  GLY B 788     1880   3220   5234    247   -572   -241       C  
ATOM   4140  C   GLY B 788     -27.611  15.921 -15.161  1.00 26.55           C  
ANISOU 4140  C   GLY B 788     1672   3186   5228    208   -569   -314       C  
ATOM   4141  O   GLY B 788     -28.347  16.031 -16.144  1.00 28.06           O  
ANISOU 4141  O   GLY B 788     1791   3407   5464    230   -691   -324       O  
ATOM   4142  N   CYS B 789     -27.733  14.930 -14.276  1.00 24.94           N  
ANISOU 4142  N   CYS B 789     1444   2990   5042    149   -433   -365       N  
ATOM   4143  CA  CYS B 789     -28.664  13.813 -14.488  1.00 24.18           C  
ANISOU 4143  CA  CYS B 789     1240   2937   5012     93   -414   -436       C  
ATOM   4144  C   CYS B 789     -29.535  13.506 -13.270  1.00 24.52           C  
ANISOU 4144  C   CYS B 789     1184   2970   5164     78   -279   -513       C  
ATOM   4145  O   CYS B 789     -29.082  13.672 -12.135  1.00 24.06           O  
ANISOU 4145  O   CYS B 789     1182   2876   5085     78   -162   -506       O  
ATOM   4146  CB  CYS B 789     -27.884  12.546 -14.852  1.00 22.89           C  
ANISOU 4146  CB  CYS B 789     1159   2795   4742      6   -379   -422       C  
ATOM   4147  SG  CYS B 789     -26.867  12.673 -16.323  1.00 20.90           S  
ANISOU 4147  SG  CYS B 789     1021   2566   4354      4   -517   -345       S  
ATOM   4148  N   PRO B 790     -30.771  13.021 -13.498  1.00 25.36           N  
ANISOU 4148  N   PRO B 790     1143   3111   5382     59   -291   -587       N  
ATOM   4149  CA  PRO B 790     -31.608  12.580 -12.380  1.00 26.45           C  
ANISOU 4149  CA  PRO B 790     1185   3245   5621     28   -149   -666       C  
ATOM   4150  C   PRO B 790     -31.004  11.396 -11.623  1.00 26.18           C  
ANISOU 4150  C   PRO B 790     1235   3200   5513    -65     -2   -666       C  
ATOM   4151  O   PRO B 790     -31.447  11.076 -10.516  1.00 27.49           O  
ANISOU 4151  O   PRO B 790     1361   3352   5731    -96    138   -714       O  
ATOM   4152  CB  PRO B 790     -32.913  12.145 -13.061  1.00 27.46           C  
ANISOU 4152  CB  PRO B 790     1145   3421   5867     11   -214   -740       C  
ATOM   4153  CG  PRO B 790     -32.914  12.810 -14.381  1.00 27.55           C  
ANISOU 4153  CG  PRO B 790     1152   3453   5861     71   -405   -700       C  
ATOM   4154  CD  PRO B 790     -31.473  12.882 -14.788  1.00 25.85           C  
ANISOU 4154  CD  PRO B 790     1118   3219   5483     64   -438   -606       C  
ATOM   4155  OXT PRO B 790     -30.089  10.726 -12.103  1.00 25.76           O  
ANISOU 4155  OXT PRO B 790     1289   3149   5349   -109    -20   -620       O  
TER    4156      PRO B 790                                                      
HETATM 4157  CAA DYH A   1      -9.015  11.391  19.705  1.00  6.43           C  
ANISOU 4157  CAA DYH A   1      686    483   1274    304    325    203       C  
HETATM 4158  NH  DYH A   1      -9.992  12.471  19.803  1.00  5.53           N  
ANISOU 4158  NH  DYH A   1      555    499   1049    303    164    233       N  
HETATM 4159  CAH DYH A   1     -10.065  13.243  21.047  1.00  6.23           C  
ANISOU 4159  CAH DYH A   1      581    645   1140    443     88    254       C  
HETATM 4160  CAG DYH A   1     -11.201  14.251  20.977  1.00  6.09           C  
ANISOU 4160  CAG DYH A   1      521    651   1141    457     39    281       C  
HETATM 4161  OAC DYH A   1     -11.139  14.990  19.744  1.00  5.90           O  
ANISOU 4161  OAC DYH A   1      494    602   1145    385     -8    348       O  
HETATM 4162  CAP DYH A   1     -11.122  15.235  22.139  1.00  6.72           C  
ANISOU 4162  CAP DYH A   1      566    725   1264    530     81    189       C  
HETATM 4163  OAQ DYH A   1      -9.904  15.973  22.077  1.00  6.53           O  
ANISOU 4163  OAQ DYH A   1      576    665   1239    499     92    106       O  
HETATM 4164  CAR DYH A   1      -8.758  15.117  22.272  1.00  6.16           C  
ANISOU 4164  CAR DYH A   1      527    713   1102    474     60    126       C  
HETATM 4165  CAS DYH A   1      -7.528  15.885  21.837  1.00  7.19           C  
ANISOU 4165  CAS DYH A   1      677    826   1228    421     57     61       C  
HETATM 4166  CAI DYH A   1      -8.738  13.940  21.306  1.00  5.54           C  
ANISOU 4166  CAI DYH A   1      477    566   1063    471     72    208       C  
HETATM 4167  OAJ DYH A   1      -8.290  14.505  20.075  1.00  5.32           O  
ANISOU 4167  OAJ DYH A   1      499    470   1053    393     65    170       O  
HETATM 4168  CAK DYH A   1      -7.460  15.654  20.329  1.00  5.07           C  
ANISOU 4168  CAK DYH A   1      463    445   1017    394     44    105       C  
HETATM 4169  CAE DYH A   1      -8.051  16.861  19.609  1.00  5.57           C  
ANISOU 4169  CAE DYH A   1      553    415   1148    364     23    134       C  
HETATM 4170  OAB DYH A   1      -9.222  16.782  19.139  1.00  6.24           O  
ANISOU 4170  OAB DYH A   1      601    500   1271    366    -10    264       O  
HETATM 4171  OAF DYH A   1      -7.353  17.892  19.492  1.00  6.10           O  
ANISOU 4171  OAF DYH A   1      648    420   1249    328     45     76       O  
HETATM 4172  CB  DYH A   1      -6.025  15.357  19.905  1.00  5.54           C  
ANISOU 4172  CB  DYH A   1      509    520   1075    355     70     77       C  
HETATM 4173  CA  DYH A   1      -5.798  15.243  18.396  1.00  5.26           C  
ANISOU 4173  CA  DYH A   1      539    411   1048    228    107     42       C  
HETATM 4174  C   DYH A   1      -4.336  15.447  18.143  1.00  5.99           C  
ANISOU 4174  C   DYH A   1      602    521   1154    193    146    -23       C  
HETATM 4175  OXT DYH A   1      -3.697  14.595  17.491  1.00  6.53           O  
ANISOU 4175  OXT DYH A   1      649    532   1299    145    281    -70       O  
HETATM 4176  O   DYH A   1      -3.825  16.479  18.608  1.00  6.05           O  
ANISOU 4176  O   DYH A   1      601    588   1111    187     87    -54       O  
HETATM 4177  N   DYH A   1      -6.223  13.954  17.862  1.00  5.97           N  
ANISOU 4177  N   DYH A   1      650    452   1167    163    221     33       N  
HETATM 4178  S   SO4 A 791       3.393   4.987  32.364  1.00 20.84           S  
HETATM 4179  O1  SO4 A 791       3.934   4.942  30.999  1.00 17.64           O  
HETATM 4180  O2  SO4 A 791       1.963   4.678  32.345  1.00 24.45           O  
HETATM 4181  O3  SO4 A 791       4.060   3.957  33.176  1.00 23.19           O  
HETATM 4182  O4  SO4 A 791       3.566   6.319  32.937  1.00 21.65           O  
HETATM 4183  S   SO4 A   3      17.611   0.954  15.333  1.00 92.53           S  
HETATM 4184  O1  SO4 A   3      17.954   1.995  14.367  1.00 92.42           O  
HETATM 4185  O2  SO4 A   3      16.228   1.127  15.768  1.00 92.46           O  
HETATM 4186  O3  SO4 A   3      17.764  -0.357  14.707  1.00 92.52           O  
HETATM 4187  O4  SO4 A   3      18.498   1.044  16.491  1.00 92.49           O  
HETATM 4188  S   SO4 A   4      -8.341  -9.550  22.596  1.00 54.65           S  
HETATM 4189  O1  SO4 A   4      -7.558  -9.619  21.364  1.00 54.25           O  
HETATM 4190  O2  SO4 A   4      -9.154 -10.757  22.724  1.00 54.75           O  
HETATM 4191  O3  SO4 A   4      -7.438  -9.453  23.744  1.00 54.58           O  
HETATM 4192  O4  SO4 A   4      -9.214  -8.373  22.560  1.00 54.60           O  
HETATM 4193  S   SO4 A   5     -18.373  28.492   8.112  1.00 81.49           S  
HETATM 4194  O1  SO4 A   5     -17.213  28.330   7.239  1.00 81.32           O  
HETATM 4195  O2  SO4 A   5     -19.531  28.891   7.316  1.00 81.50           O  
HETATM 4196  O3  SO4 A   5     -18.659  27.228   8.784  1.00 81.51           O  
HETATM 4197  O4  SO4 A   5     -18.094  29.515   9.113  1.00 81.25           O  
HETATM 4198  C1  GOL B 801      -2.841  -8.157 -17.736  1.00 41.65           C  
HETATM 4199  O1  GOL B 801      -1.907  -7.193 -18.165  1.00 41.36           O  
HETATM 4200  C2  GOL B 801      -2.130  -9.201 -16.885  1.00 41.36           C  
HETATM 4201  O2  GOL B 801      -1.520  -8.560 -15.786  1.00 42.19           O  
HETATM 4202  C3  GOL B 801      -3.155 -10.208 -16.382  1.00 40.98           C  
HETATM 4203  O3  GOL B 801      -2.509 -11.184 -15.597  1.00 40.02           O  
HETATM 4204  C1  GOL B 802     -20.809 -16.900 -13.749  1.00 16.59           C  
HETATM 4205  O1  GOL B 802     -21.564 -17.578 -12.762  1.00 11.91           O  
HETATM 4206  C2  GOL B 802     -19.713 -17.816 -14.279  1.00 16.85           C  
HETATM 4207  O2  GOL B 802     -20.305 -18.917 -14.941  1.00 16.09           O  
HETATM 4208  C3  GOL B 802     -18.796 -17.059 -15.223  1.00 16.50           C  
HETATM 4209  O3  GOL B 802     -19.471 -16.738 -16.426  1.00 17.48           O  
HETATM 4210  C1  GOL B 803     -18.169  -9.462  -1.901  1.00 33.45           C  
HETATM 4211  O1  GOL B 803     -18.818 -10.716  -1.866  1.00 31.08           O  
HETATM 4212  C2  GOL B 803     -18.236  -8.760  -0.546  1.00 34.57           C  
HETATM 4213  O2  GOL B 803     -19.561  -8.752  -0.065  1.00 35.67           O  
HETATM 4214  C3  GOL B 803     -17.335  -9.456   0.468  1.00 35.04           C  
HETATM 4215  O3  GOL B 803     -16.403  -8.529   0.978  1.00 34.83           O  
HETATM 4216  CAA DYH B   2      -9.057   7.640 -12.511  1.00  7.07           C  
ANISOU 4216  CAA DYH B   2      536    610   1540   -311     13     97       C  
HETATM 4217  NH  DYH B   2     -10.042   6.568 -12.571  1.00  5.86           N  
ANISOU 4217  NH  DYH B   2      404    613   1208   -293    202     97       N  
HETATM 4218  CAH DYH B   2     -10.080   5.774 -13.807  1.00  5.91           C  
ANISOU 4218  CAH DYH B   2      323    717   1207   -379    277    137       C  
HETATM 4219  CAG DYH B   2     -11.238   4.776 -13.735  1.00  5.51           C  
ANISOU 4219  CAG DYH B   2      255    664   1175   -387    320    130       C  
HETATM 4220  OAC DYH B   2     -11.180   4.030 -12.498  1.00  5.89           O  
ANISOU 4220  OAC DYH B   2      319    667   1253   -367    330    229       O  
HETATM 4221  CAP DYH B   2     -11.164   3.815 -14.927  1.00  7.07           C  
ANISOU 4221  CAP DYH B   2      364    891   1433   -377    234    -14       C  
HETATM 4222  OAQ DYH B   2      -9.958   3.058 -14.849  1.00  6.71           O  
ANISOU 4222  OAQ DYH B   2      326    813   1409   -318    156   -121       O  
HETATM 4223  CAR DYH B   2      -8.797   3.887 -15.045  1.00  5.52           C  
ANISOU 4223  CAR DYH B   2      150    847   1102   -287    217    -55       C  
HETATM 4224  CAS DYH B   2      -7.579   3.090 -14.606  1.00  6.59           C  
ANISOU 4224  CAS DYH B   2      305    946   1254   -225    156   -136       C  
HETATM 4225  CAI DYH B   2      -8.751   5.064 -14.070  1.00  6.02           C  
ANISOU 4225  CAI DYH B   2      294    785   1208   -372    251    103       C  
HETATM 4226  OAJ DYH B   2      -8.334   4.481 -12.834  1.00  5.43           O  
ANISOU 4226  OAJ DYH B   2      318    589   1157   -348    232     69       O  
HETATM 4227  CAK DYH B   2      -7.515   3.334 -13.094  1.00  5.60           C  
ANISOU 4227  CAK DYH B   2      310    616   1201   -310    189    -13       C  
HETATM 4228  CAE DYH B   2      -8.114   2.133 -12.381  1.00  6.09           C  
ANISOU 4228  CAE DYH B   2      390    501   1423   -321    143     35       C  
HETATM 4229  OAB DYH B   2      -9.293   2.208 -11.923  1.00  6.95           O  
ANISOU 4229  OAB DYH B   2      470    601   1571   -368    195    201       O  
HETATM 4230  OAF DYH B   2      -7.398   1.111 -12.250  1.00  6.97           O  
ANISOU 4230  OAF DYH B   2      491    498   1658   -276     33    -21       O  
HETATM 4231  CB  DYH B   2      -6.081   3.599 -12.636  1.00  6.00           C  
ANISOU 4231  CB  DYH B   2      358    702   1218   -291    158      6       C  
HETATM 4232  CA  DYH B   2      -5.836   3.751 -11.135  1.00  5.70           C  
ANISOU 4232  CA  DYH B   2      423    566   1178   -260    129     24       C  
HETATM 4233  C   DYH B   2      -4.371   3.534 -10.890  1.00  6.19           C  
ANISOU 4233  C   DYH B   2      456    655   1242   -234     65      0       C  
HETATM 4234  OXT DYH B   2      -3.724   4.366 -10.216  1.00  6.60           O  
ANISOU 4234  OXT DYH B   2      509    667   1333   -225    -48    -19       O  
HETATM 4235  O   DYH B   2      -3.856   2.489 -11.379  1.00  6.26           O  
ANISOU 4235  O   DYH B   2      423    711   1246   -184     67    -47       O  
HETATM 4236  N   DYH B   2      -6.279   5.066 -10.681  1.00  5.69           N  
ANISOU 4236  N   DYH B   2      451    529   1182   -233     60     -4       N  
HETATM 4237  S   SO4 B 791       4.806  14.639 -24.687  1.00 38.33           S  
HETATM 4238  O1  SO4 B 791       5.789  13.560 -24.803  1.00 37.19           O  
HETATM 4239  O2  SO4 B 791       4.227  14.923 -26.003  1.00 37.50           O  
HETATM 4240  O3  SO4 B 791       3.752  14.261 -23.750  1.00 34.94           O  
HETATM 4241  O4  SO4 B 791       5.460  15.857 -24.203  1.00 37.61           O  
HETATM 4242  O   HOH A   9       5.961   8.826  26.094  1.00  9.42           O  
HETATM 4243  O   HOH A  10      11.232  14.764  14.242  1.00 11.53           O  
HETATM 4244  O   HOH A  11      -3.408  17.411  24.378  1.00  8.20           O  
HETATM 4245  O   HOH A  13      -6.059  -4.356  22.815  1.00  9.28           O  
HETATM 4246  O   HOH A  18       4.297  -0.567  28.923  1.00 11.75           O  
HETATM 4247  O   HOH A  19     -20.239  21.040  13.602  1.00  9.88           O  
HETATM 4248  O   HOH A  21      -4.752  14.674   7.540  1.00  8.75           O  
HETATM 4249  O   HOH A  22       6.851  15.808  25.534  1.00 11.86           O  
HETATM 4250  O   HOH A  23      12.493  -5.403  18.685  1.00 12.05           O  
HETATM 4251  O   HOH A  24      -1.505  -3.758  -3.084  1.00 13.23           O  
HETATM 4252  O   HOH A  26      -6.940  20.273  20.811  1.00  9.24           O  
HETATM 4253  O   HOH A  28     -20.748  23.284  12.167  1.00 12.02           O  
HETATM 4254  O   HOH A  31     -18.769  33.032  20.642  1.00 13.68           O  
HETATM 4255  O   HOH A  32      -3.990  -5.487  24.342  1.00 12.83           O  
HETATM 4256  O   HOH A  33     -26.545   9.919  21.908  1.00 13.15           O  
HETATM 4257  O   HOH A  35       7.979  14.934   6.862  1.00 10.66           O  
HETATM 4258  O   HOH A  37      -7.943  31.980  14.251  1.00 11.31           O  
HETATM 4259  O   HOH A  42      -9.484  -1.958   6.514  1.00 14.37           O  
HETATM 4260  O   HOH A  44       6.665  18.268  26.762  1.00 16.49           O  
HETATM 4261  O   HOH A  45       5.975  14.989  28.093  1.00 14.01           O  
HETATM 4262  O   HOH A  46      -1.485  -4.864  25.333  1.00 13.51           O  
HETATM 4263  O   HOH A  47      -4.348  -1.762  33.468  1.00 11.48           O  
HETATM 4264  O   HOH A  48      11.374   5.746  14.407  1.00 14.38           O  
HETATM 4265  O   HOH A  49      -6.784  -3.391  36.096  1.00 10.86           O  
HETATM 4266  O   HOH A  51      -4.499  16.012  26.586  1.00 12.41           O  
HETATM 4267  O   HOH A  54     -27.006  31.202  17.291  1.00 16.37           O  
HETATM 4268  O   HOH A  60       1.682   0.804  36.440  1.00 16.77           O  
HETATM 4269  O   HOH A  61      11.402   8.778   7.371  1.00 15.34           O  
HETATM 4270  O   HOH A  62     -19.184  24.771  10.407  1.00 15.27           O  
HETATM 4271  O   HOH A  63       5.185   2.544  30.620  1.00 15.69           O  
HETATM 4272  O   HOH A  65      -8.394   4.012  30.583  1.00 13.40           O  
HETATM 4273  O   HOH A  66      -8.072  20.883   9.021  1.00 15.85           O  
HETATM 4274  O   HOH A  68      11.713  18.726  13.588  1.00 16.63           O  
HETATM 4275  O   HOH A  69      10.672   8.424   4.675  1.00 15.59           O  
HETATM 4276  O   HOH A  70     -11.778 -12.137  40.776  1.00 19.02           O  
HETATM 4277  O   HOH A  71      -8.083  -6.381  16.475  1.00 18.35           O  
HETATM 4278  O   HOH A  72     -21.181  26.641  10.730  1.00 16.21           O  
HETATM 4279  O   HOH A  76      -3.548   5.047   4.244  1.00 15.06           O  
HETATM 4280  O   HOH A  77      -9.730   1.904  11.292  1.00 17.33           O  
HETATM 4281  O   HOH A  78       5.610  -5.081  28.241  1.00 16.67           O  
HETATM 4282  O   HOH A  80      -9.610  26.962   9.030  1.00 14.55           O  
HETATM 4283  O   HOH A  81     -10.049  -7.186   2.034  1.00 20.44           O  
HETATM 4284  O   HOH A  82      13.990  -6.155  21.292  1.00 18.51           O  
HETATM 4285  O   HOH A  85      -7.238  26.224  10.563  1.00 15.75           O  
HETATM 4286  O   HOH A  86     -11.568   5.678   8.874  1.00 15.69           O  
HETATM 4287  O   HOH A  87       4.381  20.153  28.691  1.00 20.17           O  
HETATM 4288  O   HOH A  92      11.255   5.418   6.653  1.00 17.84           O  
HETATM 4289  O   HOH A  95     -27.535  34.162  22.659  1.00 16.18           O  
HETATM 4290  O   HOH A  96     -14.638  -0.172  23.316  1.00 19.26           O  
HETATM 4291  O   HOH A  98     -21.539  36.202  19.932  1.00 14.41           O  
HETATM 4292  O   HOH A 105      -4.322  21.410  13.912  1.00 15.01           O  
HETATM 4293  O   HOH A 106     -15.587  24.325   7.940  1.00 15.55           O  
HETATM 4294  O   HOH A 108      -8.473   5.622  28.305  1.00 10.45           O  
HETATM 4295  O   HOH A 111       6.026  -5.926  22.393  1.00 15.80           O  
HETATM 4296  O   HOH A 114      13.717  15.506  15.199  1.00 13.77           O  
HETATM 4297  O   HOH A 115       0.994  23.788  16.959  1.00 16.37           O  
HETATM 4298  O   HOH A 117     -10.550  -4.540  30.311  1.00 16.73           O  
HETATM 4299  O   HOH A 119     -17.245  31.939   8.767  1.00 19.63           O  
HETATM 4300  O   HOH A 121      -7.892  13.411  26.024  1.00 16.29           O  
HETATM 4301  O   HOH A 125       4.549  23.872  23.562  1.00 22.88           O  
HETATM 4302  O   HOH A 126     -10.791   9.310  26.718  1.00 17.08           O  
HETATM 4303  O   HOH A 128       0.150   4.002  34.129  1.00 16.04           O  
HETATM 4304  O   HOH A 129     -28.563  20.694  21.568  1.00 19.08           O  
HETATM 4305  O   HOH A 130       8.571   9.048  25.217  1.00 16.34           O  
HETATM 4306  O   HOH A 134       3.915   8.996  31.856  1.00 16.84           O  
HETATM 4307  O   HOH A 136       3.913  22.735  27.558  1.00 21.84           O  
HETATM 4308  O   HOH A 138      -8.080  28.890   7.521  1.00 18.99           O  
HETATM 4309  O   HOH A 139      -0.081  -8.225  11.327  1.00 20.61           O  
HETATM 4310  O   HOH A 140       5.917  23.433  11.975  1.00 19.87           O  
HETATM 4311  O   HOH A 142     -29.019  13.201  18.878  1.00 24.61           O  
HETATM 4312  O   HOH A 144      -6.128   3.515   5.978  1.00 18.68           O  
HETATM 4313  O   HOH A 145     -27.088  19.313  14.612  1.00 21.23           O  
HETATM 4314  O   HOH A 146     -29.228   9.551  21.482  1.00 16.72           O  
HETATM 4315  O   HOH A 147       2.876  -6.307  24.358  1.00 14.12           O  
HETATM 4316  O   HOH A 153       1.346  -8.516  32.929  1.00 19.42           O  
HETATM 4317  O   HOH A 154      12.670  -5.211  25.756  1.00 22.33           O  
HETATM 4318  O   HOH A 155      -0.985  21.228  17.469  1.00 17.72           O  
HETATM 4319  O   HOH A 157       3.226  -6.959  21.693  1.00 16.16           O  
HETATM 4320  O   HOH A 158      15.038  13.670  13.548  1.00 16.48           O  
HETATM 4321  O   HOH A 160     -14.564  -6.622  14.269  1.00 23.07           O  
HETATM 4322  O   HOH A 162     -24.840  12.409  17.621  1.00 16.92           O  
HETATM 4323  O   HOH A 165       4.743  -2.247  34.741  1.00 20.35           O  
HETATM 4324  O   HOH A 166      -5.507  -7.853  20.815  1.00 15.42           O  
HETATM 4325  O   HOH A 168      -1.471  -7.339  26.572  1.00 19.09           O  
HETATM 4326  O   HOH A 173     -28.393  23.953  27.198  1.00 20.51           O  
HETATM 4327  O   HOH A 174     -12.355   9.831  23.060  1.00 20.04           O  
HETATM 4328  O   HOH A 175       0.716  -4.712  23.689  1.00 16.15           O  
HETATM 4329  O   HOH A 177      -8.855  36.461  22.796  1.00 17.65           O  
HETATM 4330  O   HOH A 178      -0.683  25.468  18.125  1.00 18.57           O  
HETATM 4331  O   HOH A 183     -27.891  29.091  22.959  1.00 19.30           O  
HETATM 4332  O   HOH A 185      -9.702  11.855  29.078  1.00 18.70           O  
HETATM 4333  O   HOH A 187      -3.914  19.352  27.599  1.00 21.50           O  
HETATM 4334  O   HOH A 188      -8.691  35.000  16.555  1.00 19.81           O  
HETATM 4335  O   HOH A 194      10.971   2.347   6.732  1.00 24.64           O  
HETATM 4336  O   HOH A 197     -23.078  26.532  33.208  1.00 27.31           O  
HETATM 4337  O   HOH A 199       6.577  -2.829   5.898  1.00 24.18           O  
HETATM 4338  O   HOH A 202      -4.760   0.696  -1.169  1.00 17.44           O  
HETATM 4339  O   HOH A 203     -21.318  13.752  10.738  1.00 30.22           O  
HETATM 4340  O   HOH A 206     -19.069  34.077   9.449  1.00 22.38           O  
HETATM 4341  O   HOH A 210     -15.831   7.541  13.369  1.00 22.52           O  
HETATM 4342  O   HOH A 211     -26.235  15.885  31.952  1.00 31.47           O  
HETATM 4343  O   HOH A 213     -17.853  35.577   7.074  1.00 29.21           O  
HETATM 4344  O   HOH A 215      -5.763  16.752   5.826  1.00 14.09           O  
HETATM 4345  O   HOH A 217      -8.964   8.180  28.926  1.00 17.29           O  
HETATM 4346  O   HOH A 218      -7.781  -6.234  23.892  1.00 20.30           O  
HETATM 4347  O   HOH A 219     -20.311  16.710   7.552  1.00 19.69           O  
HETATM 4348  O   HOH A 224     -27.866  33.523  18.606  1.00 18.82           O  
HETATM 4349  O   HOH A 225      -2.608   9.677  31.901  1.00 19.10           O  
HETATM 4350  O   HOH A 227      -6.111  20.035  12.601  1.00 19.70           O  
HETATM 4351  O   HOH A 228     -22.429  21.977  10.410  1.00 18.87           O  
HETATM 4352  O   HOH A 229      -3.436   6.344   1.704  1.00 17.45           O  
HETATM 4353  O   HOH A 230     -27.060   6.861  28.538  1.00 23.86           O  
HETATM 4354  O   HOH A 231       9.691  16.943   6.066  1.00 20.12           O  
HETATM 4355  O   HOH A 235       2.642  -8.255  26.326  1.00 20.54           O  
HETATM 4356  O   HOH A 237     -14.869  19.062  33.897  1.00 23.73           O  
HETATM 4357  O   HOH A 242     -26.342  10.605  19.010  1.00 23.35           O  
HETATM 4358  O   HOH A 243     -13.405   6.978  10.932  1.00 21.46           O  
HETATM 4359  O   HOH A 247     -10.042  -6.802  14.634  1.00 23.94           O  
HETATM 4360  O   HOH A 249       8.369  24.054  10.996  1.00 22.90           O  
HETATM 4361  O   HOH A 252      10.282  21.906  19.947  1.00 21.08           O  
HETATM 4362  O   HOH A 255     -24.859  11.505  31.905  1.00 26.53           O  
HETATM 4363  O   HOH A 256     -14.295  33.728   6.378  1.00 25.04           O  
HETATM 4364  O   HOH A 257      -8.453   2.897   7.588  1.00 24.42           O  
HETATM 4365  O   HOH A 258       0.027  -3.457  21.645  1.00 24.10           O  
HETATM 4366  O   HOH A 263     -29.294  29.922  20.789  1.00 23.66           O  
HETATM 4367  O   HOH A 264      15.860   9.095  24.221  1.00 25.45           O  
HETATM 4368  O   HOH A 265     -11.984  23.129   7.130  1.00 21.83           O  
HETATM 4369  O   HOH A 266      14.004   0.177  24.337  1.00 26.60           O  
HETATM 4370  O   HOH A 268     -28.617  28.984  18.153  1.00 22.92           O  
HETATM 4371  O   HOH A 269      13.509  -2.822  15.542  1.00 24.53           O  
HETATM 4372  O   HOH A 270      -4.374  -6.987  16.485  1.00 26.98           O  
HETATM 4373  O   HOH A 277      -4.774  11.232  28.529  1.00 20.50           O  
HETATM 4374  O   HOH A 279     -15.973  10.242  11.543  1.00 26.24           O  
HETATM 4375  O   HOH A 280     -10.409  -0.976  29.095  1.00 24.10           O  
HETATM 4376  O   HOH A 281     -23.117  26.535   8.821  1.00 32.65           O  
HETATM 4377  O   HOH A 282      -4.588  -8.868  18.334  1.00 24.91           O  
HETATM 4378  O   HOH A 286     -19.812   3.849  18.776  1.00 29.35           O  
HETATM 4379  O   HOH A 288       6.313   6.145   2.413  1.00 23.41           O  
HETATM 4380  O   HOH A 289     -28.963  19.181  19.099  1.00 23.36           O  
HETATM 4381  O   HOH A 293     -25.338  32.961  10.836  1.00 31.97           O  
HETATM 4382  O   HOH A 295      -6.678  34.130  15.054  1.00 24.74           O  
HETATM 4383  O   HOH A 296     -10.102   0.699   6.602  1.00 30.64           O  
HETATM 4384  O   HOH A 297      -8.976  29.089   4.839  1.00 29.77           O  
HETATM 4385  O   HOH A 298      -2.964  -6.147   0.051  1.00 29.00           O  
HETATM 4386  O   HOH A 300      11.747  20.977  15.357  1.00 29.43           O  
HETATM 4387  O   HOH A 302     -20.371   9.520  29.604  1.00 32.55           O  
HETATM 4388  O   HOH A 303     -19.272  11.533  14.703  1.00 24.45           O  
HETATM 4389  O   HOH A 304     -11.148   7.718  30.313  1.00 24.45           O  
HETATM 4390  O   HOH A 305      -8.792  38.133  25.404  1.00 28.53           O  
HETATM 4391  O   HOH A 306      -7.605   6.253   6.369  1.00 27.16           O  
HETATM 4392  O   HOH A 307      -6.787 -10.950  42.878  1.00 24.91           O  
HETATM 4393  O   HOH A 309       1.332 -10.960  10.920  1.00 27.86           O  
HETATM 4394  O   HOH A 310     -26.117  20.117  32.989  1.00 28.18           O  
HETATM 4395  O   HOH A 313     -25.171  22.189  10.467  1.00 26.82           O  
HETATM 4396  O   HOH A 315     -25.824  23.117  32.839  1.00 29.54           O  
HETATM 4397  O   HOH A 319      10.256  19.311   7.239  1.00 21.97           O  
HETATM 4398  O   HOH A 320     -14.992  17.182  35.878  1.00 27.83           O  
HETATM 4399  O   HOH A 321       0.352  25.055  26.776  1.00 30.13           O  
HETATM 4400  O   HOH A 322       1.290  18.782  31.478  1.00 31.96           O  
HETATM 4401  O   HOH A 326     -29.607  21.353  17.801  1.00 27.99           O  
HETATM 4402  O   HOH A 327     -16.194  11.614  30.960  1.00 26.17           O  
HETATM 4403  O   HOH A 332     -14.602  36.095  26.334  1.00 26.76           O  
HETATM 4404  O   HOH A 333       9.229  23.738  15.241  1.00 31.16           O  
HETATM 4405  O   HOH A 334     -27.845  17.577  17.216  1.00 25.37           O  
HETATM 4406  O   HOH A 336      16.484  15.347  18.957  1.00 30.15           O  
HETATM 4407  O   HOH A 337      -9.415  -3.777   0.085  1.00 26.64           O  
HETATM 4408  O   HOH A 346       2.382  28.981  18.099  1.00 38.45           O  
HETATM 4409  O   HOH A 349      -2.439   9.771  29.172  1.00 10.88           O  
HETATM 4410  O   HOH A 351       0.022  10.669  29.685  1.00 12.84           O  
HETATM 4411  O   HOH A 357      -0.708  12.031  31.891  1.00 27.30           O  
HETATM 4412  O   HOH A 361       9.134  21.646   5.899  1.00 25.30           O  
HETATM 4413  O   HOH A 363     -30.708  17.500  20.398  1.00 24.90           O  
HETATM 4414  O   HOH A 365     -18.374  25.323  32.005  1.00 26.60           O  
HETATM 4415  O   HOH A 373       6.158  -5.142   4.660  1.00 31.34           O  
HETATM 4416  O   HOH A 374       6.812  -0.705  30.149  1.00 24.50           O  
HETATM 4417  O   HOH A 375     -25.143  16.203  13.701  1.00 29.13           O  
HETATM 4418  O   HOH A 376       4.224  -6.714   4.293  1.00 30.64           O  
HETATM 4419  O   HOH A 377      -8.056  22.083  32.830  1.00 34.19           O  
HETATM 4420  O   HOH A 378     -20.096  33.108  22.925  1.00 24.76           O  
HETATM 4421  O   HOH A 379      -2.067  17.302  30.760  1.00 24.88           O  
HETATM 4422  O   HOH A 380      14.556  20.437  16.370  1.00 30.22           O  
HETATM 4423  O   HOH A 383      16.164  -3.409  23.319  1.00 27.99           O  
HETATM 4424  O   HOH A 386      -6.128   7.533   1.899  1.00 28.47           O  
HETATM 4425  O   HOH A 390     -11.453   2.906   9.620  1.00 32.52           O  
HETATM 4426  O   HOH A 397     -16.719  37.221  24.785  1.00 28.89           O  
HETATM 4427  O   HOH A 398      -7.080  10.620  30.079  1.00 30.13           O  
HETATM 4428  O   HOH A 399      12.435  -3.052  27.400  1.00 35.05           O  
HETATM 4429  O   HOH A 400      11.486  -2.973  10.788  1.00 30.68           O  
HETATM 4430  O   HOH A 402      17.342  -8.959  13.026  1.00 34.43           O  
HETATM 4431  O   HOH A 403       3.536   9.505   3.593  1.00  8.13           O  
HETATM 4432  O   HOH A 404       4.550   7.366   4.014  1.00 27.37           O  
HETATM 4433  O   HOH A 409      -7.556  19.264   6.841  1.00 20.68           O  
HETATM 4434  O   HOH A 539     -27.387  11.050 -23.407  1.00 46.00           O  
HETATM 4435  O   HOH A 540       5.747  28.249   0.068  1.00 31.52           O  
HETATM 4436  O   HOH A 557       7.159  30.113  27.082  1.00 40.07           O  
HETATM 4437  O   HOH A 570      -4.717  13.679  31.143  1.00 28.29           O  
HETATM 4438  O   HOH A 575       4.821  -7.557  30.542  1.00 37.49           O  
HETATM 4439  O   HOH A 597      -8.165  28.600 -15.725  1.00 21.58           O  
HETATM 4440  O   HOH A 598      17.737  17.899  -8.095  1.00 21.37           O  
HETATM 4441  O   HOH A 792      -8.493  17.895  15.390  1.00  6.67           O  
HETATM 4442  O   HOH A 793      -1.608  20.294  14.752  1.00  7.13           O  
HETATM 4443  O   HOH A 794     -10.701  18.901  21.654  1.00  7.00           O  
HETATM 4444  O   HOH A 795     -20.028  10.109  32.272  1.00 33.78           O  
HETATM 4445  O   HOH A 796      15.520  10.974  -6.038  1.00 32.82           O  
HETATM 4446  O   HOH A 797     -13.544  18.533   2.071  1.00 43.40           O  
HETATM 4447  O   HOH A 798      12.757   9.594  27.743  1.00 28.36           O  
HETATM 4448  O   HOH A 799      15.462   9.775  26.726  1.00 32.31           O  
HETATM 4449  O   HOH A 800     -13.993   1.984   9.217  1.00 31.59           O  
HETATM 4450  O   HOH A 801      -5.763  -3.631 -23.781  1.00 34.48           O  
HETATM 4451  O   HOH A 802     -14.150  17.037  -2.098  1.00 32.96           O  
HETATM 4452  O   HOH A 803     -17.759  11.962 -19.708  1.00 35.22           O  
HETATM 4453  O   HOH A 804      -0.297  26.482  20.513  1.00 26.97           O  
HETATM 4454  O   HOH A 805     -26.194  27.384  10.808  1.00 32.53           O  
HETATM 4455  O   HOH A 806      10.869  -4.529   8.739  1.00 29.39           O  
HETATM 4456  O   HOH A 807       7.195  -5.204  -6.984  1.00 30.64           O  
HETATM 4457  O   HOH A 808     -14.992  10.454 -19.174  1.00 28.51           O  
HETATM 4458  O   HOH B   3      -1.632  -1.319  -7.558  1.00  6.53           O  
HETATM 4459  O   HOH B   6     -10.694   0.124 -14.402  1.00  7.82           O  
HETATM 4460  O   HOH B   7      -3.480   1.499 -17.084  1.00  7.85           O  
HETATM 4461  O   HOH B   8      -7.060  -1.261 -13.575  1.00  7.60           O  
HETATM 4462  O   HOH B  12      11.244   4.208  -7.146  1.00 11.52           O  
HETATM 4463  O   HOH B  14       5.860  10.131 -18.974  1.00 10.35           O  
HETATM 4464  O   HOH B  15      -4.710   4.346  -0.302  1.00  9.03           O  
HETATM 4465  O   HOH B  16      12.424  24.385 -11.490  1.00 11.05           O  
HETATM 4466  O   HOH B  17     -20.300  -2.015  -6.460  1.00  9.51           O  
HETATM 4467  O   HOH B  20       6.693   3.166 -18.444  1.00 11.36           O  
HETATM 4468  O   HOH B  25     -26.534   9.195 -14.772  1.00 12.74           O  
HETATM 4469  O   HOH B  27       4.365  19.364 -21.905  1.00 13.26           O  
HETATM 4470  O   HOH B  29     -20.911  -4.332  -5.022  1.00 11.29           O  
HETATM 4471  O   HOH B  30     -18.673 -14.151 -13.638  1.00 12.57           O  
HETATM 4472  O   HOH B  34       5.786   4.001 -20.968  1.00 12.73           O  
HETATM 4473  O   HOH B  36      -6.085  23.363 -15.821  1.00 12.02           O  
HETATM 4474  O   HOH B  38      -7.438  -7.212  -3.326  1.00 13.69           O  
HETATM 4475  O   HOH B  39      -8.137  -1.877  -1.758  1.00 14.01           O  
HETATM 4476  O   HOH B  40      -4.563   2.828 -19.387  1.00 10.01           O  
HETATM 4477  O   HOH B  41      -9.534  20.993   0.612  1.00 13.83           O  
HETATM 4478  O   HOH B  43      -8.026 -12.973  -6.978  1.00 12.30           O  
HETATM 4479  O   HOH B  50      -2.510   9.191 -22.081  1.00 14.32           O  
HETATM 4480  O   HOH B  52     -21.412  -7.563  -3.642  1.00 15.20           O  
HETATM 4481  O   HOH B  53      11.350  13.230  -7.289  1.00 16.62           O  
HETATM 4482  O   HOH B  55       0.899  -4.841  -9.817  1.00 14.98           O  
HETATM 4483  O   HOH B  56       7.934   3.997   0.291  1.00 11.89           O  
HETATM 4484  O   HOH B  57      11.712   0.254  -6.496  1.00 18.09           O  
HETATM 4485  O   HOH B  58     -27.091 -12.198 -10.456  1.00 14.36           O  
HETATM 4486  O   HOH B  59      15.061   5.391  -6.391  1.00 15.97           O  
HETATM 4487  O   HOH B  64     -15.729  -5.250  -0.719  1.00 15.21           O  
HETATM 4488  O   HOH B  67      -3.449  13.940   2.915  1.00 16.47           O  
HETATM 4489  O   HOH B  73      -1.583  22.767  10.230  1.00 14.87           O  
HETATM 4490  O   HOH B  74      -7.041  -7.312 -26.904  1.00 13.32           O  
HETATM 4491  O   HOH B  75     -19.326  -5.801  -3.311  1.00 15.30           O  
HETATM 4492  O   HOH B  79      -9.302  -2.240 -25.073  1.00 15.59           O  
HETATM 4493  O   HOH B  83       2.969  25.219 -17.420  1.00 17.04           O  
HETATM 4494  O   HOH B  84       6.068  24.760 -15.513  1.00 15.81           O  
HETATM 4495  O   HOH B  88      11.373  10.216  -0.239  1.00 16.24           O  
HETATM 4496  O   HOH B  89      -0.090   8.311 -22.778  1.00 16.28           O  
HETATM 4497  O   HOH B  90     -22.658  -3.063  -3.298  1.00 17.03           O  
HETATM 4498  O   HOH B  91      -8.372  -1.150 -28.621  1.00 13.22           O  
HETATM 4499  O   HOH B  93      11.172  13.569   0.495  1.00 15.33           O  
HETATM 4500  O   HOH B  94      12.888  24.113 -18.574  1.00 15.96           O  
HETATM 4501  O   HOH B  97      -4.054  24.528 -17.329  1.00 15.16           O  
HETATM 4502  O   HOH B  99      10.643  10.671   2.380  1.00 15.65           O  
HETATM 4503  O   HOH B 100      -7.776   4.023 -27.055  1.00 17.26           O  
HETATM 4504  O   HOH B 101      -9.661  -8.013  -1.807  1.00 15.27           O  
HETATM 4505  O   HOH B 102       5.844  -4.500  -4.724  1.00 16.48           O  
HETATM 4506  O   HOH B 103       8.424   9.897 -17.809  1.00 14.68           O  
HETATM 4507  O   HOH B 104       4.452  -4.867 -16.323  1.00 21.46           O  
HETATM 4508  O   HOH B 107      -0.944  -2.341 -10.129  1.00 16.13           O  
HETATM 4509  O   HOH B 109      -8.475  13.334 -21.173  1.00 14.65           O  
HETATM 4510  O   HOH B 110       6.513   0.711 -19.670  1.00 15.36           O  
HETATM 4511  O   HOH B 112      -1.033  -6.569 -10.960  1.00 17.72           O  
HETATM 4512  O   HOH B 113      -8.398  -9.857  -0.240  1.00 18.11           O  
HETATM 4513  O   HOH B 116      -1.459  23.898 -18.528  1.00 20.06           O  
HETATM 4514  O   HOH B 118      -0.070  27.299  -4.242  1.00 17.80           O  
HETATM 4515  O   HOH B 120     -10.343  -4.965 -24.838  1.00 15.01           O  
HETATM 4516  O   HOH B 122      -8.960 -17.504 -15.478  1.00 14.32           O  
HETATM 4517  O   HOH B 123     -29.054   5.883 -11.702  1.00 23.31           O  
HETATM 4518  O   HOH B 124      -8.050  25.456  -9.399  1.00 17.36           O  
HETATM 4519  O   HOH B 127      13.663   3.504  -8.161  1.00 16.94           O  
HETATM 4520  O   HOH B 131      13.927  25.095 -13.967  1.00 16.06           O  
HETATM 4521  O   HOH B 132      -3.945  -0.349 -20.419  1.00 19.53           O  
HETATM 4522  O   HOH B 133     -10.231  -0.806   1.620  1.00 21.73           O  
HETATM 4523  O   HOH B 135     -10.241  19.783   5.630  1.00 24.65           O  
HETATM 4524  O   HOH B 137     -11.674  13.304  -1.791  1.00 18.59           O  
HETATM 4525  O   HOH B 141       0.720  23.761 -16.714  1.00 19.05           O  
HETATM 4526  O   HOH B 143      10.318  -0.367  -0.185  1.00 19.92           O  
HETATM 4527  O   HOH B 148      -5.567  26.853 -13.741  1.00 17.89           O  
HETATM 4528  O   HOH B 149      -4.608  20.517 -26.450  1.00 18.76           O  
HETATM 4529  O   HOH B 150       4.018  -1.292 -21.556  1.00 22.33           O  
HETATM 4530  O   HOH B 151      -8.736 -16.214  -9.472  1.00 16.81           O  
HETATM 4531  O   HOH B 152     -27.143  -0.548  -7.584  1.00 22.56           O  
HETATM 4532  O   HOH B 156     -24.897   6.679 -10.445  1.00 16.02           O  
HETATM 4533  O   HOH B 159      -9.746  17.165  -4.184  1.00 19.96           O  
HETATM 4534  O   HOH B 161      -6.158  -1.144  -5.304  1.00 18.43           O  
HETATM 4535  O   HOH B 163     -14.589  25.770  -7.174  1.00 22.71           O  
HETATM 4536  O   HOH B 164      -8.825   7.020 -21.632  1.00 21.62           O  
HETATM 4537  O   HOH B 167     -20.215 -14.101 -15.833  1.00 15.37           O  
HETATM 4538  O   HOH B 169      -9.973  26.128   5.126  1.00 22.52           O  
HETATM 4539  O   HOH B 170     -25.203   2.818  -6.679  1.00 25.68           O  
HETATM 4540  O   HOH B 171     -17.400 -13.001  -1.566  1.00 20.64           O  
HETATM 4541  O   HOH B 172      -1.365  26.348 -19.764  1.00 21.43           O  
HETATM 4542  O   HOH B 176     -12.355  -1.365 -27.169  1.00 22.27           O  
HETATM 4543  O   HOH B 179      -8.454  14.870 -23.496  1.00 19.56           O  
HETATM 4544  O   HOH B 180     -14.596   0.197 -26.720  1.00 23.20           O  
HETATM 4545  O   HOH B 181      -0.214  -7.694 -13.233  1.00 20.70           O  
HETATM 4546  O   HOH B 182     -12.693   7.446 -16.134  1.00 23.62           O  
HETATM 4547  O   HOH B 184      -7.666  -0.220   0.480  1.00 16.89           O  
HETATM 4548  O   HOH B 186     -26.558  -8.472  -4.139  1.00 28.42           O  
HETATM 4549  O   HOH B 189      10.467   7.315 -20.792  1.00 24.41           O  
HETATM 4550  O   HOH B 190      -3.524  -2.072 -22.751  1.00 24.95           O  
HETATM 4551  O   HOH B 191     -11.512   9.771 -14.412  1.00 30.01           O  
HETATM 4552  O   HOH B 192     -20.729 -12.886 -18.172  1.00 19.87           O  
HETATM 4553  O   HOH B 193     -23.871   8.008 -24.995  1.00 18.51           O  
HETATM 4554  O   HOH B 195     -12.118 -17.863  -1.885  1.00 31.80           O  
HETATM 4555  O   HOH B 196      -6.535 -16.623  -5.628  1.00 37.62           O  
HETATM 4556  O   HOH B 198      15.818   9.777 -17.252  1.00 23.46           O  
HETATM 4557  O   HOH B 200      11.972  -1.048 -14.865  1.00 29.29           O  
HETATM 4558  O   HOH B 201     -21.668   4.885  -3.303  1.00 31.27           O  
HETATM 4559  O   HOH B 204     -16.581 -19.149 -17.912  1.00 21.12           O  
HETATM 4560  O   HOH B 205      -6.311  15.349   1.226  1.00 23.89           O  
HETATM 4561  O   HOH B 207       6.445  21.878   1.194  1.00 24.96           O  
HETATM 4562  O   HOH B 208      -9.093   7.359 -26.799  1.00 37.42           O  
HETATM 4563  O   HOH B 209      -9.050  22.906   7.464  1.00 30.53           O  
HETATM 4564  O   HOH B 212     -28.672   8.649 -10.804  1.00 24.73           O  
HETATM 4565  O   HOH B 214     -19.298 -14.978  -2.396  1.00 27.00           O  
HETATM 4566  O   HOH B 216       9.770   2.108   1.148  1.00 18.65           O  
HETATM 4567  O   HOH B 220     -20.500   2.200  -0.267  1.00 22.49           O  
HETATM 4568  O   HOH B 221     -29.216   9.551 -14.319  1.00 17.92           O  
HETATM 4569  O   HOH B 222      -6.899 -15.151  -7.834  1.00 19.31           O  
HETATM 4570  O   HOH B 223      -3.573  12.674   5.556  1.00 16.96           O  
HETATM 4571  O   HOH B 226     -27.446 -15.094 -15.644  1.00 16.27           O  
HETATM 4572  O   HOH B 232      -6.857   4.511 -18.436  1.00 21.09           O  
HETATM 4573  O   HOH B 233      11.839  -1.908  -8.122  1.00 24.67           O  
HETATM 4574  O   HOH B 234     -14.639  19.196 -16.181  1.00 22.23           O  
HETATM 4575  O   HOH B 236      -9.887  25.793  -7.567  1.00 21.32           O  
HETATM 4576  O   HOH B 238     -30.813   1.513 -13.369  1.00 21.53           O  
HETATM 4577  O   HOH B 239      13.144  26.263  -9.346  1.00 25.85           O  
HETATM 4578  O   HOH B 240      -4.720  18.328   8.298  1.00 17.80           O  
HETATM 4579  O   HOH B 241      12.767   3.174 -18.477  1.00 24.29           O  
HETATM 4580  O   HOH B 244      -8.941  10.616 -21.591  1.00 23.83           O  
HETATM 4581  O   HOH B 245      -3.943   4.097 -23.676  1.00 22.91           O  
HETATM 4582  O   HOH B 246      -7.812  25.269 -16.836  1.00 23.98           O  
HETATM 4583  O   HOH B 248      10.801  16.558   0.361  1.00 28.60           O  
HETATM 4584  O   HOH B 250     -26.325   8.520 -11.880  1.00 22.73           O  
HETATM 4585  O   HOH B 251      -4.350 -14.129  -9.278  1.00 23.58           O  
HETATM 4586  O   HOH B 253      -2.200   1.707 -23.140  1.00 21.04           O  
HETATM 4587  O   HOH B 254     -10.518  18.125   0.195  1.00 30.44           O  
HETATM 4588  O   HOH B 259     -12.180  -4.197   0.084  1.00 21.90           O  
HETATM 4589  O   HOH B 260       9.018  -2.669   1.336  1.00 28.88           O  
HETATM 4590  O   HOH B 261     -13.356  12.199  -3.687  1.00 26.45           O  
HETATM 4591  O   HOH B 262      -5.023  16.063   3.350  1.00 30.39           O  
HETATM 4592  O   HOH B 267     -11.006  -6.366  -0.290  1.00 25.91           O  
HETATM 4593  O   HOH B 271      -4.380  -2.419  -6.727  1.00 18.87           O  
HETATM 4594  O   HOH B 272      -3.194  -6.210 -24.745  1.00 21.88           O  
HETATM 4595  O   HOH B 273      -6.115   7.129 -20.702  1.00 24.10           O  
HETATM 4596  O   HOH B 274      13.542  21.721  -8.317  1.00 26.37           O  
HETATM 4597  O   HOH B 275     -15.876   8.950  -4.344  1.00 27.70           O  
HETATM 4598  O   HOH B 276     -11.071   9.679 -19.351  1.00 25.77           O  
HETATM 4599  O   HOH B 278      -3.404 -10.353 -25.534  1.00 29.78           O  
HETATM 4600  O   HOH B 285      10.202  -2.759 -12.701  1.00 21.91           O  
HETATM 4601  O   HOH B 287     -25.454  -3.959 -25.762  1.00 30.39           O  
HETATM 4602  O   HOH B 290      10.438   3.682 -19.708  1.00 29.72           O  
HETATM 4603  O   HOH B 291      -0.828  -4.304 -22.799  1.00 28.02           O  
HETATM 4604  O   HOH B 292     -25.360  -3.369  -3.371  1.00 25.48           O  
HETATM 4605  O   HOH B 294      16.494   3.615 -11.759  1.00 31.99           O  
HETATM 4606  O   HOH B 299       3.861  -3.741 -20.510  1.00 29.71           O  
HETATM 4607  O   HOH B 301      -8.754 -19.187 -18.887  1.00 27.16           O  
HETATM 4608  O   HOH B 308      14.006  18.870 -17.260  1.00 25.02           O  
HETATM 4609  O   HOH B 311      -0.073  -6.217 -19.646  1.00 30.55           O  
HETATM 4610  O   HOH B 312     -21.202 -11.292  -0.176  1.00 37.15           O  
HETATM 4611  O   HOH B 314      -3.782   5.938 -21.666  1.00 24.46           O  
HETATM 4612  O   HOH B 316       9.495  -4.759  -8.189  1.00 29.36           O  
HETATM 4613  O   HOH B 317      16.131  22.472 -16.271  1.00 28.97           O  
HETATM 4614  O   HOH B 318       8.069  23.542 -19.266  1.00 26.83           O  
HETATM 4615  O   HOH B 323       6.747  19.489 -23.354  1.00 27.07           O  
HETATM 4616  O   HOH B 324       8.393  -5.068  -3.764  1.00 24.60           O  
HETATM 4617  O   HOH B 325      -1.569  27.168   5.595  1.00 30.43           O  
HETATM 4618  O   HOH B 328     -15.713  11.276  -6.066  1.00 28.27           O  
HETATM 4619  O   HOH B 329     -28.633 -10.124 -11.338  1.00 24.88           O  
HETATM 4620  O   HOH B 331      -2.013  -0.263 -24.846  1.00 32.84           O  
HETATM 4621  O   HOH B 335     -13.301  24.941  -0.014  1.00 28.93           O  
HETATM 4622  O   HOH B 339      -2.829  11.357 -27.153  1.00 33.07           O  
HETATM 4623  O   HOH B 340      -5.624  20.389   9.897  1.00 26.43           O  
HETATM 4624  O   HOH B 341      -0.251  27.463 -29.391  1.00 34.88           O  
HETATM 4625  O   HOH B 343      -7.955  12.768 -25.382  1.00 30.68           O  
HETATM 4626  O   HOH B 344       6.179  11.432 -23.185  1.00 28.40           O  
HETATM 4627  O   HOH B 345     -28.151  -4.734 -20.175  1.00 24.89           O  
HETATM 4628  O   HOH B 348       1.169  29.902  -3.810  1.00 28.59           O  
HETATM 4629  O   HOH B 353     -26.913  12.343 -21.217  1.00 22.12           O  
HETATM 4630  O   HOH B 354     -14.174 -14.751   0.875  1.00 21.71           O  
HETATM 4631  O   HOH B 355     -19.370  15.718 -14.242  1.00 20.52           O  
HETATM 4632  O   HOH B 356     -27.624 -14.575 -11.877  1.00 24.87           O  
HETATM 4633  O   HOH B 358     -28.442 -16.899 -11.075  1.00 25.10           O  
HETATM 4634  O   HOH B 359      -5.474  26.450  -8.996  1.00 22.54           O  
HETATM 4635  O   HOH B 360     -19.091  -6.829 -24.301  1.00 35.09           O  
HETATM 4636  O   HOH B 362     -16.547  -6.387 -23.918  1.00 35.34           O  
HETATM 4637  O   HOH B 364      -2.856  25.109   7.059  1.00 29.77           O  
HETATM 4638  O   HOH B 366     -29.155 -10.920 -13.840  1.00 26.29           O  
HETATM 4639  O   HOH B 367       9.881  18.182   3.523  1.00 23.81           O  
HETATM 4640  O   HOH B 368      15.924   8.418  -5.505  1.00 27.31           O  
HETATM 4641  O   HOH B 369      10.061   0.812   3.557  1.00 22.37           O  
HETATM 4642  O   HOH B 370      -6.308  11.507   5.244  1.00 24.66           O  
HETATM 4643  O   HOH B 371      -0.965  27.958  -1.339  1.00 31.41           O  
HETATM 4644  O   HOH B 372     -27.653  -9.967 -15.923  1.00 23.26           O  
HETATM 4645  O   HOH B 381     -10.680  19.812 -22.077  1.00 28.40           O  
HETATM 4646  O   HOH B 382     -10.989  23.451 -22.922  1.00 26.75           O  
HETATM 4647  O   HOH B 384       7.414   2.785 -22.897  1.00 26.44           O  
HETATM 4648  O   HOH B 385      11.920   6.780   1.249  1.00 28.61           O  
HETATM 4649  O   HOH B 387       4.221  25.832   2.862  1.00 25.63           O  
HETATM 4650  O   HOH B 389      10.748  23.600  -1.526  1.00 31.27           O  
HETATM 4651  O   HOH B 391     -29.639  -2.149 -10.380  1.00 25.60           O  
HETATM 4652  O   HOH B 392       5.958  24.140   2.494  1.00 30.67           O  
HETATM 4653  O   HOH B 393     -25.680  -1.048 -26.005  1.00 34.39           O  
HETATM 4654  O   HOH B 394     -15.261 -19.207   0.326  1.00 30.07           O  
HETATM 4655  O   HOH B 395      -7.395  12.660   1.024  1.00 28.00           O  
HETATM 4656  O   HOH B 396      12.654   9.368 -20.658  1.00 24.19           O  
HETATM 4657  O   HOH B 408       4.473  11.632   3.170  1.00 24.93           O  
HETATM 4658  O   HOH B 411       0.133  22.594 -14.556  1.00 20.44           O  
HETATM 4659  O   HOH B 792      -8.560   1.115  -8.136  1.00  6.83           O  
HETATM 4660  O   HOH B 793     -28.846   3.212 -19.791  1.00 22.01           O  
HETATM 4661  O   HOH B 794     -10.845  25.318   7.482  1.00 32.98           O  
HETATM 4662  O   HOH B 795      13.889   5.834  15.811  1.00 26.15           O  
HETATM 4663  O   HOH B 796     -22.248  10.990  16.467  1.00 30.15           O  
HETATM 4664  O   HOH B 797     -16.630 -10.156 -25.745  1.00 32.27           O  
HETATM 4665  O   HOH B 798       6.317  12.897   4.843  1.00 23.40           O  
HETATM 4666  O   HOH B 799       6.657   7.830  29.855  1.00 27.31           O  
HETATM 4667  O   HOH B 800      15.965  10.561  12.551  1.00 27.62           O  
HETATM 4668  O   HOH B 804      13.687  13.626  -8.403  1.00 25.96           O  
HETATM 4669  O   HOH B 805      12.015  20.079  21.283  1.00 31.61           O  
HETATM 4670  O   HOH B 806     -13.037  21.867 -19.918  1.00 30.93           O  
HETATM 4671  O   HOH B 807     -20.061  15.496 -11.275  1.00 33.97           O  
HETATM 4672  O   HOH B 808     -13.411   2.849 -27.986  1.00 30.00           O  
HETATM 4673  O   HOH B 809       0.853  26.333 -27.136  1.00 29.94           O  
HETATM 4674  O   HOH B 810      -4.086  -3.941  -4.590  1.00 29.07           O  
HETATM 4675  O   HOH B 811      -4.095 -10.735 -19.628  1.00 25.69           O  
HETATM 4676  O   HOH B 812     -20.304   9.743 -22.516  1.00 27.56           O  
HETATM 4677  O   HOH B 813      -9.626  -3.767  38.310  1.00 29.79           O  
HETATM 4678  O   HOH B 814      15.078  19.664  -3.337  1.00 36.97           O  
HETATM 4679  O   HOH B 815     -19.498   7.575  -7.098  1.00 32.19           O  
HETATM 4680  O   HOH B 816      14.202  17.895  14.392  1.00 24.94           O  
HETATM 4681  O   HOH B 817      -5.311  -8.815   8.207  1.00 41.81           O  
HETATM 4682  O   HOH B 818     -14.306   7.011 -27.077  1.00 29.82           O  
HETATM 4683  O   HOH B 819     -22.394   7.758  -9.034  1.00 31.28           O  
HETATM 4684  O   HOH B 820      12.037  -1.096  -4.131  1.00 32.33           O  
HETATM 4685  O   HOH B 821     -22.931  -7.060 -26.179  1.00 30.45           O  
HETATM 4686  O   HOH B 822       4.727  -7.303  -3.830  1.00 40.99           O  
HETATM 4687  O   HOH B 823      -4.423  33.091  16.277  1.00 30.70           O  
HETATM 4688  O   HOH B 824     -29.160 -13.714 -14.044  1.00 24.73           O  
HETATM 4689  O   HOH B 825     -29.513  27.009  23.695  1.00 30.40           O  
HETATM 4690  O   HOH B 826     -11.915  36.954   8.793  1.00 32.11           O  
HETATM 4691  O   HOH B 827      -3.492  -9.542  10.078  1.00 35.25           O  
HETATM 4692  O   HOH B 828      10.629  22.276  10.070  1.00 34.91           O  
HETATM 4693  O   HOH B 829     -33.131  -1.584 -12.251  1.00 31.20           O  
HETATM 4694  O   HOH B 830       6.987  33.952  24.825  1.00 36.90           O  
HETATM 4695  O   HOH B 831      -4.917  28.247 -17.528  1.00 29.63           O  
HETATM 4696  O   HOH B 832      12.243  17.674   2.718  1.00 32.80           O  
HETATM 4697  O   HOH B 833      -5.577 -12.061  20.827  1.00 24.11           O  
HETATM 4698  O   HOH B 834     -25.932  34.545  28.978  1.00 33.19           O  
HETATM 4699  O   HOH B 835      -7.901  14.145   4.285  1.00 36.58           O  
HETATM 4700  O   HOH B 836     -33.339  11.196  -8.156  1.00 35.18           O  
HETATM 4701  O   HOH B 837      15.364   8.188  13.423  1.00 27.35           O  
HETATM 4702  O   HOH B 838       4.664  20.271 -27.579  1.00 30.84           O  
HETATM 4703  O   HOH B 839     -22.997  -7.717  -1.690  1.00 31.39           O  
CONECT 1638 2056                                                                
CONECT 2056 1638                                                                
CONECT 3723 4147                                                                
CONECT 4147 3723                                                                
CONECT 4157 4158                                                                
CONECT 4158 4157 4159                                                           
CONECT 4159 4158 4160 4166                                                      
CONECT 4160 4159 4161 4162                                                      
CONECT 4161 4160                                                                
CONECT 4162 4160 4163                                                           
CONECT 4163 4162 4164                                                           
CONECT 4164 4163 4165 4166                                                      
CONECT 4165 4164 4168                                                           
CONECT 4166 4159 4164 4167                                                      
CONECT 4167 4166 4168                                                           
CONECT 4168 4165 4167 4169 4172                                                 
CONECT 4169 4168 4170 4171                                                      
CONECT 4170 4169                                                                
CONECT 4171 4169                                                                
CONECT 4172 4168 4173                                                           
CONECT 4173 4172 4174 4177                                                      
CONECT 4174 4173 4175 4176                                                      
CONECT 4175 4174                                                                
CONECT 4176 4174                                                                
CONECT 4177 4173                                                                
CONECT 4178 4179 4180 4181 4182                                                 
CONECT 4179 4178                                                                
CONECT 4180 4178                                                                
CONECT 4181 4178                                                                
CONECT 4182 4178                                                                
CONECT 4183 4184 4185 4186 4187                                                 
CONECT 4184 4183                                                                
CONECT 4185 4183                                                                
CONECT 4186 4183                                                                
CONECT 4187 4183                                                                
CONECT 4188 4189 4190 4191 4192                                                 
CONECT 4189 4188                                                                
CONECT 4190 4188                                                                
CONECT 4191 4188                                                                
CONECT 4192 4188                                                                
CONECT 4193 4194 4195 4196 4197                                                 
CONECT 4194 4193                                                                
CONECT 4195 4193                                                                
CONECT 4196 4193                                                                
CONECT 4197 4193                                                                
CONECT 4198 4199 4200                                                           
CONECT 4199 4198                                                                
CONECT 4200 4198 4201 4202                                                      
CONECT 4201 4200                                                                
CONECT 4202 4200 4203                                                           
CONECT 4203 4202                                                                
CONECT 4204 4205 4206                                                           
CONECT 4205 4204                                                                
CONECT 4206 4204 4207 4208                                                      
CONECT 4207 4206                                                                
CONECT 4208 4206 4209                                                           
CONECT 4209 4208                                                                
CONECT 4210 4211 4212                                                           
CONECT 4211 4210                                                                
CONECT 4212 4210 4213 4214                                                      
CONECT 4213 4212                                                                
CONECT 4214 4212 4215                                                           
CONECT 4215 4214                                                                
CONECT 4216 4217                                                                
CONECT 4217 4216 4218                                                           
CONECT 4218 4217 4219 4225                                                      
CONECT 4219 4218 4220 4221                                                      
CONECT 4220 4219                                                                
CONECT 4221 4219 4222                                                           
CONECT 4222 4221 4223                                                           
CONECT 4223 4222 4224 4225                                                      
CONECT 4224 4223 4227                                                           
CONECT 4225 4218 4223 4226                                                      
CONECT 4226 4225 4227                                                           
CONECT 4227 4224 4226 4228 4231                                                 
CONECT 4228 4227 4229 4230                                                      
CONECT 4229 4228                                                                
CONECT 4230 4228                                                                
CONECT 4231 4227 4232                                                           
CONECT 4232 4231 4233 4236                                                      
CONECT 4233 4232 4234 4235                                                      
CONECT 4234 4233                                                                
CONECT 4235 4233                                                                
CONECT 4236 4232                                                                
CONECT 4237 4238 4239 4240 4241                                                 
CONECT 4238 4237                                                                
CONECT 4239 4237                                                                
CONECT 4240 4237                                                                
CONECT 4241 4237                                                                
MASTER      501    0   10   24   27    0   25    6 4603    2   89   40          
END                                                                             



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